HEADER MEMBRANE PROTEIN 17-MAR-16 5IU4 TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL TITLE 2 IN COMPLEX WITH ZM241385 AT 1.7A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: TNI PRO; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFAST-BAC KEYWDS G-PROTEIN-COUPLED RECEPTOR, INTEGRAL MEMBRANE PROTEIN, CHIMERA, KEYWDS 2 THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR E.SEGALA,D.GUO,R.K.Y.CHENG,A.BORTOLATO,F.DEFLORIAN,A.S.DORE, AUTHOR 2 J.C.ERREY,L.H.HEITMAN,A.P.IJZERMAN,F.H.MARSHALL,R.M.COOKE REVDAT 3 31-JAN-18 5IU4 1 REMARK REVDAT 2 27-JUL-16 5IU4 1 JRNL REVDAT 1 29-JUN-16 5IU4 0 JRNL AUTH E.SEGALA,D.GUO,R.K.CHENG,A.BORTOLATO,F.DEFLORIAN,A.S.DORE, JRNL AUTH 2 J.C.ERREY,L.H.HEITMAN,A.P.IJZERMAN,F.H.MARSHALL,R.M.COOKE JRNL TITL CONTROLLING THE DISSOCIATION OF LIGANDS FROM THE ADENOSINE JRNL TITL 2 A2A RECEPTOR THROUGH MODULATION OF SALT BRIDGE STRENGTH. JRNL REF J.MED.CHEM. V. 59 6470 2016 JRNL REFN ISSN 0022-2623 JRNL PMID 27312113 JRNL DOI 10.1021/ACS.JMEDCHEM.6B00653 REMARK 2 REMARK 2 RESOLUTION. 1.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.73 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.010 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 49292 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.169 REMARK 3 R VALUE (WORKING SET) : 0.167 REMARK 3 FREE R VALUE : 0.200 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 4682 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 33.7397 - 5.3377 0.91 2960 123 0.1748 0.1962 REMARK 3 2 5.3377 - 4.2393 0.92 3004 149 0.1536 0.1770 REMARK 3 3 4.2393 - 3.7042 0.93 3032 135 0.1441 0.1823 REMARK 3 4 3.7042 - 3.3659 0.92 2959 169 0.1436 0.1865 REMARK 3 5 3.3659 - 3.1248 0.93 3041 133 0.1528 0.1685 REMARK 3 6 3.1248 - 2.9407 0.92 2959 146 0.1483 0.1637 REMARK 3 7 2.9407 - 2.7935 0.93 2940 185 0.1438 0.1954 REMARK 3 8 2.7935 - 2.6719 0.93 3000 187 0.1398 0.1808 REMARK 3 9 2.6719 - 2.5691 0.94 3065 138 0.1359 0.1361 REMARK 3 10 2.5691 - 2.4805 0.93 2990 145 0.1415 0.1716 REMARK 3 11 2.4805 - 2.4029 0.91 2979 184 0.1439 0.1987 REMARK 3 12 2.4029 - 2.3343 0.93 2964 145 0.1483 0.2221 REMARK 3 13 2.3343 - 2.2728 0.93 3068 150 0.1481 0.2394 REMARK 3 14 2.2728 - 2.2174 0.95 3043 152 0.1552 0.1621 REMARK 3 15 2.2174 - 2.1670 0.92 2947 178 0.1567 0.1830 REMARK 3 16 2.1670 - 2.1209 0.93 3027 147 0.1612 0.1798 REMARK 3 17 2.1209 - 2.0785 0.95 3000 172 0.1696 0.2346 REMARK 3 18 2.0785 - 2.0392 0.93 3067 169 0.1797 0.1971 REMARK 3 19 2.0392 - 2.0028 0.93 3018 171 0.1862 0.1952 REMARK 3 20 2.0028 - 1.9689 0.93 2923 163 0.1890 0.2286 REMARK 3 21 1.9689 - 1.9371 0.94 3088 143 0.2084 0.2347 REMARK 3 22 1.9371 - 1.9073 0.93 3024 152 0.2090 0.2606 REMARK 3 23 1.9073 - 1.8793 0.93 2963 124 0.2314 0.2194 REMARK 3 24 1.8793 - 1.8528 0.94 3060 160 0.2392 0.2722 REMARK 3 25 1.8528 - 1.8278 0.93 3034 158 0.2422 0.2718 REMARK 3 26 1.8278 - 1.8040 0.94 2951 162 0.2478 0.2867 REMARK 3 27 1.8040 - 1.7815 0.94 3032 172 0.2703 0.2888 REMARK 3 28 1.7815 - 1.7600 0.92 3018 143 0.2810 0.3543 REMARK 3 29 1.7600 - 1.7396 0.92 2984 153 0.3045 0.2921 REMARK 3 30 1.7396 - 1.7200 0.94 2982 174 0.3137 0.3511 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.210 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3755 REMARK 3 ANGLE : 0.822 5041 REMARK 3 CHIRALITY : 0.049 571 REMARK 3 PLANARITY : 0.005 602 REMARK 3 DIHEDRAL : 15.440 2056 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' (RESID -1 THROUGH 34) REMARK 3 ORIGIN FOR THE GROUP (A): -30.8007 -3.8815 6.9616 REMARK 3 T TENSOR REMARK 3 T11: 0.1692 T22: 0.2247 REMARK 3 T33: 0.0819 T12: -0.0065 REMARK 3 T13: -0.0147 T23: -0.0175 REMARK 3 L TENSOR REMARK 3 L11: 1.9146 L22: 2.7392 REMARK 3 L33: 3.8013 L12: 0.3861 REMARK 3 L13: 0.1222 L23: -1.6625 REMARK 3 S TENSOR REMARK 3 S11: 0.0473 S12: 0.0099 S13: 0.0270 REMARK 3 S21: -0.2369 S22: -0.0259 S23: 0.2594 REMARK 3 S31: -0.0931 S32: -0.2587 S33: -0.0687 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' (RESID 35 THROUGH 38) REMARK 3 ORIGIN FOR THE GROUP (A): -30.6342 -29.9370 15.2010 REMARK 3 T TENSOR REMARK 3 T11: 0.7543 T22: 0.1781 REMARK 3 T33: 0.4939 T12: -0.2586 REMARK 3 T13: -0.1371 T23: 0.1477 REMARK 3 L TENSOR REMARK 3 L11: 0.7918 L22: 1.0439 REMARK 3 L33: 0.9159 L12: 0.9101 REMARK 3 L13: -0.8519 L23: -0.9782 REMARK 3 S TENSOR REMARK 3 S11: -0.0687 S12: -0.0205 S13: -0.3930 REMARK 3 S21: -0.0183 S22: 0.0922 S23: 0.4562 REMARK 3 S31: 0.3739 S32: -0.1280 S33: 0.3141 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' (RESID 39 THROUGH 73) REMARK 3 ORIGIN FOR THE GROUP (A): -29.8145 -4.2283 17.2360 REMARK 3 T TENSOR REMARK 3 T11: 0.0855 T22: 0.1904 REMARK 3 T33: 0.0616 T12: -0.0227 REMARK 3 T13: 0.0182 T23: -0.0081 REMARK 3 L TENSOR REMARK 3 L11: 1.5264 L22: 3.7014 REMARK 3 L33: 1.3721 L12: -0.4125 REMARK 3 L13: 0.6545 L23: -0.0277 REMARK 3 S TENSOR REMARK 3 S11: 0.0702 S12: -0.0492 S13: -0.0147 REMARK 3 S21: -0.1392 S22: -0.1393 S23: 0.2003 REMARK 3 S31: 0.1223 S32: -0.2262 S33: 0.0566 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' (RESID 74 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): -22.4813 -8.6623 24.0245 REMARK 3 T TENSOR REMARK 3 T11: 0.1075 T22: 0.1787 REMARK 3 T33: 0.0614 T12: -0.0127 REMARK 3 T13: -0.0139 T23: 0.0056 REMARK 3 L TENSOR REMARK 3 L11: 2.8681 L22: 7.2117 REMARK 3 L33: 1.0036 L12: -3.1752 REMARK 3 L13: -0.2198 L23: 0.6406 REMARK 3 S TENSOR REMARK 3 S11: -0.0905 S12: -0.0824 S13: -0.0435 REMARK 3 S21: 0.2377 S22: 0.0429 S23: -0.0396 REMARK 3 S31: 0.1361 S32: -0.0623 S33: 0.0238 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' (RESID 109 THROUGH 117) REMARK 3 ORIGIN FOR THE GROUP (A): -19.4789 -32.0250 28.6784 REMARK 3 T TENSOR REMARK 3 T11: 0.6535 T22: 0.3073 REMARK 3 T33: 0.5034 T12: -0.0256 REMARK 3 T13: 0.0443 T23: 0.1455 REMARK 3 L TENSOR REMARK 3 L11: 5.5329 L22: 5.1683 REMARK 3 L33: 4.1774 L12: -5.3276 REMARK 3 L13: -4.1454 L23: 4.1921 REMARK 3 S TENSOR REMARK 3 S11: -0.6063 S12: -0.7950 S13: -1.3577 REMARK 3 S21: 0.4858 S22: 0.1334 S23: 0.6957 REMARK 3 S31: 1.1196 S32: 0.3762 S33: 0.2965 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' (RESID 118 THROUGH 137) REMARK 3 ORIGIN FOR THE GROUP (A): -27.1869 -12.1164 29.8130 REMARK 3 T TENSOR REMARK 3 T11: 0.2265 T22: 0.2118 REMARK 3 T33: 0.0998 T12: -0.0233 REMARK 3 T13: -0.0002 T23: 0.0368 REMARK 3 L TENSOR REMARK 3 L11: 2.5455 L22: 2.6173 REMARK 3 L33: 1.5091 L12: 0.2276 REMARK 3 L13: -0.0229 L23: -1.0357 REMARK 3 S TENSOR REMARK 3 S11: 0.0555 S12: -0.2574 S13: -0.2576 REMARK 3 S21: 0.2870 S22: -0.1530 S23: 0.0200 REMARK 3 S31: 0.4431 S32: -0.1290 S33: 0.0666 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' (RESID 138 THROUGH 161) REMARK 3 ORIGIN FOR THE GROUP (A): -27.7291 16.7370 27.0944 REMARK 3 T TENSOR REMARK 3 T11: 0.1876 T22: 0.1797 REMARK 3 T33: 0.1786 T12: 0.0545 REMARK 3 T13: -0.0243 T23: -0.0413 REMARK 3 L TENSOR REMARK 3 L11: 3.3337 L22: 6.7864 REMARK 3 L33: 3.9057 L12: -1.9809 REMARK 3 L13: 1.9527 L23: -3.9795 REMARK 3 S TENSOR REMARK 3 S11: -0.0172 S12: -0.1117 S13: 0.4639 REMARK 3 S21: 0.0869 S22: -0.0933 S23: 0.2813 REMARK 3 S31: -0.4383 S32: -0.1018 S33: 0.0795 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' (RESID 162 THROUGH 186) REMARK 3 ORIGIN FOR THE GROUP (A): -19.3368 7.6967 25.1141 REMARK 3 T TENSOR REMARK 3 T11: 0.0861 T22: 0.1570 REMARK 3 T33: 0.0908 T12: 0.0131 REMARK 3 T13: -0.0040 T23: -0.0154 REMARK 3 L TENSOR REMARK 3 L11: 2.0145 L22: 3.1675 REMARK 3 L33: 1.9973 L12: -0.9259 REMARK 3 L13: 0.5570 L23: -0.9510 REMARK 3 S TENSOR REMARK 3 S11: 0.0441 S12: -0.0233 S13: 0.1247 REMARK 3 S21: -0.0366 S22: -0.1112 S23: 0.0840 REMARK 3 S31: -0.1330 S32: 0.0044 S33: 0.0517 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' (RESID 187 THROUGH 208) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2289 -19.8311 21.9482 REMARK 3 T TENSOR REMARK 3 T11: 0.1647 T22: 0.1586 REMARK 3 T33: 0.2448 T12: 0.0505 REMARK 3 T13: -0.0298 T23: 0.0033 REMARK 3 L TENSOR REMARK 3 L11: 2.7292 L22: 1.1403 REMARK 3 L33: 2.5168 L12: -1.3657 REMARK 3 L13: -1.1534 L23: 1.5058 REMARK 3 S TENSOR REMARK 3 S11: -0.1091 S12: -0.1327 S13: -0.3885 REMARK 3 S21: 0.1516 S22: 0.2080 S23: -0.1880 REMARK 3 S31: 0.3301 S32: 0.2181 S33: -0.1427 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' (RESID 219 THROUGH 259) REMARK 3 ORIGIN FOR THE GROUP (A): -12.4637 -13.0931 15.0019 REMARK 3 T TENSOR REMARK 3 T11: 0.1421 T22: 0.1453 REMARK 3 T33: 0.1587 T12: 0.0421 REMARK 3 T13: 0.0206 T23: 0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.9561 L22: 4.6027 REMARK 3 L33: 1.2349 L12: 0.1131 REMARK 3 L13: 0.4880 L23: 0.1010 REMARK 3 S TENSOR REMARK 3 S11: 0.0807 S12: 0.0150 S13: -0.2637 REMARK 3 S21: -0.2997 S22: 0.0217 S23: -0.2080 REMARK 3 S31: 0.2785 S32: 0.1115 S33: -0.0491 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' (RESID 260 THROUGH 265) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6203 16.4008 16.3878 REMARK 3 T TENSOR REMARK 3 T11: 0.2002 T22: 0.2295 REMARK 3 T33: 0.2463 T12: -0.0731 REMARK 3 T13: -0.0206 T23: 0.0570 REMARK 3 L TENSOR REMARK 3 L11: 4.7674 L22: 4.2645 REMARK 3 L33: 4.2928 L12: -2.3024 REMARK 3 L13: 2.3673 L23: -0.3625 REMARK 3 S TENSOR REMARK 3 S11: -0.2939 S12: 0.2004 S13: 0.5705 REMARK 3 S21: 0.0798 S22: 0.0417 S23: -0.5157 REMARK 3 S31: -0.5626 S32: 1.0450 S33: 0.3854 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' (RESID 266 THROUGH 292) REMARK 3 ORIGIN FOR THE GROUP (A): -20.4195 -4.2633 8.4043 REMARK 3 T TENSOR REMARK 3 T11: 0.1487 T22: 0.1991 REMARK 3 T33: 0.0937 T12: 0.0099 REMARK 3 T13: 0.0033 T23: -0.0079 REMARK 3 L TENSOR REMARK 3 L11: 1.6181 L22: 5.4306 REMARK 3 L33: 2.0283 L12: 1.7158 REMARK 3 L13: 0.1112 L23: -0.2409 REMARK 3 S TENSOR REMARK 3 S11: -0.1086 S12: 0.1469 S13: -0.0880 REMARK 3 S21: -0.3291 S22: 0.1439 S23: 0.1388 REMARK 3 S31: 0.1912 S32: -0.0663 S33: -0.0448 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' (RESID 293 THROUGH 307) REMARK 3 ORIGIN FOR THE GROUP (A): -29.7979 -25.3300 3.3924 REMARK 3 T TENSOR REMARK 3 T11: 0.7766 T22: 0.3745 REMARK 3 T33: 0.3005 T12: -0.1535 REMARK 3 T13: -0.0416 T23: -0.0669 REMARK 3 L TENSOR REMARK 3 L11: 8.2339 L22: 5.3174 REMARK 3 L33: 5.8713 L12: 1.0544 REMARK 3 L13: 1.1174 L23: 2.0578 REMARK 3 S TENSOR REMARK 3 S11: 0.1476 S12: 0.9047 S13: -0.9983 REMARK 3 S21: -1.0601 S22: 0.1538 S23: -0.0553 REMARK 3 S31: 0.9278 S32: -0.3134 S33: -0.2999 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' (RESID 1001 THROUGH 1021) REMARK 3 ORIGIN FOR THE GROUP (A): 5.8039 -48.9742 16.6326 REMARK 3 T TENSOR REMARK 3 T11: 0.4229 T22: 0.2192 REMARK 3 T33: 1.1191 T12: 0.1802 REMARK 3 T13: 0.1407 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 6.2923 L22: 4.9733 REMARK 3 L33: 3.1542 L12: -5.0437 REMARK 3 L13: -0.5874 L23: 1.1954 REMARK 3 S TENSOR REMARK 3 S11: -0.0323 S12: -0.0345 S13: 0.2382 REMARK 3 S21: -0.6256 S22: -0.5390 S23: -1.1795 REMARK 3 S31: -0.1293 S32: 0.2329 S33: 0.1572 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' (RESID 1022 THROUGH 1042) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9158 -52.9591 25.6483 REMARK 3 T TENSOR REMARK 3 T11: 0.3694 T22: 0.4471 REMARK 3 T33: 1.0210 T12: 0.0358 REMARK 3 T13: -0.1584 T23: -0.2059 REMARK 3 L TENSOR REMARK 3 L11: 3.3623 L22: 4.5428 REMARK 3 L33: 4.7675 L12: -2.9370 REMARK 3 L13: -2.1808 L23: -0.6393 REMARK 3 S TENSOR REMARK 3 S11: -0.3952 S12: -0.6950 S13: 1.2917 REMARK 3 S21: 0.2235 S22: -0.0930 S23: -0.3761 REMARK 3 S31: -0.6880 S32: 0.6645 S33: 0.1878 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' (RESID 1058 THROUGH 1081) REMARK 3 ORIGIN FOR THE GROUP (A): -5.1127 -57.9691 23.5501 REMARK 3 T TENSOR REMARK 3 T11: 0.3415 T22: 0.2259 REMARK 3 T33: 0.6625 T12: -0.0112 REMARK 3 T13: 0.0236 T23: 0.0863 REMARK 3 L TENSOR REMARK 3 L11: 5.4734 L22: 2.6652 REMARK 3 L33: 8.7944 L12: 0.2345 REMARK 3 L13: 1.2332 L23: 1.0715 REMARK 3 S TENSOR REMARK 3 S11: 0.0326 S12: -0.6347 S13: 0.2085 REMARK 3 S21: 0.0906 S22: 0.5025 S23: 1.1492 REMARK 3 S31: -0.0863 S32: -0.5943 S33: -0.4898 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' (RESID 1082 THROUGH 1093) REMARK 3 ORIGIN FOR THE GROUP (A): 6.1482 -65.2862 18.5885 REMARK 3 T TENSOR REMARK 3 T11: 0.6657 T22: 0.1788 REMARK 3 T33: 0.8146 T12: 0.2677 REMARK 3 T13: 0.2129 T23: 0.0533 REMARK 3 L TENSOR REMARK 3 L11: 6.1828 L22: 6.6258 REMARK 3 L33: 2.6848 L12: -3.9485 REMARK 3 L13: 2.0174 L23: -0.1205 REMARK 3 S TENSOR REMARK 3 S11: -0.2417 S12: -0.1371 S13: -0.1278 REMARK 3 S21: -0.4545 S22: -0.0607 S23: -0.1690 REMARK 3 S31: 0.1941 S32: 0.1679 S33: 0.0692 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' (RESID 1094 THROUGH 1101) REMARK 3 ORIGIN FOR THE GROUP (A): -4.4480 -55.3752 12.7478 REMARK 3 T TENSOR REMARK 3 T11: 0.7657 T22: 0.2551 REMARK 3 T33: 0.6686 T12: 0.1227 REMARK 3 T13: -0.0999 T23: 0.0499 REMARK 3 L TENSOR REMARK 3 L11: 1.5503 L22: 4.8455 REMARK 3 L33: 7.0573 L12: 0.7396 REMARK 3 L13: 1.6427 L23: -0.9258 REMARK 3 S TENSOR REMARK 3 S11: 0.2065 S12: 0.5629 S13: -0.3152 REMARK 3 S21: -1.2986 S22: -0.0411 S23: 0.6208 REMARK 3 S31: 0.0692 S32: 0.1132 S33: -0.1117 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' (RESID 1102 THROUGH 1106) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7970 -46.8407 13.5645 REMARK 3 T TENSOR REMARK 3 T11: 0.7745 T22: 0.3420 REMARK 3 T33: 0.7601 T12: 0.2985 REMARK 3 T13: -0.0217 T23: -0.0720 REMARK 3 L TENSOR REMARK 3 L11: 5.4455 L22: 7.4421 REMARK 3 L33: 1.2946 L12: -2.4377 REMARK 3 L13: 0.6247 L23: -1.9754 REMARK 3 S TENSOR REMARK 3 S11: -0.0596 S12: -0.0451 S13: -0.1569 REMARK 3 S21: -0.2196 S22: -0.0066 S23: -0.2619 REMARK 3 S31: -0.0399 S32: -0.0009 S33: 0.0577 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5IU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-MAR-16. REMARK 100 THE DEPOSITION ID IS D_1000219424. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-AUG-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686 REMARK 200 MONOCHROMATOR : DOUBLE SI(111) CRYSTAL REMARK 200 OPTICS : (DOUBLE) KB MIRROR PAIR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JANUARY 10, 2014 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49406 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720 REMARK 200 RESOLUTION RANGE LOW (A) : 33.730 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.11100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : 0.99400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.5.6 REMARK 200 STARTING MODEL: PDB CODE 4EIY REMARK 200 REMARK 200 REMARK: RECTANGULAR REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 0.2M K/NA TARTRATE, REMARK 280 27.5-40% PEG400, 0.5-1% (V/V) (+/-)-2-METHYL-2,4-PENTANEDIOL, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.92350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.92350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.71400 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.79950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.71400 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.79950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.92350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.71400 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.79950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.92350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.71400 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.79950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. 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: 11060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20630 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 48.0 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 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLY A 162 O HOH A 2501 2.05 REMARK 500 O HOH A 2642 O HOH A 2644 2.07 REMARK 500 O HOH A 2524 O HOH A 2533 2.10 REMARK 500 O HOH A 2524 O HOH A 2636 2.13 REMARK 500 O1 OLA A 2423 O HOH A 2502 2.16 REMARK 500 O HOH A 2502 O HOH A 2588 2.16 REMARK 500 O HOH A 2635 O HOH A 2648 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -50.24 -120.63 REMARK 500 VAL A 186 -56.40 -120.24 REMARK 500 VAL A 186 -58.01 -120.24 REMARK 500 TYR A1101 -61.49 -124.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 2407 REMARK 610 OLA A 2408 REMARK 610 OLA A 2409 REMARK 610 OLA A 2410 REMARK 610 OLA A 2412 REMARK 610 OLA A 2413 REMARK 610 OLA A 2414 REMARK 610 OLA A 2415 REMARK 610 OLA A 2416 REMARK 610 OLA A 2417 REMARK 610 OLA A 2418 REMARK 610 OLA A 2419 REMARK 610 OLA A 2420 REMARK 610 OLA A 2421 REMARK 610 OLA A 2422 REMARK 610 OLA A 2423 REMARK 610 OLA A 2424 REMARK 610 OLA A 2425 REMARK 610 OLB A 2426 REMARK 610 OLB A 2427 REMARK 610 OLB A 2428 REMARK 610 OLC A 2430 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A2400 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 127.3 REMARK 620 3 HOH A2546 O 100.7 122.7 REMARK 620 4 HOH A2555 O 85.9 121.8 86.5 REMARK 620 5 HOH A2612 O 88.7 69.9 83.9 167.9 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 2401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2415 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2418 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2420 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2421 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2422 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2423 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2424 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2425 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 2426 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 2427 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 2428 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2429 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2430 DBREF 5IU4 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5IU4 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5IU4 A 219 318 UNP P29274 AA2AR_HUMAN 219 318 SEQADV 5IU4 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5IU4 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5IU4 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5IU4 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5IU4 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5IU4 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5IU4 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5IU4 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5IU4 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5IU4 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5IU4 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5IU4 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5IU4 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5IU4 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5IU4 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5IU4 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5IU4 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5IU4 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5IU4 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5IU4 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5IU4 ALA A 318 UNP P29274 GLY 318 ENGINEERED MUTATION SEQADV 5IU4 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5IU4 HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 34 A 433 HIS HIS HIS HIS HET NA A2400 1 HET ZMA A2401 25 HET CLR A2402 28 HET CLR A2403 28 HET CLR A2404 28 HET CLR A2405 28 HET OLA A2406 20 HET OLA A2407 15 HET OLA A2408 7 HET OLA A2409 9 HET OLA A2410 18 HET OLA A2411 20 HET OLA A2412 15 HET OLA A2413 12 HET OLA A2414 8 HET OLA A2415 14 HET OLA A2416 7 HET OLA A2417 19 HET OLA A2418 10 HET OLA A2419 7 HET OLA A2420 17 HET OLA A2421 11 HET OLA A2422 13 HET OLA A2423 17 HET OLA A2424 12 HET OLA A2425 10 HET OLB A2426 17 HET OLB A2427 19 HET OLB A2428 20 HET OLC A2429 25 HET OLC A2430 19 HETNAM NA SODIUM ION HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3, HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 NA NA 1+ FORMUL 3 ZMA C16 H15 N7 O2 FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 20(C18 H34 O2) FORMUL 28 OLB 3(C21 H40 O4) FORMUL 31 OLC 2(C21 H40 O4) FORMUL 33 HOH *164(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ILE A 108 VAL A 116 1 9 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 LYS A 1059 GLU A 1081 1 23 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 TYR A 1101 CYS A 259 1 47 HELIX 17 AB8 PRO A 266 ILE A 292 1 27 HELIX 18 AB9 ILE A 292 SER A 305 1 14 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.05 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.02 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04 LINK OD1 ASP A 52 NA NA A2400 1555 1555 2.52 LINK OG SER A 91 NA NA A2400 1555 1555 2.50 LINK NA NA A2400 O HOH A2546 1555 1555 2.54 LINK NA NA A2400 O HOH A2555 1555 1555 2.15 LINK NA NA A2400 O HOH A2612 1555 1555 2.63 SITE 1 AC1 5 ASP A 52 SER A 91 HOH A2546 HOH A2555 SITE 2 AC1 5 HOH A2612 SITE 1 AC2 14 LEU A 85 PHE A 168 GLU A 169 MET A 177 SITE 2 AC2 14 TRP A 246 LEU A 249 HIS A 250 ASN A 253 SITE 3 AC2 14 MET A 270 ILE A 274 HOH A2543 HOH A2598 SITE 4 AC2 14 HOH A2608 HOH A2611 SITE 1 AC3 9 HIS A 75 GLY A 76 PHE A 79 PHE A 133 SITE 2 AC3 9 MET A 140 CLR A2403 OLA A2421 OLA A2422 SITE 3 AC3 9 OLB A2426 SITE 1 AC4 9 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC4 9 CLR A2402 CLR A2405 OLB A2427 OLC A2429 SITE 3 AC4 9 HOH A2526 SITE 1 AC5 7 LEU A 247 PRO A 248 CYS A 262 SER A 263 SITE 2 AC5 7 OLA A2412 HOH A2502 HOH A2614 SITE 1 AC6 8 CYS A 254 PHE A 255 PHE A 258 CLR A2403 SITE 2 AC6 8 OLA A2418 OLB A2427 OLC A2429 HOH A2589 SITE 1 AC7 3 THR A 65 OLA A2423 OLC A2429 SITE 1 AC8 1 PRO A 266 SITE 1 AC9 1 LEU A 244 SITE 1 AD1 4 PHE A 44 ALA A 97 VAL A 116 HOH A2583 SITE 1 AD2 5 GLY A 5 LEU A 267 TYR A 271 VAL A 275 SITE 2 AD2 5 HOH A2637 SITE 1 AD3 7 LEU A 96 ILE A 127 LEU A 131 CYS A 185 SITE 2 AD3 7 PRO A 189 OLA A2415 OLA A2420 SITE 1 AD4 1 CLR A2404 SITE 1 AD5 4 LEU A 19 LEU A 26 TRP A 29 PHE A 286 SITE 1 AD6 3 GLY A 123 VAL A 130 OLA A2411 SITE 1 AD7 1 OLA A2425 SITE 1 AD8 3 TRP A 32 LYS A 233 OLB A2428 SITE 1 AD9 5 LEU A 187 LEU A 194 ALA A 236 ALA A 243 SITE 2 AD9 5 CLR A2405 SITE 1 AE1 9 MET A 140 LEU A 141 TYR A 179 ALA A 184 SITE 2 AE1 9 OLA A2411 OLA A2421 OLB A2426 HOH A2508 SITE 3 AE1 9 HOH A2515 SITE 1 AE2 5 MET A 140 CLR A2402 OLA A2420 OLA A2422 SITE 2 AE2 5 HOH A2503 SITE 1 AE3 3 CLR A2402 OLA A2421 OLC A2430 SITE 1 AE4 6 PHE A 255 CYS A 262 OLA A2406 OLC A2429 SITE 2 AE4 6 HOH A2502 HOH A2588 SITE 1 AE5 2 SER A 6 HOH A2513 SITE 1 AE6 2 THR A 279 OLA A2416 SITE 1 AE7 6 TYR A 179 PHE A 258 CLR A2402 OLA A2420 SITE 2 AE7 6 OLB A2427 HOH A2564 SITE 1 AE8 9 PHE A 183 PHE A 258 CLR A2403 CLR A2405 SITE 2 AE8 9 OLB A2426 HOH A2505 HOH A2526 HOH A2589 SITE 3 AE8 9 HOH A2624 SITE 1 AE9 5 CYS A 28 TYR A 43 LEU A 54 ARG A 205 SITE 2 AE9 5 OLA A2417 SITE 1 AF1 10 LEU A 58 PHE A 62 THR A 65 PHE A 70 SITE 2 AF1 10 CYS A 71 CLR A2403 CLR A2405 OLA A2406 SITE 3 AF1 10 OLA A2423 HOH A2617 SITE 1 AF2 7 TYR A 43 LEU A 54 GLY A 118 ILE A 125 SITE 2 AF2 7 TRP A 129 PHE A 133 OLA A2422 CRYST1 39.428 179.599 139.847 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.025362 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005568 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007151 0.00000 ATOM 1 N GLY A -1 -20.812 24.252 1.360 1.00 54.10 N ANISOU 1 N GLY A -1 10832 4040 5684 -1647 -973 1064 N ATOM 2 CA GLY A -1 -21.647 23.515 2.292 1.00 74.90 C ANISOU 2 CA GLY A -1 13470 6671 8319 -1446 -903 884 C ATOM 3 C GLY A -1 -22.888 22.946 1.634 1.00 80.99 C ANISOU 3 C GLY A -1 14142 7473 9157 -1097 -822 886 C ATOM 4 O GLY A -1 -23.956 23.561 1.669 1.00 80.63 O ANISOU 4 O GLY A -1 14269 7208 9159 -834 -794 828 O ATOM 5 N ALA A 0 -22.735 21.770 1.028 1.00 81.82 N ANISOU 5 N ALA A 0 13956 7868 9263 -1090 -784 960 N ATOM 6 CA ALA A 0 -23.832 21.131 0.319 1.00 75.16 C ANISOU 6 CA ALA A 0 12992 7103 8461 -791 -732 983 C ATOM 7 C ALA A 0 -25.004 20.878 1.266 1.00 80.28 C ANISOU 7 C ALA A 0 13726 7631 9145 -520 -676 810 C ATOM 8 O ALA A 0 -24.803 20.652 2.464 1.00114.82 O ANISOU 8 O ALA A 0 18161 11974 13491 -594 -653 667 O ATOM 9 CB ALA A 0 -23.371 19.815 -0.298 1.00 70.27 C ANISOU 9 CB ALA A 0 12061 6831 7806 -851 -695 1061 C ATOM 10 N PRO A 1 -26.235 20.921 0.757 1.00105.49 N ANISOU 10 N PRO A 1 16904 10778 12401 -201 -653 827 N ATOM 11 CA PRO A 1 -27.416 20.702 1.611 1.00 45.88 C ANISOU 11 CA PRO A 1 9385 3145 4903 96 -580 676 C ATOM 12 C PRO A 1 -27.286 19.420 2.414 1.00 49.12 C ANISOU 12 C PRO A 1 9652 3733 5279 56 -531 571 C ATOM 13 O PRO A 1 -26.987 18.352 1.856 1.00 49.80 O ANISOU 13 O PRO A 1 9478 4105 5338 -14 -538 635 O ATOM 14 CB PRO A 1 -28.568 20.612 0.601 1.00 59.97 C ANISOU 14 CB PRO A 1 11038 4991 6758 397 -587 782 C ATOM 15 CG PRO A 1 -28.103 21.427 -0.561 1.00 76.91 C ANISOU 15 CG PRO A 1 13237 7092 8895 279 -663 954 C ATOM 16 CD PRO A 1 -26.607 21.261 -0.631 1.00 49.53 C ANISOU 16 CD PRO A 1 9754 3723 5341 -96 -693 996 C ATOM 17 N PRO A 2 -27.504 19.487 3.729 1.00 57.52 N ANISOU 17 N PRO A 2 10831 4688 6337 98 -466 388 N ATOM 18 CA PRO A 2 -27.263 18.300 4.568 1.00 39.66 C ANISOU 18 CA PRO A 2 8363 2664 4041 18 -415 270 C ATOM 19 C PRO A 2 -28.115 17.113 4.178 1.00 36.03 C ANISOU 19 C PRO A 2 7544 2511 3635 229 -366 267 C ATOM 20 O PRO A 2 -27.691 15.966 4.366 1.00 36.23 O ANISOU 20 O PRO A 2 7323 2808 3633 113 -350 237 O ATOM 21 CB PRO A 2 -27.601 18.791 5.987 1.00 41.29 C ANISOU 21 CB PRO A 2 8812 2654 4222 86 -345 76 C ATOM 22 CG PRO A 2 -27.637 20.297 5.898 1.00 55.53 C ANISOU 22 CG PRO A 2 10879 4196 6023 104 -369 92 C ATOM 23 CD PRO A 2 -28.063 20.612 4.496 1.00 56.76 C ANISOU 23 CD PRO A 2 10970 4340 6257 244 -414 267 C ATOM 24 N ILE A 3 -29.302 17.347 3.615 1.00 39.37 N ANISOU 24 N ILE A 3 7929 2896 4134 529 -352 311 N ATOM 25 CA ILE A 3 -30.178 16.232 3.276 1.00 47.56 C ANISOU 25 CA ILE A 3 8630 4221 5218 703 -329 314 C ATOM 26 C ILE A 3 -29.575 15.332 2.198 1.00 48.97 C ANISOU 26 C ILE A 3 8598 4657 5350 540 -397 425 C ATOM 27 O ILE A 3 -30.017 14.192 2.035 1.00 37.71 O ANISOU 27 O ILE A 3 6909 3484 3935 595 -386 404 O ATOM 28 CB ILE A 3 -31.557 16.766 2.840 1.00 48.83 C ANISOU 28 CB ILE A 3 8783 4296 5473 1046 -322 377 C ATOM 29 CG1 ILE A 3 -32.605 15.651 2.886 1.00 60.51 C ANISOU 29 CG1 ILE A 3 9921 6060 7009 1220 -290 353 C ATOM 30 CG2 ILE A 3 -31.468 17.337 1.451 1.00 53.04 C ANISOU 30 CG2 ILE A 3 9382 4767 6004 1041 -433 571 C ATOM 31 CD1 ILE A 3 -33.903 15.999 2.190 1.00 95.47 C ANISOU 31 CD1 ILE A 3 14253 10491 11532 1521 -322 476 C ATOM 32 N MET A 4 -28.565 15.804 1.459 1.00 47.14 N ANISOU 32 N MET A 4 8487 4365 5058 335 -459 546 N ATOM 33 CA MET A 4 -28.001 14.990 0.381 1.00 33.30 C ANISOU 33 CA MET A 4 6558 2854 3242 210 -495 653 C ATOM 34 C MET A 4 -27.101 13.882 0.919 1.00 34.29 C ANISOU 34 C MET A 4 6512 3194 3323 24 -444 581 C ATOM 35 O MET A 4 -27.318 12.700 0.629 1.00 29.42 O ANISOU 35 O MET A 4 5675 2810 2694 65 -425 556 O ATOM 36 CB MET A 4 -27.244 15.881 -0.609 1.00 31.06 C ANISOU 36 CB MET A 4 6446 2453 2901 66 -558 829 C ATOM 37 CG MET A 4 -28.158 16.847 -1.332 1.00 33.18 C ANISOU 37 CG MET A 4 6860 2535 3210 266 -621 935 C ATOM 38 SD MET A 4 -27.319 17.843 -2.580 1.00 41.23 S ANISOU 38 SD MET A 4 8002 3483 4182 86 -680 1130 S ATOM 39 CE MET A 4 -26.834 16.576 -3.767 1.00 48.38 C ANISOU 39 CE MET A 4 8640 4764 4979 -10 -669 1206 C ATOM 40 N GLY A 5 -26.069 14.245 1.690 1.00 29.85 N ANISOU 40 N GLY A 5 6057 2549 2734 -191 -433 559 N ATOM 41 CA GLY A 5 -25.251 13.219 2.328 1.00 25.99 C ANISOU 41 CA GLY A 5 5394 2263 2217 -347 -390 504 C ATOM 42 C GLY A 5 -26.060 12.386 3.299 1.00 24.67 C ANISOU 42 C GLY A 5 5096 2183 2093 -204 -336 344 C ATOM 43 O GLY A 5 -25.842 11.170 3.436 1.00 28.14 O ANISOU 43 O GLY A 5 5324 2843 2525 -231 -300 313 O ATOM 44 N ASER A 6 -27.004 13.025 3.991 0.53 27.48 N ANISOU 44 N ASER A 6 5585 2364 2494 -40 -318 248 N ATOM 45 N BSER A 6 -27.003 13.023 3.996 0.47 27.97 N ANISOU 45 N BSER A 6 5647 2426 2556 -41 -318 248 N ATOM 46 CA ASER A 6 -27.912 12.289 4.861 0.53 27.49 C ANISOU 46 CA ASER A 6 5451 2460 2534 117 -252 116 C ATOM 47 CA BSER A 6 -27.910 12.276 4.860 0.47 25.73 C ANISOU 47 CA BSER A 6 5226 2239 2311 117 -251 116 C ATOM 48 C ASER A 6 -28.673 11.228 4.079 0.53 23.49 C ANISOU 48 C ASER A 6 4693 2170 2062 253 -256 149 C ATOM 49 C BSER A 6 -28.659 11.215 4.069 0.47 23.47 C ANISOU 49 C BSER A 6 4688 2170 2059 250 -256 150 C ATOM 50 O ASER A 6 -28.847 10.104 4.559 0.53 22.00 O ANISOU 50 O ASER A 6 4318 2160 1882 254 -218 82 O ATOM 51 O BSER A 6 -28.813 10.082 4.534 0.47 31.44 O ANISOU 51 O BSER A 6 5511 3360 3076 248 -220 85 O ATOM 52 CB ASER A 6 -28.878 13.262 5.542 0.53 35.49 C ANISOU 52 CB ASER A 6 6653 3247 3586 317 -208 33 C ATOM 53 CB BSER A 6 -28.893 13.229 5.540 0.47 36.45 C ANISOU 53 CB BSER A 6 6766 3375 3708 319 -207 32 C ATOM 54 OG ASER A 6 -29.814 12.576 6.352 0.53 26.12 O ANISOU 54 OG ASER A 6 5315 2174 2434 481 -126 -74 O ATOM 55 OG BSER A 6 -28.208 14.181 6.328 0.47 37.83 O ANISOU 55 OG BSER A 6 7223 3323 3829 178 -210 -22 O ATOM 56 N SER A 7 -29.121 11.564 2.865 1.00 24.23 N ANISOU 56 N SER A 7 4795 2245 2167 349 -315 258 N ATOM 57 CA SER A 7 -29.869 10.611 2.048 1.00 26.26 C ANISOU 57 CA SER A 7 4845 2697 2435 449 -349 294 C ATOM 58 C SER A 7 -29.046 9.372 1.736 1.00 24.64 C ANISOU 58 C SER A 7 4501 2694 2166 291 -340 292 C ATOM 59 O SER A 7 -29.574 8.252 1.778 1.00 20.53 O ANISOU 59 O SER A 7 3807 2333 1659 334 -336 244 O ATOM 60 CB SER A 7 -30.323 11.271 0.742 1.00 30.24 C ANISOU 60 CB SER A 7 5414 3144 2931 542 -435 431 C ATOM 61 OG SER A 7 -31.213 12.337 1.020 1.00 38.08 O ANISOU 61 OG SER A 7 6516 3952 4002 738 -436 444 O ATOM 62 N VAL A 8 -27.760 9.552 1.394 1.00 21.52 N ANISOU 62 N VAL A 8 4180 2292 1704 112 -333 356 N ATOM 63 CA VAL A 8 -26.896 8.407 1.105 1.00 20.18 C ANISOU 63 CA VAL A 8 3882 2308 1476 -6 -296 365 C ATOM 64 C VAL A 8 -26.710 7.559 2.361 1.00 21.93 C ANISOU 64 C VAL A 8 3989 2610 1735 -47 -239 257 C ATOM 65 O VAL A 8 -26.875 6.337 2.338 1.00 17.75 O ANISOU 65 O VAL A 8 3315 2225 1203 -23 -217 215 O ATOM 66 CB VAL A 8 -25.542 8.877 0.542 1.00 21.65 C ANISOU 66 CB VAL A 8 4145 2488 1594 -177 -282 485 C ATOM 67 CG1 VAL A 8 -24.552 7.708 0.458 1.00 20.06 C ANISOU 67 CG1 VAL A 8 3796 2479 1346 -271 -210 497 C ATOM 68 CG2 VAL A 8 -25.730 9.545 -0.832 1.00 24.44 C ANISOU 68 CG2 VAL A 8 4604 2794 1889 -140 -334 609 C ATOM 69 N TYR A 9 -26.365 8.207 3.478 1.00 19.29 N ANISOU 69 N TYR A 9 3740 2168 1422 -119 -223 213 N ATOM 70 CA TYR A 9 -26.176 7.493 4.737 1.00 18.34 C ANISOU 70 CA TYR A 9 3529 2121 1317 -170 -178 123 C ATOM 71 C TYR A 9 -27.432 6.718 5.120 1.00 17.65 C ANISOU 71 C TYR A 9 3320 2105 1280 -11 -158 32 C ATOM 72 O TYR A 9 -27.367 5.526 5.457 1.00 17.09 O ANISOU 72 O TYR A 9 3102 2176 1216 -32 -130 0 O ATOM 73 CB TYR A 9 -25.775 8.495 5.831 1.00 19.40 C ANISOU 73 CB TYR A 9 3830 2101 1439 -271 -183 82 C ATOM 74 CG TYR A 9 -25.857 7.915 7.236 1.00 19.48 C ANISOU 74 CG TYR A 9 3785 2169 1448 -297 -143 -23 C ATOM 75 CD1 TYR A 9 -25.043 6.842 7.613 1.00 17.64 C ANISOU 75 CD1 TYR A 9 3392 2108 1201 -414 -129 0 C ATOM 76 CD2 TYR A 9 -26.771 8.403 8.151 1.00 19.58 C ANISOU 76 CD2 TYR A 9 3900 2072 1469 -184 -109 -135 C ATOM 77 CE1 TYR A 9 -25.120 6.295 8.885 1.00 17.22 C ANISOU 77 CE1 TYR A 9 3292 2114 1138 -444 -102 -78 C ATOM 78 CE2 TYR A 9 -26.862 7.864 9.439 1.00 20.18 C ANISOU 78 CE2 TYR A 9 3934 2213 1520 -212 -64 -225 C ATOM 79 CZ TYR A 9 -26.042 6.791 9.784 1.00 18.43 C ANISOU 79 CZ TYR A 9 3555 2166 1282 -350 -70 -192 C ATOM 80 OH TYR A 9 -26.111 6.256 11.041 1.00 18.20 O ANISOU 80 OH TYR A 9 3490 2205 1219 -387 -37 -262 O ATOM 81 N ILE A 10 -28.595 7.372 5.053 1.00 18.62 N ANISOU 81 N ILE A 10 3495 2135 1446 154 -170 10 N ATOM 82 CA ILE A 10 -29.834 6.725 5.472 1.00 18.75 C ANISOU 82 CA ILE A 10 3368 2237 1519 298 -147 -49 C ATOM 83 C ILE A 10 -30.184 5.562 4.549 1.00 18.62 C ANISOU 83 C ILE A 10 3190 2380 1503 307 -194 -11 C ATOM 84 O ILE A 10 -30.625 4.501 5.002 1.00 18.18 O ANISOU 84 O ILE A 10 2989 2444 1473 310 -178 -55 O ATOM 85 CB ILE A 10 -30.977 7.760 5.534 1.00 21.64 C ANISOU 85 CB ILE A 10 3805 2478 1939 496 -141 -51 C ATOM 86 CG1 ILE A 10 -30.720 8.763 6.670 1.00 21.17 C ANISOU 86 CG1 ILE A 10 3942 2241 1861 495 -74 -129 C ATOM 87 CG2 ILE A 10 -32.313 7.066 5.731 1.00 20.75 C ANISOU 87 CG2 ILE A 10 3491 2499 1894 645 -126 -65 C ATOM 88 CD1 ILE A 10 -31.723 9.891 6.723 1.00 23.27 C ANISOU 88 CD1 ILE A 10 4323 2341 2176 720 -42 -131 C ATOM 89 N THR A 11 -30.020 5.747 3.239 1.00 17.86 N ANISOU 89 N THR A 11 3139 2279 1367 303 -258 72 N ATOM 90 CA THR A 11 -30.342 4.656 2.319 1.00 17.38 C ANISOU 90 CA THR A 11 2976 2351 1276 298 -311 94 C ATOM 91 C THR A 11 -29.451 3.452 2.559 1.00 19.26 C ANISOU 91 C THR A 11 3158 2684 1477 181 -261 54 C ATOM 92 O THR A 11 -29.915 2.304 2.515 1.00 15.99 O ANISOU 92 O THR A 11 2644 2364 1068 180 -279 20 O ATOM 93 CB THR A 11 -30.205 5.134 0.877 1.00 18.25 C ANISOU 93 CB THR A 11 3183 2437 1315 303 -381 190 C ATOM 94 OG1 THR A 11 -31.056 6.275 0.689 1.00 19.70 O ANISOU 94 OG1 THR A 11 3418 2521 1546 430 -433 245 O ATOM 95 CG2 THR A 11 -30.610 4.016 -0.107 1.00 18.57 C ANISOU 95 CG2 THR A 11 3162 2602 1292 289 -449 197 C ATOM 96 N VAL A 12 -28.157 3.692 2.771 1.00 17.20 N ANISOU 96 N VAL A 12 2957 2398 1181 80 -204 75 N ATOM 97 CA VAL A 12 -27.241 2.592 3.050 1.00 14.79 C ANISOU 97 CA VAL A 12 2582 2185 854 -4 -145 62 C ATOM 98 C VAL A 12 -27.635 1.905 4.351 1.00 14.59 C ANISOU 98 C VAL A 12 2455 2199 890 -5 -119 -14 C ATOM 99 O VAL A 12 -27.668 0.670 4.431 1.00 14.73 O ANISOU 99 O VAL A 12 2390 2294 912 -15 -105 -39 O ATOM 100 CB VAL A 12 -25.786 3.100 3.085 1.00 15.00 C ANISOU 100 CB VAL A 12 2655 2201 843 -116 -96 135 C ATOM 101 CG1 VAL A 12 -24.837 2.047 3.722 1.00 18.10 C ANISOU 101 CG1 VAL A 12 2940 2695 1241 -184 -29 138 C ATOM 102 CG2 VAL A 12 -25.304 3.509 1.652 1.00 15.82 C ANISOU 102 CG2 VAL A 12 2841 2305 866 -123 -100 230 C ATOM 103 N GLU A 13 -27.967 2.689 5.384 1.00 14.37 N ANISOU 103 N GLU A 13 2452 2107 900 6 -108 -51 N ATOM 104 CA GLU A 13 -28.365 2.084 6.654 1.00 13.90 C ANISOU 104 CA GLU A 13 2305 2098 878 4 -71 -116 C ATOM 105 C GLU A 13 -29.592 1.207 6.471 1.00 15.39 C ANISOU 105 C GLU A 13 2377 2360 1109 82 -97 -139 C ATOM 106 O GLU A 13 -29.658 0.095 7.000 1.00 13.39 O ANISOU 106 O GLU A 13 2030 2186 873 43 -79 -159 O ATOM 107 CB GLU A 13 -28.658 3.168 7.696 1.00 14.69 C ANISOU 107 CB GLU A 13 2493 2106 984 28 -42 -164 C ATOM 108 CG GLU A 13 -27.420 3.905 8.243 1.00 15.02 C ANISOU 108 CG GLU A 13 2656 2076 974 -109 -36 -150 C ATOM 109 CD GLU A 13 -26.735 3.152 9.385 1.00 23.03 C ANISOU 109 CD GLU A 13 3605 3180 1967 -226 -10 -164 C ATOM 110 OE1 GLU A 13 -26.588 3.727 10.490 1.00 19.91 O ANISOU 110 OE1 GLU A 13 3303 2731 1529 -286 2 -212 O ATOM 111 OE2 GLU A 13 -26.328 1.987 9.181 1.00 20.42 O ANISOU 111 OE2 GLU A 13 3145 2962 1650 -256 -4 -125 O ATOM 112 N LEU A 14 -30.586 1.698 5.734 1.00 14.68 N ANISOU 112 N LEU A 14 2288 2250 1041 183 -150 -119 N ATOM 113 CA LEU A 14 -31.791 0.899 5.502 1.00 14.87 C ANISOU 113 CA LEU A 14 2180 2364 1107 228 -201 -115 C ATOM 114 C LEU A 14 -31.481 -0.376 4.728 1.00 14.61 C ANISOU 114 C LEU A 14 2132 2386 1032 144 -249 -110 C ATOM 115 O LEU A 14 -32.020 -1.438 5.048 1.00 17.18 O ANISOU 115 O LEU A 14 2362 2780 1387 107 -267 -126 O ATOM 116 CB LEU A 14 -32.843 1.739 4.777 1.00 19.67 C ANISOU 116 CB LEU A 14 2777 2952 1744 350 -268 -62 C ATOM 117 CG LEU A 14 -33.389 2.872 5.661 1.00 20.81 C ANISOU 117 CG LEU A 14 2934 3031 1942 479 -199 -76 C ATOM 118 CD1 LEU A 14 -34.317 3.799 4.842 1.00 22.21 C ANISOU 118 CD1 LEU A 14 3109 3171 2157 630 -263 2 C ATOM 119 CD2 LEU A 14 -34.091 2.314 6.884 1.00 21.96 C ANISOU 119 CD2 LEU A 14 2938 3268 2136 504 -126 -116 C ATOM 120 N ALA A 15 -30.600 -0.307 3.720 1.00 14.71 N ANISOU 120 N ALA A 15 2256 2364 969 113 -259 -86 N ATOM 121 CA ALA A 15 -30.208 -1.532 3.022 1.00 15.71 C ANISOU 121 CA ALA A 15 2411 2521 1037 56 -273 -98 C ATOM 122 C ALA A 15 -29.552 -2.524 3.971 1.00 13.14 C ANISOU 122 C ALA A 15 2038 2217 739 2 -197 -129 C ATOM 123 O ALA A 15 -29.825 -3.724 3.906 1.00 15.52 O ANISOU 123 O ALA A 15 2321 2535 1039 -32 -220 -155 O ATOM 124 CB ALA A 15 -29.261 -1.226 1.857 1.00 14.29 C ANISOU 124 CB ALA A 15 2362 2311 756 52 -256 -61 C ATOM 125 N ILE A 16 -28.692 -2.047 4.864 1.00 12.63 N ANISOU 125 N ILE A 16 1962 2144 693 -18 -121 -119 N ATOM 126 CA ILE A 16 -28.043 -2.958 5.802 1.00 14.04 C ANISOU 126 CA ILE A 16 2084 2356 896 -68 -62 -123 C ATOM 127 C ILE A 16 -29.070 -3.559 6.747 1.00 12.91 C ANISOU 127 C ILE A 16 1844 2250 813 -80 -81 -156 C ATOM 128 O ILE A 16 -29.005 -4.749 7.082 1.00 14.62 O ANISOU 128 O ILE A 16 2024 2484 1047 -118 -72 -159 O ATOM 129 CB ILE A 16 -26.930 -2.220 6.570 1.00 12.91 C ANISOU 129 CB ILE A 16 1944 2213 749 -115 -6 -87 C ATOM 130 CG1 ILE A 16 -25.800 -1.844 5.607 1.00 13.93 C ANISOU 130 CG1 ILE A 16 2134 2334 823 -123 23 -22 C ATOM 131 CG2 ILE A 16 -26.434 -3.072 7.761 1.00 15.68 C ANISOU 131 CG2 ILE A 16 2214 2614 1129 -168 33 -75 C ATOM 132 CD1 ILE A 16 -24.841 -0.860 6.232 1.00 18.32 C ANISOU 132 CD1 ILE A 16 2697 2888 1374 -204 42 33 C ATOM 133 N ALA A 17 -30.027 -2.742 7.212 1.00 12.32 N ANISOU 133 N ALA A 17 1727 2183 771 -40 -96 -171 N ATOM 134 CA ALA A 17 -31.033 -3.252 8.148 1.00 14.03 C ANISOU 134 CA ALA A 17 1829 2463 1040 -46 -92 -184 C ATOM 135 C ALA A 17 -31.852 -4.372 7.518 1.00 17.29 C ANISOU 135 C ALA A 17 2187 2909 1474 -80 -169 -172 C ATOM 136 O ALA A 17 -32.143 -5.382 8.168 1.00 16.45 O ANISOU 136 O ALA A 17 2011 2842 1398 -143 -166 -165 O ATOM 137 CB ALA A 17 -31.947 -2.109 8.616 1.00 14.53 C ANISOU 137 CB ALA A 17 1858 2533 1130 44 -70 -194 C ATOM 138 N AVAL A 18 -32.240 -4.198 6.258 0.88 13.46 N ANISOU 138 N AVAL A 18 1747 2405 964 -57 -253 -162 N ATOM 139 N BVAL A 18 -32.222 -4.238 6.243 0.12 14.02 N ANISOU 139 N BVAL A 18 1820 2475 1033 -60 -253 -163 N ATOM 140 CA AVAL A 18 -33.011 -5.233 5.567 0.88 15.37 C ANISOU 140 CA AVAL A 18 1970 2667 1202 -124 -357 -154 C ATOM 141 CA BVAL A 18 -33.063 -5.281 5.658 0.12 14.19 C ANISOU 141 CA BVAL A 18 1809 2523 1058 -127 -356 -153 C ATOM 142 C AVAL A 18 -32.230 -6.537 5.555 0.88 14.75 C ANISOU 142 C AVAL A 18 1978 2534 1093 -198 -336 -181 C ATOM 143 C BVAL A 18 -32.268 -6.566 5.433 0.12 25.73 C ANISOU 143 C BVAL A 18 3376 3922 2479 -201 -346 -182 C ATOM 144 O AVAL A 18 -32.749 -7.607 5.901 0.88 14.21 O ANISOU 144 O AVAL A 18 1868 2475 1056 -282 -375 -176 O ATOM 145 O BVAL A 18 -32.819 -7.668 5.547 0.12 23.46 O ANISOU 145 O BVAL A 18 3068 3636 2211 -288 -402 -180 O ATOM 146 CB AVAL A 18 -33.351 -4.776 4.136 0.88 14.99 C ANISOU 146 CB AVAL A 18 1998 2603 1095 -99 -460 -137 C ATOM 147 CB BVAL A 18 -33.738 -4.788 4.362 0.12 26.18 C ANISOU 147 CB BVAL A 18 3360 4048 2541 -101 -472 -126 C ATOM 148 CG1AVAL A 18 -33.900 -5.946 3.299 0.88 19.00 C ANISOU 148 CG1AVAL A 18 2553 3108 1558 -205 -586 -143 C ATOM 149 CG1BVAL A 18 -34.532 -3.516 4.628 0.12 15.78 C ANISOU 149 CG1BVAL A 18 1935 2778 1281 7 -469 -81 C ATOM 150 CG2AVAL A 18 -34.339 -3.614 4.173 0.88 21.81 C ANISOU 150 CG2AVAL A 18 2753 3522 2013 -8 -495 -85 C ATOM 151 CG2BVAL A 18 -32.722 -4.579 3.251 0.12 14.98 C ANISOU 151 CG2BVAL A 18 2123 2551 1017 -84 -466 -147 C ATOM 152 N LEU A 19 -30.971 -6.461 5.131 1.00 13.29 N ANISOU 152 N LEU A 19 1912 2288 848 -164 -270 -197 N ATOM 153 CA LEU A 19 -30.153 -7.659 4.985 1.00 16.72 C ANISOU 153 CA LEU A 19 2441 2658 1252 -187 -229 -215 C ATOM 154 C LEU A 19 -29.831 -8.282 6.341 1.00 13.66 C ANISOU 154 C LEU A 19 1968 2288 934 -218 -165 -192 C ATOM 155 O LEU A 19 -29.748 -9.508 6.460 1.00 18.58 O ANISOU 155 O LEU A 19 2636 2857 1568 -257 -168 -195 O ATOM 156 CB LEU A 19 -28.858 -7.316 4.257 1.00 13.14 C ANISOU 156 CB LEU A 19 2095 2171 727 -118 -146 -210 C ATOM 157 CG LEU A 19 -29.073 -6.902 2.799 1.00 13.91 C ANISOU 157 CG LEU A 19 2315 2246 725 -95 -202 -227 C ATOM 158 CD1 LEU A 19 -27.808 -6.252 2.247 1.00 16.69 C ANISOU 158 CD1 LEU A 19 2731 2599 1013 -28 -101 -193 C ATOM 159 CD2 LEU A 19 -29.453 -8.158 2.008 1.00 15.32 C ANISOU 159 CD2 LEU A 19 2635 2353 834 -137 -264 -282 C ATOM 160 N ALA A 20 -29.624 -7.450 7.362 1.00 12.75 N ANISOU 160 N ALA A 20 1756 2235 854 -204 -112 -167 N ATOM 161 CA ALA A 20 -29.345 -7.989 8.693 1.00 14.19 C ANISOU 161 CA ALA A 20 1863 2449 1079 -246 -63 -136 C ATOM 162 C ALA A 20 -30.540 -8.768 9.208 1.00 19.33 C ANISOU 162 C ALA A 20 2438 3129 1776 -316 -113 -129 C ATOM 163 O ALA A 20 -30.391 -9.851 9.788 1.00 16.67 O ANISOU 163 O ALA A 20 2096 2771 1465 -370 -104 -98 O ATOM 164 CB ALA A 20 -29.011 -6.865 9.671 1.00 12.92 C ANISOU 164 CB ALA A 20 1648 2346 915 -237 -12 -124 C ATOM 165 N ILE A 21 -31.740 -8.235 8.992 1.00 13.84 N ANISOU 165 N ILE A 21 1674 2487 1099 -318 -168 -137 N ATOM 166 CA ILE A 21 -32.952 -8.935 9.419 1.00 17.83 C ANISOU 166 CA ILE A 21 2070 3051 1654 -400 -221 -103 C ATOM 167 C ILE A 21 -33.135 -10.239 8.649 1.00 17.34 C ANISOU 167 C ILE A 21 2099 2904 1587 -494 -314 -104 C ATOM 168 O ILE A 21 -33.358 -11.301 9.246 1.00 18.55 O ANISOU 168 O ILE A 21 2233 3042 1774 -590 -326 -68 O ATOM 169 CB ILE A 21 -34.170 -8.011 9.282 1.00 18.58 C ANISOU 169 CB ILE A 21 2041 3241 1777 -357 -254 -86 C ATOM 170 CG1 ILE A 21 -33.996 -6.831 10.247 1.00 21.85 C ANISOU 170 CG1 ILE A 21 2409 3705 2187 -260 -141 -98 C ATOM 171 CG2 ILE A 21 -35.463 -8.774 9.587 1.00 21.42 C ANISOU 171 CG2 ILE A 21 2252 3691 2194 -458 -317 -20 C ATOM 172 CD1 ILE A 21 -34.936 -5.663 9.982 1.00 19.22 C ANISOU 172 CD1 ILE A 21 1999 3427 1877 -151 -143 -89 C ATOM 173 N LEU A 22 -33.071 -10.184 7.311 1.00 17.82 N ANISOU 173 N LEU A 22 2283 2897 1592 -479 -384 -145 N ATOM 174 CA LEU A 22 -33.368 -11.375 6.514 1.00 16.63 C ANISOU 174 CA LEU A 22 2262 2648 1409 -583 -487 -165 C ATOM 175 C LEU A 22 -32.384 -12.496 6.804 1.00 17.27 C ANISOU 175 C LEU A 22 2478 2600 1484 -584 -420 -180 C ATOM 176 O LEU A 22 -32.777 -13.653 6.976 1.00 19.08 O ANISOU 176 O LEU A 22 2760 2754 1734 -697 -479 -165 O ATOM 177 CB LEU A 22 -33.344 -11.041 5.018 1.00 17.03 C ANISOU 177 CB LEU A 22 2458 2649 1365 -557 -562 -216 C ATOM 178 CG LEU A 22 -34.499 -10.168 4.543 1.00 23.64 C ANISOU 178 CG LEU A 22 3173 3600 2210 -573 -674 -177 C ATOM 179 CD1 LEU A 22 -34.311 -9.836 3.075 1.00 28.46 C ANISOU 179 CD1 LEU A 22 3952 4159 2703 -547 -745 -218 C ATOM 180 CD2 LEU A 22 -35.821 -10.880 4.783 1.00 34.49 C ANISOU 180 CD2 LEU A 22 4425 5038 3641 -733 -807 -116 C ATOM 181 N GLY A 23 -31.094 -12.177 6.840 1.00 17.79 N ANISOU 181 N GLY A 23 2600 2636 1525 -461 -301 -193 N ATOM 182 CA GLY A 23 -30.108 -13.227 7.015 1.00 19.51 C ANISOU 182 CA GLY A 23 2936 2735 1743 -424 -229 -187 C ATOM 183 C GLY A 23 -30.194 -13.861 8.383 1.00 16.76 C ANISOU 183 C GLY A 23 2483 2409 1475 -485 -208 -115 C ATOM 184 O GLY A 23 -30.103 -15.083 8.522 1.00 16.62 O ANISOU 184 O GLY A 23 2567 2269 1477 -526 -219 -98 O ATOM 185 N ASN A 24 -30.401 -13.050 9.408 1.00 15.04 N ANISOU 185 N ASN A 24 2085 2335 1294 -494 -177 -70 N ATOM 186 CA ASN A 24 -30.387 -13.607 10.749 1.00 16.27 C ANISOU 186 CA ASN A 24 2152 2528 1501 -551 -146 7 C ATOM 187 C ASN A 24 -31.713 -14.240 11.136 1.00 18.57 C ANISOU 187 C ASN A 24 2378 2846 1833 -697 -227 43 C ATOM 188 O ASN A 24 -31.715 -15.181 11.931 1.00 16.95 O ANISOU 188 O ASN A 24 2169 2609 1663 -770 -224 112 O ATOM 189 CB ASN A 24 -29.953 -12.529 11.733 1.00 17.09 C ANISOU 189 CB ASN A 24 2130 2768 1596 -507 -73 35 C ATOM 190 CG ASN A 24 -28.478 -12.242 11.598 1.00 18.77 C ANISOU 190 CG ASN A 24 2389 2957 1785 -408 -5 50 C ATOM 191 OD1 ASN A 24 -27.657 -13.085 11.962 1.00 18.10 O ANISOU 191 OD1 ASN A 24 2332 2824 1722 -386 29 115 O ATOM 192 ND2 ASN A 24 -28.131 -11.105 10.977 1.00 14.17 N ANISOU 192 ND2 ASN A 24 1815 2406 1164 -346 13 7 N ATOM 193 N VAL A 25 -32.836 -13.775 10.586 1.00 16.54 N ANISOU 193 N VAL A 25 2056 2654 1575 -749 -305 19 N ATOM 194 CA VAL A 25 -34.064 -14.573 10.684 1.00 22.22 C ANISOU 194 CA VAL A 25 2720 3389 2335 -915 -407 72 C ATOM 195 C VAL A 25 -33.850 -15.961 10.085 1.00 19.73 C ANISOU 195 C VAL A 25 2617 2870 2011 -1004 -483 57 C ATOM 196 O VAL A 25 -34.303 -16.966 10.641 1.00 21.60 O ANISOU 196 O VAL A 25 2853 3064 2289 -1145 -527 128 O ATOM 197 CB VAL A 25 -35.247 -13.837 10.023 1.00 24.77 C ANISOU 197 CB VAL A 25 2926 3825 2661 -947 -495 69 C ATOM 198 CG1 VAL A 25 -36.389 -14.804 9.699 1.00 24.08 C ANISOU 198 CG1 VAL A 25 2819 3726 2603 -1151 -646 127 C ATOM 199 CG2 VAL A 25 -35.756 -12.713 10.955 1.00 22.04 C ANISOU 199 CG2 VAL A 25 2356 3675 2345 -872 -404 111 C ATOM 200 N LEU A 26 -33.147 -16.046 8.946 1.00 21.96 N ANISOU 200 N LEU A 26 3103 3011 2229 -921 -489 -33 N ATOM 201 CA LEU A 26 -32.886 -17.350 8.332 1.00 24.06 C ANISOU 201 CA LEU A 26 3626 3050 2466 -976 -541 -69 C ATOM 202 C LEU A 26 -32.050 -18.249 9.248 1.00 19.77 C ANISOU 202 C LEU A 26 3137 2402 1972 -934 -450 -8 C ATOM 203 O LEU A 26 -32.273 -19.465 9.325 1.00 22.21 O ANISOU 203 O LEU A 26 3591 2547 2302 -1043 -509 16 O ATOM 204 CB LEU A 26 -32.186 -17.144 6.991 1.00 26.36 C ANISOU 204 CB LEU A 26 4129 3232 2656 -854 -521 -180 C ATOM 205 CG LEU A 26 -32.011 -18.356 6.088 1.00 47.00 C ANISOU 205 CG LEU A 26 7066 5592 5198 -892 -571 -255 C ATOM 206 CD1 LEU A 26 -33.377 -18.898 5.672 1.00 28.62 C ANISOU 206 CD1 LEU A 26 4792 3229 2852 -1144 -777 -257 C ATOM 207 CD2 LEU A 26 -31.160 -17.980 4.874 1.00 33.97 C ANISOU 207 CD2 LEU A 26 5603 3874 3429 -725 -497 -358 C ATOM 208 N VAL A 27 -31.079 -17.666 9.942 1.00 18.90 N ANISOU 208 N VAL A 27 2921 2381 1880 -786 -321 28 N ATOM 209 CA VAL A 27 -30.295 -18.422 10.917 1.00 20.73 C ANISOU 209 CA VAL A 27 3161 2553 2162 -745 -248 118 C ATOM 210 C VAL A 27 -31.198 -19.004 12.004 1.00 25.84 C ANISOU 210 C VAL A 27 3703 3249 2866 -923 -305 221 C ATOM 211 O VAL A 27 -31.114 -20.194 12.339 1.00 20.87 O ANISOU 211 O VAL A 27 3189 2466 2273 -982 -327 284 O ATOM 212 CB VAL A 27 -29.204 -17.521 11.521 1.00 17.12 C ANISOU 212 CB VAL A 27 2569 2232 1704 -597 -131 158 C ATOM 213 CG1 VAL A 27 -28.619 -18.161 12.792 1.00 17.40 C ANISOU 213 CG1 VAL A 27 2547 2274 1790 -594 -87 288 C ATOM 214 CG2 VAL A 27 -28.124 -17.235 10.484 1.00 17.12 C ANISOU 214 CG2 VAL A 27 2682 2165 1659 -422 -57 96 C ATOM 215 N CYS A 28 -32.051 -18.161 12.599 1.00 22.55 N ANISOU 215 N CYS A 28 3069 3045 2455 -999 -317 249 N ATOM 216 CA CYS A 28 -32.902 -18.629 13.689 1.00 21.97 C ANISOU 216 CA CYS A 28 2867 3059 2423 -1160 -343 363 C ATOM 217 C CYS A 28 -33.875 -19.685 13.194 1.00 24.40 C ANISOU 217 C CYS A 28 3270 3242 2759 -1356 -477 384 C ATOM 218 O CYS A 28 -34.155 -20.668 13.895 1.00 25.54 O ANISOU 218 O CYS A 28 3432 3328 2945 -1491 -506 491 O ATOM 219 CB CYS A 28 -33.665 -17.458 14.310 1.00 19.39 C ANISOU 219 CB CYS A 28 2298 2986 2084 -1169 -303 378 C ATOM 220 SG CYS A 28 -32.608 -16.259 15.127 1.00 21.93 S ANISOU 220 SG CYS A 28 2541 3439 2354 -999 -167 361 S ATOM 221 N TRP A 29 -34.414 -19.478 11.986 1.00 22.81 N ANISOU 221 N TRP A 29 3136 3001 2529 -1394 -573 295 N ATOM 222 CA TRP A 29 -35.346 -20.428 11.385 1.00 23.84 C ANISOU 222 CA TRP A 29 3380 3010 2668 -1614 -735 308 C ATOM 223 C TRP A 29 -34.696 -21.795 11.195 1.00 27.46 C ANISOU 223 C TRP A 29 4144 3164 3125 -1638 -756 297 C ATOM 224 O TRP A 29 -35.321 -22.826 11.468 1.00 29.92 O ANISOU 224 O TRP A 29 4524 3370 3473 -1848 -855 377 O ATOM 225 CB TRP A 29 -35.831 -19.856 10.049 1.00 29.59 C ANISOU 225 CB TRP A 29 4154 3752 3337 -1625 -838 207 C ATOM 226 CG TRP A 29 -37.090 -20.420 9.492 1.00 53.76 C ANISOU 226 CG TRP A 29 7227 6799 6400 -1880 -1032 245 C ATOM 227 CD1 TRP A 29 -37.787 -21.492 9.953 1.00 81.49 C ANISOU 227 CD1 TRP A 29 10747 10257 9960 -2041 -1091 351 C ATOM 228 CD2 TRP A 29 -37.809 -19.931 8.351 1.00104.62 C ANISOU 228 CD2 TRP A 29 13657 13298 12795 -1875 -1126 201 C ATOM 229 NE1 TRP A 29 -38.896 -21.707 9.170 1.00 82.75 N ANISOU 229 NE1 TRP A 29 10898 10441 10101 -2152 -1223 374 N ATOM 230 CE2 TRP A 29 -38.932 -20.761 8.179 1.00 64.02 C ANISOU 230 CE2 TRP A 29 8511 8138 7676 -2054 -1246 288 C ATOM 231 CE3 TRP A 29 -37.611 -18.870 7.460 1.00100.78 C ANISOU 231 CE3 TRP A 29 13166 12879 12247 -1740 -1122 111 C ATOM 232 CZ2 TRP A 29 -39.859 -20.564 7.152 1.00 79.63 C ANISOU 232 CZ2 TRP A 29 10469 10166 9619 -2115 -1369 292 C ATOM 233 CZ3 TRP A 29 -38.530 -18.674 6.438 1.00 54.99 C ANISOU 233 CZ3 TRP A 29 7353 7122 6420 -1788 -1237 117 C ATOM 234 CH2 TRP A 29 -39.640 -19.518 6.295 1.00 81.74 C ANISOU 234 CH2 TRP A 29 10727 10495 9834 -1979 -1362 208 C ATOM 235 N ALA A 30 -33.440 -21.820 10.731 1.00 24.51 N ANISOU 235 N ALA A 30 3957 2643 2713 -1419 -657 210 N ATOM 236 CA ALA A 30 -32.726 -23.081 10.529 1.00 26.03 C ANISOU 236 CA ALA A 30 4454 2531 2907 -1379 -644 198 C ATOM 237 C ALA A 30 -32.533 -23.841 11.834 1.00 26.55 C ANISOU 237 C ALA A 30 4466 2566 3056 -1422 -605 352 C ATOM 238 O ALA A 30 -32.742 -25.057 11.883 1.00 29.15 O ANISOU 238 O ALA A 30 5001 2663 3412 -1547 -677 395 O ATOM 239 CB ALA A 30 -31.368 -22.825 9.874 1.00 25.28 C ANISOU 239 CB ALA A 30 4502 2342 2763 -1094 -505 104 C ATOM 240 N VAL A 31 -32.111 -23.151 12.898 1.00 24.90 N ANISOU 240 N VAL A 31 4009 2576 2877 -1326 -500 439 N ATOM 241 CA VAL A 31 -31.894 -23.833 14.173 1.00 25.50 C ANISOU 241 CA VAL A 31 4033 2644 3011 -1367 -468 600 C ATOM 242 C VAL A 31 -33.208 -24.386 14.715 1.00 34.45 C ANISOU 242 C VAL A 31 5093 3818 4178 -1657 -580 705 C ATOM 243 O VAL A 31 -33.268 -25.514 15.219 1.00 30.37 O ANISOU 243 O VAL A 31 4697 3137 3707 -1768 -620 816 O ATOM 244 CB VAL A 31 -31.224 -22.876 15.178 1.00 24.58 C ANISOU 244 CB VAL A 31 3676 2776 2887 -1233 -350 664 C ATOM 245 CG1 VAL A 31 -31.029 -23.561 16.530 1.00 24.41 C ANISOU 245 CG1 VAL A 31 3602 2770 2903 -1290 -330 844 C ATOM 246 CG2 VAL A 31 -29.893 -22.365 14.616 1.00 22.52 C ANISOU 246 CG2 VAL A 31 3470 2484 2602 -974 -252 589 C ATOM 247 N TRP A 32 -34.273 -23.593 14.631 1.00 26.49 N ANISOU 247 N TRP A 32 3875 3036 3154 -1779 -627 689 N ATOM 248 CA TRP A 32 -35.583 -24.036 15.086 1.00 35.23 C ANISOU 248 CA TRP A 32 4860 4229 4295 -2058 -727 810 C ATOM 249 C TRP A 32 -36.039 -25.289 14.341 1.00 39.10 C ANISOU 249 C TRP A 32 5608 4454 4795 -2204 -872 789 C ATOM 250 O TRP A 32 -36.625 -26.203 14.937 1.00 40.23 O ANISOU 250 O TRP A 32 5745 4572 4967 -2326 -918 897 O ATOM 251 CB TRP A 32 -36.589 -22.900 14.897 1.00 40.62 C ANISOU 251 CB TRP A 32 5273 5204 4958 -2058 -731 775 C ATOM 252 CG TRP A 32 -38.011 -23.283 15.235 1.00 50.38 C ANISOU 252 CG TRP A 32 6357 6573 6212 -2189 -795 873 C ATOM 253 CD1 TRP A 32 -38.866 -24.030 14.476 1.00 59.24 C ANISOU 253 CD1 TRP A 32 7576 7594 7340 -2345 -944 879 C ATOM 254 CD2 TRP A 32 -38.738 -22.917 16.413 1.00 71.78 C ANISOU 254 CD2 TRP A 32 8806 9542 8927 -2173 -706 983 C ATOM 255 NE1 TRP A 32 -40.075 -24.164 15.116 1.00 63.06 N ANISOU 255 NE1 TRP A 32 7848 8268 7845 -2443 -957 1007 N ATOM 256 CE2 TRP A 32 -40.023 -23.488 16.307 1.00 66.72 C ANISOU 256 CE2 TRP A 32 8095 8948 8309 -2330 -804 1068 C ATOM 257 CE3 TRP A 32 -38.424 -22.168 17.552 1.00 52.82 C ANISOU 257 CE3 TRP A 32 6244 7328 6497 -2039 -552 1013 C ATOM 258 CZ2 TRP A 32 -40.994 -23.328 17.293 1.00 70.54 C ANISOU 258 CZ2 TRP A 32 8343 9661 8797 -2352 -741 1188 C ATOM 259 CZ3 TRP A 32 -39.392 -22.010 18.531 1.00 50.36 C ANISOU 259 CZ3 TRP A 32 5732 7226 6178 -2051 -491 1109 C ATOM 260 CH2 TRP A 32 -40.662 -22.584 18.392 1.00 59.60 C ANISOU 260 CH2 TRP A 32 6823 8441 7380 -2203 -579 1200 C ATOM 261 N LEU A 33 -35.779 -25.349 13.033 1.00 35.02 N ANISOU 261 N LEU A 33 5334 3738 4234 -2179 -941 640 N ATOM 262 CA LEU A 33 -36.336 -26.414 12.208 1.00 37.08 C ANISOU 262 CA LEU A 33 5840 3782 4465 -2302 -1081 594 C ATOM 263 C LEU A 33 -35.516 -27.698 12.244 1.00 42.71 C ANISOU 263 C LEU A 33 6899 4137 5193 -2260 -1066 591 C ATOM 264 O LEU A 33 -36.090 -28.786 12.144 1.00 46.42 O ANISOU 264 O LEU A 33 7511 4464 5661 -2400 -1167 622 O ATOM 265 CB LEU A 33 -36.457 -25.943 10.761 1.00 40.02 C ANISOU 265 CB LEU A 33 6341 4113 4750 -2269 -1152 429 C ATOM 266 CG LEU A 33 -37.562 -24.958 10.387 1.00 69.72 C ANISOU 266 CG LEU A 33 9822 8175 8495 -2326 -1216 439 C ATOM 267 CD1 LEU A 33 -37.475 -24.672 8.897 1.00 62.52 C ANISOU 267 CD1 LEU A 33 9106 7168 7482 -2273 -1284 283 C ATOM 268 CD2 LEU A 33 -38.930 -25.520 10.750 1.00 57.90 C ANISOU 268 CD2 LEU A 33 8171 6796 7031 -2529 -1321 580 C ATOM 269 N ASN A 34 -34.196 -27.606 12.352 1.00 33.91 N ANISOU 269 N ASN A 34 5927 2866 4091 -2054 -938 565 N ATOM 270 CA ASN A 34 -33.306 -28.749 12.164 1.00 41.76 C ANISOU 270 CA ASN A 34 7276 3496 5093 -1921 -893 543 C ATOM 271 C ASN A 34 -32.740 -29.191 13.512 1.00 49.87 C ANISOU 271 C ASN A 34 8216 4521 6212 -1863 -807 734 C ATOM 272 O ASN A 34 -31.973 -28.451 14.139 1.00 35.26 O ANISOU 272 O ASN A 34 6152 2869 4378 -1664 -674 785 O ATOM 273 CB ASN A 34 -32.189 -28.387 11.187 1.00 34.85 C ANISOU 273 CB ASN A 34 6600 2488 4153 -1626 -776 382 C ATOM 274 CG ASN A 34 -31.313 -29.575 10.824 1.00 47.23 C ANISOU 274 CG ASN A 34 8571 3653 5721 -1459 -713 344 C ATOM 275 OD1 ASN A 34 -31.416 -30.656 11.412 1.00 48.41 O ANISOU 275 OD1 ASN A 34 8799 3664 5932 -1515 -741 443 O ATOM 276 ND2 ASN A 34 -30.427 -29.370 9.860 1.00 51.64 N ANISOU 276 ND2 ASN A 34 9315 4099 6205 -1191 -596 197 N ATOM 277 N ASER A 35 -33.096 -30.408 13.941 0.54 39.34 N ANISOU 277 N ASER A 35 6803 2942 5204 -1919 -1076 998 N ATOM 278 N BSER A 35 -33.116 -30.401 13.946 0.46 39.35 N ANISOU 278 N BSER A 35 6803 2943 5206 -1920 -1076 999 N ATOM 279 CA ASER A 35 -32.609 -30.908 15.223 0.54 39.33 C ANISOU 279 CA ASER A 35 6824 2908 5211 -1865 -976 1035 C ATOM 280 CA BSER A 35 -32.615 -30.933 15.211 0.46 39.35 C ANISOU 280 CA BSER A 35 6828 2909 5214 -1866 -976 1035 C ATOM 281 C ASER A 35 -31.105 -31.152 15.197 0.54 57.51 C ANISOU 281 C ASER A 35 9214 5225 7413 -1803 -981 1006 C ATOM 282 C BSER A 35 -31.104 -31.112 15.187 0.46 54.53 C ANISOU 282 C BSER A 35 8835 4850 7033 -1803 -983 1005 C ATOM 283 O ASER A 35 -30.453 -31.093 16.246 0.54 40.57 O ANISOU 283 O ASER A 35 7081 3099 5234 -1749 -915 1044 O ATOM 284 O BSER A 35 -30.447 -30.977 16.226 0.46 38.19 O ANISOU 284 O BSER A 35 6779 2806 4927 -1748 -919 1042 O ATOM 285 CB ASER A 35 -33.350 -32.190 15.617 0.54 58.67 C ANISOU 285 CB ASER A 35 9263 5257 7772 -1908 -922 1065 C ATOM 286 CB BSER A 35 -33.290 -32.268 15.535 0.46 58.88 C ANISOU 286 CB BSER A 35 9297 5280 7796 -1909 -927 1061 C ATOM 287 OG ASER A 35 -32.906 -33.311 14.869 0.54 41.29 O ANISOU 287 OG ASER A 35 7132 2987 5569 -1931 -950 1021 O ATOM 288 OG BSER A 35 -34.617 -32.081 15.988 0.46 41.32 O ANISOU 288 OG BSER A 35 6987 3041 5671 -1952 -890 1110 O ATOM 289 N ASN A 36 -30.537 -31.415 14.017 1.00 38.61 N ANISOU 289 N ASN A 36 6878 2823 4968 -1813 -1055 945 N ATOM 290 CA ASN A 36 -29.088 -31.532 13.900 1.00 37.97 C ANISOU 290 CA ASN A 36 6875 2757 4795 -1750 -1059 921 C ATOM 291 C ASN A 36 -28.374 -30.222 14.225 1.00 45.99 C ANISOU 291 C ASN A 36 7887 3886 5703 -1697 -1077 922 C ATOM 292 O ASN A 36 -27.164 -30.232 14.468 1.00 47.28 O ANISOU 292 O ASN A 36 8101 4074 5789 -1641 -1067 924 O ATOM 293 CB ASN A 36 -28.703 -31.988 12.490 1.00 45.36 C ANISOU 293 CB ASN A 36 7874 3660 5700 -1774 -1124 850 C ATOM 294 CG ASN A 36 -29.141 -33.414 12.198 1.00 50.25 C ANISOU 294 CG ASN A 36 8522 4158 6413 -1826 -1087 839 C ATOM 295 OD1 ASN A 36 -29.361 -34.202 13.113 1.00 58.63 O ANISOU 295 OD1 ASN A 36 9571 5153 7553 -1819 -1006 890 O ATOM 296 ND2 ASN A 36 -29.271 -33.747 10.920 1.00 54.45 N ANISOU 296 ND2 ASN A 36 9093 4661 6934 -1881 -1140 774 N ATOM 297 N LEU A 37 -29.087 -29.097 14.230 1.00 36.13 N ANISOU 297 N LEU A 37 6577 2701 4448 -1715 -1098 925 N ATOM 298 CA LEU A 37 -28.497 -27.806 14.573 1.00 34.93 C ANISOU 298 CA LEU A 37 6423 2650 4197 -1672 -1102 922 C ATOM 299 C LEU A 37 -28.802 -27.379 16.004 1.00 34.89 C ANISOU 299 C LEU A 37 6377 2667 4213 -1657 -1002 980 C ATOM 300 O LEU A 37 -28.354 -26.308 16.431 1.00 34.03 O ANISOU 300 O LEU A 37 6270 2639 4022 -1630 -984 977 O ATOM 301 CB LEU A 37 -28.977 -26.723 13.595 1.00 34.41 C ANISOU 301 CB LEU A 37 6323 2642 4109 -1696 -1177 887 C ATOM 302 CG LEU A 37 -28.456 -26.827 12.158 1.00 40.03 C ANISOU 302 CG LEU A 37 7084 3365 4759 -1703 -1281 825 C ATOM 303 CD1 LEU A 37 -29.198 -25.862 11.235 1.00 33.96 C ANISOU 303 CD1 LEU A 37 6261 2647 3997 -1739 -1353 813 C ATOM 304 CD2 LEU A 37 -26.942 -26.580 12.099 1.00 33.20 C ANISOU 304 CD2 LEU A 37 6297 2551 3765 -1640 -1300 792 C ATOM 305 N GLN A 38 -29.546 -28.186 16.757 1.00 39.07 N ANISOU 305 N GLN A 38 6873 3125 4845 -1678 -930 1031 N ATOM 306 CA GLN A 38 -29.961 -27.813 18.111 1.00 45.75 C ANISOU 306 CA GLN A 38 7679 3985 5718 -1669 -825 1088 C ATOM 307 C GLN A 38 -28.967 -28.393 19.110 1.00 36.01 C ANISOU 307 C GLN A 38 6491 2759 4433 -1633 -774 1126 C ATOM 308 O GLN A 38 -29.128 -29.502 19.609 1.00 36.87 O ANISOU 308 O GLN A 38 6599 2798 4612 -1637 -729 1168 O ATOM 309 CB GLN A 38 -31.386 -28.270 18.376 1.00 37.04 C ANISOU 309 CB GLN A 38 6508 2807 4759 -1713 -773 1127 C ATOM 310 CG GLN A 38 -32.379 -27.564 17.480 1.00 37.10 C ANISOU 310 CG GLN A 38 6455 2821 4821 -1752 -819 1110 C ATOM 311 CD GLN A 38 -33.749 -28.211 17.486 1.00 45.30 C ANISOU 311 CD GLN A 38 7428 3781 6003 -1807 -793 1148 C ATOM 312 OE1 GLN A 38 -34.002 -29.154 18.233 1.00 52.12 O ANISOU 312 OE1 GLN A 38 8293 4582 6928 -1812 -730 1183 O ATOM 313 NE2 GLN A 38 -34.641 -27.708 16.642 1.00 50.19 N ANISOU 313 NE2 GLN A 38 7986 4406 6678 -1852 -844 1148 N ATOM 314 N ASN A 39 -27.932 -27.611 19.398 1.00 30.64 N ANISOU 314 N ASN A 39 4970 2705 3968 -1100 -770 336 N ATOM 315 CA ASN A 39 -26.910 -27.910 20.388 1.00 31.21 C ANISOU 315 CA ASN A 39 5111 2728 4019 -1064 -763 435 C ATOM 316 C ASN A 39 -26.565 -26.600 21.075 1.00 30.55 C ANISOU 316 C ASN A 39 4933 2842 3833 -1031 -633 479 C ATOM 317 O ASN A 39 -26.952 -25.526 20.615 1.00 29.48 O ANISOU 317 O ASN A 39 4690 2862 3650 -1005 -552 416 O ATOM 318 CB ASN A 39 -25.662 -28.517 19.743 1.00 33.02 C ANISOU 318 CB ASN A 39 5442 2824 4279 -881 -842 356 C ATOM 319 CG ASN A 39 -25.196 -27.714 18.532 1.00 64.45 C ANISOU 319 CG ASN A 39 9379 6899 8211 -708 -785 212 C ATOM 320 OD1 ASN A 39 -24.788 -26.562 18.665 1.00 36.16 O ANISOU 320 OD1 ASN A 39 5702 3478 4561 -646 -676 215 O ATOM 321 ND2 ASN A 39 -25.276 -28.312 17.348 1.00 58.79 N ANISOU 321 ND2 ASN A 39 8744 6074 7519 -633 -858 87 N ATOM 322 N VAL A 40 -25.797 -26.683 22.166 1.00 33.26 N ANISOU 322 N VAL A 40 5329 3165 4142 -1022 -634 582 N ATOM 323 CA VAL A 40 -25.514 -25.491 22.971 1.00 31.69 C ANISOU 323 CA VAL A 40 5062 3133 3844 -1006 -535 628 C ATOM 324 C VAL A 40 -24.779 -24.433 22.156 1.00 29.18 C ANISOU 324 C VAL A 40 4654 2923 3509 -841 -487 519 C ATOM 325 O VAL A 40 -25.060 -23.230 22.271 1.00 26.99 O ANISOU 325 O VAL A 40 4278 2810 3166 -843 -392 505 O ATOM 326 CB VAL A 40 -24.722 -25.880 24.237 1.00 27.09 C ANISOU 326 CB VAL A 40 4587 2478 3227 -1012 -590 750 C ATOM 327 CG1 VAL A 40 -24.121 -24.647 24.884 1.00 32.99 C ANISOU 327 CG1 VAL A 40 5281 3370 3884 -946 -532 763 C ATOM 328 CG2 VAL A 40 -25.626 -26.594 25.202 1.00 33.28 C ANISOU 328 CG2 VAL A 40 5412 3248 3986 -1155 -569 848 C ATOM 329 N THR A 41 -23.799 -24.850 21.349 1.00 27.97 N ANISOU 329 N THR A 41 4534 2675 3419 -694 -542 444 N ATOM 330 CA THR A 41 -23.055 -23.889 20.539 1.00 26.66 C ANISOU 330 CA THR A 41 4284 2602 3245 -542 -472 355 C ATOM 331 C THR A 41 -24.000 -23.012 19.728 1.00 31.73 C ANISOU 331 C THR A 41 4850 3377 3830 -565 -392 283 C ATOM 332 O THR A 41 -23.840 -21.784 19.663 1.00 21.99 O ANISOU 332 O THR A 41 3524 2283 2550 -521 -307 267 O ATOM 333 CB THR A 41 -22.089 -24.619 19.597 1.00 38.47 C ANISOU 333 CB THR A 41 5832 3966 4820 -385 -512 273 C ATOM 334 OG1 THR A 41 -21.649 -25.844 20.196 1.00 32.53 O ANISOU 334 OG1 THR A 41 5180 3038 4142 -395 -629 330 O ATOM 335 CG2 THR A 41 -20.886 -23.760 19.331 1.00 27.20 C ANISOU 335 CG2 THR A 41 4314 2604 3416 -233 -437 243 C ATOM 336 N ASN A 42 -25.008 -23.627 19.126 1.00 24.36 N ANISOU 336 N ASN A 42 3955 2390 2912 -639 -437 240 N ATOM 337 CA ASN A 42 -25.920 -22.898 18.271 1.00 19.06 C ANISOU 337 CA ASN A 42 3221 1820 2202 -652 -401 165 C ATOM 338 C ASN A 42 -26.971 -22.117 19.049 1.00 20.19 C ANISOU 338 C ASN A 42 3257 2096 2317 -787 -340 224 C ATOM 339 O ASN A 42 -27.602 -21.225 18.477 1.00 20.02 O ANISOU 339 O ASN A 42 3157 2182 2268 -779 -301 169 O ATOM 340 CB ASN A 42 -26.575 -23.865 17.283 1.00 19.39 C ANISOU 340 CB ASN A 42 3346 1736 2285 -670 -505 84 C ATOM 341 CG ASN A 42 -25.630 -24.262 16.153 1.00 32.38 C ANISOU 341 CG ASN A 42 5095 3290 3917 -493 -527 -20 C ATOM 342 OD1 ASN A 42 -24.582 -23.635 15.958 1.00 25.31 O ANISOU 342 OD1 ASN A 42 4177 2452 2989 -358 -437 -34 O ATOM 343 ND2 ASN A 42 -25.998 -25.284 15.397 1.00 25.93 N ANISOU 343 ND2 ASN A 42 4393 2328 3133 -491 -640 -96 N ATOM 344 N TYR A 43 -27.191 -22.412 20.331 1.00 21.44 N ANISOU 344 N TYR A 43 3419 2248 2479 -903 -325 335 N ATOM 345 CA TYR A 43 -28.041 -21.494 21.092 1.00 20.82 C ANISOU 345 CA TYR A 43 3238 2316 2356 -998 -228 382 C ATOM 346 C TYR A 43 -27.361 -20.139 21.250 1.00 17.09 C ANISOU 346 C TYR A 43 2705 1977 1810 -894 -153 362 C ATOM 347 O TYR A 43 -28.021 -19.089 21.198 1.00 18.18 O ANISOU 347 O TYR A 43 2743 2245 1919 -907 -83 334 O ATOM 348 CB TYR A 43 -28.393 -22.082 22.451 1.00 18.48 C ANISOU 348 CB TYR A 43 2987 1986 2049 -1138 -204 510 C ATOM 349 CG TYR A 43 -29.055 -23.434 22.312 1.00 28.51 C ANISOU 349 CG TYR A 43 4312 3106 3414 -1256 -281 544 C ATOM 350 CD1 TYR A 43 -29.802 -23.742 21.176 1.00 25.15 C ANISOU 350 CD1 TYR A 43 3843 2636 3078 -1274 -347 454 C ATOM 351 CD2 TYR A 43 -28.904 -24.405 23.278 1.00 29.95 C ANISOU 351 CD2 TYR A 43 4604 3176 3601 -1346 -307 664 C ATOM 352 CE1 TYR A 43 -30.401 -24.989 21.015 1.00 29.59 C ANISOU 352 CE1 TYR A 43 4454 3039 3749 -1386 -441 477 C ATOM 353 CE2 TYR A 43 -29.511 -25.660 23.128 1.00 31.98 C ANISOU 353 CE2 TYR A 43 4895 3293 3962 -1432 -380 686 C ATOM 354 CZ TYR A 43 -30.249 -25.939 21.996 1.00 51.09 C ANISOU 354 CZ TYR A 43 7267 5657 6489 -1471 -450 599 C ATOM 355 OH TYR A 43 -30.840 -27.173 21.843 1.00 43.94 O ANISOU 355 OH TYR A 43 6384 4613 5698 -1540 -533 610 O ATOM 356 N PHE A 44 -26.037 -20.136 21.425 1.00 18.71 N ANISOU 356 N PHE A 44 2961 2142 2006 -788 -177 375 N ATOM 357 CA PHE A 44 -25.315 -18.864 21.428 1.00 17.23 C ANISOU 357 CA PHE A 44 2706 2058 1782 -688 -122 351 C ATOM 358 C PHE A 44 -25.302 -18.230 20.042 1.00 15.05 C ANISOU 358 C PHE A 44 2377 1826 1514 -591 -92 253 C ATOM 359 O PHE A 44 -25.373 -17.002 19.912 1.00 15.60 O ANISOU 359 O PHE A 44 2369 2009 1551 -557 -31 230 O ATOM 360 CB PHE A 44 -23.894 -19.064 21.956 1.00 15.43 C ANISOU 360 CB PHE A 44 2522 1760 1580 -605 -170 392 C ATOM 361 CG PHE A 44 -23.858 -19.453 23.413 1.00 15.88 C ANISOU 361 CG PHE A 44 2654 1785 1594 -690 -211 495 C ATOM 362 CD1 PHE A 44 -23.567 -20.752 23.786 1.00 18.95 C ANISOU 362 CD1 PHE A 44 3154 2028 2019 -719 -301 554 C ATOM 363 CD2 PHE A 44 -24.156 -18.521 24.399 1.00 25.62 C ANISOU 363 CD2 PHE A 44 3869 3127 2738 -737 -162 532 C ATOM 364 CE1 PHE A 44 -23.557 -21.129 25.131 1.00 26.30 C ANISOU 364 CE1 PHE A 44 4185 2920 2887 -799 -343 663 C ATOM 365 CE2 PHE A 44 -24.142 -18.888 25.751 1.00 24.46 C ANISOU 365 CE2 PHE A 44 3829 2949 2515 -810 -194 630 C ATOM 366 CZ PHE A 44 -23.852 -20.202 26.107 1.00 27.06 C ANISOU 366 CZ PHE A 44 4279 3132 2872 -844 -285 701 C ATOM 367 N VAL A 45 -25.222 -19.050 18.991 1.00 15.26 N ANISOU 367 N VAL A 45 2467 1757 1575 -542 -138 195 N ATOM 368 CA VAL A 45 -25.359 -18.525 17.632 1.00 15.58 C ANISOU 368 CA VAL A 45 2498 1832 1588 -455 -113 104 C ATOM 369 C VAL A 45 -26.712 -17.838 17.453 1.00 14.98 C ANISOU 369 C VAL A 45 2352 1853 1485 -535 -107 79 C ATOM 370 O VAL A 45 -26.810 -16.773 16.835 1.00 16.08 O ANISOU 370 O VAL A 45 2446 2079 1585 -475 -65 39 O ATOM 371 CB VAL A 45 -25.157 -19.665 16.611 1.00 21.85 C ANISOU 371 CB VAL A 45 3408 2491 2403 -393 -178 37 C ATOM 372 CG1 VAL A 45 -25.632 -19.254 15.229 1.00 17.15 C ANISOU 372 CG1 VAL A 45 2847 1923 1748 -329 -177 -59 C ATOM 373 CG2 VAL A 45 -23.700 -20.094 16.578 1.00 18.25 C ANISOU 373 CG2 VAL A 45 2993 1954 1988 -271 -157 42 C ATOM 374 N VAL A 46 -27.775 -18.413 18.020 1.00 15.95 N ANISOU 374 N VAL A 46 2457 1959 1644 -672 -146 109 N ATOM 375 CA VAL A 46 -29.085 -17.765 17.913 1.00 14.46 C ANISOU 375 CA VAL A 46 2169 1860 1467 -747 -138 86 C ATOM 376 C VAL A 46 -29.136 -16.482 18.735 1.00 15.68 C ANISOU 376 C VAL A 46 2223 2152 1582 -750 -38 120 C ATOM 377 O VAL A 46 -29.737 -15.490 18.310 1.00 16.32 O ANISOU 377 O VAL A 46 2225 2321 1656 -728 -19 76 O ATOM 378 CB VAL A 46 -30.205 -18.742 18.315 1.00 21.42 C ANISOU 378 CB VAL A 46 3030 2678 2430 -901 -189 117 C ATOM 379 CG1 VAL A 46 -31.520 -17.986 18.527 1.00 17.55 C ANISOU 379 CG1 VAL A 46 2391 2294 1982 -985 -149 111 C ATOM 380 CG2 VAL A 46 -30.377 -19.780 17.236 1.00 25.53 C ANISOU 380 CG2 VAL A 46 3642 3062 2997 -889 -317 49 C ATOM 381 N SER A 47 -28.544 -16.475 19.937 1.00 14.66 N ANISOU 381 N SER A 47 2109 2036 1426 -774 10 196 N ATOM 382 CA ASER A 47 -28.495 -15.230 20.703 0.81 17.75 C ANISOU 382 CA ASER A 47 2433 2546 1767 -760 89 213 C ATOM 383 CA BSER A 47 -28.488 -15.233 20.706 0.19 16.75 C ANISOU 383 CA BSER A 47 2306 2418 1640 -760 89 213 C ATOM 384 C SER A 47 -27.778 -14.138 19.918 1.00 17.08 C ANISOU 384 C SER A 47 2322 2505 1664 -633 101 162 C ATOM 385 O SER A 47 -28.217 -12.980 19.898 1.00 15.17 O ANISOU 385 O SER A 47 2002 2356 1405 -615 142 134 O ATOM 386 CB ASER A 47 -27.817 -15.461 22.053 0.81 19.44 C ANISOU 386 CB ASER A 47 2707 2742 1936 -789 107 295 C ATOM 387 CB BSER A 47 -27.789 -15.469 22.046 0.19 16.77 C ANISOU 387 CB BSER A 47 2370 2402 1598 -788 105 296 C ATOM 388 OG ASER A 47 -27.827 -14.265 22.809 0.81 14.18 O ANISOU 388 OG ASER A 47 1995 2180 1212 -774 169 298 O ATOM 389 OG BSER A 47 -26.412 -15.751 21.862 0.19 22.92 O ANISOU 389 OG BSER A 47 3214 3104 2391 -695 52 304 O ATOM 390 N LEU A 48 -26.685 -14.494 19.244 1.00 12.95 N ANISOU 390 N LEU A 48 1860 1908 1151 -541 74 151 N ATOM 391 CA LEU A 48 -25.953 -13.547 18.413 1.00 14.77 C ANISOU 391 CA LEU A 48 2071 2168 1374 -425 108 117 C ATOM 392 C LEU A 48 -26.787 -13.092 17.210 1.00 15.45 C ANISOU 392 C LEU A 48 2147 2287 1435 -398 99 51 C ATOM 393 O LEU A 48 -26.789 -11.903 16.852 1.00 15.89 O ANISOU 393 O LEU A 48 2158 2410 1471 -348 135 36 O ATOM 394 CB LEU A 48 -24.641 -14.219 17.984 1.00 15.65 C ANISOU 394 CB LEU A 48 2244 2184 1518 -337 103 124 C ATOM 395 CG LEU A 48 -23.599 -13.506 17.163 1.00 20.74 C ANISOU 395 CG LEU A 48 2871 2832 2177 -215 166 110 C ATOM 396 CD1 LEU A 48 -23.135 -12.252 17.915 1.00 17.47 C ANISOU 396 CD1 LEU A 48 2366 2487 1786 -212 198 149 C ATOM 397 CD2 LEU A 48 -22.427 -14.484 16.885 1.00 21.51 C ANISOU 397 CD2 LEU A 48 3018 2820 2333 -137 169 115 C ATOM 398 N ALA A 49 -27.524 -14.010 16.582 1.00 14.70 N ANISOU 398 N ALA A 49 2104 2135 1347 -433 33 12 N ATOM 399 CA ALA A 49 -28.415 -13.600 15.496 1.00 11.93 C ANISOU 399 CA ALA A 49 1753 1805 973 -412 -14 -53 C ATOM 400 C ALA A 49 -29.554 -12.720 15.989 1.00 13.82 C ANISOU 400 C ALA A 49 1869 2140 1241 -479 -10 -55 C ATOM 401 O ALA A 49 -29.992 -11.813 15.270 1.00 14.39 O ANISOU 401 O ALA A 49 1916 2256 1294 -429 -30 -95 O ATOM 402 CB ALA A 49 -28.981 -14.826 14.773 1.00 12.96 C ANISOU 402 CB ALA A 49 1969 1835 1120 -441 -119 -102 C ATOM 403 N ALA A 50 -30.050 -12.972 17.203 1.00 13.64 N ANISOU 403 N ALA A 50 1773 2146 1262 -584 20 -12 N ATOM 404 CA ALA A 50 -31.087 -12.110 17.769 1.00 21.96 C ANISOU 404 CA ALA A 50 2700 3296 2349 -634 56 -18 C ATOM 405 C ALA A 50 -30.572 -10.694 17.964 1.00 15.31 C ANISOU 405 C ALA A 50 1824 2531 1463 -554 116 -19 C ATOM 406 O ALA A 50 -31.283 -9.727 17.676 1.00 14.62 O ANISOU 406 O ALA A 50 1659 2502 1394 -530 110 -58 O ATOM 407 CB ALA A 50 -31.592 -12.674 19.103 1.00 14.83 C ANISOU 407 CB ALA A 50 1749 2408 1478 -756 116 39 C ATOM 408 N ALA A 51 -29.333 -10.549 18.454 1.00 12.88 N ANISOU 408 N ALA A 51 1568 2212 1115 -511 159 23 N ATOM 409 CA ALA A 51 -28.740 -9.220 18.567 1.00 13.97 C ANISOU 409 CA ALA A 51 1676 2399 1232 -438 197 23 C ATOM 410 C ALA A 51 -28.662 -8.543 17.208 1.00 15.57 C ANISOU 410 C ALA A 51 1896 2595 1424 -350 172 -13 C ATOM 411 O ALA A 51 -28.891 -7.335 17.097 1.00 14.25 O ANISOU 411 O ALA A 51 1680 2477 1259 -312 181 -29 O ATOM 412 CB ALA A 51 -27.346 -9.308 19.207 1.00 14.87 C ANISOU 412 CB ALA A 51 1836 2477 1337 -410 217 73 C ATOM 413 N ASP A 52 -28.313 -9.300 16.168 1.00 13.10 N ANISOU 413 N ASP A 52 1672 2215 1090 -312 141 -24 N ATOM 414 CA ASP A 52 -28.175 -8.701 14.843 1.00 13.50 C ANISOU 414 CA ASP A 52 1779 2254 1096 -221 129 -48 C ATOM 415 C ASP A 52 -29.532 -8.363 14.243 1.00 18.29 C ANISOU 415 C ASP A 52 2361 2885 1705 -234 43 -102 C ATOM 416 O ASP A 52 -29.655 -7.364 13.522 1.00 13.57 O ANISOU 416 O ASP A 52 1778 2304 1075 -169 28 -112 O ATOM 417 CB ASP A 52 -27.373 -9.630 13.925 1.00 14.85 C ANISOU 417 CB ASP A 52 2075 2343 1223 -162 136 -53 C ATOM 418 CG ASP A 52 -25.897 -9.667 14.296 1.00 32.98 C ANISOU 418 CG ASP A 52 4373 4613 3546 -118 226 -1 C ATOM 419 OD1 ASP A 52 -25.377 -8.649 14.806 1.00 22.36 O ANISOU 419 OD1 ASP A 52 2955 3307 2235 -106 275 38 O ATOM 420 OD2 ASP A 52 -25.252 -10.709 14.089 1.00 26.15 O ANISOU 420 OD2 ASP A 52 3574 3678 2684 -92 237 -2 O ATOM 421 N ILE A 53 -30.563 -9.164 14.528 1.00 15.70 N ANISOU 421 N ILE A 53 1989 2549 1427 -318 -20 -130 N ATOM 422 CA ILE A 53 -31.915 -8.784 14.113 1.00 15.25 C ANISOU 422 CA ILE A 53 1862 2515 1418 -337 -113 -181 C ATOM 423 C ILE A 53 -32.304 -7.454 14.740 1.00 13.74 C ANISOU 423 C ILE A 53 1549 2407 1265 -326 -68 -179 C ATOM 424 O ILE A 53 -32.916 -6.595 14.094 1.00 15.62 O ANISOU 424 O ILE A 53 1761 2658 1514 -276 -135 -213 O ATOM 425 CB ILE A 53 -32.933 -9.887 14.481 1.00 15.13 C ANISOU 425 CB ILE A 53 1781 2472 1494 -450 -173 -200 C ATOM 426 CG1 ILE A 53 -32.701 -11.128 13.628 1.00 15.53 C ANISOU 426 CG1 ILE A 53 1969 2418 1513 -447 -261 -225 C ATOM 427 CG2 ILE A 53 -34.367 -9.368 14.295 1.00 19.28 C ANISOU 427 CG2 ILE A 53 2173 3031 2121 -477 -257 -249 C ATOM 428 CD1 ILE A 53 -33.491 -12.361 14.100 1.00 15.62 C ANISOU 428 CD1 ILE A 53 1927 2377 1630 -574 -315 -225 C ATOM 429 N LEU A 54 -31.975 -7.270 16.018 1.00 12.87 N ANISOU 429 N LEU A 54 1376 2345 1170 -367 33 -144 N ATOM 430 CA LEU A 54 -32.309 -6.024 16.700 1.00 10.60 C ANISOU 430 CA LEU A 54 989 2128 910 -348 79 -155 C ATOM 431 C LEU A 54 -31.439 -4.855 16.240 1.00 10.44 C ANISOU 431 C LEU A 54 1020 2101 844 -252 88 -140 C ATOM 432 O LEU A 54 -31.848 -3.709 16.406 1.00 12.97 O ANISOU 432 O LEU A 54 1276 2458 1194 -215 85 -164 O ATOM 433 CB LEU A 54 -32.187 -6.212 18.215 1.00 11.10 C ANISOU 433 CB LEU A 54 1008 2234 975 -414 179 -126 C ATOM 434 CG LEU A 54 -33.171 -7.203 18.828 1.00 15.26 C ANISOU 434 CG LEU A 54 1467 2774 1557 -522 203 -124 C ATOM 435 CD1 LEU A 54 -32.826 -7.438 20.289 1.00 17.85 C ANISOU 435 CD1 LEU A 54 1826 3110 1847 -561 295 -79 C ATOM 436 CD2 LEU A 54 -34.629 -6.701 18.682 1.00 20.90 C ANISOU 436 CD2 LEU A 54 2030 3534 2376 -534 185 -180 C ATOM 437 N VAL A 55 -30.243 -5.105 15.698 1.00 11.41 N ANISOU 437 N VAL A 55 1251 2174 910 -210 107 -100 N ATOM 438 CA VAL A 55 -29.523 -4.021 15.029 1.00 10.45 C ANISOU 438 CA VAL A 55 1175 2035 762 -127 120 -75 C ATOM 439 C VAL A 55 -30.344 -3.498 13.853 1.00 11.80 C ANISOU 439 C VAL A 55 1377 2193 912 -75 33 -107 C ATOM 440 O VAL A 55 -30.460 -2.284 13.639 1.00 13.88 O ANISOU 440 O VAL A 55 1625 2463 1187 -25 16 -103 O ATOM 441 CB VAL A 55 -28.129 -4.497 14.575 1.00 11.50 C ANISOU 441 CB VAL A 55 1401 2112 855 -92 179 -23 C ATOM 442 CG1 VAL A 55 -27.502 -3.475 13.589 1.00 12.17 C ANISOU 442 CG1 VAL A 55 1545 2169 910 -10 208 14 C ATOM 443 CG2 VAL A 55 -27.210 -4.733 15.814 1.00 11.98 C ANISOU 443 CG2 VAL A 55 1421 2152 979 -125 227 13 C ATOM 444 N GLY A 56 -30.949 -4.406 13.092 1.00 10.41 N ANISOU 444 N GLY A 56 1258 1988 711 -85 -45 -140 N ATOM 445 CA GLY A 56 -31.752 -3.977 11.952 1.00 11.26 C ANISOU 445 CA GLY A 56 1416 2070 791 -31 -164 -175 C ATOM 446 C GLY A 56 -33.059 -3.313 12.358 1.00 14.48 C ANISOU 446 C GLY A 56 1677 2520 1306 -49 -241 -224 C ATOM 447 O GLY A 56 -33.465 -2.304 11.780 1.00 18.19 O ANISOU 447 O GLY A 56 2154 2979 1777 15 -315 -234 O ATOM 448 N VAL A 57 -33.744 -3.880 13.346 1.00 14.17 N ANISOU 448 N VAL A 57 1501 2522 1361 -134 -220 -252 N ATOM 449 CA VAL A 57 -35.066 -3.387 13.733 1.00 16.51 C ANISOU 449 CA VAL A 57 1631 2858 1783 -151 -273 -304 C ATOM 450 C VAL A 57 -34.975 -2.123 14.589 1.00 18.40 C ANISOU 450 C VAL A 57 1786 3151 2055 -115 -191 -305 C ATOM 451 O VAL A 57 -35.827 -1.230 14.488 1.00 17.04 O ANISOU 451 O VAL A 57 1520 2990 1963 -69 -252 -348 O ATOM 452 CB VAL A 57 -35.816 -4.521 14.462 1.00 24.46 C ANISOU 452 CB VAL A 57 2525 3885 2883 -262 -250 -322 C ATOM 453 CG1 VAL A 57 -37.064 -4.009 15.176 1.00 23.29 C ANISOU 453 CG1 VAL A 57 2168 3795 2885 -288 -234 -368 C ATOM 454 CG2 VAL A 57 -36.169 -5.612 13.473 1.00 21.51 C ANISOU 454 CG2 VAL A 57 2223 3438 2511 -290 -385 -343 C ATOM 455 N LEU A 58 -33.977 -2.031 15.476 1.00 12.19 N ANISOU 455 N LEU A 58 1027 2386 1217 -131 -67 -264 N ATOM 456 CA LEU A 58 -33.930 -0.924 16.425 1.00 11.72 C ANISOU 456 CA LEU A 58 899 2368 1187 -103 -1 -279 C ATOM 457 C LEU A 58 -32.673 -0.077 16.312 1.00 13.23 C ANISOU 457 C LEU A 58 1186 2523 1319 -47 23 -232 C ATOM 458 O LEU A 58 -32.766 1.156 16.239 1.00 11.97 O ANISOU 458 O LEU A 58 1007 2351 1190 16 -7 -247 O ATOM 459 CB LEU A 58 -34.060 -1.469 17.866 1.00 12.61 C ANISOU 459 CB LEU A 58 944 2538 1308 -178 115 -284 C ATOM 460 CG LEU A 58 -35.433 -2.060 18.218 1.00 18.02 C ANISOU 460 CG LEU A 58 1490 3267 2089 -240 131 -326 C ATOM 461 CD1 LEU A 58 -35.381 -2.628 19.633 1.00 18.04 C ANISOU 461 CD1 LEU A 58 1515 3275 2064 -303 255 -298 C ATOM 462 CD2 LEU A 58 -36.566 -1.020 18.063 1.00 17.15 C ANISOU 462 CD2 LEU A 58 1244 3181 2093 -177 88 -397 C ATOM 463 N ALA A 59 -31.482 -0.688 16.307 1.00 10.48 N ANISOU 463 N ALA A 59 929 2147 907 -70 72 -173 N ATOM 464 CA ALA A 59 -30.289 0.146 16.385 1.00 12.68 C ANISOU 464 CA ALA A 59 1257 2389 1172 -31 104 -126 C ATOM 465 C ALA A 59 -30.130 0.996 15.134 1.00 12.14 C ANISOU 465 C ALA A 59 1253 2268 1092 40 54 -96 C ATOM 466 O ALA A 59 -29.688 2.145 15.220 1.00 10.63 O ANISOU 466 O ALA A 59 1061 2045 932 77 54 -75 O ATOM 467 CB ALA A 59 -29.027 -0.701 16.618 1.00 13.12 C ANISOU 467 CB ALA A 59 1371 2418 1195 -64 163 -68 C ATOM 468 N ILE A 60 -30.482 0.459 13.965 1.00 10.34 N ANISOU 468 N ILE A 60 1099 2018 813 59 3 -92 N ATOM 469 CA ILE A 60 -30.275 1.244 12.746 1.00 10.85 C ANISOU 469 CA ILE A 60 1265 2026 832 130 -37 -50 C ATOM 470 C ILE A 60 -31.310 2.368 12.682 1.00 13.04 C ANISOU 470 C ILE A 60 1484 2301 1168 175 -137 -92 C ATOM 471 O ILE A 60 -30.917 3.510 12.427 1.00 11.24 O ANISOU 471 O ILE A 60 1291 2027 951 221 -143 -51 O ATOM 472 CB ILE A 60 -30.249 0.346 11.497 1.00 14.58 C ANISOU 472 CB ILE A 60 1875 2466 1200 151 -65 -36 C ATOM 473 CG1 ILE A 60 -28.888 -0.387 11.464 1.00 16.03 C ANISOU 473 CG1 ILE A 60 2123 2629 1337 139 62 22 C ATOM 474 CG2 ILE A 60 -30.506 1.173 10.208 1.00 18.88 C ANISOU 474 CG2 ILE A 60 2544 2955 1674 230 -145 -8 C ATOM 475 CD1 ILE A 60 -28.722 -1.393 10.298 1.00 12.73 C ANISOU 475 CD1 ILE A 60 1861 2174 800 171 60 24 C ATOM 476 N PRO A 61 -32.608 2.139 12.934 1.00 13.51 N ANISOU 476 N PRO A 61 1444 2400 1289 164 -216 -171 N ATOM 477 CA PRO A 61 -33.510 3.301 13.072 1.00 11.96 C ANISOU 477 CA PRO A 61 1163 2200 1183 218 -297 -219 C ATOM 478 C PRO A 61 -33.051 4.313 14.115 1.00 11.56 C ANISOU 478 C PRO A 61 1052 2154 1186 229 -228 -223 C ATOM 479 O PRO A 61 -33.198 5.518 13.893 1.00 13.33 O ANISOU 479 O PRO A 61 1281 2330 1452 294 -289 -224 O ATOM 480 CB PRO A 61 -34.851 2.654 13.457 1.00 14.96 C ANISOU 480 CB PRO A 61 1399 2633 1652 185 -345 -303 C ATOM 481 CG PRO A 61 -34.823 1.334 12.736 1.00 14.72 C ANISOU 481 CG PRO A 61 1449 2590 1553 141 -378 -288 C ATOM 482 CD PRO A 61 -33.372 0.874 12.881 1.00 11.61 C ANISOU 482 CD PRO A 61 1168 2189 1056 112 -253 -217 C ATOM 483 N PHE A 62 -32.501 3.863 15.250 1.00 10.85 N ANISOU 483 N PHE A 62 921 2109 1093 171 -120 -228 N ATOM 484 CA PHE A 62 -32.003 4.815 16.243 1.00 10.66 C ANISOU 484 CA PHE A 62 869 2075 1107 186 -79 -241 C ATOM 485 C PHE A 62 -30.816 5.610 15.707 1.00 11.74 C ANISOU 485 C PHE A 62 1100 2128 1234 210 -85 -158 C ATOM 486 O PHE A 62 -30.696 6.817 15.973 1.00 12.82 O ANISOU 486 O PHE A 62 1228 2215 1429 251 -119 -167 O ATOM 487 CB PHE A 62 -31.581 4.081 17.529 1.00 11.14 C ANISOU 487 CB PHE A 62 902 2189 1142 119 17 -256 C ATOM 488 CG PHE A 62 -32.719 3.511 18.345 1.00 12.60 C ANISOU 488 CG PHE A 62 986 2455 1346 89 60 -331 C ATOM 489 CD1 PHE A 62 -34.050 3.689 17.992 1.00 14.10 C ANISOU 489 CD1 PHE A 62 1078 2669 1609 121 13 -391 C ATOM 490 CD2 PHE A 62 -32.426 2.785 19.500 1.00 10.42 C ANISOU 490 CD2 PHE A 62 712 2225 1022 27 149 -333 C ATOM 491 CE1 PHE A 62 -35.084 3.139 18.777 1.00 19.09 C ANISOU 491 CE1 PHE A 62 1592 3377 2285 84 81 -450 C ATOM 492 CE2 PHE A 62 -33.426 2.242 20.295 1.00 13.04 C ANISOU 492 CE2 PHE A 62 973 2615 1366 -11 214 -379 C ATOM 493 CZ PHE A 62 -34.777 2.429 19.942 1.00 16.80 C ANISOU 493 CZ PHE A 62 1336 3114 1933 14 193 -435 C ATOM 494 N ALA A 63 -29.908 4.945 14.971 1.00 11.94 N ANISOU 494 N ALA A 63 1212 2128 1197 185 -42 -75 N ATOM 495 CA ALA A 63 -28.741 5.630 14.408 1.00 11.66 C ANISOU 495 CA ALA A 63 1251 2012 1169 199 -14 21 C ATOM 496 C ALA A 63 -29.157 6.674 13.381 1.00 13.21 C ANISOU 496 C ALA A 63 1511 2143 1366 264 -91 52 C ATOM 497 O ALA A 63 -28.603 7.780 13.329 1.00 12.11 O ANISOU 497 O ALA A 63 1390 1928 1284 281 -99 103 O ATOM 498 CB ALA A 63 -27.803 4.612 13.742 1.00 10.87 C ANISOU 498 CB ALA A 63 1224 1904 1001 173 71 95 C ATOM 499 N ILE A 64 -30.132 6.328 12.538 1.00 11.53 N ANISOU 499 N ILE A 64 1339 1945 1095 298 -164 27 N ATOM 500 CA ILE A 64 -30.672 7.310 11.601 1.00 12.54 C ANISOU 500 CA ILE A 64 1540 2006 1219 368 -271 51 C ATOM 501 C ILE A 64 -31.227 8.509 12.365 1.00 14.85 C ANISOU 501 C ILE A 64 1735 2274 1632 405 -342 -10 C ATOM 502 O ILE A 64 -30.982 9.672 12.016 1.00 14.63 O ANISOU 502 O ILE A 64 1760 2156 1641 445 -388 41 O ATOM 503 CB ILE A 64 -31.748 6.642 10.725 1.00 13.18 C ANISOU 503 CB ILE A 64 1667 2107 1234 398 -378 10 C ATOM 504 CG1 ILE A 64 -31.091 5.606 9.805 1.00 14.04 C ANISOU 504 CG1 ILE A 64 1921 2212 1201 381 -314 72 C ATOM 505 CG2 ILE A 64 -32.558 7.703 9.934 1.00 17.32 C ANISOU 505 CG2 ILE A 64 2247 2559 1775 481 -535 13 C ATOM 506 CD1 ILE A 64 -32.088 4.680 9.076 1.00 16.28 C ANISOU 506 CD1 ILE A 64 2255 2513 1418 397 -431 13 C ATOM 507 N THR A 65 -32.004 8.232 13.415 1.00 13.38 N ANISOU 507 N THR A 65 1412 2163 1510 395 -344 -121 N ATOM 508 CA THR A 65 -32.614 9.297 14.199 1.00 13.13 C ANISOU 508 CA THR A 65 1287 2114 1586 446 -396 -202 C ATOM 509 C THR A 65 -31.553 10.212 14.811 1.00 12.93 C ANISOU 509 C THR A 65 1288 2022 1604 437 -360 -167 C ATOM 510 O THR A 65 -31.653 11.437 14.713 1.00 14.27 O ANISOU 510 O THR A 65 1473 2104 1844 494 -438 -168 O ATOM 511 CB THR A 65 -33.512 8.690 15.291 1.00 14.56 C ANISOU 511 CB THR A 65 1325 2399 1809 429 -352 -318 C ATOM 512 OG1 THR A 65 -34.484 7.830 14.674 1.00 18.79 O ANISOU 512 OG1 THR A 65 1819 2980 2339 424 -400 -343 O ATOM 513 CG2 THR A 65 -34.244 9.781 16.045 1.00 14.96 C ANISOU 513 CG2 THR A 65 1283 2435 1966 503 -389 -417 C ATOM 514 N AILE A 66 -30.514 9.634 15.422 0.54 12.09 N ANISOU 514 N AILE A 66 1187 1940 1468 366 -261 -134 N ATOM 515 N BILE A 66 -30.521 9.642 15.444 0.46 15.45 N ANISOU 515 N BILE A 66 1610 2365 1894 366 -261 -136 N ATOM 516 CA AILE A 66 -29.553 10.474 16.130 0.54 13.92 C ANISOU 516 CA AILE A 66 1424 2099 1766 353 -255 -117 C ATOM 517 CA BILE A 66 -29.564 10.513 16.127 0.46 13.12 C ANISOU 517 CA BILE A 66 1323 1996 1667 355 -258 -118 C ATOM 518 C AILE A 66 -28.630 11.214 15.173 0.54 18.87 C ANISOU 518 C AILE A 66 2135 2610 2424 349 -268 12 C ATOM 519 C BILE A 66 -28.680 11.265 15.150 0.46 12.60 C ANISOU 519 C BILE A 66 1342 1813 1632 353 -273 10 C ATOM 520 O AILE A 66 -27.973 12.181 15.577 0.54 27.33 O ANISOU 520 O AILE A 66 3207 3589 3589 344 -299 31 O ATOM 521 O BILE A 66 -28.088 12.285 15.522 0.46 13.05 O ANISOU 521 O BILE A 66 1401 1776 1783 353 -310 28 O ATOM 522 CB AILE A 66 -28.737 9.643 17.141 0.54 16.85 C ANISOU 522 CB AILE A 66 1770 2521 2113 282 -175 -125 C ATOM 523 CB BILE A 66 -28.663 9.761 17.128 0.46 11.39 C ANISOU 523 CB BILE A 66 1081 1817 1429 284 -180 -120 C ATOM 524 CG1AILE A 66 -28.193 10.536 18.254 0.54 11.67 C ANISOU 524 CG1AILE A 66 1101 1802 1530 284 -215 -171 C ATOM 525 CG1BILE A 66 -27.787 8.723 16.428 0.46 12.27 C ANISOU 525 CG1BILE A 66 1234 1942 1485 228 -100 -17 C ATOM 526 CG2AILE A 66 -27.605 8.891 16.448 0.54 11.65 C ANISOU 526 CG2AILE A 66 1158 1846 1422 226 -103 -7 C ATOM 527 CG2BILE A 66 -29.490 9.111 18.195 0.46 11.20 C ANISOU 527 CG2BILE A 66 995 1898 1364 280 -149 -233 C ATOM 528 CD1AILE A 66 -27.654 9.741 19.448 0.54 11.70 C ANISOU 528 CD1AILE A 66 1093 1860 1494 231 -170 -206 C ATOM 529 CD1BILE A 66 -26.651 8.254 17.293 0.46 47.19 C ANISOU 529 CD1BILE A 66 5636 6361 5932 168 -54 3 C ATOM 530 N SER A 67 -28.557 10.786 13.911 1.00 13.44 N ANISOU 530 N SER A 67 1529 1917 1659 350 -242 102 N ATOM 531 CA SER A 67 -27.761 11.507 12.930 1.00 13.70 C ANISOU 531 CA SER A 67 1660 1841 1706 349 -227 238 C ATOM 532 C SER A 67 -28.403 12.847 12.597 1.00 19.19 C ANISOU 532 C SER A 67 2391 2439 2460 416 -353 236 C ATOM 533 O SER A 67 -27.735 13.722 12.038 1.00 17.80 O ANISOU 533 O SER A 67 2287 2147 2329 409 -352 349 O ATOM 534 CB SER A 67 -27.594 10.664 11.648 1.00 14.54 C ANISOU 534 CB SER A 67 1879 1970 1677 349 -157 326 C ATOM 535 OG SER A 67 -28.773 10.698 10.845 1.00 16.72 O ANISOU 535 OG SER A 67 2224 2253 1874 415 -264 295 O ATOM 536 N THR A 68 -29.690 13.020 12.910 1.00 15.59 N ANISOU 536 N THR A 68 1883 2021 2020 481 -457 116 N ATOM 537 CA THR A 68 -30.355 14.279 12.571 1.00 15.90 C ANISOU 537 CA THR A 68 1954 1958 2129 560 -593 106 C ATOM 538 C THR A 68 -30.126 15.364 13.608 1.00 23.66 C ANISOU 538 C THR A 68 2877 2864 3249 573 -637 47 C ATOM 539 O THR A 68 -30.433 16.529 13.332 1.00 22.39 O ANISOU 539 O THR A 68 2756 2587 3166 633 -749 56 O ATOM 540 CB THR A 68 -31.875 14.093 12.414 1.00 25.99 C ANISOU 540 CB THR A 68 3180 3292 3402 639 -700 -3 C ATOM 541 OG1 THR A 68 -32.465 13.864 13.694 1.00 19.91 O ANISOU 541 OG1 THR A 68 2260 2608 2695 648 -677 -151 O ATOM 542 CG2 THR A 68 -32.204 12.913 11.524 1.00 19.00 C ANISOU 542 CG2 THR A 68 2347 2482 2389 624 -686 27 C ATOM 543 N GLY A 69 -29.644 15.018 14.797 1.00 19.05 N ANISOU 543 N GLY A 69 2214 2333 2691 526 -571 -21 N ATOM 544 CA GLY A 69 -29.490 16.030 15.827 1.00 19.73 C ANISOU 544 CA GLY A 69 2266 2340 2890 549 -633 -101 C ATOM 545 C GLY A 69 -30.788 16.599 16.348 1.00 23.34 C ANISOU 545 C GLY A 69 2667 2809 3393 656 -719 -253 C ATOM 546 O GLY A 69 -30.797 17.716 16.876 1.00 25.77 O ANISOU 546 O GLY A 69 2981 3011 3800 706 -803 -313 O ATOM 547 N PHE A 70 -31.886 15.851 16.231 1.00 18.95 N ANISOU 547 N PHE A 70 2047 2371 2783 693 -698 -323 N ATOM 548 CA PHE A 70 -33.210 16.346 16.583 1.00 18.23 C ANISOU 548 CA PHE A 70 1872 2293 2761 802 -766 -462 C ATOM 549 C PHE A 70 -33.293 16.692 18.071 1.00 18.66 C ANISOU 549 C PHE A 70 1872 2368 2850 834 -725 -607 C ATOM 550 O PHE A 70 -32.540 16.170 18.910 1.00 21.72 O ANISOU 550 O PHE A 70 2273 2804 3174 763 -638 -615 O ATOM 551 CB PHE A 70 -34.270 15.295 16.221 1.00 19.19 C ANISOU 551 CB PHE A 70 1908 2544 2841 811 -737 -499 C ATOM 552 CG PHE A 70 -34.336 14.148 17.182 1.00 19.23 C ANISOU 552 CG PHE A 70 1835 2694 2779 749 -594 -563 C ATOM 553 CD1 PHE A 70 -33.284 13.257 17.308 1.00 20.14 C ANISOU 553 CD1 PHE A 70 2005 2851 2795 643 -500 -483 C ATOM 554 CD2 PHE A 70 -35.452 13.971 17.985 1.00 32.95 C ANISOU 554 CD2 PHE A 70 3440 4519 4562 801 -547 -701 C ATOM 555 CE1 PHE A 70 -33.342 12.206 18.203 1.00 27.11 C ANISOU 555 CE1 PHE A 70 2833 3853 3613 587 -382 -532 C ATOM 556 CE2 PHE A 70 -35.507 12.931 18.886 1.00 22.33 C ANISOU 556 CE2 PHE A 70 2040 3298 3146 738 -404 -744 C ATOM 557 CZ PHE A 70 -34.470 12.045 18.992 1.00 25.15 C ANISOU 557 CZ PHE A 70 2473 3690 3394 630 -332 -658 C ATOM 558 N CYS A 71 -34.222 17.596 18.387 1.00 20.59 N ANISOU 558 N CYS A 71 2066 2567 3192 953 -797 -727 N ATOM 559 CA CYS A 71 -34.425 18.039 19.761 1.00 22.24 C ANISOU 559 CA CYS A 71 2245 2785 3420 1012 -757 -884 C ATOM 560 C CYS A 71 -35.025 16.913 20.593 1.00 24.90 C ANISOU 560 C CYS A 71 2489 3301 3671 991 -597 -969 C ATOM 561 O CYS A 71 -36.023 16.301 20.202 1.00 25.20 O ANISOU 561 O CYS A 71 2416 3431 3729 1009 -560 -987 O ATOM 562 CB CYS A 71 -35.350 19.261 19.794 1.00 24.15 C ANISOU 562 CB CYS A 71 2460 2932 3784 1141 -854 -986 C ATOM 563 SG CYS A 71 -34.660 20.770 19.051 1.00 33.58 S ANISOU 563 SG CYS A 71 3785 3889 5085 1160 -1043 -894 S ATOM 564 N ALA A 72 -34.438 16.652 21.758 1.00 19.17 N ANISOU 564 N ALA A 72 1813 2614 2857 953 -513 -1021 N ATOM 565 CA ALA A 72 -34.889 15.540 22.579 1.00 19.32 C ANISOU 565 CA ALA A 72 1774 2794 2774 918 -349 -1077 C ATOM 566 C ALA A 72 -34.563 15.800 24.040 1.00 24.36 C ANISOU 566 C ALA A 72 2493 3436 3328 944 -291 -1189 C ATOM 567 O ALA A 72 -33.560 16.441 24.363 1.00 22.77 O ANISOU 567 O ALA A 72 2409 3122 3121 932 -386 -1181 O ATOM 568 CB ALA A 72 -34.234 14.223 22.120 1.00 18.88 C ANISOU 568 CB ALA A 72 1734 2812 2626 781 -293 -941 C ATOM 569 N ALA A 73 -35.416 15.297 24.925 1.00 20.39 N ANISOU 569 N ALA A 73 1936 3054 2757 972 -137 -1286 N ATOM 570 CA ALA A 73 -35.028 15.191 26.321 1.00 21.94 C ANISOU 570 CA ALA A 73 2252 3275 2808 960 -59 -1351 C ATOM 571 C ALA A 73 -33.727 14.404 26.415 1.00 19.50 C ANISOU 571 C ALA A 73 2043 2969 2397 844 -85 -1254 C ATOM 572 O ALA A 73 -33.558 13.368 25.754 1.00 18.90 O ANISOU 572 O ALA A 73 1916 2957 2308 744 -49 -1134 O ATOM 573 CB ALA A 73 -36.134 14.514 27.135 1.00 29.76 C ANISOU 573 CB ALA A 73 3194 4385 3728 935 136 -1363 C ATOM 574 N CYS A 74 -32.781 14.914 27.205 1.00 19.79 N ANISOU 574 N CYS A 74 2047 2670 2802 685 -409 -650 N ATOM 575 CA CYS A 74 -31.428 14.376 27.116 1.00 19.88 C ANISOU 575 CA CYS A 74 2076 2645 2833 604 -472 -632 C ATOM 576 C CYS A 74 -31.378 12.887 27.466 1.00 21.45 C ANISOU 576 C CYS A 74 2323 2979 2847 567 -421 -613 C ATOM 577 O CYS A 74 -30.623 12.130 26.850 1.00 21.43 O ANISOU 577 O CYS A 74 2297 2994 2852 482 -425 -535 O ATOM 578 CB CYS A 74 -30.469 15.173 28.005 1.00 20.49 C ANISOU 578 CB CYS A 74 2190 2568 3026 645 -620 -782 C ATOM 579 SG CYS A 74 -28.710 14.689 27.777 1.00 31.31 S ANISOU 579 SG CYS A 74 3501 3830 4566 543 -722 -775 S ATOM 580 N HIS A 75 -32.157 12.437 28.455 1.00 17.24 N ANISOU 580 N HIS A 75 1868 2525 2157 643 -339 -670 N ATOM 581 CA HIS A 75 -32.064 11.018 28.805 1.00 17.43 C ANISOU 581 CA HIS A 75 1948 2644 2029 616 -261 -631 C ATOM 582 C HIS A 75 -32.747 10.100 27.775 1.00 19.59 C ANISOU 582 C HIS A 75 2097 3003 2344 523 -166 -513 C ATOM 583 O HIS A 75 -32.312 8.954 27.581 1.00 17.97 O ANISOU 583 O HIS A 75 1900 2847 2080 455 -148 -460 O ATOM 584 CB HIS A 75 -32.610 10.795 30.204 1.00 24.97 C ANISOU 584 CB HIS A 75 3064 3621 2801 757 -149 -699 C ATOM 585 CG HIS A 75 -31.731 11.386 31.264 1.00 32.88 C ANISOU 585 CG HIS A 75 4252 4541 3701 886 -314 -848 C ATOM 586 ND1 HIS A 75 -31.831 12.701 31.667 1.00 44.36 N ANISOU 586 ND1 HIS A 75 5742 5899 5212 988 -412 -973 N ATOM 587 CD2 HIS A 75 -30.683 10.864 31.941 1.00 27.07 C ANISOU 587 CD2 HIS A 75 3666 3782 2838 940 -450 -918 C ATOM 588 CE1 HIS A 75 -30.906 12.951 32.577 1.00 25.85 C ANISOU 588 CE1 HIS A 75 3567 3471 2783 1107 -617 -1132 C ATOM 589 NE2 HIS A 75 -30.194 11.854 32.758 1.00 27.62 N ANISOU 589 NE2 HIS A 75 3862 3737 2894 1086 -654 -1103 N ATOM 590 N GLY A 76 -33.778 10.573 27.080 1.00 19.30 N ANISOU 590 N GLY A 76 1944 2968 2421 533 -141 -490 N ATOM 591 CA GLY A 76 -34.275 9.810 25.944 1.00 19.81 C ANISOU 591 CA GLY A 76 1897 3080 2548 472 -150 -421 C ATOM 592 C GLY A 76 -33.260 9.711 24.823 1.00 17.72 C ANISOU 592 C GLY A 76 1666 2802 2266 420 -253 -350 C ATOM 593 O GLY A 76 -33.095 8.654 24.210 1.00 18.79 O ANISOU 593 O GLY A 76 1792 2984 2363 370 -263 -306 O ATOM 594 N CYS A 77 -32.571 10.817 24.535 1.00 20.56 N ANISOU 594 N CYS A 77 2065 3073 2674 444 -306 -333 N ATOM 595 CA CYS A 77 -31.486 10.798 23.563 1.00 18.59 C ANISOU 595 CA CYS A 77 1855 2769 2439 412 -324 -238 C ATOM 596 C CYS A 77 -30.423 9.779 23.970 1.00 15.00 C ANISOU 596 C CYS A 77 1426 2339 1936 333 -311 -237 C ATOM 597 O CYS A 77 -29.917 9.003 23.140 1.00 13.65 O ANISOU 597 O CYS A 77 1275 2188 1723 300 -291 -158 O ATOM 598 CB CYS A 77 -30.890 12.207 23.477 1.00 22.78 C ANISOU 598 CB CYS A 77 2391 3149 3115 443 -331 -221 C ATOM 599 SG CYS A 77 -29.482 12.334 22.389 1.00 23.54 S ANISOU 599 SG CYS A 77 2515 3113 3316 417 -254 -72 S ATOM 600 N ALEU A 78 -30.062 9.761 25.257 0.52 14.13 N ANISOU 600 N ALEU A 78 1340 2219 1811 330 -336 -333 N ATOM 601 N BLEU A 78 -30.099 9.759 25.254 0.48 18.49 N ANISOU 601 N BLEU A 78 1891 2772 2361 331 -335 -333 N ATOM 602 CA ALEU A 78 -29.094 8.778 25.734 0.52 13.25 C ANISOU 602 CA ALEU A 78 1266 2124 1645 284 -358 -347 C ATOM 603 CA BLEU A 78 -29.120 8.819 25.766 0.48 28.44 C ANISOU 603 CA BLEU A 78 3190 4046 3569 287 -359 -350 C ATOM 604 C ALEU A 78 -29.538 7.360 25.426 0.52 17.91 C ANISOU 604 C ALEU A 78 1862 2828 2115 242 -291 -292 C ATOM 605 C BLEU A 78 -29.528 7.377 25.487 0.48 12.48 C ANISOU 605 C BLEU A 78 1176 2139 1425 244 -292 -296 C ATOM 606 O ALEU A 78 -28.720 6.519 25.035 0.52 13.16 O ANISOU 606 O ALEU A 78 1268 2234 1497 190 -293 -246 O ATOM 607 O BLEU A 78 -28.683 6.544 25.141 0.48 17.92 O ANISOU 607 O BLEU A 78 1875 2835 2100 192 -297 -253 O ATOM 608 CB ALEU A 78 -28.870 8.919 27.243 0.52 18.35 C ANISOU 608 CB ALEU A 78 2000 2747 2225 353 -428 -478 C ATOM 609 CB BLEU A 78 -28.949 9.077 27.257 0.48 20.45 C ANISOU 609 CB BLEU A 78 2264 3007 2500 360 -429 -484 C ATOM 610 CG ALEU A 78 -27.880 9.940 27.767 0.52 15.19 C ANISOU 610 CG ALEU A 78 1596 2196 1978 390 -583 -590 C ATOM 611 CG BLEU A 78 -27.687 8.614 27.928 0.48 14.49 C ANISOU 611 CG BLEU A 78 1562 2201 1743 365 -548 -553 C ATOM 612 CD1ALEU A 78 -27.914 9.872 29.282 0.52 16.36 C ANISOU 612 CD1ALEU A 78 1908 2349 1960 522 -678 -741 C ATOM 613 CD1BLEU A 78 -26.437 9.124 27.201 0.48 14.78 C ANISOU 613 CD1BLEU A 78 1473 2094 2047 297 -621 -535 C ATOM 614 CD2ALEU A 78 -26.472 9.674 27.249 0.52 15.10 C ANISOU 614 CD2ALEU A 78 1497 2088 2152 312 -644 -561 C ATOM 615 CD2BLEU A 78 -27.748 9.142 29.356 0.48 16.00 C ANISOU 615 CD2BLEU A 78 1895 2350 1836 509 -658 -713 C ATOM 616 N PHE A 79 -30.825 7.056 25.610 1.00 12.67 N ANISOU 616 N PHE A 79 1173 2231 1411 265 -223 -303 N ATOM 617 CA PHE A 79 -31.259 5.689 25.356 1.00 12.31 C ANISOU 617 CA PHE A 79 1098 2251 1330 218 -166 -268 C ATOM 618 C PHE A 79 -31.087 5.324 23.882 1.00 14.00 C ANISOU 618 C PHE A 79 1281 2474 1566 189 -229 -212 C ATOM 619 O PHE A 79 -30.614 4.230 23.553 1.00 15.05 O ANISOU 619 O PHE A 79 1432 2631 1655 143 -228 -183 O ATOM 620 CB PHE A 79 -32.724 5.470 25.778 1.00 14.93 C ANISOU 620 CB PHE A 79 1348 2601 1725 245 -60 -293 C ATOM 621 CG PHE A 79 -33.197 4.058 25.533 1.00 17.45 C ANISOU 621 CG PHE A 79 1592 2939 2099 186 1 -269 C ATOM 622 CD1 PHE A 79 -32.828 3.025 26.403 1.00 17.54 C ANISOU 622 CD1 PHE A 79 1681 2954 2030 167 120 -236 C ATOM 623 CD2 PHE A 79 -33.979 3.743 24.427 1.00 17.86 C ANISOU 623 CD2 PHE A 79 1510 2984 2293 169 -85 -290 C ATOM 624 CE1 PHE A 79 -33.232 1.713 26.167 1.00 24.16 C ANISOU 624 CE1 PHE A 79 2437 3779 2964 106 188 -208 C ATOM 625 CE2 PHE A 79 -34.394 2.439 24.186 1.00 18.48 C ANISOU 625 CE2 PHE A 79 1495 3045 2480 114 -64 -298 C ATOM 626 CZ PHE A 79 -34.029 1.420 25.058 1.00 26.13 C ANISOU 626 CZ PHE A 79 2514 4007 3406 68 92 -249 C ATOM 627 N AILE A 80 -31.505 6.234 22.994 0.50 12.26 N ANISOU 627 N AILE A 80 1043 2224 1391 246 -286 -198 N ATOM 628 N BILE A 80 -31.461 6.210 22.960 0.50 13.48 N ANISOU 628 N BILE A 80 1201 2379 1543 245 -287 -196 N ATOM 629 CA AILE A 80 -31.335 6.084 21.548 0.50 14.38 C ANISOU 629 CA AILE A 80 1364 2483 1617 291 -347 -141 C ATOM 630 CA BILE A 80 -31.290 5.813 21.563 0.50 12.28 C ANISOU 630 CA BILE A 80 1096 2227 1341 278 -345 -143 C ATOM 631 C AILE A 80 -29.871 5.872 21.202 0.50 11.90 C ANISOU 631 C AILE A 80 1131 2131 1259 263 -293 -59 C ATOM 632 C BILE A 80 -29.858 5.961 21.081 0.50 21.84 C ANISOU 632 C BILE A 80 2398 3384 2518 273 -293 -51 C ATOM 633 O AILE A 80 -29.522 5.035 20.353 0.50 11.83 O ANISOU 633 O AILE A 80 1186 2138 1172 278 -296 -18 O ATOM 634 O BILE A 80 -29.522 5.431 20.012 0.50 12.72 O ANISOU 634 O BILE A 80 1327 2227 1280 318 -293 7 O ATOM 635 CB AILE A 80 -31.897 7.332 20.836 0.50 16.58 C ANISOU 635 CB AILE A 80 1666 2711 1922 400 -401 -123 C ATOM 636 CB BILE A 80 -32.230 6.573 20.614 0.50 13.33 C ANISOU 636 CB BILE A 80 1236 2337 1491 394 -440 -151 C ATOM 637 CG1AILE A 80 -33.416 7.395 20.990 0.50 17.24 C ANISOU 637 CG1AILE A 80 1635 2821 2096 440 -479 -218 C ATOM 638 CG1BILE A 80 -31.943 8.073 20.632 0.50 13.74 C ANISOU 638 CG1BILE A 80 1329 2312 1580 447 -404 -102 C ATOM 639 CG2AILE A 80 -31.474 7.370 19.374 0.50 24.78 C ANISOU 639 CG2AILE A 80 2852 3713 2852 507 -427 -32 C ATOM 640 CG2BILE A 80 -33.662 6.262 20.974 0.50 14.44 C ANISOU 640 CG2BILE A 80 1230 2506 1752 396 -499 -256 C ATOM 641 CD1AILE A 80 -34.150 6.454 20.064 0.50 29.34 C ANISOU 641 CD1AILE A 80 3139 4376 3633 489 -619 -273 C ATOM 642 CD1BILE A 80 -32.694 8.816 19.530 0.50 15.63 C ANISOU 642 CD1BILE A 80 1633 2514 1793 599 -498 -80 C ATOM 643 N ALA A 81 -28.996 6.641 21.838 1.00 11.89 N ANISOU 643 N ALA A 81 1118 2056 1342 235 -249 -48 N ATOM 644 CA ALA A 81 -27.575 6.583 21.517 1.00 11.92 C ANISOU 644 CA ALA A 81 1141 1977 1411 208 -184 25 C ATOM 645 C ALA A 81 -26.958 5.279 22.004 1.00 12.26 C ANISOU 645 C ALA A 81 1176 2072 1409 138 -193 -3 C ATOM 646 O ALA A 81 -26.073 4.723 21.344 1.00 12.69 O ANISOU 646 O ALA A 81 1254 2094 1472 130 -132 67 O ATOM 647 CB ALA A 81 -26.838 7.755 22.165 1.00 14.71 C ANISOU 647 CB ALA A 81 1430 2198 1963 193 -183 1 C ATOM 648 N CYS A 82 -27.384 4.802 23.180 1.00 11.09 N ANISOU 648 N CYS A 82 1014 1989 1212 108 -243 -92 N ATOM 649 CA CYS A 82 -26.685 3.714 23.868 1.00 11.72 C ANISOU 649 CA CYS A 82 1112 2090 1250 66 -256 -116 C ATOM 650 C CYS A 82 -27.252 2.333 23.597 1.00 13.88 C ANISOU 650 C CYS A 82 1406 2449 1420 38 -224 -98 C ATOM 651 O CYS A 82 -26.574 1.343 23.878 1.00 11.10 O ANISOU 651 O CYS A 82 1080 2103 1036 9 -221 -91 O ATOM 652 CB CYS A 82 -26.699 3.951 25.389 1.00 12.85 C ANISOU 652 CB CYS A 82 1295 2226 1362 100 -315 -213 C ATOM 653 SG CYS A 82 -25.691 5.359 25.874 1.00 16.78 S ANISOU 653 SG CYS A 82 1752 2578 2045 134 -433 -294 S ATOM 654 N PHE A 83 -28.465 2.219 23.054 1.00 12.16 N ANISOU 654 N PHE A 83 1161 2274 1187 53 -219 -103 N ATOM 655 CA PHE A 83 -29.033 0.883 22.913 1.00 10.30 C ANISOU 655 CA PHE A 83 903 2076 935 20 -208 -115 C ATOM 656 C PHE A 83 -28.127 -0.024 22.070 1.00 12.71 C ANISOU 656 C PHE A 83 1259 2377 1192 6 -224 -77 C ATOM 657 O PHE A 83 -28.026 -1.229 22.330 1.00 11.64 O ANISOU 657 O PHE A 83 1124 2252 1047 -37 -204 -82 O ATOM 658 CB PHE A 83 -30.440 0.948 22.321 1.00 13.36 C ANISOU 658 CB PHE A 83 1208 2469 1398 48 -255 -163 C ATOM 659 CG PHE A 83 -31.094 -0.395 22.256 1.00 13.00 C ANISOU 659 CG PHE A 83 1088 2416 1437 4 -255 -200 C ATOM 660 CD1 PHE A 83 -31.435 -1.059 23.429 1.00 17.15 C ANISOU 660 CD1 PHE A 83 1568 2921 2026 -46 -114 -188 C ATOM 661 CD2 PHE A 83 -31.337 -1.017 21.034 1.00 15.90 C ANISOU 661 CD2 PHE A 83 1451 2769 1822 37 -389 -248 C ATOM 662 CE1 PHE A 83 -32.022 -2.329 23.384 1.00 22.17 C ANISOU 662 CE1 PHE A 83 2109 3506 2808 -96 -77 -209 C ATOM 663 CE2 PHE A 83 -31.922 -2.284 20.984 1.00 18.61 C ANISOU 663 CE2 PHE A 83 1695 3068 2308 -10 -413 -309 C ATOM 664 CZ PHE A 83 -32.265 -2.938 22.161 1.00 17.24 C ANISOU 664 CZ PHE A 83 1431 2858 2263 -93 -243 -281 C ATOM 665 N VAL A 84 -27.470 0.530 21.047 1.00 10.79 N ANISOU 665 N VAL A 84 1072 2104 924 58 -227 -26 N ATOM 666 CA VAL A 84 -26.603 -0.309 20.209 1.00 9.82 C ANISOU 666 CA VAL A 84 1019 1967 747 75 -201 19 C ATOM 667 C VAL A 84 -25.446 -0.896 21.028 1.00 10.08 C ANISOU 667 C VAL A 84 1025 1978 826 7 -157 34 C ATOM 668 O VAL A 84 -24.917 -1.975 20.694 1.00 10.71 O ANISOU 668 O VAL A 84 1137 2059 874 -2 -141 48 O ATOM 669 CB VAL A 84 -26.065 0.493 19.014 1.00 10.58 C ANISOU 669 CB VAL A 84 1211 2003 806 180 -135 107 C ATOM 670 CG1 VAL A 84 -25.159 1.630 19.498 1.00 10.71 C ANISOU 670 CG1 VAL A 84 1166 1932 971 153 -43 165 C ATOM 671 CG2 VAL A 84 -25.320 -0.441 17.981 1.00 11.04 C ANISOU 671 CG2 VAL A 84 1386 2041 766 246 -74 157 C ATOM 672 N LEU A 85 -25.029 -0.200 22.090 1.00 10.37 N ANISOU 672 N LEU A 85 1016 1984 940 -18 -168 14 N ATOM 673 CA LEU A 85 -23.973 -0.718 22.952 1.00 11.90 C ANISOU 673 CA LEU A 85 1197 2144 1181 -45 -195 -5 C ATOM 674 C LEU A 85 -24.424 -1.972 23.689 1.00 11.66 C ANISOU 674 C LEU A 85 1215 2170 1046 -65 -205 -30 C ATOM 675 O LEU A 85 -23.607 -2.852 23.975 1.00 11.30 O ANISOU 675 O LEU A 85 1191 2105 999 -72 -220 -25 O ATOM 676 CB LEU A 85 -23.530 0.352 23.953 1.00 13.71 C ANISOU 676 CB LEU A 85 1389 2308 1511 -26 -272 -66 C ATOM 677 CG LEU A 85 -23.105 1.682 23.319 1.00 10.39 C ANISOU 677 CG LEU A 85 892 1787 1268 -16 -237 -36 C ATOM 678 CD1 LEU A 85 -22.731 2.691 24.432 1.00 11.23 C ANISOU 678 CD1 LEU A 85 949 1805 1511 7 -367 -142 C ATOM 679 CD2 LEU A 85 -21.943 1.462 22.302 1.00 13.34 C ANISOU 679 CD2 LEU A 85 1212 2066 1790 -22 -125 54 C ATOM 680 N VAL A 86 -25.714 -2.063 23.990 1.00 9.07 N ANISOU 680 N VAL A 86 893 1888 667 -67 -176 -47 N ATOM 681 CA VAL A 86 -26.269 -3.273 24.580 1.00 9.72 C ANISOU 681 CA VAL A 86 1003 1983 708 -86 -119 -41 C ATOM 682 C VAL A 86 -26.127 -4.445 23.612 1.00 10.03 C ANISOU 682 C VAL A 86 1024 2017 769 -125 -121 -26 C ATOM 683 O VAL A 86 -25.757 -5.556 23.996 1.00 11.48 O ANISOU 683 O VAL A 86 1246 2181 936 -140 -92 -6 O ATOM 684 CB VAL A 86 -27.746 -3.046 24.943 1.00 10.73 C ANISOU 684 CB VAL A 86 1084 2118 874 -84 -42 -55 C ATOM 685 CG1 VAL A 86 -28.319 -4.334 25.548 1.00 10.63 C ANISOU 685 CG1 VAL A 86 1078 2070 892 -105 83 -21 C ATOM 686 CG2 VAL A 86 -27.874 -1.866 25.911 1.00 10.30 C ANISOU 686 CG2 VAL A 86 1078 2065 770 -19 -33 -78 C ATOM 687 N LEU A 87 -26.480 -4.217 22.349 1.00 9.26 N ANISOU 687 N LEU A 87 897 1929 692 -113 -165 -43 N ATOM 688 CA LEU A 87 -26.437 -5.273 21.347 1.00 10.17 C ANISOU 688 CA LEU A 87 1030 2030 803 -110 -201 -61 C ATOM 689 C LEU A 87 -25.002 -5.693 21.060 1.00 15.46 C ANISOU 689 C LEU A 87 1763 2683 1427 -95 -173 -14 C ATOM 690 O LEU A 87 -24.717 -6.887 20.900 1.00 12.93 O ANISOU 690 O LEU A 87 1465 2344 1105 -110 -173 -22 O ATOM 691 CB LEU A 87 -27.120 -4.775 20.070 1.00 9.90 C ANISOU 691 CB LEU A 87 1012 2001 747 -35 -292 -107 C ATOM 692 CG LEU A 87 -28.578 -4.344 20.245 1.00 10.54 C ANISOU 692 CG LEU A 87 991 2080 935 -38 -351 -175 C ATOM 693 CD1 LEU A 87 -29.180 -3.947 18.868 1.00 11.55 C ANISOU 693 CD1 LEU A 87 1171 2198 1020 82 -508 -244 C ATOM 694 CD2 LEU A 87 -29.426 -5.455 20.893 1.00 11.18 C ANISOU 694 CD2 LEU A 87 949 2110 1188 -118 -324 -222 C ATOM 695 N ALA A 88 -24.082 -4.724 20.973 1.00 9.97 N ANISOU 695 N ALA A 88 1074 1970 743 -66 -139 31 N ATOM 696 CA ALA A 88 -22.685 -5.085 20.777 1.00 9.82 C ANISOU 696 CA ALA A 88 1063 1902 767 -55 -89 75 C ATOM 697 C ALA A 88 -22.171 -5.891 21.956 1.00 13.52 C ANISOU 697 C ALA A 88 1514 2359 1265 -96 -128 56 C ATOM 698 O ALA A 88 -21.420 -6.866 21.779 1.00 9.94 O ANISOU 698 O ALA A 88 1073 1877 825 -94 -113 68 O ATOM 699 CB ALA A 88 -21.824 -3.828 20.574 1.00 9.48 C ANISOU 699 CB ALA A 88 972 1791 840 -27 -26 125 C ATOM 700 N GLN A 89 -22.573 -5.501 23.172 1.00 9.36 N ANISOU 700 N GLN A 89 988 1847 723 -105 -175 27 N ATOM 701 CA GLN A 89 -22.082 -6.193 24.359 1.00 9.77 C ANISOU 701 CA GLN A 89 1090 1876 745 -85 -222 13 C ATOM 702 C GLN A 89 -22.614 -7.605 24.402 1.00 11.82 C ANISOU 702 C GLN A 89 1403 2143 946 -109 -164 40 C ATOM 703 O GLN A 89 -21.874 -8.539 24.722 1.00 12.37 O ANISOU 703 O GLN A 89 1515 2177 1008 -90 -182 54 O ATOM 704 CB GLN A 89 -22.487 -5.461 25.640 1.00 9.57 C ANISOU 704 CB GLN A 89 1125 1856 655 -33 -270 -23 C ATOM 705 CG GLN A 89 -21.609 -5.877 26.856 1.00 13.48 C ANISOU 705 CG GLN A 89 1725 2303 1094 59 -382 -58 C ATOM 706 CD GLN A 89 -20.126 -5.630 26.572 1.00 15.37 C ANISOU 706 CD GLN A 89 1858 2466 1517 69 -514 -108 C ATOM 707 OE1 GLN A 89 -19.770 -4.560 26.094 1.00 15.29 O ANISOU 707 OE1 GLN A 89 1724 2414 1672 43 -537 -136 O ATOM 708 NE2 GLN A 89 -19.263 -6.622 26.858 1.00 13.60 N ANISOU 708 NE2 GLN A 89 1666 2198 1305 109 -582 -113 N ATOM 709 N SER A 90 -23.902 -7.771 24.073 1.00 10.87 N ANISOU 709 N SER A 90 1259 2045 828 -146 -103 39 N ATOM 710 CA SER A 90 -24.478 -9.107 24.001 1.00 11.46 C ANISOU 710 CA SER A 90 1334 2081 940 -183 -44 51 C ATOM 711 C SER A 90 -23.745 -9.956 22.979 1.00 14.77 C ANISOU 711 C SER A 90 1754 2481 1378 -188 -86 36 C ATOM 712 O SER A 90 -23.507 -11.145 23.214 1.00 13.71 O ANISOU 712 O SER A 90 1651 2295 1264 -199 -60 55 O ATOM 713 CB SER A 90 -25.959 -9.026 23.633 1.00 12.13 C ANISOU 713 CB SER A 90 1327 2155 1127 -223 -12 16 C ATOM 714 OG SER A 90 -26.526 -10.328 23.566 1.00 15.87 O ANISOU 714 OG SER A 90 1756 2545 1727 -267 39 12 O ATOM 715 N SER A 91 -23.387 -9.358 21.836 1.00 11.41 N ANISOU 715 N SER A 91 1318 2081 937 -160 -126 14 N ATOM 716 CA SER A 91 -22.631 -10.075 20.809 1.00 11.20 C ANISOU 716 CA SER A 91 1331 2028 896 -124 -129 7 C ATOM 717 C SER A 91 -21.298 -10.568 21.367 1.00 12.00 C ANISOU 717 C SER A 91 1439 2094 1026 -116 -106 49 C ATOM 718 O SER A 91 -20.891 -11.707 21.115 1.00 14.03 O ANISOU 718 O SER A 91 1726 2312 1294 -108 -99 44 O ATOM 719 CB SER A 91 -22.388 -9.165 19.596 1.00 13.23 C ANISOU 719 CB SER A 91 1628 2301 1098 -46 -112 14 C ATOM 720 OG SER A 91 -23.614 -8.828 18.940 1.00 12.60 O ANISOU 720 OG SER A 91 1567 2244 975 -14 -187 -47 O ATOM 721 N ILE A 92 -20.604 -9.697 22.103 1.00 10.95 N ANISOU 721 N ILE A 92 1270 1958 934 -105 -122 69 N ATOM 722 CA AILE A 92 -19.322 -10.042 22.719 0.46 13.83 C ANISOU 722 CA AILE A 92 1613 2265 1376 -77 -162 76 C ATOM 723 CA BILE A 92 -19.319 -10.073 22.686 0.54 11.90 C ANISOU 723 CA BILE A 92 1370 2021 1132 -77 -160 76 C ATOM 724 C ILE A 92 -19.482 -11.236 23.654 1.00 14.04 C ANISOU 724 C ILE A 92 1723 2275 1338 -70 -194 82 C ATOM 725 O ILE A 92 -18.691 -12.184 23.631 1.00 14.32 O ANISOU 725 O ILE A 92 1770 2261 1410 -46 -207 89 O ATOM 726 CB AILE A 92 -18.759 -8.816 23.465 0.46 9.84 C ANISOU 726 CB AILE A 92 1043 1732 962 -53 -242 49 C ATOM 727 CB BILE A 92 -18.667 -8.857 23.363 0.54 22.30 C ANISOU 727 CB BILE A 92 2615 3306 2552 -53 -235 52 C ATOM 728 CG1AILE A 92 -18.176 -7.790 22.484 0.46 27.42 C ANISOU 728 CG1AILE A 92 3162 3914 3344 -52 -161 72 C ATOM 729 CG1BILE A 92 -18.241 -7.853 22.297 0.54 10.51 C ANISOU 729 CG1BILE A 92 1028 1777 1189 -53 -141 80 C ATOM 730 CG2AILE A 92 -17.727 -9.239 24.521 0.46 22.10 C ANISOU 730 CG2AILE A 92 2598 3218 2582 7 -380 9 C ATOM 731 CG2BILE A 92 -17.456 -9.285 24.204 0.54 10.72 C ANISOU 731 CG2BILE A 92 1122 1761 1191 1 -358 15 C ATOM 732 CD1AILE A 92 -16.760 -8.100 22.019 0.46 13.84 C ANISOU 732 CD1AILE A 92 1339 2088 1833 -24 -107 92 C ATOM 733 CD1BILE A 92 -17.789 -6.569 22.877 0.54 10.56 C ANISOU 733 CD1BILE A 92 932 1723 1359 -46 -212 44 C ATOM 734 N PHE A 93 -20.514 -11.199 24.502 1.00 11.54 N ANISOU 734 N PHE A 93 1472 1980 932 -77 -177 95 N ATOM 735 CA PHE A 93 -20.738 -12.310 25.423 1.00 17.23 C ANISOU 735 CA PHE A 93 2304 2654 1590 -46 -141 139 C ATOM 736 C PHE A 93 -21.042 -13.597 24.656 1.00 16.50 C ANISOU 736 C PHE A 93 2190 2517 1563 -102 -71 152 C ATOM 737 O PHE A 93 -20.551 -14.671 25.012 1.00 12.43 O ANISOU 737 O PHE A 93 1739 1937 1047 -71 -64 185 O ATOM 738 CB PHE A 93 -21.883 -11.980 26.395 1.00 13.16 C ANISOU 738 CB PHE A 93 1868 2144 989 -25 -52 177 C ATOM 739 CG PHE A 93 -21.501 -11.019 27.510 1.00 18.09 C ANISOU 739 CG PHE A 93 2597 2784 1494 88 -143 155 C ATOM 740 CD1 PHE A 93 -22.351 -9.986 27.880 1.00 12.88 C ANISOU 740 CD1 PHE A 93 1946 2162 785 100 -100 144 C ATOM 741 CD2 PHE A 93 -20.304 -11.161 28.191 1.00 29.91 C ANISOU 741 CD2 PHE A 93 4184 4241 2939 204 -303 122 C ATOM 742 CE1 PHE A 93 -22.014 -9.112 28.901 1.00 15.70 C ANISOU 742 CE1 PHE A 93 2424 2520 1022 229 -210 96 C ATOM 743 CE2 PHE A 93 -19.960 -10.287 29.213 1.00 35.14 C ANISOU 743 CE2 PHE A 93 4944 4886 3521 328 -442 58 C ATOM 744 CZ PHE A 93 -20.823 -9.259 29.567 1.00 21.59 C ANISOU 744 CZ PHE A 93 3243 3197 1765 326 -383 44 C ATOM 745 N SER A 94 -21.843 -13.512 23.589 1.00 10.91 N ANISOU 745 N SER A 94 1401 1827 916 -166 -50 108 N ATOM 746 CA SER A 94 -22.113 -14.719 22.805 1.00 13.02 C ANISOU 746 CA SER A 94 1651 2030 1265 -197 -41 75 C ATOM 747 C SER A 94 -20.842 -15.261 22.160 1.00 14.24 C ANISOU 747 C SER A 94 1834 2171 1407 -151 -79 62 C ATOM 748 O SER A 94 -20.617 -16.479 22.141 1.00 15.41 O ANISOU 748 O SER A 94 2011 2242 1601 -150 -68 63 O ATOM 749 CB SER A 94 -23.174 -14.435 21.749 1.00 13.96 C ANISOU 749 CB SER A 94 1699 2159 1446 -227 -87 -13 C ATOM 750 OG SER A 94 -24.417 -14.164 22.399 1.00 17.82 O ANISOU 750 OG SER A 94 2120 2623 2026 -278 -29 -2 O ATOM 751 N LEU A 95 -20.015 -14.378 21.601 1.00 14.39 N ANISOU 751 N LEU A 95 1834 2239 1395 -108 -95 56 N ATOM 752 CA LEU A 95 -18.785 -14.820 20.944 1.00 12.88 C ANISOU 752 CA LEU A 95 1648 2012 1235 -52 -75 57 C ATOM 753 C LEU A 95 -17.831 -15.464 21.934 1.00 16.47 C ANISOU 753 C LEU A 95 2101 2411 1744 -29 -108 90 C ATOM 754 O LEU A 95 -17.168 -16.458 21.613 1.00 16.69 O ANISOU 754 O LEU A 95 2145 2381 1816 3 -95 86 O ATOM 755 CB LEU A 95 -18.092 -13.638 20.256 1.00 11.67 C ANISOU 755 CB LEU A 95 1450 1880 1104 -5 -19 75 C ATOM 756 CG LEU A 95 -18.823 -13.104 19.031 1.00 10.84 C ANISOU 756 CG LEU A 95 1408 1812 899 36 19 52 C ATOM 757 CD1 LEU A 95 -18.246 -11.708 18.654 1.00 17.26 C ANISOU 757 CD1 LEU A 95 2180 2624 1753 78 118 113 C ATOM 758 CD2 LEU A 95 -18.676 -14.060 17.846 1.00 13.14 C ANISOU 758 CD2 LEU A 95 1809 2066 1118 124 49 11 C ATOM 759 N LEU A 96 -17.727 -14.894 23.132 1.00 12.93 N ANISOU 759 N LEU A 96 1657 1974 1283 -16 -172 110 N ATOM 760 CA LEU A 96 -16.869 -15.480 24.156 1.00 13.32 C ANISOU 760 CA LEU A 96 1751 1961 1349 54 -259 124 C ATOM 761 C LEU A 96 -17.387 -16.852 24.575 1.00 17.91 C ANISOU 761 C LEU A 96 2449 2487 1868 57 -211 171 C ATOM 762 O LEU A 96 -16.608 -17.804 24.733 1.00 17.37 O ANISOU 762 O LEU A 96 2414 2349 1838 111 -245 182 O ATOM 763 CB LEU A 96 -16.786 -14.525 25.354 1.00 12.15 C ANISOU 763 CB LEU A 96 1640 1827 1150 115 -376 108 C ATOM 764 CG LEU A 96 -15.924 -14.954 26.539 1.00 22.43 C ANISOU 764 CG LEU A 96 3038 3058 2426 249 -540 93 C ATOM 765 CD1 LEU A 96 -14.521 -15.282 26.070 1.00 27.36 C ANISOU 765 CD1 LEU A 96 3522 3609 3265 280 -624 45 C ATOM 766 CD2 LEU A 96 -15.906 -13.843 27.608 1.00 24.62 C ANISOU 766 CD2 LEU A 96 3377 3345 2632 343 -698 35 C ATOM 767 N ALA A 97 -18.709 -16.979 24.729 1.00 15.37 N ANISOU 767 N ALA A 97 2170 2172 1499 -2 -116 202 N ATOM 768 CA ALA A 97 -19.304 -18.256 25.106 1.00 19.30 C ANISOU 768 CA ALA A 97 2745 2571 2017 -13 -20 262 C ATOM 769 C ALA A 97 -19.045 -19.313 24.049 1.00 15.96 C ANISOU 769 C ALA A 97 2270 2088 1706 -49 -20 215 C ATOM 770 O ALA A 97 -18.772 -20.474 24.374 1.00 15.57 O ANISOU 770 O ALA A 97 2285 1936 1693 -19 9 257 O ATOM 771 CB ALA A 97 -20.809 -18.102 25.318 1.00 17.33 C ANISOU 771 CB ALA A 97 2477 2303 1804 -83 110 293 C ATOM 772 N ILE A 98 -19.183 -18.941 22.777 1.00 15.60 N ANISOU 772 N ILE A 98 2140 2093 1695 -88 -48 126 N ATOM 773 CA ILE A 98 -18.940 -19.887 21.695 1.00 13.09 C ANISOU 773 CA ILE A 98 1817 1717 1441 -79 -64 56 C ATOM 774 C ILE A 98 -17.505 -20.381 21.753 1.00 17.98 C ANISOU 774 C ILE A 98 2461 2307 2065 -1 -78 78 C ATOM 775 O ILE A 98 -17.249 -21.579 21.613 1.00 20.39 O ANISOU 775 O ILE A 98 2801 2517 2430 18 -72 69 O ATOM 776 CB ILE A 98 -19.276 -19.237 20.337 1.00 12.82 C ANISOU 776 CB ILE A 98 1760 1745 1366 -66 -100 -42 C ATOM 777 CG1 ILE A 98 -20.792 -19.038 20.224 1.00 14.69 C ANISOU 777 CG1 ILE A 98 1949 1971 1663 -134 -135 -99 C ATOM 778 CG2 ILE A 98 -18.710 -20.083 19.183 1.00 13.96 C ANISOU 778 CG2 ILE A 98 1961 1837 1507 11 -117 -119 C ATOM 779 CD1 ILE A 98 -21.286 -18.133 19.039 1.00 15.65 C ANISOU 779 CD1 ILE A 98 2080 2163 1703 -86 -214 -195 C ATOM 780 N ALA A 99 -16.549 -19.474 21.999 1.00 15.41 N ANISOU 780 N ALA A 99 2093 2037 1725 47 -105 100 N ATOM 781 CA ALA A 99 -15.150 -19.893 22.080 1.00 17.18 C ANISOU 781 CA ALA A 99 2288 2207 2034 125 -133 105 C ATOM 782 C ALA A 99 -14.955 -20.860 23.234 1.00 17.47 C ANISOU 782 C ALA A 99 2412 2163 2064 169 -194 155 C ATOM 783 O ALA A 99 -14.293 -21.897 23.099 1.00 17.02 O ANISOU 783 O ALA A 99 2371 2021 2073 219 -199 153 O ATOM 784 CB ALA A 99 -14.230 -18.685 22.255 1.00 18.02 C ANISOU 784 CB ALA A 99 2281 2342 2224 161 -172 102 C ATOM 785 N ILE A 100 -15.526 -20.523 24.389 1.00 15.77 N ANISOU 785 N ILE A 100 2282 1961 1750 179 -225 209 N ATOM 786 CA ILE A 100 -15.332 -21.353 25.566 1.00 20.82 C ANISOU 786 CA ILE A 100 3072 2513 2326 276 -262 281 C ATOM 787 C ILE A 100 -15.990 -22.708 25.366 1.00 18.25 C ANISOU 787 C ILE A 100 2811 2081 2044 231 -134 332 C ATOM 788 O ILE A 100 -15.426 -23.738 25.736 1.00 19.09 O ANISOU 788 O ILE A 100 3001 2084 2170 311 -151 374 O ATOM 789 CB ILE A 100 -15.853 -20.626 26.818 1.00 17.00 C ANISOU 789 CB ILE A 100 2724 2059 1678 342 -287 334 C ATOM 790 CG1 ILE A 100 -14.907 -19.460 27.151 1.00 21.24 C ANISOU 790 CG1 ILE A 100 3195 2649 2225 422 -490 249 C ATOM 791 CG2 ILE A 100 -15.982 -21.600 28.005 1.00 17.92 C ANISOU 791 CG2 ILE A 100 3081 2062 1664 475 -246 451 C ATOM 792 CD1 ILE A 100 -15.438 -18.519 28.208 1.00 22.31 C ANISOU 792 CD1 ILE A 100 3462 2827 2186 497 -541 260 C ATOM 793 N ASP A 101 -17.179 -22.728 24.753 1.00 16.47 N ANISOU 793 N ASP A 101 2529 1857 1873 110 -24 315 N ATOM 794 CA ASP A 101 -17.855 -23.989 24.463 1.00 18.81 C ANISOU 794 CA ASP A 101 2831 2011 2305 53 75 328 C ATOM 795 C ASP A 101 -16.982 -24.898 23.607 1.00 21.12 C ANISOU 795 C ASP A 101 3098 2248 2680 83 14 254 C ATOM 796 O ASP A 101 -16.864 -26.107 23.864 1.00 20.78 O ANISOU 796 O ASP A 101 3116 2061 2719 109 55 298 O ATOM 797 CB ASP A 101 -19.178 -23.707 23.745 1.00 19.68 C ANISOU 797 CB ASP A 101 2828 2123 2528 -71 123 257 C ATOM 798 CG ASP A 101 -19.873 -24.973 23.312 1.00 33.59 C ANISOU 798 CG ASP A 101 4541 3703 4520 -136 174 218 C ATOM 799 OD1 ASP A 101 -20.484 -25.618 24.176 1.00 29.36 O ANISOU 799 OD1 ASP A 101 4039 3017 4100 -154 330 336 O ATOM 800 OD2 ASP A 101 -19.807 -25.332 22.118 1.00 29.67 O ANISOU 800 OD2 ASP A 101 3985 3191 4098 -149 69 70 O ATOM 801 N ARG A 102 -16.381 -24.335 22.558 1.00 19.07 N ANISOU 801 N ARG A 102 2758 2084 2402 93 -52 152 N ATOM 802 CA ARG A 102 -15.514 -25.139 21.701 1.00 18.95 C ANISOU 802 CA ARG A 102 2736 2014 2451 151 -72 85 C ATOM 803 C ARG A 102 -14.250 -25.590 22.430 1.00 25.06 C ANISOU 803 C ARG A 102 3537 2737 3246 254 -114 146 C ATOM 804 O ARG A 102 -13.728 -26.672 22.134 1.00 21.52 O ANISOU 804 O ARG A 102 3112 2186 2877 302 -111 126 O ATOM 805 CB ARG A 102 -15.151 -24.358 20.435 1.00 21.47 C ANISOU 805 CB ARG A 102 3003 2430 2725 180 -66 -6 C ATOM 806 CG ARG A 102 -16.334 -23.992 19.519 1.00 26.23 C ANISOU 806 CG ARG A 102 3615 3070 3283 131 -80 -100 C ATOM 807 CD ARG A 102 -17.003 -25.235 18.929 1.00 34.62 C ANISOU 807 CD ARG A 102 4716 3998 4441 122 -128 -206 C ATOM 808 NE ARG A 102 -17.915 -25.872 19.875 1.00 73.04 N ANISOU 808 NE ARG A 102 9545 8749 9456 20 -114 -154 N ATOM 809 CZ ARG A 102 -18.067 -27.186 20.001 1.00 44.19 C ANISOU 809 CZ ARG A 102 5902 4919 5968 5 -108 -168 C ATOM 810 NH1 ARG A 102 -17.358 -28.010 19.243 1.00 44.54 N ANISOU 810 NH1 ARG A 102 5998 4900 6024 87 -152 -255 N ATOM 811 NH2 ARG A 102 -18.914 -27.678 20.898 1.00 36.73 N ANISOU 811 NH2 ARG A 102 4921 3842 5193 -82 -27 -83 N ATOM 812 N TYR A 103 -13.742 -24.791 23.375 1.00 20.36 N ANISOU 812 N TYR A 103 2942 2198 2595 307 -186 198 N ATOM 813 CA TYR A 103 -12.584 -25.241 24.154 1.00 22.62 C ANISOU 813 CA TYR A 103 3260 2414 2920 436 -294 228 C ATOM 814 C TYR A 103 -12.932 -26.425 25.048 1.00 24.81 C ANISOU 814 C TYR A 103 3715 2562 3148 490 -273 326 C ATOM 815 O TYR A 103 -12.151 -27.379 25.156 1.00 25.30 O ANISOU 815 O TYR A 103 3812 2520 3279 582 -319 335 O ATOM 816 CB TYR A 103 -12.013 -24.115 25.012 1.00 18.44 C ANISOU 816 CB TYR A 103 2702 1945 2358 511 -443 221 C ATOM 817 CG TYR A 103 -10.874 -24.592 25.900 1.00 28.79 C ANISOU 817 CG TYR A 103 4059 3162 3719 681 -630 220 C ATOM 818 CD1 TYR A 103 -9.610 -24.821 25.372 1.00 25.66 C ANISOU 818 CD1 TYR A 103 3493 2706 3550 736 -694 147 C ATOM 819 CD2 TYR A 103 -11.072 -24.845 27.252 1.00 38.02 C ANISOU 819 CD2 TYR A 103 5458 4282 4706 815 -733 292 C ATOM 820 CE1 TYR A 103 -8.565 -25.256 26.171 1.00 33.12 C ANISOU 820 CE1 TYR A 103 4453 3548 4582 906 -909 121 C ATOM 821 CE2 TYR A 103 -10.028 -25.298 28.059 1.00 33.22 C ANISOU 821 CE2 TYR A 103 4927 3577 4118 1016 -956 272 C ATOM 822 CZ TYR A 103 -8.780 -25.496 27.511 1.00 30.68 C ANISOU 822 CZ TYR A 103 4393 3200 4064 1052 -1068 174 C ATOM 823 OH TYR A 103 -7.745 -25.943 28.308 1.00 36.51 O ANISOU 823 OH TYR A 103 5185 3826 4862 1264 -1331 131 O ATOM 824 N ILE A 104 -14.076 -26.374 25.726 1.00 23.44 N ANISOU 824 N ILE A 104 3659 2374 2874 451 -176 417 N ATOM 825 CA ILE A 104 -14.487 -27.520 26.547 1.00 21.48 C ANISOU 825 CA ILE A 104 3593 1963 2606 510 -73 549 C ATOM 826 C ILE A 104 -14.640 -28.771 25.686 1.00 27.94 C ANISOU 826 C ILE A 104 4351 2649 3617 436 9 515 C ATOM 827 O ILE A 104 -14.235 -29.876 26.081 1.00 27.08 O ANISOU 827 O ILE A 104 4350 2391 3550 524 25 584 O ATOM 828 CB ILE A 104 -15.790 -27.193 27.297 1.00 21.89 C ANISOU 828 CB ILE A 104 3749 1995 2573 473 101 666 C ATOM 829 CG1 ILE A 104 -15.597 -25.980 28.209 1.00 25.82 C ANISOU 829 CG1 ILE A 104 4349 2613 2847 584 0 684 C ATOM 830 CG2 ILE A 104 -16.270 -28.413 28.111 1.00 26.73 C ANISOU 830 CG2 ILE A 104 4553 2393 3209 541 296 842 C ATOM 831 CD1 ILE A 104 -16.911 -25.418 28.759 1.00 33.65 C ANISOU 831 CD1 ILE A 104 5411 3614 3761 540 195 777 C ATOM 832 N ALA A 105 -15.219 -28.622 24.497 1.00 24.59 N ANISOU 832 N ALA A 105 3775 2262 3306 298 37 395 N ATOM 833 CA ALA A 105 -15.438 -29.786 23.639 1.00 25.61 C ANISOU 833 CA ALA A 105 3861 2250 3621 247 70 320 C ATOM 834 C ALA A 105 -14.121 -30.408 23.168 1.00 28.04 C ANISOU 834 C ALA A 105 4168 2533 3952 351 -17 260 C ATOM 835 O ALA A 105 -14.014 -31.634 23.068 1.00 33.84 O ANISOU 835 O ALA A 105 4944 3100 4812 375 9 262 O ATOM 836 CB ALA A 105 -16.309 -29.398 22.446 1.00 24.48 C ANISOU 836 CB ALA A 105 3592 2154 3554 132 51 166 C ATOM 837 N ILE A 106 -13.101 -29.598 22.901 1.00 31.94 N ANISOU 837 N ILE A 106 4600 3164 4373 418 -102 212 N ATOM 838 CA ILE A 106 -11.834 -30.161 22.436 1.00 29.57 C ANISOU 838 CA ILE A 106 4264 2819 4153 523 -148 158 C ATOM 839 C ILE A 106 -10.935 -30.613 23.586 1.00 42.29 C ANISOU 839 C ILE A 106 5948 4352 5769 659 -240 252 C ATOM 840 O ILE A 106 -10.119 -31.521 23.407 1.00 36.25 O ANISOU 840 O ILE A 106 5183 3482 5110 747 -267 231 O ATOM 841 CB ILE A 106 -11.086 -29.163 21.536 1.00 42.74 C ANISOU 841 CB ILE A 106 5800 4616 5824 547 -145 72 C ATOM 842 CG1 ILE A 106 -10.026 -29.888 20.703 1.00 37.04 C ANISOU 842 CG1 ILE A 106 5035 3818 5221 648 -108 4 C ATOM 843 CG2 ILE A 106 -10.400 -28.079 22.371 1.00 33.56 C ANISOU 843 CG2 ILE A 106 4563 3535 4654 593 -238 117 C ATOM 844 CD1 ILE A 106 -9.804 -29.249 19.366 1.00 73.48 C ANISOU 844 CD1 ILE A 106 9594 8508 9816 670 8 -79 C ATOM 845 N ALA A 107 -11.053 -30.001 24.761 1.00 40.29 N ANISOU 845 N ALA A 107 5779 4138 5390 707 -308 342 N ATOM 846 CA ALA A 107 -10.090 -30.248 25.825 1.00 35.52 C ANISOU 846 CA ALA A 107 5271 3470 4756 893 -469 393 C ATOM 847 C ALA A 107 -10.569 -31.318 26.793 1.00 49.58 C ANISOU 847 C ALA A 107 7303 5091 6443 979 -407 545 C ATOM 848 O ALA A 107 -9.759 -32.087 27.318 1.00 45.56 O ANISOU 848 O ALA A 107 6895 4467 5947 1147 -513 580 O ATOM 849 CB ALA A 107 -9.791 -28.946 26.578 1.00 41.04 C ANISOU 849 CB ALA A 107 5958 4281 5355 961 -632 374 C ATOM 850 N ILE A 108 -11.870 -31.384 27.047 1.00 35.01 N ANISOU 850 N ILE A 108 5557 3215 4531 882 -218 645 N ATOM 851 CA ILE A 108 -12.411 -32.440 27.896 1.00 42.07 C ANISOU 851 CA ILE A 108 6683 3912 5390 958 -65 825 C ATOM 852 C ILE A 108 -13.662 -33.017 27.244 1.00 41.49 C ANISOU 852 C ILE A 108 6521 3728 5516 757 173 840 C ATOM 853 O ILE A 108 -14.763 -32.888 27.794 1.00 39.89 O ANISOU 853 O ILE A 108 6393 3464 5300 708 371 964 O ATOM 854 CB ILE A 108 -12.700 -31.919 29.311 1.00 50.80 C ANISOU 854 CB ILE A 108 8057 5023 6220 1125 -49 978 C ATOM 855 CG1 ILE A 108 -13.409 -30.566 29.250 1.00 41.48 C ANISOU 855 CG1 ILE A 108 6789 4019 4954 1013 -24 931 C ATOM 856 CG2 ILE A 108 -11.408 -31.813 30.105 1.00 75.62 C ANISOU 856 CG2 ILE A 108 11307 8209 9216 1361 -334 934 C ATOM 857 CD1 ILE A 108 -13.998 -30.139 30.580 1.00 58.31 C ANISOU 857 CD1 ILE A 108 9178 6154 6824 1147 73 1074 C ATOM 858 N PRO A 109 -13.545 -33.669 26.085 1.00 48.18 N ANISOU 858 N PRO A 109 7962 4498 5848 660 17 1272 N ATOM 859 CA PRO A 109 -14.751 -34.188 25.418 1.00 41.39 C ANISOU 859 CA PRO A 109 7200 3189 5336 406 110 1238 C ATOM 860 C PRO A 109 -15.515 -35.227 26.232 1.00 69.99 C ANISOU 860 C PRO A 109 10939 6513 9140 449 405 1539 C ATOM 861 O PRO A 109 -16.715 -35.409 25.995 1.00 45.92 O ANISOU 861 O PRO A 109 7869 3163 6416 187 514 1440 O ATOM 862 CB PRO A 109 -14.202 -34.785 24.114 1.00 52.55 C ANISOU 862 CB PRO A 109 8700 4354 6912 424 46 1076 C ATOM 863 CG PRO A 109 -12.744 -35.027 24.384 1.00 50.84 C ANISOU 863 CG PRO A 109 8491 4358 6466 728 17 1181 C ATOM 864 CD PRO A 109 -12.322 -33.924 25.302 1.00 44.49 C ANISOU 864 CD PRO A 109 7501 4045 5357 800 -68 1144 C ATOM 865 N LEU A 110 -14.871 -35.903 27.189 1.00 47.34 N ANISOU 865 N LEU A 110 8194 3716 6078 810 578 1882 N ATOM 866 CA LEU A 110 -15.564 -36.945 27.941 1.00 57.84 C ANISOU 866 CA LEU A 110 9669 4714 7593 889 970 2192 C ATOM 867 C LEU A 110 -16.601 -36.368 28.896 1.00 93.54 C ANISOU 867 C LEU A 110 14135 9326 12079 781 1099 2296 C ATOM 868 O LEU A 110 -17.572 -37.052 29.242 1.00 57.18 O ANISOU 868 O LEU A 110 9520 4429 7776 640 1403 2350 O ATOM 869 CB LEU A 110 -14.558 -37.799 28.712 1.00 60.42 C ANISOU 869 CB LEU A 110 10110 5213 7633 1368 1099 2465 C ATOM 870 CG LEU A 110 -13.624 -38.658 27.864 1.00 79.39 C ANISOU 870 CG LEU A 110 12574 7469 10120 1478 1051 2398 C ATOM 871 CD1 LEU A 110 -12.718 -39.497 28.753 1.00 70.99 C ANISOU 871 CD1 LEU A 110 11639 6601 8734 1994 1209 2660 C ATOM 872 CD2 LEU A 110 -14.428 -39.537 26.916 1.00 63.49 C ANISOU 872 CD2 LEU A 110 10542 4930 8652 1115 1203 2228 C ATOM 873 N ARG A 111 -16.420 -35.127 29.340 1.00 53.11 N ANISOU 873 N ARG A 111 8887 4682 6609 811 850 2226 N ATOM 874 CA ARG A 111 -17.347 -34.514 30.281 1.00 62.18 C ANISOU 874 CA ARG A 111 9981 5965 7680 734 947 2327 C ATOM 875 C ARG A 111 -18.084 -33.322 29.693 1.00 62.95 C ANISOU 875 C ARG A 111 9854 6184 7879 307 689 1955 C ATOM 876 O ARG A 111 -18.826 -32.651 30.418 1.00 45.38 O ANISOU 876 O ARG A 111 7551 4122 5568 220 716 1993 O ATOM 877 CB ARG A 111 -16.615 -34.101 31.559 1.00 75.80 C ANISOU 877 CB ARG A 111 11704 8233 8862 1203 886 2533 C ATOM 878 CG ARG A 111 -15.265 -33.458 31.341 1.00 62.83 C ANISOU 878 CG ARG A 111 9878 7090 6904 1389 513 2266 C ATOM 879 CD ARG A 111 -14.592 -33.189 32.680 1.00117.59 C ANISOU 879 CD ARG A 111 16762 14598 13319 1933 445 2382 C ATOM 880 NE ARG A 111 -13.136 -33.208 32.585 1.00110.30 N ANISOU 880 NE ARG A 111 15709 14058 12141 2284 209 2177 N ATOM 881 CZ ARG A 111 -12.318 -33.051 33.620 1.00105.68 C ANISOU 881 CZ ARG A 111 15015 14056 11082 2855 73 2142 C ATOM 882 NH1 ARG A 111 -12.813 -32.859 34.837 1.00111.20 N ANISOU 882 NH1 ARG A 111 15716 14999 11535 3097 164 2277 N ATOM 883 NH2 ARG A 111 -11.005 -33.085 33.440 1.00 88.88 N ANISOU 883 NH2 ARG A 111 12709 12274 8789 3146 -152 1859 N ATOM 884 N TYR A 112 -17.905 -33.046 28.399 1.00 42.65 N ANISOU 884 N TYR A 112 7210 3540 5456 95 463 1615 N ATOM 885 CA TYR A 112 -18.606 -31.932 27.772 1.00 37.09 C ANISOU 885 CA TYR A 112 6360 2940 4792 -205 256 1283 C ATOM 886 C TYR A 112 -20.119 -32.064 27.940 1.00 73.09 C ANISOU 886 C TYR A 112 10870 7248 9652 -459 407 1234 C ATOM 887 O TYR A 112 -20.777 -31.172 28.490 1.00 41.80 O ANISOU 887 O TYR A 112 6807 3502 5572 -570 363 1206 O ATOM 888 CB TYR A 112 -18.224 -31.837 26.290 1.00 35.39 C ANISOU 888 CB TYR A 112 6158 2615 4673 -274 69 970 C ATOM 889 CG TYR A 112 -19.033 -30.803 25.542 1.00 33.12 C ANISOU 889 CG TYR A 112 5797 2394 4392 -470 -96 647 C ATOM 890 CD1 TYR A 112 -18.625 -29.481 25.495 1.00 30.72 C ANISOU 890 CD1 TYR A 112 5449 2413 3812 -462 -212 542 C ATOM 891 CD2 TYR A 112 -20.222 -31.144 24.905 1.00 57.41 C ANISOU 891 CD2 TYR A 112 8836 5213 7764 -629 -107 406 C ATOM 892 CE1 TYR A 112 -19.374 -28.522 24.825 1.00 35.76 C ANISOU 892 CE1 TYR A 112 6085 3096 4405 -561 -309 291 C ATOM 893 CE2 TYR A 112 -20.975 -30.197 24.235 1.00 45.75 C ANISOU 893 CE2 TYR A 112 7311 3856 6217 -699 -280 95 C ATOM 894 CZ TYR A 112 -20.547 -28.889 24.198 1.00 39.88 C ANISOU 894 CZ TYR A 112 6602 3416 5134 -642 -367 82 C ATOM 895 OH TYR A 112 -21.301 -27.950 23.528 1.00 36.15 O ANISOU 895 OH TYR A 112 6145 3043 4548 -634 -488 -186 O ATOM 896 N ASN A 113 -20.691 -33.183 27.485 1.00 44.56 N ANISOU 896 N ASN A 113 7293 3166 6472 -564 608 1178 N ATOM 897 CA ASN A 113 -22.147 -33.302 27.450 1.00 97.43 C ANISOU 897 CA ASN A 113 13854 9605 13561 -849 747 969 C ATOM 898 C ASN A 113 -22.768 -33.198 28.838 1.00 54.48 C ANISOU 898 C ASN A 113 8422 4190 8087 -854 1040 1285 C ATOM 899 O ASN A 113 -23.891 -32.700 28.976 1.00 53.01 O ANISOU 899 O ASN A 113 8079 4010 8054 -1086 1048 1096 O ATOM 900 CB ASN A 113 -22.550 -34.611 26.774 1.00 49.73 C ANISOU 900 CB ASN A 113 7793 3024 8078 -962 973 782 C ATOM 901 CG ASN A 113 -22.419 -34.545 25.266 1.00 83.82 C ANISOU 901 CG ASN A 113 12031 7345 12471 -991 629 310 C ATOM 902 OD1 ASN A 113 -22.594 -33.481 24.660 1.00 71.07 O ANISOU 902 OD1 ASN A 113 10345 6052 10607 -997 286 38 O ATOM 903 ND2 ASN A 113 -22.109 -35.678 24.648 1.00 90.66 N ANISOU 903 ND2 ASN A 113 12918 7919 13609 -944 715 221 N ATOM 904 N GLY A 114 -22.061 -33.650 29.875 1.00 55.97 N ANISOU 904 N GLY A 114 8803 4421 8041 -544 1280 1756 N ATOM 905 CA GLY A 114 -22.569 -33.495 31.225 1.00 54.79 C ANISOU 905 CA GLY A 114 8680 4392 7744 -438 1526 2059 C ATOM 906 C GLY A 114 -22.360 -32.118 31.813 1.00 53.43 C ANISOU 906 C GLY A 114 8435 4778 7087 -364 1235 2082 C ATOM 907 O GLY A 114 -23.105 -31.716 32.711 1.00 54.35 O ANISOU 907 O GLY A 114 8523 4988 7140 -388 1378 2216 O ATOM 908 N LEU A 115 -21.362 -31.386 31.325 1.00 45.82 N ANISOU 908 N LEU A 115 7405 4196 5810 -280 844 1904 N ATOM 909 CA LEU A 115 -21.066 -30.055 31.836 1.00 42.92 C ANISOU 909 CA LEU A 115 6900 4367 5042 -228 577 1820 C ATOM 910 C LEU A 115 -21.865 -28.976 31.120 1.00 52.49 C ANISOU 910 C LEU A 115 7953 5637 6353 -586 363 1457 C ATOM 911 O LEU A 115 -22.394 -28.065 31.764 1.00 38.75 O ANISOU 911 O LEU A 115 6114 4154 4454 -655 313 1441 O ATOM 912 CB LEU A 115 -19.566 -29.771 31.708 1.00 52.54 C ANISOU 912 CB LEU A 115 8083 5931 5947 32 348 1747 C ATOM 913 CG LEU A 115 -19.086 -28.330 31.883 1.00 67.32 C ANISOU 913 CG LEU A 115 9741 8295 7541 7 82 1485 C ATOM 914 CD1 LEU A 115 -19.516 -27.771 33.225 1.00 67.93 C ANISOU 914 CD1 LEU A 115 9740 8709 7361 136 112 1619 C ATOM 915 CD2 LEU A 115 -17.576 -28.252 31.731 1.00 58.54 C ANISOU 915 CD2 LEU A 115 8545 7453 6246 251 -66 1342 C ATOM 916 N VAL A 116 -21.989 -29.081 29.804 1.00 34.11 N ANISOU 916 N VAL A 116 5620 3086 4253 -758 243 1167 N ATOM 917 CA VAL A 116 -22.534 -28.018 28.970 1.00 32.04 C ANISOU 917 CA VAL A 116 5271 2927 3974 -947 24 817 C ATOM 918 C VAL A 116 -23.893 -28.500 28.482 1.00 39.40 C ANISOU 918 C VAL A 116 6138 3547 5284 -1157 85 603 C ATOM 919 O VAL A 116 -23.977 -29.297 27.543 1.00 47.40 O ANISOU 919 O VAL A 116 7165 4270 6574 -1179 80 407 O ATOM 920 CB VAL A 116 -21.596 -27.679 27.806 1.00 38.46 C ANISOU 920 CB VAL A 116 6147 3779 4688 -866 -149 613 C ATOM 921 CG1 VAL A 116 -22.097 -26.476 27.039 1.00 40.80 C ANISOU 921 CG1 VAL A 116 6434 4195 4875 -945 -296 321 C ATOM 922 CG2 VAL A 116 -20.183 -27.433 28.327 1.00 41.08 C ANISOU 922 CG2 VAL A 116 6469 4375 4764 -673 -158 751 C ATOM 923 N THR A 117 -24.960 -28.028 29.125 1.00 40.04 N ANISOU 923 N THR A 117 6109 3701 5402 -1303 140 584 N ATOM 924 CA THR A 117 -26.316 -28.471 28.838 1.00 34.94 C ANISOU 924 CA THR A 117 5319 2787 5170 -1516 230 313 C ATOM 925 C THR A 117 -27.139 -27.311 28.300 1.00 36.34 C ANISOU 925 C THR A 117 5384 3210 5212 -1590 -39 -53 C ATOM 926 O THR A 117 -26.822 -26.142 28.525 1.00 30.30 O ANISOU 926 O THR A 117 4673 2781 4059 -1521 -179 21 O ATOM 927 CB THR A 117 -27.010 -29.020 30.093 1.00 42.83 C ANISOU 927 CB THR A 117 6279 3604 6390 -1611 611 590 C ATOM 928 OG1 THR A 117 -27.170 -27.956 31.043 1.00 37.69 O ANISOU 928 OG1 THR A 117 5614 3323 5384 -1585 555 768 O ATOM 929 CG2 THR A 117 -26.196 -30.145 30.717 1.00 41.12 C ANISOU 929 CG2 THR A 117 6251 3147 6226 -1424 943 1020 C ATOM 930 N GLY A 118 -28.234 -27.652 27.619 1.00 32.80 N ANISOU 930 N GLY A 118 5938 2138 4387 -672 127 661 N ATOM 931 CA GLY A 118 -29.096 -26.618 27.068 1.00 30.22 C ANISOU 931 CA GLY A 118 5511 2034 3936 -759 103 518 C ATOM 932 C GLY A 118 -29.693 -25.716 28.130 1.00 32.45 C ANISOU 932 C GLY A 118 5653 2567 4111 -845 105 637 C ATOM 933 O GLY A 118 -29.795 -24.500 27.941 1.00 34.05 O ANISOU 933 O GLY A 118 5742 2997 4198 -813 99 569 O ATOM 934 N THR A 119 -30.100 -26.294 29.259 1.00 30.83 N ANISOU 934 N THR A 119 5456 2319 3940 -953 122 817 N ATOM 935 CA THR A 119 -30.689 -25.494 30.329 1.00 30.39 C ANISOU 935 CA THR A 119 5285 2499 3764 -1033 147 927 C ATOM 936 C THR A 119 -29.664 -24.546 30.938 1.00 29.65 C ANISOU 936 C THR A 119 5142 2578 3547 -878 143 993 C ATOM 937 O THR A 119 -29.980 -23.391 31.242 1.00 35.11 O ANISOU 937 O THR A 119 5727 3500 4112 -887 156 962 O ATOM 938 CB THR A 119 -31.280 -26.411 31.405 1.00 40.54 C ANISOU 938 CB THR A 119 6605 3695 5102 -1178 179 1124 C ATOM 939 OG1 THR A 119 -32.212 -27.307 30.794 1.00 48.70 O ANISOU 939 OG1 THR A 119 7680 4548 6276 -1335 169 1062 O ATOM 940 CG2 THR A 119 -32.010 -25.591 32.458 1.00 46.66 C ANISOU 940 CG2 THR A 119 7269 4722 5736 -1267 232 1218 C ATOM 941 N ARG A 120 -28.422 -25.005 31.101 1.00 28.94 N ANISOU 941 N ARG A 120 5120 2370 3504 -734 121 1083 N ATOM 942 CA ARG A 120 -27.391 -24.112 31.616 1.00 31.34 C ANISOU 942 CA ARG A 120 5368 2831 3707 -595 93 1147 C ATOM 943 C ARG A 120 -27.042 -23.033 30.597 1.00 28.37 C ANISOU 943 C ARG A 120 4916 2572 3290 -489 80 967 C ATOM 944 O ARG A 120 -26.821 -21.868 30.963 1.00 28.61 O ANISOU 944 O ARG A 120 4857 2808 3207 -451 62 962 O ATOM 945 CB ARG A 120 -26.151 -24.914 32.005 1.00 31.00 C ANISOU 945 CB ARG A 120 5395 2628 3755 -469 63 1311 C ATOM 946 CG ARG A 120 -26.343 -25.772 33.246 1.00 41.52 C ANISOU 946 CG ARG A 120 6777 3900 5100 -557 63 1536 C ATOM 947 CD ARG A 120 -25.137 -26.651 33.494 1.00 37.95 C ANISOU 947 CD ARG A 120 6327 3302 4792 -405 39 1673 C ATOM 948 NE ARG A 120 -25.433 -27.658 34.502 1.00 48.50 N ANISOU 948 NE ARG A 120 7666 4578 6183 -469 65 1845 N ATOM 949 CZ ARG A 120 -24.685 -28.728 34.739 1.00 44.94 C ANISOU 949 CZ ARG A 120 7239 3949 5888 -371 77 1976 C ATOM 950 NH1 ARG A 120 -25.046 -29.585 35.681 1.00 48.72 N ANISOU 950 NH1 ARG A 120 7750 4379 6381 -435 116 2123 N ATOM 951 NH2 ARG A 120 -23.583 -28.941 34.036 1.00 49.78 N ANISOU 951 NH2 ARG A 120 7846 4431 6638 -203 64 1959 N ATOM 952 N ALA A 121 -26.997 -23.397 29.310 1.00 28.10 N ANISOU 952 N ALA A 121 4925 2409 3343 -445 90 817 N ATOM 953 CA ALA A 121 -26.761 -22.395 28.269 1.00 25.82 C ANISOU 953 CA ALA A 121 4565 2240 3006 -356 84 657 C ATOM 954 C ALA A 121 -27.842 -21.325 28.278 1.00 25.71 C ANISOU 954 C ALA A 121 4441 2438 2890 -469 81 576 C ATOM 955 O ALA A 121 -27.547 -20.129 28.155 1.00 21.91 O ANISOU 955 O ALA A 121 3860 2128 2336 -399 69 536 O ATOM 956 CB ALA A 121 -26.699 -23.062 26.896 1.00 24.49 C ANISOU 956 CB ALA A 121 4486 1901 2917 -315 102 503 C ATOM 957 N ALA A 122 -29.106 -21.729 28.424 1.00 24.87 N ANISOU 957 N ALA A 122 4339 2314 2798 -643 96 562 N ATOM 958 CA ALA A 122 -30.181 -20.739 28.378 1.00 30.65 C ANISOU 958 CA ALA A 122 4946 3237 3461 -741 104 494 C ATOM 959 C ALA A 122 -30.093 -19.778 29.557 1.00 30.10 C ANISOU 959 C ALA A 122 4795 3354 3287 -726 128 584 C ATOM 960 O ALA A 122 -30.383 -18.583 29.414 1.00 24.50 O ANISOU 960 O ALA A 122 3975 2815 2519 -711 133 513 O ATOM 961 CB ALA A 122 -31.543 -21.429 28.347 1.00 28.91 C ANISOU 961 CB ALA A 122 4728 2955 3301 -935 116 486 C ATOM 962 N GLY A 123 -29.690 -20.277 30.731 1.00 28.83 N ANISOU 962 N GLY A 123 4696 3159 3098 -731 140 742 N ATOM 963 CA GLY A 123 -29.488 -19.387 31.861 1.00 30.95 C ANISOU 963 CA GLY A 123 4919 3604 3238 -713 152 814 C ATOM 964 C GLY A 123 -28.343 -18.415 31.637 1.00 26.30 C ANISOU 964 C GLY A 123 4287 3095 2609 -559 97 774 C ATOM 965 O GLY A 123 -28.440 -17.237 31.988 1.00 23.55 O ANISOU 965 O GLY A 123 3862 2912 2173 -548 101 730 O ATOM 966 N ILE A 124 -27.228 -18.905 31.083 1.00 22.63 N ANISOU 966 N ILE A 124 3871 2505 2224 -437 51 795 N ATOM 967 CA ILE A 124 -26.100 -18.029 30.774 1.00 21.26 C ANISOU 967 CA ILE A 124 3637 2398 2041 -291 0 774 C ATOM 968 C ILE A 124 -26.513 -16.941 29.785 1.00 20.67 C ANISOU 968 C ILE A 124 3461 2432 1960 -274 11 614 C ATOM 969 O ILE A 124 -26.171 -15.763 29.959 1.00 19.18 O ANISOU 969 O ILE A 124 3188 2377 1722 -225 -15 591 O ATOM 970 CB ILE A 124 -24.920 -18.869 30.249 1.00 20.09 C ANISOU 970 CB ILE A 124 3546 2081 2005 -158 -23 831 C ATOM 971 CG1 ILE A 124 -24.380 -19.765 31.377 1.00 24.44 C ANISOU 971 CG1 ILE A 124 4173 2544 2568 -161 -53 1027 C ATOM 972 CG2 ILE A 124 -23.838 -17.981 29.662 1.00 20.02 C ANISOU 972 CG2 ILE A 124 3452 2137 2016 -9 -58 801 C ATOM 973 CD1 ILE A 124 -23.534 -20.914 30.870 1.00 33.48 C ANISOU 973 CD1 ILE A 124 5388 3469 3865 -52 -47 1090 C ATOM 974 N ILE A 125 -27.261 -17.310 28.737 1.00 21.07 N ANISOU 974 N ILE A 125 3518 2423 2063 -320 40 507 N ATOM 975 CA ILE A 125 -27.713 -16.311 27.762 1.00 16.80 C ANISOU 975 CA ILE A 125 2877 1992 1514 -311 39 376 C ATOM 976 C ILE A 125 -28.571 -15.246 28.435 1.00 16.19 C ANISOU 976 C ILE A 125 2698 2081 1374 -388 60 360 C ATOM 977 O ILE A 125 -28.414 -14.048 28.179 1.00 16.51 O ANISOU 977 O ILE A 125 2639 2235 1398 -331 47 310 O ATOM 978 CB ILE A 125 -28.468 -17.000 26.608 1.00 18.62 C ANISOU 978 CB ILE A 125 3147 2133 1793 -375 47 274 C ATOM 979 CG1 ILE A 125 -27.495 -17.858 25.804 1.00 20.34 C ANISOU 979 CG1 ILE A 125 3471 2191 2065 -265 44 255 C ATOM 980 CG2 ILE A 125 -29.174 -15.955 25.697 1.00 16.52 C ANISOU 980 CG2 ILE A 125 2765 2005 1508 -397 34 164 C ATOM 981 CD1 ILE A 125 -28.191 -18.826 24.852 1.00 19.28 C ANISOU 981 CD1 ILE A 125 3431 1926 1968 -347 45 151 C ATOM 982 N ALA A 126 -29.487 -15.662 29.321 1.00 20.85 N ANISOU 982 N ALA A 126 3309 2678 1935 -514 105 408 N ATOM 983 CA ALA A 126 -30.307 -14.688 30.041 1.00 19.64 C ANISOU 983 CA ALA A 126 3065 2676 1721 -575 154 392 C ATOM 984 C ALA A 126 -29.432 -13.753 30.872 1.00 18.09 C ANISOU 984 C ALA A 126 2860 2572 1442 -492 132 419 C ATOM 985 O ALA A 126 -29.604 -12.523 30.856 1.00 17.89 O ANISOU 985 O ALA A 126 2741 2657 1399 -464 142 348 O ATOM 986 CB ALA A 126 -31.310 -15.416 30.946 1.00 18.27 C ANISOU 986 CB ALA A 126 2925 2493 1524 -716 225 466 C ATOM 987 N ILE A 127 -28.476 -14.329 31.603 1.00 16.93 N ANISOU 987 N ILE A 127 2810 2369 1253 -456 92 526 N ATOM 988 CA ILE A 127 -27.581 -13.528 32.430 1.00 16.72 C ANISOU 988 CA ILE A 127 2786 2425 1143 -394 41 561 C ATOM 989 C ILE A 127 -26.800 -12.558 31.566 1.00 18.53 C ANISOU 989 C ILE A 127 2926 2679 1434 -280 -18 491 C ATOM 990 O ILE A 127 -26.659 -11.372 31.900 1.00 15.79 O ANISOU 990 O ILE A 127 2520 2431 1047 -260 -36 442 O ATOM 991 CB ILE A 127 -26.648 -14.449 33.245 1.00 17.87 C ANISOU 991 CB ILE A 127 3040 2497 1252 -377 -16 715 C ATOM 992 CG1 ILE A 127 -27.456 -15.146 34.352 1.00 20.26 C ANISOU 992 CG1 ILE A 127 3424 2814 1459 -501 48 803 C ATOM 993 CG2 ILE A 127 -25.473 -13.647 33.800 1.00 20.79 C ANISOU 993 CG2 ILE A 127 3398 2935 1567 -300 -113 753 C ATOM 994 CD1 ILE A 127 -26.681 -16.216 35.100 1.00 24.41 C ANISOU 994 CD1 ILE A 127 4039 3252 1983 -482 -5 968 C ATOM 995 N CYS A 128 -26.312 -13.036 30.419 1.00 15.47 N ANISOU 995 N CYS A 128 2530 2199 1147 -206 -39 482 N ATOM 996 CA CYS A 128 -25.503 -12.182 29.572 1.00 17.09 C ANISOU 996 CA CYS A 128 2649 2432 1413 -94 -83 443 C ATOM 997 C CYS A 128 -26.322 -11.032 28.994 1.00 18.47 C ANISOU 997 C CYS A 128 2712 2706 1599 -115 -54 329 C ATOM 998 O CYS A 128 -25.808 -9.928 28.861 1.00 13.68 O ANISOU 998 O CYS A 128 2022 2161 1014 -53 -91 309 O ATOM 999 CB CYS A 128 -24.850 -13.015 28.474 1.00 22.10 C ANISOU 999 CB CYS A 128 3314 2950 2134 -6 -85 457 C ATOM 1000 SG CYS A 128 -23.536 -14.041 29.179 1.00 24.04 S ANISOU 1000 SG CYS A 128 3646 3080 2410 68 -132 618 S ATOM 1001 N TRP A 129 -27.600 -11.260 28.660 1.00 13.16 N ANISOU 1001 N TRP A 129 2025 2044 931 -205 5 269 N ATOM 1002 CA TRP A 129 -28.429 -10.162 28.168 1.00 15.42 C ANISOU 1002 CA TRP A 129 2187 2425 1247 -222 29 184 C ATOM 1003 C TRP A 129 -28.677 -9.116 29.257 1.00 13.19 C ANISOU 1003 C TRP A 129 1863 2233 917 -243 55 164 C ATOM 1004 O TRP A 129 -28.639 -7.910 28.986 1.00 14.46 O ANISOU 1004 O TRP A 129 1923 2452 1119 -197 45 114 O ATOM 1005 CB TRP A 129 -29.752 -10.700 27.621 1.00 12.95 C ANISOU 1005 CB TRP A 129 1854 2105 961 -324 73 143 C ATOM 1006 CG TRP A 129 -29.665 -11.111 26.190 1.00 12.78 C ANISOU 1006 CG TRP A 129 1833 2036 985 -296 36 106 C ATOM 1007 CD1 TRP A 129 -29.532 -12.381 25.694 1.00 14.37 C ANISOU 1007 CD1 TRP A 129 2146 2123 1192 -316 25 108 C ATOM 1008 CD2 TRP A 129 -29.672 -10.231 25.055 1.00 16.30 C ANISOU 1008 CD2 TRP A 129 2176 2548 1468 -241 6 59 C ATOM 1009 NE1 TRP A 129 -29.462 -12.337 24.308 1.00 18.01 N ANISOU 1009 NE1 TRP A 129 2592 2581 1669 -277 -6 47 N ATOM 1010 CE2 TRP A 129 -29.548 -11.031 23.900 1.00 18.35 C ANISOU 1010 CE2 TRP A 129 2501 2744 1726 -232 -20 28 C ATOM 1011 CE3 TRP A 129 -29.783 -8.841 24.913 1.00 12.73 C ANISOU 1011 CE3 TRP A 129 1588 2195 1052 -198 2 43 C ATOM 1012 CZ2 TRP A 129 -29.539 -10.489 22.605 1.00 18.45 C ANISOU 1012 CZ2 TRP A 129 2451 2815 1746 -187 -53 -11 C ATOM 1013 CZ3 TRP A 129 -29.778 -8.300 23.623 1.00 14.63 C ANISOU 1013 CZ3 TRP A 129 1751 2482 1326 -152 -34 22 C ATOM 1014 CH2 TRP A 129 -29.647 -9.126 22.491 1.00 16.64 C ANISOU 1014 CH2 TRP A 129 2077 2695 1552 -148 -61 -1 C ATOM 1015 N VAL A 130 -28.909 -9.550 30.500 1.00 13.47 N ANISOU 1015 N VAL A 130 1982 2275 860 -310 93 204 N ATOM 1016 CA VAL A 130 -29.076 -8.580 31.581 1.00 13.81 C ANISOU 1016 CA VAL A 130 2017 2402 828 -325 126 167 C ATOM 1017 C VAL A 130 -27.798 -7.769 31.766 1.00 16.00 C ANISOU 1017 C VAL A 130 2294 2687 1099 -241 28 169 C ATOM 1018 O VAL A 130 -27.834 -6.537 31.890 1.00 17.35 O ANISOU 1018 O VAL A 130 2399 2907 1288 -216 29 94 O ATOM 1019 CB VAL A 130 -29.505 -9.277 32.891 1.00 17.19 C ANISOU 1019 CB VAL A 130 2555 2849 1126 -415 188 223 C ATOM 1020 CG1 VAL A 130 -29.465 -8.280 34.037 1.00 19.37 C ANISOU 1020 CG1 VAL A 130 2859 3213 1288 -420 215 171 C ATOM 1021 CG2 VAL A 130 -30.913 -9.828 32.765 1.00 20.03 C ANISOU 1021 CG2 VAL A 130 2878 3216 1516 -510 298 220 C ATOM 1022 N LEU A 131 -26.645 -8.447 31.806 1.00 13.72 N ANISOU 1022 N LEU A 131 2071 2339 802 -197 -58 262 N ATOM 1023 CA ALEU A 131 -25.383 -7.725 31.957 0.79 20.78 C ANISOU 1023 CA ALEU A 131 2943 3239 1713 -125 -165 286 C ATOM 1024 CA BLEU A 131 -25.370 -7.746 31.947 0.21 13.21 C ANISOU 1024 CA BLEU A 131 1986 2279 755 -124 -166 288 C ATOM 1025 C LEU A 131 -25.141 -6.769 30.795 1.00 17.19 C ANISOU 1025 C LEU A 131 2355 2788 1389 -48 -185 235 C ATOM 1026 O LEU A 131 -24.571 -5.684 30.989 1.00 14.01 O ANISOU 1026 O LEU A 131 1899 2411 1015 -17 -246 211 O ATOM 1027 CB ALEU A 131 -24.218 -8.701 32.080 0.79 16.34 C ANISOU 1027 CB ALEU A 131 2446 2608 1155 -81 -248 419 C ATOM 1028 CB BLEU A 131 -24.233 -8.767 32.026 0.21 16.48 C ANISOU 1028 CB BLEU A 131 2464 2621 1177 -80 -244 421 C ATOM 1029 CG ALEU A 131 -24.219 -9.563 33.335 0.79 15.01 C ANISOU 1029 CG ALEU A 131 2408 2439 858 -151 -258 506 C ATOM 1030 CG BLEU A 131 -22.952 -8.444 32.794 0.21 25.14 C ANISOU 1030 CG BLEU A 131 3577 3724 2250 -47 -369 498 C ATOM 1031 CD1ALEU A 131 -23.049 -10.534 33.252 0.79 22.24 C ANISOU 1031 CD1ALEU A 131 3350 3257 1842 -78 -331 641 C ATOM 1032 CD1BLEU A 131 -23.256 -8.103 34.247 0.21 15.35 C ANISOU 1032 CD1BLEU A 131 2418 2536 879 -122 -370 458 C ATOM 1033 CD2ALEU A 131 -24.148 -8.698 34.587 0.79 15.80 C ANISOU 1033 CD2ALEU A 131 2535 2603 865 -183 -285 453 C ATOM 1034 CD2BLEU A 131 -22.017 -9.636 32.728 0.21 23.88 C ANISOU 1034 CD2BLEU A 131 3456 3467 2152 14 -410 629 C ATOM 1035 N ASER A 132 -25.539 -7.161 29.582 0.82 12.74 N ANISOU 1035 N ASER A 132 1742 2197 902 -22 -144 224 N ATOM 1036 N BSER A 132 -25.570 -7.138 29.584 0.18 16.34 N ANISOU 1036 N BSER A 132 2196 2654 1357 -23 -142 222 N ATOM 1037 CA ASER A 132 -25.373 -6.295 28.418 0.82 14.55 C ANISOU 1037 CA ASER A 132 1847 2443 1238 48 -157 194 C ATOM 1038 CA BSER A 132 -25.351 -6.269 28.432 0.18 13.48 C ANISOU 1038 CA BSER A 132 1710 2308 1103 49 -159 195 C ATOM 1039 C ASER A 132 -26.194 -5.009 28.547 0.82 18.78 C ANISOU 1039 C ASER A 132 2290 3040 1805 21 -123 107 C ATOM 1040 C BSER A 132 -26.210 -5.010 28.503 0.18 10.36 C ANISOU 1040 C BSER A 132 1222 1974 741 22 -123 107 C ATOM 1041 O ASER A 132 -25.730 -3.926 28.167 0.82 10.89 O ANISOU 1041 O ASER A 132 1196 2053 889 76 -164 99 O ATOM 1042 O BSER A 132 -25.777 -3.944 28.051 0.18 15.32 O ANISOU 1042 O BSER A 132 1751 2615 1456 78 -161 99 O ATOM 1043 CB ASER A 132 -25.769 -7.042 27.140 0.82 10.88 C ANISOU 1043 CB ASER A 132 1374 1950 809 63 -120 191 C ATOM 1044 CB BSER A 132 -25.620 -7.027 27.128 0.18 14.27 C ANISOU 1044 CB BSER A 132 1803 2377 1243 73 -127 198 C ATOM 1045 OG ASER A 132 -24.936 -8.165 26.930 0.82 12.39 O ANISOU 1045 OG ASER A 132 1649 2063 994 110 -137 259 O ATOM 1046 OG BSER A 132 -27.003 -7.082 26.823 0.18 10.34 O ANISOU 1046 OG BSER A 132 1279 1911 739 -4 -66 132 O ATOM 1047 N PHE A 133 -27.417 -5.104 29.065 1.00 13.53 N ANISOU 1047 N PHE A 133 1643 2406 1093 -59 -41 51 N ATOM 1048 CA PHE A 133 -28.191 -3.890 29.317 1.00 13.38 C ANISOU 1048 CA PHE A 133 1537 2432 1116 -71 10 -32 C ATOM 1049 C PHE A 133 -27.496 -3.027 30.361 1.00 15.70 C ANISOU 1049 C PHE A 133 1870 2727 1370 -59 -32 -67 C ATOM 1050 O PHE A 133 -27.413 -1.801 30.207 1.00 14.80 O ANISOU 1050 O PHE A 133 1669 2609 1344 -22 -47 -118 O ATOM 1051 CB PHE A 133 -29.618 -4.220 29.763 1.00 15.03 C ANISOU 1051 CB PHE A 133 1748 2675 1287 -154 125 -72 C ATOM 1052 CG PHE A 133 -30.568 -4.405 28.613 1.00 15.75 C ANISOU 1052 CG PHE A 133 1732 2781 1470 -171 154 -67 C ATOM 1053 CD1 PHE A 133 -30.765 -5.661 28.043 1.00 15.23 C ANISOU 1053 CD1 PHE A 133 1717 2688 1383 -215 141 -23 C ATOM 1054 CD2 PHE A 133 -31.228 -3.316 28.081 1.00 18.60 C ANISOU 1054 CD2 PHE A 133 1946 3176 1946 -144 181 -104 C ATOM 1055 CE1 PHE A 133 -31.634 -5.844 26.961 1.00 19.21 C ANISOU 1055 CE1 PHE A 133 2133 3209 1958 -248 142 -24 C ATOM 1056 CE2 PHE A 133 -32.103 -3.478 26.987 1.00 25.89 C ANISOU 1056 CE2 PHE A 133 2763 4125 2950 -168 182 -83 C ATOM 1057 CZ PHE A 133 -32.293 -4.746 26.421 1.00 19.99 C ANISOU 1057 CZ PHE A 133 2075 3361 2158 -226 155 -48 C ATOM 1058 N ALA A 134 -26.963 -3.649 31.419 1.00 12.96 N ANISOU 1058 N ALA A 134 1656 2377 892 -96 -64 -35 N ATOM 1059 CA ALA A 134 -26.323 -2.859 32.466 1.00 13.06 C ANISOU 1059 CA ALA A 134 1725 2397 840 -105 -125 -77 C ATOM 1060 C ALA A 134 -25.079 -2.146 31.934 1.00 18.85 C ANISOU 1060 C ALA A 134 2384 3092 1686 -38 -254 -40 C ATOM 1061 O ALA A 134 -24.855 -0.968 32.232 1.00 15.54 O ANISOU 1061 O ALA A 134 1931 2662 1310 -33 -292 -111 O ATOM 1062 CB ALA A 134 -25.966 -3.758 33.653 1.00 17.24 C ANISOU 1062 CB ALA A 134 2413 2945 1192 -164 -154 -23 C ATOM 1063 N ILE A 135 -24.264 -2.846 31.150 1.00 12.44 N ANISOU 1063 N ILE A 135 1543 2251 931 14 -314 72 N ATOM 1064 CA ILE A 135 -23.053 -2.246 30.577 1.00 13.84 C ANISOU 1064 CA ILE A 135 1629 2398 1231 83 -421 135 C ATOM 1065 C ILE A 135 -23.395 -1.188 29.540 1.00 14.54 C ANISOU 1065 C ILE A 135 1573 2485 1467 129 -390 96 C ATOM 1066 O ILE A 135 -22.874 -0.071 29.587 1.00 12.93 O ANISOU 1066 O ILE A 135 1298 2258 1355 144 -455 81 O ATOM 1067 CB ILE A 135 -22.153 -3.337 29.975 1.00 14.24 C ANISOU 1067 CB ILE A 135 1683 2419 1308 142 -458 268 C ATOM 1068 CG1 ILE A 135 -21.500 -4.127 31.093 1.00 14.41 C ANISOU 1068 CG1 ILE A 135 1824 2422 1230 106 -526 335 C ATOM 1069 CG2 ILE A 135 -21.094 -2.721 29.040 1.00 13.71 C ANISOU 1069 CG2 ILE A 135 1513 2268 1428 211 -488 311 C ATOM 1070 CD1 ILE A 135 -20.821 -5.416 30.595 1.00 20.56 C ANISOU 1070 CD1 ILE A 135 2631 3117 2062 164 -512 436 C ATOM 1071 N GLY A 136 -24.269 -1.519 28.586 1.00 10.91 N ANISOU 1071 N GLY A 136 1066 2044 1037 145 -301 88 N ATOM 1072 CA GLY A 136 -24.542 -0.600 27.489 1.00 11.71 C ANISOU 1072 CA GLY A 136 1023 2152 1274 193 -284 86 C ATOM 1073 C GLY A 136 -25.331 0.622 27.910 1.00 14.20 C ANISOU 1073 C GLY A 136 1282 2463 1649 168 -247 -13 C ATOM 1074 O GLY A 136 -25.174 1.696 27.323 1.00 13.69 O ANISOU 1074 O GLY A 136 1109 2366 1725 206 -267 -2 O ATOM 1075 N LEU A 137 -26.162 0.496 28.949 1.00 10.62 N ANISOU 1075 N LEU A 137 914 2023 1099 105 -179 -106 N ATOM 1076 CA LEU A 137 -26.927 1.631 29.438 1.00 11.14 C ANISOU 1076 CA LEU A 137 938 2074 1221 94 -118 -215 C ATOM 1077 C LEU A 137 -26.323 2.272 30.679 1.00 12.16 C ANISOU 1077 C LEU A 137 1163 2167 1292 65 -170 -296 C ATOM 1078 O LEU A 137 -26.985 3.096 31.306 1.00 13.63 O ANISOU 1078 O LEU A 137 1357 2332 1490 52 -99 -415 O ATOM 1079 CB LEU A 137 -28.382 1.220 29.728 1.00 11.57 C ANISOU 1079 CB LEU A 137 1004 2171 1220 51 21 -272 C ATOM 1080 CG LEU A 137 -29.125 0.650 28.505 1.00 10.86 C ANISOU 1080 CG LEU A 137 817 2119 1191 58 54 -204 C ATOM 1081 CD1 LEU A 137 -30.585 0.290 28.857 1.00 14.13 C ANISOU 1081 CD1 LEU A 137 1217 2573 1577 2 183 -247 C ATOM 1082 CD2 LEU A 137 -29.059 1.607 27.312 1.00 10.81 C ANISOU 1082 CD2 LEU A 137 648 2100 1358 124 15 -160 C ATOM 1083 N THR A 138 -25.092 1.921 31.048 1.00 12.01 N ANISOU 1083 N THR A 138 1348 2079 1135 112 -453 33 N ATOM 1084 CA THR A 138 -24.434 2.609 32.158 1.00 10.96 C ANISOU 1084 CA THR A 138 1102 2133 929 56 -266 50 C ATOM 1085 C THR A 138 -24.483 4.136 32.056 1.00 12.24 C ANISOU 1085 C THR A 138 1262 2341 1046 76 -172 -31 C ATOM 1086 O THR A 138 -24.693 4.779 33.102 1.00 12.45 O ANISOU 1086 O THR A 138 1220 2469 1043 22 -82 -43 O ATOM 1087 CB THR A 138 -22.989 2.077 32.292 1.00 12.63 C ANISOU 1087 CB THR A 138 1359 2381 1057 91 -219 105 C ATOM 1088 OG1 THR A 138 -23.025 0.861 33.056 1.00 15.66 O ANISOU 1088 OG1 THR A 138 1687 2774 1490 25 -270 197 O ATOM 1089 CG2 THR A 138 -22.064 3.088 33.006 1.00 13.31 C ANISOU 1089 CG2 THR A 138 1383 2598 1076 36 -111 122 C ATOM 1090 N PRO A 139 -24.364 4.778 30.872 1.00 11.81 N ANISOU 1090 N PRO A 139 1313 2204 971 168 -195 -86 N ATOM 1091 CA PRO A 139 -24.551 6.242 30.831 1.00 11.29 C ANISOU 1091 CA PRO A 139 1234 2153 902 170 -134 -147 C ATOM 1092 C PRO A 139 -25.892 6.718 31.369 1.00 13.48 C ANISOU 1092 C PRO A 139 1418 2442 1263 150 -116 -179 C ATOM 1093 O PRO A 139 -25.950 7.826 31.909 1.00 11.55 O ANISOU 1093 O PRO A 139 1177 2228 985 157 -33 -238 O ATOM 1094 CB PRO A 139 -24.410 6.574 29.331 1.00 9.77 C ANISOU 1094 CB PRO A 139 1170 1860 684 288 -179 -159 C ATOM 1095 CG PRO A 139 -23.395 5.521 28.858 1.00 11.44 C ANISOU 1095 CG PRO A 139 1479 2060 809 378 -170 -90 C ATOM 1096 CD PRO A 139 -23.953 4.270 29.543 1.00 10.15 C ANISOU 1096 CD PRO A 139 1275 1879 702 305 -263 -87 C ATOM 1097 N AMET A 140 -26.964 5.928 31.249 0.53 13.20 N ANISOU 1097 N AMET A 140 1297 2367 1351 137 -199 -117 N ATOM 1098 N BMET A 140 -26.965 5.926 31.215 0.47 10.90 N ANISOU 1098 N BMET A 140 1008 2072 1060 138 -203 -117 N ATOM 1099 CA AMET A 140 -28.254 6.333 31.815 0.53 12.02 C ANISOU 1099 CA AMET A 140 985 2259 1324 146 -134 -62 C ATOM 1100 CA BMET A 140 -28.278 6.283 31.761 0.47 14.93 C ANISOU 1100 CA BMET A 140 1352 2620 1700 144 -145 -58 C ATOM 1101 C AMET A 140 -28.273 6.281 33.338 0.53 12.69 C ANISOU 1101 C AMET A 140 989 2499 1332 139 50 -13 C ATOM 1102 C BMET A 140 -28.258 6.412 33.275 0.47 27.10 C ANISOU 1102 C BMET A 140 2825 4318 3152 146 51 -27 C ATOM 1103 O AMET A 140 -29.232 6.770 33.946 0.53 19.08 O ANISOU 1103 O AMET A 140 1686 3375 2187 216 191 45 O ATOM 1104 O BMET A 140 -29.116 7.099 33.840 0.47 13.91 O ANISOU 1104 O BMET A 140 1075 2706 1506 233 195 -1 O ATOM 1105 CB AMET A 140 -29.377 5.451 31.259 0.53 19.99 C ANISOU 1105 CB AMET A 140 1870 3169 2556 103 -320 74 C ATOM 1106 CB BMET A 140 -29.331 5.231 31.383 0.47 13.23 C ANISOU 1106 CB BMET A 140 1004 2320 1701 88 -323 90 C ATOM 1107 CG AMET A 140 -29.477 5.474 29.730 0.53 16.91 C ANISOU 1107 CG AMET A 140 1636 2594 2194 131 -555 14 C ATOM 1108 CG BMET A 140 -29.477 4.946 29.885 0.47 13.39 C ANISOU 1108 CG BMET A 140 1173 2141 1772 98 -594 52 C ATOM 1109 SD AMET A 140 -30.974 4.686 29.097 0.53 15.45 S ANISOU 1109 SD AMET A 140 1318 2234 2318 47 -885 189 S ATOM 1110 SD BMET A 140 -30.163 6.358 29.015 0.47 19.34 S ANISOU 1110 SD BMET A 140 1934 2835 2580 182 -611 0 S ATOM 1111 CE AMET A 140 -32.257 5.882 29.472 0.53 16.70 C ANISOU 1111 CE AMET A 140 1180 2480 2687 94 -734 313 C ATOM 1112 CE BMET A 140 -31.855 6.386 29.618 0.47 28.50 C ANISOU 1112 CE BMET A 140 2735 4027 4065 145 -608 226 C ATOM 1113 N ALEU A 141 -27.253 5.699 33.964 0.53 19.18 N ANISOU 1113 N ALEU A 141 1876 3385 2025 78 62 -15 N ATOM 1114 N BLEU A 141 -27.320 5.745 33.942 0.47 12.16 N ANISOU 1114 N BLEU A 141 983 2494 1143 83 64 -16 N ATOM 1115 CA ALEU A 141 -27.135 5.720 35.417 0.53 14.66 C ANISOU 1115 CA ALEU A 141 1302 2956 1312 84 210 16 C ATOM 1116 CA BLEU A 141 -27.252 5.791 35.397 0.47 24.38 C ANISOU 1116 CA BLEU A 141 2526 4185 2552 94 218 16 C ATOM 1117 C ALEU A 141 -26.399 6.952 35.923 0.53 13.14 C ANISOU 1117 C ALEU A 141 1302 2767 923 122 255 -139 C ATOM 1118 C BLEU A 141 -26.532 7.029 35.911 0.47 49.22 C ANISOU 1118 C BLEU A 141 5866 7335 5499 135 266 -141 C ATOM 1119 O ALEU A 141 -26.249 7.107 37.139 0.53 33.22 O ANISOU 1119 O ALEU A 141 3941 5380 3300 148 333 -149 O ATOM 1120 O BLEU A 141 -26.502 7.251 37.125 0.47 14.59 O ANISOU 1120 O BLEU A 141 1575 3022 948 178 362 -153 O ATOM 1121 CB ALEU A 141 -26.440 4.447 35.908 0.53 24.73 C ANISOU 1121 CB ALEU A 141 2554 4283 2561 -13 156 116 C ATOM 1122 CB BLEU A 141 -26.571 4.530 35.935 0.47 12.90 C ANISOU 1122 CB BLEU A 141 1048 2788 1066 -4 170 117 C ATOM 1123 CG ALEU A 141 -27.070 3.140 35.412 0.53 16.42 C ANISOU 1123 CG ALEU A 141 1357 3162 1720 -72 36 269 C ATOM 1124 CG BLEU A 141 -27.340 3.196 35.943 0.47 27.75 C ANISOU 1124 CG BLEU A 141 2746 4663 3136 -62 112 315 C ATOM 1125 CD1ALEU A 141 -26.272 1.942 35.873 0.53 19.99 C ANISOU 1125 CD1ALEU A 141 1817 3634 2145 -151 -26 356 C ATOM 1126 CD1BLEU A 141 -27.787 2.730 34.549 0.47 24.50 C ANISOU 1126 CD1BLEU A 141 2314 4063 2930 -88 -102 322 C ATOM 1127 CD2ALEU A 141 -28.539 3.026 35.845 0.53 19.36 C ANISOU 1127 CD2ALEU A 141 1508 3591 2256 -50 122 452 C ATOM 1128 CD2BLEU A 141 -26.508 2.121 36.622 0.47 17.75 C ANISOU 1128 CD2BLEU A 141 1492 3448 1806 -143 77 400 C ATOM 1129 N GLY A 142 -25.953 7.834 35.026 1.00 13.80 N ANISOU 1129 N GLY A 142 1471 2737 1035 123 173 -242 N ATOM 1130 CA GLY A 142 -25.435 9.120 35.447 1.00 15.05 C ANISOU 1130 CA GLY A 142 1809 2840 1070 142 156 -369 C ATOM 1131 C GLY A 142 -24.109 9.490 34.824 1.00 15.29 C ANISOU 1131 C GLY A 142 1891 2787 1133 37 8 -366 C ATOM 1132 O GLY A 142 -23.656 10.635 34.941 1.00 14.54 O ANISOU 1132 O GLY A 142 1924 2590 1009 16 -76 -438 O ATOM 1133 N TRP A 143 -23.482 8.528 34.150 1.00 11.51 N ANISOU 1133 N TRP A 143 1310 2335 727 -11 -26 -255 N ATOM 1134 CA TRP A 143 -22.215 8.772 33.474 1.00 11.90 C ANISOU 1134 CA TRP A 143 1349 2341 832 -63 -102 -167 C ATOM 1135 C TRP A 143 -22.550 9.316 32.086 1.00 12.22 C ANISOU 1135 C TRP A 143 1391 2299 953 25 -84 -172 C ATOM 1136 O TRP A 143 -22.455 8.637 31.060 1.00 12.60 O ANISOU 1136 O TRP A 143 1422 2345 1022 104 -59 -105 O ATOM 1137 CB TRP A 143 -21.377 7.506 33.420 1.00 10.70 C ANISOU 1137 CB TRP A 143 1113 2259 693 -84 -98 -28 C ATOM 1138 CG TRP A 143 -19.937 7.749 33.049 1.00 16.10 C ANISOU 1138 CG TRP A 143 1731 2936 1450 -123 -136 140 C ATOM 1139 CD1 TRP A 143 -19.338 8.941 32.679 1.00 11.74 C ANISOU 1139 CD1 TRP A 143 1164 2313 983 -170 -197 209 C ATOM 1140 CD2 TRP A 143 -18.903 6.765 33.053 1.00 11.23 C ANISOU 1140 CD2 TRP A 143 1013 2384 869 -116 -115 320 C ATOM 1141 NE1 TRP A 143 -17.990 8.726 32.426 1.00 12.60 N ANISOU 1141 NE1 TRP A 143 1127 2458 1204 -196 -202 464 N ATOM 1142 CE2 TRP A 143 -17.709 7.400 32.652 1.00 12.26 C ANISOU 1142 CE2 TRP A 143 1033 2503 1122 -145 -137 527 C ATOM 1143 CE3 TRP A 143 -18.877 5.396 33.358 1.00 12.25 C ANISOU 1143 CE3 TRP A 143 1120 2568 966 -80 -83 355 C ATOM 1144 CZ2 TRP A 143 -16.504 6.707 32.533 1.00 13.66 C ANISOU 1144 CZ2 TRP A 143 1055 2746 1391 -110 -89 785 C ATOM 1145 CZ3 TRP A 143 -17.675 4.723 33.246 1.00 12.48 C ANISOU 1145 CZ3 TRP A 143 1041 2640 1061 -43 -53 565 C ATOM 1146 CH2 TRP A 143 -16.517 5.372 32.832 1.00 13.01 C ANISOU 1146 CH2 TRP A 143 977 2717 1248 -43 -38 783 C ATOM 1147 N ASN A 144 -22.920 10.592 32.065 1.00 12.09 N ANISOU 1147 N ASN A 144 1440 2196 958 32 -111 -254 N ATOM 1148 CA ASN A 144 -23.407 11.201 30.833 1.00 13.91 C ANISOU 1148 CA ASN A 144 1679 2346 1260 117 -103 -257 C ATOM 1149 C ASN A 144 -23.132 12.701 30.884 1.00 15.25 C ANISOU 1149 C ASN A 144 1916 2395 1483 77 -177 -282 C ATOM 1150 O ASN A 144 -22.699 13.241 31.907 1.00 17.65 O ANISOU 1150 O ASN A 144 2299 2650 1758 -10 -264 -329 O ATOM 1151 CB ASN A 144 -24.896 10.878 30.629 1.00 14.12 C ANISOU 1151 CB ASN A 144 1685 2372 1308 206 -67 -336 C ATOM 1152 CG ASN A 144 -25.787 11.477 31.709 1.00 12.79 C ANISOU 1152 CG ASN A 144 1534 2205 1122 239 -8 -438 C ATOM 1153 OD1 ASN A 144 -25.803 12.678 31.898 1.00 19.72 O ANISOU 1153 OD1 ASN A 144 2506 2990 1995 266 -23 -514 O ATOM 1154 ND2 ASN A 144 -26.535 10.629 32.422 1.00 13.68 N ANISOU 1154 ND2 ASN A 144 1564 2412 1221 262 68 -417 N ATOM 1155 N ASN A 145 -23.348 13.377 29.755 1.00 13.54 N ANISOU 1155 N ASN A 145 1702 2102 1341 139 -180 -242 N ATOM 1156 CA ASN A 145 -23.146 14.823 29.688 1.00 15.43 C ANISOU 1156 CA ASN A 145 2002 2190 1670 98 -274 -242 C ATOM 1157 C ASN A 145 -24.453 15.599 29.767 1.00 19.74 C ANISOU 1157 C ASN A 145 2631 2640 2229 202 -261 -405 C ATOM 1158 O ASN A 145 -24.502 16.749 29.315 1.00 20.50 O ANISOU 1158 O ASN A 145 2780 2590 2420 212 -332 -395 O ATOM 1159 CB ASN A 145 -22.408 15.215 28.401 1.00 16.90 C ANISOU 1159 CB ASN A 145 2119 2352 1950 105 -273 -27 C ATOM 1160 CG ASN A 145 -21.019 14.612 28.314 1.00 22.49 C ANISOU 1160 CG ASN A 145 2705 3155 2684 42 -245 206 C ATOM 1161 OD1 ASN A 145 -20.353 14.428 29.322 1.00 25.51 O ANISOU 1161 OD1 ASN A 145 3057 3550 3087 -87 -328 225 O ATOM 1162 ND2 ASN A 145 -20.577 14.317 27.100 1.00 29.41 N ANISOU 1162 ND2 ASN A 145 3524 4100 3549 161 -123 405 N ATOM 1163 N CYS A 146 -25.514 14.999 30.315 1.00 15.90 N ANISOU 1163 N CYS A 146 2130 2231 1682 291 -165 -511 N ATOM 1164 CA CYS A 146 -26.799 15.698 30.362 1.00 21.31 C ANISOU 1164 CA CYS A 146 2837 2844 2414 431 -111 -603 C ATOM 1165 C CYS A 146 -26.782 16.860 31.349 1.00 24.34 C ANISOU 1165 C CYS A 146 3420 3085 2743 481 -139 -744 C ATOM 1166 O CYS A 146 -27.570 17.807 31.213 1.00 26.02 O ANISOU 1166 O CYS A 146 3694 3176 3017 616 -116 -809 O ATOM 1167 CB CYS A 146 -27.914 14.718 30.709 1.00 19.92 C ANISOU 1167 CB CYS A 146 2532 2800 2238 515 11 -592 C ATOM 1168 SG CYS A 146 -28.244 13.523 29.362 1.00 26.31 S ANISOU 1168 SG CYS A 146 3196 3664 3138 480 -66 -458 S ATOM 1169 N GLY A 147 -25.911 16.799 32.357 1.00 26.28 N ANISOU 1169 N GLY A 147 3802 3321 2864 389 -215 -796 N ATOM 1170 CA GLY A 147 -25.759 17.902 33.283 1.00 26.58 C ANISOU 1170 CA GLY A 147 4129 3163 2808 432 -327 -953 C ATOM 1171 C GLY A 147 -25.140 19.142 32.675 1.00 31.47 C ANISOU 1171 C GLY A 147 4839 3535 3582 335 -552 -925 C ATOM 1172 O GLY A 147 -25.304 20.231 33.223 1.00 35.28 O ANISOU 1172 O GLY A 147 5597 3784 4022 414 -669 -1077 O ATOM 1173 N GLN A 148 -24.444 19.009 31.549 1.00 24.94 N ANISOU 1173 N GLN A 148 3807 2741 2929 189 -610 -717 N ATOM 1174 CA GLN A 148 -23.765 20.134 30.902 1.00 29.41 C ANISOU 1174 CA GLN A 148 4395 3093 3685 73 -814 -598 C ATOM 1175 C GLN A 148 -24.199 20.243 29.443 1.00 31.91 C ANISOU 1175 C GLN A 148 4534 3460 4131 141 -704 -455 C ATOM 1176 O GLN A 148 -23.396 20.059 28.526 1.00 34.70 O ANISOU 1176 O GLN A 148 4725 3878 4581 48 -710 -212 O ATOM 1177 CB GLN A 148 -22.250 19.971 31.007 1.00 47.98 C ANISOU 1177 CB GLN A 148 6660 5436 6136 -171 -1003 -387 C ATOM 1178 CG GLN A 148 -21.754 19.458 32.362 1.00112.00 C ANISOU 1178 CG GLN A 148 14902 13563 14090 -255 -1114 -486 C ATOM 1179 CD GLN A 148 -21.648 17.938 32.424 1.00 55.48 C ANISOU 1179 CD GLN A 148 7553 6704 6824 -239 -906 -421 C ATOM 1180 OE1 GLN A 148 -21.207 17.296 31.472 1.00 78.36 O ANISOU 1180 OE1 GLN A 148 10206 9750 9816 -261 -791 -206 O ATOM 1181 NE2 GLN A 148 -22.054 17.361 33.547 1.00 41.39 N ANISOU 1181 NE2 GLN A 148 5908 4996 4821 -174 -853 -596 N ATOM 1182 N PRO A 149 -25.476 20.530 29.190 1.00 27.57 N ANISOU 1182 N PRO A 149 4014 2887 3573 327 -594 -573 N ATOM 1183 CA PRO A 149 -25.952 20.566 27.801 1.00 24.79 C ANISOU 1183 CA PRO A 149 3523 2578 3318 391 -533 -438 C ATOM 1184 C PRO A 149 -25.266 21.668 27.007 1.00 29.14 C ANISOU 1184 C PRO A 149 4080 2955 4036 301 -680 -263 C ATOM 1185 O PRO A 149 -24.878 22.708 27.549 1.00 27.87 O ANISOU 1185 O PRO A 149 4059 2559 3971 227 -859 -300 O ATOM 1186 CB PRO A 149 -27.453 20.847 27.952 1.00 26.81 C ANISOU 1186 CB PRO A 149 3805 2799 3584 595 -437 -582 C ATOM 1187 CG PRO A 149 -27.560 21.596 29.231 1.00 31.63 C ANISOU 1187 CG PRO A 149 4638 3244 4135 666 -470 -777 C ATOM 1188 CD PRO A 149 -26.531 20.943 30.134 1.00 31.00 C ANISOU 1188 CD PRO A 149 4621 3239 3918 516 -525 -803 C ATOM 1189 N LYS A 150 -25.117 21.433 25.703 1.00 25.48 N ANISOU 1189 N LYS A 150 3492 2590 3599 318 -621 -55 N ATOM 1190 CA LYS A 150 -24.672 22.491 24.793 1.00 24.60 C ANISOU 1190 CA LYS A 150 3359 2338 3650 274 -716 165 C ATOM 1191 C LYS A 150 -25.862 23.402 24.522 1.00 27.89 C ANISOU 1191 C LYS A 150 3860 2589 4148 403 -759 51 C ATOM 1192 O LYS A 150 -26.660 23.182 23.603 1.00 23.49 O ANISOU 1192 O LYS A 150 3260 2108 3558 528 -692 88 O ATOM 1193 CB LYS A 150 -24.095 21.909 23.508 1.00 26.60 C ANISOU 1193 CB LYS A 150 3494 2772 3840 309 -595 445 C ATOM 1194 CG LYS A 150 -22.837 21.090 23.746 1.00 29.46 C ANISOU 1194 CG LYS A 150 3747 3289 4158 219 -523 611 C ATOM 1195 CD LYS A 150 -22.001 20.960 22.500 1.00 32.39 C ANISOU 1195 CD LYS A 150 4013 3784 4511 286 -388 978 C ATOM 1196 CE LYS A 150 -20.886 19.942 22.697 1.00 40.21 C ANISOU 1196 CE LYS A 150 4880 4961 5438 274 -254 1147 C ATOM 1197 NZ LYS A 150 -20.026 20.267 23.862 1.00 92.72 N ANISOU 1197 NZ LYS A 150 11417 11517 12295 35 -418 1201 N ATOM 1198 N GLU A 151 -25.973 24.453 25.336 1.00 40.12 N ANISOU 1198 N GLU A 151 5557 3881 5806 386 -901 -84 N ATOM 1199 CA GLU A 151 -27.137 25.334 25.266 1.00 36.69 C ANISOU 1199 CA GLU A 151 5217 3270 5454 556 -918 -211 C ATOM 1200 C GLU A 151 -27.164 26.150 23.983 1.00 32.36 C ANISOU 1200 C GLU A 151 4608 2621 5068 553 -993 19 C ATOM 1201 O GLU A 151 -28.246 26.436 23.458 1.00 37.53 O ANISOU 1201 O GLU A 151 5245 3247 5767 712 -955 -6 O ATOM 1202 CB GLU A 151 -27.158 26.264 26.482 1.00 43.00 C ANISOU 1202 CB GLU A 151 6276 3780 6282 586 -1058 -431 C ATOM 1203 CG GLU A 151 -28.495 26.351 27.183 1.00 96.53 C ANISOU 1203 CG GLU A 151 13167 10533 12978 867 -906 -680 C ATOM 1204 CD GLU A 151 -28.952 25.017 27.737 1.00 41.48 C ANISOU 1204 CD GLU A 151 6081 3863 5818 942 -679 -761 C ATOM 1205 OE1 GLU A 151 -29.587 24.243 26.987 1.00 66.63 O ANISOU 1205 OE1 GLU A 151 9035 7260 9022 981 -553 -651 O ATOM 1206 OE2 GLU A 151 -28.685 24.741 28.925 1.00 71.13 O ANISOU 1206 OE2 GLU A 151 9997 7623 9408 956 -658 -924 O ATOM 1207 N GLY A 152 -26.005 26.550 23.464 1.00 33.35 N ANISOU 1207 N GLY A 152 4676 2692 5304 378 -1100 287 N ATOM 1208 CA GLY A 152 -26.004 27.323 22.232 1.00 37.87 C ANISOU 1208 CA GLY A 152 5186 3186 6016 387 -1148 553 C ATOM 1209 C GLY A 152 -26.492 26.507 21.054 1.00 37.58 C ANISOU 1209 C GLY A 152 5060 3409 5808 520 -980 664 C ATOM 1210 O GLY A 152 -27.223 27.010 20.195 1.00 34.60 O ANISOU 1210 O GLY A 152 4696 2974 5476 627 -1010 738 O ATOM 1211 N LYS A 153 -26.109 25.229 21.013 1.00 29.35 N ANISOU 1211 N LYS A 153 3965 2630 4558 525 -836 669 N ATOM 1212 CA LYS A 153 -26.581 24.336 19.963 1.00 27.86 C ANISOU 1212 CA LYS A 153 3783 2644 4160 667 -733 725 C ATOM 1213 C LYS A 153 -28.074 24.052 20.113 1.00 27.35 C ANISOU 1213 C LYS A 153 3749 2564 4080 786 -773 488 C ATOM 1214 O LYS A 153 -28.811 24.015 19.120 1.00 27.87 O ANISOU 1214 O LYS A 153 3846 2643 4099 891 -828 557 O ATOM 1215 CB LYS A 153 -25.766 23.043 19.999 1.00 38.43 C ANISOU 1215 CB LYS A 153 5096 4215 5290 661 -591 767 C ATOM 1216 CG LYS A 153 -25.930 22.158 18.798 1.00 38.12 C ANISOU 1216 CG LYS A 153 5153 4342 4988 827 -512 861 C ATOM 1217 CD LYS A 153 -25.090 20.909 18.933 1.00 34.39 C ANISOU 1217 CD LYS A 153 4687 4062 4318 856 -363 886 C ATOM 1218 CE LYS A 153 -23.605 21.225 19.012 1.00 33.55 C ANISOU 1218 CE LYS A 153 4439 4009 4299 779 -239 1186 C ATOM 1219 NZ LYS A 153 -22.767 20.025 18.763 1.00 42.37 N ANISOU 1219 NZ LYS A 153 5572 5332 5194 898 -43 1297 N ATOM 1220 N ALA A 154 -28.541 23.859 21.351 1.00 24.27 N ANISOU 1220 N ALA A 154 3342 2146 3735 778 -753 245 N ATOM 1221 CA ALA A 154 -29.969 23.648 21.577 1.00 32.44 C ANISOU 1221 CA ALA A 154 4331 3175 4819 904 -756 101 C ATOM 1222 C ALA A 154 -30.783 24.867 21.155 1.00 32.75 C ANISOU 1222 C ALA A 154 4372 3015 5055 1004 -846 147 C ATOM 1223 O ALA A 154 -31.829 24.731 20.505 1.00 31.70 O ANISOU 1223 O ALA A 154 4171 2896 4976 1100 -906 200 O ATOM 1224 CB ALA A 154 -30.229 23.315 23.048 1.00 26.09 C ANISOU 1224 CB ALA A 154 3511 2392 4011 921 -657 -115 C ATOM 1225 N HIS A 155 -30.328 26.072 21.512 1.00 29.29 N ANISOU 1225 N HIS A 155 4017 2361 4750 975 -896 144 N ATOM 1226 CA HIS A 155 -31.096 27.255 21.116 1.00 29.88 C ANISOU 1226 CA HIS A 155 4108 2229 5016 1081 -977 189 C ATOM 1227 C HIS A 155 -31.086 27.447 19.605 1.00 31.60 C ANISOU 1227 C HIS A 155 4292 2505 5209 1050 -1045 441 C ATOM 1228 O HIS A 155 -32.080 27.903 19.028 1.00 30.61 O ANISOU 1228 O HIS A 155 4121 2361 5149 1127 -1068 486 O ATOM 1229 CB HIS A 155 -30.564 28.506 21.812 1.00 35.54 C ANISOU 1229 CB HIS A 155 4969 2681 5854 1033 -1048 123 C ATOM 1230 CG HIS A 155 -30.927 28.588 23.260 1.00 41.50 C ANISOU 1230 CG HIS A 155 5839 3362 6567 1135 -964 -154 C ATOM 1231 ND1 HIS A 155 -32.228 28.707 23.696 1.00 84.52 N ANISOU 1231 ND1 HIS A 155 11248 8840 12024 1346 -805 -259 N ATOM 1232 CD2 HIS A 155 -30.158 28.576 24.373 1.00 40.63 C ANISOU 1232 CD2 HIS A 155 5895 3163 6379 1066 -1004 -313 C ATOM 1233 CE1 HIS A 155 -32.246 28.758 25.015 1.00 83.36 C ANISOU 1233 CE1 HIS A 155 11254 8646 11773 1432 -706 -470 C ATOM 1234 NE2 HIS A 155 -31.002 28.677 25.451 1.00 70.28 N ANISOU 1234 NE2 HIS A 155 9745 6917 10040 1256 -846 -530 N ATOM 1235 N SER A 156 -29.972 27.131 18.944 1.00 30.47 N ANISOU 1235 N SER A 156 4177 2443 4956 957 -1058 633 N ATOM 1236 CA SER A 156 -29.916 27.357 17.501 1.00 41.43 C ANISOU 1236 CA SER A 156 5585 3907 6251 972 -1074 878 C ATOM 1237 C SER A 156 -30.881 26.440 16.761 1.00 41.29 C ANISOU 1237 C SER A 156 5579 4051 6059 1066 -1094 846 C ATOM 1238 O SER A 156 -31.364 26.792 15.684 1.00 40.83 O ANISOU 1238 O SER A 156 5556 4004 5953 1112 -1151 973 O ATOM 1239 CB SER A 156 -28.489 27.171 16.978 1.00 32.89 C ANISOU 1239 CB SER A 156 4520 2924 5051 900 -1002 1135 C ATOM 1240 OG SER A 156 -28.043 25.840 17.172 1.00 52.92 O ANISOU 1240 OG SER A 156 7073 5660 7375 916 -906 1084 O ATOM 1241 N AGLN A 157 -31.168 25.270 17.327 0.80 39.34 N ANISOU 1241 N AGLN A 157 5309 3915 5725 1077 -1077 684 N ATOM 1242 N BGLN A 157 -31.176 25.266 17.309 0.20 31.25 N ANISOU 1242 N BGLN A 157 4285 2891 4699 1078 -1078 685 N ATOM 1243 CA AGLN A 157 -32.112 24.318 16.764 0.80 42.17 C ANISOU 1243 CA AGLN A 157 5670 4387 5965 1109 -1156 647 C ATOM 1244 CA BGLN A 157 -32.137 24.368 16.685 0.20 36.27 C ANISOU 1244 CA BGLN A 157 4927 3637 5218 1111 -1161 658 C ATOM 1245 C AGLN A 157 -33.534 24.536 17.262 0.80 41.12 C ANISOU 1245 C AGLN A 157 5374 4192 6059 1136 -1204 560 C ATOM 1246 C BGLN A 157 -33.567 24.630 17.139 0.20 35.57 C ANISOU 1246 C BGLN A 157 4676 3482 5357 1138 -1214 577 C ATOM 1247 O AGLN A 157 -34.412 23.725 16.956 0.80 49.07 O ANISOU 1247 O AGLN A 157 6333 5267 7045 1123 -1307 556 O ATOM 1248 O BGLN A 157 -34.487 23.948 16.676 0.20 34.73 O ANISOU 1248 O BGLN A 157 4531 3433 5232 1128 -1331 592 O ATOM 1249 CB AGLN A 157 -31.666 22.887 17.084 0.80 31.69 C ANISOU 1249 CB AGLN A 157 4397 3203 4442 1089 -1124 552 C ATOM 1250 CB BGLN A 157 -31.760 22.908 16.965 0.20 32.45 C ANISOU 1250 CB BGLN A 157 4497 3298 4536 1091 -1137 561 C ATOM 1251 CG AGLN A 157 -30.246 22.579 16.654 0.80 39.43 C ANISOU 1251 CG AGLN A 157 5519 4278 5184 1102 -1014 668 C ATOM 1252 CG BGLN A 157 -32.316 21.927 15.941 0.20 39.44 C ANISOU 1252 CG BGLN A 157 5498 4264 5222 1093 -1266 574 C ATOM 1253 CD AGLN A 157 -30.024 21.107 16.420 0.80 32.97 C ANISOU 1253 CD AGLN A 157 4820 3608 4098 1118 -995 595 C ATOM 1254 CD BGLN A 157 -32.126 20.484 16.350 0.20 53.55 C ANISOU 1254 CD BGLN A 157 7336 6147 6863 1061 -1266 449 C ATOM 1255 OE1AGLN A 157 -28.931 20.683 16.043 0.80112.29 O ANISOU 1255 OE1AGLN A 157 14973 13764 13928 1159 -854 687 O ATOM 1256 OE1BGLN A 157 -32.901 19.610 15.962 0.20 61.75 O ANISOU 1256 OE1BGLN A 157 8419 7184 7860 1021 -1425 401 O ATOM 1257 NE2AGLN A 157 -31.067 20.311 16.637 0.80 66.75 N ANISOU 1257 NE2AGLN A 157 9064 7882 8417 1081 -1128 453 N ATOM 1258 NE2BGLN A 157 -31.091 20.226 17.134 0.20 51.77 N ANISOU 1258 NE2BGLN A 157 7109 5984 6579 1067 -1111 407 N ATOM 1259 N GLY A 158 -33.782 25.604 18.019 1.00 28.98 N ANISOU 1259 N GLY A 158 3758 2517 4736 1181 -1132 511 N ATOM 1260 CA GLY A 158 -35.117 25.854 18.522 1.00 35.73 C ANISOU 1260 CA GLY A 158 4450 3338 5788 1267 -1107 474 C ATOM 1261 C GLY A 158 -35.610 24.837 19.524 1.00 34.70 C ANISOU 1261 C GLY A 158 4183 3315 5685 1290 -1019 375 C ATOM 1262 O GLY A 158 -36.822 24.701 19.700 1.00 39.80 O ANISOU 1262 O GLY A 158 4651 3995 6478 1354 -1010 433 O ATOM 1263 N CYS A 159 -34.703 24.118 20.191 1.00 33.28 N ANISOU 1263 N CYS A 159 4065 3199 5380 1243 -951 258 N ATOM 1264 CA CYS A 159 -35.107 23.101 21.155 1.00 35.75 C ANISOU 1264 CA CYS A 159 4246 3629 5710 1261 -859 181 C ATOM 1265 C CYS A 159 -35.801 23.734 22.355 1.00 42.87 C ANISOU 1265 C CYS A 159 5048 4487 6755 1426 -648 115 C ATOM 1266 O CYS A 159 -35.549 24.884 22.710 1.00 36.27 O ANISOU 1266 O CYS A 159 4338 3499 5944 1511 -574 40 O ATOM 1267 CB CYS A 159 -33.903 22.293 21.630 1.00 34.57 C ANISOU 1267 CB CYS A 159 4205 3555 5376 1188 -824 64 C ATOM 1268 SG CYS A 159 -33.145 21.296 20.329 1.00 33.35 S ANISOU 1268 SG CYS A 159 4206 3496 4968 1073 -991 154 S ATOM 1269 N GLY A 160 -36.691 22.964 22.976 1.00 40.25 N ANISOU 1269 N GLY A 160 4512 4283 6497 1483 -551 165 N ATOM 1270 CA GLY A 160 -37.424 23.429 24.130 1.00 42.22 C ANISOU 1270 CA GLY A 160 4683 4544 6813 1706 -297 140 C ATOM 1271 C GLY A 160 -36.610 23.303 25.397 1.00 44.37 C ANISOU 1271 C GLY A 160 5108 4822 6930 1761 -100 -60 C ATOM 1272 O GLY A 160 -35.469 22.842 25.407 1.00 34.61 O ANISOU 1272 O GLY A 160 4007 3594 5550 1606 -190 -189 O ATOM 1273 N GLU A 161 -37.223 23.716 26.500 1.00 44.16 N ANISOU 1273 N GLU A 161 5094 4820 6866 1994 105 -142 N ATOM 1274 CA GLU A 161 -36.533 23.661 27.778 1.00 37.03 C ANISOU 1274 CA GLU A 161 4346 3875 5847 1978 302 -336 C ATOM 1275 C GLU A 161 -36.375 22.222 28.237 1.00 45.25 C ANISOU 1275 C GLU A 161 5259 5154 6779 1886 356 -302 C ATOM 1276 O GLU A 161 -37.296 21.408 28.123 1.00 61.85 O ANISOU 1276 O GLU A 161 7066 7426 9007 1885 361 -121 O ATOM 1277 CB GLU A 161 -37.285 24.477 28.828 1.00 87.85 C ANISOU 1277 CB GLU A 161 10849 10269 12261 2213 512 -422 C ATOM 1278 CG GLU A 161 -36.834 25.925 28.897 1.00 61.08 C ANISOU 1278 CG GLU A 161 7780 6596 8830 2278 471 -573 C ATOM 1279 CD GLU A 161 -37.436 26.668 30.075 1.00129.40 C ANISOU 1279 CD GLU A 161 16590 15202 17375 2539 680 -687 C ATOM 1280 OE1 GLU A 161 -38.489 26.226 30.583 1.00126.40 O ANISOU 1280 OE1 GLU A 161 15993 15013 17020 2710 888 -570 O ATOM 1281 OE2 GLU A 161 -36.853 27.689 30.496 1.00114.51 O ANISOU 1281 OE2 GLU A 161 15066 13090 15354 2579 624 -868 O ATOM 1282 N GLY A 162 -35.187 21.909 28.755 1.00 42.69 N ANISOU 1282 N GLY A 162 4916 5131 6172 1797 540 -542 N ATOM 1283 CA GLY A 162 -34.847 20.555 29.117 1.00 50.73 C ANISOU 1283 CA GLY A 162 5862 6291 7123 1683 579 -519 C ATOM 1284 C GLY A 162 -34.487 19.664 27.951 1.00 46.08 C ANISOU 1284 C GLY A 162 5178 5757 6574 1569 446 -433 C ATOM 1285 O GLY A 162 -34.283 18.462 28.154 1.00 69.13 O ANISOU 1285 O GLY A 162 8016 8790 9459 1470 468 -403 O ATOM 1286 N GLN A 163 -34.424 20.204 26.735 1.00 38.64 N ANISOU 1286 N GLN A 163 4250 4738 5692 1581 301 -390 N ATOM 1287 CA GLN A 163 -34.067 19.426 25.560 1.00 30.40 C ANISOU 1287 CA GLN A 163 3146 3745 4661 1478 149 -325 C ATOM 1288 C GLN A 163 -32.679 19.812 25.070 1.00 28.57 C ANISOU 1288 C GLN A 163 3107 3423 4325 1413 40 -375 C ATOM 1289 O GLN A 163 -32.211 20.940 25.273 1.00 26.98 O ANISOU 1289 O GLN A 163 3072 3086 4094 1462 37 -428 O ATOM 1290 CB GLN A 163 -35.064 19.630 24.419 1.00 24.61 C ANISOU 1290 CB GLN A 163 2284 3004 4061 1518 44 -218 C ATOM 1291 CG GLN A 163 -36.468 19.132 24.689 1.00 26.07 C ANISOU 1291 CG GLN A 163 2244 3283 4380 1562 124 -126 C ATOM 1292 CD GLN A 163 -37.305 19.186 23.433 1.00 27.72 C ANISOU 1292 CD GLN A 163 2352 3525 4654 1591 -29 -21 C ATOM 1293 OE1 GLN A 163 -37.140 20.085 22.604 1.00 38.60 O ANISOU 1293 OE1 GLN A 163 3828 4799 6039 1630 -133 -15 O ATOM 1294 NE2 GLN A 163 -38.199 18.219 23.272 1.00 48.67 N ANISOU 1294 NE2 GLN A 163 4825 6327 7342 1561 -73 31 N ATOM 1295 N VAL A 164 -32.039 18.866 24.396 1.00 22.63 N ANISOU 1295 N VAL A 164 2341 2734 3523 1261 -43 -329 N ATOM 1296 CA VAL A 164 -30.750 19.078 23.752 1.00 20.91 C ANISOU 1296 CA VAL A 164 2280 2450 3214 1148 -129 -318 C ATOM 1297 C VAL A 164 -30.874 18.652 22.298 1.00 26.93 C ANISOU 1297 C VAL A 164 2997 3241 3994 1111 -263 -228 C ATOM 1298 O VAL A 164 -31.764 17.880 21.931 1.00 21.75 O ANISOU 1298 O VAL A 164 2192 2669 3404 1127 -307 -193 O ATOM 1299 CB VAL A 164 -29.623 18.275 24.436 1.00 20.49 C ANISOU 1299 CB VAL A 164 2287 2454 3046 1011 -80 -356 C ATOM 1300 CG1 VAL A 164 -29.469 18.716 25.881 1.00 26.82 C ANISOU 1300 CG1 VAL A 164 3166 3225 3800 1055 30 -453 C ATOM 1301 CG2 VAL A 164 -29.937 16.789 24.361 1.00 20.41 C ANISOU 1301 CG2 VAL A 164 2136 2582 3036 943 -74 -323 C ATOM 1302 N ALA A 165 -29.961 19.151 21.472 1.00 18.98 N ANISOU 1302 N ALA A 165 2124 2161 2926 1062 -333 -185 N ATOM 1303 CA ALA A 165 -29.765 18.543 20.162 1.00 23.99 C ANISOU 1303 CA ALA A 165 2761 2843 3510 1015 -442 -108 C ATOM 1304 C ALA A 165 -29.196 17.140 20.361 1.00 21.94 C ANISOU 1304 C ALA A 165 2468 2694 3175 899 -418 -129 C ATOM 1305 O ALA A 165 -28.133 16.974 20.974 1.00 18.10 O ANISOU 1305 O ALA A 165 2047 2211 2619 814 -347 -157 O ATOM 1306 CB ALA A 165 -28.827 19.395 19.306 1.00 22.14 C ANISOU 1306 CB ALA A 165 2682 2515 3217 995 -484 -37 C ATOM 1307 N CYS A 166 -29.914 16.128 19.884 1.00 17.19 N ANISOU 1307 N CYS A 166 1761 2173 2598 896 -490 -116 N ATOM 1308 CA CYS A 166 -29.547 14.747 20.194 1.00 17.12 C ANISOU 1308 CA CYS A 166 1710 2251 2543 798 -469 -142 C ATOM 1309 C CYS A 166 -28.438 14.333 19.240 1.00 25.24 C ANISOU 1309 C CYS A 166 2864 3288 3437 740 -517 -111 C ATOM 1310 O CYS A 166 -28.698 13.962 18.094 1.00 22.58 O ANISOU 1310 O CYS A 166 2553 2963 3062 764 -635 -79 O ATOM 1311 CB CYS A 166 -30.756 13.819 20.085 1.00 19.14 C ANISOU 1311 CB CYS A 166 1804 2566 2903 806 -540 -139 C ATOM 1312 SG CYS A 166 -30.351 12.127 20.564 1.00 23.84 S ANISOU 1312 SG CYS A 166 2354 3238 3466 682 -514 -165 S ATOM 1313 N LEU A 167 -27.196 14.421 19.714 1.00 18.72 N ANISOU 1313 N LEU A 167 2119 2456 2537 674 -427 -116 N ATOM 1314 CA LEU A 167 -26.003 14.056 18.965 1.00 14.18 C ANISOU 1314 CA LEU A 167 1646 1899 1844 627 -430 -72 C ATOM 1315 C LEU A 167 -25.151 13.171 19.856 1.00 14.24 C ANISOU 1315 C LEU A 167 1635 1960 1817 538 -349 -109 C ATOM 1316 O LEU A 167 -24.928 13.507 21.025 1.00 15.55 O ANISOU 1316 O LEU A 167 1779 2111 2017 505 -276 -146 O ATOM 1317 CB LEU A 167 -25.196 15.293 18.544 1.00 16.76 C ANISOU 1317 CB LEU A 167 2075 2150 2143 635 -404 -3 C ATOM 1318 CG LEU A 167 -25.937 16.183 17.537 1.00 22.33 C ANISOU 1318 CG LEU A 167 2821 2796 2867 732 -489 56 C ATOM 1319 CD1 LEU A 167 -25.224 17.503 17.369 1.00 25.18 C ANISOU 1319 CD1 LEU A 167 3272 3055 3239 729 -453 131 C ATOM 1320 CD2 LEU A 167 -26.016 15.427 16.208 1.00 25.63 C ANISOU 1320 CD2 LEU A 167 3292 3272 3175 770 -576 97 C ATOM 1321 N PHE A 168 -24.657 12.066 19.291 1.00 14.60 N ANISOU 1321 N PHE A 168 1704 2059 1783 513 -369 -99 N ATOM 1322 CA PHE A 168 -23.957 11.050 20.083 1.00 13.21 C ANISOU 1322 CA PHE A 168 1502 1935 1583 441 -308 -128 C ATOM 1323 C PHE A 168 -22.848 11.643 20.943 1.00 14.58 C ANISOU 1323 C PHE A 168 1696 2094 1750 385 -221 -117 C ATOM 1324 O PHE A 168 -22.801 11.406 22.152 1.00 13.03 O ANISOU 1324 O PHE A 168 1457 1914 1579 343 -175 -161 O ATOM 1325 CB PHE A 168 -23.370 9.978 19.162 1.00 11.86 C ANISOU 1325 CB PHE A 168 1390 1802 1314 447 -338 -112 C ATOM 1326 CG PHE A 168 -22.799 8.802 19.905 1.00 11.11 C ANISOU 1326 CG PHE A 168 1264 1750 1208 389 -292 -140 C ATOM 1327 CD1 PHE A 168 -23.567 7.681 20.117 1.00 12.94 C ANISOU 1327 CD1 PHE A 168 1444 1992 1482 373 -345 -185 C ATOM 1328 CD2 PHE A 168 -21.479 8.826 20.385 1.00 10.70 C ANISOU 1328 CD2 PHE A 168 1227 1719 1118 347 -206 -109 C ATOM 1329 CE1 PHE A 168 -23.052 6.591 20.822 1.00 13.89 C ANISOU 1329 CE1 PHE A 168 1542 2137 1597 323 -304 -199 C ATOM 1330 CE2 PHE A 168 -20.952 7.735 21.092 1.00 11.10 C ANISOU 1330 CE2 PHE A 168 1249 1808 1161 304 -172 -127 C ATOM 1331 CZ PHE A 168 -21.739 6.617 21.296 1.00 10.16 C ANISOU 1331 CZ PHE A 168 1096 1693 1073 297 -217 -171 C ATOM 1332 N GLU A 169 -21.921 12.385 20.340 1.00 11.45 N ANISOU 1332 N GLU A 169 1364 1666 1319 381 -204 -48 N ATOM 1333 CA GLU A 169 -20.772 12.812 21.142 1.00 11.27 C ANISOU 1333 CA GLU A 169 1343 1626 1312 306 -149 -31 C ATOM 1334 C GLU A 169 -21.099 13.962 22.087 1.00 14.56 C ANISOU 1334 C GLU A 169 1769 1961 1801 294 -154 -77 C ATOM 1335 O GLU A 169 -20.268 14.295 22.945 1.00 15.51 O ANISOU 1335 O GLU A 169 1899 2055 1939 227 -140 -88 O ATOM 1336 CB GLU A 169 -19.590 13.199 20.228 1.00 11.70 C ANISOU 1336 CB GLU A 169 1438 1673 1333 291 -119 81 C ATOM 1337 CG GLU A 169 -19.049 12.015 19.433 1.00 11.46 C ANISOU 1337 CG GLU A 169 1417 1729 1210 321 -89 119 C ATOM 1338 CD GLU A 169 -17.754 12.304 18.683 1.00 13.76 C ANISOU 1338 CD GLU A 169 1725 2035 1469 316 -18 247 C ATOM 1339 OE1 GLU A 169 -17.147 13.394 18.868 1.00 19.19 O ANISOU 1339 OE1 GLU A 169 2398 2663 2232 258 0 319 O ATOM 1340 OE2 GLU A 169 -17.331 11.421 17.917 1.00 13.36 O ANISOU 1340 OE2 GLU A 169 1701 2052 1323 373 22 280 O ATOM 1341 N ASP A 170 -22.281 14.568 21.963 1.00 13.74 N ANISOU 1341 N ASP A 170 1668 1812 1742 367 -183 -108 N ATOM 1342 CA ASP A 170 -22.677 15.577 22.929 1.00 14.19 C ANISOU 1342 CA ASP A 170 1747 1788 1857 385 -176 -170 C ATOM 1343 C ASP A 170 -23.251 14.971 24.204 1.00 16.23 C ANISOU 1343 C ASP A 170 1959 2100 2108 395 -131 -259 C ATOM 1344 O ASP A 170 -23.194 15.615 25.254 1.00 16.85 O ANISOU 1344 O ASP A 170 2084 2127 2190 400 -111 -323 O ATOM 1345 CB ASP A 170 -23.719 16.529 22.338 1.00 16.47 C ANISOU 1345 CB ASP A 170 2052 2002 2205 481 -213 -160 C ATOM 1346 CG ASP A 170 -23.154 17.427 21.262 1.00 35.07 C ANISOU 1346 CG ASP A 170 4479 4277 4570 478 -250 -61 C ATOM 1347 OD1 ASP A 170 -21.935 17.413 21.032 1.00 20.15 O ANISOU 1347 OD1 ASP A 170 2615 2386 2654 397 -233 5 O ATOM 1348 OD2 ASP A 170 -23.939 18.168 20.651 1.00 23.84 O ANISOU 1348 OD2 ASP A 170 3078 2793 3189 561 -290 -34 O ATOM 1349 N VAL A 171 -23.824 13.767 24.151 1.00 12.51 N ANISOU 1349 N VAL A 171 1407 1722 1623 402 -116 -262 N ATOM 1350 CA VAL A 171 -24.468 13.205 25.335 1.00 12.14 C ANISOU 1350 CA VAL A 171 1306 1729 1579 417 -54 -317 C ATOM 1351 C VAL A 171 -23.702 12.024 25.941 1.00 15.78 C ANISOU 1351 C VAL A 171 1754 2264 1978 340 -26 -314 C ATOM 1352 O VAL A 171 -23.758 11.835 27.163 1.00 14.61 O ANISOU 1352 O VAL A 171 1610 2145 1797 338 32 -354 O ATOM 1353 CB VAL A 171 -25.940 12.820 25.053 1.00 15.08 C ANISOU 1353 CB VAL A 171 1569 2135 2027 486 -53 -309 C ATOM 1354 CG1 VAL A 171 -26.723 14.063 24.589 1.00 18.78 C ANISOU 1354 CG1 VAL A 171 2045 2527 2563 581 -81 -311 C ATOM 1355 CG2 VAL A 171 -26.067 11.651 24.038 1.00 13.93 C ANISOU 1355 CG2 VAL A 171 1368 2037 1888 450 -122 -264 C ATOM 1356 N VAL A 172 -22.994 11.230 25.146 1.00 11.49 N ANISOU 1356 N VAL A 172 1207 1752 1407 291 -60 -266 N ATOM 1357 CA VAL A 172 -22.268 10.068 25.651 1.00 10.04 C ANISOU 1357 CA VAL A 172 1009 1630 1175 232 -38 -257 C ATOM 1358 C VAL A 172 -20.833 10.494 25.954 1.00 10.82 C ANISOU 1358 C VAL A 172 1164 1712 1235 176 -44 -242 C ATOM 1359 O VAL A 172 -20.124 10.933 25.032 1.00 12.55 O ANISOU 1359 O VAL A 172 1406 1904 1459 164 -70 -191 O ATOM 1360 CB VAL A 172 -22.287 8.904 24.648 1.00 13.67 C ANISOU 1360 CB VAL A 172 1441 2122 1630 228 -75 -222 C ATOM 1361 CG1 VAL A 172 -21.642 7.656 25.279 1.00 10.12 C ANISOU 1361 CG1 VAL A 172 978 1722 1146 180 -49 -213 C ATOM 1362 CG2 VAL A 172 -23.698 8.581 24.195 1.00 13.69 C ANISOU 1362 CG2 VAL A 172 1380 2121 1699 269 -112 -231 C ATOM 1363 N PRO A 173 -20.346 10.326 27.190 1.00 13.25 N ANISOU 1363 N PRO A 173 1488 2042 1506 139 -26 -270 N ATOM 1364 CA PRO A 173 -18.983 10.772 27.519 1.00 14.68 C ANISOU 1364 CA PRO A 173 1705 2199 1672 75 -63 -253 C ATOM 1365 C PRO A 173 -17.950 9.937 26.781 1.00 9.64 C ANISOU 1365 C PRO A 173 1023 1607 1032 40 -66 -175 C ATOM 1366 O PRO A 173 -18.080 8.714 26.690 1.00 10.31 O ANISOU 1366 O PRO A 173 1076 1751 1092 54 -42 -162 O ATOM 1367 CB PRO A 173 -18.883 10.539 29.042 1.00 13.50 C ANISOU 1367 CB PRO A 173 1590 2077 1461 61 -57 -308 C ATOM 1368 CG PRO A 173 -20.336 10.438 29.528 1.00 15.77 C ANISOU 1368 CG PRO A 173 1874 2383 1735 137 11 -356 C ATOM 1369 CD PRO A 173 -21.066 9.788 28.355 1.00 11.29 C ANISOU 1369 CD PRO A 173 1225 1837 1226 161 26 -310 C ATOM 1370 N AMET A 174 -16.897 10.595 26.286 0.79 9.99 N ANISOU 1370 N AMET A 174 1065 1619 1111 -2 -91 -115 N ATOM 1371 N BMET A 174 -16.906 10.605 26.274 0.21 9.99 N ANISOU 1371 N BMET A 174 1066 1618 1112 -1 -91 -115 N ATOM 1372 CA AMET A 174 -15.885 9.824 25.572 0.79 11.30 C ANISOU 1372 CA AMET A 174 1180 1838 1274 -11 -67 -29 C ATOM 1373 CA BMET A 174 -15.846 9.872 25.588 0.21 18.67 C ANISOU 1373 CA BMET A 174 2113 2770 2210 -14 -69 -27 C ATOM 1374 C AMET A 174 -14.998 9.023 26.530 0.79 9.75 C ANISOU 1374 C AMET A 174 946 1694 1063 -53 -81 -20 C ATOM 1375 C BMET A 174 -15.045 9.005 26.549 0.21 9.73 C ANISOU 1375 C BMET A 174 945 1692 1059 -52 -81 -23 C ATOM 1376 O AMET A 174 -14.425 8.008 26.120 0.79 9.56 O ANISOU 1376 O AMET A 174 880 1727 1024 -31 -48 32 O ATOM 1377 O BMET A 174 -14.578 7.929 26.157 0.21 14.79 O ANISOU 1377 O BMET A 174 1548 2390 1680 -26 -47 23 O ATOM 1378 CB AMET A 174 -15.036 10.756 24.696 0.79 16.22 C ANISOU 1378 CB AMET A 174 1788 2421 1953 -37 -64 65 C ATOM 1379 CB BMET A 174 -14.898 10.822 24.853 0.21 10.54 C ANISOU 1379 CB BMET A 174 1065 1699 1242 -50 -72 66 C ATOM 1380 CG AMET A 174 -14.371 10.108 23.511 0.79 17.35 C ANISOU 1380 CG AMET A 174 1897 2623 2073 8 1 164 C ATOM 1381 CG BMET A 174 -15.501 11.513 23.652 0.21 10.78 C ANISOU 1381 CG BMET A 174 1134 1686 1275 2 -50 99 C ATOM 1382 SD AMET A 174 -15.499 9.211 22.419 0.79 13.87 S ANISOU 1382 SD AMET A 174 1516 2213 1540 122 29 125 S ATOM 1383 SD BMET A 174 -16.185 10.388 22.423 0.21 49.73 S ANISOU 1383 SD BMET A 174 6091 6686 6119 109 -5 103 S ATOM 1384 CE AMET A 174 -15.931 10.416 21.170 0.79 21.93 C ANISOU 1384 CE AMET A 174 2595 3179 2560 165 33 180 C ATOM 1385 CE BMET A 174 -14.688 9.782 21.665 0.21 26.40 C ANISOU 1385 CE BMET A 174 3091 3798 3142 123 70 226 C ATOM 1386 N ASN A 175 -14.849 9.448 27.797 1.00 10.16 N ANISOU 1386 N ASN A 175 1024 1725 1110 -102 -137 -71 N ATOM 1387 CA ASN A 175 -14.103 8.597 28.716 1.00 11.61 C ANISOU 1387 CA ASN A 175 1181 1965 1264 -130 -164 -59 C ATOM 1388 C ASN A 175 -14.863 7.304 28.979 1.00 9.99 C ANISOU 1388 C ASN A 175 983 1817 997 -78 -111 -82 C ATOM 1389 O ASN A 175 -14.257 6.232 29.033 1.00 9.74 O ANISOU 1389 O ASN A 175 912 1834 956 -71 -102 -34 O ATOM 1390 CB ASN A 175 -13.731 9.308 30.021 1.00 12.79 C ANISOU 1390 CB ASN A 175 1382 2079 1399 -187 -257 -113 C ATOM 1391 CG ASN A 175 -14.888 10.029 30.698 1.00 15.80 C ANISOU 1391 CG ASN A 175 1869 2411 1723 -151 -255 -222 C ATOM 1392 OD1 ASN A 175 -16.059 9.751 30.465 1.00 14.27 O ANISOU 1392 OD1 ASN A 175 1687 2233 1502 -84 -176 -251 O ATOM 1393 ND2 ASN A 175 -14.531 10.956 31.583 1.00 16.25 N ANISOU 1393 ND2 ASN A 175 2003 2405 1768 -190 -351 -282 N ATOM 1394 N TYR A 176 -16.196 7.366 29.046 1.00 10.37 N ANISOU 1394 N TYR A 176 1068 1851 1022 -37 -74 -140 N ATOM 1395 CA TYR A 176 -16.972 6.128 29.048 1.00 13.08 C ANISOU 1395 CA TYR A 176 1393 2230 1345 -1 -27 -138 C ATOM 1396 C TYR A 176 -16.691 5.303 27.793 1.00 13.67 C ANISOU 1396 C TYR A 176 1436 2312 1447 26 -16 -91 C ATOM 1397 O TYR A 176 -16.413 4.103 27.875 1.00 9.80 O ANISOU 1397 O TYR A 176 931 1846 945 36 -8 -63 O ATOM 1398 CB TYR A 176 -18.480 6.421 29.173 1.00 9.55 C ANISOU 1398 CB TYR A 176 957 1767 906 36 11 -188 C ATOM 1399 CG TYR A 176 -19.286 5.170 28.891 1.00 8.87 C ANISOU 1399 CG TYR A 176 827 1698 845 53 40 -167 C ATOM 1400 CD1 TYR A 176 -19.742 4.921 27.598 1.00 8.70 C ANISOU 1400 CD1 TYR A 176 784 1649 871 77 18 -162 C ATOM 1401 CD2 TYR A 176 -19.559 4.220 29.881 1.00 9.13 C ANISOU 1401 CD2 TYR A 176 849 1765 855 44 76 -144 C ATOM 1402 CE1 TYR A 176 -20.455 3.771 27.299 1.00 10.85 C ANISOU 1402 CE1 TYR A 176 1024 1915 1184 80 9 -150 C ATOM 1403 CE2 TYR A 176 -20.300 3.068 29.589 1.00 9.70 C ANISOU 1403 CE2 TYR A 176 874 1830 981 42 89 -113 C ATOM 1404 CZ TYR A 176 -20.714 2.845 28.278 1.00 15.61 C ANISOU 1404 CZ TYR A 176 1602 2537 1793 55 43 -123 C ATOM 1405 OH TYR A 176 -21.421 1.716 27.912 1.00 15.34 O ANISOU 1405 OH TYR A 176 1530 2471 1827 42 18 -103 O ATOM 1406 N MET A 177 -16.772 5.928 26.609 1.00 9.41 N ANISOU 1406 N MET A 177 902 1744 930 50 -16 -83 N ATOM 1407 CA MET A 177 -16.645 5.159 25.370 1.00 8.38 C ANISOU 1407 CA MET A 177 776 1619 789 102 -5 -54 C ATOM 1408 C MET A 177 -15.270 4.503 25.235 1.00 10.45 C ANISOU 1408 C MET A 177 1012 1918 1039 112 17 10 C ATOM 1409 O MET A 177 -15.151 3.411 24.665 1.00 11.22 O ANISOU 1409 O MET A 177 1128 2022 1114 167 31 17 O ATOM 1410 CB MET A 177 -16.914 6.071 24.164 1.00 8.95 C ANISOU 1410 CB MET A 177 877 1661 862 137 -7 -44 C ATOM 1411 CG MET A 177 -18.395 6.450 24.009 1.00 10.09 C ANISOU 1411 CG MET A 177 1037 1769 1028 156 -38 -100 C ATOM 1412 SD MET A 177 -19.463 4.967 23.898 1.00 10.25 S ANISOU 1412 SD MET A 177 1048 1788 1060 176 -72 -140 S ATOM 1413 CE MET A 177 -18.902 4.249 22.350 1.00 9.79 C ANISOU 1413 CE MET A 177 1061 1724 935 248 -95 -123 C ATOM 1414 N VAL A 178 -14.215 5.168 25.699 1.00 9.14 N ANISOU 1414 N VAL A 178 804 1768 901 66 13 58 N ATOM 1415 CA VAL A 178 -12.849 4.634 25.521 1.00 9.30 C ANISOU 1415 CA VAL A 178 765 1832 936 83 39 140 C ATOM 1416 C VAL A 178 -12.452 3.684 26.646 1.00 10.42 C ANISOU 1416 C VAL A 178 882 2002 1074 66 11 142 C ATOM 1417 O VAL A 178 -12.056 2.537 26.390 1.00 10.90 O ANISOU 1417 O VAL A 178 935 2083 1123 126 38 170 O ATOM 1418 CB VAL A 178 -11.838 5.789 25.381 1.00 10.00 C ANISOU 1418 CB VAL A 178 789 1920 1089 31 37 218 C ATOM 1419 CG1 VAL A 178 -10.381 5.259 25.392 1.00 12.82 C ANISOU 1419 CG1 VAL A 178 1045 2333 1493 42 62 321 C ATOM 1420 CG2 VAL A 178 -12.102 6.515 24.073 1.00 12.58 C ANISOU 1420 CG2 VAL A 178 1147 2224 1410 71 87 250 C ATOM 1421 N TYR A 179 -12.545 4.121 27.917 1.00 9.85 N ANISOU 1421 N TYR A 179 815 1928 1000 -3 -48 111 N ATOM 1422 CA TYR A 179 -12.019 3.287 28.997 1.00 12.47 C ANISOU 1422 CA TYR A 179 1130 2294 1314 -14 -84 133 C ATOM 1423 C TYR A 179 -12.972 2.174 29.369 1.00 11.64 C ANISOU 1423 C TYR A 179 1077 2183 1163 18 -60 100 C ATOM 1424 O TYR A 179 -12.549 1.043 29.635 1.00 14.00 O ANISOU 1424 O TYR A 179 1365 2497 1458 48 -59 141 O ATOM 1425 CB TYR A 179 -11.755 4.125 30.253 1.00 10.63 C ANISOU 1425 CB TYR A 179 913 2060 1067 -87 -169 108 C ATOM 1426 CG TYR A 179 -10.620 5.113 30.123 1.00 13.37 C ANISOU 1426 CG TYR A 179 1190 2398 1492 -146 -231 157 C ATOM 1427 CD1 TYR A 179 -10.772 6.422 30.560 1.00 13.09 C ANISOU 1427 CD1 TYR A 179 1198 2307 1467 -212 -302 104 C ATOM 1428 CD2 TYR A 179 -9.400 4.730 29.606 1.00 18.00 C ANISOU 1428 CD2 TYR A 179 1664 3022 2155 -135 -221 262 C ATOM 1429 CE1 TYR A 179 -9.725 7.334 30.492 1.00 16.55 C ANISOU 1429 CE1 TYR A 179 1568 2716 2006 -288 -382 158 C ATOM 1430 CE2 TYR A 179 -8.350 5.635 29.507 1.00 15.30 C ANISOU 1430 CE2 TYR A 179 1227 2669 1916 -205 -279 332 C ATOM 1431 CZ TYR A 179 -8.520 6.933 29.950 1.00 20.99 C ANISOU 1431 CZ TYR A 179 1990 3323 2662 -293 -368 281 C ATOM 1432 OH TYR A 179 -7.483 7.822 29.866 1.00 22.39 O ANISOU 1432 OH TYR A 179 2068 3470 2970 -381 -445 358 O ATOM 1433 N PHE A 180 -14.252 2.495 29.487 1.00 11.93 N ANISOU 1433 N PHE A 180 1161 2193 1179 10 -42 37 N ATOM 1434 CA PHE A 180 -15.210 1.526 29.985 1.00 12.00 C ANISOU 1434 CA PHE A 180 1195 2194 1169 20 -18 27 C ATOM 1435 C PHE A 180 -15.725 0.681 28.831 1.00 11.26 C ANISOU 1435 C PHE A 180 1104 2059 1115 61 0 23 C ATOM 1436 O PHE A 180 -15.565 -0.540 28.832 1.00 16.32 O ANISOU 1436 O PHE A 180 1751 2681 1768 84 -2 53 O ATOM 1437 CB PHE A 180 -16.333 2.264 30.729 1.00 9.66 C ANISOU 1437 CB PHE A 180 929 1897 844 0 4 -23 C ATOM 1438 CG PHE A 180 -17.270 1.356 31.512 1.00 13.17 C ANISOU 1438 CG PHE A 180 1380 2348 1275 2 49 -1 C ATOM 1439 CD1 PHE A 180 -17.086 1.173 32.885 1.00 15.06 C ANISOU 1439 CD1 PHE A 180 1657 2630 1436 -4 59 25 C ATOM 1440 CD2 PHE A 180 -18.342 0.714 30.894 1.00 12.12 C ANISOU 1440 CD2 PHE A 180 1215 2178 1211 8 75 2 C ATOM 1441 CE1 PHE A 180 -17.960 0.372 33.633 1.00 17.92 C ANISOU 1441 CE1 PHE A 180 2021 3003 1783 0 124 71 C ATOM 1442 CE2 PHE A 180 -19.213 -0.088 31.624 1.00 12.35 C ANISOU 1442 CE2 PHE A 180 1227 2208 1259 -6 123 47 C ATOM 1443 CZ PHE A 180 -19.024 -0.263 33.003 1.00 14.60 C ANISOU 1443 CZ PHE A 180 1546 2542 1461 -7 163 91 C ATOM 1444 N ASN A 181 -16.290 1.318 27.799 1.00 9.06 N ANISOU 1444 N ASN A 181 833 1754 855 78 1 -16 N ATOM 1445 CA ASN A 181 -16.868 0.499 26.750 1.00 12.84 C ANISOU 1445 CA ASN A 181 1337 2185 1356 118 -14 -35 C ATOM 1446 C ASN A 181 -15.780 -0.212 25.950 1.00 18.68 C ANISOU 1446 C ASN A 181 2101 2923 2075 185 -8 -8 C ATOM 1447 O ASN A 181 -15.772 -1.448 25.865 1.00 18.22 O ANISOU 1447 O ASN A 181 2071 2823 2027 215 -24 -6 O ATOM 1448 CB ASN A 181 -17.797 1.322 25.857 1.00 11.54 C ANISOU 1448 CB ASN A 181 1184 1996 1205 130 -32 -80 C ATOM 1449 CG ASN A 181 -18.624 0.431 24.959 1.00 19.24 C ANISOU 1449 CG ASN A 181 2191 2911 2208 158 -85 -113 C ATOM 1450 OD1 ASN A 181 -18.232 0.145 23.825 1.00 20.02 O ANISOU 1450 OD1 ASN A 181 2351 2988 2266 222 -108 -127 O ATOM 1451 ND2 ASN A 181 -19.744 -0.059 25.477 1.00 16.58 N ANISOU 1451 ND2 ASN A 181 1817 2544 1940 113 -108 -119 N ATOM 1452 N PHE A 182 -14.811 0.531 25.416 1.00 10.71 N ANISOU 1452 N PHE A 182 1076 1950 1043 213 22 23 N ATOM 1453 CA PHE A 182 -13.833 -0.093 24.537 1.00 9.78 C ANISOU 1453 CA PHE A 182 975 1841 900 303 57 58 C ATOM 1454 C PHE A 182 -12.833 -0.936 25.312 1.00 13.92 C ANISOU 1454 C PHE A 182 1456 2389 1444 316 68 113 C ATOM 1455 O PHE A 182 -12.729 -2.149 25.100 1.00 14.96 O ANISOU 1455 O PHE A 182 1631 2482 1570 381 66 108 O ATOM 1456 CB PHE A 182 -13.084 0.975 23.720 1.00 10.41 C ANISOU 1456 CB PHE A 182 1030 1963 964 331 109 107 C ATOM 1457 CG PHE A 182 -12.110 0.399 22.695 1.00 12.95 C ANISOU 1457 CG PHE A 182 1369 2308 1244 452 181 156 C ATOM 1458 CD1 PHE A 182 -12.389 -0.798 22.045 1.00 10.89 C ANISOU 1458 CD1 PHE A 182 1207 2000 930 551 174 104 C ATOM 1459 CD2 PHE A 182 -10.918 1.058 22.385 1.00 11.66 C ANISOU 1459 CD2 PHE A 182 1123 2206 1101 473 258 259 C ATOM 1460 CE1 PHE A 182 -11.525 -1.309 21.085 1.00 11.73 C ANISOU 1460 CE1 PHE A 182 1355 2127 976 692 254 137 C ATOM 1461 CE2 PHE A 182 -10.035 0.545 21.441 1.00 17.53 C ANISOU 1461 CE2 PHE A 182 1874 2984 1801 606 356 318 C ATOM 1462 CZ PHE A 182 -10.331 -0.650 20.789 1.00 21.44 C ANISOU 1462 CZ PHE A 182 2492 3439 2216 729 361 250 C ATOM 1463 N PHE A 183 -12.032 -0.303 26.168 1.00 9.78 N ANISOU 1463 N PHE A 183 851 1919 947 261 64 169 N ATOM 1464 CA PHE A 183 -10.933 -1.055 26.774 1.00 10.15 C ANISOU 1464 CA PHE A 183 842 1996 1017 287 63 237 C ATOM 1465 C PHE A 183 -11.470 -2.196 27.638 1.00 13.33 C ANISOU 1465 C PHE A 183 1291 2360 1414 279 25 221 C ATOM 1466 O PHE A 183 -11.073 -3.362 27.470 1.00 14.66 O ANISOU 1466 O PHE A 183 1478 2499 1592 354 35 245 O ATOM 1467 CB PHE A 183 -10.032 -0.141 27.617 1.00 12.06 C ANISOU 1467 CB PHE A 183 990 2295 1299 213 25 295 C ATOM 1468 CG PHE A 183 -9.147 0.809 26.824 1.00 13.19 C ANISOU 1468 CG PHE A 183 1050 2472 1488 218 66 359 C ATOM 1469 CD1 PHE A 183 -9.152 0.847 25.445 1.00 15.68 C ANISOU 1469 CD1 PHE A 183 1389 2785 1782 302 154 370 C ATOM 1470 CD2 PHE A 183 -8.300 1.672 27.501 1.00 15.37 C ANISOU 1470 CD2 PHE A 183 1229 2779 1830 134 7 416 C ATOM 1471 CE1 PHE A 183 -8.319 1.723 24.742 1.00 21.03 C ANISOU 1471 CE1 PHE A 183 1984 3501 2507 306 212 459 C ATOM 1472 CE2 PHE A 183 -7.476 2.550 26.807 1.00 17.59 C ANISOU 1472 CE2 PHE A 183 1415 3083 2187 120 44 500 C ATOM 1473 CZ PHE A 183 -7.501 2.577 25.416 1.00 17.66 C ANISOU 1473 CZ PHE A 183 1437 3098 2174 208 162 531 C ATOM 1474 N ALA A 184 -12.367 -1.877 28.586 1.00 11.43 N ANISOU 1474 N ALA A 184 1071 2114 1159 195 -8 190 N ATOM 1475 CA ALA A 184 -12.785 -2.898 29.552 1.00 12.69 C ANISOU 1475 CA ALA A 184 1261 2247 1314 180 -28 210 C ATOM 1476 C ALA A 184 -13.772 -3.891 28.954 1.00 16.53 C ANISOU 1476 C ALA A 184 1806 2646 1829 203 -23 176 C ATOM 1477 O ALA A 184 -13.633 -5.093 29.161 1.00 15.10 O ANISOU 1477 O ALA A 184 1652 2414 1672 234 -36 211 O ATOM 1478 CB ALA A 184 -13.413 -2.256 30.797 1.00 12.93 C ANISOU 1478 CB ALA A 184 1301 2311 1302 103 -41 201 C ATOM 1479 N CYS A 185 -14.788 -3.411 28.237 1.00 13.34 N ANISOU 1479 N CYS A 185 1421 2212 1434 184 -23 112 N ATOM 1480 CA CYS A 185 -15.914 -4.263 27.858 1.00 9.91 C ANISOU 1480 CA CYS A 185 1027 1687 1050 173 -52 81 C ATOM 1481 C CYS A 185 -15.799 -4.872 26.467 1.00 12.95 C ANISOU 1481 C CYS A 185 1483 2000 1439 254 -85 30 C ATOM 1482 O CYS A 185 -16.550 -5.799 26.163 1.00 14.14 O ANISOU 1482 O CYS A 185 1681 2050 1642 247 -141 2 O ATOM 1483 CB CYS A 185 -17.222 -3.472 27.943 1.00 14.82 C ANISOU 1483 CB CYS A 185 1621 2314 1696 109 -52 46 C ATOM 1484 SG CYS A 185 -17.551 -3.106 29.717 1.00 19.81 S ANISOU 1484 SG CYS A 185 2209 3014 2305 42 1 104 S ATOM 1485 N VAL A 186 -14.879 -4.401 25.630 1.00 11.33 N ANISOU 1485 N VAL A 186 1291 1837 1177 334 -52 21 N ATOM 1486 CA VAL A 186 -14.762 -4.910 24.268 1.00 10.83 C ANISOU 1486 CA VAL A 186 1322 1715 1077 439 -68 -34 C ATOM 1487 C VAL A 186 -13.367 -5.505 24.050 1.00 15.48 C ANISOU 1487 C VAL A 186 1923 2325 1635 556 -10 10 C ATOM 1488 O VAL A 186 -13.218 -6.687 23.704 1.00 15.13 O ANISOU 1488 O VAL A 186 1963 2194 1593 638 -34 -15 O ATOM 1489 CB VAL A 186 -15.056 -3.781 23.250 1.00 10.59 C ANISOU 1489 CB VAL A 186 1311 1722 991 459 -58 -72 C ATOM 1490 CG1 VAL A 186 -14.699 -4.243 21.811 1.00 11.55 C ANISOU 1490 CG1 VAL A 186 1556 1806 1028 601 -56 -120 C ATOM 1491 CG2 VAL A 186 -16.531 -3.357 23.324 1.00 16.18 C ANISOU 1491 CG2 VAL A 186 2009 2393 1744 368 -129 -120 C ATOM 1492 N ALEU A 187 -12.334 -4.698 24.284 0.73 13.89 N ANISOU 1492 N ALEU A 187 1785 1774 1720 200 78 22 N ATOM 1493 N BLEU A 187 -12.336 -4.681 24.254 0.27 11.48 N ANISOU 1493 N BLEU A 187 1482 1466 1413 200 81 22 N ATOM 1494 CA ALEU A 187 -10.969 -5.124 23.978 0.73 15.64 C ANISOU 1494 CA ALEU A 187 1927 1951 2065 141 118 -58 C ATOM 1495 CA BLEU A 187 -10.961 -5.109 23.998 0.27 15.96 C ANISOU 1495 CA BLEU A 187 1966 1992 2106 140 117 -59 C ATOM 1496 C ALEU A 187 -10.527 -6.283 24.865 0.73 17.15 C ANISOU 1496 C ALEU A 187 2001 2243 2273 155 -22 -88 C ATOM 1497 C BLEU A 187 -10.573 -6.300 24.861 0.27 11.70 C ANISOU 1497 C BLEU A 187 1314 1554 1578 157 -24 -84 C ATOM 1498 O ALEU A 187 -9.967 -7.274 24.376 0.73 22.48 O ANISOU 1498 O ALEU A 187 2644 2915 2981 154 -36 -86 O ATOM 1499 O BLEU A 187 -10.080 -7.317 24.355 0.27 11.63 O ANISOU 1499 O BLEU A 187 1277 1543 1597 158 -39 -75 O ATOM 1500 CB ALEU A 187 -10.020 -3.932 24.121 0.73 18.03 C ANISOU 1500 CB ALEU A 187 2196 2158 2496 70 238 -181 C ATOM 1501 CB BLEU A 187 -9.996 -3.951 24.251 0.27 16.43 C ANISOU 1501 CB BLEU A 187 1981 1965 2295 69 225 -189 C ATOM 1502 CG ALEU A 187 -8.600 -4.087 23.573 0.73 25.56 C ANISOU 1502 CG ALEU A 187 3070 3054 3587 -7 330 -285 C ATOM 1503 CG BLEU A 187 -9.596 -3.108 23.048 0.27 14.64 C ANISOU 1503 CG BLEU A 187 1850 1583 2131 25 432 -182 C ATOM 1504 CD1ALEU A 187 -8.647 -4.690 22.172 0.73 20.00 C ANISOU 1504 CD1ALEU A 187 2448 2309 2842 10 399 -188 C ATOM 1505 CD1BLEU A 187 -8.406 -2.214 23.378 0.27 15.32 C ANISOU 1505 CD1BLEU A 187 1849 1579 2394 -83 551 -351 C ATOM 1506 CD2ALEU A 187 -7.937 -2.710 23.546 0.73 24.28 C ANISOU 1506 CD2ALEU A 187 2904 2763 3557 -97 502 -400 C ATOM 1507 CD2BLEU A 187 -9.305 -3.984 21.825 0.27 16.36 C ANISOU 1507 CD2BLEU A 187 2095 1794 2328 35 471 -121 C ATOM 1508 N VAL A 188 -10.748 -6.179 26.175 1.00 15.19 N ANISOU 1508 N VAL A 188 1693 2087 1992 188 -122 -114 N ATOM 1509 CA VAL A 188 -10.366 -7.272 27.069 1.00 16.08 C ANISOU 1509 CA VAL A 188 1717 2301 2092 241 -244 -118 C ATOM 1510 C VAL A 188 -11.084 -8.571 26.714 1.00 20.64 C ANISOU 1510 C VAL A 188 2354 2881 2606 272 -286 16 C ATOM 1511 O VAL A 188 -10.406 -9.599 26.565 1.00 17.24 O ANISOU 1511 O VAL A 188 1889 2443 2220 292 -311 15 O ATOM 1512 CB VAL A 188 -10.558 -6.862 28.539 1.00 15.06 C ANISOU 1512 CB VAL A 188 1520 2292 1910 295 -336 -161 C ATOM 1513 CG1 VAL A 188 -10.467 -8.120 29.434 1.00 22.28 C ANISOU 1513 CG1 VAL A 188 2389 3316 2761 391 -452 -100 C ATOM 1514 CG2 VAL A 188 -9.497 -5.871 28.938 1.00 17.54 C ANISOU 1514 CG2 VAL A 188 1723 2617 2326 260 -304 -353 C ATOM 1515 N PRO A 189 -12.412 -8.595 26.519 1.00 15.91 N ANISOU 1515 N PRO A 189 1838 2291 1917 276 -286 113 N ATOM 1516 CA PRO A 189 -13.036 -9.852 26.073 1.00 18.58 C ANISOU 1516 CA PRO A 189 2212 2618 2228 279 -302 199 C ATOM 1517 C PRO A 189 -12.533 -10.355 24.726 1.00 14.29 C ANISOU 1517 C PRO A 189 1684 1995 1749 250 -240 176 C ATOM 1518 O PRO A 189 -12.373 -11.575 24.560 1.00 16.27 O ANISOU 1518 O PRO A 189 1924 2222 2037 255 -261 199 O ATOM 1519 CB PRO A 189 -14.535 -9.500 26.025 1.00 19.52 C ANISOU 1519 CB PRO A 189 2391 2786 2241 279 -300 255 C ATOM 1520 CG PRO A 189 -14.701 -8.410 27.025 1.00 18.69 C ANISOU 1520 CG PRO A 189 2271 2742 2090 304 -330 232 C ATOM 1521 CD PRO A 189 -13.437 -7.588 26.901 1.00 13.16 C ANISOU 1521 CD PRO A 189 1534 1983 1485 286 -286 131 C ATOM 1522 N LEU A 190 -12.285 -9.473 23.754 1.00 12.23 N ANISOU 1522 N LEU A 190 1456 1689 1501 227 -152 135 N ATOM 1523 CA LEU A 190 -11.746 -9.954 22.479 1.00 13.10 C ANISOU 1523 CA LEU A 190 1574 1744 1658 212 -89 111 C ATOM 1524 C LEU A 190 -10.368 -10.582 22.676 1.00 12.92 C ANISOU 1524 C LEU A 190 1469 1697 1744 203 -108 46 C ATOM 1525 O LEU A 190 -10.061 -11.627 22.085 1.00 14.55 O ANISOU 1525 O LEU A 190 1659 1880 1988 209 -116 41 O ATOM 1526 CB LEU A 190 -11.685 -8.816 21.460 1.00 13.43 C ANISOU 1526 CB LEU A 190 1681 1742 1679 208 32 100 C ATOM 1527 CG LEU A 190 -13.024 -8.318 20.895 1.00 18.47 C ANISOU 1527 CG LEU A 190 2412 2421 2185 261 58 161 C ATOM 1528 CD1 LEU A 190 -12.816 -7.050 20.049 1.00 18.55 C ANISOU 1528 CD1 LEU A 190 2511 2366 2170 288 199 172 C ATOM 1529 CD2 LEU A 190 -13.679 -9.418 20.048 1.00 20.30 C ANISOU 1529 CD2 LEU A 190 2639 2709 2366 287 29 167 C ATOM 1530 N LEU A 191 -9.527 -9.971 23.517 1.00 12.48 N ANISOU 1530 N LEU A 191 1345 1659 1737 197 -121 -24 N ATOM 1531 CA LEU A 191 -8.218 -10.567 23.797 1.00 17.04 C ANISOU 1531 CA LEU A 191 1823 2252 2400 213 -155 -111 C ATOM 1532 C LEU A 191 -8.360 -11.896 24.531 1.00 19.33 C ANISOU 1532 C LEU A 191 2101 2578 2664 292 -263 -48 C ATOM 1533 O LEU A 191 -7.617 -12.842 24.252 1.00 19.38 O ANISOU 1533 O LEU A 191 2074 2567 2723 326 -281 -74 O ATOM 1534 CB LEU A 191 -7.346 -9.587 24.590 1.00 16.76 C ANISOU 1534 CB LEU A 191 1691 2259 2417 196 -149 -239 C ATOM 1535 CG LEU A 191 -6.911 -8.321 23.830 1.00 20.86 C ANISOU 1535 CG LEU A 191 2218 2700 3008 102 1 -319 C ATOM 1536 CD1 LEU A 191 -6.183 -7.328 24.747 1.00 23.03 C ANISOU 1536 CD1 LEU A 191 2382 3012 3355 67 13 -477 C ATOM 1537 CD2 LEU A 191 -6.067 -8.689 22.598 1.00 17.82 C ANISOU 1537 CD2 LEU A 191 1820 2259 2693 64 92 -359 C ATOM 1538 N LEU A 192 -9.321 -11.998 25.457 1.00 14.33 N ANISOU 1538 N LEU A 192 1505 1987 1951 327 -321 41 N ATOM 1539 CA LEU A 192 -9.607 -13.286 26.090 1.00 19.21 C ANISOU 1539 CA LEU A 192 2146 2608 2545 398 -383 134 C ATOM 1540 C LEU A 192 -10.046 -14.324 25.065 1.00 18.31 C ANISOU 1540 C LEU A 192 2089 2399 2469 364 -342 179 C ATOM 1541 O LEU A 192 -9.627 -15.489 25.127 1.00 21.06 O ANISOU 1541 O LEU A 192 2441 2698 2864 416 -360 203 O ATOM 1542 CB LEU A 192 -10.689 -13.121 27.158 1.00 18.72 C ANISOU 1542 CB LEU A 192 2121 2607 2386 424 -421 227 C ATOM 1543 CG LEU A 192 -10.298 -12.318 28.393 1.00 25.08 C ANISOU 1543 CG LEU A 192 2858 3532 3140 487 -482 178 C ATOM 1544 CD1 LEU A 192 -11.511 -12.151 29.303 1.00 35.66 C ANISOU 1544 CD1 LEU A 192 4240 4937 4372 507 -509 276 C ATOM 1545 CD2 LEU A 192 -9.193 -13.049 29.107 1.00 28.52 C ANISOU 1545 CD2 LEU A 192 3228 4024 3583 610 -546 150 C ATOM 1546 N MET A 193 -10.895 -13.923 24.115 1.00 18.26 N ANISOU 1546 N MET A 193 2126 2372 2441 293 -285 180 N ATOM 1547 CA MET A 193 -11.303 -14.825 23.039 1.00 22.33 C ANISOU 1547 CA MET A 193 2667 2826 2991 262 -248 178 C ATOM 1548 C MET A 193 -10.098 -15.318 22.257 1.00 17.75 C ANISOU 1548 C MET A 193 2048 2200 2498 275 -231 103 C ATOM 1549 O MET A 193 -10.002 -16.501 21.920 1.00 19.70 O ANISOU 1549 O MET A 193 2298 2383 2806 288 -233 100 O ATOM 1550 CB MET A 193 -12.267 -14.117 22.076 1.00 20.10 C ANISOU 1550 CB MET A 193 2418 2577 2641 219 -198 160 C ATOM 1551 CG MET A 193 -13.667 -13.986 22.525 1.00 31.21 C ANISOU 1551 CG MET A 193 3856 4037 3967 204 -211 211 C ATOM 1552 SD MET A 193 -14.556 -13.115 21.212 1.00 26.96 S ANISOU 1552 SD MET A 193 3348 3568 3328 208 -158 165 S ATOM 1553 CE MET A 193 -15.453 -11.956 22.258 1.00 24.21 C ANISOU 1553 CE MET A 193 3030 3296 2872 225 -186 219 C ATOM 1554 N LEU A 194 -9.197 -14.404 21.910 1.00 19.24 N ANISOU 1554 N LEU A 194 2197 2414 2701 266 -200 31 N ATOM 1555 CA LEU A 194 -7.983 -14.786 21.204 1.00 20.07 C ANISOU 1555 CA LEU A 194 2246 2495 2883 275 -177 -55 C ATOM 1556 C LEU A 194 -7.207 -15.832 21.991 1.00 20.12 C ANISOU 1556 C LEU A 194 2211 2491 2942 355 -252 -60 C ATOM 1557 O LEU A 194 -6.753 -16.833 21.431 1.00 21.21 O ANISOU 1557 O LEU A 194 2338 2580 3139 384 -254 -89 O ATOM 1558 CB LEU A 194 -7.131 -13.543 20.951 1.00 17.92 C ANISOU 1558 CB LEU A 194 1929 2250 2630 237 -111 -135 C ATOM 1559 CG LEU A 194 -5.773 -13.792 20.310 1.00 22.91 C ANISOU 1559 CG LEU A 194 2480 2879 3344 236 -76 -245 C ATOM 1560 CD1 LEU A 194 -5.933 -14.512 18.963 1.00 21.27 C ANISOU 1560 CD1 LEU A 194 2302 2638 3142 234 -34 -246 C ATOM 1561 CD2 LEU A 194 -5.027 -12.474 20.181 1.00 31.13 C ANISOU 1561 CD2 LEU A 194 3475 3932 4420 170 20 -330 C ATOM 1562 N GLY A 195 -7.065 -15.622 23.305 1.00 19.55 N ANISOU 1562 N GLY A 195 2119 2473 2836 412 -314 -33 N ATOM 1563 CA GLY A 195 -6.377 -16.608 24.129 1.00 16.97 C ANISOU 1563 CA GLY A 195 1769 2156 2524 534 -385 -19 C ATOM 1564 C GLY A 195 -7.072 -17.956 24.136 1.00 19.52 C ANISOU 1564 C GLY A 195 2182 2371 2865 568 -382 93 C ATOM 1565 O GLY A 195 -6.418 -19.001 24.084 1.00 23.70 O ANISOU 1565 O GLY A 195 2714 2846 3446 654 -399 88 O ATOM 1566 N VAL A 196 -8.403 -17.955 24.214 1.00 17.74 N ANISOU 1566 N VAL A 196 2028 2108 2604 502 -351 183 N ATOM 1567 CA VAL A 196 -9.149 -19.213 24.144 1.00 21.75 C ANISOU 1567 CA VAL A 196 2613 2494 3158 497 -316 264 C ATOM 1568 C VAL A 196 -8.924 -19.910 22.802 1.00 21.43 C ANISOU 1568 C VAL A 196 2560 2370 3213 453 -276 176 C ATOM 1569 O VAL A 196 -8.709 -21.126 22.747 1.00 18.00 O ANISOU 1569 O VAL A 196 2159 1820 2860 499 -260 193 O ATOM 1570 CB VAL A 196 -10.646 -18.975 24.403 1.00 21.75 C ANISOU 1570 CB VAL A 196 2662 2496 3106 413 -281 337 C ATOM 1571 CG1 VAL A 196 -11.404 -20.272 24.245 1.00 16.76 C ANISOU 1571 CG1 VAL A 196 2090 1726 2552 375 -216 384 C ATOM 1572 CG2 VAL A 196 -10.855 -18.397 25.792 1.00 21.70 C ANISOU 1572 CG2 VAL A 196 2667 2579 3000 472 -322 424 C ATOM 1573 N TYR A 197 -8.994 -19.162 21.696 1.00 17.22 N ANISOU 1573 N TYR A 197 1984 1890 2668 376 -249 84 N ATOM 1574 CA TYR A 197 -8.777 -19.795 20.393 1.00 18.65 C ANISOU 1574 CA TYR A 197 2141 2023 2921 350 -215 -11 C ATOM 1575 C TYR A 197 -7.363 -20.342 20.266 1.00 26.06 C ANISOU 1575 C TYR A 197 3036 2939 3927 433 -242 -71 C ATOM 1576 O TYR A 197 -7.170 -21.431 19.719 1.00 24.10 O ANISOU 1576 O TYR A 197 2792 2602 3764 454 -230 -113 O ATOM 1577 CB TYR A 197 -9.110 -18.828 19.243 1.00 17.12 C ANISOU 1577 CB TYR A 197 1921 1916 2668 286 -173 -81 C ATOM 1578 CG TYR A 197 -10.609 -18.806 19.017 1.00 20.71 C ANISOU 1578 CG TYR A 197 2406 2388 3073 227 -149 -65 C ATOM 1579 CD1 TYR A 197 -11.267 -19.951 18.600 1.00 16.47 C ANISOU 1579 CD1 TYR A 197 1867 1785 2607 195 -128 -111 C ATOM 1580 CD2 TYR A 197 -11.381 -17.672 19.306 1.00 18.51 C ANISOU 1580 CD2 TYR A 197 2151 2195 2687 205 -145 -20 C ATOM 1581 CE1 TYR A 197 -12.640 -19.972 18.428 1.00 20.01 C ANISOU 1581 CE1 TYR A 197 2314 2270 3018 135 -104 -133 C ATOM 1582 CE2 TYR A 197 -12.763 -17.687 19.137 1.00 20.85 C ANISOU 1582 CE2 TYR A 197 2459 2534 2929 165 -131 -25 C ATOM 1583 CZ TYR A 197 -13.384 -18.832 18.699 1.00 21.86 C ANISOU 1583 CZ TYR A 197 2563 2615 3126 126 -111 -89 C ATOM 1584 OH TYR A 197 -14.751 -18.875 18.542 1.00 24.37 O ANISOU 1584 OH TYR A 197 2864 2996 3399 79 -95 -131 O ATOM 1585 N LEU A 198 -6.364 -19.619 20.775 1.00 19.53 N ANISOU 1585 N LEU A 198 2156 2196 3069 482 -278 -96 N ATOM 1586 CA LEU A 198 -5.002 -20.156 20.789 1.00 25.22 C ANISOU 1586 CA LEU A 198 2817 2925 3842 579 -314 -170 C ATOM 1587 C LEU A 198 -4.933 -21.471 21.557 1.00 24.64 C ANISOU 1587 C LEU A 198 2805 2752 3804 701 -351 -91 C ATOM 1588 O LEU A 198 -4.293 -22.432 21.109 1.00 21.55 O ANISOU 1588 O LEU A 198 2407 2296 3486 769 -356 -142 O ATOM 1589 CB LEU A 198 -4.038 -19.134 21.395 1.00 25.32 C ANISOU 1589 CB LEU A 198 2740 3066 3815 609 -346 -236 C ATOM 1590 CG LEU A 198 -3.804 -17.887 20.535 1.00 50.15 C ANISOU 1590 CG LEU A 198 5828 6272 6955 494 -274 -326 C ATOM 1591 CD1 LEU A 198 -2.929 -16.871 21.261 1.00 32.42 C ANISOU 1591 CD1 LEU A 198 3484 4134 4699 500 -287 -413 C ATOM 1592 CD2 LEU A 198 -3.191 -18.268 19.189 1.00 39.59 C ANISOU 1592 CD2 LEU A 198 4449 4919 5673 472 -223 -422 C ATOM 1593 N ARG A 199 -5.605 -21.542 22.708 1.00 23.53 N ANISOU 1593 N ARG A 199 2736 2594 3612 739 -365 40 N ATOM 1594 CA ARG A 199 -5.613 -22.784 23.473 1.00 23.93 C ANISOU 1594 CA ARG A 199 2876 2528 3688 868 -367 150 C ATOM 1595 C ARG A 199 -6.331 -23.910 22.728 1.00 22.82 C ANISOU 1595 C ARG A 199 2810 2199 3663 800 -288 165 C ATOM 1596 O ARG A 199 -5.901 -25.065 22.800 1.00 23.42 O ANISOU 1596 O ARG A 199 2941 2146 3813 905 -273 189 O ATOM 1597 CB ARG A 199 -6.247 -22.548 24.842 1.00 26.56 C ANISOU 1597 CB ARG A 199 3273 2894 3925 921 -378 298 C ATOM 1598 CG ARG A 199 -5.423 -21.650 25.746 1.00 42.43 C ANISOU 1598 CG ARG A 199 5200 5096 5827 1029 -466 261 C ATOM 1599 CD ARG A 199 -6.078 -21.499 27.110 1.00 38.28 C ANISOU 1599 CD ARG A 199 4736 4616 5191 1103 -479 407 C ATOM 1600 NE ARG A 199 -5.136 -20.967 28.090 1.00 84.76 N ANISOU 1600 NE ARG A 199 10535 10693 10976 1238 -564 353 N ATOM 1601 CZ ARG A 199 -4.273 -21.713 28.774 1.00 95.42 C ANISOU 1601 CZ ARG A 199 11895 12076 12286 1375 -583 368 C ATOM 1602 NH1 ARG A 199 -4.237 -23.025 28.587 1.00 85.88 N ANISOU 1602 NH1 ARG A 199 10788 10704 11137 1450 -539 458 N ATOM 1603 NH2 ARG A 199 -3.446 -21.149 29.644 1.00 80.62 N ANISOU 1603 NH2 ARG A 199 9931 10390 10311 1441 -641 279 N ATOM 1604 N ILE A 200 -7.430 -23.604 22.025 1.00 18.30 N ANISOU 1604 N ILE A 200 2235 1612 3108 636 -234 136 N ATOM 1605 CA ILE A 200 -8.137 -24.632 21.254 1.00 20.92 C ANISOU 1605 CA ILE A 200 2600 1788 3559 557 -158 96 C ATOM 1606 C ILE A 200 -7.220 -25.230 20.191 1.00 19.15 C ANISOU 1606 C ILE A 200 2324 1531 3423 593 -169 -40 C ATOM 1607 O ILE A 200 -7.110 -26.456 20.043 1.00 23.72 O ANISOU 1607 O ILE A 200 2950 1943 4119 634 -128 -51 O ATOM 1608 CB ILE A 200 -9.394 -24.038 20.599 1.00 19.10 C ANISOU 1608 CB ILE A 200 2337 1617 3302 397 -119 42 C ATOM 1609 CG1 ILE A 200 -10.478 -23.727 21.634 1.00 18.65 C ANISOU 1609 CG1 ILE A 200 2337 1566 3184 352 -93 168 C ATOM 1610 CG2 ILE A 200 -9.920 -24.975 19.530 1.00 18.34 C ANISOU 1610 CG2 ILE A 200 2221 1419 3329 316 -57 -80 C ATOM 1611 CD1 ILE A 200 -11.631 -22.892 21.049 1.00 21.86 C ANISOU 1611 CD1 ILE A 200 2696 2086 3525 226 -78 103 C ATOM 1612 N PHE A 201 -6.591 -24.365 19.397 1.00 24.01 N ANISOU 1612 N PHE A 201 2842 2296 3986 574 -207 -151 N ATOM 1613 CA PHE A 201 -5.770 -24.852 18.295 1.00 22.98 C ANISOU 1613 CA PHE A 201 2647 2161 3924 600 -211 -291 C ATOM 1614 C PHE A 201 -4.523 -25.561 18.805 1.00 26.38 C ANISOU 1614 C PHE A 201 3084 2547 4394 762 -258 -286 C ATOM 1615 O PHE A 201 -4.098 -26.564 18.221 1.00 27.80 O ANISOU 1615 O PHE A 201 3261 2630 4672 813 -248 -363 O ATOM 1616 CB PHE A 201 -5.430 -23.692 17.359 1.00 23.94 C ANISOU 1616 CB PHE A 201 2675 2454 3968 542 -213 -389 C ATOM 1617 CG PHE A 201 -6.629 -23.151 16.628 1.00 20.01 C ANISOU 1617 CG PHE A 201 2176 2008 3420 427 -167 -411 C ATOM 1618 CD1 PHE A 201 -6.981 -21.817 16.731 1.00 27.68 C ANISOU 1618 CD1 PHE A 201 3144 3096 4277 380 -157 -368 C ATOM 1619 CD2 PHE A 201 -7.428 -23.995 15.871 1.00 27.85 C ANISOU 1619 CD2 PHE A 201 3165 2936 4481 379 -131 -491 C ATOM 1620 CE1 PHE A 201 -8.084 -21.329 16.071 1.00 27.71 C ANISOU 1620 CE1 PHE A 201 3152 3164 4214 313 -121 -387 C ATOM 1621 CE2 PHE A 201 -8.535 -23.519 15.209 1.00 27.19 C ANISOU 1621 CE2 PHE A 201 3060 2938 4332 302 -100 -537 C ATOM 1622 CZ PHE A 201 -8.870 -22.174 15.315 1.00 23.92 C ANISOU 1622 CZ PHE A 201 2655 2653 3781 281 -99 -475 C ATOM 1623 N ALA A 202 -3.951 -25.090 19.920 1.00 23.47 N ANISOU 1623 N ALA A 202 2718 2255 3943 863 -312 -208 N ATOM 1624 CA ALA A 202 -2.824 -25.802 20.514 1.00 34.03 C ANISOU 1624 CA ALA A 202 4061 3576 5291 1058 -366 -204 C ATOM 1625 C ALA A 202 -3.258 -27.162 21.056 1.00 28.01 C ANISOU 1625 C ALA A 202 3443 2593 4606 1150 -321 -80 C ATOM 1626 O ALA A 202 -2.530 -28.154 20.927 1.00 24.75 O ANISOU 1626 O ALA A 202 3056 2089 4260 1288 -329 -110 O ATOM 1627 CB ALA A 202 -2.192 -24.954 21.620 1.00 32.76 C ANISOU 1627 CB ALA A 202 3852 3584 5010 1156 -439 -174 C ATOM 1628 N ALA A 203 -4.453 -27.237 21.652 1.00 28.15 N ANISOU 1628 N ALA A 203 3560 2513 4621 1077 -257 58 N ATOM 1629 CA ALA A 203 -4.941 -28.524 22.137 1.00 26.64 C ANISOU 1629 CA ALA A 203 3520 2079 4524 1138 -170 182 C ATOM 1630 C ALA A 203 -5.204 -29.478 20.978 1.00 31.02 C ANISOU 1630 C ALA A 203 4075 2458 5252 1047 -98 62 C ATOM 1631 O ALA A 203 -4.841 -30.656 21.042 1.00 28.25 O ANISOU 1631 O ALA A 203 3813 1920 5001 1159 -53 86 O ATOM 1632 CB ALA A 203 -6.197 -28.329 22.988 1.00 31.48 C ANISOU 1632 CB ALA A 203 4222 2639 5101 1053 -98 340 C ATOM 1633 N ALA A 204 -5.796 -28.978 19.894 1.00 34.63 N ANISOU 1633 N ALA A 204 4434 2988 5734 860 -87 -79 N ATOM 1634 CA ALA A 204 -6.001 -29.805 18.711 1.00 32.93 C ANISOU 1634 CA ALA A 204 4185 2658 5669 782 -34 -237 C ATOM 1635 C ALA A 204 -4.677 -30.299 18.144 1.00 35.67 C ANISOU 1635 C ALA A 204 4484 3014 6054 920 -92 -346 C ATOM 1636 O ALA A 204 -4.543 -31.476 17.792 1.00 32.70 O ANISOU 1636 O ALA A 204 4158 2471 5796 952 -40 -396 O ATOM 1637 CB ALA A 204 -6.770 -29.015 17.654 1.00 28.41 C ANISOU 1637 CB ALA A 204 3498 2234 5061 604 -34 -376 C ATOM 1638 N ARG A 205 -3.686 -29.411 18.047 1.00 28.59 N ANISOU 1638 N ARG A 205 3491 2334 5036 986 -188 -391 N ATOM 1639 CA ARG A 205 -2.387 -29.805 17.505 1.00 31.37 C ANISOU 1639 CA ARG A 205 3776 2735 5408 1112 -243 -512 C ATOM 1640 C ARG A 205 -1.739 -30.896 18.353 1.00 34.32 C ANISOU 1640 C ARG A 205 4271 2993 5776 1294 -233 -401 C ATOM 1641 O ARG A 205 -1.163 -31.855 17.819 1.00 33.95 O ANISOU 1641 O ARG A 205 4236 2878 5784 1356 -216 -474 O ATOM 1642 CB ARG A 205 -1.476 -28.575 17.407 1.00 32.68 C ANISOU 1642 CB ARG A 205 3811 3159 5447 1130 -323 -577 C ATOM 1643 CG ARG A 205 -0.053 -28.895 16.992 1.00 69.38 C ANISOU 1643 CG ARG A 205 8382 7915 10066 1233 -369 -688 C ATOM 1644 CD ARG A 205 0.833 -27.669 17.090 1.00 42.69 C ANISOU 1644 CD ARG A 205 4873 4773 6575 1231 -421 -753 C ATOM 1645 NE ARG A 205 0.724 -27.030 18.396 1.00 81.94 N ANISOU 1645 NE ARG A 205 9874 9798 11461 1283 -456 -635 N ATOM 1646 CZ ARG A 205 1.333 -25.897 18.725 1.00 98.58 C ANISOU 1646 CZ ARG A 205 11876 12099 13482 1265 -490 -687 C ATOM 1647 NH1 ARG A 205 2.101 -25.277 17.841 1.00107.63 N ANISOU 1647 NH1 ARG A 205 12891 13382 14623 1189 -477 -842 N ATOM 1648 NH2 ARG A 205 1.174 -25.384 19.937 1.00124.71 N ANISOU 1648 NH2 ARG A 205 15211 15465 16710 1313 -523 -591 N ATOM 1649 N ARG A 206 -1.838 -30.772 19.679 1.00 33.02 N ANISOU 1649 N ARG A 206 4201 2814 5531 1398 -235 -221 N ATOM 1650 CA ARG A 206 -1.251 -31.766 20.573 1.00 32.27 C ANISOU 1650 CA ARG A 206 4232 2626 5405 1606 -201 -88 C ATOM 1651 C ARG A 206 -1.960 -33.111 20.468 1.00 41.94 C ANISOU 1651 C ARG A 206 5635 3554 6747 1594 -79 -32 C ATOM 1652 O ARG A 206 -1.315 -34.166 20.503 1.00 38.39 O ANISOU 1652 O ARG A 206 5272 2997 6317 1746 -38 -14 O ATOM 1653 CB ARG A 206 -1.295 -31.247 22.010 1.00 40.32 C ANISOU 1653 CB ARG A 206 5283 3729 6307 1703 -223 94 C ATOM 1654 CG ARG A 206 -0.811 -32.252 23.028 1.00 42.19 C ANISOU 1654 CG ARG A 206 5598 3870 6561 1875 -214 236 C ATOM 1655 CD ARG A 206 -0.721 -31.652 24.417 1.00113.61 C ANISOU 1655 CD ARG A 206 14654 13084 15429 1958 -285 357 C ATOM 1656 NE ARG A 206 -0.078 -32.573 25.350 1.00139.83 N ANISOU 1656 NE ARG A 206 18062 16379 18687 2154 -297 460 N ATOM 1657 CZ ARG A 206 0.247 -32.266 26.602 1.00129.79 C ANISOU 1657 CZ ARG A 206 16807 15278 17228 2281 -348 549 C ATOM 1658 NH1 ARG A 206 -0.009 -31.054 27.076 1.00130.13 N ANISOU 1658 NH1 ARG A 206 16773 15520 17150 2217 -397 539 N ATOM 1659 NH2 ARG A 206 0.830 -33.171 27.377 1.00103.38 N ANISOU 1659 NH2 ARG A 206 13558 11911 13812 2482 -345 639 N ATOM 1660 N GLN A 207 -3.288 -33.103 20.355 1.00 35.92 N ANISOU 1660 N GLN A 207 4916 2661 6072 1399 -10 -14 N ATOM 1661 CA GLN A 207 -4.011 -34.370 20.332 1.00 41.13 C ANISOU 1661 CA GLN A 207 5718 3052 6856 1335 107 18 C ATOM 1662 C GLN A 207 -3.745 -35.136 19.045 1.00 33.64 C ANISOU 1662 C GLN A 207 4709 2035 6037 1278 134 -176 C ATOM 1663 O GLN A 207 -3.632 -36.364 19.066 1.00 35.94 O ANISOU 1663 O GLN A 207 5123 2130 6404 1338 195 -165 O ATOM 1664 CB GLN A 207 -5.502 -34.126 20.514 1.00 38.33 C ANISOU 1664 CB GLN A 207 5377 2620 6568 1113 208 70 C ATOM 1665 CG GLN A 207 -5.847 -33.493 21.832 1.00 39.10 C ANISOU 1665 CG GLN A 207 5543 2780 6535 1162 197 273 C ATOM 1666 CD GLN A 207 -7.339 -33.356 22.015 1.00 55.87 C ANISOU 1666 CD GLN A 207 7683 4826 8720 946 319 322 C ATOM 1667 OE1 GLN A 207 -8.120 -34.033 21.343 1.00 53.88 O ANISOU 1667 OE1 GLN A 207 7421 4431 8620 777 427 218 O ATOM 1668 NE2 GLN A 207 -7.748 -32.477 22.924 1.00 38.45 N ANISOU 1668 NE2 GLN A 207 5486 2734 6391 950 299 459 N ATOM 1669 N LEU A 208 -3.644 -34.431 17.919 1.00 41.48 N ANISOU 1669 N LEU A 208 5513 3197 7051 1165 78 -361 N ATOM 1670 CA LEU A 208 -3.304 -35.090 16.664 1.00 39.31 C ANISOU 1670 CA LEU A 208 5156 2910 6869 1125 79 -559 C ATOM 1671 C LEU A 208 -1.899 -35.672 16.722 1.00 44.91 C ANISOU 1671 C LEU A 208 5897 3637 7528 1344 29 -560 C ATOM 1672 O LEU A 208 -1.668 -36.802 16.276 1.00 43.12 O ANISOU 1672 O LEU A 208 5725 3266 7391 1383 76 -625 O ATOM 1673 CB LEU A 208 -3.437 -34.101 15.503 1.00 43.58 C ANISOU 1673 CB LEU A 208 5494 3673 7392 988 14 -745 C ATOM 1674 CG LEU A 208 -4.859 -33.733 15.063 1.00 92.92 C ANISOU 1674 CG LEU A 208 11684 9919 13702 776 73 -815 C ATOM 1675 CD1 LEU A 208 -4.836 -32.612 14.034 1.00112.39 C ANISOU 1675 CD1 LEU A 208 13977 12637 16088 707 -1 -967 C ATOM 1676 CD2 LEU A 208 -5.594 -34.949 14.507 1.00 48.89 C ANISOU 1676 CD2 LEU A 208 6127 4168 8282 667 176 -922 C ATOM 1677 N ALA A1001 -0.951 -34.917 17.284 1.00 52.06 N ANISOU 1677 N ALA A1001 6643 3290 9847 1646 -687 -965 N ATOM 1678 CA ALA A1001 0.403 -35.429 17.463 1.00 54.82 C ANISOU 1678 CA ALA A1001 6687 3489 10652 1465 -595 -816 C ATOM 1679 C ALA A1001 0.405 -36.669 18.346 1.00 55.42 C ANISOU 1679 C ALA A1001 6523 3859 10675 1368 -748 -947 C ATOM 1680 O ALA A1001 1.115 -37.643 18.064 1.00 51.42 O ANISOU 1680 O ALA A1001 5912 3350 10277 1319 -538 -793 O ATOM 1681 CB ALA A1001 1.300 -34.342 18.053 1.00 56.61 C ANISOU 1681 CB ALA A1001 6623 3415 11470 1288 -761 -826 C ATOM 1682 N ASP A1002 -0.401 -36.662 19.411 1.00 48.64 N ANISOU 1682 N ASP A1002 5588 3259 9633 1367 -1103 -1218 N ATOM 1683 CA ASP A1002 -0.482 -37.829 20.282 1.00 46.50 C ANISOU 1683 CA ASP A1002 5136 3251 9281 1327 -1220 -1316 C ATOM 1684 C ASP A1002 -1.034 -39.045 19.542 1.00 63.82 C ANISOU 1684 C ASP A1002 7502 5604 11141 1395 -931 -1226 C ATOM 1685 O ASP A1002 -0.579 -40.173 19.769 1.00 50.31 O ANISOU 1685 O ASP A1002 5656 3954 9505 1344 -826 -1152 O ATOM 1686 CB ASP A1002 -1.331 -37.510 21.512 1.00 45.72 C ANISOU 1686 CB ASP A1002 4971 3406 8995 1374 -1640 -1611 C ATOM 1687 CG ASP A1002 -0.670 -36.497 22.434 1.00 51.21 C ANISOU 1687 CG ASP A1002 5438 3969 10051 1329 -2009 -1774 C ATOM 1688 OD1 ASP A1002 0.571 -36.359 22.377 1.00 80.94 O ANISOU 1688 OD1 ASP A1002 8984 7472 14299 1215 -1956 -1670 O ATOM 1689 OD2 ASP A1002 -1.389 -35.841 23.217 1.00 92.22 O ANISOU 1689 OD2 ASP A1002 10646 9327 15065 1413 -2372 -2031 O ATOM 1690 N LEU A1003 -2.011 -38.842 18.652 1.00 48.19 N ANISOU 1690 N LEU A1003 5808 3687 8814 1524 -813 -1249 N ATOM 1691 CA LEU A1003 -2.519 -39.953 17.847 1.00 42.37 C ANISOU 1691 CA LEU A1003 5210 3077 7812 1600 -571 -1215 C ATOM 1692 C LEU A1003 -1.429 -40.527 16.954 1.00 43.45 C ANISOU 1692 C LEU A1003 5386 3026 8098 1627 -261 -976 C ATOM 1693 O LEU A1003 -1.257 -41.749 16.865 1.00 47.07 O ANISOU 1693 O LEU A1003 5777 3568 8538 1601 -143 -944 O ATOM 1694 CB LEU A1003 -3.705 -39.501 16.994 1.00 42.33 C ANISOU 1694 CB LEU A1003 5464 3168 7452 1753 -531 -1315 C ATOM 1695 CG LEU A1003 -5.043 -39.248 17.682 1.00 51.11 C ANISOU 1695 CG LEU A1003 6533 4567 8320 1740 -838 -1579 C ATOM 1696 CD1 LEU A1003 -5.963 -38.512 16.730 1.00 55.65 C ANISOU 1696 CD1 LEU A1003 7340 5193 8612 1894 -820 -1650 C ATOM 1697 CD2 LEU A1003 -5.663 -40.560 18.124 1.00 51.89 C ANISOU 1697 CD2 LEU A1003 6487 4901 8327 1671 -858 -1690 C ATOM 1698 N GLU A1004 -0.696 -39.656 16.262 1.00 58.45 N ANISOU 1698 N GLU A1004 7389 4662 10156 1690 -131 -804 N ATOM 1699 CA GLU A1004 0.345 -40.133 15.363 1.00 79.47 C ANISOU 1699 CA GLU A1004 10057 7168 12969 1729 141 -575 C ATOM 1700 C GLU A1004 1.498 -40.762 16.132 1.00 77.33 C ANISOU 1700 C GLU A1004 9403 6855 13122 1490 147 -478 C ATOM 1701 O GLU A1004 2.101 -41.732 15.657 1.00 61.50 O ANISOU 1701 O GLU A1004 7341 4861 11167 1486 355 -350 O ATOM 1702 CB GLU A1004 0.839 -38.986 14.482 1.00 61.34 C ANISOU 1702 CB GLU A1004 7913 4585 10807 1840 289 -385 C ATOM 1703 CG GLU A1004 1.561 -39.442 13.226 1.00110.22 C ANISOU 1703 CG GLU A1004 14162 10679 17036 1964 607 -155 C ATOM 1704 CD GLU A1004 0.798 -40.518 12.470 1.00 93.69 C ANISOU 1704 CD GLU A1004 12272 8837 14488 2203 603 -319 C ATOM 1705 OE1 GLU A1004 1.407 -41.557 12.145 1.00 80.74 O ANISOU 1705 OE1 GLU A1004 10504 7246 12928 2164 777 -231 O ATOM 1706 OE2 GLU A1004 -0.409 -40.330 12.205 1.00 97.81 O ANISOU 1706 OE2 GLU A1004 13061 9513 14591 2439 414 -559 O ATOM 1707 N ASP A1005 1.805 -40.242 17.324 1.00 50.99 N ANISOU 1707 N ASP A1005 5800 3488 10086 1324 -102 -563 N ATOM 1708 CA ASP A1005 2.867 -40.829 18.133 1.00 49.67 C ANISOU 1708 CA ASP A1005 5267 3301 10306 1160 -141 -509 C ATOM 1709 C ASP A1005 2.500 -42.233 18.593 1.00 67.69 C ANISOU 1709 C ASP A1005 7528 5827 12364 1175 -144 -569 C ATOM 1710 O ASP A1005 3.352 -43.127 18.602 1.00 55.22 O ANISOU 1710 O ASP A1005 5787 4230 10963 1119 9 -432 O ATOM 1711 CB ASP A1005 3.177 -39.940 19.334 1.00 69.26 C ANISOU 1711 CB ASP A1005 7478 5714 13124 1054 -496 -667 C ATOM 1712 CG ASP A1005 4.095 -38.784 18.984 1.00 79.09 C ANISOU 1712 CG ASP A1005 8564 6624 14861 957 -439 -552 C ATOM 1713 OD1 ASP A1005 4.931 -38.934 18.066 1.00 80.46 O ANISOU 1713 OD1 ASP A1005 8695 6621 15254 924 -84 -284 O ATOM 1714 OD2 ASP A1005 3.984 -37.725 19.635 1.00 80.78 O ANISOU 1714 OD2 ASP A1005 8675 6749 15269 918 -742 -731 O ATOM 1715 N ASN A1006 1.241 -42.447 18.984 1.00 52.36 N ANISOU 1715 N ASN A1006 5728 4099 10066 1249 -293 -759 N ATOM 1716 CA ASN A1006 0.834 -43.785 19.395 1.00 67.79 C ANISOU 1716 CA ASN A1006 7651 6239 11868 1257 -247 -790 C ATOM 1717 C ASN A1006 0.801 -44.743 18.211 1.00 41.73 C ANISOU 1717 C ASN A1006 4506 2930 8418 1309 43 -698 C ATOM 1718 O ASN A1006 1.099 -45.933 18.367 1.00 51.37 O ANISOU 1718 O ASN A1006 5634 4192 9692 1273 160 -633 O ATOM 1719 CB ASN A1006 -0.526 -43.737 20.091 1.00 61.88 C ANISOU 1719 CB ASN A1006 6964 5702 10847 1310 -447 -1005 C ATOM 1720 CG ASN A1006 -0.404 -43.641 21.604 1.00 75.92 C ANISOU 1720 CG ASN A1006 8537 7583 12726 1311 -708 -1087 C ATOM 1721 OD1 ASN A1006 0.549 -44.148 22.195 1.00 94.77 O ANISOU 1721 OD1 ASN A1006 10744 9939 15326 1292 -696 -980 O ATOM 1722 ND2 ASN A1006 -1.375 -42.996 22.237 1.00 65.71 N ANISOU 1722 ND2 ASN A1006 7285 6441 11239 1374 -956 -1286 N ATOM 1723 N TRP A1007 0.451 -44.240 17.027 1.00 54.58 N ANISOU 1723 N TRP A1007 6384 4504 9849 1432 146 -701 N ATOM 1724 CA TRP A1007 0.491 -45.063 15.826 1.00 44.94 C ANISOU 1724 CA TRP A1007 5323 3283 8468 1552 366 -655 C ATOM 1725 C TRP A1007 1.921 -45.478 15.494 1.00 50.30 C ANISOU 1725 C TRP A1007 5846 3821 9445 1489 575 -420 C ATOM 1726 O TRP A1007 2.188 -46.652 15.203 1.00 44.10 O ANISOU 1726 O TRP A1007 5026 3076 8653 1492 710 -386 O ATOM 1727 CB TRP A1007 -0.147 -44.302 14.663 1.00 43.63 C ANISOU 1727 CB TRP A1007 5481 3100 7995 1792 399 -714 C ATOM 1728 CG TRP A1007 -0.131 -45.068 13.384 1.00 65.57 C ANISOU 1728 CG TRP A1007 8431 5910 10571 2005 548 -730 C ATOM 1729 CD1 TRP A1007 0.628 -44.808 12.281 1.00 51.42 C ANISOU 1729 CD1 TRP A1007 6713 3999 8827 2164 700 -595 C ATOM 1730 CD2 TRP A1007 -0.902 -46.235 13.077 1.00 49.14 C ANISOU 1730 CD2 TRP A1007 6417 3986 8268 2076 557 -902 C ATOM 1731 NE1 TRP A1007 0.374 -45.739 11.304 1.00 76.03 N ANISOU 1731 NE1 TRP A1007 9930 7227 11730 2370 730 -734 N ATOM 1732 CE2 TRP A1007 -0.561 -46.628 11.768 1.00 46.02 C ANISOU 1732 CE2 TRP A1007 6164 3589 7734 2335 638 -924 C ATOM 1733 CE3 TRP A1007 -1.851 -46.984 13.783 1.00 47.54 C ANISOU 1733 CE3 TRP A1007 6109 3909 8044 1925 489 -1058 C ATOM 1734 CZ2 TRP A1007 -1.139 -47.733 11.146 1.00 52.29 C ANISOU 1734 CZ2 TRP A1007 7064 4502 8300 2485 666 -1090 C ATOM 1735 CZ3 TRP A1007 -2.423 -48.077 13.168 1.00 44.26 C ANISOU 1735 CZ3 TRP A1007 5745 3564 7507 1993 551 -1199 C ATOM 1736 CH2 TRP A1007 -2.064 -48.443 11.860 1.00 59.57 C ANISOU 1736 CH2 TRP A1007 7888 5486 9260 2269 676 -1193 C ATOM 1737 N GLU A1008 2.859 -44.527 15.547 1.00 45.86 N ANISOU 1737 N GLU A1008 5157 3078 9188 1419 620 -253 N ATOM 1738 CA GLU A1008 4.260 -44.844 15.278 1.00 48.39 C ANISOU 1738 CA GLU A1008 5267 3262 9858 1338 861 -4 C ATOM 1739 C GLU A1008 4.825 -45.784 16.331 1.00 57.23 C ANISOU 1739 C GLU A1008 6114 4450 11182 1196 803 9 C ATOM 1740 O GLU A1008 5.563 -46.721 16.004 1.00 56.49 O ANISOU 1740 O GLU A1008 5938 4348 11178 1190 1007 147 O ATOM 1741 CB GLU A1008 5.100 -43.569 15.226 1.00 50.30 C ANISOU 1741 CB GLU A1008 5357 3267 10486 1260 925 163 C ATOM 1742 CG GLU A1008 4.695 -42.578 14.163 1.00 51.90 C ANISOU 1742 CG GLU A1008 5836 3354 10530 1426 1044 226 C ATOM 1743 CD GLU A1008 5.389 -41.240 14.345 1.00115.22 C ANISOU 1743 CD GLU A1008 13674 11104 18999 1306 1076 370 C ATOM 1744 OE1 GLU A1008 6.406 -41.195 15.069 1.00118.36 O ANISOU 1744 OE1 GLU A1008 13681 11394 19897 1103 1056 439 O ATOM 1745 OE2 GLU A1008 4.915 -40.235 13.774 1.00106.44 O ANISOU 1745 OE2 GLU A1008 12793 9876 17772 1428 1104 398 O ATOM 1746 N THR A1009 4.505 -45.537 17.604 1.00 51.84 N ANISOU 1746 N THR A1009 5302 3837 10558 1122 523 -128 N ATOM 1747 CA THR A1009 4.981 -46.412 18.672 1.00 55.89 C ANISOU 1747 CA THR A1009 5598 4425 11211 1064 452 -112 C ATOM 1748 C THR A1009 4.523 -47.846 18.451 1.00 57.45 C ANISOU 1748 C THR A1009 5914 4743 11170 1113 596 -110 C ATOM 1749 O THR A1009 5.283 -48.796 18.680 1.00 54.91 O ANISOU 1749 O THR A1009 5466 4417 10980 1093 715 16 O ATOM 1750 CB THR A1009 4.495 -45.898 20.025 1.00 57.46 C ANISOU 1750 CB THR A1009 5707 4719 11406 1068 111 -288 C ATOM 1751 OG1 THR A1009 5.188 -44.689 20.355 1.00 66.53 O ANISOU 1751 OG1 THR A1009 6662 5716 12900 1002 -64 -317 O ATOM 1752 CG2 THR A1009 4.729 -46.944 21.113 1.00 57.40 C ANISOU 1752 CG2 THR A1009 5573 4841 11397 1111 60 -263 C ATOM 1753 N LEU A1010 3.285 -48.021 17.993 1.00 45.30 N ANISOU 1753 N LEU A1010 4605 3295 9312 1181 580 -263 N ATOM 1754 CA LEU A1010 2.789 -49.359 17.696 1.00 42.51 C ANISOU 1754 CA LEU A1010 4330 3006 8816 1208 703 -302 C ATOM 1755 C LEU A1010 3.629 -50.027 16.612 1.00 45.88 C ANISOU 1755 C LEU A1010 4788 3351 9293 1246 946 -172 C ATOM 1756 O LEU A1010 4.091 -51.163 16.778 1.00 44.17 O ANISOU 1756 O LEU A1010 4487 3124 9173 1218 1066 -88 O ATOM 1757 CB LEU A1010 1.317 -49.282 17.285 1.00 47.76 C ANISOU 1757 CB LEU A1010 5195 3764 9188 1279 618 -531 C ATOM 1758 CG LEU A1010 0.715 -50.542 16.662 1.00 65.14 C ANISOU 1758 CG LEU A1010 7474 5989 11289 1312 728 -634 C ATOM 1759 CD1 LEU A1010 0.879 -51.710 17.591 1.00 54.68 C ANISOU 1759 CD1 LEU A1010 5970 4646 10161 1212 806 -552 C ATOM 1760 CD2 LEU A1010 -0.755 -50.326 16.343 1.00 68.61 C ANISOU 1760 CD2 LEU A1010 8054 6526 11488 1376 611 -887 C ATOM 1761 N ASN A1011 3.862 -49.326 15.502 1.00 50.22 N ANISOU 1761 N ASN A1011 5468 3836 9778 1341 1035 -136 N ATOM 1762 CA ASN A1011 4.561 -49.946 14.378 1.00 54.30 C ANISOU 1762 CA ASN A1011 6042 4299 10292 1441 1274 -24 C ATOM 1763 C ASN A1011 6.055 -50.100 14.650 1.00 47.76 C ANISOU 1763 C ASN A1011 4966 3372 9809 1345 1451 241 C ATOM 1764 O ASN A1011 6.664 -51.097 14.238 1.00 48.70 O ANISOU 1764 O ASN A1011 5060 3479 9963 1384 1627 332 O ATOM 1765 CB ASN A1011 4.312 -49.132 13.110 1.00 52.03 C ANISOU 1765 CB ASN A1011 5983 3983 9804 1641 1338 -46 C ATOM 1766 CG ASN A1011 2.885 -49.264 12.622 1.00 56.05 C ANISOU 1766 CG ASN A1011 6743 4618 9936 1811 1159 -350 C ATOM 1767 OD1 ASN A1011 2.299 -50.347 12.690 1.00 65.69 O ANISOU 1767 OD1 ASN A1011 7979 5917 11062 1814 1103 -516 O ATOM 1768 ND2 ASN A1011 2.314 -48.168 12.138 1.00 65.22 N ANISOU 1768 ND2 ASN A1011 8085 5786 10910 1961 1072 -425 N ATOM 1769 N ASP A1012 6.664 -49.133 15.339 1.00 48.29 N ANISOU 1769 N ASP A1012 4831 3360 10157 1233 1389 344 N ATOM 1770 CA ASP A1012 8.070 -49.263 15.712 1.00 50.03 C ANISOU 1770 CA ASP A1012 4758 3487 10766 1143 1512 557 C ATOM 1771 C ASP A1012 8.296 -50.494 16.578 1.00 49.37 C ANISOU 1771 C ASP A1012 4574 3487 10698 1114 1461 551 C ATOM 1772 O ASP A1012 9.192 -51.308 16.309 1.00 50.64 O ANISOU 1772 O ASP A1012 4651 3618 10973 1135 1652 701 O ATOM 1773 CB ASP A1012 8.540 -48.010 16.450 1.00 63.51 C ANISOU 1773 CB ASP A1012 6223 5081 12827 1028 1359 578 C ATOM 1774 CG ASP A1012 8.579 -46.787 15.557 1.00 71.21 C ANISOU 1774 CG ASP A1012 7255 5906 13894 1051 1492 666 C ATOM 1775 OD1 ASP A1012 8.630 -46.958 14.320 1.00 75.01 O ANISOU 1775 OD1 ASP A1012 7919 6364 14216 1182 1778 795 O ATOM 1776 OD2 ASP A1012 8.565 -45.657 16.094 1.00 70.80 O ANISOU 1776 OD2 ASP A1012 7075 5750 14075 965 1311 608 O ATOM 1777 N ASN A1013 7.493 -50.649 17.631 1.00 47.74 N ANISOU 1777 N ASN A1013 4385 3383 10372 1094 1227 401 N ATOM 1778 CA ASN A1013 7.729 -51.756 18.549 1.00 62.27 C ANISOU 1778 CA ASN A1013 6139 5286 12233 1108 1209 444 C ATOM 1779 C ASN A1013 7.444 -53.107 17.903 1.00 48.32 C ANISOU 1779 C ASN A1013 4519 3528 10313 1152 1402 453 C ATOM 1780 O ASN A1013 8.067 -54.107 18.275 1.00 48.50 O ANISOU 1780 O ASN A1013 4463 3542 10421 1177 1497 570 O ATOM 1781 CB ASN A1013 6.910 -51.566 19.821 1.00 56.86 C ANISOU 1781 CB ASN A1013 5450 4710 11445 1130 958 319 C ATOM 1782 CG ASN A1013 7.639 -50.731 20.854 1.00 53.22 C ANISOU 1782 CG ASN A1013 4769 4259 11192 1146 730 320 C ATOM 1783 OD1 ASN A1013 8.863 -50.796 20.961 1.00 76.27 O ANISOU 1783 OD1 ASN A1013 7494 7119 14365 1144 767 435 O ATOM 1784 ND2 ASN A1013 6.895 -49.946 21.621 1.00 47.18 N ANISOU 1784 ND2 ASN A1013 4021 3577 10330 1181 472 161 N ATOM 1785 N LEU A1014 6.526 -53.162 16.934 1.00 48.87 N ANISOU 1785 N LEU A1014 4797 3605 10167 1188 1438 311 N ATOM 1786 CA LEU A1014 6.363 -54.394 16.165 1.00 52.64 C ANISOU 1786 CA LEU A1014 5389 4057 10553 1250 1588 272 C ATOM 1787 C LEU A1014 7.648 -54.755 15.431 1.00 49.31 C ANISOU 1787 C LEU A1014 4918 3572 10247 1312 1801 452 C ATOM 1788 O LEU A1014 8.045 -55.928 15.399 1.00 50.26 O ANISOU 1788 O LEU A1014 5021 3660 10414 1344 1916 506 O ATOM 1789 CB LEU A1014 5.205 -54.256 15.178 1.00 48.45 C ANISOU 1789 CB LEU A1014 5084 3556 9770 1335 1528 34 C ATOM 1790 CG LEU A1014 3.803 -54.407 15.763 1.00 46.62 C ANISOU 1790 CG LEU A1014 4892 3375 9445 1282 1372 -170 C ATOM 1791 CD1 LEU A1014 2.747 -54.020 14.739 1.00 57.48 C ANISOU 1791 CD1 LEU A1014 6476 4801 10561 1404 1273 -423 C ATOM 1792 CD2 LEU A1014 3.591 -55.840 16.232 1.00 56.04 C ANISOU 1792 CD2 LEU A1014 6011 4508 10774 1227 1465 -167 C ATOM 1793 N LYS A1015 8.315 -53.758 14.838 1.00 50.22 N ANISOU 1793 N LYS A1015 4998 3650 10435 1338 1883 564 N ATOM 1794 CA LYS A1015 9.587 -54.016 14.165 1.00 52.44 C ANISOU 1794 CA LYS A1015 5194 3864 10866 1403 2132 777 C ATOM 1795 C LYS A1015 10.643 -54.502 15.151 1.00 53.22 C ANISOU 1795 C LYS A1015 5044 3942 11235 1327 2150 939 C ATOM 1796 O LYS A1015 11.421 -55.412 14.841 1.00 62.95 O ANISOU 1796 O LYS A1015 6247 5152 12520 1397 2315 1052 O ATOM 1797 CB LYS A1015 10.073 -52.754 13.450 1.00 53.86 C ANISOU 1797 CB LYS A1015 5341 3972 11153 1433 2271 919 C ATOM 1798 CG LYS A1015 9.165 -52.246 12.340 1.00 72.68 C ANISOU 1798 CG LYS A1015 8009 6382 13224 1594 2282 794 C ATOM 1799 CD LYS A1015 9.661 -50.906 11.809 1.00108.63 C ANISOU 1799 CD LYS A1015 12514 10828 17932 1619 2462 1000 C ATOM 1800 CE LYS A1015 8.785 -50.373 10.681 1.00104.13 C ANISOU 1800 CE LYS A1015 12264 10295 17007 1849 2484 900 C ATOM 1801 NZ LYS A1015 9.002 -51.103 9.400 1.00106.35 N ANISOU 1801 NZ LYS A1015 12732 10628 17050 2127 2696 933 N ATOM 1802 N VAL A1016 10.684 -53.901 16.344 1.00 55.70 N ANISOU 1802 N VAL A1016 5188 4272 11702 1227 1951 931 N ATOM 1803 CA VAL A1016 11.630 -54.322 17.378 1.00 67.48 C ANISOU 1803 CA VAL A1016 6462 5771 13407 1223 1897 1041 C ATOM 1804 C VAL A1016 11.439 -55.797 17.714 1.00 65.70 C ANISOU 1804 C VAL A1016 6336 5594 13032 1298 1944 1044 C ATOM 1805 O VAL A1016 12.410 -56.555 17.841 1.00 58.01 O ANISOU 1805 O VAL A1016 5269 4606 12165 1367 2050 1181 O ATOM 1806 CB VAL A1016 11.476 -53.427 18.625 1.00 53.31 C ANISOU 1806 CB VAL A1016 4521 4017 11719 1175 1602 954 C ATOM 1807 CG1 VAL A1016 12.263 -53.983 19.794 1.00 59.59 C ANISOU 1807 CG1 VAL A1016 5148 4881 12614 1266 1484 1011 C ATOM 1808 CG2 VAL A1016 11.923 -52.013 18.314 1.00 54.72 C ANISOU 1808 CG2 VAL A1016 4531 4077 12183 1083 1572 971 C ATOM 1809 N ILE A1017 10.185 -56.232 17.847 1.00 51.95 N ANISOU 1809 N ILE A1017 4772 3887 11079 1290 1882 898 N ATOM 1810 CA ILE A1017 9.914 -57.630 18.172 1.00 69.61 C ANISOU 1810 CA ILE A1017 7079 6109 13260 1340 1963 916 C ATOM 1811 C ILE A1017 10.382 -58.549 17.049 1.00 55.45 C ANISOU 1811 C ILE A1017 5365 4240 11463 1405 2172 944 C ATOM 1812 O ILE A1017 10.957 -59.617 17.301 1.00 55.16 O ANISOU 1812 O ILE A1017 5300 4165 11495 1474 2279 1053 O ATOM 1813 CB ILE A1017 8.418 -57.824 18.470 1.00 50.93 C ANISOU 1813 CB ILE A1017 4837 3752 10761 1292 1884 752 C ATOM 1814 CG1 ILE A1017 8.046 -57.102 19.767 1.00 50.11 C ANISOU 1814 CG1 ILE A1017 4658 3742 10641 1292 1689 754 C ATOM 1815 CG2 ILE A1017 8.077 -59.304 18.538 1.00 52.05 C ANISOU 1815 CG2 ILE A1017 5034 3803 10938 1318 2034 771 C ATOM 1816 CD1 ILE A1017 6.559 -56.979 19.989 1.00 55.64 C ANISOU 1816 CD1 ILE A1017 5455 4460 11226 1244 1613 594 C ATOM 1817 N GLU A1018 10.145 -58.151 15.796 1.00 53.61 N ANISOU 1817 N GLU A1018 5252 3991 11125 1431 2223 843 N ATOM 1818 CA GLU A1018 10.506 -59.002 14.666 1.00 55.26 C ANISOU 1818 CA GLU A1018 5569 4148 11281 1559 2386 828 C ATOM 1819 C GLU A1018 12.001 -59.276 14.627 1.00 71.82 C ANISOU 1819 C GLU A1018 7523 6227 13537 1627 2551 1062 C ATOM 1820 O GLU A1018 12.424 -60.406 14.354 1.00 65.81 O ANISOU 1820 O GLU A1018 6799 5421 12785 1729 2661 1089 O ATOM 1821 CB GLU A1018 10.063 -58.363 13.354 1.00 61.72 C ANISOU 1821 CB GLU A1018 6555 4985 11910 1660 2396 691 C ATOM 1822 CG GLU A1018 8.571 -58.360 13.140 1.00 66.26 C ANISOU 1822 CG GLU A1018 7298 5579 12299 1660 2222 401 C ATOM 1823 CD GLU A1018 8.184 -57.642 11.871 1.00103.46 C ANISOU 1823 CD GLU A1018 12192 10340 16778 1834 2200 262 C ATOM 1824 OE1 GLU A1018 9.084 -57.325 11.064 1.00128.40 O ANISOU 1824 OE1 GLU A1018 15363 13503 19921 1972 2373 414 O ATOM 1825 OE2 GLU A1018 6.979 -57.391 11.682 1.00 97.50 O ANISOU 1825 OE2 GLU A1018 11566 9626 15854 1860 2024 13 O ATOM 1826 N LYS A1019 12.820 -58.259 14.887 1.00 57.59 N ANISOU 1826 N LYS A1019 5539 4443 11899 1577 2565 1221 N ATOM 1827 CA LYS A1019 14.266 -58.422 14.824 1.00 63.26 C ANISOU 1827 CA LYS A1019 6078 5137 12820 1639 2720 1439 C ATOM 1828 C LYS A1019 14.909 -58.531 16.202 1.00 70.38 C ANISOU 1828 C LYS A1019 6767 6071 13903 1609 2588 1526 C ATOM 1829 O LYS A1019 16.124 -58.351 16.328 1.00 72.31 O ANISOU 1829 O LYS A1019 6799 6304 14373 1644 2647 1677 O ATOM 1830 CB LYS A1019 14.897 -57.285 14.022 1.00 81.44 C ANISOU 1830 CB LYS A1019 8282 7395 15266 1635 2876 1577 C ATOM 1831 CG LYS A1019 14.516 -55.901 14.466 1.00 60.15 C ANISOU 1831 CG LYS A1019 5482 4677 12697 1489 2737 1547 C ATOM 1832 CD LYS A1019 15.217 -54.862 13.604 1.00106.66 C ANISOU 1832 CD LYS A1019 11256 10463 18807 1491 2974 1743 C ATOM 1833 CE LYS A1019 15.046 -55.168 12.121 1.00 92.62 C ANISOU 1833 CE LYS A1019 9731 8702 16759 1689 3233 1787 C ATOM 1834 NZ LYS A1019 15.747 -54.177 11.256 1.00106.92 N ANISOU 1834 NZ LYS A1019 11445 10404 18774 1737 3550 2059 N ATOM 1835 N ALA A1020 14.127 -58.841 17.232 1.00 58.93 N ANISOU 1835 N ALA A1020 5369 4668 12355 1583 2411 1432 N ATOM 1836 CA ALA A1020 14.707 -59.168 18.524 1.00 95.34 C ANISOU 1836 CA ALA A1020 9835 9345 17043 1663 2288 1510 C ATOM 1837 C ALA A1020 15.423 -60.512 18.444 1.00 61.95 C ANISOU 1837 C ALA A1020 5631 5097 12811 1810 2445 1625 C ATOM 1838 O ALA A1020 15.105 -61.362 17.607 1.00 62.05 O ANISOU 1838 O ALA A1020 5809 5031 12737 1830 2608 1598 O ATOM 1839 CB ALA A1020 13.627 -59.203 19.605 1.00 60.06 C ANISOU 1839 CB ALA A1020 5449 4940 12431 1658 2112 1420 C ATOM 1840 N ASP A1021 16.410 -60.701 19.317 1.00 63.91 N ANISOU 1840 N ASP A1021 5706 5424 13151 1945 2367 1723 N ATOM 1841 CA ASP A1021 17.147 -61.955 19.335 1.00 66.08 C ANISOU 1841 CA ASP A1021 5999 5691 13417 2118 2502 1839 C ATOM 1842 C ASP A1021 17.068 -62.691 20.666 1.00 80.52 C ANISOU 1842 C ASP A1021 7851 7601 15143 2298 2404 1895 C ATOM 1843 O ASP A1021 17.651 -63.774 20.789 1.00103.37 O ANISOU 1843 O ASP A1021 10772 10480 18023 2468 2516 2003 O ATOM 1844 CB ASP A1021 18.617 -61.727 18.949 1.00112.52 C ANISOU 1844 CB ASP A1021 11655 11603 19494 2195 2560 1933 C ATOM 1845 CG ASP A1021 19.426 -61.084 20.058 1.00154.39 C ANISOU 1845 CG ASP A1021 16680 17053 24930 2293 2318 1916 C ATOM 1846 OD1 ASP A1021 18.938 -60.111 20.666 1.00 90.56 O ANISOU 1846 OD1 ASP A1021 8527 9019 16863 2214 2102 1804 O ATOM 1847 OD2 ASP A1021 20.556 -61.556 20.317 1.00138.47 O ANISOU 1847 OD2 ASP A1021 14501 15118 22994 2476 2317 1979 O ATOM 1848 N ASN A1022 16.363 -62.150 21.657 1.00 66.11 N ANISOU 1848 N ASN A1022 4858 9886 10375 1288 710 2223 N ATOM 1849 CA ASN A1022 16.118 -62.872 22.897 1.00 80.99 C ANISOU 1849 CA ASN A1022 6808 12068 11896 1485 704 1969 C ATOM 1850 C ASN A1022 14.734 -62.508 23.411 1.00 79.43 C ANISOU 1850 C ASN A1022 6684 11669 11828 1447 543 1550 C ATOM 1851 O ASN A1022 14.113 -61.542 22.959 1.00 60.46 O ANISOU 1851 O ASN A1022 4209 8930 9833 1223 351 1416 O ATOM 1852 CB ASN A1022 17.192 -62.580 23.952 1.00 73.96 C ANISOU 1852 CB ASN A1022 5506 11618 10976 1459 473 1865 C ATOM 1853 CG ASN A1022 17.317 -61.108 24.261 1.00 72.23 C ANISOU 1853 CG ASN A1022 4844 11351 11250 1109 40 1573 C ATOM 1854 OD1 ASN A1022 16.461 -60.529 24.927 1.00 82.64 O ANISOU 1854 OD1 ASN A1022 6106 12581 12711 1024 -215 1179 O ATOM 1855 ND2 ASN A1022 18.395 -60.493 23.787 1.00 85.98 N ANISOU 1855 ND2 ASN A1022 6289 13123 13257 893 -32 1766 N ATOM 1856 N ALA A1023 14.259 -63.302 24.375 1.00 72.98 N ANISOU 1856 N ALA A1023 6047 11023 10659 1672 640 1355 N ATOM 1857 CA ALA A1023 12.912 -63.119 24.904 1.00 57.22 C ANISOU 1857 CA ALA A1023 4161 8846 8734 1693 561 984 C ATOM 1858 C ALA A1023 12.775 -61.817 25.682 1.00 80.23 C ANISOU 1858 C ALA A1023 6786 11756 11943 1464 107 581 C ATOM 1859 O ALA A1023 11.680 -61.246 25.736 1.00 92.65 O ANISOU 1859 O ALA A1023 8519 12991 13693 1329 -36 260 O ATOM 1860 CB ALA A1023 12.533 -64.302 25.794 1.00 59.10 C ANISOU 1860 CB ALA A1023 4722 9224 8510 1962 812 889 C ATOM 1861 N ALA A1024 13.859 -61.340 26.295 1.00 64.89 N ANISOU 1861 N ALA A1024 4445 10168 10041 1407 -133 565 N ATOM 1862 CA ALA A1024 13.774 -60.111 27.077 1.00 67.66 C ANISOU 1862 CA ALA A1024 4579 10483 10647 1162 -586 123 C ATOM 1863 C ALA A1024 13.507 -58.907 26.185 1.00 92.22 C ANISOU 1863 C ALA A1024 7677 13097 14267 767 -772 60 C ATOM 1864 O ALA A1024 12.789 -57.982 26.582 1.00 65.13 O ANISOU 1864 O ALA A1024 4303 9400 11043 594 -1035 -337 O ATOM 1865 CB ALA A1024 15.056 -59.910 27.884 1.00102.65 C ANISOU 1865 CB ALA A1024 8558 15430 15014 1168 -827 103 C ATOM 1866 N GLN A1025 14.077 -58.900 24.976 1.00 62.55 N ANISOU 1866 N GLN A1025 3871 9200 10697 659 -609 467 N ATOM 1867 CA GLN A1025 13.815 -57.811 24.041 1.00 53.92 C ANISOU 1867 CA GLN A1025 2812 7615 10060 347 -716 469 C ATOM 1868 C GLN A1025 12.365 -57.823 23.577 1.00 50.55 C ANISOU 1868 C GLN A1025 2807 6777 9621 401 -638 321 C ATOM 1869 O GLN A1025 11.735 -56.766 23.466 1.00 60.80 O ANISOU 1869 O GLN A1025 4164 7711 11228 198 -842 73 O ATOM 1870 CB GLN A1025 14.762 -57.902 22.846 1.00 57.27 C ANISOU 1870 CB GLN A1025 3118 8004 10637 297 -497 988 C ATOM 1871 CG GLN A1025 16.218 -57.648 23.213 1.00 81.67 C ANISOU 1871 CG GLN A1025 5776 11454 13799 168 -599 1108 C ATOM 1872 CD GLN A1025 17.171 -57.879 22.057 1.00 73.45 C ANISOU 1872 CD GLN A1025 4709 10392 12807 179 -306 1641 C ATOM 1873 OE1 GLN A1025 16.786 -58.408 21.014 1.00 61.81 O ANISOU 1873 OE1 GLN A1025 3529 8700 11255 349 -8 1967 O ATOM 1874 NE2 GLN A1025 18.426 -57.480 22.237 1.00110.22 N ANISOU 1874 NE2 GLN A1025 9015 15276 17587 11 -391 1723 N ATOM 1875 N VAL A1026 11.823 -59.010 23.293 1.00 56.85 N ANISOU 1875 N VAL A1026 3896 7625 10079 672 -338 469 N ATOM 1876 CA VAL A1026 10.406 -59.115 22.949 1.00 44.84 C ANISOU 1876 CA VAL A1026 2721 5775 8543 719 -287 289 C ATOM 1877 C VAL A1026 9.548 -58.598 24.093 1.00 47.94 C ANISOU 1877 C VAL A1026 3112 6134 8968 695 -516 -191 C ATOM 1878 O VAL A1026 8.587 -57.847 23.879 1.00 44.56 O ANISOU 1878 O VAL A1026 2806 5365 8758 589 -656 -413 O ATOM 1879 CB VAL A1026 10.053 -60.569 22.582 1.00 49.86 C ANISOU 1879 CB VAL A1026 3639 6494 8813 986 79 491 C ATOM 1880 CG1 VAL A1026 8.574 -60.707 22.294 1.00 42.17 C ANISOU 1880 CG1 VAL A1026 2955 5215 7853 1003 102 265 C ATOM 1881 CG2 VAL A1026 10.884 -61.032 21.382 1.00 47.75 C ANISOU 1881 CG2 VAL A1026 3428 6222 8491 1041 315 971 C ATOM 1882 N LYS A1027 9.893 -58.971 25.330 1.00 49.75 N ANISOU 1882 N LYS A1027 3213 6728 8960 834 -550 -346 N ATOM 1883 CA LYS A1027 9.110 -58.536 26.483 1.00 94.01 C ANISOU 1883 CA LYS A1027 8853 12325 14541 875 -736 -790 C ATOM 1884 C LYS A1027 9.112 -57.019 26.612 1.00 59.10 C ANISOU 1884 C LYS A1027 4304 7651 10500 587 -1107 -1068 C ATOM 1885 O LYS A1027 8.061 -56.401 26.824 1.00 51.09 O ANISOU 1885 O LYS A1027 3442 6354 9614 558 -1216 -1360 O ATOM 1886 CB LYS A1027 9.649 -59.178 27.761 1.00 65.33 C ANISOU 1886 CB LYS A1027 5109 9169 10544 1124 -711 -872 C ATOM 1887 CG LYS A1027 9.029 -58.608 29.026 1.00 63.03 C ANISOU 1887 CG LYS A1027 4846 8900 10204 1192 -934 -1333 C ATOM 1888 CD LYS A1027 9.560 -59.295 30.267 1.00 66.90 C ANISOU 1888 CD LYS A1027 5259 9890 10269 1512 -893 -1393 C ATOM 1889 CE LYS A1027 8.781 -58.865 31.499 1.00 76.13 C ANISOU 1889 CE LYS A1027 6545 11058 11324 1665 -1044 -1832 C ATOM 1890 NZ LYS A1027 9.225 -59.608 32.710 1.00 93.30 N ANISOU 1890 NZ LYS A1027 8697 13733 13020 2062 -965 -1871 N ATOM 1891 N ASP A1028 10.293 -56.404 26.487 1.00 64.87 N ANISOU 1891 N ASP A1028 4749 8468 11431 370 -1283 -976 N ATOM 1892 CA ASP A1028 10.414 -54.954 26.607 1.00 55.65 C ANISOU 1892 CA ASP A1028 3458 7022 10663 57 -1610 -1241 C ATOM 1893 C ASP A1028 9.479 -54.236 25.646 1.00 53.44 C ANISOU 1893 C ASP A1028 3411 6210 10683 -59 -1579 -1231 C ATOM 1894 O ASP A1028 8.752 -53.315 26.038 1.00 73.89 O ANISOU 1894 O ASP A1028 6109 8520 13445 -137 -1764 -1571 O ATOM 1895 CB ASP A1028 11.862 -54.524 26.346 1.00 80.01 C ANISOU 1895 CB ASP A1028 6173 10241 13987 -196 -1725 -1053 C ATOM 1896 CG ASP A1028 12.702 -54.481 27.608 1.00111.93 C ANISOU 1896 CG ASP A1028 9951 14726 17850 -201 -1972 -1296 C ATOM 1897 OD1 ASP A1028 12.640 -53.462 28.328 1.00120.56 O ANISOU 1897 OD1 ASP A1028 11063 15684 19059 -387 -2259 -1686 O ATOM 1898 OD2 ASP A1028 13.438 -55.456 27.872 1.00112.68 O ANISOU 1898 OD2 ASP A1028 9866 15303 17644 6 -1861 -1081 O ATOM 1899 N ALA A1029 9.492 -54.638 24.373 1.00 51.50 N ANISOU 1899 N ALA A1029 3263 5829 10477 -34 -1342 -837 N ATOM 1900 CA ALA A1029 8.668 -53.950 23.383 1.00 53.02 C ANISOU 1900 CA ALA A1029 3668 5556 10920 -97 -1323 -797 C ATOM 1901 C ALA A1029 7.184 -54.199 23.621 1.00 48.28 C ANISOU 1901 C ALA A1029 3327 4847 10172 94 -1300 -1039 C ATOM 1902 O ALA A1029 6.358 -53.300 23.406 1.00 52.83 O ANISOU 1902 O ALA A1029 4030 5077 10965 49 -1408 -1206 O ATOM 1903 CB ALA A1029 9.068 -54.375 21.972 1.00 51.81 C ANISOU 1903 CB ALA A1029 3580 5323 10782 -61 -1082 -319 C ATOM 1904 N LEU A1030 6.820 -55.404 24.069 1.00 46.08 N ANISOU 1904 N LEU A1030 3120 4849 9540 318 -1134 -1046 N ATOM 1905 CA LEU A1030 5.406 -55.706 24.288 1.00 44.80 C ANISOU 1905 CA LEU A1030 3155 4588 9280 481 -1076 -1256 C ATOM 1906 C LEU A1030 4.843 -54.909 25.458 1.00 45.77 C ANISOU 1906 C LEU A1030 3268 4651 9471 487 -1279 -1674 C ATOM 1907 O LEU A1030 3.689 -54.470 25.416 1.00 45.38 O ANISOU 1907 O LEU A1030 3348 4364 9529 541 -1316 -1852 O ATOM 1908 CB LEU A1030 5.208 -57.203 24.520 1.00 49.27 C ANISOU 1908 CB LEU A1030 3800 5430 9491 698 -798 -1155 C ATOM 1909 CG LEU A1030 5.333 -58.132 23.314 1.00 45.79 C ANISOU 1909 CG LEU A1030 3484 4978 8938 746 -558 -803 C ATOM 1910 CD1 LEU A1030 5.553 -59.569 23.774 1.00 54.01 C ANISOU 1910 CD1 LEU A1030 4580 6318 9624 941 -262 -691 C ATOM 1911 CD2 LEU A1030 4.089 -58.028 22.447 1.00 39.04 C ANISOU 1911 CD2 LEU A1030 2805 3833 8195 754 -564 -860 C ATOM 1912 N ATHR A1031 5.638 -54.713 26.514 0.52 51.19 N ANISOU 1912 N ATHR A1031 3805 5566 10079 458 -1418 -1838 N ATOM 1913 N BTHR A1031 5.644 -54.723 26.510 0.48 51.20 N ANISOU 1913 N BTHR A1031 3806 5570 10079 459 -1416 -1835 N ATOM 1914 CA ATHR A1031 5.163 -53.918 27.642 0.52 57.38 C ANISOU 1914 CA ATHR A1031 4623 6283 10894 485 -1624 -2257 C ATOM 1915 CA BTHR A1031 5.207 -53.924 27.648 0.48 57.24 C ANISOU 1915 CA BTHR A1031 4599 6274 10875 482 -1626 -2253 C ATOM 1916 C ATHR A1031 4.902 -52.476 27.225 0.52 59.36 C ANISOU 1916 C ATHR A1031 4926 6094 11534 274 -1828 -2396 C ATOM 1917 C BTHR A1031 4.916 -52.488 27.230 0.48 57.39 C ANISOU 1917 C BTHR A1031 4673 5850 11281 274 -1827 -2394 C ATOM 1918 O ATHR A1031 3.918 -51.865 27.659 0.52 65.69 O ANISOU 1918 O ATHR A1031 5878 6683 12399 358 -1896 -2667 O ATOM 1919 O BTHR A1031 3.919 -51.896 27.662 0.48 63.70 O ANISOU 1919 O BTHR A1031 5624 6439 12139 363 -1892 -2663 O ATOM 1920 CB ATHR A1031 6.165 -53.966 28.796 0.52 66.22 C ANISOU 1920 CB ATHR A1031 5573 7761 11827 500 -1781 -2424 C ATOM 1921 CB BTHR A1031 6.271 -53.964 28.745 0.48 66.02 C ANISOU 1921 CB BTHR A1031 5529 7744 11811 482 -1786 -2403 C ATOM 1922 OG1ATHR A1031 7.418 -53.415 28.373 0.52 59.59 O ANISOU 1922 OG1ATHR A1031 4502 6929 11212 213 -1945 -2300 O ATOM 1923 OG1BTHR A1031 6.530 -55.327 29.106 0.48 56.54 O ANISOU 1923 OG1BTHR A1031 4307 6954 10223 735 -1550 -2228 O ATOM 1924 CG2ATHR A1031 6.366 -55.400 29.270 0.52 55.67 C ANISOU 1924 CG2ATHR A1031 4224 6858 10069 783 -1533 -2268 C ATOM 1925 CG2BTHR A1031 5.810 -53.194 29.973 0.48 55.11 C ANISOU 1925 CG2BTHR A1031 4231 6312 10395 551 -2008 -2866 C ATOM 1926 N LYS A1032 5.770 -51.915 26.378 1.00 62.56 N ANISOU 1926 N LYS A1032 5219 6343 12209 22 -1887 -2188 N ATOM 1927 CA LYS A1032 5.525 -50.570 25.867 1.00 56.70 C ANISOU 1927 CA LYS A1032 4560 5130 11852 -160 -2008 -2263 C ATOM 1928 C LYS A1032 4.329 -50.541 24.927 1.00 71.09 C ANISOU 1928 C LYS A1032 6596 6688 13727 -8 -1869 -2133 C ATOM 1929 O LYS A1032 3.609 -49.536 24.873 1.00 54.38 O ANISOU 1929 O LYS A1032 4624 4223 11816 -5 -1948 -2298 O ATOM 1930 CB LYS A1032 6.766 -50.036 25.151 1.00 58.61 C ANISOU 1930 CB LYS A1032 4621 5255 12394 -456 -2040 -2024 C ATOM 1931 CG LYS A1032 7.942 -49.718 26.065 1.00 61.05 C ANISOU 1931 CG LYS A1032 4719 5784 12693 -647 -2217 -2186 C ATOM 1932 CD LYS A1032 9.153 -49.290 25.252 1.00 63.46 C ANISOU 1932 CD LYS A1032 4844 6001 13268 -916 -2161 -1866 C ATOM 1933 CE LYS A1032 10.265 -48.771 26.142 1.00 68.02 C ANISOU 1933 CE LYS A1032 5231 6766 13846 -1136 -2348 -2055 C ATOM 1934 NZ LYS A1032 11.461 -48.369 25.350 1.00105.92 N ANISOU 1934 NZ LYS A1032 9813 11490 18941 -1411 -2266 -1734 N ATOM 1935 N MET A1033 4.097 -51.623 24.179 1.00 49.97 N ANISOU 1935 N MET A1033 3949 4176 10860 133 -1668 -1850 N ATOM 1936 CA MET A1033 2.909 -51.673 23.334 1.00 48.30 C ANISOU 1936 CA MET A1033 3909 3777 10666 290 -1583 -1775 C ATOM 1937 C MET A1033 1.643 -51.758 24.173 1.00 59.02 C ANISOU 1937 C MET A1033 5343 5159 11922 478 -1599 -2086 C ATOM 1938 O MET A1033 0.621 -51.157 23.823 1.00 52.85 O ANISOU 1938 O MET A1033 4669 4140 11272 574 -1634 -2159 O ATOM 1939 CB MET A1033 2.978 -52.859 22.372 1.00 45.73 C ANISOU 1939 CB MET A1033 3610 3622 10143 380 -1387 -1449 C ATOM 1940 CG MET A1033 3.966 -52.696 21.242 1.00 66.42 C ANISOU 1940 CG MET A1033 6216 6148 12874 271 -1323 -1078 C ATOM 1941 SD MET A1033 4.029 -54.172 20.208 1.00 54.37 S ANISOU 1941 SD MET A1033 4788 4826 11044 422 -1084 -735 S ATOM 1942 CE MET A1033 2.382 -54.154 19.537 1.00 47.70 C ANISOU 1942 CE MET A1033 4131 3809 10185 599 -1127 -858 C ATOM 1943 N ARG A1034 1.688 -52.509 25.275 1.00 47.11 N ANISOU 1943 N ARG A1034 3777 3948 10174 569 -1548 -2244 N ATOM 1944 CA ARG A1034 0.478 -52.725 26.061 1.00 47.14 C ANISOU 1944 CA ARG A1034 3847 3989 10075 781 -1492 -2489 C ATOM 1945 C ARG A1034 0.030 -51.439 26.741 1.00 63.02 C ANISOU 1945 C ARG A1034 5940 5783 12220 788 -1661 -2768 C ATOM 1946 O ARG A1034 -1.158 -51.101 26.721 1.00 55.69 O ANISOU 1946 O ARG A1034 5097 4856 11207 870 -1608 -2749 O ATOM 1947 CB ARG A1034 0.707 -53.827 27.094 1.00 60.78 C ANISOU 1947 CB ARG A1034 5526 6079 11490 916 -1344 -2549 C ATOM 1948 CG ARG A1034 -0.584 -54.343 27.714 1.00 50.90 C ANISOU 1948 CG ARG A1034 4378 4938 10023 1070 -1166 -2627 C ATOM 1949 CD ARG A1034 -0.318 -55.305 28.857 1.00 54.39 C ANISOU 1949 CD ARG A1034 4833 5697 10135 1231 -986 -2666 C ATOM 1950 NE ARG A1034 -1.545 -55.972 29.280 1.00 63.41 N ANISOU 1950 NE ARG A1034 6113 6943 11038 1301 -736 -2585 N ATOM 1951 CZ ARG A1034 -2.431 -55.443 30.116 1.00 58.49 C ANISOU 1951 CZ ARG A1034 5571 6294 10359 1398 -735 -2722 C ATOM 1952 NH1 ARG A1034 -2.228 -54.233 30.622 1.00 83.65 N ANISOU 1952 NH1 ARG A1034 8760 9352 13671 1435 -981 -2974 N ATOM 1953 NH2 ARG A1034 -3.520 -56.123 30.443 1.00 78.13 N ANISOU 1953 NH2 ARG A1034 8142 8859 12684 1464 -479 -2600 N ATOM 1954 N ALA A1035 0.971 -50.711 27.347 1.00 56.52 N ANISOU 1954 N ALA A1035 5095 4889 11491 647 -1845 -2946 N ATOM 1955 CA ALA A1035 0.657 -49.419 27.943 1.00 54.84 C ANISOU 1955 CA ALA A1035 5001 4507 11330 635 -1971 -3138 C ATOM 1956 C ALA A1035 0.174 -48.420 26.898 1.00 61.61 C ANISOU 1956 C ALA A1035 5956 5084 12368 575 -1948 -2932 C ATOM 1957 O ALA A1035 -0.683 -47.578 27.192 1.00 65.72 O ANISOU 1957 O ALA A1035 6620 5492 12860 670 -1946 -3015 O ATOM 1958 CB ALA A1035 1.884 -48.877 28.679 1.00 57.90 C ANISOU 1958 CB ALA A1035 5330 4904 11765 444 -2178 -3345 C ATOM 1959 N ALA A1036 0.704 -48.497 25.676 1.00 67.60 N ANISOU 1959 N ALA A1036 6663 5724 13297 445 -1916 -2657 N ATOM 1960 CA ALA A1036 0.253 -47.597 24.621 1.00 55.84 C ANISOU 1960 CA ALA A1036 5290 3979 11947 441 -1875 -2455 C ATOM 1961 C ALA A1036 -1.140 -47.971 24.135 1.00 87.23 C ANISOU 1961 C ALA A1036 9321 8062 15760 652 -1779 -2364 C ATOM 1962 O ALA A1036 -1.950 -47.091 23.821 1.00 84.78 O ANISOU 1962 O ALA A1036 9139 7601 15473 740 -1767 -2338 O ATOM 1963 CB ALA A1036 1.239 -47.612 23.457 1.00 55.79 C ANISOU 1963 CB ALA A1036 5230 3824 12145 276 -1842 -2163 C ATOM 1964 N ALA A1037 -1.432 -49.272 24.059 1.00 57.31 N ANISOU 1964 N ALA A1037 5440 4535 11800 723 -1700 -2315 N ATOM 1965 CA ALA A1037 -2.748 -49.713 23.606 1.00 51.87 C ANISOU 1965 CA ALA A1037 4773 3982 10952 858 -1620 -2245 C ATOM 1966 C ALA A1037 -3.841 -49.218 24.545 1.00 66.69 C ANISOU 1966 C ALA A1037 6702 5896 12743 984 -1609 -2434 C ATOM 1967 O ALA A1037 -4.879 -48.718 24.099 1.00 66.08 O ANISOU 1967 O ALA A1037 6681 5761 12664 1092 -1601 -2389 O ATOM 1968 CB ALA A1037 -2.782 -51.239 23.491 1.00 47.03 C ANISOU 1968 CB ALA A1037 4077 3629 10163 858 -1504 -2180 C ATOM 1969 N LEU A1038 -3.625 -49.354 25.856 1.00 56.16 N ANISOU 1969 N LEU A1038 5359 4658 11323 1006 -1603 -2642 N ATOM 1970 CA LEU A1038 -4.581 -48.820 26.819 1.00 53.39 C ANISOU 1970 CA LEU A1038 5098 4313 10876 1152 -1571 -2803 C ATOM 1971 C LEU A1038 -4.652 -47.301 26.746 1.00 74.79 C ANISOU 1971 C LEU A1038 7965 6721 13731 1169 -1658 -2854 C ATOM 1972 O LEU A1038 -5.714 -46.715 26.986 1.00 74.36 O ANISOU 1972 O LEU A1038 8011 6609 13632 1324 -1606 -2889 O ATOM 1973 CB LEU A1038 -4.205 -49.262 28.232 1.00 67.21 C ANISOU 1973 CB LEU A1038 6853 6220 12463 1207 -1546 -3010 C ATOM 1974 CG LEU A1038 -4.036 -50.762 28.462 1.00 71.34 C ANISOU 1974 CG LEU A1038 7274 7025 12807 1215 -1401 -2953 C ATOM 1975 CD1 LEU A1038 -3.786 -51.045 29.935 1.00 82.67 C ANISOU 1975 CD1 LEU A1038 8763 8615 14031 1348 -1356 -3152 C ATOM 1976 CD2 LEU A1038 -5.258 -51.514 27.965 1.00 81.35 C ANISOU 1976 CD2 LEU A1038 8507 8416 13988 1252 -1224 -2788 C ATOM 1977 N ASP A1039 -3.535 -46.654 26.412 1.00 80.14 N ANISOU 1977 N ASP A1039 8676 7186 14589 1007 -1761 -2844 N ATOM 1978 CA ASP A1039 -3.520 -45.201 26.289 1.00 62.14 C ANISOU 1978 CA ASP A1039 6583 4572 12454 985 -1798 -2874 C ATOM 1979 C ASP A1039 -4.344 -44.741 25.092 1.00 71.39 C ANISOU 1979 C ASP A1039 7828 5612 13686 1095 -1726 -2651 C ATOM 1980 O ASP A1039 -4.994 -43.691 25.146 1.00 99.86 O ANISOU 1980 O ASP A1039 11618 9007 17318 1217 -1685 -2680 O ATOM 1981 CB ASP A1039 -2.077 -44.712 26.177 1.00 62.82 C ANISOU 1981 CB ASP A1039 6664 4466 12739 732 -1893 -2892 C ATOM 1982 CG ASP A1039 -1.934 -43.244 26.495 1.00 88.43 C ANISOU 1982 CG ASP A1039 10128 7364 16108 663 -1918 -3018 C ATOM 1983 OD1 ASP A1039 -1.997 -42.891 27.691 1.00116.63 O ANISOU 1983 OD1 ASP A1039 13801 10935 19577 692 -1980 -3293 O ATOM 1984 OD2 ASP A1039 -1.746 -42.447 25.552 1.00122.79 O ANISOU 1984 OD2 ASP A1039 14577 11429 20649 588 -1859 -2843 O ATOM 1985 N ALA A1040 -4.328 -45.512 24.002 1.00 64.16 N ANISOU 1985 N ALA A1040 6795 4814 12769 1083 -1706 -2434 N ATOM 1986 CA ALA A1040 -5.168 -45.205 22.851 1.00 83.82 C ANISOU 1986 CA ALA A1040 9349 7237 15260 1235 -1663 -2238 C ATOM 1987 C ALA A1040 -6.616 -45.620 23.060 1.00 82.00 C ANISOU 1987 C ALA A1040 9060 7223 14874 1436 -1626 -2288 C ATOM 1988 O ALA A1040 -7.494 -45.156 22.324 1.00 87.13 O ANISOU 1988 O ALA A1040 9767 7819 15518 1619 -1607 -2181 O ATOM 1989 CB ALA A1040 -4.619 -45.882 21.593 1.00 66.62 C ANISOU 1989 CB ALA A1040 7104 5109 13100 1170 -1666 -1998 C ATOM 1990 N GLN A1041 -6.883 -46.482 24.042 1.00114.26 N ANISOU 1990 N GLN A1041 13028 11551 18836 1421 -1597 -2435 N ATOM 1991 CA GLN A1041 -8.253 -46.872 24.345 1.00 90.62 C ANISOU 1991 CA GLN A1041 9960 8741 15732 1586 -1524 -2475 C ATOM 1992 C GLN A1041 -8.977 -45.803 25.154 1.00 91.15 C ANISOU 1992 C GLN A1041 10175 8666 15791 1771 -1469 -2583 C ATOM 1993 O GLN A1041 -10.203 -45.683 25.058 1.00119.33 O ANISOU 1993 O GLN A1041 13711 12299 19330 1967 -1407 -2551 O ATOM 1994 CB GLN A1041 -8.262 -48.206 25.094 1.00 71.15 C ANISOU 1994 CB GLN A1041 7350 6551 13134 1510 -1446 -2551 C ATOM 1995 CG GLN A1041 -9.632 -48.851 25.214 1.00 90.26 C ANISOU 1995 CG GLN A1041 9650 9161 15484 1624 -1340 -2551 C ATOM 1996 CD GLN A1041 -9.571 -50.239 25.822 1.00 78.30 C ANISOU 1996 CD GLN A1041 8027 7874 13850 1531 -1209 -2581 C ATOM 1997 OE1 GLN A1041 -8.607 -50.591 26.500 1.00 97.80 O ANISOU 1997 OE1 GLN A1041 10540 10381 16238 1450 -1179 -2630 O ATOM 1998 NE2 GLN A1041 -10.603 -51.039 25.576 1.00108.33 N ANISOU 1998 NE2 GLN A1041 11687 11821 17651 1554 -1120 -2552 N ATOM 1999 N LYS A1042 -8.243 -45.022 25.942 1.00 76.32 N ANISOU 1999 N LYS A1042 8463 6593 13944 1722 -1491 -2716 N ATOM 2000 CA LYS A1042 -8.837 -43.950 26.732 1.00 73.17 C ANISOU 2000 CA LYS A1042 8272 6011 13519 1902 -1425 -2832 C ATOM 2001 C LYS A1042 -9.421 -42.862 25.833 1.00 73.25 C ANISOU 2001 C LYS A1042 8427 5778 13626 2065 -1391 -2695 C ATOM 2002 O LYS A1042 -10.589 -42.492 25.967 1.00 96.29 O ANISOU 2002 O LYS A1042 11388 8705 16491 2322 -1291 -2669 O ATOM 2003 CB LYS A1042 -7.800 -43.343 27.681 1.00 86.87 C ANISOU 2003 CB LYS A1042 10177 7561 15267 1778 -1488 -3038 C ATOM 2004 CG LYS A1042 -7.302 -44.291 28.763 1.00100.73 C ANISOU 2004 CG LYS A1042 11832 9562 16877 1711 -1512 -3197 C ATOM 2005 CD LYS A1042 -6.329 -43.584 29.697 1.00117.75 C ANISOU 2005 CD LYS A1042 14162 11541 19038 1613 -1620 -3443 C ATOM 2006 CE LYS A1042 -5.885 -44.487 30.838 1.00111.61 C ANISOU 2006 CE LYS A1042 13310 11027 18069 1625 -1649 -3617 C ATOM 2007 NZ LYS A1042 -4.993 -43.773 31.797 1.00 95.65 N ANISOU 2007 NZ LYS A1042 11458 8859 16024 1550 -1798 -3905 N ATOM 2008 N MET A1058 -18.589 -47.928 18.985 1.00 83.29 N ANISOU 2008 N MET A1058 7301 9099 15246 3925 -755 1723 N ATOM 2009 CA MET A1058 -17.825 -48.112 20.216 1.00 98.90 C ANISOU 2009 CA MET A1058 9374 11011 17193 3779 -385 1508 C ATOM 2010 C MET A1058 -17.672 -49.588 20.570 1.00106.12 C ANISOU 2010 C MET A1058 9907 12276 18137 3238 -254 1641 C ATOM 2011 O MET A1058 -16.701 -49.977 21.218 1.00 77.91 O ANISOU 2011 O MET A1058 6542 8550 14509 2962 -37 1556 O ATOM 2012 CB MET A1058 -18.485 -47.364 21.377 1.00106.00 C ANISOU 2012 CB MET A1058 10057 12134 18083 4332 -132 1196 C ATOM 2013 CG MET A1058 -18.253 -45.861 21.361 1.00124.85 C ANISOU 2013 CG MET A1058 13016 14008 20415 4838 -194 984 C ATOM 2014 SD MET A1058 -16.515 -45.426 21.575 1.00150.50 S ANISOU 2014 SD MET A1058 17089 16559 23534 4483 -71 847 S ATOM 2015 CE MET A1058 -16.170 -46.185 23.161 1.00101.62 C ANISOU 2015 CE MET A1058 10567 10746 17297 4287 383 599 C ATOM 2016 N LYS A1059 -18.635 -50.408 20.146 1.00106.16 N ANISOU 2016 N LYS A1059 9373 12756 18206 3082 -398 1843 N ATOM 2017 CA LYS A1059 -18.547 -51.840 20.418 1.00114.52 C ANISOU 2017 CA LYS A1059 10126 14111 19274 2524 -315 1998 C ATOM 2018 C LYS A1059 -17.498 -52.502 19.534 1.00 70.03 C ANISOU 2018 C LYS A1059 4891 8086 13633 2049 -545 2160 C ATOM 2019 O LYS A1059 -16.718 -53.338 20.004 1.00 80.24 O ANISOU 2019 O LYS A1059 6273 9315 14900 1684 -415 2177 O ATOM 2020 CB LYS A1059 -19.916 -52.491 20.228 1.00 79.28 C ANISOU 2020 CB LYS A1059 5004 10280 14839 2431 -410 2131 C ATOM 2021 CG LYS A1059 -20.997 -51.878 21.107 1.00115.43 C ANISOU 2021 CG LYS A1059 9119 15351 19388 2908 -188 1923 C ATOM 2022 CD LYS A1059 -22.384 -52.349 20.708 1.00115.70 C ANISOU 2022 CD LYS A1059 8508 16017 19435 2850 -345 2013 C ATOM 2023 CE LYS A1059 -23.454 -51.572 21.452 1.00 97.86 C ANISOU 2023 CE LYS A1059 5786 14242 17156 3418 -179 1737 C ATOM 2024 NZ LYS A1059 -24.818 -51.983 21.037 1.00129.91 N ANISOU 2024 NZ LYS A1059 9175 18946 21239 3365 -344 1775 N ATOM 2025 N ASP A1060 -17.467 -52.144 18.249 1.00 81.17 N ANISOU 2025 N ASP A1060 6547 9266 15027 2066 -893 2268 N ATOM 2026 CA ASP A1060 -16.402 -52.617 17.372 1.00 75.71 C ANISOU 2026 CA ASP A1060 6285 8225 14257 1660 -1107 2357 C ATOM 2027 C ASP A1060 -15.083 -51.925 17.689 1.00 74.27 C ANISOU 2027 C ASP A1060 6702 7570 13949 1695 -950 2168 C ATOM 2028 O ASP A1060 -14.010 -52.498 17.467 1.00 75.37 O ANISOU 2028 O ASP A1060 7147 7516 13975 1328 -985 2153 O ATOM 2029 CB ASP A1060 -16.802 -52.392 15.915 1.00 84.33 C ANISOU 2029 CB ASP A1060 7452 9294 15294 1660 -1497 2511 C ATOM 2030 CG ASP A1060 -18.289 -52.605 15.685 1.00124.31 C ANISOU 2030 CG ASP A1060 11927 14862 20442 1801 -1627 2618 C ATOM 2031 OD1 ASP A1060 -18.951 -51.692 15.145 1.00118.01 O ANISOU 2031 OD1 ASP A1060 11114 14099 19624 2215 -1781 2637 O ATOM 2032 OD2 ASP A1060 -18.797 -53.685 16.056 1.00103.79 O ANISOU 2032 OD2 ASP A1060 8897 12642 17897 1488 -1576 2675 O ATOM 2033 N PHE A1061 -15.149 -50.694 18.202 1.00 77.29 N ANISOU 2033 N PHE A1061 7270 7785 14310 2123 -787 1990 N ATOM 2034 CA PHE A1061 -13.968 -50.049 18.765 1.00 80.17 C ANISOU 2034 CA PHE A1061 8153 7773 14535 2115 -581 1757 C ATOM 2035 C PHE A1061 -13.434 -50.846 19.945 1.00 58.31 C ANISOU 2035 C PHE A1061 5243 5137 11774 1929 -278 1639 C ATOM 2036 O PHE A1061 -12.244 -51.179 19.998 1.00 54.13 O ANISOU 2036 O PHE A1061 5055 4417 11095 1619 -233 1554 O ATOM 2037 CB PHE A1061 -14.313 -48.614 19.186 1.00 99.03 C ANISOU 2037 CB PHE A1061 10738 9971 16919 2632 -482 1572 C ATOM 2038 CG PHE A1061 -13.373 -48.022 20.213 1.00108.48 C ANISOU 2038 CG PHE A1061 12303 10908 18006 2663 -193 1266 C ATOM 2039 CD1 PHE A1061 -12.243 -47.327 19.820 1.00 84.35 C ANISOU 2039 CD1 PHE A1061 9875 7424 14751 2475 -242 1173 C ATOM 2040 CD2 PHE A1061 -13.638 -48.137 21.570 1.00114.14 C ANISOU 2040 CD2 PHE A1061 12725 11869 18775 2858 135 1061 C ATOM 2041 CE1 PHE A1061 -11.389 -46.775 20.759 1.00 96.35 C ANISOU 2041 CE1 PHE A1061 11716 8739 16154 2464 0 872 C ATOM 2042 CE2 PHE A1061 -12.783 -47.593 22.510 1.00105.17 C ANISOU 2042 CE2 PHE A1061 11922 10527 17510 2879 387 750 C ATOM 2043 CZ PHE A1061 -11.659 -46.911 22.104 1.00 75.17 C ANISOU 2043 CZ PHE A1061 8743 6274 13543 2677 305 649 C ATOM 2044 N ARG A1062 -14.309 -51.159 20.906 1.00 60.78 N ANISOU 2044 N ARG A1062 5045 5842 12206 2116 -58 1623 N ATOM 2045 CA ARG A1062 -13.883 -51.889 22.095 1.00 58.63 C ANISOU 2045 CA ARG A1062 4620 5757 11899 1965 263 1535 C ATOM 2046 C ARG A1062 -13.406 -53.290 21.741 1.00 54.75 C ANISOU 2046 C ARG A1062 4168 5362 11271 1404 132 1694 C ATOM 2047 O ARG A1062 -12.419 -53.773 22.306 1.00 59.30 O ANISOU 2047 O ARG A1062 5019 5884 11630 1161 275 1571 O ATOM 2048 CB ARG A1062 -15.021 -51.941 23.116 1.00 95.48 C ANISOU 2048 CB ARG A1062 8735 10950 16593 2202 530 1491 C ATOM 2049 CG ARG A1062 -14.775 -52.889 24.282 1.00126.92 C ANISOU 2049 CG ARG A1062 12544 15269 20409 1925 842 1467 C ATOM 2050 CD ARG A1062 -15.583 -52.493 25.512 1.00110.24 C ANISOU 2050 CD ARG A1062 10043 13613 18230 2253 1198 1298 C ATOM 2051 NE ARG A1062 -15.106 -51.240 26.092 1.00148.39 N ANISOU 2051 NE ARG A1062 15237 18182 22963 2657 1361 924 N ATOM 2052 CZ ARG A1062 -14.053 -51.143 26.898 1.00135.95 C ANISOU 2052 CZ ARG A1062 13990 16455 21210 2592 1592 702 C ATOM 2053 NH1 ARG A1062 -13.360 -52.225 27.222 1.00 73.47 N ANISOU 2053 NH1 ARG A1062 6152 8649 13113 2148 1655 814 N ATOM 2054 NH2 ARG A1062 -13.688 -49.962 27.379 1.00107.76 N ANISOU 2054 NH2 ARG A1062 10762 12646 17537 2917 1697 338 N ATOM 2055 N HIS A1063 -14.082 -53.952 20.796 1.00 55.56 N ANISOU 2055 N HIS A1063 4016 5605 11489 1212 -163 1947 N ATOM 2056 CA HIS A1063 -13.656 -55.288 20.391 1.00 65.73 C ANISOU 2056 CA HIS A1063 5395 6919 12662 698 -323 2065 C ATOM 2057 C HIS A1063 -12.252 -55.261 19.801 1.00 52.70 C ANISOU 2057 C HIS A1063 4326 4878 10820 526 -450 1942 C ATOM 2058 O HIS A1063 -11.419 -56.111 20.134 1.00 45.44 O ANISOU 2058 O HIS A1063 3618 3934 9713 247 -396 1871 O ATOM 2059 CB HIS A1063 -14.645 -55.886 19.389 1.00 62.82 C ANISOU 2059 CB HIS A1063 4670 6749 12448 522 -650 2312 C ATOM 2060 CG HIS A1063 -14.431 -57.347 19.127 1.00 81.23 C ANISOU 2060 CG HIS A1063 7048 9121 14694 -5 -799 2413 C ATOM 2061 ND1 HIS A1063 -14.386 -58.286 20.137 1.00 65.48 N ANISOU 2061 ND1 HIS A1063 4984 7283 12614 -265 -580 2437 N ATOM 2062 CD2 HIS A1063 -14.253 -58.030 17.971 1.00 69.59 C ANISOU 2062 CD2 HIS A1063 5720 7525 13197 -308 -1156 2489 C ATOM 2063 CE1 HIS A1063 -14.192 -59.484 19.614 1.00 51.87 C ANISOU 2063 CE1 HIS A1063 3394 5468 10845 -696 -809 2527 C ATOM 2064 NE2 HIS A1063 -14.107 -59.357 18.302 1.00 59.35 N ANISOU 2064 NE2 HIS A1063 4462 6260 11829 -724 -1156 2532 N ATOM 2065 N GLY A1064 -11.973 -54.287 18.930 1.00 48.30 N ANISOU 2065 N GLY A1064 4028 4036 10289 695 -620 1924 N ATOM 2066 CA GLY A1064 -10.650 -54.194 18.331 1.00 44.85 C ANISOU 2066 CA GLY A1064 4096 3312 9634 494 -718 1807 C ATOM 2067 C GLY A1064 -9.548 -54.057 19.365 1.00 42.42 C ANISOU 2067 C GLY A1064 4060 2931 9128 468 -422 1542 C ATOM 2068 O GLY A1064 -8.520 -54.732 19.287 1.00 42.84 O ANISOU 2068 O GLY A1064 4346 3023 8910 195 -441 1414 O ATOM 2069 N PHE A1065 -9.755 -53.194 20.360 1.00 44.27 N ANISOU 2069 N PHE A1065 4251 3150 9421 769 -146 1402 N ATOM 2070 CA PHE A1065 -8.741 -53.039 21.399 1.00 53.67 C ANISOU 2070 CA PHE A1065 5673 4325 10396 739 130 1125 C ATOM 2071 C PHE A1065 -8.702 -54.242 22.337 1.00 66.88 C ANISOU 2071 C PHE A1065 7151 6320 11940 583 285 1131 C ATOM 2072 O PHE A1065 -7.638 -54.565 22.879 1.00 45.49 O ANISOU 2072 O PHE A1065 4665 3638 8982 450 392 954 O ATOM 2073 CB PHE A1065 -8.974 -51.742 22.177 1.00 53.36 C ANISOU 2073 CB PHE A1065 5680 4156 10439 1107 366 930 C ATOM 2074 CG PHE A1065 -8.395 -50.525 21.503 1.00 58.91 C ANISOU 2074 CG PHE A1065 6830 4521 11032 1114 255 812 C ATOM 2075 CD1 PHE A1065 -7.041 -50.252 21.590 1.00 45.08 C ANISOU 2075 CD1 PHE A1065 5472 2665 8992 863 310 586 C ATOM 2076 CD2 PHE A1065 -9.199 -49.664 20.775 1.00 59.07 C ANISOU 2076 CD2 PHE A1065 6885 4406 11153 1340 84 929 C ATOM 2077 CE1 PHE A1065 -6.501 -49.150 20.968 1.00 45.54 C ANISOU 2077 CE1 PHE A1065 5949 2477 8878 791 211 510 C ATOM 2078 CE2 PHE A1065 -8.662 -48.546 20.153 1.00 52.75 C ANISOU 2078 CE2 PHE A1065 6560 3305 10178 1310 -20 859 C ATOM 2079 CZ PHE A1065 -7.316 -48.289 20.250 1.00 55.95 C ANISOU 2079 CZ PHE A1065 7357 3596 10307 1010 51 662 C ATOM 2080 N ASP A1066 -9.836 -54.922 22.531 1.00 43.27 N ANISOU 2080 N ASP A1066 3753 3591 9098 580 286 1346 N ATOM 2081 CA ASP A1066 -9.838 -56.138 23.343 1.00 42.75 C ANISOU 2081 CA ASP A1066 3557 3784 8903 365 402 1425 C ATOM 2082 C ASP A1066 -8.986 -57.224 22.701 1.00 62.82 C ANISOU 2082 C ASP A1066 6370 6197 11302 39 163 1466 C ATOM 2083 O ASP A1066 -8.214 -57.907 23.387 1.00 46.46 O ANISOU 2083 O ASP A1066 4468 4176 9007 -66 254 1392 O ATOM 2084 CB ASP A1066 -11.267 -56.645 23.545 1.00 46.29 C ANISOU 2084 CB ASP A1066 3502 4548 9538 336 431 1677 C ATOM 2085 CG ASP A1066 -12.018 -55.887 24.626 1.00 69.90 C ANISOU 2085 CG ASP A1066 6165 7824 12569 664 767 1592 C ATOM 2086 OD1 ASP A1066 -11.372 -55.335 25.542 1.00 76.12 O ANISOU 2086 OD1 ASP A1066 7138 8603 13181 836 1021 1346 O ATOM 2087 OD2 ASP A1066 -13.266 -55.860 24.566 1.00 85.40 O ANISOU 2087 OD2 ASP A1066 7658 10069 14721 753 774 1746 O ATOM 2088 N ILE A1067 -9.122 -57.408 21.386 1.00 39.18 N ANISOU 2088 N ILE A1067 3418 3054 8413 -91 -158 1571 N ATOM 2089 CA ILE A1067 -8.246 -58.330 20.672 1.00 53.66 C ANISOU 2089 CA ILE A1067 5535 4762 10093 -342 -396 1537 C ATOM 2090 C ILE A1067 -6.795 -57.890 20.827 1.00 33.93 C ANISOU 2090 C ILE A1067 3394 2213 7284 -282 -310 1234 C ATOM 2091 O ILE A1067 -5.906 -58.697 21.129 1.00 42.44 O ANISOU 2091 O ILE A1067 4659 3363 8104 -362 -317 1108 O ATOM 2092 CB ILE A1067 -8.649 -58.418 19.189 1.00 37.08 C ANISOU 2092 CB ILE A1067 3412 2642 8033 -440 -736 1610 C ATOM 2093 CG1 ILE A1067 -10.136 -58.738 19.042 1.00 46.95 C ANISOU 2093 CG1 ILE A1067 4238 3976 9623 -517 -835 1913 C ATOM 2094 CG2 ILE A1067 -7.821 -59.472 18.467 1.00 46.26 C ANISOU 2094 CG2 ILE A1067 4847 3900 8828 -597 -939 1433 C ATOM 2095 CD1 ILE A1067 -10.670 -58.479 17.638 1.00 45.33 C ANISOU 2095 CD1 ILE A1067 3953 3733 9536 -549 -1168 2024 C ATOM 2096 N LEU A1068 -6.543 -56.595 20.650 1.00 34.13 N ANISOU 2096 N LEU A1068 3520 2131 7315 -138 -234 1112 N ATOM 2097 CA LEU A1068 -5.170 -56.102 20.637 1.00 34.43 C ANISOU 2097 CA LEU A1068 3876 2168 7037 -171 -175 828 C ATOM 2098 C LEU A1068 -4.487 -56.349 21.976 1.00 33.91 C ANISOU 2098 C LEU A1068 3851 2168 6866 -125 71 672 C ATOM 2099 O LEU A1068 -3.389 -56.916 22.033 1.00 36.22 O ANISOU 2099 O LEU A1068 4308 2553 6900 -219 31 512 O ATOM 2100 CB LEU A1068 -5.152 -54.616 20.295 1.00 36.06 C ANISOU 2100 CB LEU A1068 4217 2216 7268 -71 -129 754 C ATOM 2101 CG LEU A1068 -3.743 -54.090 20.025 1.00 43.18 C ANISOU 2101 CG LEU A1068 5444 3120 7842 -219 -108 508 C ATOM 2102 CD1 LEU A1068 -3.254 -54.646 18.702 1.00 42.81 C ANISOU 2102 CD1 LEU A1068 5496 3204 7564 -410 -345 534 C ATOM 2103 CD2 LEU A1068 -3.697 -52.574 20.037 1.00 33.94 C ANISOU 2103 CD2 LEU A1068 4471 1728 6695 -150 -12 429 C ATOM 2104 N VAL A1069 -5.133 -55.939 23.066 1.00 42.27 N ANISOU 2104 N VAL A1069 4737 3316 8006 56 325 676 N ATOM 2105 CA VAL A1069 -4.559 -56.135 24.392 1.00 33.30 C ANISOU 2105 CA VAL A1069 3626 2390 6636 118 566 506 C ATOM 2106 C VAL A1069 -4.413 -57.619 24.701 1.00 34.31 C ANISOU 2106 C VAL A1069 3738 2661 6639 4 485 649 C ATOM 2107 O VAL A1069 -3.394 -58.053 25.251 1.00 34.31 O ANISOU 2107 O VAL A1069 3894 2787 6356 3 518 494 O ATOM 2108 CB VAL A1069 -5.411 -55.404 25.445 1.00 54.71 C ANISOU 2108 CB VAL A1069 6131 5211 9447 348 856 480 C ATOM 2109 CG1 VAL A1069 -4.887 -55.677 26.842 1.00 37.78 C ANISOU 2109 CG1 VAL A1069 3994 3344 7015 401 1101 325 C ATOM 2110 CG2 VAL A1069 -5.415 -53.900 25.151 1.00 43.31 C ANISOU 2110 CG2 VAL A1069 4811 3525 8121 499 908 295 C ATOM 2111 N GLY A1070 -5.416 -58.425 24.334 1.00 33.34 N ANISOU 2111 N GLY A1070 3439 2510 6717 -97 355 946 N ATOM 2112 CA GLY A1070 -5.314 -59.862 24.552 1.00 35.70 C ANISOU 2112 CA GLY A1070 3803 2838 6924 -242 241 1106 C ATOM 2113 C GLY A1070 -4.168 -60.493 23.781 1.00 37.42 C ANISOU 2113 C GLY A1070 4315 2931 6973 -307 -16 961 C ATOM 2114 O GLY A1070 -3.468 -61.375 24.293 1.00 33.71 O ANISOU 2114 O GLY A1070 4017 2503 6289 -285 -52 929 O ATOM 2115 N GLN A1071 -3.967 -60.063 22.533 1.00 32.95 N ANISOU 2115 N GLN A1071 3809 2233 6477 -363 -206 875 N ATOM 2116 CA GLN A1071 -2.879 -60.609 21.728 1.00 33.20 C ANISOU 2116 CA GLN A1071 4073 2254 6286 -403 -430 686 C ATOM 2117 C GLN A1071 -1.524 -60.157 22.247 1.00 35.73 C ANISOU 2117 C GLN A1071 4528 2730 6318 -296 -302 381 C ATOM 2118 O GLN A1071 -0.530 -60.879 22.101 1.00 32.69 O ANISOU 2118 O GLN A1071 4292 2428 5699 -252 -433 215 O ATOM 2119 CB GLN A1071 -3.052 -60.204 20.264 1.00 27.96 C ANISOU 2119 CB GLN A1071 3411 1641 5573 -473 -602 639 C ATOM 2120 CG GLN A1071 -4.215 -60.884 19.565 1.00 38.57 C ANISOU 2120 CG GLN A1071 4624 2992 7040 -559 -777 833 C ATOM 2121 CD GLN A1071 -4.442 -60.350 18.166 1.00 38.57 C ANISOU 2121 CD GLN A1071 4601 3021 7033 -604 -945 824 C ATOM 2122 OE1 GLN A1071 -4.273 -59.160 17.911 1.00 38.35 O ANISOU 2122 OE1 GLN A1071 4588 2979 7006 -566 -871 785 O ATOM 2123 NE2 GLN A1071 -4.838 -61.230 17.253 1.00 40.42 N ANISOU 2123 NE2 GLN A1071 4826 3266 7266 -696 -1184 874 N ATOM 2124 N ILE A1072 -1.463 -58.974 22.855 1.00 29.69 N ANISOU 2124 N ILE A1072 3703 2045 5531 -236 -55 268 N ATOM 2125 CA ILE A1072 -0.239 -58.544 23.518 1.00 26.62 C ANISOU 2125 CA ILE A1072 3406 1878 4830 -174 87 -43 C ATOM 2126 C ILE A1072 0.018 -59.404 24.754 1.00 35.67 C ANISOU 2126 C ILE A1072 4555 3211 5788 -30 172 -31 C ATOM 2127 O ILE A1072 1.139 -59.881 24.976 1.00 33.33 O ANISOU 2127 O ILE A1072 4356 3112 5194 50 107 -230 O ATOM 2128 CB ILE A1072 -0.330 -57.037 23.839 1.00 27.31 C ANISOU 2128 CB ILE A1072 3475 1934 4968 -178 311 -178 C ATOM 2129 CG1 ILE A1072 -0.320 -56.229 22.534 1.00 27.27 C ANISOU 2129 CG1 ILE A1072 3557 1729 5074 -334 183 -178 C ATOM 2130 CG2 ILE A1072 0.802 -56.601 24.765 1.00 31.51 C ANISOU 2130 CG2 ILE A1072 4067 2729 5176 -148 484 -510 C ATOM 2131 CD1 ILE A1072 -0.661 -54.772 22.697 1.00 28.64 C ANISOU 2131 CD1 ILE A1072 3782 1718 5383 -322 349 -235 C ATOM 2132 N ASP A1073 -1.029 -59.674 25.543 1.00 28.74 N ANISOU 2132 N ASP A1073 3559 2305 5056 10 300 222 N ATOM 2133 CA ASP A1073 -0.878 -60.551 26.704 1.00 30.49 C ANISOU 2133 CA ASP A1073 3816 2691 5077 113 371 313 C ATOM 2134 C ASP A1073 -0.460 -61.963 26.301 1.00 39.97 C ANISOU 2134 C ASP A1073 5208 3778 6201 122 86 415 C ATOM 2135 O ASP A1073 0.352 -62.600 26.988 1.00 34.71 O ANISOU 2135 O ASP A1073 4677 3260 5250 278 54 348 O ATOM 2136 CB ASP A1073 -2.186 -60.598 27.496 1.00 32.17 C ANISOU 2136 CB ASP A1073 3840 2928 5455 88 569 605 C ATOM 2137 CG ASP A1073 -2.525 -59.273 28.142 1.00 62.98 C ANISOU 2137 CG ASP A1073 7575 6978 9377 182 869 446 C ATOM 2138 OD1 ASP A1073 -1.606 -58.455 28.365 1.00 50.55 O ANISOU 2138 OD1 ASP A1073 6085 5509 7611 255 953 111 O ATOM 2139 OD2 ASP A1073 -3.717 -59.056 28.434 1.00 47.27 O ANISOU 2139 OD2 ASP A1073 5361 5014 7587 180 1018 634 O ATOM 2140 N ASP A1074 -1.040 -62.492 25.221 1.00 30.19 N ANISOU 2140 N ASP A1074 3996 2268 5208 -21 -139 573 N ATOM 2141 CA ASP A1074 -0.641 -63.817 24.751 1.00 33.32 C ANISOU 2141 CA ASP A1074 4623 2489 5548 3 -435 615 C ATOM 2142 C ASP A1074 0.856 -63.857 24.477 1.00 29.24 C ANISOU 2142 C ASP A1074 4239 2153 4719 201 -549 247 C ATOM 2143 O ASP A1074 1.561 -64.777 24.916 1.00 31.95 O ANISOU 2143 O ASP A1074 4766 2528 4847 403 -673 205 O ATOM 2144 CB ASP A1074 -1.414 -64.192 23.480 1.00 36.10 C ANISOU 2144 CB ASP A1074 4972 2556 6189 -202 -671 747 C ATOM 2145 CG ASP A1074 -2.890 -64.419 23.725 1.00 49.73 C ANISOU 2145 CG ASP A1074 6536 4153 8205 -420 -610 1118 C ATOM 2146 OD1 ASP A1074 -3.295 -64.522 24.902 1.00 52.93 O ANISOU 2146 OD1 ASP A1074 6873 4670 8567 -416 -397 1305 O ATOM 2147 OD2 ASP A1074 -3.643 -64.507 22.725 1.00 37.50 O ANISOU 2147 OD2 ASP A1074 4887 2620 6742 -562 -724 1127 O ATOM 2148 N ALA A1075 1.356 -62.855 23.745 1.00 28.91 N ANISOU 2148 N ALA A1075 4099 2251 4636 147 -515 -13 N ATOM 2149 CA ALA A1075 2.770 -62.826 23.380 1.00 48.03 C ANISOU 2149 CA ALA A1075 6570 4940 6741 275 -606 -381 C ATOM 2150 C ALA A1075 3.649 -62.576 24.599 1.00 45.82 C ANISOU 2150 C ALA A1075 6253 5013 6144 456 -438 -566 C ATOM 2151 O ALA A1075 4.734 -63.153 24.713 1.00 34.09 O ANISOU 2151 O ALA A1075 4824 3766 4364 678 -565 -788 O ATOM 2152 CB ALA A1075 3.014 -61.765 22.303 1.00 27.45 C ANISOU 2152 CB ALA A1075 3871 2409 4151 79 -587 -560 C ATOM 2153 N ALEU A1076 3.197 -61.724 25.522 0.43 33.21 N ANISOU 2153 N ALEU A1076 4547 3488 4583 393 -165 -505 N ATOM 2154 N BLEU A1076 3.196 -61.715 25.516 0.57 33.15 N ANISOU 2154 N BLEU A1076 4539 3480 4576 392 -164 -506 N ATOM 2155 CA ALEU A1076 3.972 -61.444 26.727 0.43 50.20 C ANISOU 2155 CA ALEU A1076 6655 6007 6411 542 -5 -696 C ATOM 2156 CA BLEU A1076 3.956 -61.448 26.734 0.57 58.40 C ANISOU 2156 CA BLEU A1076 7694 7042 7452 542 -4 -691 C ATOM 2157 C ALEU A1076 4.107 -62.678 27.611 0.43 50.27 C ANISOU 2157 C ALEU A1076 6796 6058 6246 795 -104 -528 C ATOM 2158 C BLEU A1076 4.130 -62.712 27.562 0.57 47.85 C ANISOU 2158 C BLEU A1076 6495 5746 5941 798 -117 -531 C ATOM 2159 O ALEU A1076 5.141 -62.861 28.266 0.43 40.29 O ANISOU 2159 O ALEU A1076 5536 5147 4627 1011 -127 -736 O ATOM 2160 O BLEU A1076 5.200 -62.947 28.138 0.57 50.83 O ANISOU 2160 O BLEU A1076 6882 6468 5964 1021 -161 -745 O ATOM 2161 CB ALEU A1076 3.326 -60.297 27.506 0.43 40.08 C ANISOU 2161 CB ALEU A1076 5255 4755 5219 433 304 -680 C ATOM 2162 CB BLEU A1076 3.258 -60.369 27.563 0.57 38.89 C ANISOU 2162 CB BLEU A1076 5107 4594 5075 442 304 -653 C ATOM 2163 CG ALEU A1076 3.974 -59.853 28.817 0.43 49.93 C ANISOU 2163 CG ALEU A1076 6447 6392 6133 545 498 -899 C ATOM 2164 CG BLEU A1076 3.589 -58.916 27.234 0.57 37.94 C ANISOU 2164 CG BLEU A1076 4916 4539 4962 263 451 -939 C ATOM 2165 CD1ALEU A1076 5.392 -59.356 28.590 0.43 35.22 C ANISOU 2165 CD1ALEU A1076 4540 4881 3962 517 454 -1330 C ATOM 2166 CD1BLEU A1076 2.531 -57.987 27.813 0.57 28.87 C ANISOU 2166 CD1BLEU A1076 3698 3241 4032 217 704 -841 C ATOM 2167 CD2ALEU A1076 3.130 -58.778 29.475 0.43 34.24 C ANISOU 2167 CD2ALEU A1076 4367 4355 4287 460 790 -888 C ATOM 2168 CD2BLEU A1076 4.966 -58.571 27.779 0.57 47.91 C ANISOU 2168 CD2BLEU A1076 6142 6244 5817 299 497 -1331 C ATOM 2169 N LYS A1077 3.082 -63.531 27.647 1.00 42.66 N ANISOU 2169 N LYS A1077 5946 4747 5514 756 -176 -140 N ATOM 2170 CA LYS A1077 3.183 -64.772 28.402 1.00 38.71 C ANISOU 2170 CA LYS A1077 5656 4192 4859 957 -304 80 C ATOM 2171 C LYS A1077 4.214 -65.706 27.779 1.00 34.21 C ANISOU 2171 C LYS A1077 5279 3593 4128 1218 -634 -104 C ATOM 2172 O LYS A1077 4.993 -66.346 28.494 1.00 40.52 O ANISOU 2172 O LYS A1077 6209 4566 4622 1530 -737 -144 O ATOM 2173 CB LYS A1077 1.818 -65.449 28.478 1.00 35.08 C ANISOU 2173 CB LYS A1077 5283 3348 4697 756 -309 545 C ATOM 2174 CG LYS A1077 1.865 -66.789 29.175 1.00 38.29 C ANISOU 2174 CG LYS A1077 5992 3594 4964 897 -467 837 C ATOM 2175 CD LYS A1077 0.478 -67.301 29.473 1.00 42.41 C ANISOU 2175 CD LYS A1077 6549 3833 5732 594 -394 1316 C ATOM 2176 CE LYS A1077 0.558 -68.666 30.103 1.00 44.30 C ANISOU 2176 CE LYS A1077 7172 3832 5827 682 -578 1645 C ATOM 2177 NZ LYS A1077 1.221 -69.651 29.206 1.00 90.29 N ANISOU 2177 NZ LYS A1077 13335 9283 11687 872 -979 1523 N ATOM 2178 N LEU A1078 4.228 -65.800 26.446 1.00 32.92 N ANISOU 2178 N LEU A1078 5130 3237 4143 1129 -811 -228 N ATOM 2179 CA LEU A1078 5.232 -66.618 25.775 1.00 44.16 C ANISOU 2179 CA LEU A1078 6698 4686 5393 1413 -1111 -481 C ATOM 2180 C LEU A1078 6.629 -66.060 26.000 1.00 47.11 C ANISOU 2180 C LEU A1078 6882 5644 5374 1632 -1063 -912 C ATOM 2181 O LEU A1078 7.573 -66.820 26.250 1.00 53.03 O ANISOU 2181 O LEU A1078 7726 6579 5843 2025 -1256 -1076 O ATOM 2182 CB LEU A1078 4.926 -66.708 24.282 1.00 34.21 C ANISOU 2182 CB LEU A1078 5454 3178 4365 1240 -1279 -560 C ATOM 2183 CG LEU A1078 3.633 -67.445 23.938 1.00 33.67 C ANISOU 2183 CG LEU A1078 5573 2556 4663 1022 -1401 -182 C ATOM 2184 CD1 LEU A1078 3.296 -67.268 22.469 1.00 44.12 C ANISOU 2184 CD1 LEU A1078 6843 3738 6184 810 -1534 -289 C ATOM 2185 CD2 LEU A1078 3.777 -68.929 24.308 1.00 37.08 C ANISOU 2185 CD2 LEU A1078 6386 2658 5045 1279 -1668 -41 C ATOM 2186 N ALA A1079 6.774 -64.736 25.912 1.00 51.43 N ANISOU 2186 N ALA A1079 7164 6486 5891 1383 -822 -1103 N ATOM 2187 CA ALA A1079 8.062 -64.102 26.175 1.00 50.72 C ANISOU 2187 CA ALA A1079 6859 6989 5422 1480 -750 -1516 C ATOM 2188 C ALA A1079 8.577 -64.461 27.563 1.00 57.69 C ANISOU 2188 C ALA A1079 7759 8167 5995 1788 -732 -1515 C ATOM 2189 O ALA A1079 9.739 -64.852 27.723 1.00 60.94 O ANISOU 2189 O ALA A1079 8092 8990 6071 2102 -875 -1781 O ATOM 2190 CB ALA A1079 7.940 -62.584 26.022 1.00 57.05 C ANISOU 2190 CB ALA A1079 7458 7931 6286 1087 -478 -1649 C ATOM 2191 N ASN A1080 7.717 -64.345 28.581 1.00 43.37 N ANISOU 2191 N ASN A1080 6016 6188 4275 1709 -556 -1201 N ATOM 2192 CA ASN A1080 8.120 -64.634 29.954 1.00 36.87 C ANISOU 2192 CA ASN A1080 5219 5670 3120 1972 -522 -1159 C ATOM 2193 C ASN A1080 8.460 -66.105 30.181 1.00 42.16 C ANISOU 2193 C ASN A1080 6164 6206 3647 2401 -833 -987 C ATOM 2194 O ASN A1080 9.156 -66.423 31.149 1.00 66.59 O ANISOU 2194 O ASN A1080 9274 9655 6373 2722 -891 -1030 O ATOM 2195 CB ASN A1080 7.018 -64.200 30.916 1.00 41.61 C ANISOU 2195 CB ASN A1080 5829 6138 3843 1768 -246 -847 C ATOM 2196 CG ASN A1080 6.852 -62.691 30.964 1.00 59.10 C ANISOU 2196 CG ASN A1080 7805 8530 6122 1458 53 -1083 C ATOM 2197 OD1 ASN A1080 7.833 -61.950 30.972 1.00103.80 O ANISOU 2197 OD1 ASN A1080 13295 14604 11541 1432 97 -1490 O ATOM 2198 ND2 ASN A1080 5.608 -62.230 30.990 1.00 62.36 N ANISOU 2198 ND2 ASN A1080 8207 8628 6858 1220 250 -838 N ATOM 2199 N GLU A1081 7.969 -67.004 29.334 1.00 47.08 N ANISOU 2199 N GLU A1081 7034 6308 4547 2421 -1050 -793 N ATOM 2200 CA GLU A1081 8.370 -68.402 29.342 1.00 54.56 C ANISOU 2200 CA GLU A1081 8309 7029 5391 2849 -1394 -692 C ATOM 2201 C GLU A1081 9.637 -68.649 28.537 1.00 78.29 C ANISOU 2201 C GLU A1081 11214 10351 8181 3209 -1633 -1168 C ATOM 2202 O GLU A1081 10.047 -69.806 28.394 1.00 67.96 O ANISOU 2202 O GLU A1081 10186 8839 6796 3643 -1954 -1163 O ATOM 2203 CB GLU A1081 7.241 -69.279 28.788 1.00 45.96 C ANISOU 2203 CB GLU A1081 7561 5200 4702 2670 -1533 -301 C ATOM 2204 CG GLU A1081 6.002 -69.345 29.660 1.00 44.48 C ANISOU 2204 CG GLU A1081 7490 4729 4680 2363 -1341 217 C ATOM 2205 CD GLU A1081 4.798 -69.866 28.903 1.00 88.99 C ANISOU 2205 CD GLU A1081 13312 9745 10755 2015 -1418 528 C ATOM 2206 OE1 GLU A1081 4.926 -70.108 27.685 1.00 60.57 O ANISOU 2206 OE1 GLU A1081 9758 5928 7327 2016 -1620 319 O ATOM 2207 OE2 GLU A1081 3.725 -70.030 29.520 1.00108.71 O ANISOU 2207 OE2 GLU A1081 15883 12024 13399 1725 -1275 964 O ATOM 2208 N GLY A1082 10.252 -67.602 27.990 1.00 56.76 N ANISOU 2208 N GLY A1082 7576 5185 8805 3012 1211 597 N ATOM 2209 CA GLY A1082 11.447 -67.783 27.191 1.00 71.59 C ANISOU 2209 CA GLY A1082 9388 6954 10858 2902 1153 536 C ATOM 2210 C GLY A1082 11.222 -68.386 25.823 1.00 74.74 C ANISOU 2210 C GLY A1082 9829 7264 11303 2656 1357 620 C ATOM 2211 O GLY A1082 12.166 -68.904 25.225 1.00 65.07 O ANISOU 2211 O GLY A1082 8573 5976 10175 2613 1402 630 O ATOM 2212 N LYS A1083 9.997 -68.331 25.303 1.00 55.29 N ANISOU 2212 N LYS A1083 7427 4792 8787 2524 1465 660 N ATOM 2213 CA LYS A1083 9.683 -68.877 23.983 1.00 54.94 C ANISOU 2213 CA LYS A1083 7431 4653 8790 2332 1597 689 C ATOM 2214 C LYS A1083 9.681 -67.722 22.982 1.00 54.00 C ANISOU 2214 C LYS A1083 7299 4512 8708 2219 1523 576 C ATOM 2215 O LYS A1083 8.641 -67.163 22.644 1.00 45.84 O ANISOU 2215 O LYS A1083 6302 3475 7640 2147 1494 535 O ATOM 2216 CB LYS A1083 8.344 -69.613 24.013 1.00 47.72 C ANISOU 2216 CB LYS A1083 6576 3700 7857 2283 1727 794 C ATOM 2217 CG LYS A1083 8.213 -70.647 25.134 1.00 53.89 C ANISOU 2217 CG LYS A1083 7370 4487 8620 2421 1856 986 C ATOM 2218 CD LYS A1083 6.843 -71.323 25.106 1.00 50.27 C ANISOU 2218 CD LYS A1083 6919 3940 8241 2362 2021 1132 C ATOM 2219 CE LYS A1083 6.713 -72.371 26.199 1.00 59.72 C ANISOU 2219 CE LYS A1083 8120 5121 9451 2513 2212 1404 C ATOM 2220 NZ LYS A1083 5.384 -73.055 26.174 1.00 56.02 N ANISOU 2220 NZ LYS A1083 7597 4519 9168 2445 2405 1594 N ATOM 2221 N VAL A1084 10.876 -67.382 22.482 1.00 47.75 N ANISOU 2221 N VAL A1084 6445 3688 8010 2218 1517 551 N ATOM 2222 CA VAL A1084 11.040 -66.172 21.670 1.00 54.79 C ANISOU 2222 CA VAL A1084 7306 4533 8977 2144 1485 509 C ATOM 2223 C VAL A1084 10.329 -66.313 20.327 1.00 59.11 C ANISOU 2223 C VAL A1084 7968 5032 9461 2027 1608 529 C ATOM 2224 O VAL A1084 9.490 -65.481 19.960 1.00 47.90 O ANISOU 2224 O VAL A1084 6596 3594 8009 1970 1532 483 O ATOM 2225 CB VAL A1084 12.531 -65.851 21.470 1.00 59.49 C ANISOU 2225 CB VAL A1084 7767 5076 9760 2186 1523 542 C ATOM 2226 CG1 VAL A1084 12.698 -64.455 20.885 1.00 61.73 C ANISOU 2226 CG1 VAL A1084 7983 5272 10198 2124 1496 552 C ATOM 2227 CG2 VAL A1084 13.290 -66.001 22.773 1.00 72.79 C ANISOU 2227 CG2 VAL A1084 9355 6797 11505 2348 1355 487 C ATOM 2228 N LYS A1085 10.692 -67.345 19.558 1.00 46.60 N ANISOU 2228 N LYS A1085 6439 3412 7855 2030 1765 573 N ATOM 2229 CA LYS A1085 10.084 -67.579 18.249 1.00 69.68 C ANISOU 2229 CA LYS A1085 9502 6274 10699 1992 1839 549 C ATOM 2230 C LYS A1085 8.566 -67.630 18.341 1.00 56.42 C ANISOU 2230 C LYS A1085 7898 4581 8959 1932 1701 473 C ATOM 2231 O LYS A1085 7.860 -67.049 17.507 1.00 47.78 O ANISOU 2231 O LYS A1085 6892 3444 7820 1899 1649 418 O ATOM 2232 CB LYS A1085 10.609 -68.890 17.656 1.00 48.00 C ANISOU 2232 CB LYS A1085 6820 3483 7936 2065 1961 553 C ATOM 2233 CG LYS A1085 12.091 -68.891 17.316 1.00 49.56 C ANISOU 2233 CG LYS A1085 6940 3685 8207 2153 2148 635 C ATOM 2234 CD LYS A1085 12.372 -68.148 16.016 1.00 64.51 C ANISOU 2234 CD LYS A1085 8901 5540 10069 2195 2342 701 C ATOM 2235 CE LYS A1085 13.818 -68.350 15.574 1.00 53.09 C ANISOU 2235 CE LYS A1085 7363 4088 8722 2319 2610 820 C ATOM 2236 NZ LYS A1085 14.008 -68.077 14.122 1.00 98.56 N ANISOU 2236 NZ LYS A1085 13265 9811 14372 2448 2889 915 N ATOM 2237 N GLU A1086 8.050 -68.336 19.345 1.00 45.51 N ANISOU 2237 N GLU A1086 6477 3218 7596 1937 1662 490 N ATOM 2238 CA GLU A1086 6.612 -68.438 19.528 1.00 47.40 C ANISOU 2238 CA GLU A1086 6740 3423 7845 1893 1587 458 C ATOM 2239 C GLU A1086 6.022 -67.083 19.886 1.00 44.20 C ANISOU 2239 C GLU A1086 6299 3082 7412 1879 1481 412 C ATOM 2240 O GLU A1086 4.911 -66.750 19.455 1.00 43.95 O ANISOU 2240 O GLU A1086 6308 3005 7387 1839 1395 343 O ATOM 2241 CB GLU A1086 6.311 -69.474 20.609 1.00 57.30 C ANISOU 2241 CB GLU A1086 7941 4666 9163 1930 1661 565 C ATOM 2242 CG GLU A1086 4.882 -69.958 20.664 1.00 62.58 C ANISOU 2242 CG GLU A1086 8605 5234 9937 1889 1660 585 C ATOM 2243 CD GLU A1086 4.708 -71.096 21.648 1.00 69.61 C ANISOU 2243 CD GLU A1086 9435 6071 10944 1935 1808 768 C ATOM 2244 OE1 GLU A1086 5.710 -71.779 21.948 1.00 96.93 O ANISOU 2244 OE1 GLU A1086 12905 9536 14388 1992 1862 833 O ATOM 2245 OE2 GLU A1086 3.573 -71.303 22.126 1.00 97.52 O ANISOU 2245 OE2 GLU A1086 12897 9545 14610 1926 1890 871 O ATOM 2246 N ALA A1087 6.766 -66.282 20.657 1.00 44.00 N ANISOU 2246 N ALA A1087 6199 3138 7382 1935 1443 422 N ATOM 2247 CA ALA A1087 6.300 -64.944 21.018 1.00 50.39 C ANISOU 2247 CA ALA A1087 6978 3980 8187 1958 1288 340 C ATOM 2248 C ALA A1087 6.285 -64.017 19.810 1.00 52.68 C ANISOU 2248 C ALA A1087 7332 4192 8492 1885 1227 293 C ATOM 2249 O ALA A1087 5.353 -63.220 19.643 1.00 42.89 O ANISOU 2249 O ALA A1087 6124 2931 7243 1872 1095 214 O ATOM 2250 CB ALA A1087 7.178 -64.356 22.124 1.00 44.05 C ANISOU 2250 CB ALA A1087 6085 3239 7413 2079 1191 315 C ATOM 2251 N GLN A1088 7.315 -64.102 18.963 1.00 43.86 N ANISOU 2251 N GLN A1088 6236 3024 7405 1863 1346 361 N ATOM 2252 CA GLN A1088 7.357 -63.280 17.757 1.00 48.98 C ANISOU 2252 CA GLN A1088 6965 3582 8062 1830 1366 384 C ATOM 2253 C GLN A1088 6.246 -63.660 16.783 1.00 44.28 C ANISOU 2253 C GLN A1088 6521 2938 7364 1814 1333 317 C ATOM 2254 O GLN A1088 5.680 -62.791 16.109 1.00 44.47 O ANISOU 2254 O GLN A1088 6630 2895 7372 1806 1238 287 O ATOM 2255 CB GLN A1088 8.725 -63.402 17.092 1.00 45.75 C ANISOU 2255 CB GLN A1088 6532 3128 7722 1858 1595 521 C ATOM 2256 CG GLN A1088 9.852 -62.839 17.920 1.00 46.43 C ANISOU 2256 CG GLN A1088 6434 3205 8002 1876 1581 574 C ATOM 2257 CD GLN A1088 11.211 -63.172 17.335 1.00 49.37 C ANISOU 2257 CD GLN A1088 6725 3532 8501 1915 1855 731 C ATOM 2258 OE1 GLN A1088 11.572 -64.344 17.215 1.00 53.95 O ANISOU 2258 OE1 GLN A1088 7333 4163 9003 1965 1990 741 O ATOM 2259 NE2 GLN A1088 11.967 -62.146 16.962 1.00 49.96 N ANISOU 2259 NE2 GLN A1088 6680 3489 8815 1900 1948 870 N ATOM 2260 N ALA A1089 5.932 -64.954 16.679 1.00 44.42 N ANISOU 2260 N ALA A1089 6578 2956 7345 1825 1374 285 N ATOM 2261 CA ALA A1089 4.809 -65.363 15.843 1.00 50.84 C ANISOU 2261 CA ALA A1089 7512 3678 8126 1831 1262 175 C ATOM 2262 C ALA A1089 3.490 -64.856 16.415 1.00 52.07 C ANISOU 2262 C ALA A1089 7618 3834 8333 1794 1075 90 C ATOM 2263 O ALA A1089 2.636 -64.356 15.671 1.00 46.94 O ANISOU 2263 O ALA A1089 7053 3102 7679 1803 922 -7 O ATOM 2264 CB ALA A1089 4.789 -66.884 15.689 1.00 45.77 C ANISOU 2264 CB ALA A1089 6900 2979 7510 1862 1297 142 C ATOM 2265 N ALA A1090 3.309 -64.966 17.736 1.00 43.49 N ANISOU 2265 N ALA A1090 6398 2833 7293 1786 1101 130 N ATOM 2266 CA ALA A1090 2.122 -64.398 18.371 1.00 47.20 C ANISOU 2266 CA ALA A1090 6808 3320 7804 1800 991 71 C ATOM 2267 C ALA A1090 2.011 -62.906 18.091 1.00 51.55 C ANISOU 2267 C ALA A1090 7393 3868 8324 1813 828 -5 C ATOM 2268 O ALA A1090 0.906 -62.378 17.886 1.00 43.01 O ANISOU 2268 O ALA A1090 6336 2740 7264 1832 676 -106 O ATOM 2269 CB ALA A1090 2.158 -64.652 19.879 1.00 43.26 C ANISOU 2269 CB ALA A1090 6175 2931 7332 1857 1108 157 C ATOM 2270 N ALA A1091 3.149 -62.209 18.081 1.00 42.71 N ANISOU 2270 N ALA A1091 6270 2767 7190 1813 849 48 N ATOM 2271 CA ALA A1091 3.124 -60.766 17.895 1.00 42.84 C ANISOU 2271 CA ALA A1091 6314 2731 7232 1827 684 2 C ATOM 2272 C ALA A1091 2.804 -60.396 16.455 1.00 56.46 C ANISOU 2272 C ALA A1091 8186 4326 8939 1800 634 2 C ATOM 2273 O ALA A1091 2.272 -59.310 16.201 1.00 53.64 O ANISOU 2273 O ALA A1091 7877 3892 8612 1816 449 -56 O ATOM 2274 CB ALA A1091 4.458 -60.154 18.327 1.00 43.23 C ANISOU 2274 CB ALA A1091 6299 2776 7349 1843 714 77 C ATOM 2275 N GLU A1092 3.112 -61.281 15.502 1.00 44.45 N ANISOU 2275 N GLU A1092 6757 2769 7363 1797 784 56 N ATOM 2276 CA GLU A1092 2.749 -61.013 14.116 1.00 47.64 C ANISOU 2276 CA GLU A1092 7334 3049 7718 1836 749 46 C ATOM 2277 C GLU A1092 1.236 -60.949 13.943 1.00 50.95 C ANISOU 2277 C GLU A1092 7760 3404 8195 1846 491 -136 C ATOM 2278 O GLU A1092 0.742 -60.248 13.051 1.00 53.32 O ANISOU 2278 O GLU A1092 8155 3590 8513 1879 385 -165 O ATOM 2279 CB GLU A1092 3.356 -62.075 13.200 1.00 53.35 C ANISOU 2279 CB GLU A1092 8184 3752 8333 1905 958 99 C ATOM 2280 CG GLU A1092 3.616 -61.595 11.782 1.00114.57 C ANISOU 2280 CG GLU A1092 16183 11404 15944 2026 1074 193 C ATOM 2281 CD GLU A1092 4.829 -60.688 11.687 1.00113.93 C ANISOU 2281 CD GLU A1092 16106 11308 15874 2037 1310 445 C ATOM 2282 OE1 GLU A1092 5.825 -60.951 12.395 1.00100.40 O ANISOU 2282 OE1 GLU A1092 14225 9664 14257 1987 1468 534 O ATOM 2283 OE2 GLU A1092 4.786 -59.712 10.907 1.00 83.81 O ANISOU 2283 OE2 GLU A1092 12447 7387 12009 2099 1335 572 O ATOM 2284 N GLN A1093 0.485 -61.653 14.796 1.00 44.73 N ANISOU 2284 N GLN A1093 6869 2670 7456 1833 423 -230 N ATOM 2285 CA GLN A1093 -0.972 -61.576 14.740 1.00 58.03 C ANISOU 2285 CA GLN A1093 8553 4279 9216 1869 193 -392 C ATOM 2286 C GLN A1093 -1.463 -60.160 14.975 1.00 63.38 C ANISOU 2286 C GLN A1093 9200 4994 9887 1866 39 -432 C ATOM 2287 O GLN A1093 -2.519 -59.775 14.460 1.00 58.50 O ANISOU 2287 O GLN A1093 8562 4344 9323 1851 -138 -542 O ATOM 2288 CB GLN A1093 -1.592 -62.513 15.775 1.00 45.02 C ANISOU 2288 CB GLN A1093 6831 2693 7583 1879 282 -383 C ATOM 2289 CG GLN A1093 -1.097 -63.932 15.673 1.00 45.48 C ANISOU 2289 CG GLN A1093 6881 2723 7677 1846 429 -321 C ATOM 2290 CD GLN A1093 -1.381 -64.539 14.321 1.00 74.41 C ANISOU 2290 CD GLN A1093 10698 6205 11368 1897 257 -457 C ATOM 2291 OE1 GLN A1093 -2.509 -64.943 14.035 1.00 95.29 O ANISOU 2291 OE1 GLN A1093 13443 8743 14019 1940 119 -555 O ATOM 2292 NE2 GLN A1093 -0.359 -64.603 13.475 1.00 53.74 N ANISOU 2292 NE2 GLN A1093 8128 3579 8710 1907 346 -430 N ATOM 2293 N LEU A1094 -0.712 -59.378 15.756 1.00 41.59 N ANISOU 2293 N LEU A1094 6800 2338 6666 1430 -317 237 N ATOM 2294 CA LEU A1094 -1.074 -57.992 16.022 1.00 40.01 C ANISOU 2294 CA LEU A1094 6493 2226 6483 1269 -241 402 C ATOM 2295 C LEU A1094 -1.303 -57.201 14.743 1.00 41.46 C ANISOU 2295 C LEU A1094 6907 2452 6393 1293 -290 392 C ATOM 2296 O LEU A1094 -2.106 -56.263 14.737 1.00 42.64 O ANISOU 2296 O LEU A1094 7058 2558 6586 1200 -381 494 O ATOM 2297 CB LEU A1094 0.011 -57.322 16.864 1.00 38.56 C ANISOU 2297 CB LEU A1094 6125 2242 6284 1198 48 529 C ATOM 2298 CG LEU A1094 0.120 -57.872 18.285 1.00 37.00 C ANISOU 2298 CG LEU A1094 5715 2000 6344 1121 65 578 C ATOM 2299 CD1 LEU A1094 1.411 -57.430 18.928 1.00 43.27 C ANISOU 2299 CD1 LEU A1094 6357 2992 7092 1078 315 688 C ATOM 2300 CD2 LEU A1094 -1.081 -57.443 19.124 1.00 38.45 C ANISOU 2300 CD2 LEU A1094 5817 2240 6553 908 -48 614 C ATOM 2301 N LYS A1095 -0.611 -57.554 13.655 1.00 43.65 N ANISOU 2301 N LYS A1095 7402 2810 6372 1435 -229 269 N ATOM 2302 CA LYS A1095 -0.739 -56.772 12.425 1.00 46.78 C ANISOU 2302 CA LYS A1095 8067 3252 6455 1430 -261 272 C ATOM 2303 C LYS A1095 -2.125 -56.917 11.811 1.00 48.17 C ANISOU 2303 C LYS A1095 8419 3197 6688 1414 -641 231 C ATOM 2304 O LYS A1095 -2.685 -55.943 11.293 1.00 50.72 O ANISOU 2304 O LYS A1095 8864 3499 6909 1350 -753 319 O ATOM 2305 CB LYS A1095 0.341 -57.174 11.427 1.00 59.53 C ANISOU 2305 CB LYS A1095 9878 5034 7708 1588 -67 142 C ATOM 2306 CG LYS A1095 1.718 -56.706 11.836 1.00 73.84 C ANISOU 2306 CG LYS A1095 11474 7165 9417 1563 313 232 C ATOM 2307 CD LYS A1095 2.768 -57.145 10.846 1.00 87.70 C ANISOU 2307 CD LYS A1095 13361 9143 10817 1753 546 100 C ATOM 2308 CE LYS A1095 4.098 -56.510 11.181 1.00 82.99 C ANISOU 2308 CE LYS A1095 12490 8933 10108 1670 917 235 C ATOM 2309 NZ LYS A1095 5.188 -57.020 10.307 1.00110.20 N ANISOU 2309 NZ LYS A1095 15970 12668 13232 1895 1201 105 N ATOM 2310 N THR A1096 -2.701 -58.119 11.869 1.00 47.11 N ANISOU 2310 N THR A1096 8309 2877 6712 1458 -873 113 N ATOM 2311 CA THR A1096 -4.070 -58.296 11.395 1.00 53.53 C ANISOU 2311 CA THR A1096 9222 3496 7621 1388 -1273 105 C ATOM 2312 C THR A1096 -5.038 -57.421 12.181 1.00 46.76 C ANISOU 2312 C THR A1096 8065 2644 7059 1263 -1354 282 C ATOM 2313 O THR A1096 -5.934 -56.794 11.603 1.00 51.59 O ANISOU 2313 O THR A1096 8739 3210 7654 1241 -1590 342 O ATOM 2314 CB THR A1096 -4.476 -59.766 11.495 1.00 58.03 C ANISOU 2314 CB THR A1096 9856 3867 8324 1387 -1509 -26 C ATOM 2315 OG1 THR A1096 -3.633 -60.551 10.643 1.00 69.41 O ANISOU 2315 OG1 THR A1096 11656 5266 9451 1570 -1451 -217 O ATOM 2316 CG2 THR A1096 -5.928 -59.949 11.077 1.00 52.69 C ANISOU 2316 CG2 THR A1096 9194 3063 7761 1236 -1934 -1 C ATOM 2317 N THR A1097 -4.867 -57.362 13.503 1.00 44.36 N ANISOU 2317 N THR A1097 7411 2453 6992 1182 -1130 362 N ATOM 2318 CA THR A1097 -5.725 -56.511 14.319 1.00 49.02 C ANISOU 2318 CA THR A1097 7704 3132 7789 1085 -1101 504 C ATOM 2319 C THR A1097 -5.479 -55.038 14.025 1.00 48.50 C ANISOU 2319 C THR A1097 7755 3110 7563 1130 -996 610 C ATOM 2320 O THR A1097 -6.425 -54.243 13.964 1.00 43.56 O ANISOU 2320 O THR A1097 7060 2490 6999 1140 -1118 687 O ATOM 2321 CB THR A1097 -5.499 -56.807 15.797 1.00 40.97 C ANISOU 2321 CB THR A1097 6396 2222 6949 988 -858 547 C ATOM 2322 OG1 THR A1097 -5.615 -58.222 16.012 1.00 46.83 O ANISOU 2322 OG1 THR A1097 7108 2899 7788 931 -972 454 O ATOM 2323 CG2 THR A1097 -6.526 -56.072 16.651 1.00 40.39 C ANISOU 2323 CG2 THR A1097 6070 2228 7047 923 -843 652 C ATOM 2324 N ARG A1098 -4.214 -54.657 13.846 1.00 43.32 N ANISOU 2324 N ARG A1098 7301 2474 6684 1165 -785 623 N ATOM 2325 CA ARG A1098 -3.893 -53.272 13.515 1.00 50.48 C ANISOU 2325 CA ARG A1098 8381 3436 7364 1139 -682 736 C ATOM 2326 C ARG A1098 -4.556 -52.853 12.210 1.00 57.34 C ANISOU 2326 C ARG A1098 9539 4219 8029 1197 -953 725 C ATOM 2327 O ARG A1098 -5.139 -51.766 12.120 1.00 55.33 O ANISOU 2327 O ARG A1098 9342 3924 7756 1203 -1046 829 O ATOM 2328 CB ARG A1098 -2.378 -53.100 13.434 1.00 42.24 C ANISOU 2328 CB ARG A1098 7418 2578 6054 1079 -365 747 C ATOM 2329 CG ARG A1098 -1.915 -51.687 13.154 1.00 46.62 C ANISOU 2329 CG ARG A1098 8180 3192 6341 970 -248 889 C ATOM 2330 CD ARG A1098 -0.568 -51.716 12.477 1.00 59.86 C ANISOU 2330 CD ARG A1098 9980 5096 7669 906 -5 875 C ATOM 2331 NE ARG A1098 -0.598 -52.551 11.280 1.00 60.20 N ANISOU 2331 NE ARG A1098 10206 5149 7520 1037 -99 715 N ATOM 2332 CZ ARG A1098 0.484 -53.041 10.685 1.00 59.22 C ANISOU 2332 CZ ARG A1098 10130 5237 7135 1077 126 634 C ATOM 2333 NH1 ARG A1098 1.687 -52.784 11.186 1.00 57.67 N ANISOU 2333 NH1 ARG A1098 9743 5299 6870 977 444 718 N ATOM 2334 NH2 ARG A1098 0.362 -53.795 9.599 1.00 50.17 N ANISOU 2334 NH2 ARG A1098 9219 4055 5789 1222 31 470 N ATOM 2335 N ASN A1099 -4.499 -53.716 11.194 1.00 47.19 N ANISOU 2335 N ASN A1099 8447 2910 6573 1244 -1092 590 N ATOM 2336 CA ASN A1099 -5.056 -53.370 9.891 1.00 50.14 C ANISOU 2336 CA ASN A1099 9154 3193 6703 1278 -1372 578 C ATOM 2337 C ASN A1099 -6.578 -53.346 9.928 1.00 50.50 C ANISOU 2337 C ASN A1099 9060 3096 7030 1312 -1766 621 C ATOM 2338 O ASN A1099 -7.206 -52.418 9.409 1.00 60.88 O ANISOU 2338 O ASN A1099 10506 4358 8268 1348 -1965 711 O ATOM 2339 CB ASN A1099 -4.567 -54.359 8.829 1.00 58.37 C ANISOU 2339 CB ASN A1099 10486 4235 7456 1321 -1405 405 C ATOM 2340 CG ASN A1099 -3.055 -54.393 8.713 1.00 51.53 C ANISOU 2340 CG ASN A1099 9701 3574 6303 1329 -992 362 C ATOM 2341 OD1 ASN A1099 -2.364 -53.466 9.139 1.00 56.76 O ANISOU 2341 OD1 ASN A1099 10288 4382 6897 1242 -728 491 O ATOM 2342 ND2 ASN A1099 -2.531 -55.469 8.134 1.00 64.41 N ANISOU 2342 ND2 ASN A1099 11490 5223 7759 1434 -939 182 N ATOM 2343 N ALA A1100 -7.192 -54.362 10.538 1.00 59.85 N ANISOU 2343 N ALA A1100 9952 4251 8537 1286 -1882 567 N ATOM 2344 CA ALA A1100 -8.644 -54.488 10.483 1.00 52.69 C ANISOU 2344 CA ALA A1100 8834 3303 7881 1271 -2247 606 C ATOM 2345 C ALA A1100 -9.354 -53.531 11.434 1.00 61.42 C ANISOU 2345 C ALA A1100 9563 4531 9241 1301 -2146 737 C ATOM 2346 O ALA A1100 -10.495 -53.144 11.163 1.00 63.85 O ANISOU 2346 O ALA A1100 9752 4824 9683 1364 -2440 804 O ATOM 2347 CB ALA A1100 -9.060 -55.925 10.791 1.00 62.61 C ANISOU 2347 CB ALA A1100 9937 4488 9365 1174 -2416 521 C ATOM 2348 N TYR A1101 -8.715 -53.143 12.541 1.00 54.64 N ANISOU 2348 N TYR A1101 8534 3785 8440 1278 -1748 774 N ATOM 2349 CA TYR A1101 -9.376 -52.356 13.578 1.00 47.58 C ANISOU 2349 CA TYR A1101 7334 2985 7759 1328 -1614 870 C ATOM 2350 C TYR A1101 -8.639 -51.062 13.897 1.00 55.89 C ANISOU 2350 C TYR A1101 8543 4077 8615 1359 -1315 941 C ATOM 2351 O TYR A1101 -9.203 -49.979 13.716 1.00 50.23 O ANISOU 2351 O TYR A1101 7882 3344 7858 1473 -1384 1011 O ATOM 2352 CB TYR A1101 -9.535 -53.182 14.860 1.00 45.97 C ANISOU 2352 CB TYR A1101 6780 2851 7834 1234 -1457 857 C ATOM 2353 CG TYR A1101 -10.434 -54.387 14.733 1.00 52.85 C ANISOU 2353 CG TYR A1101 7450 3657 8973 1153 -1782 829 C ATOM 2354 CD1 TYR A1101 -11.813 -54.264 14.846 1.00 61.08 C ANISOU 2354 CD1 TYR A1101 8178 4708 10321 1203 -2046 916 C ATOM 2355 CD2 TYR A1101 -9.902 -55.651 14.525 1.00 49.96 C ANISOU 2355 CD2 TYR A1101 7204 3212 8568 1031 -1839 729 C ATOM 2356 CE1 TYR A1101 -12.637 -55.365 14.740 1.00 54.64 C ANISOU 2356 CE1 TYR A1101 7158 3810 9792 1079 -2395 938 C ATOM 2357 CE2 TYR A1101 -10.718 -56.757 14.417 1.00 50.05 C ANISOU 2357 CE2 TYR A1101 7097 3110 8811 912 -2176 718 C ATOM 2358 CZ TYR A1101 -12.086 -56.609 14.526 1.00 54.16 C ANISOU 2358 CZ TYR A1101 7289 3646 9644 900 -2456 833 C ATOM 2359 OH TYR A1101 -12.905 -57.708 14.421 1.00 81.13 O ANISOU 2359 OH TYR A1101 10553 7042 13230 688 -2769 832 O ATOM 2360 N ILE A1102 -7.393 -51.146 14.370 1.00 50.72 N ANISOU 2360 N ILE A1102 7484 3668 8119 2691 -57 -523 N ATOM 2361 CA ILE A1102 -6.746 -50.002 15.008 1.00 50.29 C ANISOU 2361 CA ILE A1102 7443 3688 7978 2709 -89 -502 C ATOM 2362 C ILE A1102 -6.594 -48.843 14.034 1.00 50.03 C ANISOU 2362 C ILE A1102 7493 3662 7854 2679 -67 -579 C ATOM 2363 O ILE A1102 -6.789 -47.679 14.402 1.00 49.71 O ANISOU 2363 O ILE A1102 7485 3671 7730 2683 -126 -586 O ATOM 2364 CB ILE A1102 -5.387 -50.415 15.599 1.00 52.76 C ANISOU 2364 CB ILE A1102 7669 3950 8426 2740 -84 -433 C ATOM 2365 CG1 ILE A1102 -5.528 -51.712 16.410 1.00 51.54 C ANISOU 2365 CG1 ILE A1102 7430 3770 8384 2788 -92 -323 C ATOM 2366 CG2 ILE A1102 -4.828 -49.278 16.447 1.00 51.11 C ANISOU 2366 CG2 ILE A1102 7483 3780 8155 2777 -205 -427 C ATOM 2367 CD1 ILE A1102 -6.484 -51.606 17.590 1.00 51.69 C ANISOU 2367 CD1 ILE A1102 7474 3883 8283 2874 -168 -237 C ATOM 2368 N GLN A1103 -6.231 -49.132 12.783 1.00 53.38 N ANISOU 2368 N GLN A1103 7966 4023 8292 2676 23 -634 N ATOM 2369 CA GLN A1103 -6.052 -48.042 11.830 1.00 69.16 C ANISOU 2369 CA GLN A1103 10057 6021 10199 2695 66 -659 C ATOM 2370 C GLN A1103 -7.365 -47.322 11.546 1.00 56.90 C ANISOU 2370 C GLN A1103 8603 4529 8487 2686 -27 -694 C ATOM 2371 O GLN A1103 -7.370 -46.103 11.338 1.00 50.29 O ANISOU 2371 O GLN A1103 7801 3703 7605 2695 -33 -671 O ATOM 2372 CB GLN A1103 -5.433 -48.562 10.534 1.00 62.11 C ANISOU 2372 CB GLN A1103 9253 5063 9283 2761 206 -704 C ATOM 2373 CG GLN A1103 -5.036 -47.449 9.573 1.00 70.87 C ANISOU 2373 CG GLN A1103 10466 6161 10299 2836 309 -662 C ATOM 2374 CD GLN A1103 -4.433 -47.971 8.288 1.00 79.83 C ANISOU 2374 CD GLN A1103 11749 7255 11326 2967 507 -685 C ATOM 2375 OE1 GLN A1103 -3.663 -48.931 8.294 1.00106.83 O ANISOU 2375 OE1 GLN A1103 15102 10623 14867 2991 609 -700 O ATOM 2376 NE2 GLN A1103 -4.785 -47.343 7.174 1.00 92.26 N ANISOU 2376 NE2 GLN A1103 13550 8854 12652 3082 574 -679 N ATOM 2377 N LYS A1104 -8.487 -48.046 11.555 1.00 50.30 N ANISOU 2377 N LYS A1104 7785 3699 7628 2676 -110 -730 N ATOM 2378 CA LYS A1104 -9.781 -47.397 11.371 1.00 61.25 C ANISOU 2378 CA LYS A1104 9222 5113 8938 2679 -216 -737 C ATOM 2379 C LYS A1104 -10.093 -46.444 12.519 1.00 53.22 C ANISOU 2379 C LYS A1104 8124 4164 7933 2671 -228 -673 C ATOM 2380 O LYS A1104 -10.625 -45.349 12.296 1.00 49.34 O ANISOU 2380 O LYS A1104 7672 3689 7385 2681 -263 -670 O ATOM 2381 CB LYS A1104 -10.881 -48.448 11.226 1.00 60.94 C ANISOU 2381 CB LYS A1104 9167 5007 8979 2678 -324 -765 C ATOM 2382 CG LYS A1104 -10.702 -49.341 10.009 1.00 64.67 C ANISOU 2382 CG LYS A1104 9778 5388 9407 2708 -371 -892 C ATOM 2383 CD LYS A1104 -11.808 -50.378 9.903 1.00102.14 C ANISOU 2383 CD LYS A1104 14482 10010 14315 2695 -549 -937 C ATOM 2384 CE LYS A1104 -11.624 -51.257 8.671 1.00106.25 C ANISOU 2384 CE LYS A1104 15188 10419 14765 2741 -650 -1127 C ATOM 2385 NZ LYS A1104 -10.361 -52.052 8.709 1.00 75.24 N ANISOU 2385 NZ LYS A1104 11252 6473 10862 2751 -461 -1157 N ATOM 2386 N TYR A1105 -9.772 -46.835 13.754 1.00 49.17 N ANISOU 2386 N TYR A1105 7524 3681 7476 2682 -208 -627 N ATOM 2387 CA TYR A1105 -9.974 -45.926 14.878 1.00 49.10 C ANISOU 2387 CA TYR A1105 7508 3735 7413 2726 -231 -608 C ATOM 2388 C TYR A1105 -9.088 -44.694 14.746 1.00 49.16 C ANISOU 2388 C TYR A1105 7552 3722 7404 2706 -254 -654 C ATOM 2389 O TYR A1105 -9.547 -43.565 14.943 1.00 49.63 O ANISOU 2389 O TYR A1105 7642 3791 7424 2723 -289 -681 O ATOM 2390 CB TYR A1105 -9.706 -46.632 16.208 1.00 49.52 C ANISOU 2390 CB TYR A1105 7524 3823 7467 2800 -230 -552 C ATOM 2391 CG TYR A1105 -9.743 -45.681 17.391 1.00 59.35 C ANISOU 2391 CG TYR A1105 8843 5133 8576 2902 -278 -579 C ATOM 2392 CD1 TYR A1105 -10.911 -45.003 17.724 1.00100.30 C ANISOU 2392 CD1 TYR A1105 14061 10361 13686 2973 -243 -576 C ATOM 2393 CD2 TYR A1105 -8.609 -45.446 18.164 1.00 86.37 C ANISOU 2393 CD2 TYR A1105 12314 8549 11955 2951 -379 -624 C ATOM 2394 CE1 TYR A1105 -10.954 -44.122 18.796 1.00 64.69 C ANISOU 2394 CE1 TYR A1105 9665 5901 9014 3103 -277 -639 C ATOM 2395 CE2 TYR A1105 -8.643 -44.568 19.243 1.00 80.48 C ANISOU 2395 CE2 TYR A1105 11694 7840 11046 3079 -479 -704 C ATOM 2396 CZ TYR A1105 -9.820 -43.912 19.554 1.00 70.73 C ANISOU 2396 CZ TYR A1105 10524 6661 9688 3162 -411 -723 C ATOM 2397 OH TYR A1105 -9.869 -43.038 20.621 1.00 90.25 O ANISOU 2397 OH TYR A1105 13164 9163 11963 3325 -496 -837 O ATOM 2398 N LEU A1106 -7.810 -44.896 14.415 1.00 53.66 N ANISOU 2398 N LEU A1106 8096 4231 8063 2681 -228 -649 N ATOM 2399 CA LEU A1106 -6.895 -43.777 14.213 1.00 51.17 C ANISOU 2399 CA LEU A1106 7767 3833 7843 2671 -245 -650 C ATOM 2400 C LEU A1106 -7.445 -42.787 13.191 1.00 50.02 C ANISOU 2400 C LEU A1106 7672 3661 7672 2664 -211 -640 C ATOM 2401 O LEU A1106 -7.469 -41.573 13.429 1.00 50.48 O ANISOU 2401 O LEU A1106 7725 3670 7784 2664 -267 -651 O ATOM 2402 CB LEU A1106 -5.525 -44.301 13.767 1.00 50.58 C ANISOU 2402 CB LEU A1106 7619 3660 7939 2670 -166 -594 C ATOM 2403 CG LEU A1106 -4.608 -43.274 13.090 1.00100.48 C ANISOU 2403 CG LEU A1106 13890 9837 14449 2680 -112 -528 C ATOM 2404 CD1 LEU A1106 -3.900 -42.394 14.114 1.00 63.28 C ANISOU 2404 CD1 LEU A1106 9107 5033 9904 2669 -283 -540 C ATOM 2405 CD2 LEU A1106 -3.606 -43.942 12.150 1.00 53.86 C ANISOU 2405 CD2 LEU A1106 7933 3843 8690 2725 65 -444 C ATOM 2406 N GLU A 219 -7.902 -43.296 12.046 1.00 50.42 N ANISOU 2406 N GLU A 219 8139 3158 7862 1483 -1141 -545 N ATOM 2407 CA GLU A 219 -8.403 -42.417 10.993 1.00 45.44 C ANISOU 2407 CA GLU A 219 7564 2603 7098 1445 -1019 -625 C ATOM 2408 C GLU A 219 -9.684 -41.710 11.417 1.00 43.22 C ANISOU 2408 C GLU A 219 7290 2435 6697 1265 -1128 -514 C ATOM 2409 O GLU A 219 -9.884 -40.537 11.087 1.00 41.56 O ANISOU 2409 O GLU A 219 7036 2349 6405 1237 -1032 -529 O ATOM 2410 CB GLU A 219 -8.624 -43.213 9.708 1.00 50.59 C ANISOU 2410 CB GLU A 219 8413 3119 7690 1474 -993 -758 C ATOM 2411 CG GLU A 219 -7.338 -43.671 9.039 1.00 61.74 C ANISOU 2411 CG GLU A 219 9816 4427 9217 1659 -806 -898 C ATOM 2412 CD GLU A 219 -7.567 -44.771 8.017 1.00 75.54 C ANISOU 2412 CD GLU A 219 11778 6005 10920 1685 -828 -1013 C ATOM 2413 OE1 GLU A 219 -8.741 -45.111 7.753 1.00 93.18 O ANISOU 2413 OE1 GLU A 219 14172 8211 13022 1557 -998 -986 O ATOM 2414 OE2 GLU A 219 -6.571 -45.301 7.480 1.00 73.53 O ANISOU 2414 OE2 GLU A 219 11529 5637 10772 1833 -673 -1132 O ATOM 2415 N ARG A 220 -10.563 -42.399 12.153 1.00 43.44 N ANISOU 2415 N ARG A 220 7367 2415 6723 1139 -1316 -400 N ATOM 2416 CA ARG A 220 -11.794 -41.753 12.602 1.00 44.64 C ANISOU 2416 CA ARG A 220 7503 2662 6796 963 -1394 -291 C ATOM 2417 C ARG A 220 -11.510 -40.698 13.665 1.00 39.66 C ANISOU 2417 C ARG A 220 6710 2178 6182 948 -1346 -190 C ATOM 2418 O ARG A 220 -12.113 -39.619 13.647 1.00 42.65 O ANISOU 2418 O ARG A 220 7041 2676 6489 868 -1305 -159 O ATOM 2419 CB ARG A 220 -12.784 -42.794 13.123 1.00 42.53 C ANISOU 2419 CB ARG A 220 7318 2295 6546 826 -1573 -193 C ATOM 2420 CG ARG A 220 -13.634 -43.425 12.037 1.00 62.53 C ANISOU 2420 CG ARG A 220 10007 4727 9025 767 -1653 -266 C ATOM 2421 CD ARG A 220 -14.585 -44.461 12.610 1.00122.65 C ANISOU 2421 CD ARG A 220 17677 12238 16685 627 -1824 -163 C ATOM 2422 NE ARG A 220 -15.240 -45.235 11.559 1.00116.31 N ANISOU 2422 NE ARG A 220 17027 11315 15852 591 -1926 -242 N ATOM 2423 CZ ARG A 220 -16.030 -46.279 11.783 1.00105.55 C ANISOU 2423 CZ ARG A 220 15733 9832 14539 483 -2080 -181 C ATOM 2424 NH1 ARG A 220 -16.266 -46.682 13.024 1.00120.04 N ANISOU 2424 NH1 ARG A 220 17509 11651 16450 396 -2130 -39 N ATOM 2425 NH2 ARG A 220 -16.582 -46.924 10.764 1.00110.23 N ANISOU 2425 NH2 ARG A 220 16467 10315 15100 459 -2185 -261 N ATOM 2426 N ALA A 221 -10.590 -40.988 14.591 1.00 40.23 N ANISOU 2426 N ALA A 221 6701 2237 6346 1024 -1365 -141 N ATOM 2427 CA ALA A 221 -10.212 -40.006 15.605 1.00 43.87 C ANISOU 2427 CA ALA A 221 7021 2832 6817 1019 -1336 -53 C ATOM 2428 C ALA A 221 -9.600 -38.765 14.970 1.00 43.67 C ANISOU 2428 C ALA A 221 6890 2924 6777 1107 -1168 -140 C ATOM 2429 O ALA A 221 -9.920 -37.632 15.358 1.00 38.89 O ANISOU 2429 O ALA A 221 6208 2452 6117 1045 -1132 -83 O ATOM 2430 CB ALA A 221 -9.233 -40.634 16.600 1.00 40.06 C ANISOU 2430 CB ALA A 221 6489 2295 6438 1096 -1415 -2 C ATOM 2431 N ARG A 222 -8.711 -38.963 13.995 1.00 38.64 N ANISOU 2431 N ARG A 222 6253 2234 6195 1251 -1048 -278 N ATOM 2432 CA ARG A 222 -8.138 -37.846 13.253 1.00 39.45 C ANISOU 2432 CA ARG A 222 6274 2433 6283 1330 -855 -370 C ATOM 2433 C ARG A 222 -9.224 -37.044 12.553 1.00 43.44 C ANISOU 2433 C ARG A 222 6861 3010 6634 1223 -826 -388 C ATOM 2434 O ARG A 222 -9.196 -35.808 12.556 1.00 37.34 O ANISOU 2434 O ARG A 222 6002 2367 5818 1212 -737 -382 O ATOM 2435 CB ARG A 222 -7.125 -38.379 12.243 1.00 45.60 C ANISOU 2435 CB ARG A 222 7073 3111 7142 1485 -702 -517 C ATOM 2436 CG ARG A 222 -6.369 -37.338 11.452 1.00 47.62 C ANISOU 2436 CG ARG A 222 7242 3446 7404 1573 -459 -618 C ATOM 2437 CD ARG A 222 -5.436 -38.040 10.468 1.00 58.06 C ANISOU 2437 CD ARG A 222 8603 4639 8817 1713 -283 -761 C ATOM 2438 NE ARG A 222 -4.607 -39.049 11.126 1.00 89.29 N ANISOU 2438 NE ARG A 222 12495 8491 12940 1813 -352 -733 N ATOM 2439 CZ ARG A 222 -3.900 -39.976 10.484 1.00107.80 C ANISOU 2439 CZ ARG A 222 14890 10686 15383 1935 -248 -834 C ATOM 2440 NH1 ARG A 222 -3.923 -40.034 9.159 1.00102.90 N ANISOU 2440 NH1 ARG A 222 14386 9999 14712 1960 -60 -979 N ATOM 2441 NH2 ARG A 222 -3.172 -40.849 11.166 1.00 85.88 N ANISOU 2441 NH2 ARG A 222 12050 7822 12758 2025 -342 -799 N ATOM 2442 N SER A 223 -10.198 -37.735 11.953 1.00 43.57 N ANISOU 2442 N SER A 223 7043 2939 6572 1140 -917 -408 N ATOM 2443 CA SER A 223 -11.260 -37.046 11.228 1.00 35.84 C ANISOU 2443 CA SER A 223 6149 2014 5454 1035 -922 -427 C ATOM 2444 C SER A 223 -12.140 -36.232 12.167 1.00 38.94 C ANISOU 2444 C SER A 223 6454 2518 5824 899 -998 -290 C ATOM 2445 O SER A 223 -12.617 -35.155 11.795 1.00 37.77 O ANISOU 2445 O SER A 223 6293 2464 5592 851 -951 -299 O ATOM 2446 CB SER A 223 -12.097 -38.054 10.446 1.00 45.85 C ANISOU 2446 CB SER A 223 7603 3154 6664 972 -1038 -470 C ATOM 2447 OG SER A 223 -13.306 -37.472 9.994 1.00 53.98 O ANISOU 2447 OG SER A 223 8695 4229 7586 842 -1109 -452 O ATOM 2448 N THR A 224 -12.379 -36.730 13.380 1.00 35.41 N ANISOU 2448 N THR A 224 5955 2054 5444 832 -1106 -162 N ATOM 2449 CA THR A 224 -13.152 -35.955 14.344 1.00 52.75 C ANISOU 2449 CA THR A 224 8069 4351 7621 703 -1140 -28 C ATOM 2450 C THR A 224 -12.392 -34.707 14.778 1.00 42.14 C ANISOU 2450 C THR A 224 6589 3145 6276 772 -1032 -18 C ATOM 2451 O THR A 224 -12.966 -33.619 14.827 1.00 33.05 O ANISOU 2451 O THR A 224 5390 2097 5069 704 -996 16 O ATOM 2452 CB THR A 224 -13.517 -36.824 15.547 1.00 40.30 C ANISOU 2452 CB THR A 224 6500 2717 6097 615 -1251 105 C ATOM 2453 OG1 THR A 224 -14.414 -37.856 15.125 1.00 45.28 O ANISOU 2453 OG1 THR A 224 7241 3228 6735 526 -1352 103 O ATOM 2454 CG2 THR A 224 -14.194 -36.000 16.627 1.00 48.19 C ANISOU 2454 CG2 THR A 224 7421 3819 7071 491 -1243 245 C ATOM 2455 N LEU A 225 -11.095 -34.836 15.069 1.00 34.85 N ANISOU 2455 N LEU A 225 5592 2222 5429 907 -984 -49 N ATOM 2456 CA LEU A 225 -10.309 -33.663 15.447 1.00 30.58 C ANISOU 2456 CA LEU A 225 4904 1809 4905 974 -892 -45 C ATOM 2457 C LEU A 225 -10.259 -32.640 14.323 1.00 35.99 C ANISOU 2457 C LEU A 225 5582 2566 5528 1015 -748 -153 C ATOM 2458 O LEU A 225 -10.359 -31.431 14.567 1.00 35.70 O ANISOU 2458 O LEU A 225 5460 2651 5453 991 -698 -123 O ATOM 2459 CB LEU A 225 -8.895 -34.086 15.847 1.00 33.04 C ANISOU 2459 CB LEU A 225 5121 2090 5342 1110 -878 -70 C ATOM 2460 CG LEU A 225 -8.704 -34.242 17.352 1.00 59.63 C ANISOU 2460 CG LEU A 225 8440 5475 8741 1069 -1007 63 C ATOM 2461 CD1 LEU A 225 -7.438 -35.017 17.646 1.00 65.90 C ANISOU 2461 CD1 LEU A 225 9177 6192 9671 1193 -1048 33 C ATOM 2462 CD2 LEU A 225 -8.673 -32.863 18.001 1.00 49.87 C ANISOU 2462 CD2 LEU A 225 7094 4391 7462 1034 -972 123 C ATOM 2463 N GLN A 226 -10.109 -33.098 13.081 1.00 38.81 N ANISOU 2463 N GLN A 226 6043 2844 5859 1074 -676 -280 N ATOM 2464 CA GLN A 226 -10.030 -32.147 11.978 1.00 42.52 C ANISOU 2464 CA GLN A 226 6543 3375 6238 1107 -527 -385 C ATOM 2465 C GLN A 226 -11.341 -31.388 11.802 1.00 42.85 C ANISOU 2465 C GLN A 226 6652 3476 6152 972 -592 -340 C ATOM 2466 O GLN A 226 -11.326 -30.198 11.470 1.00 33.09 O ANISOU 2466 O GLN A 226 5385 2343 4845 977 -497 -367 O ATOM 2467 CB GLN A 226 -9.622 -32.878 10.698 1.00 38.85 C ANISOU 2467 CB GLN A 226 6211 2803 5748 1186 -432 -527 C ATOM 2468 CG GLN A 226 -8.187 -33.396 10.770 1.00 55.74 C ANISOU 2468 CG GLN A 226 8243 4889 8046 1334 -312 -584 C ATOM 2469 CD GLN A 226 -7.812 -34.294 9.606 1.00122.39 C ANISOU 2469 CD GLN A 226 16819 13199 16485 1407 -217 -721 C ATOM 2470 OE1 GLN A 226 -8.673 -34.749 8.853 1.00110.07 O ANISOU 2470 OE1 GLN A 226 15455 11574 14793 1342 -291 -759 O ATOM 2471 NE2 GLN A 226 -6.516 -34.555 9.456 1.00 72.94 N ANISOU 2471 NE2 GLN A 226 10447 6889 10377 1540 -54 -792 N ATOM 2472 N LYS A 227 -12.478 -32.042 12.060 1.00 35.66 N ANISOU 2472 N LYS A 227 5817 2502 5230 846 -752 -267 N ATOM 2473 CA LYS A 227 -13.764 -31.348 12.006 1.00 37.09 C ANISOU 2473 CA LYS A 227 6017 2732 5343 706 -824 -210 C ATOM 2474 C LYS A 227 -13.906 -30.339 13.143 1.00 31.59 C ANISOU 2474 C LYS A 227 5168 2155 4678 657 -811 -94 C ATOM 2475 O LYS A 227 -14.517 -29.273 12.970 1.00 31.05 O ANISOU 2475 O LYS A 227 5043 2214 4540 581 -771 -76 O ATOM 2476 CB LYS A 227 -14.904 -32.365 12.043 1.00 38.57 C ANISOU 2476 CB LYS A 227 6282 2818 5556 578 -985 -158 C ATOM 2477 CG LYS A 227 -15.013 -33.187 10.774 1.00 45.46 C ANISOU 2477 CG LYS A 227 7328 3578 6367 604 -1026 -274 C ATOM 2478 CD LYS A 227 -16.186 -34.139 10.820 1.00 60.11 C ANISOU 2478 CD LYS A 227 9238 5336 8266 471 -1201 -219 C ATOM 2479 CE LYS A 227 -16.273 -34.938 9.529 1.00 85.83 C ANISOU 2479 CE LYS A 227 12684 8479 11447 503 -1261 -337 C ATOM 2480 NZ LYS A 227 -17.360 -35.953 9.572 1.00139.07 N ANISOU 2480 NZ LYS A 227 19472 15117 18252 381 -1446 -286 N ATOM 2481 N GLU A 228 -13.383 -30.672 14.321 1.00 33.58 N ANISOU 2481 N GLU A 228 5330 2418 5010 676 -830 -7 N ATOM 2482 CA GLU A 228 -13.385 -29.721 15.427 1.00 27.91 C ANISOU 2482 CA GLU A 228 4470 1849 4287 627 -792 100 C ATOM 2483 C GLU A 228 -12.490 -28.526 15.130 1.00 23.57 C ANISOU 2483 C GLU A 228 3805 1451 3699 714 -648 34 C ATOM 2484 O GLU A 228 -12.867 -27.382 15.408 1.00 29.40 O ANISOU 2484 O GLU A 228 4451 2346 4375 645 -588 77 O ATOM 2485 CB GLU A 228 -12.941 -30.410 16.718 1.00 39.62 C ANISOU 2485 CB GLU A 228 5937 3275 5842 637 -872 203 C ATOM 2486 CG GLU A 228 -14.069 -31.010 17.530 1.00 62.02 C ANISOU 2486 CG GLU A 228 8824 6065 8675 479 -952 333 C ATOM 2487 CD GLU A 228 -13.568 -31.652 18.806 1.00108.34 C ANISOU 2487 CD GLU A 228 14700 11904 14559 481 -1005 428 C ATOM 2488 OE1 GLU A 228 -12.965 -32.742 18.722 1.00 46.88 O ANISOU 2488 OE1 GLU A 228 6966 4021 6826 549 -1064 391 O ATOM 2489 OE2 GLU A 228 -13.759 -31.059 19.889 1.00 65.58 O ANISOU 2489 OE2 GLU A 228 9257 6562 9098 416 -990 538 O ATOM 2490 N VAL A 229 -11.307 -28.761 14.551 1.00 28.88 N ANISOU 2490 N VAL A 229 4477 2072 4423 865 -579 -74 N ATOM 2491 CA VAL A 229 -10.479 -27.630 14.130 1.00 24.70 C ANISOU 2491 CA VAL A 229 3839 1672 3875 936 -417 -141 C ATOM 2492 C VAL A 229 -11.231 -26.779 13.116 1.00 31.88 C ANISOU 2492 C VAL A 229 4813 2659 4640 866 -341 -190 C ATOM 2493 O VAL A 229 -11.237 -25.544 13.198 1.00 28.11 O ANISOU 2493 O VAL A 229 4238 2335 4108 830 -259 -170 O ATOM 2494 CB VAL A 229 -9.134 -28.116 13.559 1.00 37.14 C ANISOU 2494 CB VAL A 229 5398 3153 5559 1108 -324 -259 C ATOM 2495 CG1 VAL A 229 -8.330 -26.939 13.009 1.00 30.52 C ANISOU 2495 CG1 VAL A 229 4448 2437 4712 1164 -126 -330 C ATOM 2496 CG2 VAL A 229 -8.355 -28.843 14.615 1.00 34.34 C ANISOU 2496 CG2 VAL A 229 4947 2743 5357 1164 -417 -199 C ATOM 2497 N HIS A 230 -11.894 -27.426 12.154 1.00 24.96 N ANISOU 2497 N HIS A 230 4119 1665 3701 845 -390 -251 N ATOM 2498 CA HIS A 230 -12.600 -26.676 11.118 1.00 29.43 C ANISOU 2498 CA HIS A 230 4783 2273 4126 785 -357 -301 C ATOM 2499 C HIS A 230 -13.730 -25.845 11.713 1.00 35.22 C ANISOU 2499 C HIS A 230 5423 3126 4834 641 -429 -193 C ATOM 2500 O HIS A 230 -13.947 -24.699 11.306 1.00 25.36 O ANISOU 2500 O HIS A 230 4149 1987 3500 609 -365 -205 O ATOM 2501 CB HIS A 230 -13.137 -27.634 10.054 1.00 30.21 C ANISOU 2501 CB HIS A 230 5122 2191 4167 785 -448 -384 C ATOM 2502 CG HIS A 230 -13.631 -26.949 8.818 1.00102.46 C ANISOU 2502 CG HIS A 230 14430 11345 13154 753 -426 -458 C ATOM 2503 ND1 HIS A 230 -14.953 -26.601 8.636 1.00 62.40 N ANISOU 2503 ND1 HIS A 230 9395 6277 8038 621 -578 -410 N ATOM 2504 CD2 HIS A 230 -12.981 -26.551 7.699 1.00 43.46 C ANISOU 2504 CD2 HIS A 230 7102 3856 5554 836 -272 -574 C ATOM 2505 CE1 HIS A 230 -15.094 -26.018 7.459 1.00 55.67 C ANISOU 2505 CE1 HIS A 230 8716 5406 7029 626 -553 -491 C ATOM 2506 NE2 HIS A 230 -13.912 -25.974 6.871 1.00 76.00 N ANISOU 2506 NE2 HIS A 230 11366 7978 9532 747 -354 -586 N ATOM 2507 N ALA A 231 -14.458 -26.405 12.682 1.00 25.80 N ANISOU 2507 N ALA A 231 4179 1903 3719 553 -549 -87 N ATOM 2508 CA ALA A 231 -15.544 -25.666 13.313 1.00 29.44 C ANISOU 2508 CA ALA A 231 4537 2466 4183 420 -584 12 C ATOM 2509 C ALA A 231 -15.012 -24.535 14.189 1.00 28.84 C ANISOU 2509 C ALA A 231 4301 2564 4094 433 -475 64 C ATOM 2510 O ALA A 231 -15.623 -23.458 14.261 1.00 24.21 O ANISOU 2510 O ALA A 231 3639 2092 3468 365 -443 93 O ATOM 2511 CB ALA A 231 -16.412 -26.618 14.133 1.00 27.93 C ANISOU 2511 CB ALA A 231 4345 2182 4087 319 -701 113 C ATOM 2512 N ALA A 232 -13.886 -24.762 14.878 1.00 24.27 N ANISOU 2512 N ALA A 232 3668 1993 3559 520 -436 76 N ATOM 2513 CA ALA A 232 -13.308 -23.685 15.676 1.00 23.29 C ANISOU 2513 CA ALA A 232 3408 2017 3426 534 -360 117 C ATOM 2514 C ALA A 232 -12.796 -22.561 14.783 1.00 24.28 C ANISOU 2514 C ALA A 232 3497 2238 3491 582 -239 32 C ATOM 2515 O ALA A 232 -12.882 -21.389 15.158 1.00 22.40 O ANISOU 2515 O ALA A 232 3165 2131 3215 545 -187 65 O ATOM 2516 CB ALA A 232 -12.184 -24.207 16.575 1.00 25.76 C ANISOU 2516 CB ALA A 232 3675 2290 3821 620 -388 145 C ATOM 2517 N LYS A 233 -12.254 -22.894 13.602 1.00 21.89 N ANISOU 2517 N LYS A 233 3285 1860 3171 664 -180 -76 N ATOM 2518 CA LYS A 233 -11.838 -21.842 12.678 1.00 22.81 C ANISOU 2518 CA LYS A 233 3405 2051 3209 694 -45 -150 C ATOM 2519 C LYS A 233 -13.029 -21.018 12.216 1.00 25.11 C ANISOU 2519 C LYS A 233 3748 2398 3393 590 -82 -133 C ATOM 2520 O LYS A 233 -12.943 -19.789 12.116 1.00 20.13 O ANISOU 2520 O LYS A 233 3058 1881 2711 572 -7 -130 O ATOM 2521 CB LYS A 233 -11.096 -22.435 11.476 1.00 28.77 C ANISOU 2521 CB LYS A 233 4292 2694 3947 797 52 -272 C ATOM 2522 CG LYS A 233 -9.717 -22.972 11.828 1.00 64.11 C ANISOU 2522 CG LYS A 233 8666 7123 8568 922 129 -307 C ATOM 2523 CD LYS A 233 -8.915 -23.370 10.599 1.00 72.64 C ANISOU 2523 CD LYS A 233 9859 8102 9637 1032 289 -440 C ATOM 2524 CE LYS A 233 -7.521 -23.853 10.997 1.00 57.98 C ANISOU 2524 CE LYS A 233 7851 6195 7984 1164 370 -477 C ATOM 2525 NZ LYS A 233 -6.755 -24.413 9.846 1.00 75.53 N ANISOU 2525 NZ LYS A 233 10165 8314 10219 1261 537 -612 N ATOM 2526 N SER A 234 -14.154 -21.671 11.931 1.00 18.16 N ANISOU 2526 N SER A 234 2971 1428 2500 520 -214 -120 N ATOM 2527 CA SER A 234 -15.332 -20.915 11.513 1.00 18.69 C ANISOU 2527 CA SER A 234 3063 1529 2509 425 -282 -103 C ATOM 2528 C SER A 234 -15.783 -19.946 12.602 1.00 19.40 C ANISOU 2528 C SER A 234 2974 1759 2640 357 -268 -10 C ATOM 2529 O SER A 234 -16.086 -18.777 12.324 1.00 21.76 O ANISOU 2529 O SER A 234 3240 2141 2885 329 -240 -13 O ATOM 2530 CB SER A 234 -16.467 -21.871 11.152 1.00 23.27 C ANISOU 2530 CB SER A 234 3748 1969 3123 355 -452 -98 C ATOM 2531 OG SER A 234 -16.076 -22.742 10.101 1.00 29.16 O ANISOU 2531 OG SER A 234 4697 2572 3810 420 -473 -195 O ATOM 2532 N ALA A 235 -15.823 -20.412 13.855 1.00 21.72 N ANISOU 2532 N ALA A 235 3171 2066 3017 333 -285 72 N ATOM 2533 CA ALA A 235 -16.203 -19.538 14.957 1.00 19.15 C ANISOU 2533 CA ALA A 235 2708 1859 2709 275 -250 154 C ATOM 2534 C ALA A 235 -15.211 -18.389 15.130 1.00 23.57 C ANISOU 2534 C ALA A 235 3196 2542 3219 333 -144 134 C ATOM 2535 O ALA A 235 -15.611 -17.246 15.399 1.00 18.14 O ANISOU 2535 O ALA A 235 2435 1953 2504 293 -110 158 O ATOM 2536 CB ALA A 235 -16.322 -20.359 16.242 1.00 22.01 C ANISOU 2536 CB ALA A 235 3040 2188 3136 241 -279 245 C ATOM 2537 N ALA A 236 -13.910 -18.671 14.981 1.00 21.27 N ANISOU 2537 N ALA A 236 2910 2232 2938 429 -91 88 N ATOM 2538 CA ALA A 236 -12.899 -17.624 15.121 1.00 17.99 C ANISOU 2538 CA ALA A 236 2407 1916 2513 478 5 69 C ATOM 2539 C ALA A 236 -13.018 -16.578 14.018 1.00 15.37 C ANISOU 2539 C ALA A 236 2112 1631 2098 470 77 12 C ATOM 2540 O ALA A 236 -12.755 -15.392 14.251 1.00 19.50 O ANISOU 2540 O ALA A 236 2556 2253 2600 459 135 23 O ATOM 2541 CB ALA A 236 -11.493 -18.236 15.111 1.00 16.52 C ANISOU 2541 CB ALA A 236 2193 1677 2408 585 46 26 C ATOM 2542 N ILE A 237 -13.387 -16.999 12.806 1.00 18.55 N ANISOU 2542 N ILE A 237 2659 1948 2442 473 66 -49 N ATOM 2543 CA ILE A 237 -13.601 -16.041 11.724 1.00 17.67 C ANISOU 2543 CA ILE A 237 2634 1857 2222 456 111 -95 C ATOM 2544 C ILE A 237 -14.700 -15.057 12.101 1.00 23.80 C ANISOU 2544 C ILE A 237 3348 2708 2987 371 38 -38 C ATOM 2545 O ILE A 237 -14.583 -13.853 11.863 1.00 16.53 O ANISOU 2545 O ILE A 237 2408 1859 2013 361 92 -43 O ATOM 2546 CB ILE A 237 -13.929 -16.773 10.412 1.00 20.43 C ANISOU 2546 CB ILE A 237 3199 2073 2489 468 71 -167 C ATOM 2547 CG1 ILE A 237 -12.691 -17.541 9.915 1.00 24.52 C ANISOU 2547 CG1 ILE A 237 3785 2519 3014 570 199 -244 C ATOM 2548 CG2 ILE A 237 -14.478 -15.793 9.357 1.00 19.99 C ANISOU 2548 CG2 ILE A 237 3277 2016 2301 428 56 -196 C ATOM 2549 CD1 ILE A 237 -12.997 -18.530 8.774 1.00 30.10 C ANISOU 2549 CD1 ILE A 237 4734 3067 3635 592 152 -321 C ATOM 2550 N AILE A 238 -15.778 -15.541 12.710 0.53 25.69 N ANISOU 2550 N AILE A 238 3546 2924 3292 309 -73 16 N ATOM 2551 N BILE A 238 -15.805 -15.579 12.648 0.47 13.47 N ANISOU 2551 N BILE A 238 2006 1370 1742 309 -78 13 N ATOM 2552 CA AILE A 238 -16.870 -14.637 13.058 0.53 12.81 C ANISOU 2552 CA AILE A 238 1835 1350 1683 237 -124 62 C ATOM 2553 CA BILE A 238 -16.908 -14.744 13.126 0.47 24.60 C ANISOU 2553 CA BILE A 238 3324 2838 3184 235 -129 66 C ATOM 2554 C AILE A 238 -16.468 -13.703 14.198 0.53 20.46 C ANISOU 2554 C AILE A 238 2665 2444 2666 239 -38 108 C ATOM 2555 C BILE A 238 -16.408 -13.724 14.146 0.47 11.88 C ANISOU 2555 C BILE A 238 1583 1354 1576 242 -36 104 C ATOM 2556 O AILE A 238 -16.846 -12.526 14.214 0.53 29.20 O ANISOU 2556 O AILE A 238 3724 3616 3754 214 -26 114 O ATOM 2557 O BILE A 238 -16.673 -12.521 14.038 0.47 11.35 O ANISOU 2557 O BILE A 238 1481 1351 1479 224 -19 104 O ATOM 2558 CB AILE A 238 -18.127 -15.452 13.383 0.53 27.28 C ANISOU 2558 CB AILE A 238 3642 3109 3616 166 -238 105 C ATOM 2559 CB BILE A 238 -18.014 -15.631 13.728 0.47 13.28 C ANISOU 2559 CB BILE A 238 1846 1343 1858 167 -222 121 C ATOM 2560 CG1AILE A 238 -18.697 -15.989 12.076 0.53 16.94 C ANISOU 2560 CG1AILE A 238 2482 1670 2285 152 -366 51 C ATOM 2561 CG1BILE A 238 -18.608 -16.554 12.663 0.47 37.79 C ANISOU 2561 CG1BILE A 238 5082 4304 4972 148 -351 79 C ATOM 2562 CG2AILE A 238 -19.150 -14.603 14.111 0.53 12.89 C ANISOU 2562 CG2AILE A 238 1680 1350 1867 100 -243 161 C ATOM 2563 CG2BILE A 238 -19.093 -14.781 14.367 0.47 17.97 C ANISOU 2563 CG2BILE A 238 2311 1996 2521 99 -231 173 C ATOM 2564 CD1AILE A 238 -19.685 -17.058 12.275 0.53 23.25 C ANISOU 2564 CD1AILE A 238 3267 2364 3203 87 -486 84 C ATOM 2565 CD1BILE A 238 -19.504 -15.843 11.680 0.47 30.12 C ANISOU 2565 CD1BILE A 238 4165 3297 3984 111 -460 49 C ATOM 2566 N ALA A 239 -15.688 -14.198 15.163 1.00 17.27 N ANISOU 2566 N ALA A 239 2209 2060 2294 270 3 138 N ATOM 2567 CA ALA A 239 -15.171 -13.297 16.186 1.00 18.79 C ANISOU 2567 CA ALA A 239 2307 2352 2481 277 60 172 C ATOM 2568 C ALA A 239 -14.199 -12.284 15.583 1.00 19.02 C ANISOU 2568 C ALA A 239 2325 2434 2467 320 133 123 C ATOM 2569 O ALA A 239 -14.232 -11.097 15.930 1.00 16.00 O ANISOU 2569 O ALA A 239 1887 2129 2063 302 160 135 O ATOM 2570 CB ALA A 239 -14.503 -14.099 17.305 1.00 17.36 C ANISOU 2570 CB ALA A 239 2104 2153 2338 303 48 216 C ATOM 2571 N GLY A 240 -13.357 -12.721 14.642 1.00 14.15 N ANISOU 2571 N GLY A 240 1769 1766 1843 375 179 65 N ATOM 2572 CA GLY A 240 -12.428 -11.792 14.020 1.00 13.02 C ANISOU 2572 CA GLY A 240 1615 1660 1672 405 283 23 C ATOM 2573 C GLY A 240 -13.128 -10.748 13.160 1.00 13.14 C ANISOU 2573 C GLY A 240 1705 1693 1594 360 286 8 C ATOM 2574 O GLY A 240 -12.698 -9.595 13.100 1.00 13.30 O ANISOU 2574 O GLY A 240 1690 1772 1593 353 348 6 O ATOM 2575 N LEU A 241 -14.212 -11.135 12.487 1.00 12.02 N ANISOU 2575 N LEU A 241 1672 1487 1408 328 198 -2 N ATOM 2576 CA LEU A 241 -14.964 -10.174 11.688 1.00 11.93 C ANISOU 2576 CA LEU A 241 1742 1470 1320 288 154 -11 C ATOM 2577 C LEU A 241 -15.682 -9.163 12.569 1.00 11.83 C ANISOU 2577 C LEU A 241 1604 1536 1353 247 112 38 C ATOM 2578 O LEU A 241 -15.822 -7.993 12.189 1.00 12.63 O ANISOU 2578 O LEU A 241 1727 1664 1409 231 114 34 O ATOM 2579 CB LEU A 241 -15.975 -10.900 10.800 1.00 15.06 C ANISOU 2579 CB LEU A 241 2282 1755 1685 264 25 -34 C ATOM 2580 CG LEU A 241 -15.301 -11.605 9.608 1.00 22.82 C ANISOU 2580 CG LEU A 241 3463 2641 2567 308 79 -102 C ATOM 2581 CD1 LEU A 241 -16.289 -12.491 8.890 1.00 26.06 C ANISOU 2581 CD1 LEU A 241 4023 2924 2955 284 -83 -125 C ATOM 2582 CD2 LEU A 241 -14.679 -10.592 8.643 1.00 25.88 C ANISOU 2582 CD2 LEU A 241 3980 3031 2823 318 187 -135 C ATOM 2583 N PHE A 242 -16.155 -9.591 13.741 1.00 13.05 N ANISOU 2583 N PHE A 242 1645 1719 1594 229 82 83 N ATOM 2584 CA PHE A 242 -16.699 -8.626 14.691 1.00 15.54 C ANISOU 2584 CA PHE A 242 1851 2108 1945 201 84 121 C ATOM 2585 C PHE A 242 -15.645 -7.584 15.053 1.00 12.75 C ANISOU 2585 C PHE A 242 1458 1831 1555 225 166 117 C ATOM 2586 O PHE A 242 -15.917 -6.378 15.059 1.00 11.01 O ANISOU 2586 O PHE A 242 1217 1648 1317 209 167 117 O ATOM 2587 CB PHE A 242 -17.224 -9.347 15.945 1.00 14.19 C ANISOU 2587 CB PHE A 242 1601 1944 1847 177 80 172 C ATOM 2588 CG PHE A 242 -17.817 -8.408 16.987 1.00 12.96 C ANISOU 2588 CG PHE A 242 1357 1852 1716 152 116 204 C ATOM 2589 CD1 PHE A 242 -19.189 -8.201 17.055 1.00 11.84 C ANISOU 2589 CD1 PHE A 242 1156 1686 1657 111 87 217 C ATOM 2590 CD2 PHE A 242 -17.001 -7.724 17.866 1.00 14.65 C ANISOU 2590 CD2 PHE A 242 1546 2134 1885 174 173 214 C ATOM 2591 CE1 PHE A 242 -19.735 -7.329 18.000 1.00 11.65 C ANISOU 2591 CE1 PHE A 242 1054 1710 1662 98 150 235 C ATOM 2592 CE2 PHE A 242 -17.535 -6.853 18.816 1.00 15.94 C ANISOU 2592 CE2 PHE A 242 1663 2343 2051 157 214 232 C ATOM 2593 CZ PHE A 242 -18.898 -6.648 18.884 1.00 13.80 C ANISOU 2593 CZ PHE A 242 1337 2053 1853 123 219 240 C ATOM 2594 N ALA A 243 -14.428 -8.032 15.367 1.00 12.64 N ANISOU 2594 N ALA A 243 1425 1828 1551 263 221 112 N ATOM 2595 CA ALA A 243 -13.368 -7.086 15.714 1.00 13.85 C ANISOU 2595 CA ALA A 243 1520 2038 1706 279 280 108 C ATOM 2596 C ALA A 243 -13.048 -6.156 14.535 1.00 10.57 C ANISOU 2596 C ALA A 243 1164 1616 1236 273 336 74 C ATOM 2597 O ALA A 243 -12.923 -4.935 14.704 1.00 15.49 O ANISOU 2597 O ALA A 243 1757 2282 1846 253 351 80 O ATOM 2598 CB ALA A 243 -12.123 -7.856 16.170 1.00 13.24 C ANISOU 2598 CB ALA A 243 1391 1946 1692 325 305 106 C ATOM 2599 N ALEU A 244 -12.943 -6.725 13.331 0.52 24.78 N ANISOU 2599 N ALEU A 244 3076 3351 2990 286 369 38 N ATOM 2600 N BLEU A 244 -12.943 -6.711 13.326 0.48 9.77 N ANISOU 2600 N BLEU A 244 1175 1450 1088 285 369 38 N ATOM 2601 CA ALEU A 244 -12.623 -5.937 12.148 0.52 16.55 C ANISOU 2601 CA ALEU A 244 2142 2282 1865 274 440 10 C ATOM 2602 CA BLEU A 244 -12.604 -5.882 12.176 0.48 13.02 C ANISOU 2602 CA BLEU A 244 1690 1838 1419 274 442 11 C ATOM 2603 C ALEU A 244 -13.671 -4.861 11.894 0.52 30.74 C ANISOU 2603 C ALEU A 244 3991 4083 3605 231 354 27 C ATOM 2604 C BLEU A 244 -13.675 -4.833 11.909 0.48 14.56 C ANISOU 2604 C BLEU A 244 1940 2036 1556 230 353 27 C ATOM 2605 O ALEU A 244 -13.335 -3.734 11.514 0.52 13.83 O ANISOU 2605 O ALEU A 244 1882 1952 1419 211 400 28 O ATOM 2606 O BLEU A 244 -13.362 -3.701 11.526 0.48 13.80 O ANISOU 2606 O BLEU A 244 1878 1949 1415 210 397 29 O ATOM 2607 CB ALEU A 244 -12.501 -6.861 10.935 0.52 11.26 C ANISOU 2607 CB ALEU A 244 1634 1520 1124 297 482 -35 C ATOM 2608 CB BLEU A 244 -12.397 -6.754 10.939 0.48 16.05 C ANISOU 2608 CB BLEU A 244 2235 2132 1731 297 495 -35 C ATOM 2609 CG ALEU A 244 -12.221 -6.246 9.564 0.52 17.51 C ANISOU 2609 CG ALEU A 244 2613 2255 1785 283 572 -66 C ATOM 2610 CG BLEU A 244 -11.052 -7.467 10.832 0.48 24.39 C ANISOU 2610 CG BLEU A 244 3250 3168 2848 350 641 -69 C ATOM 2611 CD1ALEU A 244 -10.888 -5.514 9.563 0.52 20.98 C ANISOU 2611 CD1ALEU A 244 2976 2730 2264 287 752 -69 C ATOM 2612 CD1BLEU A 244 -11.014 -8.244 9.543 0.48 14.73 C ANISOU 2612 CD1BLEU A 244 2229 1842 1524 375 704 -124 C ATOM 2613 CD2ALEU A 244 -12.245 -7.319 8.473 0.52 14.33 C ANISOU 2613 CD2ALEU A 244 2410 1745 1289 310 597 -118 C ATOM 2614 CD2BLEU A 244 -9.903 -6.466 10.890 0.48 30.06 C ANISOU 2614 CD2BLEU A 244 3874 3928 3619 345 779 -67 C ATOM 2615 N CYS A 245 -14.948 -5.186 12.095 1.00 12.32 N ANISOU 2615 N CYS A 245 1657 1730 1293 215 226 40 N ATOM 2616 CA CYS A 245 -16.002 -4.232 11.768 1.00 12.11 C ANISOU 2616 CA CYS A 245 1667 1685 1249 185 125 49 C ATOM 2617 C CYS A 245 -16.165 -3.159 12.834 1.00 11.94 C ANISOU 2617 C CYS A 245 1511 1739 1286 177 131 74 C ATOM 2618 O CYS A 245 -16.587 -2.041 12.516 1.00 12.24 O ANISOU 2618 O CYS A 245 1579 1766 1305 162 85 76 O ATOM 2619 CB CYS A 245 -17.338 -4.940 11.589 1.00 15.18 C ANISOU 2619 CB CYS A 245 2070 2008 1690 170 -18 52 C ATOM 2620 SG CYS A 245 -17.376 -5.993 10.094 1.00 18.81 S ANISOU 2620 SG CYS A 245 2757 2340 2049 173 -81 11 S ATOM 2621 N TRP A 246 -15.891 -3.483 14.103 1.00 11.36 N ANISOU 2621 N TRP A 246 1311 1728 1276 188 173 93 N ATOM 2622 CA TRP A 246 -16.115 -2.510 15.171 1.00 10.92 C ANISOU 2622 CA TRP A 246 1164 1730 1255 183 178 109 C ATOM 2623 C TRP A 246 -14.873 -1.716 15.541 1.00 11.62 C ANISOU 2623 C TRP A 246 1228 1865 1323 188 244 107 C ATOM 2624 O TRP A 246 -15.008 -0.612 16.071 1.00 10.15 O ANISOU 2624 O TRP A 246 1011 1705 1141 181 235 109 O ATOM 2625 CB TRP A 246 -16.625 -3.200 16.445 1.00 10.16 C ANISOU 2625 CB TRP A 246 984 1659 1217 185 183 134 C ATOM 2626 CG TRP A 246 -18.085 -3.560 16.347 1.00 9.88 C ANISOU 2626 CG TRP A 246 920 1581 1253 166 127 141 C ATOM 2627 CD1 TRP A 246 -18.611 -4.760 15.977 1.00 12.41 C ANISOU 2627 CD1 TRP A 246 1253 1846 1615 152 83 148 C ATOM 2628 CD2 TRP A 246 -19.178 -2.694 16.609 1.00 10.00 C ANISOU 2628 CD2 TRP A 246 873 1591 1335 159 104 138 C ATOM 2629 NE1 TRP A 246 -19.995 -4.689 15.984 1.00 13.22 N ANISOU 2629 NE1 TRP A 246 1290 1907 1825 129 27 154 N ATOM 2630 CE2 TRP A 246 -20.362 -3.428 16.384 1.00 14.40 C ANISOU 2630 CE2 TRP A 246 1384 2088 2000 138 47 146 C ATOM 2631 CE3 TRP A 246 -19.275 -1.354 17.012 1.00 8.30 C ANISOU 2631 CE3 TRP A 246 630 1404 1118 171 123 126 C ATOM 2632 CZ2 TRP A 246 -21.638 -2.878 16.574 1.00 13.42 C ANISOU 2632 CZ2 TRP A 246 1159 1932 2007 131 19 142 C ATOM 2633 CZ3 TRP A 246 -20.542 -0.807 17.199 1.00 8.81 C ANISOU 2633 CZ3 TRP A 246 616 1439 1292 173 100 117 C ATOM 2634 CH2 TRP A 246 -21.714 -1.570 16.962 1.00 13.77 C ANISOU 2634 CH2 TRP A 246 1173 2007 2052 154 51 125 C ATOM 2635 N LEU A 247 -13.681 -2.258 15.308 1.00 12.68 N ANISOU 2635 N LEU A 247 1363 1997 1459 202 305 100 N ATOM 2636 CA LEU A 247 -12.474 -1.557 15.744 1.00 14.56 C ANISOU 2636 CA LEU A 247 1540 2265 1726 201 353 101 C ATOM 2637 C LEU A 247 -12.327 -0.174 15.137 1.00 11.63 C ANISOU 2637 C LEU A 247 1209 1888 1323 170 374 96 C ATOM 2638 O LEU A 247 -11.855 0.726 15.855 1.00 13.58 O ANISOU 2638 O LEU A 247 1397 2161 1602 158 364 102 O ATOM 2639 CB LEU A 247 -11.214 -2.393 15.444 1.00 14.27 C ANISOU 2639 CB LEU A 247 1470 2209 1744 225 425 89 C ATOM 2640 CG LEU A 247 -10.882 -3.410 16.525 1.00 17.78 C ANISOU 2640 CG LEU A 247 1842 2660 2253 258 380 102 C ATOM 2641 CD1 LEU A 247 -9.834 -4.415 15.990 1.00 23.62 C ANISOU 2641 CD1 LEU A 247 2552 3358 3066 297 447 80 C ATOM 2642 CD2 LEU A 247 -10.386 -2.740 17.836 1.00 18.88 C ANISOU 2642 CD2 LEU A 247 1907 2832 2433 253 318 121 C ATOM 2643 N PRO A 248 -12.650 0.077 13.856 1.00 11.73 N ANISOU 2643 N PRO A 248 1339 1853 1266 154 392 88 N ATOM 2644 CA PRO A 248 -12.422 1.436 13.338 1.00 11.60 C ANISOU 2644 CA PRO A 248 1377 1818 1213 118 412 93 C ATOM 2645 C PRO A 248 -13.149 2.492 14.135 1.00 9.48 C ANISOU 2645 C PRO A 248 1068 1571 962 113 323 101 C ATOM 2646 O PRO A 248 -12.565 3.536 14.445 1.00 13.37 O ANISOU 2646 O PRO A 248 1533 2073 1475 90 337 106 O ATOM 2647 CB PRO A 248 -12.927 1.346 11.889 1.00 14.66 C ANISOU 2647 CB PRO A 248 1946 2131 1494 105 409 87 C ATOM 2648 CG PRO A 248 -12.592 -0.065 11.523 1.00 12.07 C ANISOU 2648 CG PRO A 248 1641 1786 1160 132 467 68 C ATOM 2649 CD PRO A 248 -13.018 -0.836 12.756 1.00 11.69 C ANISOU 2649 CD PRO A 248 1453 1790 1200 162 398 73 C ATOM 2650 N LEU A 249 -14.420 2.252 14.472 1.00 9.50 N ANISOU 2650 N LEU A 249 1062 1574 975 133 237 98 N ATOM 2651 CA LEU A 249 -15.162 3.234 15.254 1.00 11.23 C ANISOU 2651 CA LEU A 249 1238 1805 1225 141 179 94 C ATOM 2652 C LEU A 249 -14.537 3.433 16.635 1.00 17.85 C ANISOU 2652 C LEU A 249 1992 2697 2094 148 207 93 C ATOM 2653 O LEU A 249 -14.420 4.565 17.106 1.00 12.58 O ANISOU 2653 O LEU A 249 1321 2029 1429 143 188 85 O ATOM 2654 CB LEU A 249 -16.618 2.781 15.356 1.00 12.17 C ANISOU 2654 CB LEU A 249 1331 1903 1389 162 111 89 C ATOM 2655 CG LEU A 249 -17.739 3.710 15.815 1.00 25.91 C ANISOU 2655 CG LEU A 249 3027 3624 3192 181 56 75 C ATOM 2656 CD1 LEU A 249 -17.708 5.062 15.120 1.00 13.40 C ANISOU 2656 CD1 LEU A 249 1519 1990 1582 172 -2 71 C ATOM 2657 CD2 LEU A 249 -19.061 2.974 15.572 1.00 15.24 C ANISOU 2657 CD2 LEU A 249 1632 2231 1926 193 -7 74 C ATOM 2658 N HIS A 250 -14.131 2.343 17.305 1.00 11.22 N ANISOU 2658 N HIS A 250 1104 1889 1271 162 233 100 N ATOM 2659 CA HIS A 250 -13.468 2.488 18.604 1.00 9.84 C ANISOU 2659 CA HIS A 250 886 1743 1108 168 225 101 C ATOM 2660 C HIS A 250 -12.146 3.241 18.483 1.00 11.01 C ANISOU 2660 C HIS A 250 1013 1885 1286 143 228 100 C ATOM 2661 O HIS A 250 -11.824 4.095 19.319 1.00 11.45 O ANISOU 2661 O HIS A 250 1063 1940 1346 136 183 92 O ATOM 2662 CB HIS A 250 -13.212 1.117 19.217 1.00 8.34 C ANISOU 2662 CB HIS A 250 672 1566 929 186 230 117 C ATOM 2663 CG HIS A 250 -14.437 0.436 19.729 1.00 10.59 C ANISOU 2663 CG HIS A 250 970 1854 1200 198 236 127 C ATOM 2664 ND1 HIS A 250 -15.149 0.902 20.814 1.00 11.06 N ANISOU 2664 ND1 HIS A 250 1046 1922 1234 204 246 123 N ATOM 2665 CD2 HIS A 250 -15.045 -0.711 19.338 1.00 10.80 C ANISOU 2665 CD2 HIS A 250 993 1865 1244 200 247 140 C ATOM 2666 CE1 HIS A 250 -16.164 0.086 21.052 1.00 13.85 C ANISOU 2666 CE1 HIS A 250 1391 2269 1603 204 282 138 C ATOM 2667 NE2 HIS A 250 -16.129 -0.894 20.160 1.00 11.38 N ANISOU 2667 NE2 HIS A 250 1062 1939 1322 199 269 150 N ATOM 2668 N ILE A 251 -11.353 2.920 17.460 1.00 8.60 N ANISOU 2668 N ILE A 251 697 1561 1009 128 286 105 N ATOM 2669 CA ILE A 251 -10.078 3.601 17.260 1.00 8.94 C ANISOU 2669 CA ILE A 251 691 1587 1120 95 318 107 C ATOM 2670 C ILE A 251 -10.296 5.093 17.009 1.00 13.93 C ANISOU 2670 C ILE A 251 1374 2195 1724 57 300 107 C ATOM 2671 O ILE A 251 -9.565 5.931 17.538 1.00 9.18 O ANISOU 2671 O ILE A 251 728 1581 1180 29 266 107 O ATOM 2672 CB ILE A 251 -9.318 2.930 16.102 1.00 9.24 C ANISOU 2672 CB ILE A 251 720 1600 1192 88 434 108 C ATOM 2673 CG1 ILE A 251 -8.913 1.503 16.521 1.00 12.87 C ANISOU 2673 CG1 ILE A 251 1112 2069 1710 132 434 103 C ATOM 2674 CG2 ILE A 251 -8.107 3.792 15.620 1.00 11.85 C ANISOU 2674 CG2 ILE A 251 999 1896 1607 37 516 114 C ATOM 2675 CD1 ILE A 251 -8.304 0.651 15.373 1.00 14.24 C ANISOU 2675 CD1 ILE A 251 1311 2192 1906 132 541 76 C ATOM 2676 N ILE A 252 -11.290 5.449 16.189 1.00 8.59 N ANISOU 2676 N ILE A 252 794 1497 971 55 301 108 N ATOM 2677 CA ILE A 252 -11.594 6.864 15.992 1.00 10.40 C ANISOU 2677 CA ILE A 252 1083 1691 1177 28 262 109 C ATOM 2678 C ILE A 252 -11.936 7.529 17.328 1.00 13.01 C ANISOU 2678 C ILE A 252 1382 2038 1525 50 179 88 C ATOM 2679 O ILE A 252 -11.471 8.638 17.622 1.00 12.00 O ANISOU 2679 O ILE A 252 1259 1880 1419 21 145 84 O ATOM 2680 CB ILE A 252 -12.730 7.041 14.964 1.00 10.75 C ANISOU 2680 CB ILE A 252 1244 1693 1149 35 232 112 C ATOM 2681 CG1 ILE A 252 -12.254 6.634 13.551 1.00 12.99 C ANISOU 2681 CG1 ILE A 252 1625 1934 1375 3 317 131 C ATOM 2682 CG2 ILE A 252 -13.223 8.507 14.963 1.00 11.82 C ANISOU 2682 CG2 ILE A 252 1435 1780 1276 24 159 111 C ATOM 2683 CD1 ILE A 252 -13.445 6.527 12.532 1.00 16.29 C ANISOU 2683 CD1 ILE A 252 2187 2293 1709 16 243 133 C ATOM 2684 N ASN A 253 -12.759 6.872 18.153 1.00 9.03 N ANISOU 2684 N ASN A 253 861 1567 1004 97 155 73 N ATOM 2685 CA ASN A 253 -13.047 7.425 19.472 1.00 11.64 C ANISOU 2685 CA ASN A 253 1196 1903 1324 121 108 48 C ATOM 2686 C ASN A 253 -11.767 7.635 20.269 1.00 15.08 C ANISOU 2686 C ASN A 253 1605 2336 1789 96 66 48 C ATOM 2687 O ASN A 253 -11.633 8.629 20.994 1.00 11.34 O ANISOU 2687 O ASN A 253 1168 1834 1306 91 6 25 O ATOM 2688 CB ASN A 253 -14.025 6.520 20.229 1.00 10.78 C ANISOU 2688 CB ASN A 253 1081 1824 1190 165 130 40 C ATOM 2689 CG ASN A 253 -15.438 6.627 19.675 1.00 11.68 C ANISOU 2689 CG ASN A 253 1197 1920 1322 190 142 29 C ATOM 2690 OD1 ASN A 253 -15.772 7.595 18.982 1.00 12.15 O ANISOU 2690 OD1 ASN A 253 1282 1937 1396 187 106 21 O ATOM 2691 ND2 ASN A 253 -16.272 5.657 19.991 1.00 8.95 N ANISOU 2691 ND2 ASN A 253 820 1592 990 212 179 33 N ATOM 2692 N CYS A 254 -10.794 6.731 20.124 1.00 10.91 N ANISOU 2692 N CYS A 254 1011 1821 1313 83 82 68 N ATOM 2693 CA CYS A 254 -9.536 6.921 20.842 1.00 10.05 C ANISOU 2693 CA CYS A 254 852 1691 1277 60 10 69 C ATOM 2694 C CYS A 254 -8.813 8.178 20.361 1.00 11.33 C ANISOU 2694 C CYS A 254 990 1806 1508 2 -1 71 C ATOM 2695 O CYS A 254 -8.227 8.911 21.167 1.00 12.39 O ANISOU 2695 O CYS A 254 1124 1902 1682 -19 -103 58 O ATOM 2696 CB CYS A 254 -8.639 5.692 20.665 1.00 12.07 C ANISOU 2696 CB CYS A 254 1013 1955 1617 66 32 88 C ATOM 2697 SG CYS A 254 -9.225 4.244 21.594 1.00 13.67 S ANISOU 2697 SG CYS A 254 1256 2187 1750 123 1 95 S ATOM 2698 N PHE A 255 -8.812 8.428 19.044 1.00 12.43 N ANISOU 2698 N PHE A 255 1130 1934 1659 -30 97 89 N ATOM 2699 CA PHE A 255 -8.197 9.660 18.540 1.00 11.95 C ANISOU 2699 CA PHE A 255 1069 1817 1655 -97 105 101 C ATOM 2700 C PHE A 255 -8.925 10.895 19.060 1.00 13.15 C ANISOU 2700 C PHE A 255 1316 1937 1743 -92 14 78 C ATOM 2701 O PHE A 255 -8.283 11.862 19.480 1.00 13.53 O ANISOU 2701 O PHE A 255 1355 1934 1853 -136 -58 73 O ATOM 2702 CB PHE A 255 -8.163 9.687 17.004 1.00 10.92 C ANISOU 2702 CB PHE A 255 978 1665 1505 -134 240 130 C ATOM 2703 CG PHE A 255 -6.973 8.969 16.429 1.00 11.67 C ANISOU 2703 CG PHE A 255 967 1755 1711 -164 362 148 C ATOM 2704 CD1 PHE A 255 -7.056 7.624 16.117 1.00 13.48 C ANISOU 2704 CD1 PHE A 255 1177 2021 1923 -117 431 142 C ATOM 2705 CD2 PHE A 255 -5.774 9.636 16.249 1.00 14.45 C ANISOU 2705 CD2 PHE A 255 1229 2055 2208 -237 409 166 C ATOM 2706 CE1 PHE A 255 -5.951 6.948 15.616 1.00 13.66 C ANISOU 2706 CE1 PHE A 255 1094 2029 2066 -131 556 148 C ATOM 2707 CE2 PHE A 255 -4.646 8.960 15.756 1.00 18.10 C ANISOU 2707 CE2 PHE A 255 1561 2503 2814 -259 546 176 C ATOM 2708 CZ PHE A 255 -4.749 7.613 15.443 1.00 15.14 C ANISOU 2708 CZ PHE A 255 1173 2166 2415 -198 623 163 C ATOM 2709 N THR A 256 -10.261 10.876 19.052 1.00 10.00 N ANISOU 2709 N THR A 256 999 1557 1245 -38 11 60 N ATOM 2710 CA THR A 256 -11.011 12.033 19.524 1.00 10.76 C ANISOU 2710 CA THR A 256 1175 1612 1300 -18 -59 29 C ATOM 2711 C THR A 256 -10.673 12.324 20.977 1.00 11.29 C ANISOU 2711 C THR A 256 1256 1669 1365 -3 -149 -8 C ATOM 2712 O THR A 256 -10.504 13.488 21.368 1.00 14.86 O ANISOU 2712 O THR A 256 1761 2059 1825 -22 -224 -31 O ATOM 2713 CB THR A 256 -12.516 11.764 19.347 1.00 10.65 C ANISOU 2713 CB THR A 256 1204 1615 1227 48 -38 11 C ATOM 2714 OG1 THR A 256 -12.787 11.581 17.948 1.00 13.49 O ANISOU 2714 OG1 THR A 256 1588 1959 1578 29 2 45 O ATOM 2715 CG2 THR A 256 -13.391 12.913 19.911 1.00 15.67 C ANISOU 2715 CG2 THR A 256 1906 2201 1847 90 -94 -34 C ATOM 2716 N PHE A 257 -10.549 11.262 21.784 1.00 10.40 N ANISOU 2716 N PHE A 257 1119 1601 1230 28 -154 -12 N ATOM 2717 CA PHE A 257 -10.376 11.384 23.220 1.00 11.36 C ANISOU 2717 CA PHE A 257 1309 1703 1306 50 -247 -47 C ATOM 2718 C PHE A 257 -8.938 11.719 23.595 1.00 16.47 C ANISOU 2718 C PHE A 257 1912 2298 2047 -8 -368 -39 C ATOM 2719 O PHE A 257 -8.686 12.660 24.363 1.00 16.19 O ANISOU 2719 O PHE A 257 1957 2198 1998 -20 -482 -72 O ATOM 2720 CB PHE A 257 -10.812 10.078 23.886 1.00 10.67 C ANISOU 2720 CB PHE A 257 1239 1667 1149 98 -211 -43 C ATOM 2721 CG PHE A 257 -10.708 10.096 25.381 1.00 11.49 C ANISOU 2721 CG PHE A 257 1466 1738 1161 121 -297 -73 C ATOM 2722 CD1 PHE A 257 -9.830 9.235 26.029 1.00 16.74 C ANISOU 2722 CD1 PHE A 257 2130 2396 1836 112 -388 -51 C ATOM 2723 CD2 PHE A 257 -11.515 10.945 26.145 1.00 12.58 C ANISOU 2723 CD2 PHE A 257 1743 1840 1197 157 -288 -126 C ATOM 2724 CE1 PHE A 257 -9.731 9.232 27.425 1.00 20.01 C ANISOU 2724 CE1 PHE A 257 2709 2760 2134 131 -491 -75 C ATOM 2725 CE2 PHE A 257 -11.423 10.946 27.547 1.00 13.02 C ANISOU 2725 CE2 PHE A 257 1966 1851 1130 178 -357 -158 C ATOM 2726 CZ PHE A 257 -10.528 10.091 28.181 1.00 17.51 C ANISOU 2726 CZ PHE A 257 2561 2407 1684 161 -468 -129 C ATOM 2727 N PHE A 258 -7.980 10.955 23.065 1.00 11.95 N ANISOU 2727 N PHE A 258 1208 1743 1590 -41 -350 0 N ATOM 2728 CA PHE A 258 -6.585 11.076 23.490 1.00 13.08 C ANISOU 2728 CA PHE A 258 1265 1829 1876 -91 -475 8 C ATOM 2729 C PHE A 258 -5.826 12.176 22.760 1.00 17.35 C ANISOU 2729 C PHE A 258 1729 2310 2555 -173 -473 24 C ATOM 2730 O PHE A 258 -4.748 12.584 23.225 1.00 17.36 O ANISOU 2730 O PHE A 258 1660 2239 2698 -224 -604 23 O ATOM 2731 CB PHE A 258 -5.861 9.755 23.248 1.00 13.72 C ANISOU 2731 CB PHE A 258 1211 1940 2063 -82 -446 39 C ATOM 2732 CG PHE A 258 -6.246 8.652 24.193 1.00 13.85 C ANISOU 2732 CG PHE A 258 1301 1984 1978 -18 -501 33 C ATOM 2733 CD1 PHE A 258 -6.662 7.422 23.697 1.00 12.89 C ANISOU 2733 CD1 PHE A 258 1145 1924 1829 21 -385 54 C ATOM 2734 CD2 PHE A 258 -6.118 8.818 25.574 1.00 14.56 C ANISOU 2734 CD2 PHE A 258 1515 2021 1997 -3 -677 11 C ATOM 2735 CE1 PHE A 258 -6.981 6.367 24.567 1.00 12.12 C ANISOU 2735 CE1 PHE A 258 1121 1840 1644 70 -434 59 C ATOM 2736 CE2 PHE A 258 -6.422 7.772 26.453 1.00 17.27 C ANISOU 2736 CE2 PHE A 258 1957 2375 2231 47 -723 16 C ATOM 2737 CZ PHE A 258 -6.860 6.553 25.953 1.00 15.90 C ANISOU 2737 CZ PHE A 258 1734 2266 2041 81 -596 44 C ATOM 2738 N CYS A 259 -6.324 12.641 21.615 1.00 16.38 N ANISOU 2738 N CYS A 259 1621 2199 2405 -194 -337 42 N ATOM 2739 CA CYS A 259 -5.631 13.652 20.817 1.00 19.57 C ANISOU 2739 CA CYS A 259 1975 2537 2925 -283 -303 69 C ATOM 2740 C CYS A 259 -6.550 14.849 20.598 1.00 23.34 C ANISOU 2740 C CYS A 259 2598 2977 3293 -283 -314 55 C ATOM 2741 O CYS A 259 -7.031 15.081 19.483 1.00 19.90 O ANISOU 2741 O CYS A 259 2207 2542 2811 -297 -202 83 O ATOM 2742 CB CYS A 259 -5.152 13.090 19.478 1.00 20.77 C ANISOU 2742 CB CYS A 259 2028 2709 3154 -323 -116 116 C ATOM 2743 SG CYS A 259 -3.954 14.266 18.743 1.00 27.99 S ANISOU 2743 SG CYS A 259 2857 3521 4258 -456 -62 158 S ATOM 2744 N PRO A 260 -6.801 15.647 21.640 1.00 21.97 N ANISOU 2744 N PRO A 260 2498 3037 2813 -293 -732 71 N ATOM 2745 CA PRO A 260 -7.629 16.854 21.452 1.00 28.48 C ANISOU 2745 CA PRO A 260 3533 3575 3714 -430 -803 53 C ATOM 2746 C PRO A 260 -6.954 17.926 20.607 1.00 34.64 C ANISOU 2746 C PRO A 260 4193 4299 4671 -796 -911 143 C ATOM 2747 O PRO A 260 -7.636 18.863 20.177 1.00 33.54 O ANISOU 2747 O PRO A 260 4225 3904 4613 -923 -956 171 O ATOM 2748 CB PRO A 260 -7.865 17.342 22.888 1.00 23.36 C ANISOU 2748 CB PRO A 260 3093 2817 2967 -271 -1006 -135 C ATOM 2749 CG PRO A 260 -6.635 16.851 23.645 1.00 27.71 C ANISOU 2749 CG PRO A 260 3468 3601 3458 -218 -1143 -202 C ATOM 2750 CD PRO A 260 -6.284 15.528 23.018 1.00 23.21 C ANISOU 2750 CD PRO A 260 2685 3271 2864 -137 -917 -69 C ATOM 2751 N ASP A 261 -5.644 17.823 20.364 1.00 24.74 N ANISOU 2751 N ASP A 261 2637 3277 3486 -967 -954 208 N ATOM 2752 CA ASP A 261 -4.959 18.686 19.406 1.00 26.97 C ANISOU 2752 CA ASP A 261 2737 3567 3945 -1339 -986 381 C ATOM 2753 C ASP A 261 -5.113 18.216 17.966 1.00 29.54 C ANISOU 2753 C ASP A 261 2953 4050 4222 -1366 -693 584 C ATOM 2754 O ASP A 261 -4.720 18.943 17.046 1.00 30.57 O ANISOU 2754 O ASP A 261 2967 4193 4455 -1657 -665 782 O ATOM 2755 CB ASP A 261 -3.463 18.767 19.739 1.00 30.16 C ANISOU 2755 CB ASP A 261 2797 4203 4461 -1516 -1140 389 C ATOM 2756 CG ASP A 261 -3.191 19.441 21.073 1.00 87.61 C ANISOU 2756 CG ASP A 261 10181 11299 11809 -1532 -1509 175 C ATOM 2757 OD1 ASP A 261 -4.045 20.230 21.533 1.00 44.69 O ANISOU 2757 OD1 ASP A 261 5077 5523 6381 -1505 -1667 58 O ATOM 2758 OD2 ASP A 261 -2.116 19.185 21.658 1.00 50.11 O ANISOU 2758 OD2 ASP A 261 5185 6755 7099 -1543 -1661 105 O ATOM 2759 N CYS A 262 -5.618 17.007 17.748 1.00 24.33 N ANISOU 2759 N CYS A 262 2324 3514 3406 -1067 -492 548 N ATOM 2760 CA CYS A 262 -5.860 16.501 16.406 1.00 24.79 C ANISOU 2760 CA CYS A 262 2327 3704 3388 -1023 -257 683 C ATOM 2761 C CYS A 262 -7.236 16.959 15.955 1.00 26.88 C ANISOU 2761 C CYS A 262 2898 3659 3657 -1004 -234 698 C ATOM 2762 O CYS A 262 -8.191 16.945 16.735 1.00 25.80 O ANISOU 2762 O CYS A 262 2988 3292 3522 -854 -301 568 O ATOM 2763 CB CYS A 262 -5.803 14.968 16.372 1.00 24.87 C ANISOU 2763 CB CYS A 262 2252 3932 3266 -695 -118 604 C ATOM 2764 SG CYS A 262 -4.201 14.150 16.722 1.00 34.51 S ANISOU 2764 SG CYS A 262 3089 5573 4452 -611 -123 570 S ATOM 2765 N ASER A 263 -7.335 17.365 14.693 0.55 21.33 N ANISOU 2765 N ASER A 263 2190 2977 2939 -1138 -132 869 N ATOM 2766 N BSER A 263 -7.340 17.361 14.694 0.45 21.58 N ANISOU 2766 N BSER A 263 2222 3007 2969 -1137 -132 868 N ATOM 2767 CA ASER A 263 -8.646 17.649 14.124 0.55 26.76 C ANISOU 2767 CA ASER A 263 3150 3403 3615 -1073 -113 878 C ATOM 2768 CA BSER A 263 -8.657 17.671 14.161 0.45 19.76 C ANISOU 2768 CA BSER A 263 2269 2508 2732 -1075 -119 874 C ATOM 2769 C ASER A 263 -9.537 16.415 14.232 0.55 20.70 C ANISOU 2769 C ASER A 263 2468 2623 2774 -740 -26 738 C ATOM 2770 C BSER A 263 -9.540 16.429 14.220 0.45 21.71 C ANISOU 2770 C BSER A 263 2597 2750 2903 -743 -27 740 C ATOM 2771 O ASER A 263 -9.074 15.284 14.070 0.55 22.24 O ANISOU 2771 O ASER A 263 2509 3056 2886 -570 74 703 O ATOM 2772 O BSER A 263 -9.073 15.307 14.013 0.45 20.22 O ANISOU 2772 O BSER A 263 2253 2802 2628 -576 76 710 O ATOM 2773 CB ASER A 263 -8.513 18.081 12.663 0.55 30.04 C ANISOU 2773 CB ASER A 263 3542 3907 3965 -1197 -5 1081 C ATOM 2774 CB BSER A 263 -8.554 18.180 12.726 0.45 31.07 C ANISOU 2774 CB BSER A 263 3691 4007 4109 -1206 -22 1074 C ATOM 2775 OG ASER A 263 -8.118 19.436 12.565 0.55 25.21 O ANISOU 2775 OG ASER A 263 2966 3160 3452 -1403 -112 1144 O ATOM 2776 OG BSER A 263 -9.844 18.477 12.228 0.45 32.20 O ANISOU 2776 OG BSER A 263 4102 3893 4241 -1085 -42 1025 O ATOM 2777 N HIS A 264 -10.820 16.637 14.529 1.00 20.53 N ANISOU 2777 N HIS A 264 2679 2314 2808 -644 -81 661 N ATOM 2778 CA HIS A 264 -11.759 15.519 14.650 1.00 22.12 C ANISOU 2778 CA HIS A 264 2935 2467 3002 -374 -13 567 C ATOM 2779 C HIS A 264 -11.826 14.762 13.326 1.00 16.61 C ANISOU 2779 C HIS A 264 2187 1893 2230 -275 82 607 C ATOM 2780 O HIS A 264 -11.799 15.369 12.249 1.00 16.18 O ANISOU 2780 O HIS A 264 2172 1857 2120 -380 97 709 O ATOM 2781 CB HIS A 264 -13.152 16.047 15.023 1.00 15.81 C ANISOU 2781 CB HIS A 264 2346 1368 2293 -313 -73 510 C ATOM 2782 CG HIS A 264 -14.074 15.018 15.603 1.00 13.94 C ANISOU 2782 CG HIS A 264 2120 1073 2102 -81 -13 440 C ATOM 2783 ND1 HIS A 264 -14.588 13.963 14.871 1.00 20.51 N ANISOU 2783 ND1 HIS A 264 2911 1924 2956 50 39 430 N ATOM 2784 CD2 HIS A 264 -14.597 14.903 16.850 1.00 16.17 C ANISOU 2784 CD2 HIS A 264 2448 1289 2408 38 -7 385 C ATOM 2785 CE1 HIS A 264 -15.366 13.230 15.650 1.00 20.64 C ANISOU 2785 CE1 HIS A 264 2905 1966 2972 162 32 336 C ATOM 2786 NE2 HIS A 264 -15.379 13.772 16.859 1.00 17.20 N ANISOU 2786 NE2 HIS A 264 2509 1496 2531 168 30 334 N ATOM 2787 N ALA A 265 -11.900 13.435 13.401 1.00 12.82 N ANISOU 2787 N ALA A 265 1641 1490 1740 -55 127 527 N ATOM 2788 CA ALA A 265 -12.173 12.663 12.197 1.00 15.40 C ANISOU 2788 CA ALA A 265 1972 1873 2008 100 158 503 C ATOM 2789 C ALA A 265 -13.345 13.290 11.445 1.00 16.26 C ANISOU 2789 C ALA A 265 2262 1757 2160 74 104 523 C ATOM 2790 O ALA A 265 -14.337 13.702 12.068 1.00 15.94 O ANISOU 2790 O ALA A 265 2330 1468 2258 55 47 500 O ATOM 2791 CB ALA A 265 -12.492 11.204 12.543 1.00 16.25 C ANISOU 2791 CB ALA A 265 2051 1934 2188 339 138 395 C ATOM 2792 N PRO A 266 -13.259 13.413 10.126 1.00 15.90 N ANISOU 2792 N PRO A 266 2379 2305 1357 -178 16 172 N ATOM 2793 CA PRO A 266 -14.330 14.085 9.378 1.00 17.50 C ANISOU 2793 CA PRO A 266 2661 2418 1571 -136 -29 224 C ATOM 2794 C PRO A 266 -15.625 13.290 9.411 1.00 17.93 C ANISOU 2794 C PRO A 266 2649 2475 1688 -17 -46 220 C ATOM 2795 O PRO A 266 -15.647 12.072 9.632 1.00 14.17 O ANISOU 2795 O PRO A 266 2086 2089 1208 14 -12 184 O ATOM 2796 CB PRO A 266 -13.778 14.182 7.949 1.00 22.28 C ANISOU 2796 CB PRO A 266 3319 3054 2092 -245 -32 279 C ATOM 2797 CG PRO A 266 -12.737 13.123 7.867 1.00 22.22 C ANISOU 2797 CG PRO A 266 3209 3171 2062 -294 58 231 C ATOM 2798 CD PRO A 266 -12.162 12.959 9.256 1.00 17.21 C ANISOU 2798 CD PRO A 266 2487 2558 1493 -272 63 180 C ATOM 2799 N ALEU A 267 -16.714 14.020 9.161 0.50 19.74 N ANISOU 2799 N ALEU A 267 2912 2589 1999 48 -107 265 N ATOM 2800 N BLEU A 267 -16.725 14.015 9.180 0.50 18.47 N ANISOU 2800 N BLEU A 267 2750 2428 1840 50 -106 264 N ATOM 2801 CA ALEU A 267 -18.055 13.456 9.267 0.50 25.94 C ANISOU 2801 CA ALEU A 267 3603 3351 2903 162 -128 268 C ATOM 2802 CA BLEU A 267 -18.058 13.423 9.281 0.50 18.75 C ANISOU 2802 CA BLEU A 267 2690 2444 1992 162 -127 267 C ATOM 2803 C ALEU A 267 -18.245 12.263 8.336 0.50 14.28 C ANISOU 2803 C ALEU A 267 2078 1973 1373 137 -178 296 C ATOM 2804 C BLEU A 267 -18.229 12.237 8.339 0.50 24.24 C ANISOU 2804 C BLEU A 267 3339 3238 2632 136 -176 295 C ATOM 2805 O ALEU A 267 -18.867 11.265 8.722 0.50 36.53 O ANISOU 2805 O ALEU A 267 4797 4838 4245 196 -151 264 O ATOM 2806 O BLEU A 267 -18.831 11.222 8.715 0.50 13.72 O ANISOU 2806 O BLEU A 267 1908 1954 1351 193 -149 262 O ATOM 2807 CB ALEU A 267 -19.088 14.544 8.965 0.50 27.52 C ANISOU 2807 CB ALEU A 267 3818 3387 3250 232 -213 332 C ATOM 2808 CB BLEU A 267 -19.126 14.479 8.989 0.50 36.03 C ANISOU 2808 CB BLEU A 267 4888 4469 4331 236 -211 330 C ATOM 2809 CG ALEU A 267 -20.566 14.175 9.076 0.50 26.85 C ANISOU 2809 CG ALEU A 267 3590 3247 3366 355 -242 346 C ATOM 2810 CG BLEU A 267 -19.750 15.236 10.162 0.50 23.15 C ANISOU 2810 CG BLEU A 267 3237 2705 2853 338 -115 269 C ATOM 2811 CD1ALEU A 267 -21.143 14.755 10.354 0.50 42.70 C ANISOU 2811 CD1ALEU A 267 5555 5139 5531 459 -100 267 C ATOM 2812 CD1BLEU A 267 -18.794 16.283 10.702 0.50 68.56 C ANISOU 2812 CD1BLEU A 267 9135 8394 8521 271 -64 232 C ATOM 2813 CD2ALEU A 267 -21.310 14.688 7.860 0.50 43.18 C ANISOU 2813 CD2ALEU A 267 5663 5215 5527 363 -445 475 C ATOM 2814 CD2BLEU A 267 -21.068 15.871 9.731 0.50 20.32 C ANISOU 2814 CD2BLEU A 267 2802 2188 2729 450 -204 338 C ATOM 2815 N TRP A 268 -17.726 12.342 7.101 1.00 15.75 N ANISOU 2815 N TRP A 268 2360 2183 1440 33 -238 351 N ATOM 2816 CA TRP A 268 -17.903 11.219 6.173 1.00 15.09 C ANISOU 2816 CA TRP A 268 2282 2173 1277 -11 -272 364 C ATOM 2817 C TRP A 268 -17.251 9.949 6.720 1.00 17.82 C ANISOU 2817 C TRP A 268 2544 2636 1590 -2 -146 273 C ATOM 2818 O TRP A 268 -17.765 8.842 6.510 1.00 14.23 O ANISOU 2818 O TRP A 268 2046 2223 1137 17 -159 258 O ATOM 2819 CB TRP A 268 -17.340 11.547 4.782 1.00 15.64 C ANISOU 2819 CB TRP A 268 2526 2236 1182 -156 -316 422 C ATOM 2820 CG TRP A 268 -15.828 11.718 4.715 1.00 19.50 C ANISOU 2820 CG TRP A 268 3061 2783 1564 -258 -166 373 C ATOM 2821 CD1 TRP A 268 -15.126 12.899 4.788 1.00 25.35 C ANISOU 2821 CD1 TRP A 268 3871 3474 2288 -322 -145 397 C ATOM 2822 CD2 TRP A 268 -14.846 10.682 4.536 1.00 20.84 C ANISOU 2822 CD2 TRP A 268 3193 3057 1668 -309 -14 294 C ATOM 2823 NE1 TRP A 268 -13.780 12.652 4.664 1.00 22.01 N ANISOU 2823 NE1 TRP A 268 3434 3127 1801 -419 8 342 N ATOM 2824 CE2 TRP A 268 -13.581 11.304 4.517 1.00 24.59 C ANISOU 2824 CE2 TRP A 268 3685 3545 2114 -402 95 276 C ATOM 2825 CE3 TRP A 268 -14.916 9.287 4.404 1.00 20.27 C ANISOU 2825 CE3 TRP A 268 3065 3053 1584 -284 43 235 C ATOM 2826 CZ2 TRP A 268 -12.396 10.582 4.366 1.00 30.97 C ANISOU 2826 CZ2 TRP A 268 4421 4430 2916 -457 266 203 C ATOM 2827 CZ3 TRP A 268 -13.740 8.574 4.249 1.00 27.53 C ANISOU 2827 CZ3 TRP A 268 3941 4037 2481 -331 213 157 C ATOM 2828 CH2 TRP A 268 -12.495 9.224 4.232 1.00 31.09 C ANISOU 2828 CH2 TRP A 268 4376 4498 2938 -411 327 142 C ATOM 2829 N LEU A 269 -16.137 10.096 7.443 1.00 13.65 N ANISOU 2829 N LEU A 269 1992 2146 1049 -21 -47 221 N ATOM 2830 CA LEU A 269 -15.443 8.942 8.000 1.00 12.47 C ANISOU 2830 CA LEU A 269 1754 2081 902 -7 38 154 C ATOM 2831 C LEU A 269 -16.167 8.406 9.226 1.00 15.04 C ANISOU 2831 C LEU A 269 2005 2403 1308 88 37 124 C ATOM 2832 O LEU A 269 -16.209 7.187 9.439 1.00 13.58 O ANISOU 2832 O LEU A 269 1763 2266 1130 115 63 93 O ATOM 2833 CB LEU A 269 -14.003 9.310 8.361 1.00 15.76 C ANISOU 2833 CB LEU A 269 2149 2525 1313 -70 102 129 C ATOM 2834 CG LEU A 269 -13.138 8.176 8.929 1.00 16.45 C ANISOU 2834 CG LEU A 269 2122 2677 1450 -53 156 78 C ATOM 2835 CD1 LEU A 269 -13.028 7.044 7.908 1.00 20.65 C ANISOU 2835 CD1 LEU A 269 2640 3251 1956 -63 227 49 C ATOM 2836 CD2 LEU A 269 -11.757 8.681 9.344 1.00 16.64 C ANISOU 2836 CD2 LEU A 269 2089 2711 1521 -120 177 72 C ATOM 2837 N MET A 270 -16.725 9.298 10.050 1.00 13.94 N ANISOU 2837 N MET A 270 1882 2189 1225 131 28 127 N ATOM 2838 CA MET A 270 -17.564 8.841 11.150 1.00 14.62 C ANISOU 2838 CA MET A 270 1924 2255 1375 202 68 92 C ATOM 2839 C MET A 270 -18.675 7.952 10.616 1.00 15.08 C ANISOU 2839 C MET A 270 1911 2329 1491 245 41 110 C ATOM 2840 O MET A 270 -18.931 6.865 11.140 1.00 14.03 O ANISOU 2840 O MET A 270 1733 2233 1366 264 80 80 O ATOM 2841 CB MET A 270 -18.169 10.028 11.909 1.00 12.62 C ANISOU 2841 CB MET A 270 1715 1892 1189 242 102 80 C ATOM 2842 CG MET A 270 -17.176 10.993 12.538 1.00 16.10 C ANISOU 2842 CG MET A 270 2257 2294 1565 182 117 58 C ATOM 2843 SD MET A 270 -16.037 10.164 13.682 1.00 15.62 S ANISOU 2843 SD MET A 270 2222 2304 1409 117 126 16 S ATOM 2844 CE MET A 270 -17.149 9.418 14.869 1.00 12.21 C ANISOU 2844 CE MET A 270 1809 1842 990 171 218 -33 C ATOM 2845 N TYR A 271 -19.338 8.397 9.555 1.00 13.37 N ANISOU 2845 N TYR A 271 1695 2072 1314 245 -48 170 N ATOM 2846 CA TYR A 271 -20.499 7.643 9.104 1.00 13.39 C ANISOU 2846 CA TYR A 271 1620 2071 1395 271 -110 198 C ATOM 2847 C TYR A 271 -20.077 6.379 8.362 1.00 13.12 C ANISOU 2847 C TYR A 271 1615 2120 1249 209 -128 186 C ATOM 2848 O TYR A 271 -20.776 5.367 8.453 1.00 13.89 O ANISOU 2848 O TYR A 271 1650 2235 1391 222 -136 177 O ATOM 2849 CB TYR A 271 -21.442 8.561 8.304 1.00 13.79 C ANISOU 2849 CB TYR A 271 1657 2026 1558 289 -247 284 C ATOM 2850 CG TYR A 271 -22.207 9.441 9.312 1.00 16.27 C ANISOU 2850 CG TYR A 271 1885 2235 2061 390 -177 267 C ATOM 2851 CD1 TYR A 271 -23.240 8.903 10.072 1.00 20.82 C ANISOU 2851 CD1 TYR A 271 2321 2792 2798 456 -96 233 C ATOM 2852 CD2 TYR A 271 -21.797 10.742 9.604 1.00 28.97 C ANISOU 2852 CD2 TYR A 271 3568 3760 3678 407 -149 264 C ATOM 2853 CE1 TYR A 271 -23.905 9.656 11.035 1.00 21.70 C ANISOU 2853 CE1 TYR A 271 2365 2796 3085 542 31 192 C ATOM 2854 CE2 TYR A 271 -22.470 11.522 10.564 1.00 23.11 C ANISOU 2854 CE2 TYR A 271 2772 2900 3107 499 -44 224 C ATOM 2855 CZ TYR A 271 -23.518 10.964 11.280 1.00 19.61 C ANISOU 2855 CZ TYR A 271 2188 2435 2828 568 62 181 C ATOM 2856 OH TYR A 271 -24.182 11.696 12.240 1.00 23.42 O ANISOU 2856 OH TYR A 271 2626 2789 3484 652 222 120 O ATOM 2857 N LEU A 272 -18.918 6.393 7.689 1.00 11.93 N ANISOU 2857 N LEU A 272 1557 2010 967 137 -107 175 N ATOM 2858 CA LEU A 272 -18.390 5.156 7.123 1.00 11.75 C ANISOU 2858 CA LEU A 272 1563 2045 855 90 -67 135 C ATOM 2859 C LEU A 272 -18.102 4.131 8.212 1.00 10.96 C ANISOU 2859 C LEU A 272 1382 1981 800 144 14 77 C ATOM 2860 O LEU A 272 -18.362 2.933 8.038 1.00 12.32 O ANISOU 2860 O LEU A 272 1547 2169 966 142 20 53 O ATOM 2861 CB LEU A 272 -17.116 5.438 6.333 1.00 13.58 C ANISOU 2861 CB LEU A 272 1886 2300 974 8 1 117 C ATOM 2862 CG LEU A 272 -16.483 4.227 5.641 1.00 24.32 C ANISOU 2862 CG LEU A 272 3286 3694 2259 -40 92 55 C ATOM 2863 CD1 LEU A 272 -17.444 3.641 4.605 1.00 24.12 C ANISOU 2863 CD1 LEU A 272 3370 3644 2152 -101 2 76 C ATOM 2864 CD2 LEU A 272 -15.150 4.653 4.963 1.00 24.32 C ANISOU 2864 CD2 LEU A 272 3348 3706 2186 -123 216 25 C ATOM 2865 N ALA A 273 -17.537 4.580 9.337 1.00 10.80 N ANISOU 2865 N ALA A 273 1330 1961 813 177 61 60 N ATOM 2866 CA ALA A 273 -17.220 3.649 10.425 1.00 12.82 C ANISOU 2866 CA ALA A 273 1545 2233 1093 209 101 26 C ATOM 2867 C ALA A 273 -18.479 3.114 11.092 1.00 11.70 C ANISOU 2867 C ALA A 273 1376 2069 1002 244 103 28 C ATOM 2868 O ALA A 273 -18.507 1.953 11.526 1.00 11.30 O ANISOU 2868 O ALA A 273 1315 2026 953 250 119 11 O ATOM 2869 CB ALA A 273 -16.331 4.336 11.474 1.00 11.64 C ANISOU 2869 CB ALA A 273 1405 2074 942 203 111 21 C ATOM 2870 N ILE A 274 -19.524 3.935 11.176 1.00 10.46 N ANISOU 2870 N ILE A 274 1197 1869 909 266 96 50 N ATOM 2871 CA ILE A 274 -20.792 3.470 11.735 1.00 10.81 C ANISOU 2871 CA ILE A 274 1179 1885 1045 292 130 48 C ATOM 2872 C ILE A 274 -21.423 2.433 10.815 1.00 11.06 C ANISOU 2872 C ILE A 274 1169 1936 1097 267 62 68 C ATOM 2873 O ILE A 274 -21.899 1.390 11.266 1.00 11.03 O ANISOU 2873 O ILE A 274 1138 1935 1116 258 95 53 O ATOM 2874 CB ILE A 274 -21.733 4.664 11.981 1.00 11.62 C ANISOU 2874 CB ILE A 274 1231 1915 1270 336 156 61 C ATOM 2875 CG1 ILE A 274 -21.194 5.533 13.138 1.00 11.69 C ANISOU 2875 CG1 ILE A 274 1321 1883 1236 343 253 19 C ATOM 2876 CG2 ILE A 274 -23.174 4.222 12.292 1.00 13.18 C ANISOU 2876 CG2 ILE A 274 1308 2075 1625 361 202 64 C ATOM 2877 CD1 ILE A 274 -21.825 6.951 13.128 1.00 12.65 C ANISOU 2877 CD1 ILE A 274 1420 1908 1478 393 278 26 C ATOM 2878 N AVAL A 275 -21.469 2.732 9.516 0.50 11.34 N ANISOU 2878 N AVAL A 275 1227 1972 1109 236 -42 104 N ATOM 2879 N BVAL A 275 -21.466 2.709 9.510 0.50 11.33 N ANISOU 2879 N BVAL A 275 1227 1972 1107 235 -42 104 N ATOM 2880 CA AVAL A 275 -22.003 1.789 8.538 0.50 17.43 C ANISOU 2880 CA AVAL A 275 2009 2750 1863 181 -130 121 C ATOM 2881 CA BVAL A 275 -22.076 1.721 8.627 0.50 11.79 C ANISOU 2881 CA BVAL A 275 1286 2035 1159 184 -126 120 C ATOM 2882 C AVAL A 275 -21.229 0.477 8.587 0.50 12.70 C ANISOU 2882 C AVAL A 275 1469 2184 1171 159 -68 65 C ATOM 2883 C BVAL A 275 -21.232 0.448 8.586 0.50 11.29 C ANISOU 2883 C BVAL A 275 1291 2005 992 158 -68 64 C ATOM 2884 O AVAL A 275 -21.815 -0.610 8.556 0.50 12.01 O ANISOU 2884 O AVAL A 275 1370 2089 1104 133 -85 57 O ATOM 2885 O BVAL A 275 -21.781 -0.653 8.499 0.50 12.16 O ANISOU 2885 O BVAL A 275 1396 2108 1117 130 -86 55 O ATOM 2886 CB AVAL A 275 -21.967 2.421 7.133 0.50 12.54 C ANISOU 2886 CB AVAL A 275 1477 2113 1174 120 -257 172 C ATOM 2887 CB BVAL A 275 -22.324 2.287 7.212 0.50 28.14 C ANISOU 2887 CB BVAL A 275 3422 4082 3187 124 -273 179 C ATOM 2888 CG1AVAL A 275 -22.107 1.359 6.061 0.50 13.13 C ANISOU 2888 CG1AVAL A 275 1648 2192 1148 27 -331 167 C ATOM 2889 CG1BVAL A 275 -23.303 3.471 7.252 0.50 13.58 C ANISOU 2889 CG1BVAL A 275 1482 2172 1505 167 -365 252 C ATOM 2890 CG2AVAL A 275 -23.061 3.491 6.995 0.50 20.56 C ANISOU 2890 CG2AVAL A 275 2408 3063 2341 148 -377 252 C ATOM 2891 CG2BVAL A 275 -21.028 2.672 6.533 0.50 16.28 C ANISOU 2891 CG2BVAL A 275 2059 2603 1524 79 -236 158 C ATOM 2892 N LEU A 276 -19.902 0.561 8.673 1.00 10.80 N ANISOU 2892 N LEU A 276 1281 1967 857 168 2 28 N ATOM 2893 CA LEU A 276 -19.075 -0.647 8.764 1.00 10.97 C ANISOU 2893 CA LEU A 276 1330 1994 845 171 63 -24 C ATOM 2894 C LEU A 276 -19.451 -1.487 9.980 1.00 14.95 C ANISOU 2894 C LEU A 276 1792 2481 1407 203 84 -26 C ATOM 2895 O LEU A 276 -19.591 -2.717 9.885 1.00 12.07 O ANISOU 2895 O LEU A 276 1451 2093 1042 190 86 -46 O ATOM 2896 CB LEU A 276 -17.592 -0.282 8.836 1.00 10.99 C ANISOU 2896 CB LEU A 276 1334 2011 829 187 130 -51 C ATOM 2897 CG LEU A 276 -16.662 -1.508 8.991 1.00 14.81 C ANISOU 2897 CG LEU A 276 1805 2475 1347 215 189 -99 C ATOM 2898 CD1 LEU A 276 -16.759 -2.519 7.805 1.00 21.03 C ANISOU 2898 CD1 LEU A 276 2672 3233 2086 175 231 -152 C ATOM 2899 CD2 LEU A 276 -15.218 -1.032 9.167 1.00 11.54 C ANISOU 2899 CD2 LEU A 276 1334 2071 981 234 240 -113 C ATOM 2900 N ALA A 277 -19.592 -0.842 11.144 1.00 11.24 N ANISOU 2900 N ALA A 277 1292 2009 969 231 108 -8 N ATOM 2901 CA ALA A 277 -19.995 -1.580 12.337 1.00 12.18 C ANISOU 2901 CA ALA A 277 1419 2102 1107 232 142 -6 C ATOM 2902 C ALA A 277 -21.322 -2.288 12.105 1.00 13.31 C ANISOU 2902 C ALA A 277 1524 2229 1304 199 139 3 C ATOM 2903 O ALA A 277 -21.464 -3.470 12.430 1.00 12.13 O ANISOU 2903 O ALA A 277 1404 2054 1149 175 147 -1 O ATOM 2904 CB ALA A 277 -20.102 -0.627 13.537 1.00 10.86 C ANISOU 2904 CB ALA A 277 1271 1921 936 238 194 0 C ATOM 2905 N HIS A 278 -22.292 -1.587 11.511 1.00 11.07 N ANISOU 2905 N HIS A 278 1168 1948 1091 192 107 26 N ATOM 2906 CA HIS A 278 -23.605 -2.186 11.269 1.00 11.85 C ANISOU 2906 CA HIS A 278 1190 2027 1286 149 78 46 C ATOM 2907 C HIS A 278 -23.523 -3.351 10.287 1.00 12.27 C ANISOU 2907 C HIS A 278 1305 2076 1281 93 -4 38 C ATOM 2908 O HIS A 278 -24.298 -4.305 10.398 1.00 14.76 O ANISOU 2908 O HIS A 278 1597 2367 1644 41 -14 43 O ATOM 2909 CB HIS A 278 -24.581 -1.121 10.745 1.00 12.61 C ANISOU 2909 CB HIS A 278 1171 2108 1514 161 16 89 C ATOM 2910 CG HIS A 278 -24.933 -0.064 11.757 1.00 12.90 C ANISOU 2910 CG HIS A 278 1137 2115 1649 219 133 82 C ATOM 2911 ND1 HIS A 278 -25.487 1.152 11.408 1.00 13.62 N ANISOU 2911 ND1 HIS A 278 1135 2168 1872 264 92 114 N ATOM 2912 CD2 HIS A 278 -24.830 -0.055 13.112 1.00 12.87 C ANISOU 2912 CD2 HIS A 278 1170 2095 1624 229 294 41 C ATOM 2913 CE1 HIS A 278 -25.707 1.869 12.505 1.00 16.03 C ANISOU 2913 CE1 HIS A 278 1411 2431 2249 311 251 79 C ATOM 2914 NE2 HIS A 278 -25.308 1.163 13.552 1.00 13.57 N ANISOU 2914 NE2 HIS A 278 1195 2136 1825 279 379 32 N ATOM 2915 N ATHR A 279 -22.607 -3.274 9.316 0.53 13.84 N ANISOU 2915 N ATHR A 279 1595 2288 1377 88 -45 17 N ATOM 2916 N BTHR A 279 -22.621 -3.289 9.293 0.47 11.83 N ANISOU 2916 N BTHR A 279 1340 2032 1121 87 -47 17 N ATOM 2917 CA ATHR A 279 -22.468 -4.337 8.328 0.53 19.43 C ANISOU 2917 CA ATHR A 279 2404 2971 2009 25 -89 -14 C ATOM 2918 CA BTHR A 279 -22.546 -4.389 8.329 0.47 12.35 C ANISOU 2918 CA BTHR A 279 1504 2072 1116 21 -93 -12 C ATOM 2919 C ATHR A 279 -22.117 -5.663 8.986 0.53 16.01 C ANISOU 2919 C ATHR A 279 2010 2500 1574 35 -23 -51 C ATOM 2920 C BTHR A 279 -22.096 -5.686 8.977 0.47 12.23 C ANISOU 2920 C BTHR A 279 1533 2020 1093 36 -22 -52 C ATOM 2921 O ATHR A 279 -22.434 -6.725 8.444 0.53 12.90 O ANISOU 2921 O ATHR A 279 1684 2061 1155 -26 -56 -74 O ATOM 2922 O BTHR A 279 -22.282 -6.751 8.386 0.47 13.18 O ANISOU 2922 O BTHR A 279 1732 2095 1182 -22 -49 -80 O ATOM 2923 CB ATHR A 279 -21.406 -3.946 7.292 0.53 12.35 C ANISOU 2923 CB ATHR A 279 1614 2082 995 15 -75 -49 C ATOM 2924 CB BTHR A 279 -21.591 -4.097 7.157 0.47 19.64 C ANISOU 2924 CB BTHR A 279 2547 3000 1916 -1 -92 -47 C ATOM 2925 OG1ATHR A 279 -21.837 -2.769 6.605 0.53 19.93 O ANISOU 2925 OG1ATHR A 279 2572 3058 1941 -17 -167 4 O ATOM 2926 OG1BTHR A 279 -20.239 -4.004 7.625 0.47 14.05 O ANISOU 2926 OG1BTHR A 279 1842 2302 1193 70 22 -89 O ATOM 2927 CG2ATHR A 279 -21.190 -5.054 6.281 0.53 13.19 C ANISOU 2927 CG2ATHR A 279 1865 2142 1005 -58 -72 -107 C ATOM 2928 CG2BTHR A 279 -21.982 -2.840 6.420 0.47 12.89 C ANISOU 2928 CG2BTHR A 279 1694 2161 1042 -34 -189 7 C ATOM 2929 N ASN A 280 -21.493 -5.628 10.165 1.00 11.65 N ANISOU 2929 N ASN A 280 1435 1949 1044 100 48 -50 N ATOM 2930 CA ASN A 280 -21.193 -6.874 10.855 1.00 12.14 C ANISOU 2930 CA ASN A 280 1547 1953 1113 106 75 -61 C ATOM 2931 C ASN A 280 -22.454 -7.686 11.110 1.00 18.80 C ANISOU 2931 C ASN A 280 2384 2764 1994 30 59 -39 C ATOM 2932 O ASN A 280 -22.391 -8.914 11.196 1.00 16.88 O ANISOU 2932 O ASN A 280 2215 2454 1745 4 56 -52 O ATOM 2933 CB ASN A 280 -20.479 -6.620 12.188 1.00 12.72 C ANISOU 2933 CB ASN A 280 1621 2022 1191 158 106 -36 C ATOM 2934 CG ASN A 280 -20.081 -7.911 12.864 1.00 19.74 C ANISOU 2934 CG ASN A 280 2582 2829 2090 161 93 -27 C ATOM 2935 OD1 ASN A 280 -20.590 -8.263 13.940 1.00 18.41 O ANISOU 2935 OD1 ASN A 280 2458 2630 1907 120 102 14 O ATOM 2936 ND2 ASN A 280 -19.189 -8.650 12.210 1.00 16.47 N ANISOU 2936 ND2 ASN A 280 2192 2360 1704 205 84 -65 N ATOM 2937 N SER A 281 -23.597 -7.025 11.254 1.00 12.71 N ANISOU 2937 N SER A 281 1514 2027 1289 -6 54 -5 N ATOM 2938 CA SER A 281 -24.829 -7.782 11.475 1.00 13.62 C ANISOU 2938 CA SER A 281 1586 2111 1479 -93 51 18 C ATOM 2939 C SER A 281 -25.332 -8.480 10.218 1.00 17.29 C ANISOU 2939 C SER A 281 2079 2549 1941 -175 -66 10 C ATOM 2940 O SER A 281 -26.327 -9.211 10.299 1.00 17.22 O ANISOU 2940 O SER A 281 2032 2507 2003 -266 -91 31 O ATOM 2941 CB SER A 281 -25.910 -6.860 12.047 1.00 14.09 C ANISOU 2941 CB SER A 281 1489 2197 1666 -100 107 51 C ATOM 2942 OG SER A 281 -25.521 -6.445 13.354 1.00 13.84 O ANISOU 2942 OG SER A 281 1494 2165 1600 -61 239 45 O ATOM 2943 N VAL A 282 -24.677 -8.283 9.068 1.00 14.86 N ANISOU 2943 N VAL A 282 1857 2246 1542 -167 -130 -21 N ATOM 2944 CA VAL A 282 -25.071 -8.945 7.831 1.00 15.31 C ANISOU 2944 CA VAL A 282 2010 2262 1544 -273 -242 -38 C ATOM 2945 C VAL A 282 -24.243 -10.212 7.629 1.00 19.88 C ANISOU 2945 C VAL A 282 2759 2762 2034 -276 -183 -112 C ATOM 2946 O VAL A 282 -24.717 -11.168 7.005 1.00 21.44 O ANISOU 2946 O VAL A 282 3059 2891 2197 -381 -247 -135 O ATOM 2947 CB VAL A 282 -24.916 -7.993 6.617 1.00 15.55 C ANISOU 2947 CB VAL A 282 2090 2322 1497 -297 -336 -32 C ATOM 2948 CG1 VAL A 282 -25.264 -8.699 5.292 1.00 19.70 C ANISOU 2948 CG1 VAL A 282 2786 2789 1912 -441 -464 -54 C ATOM 2949 CG2 VAL A 282 -25.793 -6.764 6.796 1.00 15.66 C ANISOU 2949 CG2 VAL A 282 1926 2383 1642 -282 -417 52 C ATOM 2950 N VAL A 283 -23.011 -10.244 8.157 1.00 15.68 N ANISOU 2950 N VAL A 283 2253 2219 1486 -164 -72 -149 N ATOM 2951 CA VAL A 283 -22.022 -11.167 7.584 1.00 17.02 C ANISOU 2951 CA VAL A 283 2568 2300 1600 -142 -8 -234 C ATOM 2952 C VAL A 283 -22.128 -12.587 8.132 1.00 19.98 C ANISOU 2952 C VAL A 283 3009 2565 2019 -154 4 -245 C ATOM 2953 O VAL A 283 -21.821 -13.544 7.407 1.00 21.47 O ANISOU 2953 O VAL A 283 3341 2648 2168 -183 33 -321 O ATOM 2954 CB VAL A 283 -20.581 -10.647 7.749 1.00 21.67 C ANISOU 2954 CB VAL A 283 3126 2903 2204 -17 95 -267 C ATOM 2955 CG1 VAL A 283 -20.403 -9.307 7.061 1.00 31.76 C ANISOU 2955 CG1 VAL A 283 4378 4271 3420 -25 93 -263 C ATOM 2956 CG2 VAL A 283 -20.200 -10.567 9.200 1.00 22.88 C ANISOU 2956 CG2 VAL A 283 3181 3064 2447 72 103 -210 C ATOM 2957 N ASN A 284 -22.519 -12.775 9.395 1.00 18.60 N ANISOU 2957 N ASN A 284 2763 2392 1913 -143 -3 -176 N ATOM 2958 CA ASN A 284 -22.516 -14.134 9.952 1.00 22.92 C ANISOU 2958 CA ASN A 284 3401 2815 2492 -160 1 -174 C ATOM 2959 C ASN A 284 -23.340 -15.149 9.160 1.00 20.71 C ANISOU 2959 C ASN A 284 3233 2454 2183 -292 -48 -209 C ATOM 2960 O ASN A 284 -22.823 -16.251 8.906 1.00 21.73 O ANISOU 2960 O ASN A 284 3499 2445 2311 -279 -21 -266 O ATOM 2961 CB ASN A 284 -22.941 -14.103 11.426 1.00 28.34 C ANISOU 2961 CB ASN A 284 4035 3516 3217 -172 6 -86 C ATOM 2962 CG ASN A 284 -21.972 -13.318 12.274 1.00 36.81 C ANISOU 2962 CG ASN A 284 5059 4630 4296 -60 31 -55 C ATOM 2963 OD1 ASN A 284 -20.901 -12.943 11.799 1.00 23.14 O ANISOU 2963 OD1 ASN A 284 3308 2906 2577 37 43 -96 O ATOM 2964 ND2 ASN A 284 -22.328 -13.066 13.528 1.00 34.31 N ANISOU 2964 ND2 ASN A 284 4734 4333 3968 -90 47 14 N ATOM 2965 N PRO A 285 -24.579 -14.871 8.727 1.00 19.87 N ANISOU 2965 N PRO A 285 3075 2404 2069 -422 -129 -178 N ATOM 2966 CA PRO A 285 -25.295 -15.878 7.920 1.00 27.29 C ANISOU 2966 CA PRO A 285 4141 3253 2974 -571 -208 -210 C ATOM 2967 C PRO A 285 -24.500 -16.377 6.717 1.00 25.16 C ANISOU 2967 C PRO A 285 4077 2888 2593 -570 -181 -323 C ATOM 2968 O PRO A 285 -24.606 -17.557 6.362 1.00 24.98 O ANISOU 2968 O PRO A 285 4222 2729 2540 -648 -188 -377 O ATOM 2969 CB PRO A 285 -26.574 -15.137 7.493 1.00 20.47 C ANISOU 2969 CB PRO A 285 3145 2484 2148 -691 -334 -148 C ATOM 2970 CG PRO A 285 -26.811 -14.132 8.627 1.00 24.22 C ANISOU 2970 CG PRO A 285 3405 3067 2732 -609 -270 -74 C ATOM 2971 CD PRO A 285 -25.417 -13.681 9.002 1.00 31.32 C ANISOU 2971 CD PRO A 285 4342 3983 3576 -443 -164 -108 C ATOM 2972 N PHE A 286 -23.681 -15.517 6.101 1.00 22.54 N ANISOU 2972 N PHE A 286 3753 2614 2199 -493 -125 -369 N ATOM 2973 CA PHE A 286 -22.852 -15.954 4.977 1.00 23.36 C ANISOU 2973 CA PHE A 286 4065 2618 2194 -498 -36 -495 C ATOM 2974 C PHE A 286 -21.732 -16.876 5.423 1.00 25.18 C ANISOU 2974 C PHE A 286 4342 2712 2513 -361 112 -565 C ATOM 2975 O PHE A 286 -21.409 -17.844 4.724 1.00 27.06 O ANISOU 2975 O PHE A 286 4776 2795 2709 -393 189 -675 O ATOM 2976 CB PHE A 286 -22.276 -14.742 4.251 1.00 36.50 C ANISOU 2976 CB PHE A 286 5720 4377 3773 -469 8 -518 C ATOM 2977 CG PHE A 286 -23.283 -14.030 3.437 1.00 21.44 C ANISOU 2977 CG PHE A 286 3846 2542 1757 -624 -162 -465 C ATOM 2978 CD1 PHE A 286 -23.995 -12.978 3.972 1.00 25.05 C ANISOU 2978 CD1 PHE A 286 4091 3128 2300 -610 -278 -346 C ATOM 2979 CD2 PHE A 286 -23.571 -14.462 2.143 1.00 26.13 C ANISOU 2979 CD2 PHE A 286 4701 3055 2173 -797 -221 -531 C ATOM 2980 CE1 PHE A 286 -24.961 -12.330 3.214 1.00 36.28 C ANISOU 2980 CE1 PHE A 286 5519 4594 3672 -745 -471 -279 C ATOM 2981 CE2 PHE A 286 -24.531 -13.821 1.388 1.00 43.76 C ANISOU 2981 CE2 PHE A 286 6974 5339 4314 -957 -438 -457 C ATOM 2982 CZ PHE A 286 -25.228 -12.759 1.924 1.00 43.74 C ANISOU 2982 CZ PHE A 286 6717 5461 4440 -922 -574 -323 C ATOM 2983 N ILE A 287 -21.117 -16.588 6.574 1.00 26.01 N ANISOU 2983 N ILE A 287 4280 2853 2749 -212 145 -502 N ATOM 2984 CA ILE A 287 -20.056 -17.460 7.072 1.00 27.58 C ANISOU 2984 CA ILE A 287 4495 2904 3079 -74 234 -540 C ATOM 2985 C ILE A 287 -20.604 -18.845 7.369 1.00 26.27 C ANISOU 2985 C ILE A 287 4460 2581 2942 -139 185 -535 C ATOM 2986 O ILE A 287 -19.977 -19.859 7.036 1.00 29.09 O ANISOU 2986 O ILE A 287 4941 2753 3360 -87 268 -624 O ATOM 2987 CB ILE A 287 -19.391 -16.848 8.316 1.00 26.34 C ANISOU 2987 CB ILE A 287 4152 2813 3042 64 214 -445 C ATOM 2988 CG1 ILE A 287 -18.932 -15.432 8.007 1.00 25.07 C ANISOU 2988 CG1 ILE A 287 3872 2806 2847 105 254 -447 C ATOM 2989 CG2 ILE A 287 -18.210 -17.708 8.733 1.00 28.57 C ANISOU 2989 CG2 ILE A 287 4432 2926 3498 212 265 -468 C ATOM 2990 CD1 ILE A 287 -17.901 -15.399 6.895 1.00 34.96 C ANISOU 2990 CD1 ILE A 287 5173 4004 4107 157 412 -574 C ATOM 2991 N TYR A 288 -21.790 -18.916 7.991 1.00 25.26 N ANISOU 2991 N TYR A 288 4303 2508 2785 -258 66 -437 N ATOM 2992 CA TYR A 288 -22.390 -20.219 8.268 1.00 49.09 C ANISOU 2992 CA TYR A 288 7453 5377 5822 -352 18 -424 C ATOM 2993 C TYR A 288 -22.723 -20.943 6.977 1.00 27.29 C ANISOU 2993 C TYR A 288 4898 2505 2965 -477 27 -540 C ATOM 2994 O TYR A 288 -22.498 -22.151 6.865 1.00 32.66 O ANISOU 2994 O TYR A 288 5745 2985 3678 -481 60 -599 O ATOM 2995 CB TYR A 288 -23.656 -20.087 9.118 1.00 29.29 C ANISOU 2995 CB TYR A 288 4860 2958 3312 -482 -77 -304 C ATOM 2996 CG TYR A 288 -23.469 -19.374 10.432 1.00 23.68 C ANISOU 2996 CG TYR A 288 4002 2345 2652 -401 -69 -199 C ATOM 2997 CD1 TYR A 288 -22.396 -19.663 11.254 1.00 31.90 C ANISOU 2997 CD1 TYR A 288 5062 3299 3761 -261 -54 -168 C ATOM 2998 CD2 TYR A 288 -24.375 -18.393 10.845 1.00 24.60 C ANISOU 2998 CD2 TYR A 288 3966 2625 2756 -470 -84 -130 C ATOM 2999 CE1 TYR A 288 -22.230 -19.009 12.470 1.00 32.24 C ANISOU 2999 CE1 TYR A 288 5020 3419 3812 -219 -69 -69 C ATOM 3000 CE2 TYR A 288 -24.212 -17.726 12.058 1.00 23.59 C ANISOU 3000 CE2 TYR A 288 3748 2569 2645 -414 -51 -51 C ATOM 3001 CZ TYR A 288 -23.134 -18.036 12.860 1.00 33.37 C ANISOU 3001 CZ TYR A 288 5051 3724 3904 -302 -52 -21 C ATOM 3002 OH TYR A 288 -22.964 -17.357 14.055 1.00 23.54 O ANISOU 3002 OH TYR A 288 3764 2540 2639 -276 -41 58 O ATOM 3003 N ALA A 289 -23.247 -20.217 5.981 1.00 25.68 N ANISOU 3003 N ALA A 289 4712 2410 2634 -588 -15 -570 N ATOM 3004 CA ALA A 289 -23.628 -20.859 4.728 1.00 31.56 C ANISOU 3004 CA ALA A 289 5702 3047 3244 -750 -37 -674 C ATOM 3005 C ALA A 289 -22.414 -21.420 4.001 1.00 34.71 C ANISOU 3005 C ALA A 289 6290 3279 3621 -654 155 -836 C ATOM 3006 O ALA A 289 -22.463 -22.529 3.457 1.00 35.62 O ANISOU 3006 O ALA A 289 6643 3201 3690 -734 194 -936 O ATOM 3007 CB ALA A 289 -24.373 -19.870 3.830 1.00 26.31 C ANISOU 3007 CB ALA A 289 5030 2524 2442 -895 -160 -651 C ATOM 3008 N TYR A 290 -21.314 -20.665 3.974 1.00 32.46 N ANISOU 3008 N TYR A 290 5897 3051 3384 -488 296 -871 N ATOM 3009 CA TYR A 290 -20.145 -21.109 3.229 1.00 41.32 C ANISOU 3009 CA TYR A 290 7163 4016 4522 -396 525 -1037 C ATOM 3010 C TYR A 290 -19.310 -22.139 3.978 1.00 41.44 C ANISOU 3010 C TYR A 290 7139 3835 4771 -216 619 -1061 C ATOM 3011 O TYR A 290 -18.577 -22.899 3.337 1.00 35.40 O ANISOU 3011 O TYR A 290 6527 2869 4053 -162 809 -1215 O ATOM 3012 CB TYR A 290 -19.278 -19.906 2.847 1.00 42.45 C ANISOU 3012 CB TYR A 290 7193 4287 4649 -306 653 -1068 C ATOM 3013 CG TYR A 290 -19.766 -19.215 1.595 1.00 65.92 C ANISOU 3013 CG TYR A 290 10337 7347 7364 -494 630 -1108 C ATOM 3014 CD1 TYR A 290 -19.580 -19.797 0.348 1.00 75.49 C ANISOU 3014 CD1 TYR A 290 11732 8476 8474 -584 731 -1185 C ATOM 3015 CD2 TYR A 290 -20.424 -17.992 1.657 1.00 68.05 C ANISOU 3015 CD2 TYR A 290 10491 7820 7546 -565 464 -991 C ATOM 3016 CE1 TYR A 290 -20.027 -19.183 -0.804 1.00 53.39 C ANISOU 3016 CE1 TYR A 290 9058 5762 5465 -755 668 -1156 C ATOM 3017 CE2 TYR A 290 -20.874 -17.365 0.507 1.00 79.05 C ANISOU 3017 CE2 TYR A 290 12011 9285 8739 -728 393 -978 C ATOM 3018 CZ TYR A 290 -20.672 -17.968 -0.722 1.00 66.97 C ANISOU 3018 CZ TYR A 290 10689 7655 7103 -822 487 -1045 C ATOM 3019 OH TYR A 290 -21.118 -17.362 -1.875 1.00 73.95 O ANISOU 3019 OH TYR A 290 11702 8591 7803 -987 396 -995 O ATOM 3020 N ARG A 291 -19.418 -22.211 5.307 1.00 30.02 N ANISOU 3020 N ARG A 291 5512 2423 3473 -130 490 -913 N ATOM 3021 CA ARG A 291 -18.496 -23.027 6.087 1.00 33.62 C ANISOU 3021 CA ARG A 291 5910 2694 4170 57 535 -903 C ATOM 3022 C ARG A 291 -19.131 -24.195 6.823 1.00 43.87 C ANISOU 3022 C ARG A 291 7314 3839 5514 -1 406 -828 C ATOM 3023 O ARG A 291 -18.396 -25.089 7.257 1.00 36.74 O ANISOU 3023 O ARG A 291 6430 2721 4809 138 435 -835 O ATOM 3024 CB ARG A 291 -17.741 -22.160 7.112 1.00 41.13 C ANISOU 3024 CB ARG A 291 6588 3768 5273 222 489 -784 C ATOM 3025 CG ARG A 291 -16.745 -21.196 6.483 1.00 42.22 C ANISOU 3025 CG ARG A 291 6600 3993 5448 322 649 -866 C ATOM 3026 CD ARG A 291 -15.659 -20.784 7.470 1.00 33.96 C ANISOU 3026 CD ARG A 291 5304 2960 4640 515 614 -775 C ATOM 3027 NE ARG A 291 -15.034 -21.926 8.141 1.00 59.16 N ANISOU 3027 NE ARG A 291 8483 5912 8082 652 573 -745 N ATOM 3028 CZ ARG A 291 -13.848 -22.441 7.823 1.00 56.39 C ANISOU 3028 CZ ARG A 291 8058 5369 7998 825 723 -840 C ATOM 3029 NH1 ARG A 291 -13.141 -21.921 6.832 1.00 45.09 N ANISOU 3029 NH1 ARG A 291 6568 3965 6598 867 961 -985 N ATOM 3030 NH2 ARG A 291 -13.363 -23.478 8.502 1.00 44.81 N ANISOU 3030 NH2 ARG A 291 6574 3667 6784 953 639 -787 N ATOM 3031 N ILE A 292 -20.450 -24.231 6.976 1.00 30.41 N ANISOU 3031 N ILE A 292 5671 2223 3659 -201 264 -752 N ATOM 3032 CA ILE A 292 -21.109 -25.266 7.770 1.00 33.49 C ANISOU 3032 CA ILE A 292 6153 2484 4086 -283 148 -663 C ATOM 3033 C ILE A 292 -22.198 -25.920 6.927 1.00 42.13 C ANISOU 3033 C ILE A 292 7462 3516 5029 -517 108 -730 C ATOM 3034 O ILE A 292 -23.276 -25.341 6.742 1.00 30.39 O ANISOU 3034 O ILE A 292 5927 2203 3418 -692 8 -677 O ATOM 3035 CB ILE A 292 -21.686 -24.705 9.071 1.00 31.65 C ANISOU 3035 CB ILE A 292 5758 2413 3856 -317 20 -480 C ATOM 3036 CG1 ILE A 292 -20.630 -23.843 9.767 1.00 28.82 C ANISOU 3036 CG1 ILE A 292 5204 2142 3603 -119 36 -422 C ATOM 3037 CG2 ILE A 292 -22.170 -25.858 9.964 1.00 31.90 C ANISOU 3037 CG2 ILE A 292 5913 2276 3931 -397 -71 -387 C ATOM 3038 CD1 ILE A 292 -21.061 -23.300 11.098 1.00 31.94 C ANISOU 3038 CD1 ILE A 292 5491 2666 3978 -154 -67 -257 C ATOM 3039 N ARG A 293 -21.930 -27.146 6.446 1.00 40.97 N ANISOU 3039 N ARG A 293 7504 3097 4967 0 361 -1270 N ATOM 3040 CA ARG A 293 -22.856 -27.857 5.563 1.00 44.20 C ANISOU 3040 CA ARG A 293 8208 3345 5240 -173 256 -1418 C ATOM 3041 C ARG A 293 -24.260 -27.949 6.147 1.00 49.24 C ANISOU 3041 C ARG A 293 8961 3933 5816 -473 -7 -1055 C ATOM 3042 O ARG A 293 -25.252 -27.793 5.426 1.00 40.99 O ANISOU 3042 O ARG A 293 8050 3015 4510 -704 -44 -1077 O ATOM 3043 CB ARG A 293 -22.348 -29.276 5.274 1.00 51.25 C ANISOU 3043 CB ARG A 293 9234 3778 6459 35 147 -1773 C ATOM 3044 CG ARG A 293 -20.926 -29.387 4.771 1.00 77.74 C ANISOU 3044 CG ARG A 293 12416 7162 9959 376 397 -2211 C ATOM 3045 CD ARG A 293 -20.602 -30.831 4.403 1.00 82.00 C ANISOU 3045 CD ARG A 293 13105 7197 10856 595 256 -2625 C ATOM 3046 NE ARG A 293 -19.195 -31.013 4.065 1.00 79.68 N ANISOU 3046 NE ARG A 293 12525 6956 10795 963 481 -3062 N ATOM 3047 CZ ARG A 293 -18.694 -32.117 3.516 1.00128.41 C ANISOU 3047 CZ ARG A 293 18739 12872 17179 1144 528 -3395 C ATOM 3048 NH1 ARG A 293 -19.485 -33.145 3.233 1.00 92.09 N ANISOU 3048 NH1 ARG A 293 14356 7918 12715 986 345 -3455 N ATOM 3049 NH2 ARG A 293 -17.398 -32.193 3.243 1.00137.18 N ANISOU 3049 NH2 ARG A 293 19606 14134 18383 1485 713 -3667 N ATOM 3050 N GLU A 294 -24.371 -28.243 7.442 1.00 40.41 N ANISOU 3050 N GLU A 294 7777 2661 4916 -484 -201 -727 N ATOM 3051 CA GLU A 294 -25.698 -28.424 8.018 1.00 49.19 C ANISOU 3051 CA GLU A 294 8966 3755 5968 -807 -409 -407 C ATOM 3052 C GLU A 294 -26.513 -27.137 7.943 1.00 40.63 C ANISOU 3052 C GLU A 294 7738 3133 4567 -992 -310 -257 C ATOM 3053 O GLU A 294 -27.727 -27.180 7.719 1.00 36.26 O ANISOU 3053 O GLU A 294 7243 2651 3883 -1259 -426 -183 O ATOM 3054 CB GLU A 294 -25.593 -28.921 9.457 1.00 45.07 C ANISOU 3054 CB GLU A 294 8405 3055 5665 -806 -599 -48 C ATOM 3055 CG GLU A 294 -26.882 -29.535 9.975 1.00 53.26 C ANISOU 3055 CG GLU A 294 9570 3968 6699 -1180 -806 243 C ATOM 3056 CD GLU A 294 -27.210 -30.851 9.299 1.00 50.51 C ANISOU 3056 CD GLU A 294 9432 3198 6561 -1250 -948 58 C ATOM 3057 OE1 GLU A 294 -26.269 -31.619 9.010 1.00 74.80 O ANISOU 3057 OE1 GLU A 294 12597 5908 9914 -968 -982 -163 O ATOM 3058 OE2 GLU A 294 -28.407 -31.118 9.051 1.00 53.85 O ANISOU 3058 OE2 GLU A 294 9852 3709 6899 -1555 -1011 96 O ATOM 3059 N PHE A 295 -25.864 -25.977 8.106 1.00 33.57 N ANISOU 3059 N PHE A 295 6637 2533 3584 -848 -112 -232 N ATOM 3060 CA PHE A 295 -26.581 -24.723 7.904 1.00 31.02 C ANISOU 3060 CA PHE A 295 6202 2565 3020 -976 -32 -123 C ATOM 3061 C PHE A 295 -26.926 -24.534 6.436 1.00 34.85 C ANISOU 3061 C PHE A 295 6854 3130 3258 -1031 27 -318 C ATOM 3062 O PHE A 295 -28.083 -24.271 6.086 1.00 32.04 O ANISOU 3062 O PHE A 295 6529 2910 2734 -1214 -99 -238 O ATOM 3063 CB PHE A 295 -25.753 -23.535 8.406 1.00 28.80 C ANISOU 3063 CB PHE A 295 5681 2504 2756 -829 160 -72 C ATOM 3064 CG PHE A 295 -26.049 -23.151 9.822 1.00 38.30 C ANISOU 3064 CG PHE A 295 6678 3846 4030 -882 76 163 C ATOM 3065 CD1 PHE A 295 -27.285 -22.618 10.164 1.00 25.94 C ANISOU 3065 CD1 PHE A 295 5026 2479 2351 -1073 -2 317 C ATOM 3066 CD2 PHE A 295 -25.096 -23.322 10.814 1.00 30.04 C ANISOU 3066 CD2 PHE A 295 5496 2774 3143 -732 68 199 C ATOM 3067 CE1 PHE A 295 -27.569 -22.264 11.475 1.00 25.01 C ANISOU 3067 CE1 PHE A 295 4698 2553 2252 -1133 -42 474 C ATOM 3068 CE2 PHE A 295 -25.371 -22.970 12.131 1.00 32.43 C ANISOU 3068 CE2 PHE A 295 5618 3275 3430 -799 -10 394 C ATOM 3069 CZ PHE A 295 -26.607 -22.428 12.455 1.00 25.20 C ANISOU 3069 CZ PHE A 295 4624 2579 2372 -1009 -40 515 C ATOM 3070 N ARG A 296 -25.921 -24.670 5.568 1.00 36.93 N ANISOU 3070 N ARG A 296 7203 3353 3477 -872 215 -589 N ATOM 3071 CA ARG A 296 -26.103 -24.443 4.141 1.00 35.65 C ANISOU 3071 CA ARG A 296 7217 3343 2987 -928 306 -775 C ATOM 3072 C ARG A 296 -27.230 -25.297 3.578 1.00 37.79 C ANISOU 3072 C ARG A 296 7687 3521 3149 -1116 53 -876 C ATOM 3073 O ARG A 296 -28.037 -24.822 2.770 1.00 43.08 O ANISOU 3073 O ARG A 296 8443 4417 3509 -1248 -23 -850 O ATOM 3074 CB ARG A 296 -24.788 -24.729 3.412 1.00 38.16 C ANISOU 3074 CB ARG A 296 7571 3639 3288 -744 574 -1116 C ATOM 3075 CG ARG A 296 -24.852 -24.538 1.920 1.00 40.89 C ANISOU 3075 CG ARG A 296 8115 4210 3211 -819 713 -1328 C ATOM 3076 CD ARG A 296 -23.462 -24.568 1.296 1.00 49.55 C ANISOU 3076 CD ARG A 296 9165 5400 4263 -659 1075 -1656 C ATOM 3077 NE ARG A 296 -22.765 -25.844 1.450 1.00 46.10 N ANISOU 3077 NE ARG A 296 8705 4661 4150 -456 1065 -2039 N ATOM 3078 CZ ARG A 296 -21.757 -26.058 2.291 1.00 45.80 C ANISOU 3078 CZ ARG A 296 8429 4460 4512 -226 1133 -2089 C ATOM 3079 NH1 ARG A 296 -21.183 -27.251 2.347 1.00 49.01 N ANISOU 3079 NH1 ARG A 296 8834 4548 5241 -3 1074 -2440 N ATOM 3080 NH2 ARG A 296 -21.319 -25.082 3.080 1.00 42.80 N ANISOU 3080 NH2 ARG A 296 7805 4222 4234 -204 1231 -1809 N ATOM 3081 N GLN A 297 -27.303 -26.563 3.999 1.00 39.52 N ANISOU 3081 N GLN A 297 7984 3390 3641 -1137 -108 -983 N ATOM 3082 CA GLN A 297 -28.343 -27.458 3.500 1.00 42.19 C ANISOU 3082 CA GLN A 297 8500 3589 3942 -1360 -352 -1120 C ATOM 3083 C GLN A 297 -29.716 -27.073 4.039 1.00 40.53 C ANISOU 3083 C GLN A 297 8166 3542 3691 -1619 -559 -811 C ATOM 3084 O GLN A 297 -30.720 -27.168 3.326 1.00 42.22 O ANISOU 3084 O GLN A 297 8445 3882 3715 -1815 -731 -900 O ATOM 3085 CB GLN A 297 -28.008 -28.901 3.871 1.00 45.14 C ANISOU 3085 CB GLN A 297 8999 3455 4697 -1327 -472 -1288 C ATOM 3086 CG GLN A 297 -26.814 -29.481 3.129 1.00 65.71 C ANISOU 3086 CG GLN A 297 11674 5906 7387 -1047 -303 -1717 C ATOM 3087 CD GLN A 297 -26.462 -30.879 3.603 1.00 96.67 C ANISOU 3087 CD GLN A 297 15610 9316 11803 -931 -454 -1817 C ATOM 3088 OE1 GLN A 297 -26.836 -31.283 4.705 1.00 97.93 O ANISOU 3088 OE1 GLN A 297 15749 9232 12228 -1030 -638 -1472 O ATOM 3089 NE2 GLN A 297 -25.745 -31.627 2.770 1.00 76.17 N ANISOU 3089 NE2 GLN A 297 13025 6581 9336 -724 -372 -2283 N ATOM 3090 N THR A 298 -29.783 -26.645 5.300 1.00 40.69 N ANISOU 3090 N THR A 298 7979 3603 3878 -1622 -549 -483 N ATOM 3091 CA THR A 298 -31.064 -26.231 5.856 1.00 36.65 C ANISOU 3091 CA THR A 298 7287 3307 3333 -1854 -696 -242 C ATOM 3092 C THR A 298 -31.537 -24.922 5.228 1.00 35.28 C ANISOU 3092 C THR A 298 7003 3516 2887 -1808 -674 -197 C ATOM 3093 O THR A 298 -32.727 -24.771 4.932 1.00 36.27 O ANISOU 3093 O THR A 298 7049 3822 2911 -1981 -864 -176 O ATOM 3094 CB THR A 298 -30.966 -26.094 7.374 1.00 38.53 C ANISOU 3094 CB THR A 298 7328 3551 3761 -1868 -661 52 C ATOM 3095 OG1 THR A 298 -30.388 -27.285 7.927 1.00 36.64 O ANISOU 3095 OG1 THR A 298 7234 2917 3769 -1866 -713 74 O ATOM 3096 CG2 THR A 298 -32.351 -25.875 7.963 1.00 35.40 C ANISOU 3096 CG2 THR A 298 6717 3392 3341 -2147 -786 233 C ATOM 3097 N PHE A 299 -30.619 -23.964 5.022 1.00 33.57 N ANISOU 3097 N PHE A 299 6769 3408 2578 -1581 -461 -173 N ATOM 3098 CA PHE A 299 -30.960 -22.747 4.284 1.00 33.25 C ANISOU 3098 CA PHE A 299 6703 3641 2291 -1529 -454 -94 C ATOM 3099 C PHE A 299 -31.553 -23.085 2.923 1.00 38.61 C ANISOU 3099 C PHE A 299 7593 4413 2664 -1626 -618 -261 C ATOM 3100 O PHE A 299 -32.548 -22.485 2.496 1.00 38.19 O ANISOU 3100 O PHE A 299 7480 4581 2450 -1682 -817 -160 O ATOM 3101 CB PHE A 299 -29.726 -21.853 4.069 1.00 35.33 C ANISOU 3101 CB PHE A 299 6987 3938 2500 -1330 -169 -66 C ATOM 3102 CG PHE A 299 -29.171 -21.220 5.325 1.00 29.32 C ANISOU 3102 CG PHE A 299 5983 3158 1998 -1230 -31 77 C ATOM 3103 CD1 PHE A 299 -29.878 -21.228 6.510 1.00 27.88 C ANISOU 3103 CD1 PHE A 299 5582 3014 1998 -1304 -153 205 C ATOM 3104 CD2 PHE A 299 -27.925 -20.599 5.296 1.00 28.68 C ANISOU 3104 CD2 PHE A 299 5875 3068 1954 -1088 234 54 C ATOM 3105 CE1 PHE A 299 -29.344 -20.631 7.669 1.00 33.82 C ANISOU 3105 CE1 PHE A 299 6113 3805 2932 -1216 -33 290 C ATOM 3106 CE2 PHE A 299 -27.381 -20.008 6.446 1.00 26.55 C ANISOU 3106 CE2 PHE A 299 5366 2804 1919 -1008 336 134 C ATOM 3107 CZ PHE A 299 -28.098 -20.025 7.627 1.00 26.68 C ANISOU 3107 CZ PHE A 299 5188 2869 2079 -1062 190 243 C ATOM 3108 N AARG A 300 -30.920 -24.022 2.212 0.54 38.80 N ANISOU 3108 N AARG A 300 7852 4289 2600 -1622 -551 -549 N ATOM 3109 N BARG A 300 -30.951 -24.044 2.218 0.46 42.03 N ANISOU 3109 N BARG A 300 8261 4697 3013 -1627 -558 -550 N ATOM 3110 CA AARG A 300 -31.435 -24.460 0.917 0.54 60.92 C ANISOU 3110 CA AARG A 300 10807 7210 5128 -1701 -693 -763 C ATOM 3111 CA BARG A 300 -31.470 -24.412 0.905 0.46 57.17 C ANISOU 3111 CA BARG A 300 10327 6749 4646 -1701 -698 -752 C ATOM 3112 C AARG A 300 -32.874 -24.947 1.037 0.54 43.89 C ANISOU 3112 C AARG A 300 8525 5089 3064 -1912 -1020 -752 C ATOM 3113 C BARG A 300 -32.880 -24.980 1.005 0.46 44.02 C ANISOU 3113 C BARG A 300 8546 5103 3078 -1914 -1023 -762 C ATOM 3114 O AARG A 300 -33.745 -24.542 0.258 0.54 53.18 O ANISOU 3114 O AARG A 300 9628 6530 4048 -1932 -1200 -719 O ATOM 3115 O BARG A 300 -33.743 -24.659 0.179 0.46 47.32 O ANISOU 3115 O BARG A 300 8900 5778 3300 -1939 -1205 -752 O ATOM 3116 CB AARG A 300 -30.544 -25.564 0.340 0.54 46.76 C ANISOU 3116 CB AARG A 300 9189 5219 3359 -1636 -552 -1140 C ATOM 3117 CB BARG A 300 -30.529 -25.404 0.223 0.46 51.37 C ANISOU 3117 CB BARG A 300 9771 5853 3894 -1623 -538 -1122 C ATOM 3118 CG AARG A 300 -29.300 -25.072 -0.391 0.54 90.97 C ANISOU 3118 CG AARG A 300 14854 10960 8750 -1444 -224 -1238 C ATOM 3119 CG BARG A 300 -29.204 -24.787 -0.192 0.46 72.74 C ANISOU 3119 CG BARG A 300 12520 8663 6453 -1428 -188 -1156 C ATOM 3120 CD AARG A 300 -28.734 -26.147 -1.324 0.54 53.07 C ANISOU 3120 CD AARG A 300 10159 6105 3902 -1380 -139 -1691 C ATOM 3121 CD BARG A 300 -28.457 -25.655 -1.189 0.46 86.25 C ANISOU 3121 CD BARG A 300 14334 10367 8071 -1341 -42 -1576 C ATOM 3122 NE AARG A 300 -27.815 -27.061 -0.648 0.54 60.34 N ANISOU 3122 NE AARG A 300 11079 6645 5203 -1251 -24 -1923 N ATOM 3123 NE BARG A 300 -27.249 -24.992 -1.671 0.46 64.62 N ANISOU 3123 NE BARG A 300 11564 7818 5169 -1195 314 -1601 N ATOM 3124 CZ AARG A 300 -26.494 -26.914 -0.636 0.54 67.16 C ANISOU 3124 CZ AARG A 300 11886 7503 6127 -1046 286 -2058 C ATOM 3125 CZ BARG A 300 -27.225 -24.124 -2.676 0.46 51.64 C ANISOU 3125 CZ BARG A 300 9934 6533 3154 -1210 408 -1468 C ATOM 3126 NH1AARG A 300 -25.933 -25.889 -1.264 0.54 63.60 N ANISOU 3126 NH1AARG A 300 11385 7413 5367 -1003 544 -1964 N ATOM 3127 NH1BARG A 300 -26.080 -23.567 -3.045 0.46 82.82 N ANISOU 3127 NH1BARG A 300 13825 10639 7002 -1124 752 -1476 N ATOM 3128 NH2AARG A 300 -25.731 -27.791 0.004 0.54 57.10 N ANISOU 3128 NH2AARG A 300 10572 5860 5265 -881 322 -2262 N ATOM 3129 NH2BARG A 300 -28.346 -23.809 -3.313 0.46 53.08 N ANISOU 3129 NH2BARG A 300 10165 6917 3085 -1313 145 -1315 N ATOM 3130 N LYS A 301 -33.141 -25.817 2.015 1.00 52.81 N ANISOU 3130 N LYS A 301 9600 5955 4510 -2076 -1099 -764 N ATOM 3131 CA LYS A 301 -34.485 -26.368 2.180 1.00 56.16 C ANISOU 3131 CA LYS A 301 9851 6418 5071 -2321 -1355 -757 C ATOM 3132 C LYS A 301 -35.500 -25.282 2.524 1.00 43.95 C ANISOU 3132 C LYS A 301 8014 5212 3474 -2354 -1485 -513 C ATOM 3133 O LYS A 301 -36.633 -25.312 2.037 1.00 46.47 O ANISOU 3133 O LYS A 301 8167 5735 3753 -2451 -1703 -563 O ATOM 3134 CB LYS A 301 -34.489 -27.460 3.254 1.00 45.63 C ANISOU 3134 CB LYS A 301 8497 4728 4114 -2496 -1355 -718 C ATOM 3135 CG LYS A 301 -33.840 -28.766 2.832 1.00 86.00 C ANISOU 3135 CG LYS A 301 13831 9455 9391 -2458 -1324 -997 C ATOM 3136 CD LYS A 301 -34.053 -29.856 3.880 1.00 59.10 C ANISOU 3136 CD LYS A 301 10379 5690 6386 -2627 -1372 -863 C ATOM 3137 CE LYS A 301 -33.286 -31.120 3.519 1.00 73.38 C ANISOU 3137 CE LYS A 301 12391 7049 8441 -2518 -1356 -1141 C ATOM 3138 NZ LYS A 301 -33.343 -32.139 4.606 1.00104.16 N ANISOU 3138 NZ LYS A 301 16271 10561 12744 -2633 -1402 -926 N ATOM 3139 N ILE A 302 -35.123 -24.320 3.367 1.00 40.47 N ANISOU 3139 N ILE A 302 7467 4841 3070 -2245 -1361 -286 N ATOM 3140 CA ILE A 302 -36.045 -23.237 3.708 1.00 41.03 C ANISOU 3140 CA ILE A 302 7217 5217 3155 -2209 -1473 -100 C ATOM 3141 C ILE A 302 -36.361 -22.395 2.480 1.00 53.93 C ANISOU 3141 C ILE A 302 8891 7069 4531 -2028 -1606 -83 C ATOM 3142 O ILE A 302 -37.520 -22.044 2.224 1.00 51.38 O ANISOU 3142 O ILE A 302 8335 6975 4212 -2041 -1851 -63 O ATOM 3143 CB ILE A 302 -35.469 -22.364 4.832 1.00 42.41 C ANISOU 3143 CB ILE A 302 7210 5393 3511 -2032 -1236 108 C ATOM 3144 CG1 ILE A 302 -35.403 -23.141 6.145 1.00 36.57 C ANISOU 3144 CG1 ILE A 302 6350 4524 3020 -2201 -1132 162 C ATOM 3145 CG2 ILE A 302 -36.311 -21.108 4.979 1.00 38.30 C ANISOU 3145 CG2 ILE A 302 6386 5147 3018 -1915 -1349 231 C ATOM 3146 CD1 ILE A 302 -34.474 -22.504 7.165 1.00 36.43 C ANISOU 3146 CD1 ILE A 302 6243 4482 3118 -2017 -886 300 C ATOM 3147 N ILE A 303 -35.330 -22.035 1.716 1.00 45.88 N ANISOU 3147 N ILE A 303 8135 5994 3305 -1845 -1432 -76 N ATOM 3148 CA ILE A 303 -35.536 -21.178 0.552 1.00 49.77 C ANISOU 3148 CA ILE A 303 8683 6685 3541 -1678 -1527 15 C ATOM 3149 C ILE A 303 -36.345 -21.908 -0.511 1.00 52.00 C ANISOU 3149 C ILE A 303 8998 7116 3642 -1773 -1772 -189 C ATOM 3150 O ILE A 303 -37.335 -21.379 -1.027 1.00 52.98 O ANISOU 3150 O ILE A 303 8983 7475 3673 -1716 -2046 -116 O ATOM 3151 CB ILE A 303 -34.186 -20.691 -0.002 1.00 43.17 C ANISOU 3151 CB ILE A 303 8086 5782 2536 -1522 -1222 74 C ATOM 3152 CG1 ILE A 303 -33.502 -19.768 1.010 1.00 48.15 C ANISOU 3152 CG1 ILE A 303 8626 6296 3374 -1412 -1008 280 C ATOM 3153 CG2 ILE A 303 -34.382 -19.996 -1.355 1.00 47.21 C ANISOU 3153 CG2 ILE A 303 8702 6510 2724 -1409 -1320 180 C ATOM 3154 CD1 ILE A 303 -31.988 -19.807 0.945 1.00 54.40 C ANISOU 3154 CD1 ILE A 303 9574 6952 4145 -1346 -638 224 C ATOM 3155 N ARG A 304 -35.939 -23.136 -0.846 1.00 64.72 N ANISOU 3155 N ARG A 304 10781 8589 5220 -1899 -1699 -476 N ATOM 3156 CA ARG A 304 -36.647 -23.909 -1.863 1.00 74.79 C ANISOU 3156 CA ARG A 304 12084 10002 6331 -1997 -1922 -739 C ATOM 3157 C ARG A 304 -38.109 -24.101 -1.488 1.00 59.62 C ANISOU 3157 C ARG A 304 9849 8200 4602 -2153 -2232 -753 C ATOM 3158 O ARG A 304 -39.011 -23.791 -2.274 1.00100.16 O ANISOU 3158 O ARG A 304 14872 13619 9565 -2109 -2505 -781 O ATOM 3159 CB ARG A 304 -35.956 -25.259 -2.070 1.00 55.46 C ANISOU 3159 CB ARG A 304 9839 7305 3928 -2103 -1787 -1089 C ATOM 3160 CG ARG A 304 -34.649 -25.160 -2.846 1.00115.31 C ANISOU 3160 CG ARG A 304 17675 14895 11242 -1936 -1511 -1198 C ATOM 3161 CD ARG A 304 -33.883 -26.474 -2.856 1.00104.28 C ANISOU 3161 CD ARG A 304 16429 13199 9994 -1979 -1367 -1580 C ATOM 3162 NE ARG A 304 -32.563 -26.315 -3.462 1.00146.43 N ANISOU 3162 NE ARG A 304 21933 18582 15120 -1801 -1055 -1707 N ATOM 3163 CZ ARG A 304 -31.602 -27.233 -3.420 1.00125.91 C ANISOU 3163 CZ ARG A 304 19432 15727 12680 -1738 -864 -2036 C ATOM 3164 NH1 ARG A 304 -30.432 -26.999 -3.999 1.00107.01 N ANISOU 3164 NH1 ARG A 304 17116 13453 10090 -1571 -562 -2166 N ATOM 3165 NH2 ARG A 304 -31.809 -28.385 -2.797 1.00122.91 N ANISOU 3165 NH2 ARG A 304 19042 14963 12695 -1835 -975 -2228 N ATOM 3166 N SER A 305 -38.365 -24.601 -0.287 1.00 61.66 N ANISOU 3166 N SER A 305 9941 8275 5213 -2336 -2189 -731 N ATOM 3167 CA SER A 305 -39.732 -24.777 0.180 1.00 93.16 C ANISOU 3167 CA SER A 305 13566 12410 9420 -2515 -2414 -747 C ATOM 3168 C SER A 305 -40.368 -23.420 0.472 1.00 84.29 C ANISOU 3168 C SER A 305 12155 11565 8306 -2337 -2537 -513 C ATOM 3169 O SER A 305 -41.270 -23.309 1.301 1.00118.12 O ANISOU 3169 O SER A 305 16067 15971 12842 -2444 -2613 -480 O ATOM 3170 CB SER A 305 -39.766 -25.666 1.425 1.00 88.82 C ANISOU 3170 CB SER A 305 12917 11606 9224 -2781 -2278 -736 C ATOM 3171 OG SER A 305 -39.097 -26.895 1.192 1.00 76.89 O ANISOU 3171 OG SER A 305 11694 9753 7768 -2893 -2184 -937 O TER 3172 SER A 305 HETATM 3173 NA NA A2400 -23.495 -8.468 16.468 1.00 33.19 NA ANISOU 3173 NA NA A2400 3339 4145 5125 -761 1018 -1382 NA HETATM 3174 C1 ZMA A2401 -21.311 13.678 14.293 1.00 32.45 C ANISOU 3174 C1 ZMA A2401 6410 2370 3550 -1477 -1535 419 C HETATM 3175 C2 ZMA A2401 -20.980 15.032 14.472 1.00 35.63 C ANISOU 3175 C2 ZMA A2401 7235 2365 3936 -518 -1299 95 C HETATM 3176 C3 ZMA A2401 -19.794 15.359 15.144 1.00 37.25 C ANISOU 3176 C3 ZMA A2401 7520 2490 4143 -383 -689 53 C HETATM 3177 O4 ZMA A2401 -19.484 16.683 15.307 1.00 43.91 O ANISOU 3177 O4 ZMA A2401 9059 2889 4735 -1451 -1550 239 O HETATM 3178 C5 ZMA A2401 -18.935 14.345 15.639 1.00 24.47 C ANISOU 3178 C5 ZMA A2401 3585 2263 3448 354 -305 338 C HETATM 3179 C6 ZMA A2401 -19.284 13.010 15.464 1.00 18.39 C ANISOU 3179 C6 ZMA A2401 2274 1901 2814 -424 -112 24 C HETATM 3180 C7 ZMA A2401 -20.455 12.667 14.791 1.00 23.96 C ANISOU 3180 C7 ZMA A2401 4257 1914 2932 -558 -501 611 C HETATM 3181 C8 ZMA A2401 -20.853 11.207 14.576 1.00 17.18 C ANISOU 3181 C8 ZMA A2401 2747 1837 1942 -543 -154 802 C HETATM 3182 C9 ZMA A2401 -21.846 10.983 15.738 1.00 14.73 C ANISOU 3182 C9 ZMA A2401 2079 1906 1613 263 466 822 C HETATM 3183 N10 ZMA A2401 -22.240 9.591 15.928 1.00 13.91 N ANISOU 3183 N10 ZMA A2401 2011 1998 1275 813 -77 461 N HETATM 3184 C11 ZMA A2401 -21.430 8.735 16.591 1.00 11.28 C ANISOU 3184 C11 ZMA A2401 1094 1987 1204 199 345 -2 C HETATM 3185 N12 ZMA A2401 -21.830 7.437 16.760 1.00 10.71 N ANISOU 3185 N12 ZMA A2401 700 2260 1108 155 -211 -65 N HETATM 3186 N13 ZMA A2401 -20.232 9.174 17.065 1.00 12.28 N ANISOU 3186 N13 ZMA A2401 1496 1885 1286 220 -218 -275 N HETATM 3187 C14 ZMA A2401 -19.406 8.324 17.737 1.00 11.87 C ANISOU 3187 C14 ZMA A2401 1068 1991 1451 95 -266 -98 C HETATM 3188 N15 ZMA A2401 -18.239 8.804 18.183 1.00 10.73 N ANISOU 3188 N15 ZMA A2401 844 1913 1320 -119 -24 -164 N HETATM 3189 N16 ZMA A2401 -19.811 7.053 17.896 1.00 13.38 N ANISOU 3189 N16 ZMA A2401 1708 2091 1286 801 261 252 N HETATM 3190 N17 ZMA A2401 -19.130 6.050 18.534 1.00 10.67 N ANISOU 3190 N17 ZMA A2401 844 2256 953 318 278 27 N HETATM 3191 C18 ZMA A2401 -20.996 6.625 17.427 1.00 11.56 C ANISOU 3191 C18 ZMA A2401 1331 2051 1010 461 -192 -176 C HETATM 3192 N19 ZMA A2401 -21.187 5.323 17.737 1.00 11.65 N ANISOU 3192 N19 ZMA A2401 1027 2260 1139 -254 62 -201 N HETATM 3193 C20 ZMA A2401 -20.039 5.051 18.393 1.00 9.94 C ANISOU 3193 C20 ZMA A2401 872 1929 975 405 -331 -10 C HETATM 3194 C21 ZMA A2401 -19.718 3.729 18.926 1.00 11.78 C ANISOU 3194 C21 ZMA A2401 1631 2100 746 165 -78 492 C HETATM 3195 C22 ZMA A2401 -20.596 2.692 19.155 1.00 11.97 C ANISOU 3195 C22 ZMA A2401 1856 1877 815 663 -228 228 C HETATM 3196 C23 ZMA A2401 -19.722 1.712 19.653 1.00 13.03 C ANISOU 3196 C23 ZMA A2401 1905 2006 1040 449 -231 210 C HETATM 3197 C24 ZMA A2401 -18.432 2.219 19.691 1.00 15.14 C ANISOU 3197 C24 ZMA A2401 2595 1980 1178 72 638 416 C HETATM 3198 O25 ZMA A2401 -18.408 3.527 19.220 1.00 11.47 O ANISOU 3198 O25 ZMA A2401 1116 2142 1101 41 -238 381 O HETATM 3199 C1 CLR A2402 -36.390 7.595 28.269 1.00116.62 C ANISOU 3199 C1 CLR A2402 11616 17415 15281 924 -1523 885 C HETATM 3200 C2 CLR A2402 -36.052 8.980 28.860 1.00116.25 C ANISOU 3200 C2 CLR A2402 11458 17423 15287 838 -1525 889 C HETATM 3201 C3 CLR A2402 -37.247 9.628 29.504 1.00118.13 C ANISOU 3201 C3 CLR A2402 12109 17435 15340 799 -1530 874 C HETATM 3202 C4 CLR A2402 -37.899 8.699 30.546 1.00119.08 C ANISOU 3202 C4 CLR A2402 12449 17435 15362 880 -1491 870 C HETATM 3203 C5 CLR A2402 -38.084 7.279 30.064 1.00119.17 C ANISOU 3203 C5 CLR A2402 12499 17421 15358 890 -1473 853 C HETATM 3204 C6 CLR A2402 -39.241 6.649 30.351 1.00119.43 C ANISOU 3204 C6 CLR A2402 12599 17410 15370 812 -1248 828 C HETATM 3205 C7 CLR A2402 -39.509 5.173 30.106 1.00119.42 C ANISOU 3205 C7 CLR A2402 12595 17402 15378 827 -1125 837 C HETATM 3206 C8 CLR A2402 -38.253 4.448 29.638 1.00119.40 C ANISOU 3206 C8 CLR A2402 12595 17400 15371 875 -1249 869 C HETATM 3207 C9 CLR A2402 -37.469 5.322 28.648 1.00118.88 C ANISOU 3207 C9 CLR A2402 12430 17400 15338 937 -1470 896 C HETATM 3208 C10 CLR A2402 -36.956 6.615 29.299 1.00118.65 C ANISOU 3208 C10 CLR A2402 12325 17413 15343 962 -1552 876 C HETATM 3209 C11 CLR A2402 -36.370 4.510 27.958 1.00118.27 C ANISOU 3209 C11 CLR A2402 12205 17396 15336 923 -1321 922 C HETATM 3210 C12 CLR A2402 -36.807 3.122 27.467 1.00118.70 C ANISOU 3210 C12 CLR A2402 12338 17396 15368 1016 -1117 906 C HETATM 3211 C13 CLR A2402 -37.494 2.277 28.504 1.00119.74 C ANISOU 3211 C13 CLR A2402 12702 17400 15395 827 -1024 869 C HETATM 3212 C14 CLR A2402 -38.653 3.139 28.984 1.00119.86 C ANISOU 3212 C14 CLR A2402 12747 17405 15391 739 -1100 872 C HETATM 3213 C15 CLR A2402 -39.517 2.194 29.816 1.00119.21 C ANISOU 3213 C15 CLR A2402 12513 17398 15382 592 -958 873 C HETATM 3214 C16 CLR A2402 -39.269 0.827 29.183 1.00119.23 C ANISOU 3214 C16 CLR A2402 12538 17394 15369 651 -1048 874 C HETATM 3215 C17 CLR A2402 -38.217 0.986 28.086 1.00119.71 C ANISOU 3215 C17 CLR A2402 12729 17388 15369 676 -1083 864 C HETATM 3216 C18 CLR A2402 -36.482 1.917 29.630 1.00121.51 C ANISOU 3216 C18 CLR A2402 13309 17418 15441 689 -644 822 C HETATM 3217 C19 CLR A2402 -35.828 6.286 30.308 1.00121.11 C ANISOU 3217 C19 CLR A2402 13159 17419 15437 919 -1248 857 C HETATM 3218 C20 CLR A2402 -37.412 -0.308 27.878 1.00121.28 C ANISOU 3218 C20 CLR A2402 13363 17383 15335 326 -784 840 C HETATM 3219 C21 CLR A2402 -36.818 -0.383 26.471 1.00121.35 C ANISOU 3219 C21 CLR A2402 13419 17380 15310 95 -717 843 C HETATM 3220 C22 CLR A2402 -38.244 -1.587 28.146 1.00122.38 C ANISOU 3220 C22 CLR A2402 13837 17370 15293 313 -743 824 C HETATM 3221 C23 CLR A2402 -37.614 -2.886 27.610 1.00121.98 C ANISOU 3221 C23 CLR A2402 13808 17339 15199 348 -663 843 C HETATM 3222 C24 CLR A2402 -37.890 -4.079 28.534 1.00119.82 C ANISOU 3222 C24 CLR A2402 13171 17293 15063 468 -634 907 C HETATM 3223 C25 CLR A2402 -36.912 -5.255 28.364 1.00116.24 C ANISOU 3223 C25 CLR A2402 12026 17247 14893 680 -583 969 C HETATM 3224 C26 CLR A2402 -37.475 -6.341 27.450 1.00115.94 C ANISOU 3224 C26 CLR A2402 12014 17230 14809 711 -561 991 C HETATM 3225 C27 CLR A2402 -35.550 -4.808 27.841 1.00113.10 C ANISOU 3225 C27 CLR A2402 10893 17240 14839 798 -503 976 C HETATM 3226 O1 CLR A2402 -36.843 10.843 30.158 1.00117.27 O ANISOU 3226 O1 CLR A2402 11767 17438 15354 724 -1605 860 O HETATM 3227 C1 CLR A2403 -38.167 10.737 21.804 1.00 18.55 C ANISOU 3227 C1 CLR A2403 1189 2661 3199 767 -276 -167 C HETATM 3228 C2 CLR A2403 -37.860 12.231 22.088 1.00 23.41 C ANISOU 3228 C2 CLR A2403 2100 2452 4343 1012 98 -449 C HETATM 3229 C3 CLR A2403 -38.091 12.583 23.536 1.00 26.36 C ANISOU 3229 C3 CLR A2403 3065 2435 4517 955 -281 -474 C HETATM 3230 C4 CLR A2403 -37.274 11.677 24.478 1.00 20.91 C ANISOU 3230 C4 CLR A2403 1323 2714 3907 127 141 -546 C HETATM 3231 C5 CLR A2403 -37.525 10.223 24.180 1.00 21.96 C ANISOU 3231 C5 CLR A2403 1741 3074 3530 684 236 -197 C HETATM 3232 C6 CLR A2403 -37.816 9.415 25.217 1.00 19.30 C ANISOU 3232 C6 CLR A2403 895 3235 3205 305 144 -151 C HETATM 3233 C7 CLR A2403 -37.994 7.912 25.110 1.00 21.54 C ANISOU 3233 C7 CLR A2403 2251 3336 2599 1017 -62 -574 C HETATM 3234 C8 CLR A2403 -37.673 7.382 23.705 1.00 23.16 C ANISOU 3234 C8 CLR A2403 3406 3152 2243 1200 -65 -219 C HETATM 3235 C9 CLR A2403 -38.094 8.378 22.623 1.00 20.20 C ANISOU 3235 C9 CLR A2403 2231 2960 2484 849 -118 -234 C HETATM 3236 C10 CLR A2403 -37.443 9.753 22.734 1.00 18.13 C ANISOU 3236 C10 CLR A2403 1074 2765 3050 718 -34 -199 C HETATM 3237 C11 CLR A2403 -37.906 7.759 21.241 1.00 18.20 C ANISOU 3237 C11 CLR A2403 1890 2717 2308 203 227 -485 C HETATM 3238 C12 CLR A2403 -38.533 6.365 21.116 1.00 17.16 C ANISOU 3238 C12 CLR A2403 1810 2779 1930 314 -196 -253 C HETATM 3239 C13 CLR A2403 -38.160 5.393 22.197 1.00 14.39 C ANISOU 3239 C13 CLR A2403 729 2528 2212 282 -258 -18 C HETATM 3240 C14 CLR A2403 -38.468 6.117 23.500 1.00 18.35 C ANISOU 3240 C14 CLR A2403 2253 2870 1851 307 267 78 C HETATM 3241 C15 CLR A2403 -38.342 5.043 24.593 1.00 18.74 C ANISOU 3241 C15 CLR A2403 2098 2955 2068 -185 -404 309 C HETATM 3242 C16 CLR A2403 -38.766 3.771 23.851 1.00 19.91 C ANISOU 3242 C16 CLR A2403 2628 2831 2106 -499 -102 194 C HETATM 3243 C17 CLR A2403 -38.995 4.121 22.369 1.00 20.37 C ANISOU 3243 C17 CLR A2403 2292 3196 2251 -592 -94 92 C HETATM 3244 C18 CLR A2403 -36.653 4.972 22.069 1.00 16.35 C ANISOU 3244 C18 CLR A2403 935 2817 2460 601 131 -42 C HETATM 3245 C19 CLR A2403 -35.942 9.681 22.298 1.00 19.75 C ANISOU 3245 C19 CLR A2403 954 3014 3536 207 -40 -314 C HETATM 3246 C20 CLR A2403 -38.749 2.918 21.452 1.00 17.87 C ANISOU 3246 C20 CLR A2403 1506 3194 2091 -968 -391 -182 C HETATM 3247 C21 CLR A2403 -38.926 3.235 19.952 1.00 19.79 C ANISOU 3247 C21 CLR A2403 1708 3730 2083 116 -611 -506 C HETATM 3248 C22 CLR A2403 -39.732 1.779 21.805 1.00 21.31 C ANISOU 3248 C22 CLR A2403 2169 3453 2473 -1236 -503 26 C HETATM 3249 C23 CLR A2403 -39.557 0.534 20.934 1.00 23.10 C ANISOU 3249 C23 CLR A2403 2429 3461 2887 -909 -594 -4 C HETATM 3250 C24 CLR A2403 -40.433 -0.590 21.499 1.00 28.37 C ANISOU 3250 C24 CLR A2403 3254 3873 3654 -19 34 -168 C HETATM 3251 C25 CLR A2403 -39.949 -1.982 21.088 1.00 42.91 C ANISOU 3251 C25 CLR A2403 7251 4305 4746 -622 -101 -277 C HETATM 3252 C26 CLR A2403 -40.273 -3.015 22.159 1.00 49.39 C ANISOU 3252 C26 CLR A2403 9005 4630 5132 -502 325 -115 C HETATM 3253 C27 CLR A2403 -40.576 -2.406 19.765 1.00 41.55 C ANISOU 3253 C27 CLR A2403 6063 4485 5241 -673 -558 -634 C HETATM 3254 O1 CLR A2403 -37.762 13.961 23.787 1.00 24.71 O ANISOU 3254 O1 CLR A2403 1916 2465 5008 860 42 -402 O HETATM 3255 C1 CLR A2404 -8.225 10.853 13.266 1.00 19.41 C ANISOU 3255 C1 CLR A2404 2480 2227 2667 -151 585 380 C HETATM 3256 C2 CLR A2404 -8.202 12.396 13.331 1.00 20.79 C ANISOU 3256 C2 CLR A2404 2693 2341 2864 -1008 596 364 C HETATM 3257 C3 CLR A2404 -6.846 12.964 12.979 1.00 22.25 C ANISOU 3257 C3 CLR A2404 2625 2771 3059 -655 946 429 C HETATM 3258 C4 CLR A2404 -6.334 12.443 11.629 1.00 18.60 C ANISOU 3258 C4 CLR A2404 1966 2482 2620 552 293 497 C HETATM 3259 C5 CLR A2404 -6.376 10.938 11.581 1.00 16.10 C ANISOU 3259 C5 CLR A2404 1131 2314 2671 693 297 508 C HETATM 3260 C6 CLR A2404 -5.263 10.258 11.206 1.00 17.70 C ANISOU 3260 C6 CLR A2404 1387 2428 2909 630 580 425 C HETATM 3261 C7 CLR A2404 -5.217 8.755 10.965 1.00 18.20 C ANISOU 3261 C7 CLR A2404 1657 2418 2840 -474 1091 58 C HETATM 3262 C8 CLR A2404 -6.625 8.145 10.983 1.00 17.48 C ANISOU 3262 C8 CLR A2404 1419 2451 2772 -335 971 196 C HETATM 3263 C9 CLR A2404 -7.446 8.770 12.122 1.00 16.97 C ANISOU 3263 C9 CLR A2404 1451 2238 2757 52 904 293 C HETATM 3264 C10 CLR A2404 -7.682 10.269 11.946 1.00 16.83 C ANISOU 3264 C10 CLR A2404 1429 2270 2694 205 322 593 C HETATM 3265 C11 CLR A2404 -8.758 8.027 12.372 1.00 17.49 C ANISOU 3265 C11 CLR A2404 1678 2383 2583 -226 293 350 C HETATM 3266 C12 CLR A2404 -8.597 6.506 12.425 1.00 17.98 C ANISOU 3266 C12 CLR A2404 1779 2554 2500 352 821 182 C HETATM 3267 C13 CLR A2404 -7.873 5.896 11.243 1.00 19.25 C ANISOU 3267 C13 CLR A2404 1715 2872 2727 389 221 419 C HETATM 3268 C14 CLR A2404 -6.542 6.637 11.178 1.00 23.27 C ANISOU 3268 C14 CLR A2404 3008 2781 3053 -543 969 188 C HETATM 3269 C15 CLR A2404 -5.726 5.852 10.157 1.00 23.97 C ANISOU 3269 C15 CLR A2404 2863 2883 3362 -187 1298 -151 C HETATM 3270 C16 CLR A2404 -6.167 4.411 10.407 1.00 20.52 C ANISOU 3270 C16 CLR A2404 1337 3059 3401 -445 -98 233 C HETATM 3271 C17 CLR A2404 -7.391 4.434 11.331 1.00 19.54 C ANISOU 3271 C17 CLR A2404 1557 2892 2974 -858 744 296 C HETATM 3272 C18 CLR A2404 -8.707 6.071 9.939 1.00 18.78 C ANISOU 3272 C18 CLR A2404 1617 2982 2536 494 -966 427 C HETATM 3273 C19 CLR A2404 -8.711 10.509 10.794 1.00 15.87 C ANISOU 3273 C19 CLR A2404 1499 2067 2463 435 -419 922 C HETATM 3274 C20 CLR A2404 -8.343 3.252 11.039 1.00 16.70 C ANISOU 3274 C20 CLR A2404 1016 2719 2609 -145 626 345 C HETATM 3275 C21 CLR A2404 -9.630 3.308 11.887 1.00 19.53 C ANISOU 3275 C21 CLR A2404 1704 2833 2885 389 1120 741 C HETATM 3276 C22 CLR A2404 -7.613 1.918 11.309 1.00 21.78 C ANISOU 3276 C22 CLR A2404 2583 2710 2983 -286 52 764 C HETATM 3277 C23 CLR A2404 -8.463 0.653 11.119 1.00 25.97 C ANISOU 3277 C23 CLR A2404 3764 2900 3204 -681 -336 871 C HETATM 3278 C24 CLR A2404 -7.580 -0.586 11.302 1.00 30.83 C ANISOU 3278 C24 CLR A2404 5150 3372 3192 -896 -744 617 C HETATM 3279 C25 CLR A2404 -8.309 -1.938 11.212 1.00 30.39 C ANISOU 3279 C25 CLR A2404 4368 4118 3059 -891 146 596 C HETATM 3280 C26 CLR A2404 -9.219 -2.156 12.411 1.00 28.66 C ANISOU 3280 C26 CLR A2404 3724 4232 2935 659 1863 505 C HETATM 3281 C27 CLR A2404 -9.129 -2.093 9.945 1.00 37.11 C ANISOU 3281 C27 CLR A2404 6117 4579 3406 -840 627 388 C HETATM 3282 O1 CLR A2404 -6.914 14.399 12.905 1.00 25.32 O ANISOU 3282 O1 CLR A2404 3277 3010 3335 -820 1287 386 O HETATM 3283 C1 CLR A2405 -3.115 8.104 21.237 1.00 14.43 C ANISOU 3283 C1 CLR A2405 743 2656 2082 -332 5 -157 C HETATM 3284 C2 CLR A2405 -2.885 9.622 21.158 1.00 19.30 C ANISOU 3284 C2 CLR A2405 2262 2948 2125 -907 20 -178 C HETATM 3285 C3 CLR A2405 -1.907 9.985 20.077 1.00 18.05 C ANISOU 3285 C3 CLR A2405 1161 2943 2754 -444 -745 -173 C HETATM 3286 C4 CLR A2405 -2.407 9.455 18.724 1.00 17.31 C ANISOU 3286 C4 CLR A2405 934 2872 2772 -297 -517 79 C HETATM 3287 C5 CLR A2405 -2.677 7.969 18.788 1.00 18.56 C ANISOU 3287 C5 CLR A2405 1452 2860 2739 -213 -572 -83 C HETATM 3288 C6 CLR A2405 -2.124 7.167 17.853 1.00 17.38 C ANISOU 3288 C6 CLR A2405 1105 2778 2720 302 -278 -329 C HETATM 3289 C7 CLR A2405 -2.335 5.654 17.801 1.00 16.74 C ANISOU 3289 C7 CLR A2405 1067 2655 2639 215 420 -180 C HETATM 3290 C8 CLR A2405 -3.521 5.227 18.676 1.00 16.99 C ANISOU 3290 C8 CLR A2405 1343 2593 2519 -250 -47 -271 C HETATM 3291 C9 CLR A2405 -3.479 5.943 20.028 1.00 15.12 C ANISOU 3291 C9 CLR A2405 1201 2562 1982 21 271 -46 C HETATM 3292 C10 CLR A2405 -3.568 7.473 19.909 1.00 15.33 C ANISOU 3292 C10 CLR A2405 951 2804 2070 119 -573 -27 C HETATM 3293 C11 CLR A2405 -4.544 5.378 20.984 1.00 14.01 C ANISOU 3293 C11 CLR A2405 1359 2071 1894 -938 123 164 C HETATM 3294 C12 CLR A2405 -4.580 3.853 21.017 1.00 15.66 C ANISOU 3294 C12 CLR A2405 1832 2258 1859 -485 -416 77 C HETATM 3295 C13 CLR A2405 -4.697 3.192 19.662 1.00 15.06 C ANISOU 3295 C13 CLR A2405 998 2562 2162 443 161 -50 C HETATM 3296 C14 CLR A2405 -3.518 3.721 18.857 1.00 17.11 C ANISOU 3296 C14 CLR A2405 1600 2524 2378 211 941 -221 C HETATM 3297 C15 CLR A2405 -3.560 2.891 17.572 1.00 20.68 C ANISOU 3297 C15 CLR A2405 2539 2679 2641 842 995 -304 C HETATM 3298 C16 CLR A2405 -4.072 1.526 18.069 1.00 20.35 C ANISOU 3298 C16 CLR A2405 2544 2623 2564 1345 651 -194 C HETATM 3299 C17 CLR A2405 -4.481 1.675 19.544 1.00 19.32 C ANISOU 3299 C17 CLR A2405 1945 2794 2601 1143 679 124 C HETATM 3300 C18 CLR A2405 -6.068 3.555 19.008 1.00 15.15 C ANISOU 3300 C18 CLR A2405 791 2891 2074 -295 151 -68 C HETATM 3301 C19 CLR A2405 -5.034 7.940 19.624 1.00 14.30 C ANISOU 3301 C19 CLR A2405 1031 2869 1532 703 144 175 C HETATM 3302 C20 CLR A2405 -5.624 0.721 19.921 1.00 20.66 C ANISOU 3302 C20 CLR A2405 1922 2905 3023 668 601 429 C HETATM 3303 C21 CLR A2405 -6.078 0.838 21.386 1.00 17.96 C ANISOU 3303 C21 CLR A2405 1247 3095 2481 479 643 778 C HETATM 3304 C22 CLR A2405 -5.250 -0.745 19.615 1.00 23.91 C ANISOU 3304 C22 CLR A2405 1999 2804 4282 847 6 72 C HETATM 3305 C23 CLR A2405 -6.457 -1.684 19.755 1.00 33.12 C ANISOU 3305 C23 CLR A2405 4534 2886 5165 479 30 -166 C HETATM 3306 C24 CLR A2405 -6.019 -3.141 19.912 1.00 40.62 C ANISOU 3306 C24 CLR A2405 6615 3142 5675 472 76 -382 C HETATM 3307 C25 CLR A2405 -5.305 -3.668 18.673 1.00 44.42 C ANISOU 3307 C25 CLR A2405 7647 3312 5917 498 -631 -466 C HETATM 3308 C26 CLR A2405 -5.000 -5.161 18.809 1.00 43.57 C ANISOU 3308 C26 CLR A2405 7032 3466 6057 1121 -704 -468 C HETATM 3309 C27 CLR A2405 -6.131 -3.387 17.417 1.00 41.05 C ANISOU 3309 C27 CLR A2405 6410 3226 5963 -130 -1204 -626 C HETATM 3310 O1 CLR A2405 -1.825 11.410 19.984 1.00 18.79 O ANISOU 3310 O1 CLR A2405 1374 2667 3097 -477 -694 423 O HETATM 3311 C1 OLA A2406 -36.189 15.215 12.975 1.00 55.47 C ANISOU 3311 C1 OLA A2406 6374 9172 5529 607 106 844 C HETATM 3312 O1 OLA A2406 -35.435 16.200 12.724 1.00 57.60 O ANISOU 3312 O1 OLA A2406 6997 9193 5697 242 -216 950 O HETATM 3313 O2 OLA A2406 -37.150 15.395 13.735 1.00 54.49 O ANISOU 3313 O2 OLA A2406 6048 9381 5276 693 954 650 O HETATM 3314 C2 OLA A2406 -35.967 13.838 12.386 1.00 51.36 C ANISOU 3314 C2 OLA A2406 5079 8891 5545 815 150 1052 C HETATM 3315 C3 OLA A2406 -36.746 12.791 13.181 1.00 45.01 C ANISOU 3315 C3 OLA A2406 3344 8618 5141 962 1672 1196 C HETATM 3316 C4 OLA A2406 -36.045 11.442 13.272 1.00 45.18 C ANISOU 3316 C4 OLA A2406 3961 8417 4789 773 1273 1241 C HETATM 3317 C5 OLA A2406 -36.245 10.567 12.051 1.00 41.18 C ANISOU 3317 C5 OLA A2406 3217 8171 4259 295 -250 1197 C HETATM 3318 C6 OLA A2406 -36.863 9.206 12.341 1.00 40.29 C ANISOU 3318 C6 OLA A2406 2983 8196 4128 275 -80 1318 C HETATM 3319 C7 OLA A2406 -36.094 8.076 11.663 1.00 38.64 C ANISOU 3319 C7 OLA A2406 2652 7635 4396 -401 1028 1286 C HETATM 3320 C8 OLA A2406 -36.785 6.724 11.694 1.00 37.79 C ANISOU 3320 C8 OLA A2406 2472 7083 4802 -963 887 969 C HETATM 3321 C9 OLA A2406 -35.988 5.748 10.843 1.00 40.99 C ANISOU 3321 C9 OLA A2406 2585 7964 5026 -760 354 1219 C HETATM 3322 C10 OLA A2406 -36.444 4.651 10.191 1.00 44.44 C ANISOU 3322 C10 OLA A2406 3440 7961 5483 -797 1197 908 C HETATM 3323 C11 OLA A2406 -37.879 4.171 10.197 1.00 46.81 C ANISOU 3323 C11 OLA A2406 4189 7800 5796 -90 670 592 C HETATM 3324 C12 OLA A2406 -37.969 2.652 9.955 1.00 48.78 C ANISOU 3324 C12 OLA A2406 4798 7850 5888 -393 -142 489 C HETATM 3325 C13 OLA A2406 -38.388 1.854 11.207 1.00 51.47 C ANISOU 3325 C13 OLA A2406 5605 7926 6025 -382 275 430 C HETATM 3326 C14 OLA A2406 -38.965 0.466 10.881 1.00 54.49 C ANISOU 3326 C14 OLA A2406 6773 7886 6043 425 630 428 C HETATM 3327 C15 OLA A2406 -38.947 -0.506 12.076 1.00 54.29 C ANISOU 3327 C15 OLA A2406 6625 7899 6105 903 288 453 C HETATM 3328 C16 OLA A2406 -38.788 -1.983 11.673 1.00 54.23 C ANISOU 3328 C16 OLA A2406 6373 7977 6256 871 -274 405 C HETATM 3329 C17 OLA A2406 -40.042 -2.840 11.907 1.00 53.35 C ANISOU 3329 C17 OLA A2406 5960 7991 6321 1005 -276 341 C HETATM 3330 C18 OLA A2406 -40.014 -4.138 11.084 1.00 56.16 C ANISOU 3330 C18 OLA A2406 7023 8008 6309 1089 -837 368 C HETATM 3331 C1 OLA A2407 -8.659 14.498 8.293 1.00 64.16 C ANISOU 3331 C1 OLA A2407 9093 8673 6613 -1251 -281 2345 C HETATM 3332 O1 OLA A2407 -8.417 15.427 7.472 1.00 65.03 O ANISOU 3332 O1 OLA A2407 9738 8668 6302 -1229 -321 2484 O HETATM 3333 O2 OLA A2407 -8.499 14.717 9.514 1.00 68.03 O ANISOU 3333 O2 OLA A2407 10053 8650 7147 -1220 -1376 2374 O HETATM 3334 C2 OLA A2407 -9.154 13.146 7.820 1.00 61.50 C ANISOU 3334 C2 OLA A2407 8478 8666 6224 -872 288 2187 C HETATM 3335 C3 OLA A2407 -8.048 12.232 7.298 1.00 60.36 C ANISOU 3335 C3 OLA A2407 8363 8664 5906 -928 985 2176 C HETATM 3336 C4 OLA A2407 -8.616 11.139 6.406 1.00 59.58 C ANISOU 3336 C4 OLA A2407 8130 8655 5854 -956 1258 2287 C HETATM 3337 C5 OLA A2407 -8.026 9.769 6.651 1.00 59.60 C ANISOU 3337 C5 OLA A2407 8046 8693 5905 -1000 1494 2331 C HETATM 3338 C6 OLA A2407 -8.981 8.642 6.300 1.00 57.42 C ANISOU 3338 C6 OLA A2407 6934 8771 6111 -865 1533 2161 C HETATM 3339 C7 OLA A2407 -8.268 7.310 6.103 1.00 59.62 C ANISOU 3339 C7 OLA A2407 7543 8827 6281 -825 1436 1976 C HETATM 3340 C8 OLA A2407 -9.214 6.126 6.061 1.00 60.78 C ANISOU 3340 C8 OLA A2407 7769 8900 6423 -445 1264 1698 C HETATM 3341 C9 OLA A2407 -8.844 5.238 4.882 1.00 60.61 C ANISOU 3341 C9 OLA A2407 7581 8900 6547 -110 1112 1589 C HETATM 3342 C10 OLA A2407 -9.724 4.678 4.019 1.00 57.38 C ANISOU 3342 C10 OLA A2407 6323 8802 6676 -505 955 1605 C HETATM 3343 C11 OLA A2407 -11.221 4.878 4.119 1.00 51.95 C ANISOU 3343 C11 OLA A2407 4305 8667 6765 -821 1189 1732 C HETATM 3344 C12 OLA A2407 -11.969 4.169 2.977 1.00 49.23 C ANISOU 3344 C12 OLA A2407 3236 8597 6874 -623 1432 1933 C HETATM 3345 C13 OLA A2407 -11.156 4.046 1.675 1.00 52.32 C ANISOU 3345 C13 OLA A2407 4465 8527 6886 -992 1313 2108 C HETATM 3346 C1 OLA A2408 -10.687 -12.912 8.112 1.00 54.96 C ANISOU 3346 C1 OLA A2408 4440 8401 8042 -105 3206 -753 C HETATM 3347 C2 OLA A2408 -11.345 -12.542 9.428 1.00 53.59 C ANISOU 3347 C2 OLA A2408 4045 8347 7968 -416 2934 -635 C HETATM 3348 C3 OLA A2408 -10.332 -12.449 10.575 1.00 57.41 C ANISOU 3348 C3 OLA A2408 5125 8469 8221 -346 2503 -839 C HETATM 3349 C4 OLA A2408 -9.755 -11.049 10.762 1.00 56.27 C ANISOU 3349 C4 OLA A2408 4683 8476 8222 -810 2293 -804 C HETATM 3350 C5 OLA A2408 -9.076 -10.819 12.101 1.00 59.04 C ANISOU 3350 C5 OLA A2408 5764 8433 8234 -807 2559 -897 C HETATM 3351 C6 OLA A2408 -8.568 -9.402 12.343 1.00 55.08 C ANISOU 3351 C6 OLA A2408 4215 8345 8368 -913 1730 -1037 C HETATM 3352 C7 OLA A2408 -8.715 -8.999 13.808 1.00 51.01 C ANISOU 3352 C7 OLA A2408 2920 8175 8288 -366 1747 -1004 C HETATM 3353 C1 OLA A2409 -20.436 -22.140 27.722 1.00 49.99 C ANISOU 3353 C1 OLA A2409 7173 6163 5658 -619 1009 1013 C HETATM 3354 O1 OLA A2409 -20.653 -21.634 26.594 1.00 54.82 O ANISOU 3354 O1 OLA A2409 8587 6208 6034 -824 2045 1145 O HETATM 3355 O2 OLA A2409 -20.693 -23.344 27.861 1.00 56.38 O ANISOU 3355 O2 OLA A2409 9286 6096 6039 -336 337 777 O HETATM 3356 C2 OLA A2409 -19.894 -21.319 28.870 1.00 40.96 C ANISOU 3356 C2 OLA A2409 4337 6209 5017 -635 878 848 C HETATM 3357 C3 OLA A2409 -19.790 -19.847 28.476 1.00 40.47 C ANISOU 3357 C3 OLA A2409 4615 6390 4370 191 186 685 C HETATM 3358 C4 OLA A2409 -19.666 -18.911 29.664 1.00 39.27 C ANISOU 3358 C4 OLA A2409 4417 6347 4155 437 582 373 C HETATM 3359 C5 OLA A2409 -20.142 -17.507 29.376 1.00 38.40 C ANISOU 3359 C5 OLA A2409 4245 6317 4030 271 467 306 C HETATM 3360 C6 OLA A2409 -19.061 -16.549 28.903 1.00 33.39 C ANISOU 3360 C6 OLA A2409 2480 6174 4032 929 720 222 C HETATM 3361 C7 OLA A2409 -19.662 -15.174 28.641 1.00 34.18 C ANISOU 3361 C7 OLA A2409 2844 6027 4116 1884 352 397 C HETATM 3362 C1 OLA A2410 -24.969 13.372 8.008 1.00 63.58 C ANISOU 3362 C1 OLA A2410 9627 7475 7057 -1418 265 370 C HETATM 3363 O1 OLA A2410 -25.586 12.370 8.388 1.00 63.03 O ANISOU 3363 O1 OLA A2410 9771 7248 6931 -1744 652 455 O HETATM 3364 O2 OLA A2410 -25.095 14.427 8.690 1.00 65.74 O ANISOU 3364 O2 OLA A2410 9966 7651 7360 -1118 568 319 O HETATM 3365 C2 OLA A2410 -24.101 13.306 6.767 1.00 62.82 C ANISOU 3365 C2 OLA A2410 9429 7540 6899 -1297 -137 386 C HETATM 3366 C3 OLA A2410 -23.327 11.989 6.686 1.00 59.65 C ANISOU 3366 C3 OLA A2410 8321 7540 6805 -1016 -162 504 C HETATM 3367 C4 OLA A2410 -22.355 11.916 5.516 1.00 59.11 C ANISOU 3367 C4 OLA A2410 8196 7513 6749 -1095 -311 528 C HETATM 3368 C5 OLA A2410 -22.539 10.679 4.659 1.00 56.30 C ANISOU 3368 C5 OLA A2410 7271 7427 6694 -1548 -518 487 C HETATM 3369 C6 OLA A2410 -21.311 10.236 3.872 1.00 52.45 C ANISOU 3369 C6 OLA A2410 6062 7353 6513 -1755 151 437 C HETATM 3370 C7 OLA A2410 -21.515 8.854 3.254 1.00 52.01 C ANISOU 3370 C7 OLA A2410 6265 7256 6239 -1944 72 529 C HETATM 3371 C8 OLA A2410 -20.757 7.719 3.921 1.00 50.87 C ANISOU 3371 C8 OLA A2410 6189 7207 5932 -2666 566 667 C HETATM 3372 C9 OLA A2410 -21.738 6.624 4.330 1.00 47.42 C ANISOU 3372 C9 OLA A2410 5267 7134 5618 -3158 1046 799 C HETATM 3373 C10 OLA A2410 -22.086 5.539 3.594 1.00 47.54 C ANISOU 3373 C10 OLA A2410 5301 7156 5606 -2522 722 760 C HETATM 3374 C11 OLA A2410 -21.532 5.244 2.214 1.00 47.15 C ANISOU 3374 C11 OLA A2410 4722 7211 5983 -2042 -766 499 C HETATM 3375 C12 OLA A2410 -20.509 4.095 2.239 1.00 48.53 C ANISOU 3375 C12 OLA A2410 4875 7301 6263 -1990 -732 285 C HETATM 3376 C13 OLA A2410 -20.806 2.965 1.234 1.00 51.87 C ANISOU 3376 C13 OLA A2410 5927 7409 6373 -1536 -491 229 C HETATM 3377 C14 OLA A2410 -20.279 1.592 1.687 1.00 53.91 C ANISOU 3377 C14 OLA A2410 6592 7453 6440 -1054 -35 303 C HETATM 3378 C15 OLA A2410 -21.386 0.563 1.998 1.00 56.30 C ANISOU 3378 C15 OLA A2410 7515 7456 6420 -540 693 390 C HETATM 3379 C16 OLA A2410 -21.056 -0.366 3.185 1.00 56.79 C ANISOU 3379 C16 OLA A2410 7710 7484 6382 -290 694 417 C HETATM 3380 C1 OLA A2411 -28.076 -20.200 40.025 1.00 71.10 C ANISOU 3380 C1 OLA A2411 10986 8771 7257 -521 -1381 -1390 C HETATM 3381 O1 OLA A2411 -27.658 -21.382 39.841 1.00 69.84 O ANISOU 3381 O1 OLA A2411 10549 8717 7269 -567 -1192 -1258 O HETATM 3382 O2 OLA A2411 -29.137 -20.064 40.661 1.00 73.59 O ANISOU 3382 O2 OLA A2411 11768 8921 7271 -381 -1609 -1530 O HETATM 3383 C2 OLA A2411 -27.327 -18.985 39.493 1.00 68.66 C ANISOU 3383 C2 OLA A2411 10311 8600 7178 -826 -1868 -1394 C HETATM 3384 C3 OLA A2411 -27.859 -17.641 40.016 1.00 68.31 C ANISOU 3384 C3 OLA A2411 10342 8456 7156 -1038 -1825 -1378 C HETATM 3385 C4 OLA A2411 -27.512 -16.449 39.124 1.00 67.21 C ANISOU 3385 C4 OLA A2411 10088 8338 7109 -762 -1740 -1410 C HETATM 3386 C5 OLA A2411 -26.088 -15.935 39.274 1.00 65.81 C ANISOU 3386 C5 OLA A2411 9753 8302 6949 -748 -1453 -1440 C HETATM 3387 C6 OLA A2411 -25.571 -15.100 38.108 1.00 64.01 C ANISOU 3387 C6 OLA A2411 9321 8276 6725 -699 -1004 -1487 C HETATM 3388 C7 OLA A2411 -24.354 -14.248 38.468 1.00 62.23 C ANISOU 3388 C7 OLA A2411 8721 8271 6654 -711 -1212 -1461 C HETATM 3389 C8 OLA A2411 -24.494 -12.754 38.205 1.00 63.01 C ANISOU 3389 C8 OLA A2411 8953 8256 6732 -468 -891 -1494 C HETATM 3390 C9 OLA A2411 -23.683 -12.001 39.251 1.00 63.33 C ANISOU 3390 C9 OLA A2411 9110 8182 6772 -428 -200 -1603 C HETATM 3391 C10 OLA A2411 -23.613 -10.664 39.469 1.00 62.71 C ANISOU 3391 C10 OLA A2411 9083 8123 6620 -254 457 -1694 C HETATM 3392 C11 OLA A2411 -24.345 -9.590 38.690 1.00 60.99 C ANISOU 3392 C11 OLA A2411 8874 8043 6257 -114 914 -1868 C HETATM 3393 C12 OLA A2411 -24.272 -8.215 39.393 1.00 56.35 C ANISOU 3393 C12 OLA A2411 7452 7984 5973 -95 1708 -1958 C HETATM 3394 C13 OLA A2411 -22.850 -7.661 39.632 1.00 54.19 C ANISOU 3394 C13 OLA A2411 6808 7866 5915 -249 1600 -2087 C HETATM 3395 C14 OLA A2411 -22.203 -7.052 38.376 1.00 52.84 C ANISOU 3395 C14 OLA A2411 6364 7692 6022 -392 1091 -2253 C HETATM 3396 C15 OLA A2411 -22.845 -5.742 37.871 1.00 52.48 C ANISOU 3396 C15 OLA A2411 6464 7488 5988 -418 1010 -2459 C HETATM 3397 C16 OLA A2411 -22.460 -5.399 36.418 1.00 51.90 C ANISOU 3397 C16 OLA A2411 6384 7505 5829 -1039 -510 -2788 C HETATM 3398 C17 OLA A2411 -21.809 -4.022 36.234 1.00 47.63 C ANISOU 3398 C17 OLA A2411 5187 7409 5500 -1390 -1152 -2828 C HETATM 3399 C18 OLA A2411 -22.518 -3.157 35.181 1.00 44.62 C ANISOU 3399 C18 OLA A2411 4567 6984 5401 -1684 -1215 -2224 C HETATM 3400 C1 OLA A2412 -40.114 12.793 9.218 1.00 77.07 C ANISOU 3400 C1 OLA A2412 12599 9770 6913 -678 2268 2014 C HETATM 3401 O1 OLA A2412 -39.295 13.730 9.192 1.00 77.56 O ANISOU 3401 O1 OLA A2412 12673 9912 6885 -617 1742 2116 O HETATM 3402 O2 OLA A2412 -41.346 13.077 9.282 1.00 80.03 O ANISOU 3402 O2 OLA A2412 13548 9798 7060 -695 2286 2156 O HETATM 3403 C2 OLA A2412 -39.631 11.358 9.174 1.00 72.44 C ANISOU 3403 C2 OLA A2412 11185 9596 6744 -410 2690 1697 C HETATM 3404 C3 OLA A2412 -40.809 10.381 9.182 1.00 68.01 C ANISOU 3404 C3 OLA A2412 9873 9474 6495 -336 3675 1522 C HETATM 3405 C4 OLA A2412 -40.407 8.957 8.828 1.00 64.03 C ANISOU 3405 C4 OLA A2412 8643 9461 6223 -226 3839 1497 C HETATM 3406 C5 OLA A2412 -41.505 8.158 8.157 1.00 59.60 C ANISOU 3406 C5 OLA A2412 7165 9414 6068 -512 3707 1215 C HETATM 3407 C6 OLA A2412 -41.329 6.654 8.297 1.00 58.69 C ANISOU 3407 C6 OLA A2412 6876 9445 5978 -154 3585 1283 C HETATM 3408 C7 OLA A2412 -42.146 5.874 7.272 1.00 59.06 C ANISOU 3408 C7 OLA A2412 6668 9592 6182 461 3319 1207 C HETATM 3409 C8 OLA A2412 -41.947 4.372 7.325 1.00 60.12 C ANISOU 3409 C8 OLA A2412 6865 9546 6431 420 3268 902 C HETATM 3410 C9 OLA A2412 -42.967 3.787 8.286 1.00 61.02 C ANISOU 3410 C9 OLA A2412 7073 9496 6617 609 3110 611 C HETATM 3411 C10 OLA A2412 -42.936 2.554 8.846 1.00 61.98 C ANISOU 3411 C10 OLA A2412 7339 9462 6748 1070 2624 467 C HETATM 3412 C11 OLA A2412 -41.851 1.530 8.593 1.00 63.24 C ANISOU 3412 C11 OLA A2412 7724 9470 6835 765 2273 515 C HETATM 3413 C12 OLA A2412 -42.413 0.095 8.571 1.00 62.96 C ANISOU 3413 C12 OLA A2412 7550 9545 6827 686 2376 640 C HETATM 3414 C13 OLA A2412 -43.309 -0.240 9.778 1.00 61.63 C ANISOU 3414 C13 OLA A2412 7068 9604 6744 837 2763 719 C HETATM 3415 C1 OLA A2413 -36.197 -15.683 5.137 1.00 67.63 C ANISOU 3415 C1 OLA A2413 10566 8779 6352 165 265 1118 C HETATM 3416 O1 OLA A2413 -36.388 -14.488 5.500 1.00 69.37 O ANISOU 3416 O1 OLA A2413 11087 8732 6537 -353 146 1151 O HETATM 3417 O2 OLA A2413 -36.237 -16.574 6.002 1.00 68.53 O ANISOU 3417 O2 OLA A2413 11015 8728 6295 456 94 1249 O HETATM 3418 C2 OLA A2413 -35.929 -16.043 3.693 1.00 63.67 C ANISOU 3418 C2 OLA A2413 9167 8828 6198 223 874 1018 C HETATM 3419 C3 OLA A2413 -35.071 -14.984 3.000 1.00 62.13 C ANISOU 3419 C3 OLA A2413 8578 8840 6189 287 819 923 C HETATM 3420 C4 OLA A2413 -33.643 -15.453 2.760 1.00 58.42 C ANISOU 3420 C4 OLA A2413 7279 8778 6140 586 1526 847 C HETATM 3421 C5 OLA A2413 -32.913 -14.623 1.731 1.00 54.49 C ANISOU 3421 C5 OLA A2413 6020 8675 6010 559 2166 728 C HETATM 3422 C6 OLA A2413 -31.412 -14.550 1.947 1.00 49.73 C ANISOU 3422 C6 OLA A2413 4511 8612 5774 915 1571 520 C HETATM 3423 C7 OLA A2413 -31.022 -13.428 2.903 1.00 45.97 C ANISOU 3423 C7 OLA A2413 3615 8431 5422 567 2162 363 C HETATM 3424 C8 OLA A2413 -29.521 -13.217 2.990 1.00 49.27 C ANISOU 3424 C8 OLA A2413 5065 8385 5269 -344 3016 383 C HETATM 3425 C9 OLA A2413 -29.248 -11.773 3.372 1.00 50.10 C ANISOU 3425 C9 OLA A2413 5213 8728 5096 -714 2772 542 C HETATM 3426 C10 OLA A2413 -28.044 -11.168 3.317 1.00 50.18 C ANISOU 3426 C10 OLA A2413 5222 8816 5027 -917 2512 597 C HETATM 3427 C1 OLA A2414 -15.461 13.068 1.009 1.00 62.10 C ANISOU 3427 C1 OLA A2414 9713 8732 5149 -992 -969 1648 C HETATM 3428 O1 OLA A2414 -14.330 13.623 0.894 1.00 63.78 O ANISOU 3428 O1 OLA A2414 9814 8908 5513 -632 -1158 1503 O HETATM 3429 O2 OLA A2414 -16.434 13.794 1.291 1.00 59.42 O ANISOU 3429 O2 OLA A2414 8846 8709 5022 -859 -257 1612 O HETATM 3430 C2 OLA A2414 -15.631 11.571 0.811 1.00 60.58 C ANISOU 3430 C2 OLA A2414 9737 8551 4730 -957 -1539 1916 C HETATM 3431 C3 OLA A2414 -17.087 11.110 0.945 1.00 57.34 C ANISOU 3431 C3 OLA A2414 8948 8409 4431 -1310 -1101 2044 C HETATM 3432 C4 OLA A2414 -17.330 9.714 0.385 1.00 57.18 C ANISOU 3432 C4 OLA A2414 8923 8379 4422 -967 -1270 1896 C HETATM 3433 C5 OLA A2414 -16.245 8.718 0.746 1.00 56.51 C ANISOU 3433 C5 OLA A2414 8496 8397 4579 -1173 -1952 1627 C HETATM 3434 C6 OLA A2414 -16.750 7.394 1.304 1.00 53.44 C ANISOU 3434 C6 OLA A2414 7274 8387 4642 -1890 -2135 1502 C HETATM 3435 C1 OLA A2415 -28.063 -20.920 35.004 1.00 65.87 C ANISOU 3435 C1 OLA A2415 10463 7703 6862 996 301 1516 C HETATM 3436 O1 OLA A2415 -28.865 -21.846 34.689 1.00 66.76 O ANISOU 3436 O1 OLA A2415 10606 7828 6932 747 299 1171 O HETATM 3437 O2 OLA A2415 -26.858 -21.069 34.727 1.00 63.90 O ANISOU 3437 O2 OLA A2415 9933 7650 6696 780 295 1841 O HETATM 3438 C2 OLA A2415 -28.539 -19.660 35.704 1.00 64.63 C ANISOU 3438 C2 OLA A2415 10041 7565 6951 1154 166 1515 C HETATM 3439 C3 OLA A2415 -30.035 -19.407 35.486 1.00 63.61 C ANISOU 3439 C3 OLA A2415 9613 7501 7054 1184 94 1420 C HETATM 3440 C4 OLA A2415 -30.541 -18.128 36.146 1.00 62.97 C ANISOU 3440 C4 OLA A2415 9220 7498 7207 1326 149 1209 C HETATM 3441 C5 OLA A2415 -30.748 -16.978 35.177 1.00 62.90 C ANISOU 3441 C5 OLA A2415 8942 7598 7361 1133 113 877 C HETATM 3442 C6 OLA A2415 -31.827 -15.982 35.585 1.00 60.76 C ANISOU 3442 C6 OLA A2415 7942 7718 7427 1082 486 616 C HETATM 3443 C7 OLA A2415 -31.424 -14.538 35.285 1.00 61.86 C ANISOU 3443 C7 OLA A2415 8304 7818 7382 1017 844 459 C HETATM 3444 C8 OLA A2415 -30.980 -13.728 36.495 1.00 61.66 C ANISOU 3444 C8 OLA A2415 8268 7888 7273 689 519 446 C HETATM 3445 C9 OLA A2415 -30.102 -12.569 36.035 1.00 58.55 C ANISOU 3445 C9 OLA A2415 7311 7807 7127 661 377 518 C HETATM 3446 C10 OLA A2415 -29.242 -11.874 36.816 1.00 57.58 C ANISOU 3446 C10 OLA A2415 7294 7653 6930 1055 803 669 C HETATM 3447 C11 OLA A2415 -28.378 -10.728 36.332 1.00 54.40 C ANISOU 3447 C11 OLA A2415 6606 7399 6666 1230 878 882 C HETATM 3448 C12 OLA A2415 -26.916 -10.851 36.809 1.00 50.55 C ANISOU 3448 C12 OLA A2415 5421 7263 6522 1079 1184 952 C HETATM 3449 C1 OLA A2416 -18.083 -13.085 3.566 1.00 60.03 C ANISOU 3449 C1 OLA A2416 8210 7868 6730 -70 2551 3012 C HETATM 3450 C2 OLA A2416 -17.834 -11.700 4.133 1.00 60.60 C ANISOU 3450 C2 OLA A2416 8286 7837 6901 322 2087 2917 C HETATM 3451 C3 OLA A2416 -16.357 -11.471 4.463 1.00 62.94 C ANISOU 3451 C3 OLA A2416 8907 7850 7159 240 1560 2761 C HETATM 3452 C4 OLA A2416 -15.887 -10.041 4.212 1.00 63.55 C ANISOU 3452 C4 OLA A2416 8945 7868 7335 631 1490 2635 C HETATM 3453 C5 OLA A2416 -16.868 -8.993 4.703 1.00 62.78 C ANISOU 3453 C5 OLA A2416 8576 7874 7404 654 1176 2483 C HETATM 3454 C6 OLA A2416 -16.273 -7.625 5.023 1.00 61.34 C ANISOU 3454 C6 OLA A2416 8154 7859 7294 614 773 2276 C HETATM 3455 C7 OLA A2416 -17.184 -6.820 5.950 1.00 58.05 C ANISOU 3455 C7 OLA A2416 7170 7793 7094 863 898 2132 C HETATM 3456 C1 OLA A2417 -43.851 -24.193 13.339 1.00 64.25 C ANISOU 3456 C1 OLA A2417 8226 8127 8058 -2524 1354 -413 C HETATM 3457 O1 OLA A2417 -44.540 -25.041 12.716 1.00 64.12 O ANISOU 3457 O1 OLA A2417 7958 8171 8233 -2674 772 -637 O HETATM 3458 O2 OLA A2417 -42.879 -24.608 13.993 1.00 63.31 O ANISOU 3458 O2 OLA A2417 7959 8141 7954 -2399 1271 -180 O HETATM 3459 C2 OLA A2417 -44.180 -22.715 13.301 1.00 62.02 C ANISOU 3459 C2 OLA A2417 7531 8027 8006 -2261 2118 -431 C HETATM 3460 C3 OLA A2417 -43.333 -21.945 14.312 1.00 59.55 C ANISOU 3460 C3 OLA A2417 6545 7997 8085 -2143 2227 -404 C HETATM 3461 C4 OLA A2417 -43.672 -20.463 14.378 1.00 59.63 C ANISOU 3461 C4 OLA A2417 6349 8029 8279 -2082 1951 -311 C HETATM 3462 C5 OLA A2417 -42.658 -19.668 15.173 1.00 62.47 C ANISOU 3462 C5 OLA A2417 7158 8135 8442 -1709 1855 -173 C HETATM 3463 C6 OLA A2417 -41.293 -20.337 15.283 1.00 61.94 C ANISOU 3463 C6 OLA A2417 6814 8176 8545 -1525 1750 -41 C HETATM 3464 C7 OLA A2417 -40.460 -19.741 16.416 1.00 62.95 C ANISOU 3464 C7 OLA A2417 7143 8180 8597 -1145 1881 19 C HETATM 3465 C8 OLA A2417 -39.556 -18.589 16.015 1.00 60.62 C ANISOU 3465 C8 OLA A2417 6232 8138 8663 -1287 1511 41 C HETATM 3466 C9 OLA A2417 -38.301 -19.138 15.351 1.00 58.89 C ANISOU 3466 C9 OLA A2417 5528 8106 8742 -879 1813 32 C HETATM 3467 C10 OLA A2417 -37.569 -18.516 14.398 1.00 56.33 C ANISOU 3467 C10 OLA A2417 4475 8058 8871 -807 1726 125 C HETATM 3468 C11 OLA A2417 -37.895 -17.153 13.816 1.00 57.01 C ANISOU 3468 C11 OLA A2417 4637 8020 9004 27 773 296 C HETATM 3469 C12 OLA A2417 -37.150 -15.986 14.496 1.00 56.31 C ANISOU 3469 C12 OLA A2417 4360 7976 9061 -113 1676 623 C HETATM 3470 C13 OLA A2417 -37.419 -14.625 13.823 1.00 55.90 C ANISOU 3470 C13 OLA A2417 4324 7962 8953 -637 2657 907 C HETATM 3471 C14 OLA A2417 -37.741 -13.472 14.791 1.00 58.86 C ANISOU 3471 C14 OLA A2417 5406 8014 8946 -501 2254 933 C HETATM 3472 C15 OLA A2417 -38.488 -12.303 14.111 1.00 61.63 C ANISOU 3472 C15 OLA A2417 6261 8051 9103 -586 1854 883 C HETATM 3473 C16 OLA A2417 -38.291 -10.927 14.778 1.00 62.19 C ANISOU 3473 C16 OLA A2417 6110 8137 9381 -1142 1294 846 C HETATM 3474 C17 OLA A2417 -38.468 -9.738 13.815 1.00 62.85 C ANISOU 3474 C17 OLA A2417 6144 8135 9600 -1048 741 799 C HETATM 3475 C9 OLA A2418 -8.564 -15.510 16.640 1.00 44.12 C ANISOU 3475 C9 OLA A2418 3629 6240 6893 -1928 -1893 719 C HETATM 3476 C10 OLA A2418 -9.899 -15.305 16.600 1.00 44.11 C ANISOU 3476 C10 OLA A2418 3595 6327 6839 -1799 -1303 830 C HETATM 3477 C11 OLA A2418 -10.638 -14.377 17.534 1.00 41.89 C ANISOU 3477 C11 OLA A2418 2889 6419 6607 -1134 -675 797 C HETATM 3478 C12 OLA A2418 -9.894 -13.042 17.677 1.00 46.63 C ANISOU 3478 C12 OLA A2418 4653 6579 6484 87 -1271 706 C HETATM 3479 C13 OLA A2418 -10.756 -11.929 18.288 1.00 45.77 C ANISOU 3479 C13 OLA A2418 4322 6663 6405 423 -615 670 C HETATM 3480 C14 OLA A2418 -10.252 -10.543 17.872 1.00 46.46 C ANISOU 3480 C14 OLA A2418 4474 6821 6358 -121 -841 728 C HETATM 3481 C15 OLA A2418 -8.752 -10.366 18.147 1.00 46.13 C ANISOU 3481 C15 OLA A2418 4233 6890 6406 852 -576 774 C HETATM 3482 C16 OLA A2418 -8.290 -8.904 18.024 1.00 48.40 C ANISOU 3482 C16 OLA A2418 4940 6909 6539 395 -747 691 C HETATM 3483 C17 OLA A2418 -8.201 -8.188 19.376 1.00 48.46 C ANISOU 3483 C17 OLA A2418 4894 6892 6626 17 -618 677 C HETATM 3484 C18 OLA A2418 -8.127 -6.664 19.220 1.00 50.74 C ANISOU 3484 C18 OLA A2418 5659 6881 6739 152 -907 659 C HETATM 3485 C3 OLA A2419 -34.658 10.307 2.314 1.00 71.80 C ANISOU 3485 C3 OLA A2419 8632 10288 8359 45 3029 189 C HETATM 3486 C4 OLA A2419 -34.150 8.876 2.450 1.00 71.45 C ANISOU 3486 C4 OLA A2419 8569 10173 8406 120 2684 277 C HETATM 3487 C5 OLA A2419 -34.421 8.005 1.235 1.00 69.63 C ANISOU 3487 C5 OLA A2419 8008 10143 8306 -13 2704 461 C HETATM 3488 C6 OLA A2419 -34.840 6.581 1.581 1.00 64.14 C ANISOU 3488 C6 OLA A2419 6225 10155 7989 -541 3868 748 C HETATM 3489 C7 OLA A2419 -35.508 5.878 0.404 1.00 60.56 C ANISOU 3489 C7 OLA A2419 5669 10040 7300 -401 3762 432 C HETATM 3490 C8 OLA A2419 -35.693 4.382 0.576 1.00 60.21 C ANISOU 3490 C8 OLA A2419 5758 10028 7090 -319 3762 387 C HETATM 3491 C9 OLA A2419 -34.323 3.732 0.707 1.00 59.96 C ANISOU 3491 C9 OLA A2419 5464 10265 7054 -292 3140 651 C HETATM 3492 C1 OLA A2420 -31.887 7.325 36.503 1.00 44.10 C ANISOU 3492 C1 OLA A2420 4043 7879 4835 -566 406 -1168 C HETATM 3493 O1 OLA A2420 -31.116 8.303 36.532 1.00 45.88 O ANISOU 3493 O1 OLA A2420 5028 7836 4570 -317 387 -1579 O HETATM 3494 O2 OLA A2420 -33.128 7.539 36.575 1.00 47.95 O ANISOU 3494 O2 OLA A2420 4689 8112 5419 -213 -598 -737 O HETATM 3495 C2 OLA A2420 -31.346 5.919 36.387 1.00 39.89 C ANISOU 3495 C2 OLA A2420 2835 7560 4761 -1421 556 -1193 C HETATM 3496 C3 OLA A2420 -32.327 4.900 36.960 1.00 41.84 C ANISOU 3496 C3 OLA A2420 3544 7461 4893 -755 749 -1315 C HETATM 3497 C4 OLA A2420 -31.912 3.476 36.626 1.00 45.62 C ANISOU 3497 C4 OLA A2420 4737 7518 5080 -513 1049 -1276 C HETATM 3498 C5 OLA A2420 -32.058 2.520 37.787 1.00 44.64 C ANISOU 3498 C5 OLA A2420 4271 7559 5133 -293 120 -1257 C HETATM 3499 C6 OLA A2420 -30.818 1.693 38.063 1.00 46.81 C ANISOU 3499 C6 OLA A2420 5142 7531 5111 -631 591 -1306 C HETATM 3500 C7 OLA A2420 -31.144 0.208 38.073 1.00 46.19 C ANISOU 3500 C7 OLA A2420 5146 7394 5009 -608 206 -1239 C HETATM 3501 C8 OLA A2420 -29.950 -0.688 38.313 1.00 45.35 C ANISOU 3501 C8 OLA A2420 4698 7412 5121 -165 -835 -1084 C HETATM 3502 C9 OLA A2420 -30.463 -2.024 38.825 1.00 50.45 C ANISOU 3502 C9 OLA A2420 6518 7500 5149 -9 -1180 -989 C HETATM 3503 C10 OLA A2420 -30.374 -3.195 38.158 1.00 54.75 C ANISOU 3503 C10 OLA A2420 7853 7701 5247 71 -744 -902 C HETATM 3504 C11 OLA A2420 -29.737 -3.335 36.791 1.00 54.25 C ANISOU 3504 C11 OLA A2420 7541 7777 5293 69 -176 -889 C HETATM 3505 C12 OLA A2420 -28.349 -3.996 36.875 1.00 51.47 C ANISOU 3505 C12 OLA A2420 7109 7623 4823 48 366 -881 C HETATM 3506 C13 OLA A2420 -28.388 -5.534 36.918 1.00 45.08 C ANISOU 3506 C13 OLA A2420 5408 7326 4395 -482 662 -740 C HETATM 3507 C14 OLA A2420 -27.049 -6.148 36.501 1.00 43.80 C ANISOU 3507 C14 OLA A2420 5120 7198 4325 -468 654 -537 C HETATM 3508 C15 OLA A2420 -26.163 -6.573 37.684 1.00 44.90 C ANISOU 3508 C15 OLA A2420 5542 7207 4310 -320 1241 -452 C HETATM 3509 C1 OLA A2421 -33.812 5.893 32.908 1.00 64.19 C ANISOU 3509 C1 OLA A2421 6300 9059 9032 442 2153 459 C HETATM 3510 O1 OLA A2421 -32.694 6.460 32.788 1.00 66.67 O ANISOU 3510 O1 OLA A2421 7244 9139 8950 117 2713 659 O HETATM 3511 O2 OLA A2421 -34.767 6.599 33.268 1.00 65.90 O ANISOU 3511 O2 OLA A2421 6587 9188 9265 994 1281 338 O HETATM 3512 C2 OLA A2421 -34.002 4.415 32.619 1.00 61.31 C ANISOU 3512 C2 OLA A2421 5635 8822 8838 393 2126 361 C HETATM 3513 C3 OLA A2421 -32.853 3.567 33.171 1.00 60.56 C ANISOU 3513 C3 OLA A2421 5764 8638 8607 358 2749 232 C HETATM 3514 C4 OLA A2421 -32.643 2.264 32.411 1.00 61.45 C ANISOU 3514 C4 OLA A2421 6567 8490 8292 386 2349 106 C HETATM 3515 C5 OLA A2421 -31.280 1.645 32.647 1.00 58.80 C ANISOU 3515 C5 OLA A2421 6023 8421 7896 292 1748 6 C HETATM 3516 C6 OLA A2421 -31.312 0.351 33.451 1.00 59.68 C ANISOU 3516 C6 OLA A2421 6679 8399 7598 758 1239 -175 C HETATM 3517 C7 OLA A2421 -30.481 -0.741 32.787 1.00 57.53 C ANISOU 3517 C7 OLA A2421 6172 8314 7373 1045 1885 -312 C HETATM 3518 C8 OLA A2421 -29.863 -1.741 33.743 1.00 57.56 C ANISOU 3518 C8 OLA A2421 6487 8220 7162 1491 3072 -528 C HETATM 3519 C9 OLA A2421 -30.698 -3.013 33.727 1.00 53.95 C ANISOU 3519 C9 OLA A2421 5415 8143 6940 1366 3292 -669 C HETATM 3520 C5 OLA A2422 -33.317 -17.047 26.912 1.00 47.07 C ANISOU 3520 C5 OLA A2422 5550 6676 5658 -742 -1057 1029 C HETATM 3521 C6 OLA A2422 -32.782 -15.623 26.884 1.00 45.23 C ANISOU 3521 C6 OLA A2422 4782 6677 5725 225 -884 1053 C HETATM 3522 C7 OLA A2422 -33.895 -14.603 27.079 1.00 49.43 C ANISOU 3522 C7 OLA A2422 6208 6713 5861 90 -252 1024 C HETATM 3523 C8 OLA A2422 -33.441 -13.158 27.196 1.00 50.29 C ANISOU 3523 C8 OLA A2422 6280 6738 6089 -301 -280 929 C HETATM 3524 C9 OLA A2422 -33.446 -12.810 28.672 1.00 52.63 C ANISOU 3524 C9 OLA A2422 6778 6715 6503 274 253 816 C HETATM 3525 C10 OLA A2422 -33.629 -11.602 29.249 1.00 52.83 C ANISOU 3525 C10 OLA A2422 6574 6695 6804 24 219 858 C HETATM 3526 C11 OLA A2422 -33.864 -10.302 28.518 1.00 49.48 C ANISOU 3526 C11 OLA A2422 5442 6632 6725 -254 1005 789 C HETATM 3527 C12 OLA A2422 -33.104 -9.179 29.238 1.00 48.76 C ANISOU 3527 C12 OLA A2422 5370 6639 6517 321 1786 588 C HETATM 3528 C13 OLA A2422 -33.935 -7.908 29.477 1.00 49.07 C ANISOU 3528 C13 OLA A2422 5524 6669 6450 484 1369 446 C HETATM 3529 C14 OLA A2422 -33.381 -7.084 30.647 1.00 47.04 C ANISOU 3529 C14 OLA A2422 4756 6677 6441 801 884 292 C HETATM 3530 C15 OLA A2422 -33.846 -5.617 30.660 1.00 47.49 C ANISOU 3530 C15 OLA A2422 4892 6658 6493 952 1022 152 C HETATM 3531 C16 OLA A2422 -33.590 -4.950 32.018 1.00 46.36 C ANISOU 3531 C16 OLA A2422 4651 6587 6376 1394 911 98 C HETATM 3532 C17 OLA A2422 -32.270 -5.416 32.639 1.00 44.59 C ANISOU 3532 C17 OLA A2422 4248 6478 6218 1873 555 265 C HETATM 3533 C1 OLA A2423 -41.805 15.915 13.584 1.00 60.37 C ANISOU 3533 C1 OLA A2423 8972 7306 6660 1691 263 1813 C HETATM 3534 O1 OLA A2423 -42.479 16.924 13.303 1.00 67.53 O ANISOU 3534 O1 OLA A2423 11208 7411 7040 1507 1201 1873 O HETATM 3535 O2 OLA A2423 -40.714 16.083 14.195 1.00 57.84 O ANISOU 3535 O2 OLA A2423 7845 7318 6812 1980 111 1895 O HETATM 3536 C2 OLA A2423 -42.298 14.538 13.196 1.00 51.76 C ANISOU 3536 C2 OLA A2423 6518 7163 5984 1203 606 1593 C HETATM 3537 C3 OLA A2423 -41.443 13.445 13.836 1.00 46.46 C ANISOU 3537 C3 OLA A2423 5079 7128 5444 643 1567 1478 C HETATM 3538 C4 OLA A2423 -41.423 12.171 13.012 1.00 43.57 C ANISOU 3538 C4 OLA A2423 4077 7277 5202 158 585 1387 C HETATM 3539 C5 OLA A2423 -41.169 10.936 13.839 1.00 41.45 C ANISOU 3539 C5 OLA A2423 3386 7364 4999 321 618 1353 C HETATM 3540 C6 OLA A2423 -41.599 9.640 13.177 1.00 41.81 C ANISOU 3540 C6 OLA A2423 3388 7599 4897 661 1568 1213 C HETATM 3541 C7 OLA A2423 -40.533 8.568 13.353 1.00 42.94 C ANISOU 3541 C7 OLA A2423 3880 7662 4772 312 1274 1163 C HETATM 3542 C8 OLA A2423 -41.064 7.200 13.718 1.00 42.17 C ANISOU 3542 C8 OLA A2423 3583 7724 4716 -131 1544 967 C HETATM 3543 C9 OLA A2423 -41.025 6.317 12.488 1.00 43.66 C ANISOU 3543 C9 OLA A2423 4161 7657 4772 86 1036 683 C HETATM 3544 C10 OLA A2423 -41.618 5.112 12.371 1.00 45.72 C ANISOU 3544 C10 OLA A2423 4995 7619 4758 524 328 601 C HETATM 3545 C11 OLA A2423 -42.428 4.439 13.458 1.00 49.12 C ANISOU 3545 C11 OLA A2423 6330 7607 4726 1142 -452 387 C HETATM 3546 C12 OLA A2423 -42.638 2.971 13.066 1.00 46.73 C ANISOU 3546 C12 OLA A2423 5476 7667 4611 534 -1286 208 C HETATM 3547 C13 OLA A2423 -43.527 2.128 13.991 1.00 45.53 C ANISOU 3547 C13 OLA A2423 4970 7813 4515 557 -1153 -36 C HETATM 3548 C14 OLA A2423 -43.252 0.636 13.755 1.00 41.73 C ANISOU 3548 C14 OLA A2423 3353 7869 4635 809 -1285 -176 C HETATM 3549 C15 OLA A2423 -44.173 -0.335 14.515 1.00 43.86 C ANISOU 3549 C15 OLA A2423 3968 7983 4713 500 -1579 -324 C HETATM 3550 C1 OLA A2424 -32.216 15.098 8.062 1.00 75.07 C ANISOU 3550 C1 OLA A2424 10822 6654 11048 44 16 -7 C HETATM 3551 O1 OLA A2424 -31.340 14.193 8.003 1.00 73.87 O ANISOU 3551 O1 OLA A2424 10546 6629 10893 1111 742 306 O HETATM 3552 O2 OLA A2424 -31.829 16.265 8.225 1.00 77.75 O ANISOU 3552 O2 OLA A2424 11660 6635 11246 -733 -477 -245 O HETATM 3553 C2 OLA A2424 -33.696 14.796 7.937 1.00 70.47 C ANISOU 3553 C2 OLA A2424 9125 6683 10967 -105 -672 -95 C HETATM 3554 C3 OLA A2424 -33.934 13.356 7.483 1.00 67.42 C ANISOU 3554 C3 OLA A2424 8075 6694 10848 -346 -1010 -196 C HETATM 3555 C4 OLA A2424 -34.866 12.586 8.410 1.00 64.76 C ANISOU 3555 C4 OLA A2424 7196 6725 10685 -233 -762 -230 C HETATM 3556 C5 OLA A2424 -35.814 11.658 7.677 1.00 61.32 C ANISOU 3556 C5 OLA A2424 6120 6727 10450 -428 -990 -260 C HETATM 3557 C6 OLA A2424 -35.465 10.180 7.777 1.00 58.82 C ANISOU 3557 C6 OLA A2424 5480 6662 10206 -170 -1073 -232 C HETATM 3558 C7 OLA A2424 -36.630 9.293 7.344 1.00 58.48 C ANISOU 3558 C7 OLA A2424 5469 6642 10110 137 -1014 -314 C HETATM 3559 C8 OLA A2424 -36.244 7.879 6.947 1.00 56.87 C ANISOU 3559 C8 OLA A2424 4899 6562 10147 736 -794 -532 C HETATM 3560 C9 OLA A2424 -36.936 7.514 5.639 1.00 56.68 C ANISOU 3560 C9 OLA A2424 4693 6541 10303 494 -209 -826 C HETATM 3561 C10 OLA A2424 -37.370 6.280 5.289 1.00 53.82 C ANISOU 3561 C10 OLA A2424 3559 6492 10398 1027 -199 -1034 C HETATM 3562 C9 OLA A2425 -21.100 -11.668 0.352 1.00 48.05 C ANISOU 3562 C9 OLA A2425 5273 6693 6289 1273 -113 -668 C HETATM 3563 C10 OLA A2425 -21.325 -10.589 1.140 1.00 48.91 C ANISOU 3563 C10 OLA A2425 5499 6678 6405 1063 -405 -801 C HETATM 3564 C11 OLA A2425 -20.972 -10.531 2.615 1.00 50.24 C ANISOU 3564 C11 OLA A2425 5889 6655 6544 680 -155 -906 C HETATM 3565 C12 OLA A2425 -21.747 -9.431 3.371 1.00 50.52 C ANISOU 3565 C12 OLA A2425 6107 6633 6457 654 -254 -1020 C HETATM 3566 C13 OLA A2425 -21.324 -7.996 2.987 1.00 47.67 C ANISOU 3566 C13 OLA A2425 5344 6568 6200 816 -729 -1168 C HETATM 3567 C14 OLA A2425 -22.257 -6.905 3.538 1.00 47.87 C ANISOU 3567 C14 OLA A2425 5870 6583 5735 362 -171 -1284 C HETATM 3568 C15 OLA A2425 -22.866 -6.010 2.440 1.00 45.44 C ANISOU 3568 C15 OLA A2425 5430 6526 5309 665 -345 -1439 C HETATM 3569 C16 OLA A2425 -23.770 -4.885 2.965 1.00 45.31 C ANISOU 3569 C16 OLA A2425 5816 6561 4840 767 -133 -1396 C HETATM 3570 C17 OLA A2425 -23.568 -3.553 2.228 1.00 44.56 C ANISOU 3570 C17 OLA A2425 5831 6669 4430 1616 774 -1265 C HETATM 3571 C18 OLA A2425 -24.881 -2.771 2.067 1.00 41.29 C ANISOU 3571 C18 OLA A2425 4878 6741 4069 2074 1250 -1173 C HETATM 3572 C1 OLB A2426 -3.937 6.466 30.173 1.00 67.85 C ANISOU 3572 C1 OLB A2426 9246 7743 8791 -619 -140 119 C HETATM 3573 C2 OLB A2426 -3.656 5.032 30.612 1.00 62.46 C ANISOU 3573 C2 OLB A2426 7535 7528 8668 -217 100 -41 C HETATM 3574 C3 OLB A2426 -4.405 4.034 29.729 1.00 57.91 C ANISOU 3574 C3 OLB A2426 6071 7311 8623 -237 528 -137 C HETATM 3575 C4 OLB A2426 -3.968 2.588 29.938 1.00 58.49 C ANISOU 3575 C4 OLB A2426 6369 7143 8712 -804 346 -201 C HETATM 3576 C5 OLB A2426 -5.112 1.617 29.657 1.00 59.76 C ANISOU 3576 C5 OLB A2426 6738 7136 8831 -715 -599 -305 C HETATM 3577 O19 OLB A2426 -4.529 6.655 29.169 1.00 73.60 O ANISOU 3577 O19 OLB A2426 11253 7849 8864 -589 452 81 O HETATM 3578 O20 OLB A2426 -3.518 7.562 30.934 1.00 68.53 O ANISOU 3578 O20 OLB A2426 9204 7871 8965 -868 -164 292 O HETATM 3579 C21 OLB A2426 -3.043 8.617 30.147 1.00 69.78 C ANISOU 3579 C21 OLB A2426 9560 7930 9024 -810 -631 201 C HETATM 3580 C22 OLB A2426 -3.980 9.810 30.297 1.00 69.30 C ANISOU 3580 C22 OLB A2426 9397 7941 8993 -904 -963 23 C HETATM 3581 O23 OLB A2426 -3.205 10.973 30.282 1.00 68.17 O ANISOU 3581 O23 OLB A2426 9111 7987 8804 -836 -881 34 O HETATM 3582 C24 OLB A2426 -4.988 9.901 29.156 1.00 72.11 C ANISOU 3582 C24 OLB A2426 10346 7904 9147 -1132 -737 -188 C HETATM 3583 O25 OLB A2426 -5.474 11.215 29.089 1.00 73.70 O ANISOU 3583 O25 OLB A2426 10893 7846 9265 -1410 -564 -303 O HETATM 3584 C6 OLB A2426 -4.631 0.208 29.312 1.00 62.91 C ANISOU 3584 C6 OLB A2426 7719 7161 9022 -882 -472 -345 C HETATM 3585 C7 OLB A2426 -5.801 -0.753 29.085 1.00 64.90 C ANISOU 3585 C7 OLB A2426 8303 7164 9191 -718 -686 -383 C HETATM 3586 C8 OLB A2426 -5.538 -1.752 27.959 1.00 63.03 C ANISOU 3586 C8 OLB A2426 7628 7052 9269 -682 -1174 -377 C HETATM 3587 C9 OLB A2426 -6.408 -2.995 28.144 1.00 61.38 C ANISOU 3587 C9 OLB A2426 7068 6897 9358 -731 -1316 -333 C HETATM 3588 C10 OLB A2426 -6.102 -4.111 27.511 1.00 59.01 C ANISOU 3588 C10 OLB A2426 6243 6761 9417 -876 -929 -325 C HETATM 3589 C1 OLB A2427 -2.182 9.563 25.537 1.00 54.94 C ANISOU 3589 C1 OLB A2427 5029 9173 6673 3209 1470 -342 C HETATM 3590 C2 OLB A2427 -2.300 8.222 26.236 1.00 51.62 C ANISOU 3590 C2 OLB A2427 4597 8401 6617 2576 1890 -417 C HETATM 3591 C3 OLB A2427 -2.742 7.172 25.228 1.00 50.26 C ANISOU 3591 C3 OLB A2427 4279 8551 6265 2720 1379 -225 C HETATM 3592 C4 OLB A2427 -2.846 5.796 25.861 1.00 48.67 C ANISOU 3592 C4 OLB A2427 3739 8655 6097 2698 539 -161 C HETATM 3593 C5 OLB A2427 -3.585 4.806 24.975 1.00 47.11 C ANISOU 3593 C5 OLB A2427 3248 8558 6094 2216 618 -128 C HETATM 3594 O19 OLB A2427 -2.396 9.600 24.381 1.00 59.80 O ANISOU 3594 O19 OLB A2427 6108 9278 7337 2871 1055 -529 O HETATM 3595 O20 OLB A2427 -1.834 10.736 26.207 1.00 57.69 O ANISOU 3595 O20 OLB A2427 5751 9343 6827 2779 1648 -155 O HETATM 3596 C21 OLB A2427 -1.949 11.868 25.388 1.00 60.59 C ANISOU 3596 C21 OLB A2427 6349 9383 7289 2166 226 -202 C HETATM 3597 C22 OLB A2427 -1.860 13.132 26.233 1.00 65.71 C ANISOU 3597 C22 OLB A2427 7667 9494 7807 1699 -38 -339 C HETATM 3598 O23 OLB A2427 -0.645 13.764 25.950 1.00 69.20 O ANISOU 3598 O23 OLB A2427 8743 9464 8085 1899 1118 -409 O HETATM 3599 C24 OLB A2427 -2.964 14.125 25.896 1.00 74.86 C ANISOU 3599 C24 OLB A2427 10756 9771 7918 353 -820 -381 C HETATM 3600 O25 OLB A2427 -2.740 14.560 24.582 1.00 78.14 O ANISOU 3600 O25 OLB A2427 11766 9920 8005 -179 -672 -457 O HETATM 3601 C6 OLB A2427 -2.915 3.443 24.987 1.00 45.53 C ANISOU 3601 C6 OLB A2427 2852 8422 6025 1915 -103 -74 C HETATM 3602 C7 OLB A2427 -3.872 2.272 25.129 1.00 45.47 C ANISOU 3602 C7 OLB A2427 2716 8395 6167 1467 -850 -118 C HETATM 3603 C8 OLB A2427 -3.284 1.025 24.486 1.00 51.29 C ANISOU 3603 C8 OLB A2427 4203 8819 6466 880 -634 -92 C HETATM 3604 C9 OLB A2427 -4.023 -0.230 24.942 1.00 58.79 C ANISOU 3604 C9 OLB A2427 6693 8805 6840 677 -176 -53 C HETATM 3605 C10 OLB A2427 -3.677 -1.379 24.399 1.00 62.44 C ANISOU 3605 C10 OLB A2427 7632 8778 7315 -198 -119 -170 C HETATM 3606 C11 OLB A2427 -4.364 -2.679 24.804 1.00 64.09 C ANISOU 3606 C11 OLB A2427 7940 8705 7706 -612 -242 -343 C HETATM 3607 C12 OLB A2427 -3.679 -3.856 24.114 1.00 62.73 C ANISOU 3607 C12 OLB A2427 7344 8624 7865 -1 -40 -484 C HETATM 3608 C1 OLB A2428 -33.951 -21.712 18.545 1.00 70.05 C ANISOU 3608 C1 OLB A2428 8411 9453 8750 -1719 175 -512 C HETATM 3609 C2 OLB A2428 -34.433 -20.705 17.510 1.00 63.81 C ANISOU 3609 C2 OLB A2428 6698 9315 8233 -2101 262 -520 C HETATM 3610 C3 OLB A2428 -35.505 -19.802 18.103 1.00 63.56 C ANISOU 3610 C3 OLB A2428 6781 9327 8041 -2053 695 -441 C HETATM 3611 C4 OLB A2428 -35.669 -18.516 17.308 1.00 64.33 C ANISOU 3611 C4 OLB A2428 6987 9442 8013 -1443 1788 -343 C HETATM 3612 C5 OLB A2428 -36.341 -17.446 18.152 1.00 63.40 C ANISOU 3612 C5 OLB A2428 6659 9472 7958 -978 1902 -250 C HETATM 3613 O19 OLB A2428 -33.019 -21.453 19.225 1.00 76.17 O ANISOU 3613 O19 OLB A2428 10542 9426 8972 -1684 813 -365 O HETATM 3614 O20 OLB A2428 -34.608 -22.936 18.702 1.00 73.42 O ANISOU 3614 O20 OLB A2428 9220 9653 9022 -925 347 -545 O HETATM 3615 C21 OLB A2428 -33.779 -23.956 19.177 1.00 77.00 C ANISOU 3615 C21 OLB A2428 10207 9803 9248 -858 39 -522 C HETATM 3616 C22 OLB A2428 -34.364 -24.460 20.492 1.00 79.73 C ANISOU 3616 C22 OLB A2428 10928 9943 9421 -591 -161 -516 C HETATM 3617 O23 OLB A2428 -35.752 -24.541 20.336 1.00 82.34 O ANISOU 3617 O23 OLB A2428 11887 9823 9577 -476 -281 -469 O HETATM 3618 C24 OLB A2428 -33.844 -25.844 20.870 1.00 81.07 C ANISOU 3618 C24 OLB A2428 11116 10240 9448 -462 -316 -565 C HETATM 3619 O25 OLB A2428 -34.571 -26.312 21.972 1.00 82.12 O ANISOU 3619 O25 OLB A2428 11364 10432 9407 -377 -88 -579 O HETATM 3620 C6 OLB A2428 -35.296 -16.618 18.885 1.00 59.46 C ANISOU 3620 C6 OLB A2428 5466 9451 7676 -1053 1647 -227 C HETATM 3621 C7 OLB A2428 -34.929 -15.373 18.093 1.00 56.28 C ANISOU 3621 C7 OLB A2428 4718 9353 7313 -699 1987 -247 C HETATM 3622 C8 OLB A2428 -35.439 -14.139 18.815 1.00 53.75 C ANISOU 3622 C8 OLB A2428 4125 9293 7004 -395 1838 -387 C HETATM 3623 C9 OLB A2428 -35.213 -12.887 17.978 1.00 52.15 C ANISOU 3623 C9 OLB A2428 3654 9261 6901 -280 1362 -478 C HETATM 3624 C10 OLB A2428 -35.647 -11.767 18.506 1.00 54.83 C ANISOU 3624 C10 OLB A2428 4495 9242 7095 -464 744 -379 C HETATM 3625 C11 OLB A2428 -35.512 -10.420 17.814 1.00 55.78 C ANISOU 3625 C11 OLB A2428 4646 9199 7348 -729 1253 -345 C HETATM 3626 C12 OLB A2428 -36.738 -9.600 18.218 1.00 61.31 C ANISOU 3626 C12 OLB A2428 6624 9138 7532 -796 1845 -330 C HETATM 3627 C13 OLB A2428 -37.061 -9.743 19.706 1.00 62.91 C ANISOU 3627 C13 OLB A2428 7259 9068 7576 -988 1859 -266 C HETATM 3628 C18 OLC A2429 -40.484 -5.531 17.225 1.00 66.61 C ANISOU 3628 C18 OLC A2429 8702 7434 9171 1079 1424 705 C HETATM 3629 C10 OLC A2429 -38.584 3.107 14.677 1.00 48.46 C ANISOU 3629 C10 OLC A2429 4344 7008 7062 331 -314 531 C HETATM 3630 C9 OLC A2429 -37.957 4.245 14.867 1.00 43.53 C ANISOU 3630 C9 OLC A2429 2653 6987 6901 -89 -308 606 C HETATM 3631 C17 OLC A2429 -40.745 -4.652 16.002 1.00 64.17 C ANISOU 3631 C17 OLC A2429 7967 7379 9034 1220 1364 737 C HETATM 3632 C11 OLC A2429 -38.569 2.056 15.779 1.00 49.39 C ANISOU 3632 C11 OLC A2429 4529 6990 7246 880 331 425 C HETATM 3633 C8 OLC A2429 -37.231 4.463 16.186 1.00 43.03 C ANISOU 3633 C8 OLC A2429 2470 7167 6714 -866 -358 837 C HETATM 3634 C24 OLC A2429 -37.737 16.678 17.618 1.00 67.86 C ANISOU 3634 C24 OLC A2429 10519 7715 7548 979 574 -87 C HETATM 3635 C16 OLC A2429 -41.394 -3.329 16.388 1.00 62.44 C ANISOU 3635 C16 OLC A2429 7642 7281 8803 930 1117 729 C HETATM 3636 C12 OLC A2429 -39.305 0.808 15.310 1.00 47.15 C ANISOU 3636 C12 OLC A2429 3267 6960 7689 711 323 417 C HETATM 3637 C7 OLC A2429 -36.756 5.901 16.257 1.00 44.72 C ANISOU 3637 C7 OLC A2429 3034 7237 6719 -558 587 1158 C HETATM 3638 C15 OLC A2429 -40.802 -2.140 15.638 1.00 58.17 C ANISOU 3638 C15 OLC A2429 6240 7239 8623 753 663 608 C HETATM 3639 C13 OLC A2429 -40.084 0.182 16.462 1.00 51.94 C ANISOU 3639 C13 OLC A2429 4577 7026 8131 1335 37 454 C HETATM 3640 C6 OLC A2429 -37.877 6.758 16.804 1.00 40.06 C ANISOU 3640 C6 OLC A2429 2118 6706 6396 -822 839 575 C HETATM 3641 C14 OLC A2429 -39.892 -1.329 16.555 1.00 55.91 C ANISOU 3641 C14 OLC A2429 5654 7162 8428 1342 -23 489 C HETATM 3642 C5 OLC A2429 -37.406 8.070 17.404 1.00 40.18 C ANISOU 3642 C5 OLC A2429 2391 6540 6334 -1170 1197 458 C HETATM 3643 C4 OLC A2429 -38.067 9.240 16.696 1.00 41.64 C ANISOU 3643 C4 OLC A2429 2671 7099 6052 -987 1426 687 C HETATM 3644 C3 OLC A2429 -37.941 10.531 17.491 1.00 43.02 C ANISOU 3644 C3 OLC A2429 3345 6969 6033 -937 882 290 C HETATM 3645 C2 OLC A2429 -38.251 11.750 16.628 1.00 46.73 C ANISOU 3645 C2 OLC A2429 4608 6899 6247 -906 825 203 C HETATM 3646 C21 OLC A2429 -39.686 15.048 17.730 1.00 56.73 C ANISOU 3646 C21 OLC A2429 7311 7236 7008 111 1114 324 C HETATM 3647 C1 OLC A2429 -38.970 12.838 17.418 1.00 49.08 C ANISOU 3647 C1 OLC A2429 5150 7013 6484 -316 176 256 C HETATM 3648 C22 OLC A2429 -38.556 15.728 18.492 1.00 63.50 C ANISOU 3648 C22 OLC A2429 9182 7474 7472 594 850 287 C HETATM 3649 O19 OLC A2429 -39.413 12.589 18.488 1.00 49.24 O ANISOU 3649 O19 OLC A2429 5174 7026 6509 605 911 209 O HETATM 3650 O25 OLC A2429 -38.375 17.926 17.546 1.00 72.52 O ANISOU 3650 O25 OLC A2429 12037 7904 7613 680 613 -245 O HETATM 3651 O23 OLC A2429 -39.117 16.455 19.550 1.00 68.63 O ANISOU 3651 O23 OLC A2429 10579 7572 7927 -72 37 554 O HETATM 3652 O20 OLC A2429 -39.096 14.119 16.874 1.00 50.95 O ANISOU 3652 O20 OLC A2429 5537 7119 6703 -804 230 364 O HETATM 3653 C10 OLC A2430 -33.638 -9.140 23.372 1.00 52.06 C ANISOU 3653 C10 OLC A2430 5777 7784 6220 -1106 718 450 C HETATM 3654 C9 OLC A2430 -33.475 -10.416 23.115 1.00 49.34 C ANISOU 3654 C9 OLC A2430 4753 7747 6247 -1290 748 703 C HETATM 3655 C11 OLC A2430 -33.972 -8.591 24.744 1.00 48.10 C ANISOU 3655 C11 OLC A2430 4600 7703 5974 -1428 525 316 C HETATM 3656 C8 OLC A2430 -33.608 -11.498 24.162 1.00 47.03 C ANISOU 3656 C8 OLC A2430 4077 7728 6064 -681 209 609 C HETATM 3657 C24 OLC A2430 -31.786 -24.008 25.324 1.00 67.74 C ANISOU 3657 C24 OLC A2430 10300 7341 8097 -1404 -667 -38 C HETATM 3658 C12 OLC A2430 -34.162 -7.092 24.535 1.00 51.56 C ANISOU 3658 C12 OLC A2430 5990 7690 5912 -1733 1031 325 C HETATM 3659 C7 OLC A2430 -32.602 -12.554 23.736 1.00 46.66 C ANISOU 3659 C7 OLC A2430 4152 7736 5842 -1550 1958 378 C HETATM 3660 C6 OLC A2430 -33.209 -13.679 22.911 1.00 44.18 C ANISOU 3660 C6 OLC A2430 3475 7725 5588 -1251 1220 138 C HETATM 3661 C5 OLC A2430 -32.165 -14.766 22.699 1.00 45.73 C ANISOU 3661 C5 OLC A2430 4165 7595 5614 -1344 1368 164 C HETATM 3662 C4 OLC A2430 -32.786 -16.066 22.219 1.00 49.27 C ANISOU 3662 C4 OLC A2430 5487 7462 5771 -1426 691 228 C HETATM 3663 C3 OLC A2430 -31.852 -17.253 22.415 1.00 46.99 C ANISOU 3663 C3 OLC A2430 4465 7377 6012 -1555 288 284 C HETATM 3664 C2 OLC A2430 -32.686 -18.460 22.825 1.00 52.56 C ANISOU 3664 C2 OLC A2430 5990 7430 6550 -1566 11 137 C HETATM 3665 C21 OLC A2430 -31.596 -21.832 24.000 1.00 63.28 C ANISOU 3665 C21 OLC A2430 8579 7345 8118 -1122 -255 16 C HETATM 3666 C1 OLC A2430 -31.880 -19.747 22.915 1.00 56.51 C ANISOU 3666 C1 OLC A2430 6674 7502 7294 -1287 424 -141 C HETATM 3667 C22 OLC A2430 -32.313 -23.178 24.154 1.00 64.81 C ANISOU 3667 C22 OLC A2430 9012 7290 8322 -1051 -440 -85 C HETATM 3668 O19 OLC A2430 -30.759 -19.754 22.543 1.00 61.94 O ANISOU 3668 O19 OLC A2430 8510 7632 7391 -1646 28 -462 O HETATM 3669 O25 OLC A2430 -32.532 -25.192 25.412 1.00 67.43 O ANISOU 3669 O25 OLC A2430 10344 7322 7954 -1952 -1270 -26 O HETATM 3670 O23 OLC A2430 -33.679 -22.950 24.363 1.00 60.19 O ANISOU 3670 O23 OLC A2430 7065 7186 8619 -1156 -957 -311 O HETATM 3671 O20 OLC A2430 -32.479 -20.906 23.431 1.00 62.97 O ANISOU 3671 O20 OLC A2430 8682 7447 7796 -805 400 9 O HETATM 3672 O HOH A2501 -32.907 17.080 28.801 1.00 64.37 O HETATM 3673 O HOH A2502 -44.555 16.791 12.726 1.00 55.68 O HETATM 3674 O HOH A2503 -31.147 8.030 32.408 1.00 63.56 O HETATM 3675 O HOH A2504 1.451 -46.602 20.546 1.00 47.51 O HETATM 3676 O HOH A2505 -2.862 16.863 24.363 1.00 60.48 O HETATM 3677 O HOH A2506 -23.502 15.563 33.327 1.00 35.68 O HETATM 3678 O HOH A2507 -24.816 13.901 11.806 1.00 35.73 O HETATM 3679 O HOH A2508 -29.182 9.324 35.654 1.00 40.51 O HETATM 3680 O HOH A2509 -19.622 13.398 25.142 1.00 52.80 O HETATM 3681 O HOH A2510 3.712 -72.947 23.842 1.00 42.57 O HETATM 3682 O HOH A2511 -22.779 -28.018 21.510 1.00 53.94 O HETATM 3683 O HOH A2512 -22.203 17.862 25.767 1.00 43.41 O HETATM 3684 O HOH A2513 -29.010 12.386 8.738 1.00 34.60 O HETATM 3685 O HOH A2514 0.007 -27.981 20.823 1.00 47.70 O HETATM 3686 O HOH A2515 -7.778 10.112 30.952 1.00 36.65 O HETATM 3687 O HOH A2516 -16.881 -25.131 9.646 1.00 36.98 O HETATM 3688 O HOH A2517 -6.771 20.828 21.624 1.00 69.51 O HETATM 3689 O HOH A2518 -21.383 -33.456 22.371 1.00 58.37 O HETATM 3690 O HOH A2519 -4.402 -63.424 26.983 1.00 42.51 O HETATM 3691 O HOH A2520 -16.299 -16.848 19.058 1.00 19.68 O HETATM 3692 O HOH A2521 -2.687 -64.611 20.294 1.00 36.15 O HETATM 3693 O HOH A2522 -13.018 -33.326 21.336 1.00 45.89 O HETATM 3694 O HOH A2523 -26.067 -11.879 25.625 1.00 23.33 O HETATM 3695 O HOH A2524 -9.417 15.015 18.383 1.00 35.36 O HETATM 3696 O HOH A2525 -11.310 15.236 23.166 1.00 32.69 O HETATM 3697 O HOH A2526 -40.009 15.051 22.937 1.00 47.79 O HETATM 3698 O HOH A2527 -18.071 12.948 23.510 1.00 23.20 O HETATM 3699 O HOH A2528 -14.480 -58.127 22.770 1.00 49.46 O HETATM 3700 O HOH A2529 -10.094 14.754 25.164 1.00 31.56 O HETATM 3701 O HOH A2530 -19.276 -35.664 26.622 1.00 45.98 O HETATM 3702 O HOH A2531 -28.708 2.619 19.631 1.00 14.14 O HETATM 3703 O HOH A2532 -24.602 23.689 29.995 1.00 42.22 O HETATM 3704 O HOH A2533 -10.761 15.662 19.860 1.00 46.01 O HETATM 3705 O HOH A2534 -18.657 10.358 22.887 1.00 24.37 O HETATM 3706 O HOH A2535 -8.631 -58.076 26.012 1.00 45.29 O HETATM 3707 O HOH A2536 -16.516 -29.269 11.209 1.00 43.22 O HETATM 3708 O HOH A2537 -25.090 -15.878 14.688 1.00 23.05 O HETATM 3709 O HOH A2538 -21.270 -27.484 18.127 1.00 49.24 O HETATM 3710 O HOH A2539 -12.923 17.559 11.211 1.00 45.37 O HETATM 3711 O HOH A2540 2.897 -38.259 22.019 1.00 68.28 O HETATM 3712 O HOH A2541 -10.191 -57.057 27.217 1.00 57.38 O HETATM 3713 O HOH A2542 -18.954 -11.347 13.054 1.00 18.84 O HETATM 3714 O HOH A2543 -17.166 17.217 16.545 1.00 38.17 O HETATM 3715 O HOH A2544 -25.602 -14.481 24.786 1.00 21.32 O HETATM 3716 O HOH A2545 -20.889 16.488 18.740 1.00 27.03 O HETATM 3717 O HOH A2546 -22.113 -6.620 15.418 1.00 18.77 O HETATM 3718 O HOH A2547 8.832 -66.491 15.066 1.00 45.22 O HETATM 3719 O HOH A2548 18.359 -58.672 25.763 1.00 61.79 O HETATM 3720 O HOH A2549 -28.035 5.529 17.773 1.00 18.66 O HETATM 3721 O HOH A2550 -14.986 10.034 17.807 1.00 13.21 O HETATM 3722 O HOH A2551 -0.737 -62.608 20.009 1.00 31.59 O HETATM 3723 O HOH A2552 -25.913 -12.086 21.544 1.00 17.36 O HETATM 3724 O HOH A2553 -25.635 5.326 18.741 1.00 20.43 O HETATM 3725 O HOH A2554 -25.355 -13.375 13.625 1.00 20.21 O HETATM 3726 O HOH A2555 -22.432 -9.817 15.177 1.00 37.63 O HETATM 3727 O HOH A2556 -26.208 18.552 22.092 1.00 18.07 O HETATM 3728 O HOH A2557 2.840 -68.330 18.677 1.00 45.71 O HETATM 3729 O HOH A2558 -19.526 -1.490 22.073 1.00 14.93 O HETATM 3730 O HOH A2559 -24.811 16.726 2.072 1.00 35.72 O HETATM 3731 O HOH A2560 -28.235 11.371 34.590 1.00 39.56 O HETATM 3732 O HOH A2561 -23.977 -11.125 11.357 1.00 26.13 O HETATM 3733 O HOH A2562 -25.343 2.485 15.939 1.00 15.67 O HETATM 3734 O HOH A2563 -7.103 -60.134 14.753 1.00 52.43 O HETATM 3735 O HOH A2564 -7.462 12.517 27.740 1.00 56.03 O HETATM 3736 O HOH A2565 -16.309 0.677 12.609 1.00 12.84 O HETATM 3737 O HOH A2566 0.328 -67.199 25.241 1.00 36.78 O HETATM 3738 O HOH A2567 -14.134 -27.919 19.726 1.00 36.67 O HETATM 3739 O HOH A2568 -23.484 -4.732 14.023 1.00 14.15 O HETATM 3740 O HOH A2569 -25.859 7.703 13.379 1.00 15.07 O HETATM 3741 O HOH A2570 -4.642 -63.876 17.979 1.00 39.18 O HETATM 3742 O HOH A2571 7.221 -60.671 15.268 1.00 41.99 O HETATM 3743 O HOH A2572 -14.601 -26.945 17.514 1.00 33.49 O HETATM 3744 O HOH A2573 -27.769 3.005 17.026 1.00 13.05 O HETATM 3745 O HOH A2574 -25.374 11.825 16.480 1.00 15.64 O HETATM 3746 O HOH A2575 -9.600 -28.798 9.808 1.00 60.03 O HETATM 3747 O HOH A2576 -36.426 -30.350 17.604 1.00 49.99 O HETATM 3748 O HOH A2577 -4.501 -25.930 25.038 1.00 37.30 O HETATM 3749 O HOH A2578 14.963 -55.688 18.538 1.00 43.75 O HETATM 3750 O HOH A2579 -20.859 -2.547 24.313 1.00 16.30 O HETATM 3751 O HOH A2580 -18.089 16.004 19.138 1.00 28.59 O HETATM 3752 O HOH A2581 -11.124 12.126 15.773 1.00 17.03 O HETATM 3753 O HOH A2582 5.752 -75.821 26.403 1.00 31.73 O HETATM 3754 O HOH A2583 -21.892 -24.345 30.190 1.00 66.96 O HETATM 3755 O HOH A2584 -33.942 13.936 30.283 1.00 33.56 O HETATM 3756 O HOH A2585 -17.999 -17.287 16.892 1.00 23.96 O HETATM 3757 O HOH A2586 -19.210 -33.072 33.177 1.00 55.01 O HETATM 3758 O HOH A2587 -31.427 21.812 27.836 1.00 78.29 O HETATM 3759 O HOH A2588 -44.474 18.913 13.124 1.00 61.46 O HETATM 3760 O HOH A2589 -2.228 13.274 22.120 1.00 23.46 O HETATM 3761 O HOH A2590 -27.510 -11.541 6.784 1.00 30.95 O HETATM 3762 O HOH A2591 -16.283 16.753 8.560 1.00 34.56 O HETATM 3763 O HOH A2592 -30.043 18.044 29.839 1.00 39.26 O HETATM 3764 O HOH A2593 -21.902 13.825 17.891 1.00 17.90 O HETATM 3765 O HOH A2594 -25.839 18.829 24.805 1.00 20.89 O HETATM 3766 O HOH A2595 -15.702 -39.553 17.015 1.00 53.61 O HETATM 3767 O HOH A2596 2.569 -52.761 30.020 1.00 63.21 O HETATM 3768 O HOH A2597 -15.250 3.573 21.811 1.00 13.39 O HETATM 3769 O HOH A2598 -23.694 4.172 17.009 1.00 24.39 O HETATM 3770 O HOH A2599 0.565 -61.959 29.763 1.00 36.26 O HETATM 3771 O HOH A2600 -12.133 -35.755 27.995 1.00 49.47 O HETATM 3772 O HOH A2601 -25.602 16.881 26.676 1.00 32.05 O HETATM 3773 O HOH A2602 -27.728 20.814 22.394 1.00 19.70 O HETATM 3774 O HOH A2603 -18.236 -2.834 20.017 1.00 15.18 O HETATM 3775 O HOH A2604 -18.462 -23.249 13.889 1.00 47.09 O HETATM 3776 O HOH A2605 -10.400 19.321 20.823 1.00 34.46 O HETATM 3777 O HOH A2606 -17.119 13.490 26.118 1.00 28.69 O HETATM 3778 O HOH A2607 -10.887 17.518 17.658 1.00 49.23 O HETATM 3779 O HOH A2608 -24.799 9.935 14.474 1.00 18.99 O HETATM 3780 O HOH A2609 -17.243 15.042 6.100 1.00 27.34 O HETATM 3781 O HOH A2610 -17.520 13.744 29.586 1.00 48.65 O HETATM 3782 O HOH A2611 -24.445 6.605 15.731 1.00 30.86 O HETATM 3783 O HOH A2612 -24.773 -6.480 17.610 1.00 37.50 O HETATM 3784 O HOH A2613 2.201 -29.318 19.503 1.00 58.46 O HETATM 3785 O HOH A2614 -5.071 15.540 10.910 1.00 65.55 O HETATM 3786 O HOH A2615 -11.941 14.945 4.882 1.00 44.38 O HETATM 3787 O HOH A2616 -3.458 16.249 21.578 1.00 33.56 O HETATM 3788 O HOH A2617 -35.940 18.813 16.111 1.00 44.64 O HETATM 3789 O HOH A2618 -15.814 -33.303 15.621 1.00 66.76 O HETATM 3790 O HOH A2619 -15.163 12.333 28.500 1.00 19.65 O HETATM 3791 O HOH A2620 -10.508 -37.346 18.280 1.00 53.52 O HETATM 3792 O HOH A2621 -19.832 -30.514 21.197 1.00 56.72 O HETATM 3793 O HOH A2622 -5.564 -61.429 28.352 1.00 53.73 O HETATM 3794 O HOH A2623 -20.706 -11.331 15.385 1.00 31.67 O HETATM 3795 O HOH A2624 0.539 13.413 28.704 1.00 40.01 O HETATM 3796 O HOH A2625 -24.666 -3.948 18.105 1.00 66.35 O HETATM 3797 O HOH A2626 -28.273 -28.661 33.781 1.00 60.09 O HETATM 3798 O HOH A2627 -25.052 -29.567 22.791 1.00 48.48 O HETATM 3799 O HOH A2628 -30.871 -29.885 6.373 1.00 50.05 O HETATM 3800 O HOH A2629 -20.530 -18.421 15.598 1.00 32.27 O HETATM 3801 O HOH A2630 -5.479 -31.334 24.657 1.00 47.24 O HETATM 3802 O HOH A2631 -11.867 19.519 14.914 1.00 44.61 O HETATM 3803 O HOH A2632 -32.497 23.949 25.928 1.00 56.70 O HETATM 3804 O HOH A2633 -19.238 16.700 24.632 1.00 50.02 O HETATM 3805 O HOH A2634 -21.629 -29.040 8.934 1.00 48.76 O HETATM 3806 O HOH A2635 -17.191 12.233 32.670 1.00 48.20 O HETATM 3807 O HOH A2636 -9.041 13.522 16.914 1.00 24.32 O HETATM 3808 O HOH A2637 -24.594 15.490 4.717 1.00 58.91 O HETATM 3809 O HOH A2638 8.636 -62.019 13.407 1.00 40.92 O HETATM 3810 O HOH A2639 -20.986 12.460 34.865 1.00 47.73 O HETATM 3811 O HOH A2640 -23.847 -27.026 13.719 1.00 48.40 O HETATM 3812 O HOH A2641 -21.647 22.950 27.178 1.00 44.86 O HETATM 3813 O HOH A2642 -11.416 10.501 32.474 1.00 39.95 O HETATM 3814 O HOH A2643 -18.327 -26.512 4.286 1.00 58.53 O HETATM 3815 O HOH A2644 -11.423 12.168 31.252 1.00 40.55 O HETATM 3816 O HOH A2645 -15.902 16.667 12.146 1.00 54.21 O HETATM 3817 O HOH A2646 -16.602 -30.858 15.276 1.00 50.00 O HETATM 3818 O AHOH A2647 -19.443 -28.425 8.334 0.46 21.32 O HETATM 3819 O BHOH A2647 -18.857 -28.056 6.681 0.54 26.60 O HETATM 3820 O HOH A2648 -19.323 12.595 32.483 1.00 46.95 O HETATM 3821 O HOH A2649 -15.910 14.283 22.066 1.00 43.41 O HETATM 3822 O HOH A2650 -21.302 -24.679 32.379 1.00 56.78 O HETATM 3823 O HOH A2651 8.050 -75.126 27.489 1.00 40.39 O HETATM 3824 O HOH A2652 6.443 -70.992 17.452 1.00 36.12 O HETATM 3825 O HOH A2653 -13.283 13.637 23.951 1.00 26.67 O HETATM 3826 O HOH A2654 -30.959 20.045 29.093 1.00 98.92 O HETATM 3827 O HOH A2655 -18.609 -34.565 22.793 1.00 69.50 O HETATM 3828 O HOH A2656 -34.624 10.828 33.604 1.00 54.63 O HETATM 3829 O HOH A2657 -15.751 -30.454 8.342 1.00 56.71 O HETATM 3830 O HOH A2658 22.047 -58.707 23.252 1.00 61.65 O HETATM 3831 O HOH A2659 -31.841 -29.546 27.097 1.00 65.59 O HETATM 3832 O HOH A2660 -21.224 21.449 34.978 1.00 56.73 O HETATM 3833 O HOH A2661 -8.896 -17.254 11.853 1.00 57.30 O HETATM 3834 O HOH A2662 -14.167 17.737 8.118 1.00 56.41 O HETATM 3835 O HOH A2663 4.217 -70.470 16.603 1.00 48.91 O HETATM 3836 O HOH A2664 -20.316 -21.636 15.034 1.00 50.74 O CONECT 419 3173 CONECT 563 1268 CONECT 579 1168 CONECT 599 1312 CONECT 720 3173 CONECT 1168 579 CONECT 1268 563 CONECT 1312 599 CONECT 2743 2764 CONECT 2764 2743 CONECT 3173 419 720 3717 3726 CONECT 3173 3783 CONECT 3174 3175 3180 CONECT 3175 3174 3176 CONECT 3176 3175 3177 3178 CONECT 3177 3176 CONECT 3178 3176 3179 CONECT 3179 3178 3180 CONECT 3180 3174 3179 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 3186 CONECT 3185 3184 3191 CONECT 3186 3184 3187 CONECT 3187 3186 3188 3189 CONECT 3188 3187 CONECT 3189 3187 3190 3191 CONECT 3190 3189 3193 CONECT 3191 3185 3189 3192 CONECT 3192 3191 3193 CONECT 3193 3190 3192 3194 CONECT 3194 3193 3195 3198 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3194 3197 CONECT 3199 3200 3208 CONECT 3200 3199 3201 CONECT 3201 3200 3202 3226 CONECT 3202 3201 3203 CONECT 3203 3202 3204 3208 CONECT 3204 3203 3205 CONECT 3205 3204 3206 CONECT 3206 3205 3207 3212 CONECT 3207 3206 3208 3209 CONECT 3208 3199 3203 3207 3217 CONECT 3209 3207 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 3215 3216 CONECT 3212 3206 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3211 3214 3218 CONECT 3216 3211 CONECT 3217 3208 CONECT 3218 3215 3219 3220 CONECT 3219 3218 CONECT 3220 3218 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 3225 CONECT 3224 3223 CONECT 3225 3223 CONECT 3226 3201 CONECT 3227 3228 3236 CONECT 3228 3227 3229 CONECT 3229 3228 3230 3254 CONECT 3230 3229 3231 CONECT 3231 3230 3232 3236 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 3240 CONECT 3235 3234 3236 3237 CONECT 3236 3227 3231 3235 3245 CONECT 3237 3235 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 3243 3244 CONECT 3240 3234 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3239 3242 3246 CONECT 3244 3239 CONECT 3245 3236 CONECT 3246 3243 3247 3248 CONECT 3247 3246 CONECT 3248 3246 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 3253 CONECT 3252 3251 CONECT 3253 3251 CONECT 3254 3229 CONECT 3255 3256 3264 CONECT 3256 3255 3257 CONECT 3257 3256 3258 3282 CONECT 3258 3257 3259 CONECT 3259 3258 3260 3264 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 3268 CONECT 3263 3262 3264 3265 CONECT 3264 3255 3259 3263 3273 CONECT 3265 3263 3266 CONECT 3266 3265 3267 CONECT 3267 3266 3268 3271 3272 CONECT 3268 3262 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 CONECT 3271 3267 3270 3274 CONECT 3272 3267 CONECT 3273 3264 CONECT 3274 3271 3275 3276 CONECT 3275 3274 CONECT 3276 3274 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 3281 CONECT 3280 3279 CONECT 3281 3279 CONECT 3282 3257 CONECT 3283 3284 3292 CONECT 3284 3283 3285 CONECT 3285 3284 3286 3310 CONECT 3286 3285 3287 CONECT 3287 3286 3288 3292 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 3291 3296 CONECT 3291 3290 3292 3293 CONECT 3292 3283 3287 3291 3301 CONECT 3293 3291 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 3299 3300 CONECT 3296 3290 3295 3297 CONECT 3297 3296 3298 CONECT 3298 3297 3299 CONECT 3299 3295 3298 3302 CONECT 3300 3295 CONECT 3301 3292 CONECT 3302 3299 3303 3304 CONECT 3303 3302 CONECT 3304 3302 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 CONECT 3307 3306 3308 3309 CONECT 3308 3307 CONECT 3309 3307 CONECT 3310 3285 CONECT 3311 3312 3313 3314 CONECT 3312 3311 CONECT 3313 3311 CONECT 3314 3311 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 3322 CONECT 3322 3321 3323 CONECT 3323 3322 3324 CONECT 3324 3323 3325 CONECT 3325 3324 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 3329 CONECT 3329 3328 3330 CONECT 3330 3329 CONECT 3331 3332 3333 3334 CONECT 3332 3331 CONECT 3333 3331 CONECT 3334 3331 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 CONECT 3346 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 CONECT 3353 3354 3355 3356 CONECT 3354 3353 CONECT 3355 3353 CONECT 3356 3353 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 CONECT 3362 3363 3364 3365 CONECT 3363 3362 CONECT 3364 3362 CONECT 3365 3362 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 CONECT 3380 3381 3382 3383 CONECT 3381 3380 CONECT 3382 3380 CONECT 3383 3380 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 CONECT 3400 3401 3402 3403 CONECT 3401 3400 CONECT 3402 3400 CONECT 3403 3400 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3414 CONECT 3414 3413 CONECT 3415 3416 3417 3418 CONECT 3416 3415 CONECT 3417 3415 CONECT 3418 3415 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 CONECT 3427 3428 3429 3430 CONECT 3428 3427 CONECT 3429 3427 CONECT 3430 3427 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 CONECT 3435 3436 3437 3438 CONECT 3436 3435 CONECT 3437 3435 CONECT 3438 3435 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 CONECT 3448 3447 CONECT 3449 3450 CONECT 3450 3449 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 CONECT 3456 3457 3458 3459 CONECT 3457 3456 CONECT 3458 3456 CONECT 3459 3456 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3464 CONECT 3464 3463 3465 CONECT 3465 3464 3466 CONECT 3466 3465 3467 CONECT 3467 3466 3468 CONECT 3468 3467 3469 CONECT 3469 3468 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 CONECT 3475 3476 CONECT 3476 3475 3477 CONECT 3477 3476 3478 CONECT 3478 3477 3479 CONECT 3479 3478 3480 CONECT 3480 3479 3481 CONECT 3481 3480 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 CONECT 3484 3483 CONECT 3485 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 CONECT 3492 3493 3494 3495 CONECT 3493 3492 CONECT 3494 3492 CONECT 3495 3492 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3498 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 CONECT 3504 3503 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 CONECT 3509 3510 3511 3512 CONECT 3510 3509 CONECT 3511 3509 CONECT 3512 3509 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 CONECT 3520 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 CONECT 3533 3534 3535 3536 CONECT 3534 3533 CONECT 3535 3533 CONECT 3536 3533 3537 CONECT 3537 3536 3538 CONECT 3538 3537 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3549 CONECT 3549 3548 CONECT 3550 3551 3552 3553 CONECT 3551 3550 CONECT 3552 3550 CONECT 3553 3550 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 CONECT 3562 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 3567 CONECT 3567 3566 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3571 CONECT 3571 3570 CONECT 3572 3573 3577 3578 CONECT 3573 3572 3574 CONECT 3574 3573 3575 CONECT 3575 3574 3576 CONECT 3576 3575 3584 CONECT 3577 3572 CONECT 3578 3572 3579 CONECT 3579 3578 3580 CONECT 3580 3579 3581 3582 CONECT 3581 3580 CONECT 3582 3580 3583 CONECT 3583 3582 CONECT 3584 3576 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3587 CONECT 3589 3590 3594 3595 CONECT 3590 3589 3591 CONECT 3591 3590 3592 CONECT 3592 3591 3593 CONECT 3593 3592 3601 CONECT 3594 3589 CONECT 3595 3589 3596 CONECT 3596 3595 3597 CONECT 3597 3596 3598 3599 CONECT 3598 3597 CONECT 3599 3597 3600 CONECT 3600 3599 CONECT 3601 3593 3602 CONECT 3602 3601 3603 CONECT 3603 3602 3604 CONECT 3604 3603 3605 CONECT 3605 3604 3606 CONECT 3606 3605 3607 CONECT 3607 3606 CONECT 3608 3609 3613 3614 CONECT 3609 3608 3610 CONECT 3610 3609 3611 CONECT 3611 3610 3612 CONECT 3612 3611 3620 CONECT 3613 3608 CONECT 3614 3608 3615 CONECT 3615 3614 3616 CONECT 3616 3615 3617 3618 CONECT 3617 3616 CONECT 3618 3616 3619 CONECT 3619 3618 CONECT 3620 3612 3621 CONECT 3621 3620 3622 CONECT 3622 3621 3623 CONECT 3623 3622 3624 CONECT 3624 3623 3625 CONECT 3625 3624 3626 CONECT 3626 3625 3627 CONECT 3627 3626 CONECT 3628 3631 CONECT 3629 3630 3632 CONECT 3630 3629 3633 CONECT 3631 3628 3635 CONECT 3632 3629 3636 CONECT 3633 3630 3637 CONECT 3634 3648 3650 CONECT 3635 3631 3638 CONECT 3636 3632 3639 CONECT 3637 3633 3640 CONECT 3638 3635 3641 CONECT 3639 3636 3641 CONECT 3640 3637 3642 CONECT 3641 3638 3639 CONECT 3642 3640 3643 CONECT 3643 3642 3644 CONECT 3644 3643 3645 CONECT 3645 3644 3647 CONECT 3646 3648 3652 CONECT 3647 3645 3649 3652 CONECT 3648 3634 3646 3651 CONECT 3649 3647 CONECT 3650 3634 CONECT 3651 3648 CONECT 3652 3646 3647 CONECT 3653 3654 3655 CONECT 3654 3653 3656 CONECT 3655 3653 3658 CONECT 3656 3654 3659 CONECT 3657 3667 3669 CONECT 3658 3655 CONECT 3659 3656 3660 CONECT 3660 3659 3661 CONECT 3661 3660 3662 CONECT 3662 3661 3663 CONECT 3663 3662 3664 CONECT 3664 3663 3666 CONECT 3665 3667 3671 CONECT 3666 3664 3668 3671 CONECT 3667 3657 3665 3670 CONECT 3668 3666 CONECT 3669 3657 CONECT 3670 3667 CONECT 3671 3665 3666 CONECT 3717 3173 CONECT 3726 3173 CONECT 3783 3173 MASTER 771 0 31 18 2 0 53 6 3661 1 513 34 END