HEADER MEMBRANE PROTEIN 17-MAR-16 5IU7 TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL TITLE 2 IN COMPLEX WITH COMPOUND 12C AT 1.9A 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_VECTOR_TYPE: BACMID; 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 2 27-JUL-16 5IU7 1 JRNL REVDAT 1 29-JUN-16 5IU7 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. 1.90 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.71 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 39555 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.172 REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.198 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 3726 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 33.7130 - 5.6914 0.97 2611 110 0.1827 0.1920 REMARK 3 2 5.6914 - 4.5209 0.98 2650 127 0.1693 0.1880 REMARK 3 3 4.5209 - 3.9504 0.99 2630 130 0.1454 0.1899 REMARK 3 4 3.9504 - 3.5897 0.99 2624 133 0.1454 0.1584 REMARK 3 5 3.5897 - 3.3326 1.00 2669 133 0.1486 0.1744 REMARK 3 6 3.3326 - 3.1363 1.00 2705 125 0.1451 0.1758 REMARK 3 7 3.1363 - 2.9793 1.00 2643 115 0.1478 0.1535 REMARK 3 8 2.9793 - 2.8497 0.99 2615 167 0.1378 0.1729 REMARK 3 9 2.8497 - 2.7400 1.00 2666 169 0.1403 0.1641 REMARK 3 10 2.7400 - 2.6455 1.00 2617 143 0.1389 0.1567 REMARK 3 11 2.6455 - 2.5628 1.00 2676 129 0.1484 0.1547 REMARK 3 12 2.5628 - 2.4896 1.00 2660 127 0.1506 0.1781 REMARK 3 13 2.4896 - 2.4241 0.99 2587 188 0.1584 0.2076 REMARK 3 14 2.4241 - 2.3650 0.99 2689 120 0.1586 0.2140 REMARK 3 15 2.3650 - 2.3112 0.99 2610 146 0.1688 0.2523 REMARK 3 16 2.3112 - 2.2620 1.00 2697 121 0.1752 0.2253 REMARK 3 17 2.2620 - 2.2168 0.99 2653 141 0.1796 0.1831 REMARK 3 18 2.2168 - 2.1750 0.99 2586 160 0.1966 0.2091 REMARK 3 19 2.1750 - 2.1361 0.99 2678 116 0.2058 0.2295 REMARK 3 20 2.1361 - 2.0999 1.00 2633 155 0.2104 0.2366 REMARK 3 21 2.0999 - 2.0661 0.99 2644 133 0.2248 0.2653 REMARK 3 22 2.0661 - 2.0343 1.00 2658 170 0.2348 0.2487 REMARK 3 23 2.0343 - 2.0044 1.00 2646 146 0.2410 0.2950 REMARK 3 24 2.0044 - 1.9761 1.00 2637 151 0.2642 0.2854 REMARK 3 25 1.9761 - 1.9494 1.00 2686 126 0.2770 0.3640 REMARK 3 26 1.9494 - 1.9241 1.00 2681 134 0.2889 0.3406 REMARK 3 27 1.9241 - 1.9001 1.00 2694 111 0.2973 0.3146 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) : 0.200 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.370 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.90 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 : 0.010 3863 REMARK 3 ANGLE : 0.811 5186 REMARK 3 CHIRALITY : 0.050 585 REMARK 3 PLANARITY : 0.005 622 REMARK 3 DIHEDRAL : 15.865 2142 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): -11.3183 -4.7035 7.1391 REMARK 3 T TENSOR REMARK 3 T11: 0.1752 T22: 0.2006 REMARK 3 T33: 0.0878 T12: -0.0150 REMARK 3 T13: -0.0119 T23: -0.0098 REMARK 3 L TENSOR REMARK 3 L11: 1.5243 L22: 7.6265 REMARK 3 L33: 3.2997 L12: -0.1157 REMARK 3 L13: 0.0662 L23: -2.3118 REMARK 3 S TENSOR REMARK 3 S11: 0.1092 S12: -0.0257 S13: -0.0073 REMARK 3 S21: -0.3030 S22: -0.0574 S23: 0.4231 REMARK 3 S31: -0.0378 S32: -0.1848 S33: -0.0187 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' (RESID 35 THROUGH 38) REMARK 3 ORIGIN FOR THE GROUP (A): -10.8679 -30.0406 15.1594 REMARK 3 T TENSOR REMARK 3 T11: 0.6412 T22: 0.2759 REMARK 3 T33: 0.4597 T12: -0.1529 REMARK 3 T13: -0.0705 T23: 0.0777 REMARK 3 L TENSOR REMARK 3 L11: 9.0153 L22: 1.9846 REMARK 3 L33: 0.0853 L12: 4.2168 REMARK 3 L13: 0.6399 L23: 0.3209 REMARK 3 S TENSOR REMARK 3 S11: 0.0050 S12: -0.0696 S13: -1.4862 REMARK 3 S21: -0.1191 S22: 0.1439 S23: 0.5503 REMARK 3 S31: 1.2678 S32: -0.5444 S33: -0.0690 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' (RESID 39 THROUGH 73) REMARK 3 ORIGIN FOR THE GROUP (A): -10.1990 -4.3202 17.1719 REMARK 3 T TENSOR REMARK 3 T11: 0.1085 T22: 0.1723 REMARK 3 T33: 0.0572 T12: -0.0211 REMARK 3 T13: 0.0153 T23: 0.0100 REMARK 3 L TENSOR REMARK 3 L11: 1.7059 L22: 7.4395 REMARK 3 L33: 1.1803 L12: -1.2635 REMARK 3 L13: 0.5427 L23: -0.0226 REMARK 3 S TENSOR REMARK 3 S11: 0.0646 S12: -0.0525 S13: -0.0584 REMARK 3 S21: -0.0428 S22: -0.0406 S23: 0.1778 REMARK 3 S31: 0.0912 S32: -0.1787 S33: -0.0399 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' (RESID 74 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): -2.4406 -9.3621 24.0002 REMARK 3 T TENSOR REMARK 3 T11: 0.1447 T22: 0.1825 REMARK 3 T33: 0.0748 T12: -0.0175 REMARK 3 T13: -0.0210 T23: 0.0108 REMARK 3 L TENSOR REMARK 3 L11: 3.3533 L22: 7.9338 REMARK 3 L33: 0.9210 L12: -4.0424 REMARK 3 L13: -0.2119 L23: 0.7885 REMARK 3 S TENSOR REMARK 3 S11: -0.0662 S12: -0.1164 S13: -0.0410 REMARK 3 S21: 0.1958 S22: 0.0531 S23: -0.0753 REMARK 3 S31: 0.1594 S32: -0.0788 S33: 0.0230 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' (RESID 109 THROUGH 117) REMARK 3 ORIGIN FOR THE GROUP (A): 0.1727 -32.2049 28.6610 REMARK 3 T TENSOR REMARK 3 T11: 0.7043 T22: 0.4119 REMARK 3 T33: 0.5135 T12: -0.0402 REMARK 3 T13: 0.0359 T23: 0.1473 REMARK 3 L TENSOR REMARK 3 L11: 4.9340 L22: 9.5216 REMARK 3 L33: 4.0907 L12: -5.6801 REMARK 3 L13: -0.8874 L23: 4.0410 REMARK 3 S TENSOR REMARK 3 S11: -0.6799 S12: -1.0615 S13: -1.4159 REMARK 3 S21: 1.2183 S22: 0.1455 S23: 0.2858 REMARK 3 S31: 0.9062 S32: 0.6784 S33: 0.6861 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' (RESID 118 THROUGH 137) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5946 -12.3535 29.6952 REMARK 3 T TENSOR REMARK 3 T11: 0.2388 T22: 0.2142 REMARK 3 T33: 0.1066 T12: -0.0365 REMARK 3 T13: -0.0004 T23: 0.0286 REMARK 3 L TENSOR REMARK 3 L11: 2.3886 L22: 7.7017 REMARK 3 L33: 2.2768 L12: 1.3334 REMARK 3 L13: -0.5336 L23: -2.1276 REMARK 3 S TENSOR REMARK 3 S11: 0.0693 S12: -0.1589 S13: -0.2361 REMARK 3 S21: 0.3158 S22: -0.1101 S23: 0.0481 REMARK 3 S31: 0.5035 S32: -0.2082 S33: 0.0619 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' (RESID 138 THROUGH 161) REMARK 3 ORIGIN FOR THE GROUP (A): -7.9737 16.7132 27.1974 REMARK 3 T TENSOR REMARK 3 T11: 0.2853 T22: 0.2150 REMARK 3 T33: 0.2596 T12: 0.0527 REMARK 3 T13: -0.0318 T23: -0.0335 REMARK 3 L TENSOR REMARK 3 L11: 3.0385 L22: 2.1817 REMARK 3 L33: 4.8470 L12: -1.8265 REMARK 3 L13: 1.8637 L23: -2.9872 REMARK 3 S TENSOR REMARK 3 S11: -0.1050 S12: -0.1429 S13: 0.6013 REMARK 3 S21: 0.2489 S22: -0.0686 S23: -0.0445 REMARK 3 S31: -0.7239 S32: -0.0897 S33: 0.0939 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' (RESID 162 THROUGH 186) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4129 7.6086 25.1851 REMARK 3 T TENSOR REMARK 3 T11: 0.1123 T22: 0.1524 REMARK 3 T33: 0.0881 T12: -0.0098 REMARK 3 T13: 0.0097 T23: 0.0059 REMARK 3 L TENSOR REMARK 3 L11: 4.5110 L22: 7.3394 REMARK 3 L33: 2.7479 L12: -3.9268 REMARK 3 L13: 1.1790 L23: -1.4618 REMARK 3 S TENSOR REMARK 3 S11: 0.0111 S12: 0.0065 S13: 0.2342 REMARK 3 S21: 0.0412 S22: -0.1046 S23: -0.1238 REMARK 3 S31: -0.1691 S32: 0.0223 S33: 0.0671 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' (RESID 187 THROUGH 208) REMARK 3 ORIGIN FOR THE GROUP (A): 12.6758 -20.6022 21.6939 REMARK 3 T TENSOR REMARK 3 T11: 0.1983 T22: 0.1889 REMARK 3 T33: 0.2904 T12: 0.0368 REMARK 3 T13: -0.0418 T23: 0.0095 REMARK 3 L TENSOR REMARK 3 L11: 2.9899 L22: 1.5391 REMARK 3 L33: 2.6850 L12: -1.5878 REMARK 3 L13: -1.4641 L23: 1.9497 REMARK 3 S TENSOR REMARK 3 S11: -0.0856 S12: -0.1488 S13: -0.4136 REMARK 3 S21: 0.2869 S22: 0.2162 S23: -0.3241 REMARK 3 S31: 0.4088 S32: 0.1867 S33: -0.2004 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' (RESID 219 THROUGH 259) REMARK 3 ORIGIN FOR THE GROUP (A): 7.3215 -13.3990 14.9511 REMARK 3 T TENSOR REMARK 3 T11: 0.1716 T22: 0.1704 REMARK 3 T33: 0.1813 T12: 0.0553 REMARK 3 T13: 0.0160 T23: 0.0210 REMARK 3 L TENSOR REMARK 3 L11: 0.9278 L22: 6.8001 REMARK 3 L33: 1.3902 L12: -0.0193 REMARK 3 L13: 0.3629 L23: 0.4229 REMARK 3 S TENSOR REMARK 3 S11: 0.0732 S12: 0.0257 S13: -0.2870 REMARK 3 S21: -0.3578 S22: 0.0301 S23: -0.2997 REMARK 3 S31: 0.3017 S32: 0.1776 S33: -0.0720 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' (RESID 260 THROUGH 265) REMARK 3 ORIGIN FOR THE GROUP (A): 11.1494 16.3050 16.4813 REMARK 3 T TENSOR REMARK 3 T11: 0.2586 T22: 0.3104 REMARK 3 T33: 0.2606 T12: -0.0576 REMARK 3 T13: 0.0373 T23: 0.0662 REMARK 3 L TENSOR REMARK 3 L11: 4.9063 L22: 8.5943 REMARK 3 L33: 3.0717 L12: -2.3551 REMARK 3 L13: 3.0745 L23: 1.4473 REMARK 3 S TENSOR REMARK 3 S11: -0.5208 S12: 0.4944 S13: 0.6104 REMARK 3 S21: -0.2161 S22: 0.3497 S23: -0.3791 REMARK 3 S31: -0.6312 S32: 0.9301 S33: 0.1294 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' (RESID 266 THROUGH 292) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6061 -4.6234 8.3494 REMARK 3 T TENSOR REMARK 3 T11: 0.1615 T22: 0.1882 REMARK 3 T33: 0.0804 T12: 0.0102 REMARK 3 T13: 0.0094 T23: 0.0104 REMARK 3 L TENSOR REMARK 3 L11: 1.6096 L22: 7.3567 REMARK 3 L33: 1.5022 L12: 2.1576 REMARK 3 L13: 0.5490 L23: -0.2604 REMARK 3 S TENSOR REMARK 3 S11: -0.0363 S12: 0.1205 S13: 0.0140 REMARK 3 S21: -0.3824 S22: 0.0108 S23: 0.1675 REMARK 3 S31: 0.1123 S32: 0.0729 S33: -0.0068 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' (RESID 293 THROUGH 307) REMARK 3 ORIGIN FOR THE GROUP (A): -11.3090 -25.0313 3.2120 REMARK 3 T TENSOR REMARK 3 T11: 0.6845 T22: 0.3298 REMARK 3 T33: 0.3122 T12: -0.1421 REMARK 3 T13: -0.0366 T23: -0.0509 REMARK 3 L TENSOR REMARK 3 L11: 7.2731 L22: 7.4271 REMARK 3 L33: 7.3775 L12: 0.2531 REMARK 3 L13: 2.9099 L23: 0.6655 REMARK 3 S TENSOR REMARK 3 S11: -0.0361 S12: 0.7820 S13: -0.6891 REMARK 3 S21: -1.2175 S22: 0.3181 S23: 0.3992 REMARK 3 S31: 0.6950 S32: -0.3446 S33: -0.3242 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' (RESID 1001 THROUGH 1021) REMARK 3 ORIGIN FOR THE GROUP (A): 25.4454 -49.1566 16.6910 REMARK 3 T TENSOR REMARK 3 T11: 0.4857 T22: 0.3804 REMARK 3 T33: 1.0790 T12: 0.1246 REMARK 3 T13: 0.1498 T23: 0.0902 REMARK 3 L TENSOR REMARK 3 L11: 6.0261 L22: 9.2389 REMARK 3 L33: 5.6785 L12: -6.7586 REMARK 3 L13: 0.3780 L23: 2.6259 REMARK 3 S TENSOR REMARK 3 S11: -0.0836 S12: -0.0308 S13: 0.6351 REMARK 3 S21: -1.0692 S22: -0.3671 S23: -1.0822 REMARK 3 S31: -0.0366 S32: 0.0729 S33: 0.4381 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' (RESID 1022 THROUGH 1042) REMARK 3 ORIGIN FOR THE GROUP (A): 23.6603 -53.1430 25.8393 REMARK 3 T TENSOR REMARK 3 T11: 0.4377 T22: 0.4567 REMARK 3 T33: 0.9384 T12: 0.0234 REMARK 3 T13: -0.1157 T23: -0.1490 REMARK 3 L TENSOR REMARK 3 L11: 4.2111 L22: 3.3789 REMARK 3 L33: 8.0352 L12: -3.3254 REMARK 3 L13: -4.1127 L23: 1.5115 REMARK 3 S TENSOR REMARK 3 S11: -0.3866 S12: -1.2920 S13: 1.1900 REMARK 3 S21: 0.1964 S22: 0.0229 S23: -0.8864 REMARK 3 S31: -0.4979 S32: 0.6399 S33: 0.4018 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' (RESID 1059 THROUGH 1081) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1798 -58.5583 23.7831 REMARK 3 T TENSOR REMARK 3 T11: 0.4908 T22: 0.4249 REMARK 3 T33: 0.6736 T12: 0.0419 REMARK 3 T13: 0.0261 T23: 0.1379 REMARK 3 L TENSOR REMARK 3 L11: 3.7448 L22: 6.1922 REMARK 3 L33: 2.5897 L12: -0.9341 REMARK 3 L13: 2.3953 L23: 1.1570 REMARK 3 S TENSOR REMARK 3 S11: -0.2112 S12: -1.2781 S13: 0.0511 REMARK 3 S21: 0.4131 S22: 0.6544 S23: 0.8436 REMARK 3 S31: 0.1650 S32: -0.4437 S33: -0.4715 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' (RESID 1082 THROUGH 1093) REMARK 3 ORIGIN FOR THE GROUP (A): 25.8411 -65.4125 18.7479 REMARK 3 T TENSOR REMARK 3 T11: 0.7484 T22: 0.4208 REMARK 3 T33: 0.8829 T12: 0.2193 REMARK 3 T13: 0.1911 T23: 0.1084 REMARK 3 L TENSOR REMARK 3 L11: 3.4269 L22: 5.5764 REMARK 3 L33: 2.7925 L12: -3.3451 REMARK 3 L13: 2.7183 L23: -3.2335 REMARK 3 S TENSOR REMARK 3 S11: -0.1459 S12: -0.2154 S13: -0.1017 REMARK 3 S21: -0.3496 S22: 0.0522 S23: 0.1485 REMARK 3 S31: 0.6521 S32: 0.3426 S33: 0.2293 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' (RESID 1094 THROUGH 1101) REMARK 3 ORIGIN FOR THE GROUP (A): 15.0829 -55.5214 12.9657 REMARK 3 T TENSOR REMARK 3 T11: 0.8443 T22: 0.3509 REMARK 3 T33: 0.8277 T12: 0.1671 REMARK 3 T13: -0.0696 T23: 0.0607 REMARK 3 L TENSOR REMARK 3 L11: 6.3728 L22: 3.7939 REMARK 3 L33: 6.9188 L12: 2.6734 REMARK 3 L13: 3.1321 L23: -0.9242 REMARK 3 S TENSOR REMARK 3 S11: 0.6619 S12: 0.6689 S13: -0.6906 REMARK 3 S21: -1.5815 S22: -0.1070 S23: 0.7227 REMARK 3 S31: 0.9739 S32: 0.2691 S33: -0.4783 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' (RESID 1102 THROUGH 1106) REMARK 3 ORIGIN FOR THE GROUP (A): 11.8705 -46.9974 13.6956 REMARK 3 T TENSOR REMARK 3 T11: 0.8238 T22: 0.3593 REMARK 3 T33: 0.5783 T12: 0.2289 REMARK 3 T13: -0.0573 T23: -0.0392 REMARK 3 L TENSOR REMARK 3 L11: 6.6958 L22: 9.6403 REMARK 3 L33: 7.8340 L12: 1.4018 REMARK 3 L13: 2.3897 L23: -3.1539 REMARK 3 S TENSOR REMARK 3 S11: 0.0572 S12: 0.1088 S13: -0.6455 REMARK 3 S21: -0.9851 S22: -0.3012 S23: -0.5631 REMARK 3 S31: -0.2014 S32: -0.0531 S33: 0.2094 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 5IU7 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_1000219434. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JUL-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.3-5.4 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 MARCH 1, 2015 REMARK 200 DATA SCALING SOFTWARE : AIMLESS VERSION 0.5.9 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39593 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 33.710 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.40 REMARK 200 R MERGE FOR SHELL (I) : 1.00700 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 2.5.7 REMARK 200 STARTING MODEL: 5IU4 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.LM TRI-SODIUM CITRATE PH 5.3-5.4, REMARK 280 0.05M SODIUM THIOCYANATE, 29-32% PEG400, 2% (V/V) 2,5-HEXANEDIOL, 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 69.91750 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 69.91750 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 19.69200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.01800 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.69200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.01800 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.91750 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.69200 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.01800 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.91750 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.69200 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.01800 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: 10390 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 47.0 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 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 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 HOH A 2514 O HOH A 2643 2.01 REMARK 500 O HOH A 2573 O HOH A 2624 2.06 REMARK 500 OH TYR A 271 O HOH A 2501 2.09 REMARK 500 O HOH A 2616 O HOH A 2633 2.13 REMARK 500 O GLY A 162 O HOH A 2502 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 2626 O HOH A 2629 3555 2.12 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 -53.04 -122.94 REMARK 500 LEU A 58 -53.04 -120.75 REMARK 500 TYR A1101 -59.31 -134.13 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 2411 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 OLB A 2424 REMARK 610 OLB A 2425 REMARK 610 OLB A 2426 REMARK 610 OLB A 2427 REMARK 610 OLB A 2429 REMARK 610 OLB A 2430 REMARK 610 OLC A 2431 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 128.0 REMARK 620 3 HOH A2582 O 100.8 124.9 REMARK 620 4 HOH A2604 O 84.7 114.4 91.2 REMARK 620 5 HOH A2607 O 86.9 70.4 91.3 171.5 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 6DY 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 2409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2414 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2415 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2418 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2419 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 OLB A 2424 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB 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 OLB A 2429 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 2430 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2431 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5IU4 RELATED DB: PDB DBREF 5IU7 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5IU7 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5IU7 A 219 315 UNP P29274 AA2AR_HUMAN 219 315 SEQADV 5IU7 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5IU7 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5IU7 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5IU7 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5IU7 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5IU7 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5IU7 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5IU7 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5IU7 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5IU7 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5IU7 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5IU7 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5IU7 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5IU7 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5IU7 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5IU7 ALA A 316 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ALA A 317 UNP P29274 EXPRESSION TAG SEQADV 5IU7 ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5IU7 HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5IU7 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 6DY A2401 30 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 18 HET OLA A2410 20 HET OLA A2411 15 HET OLA A2412 12 HET OLA A2413 8 HET OLA A2414 15 HET OLA A2415 14 HET OLA A2416 8 HET OLA A2417 19 HET OLA A2418 11 HET OLA A2419 11 HET OLA A2420 11 HET OLA A2421 10 HET OLA A2422 12 HET OLA A2423 8 HET OLB A2424 19 HET OLB A2425 16 HET OLB A2426 22 HET OLB A2427 19 HET OLB A2428 25 HET OLB A2429 20 HET OLB A2430 19 HET OLC A2431 21 HETNAM NA SODIUM ION HETNAM 6DY 2-(FURAN-2-YL)-N~5~-[2-(4-PHENYLPIPERIDIN-1-YL) HETNAM 2 6DY ETHYL][1,2,4]TRIAZOLO[1,5-A][1,3,5]TRIAZINE-5,7- HETNAM 3 6DY DIAMINE 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 6DY C21 H24 N8 O FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 18(C18 H34 O2) FORMUL 26 OLB 7(C21 H40 O4) FORMUL 33 OLC C21 H40 O4 FORMUL 34 HOH *157(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 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 VAL A 307 1 16 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 2.06 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.02 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.05 LINK OD1 ASP A 52 NA NA A2400 1555 1555 2.40 LINK OG SER A 91 NA NA A2400 1555 1555 2.51 LINK NA NA A2400 O HOH A2582 1555 1555 2.48 LINK NA NA A2400 O HOH A2604 1555 1555 2.25 LINK NA NA A2400 O HOH A2607 1555 1555 2.62 SITE 1 AC1 5 ASP A 52 SER A 91 HOH A2582 HOH A2604 SITE 2 AC1 5 HOH A2607 SITE 1 AC2 17 LEU A 85 PHE A 168 GLU A 169 MET A 177 SITE 2 AC2 17 TRP A 246 LEU A 249 HIS A 250 ASN A 253 SITE 3 AC2 17 HIS A 264 ALA A 265 LEU A 267 MET A 270 SITE 4 AC2 17 ILE A 274 HOH A2514 HOH A2554 HOH A2570 SITE 5 AC2 17 HOH A2579 SITE 1 AC3 4 HIS A 75 GLY A 76 CLR A2403 OLA A2421 SITE 1 AC4 8 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC4 8 CLR A2402 CLR A2405 OLB A2430 HOH A2526 SITE 1 AC5 7 LEU A 244 LEU A 247 PRO A 248 CYS A 262 SITE 2 AC5 7 SER A 263 OLB A2426 HOH A2596 SITE 1 AC6 6 PHE A 255 PHE A 258 CLR A2403 OLB A2426 SITE 2 AC6 6 OLB A2427 HOH A2590 SITE 1 AC7 4 THR A 65 OLA A2411 OLB A2426 OLB A2427 SITE 1 AC8 2 PRO A 266 HOH A2503 SITE 1 AC9 7 GLY A 5 SER A 6 LEU A 267 TYR A 271 SITE 2 AC9 7 LEU A 272 VAL A 275 HOH A2639 SITE 1 AD1 7 ILE A 127 CYS A 185 PRO A 189 LEU A 192 SITE 2 AD1 7 ARG A 199 OLA A2415 OLC A2431 SITE 1 AD2 2 OLA A2406 HOH A2532 SITE 1 AD3 3 LEU A 19 TRP A 29 PHE A 286 SITE 1 AD4 4 ILE A 125 PHE A 133 OLA A2421 OLB A2428 SITE 1 AD5 4 GLY A 123 ILE A 127 VAL A 130 OLA A2410 SITE 1 AD6 2 LEU A 241 LEU A 244 SITE 1 AD7 6 TRP A 29 TRP A 32 VAL A 229 LYS A 233 SITE 2 AD7 6 OLB A2429 HOH A2566 SITE 1 AD8 3 THR A 279 VAL A 283 OLA A2423 SITE 1 AD9 2 SER A 7 OLB A2425 SITE 1 AE1 3 GLY A 195 LEU A 198 ARG A 199 SITE 1 AE2 5 MET A 140 LEU A 141 CLR A2402 OLA A2414 SITE 2 AE2 5 OLC A2431 SITE 1 AE3 4 LEU A 187 LEU A 194 LEU A 198 ALA A 236 SITE 1 AE4 2 ILE A 287 OLA A2418 SITE 1 AE5 4 TYR A 179 PHE A 257 OLB A2430 HOH A2531 SITE 1 AE6 4 SER A 6 SER A 67 THR A 68 OLA A2419 SITE 1 AE7 6 PHE A 255 CYS A 262 CLR A2404 CLR A2405 SITE 2 AE7 6 OLA A2406 OLB A2427 SITE 1 AE8 9 PRO A 61 THR A 65 PHE A 70 CYS A 71 SITE 2 AE8 9 GLN A 163 ASP A 261 CLR A2405 OLA A2406 SITE 3 AE8 9 OLB A2426 SITE 1 AE9 5 TYR A 43 LEU A 58 GLY A 118 TRP A 129 SITE 2 AE9 5 OLA A2414 SITE 1 AF1 7 CYS A 28 GLN A 38 TYR A 43 VAL A 46 SITE 2 AF1 7 ALA A 50 ARG A 205 OLA A2417 SITE 1 AF2 6 PHE A 258 CLR A2403 OLB A2424 HOH A2526 SITE 2 AF2 6 HOH A2590 HOH A2595 SITE 1 AF3 12 HIS A 75 ALA A 134 MET A 140 LEU A 141 SITE 2 AF3 12 GLY A 142 ASN A 144 TYR A 179 ALA A 184 SITE 3 AF3 12 OLA A2410 OLA A2421 HOH A2531 HOH A2603 CRYST1 39.384 180.036 139.835 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 0.025391 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005554 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007151 0.00000 ATOM 1 N ASP A -3 -4.733 26.850 4.021 1.00 89.77 N ATOM 2 CA ASP A -3 -3.552 27.645 3.703 1.00 90.16 C ATOM 3 C ASP A -3 -2.839 27.113 2.468 1.00 88.27 C ATOM 4 O ASP A -3 -3.475 26.675 1.511 1.00 87.74 O ATOM 5 CB ASP A -3 -2.586 27.669 4.890 1.00 91.88 C ATOM 6 CG ASP A -3 -2.694 28.940 5.699 1.00 93.87 C ATOM 7 OD1 ASP A -3 -2.778 30.026 5.085 1.00 94.62 O ATOM 8 OD2 ASP A -3 -2.700 28.854 6.946 1.00 94.45 O ATOM 9 N ASP A -2 -1.504 27.160 2.508 1.00 86.24 N ATOM 10 CA ASP A -2 -0.665 26.632 1.439 1.00 81.35 C ATOM 11 C ASP A -2 -0.743 25.114 1.332 1.00 73.57 C ATOM 12 O ASP A -2 -0.244 24.549 0.351 1.00 73.63 O ATOM 13 CB ASP A -2 0.785 27.077 1.661 1.00 83.84 C ATOM 14 CG ASP A -2 1.614 27.047 0.388 1.00 87.09 C ATOM 15 OD1 ASP A -2 1.033 26.874 -0.701 1.00 90.23 O ATOM 16 OD2 ASP A -2 2.850 27.214 0.474 1.00 87.21 O ATOM 17 N GLY A -1 -1.347 24.445 2.310 1.00111.38 N ANISOU 17 N GLY A -1 17276 11099 13943 -1470 -149 1023 N ATOM 18 CA GLY A -1 -1.541 23.014 2.238 1.00 98.24 C ANISOU 18 CA GLY A -1 15405 9686 12234 -1376 -74 1009 C ATOM 19 C GLY A -1 -2.854 22.652 1.567 1.00 85.32 C ANISOU 19 C GLY A -1 13896 8130 10390 -1043 47 931 C ATOM 20 O GLY A -1 -3.829 23.398 1.619 1.00 84.20 O ANISOU 20 O GLY A -1 14008 7857 10128 -863 26 823 O ATOM 21 N ALA A 0 -2.859 21.484 0.928 1.00 75.90 N ANISOU 21 N ALA A 0 12510 7155 9174 -955 167 998 N ATOM 22 CA ALA A 0 -4.046 20.989 0.251 1.00 68.51 C ANISOU 22 CA ALA A 0 11656 6316 8057 -655 235 940 C ATOM 23 C ALA A 0 -5.215 20.870 1.231 1.00 62.27 C ANISOU 23 C ALA A 0 10999 5495 7165 -495 137 732 C ATOM 24 O ALA A 0 -5.005 20.731 2.441 1.00 62.41 O ANISOU 24 O ALA A 0 11021 5486 7205 -622 49 620 O ATOM 25 CB ALA A 0 -3.758 19.630 -0.379 1.00 67.55 C ANISOU 25 CB ALA A 0 11317 6436 7912 -616 353 1018 C ATOM 26 N PRO A 1 -6.453 20.931 0.737 1.00 55.47 N ANISOU 26 N PRO A 1 10236 4633 6207 -209 149 690 N ATOM 27 CA PRO A 1 -7.626 20.738 1.617 1.00 50.49 C ANISOU 27 CA PRO A 1 9663 3982 5538 -11 112 527 C ATOM 28 C PRO A 1 -7.498 19.456 2.418 1.00 44.52 C ANISOU 28 C PRO A 1 8757 3383 4775 -75 105 449 C ATOM 29 O PRO A 1 -7.205 18.389 1.857 1.00 42.67 O ANISOU 29 O PRO A 1 8292 3388 4534 -96 129 508 O ATOM 30 CB PRO A 1 -8.801 20.662 0.631 1.00 50.41 C ANISOU 30 CB PRO A 1 9643 4018 5494 285 104 576 C ATOM 31 CG PRO A 1 -8.334 21.427 -0.571 1.00 50.33 C ANISOU 31 CG PRO A 1 9715 3946 5462 239 117 721 C ATOM 32 CD PRO A 1 -6.842 21.240 -0.654 1.00 52.06 C ANISOU 32 CD PRO A 1 9855 4209 5718 -52 187 805 C ATOM 33 N PRO A 2 -7.693 19.521 3.738 1.00 41.77 N ANISOU 33 N PRO A 2 8480 2974 4415 -103 81 290 N ATOM 34 CA PRO A 2 -7.476 18.324 4.570 1.00 34.29 C ANISOU 34 CA PRO A 2 7316 2256 3458 -188 62 200 C ATOM 35 C PRO A 2 -8.341 17.136 4.181 1.00 30.69 C ANISOU 35 C PRO A 2 6590 2070 2999 19 107 182 C ATOM 36 O PRO A 2 -7.931 15.988 4.397 1.00 31.91 O ANISOU 36 O PRO A 2 6522 2444 3157 -73 95 171 O ATOM 37 CB PRO A 2 -7.804 18.823 5.987 1.00 38.94 C ANISOU 37 CB PRO A 2 8159 2662 3976 -189 53 30 C ATOM 38 CG PRO A 2 -7.627 20.311 5.921 1.00 43.67 C ANISOU 38 CG PRO A 2 9006 3021 4566 -226 28 47 C ATOM 39 CD PRO A 2 -8.064 20.700 4.542 1.00 45.23 C ANISOU 39 CD PRO A 2 9162 3201 4822 -57 81 178 C ATOM 40 N ILE A 3 -9.523 17.364 3.609 1.00 33.11 N ANISOU 40 N ILE A 3 6905 2353 3322 287 133 195 N ATOM 41 CA ILE A 3 -10.376 16.237 3.252 1.00 34.46 C ANISOU 41 CA ILE A 3 6817 2756 3522 448 119 194 C ATOM 42 C ILE A 3 -9.758 15.354 2.164 1.00 34.15 C ANISOU 42 C ILE A 3 6647 2894 3434 360 74 297 C ATOM 43 O ILE A 3 -10.163 14.196 2.012 1.00 33.43 O ANISOU 43 O ILE A 3 6357 3001 3342 413 41 278 O ATOM 44 CB ILE A 3 -11.764 16.724 2.799 1.00 40.11 C ANISOU 44 CB ILE A 3 7536 3384 4319 740 102 231 C ATOM 45 CG1 ILE A 3 -12.772 15.573 2.825 1.00 44.18 C ANISOU 45 CG1 ILE A 3 7753 4110 4923 880 66 217 C ATOM 46 CG2 ILE A 3 -11.680 17.260 1.395 1.00 42.47 C ANISOU 46 CG2 ILE A 3 7956 3599 4581 779 10 381 C ATOM 47 CD1 ILE A 3 -14.118 15.917 2.235 1.00 48.71 C ANISOU 47 CD1 ILE A 3 8243 4619 5647 1148 -12 309 C ATOM 48 N MET A 4 -8.794 15.854 1.386 1.00 32.99 N ANISOU 48 N MET A 4 6628 2661 3246 232 96 415 N ATOM 49 CA MET A 4 -8.247 15.016 0.319 1.00 31.26 C ANISOU 49 CA MET A 4 6342 2579 2955 192 123 519 C ATOM 50 C MET A 4 -7.360 13.908 0.883 1.00 30.59 C ANISOU 50 C MET A 4 6043 2676 2903 30 179 489 C ATOM 51 O MET A 4 -7.584 12.723 0.604 1.00 25.69 O ANISOU 51 O MET A 4 5290 2231 2239 87 174 468 O ATOM 52 CB MET A 4 -7.491 15.875 -0.689 1.00 31.79 C ANISOU 52 CB MET A 4 6616 2485 2976 124 197 681 C ATOM 53 CG MET A 4 -8.391 16.866 -1.404 1.00 30.76 C ANISOU 53 CG MET A 4 6712 2179 2796 304 119 733 C ATOM 54 SD MET A 4 -7.542 17.871 -2.623 1.00 36.21 S ANISOU 54 SD MET A 4 7535 2770 3455 218 216 869 S ATOM 55 CE MET A 4 -7.086 16.621 -3.850 1.00 34.99 C ANISOU 55 CE MET A 4 7313 2815 3166 229 307 926 C ATOM 56 N GLY A 5 -6.352 14.270 1.691 1.00 25.98 N ANISOU 56 N GLY A 5 5431 2033 2407 -180 204 497 N ATOM 57 CA GLY A 5 -5.551 13.248 2.340 1.00 24.80 C ANISOU 57 CA GLY A 5 5057 2043 2323 -325 216 486 C ATOM 58 C GLY A 5 -6.373 12.409 3.297 1.00 26.32 C ANISOU 58 C GLY A 5 5141 2371 2489 -244 150 327 C ATOM 59 O GLY A 5 -6.168 11.192 3.416 1.00 23.37 O ANISOU 59 O GLY A 5 4581 2176 2121 -258 164 316 O ATOM 60 N ASER A 6 -7.310 13.049 4.002 0.53 26.72 N ANISOU 60 N ASER A 6 5317 2319 2515 -147 108 213 N ATOM 61 N BSER A 6 -7.324 13.039 3.990 0.47 26.74 N ANISOU 61 N BSER A 6 5319 2323 2517 -144 108 213 N ATOM 62 CA ASER A 6 -8.210 12.318 4.884 0.53 26.12 C ANISOU 62 CA ASER A 6 5148 2351 2425 -45 103 86 C ATOM 63 CA BSER A 6 -8.200 12.291 4.884 0.47 26.06 C ANISOU 63 CA BSER A 6 5136 2348 2418 -46 103 86 C ATOM 64 C ASER A 6 -8.965 11.231 4.129 0.53 25.38 C ANISOU 64 C ASER A 6 4876 2435 2332 102 97 101 C ATOM 65 C BSER A 6 -8.982 11.224 4.132 0.47 25.34 C ANISOU 65 C BSER A 6 4869 2432 2327 104 97 100 C ATOM 66 O ASER A 6 -9.075 10.101 4.612 0.53 24.42 O ANISOU 66 O ASER A 6 4589 2471 2217 87 96 53 O ATOM 67 O BSER A 6 -9.134 10.102 4.623 0.47 24.44 O ANISOU 67 O BSER A 6 4591 2474 2222 94 96 50 O ATOM 68 CB ASER A 6 -9.184 13.295 5.546 0.53 27.90 C ANISOU 68 CB ASER A 6 5557 2400 2642 95 136 -4 C ATOM 69 CB BSER A 6 -9.147 13.249 5.604 0.47 27.87 C ANISOU 69 CB BSER A 6 5549 2404 2637 86 135 -8 C ATOM 70 OG ASER A 6 -10.172 12.601 6.280 0.53 29.73 O ANISOU 70 OG ASER A 6 5678 2730 2889 230 193 -93 O ATOM 71 OG BSER A 6 -8.416 14.087 6.473 0.47 27.77 O ANISOU 71 OG BSER A 6 5761 2208 2583 -81 108 -51 O ATOM 72 N SER A 7 -9.476 11.550 2.930 1.00 24.60 N ANISOU 72 N SER A 7 4838 2292 2215 230 65 176 N ATOM 73 CA SER A 7 -10.244 10.570 2.159 1.00 24.77 C ANISOU 73 CA SER A 7 4750 2440 2222 346 -12 195 C ATOM 74 C SER A 7 -9.399 9.357 1.799 1.00 21.53 C ANISOU 74 C SER A 7 4260 2173 1747 242 18 218 C ATOM 75 O SER A 7 -9.902 8.228 1.797 1.00 20.98 O ANISOU 75 O SER A 7 4065 2228 1678 278 -38 180 O ATOM 76 CB SER A 7 -10.807 11.205 0.883 1.00 27.73 C ANISOU 76 CB SER A 7 5278 2705 2552 476 -106 290 C ATOM 77 OG SER A 7 -11.772 12.190 1.214 1.00 32.25 O ANISOU 77 OG SER A 7 5877 3147 3228 620 -136 282 O ATOM 78 N VAL A 8 -8.121 9.569 1.469 1.00 20.50 N ANISOU 78 N VAL A 8 4195 2008 1585 118 120 298 N ATOM 79 CA VAL A 8 -7.244 8.447 1.143 1.00 19.81 C ANISOU 79 CA VAL A 8 4023 2033 1469 52 207 342 C ATOM 80 C VAL A 8 -7.020 7.586 2.379 1.00 22.83 C ANISOU 80 C VAL A 8 4195 2542 1937 -35 196 265 C ATOM 81 O VAL A 8 -7.175 6.360 2.342 1.00 20.49 O ANISOU 81 O VAL A 8 3803 2363 1618 -5 190 234 O ATOM 82 CB VAL A 8 -5.910 8.945 0.559 1.00 21.03 C ANISOU 82 CB VAL A 8 4241 2107 1641 -49 366 488 C ATOM 83 CG1 VAL A 8 -4.926 7.770 0.377 1.00 20.72 C ANISOU 83 CG1 VAL A 8 4070 2173 1630 -91 512 555 C ATOM 84 CG2 VAL A 8 -6.132 9.699 -0.772 1.00 22.65 C ANISOU 84 CG2 VAL A 8 4713 2178 1716 47 402 581 C ATOM 85 N TYR A 9 -6.634 8.221 3.489 1.00 21.48 N ANISOU 85 N TYR A 9 3995 2322 1843 -151 177 236 N ATOM 86 CA TYR A 9 -6.423 7.500 4.738 1.00 17.74 C ANISOU 86 CA TYR A 9 3385 1941 1415 -241 138 170 C ATOM 87 C TYR A 9 -7.660 6.687 5.134 1.00 17.35 C ANISOU 87 C TYR A 9 3271 1989 1333 -119 106 64 C ATOM 88 O TYR A 9 -7.565 5.491 5.426 1.00 18.94 O ANISOU 88 O TYR A 9 3341 2313 1541 -138 105 48 O ATOM 89 CB TYR A 9 -6.039 8.505 5.837 1.00 20.53 C ANISOU 89 CB TYR A 9 3839 2168 1795 -377 75 139 C ATOM 90 CG TYR A 9 -6.090 7.892 7.221 1.00 22.17 C ANISOU 90 CG TYR A 9 4009 2434 1982 -446 12 52 C ATOM 91 CD1 TYR A 9 -5.204 6.874 7.588 1.00 20.60 C ANISOU 91 CD1 TYR A 9 3638 2347 1842 -560 -28 109 C ATOM 92 CD2 TYR A 9 -7.031 8.318 8.153 1.00 22.48 C ANISOU 92 CD2 TYR A 9 4204 2400 1939 -377 16 -73 C ATOM 93 CE1 TYR A 9 -5.261 6.293 8.856 1.00 20.31 C ANISOU 93 CE1 TYR A 9 3608 2351 1759 -623 -104 42 C ATOM 94 CE2 TYR A 9 -7.087 7.761 9.421 1.00 23.87 C ANISOU 94 CE2 TYR A 9 4412 2608 2050 -433 -13 -145 C ATOM 95 CZ TYR A 9 -6.206 6.743 9.763 1.00 23.38 C ANISOU 95 CZ TYR A 9 4199 2662 2024 -565 -94 -89 C ATOM 96 OH TYR A 9 -6.273 6.190 11.019 1.00 23.95 O ANISOU 96 OH TYR A 9 4343 2752 2006 -622 -140 -149 O ATOM 97 N ILE A 10 -8.836 7.321 5.127 1.00 18.22 N ANISOU 97 N ILE A 10 3452 2032 1438 11 87 12 N ATOM 98 CA ILE A 10 -10.072 6.654 5.546 1.00 19.94 C ANISOU 98 CA ILE A 10 3556 2324 1695 123 76 -51 C ATOM 99 C ILE A 10 -10.412 5.501 4.611 1.00 19.64 C ANISOU 99 C ILE A 10 3415 2392 1656 167 5 -18 C ATOM 100 O ILE A 10 -10.836 4.429 5.053 1.00 20.66 O ANISOU 100 O ILE A 10 3406 2621 1821 162 -8 -49 O ATOM 101 CB ILE A 10 -11.227 7.677 5.621 1.00 21.06 C ANISOU 101 CB ILE A 10 3757 2348 1897 279 93 -67 C ATOM 102 CG1 ILE A 10 -10.992 8.671 6.774 1.00 22.63 C ANISOU 102 CG1 ILE A 10 4128 2411 2060 246 185 -133 C ATOM 103 CG2 ILE A 10 -12.586 6.962 5.753 1.00 19.70 C ANISOU 103 CG2 ILE A 10 3389 2251 1846 408 81 -70 C ATOM 104 CD1 ILE A 10 -11.982 9.847 6.809 1.00 23.19 C ANISOU 104 CD1 ILE A 10 4307 2315 2190 428 253 -141 C ATOM 105 N THR A 11 -10.243 5.698 3.304 1.00 16.78 N ANISOU 105 N THR A 11 3162 1984 1230 203 -43 49 N ATOM 106 CA THR A 11 -10.559 4.627 2.362 1.00 16.71 C ANISOU 106 CA THR A 11 3158 2027 1165 238 -137 69 C ATOM 107 C THR A 11 -9.667 3.413 2.592 1.00 18.71 C ANISOU 107 C THR A 11 3353 2375 1382 151 -59 58 C ATOM 108 O THR A 11 -10.135 2.264 2.558 1.00 16.72 O ANISOU 108 O THR A 11 3036 2184 1132 156 -129 28 O ATOM 109 CB THR A 11 -10.407 5.149 0.927 1.00 17.96 C ANISOU 109 CB THR A 11 3549 2081 1195 293 -182 145 C ATOM 110 OG1 THR A 11 -11.325 6.235 0.726 1.00 20.29 O ANISOU 110 OG1 THR A 11 3884 2279 1546 390 -285 171 O ATOM 111 CG2 THR A 11 -10.696 4.039 -0.102 1.00 18.45 C ANISOU 111 CG2 THR A 11 3728 2150 1132 321 -302 154 C ATOM 112 N VAL A 12 -8.370 3.652 2.811 1.00 18.97 N ANISOU 112 N VAL A 12 3394 2403 1412 67 74 101 N ATOM 113 CA VAL A 12 -7.439 2.554 3.063 1.00 16.90 C ANISOU 113 CA VAL A 12 3041 2217 1164 5 158 123 C ATOM 114 C VAL A 12 -7.809 1.844 4.359 1.00 16.20 C ANISOU 114 C VAL A 12 2788 2220 1146 -45 108 52 C ATOM 115 O VAL A 12 -7.831 0.607 4.420 1.00 15.59 O ANISOU 115 O VAL A 12 2651 2206 1065 -43 103 38 O ATOM 116 CB VAL A 12 -5.988 3.085 3.091 1.00 19.57 C ANISOU 116 CB VAL A 12 3352 2519 1565 -82 291 230 C ATOM 117 CG1 VAL A 12 -5.004 2.006 3.630 1.00 20.68 C ANISOU 117 CG1 VAL A 12 3322 2737 1797 -144 360 280 C ATOM 118 CG2 VAL A 12 -5.563 3.598 1.693 1.00 19.22 C ANISOU 118 CG2 VAL A 12 3489 2375 1437 -20 410 328 C ATOM 119 N GLU A 13 -8.122 2.614 5.411 1.00 15.54 N ANISOU 119 N GLU A 13 2678 2120 1107 -83 86 8 N ATOM 120 CA GLU A 13 -8.559 2.013 6.676 1.00 15.02 C ANISOU 120 CA GLU A 13 2521 2118 1069 -116 73 -53 C ATOM 121 C GLU A 13 -9.788 1.132 6.484 1.00 16.07 C ANISOU 121 C GLU A 13 2571 2302 1231 -36 33 -87 C ATOM 122 O GLU A 13 -9.860 0.027 7.029 1.00 16.93 O ANISOU 122 O GLU A 13 2593 2481 1358 -72 34 -99 O ATOM 123 CB GLU A 13 -8.863 3.103 7.712 1.00 15.08 C ANISOU 123 CB GLU A 13 2612 2049 1067 -133 91 -105 C ATOM 124 CG GLU A 13 -7.644 3.851 8.246 1.00 15.99 C ANISOU 124 CG GLU A 13 2820 2093 1164 -273 64 -75 C ATOM 125 CD GLU A 13 -6.949 3.090 9.382 1.00 22.39 C ANISOU 125 CD GLU A 13 3591 2955 1962 -399 11 -69 C ATOM 126 OE1 GLU A 13 -6.733 3.691 10.472 1.00 24.69 O ANISOU 126 OE1 GLU A 13 4034 3160 2186 -492 -44 -106 O ATOM 127 OE2 GLU A 13 -6.636 1.887 9.189 1.00 19.83 O ANISOU 127 OE2 GLU A 13 3122 2733 1678 -402 12 -26 O ATOM 128 N LEU A 14 -10.788 1.615 5.745 1.00 16.40 N ANISOU 128 N LEU A 14 2631 2297 1304 61 -27 -83 N ATOM 129 CA LEU A 14 -11.991 0.807 5.539 1.00 18.32 C ANISOU 129 CA LEU A 14 2756 2572 1634 107 -120 -82 C ATOM 130 C LEU A 14 -11.685 -0.474 4.769 1.00 16.75 C ANISOU 130 C LEU A 14 2593 2400 1372 67 -204 -73 C ATOM 131 O LEU A 14 -12.231 -1.534 5.087 1.00 18.34 O ANISOU 131 O LEU A 14 2687 2643 1638 34 -252 -81 O ATOM 132 CB LEU A 14 -13.075 1.625 4.820 1.00 18.84 C ANISOU 132 CB LEU A 14 2813 2564 1783 215 -224 -45 C ATOM 133 CG LEU A 14 -13.626 2.783 5.675 1.00 23.78 C ANISOU 133 CG LEU A 14 3396 3136 2504 297 -103 -52 C ATOM 134 CD1 LEU A 14 -14.579 3.687 4.863 1.00 26.21 C ANISOU 134 CD1 LEU A 14 3688 3350 2919 429 -211 14 C ATOM 135 CD2 LEU A 14 -14.309 2.250 6.932 1.00 24.23 C ANISOU 135 CD2 LEU A 14 3288 3243 2676 304 26 -67 C ATOM 136 N ALA A 15 -10.840 -0.394 3.731 1.00 16.16 N ANISOU 136 N ALA A 15 2696 2278 1166 77 -199 -50 N ATOM 137 CA ALA A 15 -10.400 -1.596 3.023 1.00 15.97 C ANISOU 137 CA ALA A 15 2782 2241 1044 65 -217 -49 C ATOM 138 C ALA A 15 -9.749 -2.598 3.982 1.00 17.96 C ANISOU 138 C ALA A 15 2915 2568 1340 3 -117 -59 C ATOM 139 O ALA A 15 -10.052 -3.798 3.957 1.00 18.30 O ANISOU 139 O ALA A 15 2956 2613 1384 -17 -175 -78 O ATOM 140 CB ALA A 15 -9.415 -1.214 1.910 1.00 14.71 C ANISOU 140 CB ALA A 15 2852 2004 734 111 -118 -3 C ATOM 141 N ILE A 16 -8.842 -2.123 4.827 1.00 14.93 N ANISOU 141 N ILE A 16 2450 2227 997 -39 3 -36 N ATOM 142 CA ILE A 16 -8.210 -3.013 5.801 1.00 15.89 C ANISOU 142 CA ILE A 16 2463 2409 1165 -101 54 -23 C ATOM 143 C ILE A 16 -9.253 -3.627 6.727 1.00 17.08 C ANISOU 143 C ILE A 16 2513 2607 1370 -134 -6 -68 C ATOM 144 O ILE A 16 -9.196 -4.826 7.042 1.00 16.92 O ANISOU 144 O ILE A 16 2456 2609 1365 -161 -11 -64 O ATOM 145 CB ILE A 16 -7.129 -2.252 6.590 1.00 14.77 C ANISOU 145 CB ILE A 16 2263 2281 1068 -170 111 27 C ATOM 146 CG1 ILE A 16 -5.984 -1.887 5.640 1.00 17.13 C ANISOU 146 CG1 ILE A 16 2603 2531 1374 -146 212 119 C ATOM 147 CG2 ILE A 16 -6.629 -3.082 7.810 1.00 13.40 C ANISOU 147 CG2 ILE A 16 1986 2163 941 -247 97 51 C ATOM 148 CD1 ILE A 16 -5.124 -0.820 6.184 1.00 19.22 C ANISOU 148 CD1 ILE A 16 2810 2775 1717 -239 214 184 C ATOM 149 N ALA A 17 -10.221 -2.822 7.176 1.00 16.64 N ANISOU 149 N ALA A 17 2412 2550 1360 -119 -21 -96 N ATOM 150 CA ALA A 17 -11.220 -3.322 8.117 1.00 14.23 C ANISOU 150 CA ALA A 17 1993 2278 1135 -136 -7 -109 C ATOM 151 C ALA A 17 -12.020 -4.470 7.510 1.00 16.60 C ANISOU 151 C ALA A 17 2232 2571 1504 -145 -115 -96 C ATOM 152 O ALA A 17 -12.263 -5.483 8.168 1.00 19.62 O ANISOU 152 O ALA A 17 2542 2980 1933 -199 -97 -83 O ATOM 153 CB ALA A 17 -12.143 -2.183 8.568 1.00 12.96 C ANISOU 153 CB ALA A 17 1796 2089 1038 -74 53 -120 C ATOM 154 N AVAL A 18 -12.446 -4.316 6.254 0.88 16.93 N ANISOU 154 N AVAL A 18 2335 2556 1543 -107 -253 -92 N ATOM 155 N BVAL A 18 -12.414 -4.354 6.240 0.12 17.19 N ANISOU 155 N BVAL A 18 2372 2588 1572 -108 -253 -92 N ATOM 156 CA AVAL A 18 -13.198 -5.371 5.576 0.88 18.47 C ANISOU 156 CA AVAL A 18 2528 2702 1786 -146 -430 -79 C ATOM 157 CA BVAL A 18 -13.241 -5.415 5.667 0.12 18.09 C ANISOU 157 CA BVAL A 18 2464 2659 1749 -150 -425 -78 C ATOM 158 C AVAL A 18 -12.393 -6.666 5.536 0.88 16.95 C ANISOU 158 C AVAL A 18 2448 2493 1498 -192 -406 -99 C ATOM 159 C BVAL A 18 -12.428 -6.689 5.433 0.12 17.04 C ANISOU 159 C BVAL A 18 2471 2497 1506 -191 -421 -99 C ATOM 160 O AVAL A 18 -12.904 -7.754 5.837 0.88 16.37 O ANISOU 160 O AVAL A 18 2313 2404 1501 -262 -470 -88 O ATOM 161 O BVAL A 18 -12.965 -7.799 5.538 0.12 17.19 O ANISOU 161 O BVAL A 18 2456 2485 1590 -261 -512 -91 O ATOM 162 CB AVAL A 18 -13.586 -4.913 4.158 0.88 19.41 C ANISOU 162 CB AVAL A 18 2795 2731 1849 -104 -625 -72 C ATOM 163 CB BVAL A 18 -13.940 -4.935 4.379 0.12 20.10 C ANISOU 163 CB BVAL A 18 2804 2829 2004 -114 -640 -60 C ATOM 164 CG1AVAL A 18 -14.158 -6.081 3.361 0.88 22.36 C ANISOU 164 CG1AVAL A 18 3270 3011 2213 -175 -866 -69 C ATOM 165 CG1BVAL A 18 -14.818 -3.717 4.669 0.12 20.61 C ANISOU 165 CG1BVAL A 18 2693 2907 2229 -48 -634 -15 C ATOM 166 CG2AVAL A 18 -14.604 -3.751 4.241 0.88 21.08 C ANISOU 166 CG2AVAL A 18 2845 2944 2222 -47 -678 -24 C ATOM 167 CG2BVAL A 18 -12.935 -4.634 3.283 0.12 19.67 C ANISOU 167 CG2BVAL A 18 3044 2710 1719 -63 -631 -87 C ATOM 168 N LEU A 19 -11.135 -6.568 5.124 1.00 15.82 N ANISOU 168 N LEU A 19 2463 2336 1213 -145 -301 -109 N ATOM 169 CA LEU A 19 -10.312 -7.761 4.966 1.00 17.00 C ANISOU 169 CA LEU A 19 2727 2443 1291 -143 -244 -109 C ATOM 170 C LEU A 19 -9.996 -8.405 6.313 1.00 17.92 C ANISOU 170 C LEU A 19 2684 2632 1491 -197 -158 -83 C ATOM 171 O LEU A 19 -9.910 -9.632 6.406 1.00 17.81 O ANISOU 171 O LEU A 19 2714 2573 1479 -219 -170 -79 O ATOM 172 CB LEU A 19 -9.022 -7.405 4.241 1.00 15.03 C ANISOU 172 CB LEU A 19 2629 2154 926 -54 -93 -85 C ATOM 173 CG LEU A 19 -9.248 -6.925 2.803 1.00 16.63 C ANISOU 173 CG LEU A 19 3066 2251 1001 8 -152 -102 C ATOM 174 CD1 LEU A 19 -7.938 -6.292 2.284 1.00 18.29 C ANISOU 174 CD1 LEU A 19 3325 2439 1186 90 68 -42 C ATOM 175 CD2 LEU A 19 -9.707 -8.086 1.893 1.00 20.46 C ANISOU 175 CD2 LEU A 19 3755 2592 1427 9 -269 -139 C ATOM 176 N ALA A 20 -9.778 -7.590 7.349 1.00 15.48 N ANISOU 176 N ALA A 20 2246 2410 1227 -217 -81 -65 N ATOM 177 CA ALA A 20 -9.509 -8.132 8.684 1.00 17.00 C ANISOU 177 CA ALA A 20 2351 2655 1455 -275 -27 -33 C ATOM 178 C ALA A 20 -10.714 -8.896 9.212 1.00 20.39 C ANISOU 178 C ALA A 20 2705 3082 1962 -333 -63 -34 C ATOM 179 O ALA A 20 -10.574 -9.975 9.804 1.00 19.09 O ANISOU 179 O ALA A 20 2535 2908 1809 -378 -50 -2 O ATOM 180 CB ALA A 20 -9.155 -7.002 9.651 1.00 15.04 C ANISOU 180 CB ALA A 20 2068 2457 1188 -299 26 -25 C ATOM 181 N ILE A 21 -11.911 -8.345 9.011 1.00 16.62 N ANISOU 181 N ILE A 21 2145 2602 1567 -332 -104 -45 N ATOM 182 CA ILE A 21 -13.115 -9.051 9.424 1.00 18.28 C ANISOU 182 CA ILE A 21 2223 2799 1922 -395 -127 -5 C ATOM 183 C ILE A 21 -13.270 -10.353 8.644 1.00 20.38 C ANISOU 183 C ILE A 21 2555 2978 2209 -454 -283 -3 C ATOM 184 O ILE A 21 -13.426 -11.433 9.227 1.00 22.41 O ANISOU 184 O ILE A 21 2786 3212 2516 -527 -267 34 O ATOM 185 CB ILE A 21 -14.336 -8.132 9.276 1.00 19.66 C ANISOU 185 CB ILE A 21 2244 2978 2249 -362 -140 20 C ATOM 186 CG1 ILE A 21 -14.160 -6.936 10.230 1.00 20.01 C ANISOU 186 CG1 ILE A 21 2293 3068 2241 -293 57 7 C ATOM 187 CG2 ILE A 21 -15.633 -8.903 9.593 1.00 20.92 C ANISOU 187 CG2 ILE A 21 2195 3112 2640 -436 -165 106 C ATOM 188 CD1 ILE A 21 -15.142 -5.812 9.999 1.00 21.11 C ANISOU 188 CD1 ILE A 21 2314 3189 2516 -207 84 30 C ATOM 189 N LEU A 22 -13.204 -10.278 7.312 1.00 18.84 N ANISOU 189 N LEU A 22 2503 2708 1949 -426 -435 -43 N ATOM 190 CA LEU A 22 -13.494 -11.453 6.495 1.00 20.37 C ANISOU 190 CA LEU A 22 2841 2770 2130 -491 -618 -55 C ATOM 191 C LEU A 22 -12.531 -12.596 6.793 1.00 19.73 C ANISOU 191 C LEU A 22 2899 2643 1955 -485 -521 -65 C ATOM 192 O LEU A 22 -12.956 -13.738 6.993 1.00 21.59 O ANISOU 192 O LEU A 22 3148 2798 2256 -577 -597 -43 O ATOM 193 CB LEU A 22 -13.443 -11.093 5.008 1.00 23.88 C ANISOU 193 CB LEU A 22 3524 3112 2436 -444 -782 -104 C ATOM 194 CG LEU A 22 -14.616 -10.273 4.458 1.00 27.50 C ANISOU 194 CG LEU A 22 3876 3558 3014 -471 -994 -72 C ATOM 195 CD1 LEU A 22 -14.378 -9.976 2.982 1.00 30.19 C ANISOU 195 CD1 LEU A 22 4552 3775 3142 -420 -1158 -119 C ATOM 196 CD2 LEU A 22 -15.951 -10.994 4.661 1.00 30.89 C ANISOU 196 CD2 LEU A 22 4105 3936 3695 -619 -1209 3 C ATOM 197 N GLY A 23 -11.226 -12.312 6.823 1.00 18.22 N ANISOU 197 N GLY A 23 2792 2487 1642 -379 -358 -75 N ATOM 198 CA GLY A 23 -10.262 -13.386 6.984 1.00 18.34 C ANISOU 198 CA GLY A 23 2923 2440 1607 -339 -266 -58 C ATOM 199 C GLY A 23 -10.343 -14.023 8.356 1.00 19.71 C ANISOU 199 C GLY A 23 2946 2668 1875 -411 -216 4 C ATOM 200 O GLY A 23 -10.248 -15.248 8.501 1.00 19.99 O ANISOU 200 O GLY A 23 3067 2608 1922 -436 -230 24 O ATOM 201 N ASN A 24 -10.538 -13.211 9.380 1.00 15.55 N ANISOU 201 N ASN A 24 2244 2270 1396 -443 -153 35 N ATOM 202 CA ASN A 24 -10.532 -13.763 10.723 1.00 14.80 C ANISOU 202 CA ASN A 24 2078 2211 1335 -502 -88 101 C ATOM 203 C ASN A 24 -11.857 -14.407 11.087 1.00 18.00 C ANISOU 203 C ASN A 24 2402 2579 1857 -614 -121 132 C ATOM 204 O ASN A 24 -11.871 -15.372 11.853 1.00 19.99 O ANISOU 204 O ASN A 24 2669 2795 2131 -671 -86 193 O ATOM 205 CB ASN A 24 -10.114 -12.672 11.698 1.00 15.27 C ANISOU 205 CB ASN A 24 2076 2380 1345 -490 -2 120 C ATOM 206 CG ASN A 24 -8.618 -12.402 11.600 1.00 17.24 C ANISOU 206 CG ASN A 24 2365 2645 1541 -422 4 147 C ATOM 207 OD1 ASN A 24 -7.810 -13.240 12.018 1.00 18.42 O ANISOU 207 OD1 ASN A 24 2535 2764 1698 -410 0 218 O ATOM 208 ND2 ASN A 24 -8.240 -11.277 10.983 1.00 14.88 N ANISOU 208 ND2 ASN A 24 2056 2376 1223 -374 11 115 N ATOM 209 N VAL A 25 -12.975 -13.925 10.539 1.00 17.09 N ANISOU 209 N VAL A 25 2185 2460 1849 -652 -197 116 N ATOM 210 CA VAL A 25 -14.208 -14.700 10.656 1.00 20.95 C ANISOU 210 CA VAL A 25 2557 2881 2521 -777 -268 180 C ATOM 211 C VAL A 25 -14.013 -16.091 10.059 1.00 20.03 C ANISOU 211 C VAL A 25 2615 2610 2387 -841 -414 169 C ATOM 212 O VAL A 25 -14.457 -17.097 10.625 1.00 20.04 O ANISOU 212 O VAL A 25 2583 2545 2488 -949 -411 241 O ATOM 213 CB VAL A 25 -15.377 -13.947 9.994 1.00 21.20 C ANISOU 213 CB VAL A 25 2418 2915 2721 -803 -385 194 C ATOM 214 CG1 VAL A 25 -16.560 -14.900 9.732 1.00 25.05 C ANISOU 214 CG1 VAL A 25 2781 3289 3446 -964 -564 278 C ATOM 215 CG2 VAL A 25 -15.808 -12.769 10.883 1.00 20.52 C ANISOU 215 CG2 VAL A 25 2147 2947 2701 -736 -174 234 C ATOM 216 N LEU A 26 -13.322 -16.174 8.921 1.00 20.98 N ANISOU 216 N LEU A 26 2960 2647 2363 -768 -514 83 N ATOM 217 CA LEU A 26 -13.043 -17.475 8.316 1.00 21.71 C ANISOU 217 CA LEU A 26 3304 2550 2393 -795 -618 55 C ATOM 218 C LEU A 26 -12.229 -18.360 9.260 1.00 20.79 C ANISOU 218 C LEU A 26 3227 2422 2250 -762 -464 109 C ATOM 219 O LEU A 26 -12.498 -19.561 9.381 1.00 23.15 O ANISOU 219 O LEU A 26 3621 2577 2597 -849 -528 139 O ATOM 220 CB LEU A 26 -12.312 -17.272 6.987 1.00 26.00 C ANISOU 220 CB LEU A 26 4138 2999 2743 -671 -660 -42 C ATOM 221 CG LEU A 26 -12.073 -18.453 6.042 1.00 34.02 C ANISOU 221 CG LEU A 26 5533 3762 3630 -664 -762 -102 C ATOM 222 CD1 LEU A 26 -13.398 -19.091 5.588 1.00 34.90 C ANISOU 222 CD1 LEU A 26 5709 3712 3838 -874 -1083 -106 C ATOM 223 CD2 LEU A 26 -11.213 -18.016 4.839 1.00 35.13 C ANISOU 223 CD2 LEU A 26 5978 3827 3542 -490 -688 -183 C ATOM 224 N VAL A 27 -11.224 -17.790 9.930 1.00 17.91 N ANISOU 224 N VAL A 27 2798 2187 1819 -648 -295 134 N ATOM 225 CA VAL A 27 -10.455 -18.562 10.905 1.00 19.95 C ANISOU 225 CA VAL A 27 3076 2436 2067 -621 -196 214 C ATOM 226 C VAL A 27 -11.384 -19.147 11.967 1.00 22.56 C ANISOU 226 C VAL A 27 3310 2765 2497 -769 -189 297 C ATOM 227 O VAL A 27 -11.319 -20.341 12.287 1.00 24.03 O ANISOU 227 O VAL A 27 3595 2829 2708 -811 -199 353 O ATOM 228 CB VAL A 27 -9.361 -17.686 11.558 1.00 17.59 C ANISOU 228 CB VAL A 27 2689 2281 1712 -521 -90 253 C ATOM 229 CG1 VAL A 27 -8.786 -18.389 12.797 1.00 16.60 C ANISOU 229 CG1 VAL A 27 2564 2156 1589 -530 -51 366 C ATOM 230 CG2 VAL A 27 -8.253 -17.336 10.557 1.00 16.38 C ANISOU 230 CG2 VAL A 27 2611 2103 1510 -366 -47 221 C ATOM 231 N CYS A 28 -12.226 -18.290 12.571 1.00 24.00 N ANISOU 231 N CYS A 28 3309 3070 2741 -834 -131 322 N ATOM 232 CA CYS A 28 -13.110 -18.731 13.649 1.00 22.46 C ANISOU 232 CA CYS A 28 3014 2873 2645 -954 -41 427 C ATOM 233 C CYS A 28 -14.103 -19.769 13.154 1.00 24.64 C ANISOU 233 C CYS A 28 3268 2998 3097 -1102 -165 464 C ATOM 234 O CYS A 28 -14.448 -20.713 13.886 1.00 23.73 O ANISOU 234 O CYS A 28 3158 2805 3053 -1203 -112 568 O ATOM 235 CB CYS A 28 -13.873 -17.541 14.239 1.00 22.82 C ANISOU 235 CB CYS A 28 2884 3050 2737 -956 99 449 C ATOM 236 SG CYS A 28 -12.833 -16.319 15.087 1.00 23.50 S ANISOU 236 SG CYS A 28 3057 3272 2600 -834 223 416 S ATOM 237 N ATRP A 29 -14.599 -19.578 11.928 0.50 23.54 N ANISOU 237 N ATRP A 29 3118 2797 3028 -1134 -355 394 N ATOM 238 N BTRP A 29 -14.609 -19.602 11.929 0.50 23.59 N ANISOU 238 N BTRP A 29 3126 2801 3037 -1136 -357 395 N ATOM 239 CA ATRP A 29 -15.509 -20.526 11.295 0.50 26.56 C ANISOU 239 CA ATRP A 29 3517 2999 3577 -1305 -568 423 C ATOM 240 CA BTRP A 29 -15.535 -20.592 11.386 0.50 26.56 C ANISOU 240 CA BTRP A 29 3509 2996 3585 -1313 -558 433 C ATOM 241 C ATRP A 29 -14.857 -21.899 11.142 0.50 27.04 C ANISOU 241 C ATRP A 29 3866 2866 3542 -1318 -629 406 C ATOM 242 C BTRP A 29 -14.846 -21.937 11.182 0.50 27.06 C ANISOU 242 C BTRP A 29 3870 2866 3544 -1319 -623 410 C ATOM 243 O ATRP A 29 -15.481 -22.929 11.421 0.50 29.41 O ANISOU 243 O ATRP A 29 4169 3024 3983 -1481 -695 491 O ATOM 244 O BTRP A 29 -15.435 -22.990 11.450 0.50 29.35 O ANISOU 244 O BTRP A 29 4173 3010 3969 -1479 -690 493 O ATOM 245 CB ATRP A 29 -15.933 -19.958 9.936 0.50 27.24 C ANISOU 245 CB ATRP A 29 3630 3040 3679 -1316 -813 336 C ATOM 246 CB BTRP A 29 -16.145 -20.099 10.072 0.50 27.75 C ANISOU 246 CB BTRP A 29 3655 3094 3795 -1353 -816 364 C ATOM 247 CG ATRP A 29 -17.179 -20.528 9.344 0.50 30.95 C ANISOU 247 CG ATRP A 29 4022 3351 4385 -1533 -1102 397 C ATOM 248 CG BTRP A 29 -17.464 -19.391 10.231 0.50 29.82 C ANISOU 248 CG BTRP A 29 3556 3436 4340 -1453 -850 468 C ATOM 249 CD1ATRP A 29 -17.819 -21.660 9.724 0.50 34.50 C ANISOU 249 CD1ATRP A 29 4429 3661 5019 -1716 -1171 502 C ATOM 250 CD1BTRP A 29 -17.724 -18.077 9.969 0.50 30.52 C ANISOU 250 CD1BTRP A 29 3482 3656 4457 -1360 -829 448 C ATOM 251 CD2ATRP A 29 -17.938 -19.981 8.255 0.50 35.48 C ANISOU 251 CD2ATRP A 29 4552 3885 5044 -1577 -1380 374 C ATOM 252 CD2BTRP A 29 -18.699 -19.957 10.690 0.50 32.58 C ANISOU 252 CD2BTRP A 29 3634 3721 5024 -1650 -887 635 C ATOM 253 NE1ATRP A 29 -18.929 -21.863 8.943 0.50 37.29 N ANISOU 253 NE1ATRP A 29 4698 3933 5539 -1786 -1421 530 N ATOM 254 NE1BTRP A 29 -19.041 -17.789 10.230 0.50 33.75 N ANISOU 254 NE1BTRP A 29 3529 4088 5207 -1464 -844 594 N ATOM 255 CE2ATRP A 29 -19.025 -20.844 8.033 0.50 36.99 C ANISOU 255 CE2ATRP A 29 4665 3950 5440 -1700 -1559 461 C ATOM 256 CE2BTRP A 29 -19.662 -18.927 10.675 0.50 35.73 C ANISOU 256 CE2BTRP A 29 3708 4232 5634 -1602 -848 700 C ATOM 257 CE3ATRP A 29 -17.800 -18.847 7.445 0.50 36.87 C ANISOU 257 CE3ATRP A 29 4763 4133 5113 -1464 -1460 294 C ATOM 258 CE3BTRP A 29 -19.085 -21.233 11.111 0.50 34.79 C ANISOU 258 CE3BTRP A 29 3936 3871 5410 -1765 -889 715 C ATOM 259 CZ2ATRP A 29 -19.973 -20.613 7.039 0.50 38.84 C ANISOU 259 CZ2ATRP A 29 4855 4124 5779 -1728 -1834 487 C ATOM 260 CZ2BTRP A 29 -20.984 -19.135 11.066 0.50 37.39 C ANISOU 260 CZ2BTRP A 29 3615 4431 6160 -1656 -794 845 C ATOM 261 CZ3ATRP A 29 -18.746 -18.618 6.455 0.50 37.28 C ANISOU 261 CZ3ATRP A 29 4785 4119 5260 -1476 -1712 317 C ATOM 262 CZ3BTRP A 29 -20.396 -21.439 11.493 0.50 38.09 C ANISOU 262 CZ3BTRP A 29 4049 4289 6135 -1839 -847 853 C ATOM 263 CH2ATRP A 29 -19.815 -19.498 6.262 0.50 38.74 C ANISOU 263 CH2ATRP A 29 4893 4173 5652 -1612 -1907 419 C ATOM 264 CH2BTRP A 29 -21.329 -20.394 11.470 0.50 39.45 C ANISOU 264 CH2BTRP A 29 3897 4577 6517 -1782 -794 921 C ATOM 265 N ALA A 30 -13.594 -21.926 10.715 1.00 25.46 N ANISOU 265 N ALA A 30 3902 2644 3128 -1139 -584 315 N ATOM 266 CA ALA A 30 -12.883 -23.187 10.506 1.00 27.10 C ANISOU 266 CA ALA A 30 4401 2645 3249 -1096 -601 302 C ATOM 267 C ALA A 30 -12.724 -23.959 11.812 1.00 27.67 C ANISOU 267 C ALA A 30 4424 2716 3375 -1134 -470 433 C ATOM 268 O ALA A 30 -12.968 -25.172 11.867 1.00 29.20 O ANISOU 268 O ALA A 30 4765 2705 3623 -1233 -539 476 O ATOM 269 CB ALA A 30 -11.514 -22.917 9.873 1.00 24.40 C ANISOU 269 CB ALA A 30 4250 2300 2719 -855 -501 219 C ATOM 270 N VAL A 31 -12.308 -23.274 12.877 1.00 24.61 N ANISOU 270 N VAL A 31 3872 2528 2951 -1064 -299 499 N ATOM 271 CA VAL A 31 -12.119 -23.962 14.148 1.00 24.47 C ANISOU 271 CA VAL A 31 3865 2497 2934 -1095 -190 633 C ATOM 272 C VAL A 31 -13.451 -24.494 14.668 1.00 27.36 C ANISOU 272 C VAL A 31 4124 2801 3472 -1315 -183 736 C ATOM 273 O VAL A 31 -13.529 -25.623 15.167 1.00 29.25 O ANISOU 273 O VAL A 31 4472 2891 3751 -1395 -173 834 O ATOM 274 CB VAL A 31 -11.447 -23.031 15.170 1.00 23.05 C ANISOU 274 CB VAL A 31 3597 2521 2641 -997 -56 679 C ATOM 275 CG1 VAL A 31 -11.317 -23.742 16.524 1.00 23.13 C ANISOU 275 CG1 VAL A 31 3681 2499 2610 -1042 29 829 C ATOM 276 CG2 VAL A 31 -10.089 -22.536 14.636 1.00 24.20 C ANISOU 276 CG2 VAL A 31 3792 2716 2688 -803 -78 617 C ATOM 277 N TRP A 32 -14.512 -23.688 14.563 1.00 29.16 N ANISOU 277 N TRP A 32 4116 3128 3834 -1409 -172 740 N ATOM 278 CA TRP A 32 -15.838 -24.126 14.986 1.00 33.18 C ANISOU 278 CA TRP A 32 4444 3576 4586 -1617 -141 877 C ATOM 279 C TRP A 32 -16.265 -25.393 14.256 1.00 36.42 C ANISOU 279 C TRP A 32 4975 3728 5134 -1784 -374 888 C ATOM 280 O TRP A 32 -16.837 -26.308 14.861 1.00 37.03 O ANISOU 280 O TRP A 32 5021 3701 5349 -1906 -321 1009 O ATOM 281 CB TRP A 32 -16.859 -23.010 14.750 1.00 35.81 C ANISOU 281 CB TRP A 32 4470 4039 5097 -1656 -117 887 C ATOM 282 CG TRP A 32 -18.274 -23.390 15.130 1.00 45.36 C ANISOU 282 CG TRP A 32 5413 5195 6626 -1818 -54 1039 C ATOM 283 CD1 TRP A 32 -19.147 -24.157 14.403 1.00 50.35 C ANISOU 283 CD1 TRP A 32 5973 5679 7480 -1946 -283 1044 C ATOM 284 CD2 TRP A 32 -18.975 -23.011 16.323 1.00 51.17 C ANISOU 284 CD2 TRP A 32 5961 6031 7452 -1785 288 1155 C ATOM 285 NE1 TRP A 32 -20.340 -24.289 15.077 1.00 55.03 N ANISOU 285 NE1 TRP A 32 6295 6289 8323 -2011 -110 1177 N ATOM 286 CE2 TRP A 32 -20.262 -23.594 16.256 1.00 56.48 C ANISOU 286 CE2 TRP A 32 6417 6617 8425 -1907 263 1239 C ATOM 287 CE3 TRP A 32 -18.638 -22.242 17.444 1.00 51.05 C ANISOU 287 CE3 TRP A 32 5992 6150 7253 -1660 611 1187 C ATOM 288 CZ2 TRP A 32 -21.210 -23.430 17.267 1.00 60.73 C ANISOU 288 CZ2 TRP A 32 6769 7213 9094 -1908 578 1362 C ATOM 289 CZ3 TRP A 32 -19.586 -22.079 18.449 1.00 54.67 C ANISOU 289 CZ3 TRP A 32 6330 6642 7802 -1655 922 1280 C ATOM 290 CH2 TRP A 32 -20.855 -22.667 18.350 1.00 59.68 C ANISOU 290 CH2 TRP A 32 6728 7205 8743 -1776 913 1373 C ATOM 291 N LEU A 33 -15.982 -25.472 12.955 1.00 37.33 N ANISOU 291 N LEU A 33 5269 3732 5183 -1753 -616 741 N ATOM 292 CA LEU A 33 -16.514 -26.560 12.146 1.00 41.03 C ANISOU 292 CA LEU A 33 5896 3944 5748 -1899 -875 718 C ATOM 293 C LEU A 33 -15.677 -27.831 12.227 1.00 40.79 C ANISOU 293 C LEU A 33 6222 3695 5580 -1852 -870 703 C ATOM 294 O LEU A 33 -16.234 -28.929 12.178 1.00 43.82 O ANISOU 294 O LEU A 33 6667 3914 6067 -1958 -968 737 O ATOM 295 CB LEU A 33 -16.624 -26.122 10.688 1.00 45.06 C ANISOU 295 CB LEU A 33 6531 4400 6189 -1870 -1137 564 C ATOM 296 CG LEU A 33 -17.734 -25.132 10.339 1.00 49.87 C ANISOU 296 CG LEU A 33 6800 5161 6987 -1924 -1237 590 C ATOM 297 CD1 LEU A 33 -17.701 -24.847 8.845 1.00 53.76 C ANISOU 297 CD1 LEU A 33 7521 5568 7336 -1871 -1513 446 C ATOM 298 CD2 LEU A 33 -19.098 -25.678 10.761 1.00 51.79 C ANISOU 298 CD2 LEU A 33 6750 5384 7543 -2084 -1270 737 C ATOM 299 N ASN A 34 -14.359 -27.715 12.336 1.00 35.22 N ANISOU 299 N ASN A 34 5709 3018 4654 -1630 -733 649 N ATOM 300 CA ASN A 34 -13.457 -28.846 12.140 1.00 36.24 C ANISOU 300 CA ASN A 34 6199 2911 4661 -1519 -731 622 C ATOM 301 C ASN A 34 -12.912 -29.311 13.488 1.00 35.97 C ANISOU 301 C ASN A 34 6122 2926 4619 -1458 -534 774 C ATOM 302 O ASN A 34 -12.125 -28.597 14.126 1.00 33.22 O ANISOU 302 O ASN A 34 5655 2792 4174 -1289 -378 803 O ATOM 303 CB ASN A 34 -12.330 -28.448 11.188 1.00 32.83 C ANISOU 303 CB ASN A 34 5980 2472 4023 -1253 -695 473 C ATOM 304 CG ASN A 34 -11.430 -29.606 10.818 1.00 37.09 C ANISOU 304 CG ASN A 34 6908 2726 4457 -1098 -656 445 C ATOM 305 OD1 ASN A 34 -11.484 -30.689 11.419 1.00 41.20 O ANISOU 305 OD1 ASN A 34 7537 3075 5043 -1166 -653 542 O ATOM 306 ND2 ASN A 34 -10.579 -29.381 9.828 1.00 35.68 N ANISOU 306 ND2 ASN A 34 6956 2480 4119 -871 -592 324 N ATOM 307 N ASER A 35 -13.305 -30.518 13.907 0.54 42.65 N ANISOU 307 N ASER A 35 7008 3548 5649 -2161 -899 602 N ATOM 308 N BSER A 35 -13.321 -30.511 13.913 0.46 42.72 N ANISOU 308 N BSER A 35 7013 3560 5657 -2163 -898 605 N ATOM 309 CA ASER A 35 -12.823 -31.038 15.184 0.54 43.87 C ANISOU 309 CA ASER A 35 7251 3530 5888 -2057 -770 896 C ATOM 310 CA BSER A 35 -12.825 -31.057 15.174 0.46 43.90 C ANISOU 310 CA BSER A 35 7257 3527 5896 -2059 -772 894 C ATOM 311 C ASER A 35 -11.316 -31.268 15.167 0.54 43.83 C ANISOU 311 C ASER A 35 7457 3346 5850 -1745 -749 818 C ATOM 312 C BSER A 35 -11.312 -31.224 15.158 0.46 43.70 C ANISOU 312 C BSER A 35 7437 3343 5823 -1740 -748 815 C ATOM 313 O ASER A 35 -10.675 -31.241 16.225 0.54 43.19 O ANISOU 313 O ASER A 35 7407 3276 5726 -1592 -652 1096 O ATOM 314 O BSER A 35 -10.664 -31.111 16.206 0.46 42.80 O ANISOU 314 O BSER A 35 7347 3270 5646 -1576 -647 1084 O ATOM 315 CB ASER A 35 -13.558 -32.334 15.549 0.54 47.23 C ANISOU 315 CB ASER A 35 7669 3654 6623 -2276 -769 1031 C ATOM 316 CB BSER A 35 -13.499 -32.397 15.478 0.46 47.39 C ANISOU 316 CB BSER A 35 7706 3645 6655 -2270 -776 1010 C ATOM 317 OG ASER A 35 -13.138 -33.417 14.737 0.54 47.48 O ANISOU 317 OG ASER A 35 7843 3289 6908 -2268 -839 773 O ATOM 318 OG BSER A 35 -14.863 -32.215 15.804 0.46 47.33 O ANISOU 318 OG BSER A 35 7472 3849 6663 -2496 -745 1127 O ATOM 319 N ASN A 36 -10.730 -31.490 13.987 1.00 40.10 N ANISOU 319 N ASN A 36 7108 2743 5386 -1679 -835 435 N ATOM 320 CA ASN A 36 -9.278 -31.606 13.899 1.00 45.36 C ANISOU 320 CA ASN A 36 7945 3259 6031 -1375 -805 301 C ATOM 321 C ASN A 36 -8.572 -30.281 14.199 1.00 40.58 C ANISOU 321 C ASN A 36 7295 3065 5059 -1081 -740 373 C ATOM 322 O ASN A 36 -7.363 -30.283 14.446 1.00 40.80 O ANISOU 322 O ASN A 36 7452 3002 5047 -802 -691 366 O ATOM 323 CB ASN A 36 -8.865 -32.114 12.514 1.00 46.69 C ANISOU 323 CB ASN A 36 8207 3262 6271 -1430 -883 -217 C ATOM 324 CG ASN A 36 -9.486 -33.459 12.168 1.00 51.91 C ANISOU 324 CG ASN A 36 8814 3563 7348 -1673 -894 -368 C ATOM 325 OD1 ASN A 36 -9.898 -34.210 13.046 1.00 56.35 O ANISOU 325 OD1 ASN A 36 9326 3867 8217 -1726 -855 -52 O ATOM 326 ND2 ASN A 36 -9.553 -33.764 10.879 1.00 51.97 N ANISOU 326 ND2 ASN A 36 8749 3644 7354 -1809 -917 -849 N ATOM 327 N LEU A 37 -9.290 -29.156 14.177 1.00 35.31 N ANISOU 327 N LEU A 37 6417 2815 4183 -1136 -745 435 N ATOM 328 CA LEU A 37 -8.731 -27.860 14.543 1.00 33.18 C ANISOU 328 CA LEU A 37 6038 2914 3653 -874 -675 506 C ATOM 329 C LEU A 37 -9.040 -27.471 15.983 1.00 31.76 C ANISOU 329 C LEU A 37 5705 2907 3456 -865 -509 834 C ATOM 330 O LEU A 37 -8.594 -26.412 16.434 1.00 27.72 O ANISOU 330 O LEU A 37 5066 2701 2767 -661 -414 869 O ATOM 331 CB LEU A 37 -9.238 -26.764 13.589 1.00 29.23 C ANISOU 331 CB LEU A 37 5323 2757 3025 -941 -800 363 C ATOM 332 CG LEU A 37 -8.707 -26.874 12.151 1.00 32.65 C ANISOU 332 CG LEU A 37 5871 3209 3326 -966 -960 35 C ATOM 333 CD1 LEU A 37 -9.394 -25.876 11.197 1.00 29.89 C ANISOU 333 CD1 LEU A 37 5255 3226 2874 -1144 -1147 12 C ATOM 334 CD2 LEU A 37 -7.187 -26.676 12.136 1.00 29.03 C ANISOU 334 CD2 LEU A 37 5594 2751 2686 -620 -902 -89 C ATOM 335 N GLN A 38 -9.776 -28.301 16.718 1.00 35.77 N ANISOU 335 N GLN A 38 6197 3258 4135 -1109 -465 1055 N ATOM 336 CA GLN A 38 -10.198 -27.973 18.082 1.00 36.96 C ANISOU 336 CA GLN A 38 6155 3668 4219 -1210 -296 1338 C ATOM 337 C GLN A 38 -9.188 -28.539 19.077 1.00 36.63 C ANISOU 337 C GLN A 38 6204 3576 4137 -1052 -204 1557 C ATOM 338 O GLN A 38 -9.284 -29.675 19.528 1.00 39.42 O ANISOU 338 O GLN A 38 6588 3702 4687 -1165 -223 1740 O ATOM 339 CB GLN A 38 -11.615 -28.479 18.323 1.00 34.04 C ANISOU 339 CB GLN A 38 5641 3262 4031 -1590 -303 1448 C ATOM 340 CG GLN A 38 -12.616 -27.717 17.457 1.00 33.21 C ANISOU 340 CG GLN A 38 5312 3308 3998 -1700 -380 1225 C ATOM 341 CD GLN A 38 -13.990 -28.349 17.427 1.00 42.88 C ANISOU 341 CD GLN A 38 6436 4421 5435 -2068 -425 1289 C ATOM 342 OE1 GLN A 38 -14.275 -29.284 18.176 1.00 45.16 O ANISOU 342 OE1 GLN A 38 6788 4569 5801 -2248 -376 1506 O ATOM 343 NE2 GLN A 38 -14.844 -27.852 16.544 1.00 41.77 N ANISOU 343 NE2 GLN A 38 6119 4351 5401 -2189 -542 1127 N ATOM 344 N ASN A 39 -8.202 -27.714 19.414 1.00 33.73 N ANISOU 344 N ASN A 39 5131 2926 4760 -849 -926 521 N ATOM 345 CA ASN A 39 -7.178 -28.030 20.395 1.00 34.86 C ANISOU 345 CA ASN A 39 5410 3020 4816 -791 -942 601 C ATOM 346 C ASN A 39 -6.801 -26.722 21.068 1.00 32.77 C ANISOU 346 C ASN A 39 5148 2931 4373 -740 -836 632 C ATOM 347 O ASN A 39 -7.170 -25.641 20.609 1.00 30.53 O ANISOU 347 O ASN A 39 4754 2806 4040 -735 -749 574 O ATOM 348 CB ASN A 39 -5.959 -28.696 19.744 1.00 37.17 C ANISOU 348 CB ASN A 39 5750 3218 5154 -658 -1094 476 C ATOM 349 CG ASN A 39 -5.455 -27.912 18.532 1.00 39.49 C ANISOU 349 CG ASN A 39 5964 3631 5409 -540 -1070 302 C ATOM 350 OD1 ASN A 39 -5.078 -26.746 18.649 1.00 36.66 O ANISOU 350 OD1 ASN A 39 5548 3429 4953 -490 -977 290 O ATOM 351 ND2 ASN A 39 -5.475 -28.544 17.359 1.00 39.21 N ANISOU 351 ND2 ASN A 39 5956 3502 5439 -491 -1146 170 N ATOM 352 N VAL A 40 -6.044 -26.822 22.161 1.00 33.50 N ANISOU 352 N VAL A 40 5389 2971 4368 -693 -878 719 N ATOM 353 CA VAL A 40 -5.763 -25.641 22.974 1.00 31.48 C ANISOU 353 CA VAL A 40 5184 2840 3937 -648 -816 756 C ATOM 354 C VAL A 40 -5.032 -24.579 22.168 1.00 28.82 C ANISOU 354 C VAL A 40 4696 2646 3609 -549 -834 607 C ATOM 355 O VAL A 40 -5.335 -23.384 22.273 1.00 27.51 O ANISOU 355 O VAL A 40 4476 2629 3346 -550 -730 599 O ATOM 356 CB VAL A 40 -4.957 -26.027 24.223 1.00 31.91 C ANISOU 356 CB VAL A 40 5474 2764 3888 -589 -945 853 C ATOM 357 CG1 VAL A 40 -4.346 -24.773 24.822 1.00 30.20 C ANISOU 357 CG1 VAL A 40 5302 2648 3525 -502 -978 827 C ATOM 358 CG2 VAL A 40 -5.850 -26.723 25.210 1.00 35.71 C ANISOU 358 CG2 VAL A 40 6090 3190 4290 -661 -803 990 C ATOM 359 N THR A 41 -4.026 -24.988 21.391 1.00 29.35 N ANISOU 359 N THR A 41 4698 2650 3802 -453 -942 495 N ATOM 360 CA THR A 41 -3.302 -24.031 20.556 1.00 29.21 C ANISOU 360 CA THR A 41 4537 2736 3824 -357 -901 370 C ATOM 361 C THR A 41 -4.275 -23.148 19.781 1.00 27.20 C ANISOU 361 C THR A 41 4197 2641 3496 -407 -753 330 C ATOM 362 O THR A 41 -4.180 -21.916 19.802 1.00 27.50 O ANISOU 362 O THR A 41 4168 2809 3470 -382 -678 312 O ATOM 363 CB THR A 41 -2.376 -24.775 19.585 1.00 31.36 C ANISOU 363 CB THR A 41 4759 2896 4261 -254 -949 258 C ATOM 364 OG1 THR A 41 -1.691 -25.830 20.274 1.00 33.42 O ANISOU 364 OG1 THR A 41 5099 2976 4622 -220 -1114 301 O ATOM 365 CG2 THR A 41 -1.364 -23.820 18.984 1.00 28.88 C ANISOU 365 CG2 THR A 41 4305 2639 4029 -139 -870 165 C ATOM 366 N ASN A 42 -5.243 -23.768 19.121 1.00 24.83 N ANISOU 366 N ASN A 42 3900 2310 3225 -476 -742 314 N ATOM 367 CA ASN A 42 -6.169 -23.032 18.284 1.00 20.31 C ANISOU 367 CA ASN A 42 3254 1848 2616 -509 -667 262 C ATOM 368 C ASN A 42 -7.243 -22.279 19.066 1.00 22.29 C ANISOU 368 C ASN A 42 3458 2198 2813 -611 -569 360 C ATOM 369 O ASN A 42 -7.916 -21.422 18.481 1.00 22.84 O ANISOU 369 O ASN A 42 3445 2371 2864 -622 -516 317 O ATOM 370 CB ASN A 42 -6.798 -23.985 17.281 1.00 23.63 C ANISOU 370 CB ASN A 42 3702 2155 3120 -535 -757 191 C ATOM 371 CG ASN A 42 -5.821 -24.395 16.183 1.00 27.92 C ANISOU 371 CG ASN A 42 4317 2625 3665 -396 -794 56 C ATOM 372 OD1 ASN A 42 -4.738 -23.805 16.036 1.00 28.66 O ANISOU 372 OD1 ASN A 42 4391 2767 3730 -286 -708 18 O ATOM 373 ND2 ASN A 42 -6.211 -25.381 15.385 1.00 25.13 N ANISOU 373 ND2 ASN A 42 4049 2134 3367 -394 -909 -20 N ATOM 374 N TYR A 43 -7.431 -22.547 20.365 1.00 23.06 N ANISOU 374 N TYR A 43 3629 2255 2877 -670 -531 493 N ATOM 375 CA TYR A 43 -8.285 -21.646 21.144 1.00 24.31 C ANISOU 375 CA TYR A 43 3768 2510 2957 -728 -379 578 C ATOM 376 C TYR A 43 -7.631 -20.271 21.291 1.00 22.53 C ANISOU 376 C TYR A 43 3532 2426 2604 -640 -351 529 C ATOM 377 O TYR A 43 -8.310 -19.235 21.221 1.00 18.70 O ANISOU 377 O TYR A 43 2967 2057 2083 -656 -245 521 O ATOM 378 CB TYR A 43 -8.602 -22.257 22.513 1.00 25.06 C ANISOU 378 CB TYR A 43 4019 2504 3000 -789 -301 741 C ATOM 379 CG TYR A 43 -9.288 -23.596 22.368 1.00 32.56 C ANISOU 379 CG TYR A 43 4957 3291 4124 -892 -312 805 C ATOM 380 CD1 TYR A 43 -10.071 -23.869 21.243 1.00 37.34 C ANISOU 380 CD1 TYR A 43 5385 3874 4929 -952 -359 728 C ATOM 381 CD2 TYR A 43 -9.125 -24.596 23.312 1.00 32.67 C ANISOU 381 CD2 TYR A 43 5154 3147 4113 -922 -311 937 C ATOM 382 CE1 TYR A 43 -10.677 -25.090 21.075 1.00 39.44 C ANISOU 382 CE1 TYR A 43 5625 3962 5400 -1049 -410 774 C ATOM 383 CE2 TYR A 43 -9.734 -25.822 23.155 1.00 38.74 C ANISOU 383 CE2 TYR A 43 5900 3745 5075 -1023 -322 1001 C ATOM 384 CZ TYR A 43 -10.512 -26.064 22.035 1.00 41.63 C ANISOU 384 CZ TYR A 43 6054 4089 5674 -1091 -375 914 C ATOM 385 OH TYR A 43 -11.128 -27.283 21.862 1.00 45.38 O ANISOU 385 OH TYR A 43 6479 4386 6378 -1177 -413 951 O ATOM 386 N PHE A 44 -6.310 -20.245 21.484 1.00 16.70 N ANISOU 386 N PHE A 44 2852 1655 1839 -545 -461 492 N ATOM 387 CA PHE A 44 -5.593 -18.974 21.474 1.00 16.97 C ANISOU 387 CA PHE A 44 2835 1787 1827 -465 -463 433 C ATOM 388 C PHE A 44 -5.561 -18.355 20.080 1.00 17.11 C ANISOU 388 C PHE A 44 2707 1889 1905 -430 -409 326 C ATOM 389 O PHE A 44 -5.622 -17.127 19.947 1.00 17.43 O ANISOU 389 O PHE A 44 2686 2037 1900 -408 -343 299 O ATOM 390 CB PHE A 44 -4.180 -19.172 22.015 1.00 18.53 C ANISOU 390 CB PHE A 44 3089 1881 2069 -376 -624 419 C ATOM 391 CG PHE A 44 -4.146 -19.593 23.472 1.00 20.85 C ANISOU 391 CG PHE A 44 3605 2076 2241 -383 -716 524 C ATOM 392 CD1 PHE A 44 -3.841 -20.888 23.825 1.00 21.14 C ANISOU 392 CD1 PHE A 44 3760 1956 2318 -384 -830 576 C ATOM 393 CD2 PHE A 44 -4.445 -18.680 24.480 1.00 25.55 C ANISOU 393 CD2 PHE A 44 4333 2718 2656 -375 -684 572 C ATOM 394 CE1 PHE A 44 -3.821 -21.278 25.163 1.00 27.44 C ANISOU 394 CE1 PHE A 44 4825 2638 2962 -378 -915 687 C ATOM 395 CE2 PHE A 44 -4.424 -19.063 25.820 1.00 26.12 C ANISOU 395 CE2 PHE A 44 4694 2675 2554 -358 -758 672 C ATOM 396 CZ PHE A 44 -4.116 -20.361 26.154 1.00 27.30 C ANISOU 396 CZ PHE A 44 4963 2672 2738 -357 -865 724 C ATOM 397 N VAL A 45 -5.465 -19.183 19.035 1.00 17.08 N ANISOU 397 N VAL A 45 2687 1819 1983 -413 -437 264 N ATOM 398 CA VAL A 45 -5.579 -18.671 17.667 1.00 17.47 C ANISOU 398 CA VAL A 45 2687 1922 2029 -366 -380 170 C ATOM 399 C VAL A 45 -6.917 -17.960 17.473 1.00 17.57 C ANISOU 399 C VAL A 45 2657 2032 1985 -435 -335 182 C ATOM 400 O VAL A 45 -6.996 -16.898 16.839 1.00 18.12 O ANISOU 400 O VAL A 45 2692 2188 2004 -394 -279 137 O ATOM 401 CB VAL A 45 -5.393 -19.822 16.655 1.00 19.47 C ANISOU 401 CB VAL A 45 3006 2055 2337 -326 -434 97 C ATOM 402 CG1 VAL A 45 -5.898 -19.415 15.259 1.00 16.39 C ANISOU 402 CG1 VAL A 45 2660 1692 1876 -282 -405 7 C ATOM 403 CG2 VAL A 45 -3.905 -20.245 16.587 1.00 19.18 C ANISOU 403 CG2 VAL A 45 2968 1922 2396 -219 -429 61 C ATOM 404 N VAL A 46 -7.993 -18.532 18.019 1.00 18.69 N ANISOU 404 N VAL A 46 2792 2142 2169 -539 -352 249 N ATOM 405 CA VAL A 46 -9.305 -17.898 17.902 1.00 18.08 C ANISOU 405 CA VAL A 46 2624 2128 2119 -604 -308 263 C ATOM 406 C VAL A 46 -9.368 -16.615 18.724 1.00 19.43 C ANISOU 406 C VAL A 46 2759 2421 2204 -595 -188 308 C ATOM 407 O VAL A 46 -9.956 -15.623 18.287 1.00 20.12 O ANISOU 407 O VAL A 46 2769 2590 2286 -586 -154 276 O ATOM 408 CB VAL A 46 -10.406 -18.888 18.307 1.00 22.16 C ANISOU 408 CB VAL A 46 3097 2540 2784 -722 -321 336 C ATOM 409 CG1 VAL A 46 -11.748 -18.163 18.476 1.00 20.79 C ANISOU 409 CG1 VAL A 46 2776 2413 2710 -791 -235 373 C ATOM 410 CG2 VAL A 46 -10.496 -20.010 17.244 1.00 23.91 C ANISOU 410 CG2 VAL A 46 3351 2626 3109 -725 -492 257 C ATOM 411 N SER A 47 -8.809 -16.615 19.944 1.00 18.45 N ANISOU 411 N SER A 47 2718 2291 2003 -588 -146 379 N ATOM 412 CA ASER A 47 -8.766 -15.369 20.706 0.81 17.02 C ANISOU 412 CA ASER A 47 2548 2202 1715 -557 -63 399 C ATOM 413 CA BSER A 47 -8.755 -15.371 20.709 0.19 17.40 C ANISOU 413 CA BSER A 47 2598 2250 1763 -557 -64 399 C ATOM 414 C SER A 47 -8.021 -14.290 19.925 1.00 18.29 C ANISOU 414 C SER A 47 2650 2438 1860 -476 -93 310 C ATOM 415 O SER A 47 -8.430 -13.121 19.916 1.00 15.04 O ANISOU 415 O SER A 47 2188 2115 1413 -463 -29 295 O ATOM 416 CB ASER A 47 -8.124 -15.601 22.080 0.81 17.95 C ANISOU 416 CB ASER A 47 2837 2261 1722 -535 -80 469 C ATOM 417 CB BSER A 47 -8.089 -15.609 22.068 0.19 17.29 C ANISOU 417 CB BSER A 47 2754 2177 1640 -533 -84 468 C ATOM 418 OG ASER A 47 -8.062 -14.392 22.823 0.81 15.09 O ANISOU 418 OG ASER A 47 2530 1964 1238 -489 -32 470 O ATOM 419 OG BSER A 47 -6.740 -16.032 21.934 0.19 15.97 O ANISOU 419 OG BSER A 47 2623 1938 1505 -469 -237 426 O ATOM 420 N LEU A 48 -6.950 -14.674 19.224 1.00 18.85 N ANISOU 420 N LEU A 48 2724 2459 1981 -418 -163 255 N ATOM 421 CA LEU A 48 -6.207 -13.709 18.421 1.00 18.55 C ANISOU 421 CA LEU A 48 2630 2460 1960 -342 -135 191 C ATOM 422 C LEU A 48 -7.030 -13.247 17.219 1.00 15.72 C ANISOU 422 C LEU A 48 2246 2153 1572 -339 -92 147 C ATOM 423 O LEU A 48 -7.015 -12.062 16.866 1.00 15.11 O ANISOU 423 O LEU A 48 2136 2141 1465 -303 -37 128 O ATOM 424 CB LEU A 48 -4.880 -14.343 17.989 1.00 17.23 C ANISOU 424 CB LEU A 48 2462 2192 1894 -273 -166 155 C ATOM 425 CG LEU A 48 -3.876 -13.590 17.143 1.00 22.26 C ANISOU 425 CG LEU A 48 3031 2814 2612 -187 -79 108 C ATOM 426 CD1 LEU A 48 -3.361 -12.364 17.903 1.00 19.72 C ANISOU 426 CD1 LEU A 48 2631 2522 2341 -176 -92 124 C ATOM 427 CD2 LEU A 48 -2.705 -14.531 16.779 1.00 24.19 C ANISOU 427 CD2 LEU A 48 3260 2926 3005 -120 -77 79 C ATOM 428 N ALA A 49 -7.772 -14.165 16.589 1.00 14.58 N ANISOU 428 N ALA A 49 2134 1959 1445 -372 -148 128 N ATOM 429 CA ALA A 49 -8.637 -13.768 15.477 1.00 15.80 C ANISOU 429 CA ALA A 49 2301 2128 1574 -359 -182 77 C ATOM 430 C ALA A 49 -9.759 -12.853 15.956 1.00 16.29 C ANISOU 430 C ALA A 49 2259 2271 1660 -411 -161 109 C ATOM 431 O ALA A 49 -10.172 -11.933 15.239 1.00 16.39 O ANISOU 431 O ALA A 49 2267 2321 1640 -373 -176 74 O ATOM 432 CB ALA A 49 -9.206 -15.024 14.790 1.00 12.97 C ANISOU 432 CB ALA A 49 2006 1659 1264 -383 -312 36 C ATOM 433 N ALA A 50 -10.264 -13.088 17.168 1.00 18.00 N ANISOU 433 N ALA A 50 2411 2498 1929 -487 -111 181 N ATOM 434 CA ALA A 50 -11.289 -12.206 17.725 1.00 19.64 C ANISOU 434 CA ALA A 50 2518 2769 2176 -521 -33 214 C ATOM 435 C ALA A 50 -10.757 -10.791 17.930 1.00 17.22 C ANISOU 435 C ALA A 50 2220 2555 1768 -454 31 198 C ATOM 436 O ALA A 50 -11.458 -9.816 17.643 1.00 16.50 O ANISOU 436 O ALA A 50 2058 2511 1700 -439 46 179 O ATOM 437 CB ALA A 50 -11.823 -12.770 19.048 1.00 18.42 C ANISOU 437 CB ALA A 50 2347 2584 2068 -596 79 309 C ATOM 438 N ALA A 51 -9.534 -10.653 18.448 1.00 15.50 N ANISOU 438 N ALA A 51 2075 2340 1473 -413 45 205 N ATOM 439 CA ALA A 51 -8.949 -9.325 18.580 1.00 14.89 C ANISOU 439 CA ALA A 51 1992 2316 1348 -354 75 183 C ATOM 440 C ALA A 51 -8.835 -8.650 17.220 1.00 16.68 C ANISOU 440 C ALA A 51 2201 2556 1581 -304 66 135 C ATOM 441 O ALA A 51 -9.040 -7.436 17.100 1.00 16.78 O ANISOU 441 O ALA A 51 2181 2616 1578 -275 96 124 O ATOM 442 CB ALA A 51 -7.570 -9.412 19.235 1.00 13.83 C ANISOU 442 CB ALA A 51 1912 2134 1208 -319 33 187 C ATOM 443 N ASP A 52 -8.489 -9.421 16.188 1.00 15.09 N ANISOU 443 N ASP A 52 2055 2297 1381 -281 33 108 N ATOM 444 CA ASP A 52 -8.320 -8.833 14.861 1.00 16.98 C ANISOU 444 CA ASP A 52 2361 2521 1570 -211 51 72 C ATOM 445 C ASP A 52 -9.668 -8.501 14.218 1.00 18.98 C ANISOU 445 C ASP A 52 2623 2786 1802 -216 -40 48 C ATOM 446 O ASP A 52 -9.773 -7.494 13.504 1.00 18.27 O ANISOU 446 O ASP A 52 2582 2704 1655 -160 -33 36 O ATOM 447 CB ASP A 52 -7.478 -9.770 13.989 1.00 17.99 C ANISOU 447 CB ASP A 52 2600 2558 1677 -157 72 44 C ATOM 448 CG ASP A 52 -5.986 -9.768 14.390 1.00 23.55 C ANISOU 448 CG ASP A 52 3254 3222 2471 -124 174 63 C ATOM 449 OD1 ASP A 52 -5.493 -8.712 14.889 1.00 23.00 O ANISOU 449 OD1 ASP A 52 3098 3180 2462 -119 224 87 O ATOM 450 OD2 ASP A 52 -5.310 -10.813 14.205 1.00 23.76 O ANISOU 450 OD2 ASP A 52 3316 3170 2543 -100 184 48 O ATOM 451 N ILE A 53 -10.716 -9.300 14.475 1.00 16.61 N ANISOU 451 N ILE A 53 2263 2464 1584 -284 -136 46 N ATOM 452 CA ILE A 53 -12.065 -8.901 14.055 1.00 16.52 C ANISOU 452 CA ILE A 53 2189 2440 1649 -296 -251 23 C ATOM 453 C ILE A 53 -12.446 -7.567 14.695 1.00 16.36 C ANISOU 453 C ILE A 53 2057 2503 1656 -292 -166 47 C ATOM 454 O ILE A 53 -13.009 -6.682 14.037 1.00 15.92 O ANISOU 454 O ILE A 53 2002 2443 1605 -246 -240 21 O ATOM 455 CB ILE A 53 -13.098 -9.993 14.401 1.00 16.78 C ANISOU 455 CB ILE A 53 2109 2406 1861 -387 -339 31 C ATOM 456 CG1 ILE A 53 -12.842 -11.265 13.599 1.00 17.59 C ANISOU 456 CG1 ILE A 53 2341 2398 1943 -380 -476 -15 C ATOM 457 CG2 ILE A 53 -14.542 -9.487 14.152 1.00 21.17 C ANISOU 457 CG2 ILE A 53 2516 2927 2601 -406 -456 11 C ATOM 458 CD1 ILE A 53 -13.583 -12.508 14.136 1.00 21.87 C ANISOU 458 CD1 ILE A 53 2765 2855 2691 -488 -534 12 C ATOM 459 N LEU A 54 -12.145 -7.399 15.985 1.00 14.84 N ANISOU 459 N LEU A 54 1800 2368 1469 -326 -28 93 N ATOM 460 CA LEU A 54 -12.483 -6.149 16.667 1.00 15.49 C ANISOU 460 CA LEU A 54 1811 2515 1561 -307 56 103 C ATOM 461 C LEU A 54 -11.617 -4.979 16.210 1.00 14.57 C ANISOU 461 C LEU A 54 1764 2422 1349 -235 68 85 C ATOM 462 O LEU A 54 -12.037 -3.831 16.348 1.00 16.10 O ANISOU 462 O LEU A 54 1911 2646 1560 -205 88 77 O ATOM 463 CB LEU A 54 -12.387 -6.313 18.187 1.00 14.33 C ANISOU 463 CB LEU A 54 1656 2393 1396 -341 189 149 C ATOM 464 CG LEU A 54 -13.412 -7.304 18.759 1.00 18.55 C ANISOU 464 CG LEU A 54 2111 2886 2052 -416 250 195 C ATOM 465 CD1 LEU A 54 -13.095 -7.614 20.221 1.00 20.61 C ANISOU 465 CD1 LEU A 54 2470 3145 2216 -430 395 255 C ATOM 466 CD2 LEU A 54 -14.828 -6.744 18.625 1.00 19.66 C ANISOU 466 CD2 LEU A 54 2076 3016 2378 -424 281 188 C ATOM 467 N VAL A 55 -10.439 -5.229 15.642 1.00 14.08 N ANISOU 467 N VAL A 55 1800 2329 1220 -204 75 84 N ATOM 468 CA VAL A 55 -9.723 -4.136 14.986 1.00 13.74 C ANISOU 468 CA VAL A 55 1812 2274 1136 -140 117 84 C ATOM 469 C VAL A 55 -10.561 -3.595 13.831 1.00 16.54 C ANISOU 469 C VAL A 55 2232 2605 1449 -93 39 66 C ATOM 470 O VAL A 55 -10.716 -2.376 13.669 1.00 17.27 O ANISOU 470 O VAL A 55 2320 2704 1536 -55 50 72 O ATOM 471 CB VAL A 55 -8.327 -4.607 14.516 1.00 14.06 C ANISOU 471 CB VAL A 55 1923 2253 1167 -110 190 95 C ATOM 472 CG1 VAL A 55 -7.695 -3.593 13.523 1.00 10.50 C ANISOU 472 CG1 VAL A 55 1549 1752 690 -40 286 116 C ATOM 473 CG2 VAL A 55 -7.384 -4.804 15.732 1.00 16.23 C ANISOU 473 CG2 VAL A 55 2118 2522 1525 -140 211 108 C ATOM 474 N GLY A 56 -11.161 -4.496 13.046 1.00 14.40 N ANISOU 474 N GLY A 56 2034 2283 1154 -90 -78 38 N ATOM 475 CA GLY A 56 -11.983 -4.061 11.924 1.00 13.84 C ANISOU 475 CA GLY A 56 2070 2152 1037 -30 -226 9 C ATOM 476 C GLY A 56 -13.293 -3.408 12.345 1.00 17.09 C ANISOU 476 C GLY A 56 2311 2586 1597 -51 -328 -5 C ATOM 477 O GLY A 56 -13.701 -2.395 11.775 1.00 19.43 O ANISOU 477 O GLY A 56 2654 2854 1873 11 -405 -12 O ATOM 478 N AVAL A 57 -13.964 -3.986 13.343 0.70 16.87 N ANISOU 478 N AVAL A 57 2086 2590 1733 -132 -311 -3 N ATOM 479 N BVAL A 57 -13.986 -3.977 13.331 0.30 17.08 N ANISOU 479 N BVAL A 57 2112 2615 1762 -132 -314 -4 N ATOM 480 CA AVAL A 57 -15.305 -3.542 13.725 0.70 17.93 C ANISOU 480 CA AVAL A 57 2022 2716 2076 -150 -369 -16 C ATOM 481 CA BVAL A 57 -15.313 -3.430 13.622 0.30 17.88 C ANISOU 481 CA BVAL A 57 2026 2705 2061 -141 -382 -18 C ATOM 482 C AVAL A 57 -15.250 -2.258 14.553 0.70 17.96 C ANISOU 482 C AVAL A 57 1948 2793 2083 -125 -219 2 C ATOM 483 C BVAL A 57 -15.242 -2.206 14.538 0.30 17.56 C ANISOU 483 C BVAL A 57 1899 2743 2029 -122 -220 1 C ATOM 484 O AVAL A 57 -16.114 -1.382 14.416 0.70 18.73 O ANISOU 484 O AVAL A 57 1949 2868 2298 -85 -282 -19 O ATOM 485 O BVAL A 57 -16.107 -1.324 14.459 0.30 18.49 O ANISOU 485 O BVAL A 57 1917 2842 2268 -84 -274 -18 O ATOM 486 CB AVAL A 57 -16.021 -4.685 14.478 0.70 18.43 C ANISOU 486 CB AVAL A 57 1913 2755 2336 -245 -339 -1 C ATOM 487 CB BVAL A 57 -16.238 -4.507 14.217 0.30 18.86 C ANISOU 487 CB BVAL A 57 1961 2791 2414 -229 -393 -13 C ATOM 488 CG1AVAL A 57 -17.399 -4.253 14.997 0.70 20.14 C ANISOU 488 CG1AVAL A 57 1872 2941 2838 -265 -322 0 C ATOM 489 CG1BVAL A 57 -16.483 -5.620 13.213 0.30 19.31 C ANISOU 489 CG1BVAL A 57 2097 2734 2505 -241 -624 -53 C ATOM 490 CG2AVAL A 57 -16.161 -5.901 13.560 0.70 18.95 C ANISOU 490 CG2AVAL A 57 2058 2716 2428 -264 -543 -34 C ATOM 491 CG2BVAL A 57 -15.666 -5.054 15.497 0.30 16.53 C ANISOU 491 CG2BVAL A 57 1639 2565 2077 -292 -165 41 C ATOM 492 N LEU A 58 -14.239 -2.120 15.412 1.00 14.19 N ANISOU 492 N LEU A 58 1516 2382 1492 -137 -51 29 N ATOM 493 CA LEU A 58 -14.171 -1.038 16.386 1.00 16.00 C ANISOU 493 CA LEU A 58 1699 2660 1719 -112 72 31 C ATOM 494 C LEU A 58 -12.915 -0.184 16.280 1.00 15.36 C ANISOU 494 C LEU A 58 1735 2588 1515 -71 101 37 C ATOM 495 O LEU A 58 -13.021 1.048 16.214 1.00 14.83 O ANISOU 495 O LEU A 58 1660 2514 1459 -21 97 25 O ATOM 496 CB LEU A 58 -14.283 -1.607 17.815 1.00 19.48 C ANISOU 496 CB LEU A 58 2096 3132 2172 -158 226 54 C ATOM 497 CG LEU A 58 -15.648 -2.176 18.212 1.00 22.26 C ANISOU 497 CG LEU A 58 2285 3456 2716 -199 291 68 C ATOM 498 CD1 LEU A 58 -15.607 -2.687 19.639 1.00 19.65 C ANISOU 498 CD1 LEU A 58 1995 3138 2334 -228 498 112 C ATOM 499 CD2 LEU A 58 -16.762 -1.111 18.051 1.00 22.33 C ANISOU 499 CD2 LEU A 58 2142 3444 2899 -147 285 36 C ATOM 500 N ALA A 59 -11.717 -0.780 16.298 1.00 14.06 N ANISOU 500 N ALA A 59 1652 2415 1275 -91 131 56 N ATOM 501 CA ALA A 59 -10.512 0.055 16.370 1.00 15.56 C ANISOU 501 CA ALA A 59 1889 2580 1442 -63 170 66 C ATOM 502 C ALA A 59 -10.351 0.914 15.129 1.00 15.83 C ANISOU 502 C ALA A 59 1990 2565 1461 -11 158 84 C ATOM 503 O ALA A 59 -9.880 2.055 15.215 1.00 14.12 O ANISOU 503 O ALA A 59 1769 2317 1278 16 188 93 O ATOM 504 CB ALA A 59 -9.248 -0.791 16.552 1.00 15.26 C ANISOU 504 CB ALA A 59 1886 2510 1403 -88 196 83 C ATOM 505 N ILE A 60 -10.684 0.376 13.961 1.00 13.98 N ANISOU 505 N ILE A 60 1849 2298 1163 10 109 91 N ATOM 506 CA ILE A 60 -10.503 1.180 12.751 1.00 13.11 C ANISOU 506 CA ILE A 60 1882 2116 983 78 112 122 C ATOM 507 C ILE A 60 -11.551 2.293 12.701 1.00 13.32 C ANISOU 507 C ILE A 60 1873 2142 1047 116 12 106 C ATOM 508 O ILE A 60 -11.181 3.451 12.464 1.00 15.00 O ANISOU 508 O ILE A 60 2130 2310 1260 154 57 138 O ATOM 509 CB ILE A 60 -10.482 0.289 11.496 1.00 14.80 C ANISOU 509 CB ILE A 60 2292 2266 1064 118 75 127 C ATOM 510 CG1 ILE A 60 -9.091 -0.390 11.429 1.00 15.73 C ANISOU 510 CG1 ILE A 60 2452 2352 1171 109 249 158 C ATOM 511 CG2 ILE A 60 -10.791 1.123 10.214 1.00 16.37 C ANISOU 511 CG2 ILE A 60 2713 2371 1134 212 21 153 C ATOM 512 CD1 ILE A 60 -8.893 -1.465 10.292 1.00 15.11 C ANISOU 512 CD1 ILE A 60 2541 2192 1008 142 239 140 C ATOM 513 N PRO A 61 -12.846 2.033 12.919 1.00 14.96 N ANISOU 513 N PRO A 61 1980 2375 1328 108 -117 61 N ATOM 514 CA PRO A 61 -13.768 3.174 13.062 1.00 15.60 C ANISOU 514 CA PRO A 61 1977 2445 1504 151 -190 39 C ATOM 515 C PRO A 61 -13.311 4.192 14.110 1.00 15.28 C ANISOU 515 C PRO A 61 1855 2439 1510 149 -67 37 C ATOM 516 O PRO A 61 -13.483 5.396 13.895 1.00 16.66 O ANISOU 516 O PRO A 61 2047 2571 1711 203 -98 40 O ATOM 517 CB PRO A 61 -15.104 2.499 13.432 1.00 15.74 C ANISOU 517 CB PRO A 61 1821 2476 1683 123 -286 -6 C ATOM 518 CG PRO A 61 -15.048 1.185 12.710 1.00 18.56 C ANISOU 518 CG PRO A 61 2271 2798 1983 96 -380 -8 C ATOM 519 CD PRO A 61 -13.581 0.751 12.844 1.00 17.80 C ANISOU 519 CD PRO A 61 2294 2737 1731 69 -217 30 C ATOM 520 N PHE A 62 -12.724 3.750 15.229 1.00 14.28 N ANISOU 520 N PHE A 62 1671 2368 1387 98 42 28 N ATOM 521 CA PHE A 62 -12.257 4.702 16.238 1.00 13.80 C ANISOU 521 CA PHE A 62 1583 2308 1352 111 104 8 C ATOM 522 C PHE A 62 -11.076 5.512 15.716 1.00 13.51 C ANISOU 522 C PHE A 62 1623 2196 1315 124 120 48 C ATOM 523 O PHE A 62 -10.976 6.719 15.981 1.00 16.53 O ANISOU 523 O PHE A 62 1995 2532 1752 158 110 35 O ATOM 524 CB PHE A 62 -11.833 3.981 17.535 1.00 11.60 C ANISOU 524 CB PHE A 62 1293 2071 1045 70 169 -13 C ATOM 525 CG PHE A 62 -12.974 3.398 18.358 1.00 13.36 C ANISOU 525 CG PHE A 62 1448 2343 1285 62 231 -36 C ATOM 526 CD1 PHE A 62 -14.314 3.560 18.000 1.00 14.81 C ANISOU 526 CD1 PHE A 62 1519 2528 1581 85 222 -49 C ATOM 527 CD2 PHE A 62 -12.678 2.671 19.515 1.00 12.83 C ANISOU 527 CD2 PHE A 62 1433 2294 1146 36 304 -38 C ATOM 528 CE1 PHE A 62 -15.333 3.011 18.780 1.00 19.38 C ANISOU 528 CE1 PHE A 62 1997 3124 2244 72 333 -56 C ATOM 529 CE2 PHE A 62 -13.695 2.120 20.317 1.00 15.73 C ANISOU 529 CE2 PHE A 62 1763 2684 1531 30 428 -36 C ATOM 530 CZ PHE A 62 -15.023 2.286 19.960 1.00 17.65 C ANISOU 530 CZ PHE A 62 1852 2927 1929 43 470 -41 C ATOM 531 N ALA A 63 -10.155 4.858 14.995 1.00 13.84 N ANISOU 531 N ALA A 63 1732 2205 1323 100 168 99 N ATOM 532 CA ALA A 63 -9.015 5.559 14.402 1.00 13.97 C ANISOU 532 CA ALA A 63 1797 2119 1391 110 246 159 C ATOM 533 C ALA A 63 -9.466 6.594 13.374 1.00 17.19 C ANISOU 533 C ALA A 63 2309 2460 1762 169 235 203 C ATOM 534 O ALA A 63 -8.896 7.685 13.283 1.00 16.09 O ANISOU 534 O ALA A 63 2173 2230 1712 181 283 242 O ATOM 535 CB ALA A 63 -8.070 4.552 13.726 1.00 15.14 C ANISOU 535 CB ALA A 63 2004 2231 1518 91 352 208 C ATOM 536 N ILE A 64 -10.448 6.238 12.544 1.00 18.15 N ANISOU 536 N ILE A 64 2533 2597 1768 211 149 200 N ATOM 537 CA ILE A 64 -11.001 7.196 11.590 1.00 15.90 C ANISOU 537 CA ILE A 64 2384 2229 1428 285 79 237 C ATOM 538 C ILE A 64 -11.565 8.399 12.338 1.00 19.49 C ANISOU 538 C ILE A 64 2714 2685 2006 303 10 196 C ATOM 539 O ILE A 64 -11.297 9.555 11.982 1.00 18.55 O ANISOU 539 O ILE A 64 2662 2470 1916 339 29 244 O ATOM 540 CB ILE A 64 -12.059 6.498 10.709 1.00 15.69 C ANISOU 540 CB ILE A 64 2481 2197 1285 332 -89 214 C ATOM 541 CG1 ILE A 64 -11.389 5.478 9.773 1.00 13.87 C ANISOU 541 CG1 ILE A 64 2459 1923 888 344 -12 255 C ATOM 542 CG2 ILE A 64 -12.913 7.520 9.890 1.00 17.54 C ANISOU 542 CG2 ILE A 64 2847 2332 1484 425 -256 229 C ATOM 543 CD1 ILE A 64 -12.411 4.522 9.031 1.00 14.76 C ANISOU 543 CD1 ILE A 64 2698 2015 896 384 -238 202 C ATOM 544 N THR A 65 -12.297 8.139 13.429 1.00 15.82 N ANISOU 544 N THR A 65 2078 2313 1618 283 -39 111 N ATOM 545 CA THR A 65 -12.928 9.199 14.210 1.00 17.48 C ANISOU 545 CA THR A 65 2184 2520 1936 322 -79 55 C ATOM 546 C THR A 65 -11.890 10.147 14.816 1.00 17.21 C ANISOU 546 C THR A 65 2149 2428 1963 310 -12 60 C ATOM 547 O THR A 65 -12.019 11.373 14.722 1.00 17.83 O ANISOU 547 O THR A 65 2243 2425 2105 357 -52 62 O ATOM 548 CB THR A 65 -13.805 8.571 15.308 1.00 20.20 C ANISOU 548 CB THR A 65 2378 2960 2336 308 -64 -25 C ATOM 549 OG1 THR A 65 -14.814 7.730 14.713 1.00 20.89 O ANISOU 549 OG1 THR A 65 2421 3065 2450 310 -151 -29 O ATOM 550 CG2 THR A 65 -14.508 9.647 16.132 1.00 19.41 C ANISOU 550 CG2 THR A 65 2192 2843 2339 372 -59 -91 C ATOM 551 N AILE A 66 -10.836 9.593 15.424 0.54 16.63 N ANISOU 551 N AILE A 66 2053 2368 1898 249 58 60 N ATOM 552 N BILE A 66 -10.853 9.602 15.452 0.46 16.73 N ANISOU 552 N BILE A 66 2063 2381 1911 249 57 58 N ATOM 553 CA AILE A 66 -9.863 10.426 16.127 0.54 17.68 C ANISOU 553 CA AILE A 66 2159 2414 2145 235 59 45 C ATOM 554 CA BILE A 66 -9.909 10.490 16.119 0.46 17.70 C ANISOU 554 CA BILE A 66 2162 2414 2148 238 56 44 C ATOM 555 C AILE A 66 -8.939 11.163 15.168 0.54 18.58 C ANISOU 555 C AILE A 66 2316 2389 2356 223 119 145 C ATOM 556 C BILE A 66 -9.058 11.263 15.126 0.46 18.76 C ANISOU 556 C BILE A 66 2344 2410 2373 231 112 144 C ATOM 557 O AILE A 66 -8.243 12.100 15.578 0.54 20.03 O ANISOU 557 O AILE A 66 2456 2456 2697 213 96 140 O ATOM 558 O BILE A 66 -8.531 12.328 15.472 0.46 19.70 O ANISOU 558 O BILE A 66 2431 2415 2638 231 84 139 O ATOM 559 CB AILE A 66 -9.030 9.585 17.111 0.54 17.25 C ANISOU 559 CB AILE A 66 2067 2383 2105 183 59 7 C ATOM 560 CB BILE A 66 -8.995 9.721 17.079 0.46 17.30 C ANISOU 560 CB BILE A 66 2073 2377 2123 185 57 9 C ATOM 561 CG1AILE A 66 -8.429 10.481 18.200 0.54 13.63 C ANISOU 561 CG1AILE A 66 1596 1826 1755 195 -37 -63 C ATOM 562 CG1BILE A 66 -8.037 8.845 16.288 0.46 16.05 C ANISOU 562 CG1BILE A 66 1914 2195 1991 132 145 92 C ATOM 563 CG2AILE A 66 -7.933 8.814 16.361 0.54 15.64 C ANISOU 563 CG2AILE A 66 1856 2138 1949 128 144 90 C ATOM 564 CG2BILE A 66 -9.803 8.860 18.016 0.46 19.26 C ANISOU 564 CG2BILE A 66 2321 2744 2252 194 48 -62 C ATOM 565 CD1AILE A 66 -7.697 9.707 19.284 0.54 12.54 C ANISOU 565 CD1AILE A 66 1468 1683 1614 167 -107 -116 C ATOM 566 CD1BILE A 66 -7.071 8.225 17.157 0.46 20.11 C ANISOU 566 CD1BILE A 66 2372 2683 2584 89 109 61 C ATOM 567 N SER A 67 -8.899 10.762 13.896 1.00 20.67 N ANISOU 567 N SER A 67 2685 2635 2532 230 204 238 N ATOM 568 CA SER A 67 -8.126 11.511 12.914 1.00 20.01 C ANISOU 568 CA SER A 67 2690 2398 2516 235 324 356 C ATOM 569 C SER A 67 -8.796 12.841 12.574 1.00 23.05 C ANISOU 569 C SER A 67 3147 2703 2909 296 248 375 C ATOM 570 O SER A 67 -8.134 13.734 12.036 1.00 25.34 O ANISOU 570 O SER A 67 3492 2836 3301 294 344 473 O ATOM 571 CB SER A 67 -7.910 10.672 11.637 1.00 19.51 C ANISOU 571 CB SER A 67 2800 2318 2294 253 463 450 C ATOM 572 OG SER A 67 -9.104 10.581 10.860 1.00 21.15 O ANISOU 572 OG SER A 67 3180 2561 2294 327 347 445 O ATOM 573 N THR A 68 -10.097 12.994 12.861 1.00 20.40 N ANISOU 573 N THR A 68 2801 2450 2499 352 90 290 N ATOM 574 CA THR A 68 -10.774 14.264 12.603 1.00 22.89 C ANISOU 574 CA THR A 68 3167 2679 2851 422 -8 295 C ATOM 575 C THR A 68 -10.490 15.324 13.667 1.00 24.61 C ANISOU 575 C THR A 68 3266 2835 3250 416 -49 228 C ATOM 576 O THR A 68 -10.742 16.504 13.422 1.00 23.59 O ANISOU 576 O THR A 68 3182 2592 3191 464 -107 249 O ATOM 577 CB THR A 68 -12.294 14.059 12.515 1.00 23.21 C ANISOU 577 CB THR A 68 3198 2799 2820 494 -170 222 C ATOM 578 OG1 THR A 68 -12.798 13.685 13.808 1.00 20.02 O ANISOU 578 OG1 THR A 68 2612 2514 2480 482 -190 97 O ATOM 579 CG2 THR A 68 -12.648 12.963 11.493 1.00 18.22 C ANISOU 579 CG2 THR A 68 2699 2203 2022 507 -202 264 C ATOM 580 N GLY A 69 -9.990 14.948 14.843 1.00 21.93 N ANISOU 580 N GLY A 69 2808 2547 2977 369 -50 142 N ATOM 581 CA GLY A 69 -9.825 15.937 15.896 1.00 19.96 C ANISOU 581 CA GLY A 69 2501 2220 2863 387 -139 51 C ATOM 582 C GLY A 69 -11.130 16.492 16.433 1.00 23.18 C ANISOU 582 C GLY A 69 2904 2675 3230 483 -226 -56 C ATOM 583 O GLY A 69 -11.148 17.607 16.973 1.00 24.94 O ANISOU 583 O GLY A 69 3130 2793 3554 529 -302 -118 O ATOM 584 N PHE A 70 -12.218 15.732 16.316 1.00 20.98 N ANISOU 584 N PHE A 70 2602 2529 2842 518 -213 -82 N ATOM 585 CA PHE A 70 -13.536 16.204 16.729 1.00 23.34 C ANISOU 585 CA PHE A 70 2849 2853 3168 616 -258 -173 C ATOM 586 C PHE A 70 -13.552 16.580 18.212 1.00 25.79 C ANISOU 586 C PHE A 70 3152 3159 3489 661 -238 -305 C ATOM 587 O PHE A 70 -12.814 16.020 19.034 1.00 24.40 O ANISOU 587 O PHE A 70 3013 3011 3247 615 -210 -341 O ATOM 588 CB PHE A 70 -14.595 15.127 16.448 1.00 22.09 C ANISOU 588 CB PHE A 70 2615 2815 2962 625 -239 -177 C ATOM 589 CG PHE A 70 -14.538 13.956 17.392 1.00 23.02 C ANISOU 589 CG PHE A 70 2687 3054 3005 578 -130 -225 C ATOM 590 CD1 PHE A 70 -13.465 13.087 17.378 1.00 21.68 C ANISOU 590 CD1 PHE A 70 2568 2921 2748 487 -91 -176 C ATOM 591 CD2 PHE A 70 -15.563 13.731 18.294 1.00 28.25 C ANISOU 591 CD2 PHE A 70 3260 3772 3700 633 -46 -310 C ATOM 592 CE1 PHE A 70 -13.391 12.027 18.259 1.00 26.40 C ANISOU 592 CE1 PHE A 70 3152 3610 3268 450 -12 -213 C ATOM 593 CE2 PHE A 70 -15.511 12.663 19.174 1.00 30.74 C ANISOU 593 CE2 PHE A 70 3575 4177 3927 594 78 -334 C ATOM 594 CZ PHE A 70 -14.428 11.810 19.162 1.00 29.01 C ANISOU 594 CZ PHE A 70 3430 3995 3597 503 75 -286 C ATOM 595 N CYS A 71 -14.414 17.537 18.544 1.00 26.63 N ANISOU 595 N CYS A 71 3239 3210 3670 767 -265 -383 N ATOM 596 CA CYS A 71 -14.600 17.981 19.925 1.00 28.18 C ANISOU 596 CA CYS A 71 3485 3380 3842 849 -226 -522 C ATOM 597 C CYS A 71 -15.204 16.863 20.775 1.00 27.05 C ANISOU 597 C CYS A 71 3324 3368 3584 863 -64 -573 C ATOM 598 O CYS A 71 -16.206 16.253 20.391 1.00 25.24 O ANISOU 598 O CYS A 71 2963 3220 3407 871 19 -545 O ATOM 599 CB CYS A 71 -15.522 19.206 19.958 1.00 30.34 C ANISOU 599 CB CYS A 71 3730 3558 4238 977 -259 -591 C ATOM 600 SG CYS A 71 -14.830 20.719 19.202 1.00 36.48 S ANISOU 600 SG CYS A 71 4568 4135 5157 977 -442 -540 S ATOM 601 N ALA A 72 -14.628 16.618 21.952 1.00 23.62 N ANISOU 601 N ALA A 72 3036 2928 3010 872 -31 -647 N ATOM 602 CA ALA A 72 -15.121 15.529 22.783 1.00 23.69 C ANISOU 602 CA ALA A 72 3080 3040 2883 885 150 -671 C ATOM 603 C ALA A 72 -14.759 15.788 24.234 1.00 25.79 C ANISOU 603 C ALA A 72 3599 3233 2968 973 170 -790 C ATOM 604 O ALA A 72 -13.759 16.455 24.529 1.00 25.61 O ANISOU 604 O ALA A 72 3711 3092 2929 974 -27 -841 O ATOM 605 CB ALA A 72 -14.532 14.181 22.336 1.00 23.87 C ANISOU 605 CB ALA A 72 3061 3162 2845 753 146 -571 C ATOM 606 N ALA A 73 -15.580 15.255 25.138 1.00 23.31 N ANISOU 606 N ALA A 73 3364 2965 2528 1052 408 -831 N ATOM 607 CA ALA A 73 -15.149 15.139 26.524 1.00 25.68 C ANISOU 607 CA ALA A 73 3994 3200 2565 1133 437 -922 C ATOM 608 C ALA A 73 -13.878 14.299 26.571 1.00 22.44 C ANISOU 608 C ALA A 73 3675 2798 2053 1017 247 -874 C ATOM 609 O ALA A 73 -13.728 13.321 25.828 1.00 22.03 O ANISOU 609 O ALA A 73 3448 2853 2068 891 263 -762 O ATOM 610 CB ALA A 73 -16.251 14.518 27.388 1.00 28.65 C ANISOU 610 CB ALA A 73 4404 3620 2860 1157 764 -898 C ATOM 611 N CYS A 74 -12.921 14.720 27.393 1.00 21.66 N ANISOU 611 N CYS A 74 2270 3049 2909 647 -609 -782 N ATOM 612 CA CYS A 74 -11.578 14.155 27.268 1.00 25.18 C ANISOU 612 CA CYS A 74 2704 3415 3447 576 -650 -762 C ATOM 613 C CYS A 74 -11.570 12.663 27.577 1.00 23.51 C ANISOU 613 C CYS A 74 2565 3350 3017 541 -601 -723 C ATOM 614 O CYS A 74 -10.870 11.894 26.916 1.00 21.36 O ANISOU 614 O CYS A 74 2274 3065 2777 452 -563 -630 O ATOM 615 CB CYS A 74 -10.590 14.906 28.167 1.00 30.41 C ANISOU 615 CB CYS A 74 3339 3909 4308 641 -842 -945 C ATOM 616 SG CYS A 74 -8.832 14.400 27.952 1.00 35.59 S ANISOU 616 SG CYS A 74 3892 4389 5241 554 -919 -950 S ATOM 617 N HIS A 75 -12.363 12.222 28.559 1.00 22.51 N ANISOU 617 N HIS A 75 2529 3348 2677 626 -562 -775 N ATOM 618 CA HIS A 75 -12.291 10.810 28.920 1.00 25.50 C ANISOU 618 CA HIS A 75 2983 3825 2881 606 -483 -720 C ATOM 619 C HIS A 75 -12.956 9.909 27.876 1.00 23.77 C ANISOU 619 C HIS A 75 2684 3680 2669 486 -350 -578 C ATOM 620 O HIS A 75 -12.512 8.773 27.669 1.00 22.52 O ANISOU 620 O HIS A 75 2543 3551 2463 417 -318 -514 O ATOM 621 CB HIS A 75 -12.868 10.619 30.319 1.00 30.75 C ANISOU 621 CB HIS A 75 3805 4555 3322 778 -419 -785 C ATOM 622 CG HIS A 75 -12.001 11.215 31.388 1.00 34.57 C ANISOU 622 CG HIS A 75 4434 4961 3741 952 -630 -966 C ATOM 623 ND1 HIS A 75 -12.120 12.526 31.799 1.00 40.11 N ANISOU 623 ND1 HIS A 75 5145 5584 4510 1071 -762 -1116 N ATOM 624 CD2 HIS A 75 -10.959 10.700 32.080 1.00 34.54 C ANISOU 624 CD2 HIS A 75 4561 4919 3643 1046 -786 -1055 C ATOM 625 CE1 HIS A 75 -11.209 12.785 32.720 1.00 39.96 C ANISOU 625 CE1 HIS A 75 5259 5476 4449 1240 -1012 -1309 C ATOM 626 NE2 HIS A 75 -10.491 11.693 32.907 1.00 39.15 N ANISOU 626 NE2 HIS A 75 5222 5388 4264 1225 -1025 -1254 N ATOM 627 N GLY A 76 -13.984 10.390 27.181 1.00 24.43 N ANISOU 627 N GLY A 76 2678 3777 2828 478 -313 -553 N ATOM 628 CA GLY A 76 -14.494 9.632 26.046 1.00 22.05 C ANISOU 628 CA GLY A 76 2305 3506 2566 403 -288 -474 C ATOM 629 C GLY A 76 -13.486 9.585 24.916 1.00 21.58 C ANISOU 629 C GLY A 76 2283 3387 2531 360 -347 -404 C ATOM 630 O GLY A 76 -13.328 8.559 24.245 1.00 22.87 O ANISOU 630 O GLY A 76 2459 3575 2656 313 -340 -349 O ATOM 631 N CYS A 77 -12.789 10.693 24.693 1.00 20.08 N ANISOU 631 N CYS A 77 2108 3090 2431 390 -380 -399 N ATOM 632 CA CYS A 77 -11.712 10.704 23.716 1.00 24.06 C ANISOU 632 CA CYS A 77 2647 3490 3003 370 -348 -298 C ATOM 633 C CYS A 77 -10.663 9.656 24.069 1.00 21.36 C ANISOU 633 C CYS A 77 2313 3154 2648 296 -338 -288 C ATOM 634 O CYS A 77 -10.154 8.945 23.191 1.00 17.37 O ANISOU 634 O CYS A 77 1849 2634 2115 274 -281 -193 O ATOM 635 CB CYS A 77 -11.085 12.102 23.653 1.00 26.07 C ANISOU 635 CB CYS A 77 2869 3571 3464 407 -337 -291 C ATOM 636 SG CYS A 77 -9.701 12.209 22.518 1.00 29.07 S ANISOU 636 SG CYS A 77 3265 3756 4026 402 -184 -122 S ATOM 637 N ALEU A 78 -10.337 9.529 25.362 0.70 17.95 N ANISOU 637 N ALEU A 78 1872 2738 2209 293 -405 -395 N ATOM 638 N BLEU A 78 -10.361 9.525 25.356 0.30 18.86 N ANISOU 638 N BLEU A 78 1988 2855 2322 293 -404 -394 N ATOM 639 CA ALEU A 78 -9.331 8.552 25.768 0.70 19.47 C ANISOU 639 CA ALEU A 78 2085 2926 2386 252 -431 -403 C ATOM 640 CA BLEU A 78 -9.343 8.586 25.793 0.30 18.93 C ANISOU 640 CA BLEU A 78 2017 2857 2320 254 -433 -407 C ATOM 641 C ALEU A 78 -9.768 7.142 25.414 0.70 17.74 C ANISOU 641 C ALEU A 78 1910 2826 2005 202 -359 -328 C ATOM 642 C BLEU A 78 -9.754 7.143 25.523 0.30 17.62 C ANISOU 642 C BLEU A 78 1896 2811 1986 205 -363 -336 C ATOM 643 O ALEU A 78 -8.946 6.313 25.014 0.70 17.70 O ANISOU 643 O ALEU A 78 1916 2800 2008 154 -341 -275 O ATOM 644 O BLEU A 78 -8.893 6.300 25.260 0.30 17.71 O ANISOU 644 O BLEU A 78 1921 2803 2005 158 -354 -292 O ATOM 645 CB ALEU A 78 -9.050 8.636 27.275 0.70 17.90 C ANISOU 645 CB ALEU A 78 1938 2727 2135 333 -556 -552 C ATOM 646 CB BLEU A 78 -9.066 8.823 27.275 0.30 18.73 C ANISOU 646 CB BLEU A 78 2035 2820 2261 339 -564 -561 C ATOM 647 CG ALEU A 78 -8.225 9.776 27.848 0.70 19.07 C ANISOU 647 CG ALEU A 78 2032 2712 2501 400 -726 -700 C ATOM 648 CG BLEU A 78 -7.799 8.331 27.947 0.30 19.32 C ANISOU 648 CG BLEU A 78 2129 2823 2388 364 -698 -647 C ATOM 649 CD1ALEU A 78 -8.287 9.697 29.365 0.70 17.49 C ANISOU 649 CD1ALEU A 78 1977 2553 2114 562 -879 -869 C ATOM 650 CD1BLEU A 78 -6.537 8.802 27.220 0.30 16.00 C ANISOU 650 CD1BLEU A 78 1552 2204 2323 295 -731 -637 C ATOM 651 CD2ALEU A 78 -6.766 9.691 27.359 0.70 16.64 C ANISOU 651 CD2ALEU A 78 1600 2229 2492 331 -771 -691 C ATOM 652 CD2BLEU A 78 -7.839 8.875 29.364 0.30 17.13 C ANISOU 652 CD2BLEU A 78 1957 2529 2022 535 -875 -836 C ATOM 653 N PHE A 79 -11.057 6.841 25.564 1.00 15.23 N ANISOU 653 N PHE A 79 1590 2605 1591 214 -313 -331 N ATOM 654 CA PHE A 79 -11.502 5.487 25.257 1.00 15.55 C ANISOU 654 CA PHE A 79 1626 2709 1572 161 -258 -282 C ATOM 655 C PHE A 79 -11.332 5.181 23.775 1.00 16.78 C ANISOU 655 C PHE A 79 1788 2840 1748 144 -287 -225 C ATOM 656 O PHE A 79 -10.841 4.108 23.399 1.00 16.02 O ANISOU 656 O PHE A 79 1722 2748 1615 104 -279 -187 O ATOM 657 CB PHE A 79 -12.969 5.268 25.665 1.00 15.13 C ANISOU 657 CB PHE A 79 1503 2704 1540 177 -183 -304 C ATOM 658 CG PHE A 79 -13.438 3.864 25.400 1.00 18.51 C ANISOU 658 CG PHE A 79 1875 3143 2016 114 -128 -270 C ATOM 659 CD1 PHE A 79 -13.058 2.823 26.256 1.00 21.77 C ANISOU 659 CD1 PHE A 79 2346 3561 2365 95 -20 -223 C ATOM 660 CD2 PHE A 79 -14.199 3.567 24.285 1.00 18.57 C ANISOU 660 CD2 PHE A 79 1784 3128 2143 99 -213 -301 C ATOM 661 CE1 PHE A 79 -13.450 1.514 26.010 1.00 23.60 C ANISOU 661 CE1 PHE A 79 2507 3766 2695 29 43 -187 C ATOM 662 CE2 PHE A 79 -14.613 2.260 24.031 1.00 21.00 C ANISOU 662 CE2 PHE A 79 2008 3404 2566 43 -204 -307 C ATOM 663 CZ PHE A 79 -14.237 1.228 24.889 1.00 24.80 C ANISOU 663 CZ PHE A 79 2516 3879 3027 -10 -56 -239 C ATOM 664 N AILE A 80 -11.782 6.115 22.928 0.50 16.47 N ANISOU 664 N AILE A 80 1753 2769 1737 210 -322 -219 N ATOM 665 N BILE A 80 -11.721 6.097 22.894 0.50 16.56 N ANISOU 665 N BILE A 80 1768 2777 1747 210 -320 -215 N ATOM 666 CA AILE A 80 -11.580 6.053 21.481 0.50 15.05 C ANISOU 666 CA AILE A 80 1667 2546 1507 284 -341 -156 C ATOM 667 CA BILE A 80 -11.529 5.747 21.492 0.50 15.27 C ANISOU 667 CA BILE A 80 1695 2583 1524 270 -343 -157 C ATOM 668 C AILE A 80 -10.109 5.844 21.148 0.50 14.34 C ANISOU 668 C AILE A 80 1644 2380 1424 270 -247 -60 C ATOM 669 C BILE A 80 -10.070 5.873 21.064 0.50 14.40 C ANISOU 669 C BILE A 80 1659 2382 1431 276 -242 -53 C ATOM 670 O AILE A 80 -9.754 5.007 20.303 0.50 14.16 O ANISOU 670 O AILE A 80 1712 2352 1316 305 -229 -10 O ATOM 671 O BILE A 80 -9.686 5.270 20.053 0.50 14.77 O ANISOU 671 O BILE A 80 1816 2405 1391 338 -210 13 O ATOM 672 CB AILE A 80 -12.129 7.341 20.836 0.50 17.55 C ANISOU 672 CB AILE A 80 2024 2812 1831 405 -367 -145 C ATOM 673 CB BILE A 80 -12.458 6.555 20.581 0.50 18.26 C ANISOU 673 CB BILE A 80 2118 2942 1879 403 -420 -174 C ATOM 674 CG1AILE A 80 -13.657 7.399 20.967 0.50 18.34 C ANISOU 674 CG1AILE A 80 2033 2972 1965 436 -486 -257 C ATOM 675 CG1BILE A 80 -12.153 8.040 20.651 0.50 19.27 C ANISOU 675 CG1BILE A 80 2264 2990 2067 453 -354 -125 C ATOM 676 CG2AILE A 80 -11.707 7.452 19.366 0.50 18.75 C ANISOU 676 CG2AILE A 80 2364 2889 1872 557 -336 -41 C ATOM 677 CG2BILE A 80 -13.909 6.322 20.985 0.50 18.73 C ANISOU 677 CG2BILE A 80 2039 3058 2018 389 -522 -295 C ATOM 678 CD1AILE A 80 -14.372 6.400 20.066 0.50 19.46 C ANISOU 678 CD1AILE A 80 2189 3130 2074 499 -631 -322 C ATOM 679 CD1BILE A 80 -12.944 8.791 19.611 0.50 22.98 C ANISOU 679 CD1BILE A 80 2834 3425 2473 626 -423 -115 C ATOM 680 N ALA A 81 -9.231 6.592 21.821 1.00 12.93 N ANISOU 680 N ALA A 81 1406 2120 1387 231 -196 -52 N ATOM 681 CA ALA A 81 -7.801 6.543 21.537 1.00 15.48 C ANISOU 681 CA ALA A 81 1723 2316 1843 214 -93 28 C ATOM 682 C ALA A 81 -7.174 5.221 21.976 1.00 17.12 C ANISOU 682 C ALA A 81 1918 2573 2012 138 -120 4 C ATOM 683 O ALA A 81 -6.277 4.709 21.298 1.00 17.54 O ANISOU 683 O ALA A 81 2003 2559 2104 147 -23 90 O ATOM 684 CB ALA A 81 -7.088 7.715 22.220 1.00 20.81 C ANISOU 684 CB ALA A 81 2276 2844 2788 195 -92 -11 C ATOM 685 N CYS A 82 -7.615 4.660 23.111 1.00 15.55 N ANISOU 685 N CYS A 82 1694 2478 1738 88 -221 -94 N ATOM 686 CA CYS A 82 -6.896 3.579 23.781 1.00 16.07 C ANISOU 686 CA CYS A 82 1762 2561 1781 41 -253 -119 C ATOM 687 C CYS A 82 -7.479 2.189 23.540 1.00 14.74 C ANISOU 687 C CYS A 82 1647 2490 1463 9 -236 -93 C ATOM 688 O CYS A 82 -6.831 1.193 23.874 1.00 12.55 O ANISOU 688 O CYS A 82 1390 2215 1164 -22 -241 -86 O ATOM 689 CB CYS A 82 -6.858 3.828 25.305 1.00 16.81 C ANISOU 689 CB CYS A 82 1855 2670 1863 70 -359 -234 C ATOM 690 SG CYS A 82 -5.871 5.235 25.819 1.00 19.47 S ANISOU 690 SG CYS A 82 2096 2838 2463 118 -478 -342 S ATOM 691 N PHE A 83 -8.694 2.074 23.020 1.00 13.54 N ANISOU 691 N PHE A 83 1499 2396 1251 23 -239 -97 N ATOM 692 CA PHE A 83 -9.251 0.732 22.890 1.00 14.46 C ANISOU 692 CA PHE A 83 1613 2553 1327 -15 -247 -103 C ATOM 693 C PHE A 83 -8.375 -0.165 22.000 1.00 15.59 C ANISOU 693 C PHE A 83 1824 2665 1435 -12 -245 -60 C ATOM 694 O PHE A 83 -8.274 -1.371 22.242 1.00 15.12 O ANISOU 694 O PHE A 83 1763 2614 1367 -61 -244 -61 O ATOM 695 CB PHE A 83 -10.673 0.800 22.342 1.00 14.67 C ANISOU 695 CB PHE A 83 1582 2596 1395 14 -304 -158 C ATOM 696 CG PHE A 83 -11.312 -0.537 22.229 1.00 18.28 C ANISOU 696 CG PHE A 83 1976 3041 1930 -31 -331 -195 C ATOM 697 CD1 PHE A 83 -11.639 -1.271 23.390 1.00 21.34 C ANISOU 697 CD1 PHE A 83 2293 3422 2392 -102 -211 -171 C ATOM 698 CD2 PHE A 83 -11.571 -1.093 20.979 1.00 16.78 C ANISOU 698 CD2 PHE A 83 1814 2817 1745 29 -469 -254 C ATOM 699 CE1 PHE A 83 -12.224 -2.536 23.294 1.00 20.31 C ANISOU 699 CE1 PHE A 83 2067 3230 2420 -154 -199 -190 C ATOM 700 CE2 PHE A 83 -12.153 -2.344 20.882 1.00 20.36 C ANISOU 700 CE2 PHE A 83 2172 3218 2346 -15 -529 -321 C ATOM 701 CZ PHE A 83 -12.478 -3.074 22.036 1.00 20.27 C ANISOU 701 CZ PHE A 83 2036 3178 2488 -128 -379 -282 C ATOM 702 N VAL A 84 -7.719 0.402 20.978 1.00 14.93 N ANISOU 702 N VAL A 84 1814 2526 1334 64 -210 -4 N ATOM 703 CA VAL A 84 -6.841 -0.413 20.135 1.00 14.16 C ANISOU 703 CA VAL A 84 1806 2386 1189 103 -161 52 C ATOM 704 C VAL A 84 -5.686 -1.003 20.945 1.00 14.52 C ANISOU 704 C VAL A 84 1793 2404 1319 18 -120 70 C ATOM 705 O VAL A 84 -5.150 -2.071 20.600 1.00 11.94 O ANISOU 705 O VAL A 84 1511 2066 961 15 -104 89 O ATOM 706 CB VAL A 84 -6.321 0.420 18.945 1.00 12.23 C ANISOU 706 CB VAL A 84 1681 2055 912 247 -41 152 C ATOM 707 CG1 VAL A 84 -5.435 1.570 19.435 1.00 13.61 C ANISOU 707 CG1 VAL A 84 1754 2126 1292 211 83 215 C ATOM 708 CG2 VAL A 84 -5.557 -0.474 17.930 1.00 12.89 C ANISOU 708 CG2 VAL A 84 1909 2092 898 346 45 218 C ATOM 709 N LEU A 85 -5.265 -0.313 22.019 1.00 12.95 N ANISOU 709 N LEU A 85 1508 2181 1233 -25 -136 41 N ATOM 710 CA LEU A 85 -4.206 -0.845 22.875 1.00 14.35 C ANISOU 710 CA LEU A 85 1642 2318 1492 -61 -172 15 C ATOM 711 C LEU A 85 -4.660 -2.102 23.616 1.00 13.81 C ANISOU 711 C LEU A 85 1626 2330 1290 -94 -221 -10 C ATOM 712 O LEU A 85 -3.841 -2.982 23.928 1.00 14.36 O ANISOU 712 O LEU A 85 1712 2374 1371 -102 -242 -8 O ATOM 713 CB LEU A 85 -3.770 0.238 23.863 1.00 13.80 C ANISOU 713 CB LEU A 85 1491 2183 1568 -45 -255 -64 C ATOM 714 CG LEU A 85 -3.326 1.584 23.255 1.00 15.72 C ANISOU 714 CG LEU A 85 1641 2293 2038 -23 -183 -34 C ATOM 715 CD1 LEU A 85 -2.872 2.553 24.359 1.00 16.85 C ANISOU 715 CD1 LEU A 85 1678 2341 2383 -2 -335 -168 C ATOM 716 CD2 LEU A 85 -2.191 1.377 22.203 1.00 14.83 C ANISOU 716 CD2 LEU A 85 1485 2041 2110 -14 -14 76 C ATOM 717 N VAL A 86 -5.948 -2.176 23.948 1.00 11.86 N ANISOU 717 N VAL A 86 1392 2155 959 -103 -216 -26 N ATOM 718 CA VAL A 86 -6.515 -3.390 24.537 1.00 13.49 C ANISOU 718 CA VAL A 86 1628 2390 1107 -130 -183 -11 C ATOM 719 C VAL A 86 -6.377 -4.557 23.569 1.00 14.33 C ANISOU 719 C VAL A 86 1741 2474 1231 -166 -183 10 C ATOM 720 O VAL A 86 -5.994 -5.668 23.951 1.00 14.59 O ANISOU 720 O VAL A 86 1806 2485 1252 -186 -164 35 O ATOM 721 CB VAL A 86 -7.999 -3.174 24.883 1.00 14.17 C ANISOU 721 CB VAL A 86 1668 2507 1209 -135 -124 -20 C ATOM 722 CG1 VAL A 86 -8.614 -4.479 25.392 1.00 14.82 C ANISOU 722 CG1 VAL A 86 1743 2558 1330 -167 -18 26 C ATOM 723 CG2 VAL A 86 -8.187 -2.014 25.854 1.00 13.95 C ANISOU 723 CG2 VAL A 86 1665 2503 1132 -68 -117 -48 C ATOM 724 N LEU A 87 -6.739 -4.328 22.303 1.00 10.35 N ANISOU 724 N LEU A 87 1233 1965 735 -141 -217 -10 N ATOM 725 CA LEU A 87 -6.694 -5.411 21.324 1.00 10.65 C ANISOU 725 CA LEU A 87 1312 1971 762 -125 -260 -27 C ATOM 726 C LEU A 87 -5.253 -5.821 21.023 1.00 16.03 C ANISOU 726 C LEU A 87 2061 2619 1412 -102 -212 26 C ATOM 727 O LEU A 87 -4.965 -7.006 20.795 1.00 16.47 O ANISOU 727 O LEU A 87 2148 2648 1463 -112 -228 21 O ATOM 728 CB LEU A 87 -7.398 -4.960 20.045 1.00 12.18 C ANISOU 728 CB LEU A 87 1553 2159 914 -22 -349 -84 C ATOM 729 CG LEU A 87 -8.853 -4.486 20.181 1.00 13.11 C ANISOU 729 CG LEU A 87 1570 2289 1123 -27 -431 -164 C ATOM 730 CD1 LEU A 87 -9.431 -4.080 18.798 1.00 13.97 C ANISOU 730 CD1 LEU A 87 1774 2378 1157 137 -587 -249 C ATOM 731 CD2 LEU A 87 -9.710 -5.556 20.845 1.00 13.86 C ANISOU 731 CD2 LEU A 87 1520 2338 1408 -127 -436 -210 C ATOM 732 N ALA A 88 -4.337 -4.852 20.986 1.00 13.81 N ANISOU 732 N ALA A 88 1776 2309 1162 -70 -146 73 N ATOM 733 CA ALA A 88 -2.937 -5.203 20.779 1.00 14.61 C ANISOU 733 CA ALA A 88 1882 2339 1330 -52 -76 122 C ATOM 734 C ALA A 88 -2.405 -5.988 21.968 1.00 15.70 C ANISOU 734 C ALA A 88 1977 2475 1512 -115 -138 95 C ATOM 735 O ALA A 88 -1.642 -6.954 21.797 1.00 14.88 O ANISOU 735 O ALA A 88 1892 2333 1427 -112 -126 111 O ATOM 736 CB ALA A 88 -2.090 -3.940 20.553 1.00 12.37 C ANISOU 736 CB ALA A 88 1538 1964 1199 -12 31 175 C ATOM 737 N GLN A 89 -2.781 -5.579 23.184 1.00 14.31 N ANISOU 737 N GLN A 89 1777 2333 1327 -135 -203 56 N ATOM 738 CA GLN A 89 -2.334 -6.311 24.367 1.00 13.39 C ANISOU 738 CA GLN A 89 1697 2209 1182 -122 -269 36 C ATOM 739 C GLN A 89 -2.899 -7.720 24.391 1.00 12.62 C ANISOU 739 C GLN A 89 1665 2129 1001 -154 -226 76 C ATOM 740 O GLN A 89 -2.192 -8.671 24.741 1.00 15.29 O ANISOU 740 O GLN A 89 2047 2430 1331 -136 -248 90 O ATOM 741 CB GLN A 89 -2.739 -5.584 25.645 1.00 12.01 C ANISOU 741 CB GLN A 89 1560 2062 942 -65 -332 -12 C ATOM 742 CG GLN A 89 -1.873 -6.039 26.832 1.00 14.27 C ANISOU 742 CG GLN A 89 1934 2308 1181 37 -456 -61 C ATOM 743 CD GLN A 89 -0.398 -5.754 26.556 1.00 19.24 C ANISOU 743 CD GLN A 89 2443 2829 2037 51 -577 -135 C ATOM 744 OE1 GLN A 89 -0.058 -4.672 26.084 1.00 18.70 O ANISOU 744 OE1 GLN A 89 2236 2699 2169 27 -583 -171 O ATOM 745 NE2 GLN A 89 0.484 -6.727 26.853 1.00 19.64 N ANISOU 745 NE2 GLN A 89 2527 2830 2106 96 -655 -151 N ATOM 746 N SER A 90 -4.190 -7.868 24.062 1.00 12.60 N ANISOU 746 N SER A 90 1646 2156 986 -194 -175 85 N ATOM 747 CA SER A 90 -4.777 -9.203 23.980 1.00 16.16 C ANISOU 747 CA SER A 90 2101 2567 1471 -237 -134 107 C ATOM 748 C SER A 90 -4.023 -10.069 22.979 1.00 16.82 C ANISOU 748 C SER A 90 2204 2611 1574 -237 -178 92 C ATOM 749 O SER A 90 -3.778 -11.251 23.237 1.00 16.31 O ANISOU 749 O SER A 90 2169 2494 1533 -252 -162 117 O ATOM 750 CB SER A 90 -6.260 -9.114 23.587 1.00 14.89 C ANISOU 750 CB SER A 90 1848 2396 1412 -277 -117 74 C ATOM 751 OG SER A 90 -6.839 -10.416 23.515 1.00 18.08 O ANISOU 751 OG SER A 90 2201 2707 1962 -327 -85 75 O ATOM 752 N SER A 91 -3.673 -9.499 21.818 1.00 16.92 N ANISOU 752 N SER A 91 2228 2635 1567 -192 -206 64 N ATOM 753 CA SER A 91 -2.896 -10.227 20.808 1.00 14.11 C ANISOU 753 CA SER A 91 1933 2235 1192 -140 -208 59 C ATOM 754 C SER A 91 -1.567 -10.711 21.380 1.00 15.96 C ANISOU 754 C SER A 91 2165 2432 1467 -143 -177 101 C ATOM 755 O SER A 91 -1.159 -11.859 21.171 1.00 16.42 O ANISOU 755 O SER A 91 2260 2446 1532 -138 -185 100 O ATOM 756 CB SER A 91 -2.635 -9.319 19.597 1.00 13.64 C ANISOU 756 CB SER A 91 1938 2175 1068 -30 -165 68 C ATOM 757 OG SER A 91 -3.847 -8.879 18.982 1.00 14.36 O ANISOU 757 OG SER A 91 2061 2294 1100 19 -245 5 O ATOM 758 N ILE A 92 -0.871 -9.826 22.089 1.00 14.85 N ANISOU 758 N ILE A 92 1971 2288 1384 -138 -172 115 N ATOM 759 CA AILE A 92 0.410 -10.168 22.707 0.46 16.40 C ANISOU 759 CA AILE A 92 2134 2422 1674 -116 -208 112 C ATOM 760 CA BILE A 92 0.410 -10.191 22.680 0.54 16.39 C ANISOU 760 CA BILE A 92 2134 2421 1672 -116 -206 112 C ATOM 761 C ILE A 92 0.250 -11.356 23.654 1.00 17.77 C ANISOU 761 C ILE A 92 2384 2596 1770 -121 -266 117 C ATOM 762 O ILE A 92 1.066 -12.289 23.661 1.00 16.70 O ANISOU 762 O ILE A 92 2267 2406 1672 -98 -288 122 O ATOM 763 CB AILE A 92 0.981 -8.939 23.438 0.46 16.65 C ANISOU 763 CB AILE A 92 2074 2421 1832 -90 -273 68 C ATOM 764 CB BILE A 92 1.036 -8.960 23.351 0.54 16.72 C ANISOU 764 CB BILE A 92 2079 2425 1849 -90 -265 71 C ATOM 765 CG1AILE A 92 1.671 -7.993 22.447 0.46 17.77 C ANISOU 765 CG1AILE A 92 2105 2479 2169 -74 -154 96 C ATOM 766 CG1BILE A 92 1.468 -7.962 22.271 0.54 17.34 C ANISOU 766 CG1BILE A 92 2068 2439 2082 -76 -133 107 C ATOM 767 CG2AILE A 92 1.924 -9.361 24.565 0.46 16.80 C ANISOU 767 CG2AILE A 92 2087 2381 1917 -32 -426 5 C ATOM 768 CG2BILE A 92 2.191 -9.369 24.252 0.54 17.17 C ANISOU 768 CG2BILE A 92 2099 2403 2021 -37 -400 11 C ATOM 769 CD1AILE A 92 3.073 -8.427 22.076 0.46 18.80 C ANISOU 769 CD1AILE A 92 2138 2479 2525 -42 -95 109 C ATOM 770 CD1BILE A 92 1.815 -6.625 22.815 0.54 17.55 C ANISOU 770 CD1BILE A 92 1966 2400 2303 -69 -183 58 C ATOM 771 N PHE A 93 -0.795 -11.328 24.488 1.00 14.30 N ANISOU 771 N PHE A 93 2000 2200 1234 -131 -258 135 N ATOM 772 CA PHE A 93 -1.048 -12.446 25.399 1.00 16.00 C ANISOU 772 CA PHE A 93 2320 2382 1378 -106 -232 189 C ATOM 773 C PHE A 93 -1.332 -13.738 24.631 1.00 17.43 C ANISOU 773 C PHE A 93 2489 2507 1625 -169 -178 213 C ATOM 774 O PHE A 93 -0.836 -14.810 25.002 1.00 17.42 O ANISOU 774 O PHE A 93 2555 2443 1621 -140 -176 250 O ATOM 775 CB PHE A 93 -2.222 -12.128 26.336 1.00 18.48 C ANISOU 775 CB PHE A 93 2695 2720 1608 -84 -139 239 C ATOM 776 CG PHE A 93 -1.872 -11.188 27.474 1.00 22.34 C ANISOU 776 CG PHE A 93 3281 3240 1968 49 -220 206 C ATOM 777 CD1 PHE A 93 -2.681 -10.107 27.774 1.00 17.89 C ANISOU 777 CD1 PHE A 93 2705 2728 1363 62 -184 191 C ATOM 778 CD2 PHE A 93 -0.751 -11.415 28.265 1.00 29.09 C ANISOU 778 CD2 PHE A 93 4247 4055 2749 190 -368 164 C ATOM 779 CE1 PHE A 93 -2.374 -9.244 28.808 1.00 20.83 C ANISOU 779 CE1 PHE A 93 3187 3116 1610 214 -292 130 C ATOM 780 CE2 PHE A 93 -0.434 -10.548 29.328 1.00 30.04 C ANISOU 780 CE2 PHE A 93 4468 4179 2768 354 -510 81 C ATOM 781 CZ PHE A 93 -1.256 -9.455 29.586 1.00 25.29 C ANISOU 781 CZ PHE A 93 3849 3624 2135 355 -460 62 C ATOM 782 N SER A 94 -2.147 -13.665 23.570 1.00 14.04 N ANISOU 782 N SER A 94 1989 2085 1262 -230 -166 173 N ATOM 783 CA SER A 94 -2.415 -14.867 22.782 1.00 18.67 C ANISOU 783 CA SER A 94 2563 2594 1938 -261 -181 143 C ATOM 784 C SER A 94 -1.138 -15.405 22.132 1.00 18.36 C ANISOU 784 C SER A 94 2571 2533 1872 -208 -222 124 C ATOM 785 O SER A 94 -0.888 -16.620 22.148 1.00 17.80 O ANISOU 785 O SER A 94 2530 2384 1851 -212 -227 131 O ATOM 786 CB SER A 94 -3.470 -14.574 21.718 1.00 18.91 C ANISOU 786 CB SER A 94 2529 2622 2034 -275 -246 48 C ATOM 787 OG SER A 94 -4.725 -14.292 22.326 1.00 21.12 O ANISOU 787 OG SER A 94 2718 2883 2425 -334 -193 61 O ATOM 788 N LEU A 95 -0.326 -14.514 21.555 1.00 16.06 N ANISOU 788 N LEU A 95 2277 2286 1540 -154 -218 111 N ATOM 789 CA LEU A 95 0.925 -14.930 20.913 1.00 15.90 C ANISOU 789 CA LEU A 95 2278 2220 1543 -88 -193 112 C ATOM 790 C LEU A 95 1.853 -15.600 21.911 1.00 18.15 C ANISOU 790 C LEU A 95 2554 2457 1884 -86 -226 140 C ATOM 791 O LEU A 95 2.465 -16.629 21.603 1.00 19.52 O ANISOU 791 O LEU A 95 2757 2570 2091 -57 -227 136 O ATOM 792 CB LEU A 95 1.622 -13.721 20.280 1.00 16.31 C ANISOU 792 CB LEU A 95 2295 2279 1624 -26 -104 134 C ATOM 793 CG LEU A 95 0.912 -13.145 19.050 1.00 16.28 C ANISOU 793 CG LEU A 95 2374 2304 1508 49 -58 120 C ATOM 794 CD1 LEU A 95 1.466 -11.740 18.686 1.00 16.03 C ANISOU 794 CD1 LEU A 95 2304 2256 1532 106 87 187 C ATOM 795 CD2 LEU A 95 1.045 -14.117 17.862 1.00 14.70 C ANISOU 795 CD2 LEU A 95 2314 2059 1212 169 -50 83 C ATOM 796 N LEU A 96 1.955 -15.040 23.117 1.00 15.83 N ANISOU 796 N LEU A 96 2247 2184 1585 -82 -277 152 N ATOM 797 CA LEU A 96 2.809 -15.622 24.146 1.00 18.66 C ANISOU 797 CA LEU A 96 2645 2489 1957 -17 -366 154 C ATOM 798 C LEU A 96 2.270 -16.972 24.608 1.00 20.72 C ANISOU 798 C LEU A 96 3023 2707 2143 -21 -335 216 C ATOM 799 O LEU A 96 3.041 -17.900 24.869 1.00 22.12 O ANISOU 799 O LEU A 96 3248 2816 2341 35 -380 224 O ATOM 800 CB LEU A 96 2.937 -14.649 25.327 1.00 18.61 C ANISOU 800 CB LEU A 96 2652 2504 1915 53 -474 120 C ATOM 801 CG LEU A 96 3.822 -15.060 26.515 1.00 26.87 C ANISOU 801 CG LEU A 96 3788 3489 2934 199 -647 79 C ATOM 802 CD1 LEU A 96 5.242 -15.389 26.057 1.00 28.25 C ANISOU 802 CD1 LEU A 96 3829 3568 3336 227 -733 11 C ATOM 803 CD2 LEU A 96 3.837 -13.968 27.637 1.00 26.28 C ANISOU 803 CD2 LEU A 96 3765 3429 2790 322 -810 -3 C ATOM 804 N ALA A 97 0.948 -17.099 24.709 1.00 17.72 N ANISOU 804 N ALA A 97 2668 2337 1727 -83 -243 262 N ATOM 805 CA ALA A 97 0.357 -18.376 25.094 1.00 18.30 C ANISOU 805 CA ALA A 97 2810 2312 1831 -99 -156 340 C ATOM 806 C ALA A 97 0.631 -19.444 24.047 1.00 19.89 C ANISOU 806 C ALA A 97 2970 2440 2148 -139 -183 292 C ATOM 807 O ALA A 97 0.910 -20.596 24.383 1.00 21.79 O ANISOU 807 O ALA A 97 3274 2580 2427 -115 -161 341 O ATOM 808 CB ALA A 97 -1.146 -18.213 25.303 1.00 17.08 C ANISOU 808 CB ALA A 97 2616 2137 1738 -169 -25 388 C ATOM 809 N ILE A 98 0.549 -19.077 22.769 1.00 19.64 N ANISOU 809 N ILE A 98 2866 2447 2149 -167 -229 196 N ATOM 810 CA ILE A 98 0.816 -20.030 21.696 1.00 17.98 C ANISOU 810 CA ILE A 98 2664 2168 2001 -150 -275 123 C ATOM 811 C ILE A 98 2.264 -20.514 21.755 1.00 21.20 C ANISOU 811 C ILE A 98 3112 2552 2392 -76 -286 140 C ATOM 812 O ILE A 98 2.535 -21.709 21.596 1.00 22.71 O ANISOU 812 O ILE A 98 3339 2648 2643 -60 -303 131 O ATOM 813 CB ILE A 98 0.471 -19.390 20.335 1.00 17.61 C ANISOU 813 CB ILE A 98 2612 2170 1909 -110 -323 19 C ATOM 814 CG1 ILE A 98 -1.054 -19.244 20.216 1.00 17.55 C ANISOU 814 CG1 ILE A 98 2538 2137 1992 -173 -375 -41 C ATOM 815 CG2 ILE A 98 1.049 -20.240 19.185 1.00 18.12 C ANISOU 815 CG2 ILE A 98 2755 2174 1955 -10 -369 -63 C ATOM 816 CD1 ILE A 98 -1.584 -18.329 19.047 1.00 18.79 C ANISOU 816 CD1 ILE A 98 2723 2358 2059 -92 -461 -150 C ATOM 817 N ALA A 99 3.214 -19.601 22.002 1.00 20.22 N ANISOU 817 N ALA A 99 2954 2485 2243 -28 -286 153 N ATOM 818 CA ALA A 99 4.619 -19.999 22.110 1.00 19.86 C ANISOU 818 CA ALA A 99 2890 2386 2270 46 -312 149 C ATOM 819 C ALA A 99 4.816 -20.979 23.257 1.00 21.86 C ANISOU 819 C ALA A 99 3224 2572 2511 77 -379 194 C ATOM 820 O ALA A 99 5.453 -22.033 23.103 1.00 20.85 O ANISOU 820 O ALA A 99 3123 2362 2437 118 -398 190 O ATOM 821 CB ALA A 99 5.504 -18.765 22.326 1.00 16.19 C ANISOU 821 CB ALA A 99 2313 1943 1897 84 -324 131 C ATOM 822 N ILE A 100 4.281 -20.630 24.428 1.00 19.76 N ANISOU 822 N ILE A 100 3028 2330 2151 91 -400 247 N ATOM 823 CA ILE A 100 4.426 -21.479 25.605 1.00 21.96 C ANISOU 823 CA ILE A 100 3458 2533 2352 187 -430 321 C ATOM 824 C ILE A 100 3.761 -22.827 25.373 1.00 21.09 C ANISOU 824 C ILE A 100 3401 2316 2297 131 -315 393 C ATOM 825 O ILE A 100 4.321 -23.875 25.712 1.00 22.27 O ANISOU 825 O ILE A 100 3637 2366 2458 205 -336 432 O ATOM 826 CB ILE A 100 3.859 -20.765 26.850 1.00 21.38 C ANISOU 826 CB ILE A 100 3511 2502 2112 269 -427 378 C ATOM 827 CG1 ILE A 100 4.714 -19.534 27.175 1.00 26.56 C ANISOU 827 CG1 ILE A 100 4105 3219 2769 354 -615 261 C ATOM 828 CG2 ILE A 100 3.813 -21.716 28.063 1.00 22.21 C ANISOU 828 CG2 ILE A 100 3860 2509 2071 427 -389 500 C ATOM 829 CD1 ILE A 100 4.134 -18.634 28.269 1.00 28.69 C ANISOU 829 CD1 ILE A 100 4506 3541 2855 458 -644 275 C ATOM 830 N ASP A 101 2.560 -22.823 24.786 1.00 19.17 N ANISOU 830 N ASP A 101 3087 2064 2133 8 -214 395 N ATOM 831 CA ASP A 101 1.883 -24.080 24.488 1.00 22.51 C ANISOU 831 CA ASP A 101 3498 2334 2721 -55 -136 423 C ATOM 832 C ASP A 101 2.752 -24.996 23.630 1.00 23.54 C ANISOU 832 C ASP A 101 3618 2406 2922 -32 -228 339 C ATOM 833 O ASP A 101 2.839 -26.206 23.885 1.00 22.73 O ANISOU 833 O ASP A 101 3567 2156 2913 -15 -195 390 O ATOM 834 CB ASP A 101 0.552 -23.802 23.790 1.00 25.65 C ANISOU 834 CB ASP A 101 3762 2713 3270 -176 -101 362 C ATOM 835 CG ASP A 101 -0.140 -25.071 23.361 1.00 32.86 C ANISOU 835 CG ASP A 101 4601 3422 4462 -244 -78 332 C ATOM 836 OD1 ASP A 101 -0.734 -25.741 24.233 1.00 34.28 O ANISOU 836 OD1 ASP A 101 4791 3440 4794 -265 99 475 O ATOM 837 OD2 ASP A 101 -0.069 -25.415 22.157 1.00 34.68 O ANISOU 837 OD2 ASP A 101 4777 3629 4771 -249 -229 167 O ATOM 838 N ARG A 102 3.408 -24.441 22.607 1.00 23.72 N ANISOU 838 N ARG A 102 3585 2523 2906 -10 -310 224 N ATOM 839 CA ARG A 102 4.230 -25.281 21.747 1.00 22.90 C ANISOU 839 CA ARG A 102 3491 2358 2851 46 -358 149 C ATOM 840 C ARG A 102 5.509 -25.715 22.455 1.00 24.22 C ANISOU 840 C ARG A 102 3700 2492 3011 138 -389 199 C ATOM 841 O ARG A 102 6.030 -26.798 22.164 1.00 25.02 O ANISOU 841 O ARG A 102 3832 2493 3183 181 -411 177 O ATOM 842 CB ARG A 102 4.538 -24.561 20.427 1.00 25.46 C ANISOU 842 CB ARG A 102 3789 2767 3118 96 -363 46 C ATOM 843 CG ARG A 102 3.315 -24.334 19.487 1.00 31.02 C ANISOU 843 CG ARG A 102 4496 3479 3810 72 -407 -55 C ATOM 844 CD ARG A 102 2.694 -25.656 18.962 1.00 37.87 C ANISOU 844 CD ARG A 102 5383 4189 4815 71 -509 -163 C ATOM 845 NE ARG A 102 1.777 -26.261 19.938 1.00 40.71 N ANISOU 845 NE ARG A 102 5665 4425 5378 -57 -485 -95 N ATOM 846 CZ ARG A 102 1.526 -27.561 20.047 1.00 39.29 C ANISOU 846 CZ ARG A 102 5464 4051 5412 -86 -508 -112 C ATOM 847 NH1 ARG A 102 2.118 -28.425 19.240 1.00 39.86 N ANISOU 847 NH1 ARG A 102 5597 4051 5498 3 -607 -225 N ATOM 848 NH2 ARG A 102 0.678 -27.999 20.967 1.00 39.92 N ANISOU 848 NH2 ARG A 102 5466 3989 5712 -190 -402 -4 N ATOM 849 N TYR A 103 6.012 -24.909 23.399 1.00 25.53 N ANISOU 849 N TYR A 103 3869 2722 3109 189 -428 240 N ATOM 850 CA TYR A 103 7.166 -25.334 24.192 1.00 26.60 C ANISOU 850 CA TYR A 103 4051 2800 3257 314 -531 252 C ATOM 851 C TYR A 103 6.815 -26.512 25.098 1.00 26.35 C ANISOU 851 C TYR A 103 4190 2650 3172 367 -509 363 C ATOM 852 O TYR A 103 7.570 -27.489 25.184 1.00 27.55 O ANISOU 852 O TYR A 103 4390 2703 3375 448 -563 364 O ATOM 853 CB TYR A 103 7.725 -24.175 25.030 1.00 24.93 C ANISOU 853 CB TYR A 103 3809 2654 3011 396 -651 221 C ATOM 854 CG TYR A 103 8.882 -24.618 25.901 1.00 30.64 C ANISOU 854 CG TYR A 103 4583 3293 3764 570 -839 187 C ATOM 855 CD1 TYR A 103 10.118 -24.912 25.342 1.00 31.36 C ANISOU 855 CD1 TYR A 103 4526 3316 4073 613 -905 98 C ATOM 856 CD2 TYR A 103 8.723 -24.795 27.275 1.00 36.08 C ANISOU 856 CD2 TYR A 103 5496 3953 4260 728 -942 245 C ATOM 857 CE1 TYR A 103 11.176 -25.349 26.127 1.00 36.98 C ANISOU 857 CE1 TYR A 103 5263 3931 4856 787 -1121 38 C ATOM 858 CE2 TYR A 103 9.774 -25.237 28.072 1.00 39.09 C ANISOU 858 CE2 TYR A 103 5966 4246 4640 941 -1170 189 C ATOM 859 CZ TYR A 103 11.000 -25.508 27.488 1.00 41.22 C ANISOU 859 CZ TYR A 103 6039 4447 5176 957 -1284 71 C ATOM 860 OH TYR A 103 12.053 -25.949 28.262 1.00 46.78 O ANISOU 860 OH TYR A 103 6804 5046 5925 1181 -1554 -14 O ATOM 861 N ILE A 104 5.682 -26.437 25.795 1.00 28.06 N ANISOU 861 N ILE A 104 4505 2853 3305 338 -395 475 N ATOM 862 CA ILE A 104 5.268 -27.567 26.628 1.00 29.29 C ANISOU 862 CA ILE A 104 4834 2850 3445 402 -280 630 C ATOM 863 C ILE A 104 5.107 -28.824 25.779 1.00 30.53 C ANISOU 863 C ILE A 104 4921 2863 3817 310 -229 609 C ATOM 864 O ILE A 104 5.469 -29.932 26.201 1.00 31.26 O ANISOU 864 O ILE A 104 5127 2808 3941 396 -206 689 O ATOM 865 CB ILE A 104 3.971 -27.229 27.381 1.00 31.22 C ANISOU 865 CB ILE A 104 5160 3071 3631 382 -75 775 C ATOM 866 CG1 ILE A 104 4.186 -26.035 28.315 1.00 28.04 C ANISOU 866 CG1 ILE A 104 4878 2801 2974 525 -154 780 C ATOM 867 CG2 ILE A 104 3.481 -28.452 28.164 1.00 36.59 C ANISOU 867 CG2 ILE A 104 6011 3533 4357 455 144 981 C ATOM 868 CD1 ILE A 104 2.893 -25.399 28.805 1.00 28.75 C ANISOU 868 CD1 ILE A 104 5003 2908 3012 489 56 889 C ATOM 869 N ALA A 105 4.584 -28.667 24.562 1.00 27.34 N ANISOU 869 N ALA A 105 4349 2485 3553 168 -237 486 N ATOM 870 CA ALA A 105 4.321 -29.822 23.706 1.00 30.08 C ANISOU 870 CA ALA A 105 4636 2676 4116 107 -242 416 C ATOM 871 C ALA A 105 5.606 -30.538 23.284 1.00 31.93 C ANISOU 871 C ALA A 105 4905 2885 4343 204 -350 347 C ATOM 872 O ALA A 105 5.619 -31.762 23.169 1.00 35.50 O ANISOU 872 O ALA A 105 5384 3162 4942 211 -342 353 O ATOM 873 CB ALA A 105 3.521 -29.384 22.478 1.00 29.91 C ANISOU 873 CB ALA A 105 4477 2696 4191 6 -301 254 C ATOM 874 N AILE A 106 6.688 -29.791 23.055 0.70 32.40 N ANISOU 874 N AILE A 106 4939 3087 4284 280 -435 281 N ATOM 875 N BILE A 106 6.686 -29.804 23.032 0.30 32.33 N ANISOU 875 N BILE A 106 4929 3077 4279 279 -435 279 N ATOM 876 CA AILE A 106 7.944 -30.393 22.611 0.70 33.25 C ANISOU 876 CA AILE A 106 5040 3156 4438 379 -506 213 C ATOM 877 CA BILE A 106 7.937 -30.452 22.633 0.30 33.30 C ANISOU 877 CA BILE A 106 5050 3155 4448 380 -506 217 C ATOM 878 C AILE A 106 8.831 -30.823 23.781 0.70 34.21 C ANISOU 878 C AILE A 106 5255 3217 4527 510 -577 297 C ATOM 879 C BILE A 106 8.730 -30.932 23.842 0.30 34.15 C ANISOU 879 C BILE A 106 5261 3194 4520 506 -569 309 C ATOM 880 O AILE A 106 9.647 -31.740 23.635 0.70 35.38 O ANISOU 880 O AILE A 106 5420 3267 4755 591 -629 270 O ATOM 881 O BILE A 106 9.387 -31.973 23.785 0.30 35.63 O ANISOU 881 O BILE A 106 5488 3265 4785 581 -609 301 O ATOM 882 CB AILE A 106 8.702 -29.421 21.686 0.70 33.17 C ANISOU 882 CB AILE A 106 4919 3272 4413 412 -508 110 C ATOM 883 CB BILE A 106 8.799 -29.511 21.766 0.30 33.33 C ANISOU 883 CB BILE A 106 4943 3282 4439 422 -515 115 C ATOM 884 CG1AILE A 106 9.870 -30.127 20.997 0.70 35.09 C ANISOU 884 CG1AILE A 106 5136 3445 4751 519 -514 41 C ATOM 885 CG1BILE A 106 9.004 -28.185 22.482 0.30 33.25 C ANISOU 885 CG1BILE A 106 4875 3388 4369 426 -541 146 C ATOM 886 CG2AILE A 106 9.245 -28.243 22.467 0.70 33.33 C ANISOU 886 CG2AILE A 106 4875 3389 4398 445 -551 138 C ATOM 887 CG2BILE A 106 8.191 -29.285 20.406 0.30 33.42 C ANISOU 887 CG2BILE A 106 4938 3332 4429 388 -461 17 C ATOM 888 CD1AILE A 106 9.797 -30.090 19.498 0.70 39.01 C ANISOU 888 CD1AILE A 106 5638 3959 5226 556 -432 -60 C ATOM 889 CD1BILE A 106 10.382 -27.696 22.369 0.30 34.42 C ANISOU 889 CD1BILE A 106 4895 3543 4641 519 -584 88 C ATOM 890 N ALA A 107 8.708 -30.170 24.934 1.00 33.35 N ANISOU 890 N ALA A 107 5229 3158 4284 568 -605 381 N ATOM 891 CA ALA A 107 9.586 -30.458 26.057 1.00 38.93 C ANISOU 891 CA ALA A 107 6071 3809 4910 764 -742 422 C ATOM 892 C ALA A 107 9.045 -31.588 26.917 1.00 44.34 C ANISOU 892 C ALA A 107 6993 4334 5522 843 -639 597 C ATOM 893 O ALA A 107 9.816 -32.432 27.390 1.00 48.51 O ANISOU 893 O ALA A 107 7643 4752 6038 1005 -731 624 O ATOM 894 CB ALA A 107 9.790 -29.196 26.899 1.00 38.18 C ANISOU 894 CB ALA A 107 6000 3826 4681 860 -869 394 C ATOM 895 N ILE A 108 7.733 -31.637 27.115 1.00 41.33 N ANISOU 895 N ILE A 108 6666 3909 5130 743 -426 728 N ATOM 896 CA ILE A 108 7.147 -32.696 27.932 1.00 42.91 C ANISOU 896 CA ILE A 108 7074 3903 5325 821 -234 939 C ATOM 897 C ILE A 108 5.903 -33.254 27.250 1.00 37.72 C ANISOU 897 C ILE A 108 6270 3107 4955 601 -17 979 C ATOM 898 O ILE A 108 4.791 -33.128 27.784 1.00 37.64 O ANISOU 898 O ILE A 108 6298 3015 4987 561 220 1134 O ATOM 899 CB ILE A 108 6.837 -32.181 29.344 1.00 47.45 C ANISOU 899 CB ILE A 108 7899 4510 5618 1010 -149 1096 C ATOM 900 CG1 ILE A 108 6.221 -30.783 29.281 1.00 42.96 C ANISOU 900 CG1 ILE A 108 7254 4105 4963 929 -141 1052 C ATOM 901 CG2 ILE A 108 8.113 -32.167 30.182 1.00 53.70 C ANISOU 901 CG2 ILE A 108 8808 5394 6202 1250 -395 1005 C ATOM 902 CD1 ILE A 108 5.709 -30.290 30.618 1.00 45.12 C ANISOU 902 CD1 ILE A 108 7698 4456 4991 1072 -10 1153 C ATOM 903 N PRO A 109 6.043 -33.892 26.085 1.00 48.98 N ANISOU 903 N PRO A 109 6910 5310 6390 395 -411 1346 N ATOM 904 CA PRO A 109 4.856 -34.411 25.389 1.00 46.52 C ANISOU 904 CA PRO A 109 6762 4586 6329 234 -127 1305 C ATOM 905 C PRO A 109 4.076 -35.449 26.183 1.00 51.06 C ANISOU 905 C PRO A 109 7596 4825 6980 366 107 1619 C ATOM 906 O PRO A 109 2.881 -35.631 25.921 1.00 51.07 O ANISOU 906 O PRO A 109 7686 4501 7219 166 343 1536 O ATOM 907 CB PRO A 109 5.439 -35.012 24.104 1.00 46.78 C ANISOU 907 CB PRO A 109 6639 4466 6669 320 -79 1145 C ATOM 908 CG PRO A 109 6.876 -35.300 24.433 1.00 49.75 C ANISOU 908 CG PRO A 109 6814 5089 6999 599 -255 1253 C ATOM 909 CD PRO A 109 7.291 -34.202 25.365 1.00 49.11 C ANISOU 909 CD PRO A 109 6637 5413 6611 544 -493 1233 C ATOM 910 N LEU A 110 4.703 -36.128 27.150 1.00 58.04 N ANISOU 910 N LEU A 110 8614 5746 7694 722 70 1958 N ATOM 911 CA LEU A 110 4.003 -37.162 27.907 1.00 63.55 C ANISOU 911 CA LEU A 110 9642 6044 8462 883 409 2329 C ATOM 912 C LEU A 110 3.008 -36.589 28.911 1.00 63.91 C ANISOU 912 C LEU A 110 9931 6115 8238 769 595 2478 C ATOM 913 O LEU A 110 2.083 -37.300 29.318 1.00 64.85 O ANISOU 913 O LEU A 110 10283 5804 8552 751 1037 2718 O ATOM 914 CB LEU A 110 5.006 -38.058 28.632 1.00 68.69 C ANISOU 914 CB LEU A 110 10469 6707 8923 1402 316 2667 C ATOM 915 CG LEU A 110 5.948 -38.883 27.753 1.00 70.57 C ANISOU 915 CG LEU A 110 10500 6851 9463 1585 194 2570 C ATOM 916 CD1 LEU A 110 6.802 -39.806 28.610 1.00 73.50 C ANISOU 916 CD1 LEU A 110 11118 7198 9611 2162 97 2913 C ATOM 917 CD2 LEU A 110 5.168 -39.672 26.706 1.00 71.11 C ANISOU 917 CD2 LEU A 110 10522 6395 10100 1362 504 2455 C ATOM 918 N ARG A 111 3.174 -35.334 29.331 1.00 61.63 N ANISOU 918 N ARG A 111 9583 6287 7545 695 306 2333 N ATOM 919 CA ARG A 111 2.241 -34.719 30.270 1.00 63.15 C ANISOU 919 CA ARG A 111 10007 6546 7441 616 459 2441 C ATOM 920 C ARG A 111 1.524 -33.512 29.686 1.00 56.18 C ANISOU 920 C ARG A 111 8924 5812 6611 175 366 2038 C ATOM 921 O ARG A 111 0.808 -32.821 30.419 1.00 48.60 O ANISOU 921 O ARG A 111 8107 4979 5380 100 425 2057 O ATOM 922 CB ARG A 111 2.954 -34.322 31.567 1.00 69.98 C ANISOU 922 CB ARG A 111 11092 7813 7683 1043 173 2645 C ATOM 923 CG ARG A 111 4.295 -33.645 31.390 1.00 72.83 C ANISOU 923 CG ARG A 111 11141 8634 7898 1166 -402 2365 C ATOM 924 CD ARG A 111 4.998 -33.500 32.742 1.00 81.32 C ANISOU 924 CD ARG A 111 12448 10046 8404 1725 -741 2518 C ATOM 925 NE ARG A 111 6.448 -33.641 32.622 1.00 85.68 N ANISOU 925 NE ARG A 111 12715 10846 8992 2036 -1201 2339 N ATOM 926 CZ ARG A 111 7.307 -33.482 33.625 1.00 89.32 C ANISOU 926 CZ ARG A 111 13251 11645 9041 2586 -1665 2301 C ATOM 927 NH1 ARG A 111 6.867 -33.168 34.838 1.00 94.47 N ANISOU 927 NH1 ARG A 111 14330 12439 9125 2926 -1726 2471 N ATOM 928 NH2 ARG A 111 8.607 -33.637 33.413 1.00 87.93 N ANISOU 928 NH2 ARG A 111 12715 11669 9027 2839 -2082 2050 N ATOM 929 N TYR A 112 1.684 -33.250 28.386 1.00 49.46 N ANISOU 929 N TYR A 112 7797 4934 6061 -64 236 1680 N ATOM 930 CA TYR A 112 1.041 -32.090 27.778 1.00 44.79 C ANISOU 930 CA TYR A 112 7100 4458 5461 -402 131 1297 C ATOM 931 C TYR A 112 -0.481 -32.180 27.886 1.00 46.50 C ANISOU 931 C TYR A 112 7407 4378 5883 -603 439 1218 C ATOM 932 O TYR A 112 -1.140 -31.231 28.331 1.00 45.88 O ANISOU 932 O TYR A 112 7384 4477 5571 -749 395 1101 O ATOM 933 CB TYR A 112 1.479 -31.955 26.318 1.00 42.15 C ANISOU 933 CB TYR A 112 6570 4075 5371 -508 14 976 C ATOM 934 CG TYR A 112 0.703 -30.913 25.549 1.00 39.43 C ANISOU 934 CG TYR A 112 6224 3744 5013 -770 -53 584 C ATOM 935 CD1 TYR A 112 1.105 -29.588 25.537 1.00 38.13 C ANISOU 935 CD1 TYR A 112 6039 3906 4544 -890 -275 435 C ATOM 936 CD2 TYR A 112 -0.437 -31.257 24.829 1.00 44.67 C ANISOU 936 CD2 TYR A 112 6909 4062 6001 -863 87 320 C ATOM 937 CE1 TYR A 112 0.388 -28.624 24.837 1.00 36.80 C ANISOU 937 CE1 TYR A 112 5953 3717 4312 -1073 -332 96 C ATOM 938 CE2 TYR A 112 -1.162 -30.301 24.127 1.00 44.41 C ANISOU 938 CE2 TYR A 112 6924 4045 5903 -1007 -35 -81 C ATOM 939 CZ TYR A 112 -0.742 -28.988 24.137 1.00 39.67 C ANISOU 939 CZ TYR A 112 6385 3769 4917 -1098 -231 -159 C ATOM 940 OH TYR A 112 -1.456 -28.044 23.439 1.00 37.04 O ANISOU 940 OH TYR A 112 6180 3419 4476 -1185 -344 -534 O ATOM 941 N ASN A 113 -1.059 -33.320 27.488 1.00 50.45 N ANISOU 941 N ASN A 113 7883 4403 6882 -613 754 1239 N ATOM 942 CA ASN A 113 -2.515 -33.444 27.466 1.00 55.50 C ANISOU 942 CA ASN A 113 8486 4704 7899 -834 1060 1049 C ATOM 943 C ASN A 113 -3.126 -33.358 28.861 1.00 57.27 C ANISOU 943 C ASN A 113 8916 4944 7901 -813 1388 1382 C ATOM 944 O ASN A 113 -4.243 -32.848 29.015 1.00 58.27 O ANISOU 944 O ASN A 113 8986 5015 8138 -1025 1537 1162 O ATOM 945 CB ASN A 113 -2.925 -34.754 26.791 1.00 62.50 C ANISOU 945 CB ASN A 113 9246 5023 9480 -839 1329 961 C ATOM 946 CG ASN A 113 -2.828 -34.679 25.282 1.00 65.32 C ANISOU 946 CG ASN A 113 9412 5317 10090 -863 1022 460 C ATOM 947 OD1 ASN A 113 -2.862 -33.591 24.695 1.00 62.48 O ANISOU 947 OD1 ASN A 113 9036 5244 9461 -936 713 128 O ATOM 948 ND2 ASN A 113 -2.714 -35.838 24.640 1.00 70.06 N ANISOU 948 ND2 ASN A 113 9918 5518 11184 -755 1117 405 N ATOM 949 N GLY A 114 -2.426 -33.853 29.883 1.00 56.31 N ANISOU 949 N GLY A 114 9059 4894 7442 -503 1509 1894 N ATOM 950 CA GLY A 114 -2.904 -33.683 31.242 1.00 59.29 C ANISOU 950 CA GLY A 114 9738 5337 7452 -371 1813 2241 C ATOM 951 C GLY A 114 -2.706 -32.292 31.809 1.00 58.11 C ANISOU 951 C GLY A 114 9655 5758 6666 -336 1417 2130 C ATOM 952 O GLY A 114 -3.431 -31.901 32.730 1.00 62.74 O ANISOU 952 O GLY A 114 10436 6412 6992 -305 1655 2255 O ATOM 953 N LEU A 115 -1.741 -31.536 31.289 1.00 52.03 N ANISOU 953 N LEU A 115 8722 5372 5674 -337 856 1887 N ATOM 954 CA LEU A 115 -1.433 -30.224 31.843 1.00 51.42 C ANISOU 954 CA LEU A 115 8680 5797 5062 -297 450 1753 C ATOM 955 C LEU A 115 -2.204 -29.110 31.143 1.00 46.06 C ANISOU 955 C LEU A 115 7819 5197 4486 -682 306 1288 C ATOM 956 O LEU A 115 -2.767 -28.230 31.804 1.00 43.67 O ANISOU 956 O LEU A 115 7616 5112 3866 -716 249 1211 O ATOM 957 CB LEU A 115 0.073 -29.958 31.751 1.00 57.48 C ANISOU 957 CB LEU A 115 9329 6896 5616 -93 -42 1715 C ATOM 958 CG LEU A 115 0.533 -28.498 31.839 1.00 59.50 C ANISOU 958 CG LEU A 115 9444 7590 5572 -186 -528 1394 C ATOM 959 CD1 LEU A 115 0.225 -27.916 33.212 1.00 63.05 C ANISOU 959 CD1 LEU A 115 10158 8317 5482 60 -626 1508 C ATOM 960 CD2 LEU A 115 2.020 -28.371 31.519 1.00 61.19 C ANISOU 960 CD2 LEU A 115 9404 8017 5829 -64 -920 1277 C ATOM 961 N VAL A 116 -2.231 -29.142 29.812 1.00 42.06 N ANISOU 961 N VAL A 116 7092 4513 4374 -908 232 970 N ATOM 962 CA VAL A 116 -2.817 -28.092 28.997 1.00 37.59 C ANISOU 962 CA VAL A 116 6427 4006 3851 -1174 39 510 C ATOM 963 C VAL A 116 -4.165 -28.611 28.512 1.00 40.42 C ANISOU 963 C VAL A 116 6708 3966 4683 -1331 346 283 C ATOM 964 O VAL A 116 -4.236 -29.385 27.554 1.00 43.64 O ANISOU 964 O VAL A 116 6993 4053 5535 -1348 425 134 O ATOM 965 CB VAL A 116 -1.896 -27.712 27.833 1.00 38.53 C ANISOU 965 CB VAL A 116 6428 4191 4022 -1222 -240 294 C ATOM 966 CG1 VAL A 116 -2.401 -26.476 27.119 1.00 34.74 C ANISOU 966 CG1 VAL A 116 5975 3783 3441 -1412 -440 -122 C ATOM 967 CG2 VAL A 116 -0.470 -27.487 28.334 1.00 42.59 C ANISOU 967 CG2 VAL A 116 6893 5017 4272 -1063 -477 497 C ATOM 968 N THR A 117 -5.246 -28.194 29.169 1.00 37.84 N ANISOU 968 N THR A 117 6420 3651 4307 -1425 507 201 N ATOM 969 CA THR A 117 -6.583 -28.623 28.786 1.00 37.45 C ANISOU 969 CA THR A 117 6203 3220 4808 -1586 796 -107 C ATOM 970 C THR A 117 -7.381 -27.457 28.220 1.00 35.04 C ANISOU 970 C THR A 117 5834 3042 4438 -1726 496 -660 C ATOM 971 O THR A 117 -7.045 -26.282 28.414 1.00 34.85 O ANISOU 971 O THR A 117 5951 3390 3899 -1721 168 -710 O ATOM 972 CB THR A 117 -7.342 -29.219 29.979 1.00 42.96 C ANISOU 972 CB THR A 117 6954 3735 5635 -1577 1357 213 C ATOM 973 OG1 THR A 117 -7.541 -28.197 30.966 1.00 42.43 O ANISOU 973 OG1 THR A 117 7065 4054 5003 -1531 1284 296 O ATOM 974 CG2 THR A 117 -6.566 -30.387 30.597 1.00 44.74 C ANISOU 974 CG2 THR A 117 7355 3792 5852 -1357 1679 804 C ATOM 975 N GLY A 118 -8.468 -27.802 27.531 1.00 34.72 N ANISOU 975 N GLY A 118 7050 2144 3999 -1108 339 348 N ATOM 976 CA GLY A 118 -9.349 -26.779 26.999 1.00 36.25 C ANISOU 976 CA GLY A 118 7129 2594 4050 -1258 220 244 C ATOM 977 C GLY A 118 -9.949 -25.898 28.078 1.00 35.57 C ANISOU 977 C GLY A 118 6737 2822 3956 -1306 136 373 C ATOM 978 O GLY A 118 -10.067 -24.683 27.902 1.00 35.53 O ANISOU 978 O GLY A 118 6540 3069 3892 -1263 91 336 O ATOM 979 N THR A 119 -10.340 -26.498 29.204 1.00 36.59 N ANISOU 979 N THR A 119 6847 2917 4139 -1395 143 527 N ATOM 980 CA THR A 119 -10.948 -25.734 30.292 1.00 36.76 C ANISOU 980 CA THR A 119 6650 3191 4125 -1451 134 644 C ATOM 981 C THR A 119 -9.967 -24.736 30.886 1.00 33.89 C ANISOU 981 C THR A 119 6174 2994 3708 -1228 140 701 C ATOM 982 O THR A 119 -10.331 -23.588 31.164 1.00 35.68 O ANISOU 982 O THR A 119 6223 3464 3869 -1229 137 689 O ATOM 983 CB THR A 119 -11.453 -26.679 31.388 1.00 42.39 C ANISOU 983 CB THR A 119 7423 3805 4880 -1577 180 801 C ATOM 984 OG1 THR A 119 -12.545 -27.451 30.884 1.00 46.72 O ANISOU 984 OG1 THR A 119 7979 4262 5511 -1791 150 744 O ATOM 985 CG2 THR A 119 -11.927 -25.894 32.598 1.00 43.57 C ANISOU 985 CG2 THR A 119 7412 4186 4956 -1598 241 913 C ATOM 986 N ARG A 120 -8.719 -25.156 31.107 1.00 34.38 N ANISOU 986 N ARG A 120 6327 2905 3830 -1042 143 780 N ATOM 987 CA ARG A 120 -7.717 -24.221 31.611 1.00 33.51 C ANISOU 987 CA ARG A 120 6098 2929 3704 -853 93 853 C ATOM 988 C ARG A 120 -7.408 -23.143 30.576 1.00 32.94 C ANISOU 988 C ARG A 120 5894 2995 3627 -743 99 700 C ATOM 989 O ARG A 120 -7.191 -21.980 30.930 1.00 34.58 O ANISOU 989 O ARG A 120 5954 3409 3776 -681 52 711 O ATOM 990 CB ARG A 120 -6.447 -24.976 32.016 1.00 34.66 C ANISOU 990 CB ARG A 120 6320 2850 4000 -687 61 1018 C ATOM 991 CG ARG A 120 -6.656 -25.984 33.152 1.00 37.67 C ANISOU 991 CG ARG A 120 6815 3117 4382 -778 23 1199 C ATOM 992 CD ARG A 120 -5.409 -26.826 33.440 1.00 39.66 C ANISOU 992 CD ARG A 120 7058 3149 4861 -592 -25 1367 C ATOM 993 NE ARG A 120 -5.699 -27.855 34.437 1.00 44.09 N ANISOU 993 NE ARG A 120 7688 3636 5429 -674 -55 1510 N ATOM 994 CZ ARG A 120 -4.924 -28.903 34.700 1.00 47.26 C ANISOU 994 CZ ARG A 120 8095 3809 6052 -561 -72 1671 C ATOM 995 NH1 ARG A 120 -5.284 -29.775 35.635 1.00 49.23 N ANISOU 995 NH1 ARG A 120 8424 4005 6275 -652 -96 1803 N ATOM 996 NH2 ARG A 120 -3.791 -29.084 34.036 1.00 49.32 N ANISOU 996 NH2 ARG A 120 8268 3881 6590 -349 -40 1712 N ATOM 997 N ALA A 121 -7.401 -23.503 29.289 1.00 34.61 N ANISOU 997 N ALA A 121 6198 3077 3875 -733 163 554 N ATOM 998 CA ALA A 121 -7.132 -22.510 28.248 1.00 31.06 C ANISOU 998 CA ALA A 121 5668 2743 3389 -644 181 420 C ATOM 999 C ALA A 121 -8.205 -21.427 28.225 1.00 28.61 C ANISOU 999 C ALA A 121 5196 2707 2968 -777 103 361 C ATOM 1000 O ALA A 121 -7.895 -20.236 28.093 1.00 26.49 O ANISOU 1000 O ALA A 121 4772 2617 2676 -678 86 338 O ATOM 1001 CB ALA A 121 -7.031 -23.193 26.883 1.00 31.41 C ANISOU 1001 CB ALA A 121 5943 2565 3427 -650 279 270 C ATOM 1002 N ALA A 122 -9.477 -21.813 28.361 1.00 30.38 N ANISOU 1002 N ALA A 122 5428 2949 3165 -1000 64 357 N ATOM 1003 CA ALA A 122 -10.534 -20.804 28.362 1.00 31.64 C ANISOU 1003 CA ALA A 122 5380 3339 3303 -1112 14 338 C ATOM 1004 C ALA A 122 -10.401 -19.870 29.562 1.00 33.34 C ANISOU 1004 C ALA A 122 5439 3734 3496 -1031 63 426 C ATOM 1005 O ALA A 122 -10.645 -18.662 29.447 1.00 32.56 O ANISOU 1005 O ALA A 122 5167 3817 3388 -996 59 391 O ATOM 1006 CB ALA A 122 -11.909 -21.468 28.346 1.00 29.99 C ANISOU 1006 CB ALA A 122 5160 3083 3152 -1371 -29 361 C ATOM 1007 N GLY A 123 -10.006 -20.408 30.721 1.00 32.46 N ANISOU 1007 N GLY A 123 5422 3552 3359 -1011 102 545 N ATOM 1008 CA GLY A 123 -9.763 -19.549 31.867 1.00 27.82 C ANISOU 1008 CA GLY A 123 4787 3100 2684 -957 128 618 C ATOM 1009 C GLY A 123 -8.626 -18.576 31.628 1.00 27.06 C ANISOU 1009 C GLY A 123 4622 3080 2578 -769 57 587 C ATOM 1010 O GLY A 123 -8.725 -17.394 31.966 1.00 27.88 O ANISOU 1010 O GLY A 123 4627 3343 2623 -744 71 562 O ATOM 1011 N ILE A 124 -7.523 -19.062 31.054 1.00 25.95 N ANISOU 1011 N ILE A 124 4531 2803 2526 -635 7 598 N ATOM 1012 CA ILE A 124 -6.393 -18.187 30.755 1.00 25.84 C ANISOU 1012 CA ILE A 124 4414 2837 2566 -459 -44 594 C ATOM 1013 C ILE A 124 -6.805 -17.099 29.769 1.00 24.91 C ANISOU 1013 C ILE A 124 4161 2872 2431 -444 -12 455 C ATOM 1014 O ILE A 124 -6.451 -15.923 29.935 1.00 23.66 O ANISOU 1014 O ILE A 124 3883 2845 2260 -374 -45 448 O ATOM 1015 CB ILE A 124 -5.212 -19.013 30.214 1.00 27.79 C ANISOU 1015 CB ILE A 124 4708 2867 2983 -307 -32 648 C ATOM 1016 CG1 ILE A 124 -4.637 -19.903 31.330 1.00 32.85 C ANISOU 1016 CG1 ILE A 124 5438 3359 3685 -298 -117 843 C ATOM 1017 CG2 ILE A 124 -4.151 -18.098 29.603 1.00 20.41 C ANISOU 1017 CG2 ILE A 124 3624 1968 2161 -130 -32 636 C ATOM 1018 CD1 ILE A 124 -3.797 -21.055 30.795 1.00 35.03 C ANISOU 1018 CD1 ILE A 124 5773 3355 4182 -169 -47 907 C ATOM 1019 N ILE A 125 -7.550 -17.478 28.725 1.00 23.55 N ANISOU 1019 N ILE A 125 4025 2667 2255 -527 25 354 N ATOM 1020 CA ILE A 125 -8.000 -16.508 27.726 1.00 21.63 C ANISOU 1020 CA ILE A 125 3677 2553 1990 -536 13 252 C ATOM 1021 C ILE A 125 -8.830 -15.406 28.378 1.00 20.51 C ANISOU 1021 C ILE A 125 3356 2607 1831 -594 7 265 C ATOM 1022 O ILE A 125 -8.618 -14.217 28.119 1.00 18.11 O ANISOU 1022 O ILE A 125 2925 2422 1533 -512 -3 235 O ATOM 1023 CB ILE A 125 -8.790 -17.214 26.609 1.00 22.15 C ANISOU 1023 CB ILE A 125 3863 2529 2024 -677 -13 168 C ATOM 1024 CG1 ILE A 125 -7.845 -18.034 25.726 1.00 23.26 C ANISOU 1024 CG1 ILE A 125 4228 2452 2157 -586 60 112 C ATOM 1025 CG2 ILE A 125 -9.589 -16.181 25.797 1.00 21.59 C ANISOU 1025 CG2 ILE A 125 3660 2612 1930 -747 -93 116 C ATOM 1026 CD1 ILE A 125 -8.569 -18.961 24.724 1.00 23.71 C ANISOU 1026 CD1 ILE A 125 4525 2355 2130 -765 24 15 C ATOM 1027 N ALA A 126 -9.782 -15.785 29.247 1.00 23.00 N ANISOU 1027 N ALA A 126 3666 2933 2141 -730 50 317 N ATOM 1028 CA ALA A 126 -10.606 -14.789 29.938 1.00 22.16 C ANISOU 1028 CA ALA A 126 3409 2967 2045 -771 129 333 C ATOM 1029 C ALA A 126 -9.752 -13.849 30.789 1.00 23.16 C ANISOU 1029 C ALA A 126 3556 3155 2087 -653 148 343 C ATOM 1030 O ALA A 126 -9.953 -12.621 30.796 1.00 21.19 O ANISOU 1030 O ALA A 126 3183 3015 1855 -609 190 304 O ATOM 1031 CB ALA A 126 -11.644 -15.492 30.816 1.00 20.54 C ANISOU 1031 CB ALA A 126 3227 2719 1858 -928 239 406 C ATOM 1032 N ILE A 127 -8.826 -14.421 31.563 1.00 20.77 N ANISOU 1032 N ILE A 127 3420 2765 1705 -618 98 413 N ATOM 1033 CA ILE A 127 -7.952 -13.614 32.408 1.00 21.12 C ANISOU 1033 CA ILE A 127 3521 2843 1660 -548 41 445 C ATOM 1034 C ILE A 127 -7.142 -12.651 31.564 1.00 19.08 C ANISOU 1034 C ILE A 127 3120 2641 1488 -412 -36 392 C ATOM 1035 O ILE A 127 -6.984 -11.477 31.908 1.00 19.55 O ANISOU 1035 O ILE A 127 3140 2780 1510 -384 -41 362 O ATOM 1036 CB ILE A 127 -7.042 -14.532 33.242 1.00 23.16 C ANISOU 1036 CB ILE A 127 3964 2973 1862 -550 -77 575 C ATOM 1037 CG1 ILE A 127 -7.861 -15.194 34.351 1.00 24.35 C ANISOU 1037 CG1 ILE A 127 4302 3083 1867 -701 19 640 C ATOM 1038 CG2 ILE A 127 -5.865 -13.752 33.809 1.00 23.08 C ANISOU 1038 CG2 ILE A 127 3983 2972 1816 -481 -243 634 C ATOM 1039 CD1 ILE A 127 -7.145 -16.383 34.983 1.00 30.36 C ANISOU 1039 CD1 ILE A 127 5219 3692 2625 -706 -107 781 C ATOM 1040 N CYS A 128 -6.635 -13.127 30.424 1.00 18.91 N ANISOU 1040 N CYS A 128 3047 2559 1579 -332 -67 377 N ATOM 1041 CA CYS A 128 -5.815 -12.276 29.578 1.00 18.77 C ANISOU 1041 CA CYS A 128 2908 2574 1649 -202 -99 346 C ATOM 1042 C CYS A 128 -6.622 -11.132 28.968 1.00 19.70 C ANISOU 1042 C CYS A 128 2894 2829 1763 -217 -50 256 C ATOM 1043 O CYS A 128 -6.087 -10.029 28.806 1.00 16.66 O ANISOU 1043 O CYS A 128 2412 2502 1415 -136 -74 243 O ATOM 1044 CB CYS A 128 -5.152 -13.120 28.489 1.00 21.60 C ANISOU 1044 CB CYS A 128 3300 2800 2108 -116 -66 345 C ATOM 1045 SG CYS A 128 -3.837 -14.168 29.174 1.00 25.09 S ANISOU 1045 SG CYS A 128 3806 3049 2678 -27 -125 502 S ATOM 1046 N TRP A 129 -7.903 -11.364 28.633 1.00 16.53 N ANISOU 1046 N TRP A 129 2466 2465 1351 -326 1 217 N ATOM 1047 CA TRP A 129 -8.731 -10.263 28.137 1.00 17.69 C ANISOU 1047 CA TRP A 129 2448 2725 1548 -340 24 177 C ATOM 1048 C TRP A 129 -8.966 -9.215 29.219 1.00 18.04 C ANISOU 1048 C TRP A 129 2439 2833 1582 -329 106 176 C ATOM 1049 O TRP A 129 -8.934 -8.013 28.934 1.00 16.93 O ANISOU 1049 O TRP A 129 2181 2756 1495 -265 116 148 O ATOM 1050 CB TRP A 129 -10.065 -10.785 27.607 1.00 17.03 C ANISOU 1050 CB TRP A 129 2307 2645 1519 -479 17 182 C ATOM 1051 CG TRP A 129 -9.972 -11.225 26.193 1.00 18.15 C ANISOU 1051 CG TRP A 129 2514 2742 1642 -502 -88 152 C ATOM 1052 CD1 TRP A 129 -9.843 -12.501 25.732 1.00 20.35 C ANISOU 1052 CD1 TRP A 129 2981 2892 1860 -569 -123 132 C ATOM 1053 CD2 TRP A 129 -9.954 -10.371 25.032 1.00 17.82 C ANISOU 1053 CD2 TRP A 129 2410 2755 1607 -467 -162 133 C ATOM 1054 NE1 TRP A 129 -9.762 -12.495 24.354 1.00 20.35 N ANISOU 1054 NE1 TRP A 129 3078 2856 1797 -588 -200 84 N ATOM 1055 CE2 TRP A 129 -9.827 -11.203 23.904 1.00 18.28 C ANISOU 1055 CE2 TRP A 129 2666 2713 1565 -530 -235 94 C ATOM 1056 CE3 TRP A 129 -10.046 -8.986 24.848 1.00 17.23 C ANISOU 1056 CE3 TRP A 129 2161 2784 1602 -395 -166 148 C ATOM 1057 CZ2 TRP A 129 -9.808 -10.701 22.596 1.00 20.28 C ANISOU 1057 CZ2 TRP A 129 2980 2977 1748 -539 -321 76 C ATOM 1058 CZ3 TRP A 129 -10.011 -8.478 23.540 1.00 18.43 C ANISOU 1058 CZ3 TRP A 129 2325 2954 1723 -390 -264 149 C ATOM 1059 CH2 TRP A 129 -9.884 -9.335 22.441 1.00 21.48 C ANISOU 1059 CH2 TRP A 129 2941 3249 1970 -467 -342 115 C ATOM 1060 N VAL A 130 -9.205 -9.646 30.462 1.00 17.45 N ANISOU 1060 N VAL A 130 2489 2721 1420 -400 182 204 N ATOM 1061 CA VAL A 130 -9.377 -8.691 31.553 1.00 16.88 C ANISOU 1061 CA VAL A 130 2469 2669 1277 -405 298 182 C ATOM 1062 C VAL A 130 -8.104 -7.872 31.735 1.00 16.58 C ANISOU 1062 C VAL A 130 2488 2628 1183 -320 173 167 C ATOM 1063 O VAL A 130 -8.143 -6.641 31.844 1.00 17.96 O ANISOU 1063 O VAL A 130 2615 2834 1375 -282 224 115 O ATOM 1064 CB VAL A 130 -9.784 -9.413 32.853 1.00 19.57 C ANISOU 1064 CB VAL A 130 3019 2945 1473 -516 414 223 C ATOM 1065 CG1 VAL A 130 -9.732 -8.444 34.041 1.00 20.50 C ANISOU 1065 CG1 VAL A 130 3314 3043 1431 -533 536 182 C ATOM 1066 CG2 VAL A 130 -11.191 -9.996 32.727 1.00 20.05 C ANISOU 1066 CG2 VAL A 130 2963 3002 1653 -610 580 252 C ATOM 1067 N LEU A 131 -6.952 -8.542 31.751 1.00 16.44 N ANISOU 1067 N LEU A 131 2552 2553 1142 -290 6 229 N ATOM 1068 CA LEU A 131 -5.694 -7.828 31.915 1.00 18.63 C ANISOU 1068 CA LEU A 131 2834 2811 1433 -226 -148 256 C ATOM 1069 C LEU A 131 -5.423 -6.885 30.739 1.00 17.94 C ANISOU 1069 C LEU A 131 2537 2779 1499 -119 -146 214 C ATOM 1070 O LEU A 131 -4.802 -5.825 30.917 1.00 19.05 O ANISOU 1070 O LEU A 131 2649 2923 1666 -88 -211 206 O ATOM 1071 CB LEU A 131 -4.555 -8.833 32.077 1.00 17.98 C ANISOU 1071 CB LEU A 131 2808 2631 1393 -202 -319 378 C ATOM 1072 CG LEU A 131 -4.606 -9.681 33.350 1.00 25.81 C ANISOU 1072 CG LEU A 131 4037 3549 2219 -316 -381 460 C ATOM 1073 CD1 LEU A 131 -3.546 -10.799 33.281 1.00 28.49 C ANISOU 1073 CD1 LEU A 131 4368 3769 2689 -264 -544 612 C ATOM 1074 CD2 LEU A 131 -4.380 -8.804 34.588 1.00 26.52 C ANISOU 1074 CD2 LEU A 131 4272 3618 2185 -385 -446 434 C ATOM 1075 N ASER A 132 -5.860 -7.261 29.536 0.82 16.00 N ANISOU 1075 N ASER A 132 2180 2562 1339 -81 -87 194 N ATOM 1076 N BSER A 132 -5.886 -7.245 29.538 0.18 15.70 N ANISOU 1076 N BSER A 132 2140 2525 1300 -82 -85 193 N ATOM 1077 CA ASER A 132 -5.670 -6.402 28.370 0.82 13.25 C ANISOU 1077 CA ASER A 132 1680 2259 1094 5 -80 170 C ATOM 1078 CA BSER A 132 -5.671 -6.388 28.377 0.18 14.12 C ANISOU 1078 CA BSER A 132 1790 2369 1205 5 -80 169 C ATOM 1079 C ASER A 132 -6.476 -5.111 28.491 0.82 14.82 C ANISOU 1079 C ASER A 132 1787 2529 1315 -5 -11 118 C ATOM 1080 C BSER A 132 -6.489 -5.105 28.477 0.18 14.32 C ANISOU 1080 C BSER A 132 1722 2467 1253 -5 -10 118 C ATOM 1081 O ASER A 132 -5.990 -4.036 28.117 0.82 13.79 O ANISOU 1081 O ASER A 132 1568 2414 1257 63 -32 113 O ATOM 1082 O BSER A 132 -6.032 -4.038 28.050 0.18 13.75 O ANISOU 1082 O BSER A 132 1557 2412 1255 64 -29 113 O ATOM 1083 CB ASER A 132 -6.048 -7.165 27.096 0.82 13.53 C ANISOU 1083 CB ASER A 132 1708 2286 1147 6 -54 160 C ATOM 1084 CB BSER A 132 -6.009 -7.143 27.090 0.18 13.84 C ANISOU 1084 CB BSER A 132 1745 2324 1188 9 -55 161 C ATOM 1085 OG ASER A 132 -5.226 -8.310 26.926 0.82 14.27 O ANISOU 1085 OG ASER A 132 1902 2272 1248 40 -65 198 O ATOM 1086 OG BSER A 132 -7.402 -7.367 26.971 0.18 14.96 O ANISOU 1086 OG BSER A 132 1864 2512 1308 -93 -21 136 O ATOM 1087 N PHE A 133 -7.701 -5.186 29.035 1.00 15.29 N ANISOU 1087 N PHE A 133 1853 2609 1349 -83 100 93 N ATOM 1088 CA PHE A 133 -8.464 -3.965 29.282 1.00 16.63 C ANISOU 1088 CA PHE A 133 1927 2802 1590 -71 222 57 C ATOM 1089 C PHE A 133 -7.767 -3.090 30.309 1.00 18.50 C ANISOU 1089 C PHE A 133 2302 2988 1741 -62 232 11 C ATOM 1090 O PHE A 133 -7.666 -1.872 30.125 1.00 19.33 O ANISOU 1090 O PHE A 133 2333 3088 1924 -7 258 -20 O ATOM 1091 CB PHE A 133 -9.894 -4.294 29.738 1.00 16.97 C ANISOU 1091 CB PHE A 133 1925 2842 1681 -147 393 65 C ATOM 1092 CG PHE A 133 -10.856 -4.470 28.590 1.00 17.81 C ANISOU 1092 CG PHE A 133 1809 2994 1963 -166 354 125 C ATOM 1093 CD1 PHE A 133 -11.041 -5.721 28.000 1.00 17.00 C ANISOU 1093 CD1 PHE A 133 1733 2892 1833 -247 242 161 C ATOM 1094 CD2 PHE A 133 -11.553 -3.372 28.077 1.00 17.85 C ANISOU 1094 CD2 PHE A 133 1595 3021 2168 -118 398 157 C ATOM 1095 CE1 PHE A 133 -11.926 -5.885 26.924 1.00 21.13 C ANISOU 1095 CE1 PHE A 133 2096 3441 2490 -309 139 225 C ATOM 1096 CE2 PHE A 133 -12.448 -3.532 27.008 1.00 22.74 C ANISOU 1096 CE2 PHE A 133 2011 3673 2955 -165 287 251 C ATOM 1097 CZ PHE A 133 -12.629 -4.790 26.429 1.00 22.36 C ANISOU 1097 CZ PHE A 133 2022 3630 2844 -276 138 282 C ATOM 1098 N ALA A 134 -7.272 -3.696 31.393 1.00 16.28 N ANISOU 1098 N ALA A 134 2247 2652 1288 -134 186 16 N ATOM 1099 CA ALA A 134 -6.615 -2.923 32.441 1.00 17.52 C ANISOU 1099 CA ALA A 134 2607 2739 1312 -177 139 -23 C ATOM 1100 C ALA A 134 -5.357 -2.227 31.912 1.00 17.36 C ANISOU 1100 C ALA A 134 2491 2710 1394 -116 -63 8 C ATOM 1101 O ALA A 134 -5.130 -1.050 32.199 1.00 17.39 O ANISOU 1101 O ALA A 134 2537 2670 1399 -121 -65 -46 O ATOM 1102 CB ALA A 134 -6.279 -3.838 33.628 1.00 18.52 C ANISOU 1102 CB ALA A 134 3020 2801 1214 -292 59 17 C ATOM 1103 N ILE A 135 -4.538 -2.939 31.135 1.00 15.91 N ANISOU 1103 N ILE A 135 2181 2544 1319 -58 -204 98 N ATOM 1104 CA ILE A 135 -3.311 -2.362 30.576 1.00 16.10 C ANISOU 1104 CA ILE A 135 2073 2545 1499 8 -351 159 C ATOM 1105 C ILE A 135 -3.632 -1.290 29.537 1.00 15.30 C ANISOU 1105 C ILE A 135 1792 2492 1530 93 -246 118 C ATOM 1106 O ILE A 135 -3.131 -0.165 29.610 1.00 16.61 O ANISOU 1106 O ILE A 135 1925 2622 1765 99 -296 109 O ATOM 1107 CB ILE A 135 -2.424 -3.472 29.980 1.00 16.62 C ANISOU 1107 CB ILE A 135 2049 2582 1684 71 -436 274 C ATOM 1108 CG1 ILE A 135 -1.784 -4.288 31.096 1.00 20.45 C ANISOU 1108 CG1 ILE A 135 2682 2986 2102 -9 -615 367 C ATOM 1109 CG2 ILE A 135 -1.331 -2.878 29.037 1.00 18.64 C ANISOU 1109 CG2 ILE A 135 2100 2811 2170 174 -475 348 C ATOM 1110 CD1 ILE A 135 -1.208 -5.638 30.625 1.00 23.47 C ANISOU 1110 CD1 ILE A 135 2995 3309 2613 61 -633 480 C ATOM 1111 N GLY A 136 -4.490 -1.612 28.566 1.00 13.66 N ANISOU 1111 N GLY A 136 1482 2352 1357 139 -126 106 N ATOM 1112 CA GLY A 136 -4.741 -0.681 27.475 1.00 13.71 C ANISOU 1112 CA GLY A 136 1331 2398 1482 211 -73 108 C ATOM 1113 C GLY A 136 -5.564 0.526 27.878 1.00 14.80 C ANISOU 1113 C GLY A 136 1441 2527 1654 205 25 47 C ATOM 1114 O GLY A 136 -5.432 1.590 27.271 1.00 14.52 O ANISOU 1114 O GLY A 136 1295 2486 1737 263 32 62 O ATOM 1115 N LEU A 137 -6.424 0.390 28.898 1.00 11.97 N ANISOU 1115 N LEU A 137 1192 2146 1211 142 136 -15 N ATOM 1116 CA LEU A 137 -7.197 1.529 29.383 1.00 12.15 C ANISOU 1116 CA LEU A 137 1212 2113 1292 153 304 -78 C ATOM 1117 C LEU A 137 -6.601 2.159 30.635 1.00 13.83 C ANISOU 1117 C LEU A 137 1674 2213 1366 88 304 -164 C ATOM 1118 O LEU A 137 -7.283 2.932 31.305 1.00 15.25 O ANISOU 1118 O LEU A 137 1953 2304 1539 80 506 -247 O ATOM 1119 CB LEU A 137 -8.653 1.129 29.653 1.00 13.27 C ANISOU 1119 CB LEU A 137 1304 2262 1475 133 506 -83 C ATOM 1120 CG LEU A 137 -9.377 0.513 28.447 1.00 15.54 C ANISOU 1120 CG LEU A 137 1364 2642 1900 149 448 15 C ATOM 1121 CD1 LEU A 137 -10.815 0.251 28.773 1.00 17.06 C ANISOU 1121 CD1 LEU A 137 1447 2818 2216 116 633 44 C ATOM 1122 CD2 LEU A 137 -9.248 1.441 27.196 1.00 14.10 C ANISOU 1122 CD2 LEU A 137 998 2483 1877 230 353 79 C ATOM 1123 N THR A 138 -5.358 1.833 30.977 1.00 14.77 N ANISOU 1123 N THR A 138 1861 2477 1274 232 -393 57 N ATOM 1124 CA THR A 138 -4.715 2.488 32.114 1.00 15.91 C ANISOU 1124 CA THR A 138 1863 2793 1390 199 -251 34 C ATOM 1125 C THR A 138 -4.773 4.016 32.058 1.00 16.03 C ANISOU 1125 C THR A 138 1826 2831 1434 194 -183 -46 C ATOM 1126 O THR A 138 -4.955 4.632 33.126 1.00 14.70 O ANISOU 1126 O THR A 138 1555 2762 1267 158 -125 -89 O ATOM 1127 CB THR A 138 -3.267 1.980 32.237 1.00 18.71 C ANISOU 1127 CB THR A 138 2261 3217 1632 261 -191 66 C ATOM 1128 OG1 THR A 138 -3.283 0.747 32.956 1.00 19.97 O ANISOU 1128 OG1 THR A 138 2414 3400 1774 243 -224 133 O ATOM 1129 CG2 THR A 138 -2.362 2.968 33.012 1.00 18.23 C ANISOU 1129 CG2 THR A 138 2082 3309 1535 216 -82 42 C ATOM 1130 N PRO A 139 -4.662 4.682 30.893 1.00 16.90 N ANISOU 1130 N PRO A 139 2019 2846 1558 244 -199 -65 N ATOM 1131 CA PRO A 139 -4.853 6.144 30.872 1.00 14.93 C ANISOU 1131 CA PRO A 139 1736 2576 1360 227 -163 -128 C ATOM 1132 C PRO A 139 -6.208 6.619 31.399 1.00 16.17 C ANISOU 1132 C PRO A 139 1827 2739 1579 225 -166 -171 C ATOM 1133 O PRO A 139 -6.288 7.731 31.943 1.00 16.47 O ANISOU 1133 O PRO A 139 1851 2783 1624 237 -128 -247 O ATOM 1134 CB PRO A 139 -4.682 6.488 29.382 1.00 13.35 C ANISOU 1134 CB PRO A 139 1628 2278 1166 296 -192 -95 C ATOM 1135 CG PRO A 139 -3.666 5.441 28.904 1.00 15.75 C ANISOU 1135 CG PRO A 139 2002 2622 1360 374 -192 -20 C ATOM 1136 CD PRO A 139 -4.122 4.183 29.606 1.00 14.57 C ANISOU 1136 CD PRO A 139 1862 2475 1199 348 -241 -23 C ATOM 1137 N AMET A 140 -7.273 5.826 31.236 0.60 14.86 N ANISOU 1137 N AMET A 140 1625 2569 1451 221 -228 -105 N ATOM 1138 N BMET A 140 -7.264 5.812 31.266 0.40 15.02 N ANISOU 1138 N BMET A 140 1644 2593 1470 220 -227 -105 N ATOM 1139 CA AMET A 140 -8.571 6.172 31.812 0.60 15.59 C ANISOU 1139 CA AMET A 140 1597 2742 1584 241 -215 -77 C ATOM 1140 CA BMET A 140 -8.578 6.191 31.781 0.40 15.69 C ANISOU 1140 CA BMET A 140 1612 2752 1599 242 -216 -78 C ATOM 1141 C AMET A 140 -8.561 6.105 33.328 0.60 17.45 C ANISOU 1141 C AMET A 140 1719 3154 1759 254 -134 -78 C ATOM 1142 C BMET A 140 -8.622 6.219 33.300 0.40 17.38 C ANISOU 1142 C BMET A 140 1711 3141 1752 262 -132 -83 C ATOM 1143 O AMET A 140 -9.486 6.630 33.955 0.60 18.58 O ANISOU 1143 O AMET A 140 1762 3412 1887 338 -84 -61 O ATOM 1144 O BMET A 140 -9.520 6.851 33.864 0.40 17.86 O ANISOU 1144 O BMET A 140 1685 3304 1797 353 -80 -79 O ATOM 1145 CB AMET A 140 -9.674 5.245 31.279 0.60 16.15 C ANISOU 1145 CB AMET A 140 1620 2792 1725 190 -336 60 C ATOM 1146 CB BMET A 140 -9.647 5.225 31.268 0.40 16.24 C ANISOU 1146 CB BMET A 140 1635 2801 1736 189 -337 59 C ATOM 1147 CG MET A 140 -9.742 5.153 29.757 1.00 16.06 C ANISOU 1147 CG MET A 140 1750 2608 1744 193 -449 54 C ATOM 1148 SD AMET A 140 -11.258 4.449 29.065 0.60 16.40 S ANISOU 1148 SD AMET A 140 1743 2607 1883 112 -646 209 S ATOM 1149 SD BMET A 140 -10.773 6.402 29.051 0.40 28.60 S ANISOU 1149 SD BMET A 140 3297 4180 3389 262 -435 51 S ATOM 1150 CE AMET A 140 -12.531 5.664 29.465 0.60 23.95 C ANISOU 1150 CE AMET A 140 2489 3727 2884 181 -544 275 C ATOM 1151 CE BMET A 140 -12.432 5.865 29.523 0.40 24.90 C ANISOU 1151 CE BMET A 140 2614 3853 2995 202 -514 250 C ATOM 1152 N ALEU A 141 -7.547 5.472 33.919 0.53 17.18 N ANISOU 1152 N ALEU A 141 1694 3166 1667 207 -115 -84 N ATOM 1153 N BLEU A 141 -7.695 5.533 33.970 0.47 17.41 N ANISOU 1153 N BLEU A 141 1711 3205 1698 214 -112 -81 N ATOM 1154 CA ALEU A 141 -7.372 5.418 35.366 0.53 18.98 C ANISOU 1154 CA ALEU A 141 1826 3575 1811 229 -40 -93 C ATOM 1155 CA BLEU A 141 -7.630 5.571 35.427 0.47 19.06 C ANISOU 1155 CA BLEU A 141 1820 3599 1823 248 -34 -94 C ATOM 1156 C ALEU A 141 -6.619 6.625 35.909 0.53 20.64 C ANISOU 1156 C ALEU A 141 2114 3783 1947 271 3 -253 C ATOM 1157 C BLEU A 141 -6.926 6.818 35.942 0.47 20.88 C ANISOU 1157 C BLEU A 141 2136 3818 1978 299 9 -260 C ATOM 1158 O ALEU A 141 -6.341 6.673 37.117 0.53 19.39 O ANISOU 1158 O ALEU A 141 1914 3766 1688 303 45 -293 O ATOM 1159 O BLEU A 141 -6.942 7.062 37.159 0.47 19.91 O ANISOU 1159 O BLEU A 141 1973 3840 1753 368 57 -310 O ATOM 1160 CB ALEU A 141 -6.644 4.126 35.768 0.53 16.92 C ANISOU 1160 CB ALEU A 141 1537 3368 1522 156 -53 -8 C ATOM 1161 CB BLEU A 141 -6.923 4.319 35.973 0.47 17.40 C ANISOU 1161 CB BLEU A 141 1569 3464 1580 175 -39 -11 C ATOM 1162 CG ALEU A 141 -7.265 2.822 35.243 0.53 16.86 C ANISOU 1162 CG ALEU A 141 1513 3297 1597 90 -158 149 C ATOM 1163 CG BLEU A 141 -7.725 3.007 36.052 0.47 18.29 C ANISOU 1163 CG BLEU A 141 1577 3617 1756 114 -106 181 C ATOM 1164 CD1ALEU A 141 -6.522 1.617 35.780 0.53 15.67 C ANISOU 1164 CD1ALEU A 141 1360 3184 1409 46 -170 227 C ATOM 1165 CD1BLEU A 141 -8.200 2.534 34.677 0.47 17.10 C ANISOU 1165 CD1BLEU A 141 1526 3264 1709 58 -246 234 C ATOM 1166 CD2ALEU A 141 -8.759 2.735 35.602 0.53 17.03 C ANISOU 1166 CD2ALEU A 141 1363 3427 1680 84 -181 291 C ATOM 1167 CD2BLEU A 141 -6.913 1.914 36.747 0.47 15.86 C ANISOU 1167 CD2BLEU A 141 1248 3375 1403 66 -100 250 C ATOM 1168 N GLY A 142 -6.304 7.600 35.057 1.00 16.73 N ANISOU 1168 N GLY A 142 1737 3124 1497 265 -30 -333 N ATOM 1169 CA GLY A 142 -5.706 8.846 35.489 1.00 18.23 C ANISOU 1169 CA GLY A 142 2029 3251 1648 274 -50 -468 C ATOM 1170 C GLY A 142 -4.364 9.182 34.875 1.00 18.70 C ANISOU 1170 C GLY A 142 2156 3206 1743 150 -105 -455 C ATOM 1171 O GLY A 142 -3.871 10.305 35.059 1.00 17.85 O ANISOU 1171 O GLY A 142 2145 2996 1642 110 -174 -536 O ATOM 1172 N TRP A 143 -3.754 8.252 34.136 1.00 17.16 N ANISOU 1172 N TRP A 143 1921 3035 1564 100 -93 -334 N ATOM 1173 CA TRP A 143 -2.485 8.538 33.482 1.00 15.98 C ANISOU 1173 CA TRP A 143 1791 2853 1428 22 -122 -255 C ATOM 1174 C TRP A 143 -2.806 9.117 32.114 1.00 15.96 C ANISOU 1174 C TRP A 143 1844 2714 1507 57 -143 -218 C ATOM 1175 O TRP A 143 -2.698 8.454 31.081 1.00 15.09 O ANISOU 1175 O TRP A 143 1739 2608 1388 114 -124 -125 O ATOM 1176 CB TRP A 143 -1.631 7.282 33.392 1.00 16.11 C ANISOU 1176 CB TRP A 143 1748 2998 1374 24 -80 -133 C ATOM 1177 CG TRP A 143 -0.193 7.528 33.056 1.00 17.69 C ANISOU 1177 CG TRP A 143 1908 3265 1549 -37 -87 -2 C ATOM 1178 CD1 TRP A 143 0.398 8.719 32.696 1.00 18.77 C ANISOU 1178 CD1 TRP A 143 2043 3342 1748 -133 -151 50 C ATOM 1179 CD2 TRP A 143 0.850 6.546 33.069 1.00 16.92 C ANISOU 1179 CD2 TRP A 143 1744 3328 1356 -4 -35 139 C ATOM 1180 NE1 TRP A 143 1.748 8.516 32.461 1.00 17.74 N ANISOU 1180 NE1 TRP A 143 1811 3359 1570 -176 -139 250 N ATOM 1181 CE2 TRP A 143 2.044 7.194 32.693 1.00 17.19 C ANISOU 1181 CE2 TRP A 143 1703 3438 1390 -75 -55 299 C ATOM 1182 CE3 TRP A 143 0.882 5.172 33.363 1.00 17.89 C ANISOU 1182 CE3 TRP A 143 1865 3538 1396 86 17 169 C ATOM 1183 CZ2 TRP A 143 3.261 6.511 32.578 1.00 20.27 C ANISOU 1183 CZ2 TRP A 143 1993 4032 1676 -27 4 499 C ATOM 1184 CZ3 TRP A 143 2.096 4.497 33.259 1.00 15.91 C ANISOU 1184 CZ3 TRP A 143 1559 3440 1047 146 69 328 C ATOM 1185 CH2 TRP A 143 3.266 5.169 32.871 1.00 19.06 C ANISOU 1185 CH2 TRP A 143 1861 3941 1439 104 73 489 C ATOM 1186 N ASN A 144 -3.226 10.379 32.117 1.00 16.60 N ANISOU 1186 N ASN A 144 1991 2663 1652 48 -191 -299 N ATOM 1187 CA ASN A 144 -3.702 11.016 30.894 1.00 16.94 C ANISOU 1187 CA ASN A 144 2082 2578 1778 93 -206 -265 C ATOM 1188 C ASN A 144 -3.379 12.511 30.956 1.00 20.33 C ANISOU 1188 C ASN A 144 2593 2848 2282 21 -294 -297 C ATOM 1189 O ASN A 144 -2.936 13.032 31.986 1.00 19.59 O ANISOU 1189 O ASN A 144 2551 2724 2169 -55 -366 -378 O ATOM 1190 CB ASN A 144 -5.201 10.761 30.692 1.00 15.63 C ANISOU 1190 CB ASN A 144 1918 2394 1625 211 -176 -321 C ATOM 1191 CG ASN A 144 -6.042 11.320 31.827 1.00 17.59 C ANISOU 1191 CG ASN A 144 2187 2649 1849 277 -167 -448 C ATOM 1192 OD1 ASN A 144 -5.983 12.508 32.101 1.00 22.63 O ANISOU 1192 OD1 ASN A 144 2926 3166 2505 292 -213 -535 O ATOM 1193 ND2 ASN A 144 -6.823 10.462 32.499 1.00 16.33 N ANISOU 1193 ND2 ASN A 144 1938 2631 1635 336 -118 -442 N ATOM 1194 N ASN A 145 -3.588 13.197 29.837 1.00 17.40 N ANISOU 1194 N ASN A 145 2254 2361 1997 43 -313 -230 N ATOM 1195 CA ASN A 145 -3.361 14.637 29.765 1.00 21.31 C ANISOU 1195 CA ASN A 145 2847 2659 2591 -32 -424 -235 C ATOM 1196 C ASN A 145 -4.654 15.438 29.922 1.00 23.06 C ANISOU 1196 C ASN A 145 3195 2727 2838 106 -433 -390 C ATOM 1197 O ASN A 145 -4.691 16.618 29.550 1.00 23.46 O ANISOU 1197 O ASN A 145 3355 2576 2984 89 -522 -385 O ATOM 1198 CB ASN A 145 -2.679 15.021 28.443 1.00 22.21 C ANISOU 1198 CB ASN A 145 2900 2751 2788 -92 -442 -12 C ATOM 1199 CG ASN A 145 -1.295 14.403 28.276 1.00 27.73 C ANISOU 1199 CG ASN A 145 3458 3636 3443 -192 -428 193 C ATOM 1200 OD1 ASN A 145 -0.597 14.137 29.251 1.00 27.69 O ANISOU 1200 OD1 ASN A 145 3423 3704 3394 -297 -465 178 O ATOM 1201 ND2 ASN A 145 -0.889 14.184 27.017 1.00 28.16 N ANISOU 1201 ND2 ASN A 145 3420 3793 3487 -130 -369 405 N ATOM 1202 N CYS A 146 -5.714 14.827 30.464 1.00 22.48 N ANISOU 1202 N CYS A 146 3099 2760 2682 252 -346 -497 N ATOM 1203 CA CYS A 146 -7.005 15.512 30.528 1.00 25.02 C ANISOU 1203 CA CYS A 146 3500 3004 3004 433 -324 -592 C ATOM 1204 C CYS A 146 -6.981 16.673 31.509 1.00 26.48 C ANISOU 1204 C CYS A 146 3885 3019 3156 492 -420 -758 C ATOM 1205 O CYS A 146 -7.743 17.629 31.346 1.00 30.16 O ANISOU 1205 O CYS A 146 4480 3338 3641 644 -439 -822 O ATOM 1206 CB CYS A 146 -8.113 14.526 30.890 1.00 27.92 C ANISOU 1206 CB CYS A 146 3742 3577 3289 564 -216 -594 C ATOM 1207 SG CYS A 146 -8.425 13.286 29.592 1.00 33.35 S ANISOU 1207 SG CYS A 146 4279 4373 4018 517 -178 -427 S ATOM 1208 N GLY A 147 -6.105 16.622 32.511 1.00 27.23 N ANISOU 1208 N GLY A 147 4035 3120 3191 389 -498 -831 N ATOM 1209 CA GLY A 147 -5.919 17.736 33.424 1.00 30.03 C ANISOU 1209 CA GLY A 147 4639 3269 3501 427 -651 -1006 C ATOM 1210 C GLY A 147 -5.227 18.938 32.817 1.00 34.34 C ANISOU 1210 C GLY A 147 5345 3503 4200 266 -845 -962 C ATOM 1211 O GLY A 147 -5.243 20.004 33.433 1.00 39.82 O ANISOU 1211 O GLY A 147 6311 3945 4872 318 -1016 -1121 O ATOM 1212 N GLN A 148 -4.622 18.800 31.637 1.00 32.95 N ANISOU 1212 N GLN A 148 5018 3333 4167 88 -838 -738 N ATOM 1213 CA GLN A 148 -3.931 19.903 30.961 1.00 36.80 C ANISOU 1213 CA GLN A 148 5599 3560 4824 -92 -1021 -612 C ATOM 1214 C GLN A 148 -4.459 20.053 29.538 1.00 35.44 C ANISOU 1214 C GLN A 148 5330 3383 4754 -24 -920 -454 C ATOM 1215 O GLN A 148 -3.742 19.806 28.563 1.00 33.39 O ANISOU 1215 O GLN A 148 4896 3214 4576 -162 -898 -210 O ATOM 1216 CB GLN A 148 -2.423 19.664 30.952 1.00 43.69 C ANISOU 1216 CB GLN A 148 6339 4502 5759 -395 -1130 -413 C ATOM 1217 CG GLN A 148 -1.815 19.371 32.315 1.00 56.92 C ANISOU 1217 CG GLN A 148 8071 6232 7325 -483 -1229 -541 C ATOM 1218 CD GLN A 148 -1.873 17.898 32.678 1.00 64.79 C ANISOU 1218 CD GLN A 148 8864 7576 8177 -398 -1015 -548 C ATOM 1219 OE1 GLN A 148 -1.816 17.028 31.806 1.00 66.50 O ANISOU 1219 OE1 GLN A 148 8873 7992 8403 -378 -852 -381 O ATOM 1220 NE2 GLN A 148 -1.993 17.613 33.971 1.00 69.42 N ANISOU 1220 NE2 GLN A 148 9531 8227 8617 -330 -1031 -741 N ATOM 1221 N PRO A 149 -5.728 20.429 29.381 1.00 33.88 N ANISOU 1221 N PRO A 149 5229 3116 4529 220 -845 -571 N ATOM 1222 CA PRO A 149 -6.292 20.541 28.035 1.00 30.05 C ANISOU 1222 CA PRO A 149 4646 2645 4125 294 -753 -422 C ATOM 1223 C PRO A 149 -5.608 21.648 27.241 1.00 31.70 C ANISOU 1223 C PRO A 149 4920 2612 4513 133 -907 -248 C ATOM 1224 O PRO A 149 -5.193 22.675 27.787 1.00 31.89 O ANISOU 1224 O PRO A 149 5158 2347 4612 35 -1116 -305 O ATOM 1225 CB PRO A 149 -7.768 20.871 28.298 1.00 32.33 C ANISOU 1225 CB PRO A 149 5042 2903 4338 591 -671 -584 C ATOM 1226 CG PRO A 149 -7.752 21.598 29.614 1.00 35.41 C ANISOU 1226 CG PRO A 149 5697 3106 4652 669 -798 -806 C ATOM 1227 CD PRO A 149 -6.668 20.903 30.417 1.00 34.77 C ANISOU 1227 CD PRO A 149 5556 3134 4522 463 -856 -823 C ATOM 1228 N LYS A 150 -5.476 21.414 25.936 1.00 29.71 N ANISOU 1228 N LYS A 150 4487 2478 4324 107 -824 -18 N ATOM 1229 CA LYS A 150 -4.972 22.420 25.003 1.00 33.13 C ANISOU 1229 CA LYS A 150 4925 2734 4928 -15 -936 212 C ATOM 1230 C LYS A 150 -6.124 23.365 24.701 1.00 33.65 C ANISOU 1230 C LYS A 150 5163 2581 5043 182 -942 120 C ATOM 1231 O LYS A 150 -6.908 23.159 23.771 1.00 31.70 O ANISOU 1231 O LYS A 150 4815 2453 4775 343 -802 183 O ATOM 1232 CB LYS A 150 -4.421 21.776 23.735 1.00 33.59 C ANISOU 1232 CB LYS A 150 4721 3054 4986 -52 -822 500 C ATOM 1233 CG LYS A 150 -3.125 20.983 23.937 1.00 35.70 C ANISOU 1233 CG LYS A 150 4818 3543 5205 -222 -820 654 C ATOM 1234 CD LYS A 150 -2.330 20.929 22.648 1.00 42.34 C ANISOU 1234 CD LYS A 150 5442 4568 6078 -261 -773 1022 C ATOM 1235 CE LYS A 150 -1.226 19.886 22.704 1.00 49.70 C ANISOU 1235 CE LYS A 150 6180 5810 6893 -314 -702 1180 C ATOM 1236 NZ LYS A 150 -0.403 20.021 23.921 1.00 57.50 N ANISOU 1236 NZ LYS A 150 7194 6731 7923 -545 -847 1149 N ATOM 1237 N GLU A 151 -6.217 24.423 25.504 1.00 38.01 N ANISOU 1237 N GLU A 151 5996 2799 5646 183 -1124 -32 N ATOM 1238 CA GLU A 151 -7.392 25.287 25.462 1.00 42.80 C ANISOU 1238 CA GLU A 151 6812 3198 6251 444 -1120 -167 C ATOM 1239 C GLU A 151 -7.445 26.112 24.185 1.00 39.99 C ANISOU 1239 C GLU A 151 6428 2701 6064 419 -1153 71 C ATOM 1240 O GLU A 151 -8.528 26.336 23.634 1.00 41.41 O ANISOU 1240 O GLU A 151 6615 2901 6219 661 -1034 55 O ATOM 1241 CB GLU A 151 -7.404 26.201 26.685 1.00 52.05 C ANISOU 1241 CB GLU A 151 8355 4024 7398 497 -1331 -413 C ATOM 1242 CG GLU A 151 -8.772 26.354 27.297 1.00 60.71 C ANISOU 1242 CG GLU A 151 9622 5125 8321 899 -1215 -665 C ATOM 1243 CD GLU A 151 -9.291 25.060 27.880 1.00 61.14 C ANISOU 1243 CD GLU A 151 9472 5580 8177 1034 -993 -764 C ATOM 1244 OE1 GLU A 151 -10.010 24.324 27.175 1.00 59.08 O ANISOU 1244 OE1 GLU A 151 8958 5605 7885 1130 -787 -657 O ATOM 1245 OE2 GLU A 151 -8.975 24.782 29.052 1.00 64.72 O ANISOU 1245 OE2 GLU A 151 10025 6056 8509 1031 -1048 -938 O ATOM 1246 N GLY A 152 -6.296 26.597 23.712 1.00 38.42 N ANISOU 1246 N GLY A 152 6179 2378 6039 128 -1319 327 N ATOM 1247 CA GLY A 152 -6.291 27.358 22.473 1.00 40.66 C ANISOU 1247 CA GLY A 152 6401 2562 6486 97 -1346 604 C ATOM 1248 C GLY A 152 -6.795 26.545 21.296 1.00 39.34 C ANISOU 1248 C GLY A 152 5950 2763 6233 251 -1087 744 C ATOM 1249 O GLY A 152 -7.553 27.046 20.459 1.00 38.05 O ANISOU 1249 O GLY A 152 5791 2557 6111 411 -1026 819 O ATOM 1250 N LYS A 153 -6.394 25.271 21.227 1.00 36.62 N ANISOU 1250 N LYS A 153 5382 2773 5758 217 -948 770 N ATOM 1251 CA LYS A 153 -6.878 24.397 20.165 1.00 36.71 C ANISOU 1251 CA LYS A 153 5183 3110 5656 378 -744 860 C ATOM 1252 C LYS A 153 -8.371 24.113 20.318 1.00 33.79 C ANISOU 1252 C LYS A 153 4878 2785 5175 642 -626 627 C ATOM 1253 O LYS A 153 -9.117 24.131 19.332 1.00 31.41 O ANISOU 1253 O LYS A 153 4501 2578 4854 794 -538 711 O ATOM 1254 CB LYS A 153 -6.072 23.096 20.166 1.00 35.55 C ANISOU 1254 CB LYS A 153 4847 3281 5380 304 -660 916 C ATOM 1255 CG LYS A 153 -6.291 22.213 18.958 1.00 35.76 C ANISOU 1255 CG LYS A 153 4699 3612 5277 458 -506 1039 C ATOM 1256 CD LYS A 153 -5.471 20.936 19.070 1.00 37.48 C ANISOU 1256 CD LYS A 153 4793 4102 5347 427 -440 1067 C ATOM 1257 CE LYS A 153 -4.002 21.227 19.342 1.00 41.51 C ANISOU 1257 CE LYS A 153 5212 4627 5933 207 -523 1292 C ATOM 1258 NZ LYS A 153 -3.144 20.028 19.126 1.00 42.81 N ANISOU 1258 NZ LYS A 153 5225 5113 5929 246 -426 1402 N ATOM 1259 N ALA A 154 -8.821 23.836 21.545 1.00 33.40 N ANISOU 1259 N ALA A 154 4947 2702 5041 704 -625 364 N ATOM 1260 CA ALA A 154 -10.250 23.636 21.780 1.00 33.84 C ANISOU 1260 CA ALA A 154 5029 2836 4994 959 -516 201 C ATOM 1261 C ALA A 154 -11.057 24.861 21.351 1.00 34.98 C ANISOU 1261 C ALA A 154 5305 2767 5217 1133 -538 230 C ATOM 1262 O ALA A 154 -12.091 24.731 20.677 1.00 34.05 O ANISOU 1262 O ALA A 154 5091 2791 5054 1314 -430 277 O ATOM 1263 CB ALA A 154 -10.500 23.312 23.256 1.00 32.09 C ANISOU 1263 CB ALA A 154 4912 2618 4662 1018 -516 -44 C ATOM 1264 N HIS A 155 -10.589 26.061 21.713 1.00 35.23 N ANISOU 1264 N HIS A 155 5567 2446 5371 1075 -700 216 N ATOM 1265 CA HIS A 155 -11.314 27.279 21.355 1.00 39.60 C ANISOU 1265 CA HIS A 155 6294 2748 6003 1260 -740 238 C ATOM 1266 C HIS A 155 -11.328 27.505 19.848 1.00 39.59 C ANISOU 1266 C HIS A 155 6121 2818 6103 1233 -694 520 C ATOM 1267 O HIS A 155 -12.363 27.876 19.285 1.00 39.68 O ANISOU 1267 O HIS A 155 6126 2853 6098 1460 -610 553 O ATOM 1268 CB HIS A 155 -10.709 28.488 22.067 1.00 47.96 C ANISOU 1268 CB HIS A 155 7679 3367 7177 1170 -977 161 C ATOM 1269 CG HIS A 155 -10.911 28.479 23.549 1.00 59.13 C ANISOU 1269 CG HIS A 155 9289 4742 8434 1267 -1003 -143 C ATOM 1270 ND1 HIS A 155 -12.116 28.153 24.131 1.00 64.78 N ANISOU 1270 ND1 HIS A 155 9991 5673 8951 1576 -825 -315 N ATOM 1271 CD2 HIS A 155 -10.064 28.754 24.568 1.00 65.80 C ANISOU 1271 CD2 HIS A 155 10320 5404 9276 1096 -1189 -275 C ATOM 1272 CE1 HIS A 155 -12.004 28.224 25.445 1.00 69.33 C ANISOU 1272 CE1 HIS A 155 10742 6205 9395 1618 -886 -539 C ATOM 1273 NE2 HIS A 155 -10.768 28.588 25.737 1.00 70.06 N ANISOU 1273 NE2 HIS A 155 10974 6046 9598 1334 -1113 -539 N ATOM 1274 N SER A 156 -10.194 27.295 19.175 1.00 39.18 N ANISOU 1274 N SER A 156 5914 2834 6139 983 -742 748 N ATOM 1275 CA SER A 156 -10.156 27.544 17.737 1.00 44.55 C ANISOU 1275 CA SER A 156 6429 3610 6889 989 -694 1039 C ATOM 1276 C SER A 156 -11.117 26.630 16.987 1.00 43.09 C ANISOU 1276 C SER A 156 6059 3770 6543 1187 -509 1028 C ATOM 1277 O SER A 156 -11.643 27.008 15.937 1.00 44.08 O ANISOU 1277 O SER A 156 6113 3946 6689 1309 -459 1186 O ATOM 1278 CB SER A 156 -8.731 27.383 17.206 1.00 49.46 C ANISOU 1278 CB SER A 156 6884 4320 7590 726 -756 1320 C ATOM 1279 OG SER A 156 -8.266 26.064 17.421 1.00 55.11 O ANISOU 1279 OG SER A 156 7446 5342 8151 675 -666 1261 O ATOM 1280 N AGLN A 157 -11.369 25.437 17.515 0.50 40.82 N ANISOU 1280 N AGLN A 157 5699 3711 6099 1211 -431 856 N ATOM 1281 N BGLN A 157 -11.362 25.432 17.511 0.50 40.81 N ANISOU 1281 N BGLN A 157 5697 3711 6098 1210 -430 857 N ATOM 1282 CA AGLN A 157 -12.287 24.492 16.899 0.50 39.08 C ANISOU 1282 CA AGLN A 157 5328 3787 5735 1354 -317 843 C ATOM 1283 CA BGLN A 157 -12.285 24.489 16.899 0.50 39.08 C ANISOU 1283 CA BGLN A 157 5327 3787 5735 1354 -317 843 C ATOM 1284 C AGLN A 157 -13.724 24.669 17.370 0.50 38.90 C ANISOU 1284 C AGLN A 157 5351 3768 5661 1570 -262 706 C ATOM 1285 C BGLN A 157 -13.720 24.665 17.374 0.50 38.89 C ANISOU 1285 C BGLN A 157 5350 3767 5660 1569 -262 705 C ATOM 1286 O AGLN A 157 -14.600 23.901 16.957 0.50 39.36 O ANISOU 1286 O AGLN A 157 5273 4068 5615 1663 -201 714 O ATOM 1287 O BGLN A 157 -14.586 23.879 16.974 0.50 39.32 O ANISOU 1287 O BGLN A 157 5268 4065 5608 1659 -202 711 O ATOM 1288 CB AGLN A 157 -11.821 23.062 17.184 0.50 38.09 C ANISOU 1288 CB AGLN A 157 5102 3890 5479 1256 -291 766 C ATOM 1289 CB BGLN A 157 -11.837 23.053 17.181 0.50 38.08 C ANISOU 1289 CB BGLN A 157 5100 3891 5476 1258 -290 765 C ATOM 1290 CG AGLN A 157 -12.385 22.029 16.239 0.50 39.79 C ANISOU 1290 CG AGLN A 157 5184 4376 5558 1341 -244 811 C ATOM 1291 CG BGLN A 157 -10.477 22.696 16.619 0.50 38.80 C ANISOU 1291 CG BGLN A 157 5110 4071 5562 1113 -309 931 C ATOM 1292 CD AGLN A 157 -11.813 20.669 16.493 0.50 40.78 C ANISOU 1292 CD AGLN A 157 5265 4668 5561 1253 -249 739 C ATOM 1293 CD BGLN A 157 -10.219 21.214 16.692 0.50 40.52 C ANISOU 1293 CD BGLN A 157 5253 4527 5617 1094 -274 856 C ATOM 1294 OE1AGLN A 157 -10.712 20.357 16.040 0.50 41.62 O ANISOU 1294 OE1AGLN A 157 5338 4845 5630 1190 -251 848 O ATOM 1295 OE1BGLN A 157 -9.095 20.750 16.498 0.50 41.53 O ANISOU 1295 OE1BGLN A 157 5323 4758 5699 1013 -273 959 O ATOM 1296 NE2AGLN A 157 -12.548 19.846 17.235 0.50 40.10 N ANISOU 1296 NE2AGLN A 157 5170 4661 5407 1262 -249 584 N ATOM 1297 NE2BGLN A 157 -11.269 20.452 16.978 0.50 40.89 N ANISOU 1297 NE2BGLN A 157 5295 4667 5574 1176 -256 701 N ATOM 1298 N GLY A 158 -13.992 25.655 18.220 1.00 38.00 N ANISOU 1298 N GLY A 158 5432 3402 5605 1666 -298 597 N ATOM 1299 CA GLY A 158 -15.341 25.867 18.698 1.00 37.27 C ANISOU 1299 CA GLY A 158 5363 3366 5431 1917 -222 498 C ATOM 1300 C GLY A 158 -15.842 24.824 19.673 1.00 40.54 C ANISOU 1300 C GLY A 158 5699 4004 5702 1967 -159 356 C ATOM 1301 O GLY A 158 -17.056 24.692 19.845 1.00 43.93 O ANISOU 1301 O GLY A 158 6017 4633 6042 2104 -75 353 O ATOM 1302 N CYS A 159 -14.945 24.081 20.326 1.00 37.24 N ANISOU 1302 N CYS A 159 5283 3607 5259 1777 -198 261 N ATOM 1303 CA CYS A 159 -15.375 23.065 21.277 1.00 35.21 C ANISOU 1303 CA CYS A 159 4934 3568 4875 1800 -143 151 C ATOM 1304 C CYS A 159 -16.118 23.694 22.448 1.00 38.50 C ANISOU 1304 C CYS A 159 5487 3933 5210 2059 -99 18 C ATOM 1305 O CYS A 159 -15.911 24.858 22.796 1.00 42.59 O ANISOU 1305 O CYS A 159 6234 4184 5766 2126 -152 -66 O ATOM 1306 CB CYS A 159 -14.177 22.267 21.792 1.00 35.06 C ANISOU 1306 CB CYS A 159 4916 3558 4849 1559 -194 78 C ATOM 1307 SG CYS A 159 -13.354 21.290 20.518 1.00 36.61 S ANISOU 1307 SG CYS A 159 4955 3893 5061 1347 -219 232 S ATOM 1308 N GLY A 160 -16.990 22.909 23.059 1.00 38.44 N ANISOU 1308 N GLY A 160 5317 4211 5077 2160 -10 17 N ATOM 1309 CA GLY A 160 -17.725 23.379 24.208 1.00 43.08 C ANISOU 1309 CA GLY A 160 5974 4860 5535 2360 58 -77 C ATOM 1310 C GLY A 160 -16.912 23.302 25.480 1.00 46.50 C ANISOU 1310 C GLY A 160 6580 5187 5902 2340 13 -274 C ATOM 1311 O GLY A 160 -15.821 22.731 25.526 1.00 44.68 O ANISOU 1311 O GLY A 160 6373 4872 5730 2138 -64 -328 O ATOM 1312 N GLU A 161 -17.466 23.903 26.531 1.00 50.85 N ANISOU 1312 N GLU A 161 7253 5764 6305 2545 56 -371 N ATOM 1313 CA GLU A 161 -16.814 23.894 27.831 1.00 53.66 C ANISOU 1313 CA GLU A 161 7784 6047 6556 2552 4 -562 C ATOM 1314 C GLU A 161 -16.603 22.466 28.307 1.00 49.76 C ANISOU 1314 C GLU A 161 7074 5818 6016 2450 54 -539 C ATOM 1315 O GLU A 161 -17.507 21.630 28.227 1.00 54.35 O ANISOU 1315 O GLU A 161 7375 6731 6544 2499 164 -377 O ATOM 1316 CB GLU A 161 -17.647 24.674 28.847 1.00 63.50 C ANISOU 1316 CB GLU A 161 9173 7358 7598 2848 54 -633 C ATOM 1317 CG GLU A 161 -17.278 26.137 28.948 1.00 73.21 C ANISOU 1317 CG GLU A 161 10763 8208 8846 2915 -81 -775 C ATOM 1318 CD GLU A 161 -18.034 26.847 30.059 1.00 84.02 C ANISOU 1318 CD GLU A 161 12314 9647 9964 3248 -51 -864 C ATOM 1319 OE1 GLU A 161 -19.116 26.354 30.452 1.00 87.43 O ANISOU 1319 OE1 GLU A 161 12545 10455 10221 3460 112 -744 O ATOM 1320 OE2 GLU A 161 -17.545 27.892 30.542 1.00 88.98 O ANISOU 1320 OE2 GLU A 161 13289 9961 10560 3299 -208 -1033 O ATOM 1321 N GLY A 162 -15.398 22.188 28.793 1.00 49.18 N ANISOU 1321 N GLY A 162 6414 5983 6289 2408 728 -337 N ATOM 1322 CA GLY A 162 -15.043 20.857 29.222 1.00 46.38 C ANISOU 1322 CA GLY A 162 5960 5783 5879 2284 851 -261 C ATOM 1323 C GLY A 162 -14.681 19.898 28.110 1.00 46.12 C ANISOU 1323 C GLY A 162 5715 5790 6019 2061 749 -182 C ATOM 1324 O GLY A 162 -14.445 18.717 28.392 1.00 48.97 O ANISOU 1324 O GLY A 162 5960 6271 6377 1943 848 -104 O ATOM 1325 N GLN A 163 -14.642 20.349 26.858 1.00 38.84 N ANISOU 1325 N GLN A 163 4758 4769 5231 2017 546 -185 N ATOM 1326 CA GLN A 163 -14.272 19.489 25.741 1.00 34.75 C ANISOU 1326 CA GLN A 163 4094 4291 4820 1802 393 -118 C ATOM 1327 C GLN A 163 -12.887 19.852 25.222 1.00 31.55 C ANISOU 1327 C GLN A 163 3955 3755 4277 1613 208 -186 C ATOM 1328 O GLN A 163 -12.398 20.969 25.418 1.00 32.31 O ANISOU 1328 O GLN A 163 4295 3678 4305 1681 143 -269 O ATOM 1329 CB GLN A 163 -15.277 19.599 24.589 1.00 34.66 C ANISOU 1329 CB GLN A 163 3849 4281 5041 1842 248 -39 C ATOM 1330 CG GLN A 163 -16.644 19.022 24.871 1.00 35.51 C ANISOU 1330 CG GLN A 163 3581 4494 5418 1904 367 62 C ATOM 1331 CD GLN A 163 -17.533 19.118 23.657 1.00 40.02 C ANISOU 1331 CD GLN A 163 3935 5033 6238 1924 117 98 C ATOM 1332 OE1 GLN A 163 -17.384 20.027 22.839 1.00 39.76 O ANISOU 1332 OE1 GLN A 163 4079 4897 6131 1995 -58 68 O ATOM 1333 NE2 GLN A 163 -18.458 18.178 23.524 1.00 45.05 N ANISOU 1333 NE2 GLN A 163 4232 5762 7123 1853 72 159 N ATOM 1334 N VAL A 164 -12.274 18.893 24.526 1.00 22.87 N ANISOU 1334 N VAL A 164 2789 2720 3179 1385 122 -135 N ATOM 1335 CA VAL A 164 -11.000 19.091 23.850 1.00 27.74 C ANISOU 1335 CA VAL A 164 3586 3241 3713 1216 -4 -130 C ATOM 1336 C VAL A 164 -11.119 18.595 22.415 1.00 27.27 C ANISOU 1336 C VAL A 164 3444 3232 3684 1156 -138 -41 C ATOM 1337 O VAL A 164 -11.979 17.772 22.080 1.00 25.41 O ANISOU 1337 O VAL A 164 3005 3104 3544 1176 -186 -26 O ATOM 1338 CB VAL A 164 -9.838 18.354 24.557 1.00 28.57 C ANISOU 1338 CB VAL A 164 3759 3381 3714 1049 42 -170 C ATOM 1339 CG1 VAL A 164 -9.656 18.883 25.970 1.00 28.82 C ANISOU 1339 CG1 VAL A 164 3946 3348 3655 1164 110 -292 C ATOM 1340 CG2 VAL A 164 -10.096 16.838 24.569 1.00 26.51 C ANISOU 1340 CG2 VAL A 164 3302 3299 3473 956 103 -125 C ATOM 1341 N ALA A 165 -10.236 19.101 21.564 1.00 22.83 N ANISOU 1341 N ALA A 165 3048 2573 3054 1105 -207 28 N ATOM 1342 CA ALA A 165 -10.028 18.452 20.279 1.00 24.00 C ANISOU 1342 CA ALA A 165 3204 2792 3124 1083 -305 108 C ATOM 1343 C ALA A 165 -9.476 17.049 20.529 1.00 23.35 C ANISOU 1343 C ALA A 165 3043 2834 2994 929 -275 71 C ATOM 1344 O ALA A 165 -8.445 16.885 21.196 1.00 22.55 O ANISOU 1344 O ALA A 165 2991 2718 2859 796 -177 66 O ATOM 1345 CB ALA A 165 -9.074 19.280 19.415 1.00 23.26 C ANISOU 1345 CB ALA A 165 3308 2575 2955 1092 -292 254 C ATOM 1346 N CYS A 166 -10.178 16.031 20.041 1.00 21.36 N ANISOU 1346 N CYS A 166 2660 2680 2776 950 -394 35 N ATOM 1347 CA CYS A 166 -9.797 14.651 20.350 1.00 21.18 C ANISOU 1347 CA CYS A 166 2551 2742 2755 813 -381 -5 C ATOM 1348 C CYS A 166 -8.680 14.226 19.399 1.00 22.48 C ANISOU 1348 C CYS A 166 2890 2927 2726 794 -415 37 C ATOM 1349 O CYS A 166 -8.931 13.832 18.250 1.00 26.10 O ANISOU 1349 O CYS A 166 3418 3406 3091 912 -588 24 O ATOM 1350 CB CYS A 166 -10.998 13.718 20.253 1.00 24.29 C ANISOU 1350 CB CYS A 166 2707 3173 3350 830 -524 -57 C ATOM 1351 SG CYS A 166 -10.571 12.025 20.682 1.00 28.77 S ANISOU 1351 SG CYS A 166 3164 3788 3978 657 -512 -87 S ATOM 1352 N LEU A 167 -7.443 14.337 19.881 1.00 19.37 N ANISOU 1352 N LEU A 167 2572 2518 2268 680 -260 89 N ATOM 1353 CA LEU A 167 -6.235 14.014 19.137 1.00 20.62 C ANISOU 1353 CA LEU A 167 2858 2699 2279 671 -210 179 C ATOM 1354 C LEU A 167 -5.360 13.123 20.004 1.00 19.37 C ANISOU 1354 C LEU A 167 2633 2583 2143 507 -123 146 C ATOM 1355 O LEU A 167 -5.144 13.425 21.184 1.00 20.07 O ANISOU 1355 O LEU A 167 2667 2634 2324 404 -56 112 O ATOM 1356 CB LEU A 167 -5.489 15.288 18.737 1.00 21.24 C ANISOU 1356 CB LEU A 167 3054 2671 2347 706 -100 344 C ATOM 1357 CG LEU A 167 -6.298 16.115 17.722 1.00 24.78 C ANISOU 1357 CG LEU A 167 3609 3078 2728 911 -182 410 C ATOM 1358 CD1 LEU A 167 -5.776 17.531 17.647 1.00 25.47 C ANISOU 1358 CD1 LEU A 167 3770 3001 2907 915 -67 584 C ATOM 1359 CD2 LEU A 167 -6.267 15.418 16.350 1.00 28.40 C ANISOU 1359 CD2 LEU A 167 4217 3634 2938 1107 -257 451 C ATOM 1360 N PHE A 168 -4.851 12.041 19.413 1.00 18.10 N ANISOU 1360 N PHE A 168 2509 2494 1873 523 -144 145 N ATOM 1361 CA PHE A 168 -4.178 10.991 20.178 1.00 15.38 C ANISOU 1361 CA PHE A 168 2094 2194 1555 392 -94 104 C ATOM 1362 C PHE A 168 -3.095 11.553 21.095 1.00 16.53 C ANISOU 1362 C PHE A 168 2216 2295 1769 267 32 164 C ATOM 1363 O PHE A 168 -3.092 11.288 22.304 1.00 16.18 O ANISOU 1363 O PHE A 168 2108 2252 1787 173 41 93 O ATOM 1364 CB PHE A 168 -3.569 9.942 19.235 1.00 16.44 C ANISOU 1364 CB PHE A 168 2320 2387 1538 476 -121 111 C ATOM 1365 CG PHE A 168 -2.987 8.750 19.963 1.00 16.87 C ANISOU 1365 CG PHE A 168 2303 2474 1632 361 -95 63 C ATOM 1366 CD1 PHE A 168 -3.756 7.616 20.182 1.00 16.44 C ANISOU 1366 CD1 PHE A 168 2179 2411 1658 333 -231 -53 C ATOM 1367 CD2 PHE A 168 -1.673 8.781 20.455 1.00 17.67 C ANISOU 1367 CD2 PHE A 168 2383 2589 1742 279 49 150 C ATOM 1368 CE1 PHE A 168 -3.222 6.510 20.877 1.00 17.14 C ANISOU 1368 CE1 PHE A 168 2212 2508 1791 236 -197 -71 C ATOM 1369 CE2 PHE A 168 -1.132 7.684 21.146 1.00 15.79 C ANISOU 1369 CE2 PHE A 168 2090 2379 1530 196 59 110 C ATOM 1370 CZ PHE A 168 -1.911 6.551 21.349 1.00 16.07 C ANISOU 1370 CZ PHE A 168 2092 2410 1602 182 -51 4 C ATOM 1371 N GLU A 169 -2.146 12.310 20.535 1.00 15.81 N ANISOU 1371 N GLU A 169 2174 2148 1684 281 118 310 N ATOM 1372 CA GLU A 169 -1.020 12.768 21.343 1.00 18.34 C ANISOU 1372 CA GLU A 169 2429 2383 2156 145 168 361 C ATOM 1373 C GLU A 169 -1.386 13.922 22.266 1.00 21.41 C ANISOU 1373 C GLU A 169 2824 2633 2678 97 93 287 C ATOM 1374 O GLU A 169 -0.580 14.272 23.134 1.00 20.19 O ANISOU 1374 O GLU A 169 2634 2376 2660 -6 41 260 O ATOM 1375 CB GLU A 169 0.171 13.170 20.446 1.00 20.78 C ANISOU 1375 CB GLU A 169 2721 2645 2531 163 306 594 C ATOM 1376 CG GLU A 169 0.780 11.976 19.682 1.00 15.90 C ANISOU 1376 CG GLU A 169 2120 2167 1754 257 408 662 C ATOM 1377 CD GLU A 169 2.055 12.293 18.905 1.00 21.98 C ANISOU 1377 CD GLU A 169 2835 2913 2604 310 623 945 C ATOM 1378 OE1 GLU A 169 2.678 13.373 19.106 1.00 23.79 O ANISOU 1378 OE1 GLU A 169 2946 2983 3112 204 679 1108 O ATOM 1379 OE2 GLU A 169 2.442 11.448 18.067 1.00 23.32 O ANISOU 1379 OE2 GLU A 169 3076 3206 2580 478 743 1019 O ATOM 1380 N ASP A 170 -2.564 14.528 22.108 1.00 17.66 N ANISOU 1380 N ASP A 170 2401 2137 2173 193 55 238 N ATOM 1381 CA ASP A 170 -2.962 15.530 23.087 1.00 19.83 C ANISOU 1381 CA ASP A 170 2712 2284 2537 198 -13 135 C ATOM 1382 C ASP A 170 -3.481 14.892 24.371 1.00 20.11 C ANISOU 1382 C ASP A 170 2742 2404 2493 215 -26 -25 C ATOM 1383 O ASP A 170 -3.335 15.484 25.437 1.00 23.86 O ANISOU 1383 O ASP A 170 3294 2784 2988 236 -89 -132 O ATOM 1384 CB ASP A 170 -4.033 16.478 22.526 1.00 19.97 C ANISOU 1384 CB ASP A 170 2783 2242 2562 330 -30 153 C ATOM 1385 CG ASP A 170 -3.499 17.412 21.422 1.00 25.45 C ANISOU 1385 CG ASP A 170 3524 2803 3343 348 3 350 C ATOM 1386 OD1 ASP A 170 -2.277 17.401 21.139 1.00 23.78 O ANISOU 1386 OD1 ASP A 170 3273 2534 3230 250 67 494 O ATOM 1387 OD2 ASP A 170 -4.313 18.178 20.846 1.00 28.14 O ANISOU 1387 OD2 ASP A 170 3926 3090 3675 475 -16 390 O ATOM 1388 N VAL A 171 -4.113 13.718 24.299 1.00 18.20 N ANISOU 1388 N VAL A 171 2427 2319 2169 233 25 -36 N ATOM 1389 CA VAL A 171 -4.742 13.131 25.473 1.00 16.12 C ANISOU 1389 CA VAL A 171 2138 2131 1856 278 80 -113 C ATOM 1390 C VAL A 171 -3.948 11.957 26.065 1.00 16.48 C ANISOU 1390 C VAL A 171 2166 2250 1844 195 103 -113 C ATOM 1391 O VAL A 171 -4.027 11.737 27.281 1.00 18.79 O ANISOU 1391 O VAL A 171 2510 2572 2059 253 149 -161 O ATOM 1392 CB VAL A 171 -6.201 12.712 25.186 1.00 19.00 C ANISOU 1392 CB VAL A 171 2374 2571 2273 360 128 -91 C ATOM 1393 CG1 VAL A 171 -7.047 13.955 24.773 1.00 23.64 C ANISOU 1393 CG1 VAL A 171 2982 3086 2916 481 97 -98 C ATOM 1394 CG2 VAL A 171 -6.286 11.609 24.108 1.00 14.67 C ANISOU 1394 CG2 VAL A 171 1730 2079 1766 296 63 -48 C ATOM 1395 N VAL A 172 -3.225 11.180 25.263 1.00 14.38 N ANISOU 1395 N VAL A 172 1855 2020 1588 105 85 -54 N ATOM 1396 CA VAL A 172 -2.509 9.997 25.748 1.00 16.02 C ANISOU 1396 CA VAL A 172 2041 2291 1755 42 103 -49 C ATOM 1397 C VAL A 172 -1.073 10.415 26.053 1.00 15.80 C ANISOU 1397 C VAL A 172 2053 2197 1752 -24 39 -48 C ATOM 1398 O VAL A 172 -0.371 10.866 25.136 1.00 14.69 O ANISOU 1398 O VAL A 172 1883 2005 1694 -66 31 32 O ATOM 1399 CB VAL A 172 -2.532 8.832 24.737 1.00 17.86 C ANISOU 1399 CB VAL A 172 2212 2580 1994 18 98 -6 C ATOM 1400 CG1 VAL A 172 -1.866 7.584 25.383 1.00 16.99 C ANISOU 1400 CG1 VAL A 172 2085 2513 1858 -33 119 0 C ATOM 1401 CG2 VAL A 172 -3.972 8.492 24.277 1.00 18.08 C ANISOU 1401 CG2 VAL A 172 2161 2617 2093 68 71 -20 C ATOM 1402 N PRO A 173 -0.596 10.275 27.298 1.00 15.86 N ANISOU 1402 N PRO A 173 2119 2196 1711 -16 -13 -117 N ATOM 1403 CA PRO A 173 0.780 10.699 27.611 1.00 18.90 C ANISOU 1403 CA PRO A 173 2503 2482 2196 -86 -151 -133 C ATOM 1404 C PRO A 173 1.801 9.843 26.875 1.00 16.07 C ANISOU 1404 C PRO A 173 2021 2172 1912 -170 -111 -20 C ATOM 1405 O PRO A 173 1.655 8.616 26.771 1.00 14.23 O ANISOU 1405 O PRO A 173 1772 2051 1583 -154 -33 4 O ATOM 1406 CB PRO A 173 0.892 10.496 29.134 1.00 18.00 C ANISOU 1406 CB PRO A 173 2523 2374 1944 4 -248 -256 C ATOM 1407 CG PRO A 173 -0.559 10.348 29.619 1.00 20.52 C ANISOU 1407 CG PRO A 173 2924 2781 2090 151 -95 -274 C ATOM 1408 CD PRO A 173 -1.273 9.681 28.465 1.00 16.24 C ANISOU 1408 CD PRO A 173 2232 2318 1619 84 51 -159 C ATOM 1409 N AMET A 174 2.850 10.496 26.375 0.80 13.74 N ANISOU 1409 N AMET A 174 1626 1773 1822 -248 -155 67 N ATOM 1410 N BMET A 174 2.846 10.500 26.365 0.20 14.99 N ANISOU 1410 N BMET A 174 1784 1931 1981 -248 -154 68 N ATOM 1411 CA AMET A 174 3.856 9.735 25.646 0.80 15.56 C ANISOU 1411 CA AMET A 174 1726 2060 2126 -280 -64 208 C ATOM 1412 CA BMET A 174 3.884 9.759 25.659 0.20 15.67 C ANISOU 1412 CA BMET A 174 1737 2070 2146 -282 -68 208 C ATOM 1413 C AMET A 174 4.738 8.916 26.592 0.80 16.26 C ANISOU 1413 C AMET A 174 1774 2173 2231 -303 -173 158 C ATOM 1414 C BMET A 174 4.709 8.899 26.607 0.20 16.07 C ANISOU 1414 C BMET A 174 1755 2152 2200 -301 -172 154 C ATOM 1415 O AMET A 174 5.248 7.869 26.188 0.80 17.70 O ANISOU 1415 O AMET A 174 1894 2450 2381 -281 -80 232 O ATOM 1416 O BMET A 174 5.162 7.820 26.210 0.20 16.39 O ANISOU 1416 O BMET A 174 1740 2291 2197 -276 -78 224 O ATOM 1417 CB AMET A 174 4.703 10.662 24.768 0.80 18.36 C ANISOU 1417 CB AMET A 174 1938 2298 2740 -332 -5 395 C ATOM 1418 CB BMET A 174 4.799 10.703 24.883 0.20 18.25 C ANISOU 1418 CB BMET A 174 1915 2271 2750 -343 -26 389 C ATOM 1419 CG AMET A 174 5.414 9.947 23.620 0.80 19.40 C ANISOU 1419 CG AMET A 174 1971 2531 2868 -270 208 595 C ATOM 1420 CG BMET A 174 4.141 11.350 23.685 0.20 18.63 C ANISOU 1420 CG BMET A 174 2009 2314 2755 -277 129 509 C ATOM 1421 SD AMET A 174 4.255 9.121 22.486 0.80 19.22 S ANISOU 1421 SD AMET A 174 2137 2676 2489 -93 353 570 S ATOM 1422 SD BMET A 174 3.466 10.208 22.457 0.20 19.61 S ANISOU 1422 SD BMET A 174 2245 2642 2565 -109 308 546 S ATOM 1423 CE AMET A 174 3.985 10.420 21.292 0.80 20.91 C ANISOU 1423 CE AMET A 174 2383 2819 2743 -16 484 754 C ATOM 1424 CE BMET A 174 4.949 9.807 21.552 0.20 20.93 C ANISOU 1424 CE BMET A 174 2273 2848 2830 -48 514 801 C ATOM 1425 N ASN A 175 4.928 9.342 27.853 1.00 14.74 N ANISOU 1425 N ASN A 175 1647 1893 2060 -309 -388 19 N ATOM 1426 CA ASN A 175 5.662 8.469 28.777 1.00 15.01 C ANISOU 1426 CA ASN A 175 1685 1967 2051 -285 -512 -35 C ATOM 1427 C ASN A 175 4.901 7.155 28.992 1.00 15.13 C ANISOU 1427 C ASN A 175 1811 2145 1792 -197 -364 -41 C ATOM 1428 O ASN A 175 5.510 6.076 28.999 1.00 14.44 O ANISOU 1428 O ASN A 175 1671 2124 1693 -188 -338 12 O ATOM 1429 CB ASN A 175 6.033 9.162 30.113 1.00 16.73 C ANISOU 1429 CB ASN A 175 2012 2051 2295 -248 -830 -211 C ATOM 1430 CG ASN A 175 4.869 9.912 30.793 1.00 18.42 C ANISOU 1430 CG ASN A 175 2471 2234 2294 -126 -867 -365 C ATOM 1431 OD1 ASN A 175 3.688 9.651 30.552 1.00 17.20 O ANISOU 1431 OD1 ASN A 175 2395 2195 1945 -61 -641 -334 O ATOM 1432 ND2 ASN A 175 5.230 10.837 31.684 1.00 18.71 N ANISOU 1432 ND2 ASN A 175 2625 2097 2388 -73 -1182 -541 N ATOM 1433 N TYR A 176 3.564 7.213 29.078 1.00 14.00 N ANISOU 1433 N TYR A 176 1787 2048 1485 -137 -255 -78 N ATOM 1434 CA TYR A 176 2.773 5.975 29.079 1.00 13.90 C ANISOU 1434 CA TYR A 176 1804 2140 1336 -90 -102 -32 C ATOM 1435 C TYR A 176 3.046 5.156 27.819 1.00 13.01 C ANISOU 1435 C TYR A 176 1584 2062 1298 -136 -14 53 C ATOM 1436 O TYR A 176 3.285 3.944 27.882 1.00 12.34 O ANISOU 1436 O TYR A 176 1492 2014 1183 -118 14 85 O ATOM 1437 CB TYR A 176 1.265 6.279 29.189 1.00 12.03 C ANISOU 1437 CB TYR A 176 1626 1922 1021 -32 10 -46 C ATOM 1438 CG TYR A 176 0.418 5.050 28.862 1.00 13.47 C ANISOU 1438 CG TYR A 176 1750 2154 1214 -35 143 35 C ATOM 1439 CD1 TYR A 176 -0.048 4.822 27.558 1.00 13.97 C ANISOU 1439 CD1 TYR A 176 1726 2204 1377 -84 159 52 C ATOM 1440 CD2 TYR A 176 0.141 4.083 29.849 1.00 13.65 C ANISOU 1440 CD2 TYR A 176 1813 2208 1165 28 225 99 C ATOM 1441 CE1 TYR A 176 -0.792 3.681 27.240 1.00 13.11 C ANISOU 1441 CE1 TYR A 176 1554 2080 1348 -96 193 92 C ATOM 1442 CE2 TYR A 176 -0.592 2.936 29.551 1.00 15.47 C ANISOU 1442 CE2 TYR A 176 1951 2422 1504 -3 320 194 C ATOM 1443 CZ TYR A 176 -1.047 2.736 28.234 1.00 17.92 C ANISOU 1443 CZ TYR A 176 2155 2686 1966 -80 272 170 C ATOM 1444 OH TYR A 176 -1.781 1.610 27.906 1.00 18.43 O ANISOU 1444 OH TYR A 176 2121 2678 2205 -119 281 229 O ATOM 1445 N MET A 177 3.013 5.807 26.654 1.00 12.65 N ANISOU 1445 N MET A 177 1485 1995 1326 -159 28 90 N ATOM 1446 CA MET A 177 3.113 5.051 25.410 1.00 14.80 C ANISOU 1446 CA MET A 177 1732 2308 1583 -119 110 148 C ATOM 1447 C MET A 177 4.478 4.386 25.264 1.00 14.09 C ANISOU 1447 C MET A 177 1569 2242 1543 -100 129 218 C ATOM 1448 O MET A 177 4.574 3.307 24.676 1.00 13.35 O ANISOU 1448 O MET A 177 1504 2183 1384 -24 174 226 O ATOM 1449 CB MET A 177 2.843 5.967 24.204 1.00 14.44 C ANISOU 1449 CB MET A 177 1693 2247 1548 -82 167 199 C ATOM 1450 CG MET A 177 1.346 6.332 24.045 1.00 14.03 C ANISOU 1450 CG MET A 177 1702 2182 1446 -62 139 128 C ATOM 1451 SD MET A 177 0.290 4.866 23.924 1.00 14.83 S ANISOU 1451 SD MET A 177 1823 2298 1515 -30 91 55 S ATOM 1452 CE MET A 177 0.880 4.169 22.372 1.00 13.94 C ANISOU 1452 CE MET A 177 1792 2205 1300 107 82 64 C ATOM 1453 N VAL A 178 5.538 5.024 25.755 1.00 12.92 N ANISOU 1453 N VAL A 178 1315 2053 1540 -154 72 264 N ATOM 1454 CA VAL A 178 6.895 4.508 25.552 1.00 13.24 C ANISOU 1454 CA VAL A 178 1220 2111 1700 -130 103 366 C ATOM 1455 C VAL A 178 7.310 3.560 26.669 1.00 15.63 C ANISOU 1455 C VAL A 178 1539 2431 1970 -123 -18 303 C ATOM 1456 O VAL A 178 7.714 2.416 26.410 1.00 13.11 O ANISOU 1456 O VAL A 178 1215 2160 1607 -45 41 336 O ATOM 1457 CB VAL A 178 7.887 5.676 25.396 1.00 13.37 C ANISOU 1457 CB VAL A 178 1040 2039 2001 -202 87 490 C ATOM 1458 CG1 VAL A 178 9.376 5.191 25.438 1.00 15.02 C ANISOU 1458 CG1 VAL A 178 1029 2250 2429 -188 94 616 C ATOM 1459 CG2 VAL A 178 7.603 6.390 24.100 1.00 14.58 C ANISOU 1459 CG2 VAL A 178 1189 2190 2162 -157 279 624 C ATOM 1460 N TYR A 179 7.225 4.011 27.929 1.00 12.05 N ANISOU 1460 N TYR A 179 1139 1928 1511 -164 -197 208 N ATOM 1461 CA TYR A 179 7.733 3.183 29.017 1.00 12.65 C ANISOU 1461 CA TYR A 179 1258 2021 1528 -113 -325 170 C ATOM 1462 C TYR A 179 6.787 2.044 29.365 1.00 14.70 C ANISOU 1462 C TYR A 179 1680 2336 1570 -45 -230 156 C ATOM 1463 O TYR A 179 7.224 0.916 29.603 1.00 17.04 O ANISOU 1463 O TYR A 179 1985 2654 1837 13 -228 195 O ATOM 1464 CB TYR A 179 7.969 4.035 30.266 1.00 14.10 C ANISOU 1464 CB TYR A 179 1507 2128 1722 -111 -582 55 C ATOM 1465 CG TYR A 179 9.122 4.987 30.149 1.00 16.88 C ANISOU 1465 CG TYR A 179 1648 2360 2404 -198 -769 71 C ATOM 1466 CD1 TYR A 179 9.003 6.306 30.583 1.00 19.18 C ANISOU 1466 CD1 TYR A 179 1975 2512 2800 -245 -971 -36 C ATOM 1467 CD2 TYR A 179 10.348 4.565 29.660 1.00 19.62 C ANISOU 1467 CD2 TYR A 179 1744 2706 3005 -224 -757 202 C ATOM 1468 CE1 TYR A 179 10.075 7.188 30.527 1.00 20.02 C ANISOU 1468 CE1 TYR A 179 1849 2445 3312 -352 -1191 -12 C ATOM 1469 CE2 TYR A 179 11.431 5.447 29.587 1.00 22.80 C ANISOU 1469 CE2 TYR A 179 1878 2965 3821 -323 -927 263 C ATOM 1470 CZ TYR A 179 11.280 6.756 30.017 1.00 23.55 C ANISOU 1470 CZ TYR A 179 2002 2888 4058 -401 -1148 155 C ATOM 1471 OH TYR A 179 12.346 7.631 29.944 1.00 26.74 O ANISOU 1471 OH TYR A 179 2224 3097 4838 -474 -1236 217 O ATOM 1472 N PHE A 180 5.498 2.335 29.471 1.00 13.76 N ANISOU 1472 N PHE A 180 1668 2219 1341 -48 -154 122 N ATOM 1473 CA PHE A 180 4.541 1.363 29.977 1.00 15.74 C ANISOU 1473 CA PHE A 180 2021 2486 1474 3 -56 156 C ATOM 1474 C PHE A 180 4.018 0.505 28.835 1.00 16.67 C ANISOU 1474 C PHE A 180 2085 2581 1668 -29 43 191 C ATOM 1475 O PHE A 180 4.135 -0.721 28.860 1.00 19.98 O ANISOU 1475 O PHE A 180 2516 2970 2104 0 60 235 O ATOM 1476 CB PHE A 180 3.407 2.104 30.709 1.00 16.66 C ANISOU 1476 CB PHE A 180 2240 2608 1481 44 -6 131 C ATOM 1477 CG PHE A 180 2.479 1.210 31.524 1.00 19.23 C ANISOU 1477 CG PHE A 180 2643 2946 1716 125 141 236 C ATOM 1478 CD1 PHE A 180 2.657 1.064 32.901 1.00 19.02 C ANISOU 1478 CD1 PHE A 180 2783 2956 1489 282 137 270 C ATOM 1479 CD2 PHE A 180 1.393 0.568 30.922 1.00 14.83 C ANISOU 1479 CD2 PHE A 180 1990 2348 1295 66 277 317 C ATOM 1480 CE1 PHE A 180 1.777 0.261 33.670 1.00 20.76 C ANISOU 1480 CE1 PHE A 180 3067 3186 1635 388 347 440 C ATOM 1481 CE2 PHE A 180 0.519 -0.234 31.674 1.00 17.78 C ANISOU 1481 CE2 PHE A 180 2371 2699 1685 123 445 476 C ATOM 1482 CZ PHE A 180 0.704 -0.392 33.043 1.00 19.90 C ANISOU 1482 CZ PHE A 180 2798 3019 1744 288 522 567 C ATOM 1483 N ASN A 181 3.451 1.133 27.813 1.00 15.30 N ANISOU 1483 N ASN A 181 1875 2399 1538 -65 74 158 N ATOM 1484 CA ASN A 181 2.874 0.327 26.760 1.00 14.96 C ANISOU 1484 CA ASN A 181 1829 2313 1543 -53 90 145 C ATOM 1485 C ASN A 181 3.967 -0.350 25.936 1.00 21.13 C ANISOU 1485 C ASN A 181 2610 3101 2317 23 80 146 C ATOM 1486 O ASN A 181 3.970 -1.578 25.809 1.00 26.72 O ANISOU 1486 O ASN A 181 3356 3748 3047 68 51 137 O ATOM 1487 CB ASN A 181 1.949 1.157 25.877 1.00 17.32 C ANISOU 1487 CB ASN A 181 2121 2603 1858 -64 88 100 C ATOM 1488 CG ASN A 181 1.111 0.278 24.972 1.00 20.09 C ANISOU 1488 CG ASN A 181 2488 2872 2275 -36 16 47 C ATOM 1489 OD1 ASN A 181 1.497 0.004 23.839 1.00 24.60 O ANISOU 1489 OD1 ASN A 181 3126 3436 2785 61 -33 -5 O ATOM 1490 ND2 ASN A 181 -0.021 -0.206 25.483 1.00 18.53 N ANISOU 1490 ND2 ASN A 181 2228 2593 2218 -96 2 69 N ATOM 1491 N PHE A 182 4.938 0.415 25.419 1.00 15.51 N ANISOU 1491 N PHE A 182 1844 2446 1602 54 118 182 N ATOM 1492 CA PHE A 182 5.927 -0.188 24.532 1.00 14.89 C ANISOU 1492 CA PHE A 182 1756 2394 1508 182 176 221 C ATOM 1493 C PHE A 182 6.930 -1.044 25.304 1.00 17.06 C ANISOU 1493 C PHE A 182 1979 2672 1832 206 149 261 C ATOM 1494 O PHE A 182 7.025 -2.257 25.084 1.00 18.69 O ANISOU 1494 O PHE A 182 2255 2839 2007 300 137 235 O ATOM 1495 CB PHE A 182 6.655 0.887 23.716 1.00 15.38 C ANISOU 1495 CB PHE A 182 1731 2510 1602 227 292 324 C ATOM 1496 CG PHE A 182 7.636 0.323 22.709 1.00 18.20 C ANISOU 1496 CG PHE A 182 2081 2917 1916 425 431 410 C ATOM 1497 CD1 PHE A 182 7.358 -0.865 22.031 1.00 16.45 C ANISOU 1497 CD1 PHE A 182 2033 2678 1541 599 411 316 C ATOM 1498 CD2 PHE A 182 8.827 0.987 22.426 1.00 18.43 C ANISOU 1498 CD2 PHE A 182 1923 2991 2087 461 582 596 C ATOM 1499 CE1 PHE A 182 8.248 -1.377 21.097 1.00 17.72 C ANISOU 1499 CE1 PHE A 182 2235 2892 1607 852 559 385 C ATOM 1500 CE2 PHE A 182 9.723 0.482 21.499 1.00 22.80 C ANISOU 1500 CE2 PHE A 182 2460 3606 2596 692 774 718 C ATOM 1501 CZ PHE A 182 9.437 -0.706 20.830 1.00 23.58 C ANISOU 1501 CZ PHE A 182 2787 3710 2463 909 767 601 C ATOM 1502 N PHE A 183 7.724 -0.427 26.181 1.00 14.90 N ANISOU 1502 N PHE A 183 1588 2421 1651 140 101 311 N ATOM 1503 CA PHE A 183 8.821 -1.168 26.797 1.00 15.30 C ANISOU 1503 CA PHE A 183 1569 2480 1765 193 46 355 C ATOM 1504 C PHE A 183 8.288 -2.325 27.633 1.00 17.40 C ANISOU 1504 C PHE A 183 1972 2700 1938 212 -16 318 C ATOM 1505 O PHE A 183 8.681 -3.483 27.434 1.00 16.78 O ANISOU 1505 O PHE A 183 1924 2594 1859 311 -2 335 O ATOM 1506 CB PHE A 183 9.697 -0.245 27.654 1.00 15.99 C ANISOU 1506 CB PHE A 183 1508 2565 2004 120 -88 384 C ATOM 1507 CG PHE A 183 10.591 0.709 26.862 1.00 18.89 C ANISOU 1507 CG PHE A 183 1647 2932 2597 98 -15 498 C ATOM 1508 CD1 PHE A 183 10.609 0.713 25.469 1.00 18.95 C ANISOU 1508 CD1 PHE A 183 1632 2983 2584 192 218 594 C ATOM 1509 CD2 PHE A 183 11.406 1.609 27.531 1.00 20.03 C ANISOU 1509 CD2 PHE A 183 1607 3012 2990 6 -190 522 C ATOM 1510 CE1 PHE A 183 11.439 1.589 24.762 1.00 20.46 C ANISOU 1510 CE1 PHE A 183 1599 3172 3001 196 353 774 C ATOM 1511 CE2 PHE A 183 12.235 2.495 26.835 1.00 23.87 C ANISOU 1511 CE2 PHE A 183 1825 3455 3788 -39 -110 682 C ATOM 1512 CZ PHE A 183 12.243 2.486 25.446 1.00 22.87 C ANISOU 1512 CZ PHE A 183 1658 3391 3639 57 203 838 C ATOM 1513 N ALA A 184 7.356 -2.038 28.552 1.00 15.06 N ANISOU 1513 N ALA A 184 1768 2385 1570 142 -57 291 N ATOM 1514 CA ALA A 184 6.964 -3.058 29.520 1.00 17.04 C ANISOU 1514 CA ALA A 184 2129 2591 1756 180 -70 331 C ATOM 1515 C ALA A 184 5.971 -4.060 28.930 1.00 19.09 C ANISOU 1515 C ALA A 184 2439 2748 2065 169 1 340 C ATOM 1516 O ALA A 184 6.107 -5.269 29.143 1.00 19.22 O ANISOU 1516 O ALA A 184 2500 2681 2120 222 -8 391 O ATOM 1517 CB ALA A 184 6.368 -2.404 30.768 1.00 15.69 C ANISOU 1517 CB ALA A 184 2051 2445 1465 176 -92 339 C ATOM 1518 N CYS A 185 4.961 -3.579 28.206 1.00 15.39 N ANISOU 1518 N CYS A 185 1960 2256 1632 103 34 289 N ATOM 1519 CA CYS A 185 3.821 -4.412 27.847 1.00 16.36 C ANISOU 1519 CA CYS A 185 2100 2240 1877 67 31 290 C ATOM 1520 C CYS A 185 3.926 -5.015 26.453 1.00 17.21 C ANISOU 1520 C CYS A 185 2246 2265 2028 135 -57 176 C ATOM 1521 O CYS A 185 3.216 -5.988 26.162 1.00 17.67 O ANISOU 1521 O CYS A 185 2329 2147 2239 123 -145 148 O ATOM 1522 CB CYS A 185 2.535 -3.599 27.976 1.00 17.34 C ANISOU 1522 CB CYS A 185 2178 2366 2044 -20 79 299 C ATOM 1523 SG CYS A 185 2.217 -3.275 29.751 1.00 23.13 S ANISOU 1523 SG CYS A 185 2943 3164 2682 -3 214 450 S ATOM 1524 N VAL A 186 4.825 -4.505 25.614 1.00 13.15 N ANISOU 1524 N VAL A 186 1745 1854 1399 233 -39 123 N ATOM 1525 CA VAL A 186 4.989 -5.026 24.256 1.00 14.68 C ANISOU 1525 CA VAL A 186 2040 1995 1541 390 -95 15 C ATOM 1526 C VAL A 186 6.385 -5.612 24.061 1.00 16.72 C ANISOU 1526 C VAL A 186 2316 2303 1734 559 -35 47 C ATOM 1527 O VAL A 186 6.539 -6.789 23.710 1.00 16.61 O ANISOU 1527 O VAL A 186 2410 2169 1732 688 -112 -19 O ATOM 1528 CB VAL A 186 4.711 -3.920 23.213 1.00 16.59 C ANISOU 1528 CB VAL A 186 2309 2324 1671 440 -65 -32 C ATOM 1529 CG1 VAL A 186 5.127 -4.381 21.798 1.00 14.66 C ANISOU 1529 CG1 VAL A 186 2232 2071 1269 705 -85 -125 C ATOM 1530 CG2 VAL A 186 3.237 -3.505 23.227 1.00 17.09 C ANISOU 1530 CG2 VAL A 186 2356 2313 1823 313 -162 -87 C ATOM 1531 N ALEU A 187 7.415 -4.803 24.293 0.80 18.39 N ANISOU 1531 N ALEU A 187 2220 2493 2273 63 308 89 N ATOM 1532 N BLEU A 187 7.414 -4.785 24.268 0.20 17.86 N ANISOU 1532 N BLEU A 187 2156 2424 2207 64 312 90 N ATOM 1533 CA ALEU A 187 8.773 -5.242 23.990 0.80 18.58 C ANISOU 1533 CA ALEU A 187 2147 2437 2475 16 336 -3 C ATOM 1534 CA BLEU A 187 8.786 -5.221 24.018 0.20 18.74 C ANISOU 1534 CA BLEU A 187 2165 2456 2498 14 335 -7 C ATOM 1535 C ALEU A 187 9.198 -6.409 24.881 0.80 18.92 C ANISOU 1535 C ALEU A 187 2087 2573 2528 11 126 -44 C ATOM 1536 C BLEU A 187 9.152 -6.424 24.873 0.20 18.77 C ANISOU 1536 C BLEU A 187 2073 2557 2503 12 124 -38 C ATOM 1537 O ALEU A 187 9.738 -7.410 24.392 0.80 20.27 O ANISOU 1537 O ALEU A 187 2230 2729 2742 17 91 -40 O ATOM 1538 O BLEU A 187 9.623 -7.446 24.359 0.20 19.51 O ANISOU 1538 O BLEU A 187 2145 2637 2631 20 89 -26 O ATOM 1539 CB ALEU A 187 9.734 -4.061 24.123 0.80 19.49 C ANISOU 1539 CB ALEU A 187 2195 2425 2785 -48 492 -147 C ATOM 1540 CB BLEU A 187 9.767 -4.079 24.279 0.20 20.24 C ANISOU 1540 CB BLEU A 187 2275 2531 2884 -51 472 -160 C ATOM 1541 CG ALEU A 187 11.109 -4.159 23.482 0.80 22.99 C ANISOU 1541 CG ALEU A 187 2547 2758 3432 -107 612 -262 C ATOM 1542 CG BLEU A 187 10.153 -3.210 23.086 0.20 21.38 C ANISOU 1542 CG BLEU A 187 2498 2497 3129 -66 754 -150 C ATOM 1543 CD1ALEU A 187 11.027 -4.762 22.056 0.80 24.78 C ANISOU 1543 CD1ALEU A 187 2869 2944 3601 -61 707 -140 C ATOM 1544 CD1BLEU A 187 11.351 -2.326 23.417 0.20 23.40 C ANISOU 1544 CD1BLEU A 187 2629 2622 3640 -173 899 -354 C ATOM 1545 CD2ALEU A 187 11.729 -2.765 23.451 0.80 23.69 C ANISOU 1545 CD2ALEU A 187 2606 2687 3708 -185 845 -392 C ATOM 1546 CD2BLEU A 187 10.418 -4.053 21.842 0.20 23.06 C ANISOU 1546 CD2BLEU A 187 2751 2692 3320 -32 806 -72 C ATOM 1547 N VAL A 188 8.963 -6.314 26.187 1.00 17.09 N ANISOU 1547 N VAL A 188 1809 2441 2245 21 -11 -77 N ATOM 1548 CA VAL A 188 9.342 -7.413 27.082 1.00 18.84 C ANISOU 1548 CA VAL A 188 1963 2754 2441 61 -197 -87 C ATOM 1549 C VAL A 188 8.632 -8.715 26.715 1.00 20.07 C ANISOU 1549 C VAL A 188 2213 2927 2487 85 -255 65 C ATOM 1550 O VAL A 188 9.312 -9.745 26.604 1.00 19.72 O ANISOU 1550 O VAL A 188 2138 2858 2498 113 -314 61 O ATOM 1551 CB VAL A 188 9.139 -7.010 28.553 1.00 19.95 C ANISOU 1551 CB VAL A 188 2048 3022 2511 95 -321 -141 C ATOM 1552 CG1 VAL A 188 9.178 -8.266 29.445 1.00 21.04 C ANISOU 1552 CG1 VAL A 188 2184 3263 2547 181 -497 -74 C ATOM 1553 CG2 VAL A 188 10.247 -6.044 28.999 1.00 19.54 C ANISOU 1553 CG2 VAL A 188 1837 2966 2623 73 -291 -369 C ATOM 1554 N PRO A 189 7.299 -8.744 26.493 1.00 20.04 N ANISOU 1554 N PRO A 189 2312 2962 2341 77 -233 178 N ATOM 1555 CA PRO A 189 6.677 -10.011 26.050 1.00 18.62 C ANISOU 1555 CA PRO A 189 2193 2785 2098 75 -259 273 C ATOM 1556 C PRO A 189 7.196 -10.519 24.718 1.00 19.22 C ANISOU 1556 C PRO A 189 2264 2775 2265 70 -180 253 C ATOM 1557 O PRO A 189 7.319 -11.737 24.532 1.00 18.42 O ANISOU 1557 O PRO A 189 2166 2642 2191 72 -223 279 O ATOM 1558 CB PRO A 189 5.178 -9.663 25.964 1.00 18.27 C ANISOU 1558 CB PRO A 189 2221 2824 1898 62 -228 334 C ATOM 1559 CG PRO A 189 4.993 -8.567 26.976 1.00 20.92 C ANISOU 1559 CG PRO A 189 2540 3223 2184 73 -258 308 C ATOM 1560 CD PRO A 189 6.280 -7.756 26.920 1.00 19.00 C ANISOU 1560 CD PRO A 189 2224 2900 2096 75 -212 199 C ATOM 1561 N LEU A 190 7.479 -9.628 23.764 1.00 17.12 N ANISOU 1561 N LEU A 190 1999 2462 2043 71 -50 213 N ATOM 1562 CA LEU A 190 8.019 -10.098 22.490 1.00 14.33 C ANISOU 1562 CA LEU A 190 1638 2045 1762 79 31 192 C ATOM 1563 C LEU A 190 9.403 -10.728 22.680 1.00 18.70 C ANISOU 1563 C LEU A 190 2099 2534 2473 71 -21 115 C ATOM 1564 O LEU A 190 9.703 -11.773 22.095 1.00 19.24 O ANISOU 1564 O LEU A 190 2153 2572 2584 82 -42 112 O ATOM 1565 CB LEU A 190 8.068 -8.943 21.490 1.00 16.45 C ANISOU 1565 CB LEU A 190 1950 2271 2028 105 210 187 C ATOM 1566 CG LEU A 190 6.719 -8.441 20.941 1.00 19.66 C ANISOU 1566 CG LEU A 190 2458 2761 2251 170 271 259 C ATOM 1567 CD1 LEU A 190 6.950 -7.170 20.077 1.00 22.06 C ANISOU 1567 CD1 LEU A 190 2835 2991 2555 230 475 277 C ATOM 1568 CD2 LEU A 190 6.020 -9.522 20.108 1.00 21.19 C ANISOU 1568 CD2 LEU A 190 2657 3041 2352 205 237 270 C ATOM 1569 N LEU A 191 10.250 -10.121 23.518 1.00 18.77 N ANISOU 1569 N LEU A 191 2027 2535 2568 62 -50 27 N ATOM 1570 CA LEU A 191 11.562 -10.714 23.792 1.00 20.69 C ANISOU 1570 CA LEU A 191 2159 2758 2943 82 -122 -79 C ATOM 1571 C LEU A 191 11.422 -12.044 24.525 1.00 21.94 C ANISOU 1571 C LEU A 191 2340 2954 3043 147 -286 -12 C ATOM 1572 O LEU A 191 12.175 -12.995 24.257 1.00 22.66 O ANISOU 1572 O LEU A 191 2394 3008 3208 188 -331 -44 O ATOM 1573 CB LEU A 191 12.417 -9.733 24.592 1.00 22.81 C ANISOU 1573 CB LEU A 191 2309 3048 3309 67 -122 -234 C ATOM 1574 CG LEU A 191 12.903 -8.472 23.846 1.00 25.43 C ANISOU 1574 CG LEU A 191 2607 3287 3770 -11 88 -332 C ATOM 1575 CD1 LEU A 191 13.576 -7.460 24.782 1.00 24.48 C ANISOU 1575 CD1 LEU A 191 2353 3187 3760 -48 97 -519 C ATOM 1576 CD2 LEU A 191 13.861 -8.841 22.701 1.00 27.59 C ANISOU 1576 CD2 LEU A 191 2831 3480 4171 -32 195 -394 C ATOM 1577 N LEU A 192 10.449 -12.139 25.437 1.00 19.15 N ANISOU 1577 N LEU A 192 2058 2664 2556 162 -358 86 N ATOM 1578 CA LEU A 192 10.134 -13.414 26.072 1.00 21.51 C ANISOU 1578 CA LEU A 192 2420 2964 2788 219 -460 188 C ATOM 1579 C LEU A 192 9.725 -14.460 25.040 1.00 22.17 C ANISOU 1579 C LEU A 192 2564 2961 2898 186 -404 245 C ATOM 1580 O LEU A 192 10.190 -15.606 25.085 1.00 20.70 O ANISOU 1580 O LEU A 192 2393 2709 2764 238 -451 265 O ATOM 1581 CB LEU A 192 9.023 -13.226 27.105 1.00 23.58 C ANISOU 1581 CB LEU A 192 2756 3307 2898 219 -501 288 C ATOM 1582 CG LEU A 192 9.410 -12.599 28.445 1.00 30.07 C ANISOU 1582 CG LEU A 192 3520 4239 3666 292 -601 240 C ATOM 1583 CD1 LEU A 192 8.172 -12.418 29.312 1.00 30.34 C ANISOU 1583 CD1 LEU A 192 3634 4356 3538 282 -620 347 C ATOM 1584 CD2 LEU A 192 10.437 -13.487 29.151 1.00 32.41 C ANISOU 1584 CD2 LEU A 192 3783 4553 3978 433 -719 223 C ATOM 1585 N MET A 193 8.838 -14.089 24.111 1.00 21.04 N ANISOU 1585 N MET A 193 2454 2826 2714 117 -303 258 N ATOM 1586 CA MET A 193 8.438 -15.012 23.051 1.00 21.99 C ANISOU 1586 CA MET A 193 2598 2898 2860 90 -250 262 C ATOM 1587 C MET A 193 9.647 -15.498 22.271 1.00 20.47 C ANISOU 1587 C MET A 193 2341 2633 2804 121 -241 183 C ATOM 1588 O MET A 193 9.751 -16.683 21.934 1.00 20.92 O ANISOU 1588 O MET A 193 2407 2620 2921 130 -255 182 O ATOM 1589 CB MET A 193 7.473 -14.340 22.069 1.00 23.52 C ANISOU 1589 CB MET A 193 2808 3162 2968 58 -150 247 C ATOM 1590 CG MET A 193 6.076 -14.192 22.514 1.00 27.87 C ANISOU 1590 CG MET A 193 3409 3797 3383 25 -152 295 C ATOM 1591 SD MET A 193 5.176 -13.255 21.256 1.00 29.17 S ANISOU 1591 SD MET A 193 3580 4077 3426 56 -46 251 S ATOM 1592 CE MET A 193 4.315 -12.120 22.377 1.00 28.72 C ANISOU 1592 CE MET A 193 3568 4110 3236 54 -73 306 C ATOM 1593 N LEU A 194 10.537 -14.574 21.916 1.00 20.20 N ANISOU 1593 N LEU A 194 2238 2606 2831 128 -195 104 N ATOM 1594 CA LEU A 194 11.752 -14.943 21.201 1.00 22.80 C ANISOU 1594 CA LEU A 194 2488 2882 3293 151 -176 9 C ATOM 1595 C LEU A 194 12.540 -15.984 21.984 1.00 22.49 C ANISOU 1595 C LEU A 194 2421 2805 3319 223 -306 -6 C ATOM 1596 O LEU A 194 12.998 -16.979 21.420 1.00 23.98 O ANISOU 1596 O LEU A 194 2595 2933 3585 254 -320 -35 O ATOM 1597 CB LEU A 194 12.595 -13.693 20.938 1.00 21.83 C ANISOU 1597 CB LEU A 194 2290 2764 3241 129 -82 -85 C ATOM 1598 CG LEU A 194 13.979 -13.942 20.355 1.00 28.81 C ANISOU 1598 CG LEU A 194 3064 3607 4274 141 -55 -213 C ATOM 1599 CD1 LEU A 194 13.843 -14.626 18.993 1.00 31.07 C ANISOU 1599 CD1 LEU A 194 3371 3868 4566 146 17 -203 C ATOM 1600 CD2 LEU A 194 14.758 -12.636 20.248 1.00 27.68 C ANISOU 1600 CD2 LEU A 194 2842 3452 4223 89 73 -323 C ATOM 1601 N GLY A 195 12.695 -15.773 23.292 1.00 23.04 N ANISOU 1601 N GLY A 195 2489 2921 3346 274 -404 13 N ATOM 1602 CA GLY A 195 13.377 -16.761 24.114 1.00 21.57 C ANISOU 1602 CA GLY A 195 2300 2718 3176 396 -531 19 C ATOM 1603 C GLY A 195 12.676 -18.107 24.107 1.00 21.84 C ANISOU 1603 C GLY A 195 2460 2652 3185 415 -536 149 C ATOM 1604 O GLY A 195 13.325 -19.150 23.994 1.00 24.85 O ANISOU 1604 O GLY A 195 2848 2955 3637 500 -577 139 O ATOM 1605 N VAL A 196 11.342 -18.105 24.196 1.00 21.16 N ANISOU 1605 N VAL A 196 2469 2560 3011 333 -480 255 N ATOM 1606 CA VAL A 196 10.587 -19.359 24.152 1.00 20.17 C ANISOU 1606 CA VAL A 196 2451 2320 2892 315 -442 349 C ATOM 1607 C VAL A 196 10.806 -20.075 22.814 1.00 23.22 C ANISOU 1607 C VAL A 196 2798 2623 3402 276 -381 263 C ATOM 1608 O VAL A 196 11.057 -21.289 22.777 1.00 22.51 O ANISOU 1608 O VAL A 196 2755 2403 3394 322 -383 283 O ATOM 1609 CB VAL A 196 9.090 -19.113 24.428 1.00 21.07 C ANISOU 1609 CB VAL A 196 2636 2470 2899 211 -377 428 C ATOM 1610 CG1 VAL A 196 8.283 -20.392 24.203 1.00 22.69 C ANISOU 1610 CG1 VAL A 196 2923 2545 3154 150 -295 474 C ATOM 1611 CG2 VAL A 196 8.864 -18.641 25.870 1.00 22.65 C ANISOU 1611 CG2 VAL A 196 2889 2745 2972 267 -440 525 C ATOM 1612 N TYR A 197 10.719 -19.339 21.695 1.00 20.27 N ANISOU 1612 N TYR A 197 2344 2321 3037 208 -318 169 N ATOM 1613 CA TYR A 197 10.934 -19.977 20.393 1.00 21.57 C ANISOU 1613 CA TYR A 197 2457 2442 3297 189 -264 73 C ATOM 1614 C TYR A 197 12.355 -20.513 20.252 1.00 22.82 C ANISOU 1614 C TYR A 197 2558 2538 3575 280 -321 6 C ATOM 1615 O TYR A 197 12.558 -21.594 19.687 1.00 25.41 O ANISOU 1615 O TYR A 197 2882 2772 4000 298 -312 -37 O ATOM 1616 CB TYR A 197 10.601 -19.017 19.238 1.00 19.06 C ANISOU 1616 CB TYR A 197 2080 2236 2925 143 -176 2 C ATOM 1617 CG TYR A 197 9.105 -18.993 19.007 1.00 23.09 C ANISOU 1617 CG TYR A 197 2629 2811 3334 78 -121 18 C ATOM 1618 CD1 TYR A 197 8.436 -20.153 18.626 1.00 22.44 C ANISOU 1618 CD1 TYR A 197 2548 2676 3302 34 -93 -30 C ATOM 1619 CD2 TYR A 197 8.352 -17.843 19.242 1.00 23.57 C ANISOU 1619 CD2 TYR A 197 2715 2982 3258 61 -95 60 C ATOM 1620 CE1 TYR A 197 7.070 -20.172 18.461 1.00 23.30 C ANISOU 1620 CE1 TYR A 197 2660 2865 3328 -32 -43 -62 C ATOM 1621 CE2 TYR A 197 6.968 -17.848 19.065 1.00 21.51 C ANISOU 1621 CE2 TYR A 197 2471 2807 2894 16 -57 49 C ATOM 1622 CZ TYR A 197 6.339 -19.017 18.680 1.00 22.81 C ANISOU 1622 CZ TYR A 197 2614 2941 3112 -33 -33 -23 C ATOM 1623 OH TYR A 197 4.972 -19.048 18.515 1.00 26.19 O ANISOU 1623 OH TYR A 197 3026 3475 3450 -85 9 -81 O ATOM 1624 N LEU A 198 13.350 -19.774 20.742 1.00 23.22 N ANISOU 1624 N LEU A 198 2545 2646 3630 339 -378 -31 N ATOM 1625 CA LEU A 198 14.716 -20.299 20.754 1.00 25.72 C ANISOU 1625 CA LEU A 198 2789 2933 4052 444 -450 -120 C ATOM 1626 C LEU A 198 14.796 -21.616 21.513 1.00 26.55 C ANISOU 1626 C LEU A 198 2989 2925 4173 558 -529 -37 C ATOM 1627 O LEU A 198 15.474 -22.553 21.076 1.00 25.99 O ANISOU 1627 O LEU A 198 2900 2773 4203 630 -552 -93 O ATOM 1628 CB LEU A 198 15.676 -19.277 21.376 1.00 28.20 C ANISOU 1628 CB LEU A 198 2999 3351 4366 487 -502 -207 C ATOM 1629 CG LEU A 198 15.897 -18.011 20.541 1.00 34.41 C ANISOU 1629 CG LEU A 198 3692 4201 5183 382 -382 -305 C ATOM 1630 CD1 LEU A 198 16.875 -17.030 21.221 1.00 34.90 C ANISOU 1630 CD1 LEU A 198 3630 4346 5286 401 -410 -433 C ATOM 1631 CD2 LEU A 198 16.385 -18.378 19.113 1.00 36.52 C ANISOU 1631 CD2 LEU A 198 3898 4435 5543 358 -297 -394 C ATOM 1632 N ARG A 199 14.126 -21.700 22.663 1.00 27.11 N ANISOU 1632 N ARG A 199 3174 2983 4142 589 -560 103 N ATOM 1633 CA ARG A 199 14.120 -22.946 23.421 1.00 29.41 C ANISOU 1633 CA ARG A 199 3599 3141 4434 714 -594 220 C ATOM 1634 C ARG A 199 13.396 -24.057 22.665 1.00 28.32 C ANISOU 1634 C ARG A 199 3538 2828 4394 627 -485 246 C ATOM 1635 O ARG A 199 13.843 -25.209 22.686 1.00 28.80 O ANISOU 1635 O ARG A 199 3664 2739 4541 730 -489 267 O ATOM 1636 CB ARG A 199 13.486 -22.718 24.791 1.00 32.74 C ANISOU 1636 CB ARG A 199 4134 3598 4708 763 -621 375 C ATOM 1637 CG ARG A 199 14.345 -21.856 25.700 1.00 37.69 C ANISOU 1637 CG ARG A 199 4676 4400 5246 896 -751 322 C ATOM 1638 CD ARG A 199 13.736 -21.734 27.083 1.00 45.13 C ANISOU 1638 CD ARG A 199 5733 5393 6023 976 -784 475 C ATOM 1639 NE ARG A 199 14.650 -21.061 28.001 1.00 55.30 N ANISOU 1639 NE ARG A 199 6921 6869 7223 1143 -926 389 N ATOM 1640 CZ ARG A 199 15.580 -21.685 28.720 1.00 64.03 C ANISOU 1640 CZ ARG A 199 8041 8012 8277 1401 -1042 389 C ATOM 1641 NH1 ARG A 199 15.718 -23.005 28.632 1.00 67.93 N ANISOU 1641 NH1 ARG A 199 8674 8332 8803 1521 -1018 501 N ATOM 1642 NH2 ARG A 199 16.372 -20.990 29.527 1.00 66.48 N ANISOU 1642 NH2 ARG A 199 8220 8535 8503 1515 -1151 259 N ATOM 1643 N ILE A 200 12.288 -23.734 21.982 1.00 22.57 N ANISOU 1643 N ILE A 200 2794 2124 3658 452 -384 223 N ATOM 1644 CA ILE A 200 11.567 -24.758 21.223 1.00 24.58 C ANISOU 1644 CA ILE A 200 3079 2241 4018 358 -276 187 C ATOM 1645 C ILE A 200 12.472 -25.364 20.157 1.00 24.78 C ANISOU 1645 C ILE A 200 3016 2218 4182 401 -288 47 C ATOM 1646 O ILE A 200 12.609 -26.589 20.049 1.00 24.91 O ANISOU 1646 O ILE A 200 3090 2054 4320 439 -255 43 O ATOM 1647 CB ILE A 200 10.287 -24.182 20.587 1.00 24.21 C ANISOU 1647 CB ILE A 200 2986 2297 3917 190 -187 131 C ATOM 1648 CG1 ILE A 200 9.215 -23.895 21.644 1.00 26.45 C ANISOU 1648 CG1 ILE A 200 3368 2594 4086 133 -153 262 C ATOM 1649 CG2 ILE A 200 9.724 -25.179 19.573 1.00 21.93 C ANISOU 1649 CG2 ILE A 200 2662 1916 3755 100 -89 8 C ATOM 1650 CD1 ILE A 200 8.055 -23.036 21.100 1.00 22.84 C ANISOU 1650 CD1 ILE A 200 2843 2299 3535 6 -99 191 C ATOM 1651 N PHE A 201 13.111 -24.508 19.359 1.00 25.22 N ANISOU 1651 N PHE A 201 2934 2424 4226 397 -320 -70 N ATOM 1652 CA PHE A 201 13.947 -25.011 18.276 1.00 28.86 C ANISOU 1652 CA PHE A 201 3295 2866 4806 432 -322 -215 C ATOM 1653 C PHE A 201 15.183 -25.728 18.807 1.00 30.81 C ANISOU 1653 C PHE A 201 3559 3021 5128 599 -417 -212 C ATOM 1654 O PHE A 201 15.599 -26.745 18.232 1.00 31.09 O ANISOU 1654 O PHE A 201 3581 2944 5287 645 -411 -288 O ATOM 1655 CB PHE A 201 14.298 -23.857 17.326 1.00 27.66 C ANISOU 1655 CB PHE A 201 3009 2892 4607 390 -297 -322 C ATOM 1656 CG PHE A 201 13.095 -23.316 16.585 1.00 28.55 C ANISOU 1656 CG PHE A 201 3110 3104 4633 278 -202 -341 C ATOM 1657 CD1 PHE A 201 12.729 -21.985 16.684 1.00 28.48 C ANISOU 1657 CD1 PHE A 201 3098 3227 4495 243 -172 -296 C ATOM 1658 CD2 PHE A 201 12.311 -24.164 15.807 1.00 28.08 C ANISOU 1658 CD2 PHE A 201 3035 3012 4623 224 -142 -424 C ATOM 1659 CE1 PHE A 201 11.603 -21.502 16.008 1.00 27.60 C ANISOU 1659 CE1 PHE A 201 2983 3226 4279 183 -94 -315 C ATOM 1660 CE2 PHE A 201 11.192 -23.693 15.131 1.00 28.92 C ANISOU 1660 CE2 PHE A 201 3109 3252 4627 156 -71 -474 C ATOM 1661 CZ PHE A 201 10.830 -22.361 15.238 1.00 26.83 C ANISOU 1661 CZ PHE A 201 2856 3130 4207 149 -52 -410 C ATOM 1662 N ALA A 202 15.759 -25.254 19.921 1.00 29.31 N ANISOU 1662 N ALA A 202 3393 2885 4857 710 -512 -140 N ATOM 1663 CA ALA A 202 16.895 -25.967 20.505 1.00 31.86 C ANISOU 1663 CA ALA A 202 3733 3153 5220 915 -618 -146 C ATOM 1664 C ALA A 202 16.478 -27.340 21.017 1.00 32.32 C ANISOU 1664 C ALA A 202 3977 2982 5322 1000 -583 -10 C ATOM 1665 O ALA A 202 17.223 -28.317 20.875 1.00 32.81 O ANISOU 1665 O ALA A 202 4061 2930 5477 1141 -616 -45 O ATOM 1666 CB ALA A 202 17.527 -25.146 21.630 1.00 31.01 C ANISOU 1666 CB ALA A 202 3592 3194 4996 1036 -732 -128 C ATOM 1667 N ALA A 203 15.287 -27.446 21.607 1.00 32.27 N ANISOU 1667 N ALA A 203 4111 2893 5257 915 -497 143 N ATOM 1668 CA ALA A 203 14.848 -28.747 22.110 1.00 33.42 C ANISOU 1668 CA ALA A 203 4453 2783 5463 977 -411 282 C ATOM 1669 C ALA A 203 14.553 -29.716 20.968 1.00 35.91 C ANISOU 1669 C ALA A 203 4745 2927 5971 866 -299 167 C ATOM 1670 O ALA A 203 14.846 -30.913 21.071 1.00 40.37 O ANISOU 1670 O ALA A 203 5424 3265 6649 975 -256 206 O ATOM 1671 CB ALA A 203 13.625 -28.573 23.002 1.00 31.56 C ANISOU 1671 CB ALA A 203 4357 2507 5126 889 -319 456 C ATOM 1672 N ALA A 204 13.968 -29.224 19.875 1.00 32.62 N ANISOU 1672 N ALA A 204 4186 2619 5590 669 -247 17 N ATOM 1673 CA ALA A 204 13.728 -30.076 18.716 1.00 34.66 C ANISOU 1673 CA ALA A 204 4381 2769 6021 575 -157 -142 C ATOM 1674 C ALA A 204 15.039 -30.596 18.134 1.00 33.95 C ANISOU 1674 C ALA A 204 4215 2653 6030 721 -241 -257 C ATOM 1675 O ALA A 204 15.161 -31.781 17.808 1.00 35.44 O ANISOU 1675 O ALA A 204 4449 2634 6381 754 -183 -308 O ATOM 1676 CB ALA A 204 12.938 -29.302 17.660 1.00 33.96 C ANISOU 1676 CB ALA A 204 4136 2874 5895 393 -112 -291 C ATOM 1677 N ARG A 205 16.032 -29.717 17.997 1.00 35.21 N ANISOU 1677 N ARG A 205 4252 3017 6108 802 -364 -316 N ATOM 1678 CA ARG A 205 17.314 -30.120 17.425 1.00 39.30 C ANISOU 1678 CA ARG A 205 4670 3548 6715 935 -445 -452 C ATOM 1679 C ARG A 205 18.023 -31.132 18.317 1.00 38.46 C ANISOU 1679 C ARG A 205 4705 3259 6648 1165 -505 -354 C ATOM 1680 O ARG A 205 18.647 -32.085 17.825 1.00 39.63 O ANISOU 1680 O ARG A 205 4842 3287 6930 1263 -514 -447 O ATOM 1681 CB ARG A 205 18.188 -28.883 17.207 1.00 45.03 C ANISOU 1681 CB ARG A 205 5231 4529 7351 953 -534 -544 C ATOM 1682 CG ARG A 205 19.613 -29.179 16.762 1.00 55.39 C ANISOU 1682 CG ARG A 205 6418 5887 8739 1095 -623 -699 C ATOM 1683 CD ARG A 205 20.499 -27.956 16.968 1.00 61.40 C ANISOU 1683 CD ARG A 205 7038 6872 9418 1121 -695 -774 C ATOM 1684 NE ARG A 205 20.459 -27.501 18.355 1.00 66.92 N ANISOU 1684 NE ARG A 205 7821 7608 9999 1209 -769 -643 N ATOM 1685 CZ ARG A 205 20.838 -26.295 18.759 1.00 70.52 C ANISOU 1685 CZ ARG A 205 8175 8245 10374 1186 -805 -688 C ATOM 1686 NH1 ARG A 205 21.286 -25.412 17.882 1.00 72.18 N ANISOU 1686 NH1 ARG A 205 8216 8588 10620 1071 -749 -841 N ATOM 1687 NH2 ARG A 205 20.762 -25.969 20.041 1.00 72.60 N ANISOU 1687 NH2 ARG A 205 8508 8553 10525 1282 -881 -586 N ATOM 1688 N ARG A 206 17.932 -30.942 19.635 1.00 35.70 N ANISOU 1688 N ARG A 206 4497 2896 6172 1278 -544 -167 N ATOM 1689 CA ARG A 206 18.515 -31.891 20.574 1.00 36.78 C ANISOU 1689 CA ARG A 206 4804 2868 6302 1544 -589 -38 C ATOM 1690 C ARG A 206 17.801 -33.238 20.519 1.00 38.57 C ANISOU 1690 C ARG A 206 5222 2755 6676 1518 -423 55 C ATOM 1691 O ARG A 206 18.445 -34.294 20.573 1.00 38.87 O ANISOU 1691 O ARG A 206 5359 2671 6740 1676 -398 73 O ATOM 1692 CB ARG A 206 18.473 -31.308 21.987 1.00 39.83 C ANISOU 1692 CB ARG A 206 5295 3353 6487 1678 -659 141 C ATOM 1693 CG ARG A 206 18.995 -32.247 23.047 1.00 50.27 C ANISOU 1693 CG ARG A 206 6802 4584 7714 1944 -653 313 C ATOM 1694 CD ARG A 206 19.109 -31.579 24.407 1.00 61.72 C ANISOU 1694 CD ARG A 206 8287 6225 8938 2071 -733 447 C ATOM 1695 NE ARG A 206 19.719 -32.482 25.381 1.00 73.76 N ANISOU 1695 NE ARG A 206 9935 7711 10379 2308 -740 588 N ATOM 1696 CZ ARG A 206 20.037 -32.142 26.627 1.00 77.02 C ANISOU 1696 CZ ARG A 206 10375 8307 10582 2460 -828 674 C ATOM 1697 NH1 ARG A 206 19.805 -30.908 27.059 1.00 77.69 N ANISOU 1697 NH1 ARG A 206 10363 8620 10534 2392 -902 636 N ATOM 1698 NH2 ARG A 206 20.588 -33.037 27.439 1.00 78.14 N ANISOU 1698 NH2 ARG A 206 10641 8409 10641 2686 -841 783 N ATOM 1699 N GLN A 207 16.471 -33.231 20.421 1.00 38.68 N ANISOU 1699 N GLN A 207 5293 2675 6728 1283 -264 106 N ATOM 1700 CA GLN A 207 15.741 -34.495 20.424 1.00 40.78 C ANISOU 1700 CA GLN A 207 5733 2607 7153 1224 -68 170 C ATOM 1701 C GLN A 207 15.961 -35.261 19.126 1.00 38.06 C ANISOU 1701 C GLN A 207 5273 2203 6985 1136 -21 -59 C ATOM 1702 O GLN A 207 16.038 -36.493 19.133 1.00 40.36 O ANISOU 1702 O GLN A 207 5707 2275 7353 1185 78 -38 O ATOM 1703 CB GLN A 207 14.255 -34.243 20.663 1.00 42.66 C ANISOU 1703 CB GLN A 207 6026 2794 7390 980 96 240 C ATOM 1704 CG GLN A 207 13.914 -33.837 22.084 1.00 44.42 C ANISOU 1704 CG GLN A 207 6427 3030 7421 1069 101 500 C ATOM 1705 CD GLN A 207 12.433 -33.536 22.252 1.00 45.57 C ANISOU 1705 CD GLN A 207 6597 3162 7556 809 261 538 C ATOM 1706 OE1 GLN A 207 11.586 -34.190 21.642 1.00 48.54 O ANISOU 1706 OE1 GLN A 207 6960 3367 8115 607 441 430 O ATOM 1707 NE2 GLN A 207 12.116 -32.543 23.075 1.00 41.09 N ANISOU 1707 NE2 GLN A 207 6045 2787 6779 814 197 661 N ATOM 1708 N ALEU A 208 16.055 -34.548 18.004 0.60 38.68 N ANISOU 1708 N ALEU A 208 5100 2484 7113 1015 -90 -279 N ATOM 1709 N BLEU A 208 16.065 -34.550 18.001 0.40 38.53 N ANISOU 1709 N BLEU A 208 5080 2465 7094 1016 -91 -280 N ATOM 1710 CA ALEU A 208 16.368 -35.199 16.738 0.60 40.09 C ANISOU 1710 CA ALEU A 208 5142 2666 7423 956 -68 -506 C ATOM 1711 CA BLEU A 208 16.366 -35.213 16.736 0.40 40.17 C ANISOU 1711 CA BLEU A 208 5154 2674 7434 956 -67 -506 C ATOM 1712 C ALEU A 208 17.754 -35.829 16.775 0.60 41.68 C ANISOU 1712 C ALEU A 208 5371 2860 7605 1187 -169 -514 C ATOM 1713 C BLEU A 208 17.762 -35.825 16.755 0.40 41.65 C ANISOU 1713 C BLEU A 208 5364 2860 7603 1186 -170 -517 C ATOM 1714 O ALEU A 208 17.944 -36.963 16.315 0.60 44.06 O ANISOU 1714 O ALEU A 208 5714 3008 8019 1204 -100 -584 O ATOM 1715 O BLEU A 208 17.966 -36.941 16.262 0.40 43.82 O ANISOU 1715 O BLEU A 208 5671 2987 7990 1201 -104 -594 O ATOM 1716 CB ALEU A 208 16.268 -34.184 15.600 0.60 39.29 C ANISOU 1716 CB ALEU A 208 4784 2829 7314 826 -125 -717 C ATOM 1717 CB BLEU A 208 16.227 -34.223 15.578 0.40 39.30 C ANISOU 1717 CB BLEU A 208 4786 2823 7322 819 -118 -721 C ATOM 1718 CG ALEU A 208 16.813 -34.629 14.245 0.60 42.82 C ANISOU 1718 CG ALEU A 208 5056 3371 7842 804 -140 -955 C ATOM 1719 CG BLEU A 208 14.810 -33.846 15.135 0.40 37.77 C ANISOU 1719 CG BLEU A 208 4533 2704 7115 575 2 -788 C ATOM 1720 CD1ALEU A 208 15.982 -35.768 13.674 0.60 47.05 C ANISOU 1720 CD1ALEU A 208 5604 3740 8533 665 13 -1065 C ATOM 1721 CD1BLEU A 208 14.832 -32.615 14.233 0.40 38.54 C ANISOU 1721 CD1BLEU A 208 4429 3146 7070 506 -67 -913 C ATOM 1722 CD2ALEU A 208 16.856 -33.442 13.290 0.60 43.53 C ANISOU 1722 CD2ALEU A 208 4929 3756 7853 733 -194 -1109 C ATOM 1723 CD2BLEU A 208 14.127 -35.012 14.429 0.40 37.15 C ANISOU 1723 CD2BLEU A 208 4429 2448 7237 451 151 -955 C ATOM 1724 N ALA A1001 18.733 -35.110 17.329 1.00 68.27 N ANISOU 1724 N ALA A1001 8440 5036 12462 2518 -2089 -700 N ATOM 1725 CA ALA A1001 20.088 -35.639 17.430 1.00 65.55 C ANISOU 1725 CA ALA A1001 7798 4423 12684 2184 -1687 -408 C ATOM 1726 C ALA A1001 20.144 -36.847 18.358 1.00 61.62 C ANISOU 1726 C ALA A1001 6804 4422 12185 2060 -1745 -577 C ATOM 1727 O ALA A1001 20.905 -37.790 18.113 1.00 60.64 O ANISOU 1727 O ALA A1001 6536 4234 12269 1887 -1348 -343 O ATOM 1728 CB ALA A1001 21.041 -34.545 17.913 1.00 69.22 C ANISOU 1728 CB ALA A1001 8076 4461 13762 1963 -1756 -362 C ATOM 1729 N ASP A1002 19.344 -36.840 19.425 1.00 59.85 N ANISOU 1729 N ASP A1002 6363 4710 11669 2159 -2173 -949 N ATOM 1730 CA ASP A1002 19.305 -37.998 20.308 1.00 56.92 C ANISOU 1730 CA ASP A1002 5641 4816 11169 2075 -2128 -1045 C ATOM 1731 C ASP A1002 18.714 -39.213 19.600 1.00 58.19 C ANISOU 1731 C ASP A1002 5873 5168 11070 2123 -1863 -972 C ATOM 1732 O ASP A1002 19.174 -40.340 19.814 1.00 56.39 O ANISOU 1732 O ASP A1002 5438 5049 10940 1985 -1593 -849 O ATOM 1733 CB ASP A1002 18.525 -37.663 21.579 1.00 58.88 C ANISOU 1733 CB ASP A1002 5772 5549 11049 2178 -2502 -1388 C ATOM 1734 CG ASP A1002 19.243 -36.643 22.450 1.00 67.10 C ANISOU 1734 CG ASP A1002 6721 6406 12368 2136 -2799 -1534 C ATOM 1735 OD1 ASP A1002 20.457 -36.438 22.243 1.00 70.77 O ANISOU 1735 OD1 ASP A1002 7049 6429 13410 1963 -2705 -1382 O ATOM 1736 OD2 ASP A1002 18.606 -36.045 23.343 1.00 71.69 O ANISOU 1736 OD2 ASP A1002 7353 7257 12628 2275 -3111 -1823 O ATOM 1737 N LEU A1003 17.710 -39.002 18.742 1.00 55.35 N ANISOU 1737 N LEU A1003 5819 4833 10378 2340 -1965 -1086 N ATOM 1738 CA LEU A1003 17.162 -40.100 17.951 1.00 56.35 C ANISOU 1738 CA LEU A1003 6038 5102 10272 2382 -1766 -1098 C ATOM 1739 C LEU A1003 18.225 -40.719 17.052 1.00 56.90 C ANISOU 1739 C LEU A1003 6307 4825 10489 2207 -1263 -703 C ATOM 1740 O LEU A1003 18.383 -41.946 17.010 1.00 54.90 O ANISOU 1740 O LEU A1003 5923 4725 10210 2052 -1004 -633 O ATOM 1741 CB LEU A1003 15.984 -39.608 17.112 1.00 59.94 C ANISOU 1741 CB LEU A1003 6840 5629 10306 2704 -2036 -1358 C ATOM 1742 CG LEU A1003 14.655 -39.408 17.835 1.00 63.05 C ANISOU 1742 CG LEU A1003 6995 6556 10404 2808 -2421 -1786 C ATOM 1743 CD1 LEU A1003 13.658 -38.776 16.897 1.00 64.52 C ANISOU 1743 CD1 LEU A1003 7565 6769 10179 3129 -2701 -2044 C ATOM 1744 CD2 LEU A1003 14.146 -40.746 18.337 1.00 65.67 C ANISOU 1744 CD2 LEU A1003 6892 7290 10771 2655 -2284 -1922 C ATOM 1745 N GLU A1004 18.957 -39.882 16.313 1.00 62.55 N ANISOU 1745 N GLU A1004 7352 5047 11368 2248 -1083 -424 N ATOM 1746 CA GLU A1004 19.993 -40.400 15.427 1.00 68.34 C ANISOU 1746 CA GLU A1004 8271 5462 12233 2133 -533 -14 C ATOM 1747 C GLU A1004 21.160 -40.993 16.206 1.00 67.01 C ANISOU 1747 C GLU A1004 7635 5277 12550 1816 -305 143 C ATOM 1748 O GLU A1004 21.781 -41.957 15.742 1.00 65.81 O ANISOU 1748 O GLU A1004 7496 5103 12407 1720 94 362 O ATOM 1749 CB GLU A1004 20.485 -39.304 14.485 1.00 77.64 C ANISOU 1749 CB GLU A1004 9911 6085 13503 2270 -293 307 C ATOM 1750 CG GLU A1004 19.431 -38.826 13.500 1.00 85.17 C ANISOU 1750 CG GLU A1004 11476 7022 13864 2711 -466 191 C ATOM 1751 CD GLU A1004 18.830 -39.960 12.680 1.00 87.90 C ANISOU 1751 CD GLU A1004 12053 7660 13685 2924 -408 64 C ATOM 1752 OE1 GLU A1004 19.566 -40.903 12.301 1.00 86.67 O ANISOU 1752 OE1 GLU A1004 11870 7469 13593 2797 14 307 O ATOM 1753 OE2 GLU A1004 17.608 -39.901 12.417 1.00 90.75 O ANISOU 1753 OE2 GLU A1004 12601 8281 13597 3244 -828 -331 O ATOM 1754 N ASP A1005 21.470 -40.444 17.383 1.00 65.50 N ANISOU 1754 N ASP A1005 7045 5104 12737 1721 -598 -9 N ATOM 1755 CA ASP A1005 22.535 -41.018 18.199 1.00 63.79 C ANISOU 1755 CA ASP A1005 6386 4927 12924 1514 -482 46 C ATOM 1756 C ASP A1005 22.174 -42.418 18.675 1.00 60.06 C ANISOU 1756 C ASP A1005 5767 4897 12157 1509 -437 -43 C ATOM 1757 O ASP A1005 23.023 -43.314 18.666 1.00 58.80 O ANISOU 1757 O ASP A1005 5478 4716 12148 1390 -127 130 O ATOM 1758 CB ASP A1005 22.845 -40.115 19.390 1.00 66.16 C ANISOU 1758 CB ASP A1005 6373 5273 13491 1461 -900 -198 C ATOM 1759 CG ASP A1005 23.627 -38.884 18.992 1.00 73.22 C ANISOU 1759 CG ASP A1005 7284 5633 14904 1334 -842 -65 C ATOM 1760 OD1 ASP A1005 24.412 -38.971 18.025 1.00 76.74 O ANISOU 1760 OD1 ASP A1005 7834 5717 15605 1194 -328 297 O ATOM 1761 OD2 ASP A1005 23.453 -37.829 19.644 1.00 76.24 O ANISOU 1761 OD2 ASP A1005 7585 5964 15417 1372 -1275 -313 O ATOM 1762 N ASN A1006 20.924 -42.629 19.100 1.00 59.70 N ANISOU 1762 N ASN A1006 5730 5240 11712 1634 -712 -307 N ATOM 1763 CA ASN A1006 20.524 -43.967 19.524 1.00 60.51 C ANISOU 1763 CA ASN A1006 5707 5693 11591 1584 -585 -348 C ATOM 1764 C ASN A1006 20.568 -44.948 18.357 1.00 55.81 C ANISOU 1764 C ASN A1006 5373 4991 10842 1497 -219 -176 C ATOM 1765 O ASN A1006 20.982 -46.101 18.520 1.00 52.66 O ANISOU 1765 O ASN A1006 4893 4649 10466 1391 30 -63 O ATOM 1766 CB ASN A1006 19.130 -43.932 20.155 1.00 64.48 C ANISOU 1766 CB ASN A1006 6110 6601 11787 1712 -874 -650 C ATOM 1767 CG ASN A1006 19.170 -43.691 21.657 1.00 69.48 C ANISOU 1767 CG ASN A1006 6514 7530 12354 1790 -1079 -763 C ATOM 1768 OD1 ASN A1006 20.204 -43.879 22.301 1.00 74.37 O ANISOU 1768 OD1 ASN A1006 7059 8110 13087 1737 -1008 -651 O ATOM 1769 ND2 ASN A1006 18.040 -43.289 22.224 1.00 68.32 N ANISOU 1769 ND2 ASN A1006 6338 7725 11895 1918 -1308 -991 N ATOM 1770 N TRP A1007 20.154 -44.502 17.170 1.00 54.76 N ANISOU 1770 N TRP A1007 5603 4689 10515 1610 -210 -172 N ATOM 1771 CA TRP A1007 20.184 -45.354 15.987 1.00 52.97 C ANISOU 1771 CA TRP A1007 5690 4357 10081 1649 69 -62 C ATOM 1772 C TRP A1007 21.615 -45.723 15.610 1.00 53.00 C ANISOU 1772 C TRP A1007 5728 4089 10320 1561 509 308 C ATOM 1773 O TRP A1007 21.914 -46.893 15.334 1.00 51.57 O ANISOU 1773 O TRP A1007 5582 3938 10074 1518 743 386 O ATOM 1774 CB TRP A1007 19.475 -44.643 14.833 1.00 53.38 C ANISOU 1774 CB TRP A1007 6192 4287 9803 1935 -65 -159 C ATOM 1775 CG TRP A1007 19.490 -45.385 13.533 1.00 57.93 C ANISOU 1775 CG TRP A1007 7176 4747 10086 2123 151 -96 C ATOM 1776 CD1 TRP A1007 20.260 -45.108 12.441 1.00 62.19 C ANISOU 1776 CD1 TRP A1007 8153 4964 10514 2330 503 235 C ATOM 1777 CD2 TRP A1007 18.690 -46.523 13.182 1.00 56.50 C ANISOU 1777 CD2 TRP A1007 7013 4754 9700 2170 28 -391 C ATOM 1778 NE1 TRP A1007 19.994 -46.005 11.437 1.00 64.15 N ANISOU 1778 NE1 TRP A1007 8738 5230 10407 2577 566 147 N ATOM 1779 CE2 TRP A1007 19.032 -46.882 11.864 1.00 60.41 C ANISOU 1779 CE2 TRP A1007 7996 5045 9912 2464 233 -272 C ATOM 1780 CE3 TRP A1007 17.718 -47.271 13.856 1.00 53.84 C ANISOU 1780 CE3 TRP A1007 6313 4707 9435 1999 -211 -744 C ATOM 1781 CZ2 TRP A1007 18.440 -47.958 11.205 1.00 62.52 C ANISOU 1781 CZ2 TRP A1007 8399 5382 9974 2612 100 -569 C ATOM 1782 CZ3 TRP A1007 17.123 -48.331 13.201 1.00 58.05 C ANISOU 1782 CZ3 TRP A1007 6926 5265 9864 2060 -286 -1010 C ATOM 1783 CH2 TRP A1007 17.488 -48.668 11.887 1.00 60.96 C ANISOU 1783 CH2 TRP A1007 7785 5419 9957 2374 -184 -958 C ATOM 1784 N GLU A1008 22.520 -44.739 15.607 1.00 53.70 N ANISOU 1784 N GLU A1008 5774 3889 10740 1530 629 521 N ATOM 1785 CA GLU A1008 23.925 -45.026 15.322 1.00 57.96 C ANISOU 1785 CA GLU A1008 6222 4184 11615 1429 1076 850 C ATOM 1786 C GLU A1008 24.514 -45.983 16.348 1.00 57.83 C ANISOU 1786 C GLU A1008 5797 4370 11806 1284 1071 794 C ATOM 1787 O GLU A1008 25.244 -46.914 15.990 1.00 59.37 O ANISOU 1787 O GLU A1008 6005 4533 12019 1271 1403 964 O ATOM 1788 CB GLU A1008 24.736 -43.732 15.291 1.00 60.65 C ANISOU 1788 CB GLU A1008 6459 4139 12446 1357 1188 1038 C ATOM 1789 CG GLU A1008 24.364 -42.774 14.190 1.00 67.84 C ANISOU 1789 CG GLU A1008 7875 4759 13144 1541 1320 1207 C ATOM 1790 CD GLU A1008 25.011 -41.419 14.390 1.00 78.41 C ANISOU 1790 CD GLU A1008 9068 5773 14951 1371 1344 1320 C ATOM 1791 OE1 GLU A1008 25.999 -41.352 15.157 1.00 84.00 O ANISOU 1791 OE1 GLU A1008 9246 6427 16243 1111 1364 1305 O ATOM 1792 OE2 GLU A1008 24.536 -40.428 13.796 1.00 81.15 O ANISOU 1792 OE2 GLU A1008 9824 5897 15114 1523 1314 1390 O ATOM 1793 N THR A1009 24.214 -45.765 17.630 1.00 57.66 N ANISOU 1793 N THR A1009 5456 4561 11892 1249 695 553 N ATOM 1794 CA THR A1009 24.736 -46.637 18.678 1.00 59.24 C ANISOU 1794 CA THR A1009 5352 4955 12201 1227 671 498 C ATOM 1795 C THR A1009 24.275 -48.076 18.478 1.00 58.00 C ANISOU 1795 C THR A1009 5376 4974 11688 1225 849 527 C ATOM 1796 O THR A1009 25.049 -49.021 18.672 1.00 58.19 O ANISOU 1796 O THR A1009 5331 4998 11779 1225 1053 635 O ATOM 1797 CB THR A1009 24.303 -46.112 20.049 1.00 61.54 C ANISOU 1797 CB THR A1009 5423 5513 12445 1283 223 225 C ATOM 1798 OG1 THR A1009 24.924 -44.841 20.287 1.00 66.61 O ANISOU 1798 OG1 THR A1009 5910 5974 13423 1230 14 150 O ATOM 1799 CG2 THR A1009 24.700 -47.085 21.158 1.00 61.72 C ANISOU 1799 CG2 THR A1009 5327 5806 12317 1330 201 176 C ATOM 1800 N LEU A1010 23.018 -48.261 18.082 1.00 54.42 N ANISOU 1800 N LEU A1010 5136 4641 10902 1233 750 394 N ATOM 1801 CA LEU A1010 22.510 -49.600 17.818 1.00 51.06 C ANISOU 1801 CA LEU A1010 4850 4294 10256 1192 893 371 C ATOM 1802 C LEU A1010 23.310 -50.282 16.711 1.00 51.32 C ANISOU 1802 C LEU A1010 5133 4105 10261 1231 1220 569 C ATOM 1803 O LEU A1010 23.719 -51.440 16.845 1.00 49.10 O ANISOU 1803 O LEU A1010 4867 3815 9974 1209 1400 644 O ATOM 1804 CB LEU A1010 21.029 -49.512 17.455 1.00 53.03 C ANISOU 1804 CB LEU A1010 5205 4671 10274 1199 676 110 C ATOM 1805 CG LEU A1010 20.284 -50.778 17.054 1.00 56.17 C ANISOU 1805 CG LEU A1010 5698 5083 10562 1124 747 -20 C ATOM 1806 CD1 LEU A1010 20.415 -51.813 18.143 1.00 57.80 C ANISOU 1806 CD1 LEU A1010 5710 5371 10879 990 917 72 C ATOM 1807 CD2 LEU A1010 18.819 -50.446 16.799 1.00 56.27 C ANISOU 1807 CD2 LEU A1010 5675 5242 10463 1146 451 -372 C ATOM 1808 N ASN A1011 23.573 -49.566 15.619 1.00 51.70 N ANISOU 1808 N ASN A1011 5418 3960 10264 1343 1330 680 N ATOM 1809 CA ASN A1011 24.248 -50.183 14.482 1.00 53.31 C ANISOU 1809 CA ASN A1011 5917 3988 10350 1479 1675 876 C ATOM 1810 C ASN A1011 25.748 -50.338 14.719 1.00 53.15 C ANISOU 1810 C ASN A1011 5674 3865 10656 1441 2002 1139 C ATOM 1811 O ASN A1011 26.338 -51.345 14.306 1.00 53.89 O ANISOU 1811 O ASN A1011 5878 3925 10672 1526 2251 1245 O ATOM 1812 CB ASN A1011 23.970 -49.375 13.215 1.00 55.81 C ANISOU 1812 CB ASN A1011 6643 4140 10423 1716 1742 942 C ATOM 1813 CG ASN A1011 22.534 -49.519 12.750 1.00 58.05 C ANISOU 1813 CG ASN A1011 7183 4536 10338 1859 1389 597 C ATOM 1814 OD1 ASN A1011 21.937 -50.585 12.876 1.00 59.69 O ANISOU 1814 OD1 ASN A1011 7353 4856 10472 1802 1246 364 O ATOM 1815 ND2 ASN A1011 21.970 -48.448 12.221 1.00 61.96 N ANISOU 1815 ND2 ASN A1011 7921 4973 10648 2055 1236 537 N ATOM 1816 N ASP A1012 26.378 -49.364 15.380 1.00 53.60 N ANISOU 1816 N ASP A1012 5388 3864 11114 1337 1967 1195 N ATOM 1817 CA ASP A1012 27.794 -49.494 15.715 1.00 56.79 C ANISOU 1817 CA ASP A1012 5456 4195 11925 1291 2199 1341 C ATOM 1818 C ASP A1012 28.035 -50.707 16.602 1.00 54.64 C ANISOU 1818 C ASP A1012 5047 4139 11575 1296 2097 1227 C ATOM 1819 O ASP A1012 28.929 -51.520 16.341 1.00 54.84 O ANISOU 1819 O ASP A1012 5072 4161 11604 1354 2348 1340 O ATOM 1820 CB ASP A1012 28.293 -48.226 16.406 1.00 60.39 C ANISOU 1820 CB ASP A1012 5513 4557 12874 1149 2030 1286 C ATOM 1821 CG ASP A1012 28.318 -47.031 15.479 1.00 66.48 C ANISOU 1821 CG ASP A1012 6440 5019 13801 1130 2246 1485 C ATOM 1822 OD1 ASP A1012 28.426 -47.240 14.253 1.00 69.12 O ANISOU 1822 OD1 ASP A1012 7146 5236 13881 1254 2658 1741 O ATOM 1823 OD2 ASP A1012 28.232 -45.886 15.975 1.00 68.87 O ANISOU 1823 OD2 ASP A1012 6542 5200 14424 1026 1999 1382 O ATOM 1824 N ASN A1013 27.240 -50.849 17.660 1.00 53.41 N ANISOU 1824 N ASN A1013 4811 4171 11310 1277 1757 1022 N ATOM 1825 CA ASN A1013 27.469 -51.950 18.585 1.00 55.89 C ANISOU 1825 CA ASN A1013 5075 4653 11506 1332 1705 967 C ATOM 1826 C ASN A1013 27.141 -53.300 17.959 1.00 52.84 C ANISOU 1826 C ASN A1013 5012 4191 10875 1391 1933 1047 C ATOM 1827 O ASN A1013 27.726 -54.313 18.355 1.00 51.36 O ANISOU 1827 O ASN A1013 4856 4032 10628 1476 2023 1091 O ATOM 1828 CB ASN A1013 26.682 -51.712 19.868 1.00 57.79 C ANISOU 1828 CB ASN A1013 5199 5106 11653 1358 1372 785 C ATOM 1829 CG ASN A1013 27.403 -50.760 20.804 1.00 59.74 C ANISOU 1829 CG ASN A1013 5169 5464 12064 1380 1066 633 C ATOM 1830 OD1 ASN A1013 28.618 -50.860 20.976 1.00 65.07 O ANISOU 1830 OD1 ASN A1013 5695 6118 12911 1410 1083 624 O ATOM 1831 ND2 ASN A1013 26.672 -49.832 21.398 1.00 56.38 N ANISOU 1831 ND2 ASN A1013 4671 5153 11598 1391 756 466 N ATOM 1832 N LEU A1014 26.242 -53.335 16.971 1.00 53.39 N ANISOU 1832 N LEU A1014 5375 4192 10719 1340 1955 1016 N ATOM 1833 CA LEU A1014 26.056 -54.552 16.184 1.00 54.31 C ANISOU 1833 CA LEU A1014 5821 4203 10611 1399 2104 1024 C ATOM 1834 C LEU A1014 27.345 -54.948 15.475 1.00 57.34 C ANISOU 1834 C LEU A1014 6285 4474 11028 1578 2416 1216 C ATOM 1835 O LEU A1014 27.735 -56.123 15.485 1.00 58.13 O ANISOU 1835 O LEU A1014 6516 4525 11045 1673 2524 1243 O ATOM 1836 CB LEU A1014 24.927 -54.359 15.172 1.00 54.01 C ANISOU 1836 CB LEU A1014 6058 4114 10351 1407 1979 864 C ATOM 1837 CG LEU A1014 23.519 -54.646 15.683 1.00 55.87 C ANISOU 1837 CG LEU A1014 6238 4437 10553 1238 1722 610 C ATOM 1838 CD1 LEU A1014 22.464 -54.222 14.661 1.00 57.13 C ANISOU 1838 CD1 LEU A1014 6596 4573 10536 1314 1507 362 C ATOM 1839 CD2 LEU A1014 23.390 -56.125 16.016 1.00 55.89 C ANISOU 1839 CD2 LEU A1014 6312 4338 10584 1160 1815 589 C ATOM 1840 N LYS A1015 28.017 -53.977 14.843 1.00 57.94 N ANISOU 1840 N LYS A1015 6289 4497 11227 1629 2594 1364 N ATOM 1841 CA LYS A1015 29.301 -54.259 14.202 1.00 59.62 C ANISOU 1841 CA LYS A1015 6501 4682 11471 1757 2944 1560 C ATOM 1842 C LYS A1015 30.335 -54.725 15.218 1.00 61.09 C ANISOU 1842 C LYS A1015 6340 4986 11884 1721 2916 1541 C ATOM 1843 O LYS A1015 31.097 -55.661 14.951 1.00 63.41 O ANISOU 1843 O LYS A1015 6718 5300 12076 1869 3087 1598 O ATOM 1844 CB LYS A1015 29.819 -53.022 13.473 1.00 62.54 C ANISOU 1844 CB LYS A1015 6794 4933 12036 1768 3224 1771 C ATOM 1845 CG LYS A1015 28.984 -52.565 12.301 1.00 68.05 C ANISOU 1845 CG LYS A1015 7959 5521 12377 1931 3288 1823 C ATOM 1846 CD LYS A1015 29.472 -51.204 11.821 1.00 75.93 C ANISOU 1846 CD LYS A1015 8878 6349 13623 1913 3593 2081 C ATOM 1847 CE LYS A1015 28.595 -50.635 10.715 1.00 81.15 C ANISOU 1847 CE LYS A1015 10088 6920 13826 2147 3609 2126 C ATOM 1848 NZ LYS A1015 28.814 -51.334 9.419 1.00 86.83 N ANISOU 1848 NZ LYS A1015 11302 7644 14044 2543 3924 2262 N ATOM 1849 N VAL A1016 30.391 -54.064 16.378 1.00 61.52 N ANISOU 1849 N VAL A1016 6039 5135 12200 1582 2647 1420 N ATOM 1850 CA VAL A1016 31.336 -54.445 17.429 1.00 63.05 C ANISOU 1850 CA VAL A1016 5963 5468 12526 1628 2499 1317 C ATOM 1851 C VAL A1016 31.173 -55.919 17.783 1.00 61.53 C ANISOU 1851 C VAL A1016 6051 5329 12000 1791 2479 1290 C ATOM 1852 O VAL A1016 32.157 -56.657 17.926 1.00 58.25 O ANISOU 1852 O VAL A1016 5608 4964 11560 1953 2538 1287 O ATOM 1853 CB VAL A1016 31.147 -53.535 18.661 1.00 56.41 C ANISOU 1853 CB VAL A1016 4831 4741 11863 1541 2103 1115 C ATOM 1854 CG1 VAL A1016 31.940 -54.052 19.850 1.00 60.59 C ANISOU 1854 CG1 VAL A1016 5211 5450 12359 1719 1854 934 C ATOM 1855 CG2 VAL A1016 31.555 -52.117 18.337 1.00 58.08 C ANISOU 1855 CG2 VAL A1016 4738 4813 12518 1375 2124 1128 C ATOM 1856 N ILE A1017 29.925 -56.374 17.909 1.00 59.25 N ANISOU 1856 N ILE A1017 6031 4986 11495 1756 2408 1267 N ATOM 1857 CA ILE A1017 29.665 -57.771 18.247 1.00 58.52 C ANISOU 1857 CA ILE A1017 6231 4828 11177 1870 2444 1277 C ATOM 1858 C ILE A1017 30.100 -58.693 17.115 1.00 59.56 C ANISOU 1858 C ILE A1017 6652 4828 11151 1987 2664 1347 C ATOM 1859 O ILE A1017 30.663 -59.768 17.358 1.00 61.23 O ANISOU 1859 O ILE A1017 7019 5014 11233 2155 2705 1362 O ATOM 1860 CB ILE A1017 28.177 -57.960 18.592 1.00 54.77 C ANISOU 1860 CB ILE A1017 5907 4251 10654 1747 2378 1238 C ATOM 1861 CG1 ILE A1017 27.844 -57.202 19.876 1.00 56.10 C ANISOU 1861 CG1 ILE A1017 5816 4607 10894 1744 2175 1178 C ATOM 1862 CG2 ILE A1017 27.832 -59.436 18.722 1.00 54.74 C ANISOU 1862 CG2 ILE A1017 6245 4050 10503 1785 2494 1283 C ATOM 1863 CD1 ILE A1017 26.373 -57.100 20.157 1.00 55.31 C ANISOU 1863 CD1 ILE A1017 5775 4537 10703 1539 2102 1117 C ATOM 1864 N GLU A1018 29.863 -58.287 15.865 1.00 58.64 N ANISOU 1864 N GLU A1018 6662 4632 10988 1968 2787 1379 N ATOM 1865 CA GLU A1018 30.153 -59.167 14.737 1.00 62.59 C ANISOU 1865 CA GLU A1018 7507 5027 11248 2163 2953 1407 C ATOM 1866 C GLU A1018 31.642 -59.460 14.621 1.00 68.93 C ANISOU 1866 C GLU A1018 8177 5940 12075 2358 3148 1510 C ATOM 1867 O GLU A1018 32.035 -60.584 14.285 1.00 74.32 O ANISOU 1867 O GLU A1018 9117 6573 12547 2563 3202 1495 O ATOM 1868 CB GLU A1018 29.623 -58.557 13.442 1.00 64.32 C ANISOU 1868 CB GLU A1018 7940 5175 11323 2222 3027 1412 C ATOM 1869 CG GLU A1018 28.123 -58.694 13.291 1.00 66.66 C ANISOU 1869 CG GLU A1018 8461 5323 11545 2127 2780 1207 C ATOM 1870 CD GLU A1018 27.547 -57.762 12.245 1.00 72.66 C ANISOU 1870 CD GLU A1018 9392 6059 12157 2232 2763 1169 C ATOM 1871 OE1 GLU A1018 28.324 -57.159 11.470 1.00 75.48 O ANISOU 1871 OE1 GLU A1018 9802 6478 12399 2411 3022 1364 O ATOM 1872 OE2 GLU A1018 26.306 -57.628 12.210 1.00 74.98 O ANISOU 1872 OE2 GLU A1018 9762 6310 12418 2123 2481 936 O ATOM 1873 N LYS A1019 32.489 -58.472 14.904 1.00 70.17 N ANISOU 1873 N LYS A1019 7908 6221 12531 2295 3232 1580 N ATOM 1874 CA LYS A1019 33.932 -58.654 14.800 1.00 73.91 C ANISOU 1874 CA LYS A1019 8152 6796 13136 2452 3415 1635 C ATOM 1875 C LYS A1019 34.606 -58.780 16.163 1.00 73.68 C ANISOU 1875 C LYS A1019 7798 6908 13290 2469 3143 1471 C ATOM 1876 O LYS A1019 35.831 -58.644 16.261 1.00 74.35 O ANISOU 1876 O LYS A1019 7548 7098 13605 2559 3198 1428 O ATOM 1877 CB LYS A1019 34.560 -57.520 13.990 1.00 79.05 C ANISOU 1877 CB LYS A1019 8543 7420 14073 2393 3754 1820 C ATOM 1878 CG LYS A1019 34.230 -56.130 14.465 1.00 81.32 C ANISOU 1878 CG LYS A1019 8503 7657 14739 2112 3646 1811 C ATOM 1879 CD LYS A1019 34.854 -55.106 13.539 1.00 89.91 C ANISOU 1879 CD LYS A1019 9411 8607 16145 2069 4090 2065 C ATOM 1880 CE LYS A1019 34.553 -55.425 12.078 1.00 95.14 C ANISOU 1880 CE LYS A1019 10581 9197 16372 2334 4490 2301 C ATOM 1881 NZ LYS A1019 35.262 -54.501 11.140 1.00101.83 N ANISOU 1881 NZ LYS A1019 11322 9886 17484 2373 5060 2646 N ATOM 1882 N ALA A1020 33.834 -59.043 17.213 1.00 70.01 N ANISOU 1882 N ALA A1020 7438 6451 12710 2431 2850 1359 N ATOM 1883 CA ALA A1020 34.428 -59.402 18.489 1.00 73.04 C ANISOU 1883 CA ALA A1020 7686 6976 13090 2611 2580 1194 C ATOM 1884 C ALA A1020 35.119 -60.760 18.378 1.00 76.45 C ANISOU 1884 C ALA A1020 8374 7398 13277 2922 2642 1186 C ATOM 1885 O ALA A1020 34.828 -61.567 17.489 1.00 65.54 O ANISOU 1885 O ALA A1020 7357 5868 11678 2966 2838 1298 O ATOM 1886 CB ALA A1020 33.366 -59.436 19.589 1.00 69.23 C ANISOU 1886 CB ALA A1020 7353 6489 12461 2578 2350 1150 C ATOM 1887 N ASP A1021 36.054 -61.009 19.294 1.00 81.44 N ANISOU 1887 N ASP A1021 8830 8188 13925 3189 2415 1000 N ATOM 1888 CA ASP A1021 36.755 -62.284 19.320 1.00 86.08 C ANISOU 1888 CA ASP A1021 9665 8772 14269 3541 2413 954 C ATOM 1889 C ASP A1021 36.662 -62.999 20.661 1.00 86.66 C ANISOU 1889 C ASP A1021 9990 8852 14084 3835 2130 847 C ATOM 1890 O ASP A1021 37.171 -64.119 20.780 1.00 90.60 O ANISOU 1890 O ASP A1021 10769 9302 14353 4144 2104 816 O ATOM 1891 CB ASP A1021 38.230 -62.099 18.923 1.00 95.37 C ANISOU 1891 CB ASP A1021 10417 10134 15684 3713 2454 807 C ATOM 1892 CG ASP A1021 39.073 -61.491 20.031 1.00102.07 C ANISOU 1892 CG ASP A1021 10802 11214 16767 3888 2085 479 C ATOM 1893 OD1 ASP A1021 38.585 -60.559 20.709 1.00100.44 O ANISOU 1893 OD1 ASP A1021 10423 11046 16695 3724 1883 409 O ATOM 1894 OD2 ASP A1021 40.229 -61.949 20.217 1.00106.98 O ANISOU 1894 OD2 ASP A1021 11236 11994 17417 4234 1960 248 O ATOM 1895 N ASN A1022 36.022 -62.404 21.666 1.00 73.75 N ANISOU 1895 N ASN A1022 6332 10045 11644 2152 965 2957 N ATOM 1896 CA ASN A1022 35.787 -63.098 22.925 1.00 75.25 C ANISOU 1896 CA ASN A1022 6617 10709 11264 2598 938 2902 C ATOM 1897 C ASN A1022 34.437 -62.675 23.489 1.00 71.29 C ANISOU 1897 C ASN A1022 6374 9933 10779 2367 785 2510 C ATOM 1898 O ASN A1022 33.832 -61.693 23.050 1.00 68.47 O ANISOU 1898 O ASN A1022 5998 9151 10868 1884 612 2217 O ATOM 1899 CB ASN A1022 36.910 -62.844 23.939 1.00 79.82 C ANISOU 1899 CB ASN A1022 6515 12166 11647 2866 613 2701 C ATOM 1900 CG ASN A1022 37.105 -61.376 24.240 1.00 80.17 C ANISOU 1900 CG ASN A1022 5961 12328 12172 2342 135 2101 C ATOM 1901 OD1 ASN A1022 36.258 -60.742 24.868 1.00 79.75 O ANISOU 1901 OD1 ASN A1022 5966 12154 12181 2122 -109 1672 O ATOM 1902 ND2 ASN A1022 38.234 -60.828 23.804 1.00 80.83 N ANISOU 1902 ND2 ASN A1022 5472 12639 12602 2131 36 2057 N ATOM 1903 N ALA A1023 33.977 -63.434 24.488 1.00 70.34 N ANISOU 1903 N ALA A1023 6513 10075 10138 2768 887 2527 N ATOM 1904 CA ALA A1023 32.640 -63.224 25.032 1.00 67.78 C ANISOU 1904 CA ALA A1023 6483 9503 9769 2609 829 2217 C ATOM 1905 C ALA A1023 32.536 -61.917 25.806 1.00 70.48 C ANISOU 1905 C ALA A1023 6360 10084 10335 2341 299 1635 C ATOM 1906 O ALA A1023 31.450 -61.331 25.879 1.00 70.04 O ANISOU 1906 O ALA A1023 6470 9687 10455 2041 189 1332 O ATOM 1907 CB ALA A1023 32.246 -64.401 25.924 1.00 68.09 C ANISOU 1907 CB ALA A1023 6937 9745 9190 3132 1155 2418 C ATOM 1908 N ALA A1024 33.641 -61.447 26.388 1.00 72.22 N ANISOU 1908 N ALA A1024 5991 10910 10540 2447 -24 1444 N ATOM 1909 CA ALA A1024 33.595 -60.211 27.163 1.00 72.17 C ANISOU 1909 CA ALA A1024 5549 11133 10738 2169 -514 831 C ATOM 1910 C ALA A1024 33.282 -59.010 26.278 1.00 69.14 C ANISOU 1910 C ALA A1024 5106 10138 11025 1519 -632 585 C ATOM 1911 O ALA A1024 32.548 -58.104 26.691 1.00 68.07 O ANISOU 1911 O ALA A1024 4977 9824 11064 1251 -873 146 O ATOM 1912 CB ALA A1024 34.916 -60.003 27.903 1.00 76.95 C ANISOU 1912 CB ALA A1024 5477 12574 11185 2387 -825 628 C ATOM 1913 N GLN A1025 33.833 -58.983 25.059 1.00 66.77 N ANISOU 1913 N GLN A1025 4784 9506 11081 1313 -430 884 N ATOM 1914 CA GLN A1025 33.574 -57.871 24.150 1.00 63.72 C ANISOU 1914 CA GLN A1025 4406 8506 11300 778 -460 718 C ATOM 1915 C GLN A1025 32.119 -57.854 23.704 1.00 62.37 C ANISOU 1915 C GLN A1025 4803 7744 11151 685 -321 742 C ATOM 1916 O GLN A1025 31.496 -56.788 23.634 1.00 63.08 O ANISOU 1916 O GLN A1025 4927 7488 11551 370 -475 403 O ATOM 1917 CB GLN A1025 34.504 -57.950 22.939 1.00 62.05 C ANISOU 1917 CB GLN A1025 4079 8092 11406 663 -218 1092 C ATOM 1918 CG GLN A1025 35.961 -57.659 23.270 1.00 68.92 C ANISOU 1918 CG GLN A1025 4260 9536 12391 621 -382 964 C ATOM 1919 CD GLN A1025 36.896 -57.886 22.096 1.00 71.42 C ANISOU 1919 CD GLN A1025 4467 9701 12968 574 -87 1398 C ATOM 1920 OE1 GLN A1025 36.471 -58.295 21.014 1.00 68.90 O ANISOU 1920 OE1 GLN A1025 4627 8835 12716 606 239 1814 O ATOM 1921 NE2 GLN A1025 38.182 -57.620 22.308 1.00 76.16 N ANISOU 1921 NE2 GLN A1025 4405 10829 13702 503 -202 1277 N ATOM 1922 N VAL A1026 31.564 -59.026 23.392 1.00 59.67 N ANISOU 1922 N VAL A1026 4906 7293 10474 958 -6 1121 N ATOM 1923 CA VAL A1026 30.148 -59.100 23.049 1.00 53.69 C ANISOU 1923 CA VAL A1026 4611 6099 9688 869 117 1079 C ATOM 1924 C VAL A1026 29.301 -58.617 24.214 1.00 52.57 C ANISOU 1924 C VAL A1026 4448 6131 9397 867 -144 636 C ATOM 1925 O VAL A1026 28.344 -57.857 24.028 1.00 51.64 O ANISOU 1925 O VAL A1026 4462 5691 9468 651 -242 379 O ATOM 1926 CB VAL A1026 29.774 -60.532 22.625 1.00 50.68 C ANISOU 1926 CB VAL A1026 4678 5619 8958 1120 536 1495 C ATOM 1927 CG1 VAL A1026 28.314 -60.606 22.239 1.00 46.72 C ANISOU 1927 CG1 VAL A1026 4566 4744 8442 973 656 1378 C ATOM 1928 CG2 VAL A1026 30.657 -60.988 21.467 1.00 50.58 C ANISOU 1928 CG2 VAL A1026 4705 5439 9075 1156 793 1935 C ATOM 1929 N LYS A1027 29.656 -59.023 25.437 1.00 54.75 N ANISOU 1929 N LYS A1027 4556 6948 9298 1164 -258 546 N ATOM 1930 CA LYS A1027 28.866 -58.637 26.604 1.00 57.75 C ANISOU 1930 CA LYS A1027 4938 7525 9479 1226 -486 146 C ATOM 1931 C LYS A1027 28.857 -57.124 26.792 1.00 59.86 C ANISOU 1931 C LYS A1027 4918 7689 10136 880 -870 -348 C ATOM 1932 O LYS A1027 27.801 -56.524 27.024 1.00 58.96 O ANISOU 1932 O LYS A1027 4973 7358 10071 766 -970 -629 O ATOM 1933 CB LYS A1027 29.394 -59.328 27.861 1.00 61.59 C ANISOU 1933 CB LYS A1027 5287 8660 9453 1690 -533 161 C ATOM 1934 CG LYS A1027 28.721 -58.838 29.135 1.00 64.03 C ANISOU 1934 CG LYS A1027 5555 9231 9543 1793 -802 -275 C ATOM 1935 CD LYS A1027 29.314 -59.481 30.372 1.00 70.96 C ANISOU 1935 CD LYS A1027 6290 10807 9864 2337 -856 -256 C ATOM 1936 CE LYS A1027 28.551 -59.062 31.618 1.00 74.66 C ANISOU 1936 CE LYS A1027 6785 11512 10072 2488 -1082 -660 C ATOM 1937 NZ LYS A1027 29.008 -59.828 32.810 1.00 79.94 N ANISOU 1937 NZ LYS A1027 7413 12859 10102 3136 -1059 -576 N ATOM 1938 N ASP A1028 30.030 -56.490 26.697 1.00 65.83 N ANISOU 1938 N ASP A1028 5242 8595 11174 706 -1054 -473 N ATOM 1939 CA ASP A1028 30.110 -55.039 26.839 1.00 70.01 C ANISOU 1939 CA ASP A1028 5532 8951 12119 319 -1342 -966 C ATOM 1940 C ASP A1028 29.222 -54.337 25.821 1.00 64.33 C ANISOU 1940 C ASP A1028 5161 7514 11769 44 -1200 -945 C ATOM 1941 O ASP A1028 28.506 -53.386 26.155 1.00 65.01 O ANISOU 1941 O ASP A1028 5338 7384 11980 -100 -1359 -1321 O ATOM 1942 CB ASP A1028 31.559 -54.573 26.688 1.00 79.94 C ANISOU 1942 CB ASP A1028 6264 10427 13682 97 -1454 -1072 C ATOM 1943 CG ASP A1028 32.318 -54.593 27.998 1.00 92.11 C ANISOU 1943 CG ASP A1028 7319 12755 14923 277 -1789 -1433 C ATOM 1944 OD1 ASP A1028 32.219 -53.603 28.752 1.00 98.13 O ANISOU 1944 OD1 ASP A1028 7884 13601 15801 63 -2099 -2006 O ATOM 1945 OD2 ASP A1028 33.021 -55.592 28.271 1.00 95.96 O ANISOU 1945 OD2 ASP A1028 7633 13797 15030 668 -1737 -1157 O ATOM 1946 N ALA A1029 29.261 -54.789 24.567 1.00 57.16 N ANISOU 1946 N ALA A1029 4465 6251 11001 23 -892 -505 N ATOM 1947 CA ALA A1029 28.443 -54.155 23.541 1.00 55.56 C ANISOU 1947 CA ALA A1029 4589 5439 11082 -141 -752 -463 C ATOM 1948 C ALA A1029 26.956 -54.369 23.809 1.00 55.16 C ANISOU 1948 C ALA A1029 4880 5337 10743 18 -751 -560 C ATOM 1949 O ALA A1029 26.155 -53.436 23.668 1.00 55.80 O ANISOU 1949 O ALA A1029 5113 5113 10976 -73 -821 -797 O ATOM 1950 CB ALA A1029 28.835 -54.683 22.163 1.00 51.02 C ANISOU 1950 CB ALA A1029 4162 4576 10649 -134 -432 25 C ATOM 1951 N LEU A1030 26.573 -55.580 24.221 1.00 51.13 N ANISOU 1951 N LEU A1030 4494 5126 9808 266 -637 -384 N ATOM 1952 CA LEU A1030 25.163 -55.875 24.468 1.00 49.24 C ANISOU 1952 CA LEU A1030 4533 4869 9307 373 -580 -486 C ATOM 1953 C LEU A1030 24.628 -55.114 25.677 1.00 48.94 C ANISOU 1953 C LEU A1030 4404 5017 9173 400 -868 -937 C ATOM 1954 O LEU A1030 23.466 -54.689 25.682 1.00 45.61 O ANISOU 1954 O LEU A1030 4154 4455 8719 402 -895 -1128 O ATOM 1955 CB LEU A1030 24.968 -57.378 24.657 1.00 47.87 C ANISOU 1955 CB LEU A1030 4537 4917 8735 588 -300 -199 C ATOM 1956 CG LEU A1030 25.122 -58.281 23.432 1.00 45.46 C ANISOU 1956 CG LEU A1030 4446 4382 8446 580 46 217 C ATOM 1957 CD1 LEU A1030 25.316 -59.726 23.877 1.00 44.57 C ANISOU 1957 CD1 LEU A1030 4494 4501 7939 814 348 492 C ATOM 1958 CD2 LEU A1030 23.914 -58.149 22.502 1.00 38.89 C ANISOU 1958 CD2 LEU A1030 3853 3242 7680 463 154 157 C ATOM 1959 N ATHR A1031 25.449 -54.934 26.715 0.52 53.56 N ANISOU 1959 N ATHR A1031 4704 5966 9680 454 -1094 -1132 N ATOM 1960 N BTHR A1031 25.457 -54.946 26.711 0.48 53.56 N ANISOU 1960 N BTHR A1031 4704 5968 9678 455 -1091 -1128 N ATOM 1961 CA ATHR A1031 24.991 -54.175 27.876 0.52 56.45 C ANISOU 1961 CA ATHR A1031 4994 6515 9940 493 -1382 -1593 C ATOM 1962 CA BTHR A1031 25.041 -54.180 27.881 0.48 56.54 C ANISOU 1962 CA BTHR A1031 4994 6535 9953 492 -1385 -1590 C ATOM 1963 C ATHR A1031 24.716 -52.723 27.507 0.52 57.11 C ANISOU 1963 C ATHR A1031 5104 6175 10422 231 -1527 -1906 C ATOM 1964 C BTHR A1031 24.728 -52.737 27.506 0.48 57.11 C ANISOU 1964 C BTHR A1031 5102 6179 10420 232 -1525 -1902 C ATOM 1965 O ATHR A1031 23.752 -52.124 27.996 0.52 57.43 O ANISOU 1965 O ATHR A1031 5285 6155 10381 284 -1638 -2194 O ATOM 1966 O BTHR A1031 23.742 -52.163 27.983 0.48 57.29 O ANISOU 1966 O BTHR A1031 5271 6140 10355 289 -1630 -2181 O ATOM 1967 CB ATHR A1031 26.011 -54.254 29.012 0.52 61.08 C ANISOU 1967 CB ATHR A1031 5233 7639 10335 625 -1620 -1782 C ATOM 1968 CB BTHR A1031 26.128 -54.238 28.956 0.48 61.21 C ANISOU 1968 CB BTHR A1031 5225 7653 10379 607 -1622 -1772 C ATOM 1969 OG1ATHR A1031 27.294 -53.831 28.537 0.52 65.01 O ANISOU 1969 OG1ATHR A1031 5407 8118 11175 391 -1696 -1784 O ATOM 1970 OG1BTHR A1031 26.395 -55.606 29.292 0.48 60.16 O ANISOU 1970 OG1BTHR A1031 5132 7904 9822 953 -1428 -1426 O ATOM 1971 CG2ATHR A1031 26.104 -55.675 29.554 0.52 60.15 C ANISOU 1971 CG2ATHR A1031 5187 7949 9717 1020 -1430 -1467 C ATOM 1972 CG2BTHR A1031 25.690 -53.491 30.206 0.48 63.75 C ANISOU 1972 CG2BTHR A1031 5475 8203 10543 678 -1934 -2278 C ATOM 1973 N LYS A1032 25.549 -52.140 26.638 1.00 57.99 N ANISOU 1973 N LYS A1032 5113 5965 10956 -29 -1478 -1836 N ATOM 1974 CA LYS A1032 25.273 -50.788 26.159 1.00 60.32 C ANISOU 1974 CA LYS A1032 5536 5747 11634 -246 -1496 -2066 C ATOM 1975 C LYS A1032 24.060 -50.758 25.236 1.00 57.65 C ANISOU 1975 C LYS A1032 5579 5059 11265 -113 -1297 -1871 C ATOM 1976 O LYS A1032 23.327 -49.762 25.212 1.00 60.03 O ANISOU 1976 O LYS A1032 6075 5072 11660 -101 -1333 -2103 O ATOM 1977 CB LYS A1032 26.495 -50.214 25.438 1.00 62.52 C ANISOU 1977 CB LYS A1032 5630 5738 12388 -561 -1406 -2013 C ATOM 1978 CG LYS A1032 27.703 -49.975 26.332 1.00 67.27 C ANISOU 1978 CG LYS A1032 5766 6715 13078 -758 -1638 -2342 C ATOM 1979 CD LYS A1032 28.884 -49.426 25.537 1.00 71.86 C ANISOU 1979 CD LYS A1032 6128 7003 14172 -1124 -1486 -2293 C ATOM 1980 CE LYS A1032 30.040 -49.061 26.458 1.00 79.77 C ANISOU 1980 CE LYS A1032 6586 8440 15282 -1379 -1743 -2745 C ATOM 1981 NZ LYS A1032 31.204 -48.477 25.727 1.00 85.93 N ANISOU 1981 NZ LYS A1032 7165 8977 16509 -1760 -1527 -2709 N ATOM 1982 N MET A1033 23.828 -51.830 24.474 1.00 53.57 N ANISOU 1982 N MET A1033 5172 4590 10591 10 -1080 -1470 N ATOM 1983 CA MET A1033 22.651 -51.868 23.612 1.00 51.85 C ANISOU 1983 CA MET A1033 5246 4165 10290 147 -924 -1350 C ATOM 1984 C MET A1033 21.369 -51.988 24.426 1.00 49.83 C ANISOU 1984 C MET A1033 5069 4172 9692 323 -1023 -1596 C ATOM 1985 O MET A1033 20.341 -51.407 24.062 1.00 46.75 O ANISOU 1985 O MET A1033 4850 3640 9272 440 -1013 -1709 O ATOM 1986 CB MET A1033 22.752 -53.023 22.617 1.00 51.62 C ANISOU 1986 CB MET A1033 5298 4147 10169 195 -669 -929 C ATOM 1987 CG MET A1033 23.795 -52.827 21.541 1.00 56.88 C ANISOU 1987 CG MET A1033 5952 4491 11169 80 -516 -638 C ATOM 1988 SD MET A1033 24.005 -54.315 20.540 1.00 57.69 S ANISOU 1988 SD MET A1033 6161 4657 11100 164 -224 -161 S ATOM 1989 CE MET A1033 22.445 -54.351 19.669 1.00 55.93 C ANISOU 1989 CE MET A1033 6221 4343 10688 324 -130 -205 C ATOM 1990 N ARG A1034 21.401 -52.756 25.517 1.00 51.92 N ANISOU 1990 N ARG A1034 5214 4847 9668 391 -1088 -1663 N ATOM 1991 CA ARG A1034 20.188 -52.937 26.307 1.00 52.56 C ANISOU 1991 CA ARG A1034 5367 5179 9425 557 -1124 -1872 C ATOM 1992 C ARG A1034 19.771 -51.633 26.981 1.00 55.51 C ANISOU 1992 C ARG A1034 5757 5474 9859 599 -1368 -2272 C ATOM 1993 O ARG A1034 18.581 -51.301 27.017 1.00 54.28 O ANISOU 1993 O ARG A1034 5725 5332 9567 742 -1367 -2421 O ATOM 1994 CB ARG A1034 20.389 -54.039 27.346 1.00 52.55 C ANISOU 1994 CB ARG A1034 5288 5591 9087 671 -1072 -1814 C ATOM 1995 CG ARG A1034 19.092 -54.476 28.011 1.00 53.09 C ANISOU 1995 CG ARG A1034 5458 5893 8822 824 -980 -1947 C ATOM 1996 CD ARG A1034 19.336 -55.402 29.189 1.00 56.88 C ANISOU 1996 CD ARG A1034 5915 6741 8954 1004 -896 -1898 C ATOM 1997 NE ARG A1034 18.105 -56.077 29.583 1.00 60.91 N ANISOU 1997 NE ARG A1034 6557 7405 9182 1096 -653 -1931 N ATOM 1998 CZ ARG A1034 17.198 -55.566 30.409 1.00 67.87 C ANISOU 1998 CZ ARG A1034 7437 8442 9908 1223 -763 -2225 C ATOM 1999 NH1 ARG A1034 17.377 -54.362 30.942 1.00 72.52 N ANISOU 1999 NH1 ARG A1034 7944 9029 10581 1287 -1124 -2522 N ATOM 2000 NH2 ARG A1034 16.105 -56.259 30.700 1.00 69.96 N ANISOU 2000 NH2 ARG A1034 7789 8851 9941 1269 -480 -2238 N ATOM 2001 N ALA A1035 20.738 -50.882 27.513 1.00 57.48 N ANISOU 2001 N ALA A1035 5872 5659 10307 475 -1566 -2477 N ATOM 2002 CA ALA A1035 20.432 -49.583 28.103 1.00 60.09 C ANISOU 2002 CA ALA A1035 6268 5833 10729 477 -1763 -2888 C ATOM 2003 C ALA A1035 19.852 -48.628 27.065 1.00 59.08 C ANISOU 2003 C ALA A1035 6399 5215 10833 493 -1639 -2864 C ATOM 2004 O ALA A1035 18.878 -47.916 27.339 1.00 59.62 O ANISOU 2004 O ALA A1035 6643 5219 10791 676 -1687 -3085 O ATOM 2005 CB ALA A1035 21.692 -48.995 28.743 1.00 57.33 C ANISOU 2005 CB ALA A1035 5694 5497 10593 257 -1967 -3158 C ATOM 2006 N ALA A1036 20.431 -48.607 25.860 1.00 58.30 N ANISOU 2006 N ALA A1036 6346 4785 11020 366 -1453 -2574 N ATOM 2007 CA ALA A1036 19.920 -47.734 24.807 1.00 57.21 C ANISOU 2007 CA ALA A1036 6494 4205 11038 473 -1282 -2485 C ATOM 2008 C ALA A1036 18.501 -48.121 24.400 1.00 59.54 C ANISOU 2008 C ALA A1036 6920 4704 11000 795 -1218 -2403 C ATOM 2009 O ALA A1036 17.644 -47.247 24.216 1.00 61.36 O ANISOU 2009 O ALA A1036 7360 4875 11079 1005 -1174 -2457 O ATOM 2010 CB ALA A1036 20.851 -47.772 23.598 1.00 53.35 C ANISOU 2010 CB ALA A1036 6024 3453 10794 311 -1046 -2100 C ATOM 2011 N ALA A1037 18.231 -49.423 24.261 1.00 55.63 N ANISOU 2011 N ALA A1037 6290 4567 10278 810 -1162 -2218 N ATOM 2012 CA ALA A1037 16.902 -49.866 23.847 1.00 56.26 C ANISOU 2012 CA ALA A1037 6416 4907 10055 1039 -1086 -2203 C ATOM 2013 C ALA A1037 15.837 -49.404 24.835 1.00 59.17 C ANISOU 2013 C ALA A1037 6788 5517 10176 1233 -1225 -2537 C ATOM 2014 O ALA A1037 14.794 -48.875 24.438 1.00 60.57 O ANISOU 2014 O ALA A1037 7065 5736 10211 1506 -1208 -2626 O ATOM 2015 CB ALA A1037 16.876 -51.386 23.693 1.00 52.96 C ANISOU 2015 CB ALA A1037 5862 4803 9456 926 -950 -2006 C ATOM 2016 N LEU A1038 16.083 -49.598 26.133 1.00 62.18 N ANISOU 2016 N LEU A1038 7058 6103 10466 1152 -1360 -2720 N ATOM 2017 CA LEU A1038 15.166 -49.079 27.144 1.00 67.32 C ANISOU 2017 CA LEU A1038 7734 6956 10887 1356 -1491 -3038 C ATOM 2018 C LEU A1038 15.075 -47.562 27.077 1.00 73.91 C ANISOU 2018 C LEU A1038 8793 7411 11879 1498 -1576 -3236 C ATOM 2019 O LEU A1038 14.004 -46.984 27.295 1.00 76.97 O ANISOU 2019 O LEU A1038 9278 7940 12026 1754 -1585 -3348 O ATOM 2020 CB LEU A1038 15.616 -49.519 28.536 1.00 69.04 C ANISOU 2020 CB LEU A1038 7821 7443 10967 1286 -1618 -3184 C ATOM 2021 CG LEU A1038 15.691 -51.030 28.740 1.00 68.97 C ANISOU 2021 CG LEU A1038 7675 7771 10758 1212 -1455 -2969 C ATOM 2022 CD1 LEU A1038 16.137 -51.354 30.158 1.00 69.44 C ANISOU 2022 CD1 LEU A1038 7652 8113 10619 1268 -1567 -3100 C ATOM 2023 CD2 LEU A1038 14.340 -51.671 28.422 1.00 69.38 C ANISOU 2023 CD2 LEU A1038 7714 8076 10573 1309 -1256 -2946 C ATOM 2024 N ASP A1039 16.195 -46.901 26.781 1.00 78.37 N ANISOU 2024 N ASP A1039 9436 7574 12766 1277 -1562 -3167 N ATOM 2025 CA ASP A1039 16.201 -45.447 26.666 1.00 83.07 C ANISOU 2025 CA ASP A1039 10300 7817 13447 1312 -1500 -3218 C ATOM 2026 C ASP A1039 15.410 -44.990 25.444 1.00 83.94 C ANISOU 2026 C ASP A1039 10653 7794 13448 1585 -1277 -2966 C ATOM 2027 O ASP A1039 14.720 -43.967 25.491 1.00 85.81 O ANISOU 2027 O ASP A1039 11146 7915 13542 1831 -1206 -3033 O ATOM 2028 CB ASP A1039 17.645 -44.951 26.606 1.00 87.64 C ANISOU 2028 CB ASP A1039 10866 8028 14406 948 -1468 -3220 C ATOM 2029 CG ASP A1039 17.761 -43.459 26.788 1.00 96.60 C ANISOU 2029 CG ASP A1039 12293 8775 15637 907 -1368 -3373 C ATOM 2030 OD1 ASP A1039 17.531 -42.974 27.916 1.00 99.55 O ANISOU 2030 OD1 ASP A1039 12682 9250 15892 930 -1530 -3708 O ATOM 2031 OD2 ASP A1039 18.103 -42.771 25.804 1.00101.59 O ANISOU 2031 OD2 ASP A1039 13175 8985 16439 859 -1093 -3155 O ATOM 2032 N ALA A1040 15.491 -45.741 24.342 1.00 83.38 N ANISOU 2032 N ALA A1040 10519 7759 13403 1588 -1151 -2674 N ATOM 2033 CA ALA A1040 14.686 -45.423 23.169 1.00 84.45 C ANISOU 2033 CA ALA A1040 10846 7890 13353 1915 -965 -2457 C ATOM 2034 C ALA A1040 13.221 -45.793 23.362 1.00 86.94 C ANISOU 2034 C ALA A1040 11034 8716 13284 2240 -1058 -2607 C ATOM 2035 O ALA A1040 12.350 -45.190 22.723 1.00 89.91 O ANISOU 2035 O ALA A1040 11563 9168 13431 2599 -954 -2535 O ATOM 2036 CB ALA A1040 15.245 -46.130 21.933 1.00 79.47 C ANISOU 2036 CB ALA A1040 10179 7190 12826 1823 -811 -2121 C ATOM 2037 N GLN A1041 12.933 -46.765 24.232 1.00 86.75 N ANISOU 2037 N GLN A1041 10725 9073 13162 2133 -1213 -2811 N ATOM 2038 CA GLN A1041 11.548 -47.145 24.490 1.00 87.53 C ANISOU 2038 CA GLN A1041 10656 9705 12898 2380 -1257 -2984 C ATOM 2039 C GLN A1041 10.786 -46.034 25.199 1.00 91.62 C ANISOU 2039 C GLN A1041 11328 10273 13212 2651 -1321 -3150 C ATOM 2040 O GLN A1041 9.582 -45.870 24.973 1.00 94.29 O ANISOU 2040 O GLN A1041 11613 10981 13233 2962 -1306 -3196 O ATOM 2041 CB GLN A1041 11.506 -48.432 25.311 1.00 85.74 C ANISOU 2041 CB GLN A1041 10140 9814 12625 2176 -1298 -3143 C ATOM 2042 CG GLN A1041 10.143 -49.094 25.363 1.00 87.88 C ANISOU 2042 CG GLN A1041 10166 10666 12560 2315 -1243 -3301 C ATOM 2043 CD GLN A1041 10.207 -50.500 25.923 1.00 88.43 C ANISOU 2043 CD GLN A1041 10023 11013 12563 1976 -1121 -3283 C ATOM 2044 OE1 GLN A1041 11.109 -50.835 26.690 1.00 88.24 O ANISOU 2044 OE1 GLN A1041 10045 10833 12651 1770 -1137 -3213 O ATOM 2045 NE2 GLN A1041 9.252 -51.338 25.533 1.00 89.58 N ANISOU 2045 NE2 GLN A1041 9939 11587 12510 1927 -970 -3358 N ATOM 2046 N LYS A1042 11.462 -45.267 26.049 1.00 91.47 N ANISOU 2046 N LYS A1042 11482 9918 13356 2535 -1389 -3255 N ATOM 2047 CA LYS A1042 10.837 -44.152 26.747 1.00 92.76 C ANISOU 2047 CA LYS A1042 11849 10049 13348 2781 -1419 -3412 C ATOM 2048 C LYS A1042 10.465 -43.035 25.775 1.00 94.16 C ANISOU 2048 C LYS A1042 12354 9954 13470 3092 -1214 -3228 C ATOM 2049 O LYS A1042 9.343 -42.984 25.271 1.00 94.28 O ANISOU 2049 O LYS A1042 12330 10320 13174 3449 -1170 -3170 O ATOM 2050 CB LYS A1042 11.770 -43.612 27.832 1.00 94.46 C ANISOU 2050 CB LYS A1042 12170 9954 13768 2534 -1526 -3608 C ATOM 2051 CG LYS A1042 12.189 -44.640 28.870 1.00 92.63 C ANISOU 2051 CG LYS A1042 11642 10019 13533 2307 -1713 -3777 C ATOM 2052 CD LYS A1042 13.149 -44.026 29.883 1.00 95.80 C ANISOU 2052 CD LYS A1042 12113 10187 14098 2092 -1849 -4004 C ATOM 2053 CE LYS A1042 13.558 -45.028 30.951 1.00 94.86 C ANISOU 2053 CE LYS A1042 11718 10432 13894 1969 -2029 -4160 C ATOM 2054 NZ LYS A1042 14.462 -44.412 31.964 1.00 98.65 N ANISOU 2054 NZ LYS A1042 12212 10799 14471 1799 -2200 -4429 N ATOM 2055 N MET A1058 1.294 -47.990 18.618 1.00101.05 N ATOM 2056 CA MET A1058 1.944 -48.164 19.913 1.00103.45 C ATOM 2057 C MET A1058 1.984 -49.634 20.328 1.00 91.81 C ATOM 2058 O MET A1058 2.878 -50.057 21.062 1.00 91.59 O ATOM 2059 CB MET A1058 1.232 -47.336 20.986 1.00117.38 C ATOM 2060 CG MET A1058 1.437 -45.837 20.850 1.00130.14 C ATOM 2061 SD MET A1058 3.161 -45.351 21.064 1.00142.81 S ATOM 2062 CE MET A1058 3.470 -45.906 22.739 1.00156.39 C ATOM 2063 N LYS A1059 1.006 -50.411 19.859 1.00145.91 N ANISOU 2063 N LYS A1059 14893 15623 24924 967 -815 967 N ATOM 2064 CA LYS A1059 1.006 -51.838 20.157 1.00131.91 C ANISOU 2064 CA LYS A1059 13021 14059 23038 776 -544 1356 C ATOM 2065 C LYS A1059 2.073 -52.564 19.347 1.00117.95 C ANISOU 2065 C LYS A1059 11804 12070 20943 522 -765 1551 C ATOM 2066 O LYS A1059 2.773 -53.439 19.872 1.00115.16 O ANISOU 2066 O LYS A1059 11567 11987 20202 437 -487 1733 O ATOM 2067 CB LYS A1059 -0.381 -52.423 19.894 1.00130.84 C ANISOU 2067 CB LYS A1059 12399 13779 23535 694 -626 1576 C ATOM 2068 CG LYS A1059 -1.467 -51.733 20.700 1.00132.36 C ANISOU 2068 CG LYS A1059 11984 14216 24090 953 -365 1361 C ATOM 2069 CD LYS A1059 -2.862 -52.137 20.259 1.00133.51 C ANISOU 2069 CD LYS A1059 11748 14137 24844 829 -527 1496 C ATOM 2070 CE LYS A1059 -3.907 -51.329 21.005 1.00137.22 C ANISOU 2070 CE LYS A1059 11773 14857 25506 1061 -272 1193 C ATOM 2071 NZ LYS A1059 -5.284 -51.642 20.551 1.00141.55 N ANISOU 2071 NZ LYS A1059 12003 15157 26624 936 -448 1271 N ATOM 2072 N ASP A1060 2.216 -52.213 18.066 1.00109.16 N ANISOU 2072 N ASP A1060 11047 10463 19967 412 -1268 1508 N ATOM 2073 CA ASP A1060 3.313 -52.742 17.265 1.00100.09 C ANISOU 2073 CA ASP A1060 10451 9212 18367 180 -1427 1590 C ATOM 2074 C ASP A1060 4.635 -52.074 17.618 1.00 93.64 C ANISOU 2074 C ASP A1060 9964 8482 17132 271 -1284 1388 C ATOM 2075 O ASP A1060 5.697 -52.661 17.387 1.00 90.94 O ANISOU 2075 O ASP A1060 9969 8258 16326 119 -1226 1435 O ATOM 2076 CB ASP A1060 3.007 -52.562 15.779 1.00100.40 C ANISOU 2076 CB ASP A1060 10778 9159 18212 -11 -1864 1461 C ATOM 2077 CG ASP A1060 1.561 -52.871 15.444 1.00105.45 C ANISOU 2077 CG ASP A1060 11033 9646 19387 -51 -2087 1558 C ATOM 2078 OD1 ASP A1060 0.877 -51.985 14.887 1.00108.62 O ANISOU 2078 OD1 ASP A1060 11402 9882 19988 -14 -2381 1369 O ATOM 2079 OD2 ASP A1060 1.107 -53.994 15.744 1.00105.98 O ANISOU 2079 OD2 ASP A1060 10821 9748 19697 -127 -1981 1829 O ATOM 2080 N PHE A1061 4.587 -50.858 18.165 1.00 89.64 N ANISOU 2080 N PHE A1061 9341 8079 16639 489 -1210 1074 N ATOM 2081 CA PHE A1061 5.786 -50.218 18.697 1.00 82.32 C ANISOU 2081 CA PHE A1061 8648 7347 15281 577 -1037 828 C ATOM 2082 C PHE A1061 6.290 -50.957 19.927 1.00 75.05 C ANISOU 2082 C PHE A1061 7592 6934 13989 652 -581 886 C ATOM 2083 O PHE A1061 7.488 -51.242 20.047 1.00 69.71 O ANISOU 2083 O PHE A1061 7207 6361 12918 585 -492 864 O ATOM 2084 CB PHE A1061 5.481 -48.750 19.021 1.00 86.22 C ANISOU 2084 CB PHE A1061 9018 7800 15943 817 -1119 467 C ATOM 2085 CG PHE A1061 6.363 -48.149 20.097 1.00 86.78 C ANISOU 2085 CG PHE A1061 9109 8214 15648 1012 -843 180 C ATOM 2086 CD1 PHE A1061 7.511 -47.456 19.762 1.00 84.79 C ANISOU 2086 CD1 PHE A1061 9238 7798 15180 951 -983 0 C ATOM 2087 CD2 PHE A1061 6.019 -48.245 21.440 1.00 89.28 C ANISOU 2087 CD2 PHE A1061 9064 9009 15851 1260 -451 83 C ATOM 2088 CE1 PHE A1061 8.309 -46.892 20.744 1.00 85.16 C ANISOU 2088 CE1 PHE A1061 9288 8123 14946 1139 -787 -287 C ATOM 2089 CE2 PHE A1061 6.819 -47.692 22.421 1.00 88.89 C ANISOU 2089 CE2 PHE A1061 9068 9254 15451 1468 -251 -204 C ATOM 2090 CZ PHE A1061 7.962 -47.012 22.073 1.00 86.49 C ANISOU 2090 CZ PHE A1061 9127 8753 14981 1412 -446 -401 C ATOM 2091 N ARG A1062 5.385 -51.267 20.859 1.00 76.67 N ANISOU 2091 N ARG A1062 7356 7456 14318 793 -287 957 N ATOM 2092 CA ARG A1062 5.778 -51.934 22.095 1.00 75.60 C ANISOU 2092 CA ARG A1062 7121 7810 13795 880 151 1034 C ATOM 2093 C ARG A1062 6.229 -53.365 21.832 1.00 65.18 C ANISOU 2093 C ARG A1062 5977 6479 12311 634 168 1397 C ATOM 2094 O ARG A1062 7.174 -53.847 22.466 1.00 62.66 O ANISOU 2094 O ARG A1062 5836 6411 11562 649 359 1413 O ATOM 2095 CB ARG A1062 4.624 -51.895 23.100 1.00 87.74 C ANISOU 2095 CB ARG A1062 8148 9689 15502 1076 496 1046 C ATOM 2096 CG ARG A1062 4.810 -52.789 24.321 1.00 95.97 C ANISOU 2096 CG ARG A1062 9092 11221 16152 1124 964 1238 C ATOM 2097 CD ARG A1062 4.043 -52.262 25.530 1.00105.85 C ANISOU 2097 CD ARG A1062 9943 12904 17373 1424 1375 1073 C ATOM 2098 NE ARG A1062 4.611 -51.011 26.033 1.00109.52 N ANISOU 2098 NE ARG A1062 10532 13485 17594 1723 1363 598 N ATOM 2099 CZ ARG A1062 5.665 -50.939 26.844 1.00109.73 C ANISOU 2099 CZ ARG A1062 10830 13784 17080 1864 1510 443 C ATOM 2100 NH1 ARG A1062 6.274 -52.046 27.248 1.00108.33 N ANISOU 2100 NH1 ARG A1062 10840 13793 16529 1738 1681 729 N ATOM 2101 NH2 ARG A1062 6.113 -49.757 27.248 1.00110.78 N ANISOU 2101 NH2 ARG A1062 11051 13971 17070 2139 1441 -9 N ATOM 2102 N HIS A1063 5.578 -54.055 20.890 1.00 60.64 N ANISOU 2102 N HIS A1063 5363 5586 12090 422 -78 1668 N ATOM 2103 CA HIS A1063 6.015 -55.403 20.544 1.00 56.43 C ANISOU 2103 CA HIS A1063 5020 4985 11437 198 -133 1985 C ATOM 2104 C HIS A1063 7.425 -55.388 19.974 1.00 51.95 C ANISOU 2104 C HIS A1063 4941 4287 10511 117 -295 1853 C ATOM 2105 O HIS A1063 8.228 -56.280 20.268 1.00 50.47 O ANISOU 2105 O HIS A1063 4917 4240 10021 52 -195 1970 O ATOM 2106 CB HIS A1063 5.044 -56.050 19.553 1.00 59.06 C ANISOU 2106 CB HIS A1063 5240 4946 12255 8 -444 2250 C ATOM 2107 CG HIS A1063 5.248 -57.527 19.380 1.00 60.98 C ANISOU 2107 CG HIS A1063 5577 5141 12450 -195 -485 2596 C ATOM 2108 ND1 HIS A1063 5.239 -58.410 20.440 1.00 62.73 N ANISOU 2108 ND1 HIS A1063 5620 5707 12509 -204 -139 2832 N ATOM 2109 CD2 HIS A1063 5.462 -58.277 18.272 1.00 60.30 C ANISOU 2109 CD2 HIS A1063 5763 4924 12223 -360 -827 2577 C ATOM 2110 CE1 HIS A1063 5.440 -59.638 19.993 1.00 61.89 C ANISOU 2110 CE1 HIS A1063 5660 5425 12431 -400 -318 3110 C ATOM 2111 NE2 HIS A1063 5.579 -59.585 18.681 1.00 60.57 N ANISOU 2111 NE2 HIS A1063 5760 5117 12136 -448 -727 2818 N ATOM 2112 N GLY A1064 7.746 -54.373 19.166 1.00 48.06 N ANISOU 2112 N GLY A1064 4678 3519 10065 118 -543 1611 N ATOM 2113 CA GLY A1064 9.076 -54.283 18.585 1.00 45.03 C ANISOU 2113 CA GLY A1064 4723 3015 9372 22 -652 1482 C ATOM 2114 C GLY A1064 10.162 -54.116 19.631 1.00 46.07 C ANISOU 2114 C GLY A1064 4901 3502 9102 155 -372 1286 C ATOM 2115 O GLY A1064 11.185 -54.808 19.601 1.00 44.44 O ANISOU 2115 O GLY A1064 4909 3352 8623 75 -341 1310 O ATOM 2116 N PHE A1065 9.953 -53.200 20.580 1.00 48.63 N ANISOU 2116 N PHE A1065 5021 4060 9396 384 -192 1061 N ATOM 2117 CA PHE A1065 10.940 -53.028 21.642 1.00 49.25 C ANISOU 2117 CA PHE A1065 5148 4469 9094 546 32 851 C ATOM 2118 C PHE A1065 10.949 -54.210 22.604 1.00 50.48 C ANISOU 2118 C PHE A1065 5203 4967 9011 585 286 1077 C ATOM 2119 O PHE A1065 12.007 -54.541 23.156 1.00 50.36 O ANISOU 2119 O PHE A1065 5351 5128 8656 635 367 991 O ATOM 2120 CB PHE A1065 10.694 -51.720 22.389 1.00 52.94 C ANISOU 2120 CB PHE A1065 5453 5078 9584 809 116 521 C ATOM 2121 CG PHE A1065 11.326 -50.531 21.726 1.00 53.62 C ANISOU 2121 CG PHE A1065 5749 4874 9749 783 -121 232 C ATOM 2122 CD1 PHE A1065 12.694 -50.330 21.805 1.00 51.34 C ANISOU 2122 CD1 PHE A1065 5697 4598 9212 757 -131 38 C ATOM 2123 CD2 PHE A1065 10.558 -49.627 21.008 1.00 55.88 C ANISOU 2123 CD2 PHE A1065 5996 4850 10387 770 -352 166 C ATOM 2124 CE1 PHE A1065 13.282 -49.247 21.188 1.00 53.99 C ANISOU 2124 CE1 PHE A1065 6212 4652 9650 693 -327 -192 C ATOM 2125 CE2 PHE A1065 11.144 -48.538 20.387 1.00 56.29 C ANISOU 2125 CE2 PHE A1065 6275 4603 10509 718 -579 -56 C ATOM 2126 CZ PHE A1065 12.503 -48.346 20.476 1.00 55.35 C ANISOU 2126 CZ PHE A1065 6378 4508 10143 665 -548 -222 C ATOM 2127 N ASP A1066 9.794 -54.853 22.816 1.00 50.40 N ANISOU 2127 N ASP A1066 4923 5032 9194 557 398 1371 N ATOM 2128 CA ASP A1066 9.755 -56.084 23.601 1.00 52.64 C ANISOU 2128 CA ASP A1066 5144 5579 9279 533 616 1668 C ATOM 2129 C ASP A1066 10.630 -57.155 22.968 1.00 51.00 C ANISOU 2129 C ASP A1066 5229 5190 8960 331 422 1828 C ATOM 2130 O ASP A1066 11.394 -57.835 23.661 1.00 50.80 O ANISOU 2130 O ASP A1066 5332 5366 8602 370 523 1873 O ATOM 2131 CB ASP A1066 8.317 -56.601 23.737 1.00 56.70 C ANISOU 2131 CB ASP A1066 5292 6131 10120 473 747 1993 C ATOM 2132 CG ASP A1066 7.521 -55.888 24.827 1.00 65.21 C ANISOU 2132 CG ASP A1066 6032 7563 11180 720 1094 1876 C ATOM 2133 OD1 ASP A1066 8.129 -55.251 25.717 1.00 68.61 O ANISOU 2133 OD1 ASP A1066 6549 8279 11241 958 1265 1595 O ATOM 2134 OD2 ASP A1066 6.273 -55.981 24.799 1.00 69.98 O ANISOU 2134 OD2 ASP A1066 6270 8162 12156 687 1191 2050 O ATOM 2135 N ILE A1067 10.517 -57.328 21.648 1.00 45.45 N ANISOU 2135 N ILE A1067 4646 4097 8525 132 121 1900 N ATOM 2136 CA ILE A1067 11.360 -58.292 20.944 1.00 44.22 C ANISOU 2136 CA ILE A1067 4775 3756 8269 -35 -78 1995 C ATOM 2137 C ILE A1067 12.829 -57.916 21.092 1.00 41.12 C ANISOU 2137 C ILE A1067 4635 3447 7540 37 -63 1681 C ATOM 2138 O ILE A1067 13.672 -58.754 21.438 1.00 41.40 O ANISOU 2138 O ILE A1067 4803 3586 7342 35 -51 1711 O ATOM 2139 CB ILE A1067 10.955 -58.388 19.462 1.00 43.56 C ANISOU 2139 CB ILE A1067 4812 3243 8495 -224 -409 2077 C ATOM 2140 CG1 ILE A1067 9.524 -58.902 19.314 1.00 46.40 C ANISOU 2140 CG1 ILE A1067 4892 3552 9187 -296 -472 2336 C ATOM 2141 CG2 ILE A1067 11.897 -59.321 18.718 1.00 41.97 C ANISOU 2141 CG2 ILE A1067 4916 3065 7966 -334 -566 1961 C ATOM 2142 CD1 ILE A1067 8.953 -58.716 17.909 1.00 46.77 C ANISOU 2142 CD1 ILE A1067 5034 3483 9254 -383 -782 2132 C ATOM 2143 N LEU A1068 13.151 -56.641 20.853 1.00 40.45 N ANISOU 2143 N LEU A1068 4606 3300 7465 102 -83 1370 N ATOM 2144 CA LEU A1068 14.543 -56.199 20.841 1.00 38.80 C ANISOU 2144 CA LEU A1068 4604 3110 7028 132 -92 1062 C ATOM 2145 C LEU A1068 15.221 -56.461 22.179 1.00 39.57 C ANISOU 2145 C LEU A1068 4663 3558 6812 322 86 956 C ATOM 2146 O LEU A1068 16.322 -57.020 22.234 1.00 45.57 O ANISOU 2146 O LEU A1068 5578 4346 7390 306 42 871 O ATOM 2147 CB LEU A1068 14.614 -54.714 20.495 1.00 39.77 C ANISOU 2147 CB LEU A1068 4751 3098 7262 166 -142 781 C ATOM 2148 CG LEU A1068 16.009 -54.213 20.126 1.00 37.89 C ANISOU 2148 CG LEU A1068 4725 2773 6900 110 -184 497 C ATOM 2149 CD1 LEU A1068 16.364 -54.779 18.780 1.00 36.77 C ANISOU 2149 CD1 LEU A1068 4820 2349 6802 -133 -331 614 C ATOM 2150 CD2 LEU A1068 16.067 -52.690 20.100 1.00 37.93 C ANISOU 2150 CD2 LEU A1068 4719 2677 7017 171 -218 224 C ATOM 2151 N VAL A1069 14.580 -56.059 23.276 1.00 41.84 N ANISOU 2151 N VAL A1069 4754 4117 7027 523 278 942 N ATOM 2152 CA VAL A1069 15.179 -56.273 24.589 1.00 43.13 C ANISOU 2152 CA VAL A1069 4933 4617 6836 733 429 841 C ATOM 2153 C VAL A1069 15.309 -57.763 24.877 1.00 43.40 C ANISOU 2153 C VAL A1069 5042 4729 6720 659 435 1157 C ATOM 2154 O VAL A1069 16.340 -58.223 25.381 1.00 43.13 O ANISOU 2154 O VAL A1069 5165 4795 6429 735 390 1054 O ATOM 2155 CB VAL A1069 14.362 -55.550 25.677 1.00 46.13 C ANISOU 2155 CB VAL A1069 5107 5290 7132 980 659 766 C ATOM 2156 CG1 VAL A1069 14.942 -55.833 27.062 1.00 48.01 C ANISOU 2156 CG1 VAL A1069 5422 5883 6937 1217 804 683 C ATOM 2157 CG2 VAL A1069 14.337 -54.049 25.401 1.00 47.79 C ANISOU 2157 CG2 VAL A1069 5264 5381 7512 1074 586 410 C ATOM 2158 N GLY A1070 14.268 -58.541 24.566 1.00 44.26 N ANISOU 2158 N GLY A1070 5031 4764 7020 512 456 1541 N ATOM 2159 CA GLY A1070 14.344 -59.976 24.789 1.00 44.84 C ANISOU 2159 CA GLY A1070 5180 4857 6999 417 421 1871 C ATOM 2160 C GLY A1070 15.476 -60.620 24.010 1.00 42.27 C ANISOU 2160 C GLY A1070 5097 4305 6658 304 156 1780 C ATOM 2161 O GLY A1070 16.182 -61.496 24.524 1.00 42.62 O ANISOU 2161 O GLY A1070 5278 4428 6489 344 97 1833 O ATOM 2162 N GLN A1071 15.665 -60.194 22.761 1.00 40.05 N ANISOU 2162 N GLN A1071 4884 3739 6594 172 -9 1635 N ATOM 2163 CA GLN A1071 16.742 -60.746 21.946 1.00 39.04 C ANISOU 2163 CA GLN A1071 4971 3416 6447 73 -215 1513 C ATOM 2164 C GLN A1071 18.107 -60.328 22.472 1.00 39.99 C ANISOU 2164 C GLN A1071 5184 3677 6332 217 -190 1141 C ATOM 2165 O GLN A1071 19.065 -61.109 22.410 1.00 42.04 O ANISOU 2165 O GLN A1071 5570 3905 6500 216 -317 1065 O ATOM 2166 CB GLN A1071 16.571 -60.310 20.491 1.00 36.62 C ANISOU 2166 CB GLN A1071 4745 2793 6375 -98 -356 1455 C ATOM 2167 CG GLN A1071 15.383 -60.953 19.793 1.00 39.64 C ANISOU 2167 CG GLN A1071 5077 2960 7025 -247 -494 1799 C ATOM 2168 CD GLN A1071 15.178 -60.410 18.400 1.00 38.72 C ANISOU 2168 CD GLN A1071 5076 2714 6921 -353 -609 1592 C ATOM 2169 OE1 GLN A1071 15.298 -59.206 18.176 1.00 38.34 O ANISOU 2169 OE1 GLN A1071 5054 2585 6929 -341 -567 1428 O ATOM 2170 NE2 GLN A1071 14.865 -61.292 17.454 1.00 37.52 N ANISOU 2170 NE2 GLN A1071 5001 2578 6678 -427 -743 1575 N ATOM 2171 N ILE A1072 18.220 -59.102 22.992 1.00 38.85 N ANISOU 2171 N ILE A1072 4965 3669 6128 354 -61 882 N ATOM 2172 CA ILE A1072 19.461 -58.694 23.638 1.00 37.86 C ANISOU 2172 CA ILE A1072 4895 3675 5815 513 -65 523 C ATOM 2173 C ILE A1072 19.706 -59.544 24.879 1.00 39.63 C ANISOU 2173 C ILE A1072 5161 4140 5757 687 -58 615 C ATOM 2174 O ILE A1072 20.824 -60.025 25.110 1.00 39.49 O ANISOU 2174 O ILE A1072 5248 4129 5626 751 -191 441 O ATOM 2175 CB ILE A1072 19.429 -57.183 23.954 1.00 41.67 C ANISOU 2175 CB ILE A1072 5288 4220 6325 632 28 231 C ATOM 2176 CG1 ILE A1072 19.437 -56.374 22.652 1.00 39.02 C ANISOU 2176 CG1 ILE A1072 4979 3594 6251 435 -28 132 C ATOM 2177 CG2 ILE A1072 20.625 -56.782 24.807 1.00 39.02 C ANISOU 2177 CG2 ILE A1072 4985 4027 5814 828 -8 -140 C ATOM 2178 CD1 ILE A1072 19.033 -54.906 22.808 1.00 38.55 C ANISOU 2178 CD1 ILE A1072 4827 3522 6300 518 21 -64 C ATOM 2179 N ASP A1073 18.657 -59.785 25.674 1.00 41.72 N ANISOU 2179 N ASP A1073 5347 4595 5911 760 95 903 N ATOM 2180 CA ASP A1073 18.799 -60.662 26.835 1.00 45.07 C ANISOU 2180 CA ASP A1073 5864 5237 6025 900 115 1067 C ATOM 2181 C ASP A1073 19.247 -62.063 26.427 1.00 45.25 C ANISOU 2181 C ASP A1073 6022 5089 6083 767 -102 1271 C ATOM 2182 O ASP A1073 20.074 -62.682 27.114 1.00 44.41 O ANISOU 2182 O ASP A1073 6066 5055 5752 892 -232 1210 O ATOM 2183 CB ASP A1073 17.484 -60.744 27.615 1.00 48.85 C ANISOU 2183 CB ASP A1073 6218 5940 6402 947 375 1406 C ATOM 2184 CG ASP A1073 17.116 -59.435 28.296 1.00 53.31 C ANISOU 2184 CG ASP A1073 6664 6734 6856 1162 585 1158 C ATOM 2185 OD1 ASP A1073 18.019 -58.597 28.542 1.00 53.13 O ANISOU 2185 OD1 ASP A1073 6710 6742 6735 1328 500 735 O ATOM 2186 OD2 ASP A1073 15.914 -59.249 28.590 1.00 55.64 O ANISOU 2186 OD2 ASP A1073 6778 7170 7193 1171 825 1372 O ATOM 2187 N ASP A1074 18.682 -62.596 25.337 1.00 42.43 N ANISOU 2187 N ASP A1074 5625 4487 6011 534 -180 1504 N ATOM 2188 CA ASP A1074 19.088 -63.916 24.858 1.00 43.44 C ANISOU 2188 CA ASP A1074 5882 4417 6207 420 -426 1663 C ATOM 2189 C ASP A1074 20.588 -63.950 24.606 1.00 40.57 C ANISOU 2189 C ASP A1074 5640 3982 5794 497 -613 1260 C ATOM 2190 O ASP A1074 21.299 -64.835 25.101 1.00 41.34 O ANISOU 2190 O ASP A1074 5862 4087 5759 584 -792 1254 O ATOM 2191 CB ASP A1074 18.327 -64.284 23.572 1.00 44.35 C ANISOU 2191 CB ASP A1074 5949 4247 6656 183 -523 1877 C ATOM 2192 CG ASP A1074 16.847 -64.595 23.810 1.00 45.49 C ANISOU 2192 CG ASP A1074 5936 4412 6935 82 -402 2324 C ATOM 2193 OD1 ASP A1074 16.430 -64.698 24.980 1.00 45.66 O ANISOU 2193 OD1 ASP A1074 5899 4685 6763 177 -211 2516 O ATOM 2194 OD2 ASP A1074 16.101 -64.748 22.814 1.00 41.80 O ANISOU 2194 OD2 ASP A1074 5402 3705 6775 -92 -499 2481 O ATOM 2195 N ALA A1075 21.087 -62.967 23.854 1.00 40.10 N ANISOU 2195 N ALA A1075 5535 3843 5857 463 -574 919 N ATOM 2196 CA ALA A1075 22.503 -62.920 23.507 1.00 41.71 C ANISOU 2196 CA ALA A1075 5793 3976 6079 504 -701 521 C ATOM 2197 C ALA A1075 23.369 -62.634 24.728 1.00 45.38 C ANISOU 2197 C ALA A1075 6268 4643 6330 747 -730 253 C ATOM 2198 O ALA A1075 24.481 -63.165 24.842 1.00 48.27 O ANISOU 2198 O ALA A1075 6687 4970 6683 830 -918 25 O ATOM 2199 CB ALA A1075 22.734 -61.870 22.415 1.00 37.31 C ANISOU 2199 CB ALA A1075 5185 3285 5705 373 -606 277 C ATOM 2200 N ALEU A1076 22.875 -61.815 25.658 0.43 45.38 N ANISOU 2200 N ALEU A1076 6221 4853 6169 886 -570 251 N ATOM 2201 N BLEU A1076 22.882 -61.799 25.647 0.57 45.31 N ANISOU 2201 N BLEU A1076 6210 4842 6162 885 -570 246 N ATOM 2202 CA ALEU A1076 23.644 -61.511 26.860 0.43 47.31 C ANISOU 2202 CA ALEU A1076 6513 5283 6178 1149 -633 -17 C ATOM 2203 CA BLEU A1076 23.636 -61.514 26.864 0.57 47.33 C ANISOU 2203 CA BLEU A1076 6516 5287 6180 1149 -632 -14 C ATOM 2204 C ALEU A1076 23.800 -62.743 27.745 0.43 49.31 C ANISOU 2204 C ALEU A1076 6937 5614 6184 1270 -799 192 C ATOM 2205 C BLEU A1076 23.815 -62.767 27.709 0.57 49.26 C ANISOU 2205 C BLEU A1076 6931 5600 6187 1264 -804 192 C ATOM 2206 O ALEU A1076 24.841 -62.926 28.388 0.43 50.00 O ANISOU 2206 O ALEU A1076 7114 5735 6149 1458 -1005 -73 O ATOM 2207 O BLEU A1076 24.884 -62.986 28.292 0.57 49.85 O ANISOU 2207 O BLEU A1076 7093 5694 6155 1442 -1018 -75 O ATOM 2208 CB ALEU A1076 22.978 -60.371 27.631 0.43 48.58 C ANISOU 2208 CB ALEU A1076 6607 5654 6196 1293 -428 -69 C ATOM 2209 CB BLEU A1076 22.934 -60.424 27.673 0.57 48.70 C ANISOU 2209 CB BLEU A1076 6628 5678 6199 1296 -426 -46 C ATOM 2210 CG ALEU A1076 23.711 -59.843 28.865 0.43 50.20 C ANISOU 2210 CG ALEU A1076 6879 6049 6147 1598 -508 -400 C ATOM 2211 CG BLEU A1076 23.360 -58.988 27.384 0.57 47.57 C ANISOU 2211 CG BLEU A1076 6364 5490 6219 1323 -381 -453 C ATOM 2212 CD1ALEU A1076 25.123 -59.410 28.503 0.43 48.04 C ANISOU 2212 CD1ALEU A1076 6552 5624 6078 1619 -705 -876 C ATOM 2213 CD1BLEU A1076 22.378 -58.016 28.006 0.57 49.58 C ANISOU 2213 CD1BLEU A1076 6546 5925 6366 1450 -183 -426 C ATOM 2214 CD2ALEU A1076 22.935 -58.691 29.486 0.43 51.66 C ANISOU 2214 CD2ALEU A1076 6990 6425 6212 1745 -300 -465 C ATOM 2215 CD2BLEU A1076 24.764 -58.746 27.918 0.57 47.54 C ANISOU 2215 CD2BLEU A1076 6389 5496 6178 1502 -581 -893 C ATOM 2216 N LYS A1077 22.777 -63.600 27.792 1.00 50.45 N ANISOU 2216 N LYS A1077 7130 5763 6276 1161 -738 673 N ATOM 2217 CA LYS A1077 22.892 -64.841 28.548 1.00 53.86 C ANISOU 2217 CA LYS A1077 7752 6217 6494 1232 -915 934 C ATOM 2218 C LYS A1077 23.929 -65.768 27.923 1.00 51.54 C ANISOU 2218 C LYS A1077 7529 5678 6374 1194 -1252 781 C ATOM 2219 O LYS A1077 24.746 -66.365 28.633 1.00 48.08 O ANISOU 2219 O LYS A1077 7248 5245 5776 1366 -1506 677 O ATOM 2220 CB LYS A1077 21.532 -65.534 28.630 1.00 54.14 C ANISOU 2220 CB LYS A1077 7783 6274 6514 1072 -762 1507 C ATOM 2221 CG LYS A1077 21.591 -66.875 29.322 1.00 55.27 C ANISOU 2221 CG LYS A1077 8142 6391 6467 1093 -954 1847 C ATOM 2222 CD LYS A1077 20.220 -67.474 29.501 1.00 58.58 C ANISOU 2222 CD LYS A1077 8520 6843 6894 915 -759 2433 C ATOM 2223 CE LYS A1077 20.335 -68.850 30.118 1.00 64.89 C ANISOU 2223 CE LYS A1077 9559 7561 7534 900 -985 2800 C ATOM 2224 NZ LYS A1077 21.213 -69.742 29.301 1.00 67.10 N ANISOU 2224 NZ LYS A1077 9923 7505 8068 846 -1418 2657 N ATOM 2225 N LEU A1078 23.912 -65.896 26.593 1.00 49.22 N ANISOU 2225 N LEU A1078 7135 5164 6401 991 -1275 747 N ATOM 2226 CA LEU A1078 24.913 -66.717 25.917 1.00 50.14 C ANISOU 2226 CA LEU A1078 7294 5065 6693 976 -1565 541 C ATOM 2227 C LEU A1078 26.315 -66.158 26.119 1.00 52.74 C ANISOU 2227 C LEU A1078 7569 5430 7040 1149 -1666 -6 C ATOM 2228 O LEU A1078 27.268 -66.918 26.324 1.00 55.96 O ANISOU 2228 O LEU A1078 8042 5752 7469 1272 -1960 -193 O ATOM 2229 CB LEU A1078 24.588 -66.818 24.431 1.00 46.20 C ANISOU 2229 CB LEU A1078 6719 4354 6482 745 -1528 578 C ATOM 2230 CG LEU A1078 23.291 -67.547 24.099 1.00 48.18 C ANISOU 2230 CG LEU A1078 7005 4492 6809 568 -1528 1088 C ATOM 2231 CD1 LEU A1078 22.871 -67.230 22.672 1.00 47.51 C ANISOU 2231 CD1 LEU A1078 6855 4227 6970 371 -1459 1069 C ATOM 2232 CD2 LEU A1078 23.473 -69.053 24.304 1.00 49.53 C ANISOU 2232 CD2 LEU A1078 7325 4505 6990 587 -1862 1299 C ATOM 2233 N ALA A1079 26.458 -64.832 26.063 1.00 52.52 N ANISOU 2233 N ALA A1079 7405 5504 7046 1162 -1452 -277 N ATOM 2234 CA ALA A1079 27.763 -64.214 26.274 1.00 54.47 C ANISOU 2234 CA ALA A1079 7556 5769 7371 1306 -1544 -798 C ATOM 2235 C ALA A1079 28.286 -64.495 27.680 1.00 60.84 C ANISOU 2235 C ALA A1079 8495 6697 7926 1594 -1780 -897 C ATOM 2236 O ALA A1079 29.461 -64.840 27.859 1.00 63.43 O ANISOU 2236 O ALA A1079 8806 6948 8348 1733 -2053 -1239 O ATOM 2237 CB ALA A1079 27.676 -62.709 26.019 1.00 51.73 C ANISOU 2237 CB ALA A1079 7055 5482 7119 1249 -1288 -1012 C ATOM 2238 N ASN A1080 27.418 -64.358 28.692 1.00 61.30 N ANISOU 2238 N ASN A1080 8692 6945 7655 1696 -1682 -608 N ATOM 2239 CA ASN A1080 27.815 -64.616 30.075 1.00 64.38 C ANISOU 2239 CA ASN A1080 9282 7464 7715 1983 -1898 -659 C ATOM 2240 C ASN A1080 28.261 -66.059 30.289 1.00 66.63 C ANISOU 2240 C ASN A1080 9756 7608 7953 2036 -2251 -517 C ATOM 2241 O ASN A1080 29.044 -66.333 31.202 1.00 71.12 O ANISOU 2241 O ASN A1080 10482 8190 8351 2286 -2558 -708 O ATOM 2242 CB ASN A1080 26.665 -64.281 31.024 1.00 65.91 C ANISOU 2242 CB ASN A1080 9607 7911 7525 2059 -1654 -318 C ATOM 2243 CG ASN A1080 26.490 -62.792 31.223 1.00 67.70 C ANISOU 2243 CG ASN A1080 9694 8291 7737 2143 -1428 -590 C ATOM 2244 OD1 ASN A1080 27.459 -62.035 31.216 1.00 70.38 O ANISOU 2244 OD1 ASN A1080 9931 8582 8228 2253 -1558 -1072 O ATOM 2245 ND2 ASN A1080 25.248 -62.364 31.412 1.00 67.45 N ANISOU 2245 ND2 ASN A1080 9639 8431 7557 2093 -1103 -293 N ATOM 2246 N GLU A1081 27.767 -66.989 29.480 1.00 64.90 N ANISOU 2246 N GLU A1081 9541 7229 7888 1821 -2258 -192 N ATOM 2247 CA GLU A1081 28.212 -68.372 29.536 1.00 67.74 C ANISOU 2247 CA GLU A1081 10063 7399 8276 1859 -2636 -81 C ATOM 2248 C GLU A1081 29.496 -68.609 28.755 1.00 67.58 C ANISOU 2248 C GLU A1081 9889 7180 8610 1896 -2891 -571 C ATOM 2249 O GLU A1081 29.976 -69.747 28.718 1.00 71.26 O ANISOU 2249 O GLU A1081 10461 7459 9155 1954 -3250 -562 O ATOM 2250 CB GLU A1081 27.118 -69.299 28.999 1.00 69.95 C ANISOU 2250 CB GLU A1081 10404 7561 8611 1619 -2576 465 C ATOM 2251 CG GLU A1081 25.862 -69.353 29.835 1.00 74.28 C ANISOU 2251 CG GLU A1081 11092 8288 8842 1570 -2346 1004 C ATOM 2252 CD GLU A1081 24.708 -69.990 29.084 1.00 79.01 C ANISOU 2252 CD GLU A1081 11637 8756 9627 1284 -2226 1489 C ATOM 2253 OE1 GLU A1081 24.847 -70.216 27.861 1.00 78.78 O ANISOU 2253 OE1 GLU A1081 11478 8513 9942 1139 -2305 1369 O ATOM 2254 OE2 GLU A1081 23.659 -70.260 29.710 1.00 82.94 O ANISOU 2254 OE2 GLU A1081 12218 9364 9933 1206 -2051 1982 O ATOM 2255 N GLY A1082 30.044 -67.582 28.113 1.00 74.30 N ANISOU 2255 N GLY A1082 9827 7691 10714 3540 2091 1272 N ATOM 2256 CA GLY A1082 31.251 -67.754 27.328 1.00 72.62 C ANISOU 2256 CA GLY A1082 9553 7430 10610 3480 2057 1284 C ATOM 2257 C GLY A1082 31.045 -68.421 25.986 1.00 71.95 C ANISOU 2257 C GLY A1082 9518 7223 10597 3331 2204 1344 C ATOM 2258 O GLY A1082 31.981 -69.022 25.451 1.00 75.53 O ANISOU 2258 O GLY A1082 9984 7653 11062 3380 2269 1404 O ATOM 2259 N LYS A1083 29.846 -68.327 25.419 1.00 65.03 N ANISOU 2259 N LYS A1083 8691 6259 9760 3182 2240 1333 N ATOM 2260 CA LYS A1083 29.538 -68.939 24.127 1.00 61.45 C ANISOU 2260 CA LYS A1083 8351 5641 9356 3063 2305 1361 C ATOM 2261 C LYS A1083 29.524 -67.835 23.070 1.00 58.55 C ANISOU 2261 C LYS A1083 7910 5261 9075 2929 2225 1285 C ATOM 2262 O LYS A1083 28.474 -67.300 22.722 1.00 56.46 O ANISOU 2262 O LYS A1083 7642 4935 8876 2781 2172 1243 O ATOM 2263 CB LYS A1083 28.211 -69.683 24.196 1.00 57.83 C ANISOU 2263 CB LYS A1083 7992 5045 8937 2975 2342 1441 C ATOM 2264 CG LYS A1083 28.107 -70.655 25.362 1.00 60.28 C ANISOU 2264 CG LYS A1083 8324 5388 9190 3105 2429 1576 C ATOM 2265 CD LYS A1083 26.763 -71.362 25.355 1.00 63.37 C ANISOU 2265 CD LYS A1083 8746 5622 9710 2988 2446 1743 C ATOM 2266 CE LYS A1083 26.695 -72.450 26.403 1.00 66.57 C ANISOU 2266 CE LYS A1083 9157 6045 10092 3113 2543 1944 C ATOM 2267 NZ LYS A1083 25.368 -73.128 26.376 1.00 68.43 N ANISOU 2267 NZ LYS A1083 9357 6106 10539 2974 2535 2190 N ATOM 2268 N VAL A1084 30.707 -67.511 22.540 1.00 57.87 N ANISOU 2268 N VAL A1084 7741 5238 9009 2989 2226 1309 N ATOM 2269 CA VAL A1084 30.853 -66.327 21.693 1.00 59.97 C ANISOU 2269 CA VAL A1084 7874 5529 9384 2880 2147 1294 C ATOM 2270 C VAL A1084 30.110 -66.500 20.373 1.00 59.19 C ANISOU 2270 C VAL A1084 7938 5293 9258 2783 2196 1273 C ATOM 2271 O VAL A1084 29.302 -65.647 19.985 1.00 58.78 O ANISOU 2271 O VAL A1084 7847 5202 9285 2621 2102 1210 O ATOM 2272 CB VAL A1084 32.339 -66.010 21.455 1.00 66.36 C ANISOU 2272 CB VAL A1084 8498 6446 10268 2983 2156 1423 C ATOM 2273 CG1 VAL A1084 32.486 -64.654 20.791 1.00 68.58 C ANISOU 2273 CG1 VAL A1084 8576 6758 10724 2853 2037 1462 C ATOM 2274 CG2 VAL A1084 33.103 -66.060 22.759 1.00 71.30 C ANISOU 2274 CG2 VAL A1084 9011 7156 10923 3092 2060 1443 C ATOM 2275 N LYS A1085 30.387 -67.590 19.651 1.00 57.09 N ANISOU 2275 N LYS A1085 7885 4936 8870 2908 2312 1315 N ATOM 2276 CA LYS A1085 29.746 -67.806 18.356 1.00 59.11 C ANISOU 2276 CA LYS A1085 8370 5026 9063 2871 2301 1274 C ATOM 2277 C LYS A1085 28.228 -67.835 18.484 1.00 59.53 C ANISOU 2277 C LYS A1085 8505 4907 9205 2662 2164 1196 C ATOM 2278 O LYS A1085 27.515 -67.273 17.642 1.00 56.20 O ANISOU 2278 O LYS A1085 8133 4392 8829 2531 2075 1145 O ATOM 2279 CB LYS A1085 30.244 -69.107 17.733 1.00 59.65 C ANISOU 2279 CB LYS A1085 8732 4984 8948 3104 2393 1299 C ATOM 2280 CG LYS A1085 31.705 -69.095 17.347 1.00 62.61 C ANISOU 2280 CG LYS A1085 9023 5549 9218 3344 2565 1425 C ATOM 2281 CD LYS A1085 31.915 -68.496 15.970 1.00 65.24 C ANISOU 2281 CD LYS A1085 9408 5912 9469 3438 2639 1482 C ATOM 2282 CE LYS A1085 33.373 -68.605 15.566 1.00 70.80 C ANISOU 2282 CE LYS A1085 9996 6848 10055 3692 2842 1680 C ATOM 2283 NZ LYS A1085 33.565 -68.329 14.120 1.00 77.57 N ANISOU 2283 NZ LYS A1085 10989 7750 10734 3875 2961 1768 N ATOM 2284 N GLU A1086 27.719 -68.488 19.530 1.00 56.63 N ANISOU 2284 N GLU A1086 8132 4504 8882 2639 2153 1224 N ATOM 2285 CA GLU A1086 26.278 -68.567 19.726 1.00 58.08 C ANISOU 2285 CA GLU A1086 8325 4541 9200 2457 2051 1241 C ATOM 2286 C GLU A1086 25.703 -67.209 20.107 1.00 55.73 C ANISOU 2286 C GLU A1086 7798 4376 8999 2330 2012 1204 C ATOM 2287 O GLU A1086 24.588 -66.866 19.699 1.00 55.03 O ANISOU 2287 O GLU A1086 7705 4172 9032 2164 1919 1203 O ATOM 2288 CB GLU A1086 25.958 -69.614 20.792 1.00 61.87 C ANISOU 2288 CB GLU A1086 8811 4983 9715 2502 2089 1362 C ATOM 2289 CG GLU A1086 24.503 -70.008 20.849 1.00 67.40 C ANISOU 2289 CG GLU A1086 9512 5487 10611 2329 1987 1482 C ATOM 2290 CD GLU A1086 24.260 -71.203 21.742 1.00 73.83 C ANISOU 2290 CD GLU A1086 10328 6233 11491 2379 2024 1673 C ATOM 2291 OE1 GLU A1086 25.243 -71.847 22.157 1.00 74.98 O ANISOU 2291 OE1 GLU A1086 10544 6445 11499 2552 2110 1667 O ATOM 2292 OE2 GLU A1086 23.083 -71.496 22.037 1.00 79.10 O ANISOU 2292 OE2 GLU A1086 10899 6781 12373 2248 1969 1866 O ATOM 2293 N ALA A1087 26.457 -66.421 20.882 1.00 54.76 N ANISOU 2293 N ALA A1087 7497 4471 8837 2418 2044 1172 N ATOM 2294 CA ALA A1087 26.019 -65.070 21.226 1.00 58.54 C ANISOU 2294 CA ALA A1087 7804 5051 9389 2343 1955 1104 C ATOM 2295 C ALA A1087 25.975 -64.171 19.995 1.00 56.35 C ANISOU 2295 C ALA A1087 7506 4719 9185 2203 1867 1044 C ATOM 2296 O ALA A1087 25.029 -63.394 19.824 1.00 52.73 O ANISOU 2296 O ALA A1087 6990 4224 8820 2069 1780 1000 O ATOM 2297 CB ALA A1087 26.939 -64.473 22.292 1.00 54.21 C ANISOU 2297 CB ALA A1087 7124 4683 8790 2493 1913 1065 C ATOM 2298 N GLN A1088 26.988 -64.268 19.128 1.00 53.61 N ANISOU 2298 N GLN A1088 7199 4379 8792 2258 1908 1071 N ATOM 2299 CA GLN A1088 27.030 -63.436 17.928 1.00 57.30 C ANISOU 2299 CA GLN A1088 7644 4821 9307 2165 1858 1064 C ATOM 2300 C GLN A1088 25.893 -63.770 16.970 1.00 56.79 C ANISOU 2300 C GLN A1088 7786 4555 9237 2047 1808 1023 C ATOM 2301 O GLN A1088 25.271 -62.866 16.400 1.00 57.09 O ANISOU 2301 O GLN A1088 7774 4554 9364 1900 1708 982 O ATOM 2302 CB GLN A1088 28.377 -63.595 17.230 1.00 54.43 C ANISOU 2302 CB GLN A1088 7269 4540 8871 2320 1972 1176 C ATOM 2303 CG GLN A1088 29.530 -63.006 17.998 1.00 54.84 C ANISOU 2303 CG GLN A1088 7051 4760 9025 2386 1946 1261 C ATOM 2304 CD GLN A1088 30.863 -63.404 17.412 1.00 58.39 C ANISOU 2304 CD GLN A1088 7454 5305 9426 2574 2108 1449 C ATOM 2305 OE1 GLN A1088 31.206 -64.583 17.372 1.00 59.02 O ANISOU 2305 OE1 GLN A1088 7714 5368 9343 2751 2256 1475 O ATOM 2306 NE2 GLN A1088 31.617 -62.421 16.935 1.00 59.93 N ANISOU 2306 NE2 GLN A1088 7394 5598 9780 2553 2081 1616 N ATOM 2307 N ALA A1089 25.616 -65.060 16.768 1.00 54.20 N ANISOU 2307 N ALA A1089 7700 4066 8829 2108 1831 1036 N ATOM 2308 CA ALA A1089 24.480 -65.447 15.940 1.00 59.02 C ANISOU 2308 CA ALA A1089 8521 4420 9484 1986 1691 1004 C ATOM 2309 C ALA A1089 23.167 -64.953 16.539 1.00 59.52 C ANISOU 2309 C ALA A1089 8419 4441 9755 1778 1592 1019 C ATOM 2310 O ALA A1089 22.271 -64.508 15.811 1.00 58.85 O ANISOU 2310 O ALA A1089 8370 4218 9774 1621 1454 991 O ATOM 2311 CB ALA A1089 24.457 -66.966 15.762 1.00 56.28 C ANISOU 2311 CB ALA A1089 8466 3859 9058 2095 1656 1025 C ATOM 2312 N ALA A1090 23.034 -65.017 17.868 1.00 53.75 N ANISOU 2312 N ALA A1090 7509 3840 9073 1810 1672 1080 N ATOM 2313 CA ALA A1090 21.830 -64.502 18.513 1.00 53.57 C ANISOU 2313 CA ALA A1090 7309 3833 9212 1694 1638 1137 C ATOM 2314 C ALA A1090 21.699 -62.998 18.315 1.00 53.11 C ANISOU 2314 C ALA A1090 7104 3883 9191 1623 1577 1034 C ATOM 2315 O ALA A1090 20.585 -62.480 18.155 1.00 52.37 O ANISOU 2315 O ALA A1090 6934 3722 9242 1489 1498 1056 O ATOM 2316 CB ALA A1090 21.841 -64.843 20.002 1.00 54.09 C ANISOU 2316 CB ALA A1090 7245 4060 9245 1838 1774 1238 C ATOM 2317 N ALA A1091 22.824 -62.279 18.335 1.00 51.84 N ANISOU 2317 N ALA A1091 6882 3875 8939 1707 1589 949 N ATOM 2318 CA ALA A1091 22.788 -60.839 18.135 1.00 54.50 C ANISOU 2318 CA ALA A1091 7079 4281 9349 1632 1479 865 C ATOM 2319 C ALA A1091 22.467 -60.472 16.694 1.00 54.17 C ANISOU 2319 C ALA A1091 7116 4103 9364 1475 1393 847 C ATOM 2320 O ALA A1091 21.987 -59.364 16.442 1.00 52.44 O ANISOU 2320 O ALA A1091 6791 3884 9249 1362 1281 796 O ATOM 2321 CB ALA A1091 24.116 -60.213 18.557 1.00 54.64 C ANISOU 2321 CB ALA A1091 6980 4453 9329 1744 1453 835 C ATOM 2322 N GLU A1092 22.712 -61.383 15.749 1.00 54.90 N ANISOU 2322 N GLU A1092 7425 4069 9366 1499 1428 879 N ATOM 2323 CA GLU A1092 22.358 -61.129 14.357 1.00 58.03 C ANISOU 2323 CA GLU A1092 7967 4322 9760 1406 1333 856 C ATOM 2324 C GLU A1092 20.846 -61.087 14.166 1.00 54.41 C ANISOU 2324 C GLU A1092 7537 3671 9466 1216 1178 844 C ATOM 2325 O GLU A1092 20.355 -60.438 13.234 1.00 52.67 O ANISOU 2325 O GLU A1092 7359 3357 9298 1097 1055 808 O ATOM 2326 CB GLU A1092 22.983 -62.199 13.459 1.00 67.06 C ANISOU 2326 CB GLU A1092 9410 5364 10707 1566 1387 876 C ATOM 2327 CG GLU A1092 23.317 -61.720 12.055 1.00 75.60 C ANISOU 2327 CG GLU A1092 10630 6425 11669 1618 1373 879 C ATOM 2328 CD GLU A1092 24.470 -60.730 12.037 1.00 79.42 C ANISOU 2328 CD GLU A1092 10860 7163 12154 1687 1504 978 C ATOM 2329 OE1 GLU A1092 25.363 -60.843 12.902 1.00 82.68 O ANISOU 2329 OE1 GLU A1092 11100 7735 12580 1781 1613 1039 O ATOM 2330 OE2 GLU A1092 24.481 -59.838 11.164 1.00 79.68 O ANISOU 2330 OE2 GLU A1092 10849 7221 12203 1642 1472 1021 O ATOM 2331 N GLN A1093 20.099 -61.769 15.036 1.00 55.01 N ANISOU 2331 N GLN A1093 7565 3690 9646 1190 1184 915 N ATOM 2332 CA GLN A1093 18.642 -61.719 14.972 1.00 56.73 C ANISOU 2332 CA GLN A1093 7725 3740 10089 1010 1049 985 C ATOM 2333 C GLN A1093 18.120 -60.311 15.201 1.00 56.11 C ANISOU 2333 C GLN A1093 7418 3787 10114 930 1027 944 C ATOM 2334 O GLN A1093 17.041 -59.960 14.708 1.00 58.24 O ANISOU 2334 O GLN A1093 7653 3914 10561 768 889 976 O ATOM 2335 CB GLN A1093 18.045 -62.673 16.002 1.00 59.19 C ANISOU 2335 CB GLN A1093 7949 4020 10521 1032 1111 1158 C ATOM 2336 CG GLN A1093 18.575 -64.071 15.876 1.00 66.09 C ANISOU 2336 CG GLN A1093 9047 4751 11313 1116 1103 1197 C ATOM 2337 CD GLN A1093 18.315 -64.646 14.503 1.00 72.38 C ANISOU 2337 CD GLN A1093 10159 5214 12127 1035 853 1144 C ATOM 2338 OE1 GLN A1093 17.166 -64.891 14.130 1.00 76.40 O ANISOU 2338 OE1 GLN A1093 10683 5460 12886 856 627 1240 O ATOM 2339 NE2 GLN A1093 19.381 -64.856 13.735 1.00 72.60 N ANISOU 2339 NE2 GLN A1093 10450 5246 11889 1196 875 1008 N ATOM 2340 N LEU A1094 18.870 -59.497 15.947 1.00 56.73 N ANISOU 2340 N LEU A1094 8721 3632 9201 2201 -455 425 N ATOM 2341 CA LEU A1094 18.465 -58.121 16.191 1.00 51.39 C ANISOU 2341 CA LEU A1094 7761 3309 8457 1925 -142 628 C ATOM 2342 C LEU A1094 18.232 -57.361 14.894 1.00 52.99 C ANISOU 2342 C LEU A1094 8202 3625 8305 2075 -90 470 C ATOM 2343 O LEU A1094 17.408 -56.441 14.859 1.00 50.45 O ANISOU 2343 O LEU A1094 7759 3385 8026 1842 -78 611 O ATOM 2344 CB LEU A1094 19.521 -57.412 17.036 1.00 48.63 C ANISOU 2344 CB LEU A1094 7062 3368 8046 1886 359 802 C ATOM 2345 CG LEU A1094 19.673 -57.975 18.446 1.00 50.26 C ANISOU 2345 CG LEU A1094 6978 3536 8582 1625 315 1040 C ATOM 2346 CD1 LEU A1094 20.968 -57.496 19.068 1.00 47.58 C ANISOU 2346 CD1 LEU A1094 6374 3589 8117 1671 761 1165 C ATOM 2347 CD2 LEU A1094 18.475 -57.565 19.292 1.00 46.91 C ANISOU 2347 CD2 LEU A1094 6289 3127 8407 1131 230 1258 C ATOM 2348 N LYS A1095 18.933 -57.730 13.817 1.00 55.28 N ANISOU 2348 N LYS A1095 8824 3936 8242 2461 -71 175 N ATOM 2349 CA LYS A1095 18.787 -56.994 12.563 1.00 57.43 C ANISOU 2349 CA LYS A1095 9331 4387 8102 2547 -21 60 C ATOM 2350 C LYS A1095 17.383 -57.134 11.995 1.00 57.85 C ANISOU 2350 C LYS A1095 9601 4124 8257 2360 -502 53 C ATOM 2351 O LYS A1095 16.841 -56.184 11.419 1.00 57.43 O ANISOU 2351 O LYS A1095 9564 4199 8056 2231 -508 162 O ATOM 2352 CB LYS A1095 19.830 -57.464 11.554 1.00 62.17 C ANISOU 2352 CB LYS A1095 10222 5148 8252 2982 113 -293 C ATOM 2353 CG LYS A1095 21.221 -56.968 11.883 1.00 63.44 C ANISOU 2353 CG LYS A1095 10107 5790 8206 3139 649 -235 C ATOM 2354 CD LYS A1095 22.249 -57.485 10.907 1.00 69.59 C ANISOU 2354 CD LYS A1095 11097 6807 8537 3600 811 -618 C ATOM 2355 CE LYS A1095 23.574 -56.781 11.122 1.00 68.49 C ANISOU 2355 CE LYS A1095 10625 7272 8127 3685 1362 -497 C ATOM 2356 NZ LYS A1095 24.661 -57.426 10.346 1.00 73.05 N ANISOU 2356 NZ LYS A1095 11294 8140 8321 4187 1560 -897 N ATOM 2357 N THR A1096 16.771 -58.307 12.156 1.00 59.90 N ANISOU 2357 N THR A1096 10021 3956 8783 2317 -951 -39 N ATOM 2358 CA THR A1096 15.400 -58.479 11.693 1.00 61.54 C ANISOU 2358 CA THR A1096 10386 3889 9107 2078 -1443 -1 C ATOM 2359 C THR A1096 14.447 -57.585 12.471 1.00 58.13 C ANISOU 2359 C THR A1096 9515 3572 9001 1705 -1412 353 C ATOM 2360 O THR A1096 13.563 -56.946 11.886 1.00 58.64 O ANISOU 2360 O THR A1096 9588 3659 9034 1579 -1587 440 O ATOM 2361 CB THR A1096 14.989 -59.944 11.811 1.00 66.41 C ANISOU 2361 CB THR A1096 11260 4014 9959 2046 -1955 -135 C ATOM 2362 OG1 THR A1096 15.888 -60.745 11.036 1.00 73.32 O ANISOU 2362 OG1 THR A1096 12557 4760 10540 2468 -1973 -544 O ATOM 2363 CG2 THR A1096 13.576 -60.143 11.298 1.00 66.77 C ANISOU 2363 CG2 THR A1096 11459 3812 10098 1752 -2493 -72 C ATOM 2364 N THR A1097 14.622 -57.511 13.792 1.00 55.22 N ANISOU 2364 N THR A1097 8745 3298 8937 1535 -1191 549 N ATOM 2365 CA THR A1097 13.795 -56.615 14.593 1.00 52.59 C ANISOU 2365 CA THR A1097 7962 3135 8885 1223 -1085 812 C ATOM 2366 C THR A1097 14.053 -55.160 14.225 1.00 50.83 C ANISOU 2366 C THR A1097 7648 3196 8470 1313 -727 862 C ATOM 2367 O THR A1097 13.118 -54.352 14.154 1.00 50.64 O ANISOU 2367 O THR A1097 7442 3201 8599 1179 -809 984 O ATOM 2368 CB THR A1097 14.061 -56.841 16.079 1.00 50.35 C ANISOU 2368 CB THR A1097 7298 2957 8876 1004 -883 978 C ATOM 2369 OG1 THR A1097 13.972 -58.241 16.372 1.00 52.58 O ANISOU 2369 OG1 THR A1097 7724 2933 9321 917 -1262 969 O ATOM 2370 CG2 THR A1097 13.043 -56.087 16.919 1.00 48.77 C ANISOU 2370 CG2 THR A1097 6627 2940 8963 670 -812 1178 C ATOM 2371 N ARG A1098 15.317 -54.811 13.984 1.00 51.58 N ANISOU 2371 N ARG A1098 7855 3499 8243 1535 -355 784 N ATOM 2372 CA ARG A1098 15.663 -53.437 13.641 1.00 50.64 C ANISOU 2372 CA ARG A1098 7687 3636 7918 1564 -46 875 C ATOM 2373 C ARG A1098 14.993 -53.007 12.345 1.00 52.51 C ANISOU 2373 C ARG A1098 8199 3792 7960 1607 -339 862 C ATOM 2374 O ARG A1098 14.449 -51.902 12.257 1.00 53.13 O ANISOU 2374 O ARG A1098 8148 3902 8138 1507 -337 1027 O ATOM 2375 CB ARG A1098 17.181 -53.291 13.537 1.00 48.47 C ANISOU 2375 CB ARG A1098 7485 3649 7281 1753 364 815 C ATOM 2376 CG ARG A1098 17.646 -51.872 13.265 1.00 52.63 C ANISOU 2376 CG ARG A1098 7969 4450 7577 1705 671 962 C ATOM 2377 CD ARG A1098 19.028 -51.888 12.664 1.00 52.36 C ANISOU 2377 CD ARG A1098 8092 4748 7053 1901 965 879 C ATOM 2378 NE ARG A1098 19.055 -52.674 11.432 1.00 55.06 N ANISOU 2378 NE ARG A1098 8810 5050 7059 2136 737 632 N ATOM 2379 CZ ARG A1098 20.163 -53.115 10.850 1.00 56.69 C ANISOU 2379 CZ ARG A1098 9158 5536 6847 2393 943 437 C ATOM 2380 NH1 ARG A1098 21.346 -52.854 11.392 1.00 53.85 N ANISOU 2380 NH1 ARG A1098 8560 5528 6373 2437 1365 511 N ATOM 2381 NH2 ARG A1098 20.084 -53.820 9.729 1.00 60.48 N ANISOU 2381 NH2 ARG A1098 9999 5971 7009 2604 728 152 N ATOM 2382 N ASN A1099 15.014 -53.870 11.330 1.00 55.73 N ANISOU 2382 N ASN A1099 9001 4078 8095 1756 -620 661 N ATOM 2383 CA ASN A1099 14.413 -53.517 10.048 1.00 58.03 C ANISOU 2383 CA ASN A1099 9587 4330 8133 1752 -929 660 C ATOM 2384 C ASN A1099 12.893 -53.475 10.141 1.00 59.06 C ANISOU 2384 C ASN A1099 9567 4214 8659 1538 -1369 810 C ATOM 2385 O ASN A1099 12.260 -52.578 9.579 1.00 61.75 O ANISOU 2385 O ASN A1099 9895 4567 8999 1467 -1529 978 O ATOM 2386 CB ASN A1099 14.849 -54.508 8.962 1.00 62.36 C ANISOU 2386 CB ASN A1099 10615 4839 8239 1954 -1104 346 C ATOM 2387 CG ASN A1099 16.364 -54.637 8.848 1.00 63.41 C ANISOU 2387 CG ASN A1099 10832 5281 7981 2218 -654 158 C ATOM 2388 OD1 ASN A1099 17.114 -53.765 9.292 1.00 63.20 O ANISOU 2388 OD1 ASN A1099 10564 5555 7896 2201 -232 321 O ATOM 2389 ND2 ASN A1099 16.818 -55.728 8.242 1.00 65.12 N ANISOU 2389 ND2 ASN A1099 11385 5428 7930 2468 -754 -202 N ATOM 2390 N ALA A1100 12.287 -54.427 10.856 1.00 60.59 N ANISOU 2390 N ALA A1100 9620 4199 9202 1417 -1592 785 N ATOM 2391 CA ALA A1100 10.837 -54.591 10.822 1.00 62.33 C ANISOU 2391 CA ALA A1100 9701 4237 9744 1194 -2060 916 C ATOM 2392 C ALA A1100 10.097 -53.704 11.817 1.00 61.50 C ANISOU 2392 C ALA A1100 9029 4247 10093 1036 -1921 1142 C ATOM 2393 O ALA A1100 8.886 -53.518 11.665 1.00 64.19 O ANISOU 2393 O ALA A1100 9176 4526 10688 898 -2263 1275 O ATOM 2394 CB ALA A1100 10.465 -56.052 11.081 1.00 64.37 C ANISOU 2394 CB ALA A1100 10080 4232 10146 1068 -2424 814 C ATOM 2395 N TYR A1101 10.782 -53.161 12.829 1.00 57.20 N ANISOU 2395 N TYR A1101 8200 3885 9649 1056 -1434 1169 N ATOM 2396 CA TYR A1101 10.117 -52.366 13.857 1.00 55.26 C ANISOU 2396 CA TYR A1101 7422 3764 9812 922 -1261 1301 C ATOM 2397 C TYR A1101 10.866 -51.074 14.162 1.00 52.64 C ANISOU 2397 C TYR A1101 6990 3590 9420 1033 -799 1327 C ATOM 2398 O TYR A1101 10.308 -49.980 14.023 1.00 51.37 O ANISOU 2398 O TYR A1101 6668 3413 9436 1076 -817 1412 O ATOM 2399 CB TYR A1101 9.967 -53.165 15.158 1.00 53.12 C ANISOU 2399 CB TYR A1101 6822 3565 9795 692 -1179 1314 C ATOM 2400 CG TYR A1101 9.127 -54.418 15.051 1.00 56.13 C ANISOU 2400 CG TYR A1101 7250 3777 10299 487 -1674 1345 C ATOM 2401 CD1 TYR A1101 7.737 -54.355 15.083 1.00 58.78 C ANISOU 2401 CD1 TYR A1101 7264 4139 10931 295 -1998 1469 C ATOM 2402 CD2 TYR A1101 9.725 -55.671 14.943 1.00 55.96 C ANISOU 2402 CD2 TYR A1101 7581 3562 10119 480 -1840 1255 C ATOM 2403 CE1 TYR A1101 6.966 -55.505 14.996 1.00 62.53 C ANISOU 2403 CE1 TYR A1101 7783 4474 11503 34 -2486 1538 C ATOM 2404 CE2 TYR A1101 8.966 -56.822 14.854 1.00 57.76 C ANISOU 2404 CE2 TYR A1101 7905 3572 10469 251 -2348 1296 C ATOM 2405 CZ TYR A1101 7.587 -56.734 14.880 1.00 64.74 C ANISOU 2405 CZ TYR A1101 8480 4509 11611 -6 -2674 1456 C ATOM 2406 OH TYR A1101 6.826 -57.881 14.791 1.00 70.29 O ANISOU 2406 OH TYR A1101 9280 5008 12419 -303 -3215 1536 O ATOM 2407 N ILE A1102 12.126 -51.201 14.594 1.00 52.06 N ANISOU 2407 N ILE A1102 8357 3921 7503 2177 -622 -275 N ATOM 2408 CA ILE A1102 12.847 -50.067 15.167 1.00 50.79 C ANISOU 2408 CA ILE A1102 8085 3933 7279 2149 -551 -106 C ATOM 2409 C ILE A1102 12.984 -48.942 14.152 1.00 51.08 C ANISOU 2409 C ILE A1102 8433 3992 6982 2242 -389 -255 C ATOM 2410 O ILE A1102 12.788 -47.766 14.480 1.00 46.54 O ANISOU 2410 O ILE A1102 7934 3569 6179 2203 -489 -212 O ATOM 2411 CB ILE A1102 14.223 -50.509 15.696 1.00 49.27 C ANISOU 2411 CB ILE A1102 7580 3619 7521 2132 -430 147 C ATOM 2412 CG1 ILE A1102 14.101 -51.786 16.546 1.00 57.67 C ANISOU 2412 CG1 ILE A1102 8387 4578 8948 2047 -623 326 C ATOM 2413 CG2 ILE A1102 14.851 -49.380 16.493 1.00 48.35 C ANISOU 2413 CG2 ILE A1102 7345 3682 7343 1994 -505 367 C ATOM 2414 CD1 ILE A1102 13.233 -51.631 17.799 1.00 48.70 C ANISOU 2414 CD1 ILE A1102 7142 3719 7641 1828 -932 496 C ATOM 2415 N GLN A1103 13.337 -49.276 12.910 1.00 55.14 N ANISOU 2415 N GLN A1103 9180 4332 7438 2366 -134 -429 N ATOM 2416 CA GLN A1103 13.484 -48.239 11.894 1.00 56.30 C ANISOU 2416 CA GLN A1103 9658 4516 7218 2411 25 -512 C ATOM 2417 C GLN A1103 12.164 -47.520 11.630 1.00 53.69 C ANISOU 2417 C GLN A1103 9599 4299 6503 2402 -281 -631 C ATOM 2418 O GLN A1103 12.162 -46.323 11.317 1.00 50.91 O ANISOU 2418 O GLN A1103 9446 4002 5895 2400 -303 -587 O ATOM 2419 CB GLN A1103 14.039 -48.837 10.600 1.00 62.06 C ANISOU 2419 CB GLN A1103 10642 5074 7863 2549 399 -697 C ATOM 2420 CG GLN A1103 14.452 -47.781 9.587 1.00 67.17 C ANISOU 2420 CG GLN A1103 11602 5794 8127 2549 640 -685 C ATOM 2421 CD GLN A1103 15.089 -48.358 8.343 1.00 74.52 C ANISOU 2421 CD GLN A1103 12803 6614 8897 2698 1116 -868 C ATOM 2422 OE1 GLN A1103 15.520 -49.513 8.322 1.00 78.63 O ANISOU 2422 OE1 GLN A1103 13207 6962 9706 2856 1340 -996 O ATOM 2423 NE2 GLN A1103 15.153 -47.551 7.292 1.00 77.48 N ANISOU 2423 NE2 GLN A1103 13577 7072 8788 2665 1286 -883 N ATOM 2424 N LYS A1104 11.037 -48.223 11.762 1.00 55.48 N ANISOU 2424 N LYS A1104 9802 4546 6732 2389 -545 -739 N ATOM 2425 CA LYS A1104 9.740 -47.570 11.606 1.00 57.83 C ANISOU 2425 CA LYS A1104 10218 4988 6766 2407 -855 -793 C ATOM 2426 C LYS A1104 9.462 -46.611 12.758 1.00 55.08 C ANISOU 2426 C LYS A1104 9649 4836 6443 2430 -968 -653 C ATOM 2427 O LYS A1104 8.874 -45.542 12.554 1.00 56.06 O ANISOU 2427 O LYS A1104 9929 5023 6350 2532 -1105 -675 O ATOM 2428 CB LYS A1104 8.633 -48.618 11.495 1.00 61.02 C ANISOU 2428 CB LYS A1104 10560 5389 7235 2337 -1124 -882 C ATOM 2429 CG LYS A1104 8.762 -49.520 10.276 1.00 66.90 C ANISOU 2429 CG LYS A1104 11677 5875 7866 2312 -1087 -1101 C ATOM 2430 CD LYS A1104 7.637 -50.543 10.220 1.00 71.98 C ANISOU 2430 CD LYS A1104 12277 6466 8606 2161 -1459 -1160 C ATOM 2431 CE LYS A1104 7.695 -51.375 8.946 1.00 78.43 C ANISOU 2431 CE LYS A1104 13610 6966 9222 2120 -1490 -1446 C ATOM 2432 NZ LYS A1104 8.865 -52.301 8.909 1.00 81.53 N ANISOU 2432 NZ LYS A1104 14089 7051 9836 2213 -1119 -1571 N ATOM 2433 N TYR A1105 9.865 -46.978 13.977 1.00 51.90 N ANISOU 2433 N TYR A1105 8927 4508 6285 2348 -930 -515 N ATOM 2434 CA TYR A1105 9.738 -46.049 15.094 1.00 51.77 C ANISOU 2434 CA TYR A1105 8812 4656 6203 2363 -1002 -430 C ATOM 2435 C TYR A1105 10.627 -44.829 14.895 1.00 49.60 C ANISOU 2435 C TYR A1105 8779 4256 5812 2369 -929 -398 C ATOM 2436 O TYR A1105 10.196 -43.697 15.133 1.00 50.75 O ANISOU 2436 O TYR A1105 9093 4420 5768 2469 -1046 -447 O ATOM 2437 CB TYR A1105 10.077 -46.743 16.414 1.00 55.67 C ANISOU 2437 CB TYR A1105 8987 5257 6908 2215 -1007 -259 C ATOM 2438 CG TYR A1105 10.205 -45.774 17.575 1.00 63.91 C ANISOU 2438 CG TYR A1105 10049 6434 7799 2197 -1062 -202 C ATOM 2439 CD1 TYR A1105 9.120 -45.010 17.990 1.00 68.92 C ANISOU 2439 CD1 TYR A1105 10745 7254 8188 2363 -1126 -324 C ATOM 2440 CD2 TYR A1105 11.413 -45.614 18.251 1.00 67.16 C ANISOU 2440 CD2 TYR A1105 10429 6772 8316 2025 -1065 -36 C ATOM 2441 CE1 TYR A1105 9.230 -44.115 19.045 1.00 71.12 C ANISOU 2441 CE1 TYR A1105 11149 7608 8267 2381 -1154 -349 C ATOM 2442 CE2 TYR A1105 11.532 -44.720 19.312 1.00 69.03 C ANISOU 2442 CE2 TYR A1105 10791 7089 8347 1965 -1178 -21 C ATOM 2443 CZ TYR A1105 10.436 -43.977 19.704 1.00 72.07 C ANISOU 2443 CZ TYR A1105 11333 7625 8427 2155 -1203 -213 C ATOM 2444 OH TYR A1105 10.540 -43.087 20.755 1.00 76.22 O ANISOU 2444 OH TYR A1105 12085 8186 8689 2133 -1291 -273 O ATOM 2445 N LEU A1106 11.872 -45.042 14.463 1.00 48.68 N ANISOU 2445 N LEU A1106 8665 3993 5838 2267 -734 -298 N ATOM 2446 CA LEU A1106 12.785 -43.929 14.221 1.00 49.93 C ANISOU 2446 CA LEU A1106 9002 4041 5930 2191 -671 -189 C ATOM 2447 C LEU A1106 12.216 -42.963 13.187 1.00 47.29 C ANISOU 2447 C LEU A1106 9063 3628 5276 2298 -731 -287 C ATOM 2448 O LEU A1106 12.264 -41.742 13.366 1.00 47.85 O ANISOU 2448 O LEU A1106 9349 3606 5226 2283 -869 -240 O ATOM 2449 CB LEU A1106 14.149 -44.460 13.767 1.00 56.47 C ANISOU 2449 CB LEU A1106 9663 4785 7008 2089 -378 -30 C ATOM 2450 CG LEU A1106 15.071 -43.429 13.095 1.00 60.92 C ANISOU 2450 CG LEU A1106 10392 5261 7495 1976 -236 130 C ATOM 2451 CD1 LEU A1106 15.681 -42.470 14.122 1.00 60.11 C ANISOU 2451 CD1 LEU A1106 10226 5118 7494 1756 -462 338 C ATOM 2452 CD2 LEU A1106 16.157 -44.099 12.250 1.00 63.04 C ANISOU 2452 CD2 LEU A1106 10492 5512 7949 1979 195 235 C ATOM 2453 N GLU A 219 11.669 -43.496 12.094 1.00 50.99 N ANISOU 2453 N GLU A 219 8436 2976 7963 1872 -855 -420 N ATOM 2454 CA GLU A 219 11.137 -42.632 11.046 1.00 50.11 C ANISOU 2454 CA GLU A 219 8390 2943 7706 1807 -741 -507 C ATOM 2455 C GLU A 219 9.917 -41.859 11.536 1.00 47.09 C ANISOU 2455 C GLU A 219 8018 2699 7176 1618 -866 -393 C ATOM 2456 O GLU A 219 9.773 -40.667 11.239 1.00 45.32 O ANISOU 2456 O GLU A 219 7733 2612 6873 1585 -783 -410 O ATOM 2457 CB GLU A 219 10.817 -43.466 9.802 1.00 54.35 C ANISOU 2457 CB GLU A 219 9162 3325 8163 1812 -710 -642 C ATOM 2458 CG GLU A 219 12.073 -43.931 9.056 1.00 62.73 C ANISOU 2458 CG GLU A 219 10204 4257 9374 2004 -494 -795 C ATOM 2459 CD GLU A 219 11.839 -45.114 8.123 1.00 70.92 C ANISOU 2459 CD GLU A 219 11493 5099 10353 2022 -509 -908 C ATOM 2460 OE1 GLU A 219 10.670 -45.502 7.909 1.00 75.20 O ANISOU 2460 OE1 GLU A 219 12236 5613 10722 1881 -694 -877 O ATOM 2461 OE2 GLU A 219 12.834 -45.665 7.607 1.00 73.49 O ANISOU 2461 OE2 GLU A 219 11804 5288 10831 2177 -332 -1032 O ATOM 2462 N ARG A 220 9.052 -42.503 12.326 1.00 47.06 N ANISOU 2462 N ARG A 220 8078 2650 7151 1491 -1044 -274 N ATOM 2463 CA ARG A 220 7.850 -41.831 12.809 1.00 47.52 C ANISOU 2463 CA ARG A 220 8126 2809 7119 1304 -1124 -167 C ATOM 2464 C ARG A 220 8.175 -40.796 13.878 1.00 43.21 C ANISOU 2464 C ARG A 220 7405 2424 6589 1301 -1097 -59 C ATOM 2465 O ARG A 220 7.561 -39.724 13.911 1.00 41.49 O ANISOU 2465 O ARG A 220 7131 2334 6300 1205 -1072 -25 O ATOM 2466 CB ARG A 220 6.848 -42.852 13.338 1.00 55.01 C ANISOU 2466 CB ARG A 220 9184 3637 8080 1162 -1270 -75 C ATOM 2467 CG ARG A 220 6.102 -43.584 12.239 1.00 67.91 C ANISOU 2467 CG ARG A 220 10988 5140 9676 1101 -1337 -170 C ATOM 2468 CD ARG A 220 5.171 -44.650 12.806 1.00 78.36 C ANISOU 2468 CD ARG A 220 12393 6325 11057 961 -1468 -78 C ATOM 2469 NE ARG A 220 4.597 -45.492 11.758 1.00 84.98 N ANISOU 2469 NE ARG A 220 13394 7015 11878 921 -1562 -177 N ATOM 2470 CZ ARG A 220 3.865 -46.578 11.988 1.00 89.57 C ANISOU 2470 CZ ARG A 220 14063 7440 12529 816 -1678 -130 C ATOM 2471 NH1 ARG A 220 3.614 -46.959 13.234 1.00 91.36 N ANISOU 2471 NH1 ARG A 220 14247 7632 12835 737 -1685 18 N ATOM 2472 NH2 ARG A 220 3.387 -47.286 10.973 1.00 91.91 N ANISOU 2472 NH2 ARG A 220 14512 7604 12807 787 -1784 -231 N ATOM 2473 N ALA A 221 9.126 -41.098 14.764 1.00 44.04 N ANISOU 2473 N ALA A 221 7430 2516 6786 1405 -1123 -6 N ATOM 2474 CA ALA A 221 9.547 -40.118 15.762 1.00 42.66 C ANISOU 2474 CA ALA A 221 7108 2486 6616 1413 -1124 84 C ATOM 2475 C ALA A 221 10.129 -38.878 15.094 1.00 41.32 C ANISOU 2475 C ALA A 221 6791 2451 6456 1491 -979 -4 C ATOM 2476 O ALA A 221 9.793 -37.742 15.456 1.00 40.02 O ANISOU 2476 O ALA A 221 6548 2433 6225 1419 -959 52 O ATOM 2477 CB ALA A 221 10.568 -40.746 16.715 1.00 44.41 C ANISOU 2477 CB ALA A 221 7290 2644 6941 1524 -1220 135 C ATOM 2478 N ARG A 222 11.003 -39.085 14.105 1.00 42.61 N ANISOU 2478 N ARG A 222 6926 2555 6710 1637 -851 -143 N ATOM 2479 CA ARG A 222 11.579 -37.978 13.351 1.00 42.92 C ANISOU 2479 CA ARG A 222 6848 2693 6768 1709 -664 -240 C ATOM 2480 C ARG A 222 10.496 -37.165 12.655 1.00 41.00 C ANISOU 2480 C ARG A 222 6705 2531 6341 1580 -634 -263 C ATOM 2481 O ARG A 222 10.535 -35.928 12.657 1.00 39.52 O ANISOU 2481 O ARG A 222 6416 2486 6115 1564 -561 -257 O ATOM 2482 CB ARG A 222 12.575 -38.530 12.336 1.00 48.55 C ANISOU 2482 CB ARG A 222 7558 3278 7610 1868 -482 -393 C ATOM 2483 CG ARG A 222 13.261 -37.515 11.457 1.00 51.71 C ANISOU 2483 CG ARG A 222 7852 3740 8054 1943 -225 -511 C ATOM 2484 CD ARG A 222 14.084 -38.237 10.397 1.00 58.51 C ANISOU 2484 CD ARG A 222 8749 4433 9048 2072 -12 -676 C ATOM 2485 NE ARG A 222 14.964 -39.251 10.978 1.00 65.42 N ANISOU 2485 NE ARG A 222 9543 5183 10130 2206 -38 -643 N ATOM 2486 CZ ARG A 222 15.509 -40.251 10.290 1.00 74.42 C ANISOU 2486 CZ ARG A 222 10748 6133 11394 2313 92 -756 C ATOM 2487 NH1 ARG A 222 15.261 -40.386 8.992 1.00 78.38 N ANISOU 2487 NH1 ARG A 222 11393 6555 11832 2286 227 -930 N ATOM 2488 NH2 ARG A 222 16.299 -41.124 10.897 1.00 78.20 N ANISOU 2488 NH2 ARG A 222 11169 6510 12034 2449 39 -711 N ATOM 2489 N SER A 223 9.521 -37.849 12.052 1.00 42.44 N ANISOU 2489 N SER A 223 7089 2618 6419 1486 -707 -290 N ATOM 2490 CA SER A 223 8.456 -37.161 11.335 1.00 39.22 C ANISOU 2490 CA SER A 223 6788 2263 5849 1361 -723 -316 C ATOM 2491 C SER A 223 7.602 -36.322 12.279 1.00 39.76 C ANISOU 2491 C SER A 223 6760 2458 5888 1220 -811 -177 C ATOM 2492 O SER A 223 7.195 -35.205 11.934 1.00 39.68 O ANISOU 2492 O SER A 223 6728 2554 5793 1168 -774 -189 O ATOM 2493 CB SER A 223 7.599 -38.180 10.587 1.00 48.57 C ANISOU 2493 CB SER A 223 8191 3299 6963 1284 -832 -366 C ATOM 2494 OG SER A 223 6.364 -37.596 10.208 1.00 50.76 O ANISOU 2494 OG SER A 223 8538 3619 7131 1130 -929 -350 O ATOM 2495 N THR A 224 7.317 -36.840 13.474 1.00 37.08 N ANISOU 2495 N THR A 224 6380 2098 5612 1157 -914 -46 N ATOM 2496 CA THR A 224 6.556 -36.067 14.447 1.00 39.12 C ANISOU 2496 CA THR A 224 6559 2459 5847 1024 -950 88 C ATOM 2497 C THR A 224 7.317 -34.817 14.875 1.00 34.76 C ANISOU 2497 C THR A 224 5850 2070 5289 1097 -869 107 C ATOM 2498 O THR A 224 6.739 -33.731 14.956 1.00 32.22 O ANISOU 2498 O THR A 224 5474 1858 4910 1015 -845 143 O ATOM 2499 CB THR A 224 6.214 -36.942 15.652 1.00 42.89 C ANISOU 2499 CB THR A 224 7074 2855 6367 949 -1032 221 C ATOM 2500 OG1 THR A 224 5.338 -37.992 15.234 1.00 46.00 O ANISOU 2500 OG1 THR A 224 7594 3099 6784 855 -1102 207 O ATOM 2501 CG2 THR A 224 5.530 -36.130 16.735 1.00 43.90 C ANISOU 2501 CG2 THR A 224 7143 3074 6462 821 -1015 360 C ATOM 2502 N LEU A 225 8.624 -34.943 15.123 1.00 37.72 N ANISOU 2502 N LEU A 225 6134 2451 5745 1250 -834 79 N ATOM 2503 CA LEU A 225 9.426 -33.788 15.528 1.00 36.03 C ANISOU 2503 CA LEU A 225 5745 2382 5561 1319 -774 90 C ATOM 2504 C LEU A 225 9.499 -32.736 14.425 1.00 36.89 C ANISOU 2504 C LEU A 225 5818 2573 5624 1350 -630 -18 C ATOM 2505 O LEU A 225 9.434 -31.530 14.700 1.00 36.06 O ANISOU 2505 O LEU A 225 5614 2607 5480 1321 -598 16 O ATOM 2506 CB LEU A 225 10.831 -34.243 15.918 1.00 42.10 C ANISOU 2506 CB LEU A 225 6400 3112 6484 1475 -781 67 C ATOM 2507 CG LEU A 225 11.061 -34.565 17.393 1.00 48.12 C ANISOU 2507 CG LEU A 225 7154 3869 7261 1454 -942 196 C ATOM 2508 CD1 LEU A 225 12.368 -35.311 17.589 1.00 51.25 C ANISOU 2508 CD1 LEU A 225 7469 4176 7829 1609 -993 154 C ATOM 2509 CD2 LEU A 225 11.058 -33.266 18.179 1.00 49.97 C ANISOU 2509 CD2 LEU A 225 7288 4262 7435 1403 -957 270 C ATOM 2510 N GLN A 226 9.646 -33.170 13.174 1.00 37.09 N ANISOU 2510 N GLN A 226 5951 2508 5634 1407 -535 -152 N ATOM 2511 CA GLN A 226 9.724 -32.217 12.072 1.00 38.38 C ANISOU 2511 CA GLN A 226 6147 2730 5706 1430 -379 -260 C ATOM 2512 C GLN A 226 8.400 -31.486 11.876 1.00 37.46 C ANISOU 2512 C GLN A 226 6130 2676 5428 1278 -459 -218 C ATOM 2513 O GLN A 226 8.397 -30.307 11.508 1.00 34.21 O ANISOU 2513 O GLN A 226 5695 2370 4935 1274 -369 -244 O ATOM 2514 CB GLN A 226 10.173 -32.933 10.794 1.00 43.77 C ANISOU 2514 CB GLN A 226 6978 3282 6370 1512 -247 -413 C ATOM 2515 CG GLN A 226 11.632 -33.398 10.866 1.00 53.74 C ANISOU 2515 CG GLN A 226 8079 4483 7857 1675 -106 -477 C ATOM 2516 CD GLN A 226 12.023 -34.419 9.793 1.00 65.73 C ANISOU 2516 CD GLN A 226 9748 5834 9392 1750 9 -619 C ATOM 2517 OE1 GLN A 226 11.177 -34.934 9.058 1.00 69.21 O ANISOU 2517 OE1 GLN A 226 10444 6199 9652 1679 -56 -656 O ATOM 2518 NE2 GLN A 226 13.318 -34.717 9.712 1.00 70.68 N ANISOU 2518 NE2 GLN A 226 10202 6392 10262 1891 171 -701 N ATOM 2519 N LYS A 227 7.272 -32.151 12.146 1.00 39.84 N ANISOU 2519 N LYS A 227 6522 2906 5710 1146 -622 -149 N ATOM 2520 CA LYS A 227 5.984 -31.460 12.114 1.00 36.90 C ANISOU 2520 CA LYS A 227 6172 2578 5269 989 -712 -97 C ATOM 2521 C LYS A 227 5.874 -30.427 13.230 1.00 32.71 C ANISOU 2521 C LYS A 227 5469 2190 4770 944 -702 23 C ATOM 2522 O LYS A 227 5.284 -29.360 13.032 1.00 32.35 O ANISOU 2522 O LYS A 227 5365 2266 4661 857 -681 34 O ATOM 2523 CB LYS A 227 4.839 -32.463 12.209 1.00 38.51 C ANISOU 2523 CB LYS A 227 6457 2658 5518 851 -866 -53 C ATOM 2524 CG LYS A 227 4.672 -33.323 10.977 1.00 46.29 C ANISOU 2524 CG LYS A 227 7640 3506 6442 865 -920 -175 C ATOM 2525 CD LYS A 227 3.536 -34.309 11.159 1.00 53.84 C ANISOU 2525 CD LYS A 227 8637 4339 7482 724 -1085 -127 C ATOM 2526 CE LYS A 227 3.460 -35.275 9.986 1.00 61.71 C ANISOU 2526 CE LYS A 227 9845 5190 8412 750 -1163 -247 C ATOM 2527 NZ LYS A 227 2.371 -36.275 10.170 1.00 67.20 N ANISOU 2527 NZ LYS A 227 10560 5755 9218 613 -1333 -203 N ATOM 2528 N GLU A 228 6.419 -30.727 14.415 1.00 32.85 N ANISOU 2528 N GLU A 228 5389 2231 4862 977 -710 116 N ATOM 2529 CA GLU A 228 6.423 -29.742 15.497 1.00 30.62 C ANISOU 2529 CA GLU A 228 4972 2091 4572 936 -694 226 C ATOM 2530 C GLU A 228 7.328 -28.558 15.170 1.00 30.14 C ANISOU 2530 C GLU A 228 4768 2203 4482 1019 -572 162 C ATOM 2531 O GLU A 228 6.980 -27.406 15.467 1.00 30.09 O ANISOU 2531 O GLU A 228 4660 2357 4416 937 -526 207 O ATOM 2532 CB GLU A 228 6.846 -30.394 16.820 1.00 37.08 C ANISOU 2532 CB GLU A 228 5782 2872 5436 950 -755 333 C ATOM 2533 CG GLU A 228 5.747 -31.220 17.480 1.00 43.87 C ANISOU 2533 CG GLU A 228 6751 3624 6294 802 -807 438 C ATOM 2534 CD GLU A 228 6.161 -31.819 18.824 1.00 47.31 C ANISOU 2534 CD GLU A 228 7239 4020 6718 809 -852 546 C ATOM 2535 OE1 GLU A 228 6.749 -32.923 18.836 1.00 45.39 O ANISOU 2535 OE1 GLU A 228 7053 3672 6521 884 -914 521 O ATOM 2536 OE2 GLU A 228 5.879 -31.189 19.871 1.00 48.72 O ANISOU 2536 OE2 GLU A 228 7426 4258 6828 737 -826 653 O ATOM 2537 N VAL A 229 8.494 -28.812 14.566 1.00 30.72 N ANISOU 2537 N VAL A 229 4823 2229 4619 1178 -498 56 N ATOM 2538 CA VAL A 229 9.328 -27.707 14.095 1.00 30.10 C ANISOU 2538 CA VAL A 229 4608 2286 4542 1242 -339 -15 C ATOM 2539 C VAL A 229 8.553 -26.847 13.103 1.00 30.46 C ANISOU 2539 C VAL A 229 4732 2414 4426 1144 -256 -62 C ATOM 2540 O VAL A 229 8.551 -25.614 13.193 1.00 28.23 O ANISOU 2540 O VAL A 229 4340 2293 4094 1095 -188 -40 O ATOM 2541 CB VAL A 229 10.634 -28.225 13.468 1.00 32.06 C ANISOU 2541 CB VAL A 229 4825 2428 4930 1425 -218 -138 C ATOM 2542 CG1 VAL A 229 11.435 -27.051 12.912 1.00 29.94 C ANISOU 2542 CG1 VAL A 229 4414 2280 4683 1466 -3 -211 C ATOM 2543 CG2 VAL A 229 11.461 -28.981 14.488 1.00 33.40 C ANISOU 2543 CG2 VAL A 229 4869 2536 5286 1503 -329 -84 C ATOM 2544 N HIS A 230 7.883 -27.490 12.139 1.00 30.78 N ANISOU 2544 N HIS A 230 4987 2324 4383 1117 -291 -128 N ATOM 2545 CA HIS A 230 7.154 -26.743 11.122 1.00 33.08 C ANISOU 2545 CA HIS A 230 5406 2648 4516 1036 -271 -180 C ATOM 2546 C HIS A 230 6.041 -25.912 11.746 1.00 30.82 C ANISOU 2546 C HIS A 230 5011 2484 4215 880 -378 -75 C ATOM 2547 O HIS A 230 5.855 -24.740 11.395 1.00 28.48 O ANISOU 2547 O HIS A 230 4684 2305 3832 836 -326 -83 O ATOM 2548 CB HIS A 230 6.590 -27.704 10.073 1.00 40.74 C ANISOU 2548 CB HIS A 230 6659 3411 5408 1034 -362 -268 C ATOM 2549 CG HIS A 230 5.988 -27.014 8.890 1.00 50.48 C ANISOU 2549 CG HIS A 230 8097 4625 6457 978 -379 -339 C ATOM 2550 ND1 HIS A 230 4.649 -26.695 8.813 1.00 53.60 N ANISOU 2550 ND1 HIS A 230 8520 5011 6835 834 -590 -296 N ATOM 2551 CD2 HIS A 230 6.547 -26.571 7.738 1.00 55.49 C ANISOU 2551 CD2 HIS A 230 8938 5224 6922 1047 -217 -451 C ATOM 2552 CE1 HIS A 230 4.409 -26.088 7.663 1.00 56.75 C ANISOU 2552 CE1 HIS A 230 9145 5366 7052 824 -607 -377 C ATOM 2553 NE2 HIS A 230 5.545 -25.995 6.995 1.00 58.00 N ANISOU 2553 NE2 HIS A 230 9442 5507 7087 948 -368 -467 N ATOM 2554 N ALA A 231 5.302 -26.500 12.689 1.00 32.10 N ANISOU 2554 N ALA A 231 5120 2605 4472 797 -503 25 N ATOM 2555 CA ALA A 231 4.220 -25.779 13.347 1.00 30.62 C ANISOU 2555 CA ALA A 231 4817 2508 4311 652 -555 120 C ATOM 2556 C ALA A 231 4.752 -24.618 14.179 1.00 28.13 C ANISOU 2556 C ALA A 231 4327 2386 3974 662 -449 180 C ATOM 2557 O ALA A 231 4.160 -23.532 14.190 1.00 25.47 O ANISOU 2557 O ALA A 231 3912 2160 3605 583 -432 201 O ATOM 2558 CB ALA A 231 3.409 -26.744 14.213 1.00 29.16 C ANISOU 2558 CB ALA A 231 4631 2205 4244 560 -647 214 C ATOM 2559 N ALA A 232 5.879 -24.823 14.877 1.00 30.39 N ANISOU 2559 N ALA A 232 4554 2698 4295 763 -403 202 N ATOM 2560 CA ALA A 232 6.464 -23.742 15.666 1.00 26.67 C ANISOU 2560 CA ALA A 232 3935 2386 3814 777 -343 249 C ATOM 2561 C ALA A 232 6.975 -22.628 14.767 1.00 26.70 C ANISOU 2561 C ALA A 232 3884 2500 3761 811 -228 166 C ATOM 2562 O ALA A 232 6.892 -21.448 15.128 1.00 26.65 O ANISOU 2562 O ALA A 232 3776 2632 3717 763 -190 200 O ATOM 2563 CB ALA A 232 7.590 -24.271 16.553 1.00 25.47 C ANISOU 2563 CB ALA A 232 3740 2193 3746 886 -384 281 C ATOM 2564 N ALYS A 233 7.497 -22.972 13.586 0.50 25.60 N ANISOU 2564 N ALYS A 233 3840 2285 3602 891 -152 56 N ATOM 2565 N BLYS A 233 7.514 -22.979 13.594 0.50 25.58 N ANISOU 2565 N BLYS A 233 3836 2282 3601 893 -151 56 N ATOM 2566 CA ALYS A 233 7.928 -21.930 12.659 0.50 25.45 C ANISOU 2566 CA ALYS A 233 3826 2340 3502 909 -5 -18 C ATOM 2567 CA BLYS A 233 7.925 -21.951 12.643 0.50 25.50 C ANISOU 2567 CA BLYS A 233 3836 2343 3508 910 -5 -20 C ATOM 2568 C ALYS A 233 6.744 -21.102 12.172 0.50 24.85 C ANISOU 2568 C ALYS A 233 3830 2312 3299 790 -62 -6 C ATOM 2569 C BLYS A 233 6.737 -21.105 12.206 0.50 24.80 C ANISOU 2569 C BLYS A 233 3820 2308 3296 789 -65 -4 C ATOM 2570 O ALYS A 233 6.847 -19.878 12.036 0.50 23.77 O ANISOU 2570 O ALYS A 233 3636 2290 3104 761 11 -4 O ATOM 2571 O BLYS A 233 6.832 -19.875 12.134 0.50 23.73 O ANISOU 2571 O BLYS A 233 3618 2291 3107 758 5 3 O ATOM 2572 CB ALYS A 233 8.685 -22.549 11.483 0.50 26.94 C ANISOU 2572 CB ALYS A 233 4163 2399 3674 1017 132 -142 C ATOM 2573 CB BLYS A 233 8.602 -22.588 11.427 0.50 26.86 C ANISOU 2573 CB BLYS A 233 4171 2382 3654 1013 124 -144 C ATOM 2574 CG ALYS A 233 10.072 -23.046 11.868 0.50 28.56 C ANISOU 2574 CG ALYS A 233 4217 2565 4069 1155 233 -174 C ATOM 2575 CG BLYS A 233 9.063 -21.576 10.388 0.50 25.87 C ANISOU 2575 CG BLYS A 233 4118 2295 3417 1025 326 -220 C ATOM 2576 CD ALYS A 233 10.864 -23.537 10.676 0.50 31.47 C ANISOU 2576 CD ALYS A 233 4718 2798 4443 1268 444 -309 C ATOM 2577 CD BLYS A 233 9.770 -22.242 9.195 0.50 28.70 C ANISOU 2577 CD BLYS A 233 4685 2490 3730 1131 516 -350 C ATOM 2578 CE ALYS A 233 12.262 -23.989 11.094 0.50 30.40 C ANISOU 2578 CE ALYS A 233 4364 2605 4580 1414 545 -349 C ATOM 2579 CE BLYS A 233 10.156 -21.198 8.152 0.50 28.17 C ANISOU 2579 CE BLYS A 233 4753 2435 3514 1126 753 -415 C ATOM 2580 NZ ALYS A 233 12.963 -24.650 9.954 0.50 34.21 N ANISOU 2580 NZ ALYS A 233 4975 2934 5088 1516 773 -489 N ATOM 2581 NZ BLYS A 233 10.665 -21.789 6.884 0.50 33.33 N ANISOU 2581 NZ BLYS A 233 5701 2904 4057 1209 970 -543 N ATOM 2582 N SER A 234 5.607 -21.750 11.913 1.00 25.43 N ANISOU 2582 N SER A 234 4024 2280 3358 719 -213 0 N ATOM 2583 CA SER A 234 4.417 -21.014 11.501 1.00 25.67 C ANISOU 2583 CA SER A 234 4095 2323 3335 611 -320 9 C ATOM 2584 C SER A 234 3.969 -20.037 12.587 1.00 25.74 C ANISOU 2584 C SER A 234 3892 2482 3407 534 -315 105 C ATOM 2585 O SER A 234 3.719 -18.859 12.313 1.00 24.84 O ANISOU 2585 O SER A 234 3750 2454 3235 498 -301 101 O ATOM 2586 CB SER A 234 3.305 -21.998 11.149 1.00 26.76 C ANISOU 2586 CB SER A 234 4351 2290 3527 547 -512 -1 C ATOM 2587 OG SER A 234 3.724 -22.827 10.075 1.00 28.99 O ANISOU 2587 OG SER A 234 4880 2419 3715 624 -521 -103 O ATOM 2588 N ALA A 235 3.893 -20.507 13.836 1.00 24.08 N ANISOU 2588 N ALA A 235 3565 2288 3297 512 -319 191 N ATOM 2589 CA ALA A 235 3.549 -19.629 14.948 1.00 25.36 C ANISOU 2589 CA ALA A 235 3577 2570 3489 448 -280 277 C ATOM 2590 C ALA A 235 4.559 -18.489 15.111 1.00 23.79 C ANISOU 2590 C ALA A 235 3299 2518 3221 503 -179 268 C ATOM 2591 O ALA A 235 4.171 -17.333 15.351 1.00 20.00 O ANISOU 2591 O ALA A 235 2743 2139 2717 451 -154 291 O ATOM 2592 CB ALA A 235 3.442 -20.453 16.235 1.00 23.46 C ANISOU 2592 CB ALA A 235 3316 2280 3319 426 -283 370 C ATOM 2593 N ALA A 236 5.862 -18.795 15.011 1.00 23.91 N ANISOU 2593 N ALA A 236 3312 2533 3239 609 -121 230 N ATOM 2594 CA ALA A 236 6.873 -17.749 15.162 1.00 21.08 C ANISOU 2594 CA ALA A 236 2846 2290 2874 654 -29 216 C ATOM 2595 C ALA A 236 6.766 -16.701 14.056 1.00 20.48 C ANISOU 2595 C ALA A 236 2814 2263 2706 629 50 157 C ATOM 2596 O ALA A 236 7.027 -15.515 14.292 1.00 21.43 O ANISOU 2596 O ALA A 236 2844 2490 2807 608 103 171 O ATOM 2597 CB ALA A 236 8.278 -18.359 15.183 1.00 20.38 C ANISOU 2597 CB ALA A 236 2705 2152 2885 775 17 174 C ATOM 2598 N ILE A 237 6.403 -17.117 12.840 1.00 20.14 N ANISOU 2598 N ILE A 237 2944 2119 2588 633 47 89 N ATOM 2599 CA ILE A 237 6.215 -16.147 11.759 1.00 20.77 C ANISOU 2599 CA ILE A 237 3144 2210 2539 606 95 40 C ATOM 2600 C ILE A 237 5.112 -15.163 12.126 1.00 21.43 C ANISOU 2600 C ILE A 237 3164 2365 2612 510 -13 96 C ATOM 2601 O ILE A 237 5.245 -13.951 11.911 1.00 21.05 O ANISOU 2601 O ILE A 237 3103 2393 2502 490 43 94 O ATOM 2602 CB ILE A 237 5.910 -16.869 10.434 1.00 23.16 C ANISOU 2602 CB ILE A 237 3720 2349 2729 626 61 -41 C ATOM 2603 CG1 ILE A 237 7.179 -17.533 9.875 1.00 26.11 C ANISOU 2603 CG1 ILE A 237 4174 2648 3097 735 255 -118 C ATOM 2604 CG2 ILE A 237 5.262 -15.907 9.417 1.00 21.56 C ANISOU 2604 CG2 ILE A 237 3709 2117 2367 574 6 -70 C ATOM 2605 CD1 ILE A 237 6.893 -18.613 8.810 1.00 28.42 C ANISOU 2605 CD1 ILE A 237 4762 2750 3287 770 210 -199 C ATOM 2606 N AILE A 238 4.011 -15.655 12.702 0.53 20.58 N ANISOU 2606 N AILE A 238 3006 2221 2592 450 -149 144 N ATOM 2607 N BILE A 238 3.998 -15.687 12.662 0.47 20.60 N ANISOU 2607 N BILE A 238 3015 2218 2594 450 -152 142 N ATOM 2608 CA AILE A 238 2.916 -14.754 13.055 0.53 19.81 C ANISOU 2608 CA AILE A 238 2818 2168 2542 366 -225 185 C ATOM 2609 CA BILE A 238 2.881 -14.864 13.126 0.47 20.07 C ANISOU 2609 CA BILE A 238 2845 2195 2586 365 -229 189 C ATOM 2610 C AILE A 238 3.333 -13.799 14.171 0.53 19.00 C ANISOU 2610 C AILE A 238 2555 2212 2452 359 -123 242 C ATOM 2611 C BILE A 238 3.361 -13.831 14.139 0.47 18.99 C ANISOU 2611 C BILE A 238 2558 2208 2448 362 -123 240 C ATOM 2612 O AILE A 238 2.975 -12.614 14.153 0.53 17.93 O ANISOU 2612 O AILE A 238 2375 2140 2297 324 -122 248 O ATOM 2613 O BILE A 238 3.058 -12.636 14.031 0.47 17.98 O ANISOU 2613 O BILE A 238 2396 2142 2292 330 -121 241 O ATOM 2614 CB AILE A 238 1.667 -15.570 13.421 0.53 21.65 C ANISOU 2614 CB AILE A 238 3004 2298 2924 297 -349 218 C ATOM 2615 CB BILE A 238 1.783 -15.763 13.728 0.47 20.82 C ANISOU 2615 CB BILE A 238 2876 2201 2834 301 -324 234 C ATOM 2616 CG1AILE A 238 1.065 -16.149 12.139 0.53 22.51 C ANISOU 2616 CG1AILE A 238 3287 2245 3022 289 -519 148 C ATOM 2617 CG1BILE A 238 1.220 -16.713 12.665 0.47 22.78 C ANISOU 2617 CG1BILE A 238 3277 2278 3102 293 -479 175 C ATOM 2618 CG2AILE A 238 0.640 -14.710 14.159 0.53 20.85 C ANISOU 2618 CG2AILE A 238 2737 2242 2942 219 -356 269 C ATOM 2619 CG2BILE A 238 0.669 -14.921 14.339 0.47 21.02 C ANISOU 2619 CG2BILE A 238 2750 2259 2976 218 -344 279 C ATOM 2620 CD1AILE A 238 0.151 -17.295 12.390 0.53 21.72 C ANISOU 2620 CD1AILE A 238 3151 2008 3095 233 -636 167 C ATOM 2621 CD1BILE A 238 0.262 -16.043 11.697 0.47 21.73 C ANISOU 2621 CD1BILE A 238 3211 2069 2977 249 -652 130 C ATOM 2622 N ALA A 239 4.096 -14.287 15.156 1.00 18.47 N ANISOU 2622 N ALA A 239 2422 2181 2416 396 -63 282 N ATOM 2623 CA ALA A 239 4.600 -13.385 16.190 1.00 19.84 C ANISOU 2623 CA ALA A 239 2492 2467 2580 396 -5 326 C ATOM 2624 C ALA A 239 5.584 -12.370 15.611 1.00 19.08 C ANISOU 2624 C ALA A 239 2375 2445 2431 432 69 281 C ATOM 2625 O ALA A 239 5.560 -11.193 15.985 1.00 18.37 O ANISOU 2625 O ALA A 239 2224 2438 2318 401 91 298 O ATOM 2626 CB ALA A 239 5.264 -14.185 17.319 1.00 18.93 C ANISOU 2626 CB ALA A 239 2360 2332 2499 437 -14 375 C ATOM 2627 N GLY A 240 6.447 -12.803 14.688 1.00 17.58 N ANISOU 2627 N GLY A 240 2242 2207 2231 493 132 219 N ATOM 2628 CA GLY A 240 7.379 -11.869 14.070 1.00 17.74 C ANISOU 2628 CA GLY A 240 2246 2269 2224 514 255 175 C ATOM 2629 C GLY A 240 6.679 -10.821 13.221 1.00 18.28 C ANISOU 2629 C GLY A 240 2423 2347 2175 456 257 160 C ATOM 2630 O GLY A 240 7.098 -9.661 13.175 1.00 18.52 O ANISOU 2630 O GLY A 240 2413 2441 2183 436 330 161 O ATOM 2631 N LEU A 241 5.594 -11.208 12.547 1.00 16.54 N ANISOU 2631 N LEU A 241 2345 2044 1894 428 149 146 N ATOM 2632 CA LEU A 241 4.853 -10.244 11.736 1.00 16.44 C ANISOU 2632 CA LEU A 241 2458 2007 1782 382 86 132 C ATOM 2633 C LEU A 241 4.095 -9.246 12.599 1.00 15.46 C ANISOU 2633 C LEU A 241 2185 1967 1721 328 17 185 C ATOM 2634 O LEU A 241 3.945 -8.079 12.215 1.00 15.24 O ANISOU 2634 O LEU A 241 2201 1958 1631 304 11 182 O ATOM 2635 CB LEU A 241 3.884 -10.975 10.808 1.00 21.03 C ANISOU 2635 CB LEU A 241 3231 2441 2317 372 -75 97 C ATOM 2636 CG LEU A 241 4.556 -11.690 9.628 1.00 26.19 C ANISOU 2636 CG LEU A 241 4140 2976 2835 425 5 25 C ATOM 2637 CD1 LEU A 241 3.538 -12.537 8.897 1.00 27.30 C ANISOU 2637 CD1 LEU A 241 4473 2953 2945 413 -212 -10 C ATOM 2638 CD2 LEU A 241 5.211 -10.675 8.669 1.00 29.40 C ANISOU 2638 CD2 LEU A 241 4741 3364 3066 430 151 -8 C ATOM 2639 N PHE A 242 3.617 -9.672 13.763 1.00 14.64 N ANISOU 2639 N PHE A 242 1932 1897 1734 311 -18 233 N ATOM 2640 CA PHE A 242 3.060 -8.712 14.710 1.00 16.76 C ANISOU 2640 CA PHE A 242 2073 2239 2056 270 -20 276 C ATOM 2641 C PHE A 242 4.105 -7.661 15.078 1.00 14.85 C ANISOU 2641 C PHE A 242 1785 2099 1758 284 78 281 C ATOM 2642 O PHE A 242 3.830 -6.453 15.060 1.00 14.13 O ANISOU 2642 O PHE A 242 1680 2045 1644 256 74 283 O ATOM 2643 CB PHE A 242 2.544 -9.437 15.959 1.00 17.67 C ANISOU 2643 CB PHE A 242 2092 2350 2273 250 -11 328 C ATOM 2644 CG PHE A 242 1.960 -8.504 17.006 1.00 16.25 C ANISOU 2644 CG PHE A 242 1818 2222 2133 212 36 366 C ATOM 2645 CD1 PHE A 242 0.590 -8.281 17.071 1.00 14.81 C ANISOU 2645 CD1 PHE A 242 1565 1980 2081 164 8 370 C ATOM 2646 CD2 PHE A 242 2.780 -7.857 17.907 1.00 17.71 C ANISOU 2646 CD2 PHE A 242 1988 2493 2249 228 103 389 C ATOM 2647 CE1 PHE A 242 0.050 -7.421 18.029 1.00 16.19 C ANISOU 2647 CE1 PHE A 242 1662 2185 2304 138 96 394 C ATOM 2648 CE2 PHE A 242 2.249 -6.983 18.876 1.00 17.74 C ANISOU 2648 CE2 PHE A 242 1954 2526 2260 199 159 414 C ATOM 2649 CZ PHE A 242 0.892 -6.775 18.934 1.00 16.65 C ANISOU 2649 CZ PHE A 242 1754 2333 2239 157 180 416 C ATOM 2650 N ALA A 243 5.320 -8.106 15.395 1.00 13.39 N ANISOU 2650 N ALA A 243 1566 1942 1581 327 149 279 N ATOM 2651 CA ALA A 243 6.390 -7.170 15.746 1.00 16.35 C ANISOU 2651 CA ALA A 243 1867 2387 1960 334 217 278 C ATOM 2652 C ALA A 243 6.737 -6.243 14.574 1.00 17.01 C ANISOU 2652 C ALA A 243 2026 2462 1976 319 297 239 C ATOM 2653 O ALA A 243 6.900 -5.031 14.757 1.00 17.67 O ANISOU 2653 O ALA A 243 2074 2593 2045 286 318 248 O ATOM 2654 CB ALA A 243 7.629 -7.953 16.197 1.00 16.46 C ANISOU 2654 CB ALA A 243 1803 2391 2061 392 243 272 C ATOM 2655 N ALEU A 244 6.853 -6.801 13.365 0.52 17.25 N ANISOU 2655 N ALEU A 244 2199 2411 1946 339 350 197 N ATOM 2656 N BLEU A 244 6.849 -6.792 13.364 0.48 17.27 N ANISOU 2656 N BLEU A 244 2201 2413 1947 338 350 197 N ATOM 2657 CA ALEU A 244 7.188 -5.991 12.196 0.52 18.17 C ANISOU 2657 CA ALEU A 244 2465 2484 1955 320 456 165 C ATOM 2658 CA BLEU A 244 7.203 -5.958 12.220 0.48 18.09 C ANISOU 2658 CA BLEU A 244 2450 2476 1947 319 457 166 C ATOM 2659 C ALEU A 244 6.134 -4.919 11.935 0.52 17.36 C ANISOU 2659 C ALEU A 244 2454 2377 1766 270 340 184 C ATOM 2660 C BLEU A 244 6.133 -4.908 11.934 0.48 17.33 C ANISOU 2660 C BLEU A 244 2450 2372 1761 270 340 184 C ATOM 2661 O ALEU A 244 6.471 -3.788 11.567 0.52 16.30 O ANISOU 2661 O ALEU A 244 2375 2247 1573 239 410 185 O ATOM 2662 O BLEU A 244 6.457 -3.779 11.549 0.48 16.40 O ANISOU 2662 O BLEU A 244 2391 2257 1582 239 408 185 O ATOM 2663 CB ALEU A 244 7.348 -6.885 10.959 0.52 19.12 C ANISOU 2663 CB ALEU A 244 2803 2483 1980 354 528 112 C ATOM 2664 CB BLEU A 244 7.442 -6.826 10.982 0.48 19.22 C ANISOU 2664 CB BLEU A 244 2804 2500 1998 354 542 113 C ATOM 2665 CG ALEU A 244 7.605 -6.210 9.604 0.52 20.25 C ANISOU 2665 CG ALEU A 244 3215 2532 1948 334 658 79 C ATOM 2666 CG BLEU A 244 8.847 -7.410 10.799 0.48 21.39 C ANISOU 2666 CG BLEU A 244 3017 2748 2363 406 762 71 C ATOM 2667 CD1ALEU A 244 8.888 -5.373 9.643 0.52 22.23 C ANISOU 2667 CD1ALEU A 244 3361 2818 2268 318 902 75 C ATOM 2668 CD1BLEU A 244 8.964 -8.068 9.436 0.48 21.42 C ANISOU 2668 CD1BLEU A 244 3306 2609 2224 437 884 9 C ATOM 2669 CD2ALEU A 244 7.665 -7.230 8.455 0.52 18.84 C ANISOU 2669 CD2ALEU A 244 3315 2206 1639 375 721 20 C ATOM 2670 CD2BLEU A 244 9.916 -6.323 10.950 0.48 24.30 C ANISOU 2670 CD2BLEU A 244 3250 3160 2821 379 934 73 C ATOM 2671 N CYS A 245 4.853 -5.262 12.097 1.00 15.27 N ANISOU 2671 N CYS A 245 2197 2082 1523 262 162 196 N ATOM 2672 CA CYS A 245 3.774 -4.320 11.792 1.00 15.76 C ANISOU 2672 CA CYS A 245 2322 2106 1559 229 20 204 C ATOM 2673 C CYS A 245 3.601 -3.237 12.861 1.00 16.17 C ANISOU 2673 C CYS A 245 2199 2255 1689 205 27 238 C ATOM 2674 O CYS A 245 3.165 -2.124 12.542 1.00 14.84 O ANISOU 2674 O CYS A 245 2086 2063 1488 185 -33 239 O ATOM 2675 CB CYS A 245 2.456 -5.075 11.623 1.00 17.09 C ANISOU 2675 CB CYS A 245 2505 2183 1807 227 -176 196 C ATOM 2676 SG CYS A 245 2.378 -6.057 10.086 1.00 22.00 S ANISOU 2676 SG CYS A 245 3437 2633 2290 249 -270 142 S ATOM 2677 N TRP A 246 3.902 -3.541 14.127 1.00 14.62 N ANISOU 2677 N TRP A 246 1828 2145 1581 211 84 263 N ATOM 2678 CA TRP A 246 3.684 -2.584 15.213 1.00 15.08 C ANISOU 2678 CA TRP A 246 1771 2271 1686 193 92 288 C ATOM 2679 C TRP A 246 4.925 -1.782 15.585 1.00 15.54 C ANISOU 2679 C TRP A 246 1793 2397 1714 186 181 291 C ATOM 2680 O TRP A 246 4.784 -0.686 16.142 1.00 14.76 O ANISOU 2680 O TRP A 246 1661 2331 1618 166 172 299 O ATOM 2681 CB TRP A 246 3.178 -3.292 16.485 1.00 12.58 C ANISOU 2681 CB TRP A 246 1350 1974 1454 197 96 317 C ATOM 2682 CG TRP A 246 1.719 -3.633 16.392 1.00 13.08 C ANISOU 2682 CG TRP A 246 1382 1964 1625 182 26 316 C ATOM 2683 CD1 TRP A 246 1.177 -4.834 16.034 1.00 14.56 C ANISOU 2683 CD1 TRP A 246 1576 2076 1881 181 -28 313 C ATOM 2684 CD2 TRP A 246 0.626 -2.750 16.659 1.00 11.87 C ANISOU 2684 CD2 TRP A 246 1159 1781 1570 165 -1 312 C ATOM 2685 NE1 TRP A 246 -0.205 -4.745 16.047 1.00 15.98 N ANISOU 2685 NE1 TRP A 246 1673 2176 2223 156 -97 308 N ATOM 2686 CE2 TRP A 246 -0.564 -3.473 16.424 1.00 16.20 C ANISOU 2686 CE2 TRP A 246 1643 2229 2283 152 -74 305 C ATOM 2687 CE3 TRP A 246 0.537 -1.402 17.049 1.00 12.41 C ANISOU 2687 CE3 TRP A 246 1205 1881 1630 163 26 307 C ATOM 2688 CZ2 TRP A 246 -1.832 -2.907 16.599 1.00 17.94 C ANISOU 2688 CZ2 TRP A 246 1742 2376 2699 140 -109 291 C ATOM 2689 CZ3 TRP A 246 -0.730 -0.829 17.207 1.00 13.07 C ANISOU 2689 CZ3 TRP A 246 1196 1897 1873 160 -4 293 C ATOM 2690 CH2 TRP A 246 -1.896 -1.579 16.972 1.00 17.48 C ANISOU 2690 CH2 TRP A 246 1658 2351 2631 150 -67 283 C ATOM 2691 N LEU A 247 6.119 -2.306 15.327 1.00 15.40 N ANISOU 2691 N LEU A 247 1765 2384 1702 204 263 278 N ATOM 2692 CA LEU A 247 7.327 -1.600 15.746 1.00 16.70 C ANISOU 2692 CA LEU A 247 1843 2589 1915 192 328 276 C ATOM 2693 C LEU A 247 7.461 -0.206 15.148 1.00 16.57 C ANISOU 2693 C LEU A 247 1885 2562 1850 145 374 271 C ATOM 2694 O LEU A 247 7.888 0.703 15.884 1.00 17.00 O ANISOU 2694 O LEU A 247 1860 2652 1948 120 360 278 O ATOM 2695 CB LEU A 247 8.573 -2.444 15.424 1.00 19.24 C ANISOU 2695 CB LEU A 247 2105 2885 2321 225 423 252 C ATOM 2696 CG LEU A 247 8.974 -3.449 16.515 1.00 23.77 C ANISOU 2696 CG LEU A 247 2569 3471 2993 271 345 265 C ATOM 2697 CD1 LEU A 247 10.142 -4.370 16.019 1.00 25.96 C ANISOU 2697 CD1 LEU A 247 2771 3694 3397 321 438 229 C ATOM 2698 CD2 LEU A 247 9.360 -2.729 17.817 1.00 22.32 C ANISOU 2698 CD2 LEU A 247 2299 3323 2858 258 245 286 C ATOM 2699 N PRO A 248 7.144 0.044 13.866 1.00 16.31 N ANISOU 2699 N PRO A 248 2020 2462 1715 130 414 259 N ATOM 2700 CA PRO A 248 7.343 1.407 13.344 1.00 14.61 C ANISOU 2700 CA PRO A 248 1892 2218 1442 80 462 263 C ATOM 2701 C PRO A 248 6.599 2.452 14.151 1.00 14.75 C ANISOU 2701 C PRO A 248 1860 2272 1472 65 341 280 C ATOM 2702 O PRO A 248 7.177 3.486 14.492 1.00 16.23 O ANISOU 2702 O PRO A 248 2003 2476 1688 28 376 285 O ATOM 2703 CB PRO A 248 6.832 1.304 11.898 1.00 17.03 C ANISOU 2703 CB PRO A 248 2463 2415 1594 78 465 253 C ATOM 2704 CG PRO A 248 7.106 -0.135 11.530 1.00 14.65 C ANISOU 2704 CG PRO A 248 2185 2087 1293 120 523 228 C ATOM 2705 CD PRO A 248 6.717 -0.878 12.789 1.00 16.58 C ANISOU 2705 CD PRO A 248 2218 2417 1665 154 413 240 C ATOM 2706 N LEU A 249 5.338 2.197 14.489 1.00 12.82 N ANISOU 2706 N LEU A 249 1610 2026 1234 93 213 284 N ATOM 2707 CA LEU A 249 4.572 3.156 15.276 1.00 15.60 C ANISOU 2707 CA LEU A 249 1911 2394 1622 90 138 289 C ATOM 2708 C LEU A 249 5.214 3.382 16.647 1.00 17.84 C ANISOU 2708 C LEU A 249 2074 2751 1953 86 172 294 C ATOM 2709 O LEU A 249 5.349 4.529 17.105 1.00 16.60 O ANISOU 2709 O LEU A 249 1915 2599 1793 65 161 291 O ATOM 2710 CB LEU A 249 3.130 2.660 15.408 1.00 17.59 C ANISOU 2710 CB LEU A 249 2135 2608 1940 122 37 285 C ATOM 2711 CG LEU A 249 2.000 3.591 15.868 1.00 19.52 C ANISOU 2711 CG LEU A 249 2333 2819 2266 133 -32 276 C ATOM 2712 CD1 LEU A 249 2.034 4.944 15.168 1.00 16.74 C ANISOU 2712 CD1 LEU A 249 2090 2412 1858 118 -90 272 C ATOM 2713 CD2 LEU A 249 0.635 2.890 15.690 1.00 15.22 C ANISOU 2713 CD2 LEU A 249 1726 2198 1858 159 -126 264 C ATOM 2714 N HIS A 250 5.620 2.298 17.320 1.00 13.04 N ANISOU 2714 N HIS A 250 1396 2179 1380 109 188 301 N ATOM 2715 CA HIS A 250 6.271 2.450 18.622 1.00 14.33 C ANISOU 2715 CA HIS A 250 1502 2377 1566 110 168 305 C ATOM 2716 C HIS A 250 7.587 3.199 18.505 1.00 14.22 C ANISOU 2716 C HIS A 250 1441 2362 1599 75 180 294 C ATOM 2717 O HIS A 250 7.952 3.978 19.390 1.00 14.75 O ANISOU 2717 O HIS A 250 1497 2431 1678 58 120 289 O ATOM 2718 CB HIS A 250 6.546 1.091 19.258 1.00 15.40 C ANISOU 2718 CB HIS A 250 1606 2520 1725 144 152 320 C ATOM 2719 CG HIS A 250 5.325 0.381 19.736 1.00 14.38 C ANISOU 2719 CG HIS A 250 1512 2376 1576 164 158 337 C ATOM 2720 ND1 HIS A 250 4.582 0.819 20.811 1.00 14.50 N ANISOU 2720 ND1 HIS A 250 1573 2379 1557 163 174 344 N ATOM 2721 CD2 HIS A 250 4.733 -0.757 19.302 1.00 14.91 C ANISOU 2721 CD2 HIS A 250 1577 2419 1670 178 171 345 C ATOM 2722 CE1 HIS A 250 3.579 -0.019 21.016 1.00 18.15 C ANISOU 2722 CE1 HIS A 250 2038 2808 2049 171 224 360 C ATOM 2723 NE2 HIS A 250 3.641 -0.977 20.105 1.00 17.58 N ANISOU 2723 NE2 HIS A 250 1929 2729 2021 177 203 362 N ATOM 2724 N ILE A 251 8.349 2.921 17.458 1.00 13.89 N ANISOU 2724 N ILE A 251 1376 2300 1601 61 267 286 N ATOM 2725 CA ILE A 251 9.632 3.591 17.281 1.00 14.58 C ANISOU 2725 CA ILE A 251 1381 2364 1796 16 323 274 C ATOM 2726 C ILE A 251 9.425 5.083 17.045 1.00 17.07 C ANISOU 2726 C ILE A 251 1766 2656 2062 -40 330 277 C ATOM 2727 O ILE A 251 10.186 5.918 17.546 1.00 15.53 O ANISOU 2727 O ILE A 251 1498 2445 1958 -83 300 268 O ATOM 2728 CB ILE A 251 10.403 2.920 16.130 1.00 17.60 C ANISOU 2728 CB ILE A 251 1742 2704 2240 14 487 259 C ATOM 2729 CG1 ILE A 251 10.826 1.500 16.540 1.00 17.44 C ANISOU 2729 CG1 ILE A 251 1620 2693 2314 76 460 250 C ATOM 2730 CG2 ILE A 251 11.611 3.764 15.683 1.00 17.58 C ANISOU 2730 CG2 ILE A 251 1655 2647 2376 -52 622 246 C ATOM 2731 CD1 ILE A 251 11.434 0.690 15.367 1.00 18.87 C ANISOU 2731 CD1 ILE A 251 1805 2818 2545 93 648 224 C ATOM 2732 N ILE A 252 8.402 5.444 16.268 1.00 12.51 N ANISOU 2732 N ILE A 252 1335 2057 1360 -41 342 286 N ATOM 2733 CA ILE A 252 8.111 6.861 16.073 1.00 14.72 C ANISOU 2733 CA ILE A 252 1701 2299 1593 -83 322 291 C ATOM 2734 C ILE A 252 7.793 7.528 17.410 1.00 15.19 C ANISOU 2734 C ILE A 252 1714 2388 1671 -72 207 281 C ATOM 2735 O ILE A 252 8.287 8.625 17.708 1.00 15.80 O ANISOU 2735 O ILE A 252 1787 2438 1780 -118 187 275 O ATOM 2736 CB ILE A 252 6.968 7.033 15.059 1.00 14.51 C ANISOU 2736 CB ILE A 252 1849 2217 1446 -66 292 301 C ATOM 2737 CG1 ILE A 252 7.446 6.661 13.647 1.00 17.17 C ANISOU 2737 CG1 ILE A 252 2329 2484 1710 -92 417 309 C ATOM 2738 CG2 ILE A 252 6.456 8.466 15.078 1.00 16.15 C ANISOU 2738 CG2 ILE A 252 2140 2377 1621 -88 222 305 C ATOM 2739 CD1 ILE A 252 6.287 6.529 12.648 1.00 20.08 C ANISOU 2739 CD1 ILE A 252 2912 2771 1947 -62 318 314 C ATOM 2740 N ASN A 253 6.980 6.871 18.243 1.00 13.44 N ANISOU 2740 N ASN A 253 1479 2202 1425 -15 147 278 N ATOM 2741 CA ASN A 253 6.706 7.421 19.567 1.00 14.84 C ANISOU 2741 CA ASN A 253 1669 2385 1586 -1 79 263 C ATOM 2742 C ASN A 253 7.995 7.614 20.360 1.00 15.91 C ANISOU 2742 C ASN A 253 1752 2515 1778 -31 14 253 C ATOM 2743 O ASN A 253 8.144 8.614 21.081 1.00 15.43 O ANISOU 2743 O ASN A 253 1739 2421 1702 -51 -56 234 O ATOM 2744 CB ASN A 253 5.721 6.516 20.326 1.00 11.24 C ANISOU 2744 CB ASN A 253 1227 1945 1098 55 85 265 C ATOM 2745 CG ASN A 253 4.281 6.601 19.759 1.00 15.18 C ANISOU 2745 CG ASN A 253 1741 2415 1612 83 111 261 C ATOM 2746 OD1 ASN A 253 3.916 7.577 19.104 1.00 16.39 O ANISOU 2746 OD1 ASN A 253 1927 2527 1773 74 86 252 O ATOM 2747 ND2 ASN A 253 3.474 5.584 20.025 1.00 13.01 N ANISOU 2747 ND2 ASN A 253 1436 2140 1367 116 145 268 N ATOM 2748 N CYS A 254 8.952 6.684 20.232 1.00 12.40 N ANISOU 2748 N CYS A 254 1207 2081 1423 -32 16 259 N ATOM 2749 CA CYS A 254 10.223 6.876 20.936 1.00 14.31 C ANISOU 2749 CA CYS A 254 1363 2287 1787 -58 -93 243 C ATOM 2750 C CYS A 254 10.946 8.141 20.467 1.00 15.57 C ANISOU 2750 C CYS A 254 1469 2398 2048 -137 -72 231 C ATOM 2751 O CYS A 254 11.537 8.860 21.279 1.00 15.77 O ANISOU 2751 O CYS A 254 1481 2372 2138 -167 -210 210 O ATOM 2752 CB CYS A 254 11.122 5.644 20.754 1.00 16.67 C ANISOU 2752 CB CYS A 254 1524 2585 2225 -34 -91 245 C ATOM 2753 SG CYS A 254 10.533 4.139 21.636 1.00 17.48 S ANISOU 2753 SG CYS A 254 1705 2710 2226 50 -168 265 S ATOM 2754 N PHE A 255 10.951 8.409 19.154 1.00 13.85 N ANISOU 2754 N PHE A 255 1247 2172 1843 -176 93 244 N ATOM 2755 CA PHE A 255 11.570 9.633 18.644 1.00 15.76 C ANISOU 2755 CA PHE A 255 1473 2348 2168 -264 151 243 C ATOM 2756 C PHE A 255 10.854 10.876 19.169 1.00 16.30 C ANISOU 2756 C PHE A 255 1673 2395 2124 -275 52 236 C ATOM 2757 O PHE A 255 11.491 11.833 19.623 1.00 18.46 O ANISOU 2757 O PHE A 255 1916 2608 2489 -333 -25 220 O ATOM 2758 CB PHE A 255 11.578 9.619 17.099 1.00 13.40 C ANISOU 2758 CB PHE A 255 1236 2018 1836 -300 371 266 C ATOM 2759 CG PHE A 255 12.783 8.908 16.512 1.00 14.66 C ANISOU 2759 CG PHE A 255 1240 2143 2188 -329 535 258 C ATOM 2760 CD1 PHE A 255 12.719 7.548 16.189 1.00 16.35 C ANISOU 2760 CD1 PHE A 255 1431 2392 2388 -262 598 254 C ATOM 2761 CD2 PHE A 255 13.977 9.583 16.337 1.00 16.39 C ANISOU 2761 CD2 PHE A 255 1317 2277 2635 -420 631 249 C ATOM 2762 CE1 PHE A 255 13.831 6.884 15.699 1.00 18.51 C ANISOU 2762 CE1 PHE A 255 1549 2618 2865 -274 766 235 C ATOM 2763 CE2 PHE A 255 15.099 8.935 15.844 1.00 23.71 C ANISOU 2763 CE2 PHE A 255 2059 3149 3801 -441 814 231 C ATOM 2764 CZ PHE A 255 15.026 7.576 15.524 1.00 22.42 C ANISOU 2764 CZ PHE A 255 1908 3027 3585 -353 858 215 C ATOM 2765 N THR A 256 9.527 10.880 19.103 1.00 13.93 N ANISOU 2765 N THR A 256 1508 2126 1658 -217 50 243 N ATOM 2766 CA THR A 256 8.762 12.008 19.619 1.00 15.85 C ANISOU 2766 CA THR A 256 1867 2337 1820 -207 -24 227 C ATOM 2767 C THR A 256 9.115 12.276 21.076 1.00 17.49 C ANISOU 2767 C THR A 256 2083 2527 2035 -199 -164 192 C ATOM 2768 O THR A 256 9.383 13.417 21.465 1.00 20.09 O ANISOU 2768 O THR A 256 2463 2792 2379 -240 -238 170 O ATOM 2769 CB THR A 256 7.271 11.701 19.465 1.00 15.99 C ANISOU 2769 CB THR A 256 1966 2377 1732 -130 -6 228 C ATOM 2770 OG1 THR A 256 6.972 11.516 18.072 1.00 16.91 O ANISOU 2770 OG1 THR A 256 2123 2475 1826 -139 63 257 O ATOM 2771 CG2 THR A 256 6.398 12.828 20.051 1.00 16.74 C ANISOU 2771 CG2 THR A 256 2158 2422 1781 -101 -58 199 C ATOM 2772 N PHE A 257 9.164 11.213 21.882 1.00 13.78 N ANISOU 2772 N PHE A 257 1596 2095 1544 -149 -215 188 N ATOM 2773 CA PHE A 257 9.348 11.312 23.327 1.00 16.94 C ANISOU 2773 CA PHE A 257 2095 2453 1887 -126 -365 157 C ATOM 2774 C PHE A 257 10.794 11.627 23.709 1.00 19.28 C ANISOU 2774 C PHE A 257 2304 2682 2340 -187 -534 139 C ATOM 2775 O PHE A 257 11.046 12.542 24.503 1.00 20.60 O ANISOU 2775 O PHE A 257 2573 2768 2485 -210 -679 105 O ATOM 2776 CB PHE A 257 8.910 9.997 23.970 1.00 12.51 C ANISOU 2776 CB PHE A 257 1585 1930 1239 -57 -358 170 C ATOM 2777 CG PHE A 257 9.032 9.977 25.467 1.00 16.83 C ANISOU 2777 CG PHE A 257 2320 2408 1667 -28 -503 146 C ATOM 2778 CD1 PHE A 257 9.892 9.080 26.087 1.00 18.11 C ANISOU 2778 CD1 PHE A 257 2482 2538 1862 -16 -661 155 C ATOM 2779 CD2 PHE A 257 8.292 10.854 26.258 1.00 17.18 C ANISOU 2779 CD2 PHE A 257 2574 2395 1560 -7 -487 112 C ATOM 2780 CE1 PHE A 257 10.010 9.046 27.493 1.00 21.16 C ANISOU 2780 CE1 PHE A 257 3120 2826 2093 13 -831 136 C ATOM 2781 CE2 PHE A 257 8.407 10.831 27.659 1.00 15.50 C ANISOU 2781 CE2 PHE A 257 2616 2088 1186 20 -609 87 C ATOM 2782 CZ PHE A 257 9.274 9.942 28.269 1.00 21.61 C ANISOU 2782 CZ PHE A 257 3431 2821 1959 27 -796 102 C ATOM 2783 N PHE A 258 11.751 10.852 23.185 1.00 16.28 N ANISOU 2783 N PHE A 258 1730 2314 2143 -210 -526 155 N ATOM 2784 CA PHE A 258 13.152 10.978 23.588 1.00 16.84 C ANISOU 2784 CA PHE A 258 1655 2296 2446 -260 -706 132 C ATOM 2785 C PHE A 258 13.911 12.084 22.869 1.00 18.79 C ANISOU 2785 C PHE A 258 1765 2479 2896 -366 -652 124 C ATOM 2786 O PHE A 258 14.973 12.493 23.357 1.00 21.73 O ANISOU 2786 O PHE A 258 2021 2747 3489 -421 -835 94 O ATOM 2787 CB PHE A 258 13.899 9.667 23.344 1.00 18.64 C ANISOU 2787 CB PHE A 258 1695 2539 2850 -232 -705 142 C ATOM 2788 CG PHE A 258 13.532 8.561 24.292 1.00 19.40 C ANISOU 2788 CG PHE A 258 1920 2649 2803 -141 -836 150 C ATOM 2789 CD1 PHE A 258 13.025 7.359 23.807 1.00 15.69 C ANISOU 2789 CD1 PHE A 258 1434 2259 2269 -85 -689 180 C ATOM 2790 CD2 PHE A 258 13.701 8.718 25.669 1.00 22.19 C ANISOU 2790 CD2 PHE A 258 2452 2912 3069 -118 -1110 127 C ATOM 2791 CE1 PHE A 258 12.702 6.323 24.667 1.00 17.29 C ANISOU 2791 CE1 PHE A 258 1768 2457 2345 -12 -792 195 C ATOM 2792 CE2 PHE A 258 13.374 7.676 26.552 1.00 21.70 C ANISOU 2792 CE2 PHE A 258 2567 2835 2843 -40 -1215 143 C ATOM 2793 CZ PHE A 258 12.877 6.484 26.053 1.00 20.80 C ANISOU 2793 CZ PHE A 258 2410 2807 2687 9 -1047 181 C ATOM 2794 N CYS A 259 13.428 12.573 21.722 1.00 21.79 N ANISOU 2794 N CYS A 259 2164 2893 3223 -402 -421 151 N ATOM 2795 CA CYS A 259 14.131 13.600 20.948 1.00 23.99 C ANISOU 2795 CA CYS A 259 2350 3091 3674 -515 -321 157 C ATOM 2796 C CYS A 259 13.214 14.797 20.705 1.00 24.31 C ANISOU 2796 C CYS A 259 2596 3116 3523 -532 -281 166 C ATOM 2797 O CYS A 259 12.789 15.049 19.567 1.00 24.96 O ANISOU 2797 O CYS A 259 2747 3205 3532 -555 -89 202 O ATOM 2798 CB CYS A 259 14.652 13.061 19.615 1.00 26.33 C ANISOU 2798 CB CYS A 259 2507 3392 4106 -556 -51 186 C ATOM 2799 SG CYS A 259 15.789 14.253 18.827 1.00 33.95 S ANISOU 2799 SG CYS A 259 3338 4213 5347 -717 108 193 S ATOM 2800 N PRO A 260 12.916 15.575 21.749 1.00 26.79 N ANISOU 2800 N PRO A 260 3324 3569 3286 365 -47 -52 N ATOM 2801 CA PRO A 260 12.106 16.787 21.553 1.00 28.44 C ANISOU 2801 CA PRO A 260 3675 3552 3580 236 -129 63 C ATOM 2802 C PRO A 260 12.771 17.833 20.669 1.00 31.09 C ANISOU 2802 C PRO A 260 3841 3876 4094 -174 -261 165 C ATOM 2803 O PRO A 260 12.080 18.748 20.209 1.00 32.41 O ANISOU 2803 O PRO A 260 4125 3855 4336 -330 -335 303 O ATOM 2804 CB PRO A 260 11.909 17.314 22.984 1.00 30.97 C ANISOU 2804 CB PRO A 260 4262 3659 3848 544 -333 -96 C ATOM 2805 CG PRO A 260 13.086 16.769 23.743 1.00 31.32 C ANISOU 2805 CG PRO A 260 4258 3804 3839 702 -481 -291 C ATOM 2806 CD PRO A 260 13.349 15.414 23.149 1.00 28.50 C ANISOU 2806 CD PRO A 260 3710 3701 3416 686 -234 -250 C ATOM 2807 N ASP A 261 14.083 17.736 20.425 1.00 31.01 N ANISOU 2807 N ASP A 261 3553 4044 4187 -356 -294 108 N ATOM 2808 CA ASP A 261 14.757 18.601 19.464 1.00 33.24 C ANISOU 2808 CA ASP A 261 3628 4353 4649 -795 -309 271 C ATOM 2809 C ASP A 261 14.602 18.137 18.017 1.00 33.53 C ANISOU 2809 C ASP A 261 3570 4635 4534 -1013 18 476 C ATOM 2810 O ASP A 261 14.935 18.901 17.106 1.00 36.58 O ANISOU 2810 O ASP A 261 3880 5031 4987 -1383 68 689 O ATOM 2811 CB ASP A 261 16.248 18.701 19.794 1.00 39.72 C ANISOU 2811 CB ASP A 261 4117 5260 5714 -910 -442 117 C ATOM 2812 CG ASP A 261 16.509 19.405 21.110 1.00 50.44 C ANISOU 2812 CG ASP A 261 5592 6317 7257 -724 -874 -94 C ATOM 2813 OD1 ASP A 261 15.662 20.227 21.526 1.00 52.80 O ANISOU 2813 OD1 ASP A 261 6192 6329 7541 -640 -1068 -61 O ATOM 2814 OD2 ASP A 261 17.569 19.142 21.726 1.00 56.56 O ANISOU 2814 OD2 ASP A 261 6160 7129 8200 -632 -1057 -327 O ATOM 2815 N CYS A 262 14.154 16.904 17.786 1.00 30.88 N ANISOU 2815 N CYS A 262 3255 4485 3992 -786 225 418 N ATOM 2816 CA CYS A 262 13.892 16.412 16.438 1.00 32.76 C ANISOU 2816 CA CYS A 262 3468 4930 4048 -905 471 561 C ATOM 2817 C CYS A 262 12.499 16.855 16.006 1.00 28.66 C ANISOU 2817 C CYS A 262 3259 4161 3469 -896 409 726 C ATOM 2818 O CYS A 262 11.553 16.795 16.791 1.00 25.15 O ANISOU 2818 O CYS A 262 2982 3490 3082 -652 303 657 O ATOM 2819 CB CYS A 262 13.967 14.875 16.391 1.00 35.31 C ANISOU 2819 CB CYS A 262 3681 5498 4239 -630 627 388 C ATOM 2820 SG CYS A 262 15.579 14.055 16.796 1.00 41.86 S ANISOU 2820 SG CYS A 262 4116 6639 5151 -557 669 117 S ATOM 2821 N ASER A 263 12.373 17.295 14.756 0.55 26.28 N ANISOU 2821 N ASER A 263 3037 3897 3050 -1149 478 939 N ATOM 2822 N BSER A 263 12.369 17.298 14.759 0.45 29.29 N ANISOU 2822 N BSER A 263 3419 4277 3432 -1148 477 939 N ATOM 2823 CA ASER A 263 11.045 17.593 14.232 0.55 28.44 C ANISOU 2823 CA ASER A 263 3605 3921 3281 -1104 361 1057 C ATOM 2824 CA BSER A 263 11.040 17.625 14.255 0.45 28.38 C ANISOU 2824 CA BSER A 263 3599 3905 3279 -1106 355 1057 C ATOM 2825 C ASER A 263 10.155 16.361 14.344 0.55 25.34 C ANISOU 2825 C ASER A 263 3230 3537 2860 -759 416 907 C ATOM 2826 C BSER A 263 10.148 16.387 14.295 0.45 25.39 C ANISOU 2826 C BSER A 263 3242 3542 2862 -768 414 915 C ATOM 2827 O ASER A 263 10.604 15.229 14.142 0.55 23.95 O ANISOU 2827 O ASER A 263 2895 3629 2575 -634 578 793 O ATOM 2828 O BSER A 263 10.591 15.274 13.996 0.45 24.36 O ANISOU 2828 O BSER A 263 2960 3686 2609 -656 579 811 O ATOM 2829 CB ASER A 263 11.120 18.051 12.774 0.55 30.29 C ANISOU 2829 CB ASER A 263 3981 4223 3304 -1380 422 1304 C ATOM 2830 CB BSER A 263 11.124 18.177 12.831 0.45 30.45 C ANISOU 2830 CB BSER A 263 4008 4215 3345 -1399 402 1314 C ATOM 2831 OG ASER A 263 11.756 19.308 12.666 0.55 33.40 O ANISOU 2831 OG ASER A 263 4388 4506 3795 -1706 348 1483 O ATOM 2832 OG BSER A 263 11.904 17.331 12.009 0.45 32.12 O ANISOU 2832 OG BSER A 263 4067 4821 3318 -1410 683 1288 O ATOM 2833 N HIS A 264 8.891 16.583 14.695 1.00 25.63 N ANISOU 2833 N HIS A 264 3430 3258 3051 -602 267 897 N ATOM 2834 CA HIS A 264 7.957 15.469 14.821 1.00 24.04 C ANISOU 2834 CA HIS A 264 3204 3001 2931 -309 320 788 C ATOM 2835 C HIS A 264 7.861 14.721 13.491 1.00 22.70 C ANISOU 2835 C HIS A 264 3051 2975 2600 -308 347 806 C ATOM 2836 O HIS A 264 7.863 15.337 12.422 1.00 23.17 O ANISOU 2836 O HIS A 264 3276 3027 2499 -489 263 941 O ATOM 2837 CB HIS A 264 6.581 15.999 15.236 1.00 23.30 C ANISOU 2837 CB HIS A 264 3235 2531 3088 -185 174 786 C ATOM 2838 CG HIS A 264 5.666 14.959 15.797 1.00 22.47 C ANISOU 2838 CG HIS A 264 3029 2327 3180 102 285 686 C ATOM 2839 ND1 HIS A 264 5.218 13.883 15.059 1.00 22.67 N ANISOU 2839 ND1 HIS A 264 2981 2368 3263 204 299 657 N ATOM 2840 CD2 HIS A 264 5.100 14.839 17.025 1.00 21.29 C ANISOU 2840 CD2 HIS A 264 2847 2044 3200 308 397 624 C ATOM 2841 CE1 HIS A 264 4.427 13.137 15.813 1.00 24.21 C ANISOU 2841 CE1 HIS A 264 3063 2419 3717 421 414 606 C ATOM 2842 NE2 HIS A 264 4.343 13.694 17.010 1.00 23.57 N ANISOU 2842 NE2 HIS A 264 3012 2266 3676 485 516 602 N ATOM 2843 N ALA A 265 7.844 13.391 13.554 1.00 19.16 N ANISOU 2843 N ALA A 265 2461 2652 2166 -90 443 671 N ATOM 2844 CA ALA A 265 7.553 12.612 12.356 1.00 21.87 C ANISOU 2844 CA ALA A 265 2845 3068 2398 -1 390 629 C ATOM 2845 C ALA A 265 6.326 13.193 11.651 1.00 22.28 C ANISOU 2845 C ALA A 265 3119 2787 2559 -3 145 705 C ATOM 2846 O ALA A 265 5.350 13.564 12.317 1.00 19.59 O ANISOU 2846 O ALA A 265 2782 2123 2537 64 47 707 O ATOM 2847 CB ALA A 265 7.297 11.146 12.711 1.00 20.19 C ANISOU 2847 CB ALA A 265 2462 2861 2347 275 419 465 C ATOM 2848 N PRO A 266 6.343 13.304 10.328 1.00 21.05 N ANISOU 2848 N PRO A 266 2949 2856 2192 -521 -289 657 N ATOM 2849 CA PRO A 266 5.268 14.021 9.639 1.00 23.45 C ANISOU 2849 CA PRO A 266 3319 3059 2531 -488 -357 650 C ATOM 2850 C PRO A 266 3.966 13.232 9.635 1.00 24.11 C ANISOU 2850 C PRO A 266 3367 3119 2674 -376 -335 567 C ATOM 2851 O PRO A 266 3.928 12.015 9.843 1.00 19.44 O ANISOU 2851 O PRO A 266 2721 2618 2048 -333 -250 527 O ATOM 2852 CB PRO A 266 5.808 14.224 8.214 1.00 24.08 C ANISOU 2852 CB PRO A 266 3449 3174 2528 -570 -372 759 C ATOM 2853 CG PRO A 266 6.857 13.174 8.024 1.00 24.30 C ANISOU 2853 CG PRO A 266 3393 3339 2500 -597 -228 777 C ATOM 2854 CD PRO A 266 7.418 12.863 9.414 1.00 24.30 C ANISOU 2854 CD PRO A 266 3294 3366 2571 -580 -220 740 C ATOM 2855 N LEU A 267 2.882 13.974 9.405 1.00 24.29 N ANISOU 2855 N LEU A 267 3405 2996 2828 -332 -426 547 N ATOM 2856 CA LEU A 267 1.543 13.398 9.416 1.00 26.51 C ANISOU 2856 CA LEU A 267 3609 3211 3254 -231 -425 475 C ATOM 2857 C LEU A 267 1.429 12.193 8.483 1.00 22.24 C ANISOU 2857 C LEU A 267 3060 2770 2621 -224 -439 514 C ATOM 2858 O LEU A 267 0.839 11.171 8.851 1.00 20.06 O ANISOU 2858 O LEU A 267 2709 2526 2387 -160 -365 444 O ATOM 2859 CB LEU A 267 0.523 14.478 9.028 1.00 36.05 C ANISOU 2859 CB LEU A 267 4799 4210 4688 -194 -576 485 C ATOM 2860 CG LEU A 267 -0.952 14.083 8.967 1.00 44.82 C ANISOU 2860 CG LEU A 267 5771 5194 6063 -91 -612 426 C ATOM 2861 CD1 LEU A 267 -1.570 14.373 10.289 1.00 49.61 C ANISOU 2861 CD1 LEU A 267 6290 5689 6869 -21 -424 273 C ATOM 2862 CD2 LEU A 267 -1.683 14.855 7.883 1.00 51.75 C ANISOU 2862 CD2 LEU A 267 6646 5885 7130 -92 -890 526 C ATOM 2863 N TRP A 268 1.959 12.299 7.255 1.00 19.77 N ANISOU 2863 N TRP A 268 2855 2488 2167 -308 -522 619 N ATOM 2864 CA TRP A 268 1.774 11.196 6.309 1.00 20.53 C ANISOU 2864 CA TRP A 268 3006 2642 2153 -320 -529 641 C ATOM 2865 C TRP A 268 2.464 9.924 6.799 1.00 19.29 C ANISOU 2865 C TRP A 268 2784 2642 1903 -290 -334 583 C ATOM 2866 O TRP A 268 1.970 8.815 6.556 1.00 18.23 O ANISOU 2866 O TRP A 268 2640 2536 1750 -250 -316 548 O ATOM 2867 CB TRP A 268 2.281 11.578 4.910 1.00 21.26 C ANISOU 2867 CB TRP A 268 3303 2715 2059 -453 -608 753 C ATOM 2868 CG TRP A 268 3.769 11.842 4.833 1.00 25.54 C ANISOU 2868 CG TRP A 268 3884 3360 2459 -546 -441 788 C ATOM 2869 CD1 TRP A 268 4.402 13.059 4.926 1.00 25.55 C ANISOU 2869 CD1 TRP A 268 3916 3323 2469 -623 -469 849 C ATOM 2870 CD2 TRP A 268 4.803 10.867 4.639 1.00 26.98 C ANISOU 2870 CD2 TRP A 268 4050 3675 2526 -574 -216 766 C ATOM 2871 NE1 TRP A 268 5.762 12.892 4.810 1.00 25.61 N ANISOU 2871 NE1 TRP A 268 3909 3437 2386 -704 -277 872 N ATOM 2872 CE2 TRP A 268 6.035 11.561 4.627 1.00 27.36 C ANISOU 2872 CE2 TRP A 268 4088 3757 2552 -669 -111 818 C ATOM 2873 CE3 TRP A 268 4.805 9.474 4.467 1.00 26.65 C ANISOU 2873 CE3 TRP A 268 3988 3708 2431 -527 -92 705 C ATOM 2874 CZ2 TRP A 268 7.253 10.913 4.452 1.00 28.93 C ANISOU 2874 CZ2 TRP A 268 4218 4048 2726 -710 125 809 C ATOM 2875 CZ3 TRP A 268 6.021 8.830 4.296 1.00 28.85 C ANISOU 2875 CZ3 TRP A 268 4222 4075 2665 -559 143 688 C ATOM 2876 CH2 TRP A 268 7.228 9.552 4.286 1.00 28.98 C ANISOU 2876 CH2 TRP A 268 4191 4112 2708 -646 256 740 C ATOM 2877 N LEU A 269 3.608 10.071 7.474 1.00 15.63 N ANISOU 2877 N LEU A 269 2275 2257 1406 -317 -221 582 N ATOM 2878 CA LEU A 269 4.340 8.922 7.998 1.00 16.71 C ANISOU 2878 CA LEU A 269 2330 2506 1513 -291 -85 546 C ATOM 2879 C LEU A 269 3.603 8.279 9.166 1.00 19.53 C ANISOU 2879 C LEU A 269 2620 2854 1947 -211 -70 460 C ATOM 2880 O LEU A 269 3.571 7.044 9.283 1.00 16.88 O ANISOU 2880 O LEU A 269 2248 2576 1591 -171 -8 425 O ATOM 2881 CB LEU A 269 5.746 9.346 8.442 1.00 17.88 C ANISOU 2881 CB LEU A 269 2425 2697 1671 -355 -31 592 C ATOM 2882 CG LEU A 269 6.652 8.198 8.902 1.00 20.12 C ANISOU 2882 CG LEU A 269 2595 3058 1992 -334 64 580 C ATOM 2883 CD1 LEU A 269 6.823 7.182 7.768 1.00 23.55 C ANISOU 2883 CD1 LEU A 269 3039 3539 2370 -319 195 568 C ATOM 2884 CD2 LEU A 269 8.010 8.665 9.439 1.00 17.89 C ANISOU 2884 CD2 LEU A 269 2216 2780 1800 -405 56 644 C ATOM 2885 N MET A 270 3.033 9.097 10.061 1.00 19.44 N ANISOU 2885 N MET A 270 2611 2755 2020 -201 -101 417 N ATOM 2886 CA MET A 270 2.236 8.541 11.146 1.00 18.26 C ANISOU 2886 CA MET A 270 2439 2572 1928 -154 -32 322 C ATOM 2887 C MET A 270 1.099 7.713 10.595 1.00 17.46 C ANISOU 2887 C MET A 270 2283 2454 1897 -89 -35 289 C ATOM 2888 O MET A 270 0.809 6.625 11.099 1.00 17.26 O ANISOU 2888 O MET A 270 2233 2464 1861 -65 39 239 O ATOM 2889 CB MET A 270 1.650 9.639 12.034 1.00 20.41 C ANISOU 2889 CB MET A 270 2747 2711 2295 -160 -8 255 C ATOM 2890 CG MET A 270 2.618 10.672 12.484 1.00 27.38 C ANISOU 2890 CG MET A 270 3713 3572 3118 -239 -48 292 C ATOM 2891 SD MET A 270 3.548 10.150 13.914 1.00 31.11 S ANISOU 2891 SD MET A 270 4288 4078 3455 -324 -17 277 S ATOM 2892 CE MET A 270 2.452 9.092 14.859 1.00 24.43 C ANISOU 2892 CE MET A 270 3487 3196 2599 -296 133 155 C ATOM 2893 N TYR A 271 0.397 8.241 9.590 1.00 16.81 N ANISOU 2893 N TYR A 271 2192 2293 1902 -76 -152 326 N ATOM 2894 CA TYR A 271 -0.745 7.498 9.085 1.00 17.80 C ANISOU 2894 CA TYR A 271 2260 2370 2134 -30 -208 309 C ATOM 2895 C TYR A 271 -0.284 6.233 8.373 1.00 16.32 C ANISOU 2895 C TYR A 271 2130 2294 1777 -45 -199 338 C ATOM 2896 O TYR A 271 -0.960 5.202 8.462 1.00 17.27 O ANISOU 2896 O TYR A 271 2205 2415 1941 -12 -183 298 O ATOM 2897 CB TYR A 271 -1.628 8.418 8.234 1.00 25.32 C ANISOU 2897 CB TYR A 271 3195 3165 3260 -27 -405 362 C ATOM 2898 CG TYR A 271 -2.422 9.293 9.190 1.00 37.20 C ANISOU 2898 CG TYR A 271 4578 4524 5034 28 -346 283 C ATOM 2899 CD1 TYR A 271 -3.621 8.860 9.716 1.00 42.00 C ANISOU 2899 CD1 TYR A 271 5028 5033 5896 90 -271 198 C ATOM 2900 CD2 TYR A 271 -1.906 10.479 9.673 1.00 47.44 C ANISOU 2900 CD2 TYR A 271 5921 5775 6328 8 -313 274 C ATOM 2901 CE1 TYR A 271 -4.331 9.612 10.630 1.00 46.93 C ANISOU 2901 CE1 TYR A 271 5542 5502 6787 136 -135 95 C ATOM 2902 CE2 TYR A 271 -2.609 11.247 10.596 1.00 53.34 C ANISOU 2902 CE2 TYR A 271 6587 6366 7313 55 -206 173 C ATOM 2903 CZ TYR A 271 -3.822 10.807 11.068 1.00 51.14 C ANISOU 2903 CZ TYR A 271 6150 5979 7300 120 -95 75 C ATOM 2904 OH TYR A 271 -4.521 11.561 11.985 1.00 50.66 O ANISOU 2904 OH TYR A 271 6010 5738 7499 162 82 -51 O ATOM 2905 N ALEU A 272 0.866 6.280 7.696 0.50 14.58 N ANISOU 2905 N ALEU A 272 2006 2151 1381 -101 -181 396 N ATOM 2906 N BLEU A 272 0.876 6.276 7.705 0.50 14.58 N ANISOU 2906 N BLEU A 272 2006 2152 1380 -101 -180 395 N ATOM 2907 CA ALEU A 272 1.440 5.053 7.159 0.50 15.86 C ANISOU 2907 CA ALEU A 272 2218 2400 1407 -108 -102 392 C ATOM 2908 CA BLEU A 272 1.452 5.053 7.154 0.50 15.84 C ANISOU 2908 CA BLEU A 272 2217 2399 1403 -109 -101 393 C ATOM 2909 C ALEU A 272 1.692 4.044 8.273 0.50 15.31 C ANISOU 2909 C ALEU A 272 2056 2396 1365 -56 10 332 C ATOM 2910 C BLEU A 272 1.748 4.037 8.251 0.50 15.32 C ANISOU 2910 C BLEU A 272 2059 2401 1362 -58 13 333 C ATOM 2911 O ALEU A 272 1.318 2.873 8.160 0.50 15.39 O ANISOU 2911 O ALEU A 272 2066 2421 1361 -26 29 299 O ATOM 2912 O BLEU A 272 1.488 2.842 8.086 0.50 15.62 O ANISOU 2912 O BLEU A 272 2102 2459 1375 -29 39 303 O ATOM 2913 CB ALEU A 272 2.728 5.355 6.402 0.50 16.71 C ANISOU 2913 CB ALEU A 272 2413 2559 1377 -180 -23 444 C ATOM 2914 CB BLEU A 272 2.726 5.363 6.374 0.50 16.76 C ANISOU 2914 CB BLEU A 272 2422 2564 1381 -182 -24 445 C ATOM 2915 CG ALEU A 272 3.402 4.133 5.783 0.50 17.39 C ANISOU 2915 CG ALEU A 272 2548 2703 1358 -186 119 419 C ATOM 2916 CG BLEU A 272 2.609 5.743 4.898 0.50 21.15 C ANISOU 2916 CG BLEU A 272 3180 3060 1796 -277 -97 505 C ATOM 2917 CD1ALEU A 272 2.421 3.373 4.898 0.50 20.42 C ANISOU 2917 CD1ALEU A 272 3069 3031 1659 -196 35 403 C ATOM 2918 CD1BLEU A 272 3.996 5.962 4.328 0.50 22.32 C ANISOU 2918 CD1BLEU A 272 3397 3259 1823 -362 78 533 C ATOM 2919 CD2ALEU A 272 4.649 4.544 4.986 0.50 17.39 C ANISOU 2919 CD2ALEU A 272 2619 2723 1265 -272 262 456 C ATOM 2920 CD2BLEU A 272 1.882 4.648 4.125 0.50 22.74 C ANISOU 2920 CD2BLEU A 272 3499 3226 1914 -282 -147 482 C ATOM 2921 N ALA A 273 2.302 4.491 9.375 1.00 14.66 N ANISOU 2921 N ALA A 273 1925 2332 1313 -64 54 325 N ATOM 2922 CA ALA A 273 2.595 3.576 10.477 1.00 13.80 C ANISOU 2922 CA ALA A 273 1782 2256 1207 -48 110 291 C ATOM 2923 C ALA A 273 1.317 3.028 11.110 1.00 14.48 C ANISOU 2923 C ALA A 273 1861 2294 1348 -22 131 222 C ATOM 2924 O ALA A 273 1.277 1.870 11.550 1.00 13.26 O ANISOU 2924 O ALA A 273 1708 2161 1171 -11 164 198 O ATOM 2925 CB ALA A 273 3.451 4.293 11.534 1.00 11.62 C ANISOU 2925 CB ALA A 273 1514 1970 931 -101 97 313 C ATOM 2926 N ILE A 274 0.270 3.854 11.190 1.00 11.87 N ANISOU 2926 N ILE A 274 1509 1877 1124 -14 120 189 N ATOM 2927 CA ILE A 274 -0.997 3.394 11.746 1.00 12.18 C ANISOU 2927 CA ILE A 274 1499 1847 1282 5 184 116 C ATOM 2928 C ILE A 274 -1.629 2.347 10.838 1.00 15.62 C ANISOU 2928 C ILE A 274 1894 2291 1749 36 119 129 C ATOM 2929 O ILE A 274 -2.114 1.311 11.302 1.00 16.42 O ANISOU 2929 O ILE A 274 1977 2392 1868 37 179 89 O ATOM 2930 CB ILE A 274 -1.938 4.590 11.981 1.00 13.82 C ANISOU 2930 CB ILE A 274 1645 1923 1683 18 208 70 C ATOM 2931 CG1 ILE A 274 -1.383 5.483 13.115 1.00 14.33 C ANISOU 2931 CG1 ILE A 274 1804 1957 1685 -33 307 30 C ATOM 2932 CG2 ILE A 274 -3.388 4.102 12.274 1.00 13.81 C ANISOU 2932 CG2 ILE A 274 1524 1820 1902 44 290 -3 C ATOM 2933 CD1 ILE A 274 -2.051 6.863 13.202 1.00 16.10 C ANISOU 2933 CD1 ILE A 274 1981 2034 2101 -13 331 -16 C ATOM 2934 N AVAL A 275 -1.640 2.618 9.529 0.50 12.00 N ANISOU 2934 N AVAL A 275 1458 1822 1279 39 -17 189 N ATOM 2935 N BVAL A 275 -1.642 2.593 9.525 0.50 12.00 N ANISOU 2935 N BVAL A 275 1458 1822 1278 40 -17 189 N ATOM 2936 CA AVAL A 275 -2.198 1.680 8.563 0.50 13.54 C ANISOU 2936 CA AVAL A 275 1679 2000 1466 40 -116 208 C ATOM 2937 CA BVAL A 275 -2.276 1.602 8.668 0.50 13.26 C ANISOU 2937 CA BVAL A 275 1633 1963 1443 43 -107 201 C ATOM 2938 C AVAL A 275 -1.447 0.357 8.610 0.50 12.69 C ANISOU 2938 C AVAL A 275 1634 1986 1202 45 -33 192 C ATOM 2939 C BVAL A 275 -1.450 0.323 8.625 0.50 12.65 C ANISOU 2939 C BVAL A 275 1628 1981 1196 46 -31 190 C ATOM 2940 O AVAL A 275 -2.048 -0.722 8.559 0.50 12.86 O ANISOU 2940 O AVAL A 275 1650 1991 1246 53 -47 168 O ATOM 2941 O BVAL A 275 -2.011 -0.773 8.526 0.50 12.84 O ANISOU 2941 O BVAL A 275 1653 1991 1236 53 -47 168 O ATOM 2942 CB AVAL A 275 -2.167 2.309 7.155 0.50 16.70 C ANISOU 2942 CB AVAL A 275 2187 2350 1808 -2 -288 285 C ATOM 2943 CB BVAL A 275 -2.537 2.163 7.256 0.50 16.95 C ANISOU 2943 CB BVAL A 275 2185 2358 1896 7 -303 276 C ATOM 2944 CG1AVAL A 275 -2.225 1.248 6.066 0.50 16.10 C ANISOU 2944 CG1AVAL A 275 2253 2273 1591 -40 -365 305 C ATOM 2945 CG1BVAL A 275 -3.533 3.328 7.321 0.50 17.08 C ANISOU 2945 CG1BVAL A 275 2088 2232 2170 18 -426 294 C ATOM 2946 CG2AVAL A 275 -3.313 3.316 6.999 0.50 17.57 C ANISOU 2946 CG2AVAL A 275 2204 2307 2165 2 -453 314 C ATOM 2947 CG2BVAL A 275 -1.229 2.580 6.584 0.50 16.06 C ANISOU 2947 CG2BVAL A 275 2221 2319 1563 -39 -268 320 C ATOM 2948 N LEU A 276 -0.119 0.422 8.726 1.00 13.51 N ANISOU 2948 N LEU A 276 1778 2168 1186 41 47 207 N ATOM 2949 CA LEU A 276 0.687 -0.791 8.775 1.00 14.22 C ANISOU 2949 CA LEU A 276 1891 2312 1201 60 121 192 C ATOM 2950 C LEU A 276 0.348 -1.624 10.011 1.00 15.47 C ANISOU 2950 C LEU A 276 2004 2466 1408 72 154 157 C ATOM 2951 O LEU A 276 0.204 -2.853 9.924 1.00 13.14 O ANISOU 2951 O LEU A 276 1730 2167 1097 89 158 137 O ATOM 2952 CB LEU A 276 2.172 -0.426 8.756 1.00 14.58 C ANISOU 2952 CB LEU A 276 1923 2407 1208 54 193 223 C ATOM 2953 CG LEU A 276 3.144 -1.598 9.000 1.00 18.54 C ANISOU 2953 CG LEU A 276 2385 2929 1731 89 265 212 C ATOM 2954 CD1 LEU A 276 3.056 -2.685 7.876 1.00 17.41 C ANISOU 2954 CD1 LEU A 276 2324 2765 1527 111 325 171 C ATOM 2955 CD2 LEU A 276 4.587 -1.082 9.153 1.00 16.91 C ANISOU 2955 CD2 LEU A 276 2094 2741 1591 78 315 255 C ATOM 2956 N ALA A 277 0.202 -0.967 11.168 1.00 13.39 N ANISOU 2956 N ALA A 277 1719 2186 1184 44 183 146 N ATOM 2957 CA ALA A 277 -0.211 -1.677 12.370 1.00 13.93 C ANISOU 2957 CA ALA A 277 1812 2226 1255 12 233 112 C ATOM 2958 C ALA A 277 -1.543 -2.365 12.143 1.00 13.80 C ANISOU 2958 C ALA A 277 1758 2164 1321 18 247 72 C ATOM 2959 O ALA A 277 -1.708 -3.536 12.488 1.00 14.18 O ANISOU 2959 O ALA A 277 1838 2206 1344 4 260 61 O ATOM 2960 CB ALA A 277 -0.313 -0.716 13.573 1.00 11.20 C ANISOU 2960 CB ALA A 277 1516 1836 905 -51 297 86 C ATOM 2961 N HIS A 278 -2.497 -1.661 11.522 1.00 12.56 N ANISOU 2961 N HIS A 278 1523 1954 1294 33 215 62 N ATOM 2962 CA HIS A 278 -3.812 -2.244 11.298 1.00 12.88 C ANISOU 2962 CA HIS A 278 1485 1923 1487 30 195 37 C ATOM 2963 C HIS A 278 -3.751 -3.413 10.324 1.00 13.01 C ANISOU 2963 C HIS A 278 1557 1959 1428 42 84 65 C ATOM 2964 O HIS A 278 -4.517 -4.367 10.474 1.00 15.61 O ANISOU 2964 O HIS A 278 1858 2247 1825 22 83 47 O ATOM 2965 CB HIS A 278 -4.783 -1.181 10.782 1.00 15.24 C ANISOU 2965 CB HIS A 278 1661 2122 2009 45 124 42 C ATOM 2966 CG HIS A 278 -5.133 -0.137 11.794 1.00 19.48 C ANISOU 2966 CG HIS A 278 2127 2592 2681 37 278 -18 C ATOM 2967 ND1 HIS A 278 -5.740 1.053 11.453 1.00 18.71 N ANISOU 2967 ND1 HIS A 278 1914 2387 2809 67 223 -16 N ATOM 2968 CD2 HIS A 278 -4.984 -0.111 13.144 1.00 18.42 C ANISOU 2968 CD2 HIS A 278 2056 2455 2487 -10 487 -86 C ATOM 2969 CE1 HIS A 278 -5.935 1.775 12.547 1.00 19.97 C ANISOU 2969 CE1 HIS A 278 2050 2482 3054 53 428 -99 C ATOM 2970 NE2 HIS A 278 -5.480 1.095 13.583 1.00 16.61 N ANISOU 2970 NE2 HIS A 278 1758 2121 2431 -6 596 -143 N ATOM 2971 N ATHR A 279 -2.839 -3.352 9.348 0.53 15.30 N ANISOU 2971 N ATHR A 279 1941 2296 1575 60 18 101 N ATOM 2972 N BTHR A 279 -2.865 -3.365 9.316 0.47 15.28 N ANISOU 2972 N BTHR A 279 1940 2292 1575 60 14 101 N ATOM 2973 CA ATHR A 279 -2.720 -4.405 8.344 0.53 15.73 C ANISOU 2973 CA ATHR A 279 2102 2344 1531 60 -50 106 C ATOM 2974 CA BTHR A 279 -2.809 -4.459 8.344 0.47 15.63 C ANISOU 2974 CA BTHR A 279 2087 2326 1525 58 -55 105 C ATOM 2975 C ATHR A 279 -2.360 -5.738 8.982 0.53 15.38 C ANISOU 2975 C ATHR A 279 2079 2322 1443 75 24 76 C ATOM 2976 C BTHR A 279 -2.340 -5.760 8.972 0.47 15.38 C ANISOU 2976 C BTHR A 279 2081 2322 1439 75 24 76 C ATOM 2977 O ATHR A 279 -2.674 -6.799 8.430 0.53 16.62 O ANISOU 2977 O ATHR A 279 2306 2441 1569 69 -27 63 O ATOM 2978 O BTHR A 279 -2.518 -6.823 8.366 0.47 16.44 O ANISOU 2978 O BTHR A 279 2294 2423 1529 73 -20 63 O ATOM 2979 CB ATHR A 279 -1.670 -4.005 7.294 0.53 16.30 C ANISOU 2979 CB ATHR A 279 2299 2448 1448 58 -44 127 C ATOM 2980 CB BTHR A 279 -1.880 -4.149 7.156 0.47 16.33 C ANISOU 2980 CB BTHR A 279 2315 2437 1454 52 -69 127 C ATOM 2981 OG1ATHR A 279 -2.100 -2.821 6.619 0.53 18.30 O ANISOU 2981 OG1ATHR A 279 2575 2656 1724 21 -157 172 O ATOM 2982 OG1BTHR A 279 -0.536 -3.964 7.623 0.47 16.15 O ANISOU 2982 OG1BTHR A 279 2271 2489 1377 84 68 122 O ATOM 2983 CG2ATHR A 279 -1.454 -5.106 6.278 0.53 14.01 C ANISOU 2983 CG2ATHR A 279 2170 2127 1025 44 -51 105 C ATOM 2984 CG2BTHR A 279 -2.339 -2.936 6.394 0.47 18.07 C ANISOU 2984 CG2BTHR A 279 2566 2604 1696 10 -197 176 C ATOM 2985 N ASN A 280 -1.723 -5.708 10.150 1.00 13.49 N ANISOU 2985 N ASN A 280 1807 2121 1197 80 113 73 N ATOM 2986 CA ASN A 280 -1.400 -6.957 10.826 1.00 18.53 C ANISOU 2986 CA ASN A 280 2482 2750 1809 79 134 66 C ATOM 2987 C ASN A 280 -2.660 -7.778 11.104 1.00 18.35 C ANISOU 2987 C ASN A 280 2454 2671 1849 35 119 45 C ATOM 2988 O ASN A 280 -2.604 -9.014 11.143 1.00 17.65 O ANISOU 2988 O ASN A 280 2422 2553 1732 34 95 41 O ATOM 2989 CB ASN A 280 -0.649 -6.702 12.141 1.00 16.59 C ANISOU 2989 CB ASN A 280 2244 2517 1541 51 169 89 C ATOM 2990 CG ASN A 280 -0.245 -8.010 12.813 1.00 20.77 C ANISOU 2990 CG ASN A 280 2836 3005 2051 37 131 106 C ATOM 2991 OD1 ASN A 280 -0.745 -8.375 13.884 1.00 22.93 O ANISOU 2991 OD1 ASN A 280 3180 3237 2295 -46 144 109 O ATOM 2992 ND2 ASN A 280 0.607 -8.756 12.135 1.00 17.51 N ANISOU 2992 ND2 ASN A 280 2411 2581 1661 108 100 111 N ATOM 2993 N SER A 281 -3.803 -7.116 11.278 1.00 12.62 N ANISOU 2993 N SER A 281 1642 1909 1245 -3 138 32 N ATOM 2994 CA SER A 281 -5.033 -7.854 11.518 1.00 14.45 C ANISOU 2994 CA SER A 281 1823 2070 1598 -55 144 14 C ATOM 2995 C SER A 281 -5.550 -8.562 10.264 1.00 17.65 C ANISOU 2995 C SER A 281 2246 2429 2033 -48 -16 30 C ATOM 2996 O SER A 281 -6.551 -9.274 10.361 1.00 18.52 O ANISOU 2996 O SER A 281 2304 2468 2264 -98 -45 28 O ATOM 2997 CB SER A 281 -6.101 -6.908 12.072 1.00 15.89 C ANISOU 2997 CB SER A 281 1861 2193 1984 -93 245 -15 C ATOM 2998 OG SER A 281 -5.689 -6.421 13.347 1.00 18.04 O ANISOU 2998 OG SER A 281 2192 2482 2181 -135 418 -46 O ATOM 2999 N VAL A 282 -4.903 -8.368 9.105 1.00 15.56 N ANISOU 2999 N VAL A 282 2077 2183 1652 -8 -112 46 N ATOM 3000 CA VAL A 282 -5.274 -9.022 7.847 1.00 16.13 C ANISOU 3000 CA VAL A 282 2262 2187 1679 -32 -272 57 C ATOM 3001 C VAL A 282 -4.429 -10.277 7.627 1.00 20.17 C ANISOU 3001 C VAL A 282 2927 2705 2030 -5 -227 23 C ATOM 3002 O VAL A 282 -4.874 -11.225 6.963 1.00 22.53 O ANISOU 3002 O VAL A 282 3338 2927 2295 -40 -328 13 O ATOM 3003 CB VAL A 282 -5.108 -8.052 6.645 1.00 16.71 C ANISOU 3003 CB VAL A 282 2426 2242 1681 -43 -385 88 C ATOM 3004 CG1 VAL A 282 -5.476 -8.735 5.296 1.00 16.87 C ANISOU 3004 CG1 VAL A 282 2660 2161 1590 -110 -571 101 C ATOM 3005 CG2 VAL A 282 -5.951 -6.804 6.824 1.00 14.54 C ANISOU 3005 CG2 VAL A 282 1983 1925 1616 -57 -462 128 C ATOM 3006 N VAL A 283 -3.193 -10.295 8.151 1.00 16.61 N ANISOU 3006 N VAL A 283 2481 2321 1510 56 -93 6 N ATOM 3007 CA VAL A 283 -2.221 -11.249 7.605 1.00 19.58 C ANISOU 3007 CA VAL A 283 2982 2670 1787 103 -40 -34 C ATOM 3008 C VAL A 283 -2.354 -12.669 8.177 1.00 19.78 C ANISOU 3008 C VAL A 283 3032 2637 1848 106 -58 -48 C ATOM 3009 O VAL A 283 -2.046 -13.637 7.469 1.00 21.04 O ANISOU 3009 O VAL A 283 3320 2724 1951 129 -53 -94 O ATOM 3010 CB VAL A 283 -0.766 -10.756 7.772 1.00 20.59 C ANISOU 3010 CB VAL A 283 3066 2852 1904 171 90 -39 C ATOM 3011 CG1 VAL A 283 -0.544 -9.425 7.058 1.00 24.67 C ANISOU 3011 CG1 VAL A 283 3596 3414 2362 154 116 -25 C ATOM 3012 CG2 VAL A 283 -0.370 -10.678 9.234 1.00 20.77 C ANISOU 3012 CG2 VAL A 283 2966 2909 2015 183 101 0 C ATOM 3013 N ASN A 284 -2.761 -12.849 9.436 1.00 17.70 N ANISOU 3013 N ASN A 284 2681 2384 1660 71 -63 -15 N ATOM 3014 CA ASN A 284 -2.711 -14.201 10.006 1.00 20.42 C ANISOU 3014 CA ASN A 284 3080 2659 2019 62 -90 -15 C ATOM 3015 C ASN A 284 -3.526 -15.251 9.238 1.00 22.15 C ANISOU 3015 C ASN A 284 3400 2789 2228 26 -178 -41 C ATOM 3016 O ASN A 284 -3.004 -16.363 9.044 1.00 23.77 O ANISOU 3016 O ASN A 284 3702 2917 2413 66 -188 -70 O ATOM 3017 CB ASN A 284 -3.107 -14.174 11.492 1.00 18.33 C ANISOU 3017 CB ASN A 284 2774 2402 1790 -18 -71 29 C ATOM 3018 CG ASN A 284 -2.103 -13.393 12.342 1.00 21.98 C ANISOU 3018 CG ASN A 284 3207 2912 2232 -2 -30 62 C ATOM 3019 OD1 ASN A 284 -1.030 -13.019 11.861 1.00 19.99 O ANISOU 3019 OD1 ASN A 284 2923 2686 1987 84 -22 59 O ATOM 3020 ND2 ASN A 284 -2.440 -13.160 13.614 1.00 23.57 N ANISOU 3020 ND2 ASN A 284 3441 3108 2408 -104 4 93 N ATOM 3021 N PRO A 285 -4.753 -14.994 8.769 1.00 18.73 N ANISOU 3021 N PRO A 285 2946 2336 1836 -48 -262 -30 N ATOM 3022 CA PRO A 285 -5.454 -16.027 7.976 1.00 20.63 C ANISOU 3022 CA PRO A 285 3308 2468 2061 -99 -391 -45 C ATOM 3023 C PRO A 285 -4.662 -16.517 6.765 1.00 21.90 C ANISOU 3023 C PRO A 285 3683 2569 2069 -50 -390 -109 C ATOM 3024 O PRO A 285 -4.758 -17.698 6.403 1.00 22.40 O ANISOU 3024 O PRO A 285 3892 2526 2092 -66 -442 -144 O ATOM 3025 CB PRO A 285 -6.751 -15.320 7.549 1.00 20.84 C ANISOU 3025 CB PRO A 285 3243 2469 2205 -184 -521 -5 C ATOM 3026 CG PRO A 285 -6.969 -14.264 8.651 1.00 20.85 C ANISOU 3026 CG PRO A 285 3029 2553 2340 -182 -398 21 C ATOM 3027 CD PRO A 285 -5.588 -13.795 8.988 1.00 21.72 C ANISOU 3027 CD PRO A 285 3176 2756 2321 -93 -265 1 C ATOM 3028 N PHE A 286 -3.872 -15.643 6.134 1.00 20.78 N ANISOU 3028 N PHE A 286 3582 2476 1838 -2 -303 -134 N ATOM 3029 CA PHE A 286 -3.045 -16.062 5.001 1.00 23.24 C ANISOU 3029 CA PHE A 286 4120 2714 1998 28 -215 -217 C ATOM 3030 C PHE A 286 -1.913 -16.977 5.439 1.00 25.39 C ANISOU 3030 C PHE A 286 4370 2945 2332 137 -62 -275 C ATOM 3031 O PHE A 286 -1.618 -17.971 4.763 1.00 26.98 O ANISOU 3031 O PHE A 286 4754 3021 2476 153 -10 -358 O ATOM 3032 CB PHE A 286 -2.492 -14.837 4.285 1.00 27.84 C ANISOU 3032 CB PHE A 286 4747 3352 2478 28 -129 -224 C ATOM 3033 CG PHE A 286 -3.529 -14.107 3.509 1.00 28.17 C ANISOU 3033 CG PHE A 286 4891 3366 2446 -90 -328 -170 C ATOM 3034 CD1 PHE A 286 -4.316 -13.146 4.121 1.00 27.63 C ANISOU 3034 CD1 PHE A 286 4604 3364 2529 -112 -447 -84 C ATOM 3035 CD2 PHE A 286 -3.746 -14.416 2.177 1.00 30.51 C ANISOU 3035 CD2 PHE A 286 5519 3537 2536 -191 -412 -205 C ATOM 3036 CE1 PHE A 286 -5.303 -12.484 3.402 1.00 29.53 C ANISOU 3036 CE1 PHE A 286 4902 3540 2778 -214 -677 -20 C ATOM 3037 CE2 PHE A 286 -4.730 -13.759 1.453 1.00 33.25 C ANISOU 3037 CE2 PHE A 286 5957 3821 2855 -318 -668 -124 C ATOM 3038 CZ PHE A 286 -5.515 -12.804 2.068 1.00 29.91 C ANISOU 3038 CZ PHE A 286 5281 3457 2627 -323 -826 -28 C ATOM 3039 N ILE A 287 -1.268 -16.664 6.567 1.00 23.65 N ANISOU 3039 N ILE A 287 3940 2800 2247 205 -7 -230 N ATOM 3040 CA ILE A 287 -0.233 -17.558 7.087 1.00 26.60 C ANISOU 3040 CA ILE A 287 4260 3097 2749 303 63 -255 C ATOM 3041 C ILE A 287 -0.817 -18.928 7.406 1.00 26.19 C ANISOU 3041 C ILE A 287 4293 2934 2725 275 -54 -255 C ATOM 3042 O ILE A 287 -0.226 -19.962 7.061 1.00 28.41 O ANISOU 3042 O ILE A 287 4654 3077 3062 343 -1 -324 O ATOM 3043 CB ILE A 287 0.454 -16.946 8.322 1.00 25.98 C ANISOU 3043 CB ILE A 287 3975 3094 2802 340 56 -175 C ATOM 3044 CG1 ILE A 287 0.985 -15.548 8.004 1.00 26.03 C ANISOU 3044 CG1 ILE A 287 3899 3206 2784 355 159 -170 C ATOM 3045 CG2 ILE A 287 1.605 -17.840 8.763 1.00 26.37 C ANISOU 3045 CG2 ILE A 287 3954 3023 3043 439 71 -181 C ATOM 3046 CD1 ILE A 287 2.045 -15.564 6.895 1.00 28.59 C ANISOU 3046 CD1 ILE A 287 4263 3471 3127 429 360 -262 C ATOM 3047 N TYR A 288 -1.985 -18.968 8.067 1.00 21.67 N ANISOU 3047 N TYR A 288 3697 2399 2139 170 -193 -183 N ATOM 3048 CA TYR A 288 -2.607 -20.265 8.339 1.00 22.96 C ANISOU 3048 CA TYR A 288 3950 2451 2324 119 -305 -175 C ATOM 3049 C TYR A 288 -2.921 -21.006 7.045 1.00 24.16 C ANISOU 3049 C TYR A 288 4314 2484 2380 103 -328 -260 C ATOM 3050 O TYR A 288 -2.708 -22.221 6.951 1.00 27.94 O ANISOU 3050 O TYR A 288 4906 2823 2888 130 -349 -304 O ATOM 3051 CB TYR A 288 -3.887 -20.115 9.161 1.00 23.08 C ANISOU 3051 CB TYR A 288 3895 2514 2359 -14 -399 -95 C ATOM 3052 CG TYR A 288 -3.713 -19.418 10.479 1.00 25.03 C ANISOU 3052 CG TYR A 288 4012 2850 2647 -41 -353 -25 C ATOM 3053 CD1 TYR A 288 -2.654 -19.731 11.318 1.00 28.33 C ANISOU 3053 CD1 TYR A 288 4428 3234 3103 9 -358 9 C ATOM 3054 CD2 TYR A 288 -4.608 -18.437 10.887 1.00 21.77 C ANISOU 3054 CD2 TYR A 288 3493 2526 2252 -126 -316 7 C ATOM 3055 CE1 TYR A 288 -2.500 -19.089 12.549 1.00 29.30 C ANISOU 3055 CE1 TYR A 288 4503 3412 3216 -53 -346 79 C ATOM 3056 CE2 TYR A 288 -4.451 -17.780 12.102 1.00 21.22 C ANISOU 3056 CE2 TYR A 288 3363 2515 2184 -170 -242 52 C ATOM 3057 CZ TYR A 288 -3.396 -18.106 12.924 1.00 25.35 C ANISOU 3057 CZ TYR A 288 3944 3008 2681 -146 -266 90 C ATOM 3058 OH TYR A 288 -3.235 -17.450 14.135 1.00 26.08 O ANISOU 3058 OH TYR A 288 4047 3134 2730 -225 -223 139 O ATOM 3059 N ALA A 289 -3.439 -20.293 6.043 1.00 23.45 N ANISOU 3059 N ALA A 289 4314 2425 2171 44 -348 -281 N ATOM 3060 CA ALA A 289 -3.820 -20.931 4.785 1.00 24.73 C ANISOU 3060 CA ALA A 289 4754 2452 2189 -18 -410 -352 C ATOM 3061 C ALA A 289 -2.607 -21.474 4.041 1.00 31.25 C ANISOU 3061 C ALA A 289 5755 3167 2952 80 -201 -485 C ATOM 3062 O ALA A 289 -2.681 -22.539 3.408 1.00 31.96 O ANISOU 3062 O ALA A 289 6083 3092 2970 58 -210 -567 O ATOM 3063 CB ALA A 289 -4.568 -19.932 3.906 1.00 23.86 C ANISOU 3063 CB ALA A 289 4728 2375 1963 -125 -523 -321 C ATOM 3064 N TYR A 290 -1.482 -20.752 4.088 1.00 29.76 N ANISOU 3064 N TYR A 290 5450 3047 2812 183 7 -515 N ATOM 3065 CA TYR A 290 -0.316 -21.172 3.314 1.00 35.39 C ANISOU 3065 CA TYR A 290 6293 3635 3518 273 271 -657 C ATOM 3066 C TYR A 290 0.523 -22.217 4.040 1.00 35.00 C ANISOU 3066 C TYR A 290 6100 3472 3727 412 339 -688 C ATOM 3067 O TYR A 290 1.205 -23.017 3.390 1.00 34.16 O ANISOU 3067 O TYR A 290 6127 3188 3664 481 530 -825 O ATOM 3068 CB TYR A 290 0.543 -19.961 2.963 1.00 38.26 C ANISOU 3068 CB TYR A 290 6580 4094 3864 308 481 -677 C ATOM 3069 CG TYR A 290 0.094 -19.288 1.692 1.00 43.66 C ANISOU 3069 CG TYR A 290 7567 4771 4249 170 499 -712 C ATOM 3070 CD1 TYR A 290 0.421 -19.829 0.454 1.00 47.63 C ANISOU 3070 CD1 TYR A 290 8289 5153 4656 109 649 -790 C ATOM 3071 CD2 TYR A 290 -0.669 -18.123 1.723 1.00 47.24 C ANISOU 3071 CD2 TYR A 290 7976 5361 4613 75 315 -598 C ATOM 3072 CE1 TYR A 290 0.011 -19.238 -0.720 1.00 50.75 C ANISOU 3072 CE1 TYR A 290 8896 5542 4843 -50 601 -746 C ATOM 3073 CE2 TYR A 290 -1.082 -17.510 0.541 1.00 51.13 C ANISOU 3073 CE2 TYR A 290 8649 5838 4941 -69 253 -558 C ATOM 3074 CZ TYR A 290 -0.736 -18.082 -0.675 1.00 53.75 C ANISOU 3074 CZ TYR A 290 9235 6032 5157 -136 389 -626 C ATOM 3075 OH TYR A 290 -1.132 -17.512 -1.861 1.00 60.17 O ANISOU 3075 OH TYR A 290 10278 6787 5795 -293 312 -574 O ATOM 3076 N ARG A 291 0.474 -22.249 5.372 1.00 31.56 N ANISOU 3076 N ARG A 291 5419 3107 3467 442 182 -566 N ATOM 3077 CA ARG A 291 1.392 -23.083 6.135 1.00 33.26 C ANISOU 3077 CA ARG A 291 5483 3198 3957 566 189 -562 C ATOM 3078 C ARG A 291 0.731 -24.232 6.882 1.00 31.89 C ANISOU 3078 C ARG A 291 5360 2930 3828 521 -37 -498 C ATOM 3079 O ARG A 291 1.443 -25.128 7.345 1.00 33.00 O ANISOU 3079 O ARG A 291 5434 2910 4195 616 -66 -501 O ATOM 3080 CB ARG A 291 2.190 -22.224 7.136 1.00 32.44 C ANISOU 3080 CB ARG A 291 5091 3198 4036 625 172 -459 C ATOM 3081 CG ARG A 291 3.174 -21.254 6.467 1.00 35.39 C ANISOU 3081 CG ARG A 291 5368 3619 4460 694 423 -525 C ATOM 3082 CD ARG A 291 4.302 -20.858 7.416 1.00 36.48 C ANISOU 3082 CD ARG A 291 5206 3757 4899 785 394 -441 C ATOM 3083 NE ARG A 291 4.868 -22.026 8.095 1.00 40.72 N ANISOU 3083 NE ARG A 291 5646 4095 5729 872 269 -414 N ATOM 3084 CZ ARG A 291 6.081 -22.530 7.874 1.00 44.26 C ANISOU 3084 CZ ARG A 291 5928 4351 6536 1020 405 -482 C ATOM 3085 NH1 ARG A 291 6.891 -21.960 6.990 1.00 43.99 N ANISOU 3085 NH1 ARG A 291 5806 4307 6600 1088 725 -593 N ATOM 3086 NH2 ARG A 291 6.487 -23.603 8.554 1.00 44.81 N ANISOU 3086 NH2 ARG A 291 5911 4216 6897 1092 224 -434 N ATOM 3087 N ILE A 292 -0.590 -24.248 7.025 1.00 28.62 N ANISOU 3087 N ILE A 292 5045 2588 3241 374 -204 -434 N ATOM 3088 CA ILE A 292 -1.243 -25.266 7.844 1.00 30.51 C ANISOU 3088 CA ILE A 292 5321 2747 3524 303 -402 -357 C ATOM 3089 C ILE A 292 -2.307 -25.946 6.995 1.00 30.49 C ANISOU 3089 C ILE A 292 5551 2663 3370 197 -480 -409 C ATOM 3090 O ILE A 292 -3.368 -25.362 6.727 1.00 28.91 O ANISOU 3090 O ILE A 292 5377 2565 3044 72 -558 -369 O ATOM 3091 CB ILE A 292 -1.838 -24.693 9.137 1.00 31.91 C ANISOU 3091 CB ILE A 292 5363 3065 3697 197 -524 -209 C ATOM 3092 CG1 ILE A 292 -0.790 -23.841 9.863 1.00 33.17 C ANISOU 3092 CG1 ILE A 292 5338 3303 3963 276 -472 -158 C ATOM 3093 CG2 ILE A 292 -2.291 -25.843 10.056 1.00 33.76 C ANISOU 3093 CG2 ILE A 292 5665 3183 3979 112 -695 -130 C ATOM 3094 CD1 ILE A 292 -1.284 -23.163 11.148 1.00 30.30 C ANISOU 3094 CD1 ILE A 292 4901 3062 3551 153 -553 -31 C ATOM 3095 N ARG A 293 -2.013 -27.176 6.561 1.00 41.31 N ANISOU 3095 N ARG A 293 7006 3582 5108 224 959 -1541 N ATOM 3096 CA ARG A 293 -2.874 -27.886 5.618 1.00 43.14 C ANISOU 3096 CA ARG A 293 7550 3687 5153 96 886 -1682 C ATOM 3097 C ARG A 293 -4.297 -28.020 6.147 1.00 42.49 C ANISOU 3097 C ARG A 293 7621 3451 5073 -140 606 -1373 C ATOM 3098 O ARG A 293 -5.266 -27.847 5.400 1.00 42.79 O ANISOU 3098 O ARG A 293 7809 3566 4884 -371 541 -1341 O ATOM 3099 CB ARG A 293 -2.282 -29.267 5.322 1.00 47.75 C ANISOU 3099 CB ARG A 293 8162 4043 5939 362 797 -2016 C ATOM 3100 CG ARG A 293 -3.063 -30.093 4.323 1.00 53.86 C ANISOU 3100 CG ARG A 293 9178 4714 6573 250 646 -2193 C ATOM 3101 CD ARG A 293 -2.470 -31.497 4.179 1.00 65.03 C ANISOU 3101 CD ARG A 293 10592 5834 8284 533 514 -2548 C ATOM 3102 NE ARG A 293 -1.199 -31.512 3.454 1.00 74.14 N ANISOU 3102 NE ARG A 293 11566 7230 9372 859 764 -2960 N ATOM 3103 CZ ARG A 293 0.004 -31.492 4.027 1.00 77.61 C ANISOU 3103 CZ ARG A 293 11777 7693 10017 1209 842 -3034 C ATOM 3104 NH1 ARG A 293 0.121 -31.449 5.350 1.00 75.46 N ANISOU 3104 NH1 ARG A 293 11370 7208 10092 1226 696 -2755 N ATOM 3105 NH2 ARG A 293 1.096 -31.516 3.272 1.00 81.88 N ANISOU 3105 NH2 ARG A 293 12275 8474 10362 1499 1161 -3283 N ATOM 3106 N GLU A 294 -4.444 -28.315 7.438 1.00 41.47 N ANISOU 3106 N GLU A 294 7434 3144 5180 -96 438 -1133 N ATOM 3107 CA GLU A 294 -5.776 -28.520 7.996 1.00 41.39 C ANISOU 3107 CA GLU A 294 7509 3044 5173 -342 234 -832 C ATOM 3108 C GLU A 294 -6.617 -27.243 7.947 1.00 36.65 C ANISOU 3108 C GLU A 294 6774 2784 4367 -524 290 -620 C ATOM 3109 O GLU A 294 -7.836 -27.315 7.754 1.00 36.96 O ANISOU 3109 O GLU A 294 6852 2847 4345 -754 163 -491 O ATOM 3110 CB GLU A 294 -5.661 -29.046 9.424 1.00 45.03 C ANISOU 3110 CB GLU A 294 7952 3309 5850 -263 92 -587 C ATOM 3111 CG GLU A 294 -6.963 -29.570 10.000 1.00 49.05 C ANISOU 3111 CG GLU A 294 8552 3705 6381 -553 -79 -275 C ATOM 3112 CD GLU A 294 -7.398 -30.868 9.379 1.00 54.46 C ANISOU 3112 CD GLU A 294 9408 4081 7204 -680 -267 -380 C ATOM 3113 OE1 GLU A 294 -6.521 -31.661 8.974 1.00 58.06 O ANISOU 3113 OE1 GLU A 294 9924 4322 7814 -448 -312 -648 O ATOM 3114 OE2 GLU A 294 -8.622 -31.096 9.291 1.00 55.96 O ANISOU 3114 OE2 GLU A 294 9602 4286 7375 -998 -372 -209 O ATOM 3115 N PHE A 295 -5.997 -26.068 8.136 1.00 28.75 N ANISOU 3115 N PHE A 295 5598 2023 3301 -422 445 -587 N ATOM 3116 CA PHE A 295 -6.723 -24.812 7.935 1.00 27.93 C ANISOU 3116 CA PHE A 295 5414 2167 3032 -546 459 -431 C ATOM 3117 C PHE A 295 -7.051 -24.600 6.460 1.00 32.54 C ANISOU 3117 C PHE A 295 6142 2840 3381 -687 474 -546 C ATOM 3118 O PHE A 295 -8.186 -24.260 6.103 1.00 34.45 O ANISOU 3118 O PHE A 295 6409 3164 3517 -840 329 -424 O ATOM 3119 CB PHE A 295 -5.912 -23.615 8.456 1.00 25.30 C ANISOU 3119 CB PHE A 295 4910 1980 2721 -427 570 -384 C ATOM 3120 CG PHE A 295 -6.228 -23.231 9.879 1.00 30.96 C ANISOU 3120 CG PHE A 295 5507 2733 3524 -349 488 -204 C ATOM 3121 CD1 PHE A 295 -7.436 -22.615 10.197 1.00 25.23 C ANISOU 3121 CD1 PHE A 295 4727 2134 2724 -417 415 -45 C ATOM 3122 CD2 PHE A 295 -5.313 -23.486 10.904 1.00 31.24 C ANISOU 3122 CD2 PHE A 295 5472 2705 3693 -180 473 -219 C ATOM 3123 CE1 PHE A 295 -7.737 -22.265 11.506 1.00 25.93 C ANISOU 3123 CE1 PHE A 295 4710 2315 2826 -320 389 68 C ATOM 3124 CE2 PHE A 295 -5.603 -23.120 12.218 1.00 30.91 C ANISOU 3124 CE2 PHE A 295 5369 2739 3635 -108 396 -73 C ATOM 3125 CZ PHE A 295 -6.819 -22.510 12.521 1.00 27.09 C ANISOU 3125 CZ PHE A 295 4849 2413 3032 -178 384 56 C ATOM 3126 N ARG A 296 -6.051 -24.775 5.594 1.00 32.52 N ANISOU 3126 N ARG A 296 6220 2863 3274 -624 647 -786 N ATOM 3127 CA ARG A 296 -6.233 -24.552 4.167 1.00 32.78 C ANISOU 3127 CA ARG A 296 6442 3035 2978 -759 693 -897 C ATOM 3128 C ARG A 296 -7.383 -25.391 3.619 1.00 35.18 C ANISOU 3128 C ARG A 296 6950 3220 3198 -908 440 -959 C ATOM 3129 O ARG A 296 -8.254 -24.881 2.901 1.00 37.40 O ANISOU 3129 O ARG A 296 7328 3628 3254 -1073 290 -860 O ATOM 3130 CB ARG A 296 -4.925 -24.869 3.443 1.00 34.69 C ANISOU 3130 CB ARG A 296 6709 3358 3114 -643 982 -1200 C ATOM 3131 CG ARG A 296 -5.001 -24.799 1.951 1.00 38.86 C ANISOU 3131 CG ARG A 296 7484 4075 3207 -773 1078 -1357 C ATOM 3132 CD ARG A 296 -3.606 -24.786 1.337 1.00 44.65 C ANISOU 3132 CD ARG A 296 8114 5029 3821 -661 1466 -1595 C ATOM 3133 NE ARG A 296 -2.864 -26.034 1.525 1.00 45.54 N ANISOU 3133 NE ARG A 296 8107 4998 4197 -370 1509 -1934 N ATOM 3134 CZ ARG A 296 -1.815 -26.172 2.331 1.00 45.95 C ANISOU 3134 CZ ARG A 296 7878 5002 4578 -150 1654 -2026 C ATOM 3135 NH1 ARG A 296 -1.201 -27.340 2.424 1.00 48.36 N ANISOU 3135 NH1 ARG A 296 8098 5152 5123 154 1614 -2332 N ATOM 3136 NH2 ARG A 296 -1.370 -25.144 3.044 1.00 45.16 N ANISOU 3136 NH2 ARG A 296 7549 5003 4605 -211 1764 -1797 N ATOM 3137 N GLN A 297 -7.410 -26.683 3.961 1.00 35.07 N ANISOU 3137 N GLN A 297 7007 2927 3390 -862 339 -1111 N ATOM 3138 CA GLN A 297 -8.458 -27.570 3.465 1.00 37.46 C ANISOU 3138 CA GLN A 297 7503 3058 3673 -1054 59 -1189 C ATOM 3139 C GLN A 297 -9.829 -27.175 4.005 1.00 36.66 C ANISOU 3139 C GLN A 297 7233 3027 3668 -1263 -164 -855 C ATOM 3140 O GLN A 297 -10.831 -27.250 3.286 1.00 38.56 O ANISOU 3140 O GLN A 297 7550 3311 3791 -1469 -402 -859 O ATOM 3141 CB GLN A 297 -8.129 -29.021 3.829 1.00 39.78 C ANISOU 3141 CB GLN A 297 7862 2995 4257 -948 -31 -1358 C ATOM 3142 CG GLN A 297 -6.866 -29.545 3.158 1.00 53.54 C ANISOU 3142 CG GLN A 297 9634 4741 5968 -662 151 -1729 C ATOM 3143 CD GLN A 297 -6.527 -30.980 3.548 1.00 57.99 C ANISOU 3143 CD GLN A 297 10214 4926 6892 -498 -1 -1890 C ATOM 3144 OE1 GLN A 297 -6.859 -31.432 4.646 1.00 62.70 O ANISOU 3144 OE1 GLN A 297 10767 5275 7781 -552 -157 -1638 O ATOM 3145 NE2 GLN A 297 -5.856 -31.699 2.650 1.00 56.68 N ANISOU 3145 NE2 GLN A 297 10112 4727 6698 -299 47 -2308 N ATOM 3146 N THR A 298 -9.898 -26.764 5.272 1.00 33.37 N ANISOU 3146 N THR A 298 6568 2653 3457 -1201 -97 -590 N ATOM 3147 CA THR A 298 -11.176 -26.342 5.837 1.00 34.21 C ANISOU 3147 CA THR A 298 6447 2904 3648 -1352 -238 -311 C ATOM 3148 C THR A 298 -11.652 -25.030 5.217 1.00 31.98 C ANISOU 3148 C THR A 298 6084 2896 3172 -1343 -284 -232 C ATOM 3149 O THR A 298 -12.845 -24.873 4.942 1.00 33.84 O ANISOU 3149 O THR A 298 6202 3241 3415 -1491 -506 -133 O ATOM 3150 CB THR A 298 -11.058 -26.212 7.354 1.00 32.53 C ANISOU 3150 CB THR A 298 6026 2716 3619 -1253 -115 -92 C ATOM 3151 OG1 THR A 298 -10.536 -27.433 7.887 1.00 35.37 O ANISOU 3151 OG1 THR A 298 6520 2773 4145 -1250 -125 -121 O ATOM 3152 CG2 THR A 298 -12.429 -25.936 7.981 1.00 33.41 C ANISOU 3152 CG2 THR A 298 5857 3027 3809 -1406 -199 157 C ATOM 3153 N PHE A 299 -10.737 -24.075 4.998 1.00 30.75 N ANISOU 3153 N PHE A 299 5975 2837 2873 -1181 -108 -256 N ATOM 3154 CA PHE A 299 -11.080 -22.855 4.264 1.00 31.46 C ANISOU 3154 CA PHE A 299 6088 3100 2767 -1188 -196 -155 C ATOM 3155 C PHE A 299 -11.684 -23.188 2.904 1.00 35.84 C ANISOU 3155 C PHE A 299 6866 3686 3066 -1364 -423 -249 C ATOM 3156 O PHE A 299 -12.696 -22.603 2.500 1.00 36.24 O ANISOU 3156 O PHE A 299 6861 3848 3061 -1425 -689 -112 O ATOM 3157 CB PHE A 299 -9.846 -21.958 4.065 1.00 30.27 C ANISOU 3157 CB PHE A 299 6018 2994 2491 -1082 35 -161 C ATOM 3158 CG PHE A 299 -9.304 -21.321 5.337 1.00 28.18 C ANISOU 3158 CG PHE A 299 5541 2712 2454 -915 170 -70 C ATOM 3159 CD1 PHE A 299 -10.004 -21.373 6.529 1.00 27.58 C ANISOU 3159 CD1 PHE A 299 5249 2642 2588 -837 102 26 C ATOM 3160 CD2 PHE A 299 -8.070 -20.662 5.319 1.00 26.81 C ANISOU 3160 CD2 PHE A 299 5382 2547 2258 -861 368 -93 C ATOM 3161 CE1 PHE A 299 -9.474 -20.772 7.691 1.00 26.29 C ANISOU 3161 CE1 PHE A 299 4946 2482 2560 -671 202 65 C ATOM 3162 CE2 PHE A 299 -7.537 -20.074 6.470 1.00 25.05 C ANISOU 3162 CE2 PHE A 299 4985 2292 2241 -724 429 -47 C ATOM 3163 CZ PHE A 299 -8.242 -20.128 7.648 1.00 23.77 C ANISOU 3163 CZ PHE A 299 4668 2125 2237 -613 331 16 C ATOM 3164 N ARG A 300 -11.049 -24.110 2.168 1.00 38.10 N ANISOU 3164 N ARG A 300 7412 3881 3183 -1414 -346 -512 N ATOM 3165 CA ARG A 300 -11.575 -24.512 0.864 1.00 45.64 C ANISOU 3165 CA ARG A 300 8641 4872 3830 -1578 -582 -666 C ATOM 3166 C ARG A 300 -12.998 -25.038 0.981 1.00 45.89 C ANISOU 3166 C ARG A 300 8537 4848 4053 -1760 -966 -604 C ATOM 3167 O ARG A 300 -13.871 -24.675 0.183 1.00 43.30 O ANISOU 3167 O ARG A 300 8261 4646 3546 -1878 -1286 -548 O ATOM 3168 CB ARG A 300 -10.682 -25.576 0.227 1.00 53.60 C ANISOU 3168 CB ARG A 300 9934 5763 4667 -1551 -424 -1049 C ATOM 3169 CG ARG A 300 -9.315 -25.081 -0.179 1.00 59.50 C ANISOU 3169 CG ARG A 300 10767 6668 5172 -1407 -28 -1145 C ATOM 3170 CD ARG A 300 -8.608 -26.081 -1.085 1.00 67.17 C ANISOU 3170 CD ARG A 300 11849 7652 6022 -1288 112 -1502 C ATOM 3171 NE ARG A 300 -7.286 -25.580 -1.441 1.00 71.46 N ANISOU 3171 NE ARG A 300 12335 8424 6394 -1158 525 -1564 N ATOM 3172 CZ ARG A 300 -7.066 -24.679 -2.391 1.00 75.76 C ANISOU 3172 CZ ARG A 300 12967 9265 6553 -1250 643 -1433 C ATOM 3173 NH1 ARG A 300 -8.079 -24.186 -3.097 1.00 74.21 N ANISOU 3173 NH1 ARG A 300 12950 9149 6099 -1422 344 -1244 N ATOM 3174 NH2 ARG A 300 -5.829 -24.272 -2.636 1.00 81.62 N ANISOU 3174 NH2 ARG A 300 13593 10226 7193 -1178 1039 -1468 N ATOM 3175 N LYS A 301 -13.248 -25.901 1.968 1.00 44.49 N ANISOU 3175 N LYS A 301 8174 4488 4241 -1810 -959 -589 N ATOM 3176 CA LYS A 301 -14.584 -26.465 2.140 1.00 49.51 C ANISOU 3176 CA LYS A 301 8616 5090 5105 -2056 -1285 -502 C ATOM 3177 C LYS A 301 -15.613 -25.381 2.434 1.00 44.53 C ANISOU 3177 C LYS A 301 7617 4739 4565 -2037 -1424 -227 C ATOM 3178 O LYS A 301 -16.710 -25.388 1.865 1.00 45.96 O ANISOU 3178 O LYS A 301 7684 5020 4757 -2206 -1785 -201 O ATOM 3179 CB LYS A 301 -14.577 -27.506 3.258 1.00 53.61 C ANISOU 3179 CB LYS A 301 9013 5370 5986 -2146 -1198 -446 C ATOM 3180 CG LYS A 301 -14.015 -28.854 2.851 1.00 62.73 C ANISOU 3180 CG LYS A 301 10524 6145 7164 -2220 -1260 -743 C ATOM 3181 CD LYS A 301 -14.139 -29.875 3.984 1.00 66.23 C ANISOU 3181 CD LYS A 301 10847 6322 7996 -2321 -1238 -584 C ATOM 3182 CE LYS A 301 -13.476 -31.189 3.605 1.00 71.19 C ANISOU 3182 CE LYS A 301 11713 6618 8719 -2195 -1265 -850 C ATOM 3183 NZ LYS A 301 -13.563 -32.199 4.700 1.00 74.44 N ANISOU 3183 NZ LYS A 301 12039 6752 9491 -2274 -1276 -645 N ATOM 3184 N ILE A 302 -15.282 -24.449 3.328 1.00 38.62 N ANISOU 3184 N ILE A 302 6662 4108 3903 -1809 -1175 -53 N ATOM 3185 CA ILE A 302 -16.206 -23.372 3.674 1.00 38.63 C ANISOU 3185 CA ILE A 302 6310 4345 4021 -1702 -1293 147 C ATOM 3186 C ILE A 302 -16.483 -22.500 2.459 1.00 42.42 C ANISOU 3186 C ILE A 302 6959 4914 4244 -1658 -1583 163 C ATOM 3187 O ILE A 302 -17.639 -22.189 2.145 1.00 44.37 O ANISOU 3187 O ILE A 302 6976 5304 4580 -1694 -1927 246 O ATOM 3188 CB ILE A 302 -15.647 -22.530 4.838 1.00 39.77 C ANISOU 3188 CB ILE A 302 6295 4546 4269 -1433 -982 253 C ATOM 3189 CG1 ILE A 302 -15.520 -23.354 6.120 1.00 38.26 C ANISOU 3189 CG1 ILE A 302 5940 4316 4282 -1480 -745 295 C ATOM 3190 CG2 ILE A 302 -16.521 -21.303 5.070 1.00 41.23 C ANISOU 3190 CG2 ILE A 302 6171 4934 4561 -1238 -1123 381 C ATOM 3191 CD1 ILE A 302 -14.770 -22.613 7.218 1.00 35.80 C ANISOU 3191 CD1 ILE A 302 5565 4046 3990 -1214 -467 342 C ATOM 3192 N ILE A 303 -15.423 -22.086 1.760 1.00 41.23 N ANISOU 3192 N ILE A 303 7197 4699 3768 -1588 -1455 107 N ATOM 3193 CA ILE A 303 -15.588 -21.216 0.599 1.00 44.39 C ANISOU 3193 CA ILE A 303 7840 5178 3849 -1576 -1717 194 C ATOM 3194 C ILE A 303 -16.381 -21.929 -0.494 1.00 48.85 C ANISOU 3194 C ILE A 303 8558 5786 4218 -1799 -2121 78 C ATOM 3195 O ILE A 303 -17.323 -21.368 -1.064 1.00 50.89 O ANISOU 3195 O ILE A 303 8754 6152 4429 -1800 -2542 205 O ATOM 3196 CB ILE A 303 -14.215 -20.732 0.094 1.00 44.54 C ANISOU 3196 CB ILE A 303 8234 5160 3529 -1535 -1421 184 C ATOM 3197 CG1 ILE A 303 -13.570 -19.817 1.140 1.00 44.77 C ANISOU 3197 CG1 ILE A 303 8086 5135 3791 -1334 -1147 319 C ATOM 3198 CG2 ILE A 303 -14.351 -20.009 -1.238 1.00 44.84 C ANISOU 3198 CG2 ILE A 303 8624 5286 3129 -1606 -1685 312 C ATOM 3199 CD1 ILE A 303 -12.056 -19.728 1.041 1.00 46.42 C ANISOU 3199 CD1 ILE A 303 8504 5306 3829 -1340 -752 252 C ATOM 3200 N ARG A 304 -16.033 -23.186 -0.784 1.00 52.39 N ANISOU 3200 N ARG A 304 9208 6122 4574 -1973 -2050 -187 N ATOM 3201 CA ARG A 304 -16.729 -23.914 -1.847 1.00 59.13 C ANISOU 3201 CA ARG A 304 10264 6982 5219 -2202 -2471 -364 C ATOM 3202 C ARG A 304 -18.183 -24.173 -1.481 1.00 63.28 C ANISOU 3202 C ARG A 304 10339 7560 6143 -2348 -2869 -270 C ATOM 3203 O ARG A 304 -19.078 -24.006 -2.315 1.00 68.71 O ANISOU 3203 O ARG A 304 10997 8363 6746 -2409 -3298 -242 O ATOM 3204 CB ARG A 304 -16.016 -25.231 -2.156 1.00 61.13 C ANISOU 3204 CB ARG A 304 10770 7047 5408 -2261 -2256 -699 C ATOM 3205 CG ARG A 304 -14.706 -25.063 -2.904 1.00 64.77 C ANISOU 3205 CG ARG A 304 11581 7562 5465 -2096 -1879 -836 C ATOM 3206 CD ARG A 304 -13.928 -26.367 -2.983 1.00 73.66 C ANISOU 3206 CD ARG A 304 12841 8501 6645 -2047 -1643 -1194 C ATOM 3207 NE ARG A 304 -12.651 -26.187 -3.676 1.00 81.56 N ANISOU 3207 NE ARG A 304 14060 9636 7293 -1873 -1254 -1347 N ATOM 3208 CZ ARG A 304 -11.674 -27.090 -3.707 1.00 85.56 C ANISOU 3208 CZ ARG A 304 14632 10038 7838 -1726 -971 -1669 C ATOM 3209 NH1 ARG A 304 -10.551 -26.830 -4.365 1.00 86.94 N ANISOU 3209 NH1 ARG A 304 14915 10421 7697 -1577 -611 -1799 N ATOM 3210 NH2 ARG A 304 -11.813 -28.250 -3.077 1.00 86.88 N ANISOU 3210 NH2 ARG A 304 14724 9898 8390 -1725 -1058 -1845 N ATOM 3211 N SER A 305 -18.442 -24.565 -0.238 1.00 64.55 N ANISOU 3211 N SER A 305 10084 7673 6769 -2370 -2669 -191 N ATOM 3212 CA SER A 305 -19.797 -24.904 0.172 1.00 73.35 C ANISOU 3212 CA SER A 305 10695 8893 8283 -2565 -2963 -95 C ATOM 3213 C SER A 305 -20.668 -23.683 0.436 1.00 78.42 C ANISOU 3213 C SER A 305 10883 9815 9098 -2350 -3123 135 C ATOM 3214 O SER A 305 -21.898 -23.802 0.392 1.00 82.31 O ANISOU 3214 O SER A 305 10940 10475 9858 -2490 -3478 186 O ATOM 3215 CB SER A 305 -19.760 -25.785 1.426 1.00 71.91 C ANISOU 3215 CB SER A 305 10249 8592 8481 -2705 -2651 -48 C ATOM 3216 OG SER A 305 -18.949 -26.934 1.227 1.00 71.05 O ANISOU 3216 OG SER A 305 10565 8148 8281 -2850 -2553 -268 O ATOM 3217 N HIS A 306 -20.074 -22.514 0.697 1.00 79.79 N ANISOU 3217 N HIS A 306 11127 10027 9162 -2009 -2901 257 N ATOM 3218 CA HIS A 306 -20.840 -21.370 1.181 1.00 84.08 C ANISOU 3218 CA HIS A 306 11224 10768 9954 -1728 -3009 431 C ATOM 3219 C HIS A 306 -20.623 -20.066 0.422 1.00 84.14 C ANISOU 3219 C HIS A 306 11516 10744 9708 -1461 -3238 550 C ATOM 3220 O HIS A 306 -21.376 -19.117 0.664 1.00 85.62 O ANISOU 3220 O HIS A 306 11359 11042 10132 -1192 -3452 667 O ATOM 3221 CB HIS A 306 -20.546 -21.123 2.671 1.00 84.79 C ANISOU 3221 CB HIS A 306 11001 10907 10308 -1537 -2522 485 C ATOM 3222 CG HIS A 306 -20.917 -22.272 3.558 1.00 86.71 C ANISOU 3222 CG HIS A 306 10918 11215 10814 -1801 -2311 470 C ATOM 3223 ND1 HIS A 306 -20.177 -22.625 4.666 1.00 85.17 N ANISOU 3223 ND1 HIS A 306 10748 10952 10660 -1779 -1846 487 N ATOM 3224 CD2 HIS A 306 -21.951 -23.144 3.503 1.00 90.09 C ANISOU 3224 CD2 HIS A 306 10998 11755 11477 -2130 -2528 476 C ATOM 3225 CE1 HIS A 306 -20.738 -23.667 5.254 1.00 87.37 C ANISOU 3225 CE1 HIS A 306 10750 11286 11159 -2085 -1774 540 C ATOM 3226 NE2 HIS A 306 -21.816 -24.002 4.567 1.00 89.85 N ANISOU 3226 NE2 HIS A 306 10819 11706 11615 -2325 -2169 534 N ATOM 3227 N VAL A 307 -19.624 -19.967 -0.454 1.00 82.56 N ANISOU 3227 N VAL A 307 11920 10400 9049 -1518 -3188 534 N ATOM 3228 CA VAL A 307 -19.525 -18.811 -1.354 1.00 83.34 C ANISOU 3228 CA VAL A 307 12351 10465 8851 -1369 -3481 720 C ATOM 3229 C VAL A 307 -19.173 -19.268 -2.770 1.00 83.95 C ANISOU 3229 C VAL A 307 12972 10535 8389 -1598 -3630 648 C ATOM 3230 O VAL A 307 -19.510 -20.379 -3.184 1.00 84.76 O ANISOU 3230 O VAL A 307 13076 10676 8453 -1814 -3719 435 O ATOM 3231 CB VAL A 307 -18.492 -17.753 -0.861 1.00 81.03 C ANISOU 3231 CB VAL A 307 12235 10021 8532 -1147 -3124 859 C ATOM 3232 CG1 VAL A 307 -18.177 -17.911 0.624 1.00 74.77 C ANISOU 3232 CG1 VAL A 307 11074 9214 8122 -1019 -2665 764 C ATOM 3233 CG2 VAL A 307 -17.223 -17.801 -1.698 1.00 82.44 C ANISOU 3233 CG2 VAL A 307 13010 10123 8190 -1320 -2889 866 C TER 3234 VAL A 307 HETATM 3235 NA NA A2400 -3.741 -8.449 16.514 1.00 29.52 NA HETATM 3236 C10 6DY A2401 0.375 14.257 13.198 1.00 27.67 C HETATM 3237 C13 6DY A2401 0.308 12.836 15.655 1.00 23.97 C HETATM 3238 C15 6DY A2401 3.188 16.058 12.971 1.00 39.12 C HETATM 3239 C17 6DY A2401 3.783 18.289 13.690 1.00 46.41 C HETATM 3240 C21 6DY A2401 -1.276 6.652 17.486 1.00 17.48 C HETATM 3241 C23 6DY A2401 -0.237 5.005 18.487 1.00 13.69 C HETATM 3242 C18 6DY A2401 2.917 18.099 14.772 1.00 48.55 C HETATM 3243 C19 6DY A2401 2.204 16.907 14.927 1.00 43.31 C HETATM 3244 C16 6DY A2401 3.902 17.234 12.790 1.00 41.27 C HETATM 3245 C12 6DY A2401 0.951 14.212 15.581 1.00 26.27 C HETATM 3246 C14 6DY A2401 2.313 15.807 14.041 1.00 38.02 C HETATM 3247 C11 6DY A2401 1.530 14.495 14.177 1.00 30.11 C HETATM 3248 N01 6DY A2401 1.564 8.860 18.338 1.00 13.23 N HETATM 3249 C02 6DY A2401 0.360 8.413 17.842 1.00 14.33 C HETATM 3250 N03 6DY A2401 -0.468 9.251 17.187 1.00 18.71 N HETATM 3251 C04 6DY A2401 -1.703 8.777 16.675 1.00 17.65 C HETATM 3252 N05 6DY A2401 -2.459 9.718 16.048 1.00 19.06 N HETATM 3253 C06 6DY A2401 -2.157 11.071 15.845 1.00 21.46 C HETATM 3254 C07 6DY A2401 -1.213 11.254 14.653 1.00 24.02 C HETATM 3255 N08 6DY A2401 -0.794 12.686 14.647 1.00 25.89 N HETATM 3256 C09 6DY A2401 -0.218 12.871 13.262 1.00 26.34 C HETATM 3257 N20 6DY A2401 -2.094 7.513 16.815 1.00 18.25 N HETATM 3258 N22 6DY A2401 -1.396 5.350 17.794 1.00 14.14 N HETATM 3259 N24 6DY A2401 0.632 6.051 18.606 1.00 17.26 N HETATM 3260 N25 6DY A2401 0.002 7.093 18.024 1.00 13.77 N HETATM 3261 C26 6DY A2401 0.033 3.697 18.972 1.00 14.01 C HETATM 3262 C27 6DY A2401 -0.750 2.597 19.194 1.00 13.10 C HETATM 3263 C28 6DY A2401 0.100 1.513 19.675 1.00 14.54 C HETATM 3264 C29 6DY A2401 1.402 2.066 19.715 1.00 15.41 C HETATM 3265 O30 6DY A2401 1.324 3.389 19.295 1.00 14.66 O HETATM 3266 C1 CLR A2402 -16.699 8.711 28.531 1.00134.33 C HETATM 3267 C2 CLR A2402 -16.444 10.138 29.064 1.00134.11 C HETATM 3268 C3 CLR A2402 -17.634 10.738 29.757 1.00134.26 C HETATM 3269 C4 CLR A2402 -18.243 9.768 30.790 1.00135.23 C HETATM 3270 C5 CLR A2402 -18.366 8.344 30.296 1.00135.04 C HETATM 3271 C6 CLR A2402 -19.522 7.687 30.506 1.00134.51 C HETATM 3272 C7 CLR A2402 -19.727 6.199 30.279 1.00133.45 C HETATM 3273 C8 CLR A2402 -18.436 5.495 29.876 1.00132.57 C HETATM 3274 C9 CLR A2402 -17.584 6.379 28.957 1.00133.19 C HETATM 3275 C10 CLR A2402 -17.181 7.723 29.589 1.00134.89 C HETATM 3276 C11 CLR A2402 -16.411 5.564 28.406 1.00132.48 C HETATM 3277 C12 CLR A2402 -16.822 4.226 27.768 1.00131.75 C HETATM 3278 C13 CLR A2402 -17.694 3.345 28.623 1.00131.89 C HETATM 3279 C14 CLR A2402 -18.823 4.234 29.134 1.00131.26 C HETATM 3280 C15 CLR A2402 -19.739 3.263 29.873 1.00129.88 C HETATM 3281 C16 CLR A2402 -19.636 2.004 29.017 1.00128.17 C HETATM 3282 C17 CLR A2402 -18.536 2.230 27.976 1.00126.40 C HETATM 3283 C18 CLR A2402 -16.830 2.712 29.751 1.00138.42 C HETATM 3284 C19 CLR A2402 -16.040 7.547 30.624 1.00137.75 C HETATM 3285 C20 CLR A2402 -17.891 0.909 27.521 1.00120.12 C HETATM 3286 C21 CLR A2402 -17.995 0.721 26.006 1.00119.17 C HETATM 3287 C22 CLR A2402 -18.494 -0.319 28.251 1.00115.36 C HETATM 3288 C23 CLR A2402 -19.309 -1.303 27.396 1.00110.76 C HETATM 3289 C24 CLR A2402 -20.677 -1.563 28.036 1.00106.68 C HETATM 3290 C25 CLR A2402 -20.827 -2.951 28.679 1.00103.48 C HETATM 3291 C26 CLR A2402 -21.808 -2.911 29.848 1.00102.80 C HETATM 3292 C27 CLR A2402 -21.272 -4.014 27.677 1.00102.26 C HETATM 3293 O1 CLR A2402 -17.216 11.930 30.442 1.00133.43 O HETATM 3294 C1 CLR A2403 -18.372 10.762 22.011 1.00 22.99 C HETATM 3295 C2 CLR A2403 -18.044 12.235 22.311 1.00 24.77 C HETATM 3296 C3 CLR A2403 -18.292 12.569 23.752 1.00 24.84 C HETATM 3297 C4 CLR A2403 -17.431 11.670 24.659 1.00 22.06 C HETATM 3298 C5 CLR A2403 -17.675 10.214 24.334 1.00 22.87 C HETATM 3299 C6 CLR A2403 -18.010 9.393 25.344 1.00 23.82 C HETATM 3300 C7 CLR A2403 -18.204 7.888 25.222 1.00 25.70 C HETATM 3301 C8 CLR A2403 -17.884 7.353 23.809 1.00 21.78 C HETATM 3302 C9 CLR A2403 -18.259 8.379 22.724 1.00 19.37 C HETATM 3303 C10 CLR A2403 -17.615 9.757 22.877 1.00 21.93 C HETATM 3304 C11 CLR A2403 -18.061 7.767 21.328 1.00 21.16 C HETATM 3305 C12 CLR A2403 -18.789 6.418 21.178 1.00 21.17 C HETATM 3306 C13 CLR A2403 -18.416 5.393 22.218 1.00 21.51 C HETATM 3307 C14 CLR A2403 -18.678 6.077 23.559 1.00 21.12 C HETATM 3308 C15 CLR A2403 -18.541 4.940 24.585 1.00 23.70 C HETATM 3309 C16 CLR A2403 -19.035 3.710 23.812 1.00 24.33 C HETATM 3310 C17 CLR A2403 -19.236 4.100 22.334 1.00 22.04 C HETATM 3311 C18 CLR A2403 -16.918 4.949 22.059 1.00 19.11 C HETATM 3312 C19 CLR A2403 -16.147 9.710 22.359 1.00 22.65 C HETATM 3313 C20 CLR A2403 -18.950 2.903 21.412 1.00 22.22 C HETATM 3314 C21 CLR A2403 -19.120 3.226 19.915 1.00 22.48 C HETATM 3315 C22 CLR A2403 -19.855 1.698 21.769 1.00 25.57 C HETATM 3316 C23 CLR A2403 -19.630 0.451 20.897 1.00 27.88 C HETATM 3317 C24 CLR A2403 -20.648 -0.629 21.267 1.00 36.05 C HETATM 3318 C25 CLR A2403 -20.302 -2.020 20.720 1.00 44.70 C HETATM 3319 C26 CLR A2403 -20.826 -3.103 21.659 1.00 48.16 C HETATM 3320 C27 CLR A2403 -20.829 -2.246 19.296 1.00 47.40 C HETATM 3321 O1 CLR A2403 -17.986 13.956 23.968 1.00 25.68 O HETATM 3322 C1 CLR A2404 11.589 10.788 13.417 1.00 25.26 C HETATM 3323 C2 CLR A2404 11.570 12.324 13.482 1.00 26.01 C HETATM 3324 C3 CLR A2404 12.909 12.922 13.094 1.00 25.64 C HETATM 3325 C4 CLR A2404 13.411 12.412 11.729 1.00 24.87 C HETATM 3326 C5 CLR A2404 13.347 10.907 11.650 1.00 25.08 C HETATM 3327 C6 CLR A2404 14.440 10.220 11.248 1.00 25.48 C HETATM 3328 C7 CLR A2404 14.489 8.713 11.070 1.00 26.57 C HETATM 3329 C8 CLR A2404 13.079 8.114 11.034 1.00 25.25 C HETATM 3330 C9 CLR A2404 12.265 8.721 12.181 1.00 19.77 C HETATM 3331 C10 CLR A2404 12.050 10.236 12.059 1.00 24.45 C HETATM 3332 C11 CLR A2404 10.959 7.952 12.416 1.00 20.78 C HETATM 3333 C12 CLR A2404 11.185 6.443 12.531 1.00 21.32 C HETATM 3334 C13 CLR A2404 11.865 5.852 11.321 1.00 23.40 C HETATM 3335 C14 CLR A2404 13.192 6.611 11.236 1.00 27.42 C HETATM 3336 C15 CLR A2404 14.036 5.819 10.249 1.00 28.25 C HETATM 3337 C16 CLR A2404 13.626 4.371 10.520 1.00 27.80 C HETATM 3338 C17 CLR A2404 12.356 4.399 11.389 1.00 25.12 C HETATM 3339 C18 CLR A2404 10.992 6.065 10.048 1.00 21.60 C HETATM 3340 C19 CLR A2404 10.965 10.576 10.979 1.00 22.57 C HETATM 3341 C20 CLR A2404 11.417 3.230 11.066 1.00 26.63 C HETATM 3342 C21 CLR A2404 10.214 3.189 12.015 1.00 24.85 C HETATM 3343 C22 CLR A2404 12.166 1.899 11.225 1.00 28.04 C HETATM 3344 C23 CLR A2404 11.330 0.622 11.049 1.00 31.92 C HETATM 3345 C24 CLR A2404 12.258 -0.574 11.292 1.00 36.41 C HETATM 3346 C25 CLR A2404 11.581 -1.950 11.333 1.00 40.42 C HETATM 3347 C26 CLR A2404 10.634 -2.071 12.519 1.00 35.26 C HETATM 3348 C27 CLR A2404 10.845 -2.269 10.041 1.00 46.52 C HETATM 3349 O1 CLR A2404 12.760 14.346 13.023 1.00 28.75 O HETATM 3350 C1 CLR A2405 16.668 8.064 21.333 1.00 21.72 C HETATM 3351 C2 CLR A2405 16.860 9.588 21.300 1.00 21.52 C HETATM 3352 C3 CLR A2405 17.828 9.971 20.212 1.00 23.73 C HETATM 3353 C4 CLR A2405 17.353 9.446 18.838 1.00 22.61 C HETATM 3354 C5 CLR A2405 17.082 7.960 18.877 1.00 21.99 C HETATM 3355 C6 CLR A2405 17.614 7.161 17.920 1.00 22.20 C HETATM 3356 C7 CLR A2405 17.333 5.669 17.795 1.00 22.33 C HETATM 3357 C8 CLR A2405 16.186 5.227 18.709 1.00 21.68 C HETATM 3358 C9 CLR A2405 16.277 5.912 20.084 1.00 19.26 C HETATM 3359 C10 CLR A2405 16.203 7.442 19.999 1.00 21.02 C HETATM 3360 C11 CLR A2405 15.255 5.323 21.070 1.00 20.95 C HETATM 3361 C12 CLR A2405 15.205 3.794 21.061 1.00 19.74 C HETATM 3362 C13 CLR A2405 15.087 3.162 19.688 1.00 23.05 C HETATM 3363 C14 CLR A2405 16.237 3.721 18.870 1.00 22.77 C HETATM 3364 C15 CLR A2405 16.211 2.897 17.580 1.00 24.96 C HETATM 3365 C16 CLR A2405 15.738 1.523 18.058 1.00 25.65 C HETATM 3366 C17 CLR A2405 15.325 1.651 19.528 1.00 25.81 C HETATM 3367 C18 CLR A2405 13.687 3.506 19.074 1.00 17.32 C HETATM 3368 C19 CLR A2405 14.749 7.919 19.692 1.00 21.07 C HETATM 3369 C20 CLR A2405 14.188 0.673 19.885 1.00 25.97 C HETATM 3370 C21 CLR A2405 13.737 0.748 21.346 1.00 20.88 C HETATM 3371 C22 CLR A2405 14.608 -0.779 19.577 1.00 30.43 C HETATM 3372 C23 CLR A2405 13.445 -1.773 19.548 1.00 34.91 C HETATM 3373 C24 CLR A2405 13.939 -3.101 20.114 1.00 43.55 C HETATM 3374 C25 CLR A2405 14.527 -4.001 19.030 1.00 48.86 C HETATM 3375 C26 CLR A2405 14.825 -5.398 19.570 1.00 51.91 C HETATM 3376 C27 CLR A2405 13.556 -4.079 17.858 1.00 50.96 C HETATM 3377 O1 CLR A2405 17.920 11.396 20.160 1.00 21.51 O HETATM 3378 C1 OLA A2406 -16.617 15.076 13.232 1.00 57.68 C HETATM 3379 O1 OLA A2406 -15.943 16.121 12.987 1.00 60.47 O HETATM 3380 O2 OLA A2406 -17.483 15.137 14.121 1.00 56.60 O HETATM 3381 C2 OLA A2406 -16.396 13.780 12.475 1.00 54.41 C HETATM 3382 C3 OLA A2406 -17.104 12.598 13.141 1.00 48.74 C HETATM 3383 C4 OLA A2406 -16.314 11.303 13.011 1.00 42.85 C HETATM 3384 C5 OLA A2406 -16.876 10.320 12.008 1.00 37.20 C HETATM 3385 C6 OLA A2406 -16.757 8.873 12.451 1.00 36.28 C HETATM 3386 C7 OLA A2406 -16.917 7.884 11.306 1.00 35.97 C HETATM 3387 C8 OLA A2406 -17.002 6.431 11.732 1.00 36.59 C HETATM 3388 C9 OLA A2406 -16.218 5.576 10.755 1.00 41.29 C HETATM 3389 C10 OLA A2406 -16.665 4.529 10.018 1.00 47.13 C HETATM 3390 C11 OLA A2406 -18.081 3.999 10.031 1.00 50.93 C HETATM 3391 C12 OLA A2406 -18.135 2.460 9.953 1.00 53.53 C HETATM 3392 C13 OLA A2406 -18.970 1.834 11.094 1.00 57.51 C HETATM 3393 C14 OLA A2406 -19.459 0.400 10.809 1.00 59.45 C HETATM 3394 C15 OLA A2406 -19.173 -0.603 11.949 1.00 59.81 C HETATM 3395 C16 OLA A2406 -18.899 -2.036 11.457 1.00 59.67 C HETATM 3396 C17 OLA A2406 -20.045 -3.019 11.740 1.00 58.72 C HETATM 3397 C18 OLA A2406 -19.881 -4.348 10.982 1.00 58.35 C HETATM 3398 C1 OLA A2407 11.038 14.266 7.837 1.00 64.95 C HETATM 3399 O1 OLA A2407 11.216 15.374 7.258 1.00 69.11 O HETATM 3400 O2 OLA A2407 11.494 14.131 8.983 1.00 65.25 O HETATM 3401 C2 OLA A2407 10.284 13.132 7.178 1.00 59.82 C HETATM 3402 C3 OLA A2407 11.068 11.822 7.184 1.00 56.08 C HETATM 3403 C4 OLA A2407 10.601 10.885 6.080 1.00 55.68 C HETATM 3404 C5 OLA A2407 10.674 9.424 6.455 1.00 54.94 C HETATM 3405 C6 OLA A2407 12.085 8.877 6.579 1.00 56.31 C HETATM 3406 C7 OLA A2407 12.072 7.385 6.281 1.00 57.45 C HETATM 3407 C8 OLA A2407 10.717 6.879 5.824 1.00 58.32 C HETATM 3408 C9 OLA A2407 10.912 5.494 5.226 1.00 58.94 C HETATM 3409 C10 OLA A2407 10.031 4.843 4.432 1.00 57.54 C HETATM 3410 C11 OLA A2407 8.690 5.404 4.011 1.00 54.53 C HETATM 3411 C12 OLA A2407 7.946 4.413 3.102 1.00 52.65 C HETATM 3412 C13 OLA A2407 8.381 4.506 1.625 1.00 53.29 C HETATM 3413 C1 OLA A2408 -0.731 -22.541 27.617 1.00 34.36 C HETATM 3414 C2 OLA A2408 0.064 -21.611 28.512 1.00 34.22 C HETATM 3415 C3 OLA A2408 -0.622 -20.272 28.757 1.00 36.78 C HETATM 3416 C4 OLA A2408 0.301 -19.168 29.255 1.00 38.52 C HETATM 3417 C5 OLA A2408 -0.329 -17.786 29.267 1.00 38.81 C HETATM 3418 C6 OLA A2408 0.625 -16.662 28.880 1.00 39.92 C HETATM 3419 C7 OLA A2408 -0.046 -15.292 28.883 1.00 37.16 C HETATM 3420 C1 OLA A2409 -5.130 12.936 7.632 1.00 70.89 C HETATM 3421 O1 OLA A2409 -5.938 13.899 7.482 1.00 70.95 O HETATM 3422 O2 OLA A2409 -5.242 12.237 8.659 1.00 71.04 O HETATM 3423 C2 OLA A2409 -4.052 12.631 6.605 1.00 69.29 C HETATM 3424 C3 OLA A2409 -3.532 11.193 6.717 1.00 67.68 C HETATM 3425 C4 OLA A2409 -2.325 10.890 5.830 1.00 66.62 C HETATM 3426 C5 OLA A2409 -2.607 10.885 4.336 1.00 63.26 C HETATM 3427 C6 OLA A2409 -1.544 10.201 3.485 1.00 60.03 C HETATM 3428 C7 OLA A2409 -1.945 8.776 3.107 1.00 58.12 C HETATM 3429 C8 OLA A2409 -1.061 7.662 3.643 1.00 56.45 C HETATM 3430 C9 OLA A2409 -1.932 6.509 4.133 1.00 53.98 C HETATM 3431 C10 OLA A2409 -2.259 5.390 3.442 1.00 51.97 C HETATM 3432 C11 OLA A2409 -1.798 5.103 2.027 1.00 52.83 C HETATM 3433 C12 OLA A2409 -0.805 3.927 1.956 1.00 53.77 C HETATM 3434 C13 OLA A2409 -1.328 2.735 1.132 1.00 55.85 C HETATM 3435 C14 OLA A2409 -0.729 1.386 1.565 1.00 57.87 C HETATM 3436 C15 OLA A2409 -1.777 0.338 2.002 1.00 58.99 C HETATM 3437 C16 OLA A2409 -1.343 -0.507 3.219 1.00 57.37 C HETATM 3438 C1 OLA A2410 -12.031 -17.459 41.245 1.00 68.52 C HETATM 3439 O1 OLA A2410 -13.109 -18.118 41.170 1.00 68.53 O HETATM 3440 O2 OLA A2410 -11.825 -16.812 42.288 1.00 67.47 O HETATM 3441 C2 OLA A2410 -11.025 -17.450 40.104 1.00 68.07 C HETATM 3442 C3 OLA A2410 -9.603 -17.030 40.502 1.00 66.47 C HETATM 3443 C4 OLA A2410 -8.606 -17.160 39.350 1.00 65.14 C HETATM 3444 C5 OLA A2410 -7.209 -16.633 39.636 1.00 64.13 C HETATM 3445 C6 OLA A2410 -6.428 -16.215 38.395 1.00 62.80 C HETATM 3446 C7 OLA A2410 -5.187 -15.377 38.704 1.00 61.59 C HETATM 3447 C8 OLA A2410 -5.272 -13.897 38.356 1.00 61.07 C HETATM 3448 C9 OLA A2410 -3.899 -13.269 38.563 1.00 61.26 C HETATM 3449 C10 OLA A2410 -3.604 -11.971 38.836 1.00 61.30 C HETATM 3450 C11 OLA A2410 -4.598 -10.836 38.992 1.00 60.73 C HETATM 3451 C12 OLA A2410 -3.970 -9.637 39.742 1.00 60.46 C HETATM 3452 C13 OLA A2410 -4.064 -8.267 39.028 1.00 57.54 C HETATM 3453 C14 OLA A2410 -2.709 -7.547 38.918 1.00 55.93 C HETATM 3454 C15 OLA A2410 -2.784 -6.087 38.419 1.00 56.60 C HETATM 3455 C16 OLA A2410 -3.019 -5.894 36.908 1.00 54.88 C HETATM 3456 C17 OLA A2410 -2.102 -4.840 36.253 1.00 51.85 C HETATM 3457 C18 OLA A2410 -2.860 -3.648 35.649 1.00 48.48 C HETATM 3458 C1 OLA A2411 -20.238 12.610 9.406 1.00 70.98 C HETATM 3459 O1 OLA A2411 -21.461 12.939 9.344 1.00 72.02 O HETATM 3460 O2 OLA A2411 -19.400 13.495 9.662 1.00 73.52 O HETATM 3461 C2 OLA A2411 -19.788 11.182 9.181 1.00 66.05 C HETATM 3462 C3 OLA A2411 -20.990 10.249 9.030 1.00 62.32 C HETATM 3463 C4 OLA A2411 -20.583 8.788 8.934 1.00 60.13 C HETATM 3464 C5 OLA A2411 -21.608 7.912 8.246 1.00 58.56 C HETATM 3465 C6 OLA A2411 -21.418 6.429 8.537 1.00 57.70 C HETATM 3466 C7 OLA A2411 -22.248 5.536 7.620 1.00 57.88 C HETATM 3467 C8 OLA A2411 -21.927 4.058 7.752 1.00 60.85 C HETATM 3468 C9 OLA A2411 -23.220 3.261 7.665 1.00 63.60 C HETATM 3469 C10 OLA A2411 -23.483 2.097 8.305 1.00 64.42 C HETATM 3470 C11 OLA A2411 -22.508 1.404 9.230 1.00 63.73 C HETATM 3471 C12 OLA A2411 -22.481 -0.123 9.023 1.00 63.05 C HETATM 3472 C13 OLA A2411 -23.630 -0.874 9.725 1.00 61.94 C HETATM 3473 C1 OLA A2412 -16.592 -15.596 5.131 1.00 61.15 C HETATM 3474 O1 OLA A2412 -17.010 -14.544 5.685 1.00 62.43 O HETATM 3475 O2 OLA A2412 -16.502 -16.618 5.827 1.00 59.79 O HETATM 3476 C2 OLA A2412 -16.221 -15.637 3.661 1.00 61.03 C HETATM 3477 C3 OLA A2412 -14.708 -15.637 3.430 1.00 58.85 C HETATM 3478 C4 OLA A2412 -14.336 -15.716 1.956 1.00 56.55 C HETATM 3479 C5 OLA A2412 -13.249 -14.740 1.567 1.00 51.88 C HETATM 3480 C6 OLA A2412 -12.031 -14.749 2.477 1.00 46.03 C HETATM 3481 C7 OLA A2412 -11.297 -13.423 2.348 1.00 40.81 C HETATM 3482 C8 OLA A2412 -9.985 -13.355 3.087 1.00 37.98 C HETATM 3483 C9 OLA A2412 -9.543 -11.907 3.064 1.00 37.54 C HETATM 3484 C10 OLA A2412 -8.412 -11.445 3.627 1.00 40.43 C HETATM 3485 C1 OLA A2413 4.236 12.774 0.924 1.00 62.49 C HETATM 3486 O1 OLA A2413 5.398 13.237 0.744 1.00 63.77 O HETATM 3487 O2 OLA A2413 3.341 13.576 1.252 1.00 62.10 O HETATM 3488 C2 OLA A2413 3.932 11.297 0.753 1.00 61.47 C HETATM 3489 C3 OLA A2413 2.476 10.965 1.093 1.00 62.37 C HETATM 3490 C4 OLA A2413 2.157 9.475 1.012 1.00 63.20 C HETATM 3491 C5 OLA A2413 3.340 8.628 0.589 1.00 63.97 C HETATM 3492 C6 OLA A2413 3.200 7.142 0.895 1.00 64.55 C HETATM 3493 C4 OLA A2414 -14.043 -17.857 26.708 1.00 50.44 C HETATM 3494 C5 OLA A2414 -13.149 -16.637 26.670 1.00 47.82 C HETATM 3495 C6 OLA A2414 -13.694 -15.431 27.412 1.00 47.75 C HETATM 3496 C7 OLA A2414 -13.740 -14.206 26.514 1.00 50.34 C HETATM 3497 C8 OLA A2414 -13.336 -12.908 27.180 1.00 52.96 C HETATM 3498 C9 OLA A2414 -13.976 -12.822 28.551 1.00 54.01 C HETATM 3499 C10 OLA A2414 -14.365 -11.675 29.141 1.00 53.38 C HETATM 3500 C11 OLA A2414 -14.201 -10.330 28.478 1.00 51.71 C HETATM 3501 C12 OLA A2414 -13.491 -9.347 29.419 1.00 52.32 C HETATM 3502 C13 OLA A2414 -13.581 -7.900 28.911 1.00 55.33 C HETATM 3503 C14 OLA A2414 -14.383 -6.991 29.848 1.00 56.29 C HETATM 3504 C15 OLA A2414 -13.715 -6.794 31.217 1.00 54.90 C HETATM 3505 C16 OLA A2414 -13.700 -5.329 31.673 1.00 53.72 C HETATM 3506 C17 OLA A2414 -13.104 -5.171 33.077 1.00 55.01 C HETATM 3507 C18 OLA A2414 -11.673 -4.616 33.063 1.00 55.22 C HETATM 3508 C1 OLA A2415 -8.714 -20.978 35.020 1.00 69.14 C HETATM 3509 O1 OLA A2415 -7.517 -21.021 34.671 1.00 69.01 O HETATM 3510 O2 OLA A2415 -9.449 -21.970 34.736 1.00 69.78 O HETATM 3511 C2 OLA A2415 -9.245 -19.769 35.772 1.00 67.84 C HETATM 3512 C3 OLA A2415 -10.646 -19.349 35.314 1.00 67.39 C HETATM 3513 C4 OLA A2415 -11.101 -18.001 35.869 1.00 66.15 C HETATM 3514 C5 OLA A2415 -11.706 -17.080 34.822 1.00 64.60 C HETATM 3515 C6 OLA A2415 -12.333 -15.798 35.356 1.00 62.74 C HETATM 3516 C7 OLA A2415 -11.394 -14.596 35.262 1.00 61.34 C HETATM 3517 C8 OLA A2415 -11.274 -13.771 36.534 1.00 60.63 C HETATM 3518 C9 OLA A2415 -10.545 -12.463 36.243 1.00 58.04 C HETATM 3519 C10 OLA A2415 -9.391 -12.067 36.831 1.00 55.66 C HETATM 3520 C11 OLA A2415 -8.670 -10.766 36.537 1.00 51.12 C HETATM 3521 C12 OLA A2415 -7.141 -10.898 36.706 1.00 46.75 C HETATM 3522 C1 OLA A2416 8.675 -13.845 7.539 1.00 56.74 C HETATM 3523 C2 OLA A2416 8.289 -12.606 8.326 1.00 57.16 C HETATM 3524 C3 OLA A2416 8.920 -12.588 9.722 1.00 57.78 C HETATM 3525 C4 OLA A2416 9.661 -11.290 10.029 1.00 59.29 C HETATM 3526 C5 OLA A2416 10.207 -11.202 11.444 1.00 60.16 C HETATM 3527 C6 OLA A2416 10.890 -9.883 11.788 1.00 60.05 C HETATM 3528 C7 OLA A2416 11.253 -9.778 13.270 1.00 58.81 C HETATM 3529 C8 OLA A2416 11.360 -8.361 13.808 1.00 58.12 C HETATM 3530 C1 OLA A2417 -23.956 -24.634 13.220 1.00 65.69 C HETATM 3531 O1 OLA A2417 -24.691 -25.480 12.640 1.00 69.01 O HETATM 3532 O2 OLA A2417 -22.967 -25.065 13.844 1.00 65.20 O HETATM 3533 C2 OLA A2417 -24.262 -23.147 13.167 1.00 61.49 C HETATM 3534 C3 OLA A2417 -23.445 -22.364 14.199 1.00 61.06 C HETATM 3535 C4 OLA A2417 -23.817 -20.888 14.277 1.00 63.83 C HETATM 3536 C5 OLA A2417 -22.899 -20.088 15.181 1.00 66.49 C HETATM 3537 C6 OLA A2417 -21.424 -20.465 15.079 1.00 67.26 C HETATM 3538 C7 OLA A2417 -20.551 -19.728 16.097 1.00 65.43 C HETATM 3539 C8 OLA A2417 -19.796 -18.526 15.547 1.00 63.45 C HETATM 3540 C9 OLA A2417 -18.400 -18.944 15.099 1.00 61.24 C HETATM 3541 C10 OLA A2417 -17.623 -18.288 14.205 1.00 59.51 C HETATM 3542 C11 OLA A2417 -18.014 -17.009 13.486 1.00 57.44 C HETATM 3543 C12 OLA A2417 -17.518 -15.742 14.217 1.00 55.94 C HETATM 3544 C13 OLA A2417 -18.228 -14.454 13.762 1.00 57.18 C HETATM 3545 C14 OLA A2417 -17.955 -13.233 14.656 1.00 58.16 C HETATM 3546 C15 OLA A2417 -18.560 -11.925 14.095 1.00 58.00 C HETATM 3547 C16 OLA A2417 -18.693 -10.799 15.140 1.00 56.18 C HETATM 3548 C17 OLA A2417 -18.963 -9.413 14.530 1.00 53.72 C HETATM 3549 C8 OLA A2418 -1.661 -10.997 0.317 1.00 62.85 C HETATM 3550 C9 OLA A2418 -1.080 -11.349 1.683 1.00 61.01 C HETATM 3551 C10 OLA A2418 -1.408 -10.789 2.873 1.00 54.94 C HETATM 3552 C11 OLA A2418 -2.442 -9.696 3.026 1.00 49.69 C HETATM 3553 C12 OLA A2418 -1.890 -8.484 3.800 1.00 45.28 C HETATM 3554 C13 OLA A2418 -1.911 -7.176 2.989 1.00 41.84 C HETATM 3555 C14 OLA A2418 -3.146 -6.304 3.269 1.00 40.56 C HETATM 3556 C15 OLA A2418 -3.214 -5.061 2.367 1.00 39.50 C HETATM 3557 C16 OLA A2418 -4.502 -4.229 2.489 1.00 40.98 C HETATM 3558 C17 OLA A2418 -4.288 -2.800 1.965 1.00 45.07 C HETATM 3559 C18 OLA A2418 -5.594 -2.048 1.669 1.00 45.85 C HETATM 3560 C1 OLA A2419 -15.068 11.494 3.185 1.00 75.68 C HETATM 3561 O1 OLA A2419 -15.868 12.432 3.371 1.00 77.36 O HETATM 3562 O2 OLA A2419 -13.966 11.521 3.805 1.00 77.81 O HETATM 3563 C2 OLA A2419 -15.421 10.363 2.238 1.00 70.62 C HETATM 3564 C3 OLA A2419 -14.668 9.072 2.574 1.00 65.32 C HETATM 3565 C4 OLA A2419 -14.603 8.113 1.393 1.00 62.99 C HETATM 3566 C5 OLA A2419 -15.102 6.716 1.704 1.00 61.04 C HETATM 3567 C6 OLA A2419 -15.066 5.767 0.514 1.00 60.31 C HETATM 3568 C7 OLA A2419 -15.606 4.383 0.852 1.00 60.16 C HETATM 3569 C8 OLA A2419 -14.549 3.311 1.053 1.00 59.80 C HETATM 3570 C9 OLA A2419 -14.788 2.175 0.070 1.00 60.75 C HETATM 3571 C1 OLA A2420 18.250 -21.029 24.515 1.00 79.05 C HETATM 3572 O1 OLA A2420 19.373 -21.174 24.011 1.00 81.45 O HETATM 3573 O2 OLA A2420 17.323 -21.761 24.076 1.00 80.97 O HETATM 3574 C2 OLA A2420 18.027 -20.007 25.613 1.00 74.85 C HETATM 3575 C3 OLA A2420 17.379 -18.720 25.093 1.00 72.68 C HETATM 3576 C4 OLA A2420 17.415 -17.574 26.098 1.00 72.90 C HETATM 3577 C5 OLA A2420 16.441 -16.450 25.785 1.00 73.17 C HETATM 3578 C6 OLA A2420 17.070 -15.173 25.238 1.00 71.04 C HETATM 3579 C7 OLA A2420 16.191 -13.944 25.473 1.00 67.78 C HETATM 3580 C8 OLA A2420 16.345 -12.846 24.434 1.00 64.16 C HETATM 3581 C9 OLA A2420 16.585 -11.514 25.132 1.00 62.28 C HETATM 3582 C2 OLA A2421 -15.521 5.996 33.549 1.00 60.88 C HETATM 3583 C3 OLA A2421 -14.217 5.862 32.758 1.00 59.71 C HETATM 3584 C4 OLA A2421 -13.440 4.595 33.090 1.00 59.54 C HETATM 3585 C5 OLA A2421 -13.806 3.407 32.225 1.00 59.25 C HETATM 3586 C6 OLA A2421 -13.313 2.066 32.755 1.00 56.66 C HETATM 3587 C7 OLA A2421 -11.792 1.977 32.724 1.00 53.21 C HETATM 3588 C8 OLA A2421 -11.212 0.834 33.528 1.00 52.96 C HETATM 3589 C9 OLA A2421 -11.399 -0.467 32.773 1.00 53.66 C HETATM 3590 C10 OLA A2421 -10.724 -1.604 33.036 1.00 55.40 C HETATM 3591 C11 OLA A2421 -9.694 -1.689 34.135 1.00 57.98 C HETATM 3592 C4 OLA A2422 13.652 -17.511 16.775 1.00 50.94 C HETATM 3593 C5 OLA A2422 12.216 -17.346 16.315 1.00 48.77 C HETATM 3594 C6 OLA A2422 11.735 -15.905 16.193 1.00 46.24 C HETATM 3595 C7 OLA A2422 10.620 -15.599 17.192 1.00 43.66 C HETATM 3596 C8 OLA A2422 9.575 -14.621 16.703 1.00 42.67 C HETATM 3597 C9 OLA A2422 8.949 -13.923 17.896 1.00 42.19 C HETATM 3598 C10 OLA A2422 9.137 -12.626 18.223 1.00 42.24 C HETATM 3599 C11 OLA A2422 10.032 -11.711 17.423 1.00 43.48 C HETATM 3600 C12 OLA A2422 9.980 -10.268 17.947 1.00 45.18 C HETATM 3601 C13 OLA A2422 11.267 -9.812 18.659 1.00 46.60 C HETATM 3602 C14 OLA A2422 11.568 -8.323 18.438 1.00 48.43 C HETATM 3603 C15 OLA A2422 11.434 -7.457 19.706 1.00 49.05 C HETATM 3604 C5 OLA A2423 1.798 -14.840 3.422 1.00 56.32 C HETATM 3605 C6 OLA A2423 1.336 -13.555 2.750 1.00 57.97 C HETATM 3606 C7 OLA A2423 1.276 -12.382 3.725 1.00 58.96 C HETATM 3607 C8 OLA A2423 2.609 -11.974 4.322 1.00 60.88 C HETATM 3608 C9 OLA A2423 2.749 -10.459 4.249 1.00 62.59 C HETATM 3609 C10 OLA A2423 3.929 -9.801 4.233 1.00 63.26 C HETATM 3610 C11 OLA A2423 5.264 -10.516 4.281 1.00 62.70 C HETATM 3611 C12 OLA A2423 6.448 -9.537 4.416 1.00 61.49 C HETATM 3612 C1 OLB A2424 15.456 9.533 29.932 1.00 70.86 C HETATM 3613 C2 OLB A2424 15.524 8.166 30.624 1.00 66.04 C HETATM 3614 C3 OLB A2424 15.917 6.997 29.717 1.00 62.85 C HETATM 3615 C4 OLB A2424 15.699 5.641 30.393 1.00 60.49 C HETATM 3616 C5 OLB A2424 15.774 4.448 29.439 1.00 58.39 C HETATM 3617 O19 OLB A2424 16.435 10.198 29.872 1.00 70.22 O HETATM 3618 O20 OLB A2424 14.241 10.007 29.395 1.00 75.75 O HETATM 3619 C21 OLB A2424 14.239 11.303 28.841 1.00 77.53 C HETATM 3620 C22 OLB A2424 12.815 11.648 28.369 1.00 78.56 C HETATM 3621 O23 OLB A2424 12.089 12.183 29.442 1.00 78.70 O HETATM 3622 C24 OLB A2424 12.736 12.658 27.222 1.00 80.07 C HETATM 3623 O25 OLB A2424 13.641 13.706 27.434 1.00 82.37 O HETATM 3624 C6 OLB A2424 15.422 3.109 30.092 1.00 58.54 C HETATM 3625 C7 OLB A2424 15.558 1.928 29.127 1.00 60.68 C HETATM 3626 C8 OLB A2424 15.044 0.590 29.667 1.00 64.55 C HETATM 3627 C9 OLB A2424 14.587 -0.284 28.492 1.00 69.12 C HETATM 3628 C10 OLB A2424 14.014 -1.468 28.660 1.00 68.52 C HETATM 3629 C11 OLB A2424 13.580 -2.275 27.434 1.00 65.41 C HETATM 3630 C12 OLB A2424 13.712 -3.776 27.684 1.00 63.53 C HETATM 3631 C1 OLB A2425 -13.524 14.048 7.308 1.00 78.44 C HETATM 3632 C2 OLB A2425 -14.356 13.311 8.359 1.00 73.96 C HETATM 3633 C3 OLB A2425 -15.426 12.408 7.744 1.00 69.55 C HETATM 3634 C4 OLB A2425 -15.383 10.978 8.282 1.00 62.96 C HETATM 3635 C5 OLB A2425 -16.453 10.094 7.648 1.00 56.72 C HETATM 3636 O19 OLB A2425 -13.376 13.574 6.228 1.00 78.50 O HETATM 3637 O20 OLB A2425 -12.941 15.287 7.611 1.00 81.68 O HETATM 3638 C21 OLB A2425 -12.092 15.284 8.727 1.00 82.26 C HETATM 3639 C22 OLB A2425 -10.639 15.383 8.257 1.00 82.73 C HETATM 3640 O23 OLB A2425 -10.529 16.381 7.278 1.00 81.92 O HETATM 3641 C24 OLB A2425 -9.663 15.725 9.380 1.00 83.82 C HETATM 3642 O25 OLB A2425 -9.113 16.986 9.115 1.00 84.45 O HETATM 3643 C6 OLB A2425 -15.915 8.723 7.248 1.00 54.11 C HETATM 3644 C7 OLB A2425 -17.020 7.719 6.934 1.00 53.98 C HETATM 3645 C8 OLB A2425 -16.934 7.196 5.502 1.00 56.72 C HETATM 3646 C9 OLB A2425 -17.735 5.900 5.376 1.00 59.25 C HETATM 3647 C1 OLB A2426 -21.656 13.244 13.734 1.00 59.46 C HETATM 3648 C2 OLB A2426 -22.092 11.837 13.369 1.00 53.43 C HETATM 3649 C3 OLB A2426 -20.901 10.913 13.560 1.00 50.10 C HETATM 3650 C4 OLB A2426 -21.269 9.550 14.115 1.00 49.13 C HETATM 3651 C5 OLB A2426 -21.837 8.665 13.021 1.00 47.48 C HETATM 3652 O19 OLB A2426 -20.832 13.357 14.575 1.00 62.27 O HETATM 3653 O20 OLB A2426 -22.191 14.362 13.077 1.00 65.93 O HETATM 3654 C21 OLB A2426 -22.549 15.450 13.885 1.00 70.58 C HETATM 3655 C22 OLB A2426 -21.316 16.299 14.204 1.00 73.23 C HETATM 3656 O23 OLB A2426 -20.540 16.400 13.042 1.00 75.55 O HETATM 3657 C24 OLB A2426 -21.655 17.708 14.685 1.00 74.19 C HETATM 3658 O25 OLB A2426 -20.689 18.070 15.631 1.00 74.40 O HETATM 3659 C6 OLB A2426 -20.893 7.517 12.697 1.00 44.52 C HETATM 3660 C7 OLB A2426 -21.244 6.274 13.493 1.00 40.88 C HETATM 3661 C8 OLB A2426 -21.840 5.182 12.614 1.00 41.49 C HETATM 3662 C9 OLB A2426 -22.433 4.148 13.560 1.00 42.36 C HETATM 3663 C10 OLB A2426 -23.366 3.332 13.147 1.00 42.72 C HETATM 3664 C11 OLB A2426 -23.925 2.314 14.125 1.00 43.08 C HETATM 3665 C12 OLB A2426 -23.678 0.917 13.579 1.00 43.32 C HETATM 3666 C13 OLB A2426 -24.133 -0.137 14.576 1.00 45.84 C HETATM 3667 C14 OLB A2426 -23.937 -1.556 14.049 1.00 50.76 C HETATM 3668 C15 OLB A2426 -24.784 -2.562 14.830 1.00 53.83 C HETATM 3669 C1 OLB A2427 -18.965 12.582 17.684 1.00 49.96 C HETATM 3670 C2 OLB A2427 -18.259 11.477 16.892 1.00 46.41 C HETATM 3671 C3 OLB A2427 -18.798 10.088 17.239 1.00 42.52 C HETATM 3672 C4 OLB A2427 -17.759 8.978 17.327 1.00 37.49 C HETATM 3673 C5 OLB A2427 -18.083 7.757 16.475 1.00 36.71 C HETATM 3674 O19 OLB A2427 -19.422 12.329 18.744 1.00 51.85 O HETATM 3675 O20 OLB A2427 -19.059 13.889 17.189 1.00 50.77 O HETATM 3676 C21 OLB A2427 -19.878 14.744 17.940 1.00 52.88 C HETATM 3677 C22 OLB A2427 -19.039 15.522 18.957 1.00 57.07 C HETATM 3678 O23 OLB A2427 -18.223 16.444 18.283 1.00 57.28 O HETATM 3679 C24 OLB A2427 -19.910 16.267 19.976 1.00 62.67 C HETATM 3680 O25 OLB A2427 -19.384 17.542 20.240 1.00 64.92 O HETATM 3681 C6 OLB A2427 -17.762 6.454 17.205 1.00 38.68 C HETATM 3682 C7 OLB A2427 -17.242 5.311 16.329 1.00 40.74 C HETATM 3683 C8 OLB A2427 -18.284 4.732 15.384 1.00 43.47 C HETATM 3684 C9 OLB A2427 -18.142 3.217 15.307 1.00 44.83 C HETATM 3685 C10 OLB A2427 -19.228 2.468 15.261 1.00 45.60 C HETATM 3686 C11 OLB A2427 -19.122 0.946 15.175 1.00 46.19 C HETATM 3687 C12 OLB A2427 -19.985 0.291 16.254 1.00 47.68 C HETATM 3688 C1 OLB A2428 -12.425 -20.984 23.622 1.00 69.31 C HETATM 3689 C2 OLB A2428 -12.303 -20.295 22.269 1.00 62.73 C HETATM 3690 C3 OLB A2428 -11.661 -18.919 22.415 1.00 53.30 C HETATM 3691 C4 OLB A2428 -12.714 -17.822 22.359 1.00 47.42 C HETATM 3692 C5 OLB A2428 -12.095 -16.435 22.392 1.00 43.05 C HETATM 3693 O19 OLB A2428 -11.990 -20.441 24.580 1.00 73.16 O HETATM 3694 O20 OLB A2428 -13.043 -22.235 23.748 1.00 71.17 O HETATM 3695 C21 OLB A2428 -12.231 -23.203 24.349 1.00 72.58 C HETATM 3696 C22 OLB A2428 -13.106 -24.020 25.291 1.00 73.71 C HETATM 3697 O23 OLB A2428 -14.430 -23.782 24.901 1.00 74.28 O HETATM 3698 C24 OLB A2428 -12.818 -25.521 25.215 1.00 73.80 C HETATM 3699 O25 OLB A2428 -13.060 -26.095 26.472 1.00 73.70 O HETATM 3700 C6 OLB A2428 -13.137 -15.337 22.196 1.00 40.85 C HETATM 3701 C7 OLB A2428 -12.864 -14.173 23.142 1.00 40.00 C HETATM 3702 C8 OLB A2428 -13.394 -12.844 22.626 1.00 40.71 C HETATM 3703 C9 OLB A2428 -13.457 -11.853 23.786 1.00 41.45 C HETATM 3704 C10 OLB A2428 -13.808 -10.609 23.539 1.00 41.70 C HETATM 3705 C11 OLB A2428 -13.890 -9.594 24.672 1.00 43.85 C HETATM 3706 C12 OLB A2428 -13.780 -8.197 24.078 1.00 44.35 C HETATM 3707 C13 OLB A2428 -15.098 -7.460 24.228 1.00 49.20 C HETATM 3708 C14 OLB A2428 -15.038 -6.045 23.671 1.00 53.25 C HETATM 3709 C15 OLB A2428 -16.394 -5.601 23.133 1.00 55.59 C HETATM 3710 C16 OLB A2428 -16.328 -4.144 22.691 1.00 56.90 C HETATM 3711 C17 OLB A2428 -16.630 -3.155 23.815 1.00 57.95 C HETATM 3712 C18 OLB A2428 -16.555 -1.697 23.356 1.00 56.56 C HETATM 3713 C1 OLB A2429 -14.488 -23.955 19.821 1.00 73.37 C HETATM 3714 C2 OLB A2429 -15.208 -22.891 18.993 1.00 64.62 C HETATM 3715 C3 OLB A2429 -14.288 -21.707 18.697 1.00 58.32 C HETATM 3716 C4 OLB A2429 -14.764 -20.827 17.545 1.00 53.87 C HETATM 3717 C5 OLB A2429 -15.828 -19.822 17.985 1.00 51.05 C HETATM 3718 O19 OLB A2429 -13.314 -23.878 19.963 1.00 76.95 O HETATM 3719 O20 OLB A2429 -15.182 -25.018 20.417 1.00 78.16 O HETATM 3720 C21 OLB A2429 -14.332 -26.036 20.876 1.00 82.94 C HETATM 3721 C22 OLB A2429 -15.127 -27.064 21.685 1.00 87.36 C HETATM 3722 O23 OLB A2429 -15.923 -27.811 20.806 1.00 90.08 O HETATM 3723 C24 OLB A2429 -14.236 -28.042 22.450 1.00 88.52 C HETATM 3724 O25 OLB A2429 -14.164 -29.245 21.731 1.00 88.63 O HETATM 3725 C6 OLB A2429 -15.216 -18.582 18.628 1.00 53.35 C HETATM 3726 C7 OLB A2429 -16.020 -17.309 18.401 1.00 54.85 C HETATM 3727 C8 OLB A2429 -15.317 -16.060 18.931 1.00 52.47 C HETATM 3728 C9 OLB A2429 -15.755 -14.870 18.083 1.00 48.46 C HETATM 3729 C10 OLB A2429 -15.349 -13.649 18.359 1.00 47.02 C HETATM 3730 C11 OLB A2429 -15.827 -12.503 17.474 1.00 47.73 C HETATM 3731 C12 OLB A2429 -15.314 -11.172 18.007 1.00 50.65 C HETATM 3732 C13 OLB A2429 -16.122 -10.684 19.206 1.00 53.99 C HETATM 3733 C1 OLB A2430 17.724 11.575 25.793 1.00 58.90 C HETATM 3734 C2 OLB A2430 17.760 10.197 26.432 1.00 46.52 C HETATM 3735 C3 OLB A2430 17.371 9.146 25.398 1.00 40.42 C HETATM 3736 C4 OLB A2430 17.413 7.739 25.968 1.00 35.28 C HETATM 3737 C5 OLB A2430 16.573 6.754 25.166 1.00 32.87 C HETATM 3738 O19 OLB A2430 17.318 11.640 24.683 1.00 68.23 O HETATM 3739 O20 OLB A2430 18.142 12.746 26.445 1.00 61.21 O HETATM 3740 C21 OLB A2430 18.073 13.861 25.589 1.00 65.07 C HETATM 3741 C22 OLB A2430 18.218 15.179 26.357 1.00 70.58 C HETATM 3742 O23 OLB A2430 19.480 15.733 26.087 1.00 71.63 O HETATM 3743 C24 OLB A2430 17.172 16.220 25.952 1.00 74.14 C HETATM 3744 O25 OLB A2430 17.109 16.294 24.551 1.00 73.98 O HETATM 3745 C6 OLB A2430 17.176 5.363 25.203 1.00 35.66 C HETATM 3746 C7 OLB A2430 16.177 4.234 25.378 1.00 37.69 C HETATM 3747 C8 OLB A2430 16.603 3.028 24.555 1.00 39.10 C HETATM 3748 C9 OLB A2430 16.059 1.744 25.155 1.00 42.78 C HETATM 3749 C10 OLB A2430 16.236 0.622 24.494 1.00 46.41 C HETATM 3750 C11 OLB A2430 15.697 -0.688 25.060 1.00 49.10 C HETATM 3751 C12 OLB A2430 16.339 -1.864 24.323 1.00 50.01 C HETATM 3752 C10 OLC A2431 -9.839 -3.486 37.704 1.00 53.66 C HETATM 3753 C9 OLC A2431 -10.153 -2.227 37.446 1.00 52.46 C HETATM 3754 C11 OLC A2431 -9.508 -4.438 36.546 1.00 49.70 C HETATM 3755 C8 OLC A2431 -10.481 -1.226 38.553 1.00 45.77 C HETATM 3756 C24 OLC A2431 -9.205 9.747 34.972 1.00 63.46 C HETATM 3757 C12 OLC A2431 -8.791 -5.672 37.090 1.00 43.48 C HETATM 3758 C7 OLC A2431 -11.552 -0.269 38.043 1.00 44.11 C HETATM 3759 C13 OLC A2431 -7.420 -5.889 36.466 1.00 39.50 C HETATM 3760 C6 OLC A2431 -11.136 1.194 38.065 1.00 42.25 C HETATM 3761 C14 OLC A2431 -6.450 -6.555 37.436 1.00 39.48 C HETATM 3762 C5 OLC A2431 -12.298 2.136 37.740 1.00 43.14 C HETATM 3763 C4 OLC A2431 -11.759 3.428 37.141 1.00 42.31 C HETATM 3764 C3 OLC A2431 -12.730 4.583 36.950 1.00 44.88 C HETATM 3765 C2 OLC A2431 -11.908 5.829 36.620 1.00 48.35 C HETATM 3766 C21 OLC A2431 -10.783 8.296 36.344 1.00 64.48 C HETATM 3767 C1 OLC A2431 -12.736 7.048 36.218 1.00 57.57 C HETATM 3768 C22 OLC A2431 -10.205 9.689 36.133 1.00 67.14 C HETATM 3769 O19 OLC A2431 -13.859 6.908 35.883 1.00 64.60 O HETATM 3770 O25 OLC A2431 -8.626 11.026 34.887 1.00 63.03 O HETATM 3771 O23 OLC A2431 -11.267 10.590 35.942 1.00 71.74 O HETATM 3772 O20 OLC A2431 -12.177 8.331 36.241 1.00 60.63 O HETATM 3773 O HOH A2501 -4.003 13.008 13.404 1.00 55.28 O HETATM 3774 O HOH A2502 -13.153 17.048 28.858 1.00 46.50 O HETATM 3775 O HOH A2503 10.349 15.153 10.648 1.00 41.58 O HETATM 3776 O HOH A2504 21.236 -46.848 20.663 1.00 47.72 O HETATM 3777 O HOH A2505 6.613 -33.605 21.159 1.00 45.00 O HETATM 3778 O HOH A2506 -2.858 -27.978 21.452 1.00 47.22 O HETATM 3779 O HOH A2507 15.106 -37.795 20.965 1.00 50.24 O HETATM 3780 O HOH A2508 19.822 -51.105 21.676 1.00 47.50 O HETATM 3781 O HOH A2509 9.110 -34.221 21.807 1.00 45.68 O HETATM 3782 O HOH A2510 -9.407 12.369 8.676 1.00 42.97 O HETATM 3783 O HOH A2511 -4.715 23.556 30.131 1.00 43.11 O HETATM 3784 O HOH A2512 -5.278 -16.020 14.712 1.00 20.03 O HETATM 3785 O HOH A2513 16.892 -64.690 20.373 1.00 39.70 O HETATM 3786 O HOH A2514 -4.564 6.857 17.166 1.00 52.58 O HETATM 3787 O HOH A2515 25.542 -73.526 20.215 1.00 53.22 O HETATM 3788 O HOH A2516 7.136 17.617 11.441 1.00 38.35 O HETATM 3789 O HOH A2517 -5.666 -13.414 13.460 1.00 20.27 O HETATM 3790 O HOH A2518 23.665 -47.501 26.443 1.00 50.48 O HETATM 3791 O HOH A2519 2.711 -25.309 9.882 1.00 44.35 O HETATM 3792 O HOH A2520 -3.074 -31.485 35.301 1.00 63.33 O HETATM 3793 O HOH A2521 5.481 -58.426 23.060 1.00 65.09 O HETATM 3794 O HOH A2522 -4.766 -30.762 25.374 1.00 52.82 O HETATM 3795 O HOH A2523 -8.989 2.581 19.623 1.00 15.68 O HETATM 3796 O HOH A2524 1.099 10.256 23.031 1.00 25.06 O HETATM 3797 O HOH A2525 -1.048 16.382 19.037 1.00 28.60 O HETATM 3798 O HOH A2526 -20.125 15.140 22.971 1.00 42.95 O HETATM 3799 O HOH A2527 15.400 -63.751 27.225 1.00 52.90 O HETATM 3800 O HOH A2528 0.836 -11.479 13.084 1.00 20.61 O HETATM 3801 O HOH A2529 5.312 -27.020 17.494 1.00 27.61 O HETATM 3802 O HOH A2530 -11.451 7.956 32.418 1.00 45.06 O HETATM 3803 O HOH A2531 11.932 10.021 31.032 1.00 41.31 O HETATM 3804 O HOH A2532 -23.608 14.515 9.471 1.00 66.50 O HETATM 3805 O HOH A2533 -6.509 18.496 22.327 1.00 20.25 O HETATM 3806 O HOH A2534 1.613 12.880 23.743 1.00 25.33 O HETATM 3807 O HOH A2535 -11.393 21.771 27.756 1.00 51.24 O HETATM 3808 O HOH A2536 22.249 -52.704 30.128 1.00 61.85 O HETATM 3809 O HOH A2537 3.295 -16.976 19.090 1.00 21.18 O HETATM 3810 O HOH A2538 -5.816 5.350 18.748 1.00 18.14 O HETATM 3811 O HOH A2539 -4.222 -11.127 11.367 1.00 21.73 O HETATM 3812 O HOH A2540 23.832 -73.198 23.982 1.00 52.68 O HETATM 3813 O HOH A2541 -6.397 -11.914 25.688 1.00 23.71 O HETATM 3814 O HOH A2542 -3.672 -4.789 14.008 1.00 17.31 O HETATM 3815 O HOH A2543 18.846 -62.936 20.141 1.00 38.73 O HETATM 3816 O HOH A2544 0.308 -35.860 26.631 1.00 47.17 O HETATM 3817 O HOH A2545 -5.540 2.484 15.873 1.00 19.35 O HETATM 3818 O HOH A2546 4.751 10.029 17.888 1.00 15.63 O HETATM 3819 O HOH A2547 -8.033 -28.840 33.547 1.00 69.45 O HETATM 3820 O HOH A2548 -6.155 -12.163 21.511 1.00 18.99 O HETATM 3821 O HOH A2549 8.433 15.190 23.256 1.00 39.63 O HETATM 3822 O HOH A2550 -5.050 16.794 2.174 1.00 37.55 O HETATM 3823 O HOH A2551 -6.186 7.698 13.311 1.00 18.91 O HETATM 3824 O HOH A2552 3.000 -29.430 11.572 1.00 46.18 O HETATM 3825 O HOH A2553 0.286 -1.657 22.068 1.00 17.04 O HETATM 3826 O HOH A2554 -2.919 14.310 15.121 1.00 26.61 O HETATM 3827 O HOH A2555 20.169 -67.314 25.141 1.00 42.08 O HETATM 3828 O HOH A2556 9.606 14.652 25.452 1.00 37.45 O HETATM 3829 O HOH A2557 -8.019 2.956 16.992 1.00 15.08 O HETATM 3830 O HOH A2558 -5.661 11.764 16.405 1.00 24.00 O HETATM 3831 O HOH A2559 -5.996 -14.560 24.740 1.00 25.05 O HETATM 3832 O HOH A2560 -1.132 -2.695 24.279 1.00 19.68 O HETATM 3833 O HOH A2561 20.259 -61.940 29.758 1.00 41.53 O HETATM 3834 O HOH A2562 -14.104 13.831 30.405 1.00 46.76 O HETATM 3835 O HOH A2563 3.137 16.679 8.931 1.00 35.05 O HETATM 3836 O HOH A2564 27.917 -72.525 22.215 1.00 56.45 O HETATM 3837 O HOH A2565 3.440 0.623 12.729 1.00 16.60 O HETATM 3838 O HOH A2566 15.062 -26.828 15.519 1.00 44.47 O HETATM 3839 O HOH A2567 -3.906 15.178 33.442 1.00 41.87 O HETATM 3840 O HOH A2568 8.567 15.720 20.160 1.00 54.66 O HETATM 3841 O HOH A2569 34.721 -55.768 18.490 1.00 50.89 O HETATM 3842 O HOH A2570 -3.821 4.220 17.042 1.00 26.02 O HETATM 3843 O HOH A2571 -8.248 5.457 17.677 1.00 19.55 O HETATM 3844 O HOH A2572 -2.950 18.111 26.275 1.00 56.94 O HETATM 3845 O HOH A2573 10.104 14.969 18.321 1.00 58.01 O HETATM 3846 O HOH A2574 15.338 -25.939 24.925 1.00 38.80 O HETATM 3847 O HOH A2575 15.016 -64.032 17.999 1.00 43.09 O HETATM 3848 O HOH A2576 -7.646 -11.537 6.702 1.00 34.54 O HETATM 3849 O HOH A2577 3.669 15.498 20.645 1.00 48.42 O HETATM 3850 O HOH A2578 8.717 12.050 15.940 1.00 20.34 O HETATM 3851 O HOH A2579 -4.828 9.862 14.548 1.00 25.26 O HETATM 3852 O HOH A2580 1.546 -2.847 20.110 1.00 19.53 O HETATM 3853 O HOH A2581 26.959 -60.794 15.535 1.00 46.36 O HETATM 3854 O HOH A2582 -2.367 -6.685 15.436 1.00 21.02 O HETATM 3855 O HOH A2583 -12.621 23.957 26.203 1.00 49.76 O HETATM 3856 O HOH A2584 29.075 -70.577 20.836 1.00 38.38 O HETATM 3857 O HOH A2585 1.366 -23.290 13.932 1.00 39.65 O HETATM 3858 O HOH A2586 5.591 -27.988 19.636 1.00 37.17 O HETATM 3859 O HOH A2587 14.029 -61.368 28.384 1.00 48.19 O HETATM 3860 O HOH A2588 1.752 -17.386 16.847 1.00 21.60 O HETATM 3861 O HOH A2589 4.454 3.488 21.837 1.00 16.18 O HETATM 3862 O HOH A2590 17.552 13.218 22.317 1.00 32.38 O HETATM 3863 O HOH A2591 -16.668 -30.740 17.632 1.00 51.68 O HETATM 3864 O HOH A2592 -15.635 -31.830 12.886 1.00 53.19 O HETATM 3865 O HOH A2593 -0.867 -11.455 15.281 1.00 30.95 O HETATM 3866 O HOH A2594 7.356 -35.976 28.199 1.00 47.11 O HETATM 3867 O HOH A2595 16.209 16.234 21.836 1.00 36.89 O HETATM 3868 O HOH A2596 14.650 15.892 11.502 1.00 50.58 O HETATM 3869 O HOH A2597 -8.009 20.816 22.516 1.00 21.06 O HETATM 3870 O HOH A2598 -6.044 18.759 24.933 1.00 22.91 O HETATM 3871 O HOH A2599 1.639 16.088 19.112 1.00 36.26 O HETATM 3872 O HOH A2600 -2.175 13.783 18.019 1.00 19.46 O HETATM 3873 O HOH A2601 2.250 13.645 29.646 1.00 47.08 O HETATM 3874 O HOH A2602 -3.199 28.881 -0.384 1.00 50.32 O HETATM 3875 O HOH A2603 -8.158 11.007 37.776 1.00 34.59 O HETATM 3876 O HOH A2604 -2.694 -10.049 15.336 1.00 29.98 O HETATM 3877 O HOH A2605 -5.939 17.028 26.906 1.00 35.02 O HETATM 3878 O HOH A2606 8.007 19.373 15.087 1.00 55.58 O HETATM 3879 O HOH A2607 -5.264 -6.650 17.656 1.00 32.43 O HETATM 3880 O HOH A2608 14.351 -31.417 24.665 1.00 48.12 O HETATM 3881 O HOH A2609 4.646 12.202 28.589 1.00 24.62 O HETATM 3882 O HOH A2610 -9.911 17.973 29.340 1.00 52.44 O HETATM 3883 O HOH A2611 -1.343 -33.531 22.137 1.00 63.62 O HETATM 3884 O HOH A2612 2.464 13.468 26.220 1.00 28.23 O HETATM 3885 O HOH A2613 7.968 14.906 5.054 1.00 58.48 O HETATM 3886 O HOH A2614 25.507 -76.129 26.481 1.00 36.61 O HETATM 3887 O HOH A2615 14.853 17.920 13.085 1.00 46.79 O HETATM 3888 O HOH A2616 0.963 -26.877 4.551 1.00 47.55 O HETATM 3889 O HOH A2617 -5.342 -29.694 23.039 1.00 47.07 O HETATM 3890 O HOH A2618 -4.933 -4.038 18.062 1.00 51.89 O HETATM 3891 O HOH A2619 -1.956 -29.168 9.103 1.00 35.52 O HETATM 3892 O HOH A2620 -0.060 -31.028 21.074 1.00 48.52 O HETATM 3893 O HOH A2621 20.860 -44.594 25.271 1.00 64.80 O HETATM 3894 O HOH A2622 2.310 15.230 6.188 1.00 34.71 O HETATM 3895 O HOH A2623 -16.448 18.526 16.364 1.00 44.47 O HETATM 3896 O HOH A2624 10.710 13.474 17.043 1.00 31.79 O HETATM 3897 O HOH A2625 3.638 -33.452 15.508 1.00 42.47 O HETATM 3898 O HOH A2626 -2.265 11.993 37.262 1.00 45.56 O HETATM 3899 O HOH A2627 -1.208 12.059 34.644 1.00 45.55 O HETATM 3900 O HOH A2628 -11.598 -30.122 6.331 1.00 64.20 O HETATM 3901 O HOH A2629 0.204 12.472 32.798 1.00 46.63 O HETATM 3902 O HOH A2630 21.607 17.680 27.706 1.00 61.73 O HETATM 3903 O HOH A2631 -10.975 20.338 3.433 1.00 41.75 O HETATM 3904 O HOH A2632 -20.019 19.875 26.905 1.00 62.76 O HETATM 3905 O HOH A2633 2.781 -25.908 3.997 1.00 60.17 O HETATM 3906 O HOH A2634 -1.830 22.960 27.296 1.00 46.28 O HETATM 3907 O AHOH A2635 0.459 -28.458 8.544 0.46 21.67 O HETATM 3908 O BHOH A2635 0.834 -28.236 6.824 0.54 22.44 O HETATM 3909 O HOH A2636 -1.039 18.350 16.974 1.00 42.68 O HETATM 3910 O HOH A2637 -0.473 -18.850 15.650 1.00 39.66 O HETATM 3911 O HOH A2638 3.085 -30.927 15.341 1.00 48.68 O HETATM 3912 O HOH A2639 -4.002 15.241 4.936 1.00 57.99 O HETATM 3913 O HOH A2640 4.407 -30.044 7.935 1.00 52.89 O HETATM 3914 O HOH A2641 2.575 -33.075 22.086 1.00 59.52 O HETATM 3915 O HOH A2642 18.376 -48.095 20.890 1.00 69.05 O HETATM 3916 O HOH A2643 -5.055 6.315 15.291 1.00 32.88 O HETATM 3917 O HOH A2644 3.898 14.090 22.390 1.00 37.51 O HETATM 3918 O HOH A2645 27.901 -75.366 27.568 1.00 48.44 O HETATM 3919 O HOH A2646 -19.612 -28.744 13.385 1.00 64.48 O HETATM 3920 O HOH A2647 1.143 -34.758 22.849 1.00 67.39 O HETATM 3921 O HOH A2648 28.655 -62.264 13.567 1.00 56.35 O HETATM 3922 O HOH A2649 -11.551 16.162 31.572 1.00 65.57 O HETATM 3923 O HOH A2650 25.781 -71.210 17.465 1.00 55.21 O HETATM 3924 O HOH A2651 -11.572 -22.346 -2.682 1.00 33.38 O HETATM 3925 O HOH A2652 6.241 13.599 24.035 1.00 30.37 O HETATM 3926 O HOH A2653 1.369 -27.178 11.212 1.00 47.85 O HETATM 3927 O HOH A2654 -4.715 -2.519 15.386 1.00 43.07 O HETATM 3928 O HOH A2655 -14.602 -29.270 7.897 1.00 59.18 O HETATM 3929 O HOH A2656 -1.867 17.086 15.037 1.00 57.13 O HETATM 3930 O HOH A2657 -0.429 -21.395 15.080 1.00 42.59 O CONECT 449 3235 CONECT 600 1307 CONECT 616 1207 CONECT 636 1351 CONECT 757 3235 CONECT 1207 616 CONECT 1307 600 CONECT 1351 636 CONECT 2799 2820 CONECT 2820 2799 CONECT 3235 449 757 3854 3876 CONECT 3235 3879 CONECT 3236 3247 3256 CONECT 3237 3245 3255 CONECT 3238 3244 3246 CONECT 3239 3242 3244 CONECT 3240 3257 3258 3260 CONECT 3241 3258 3259 3261 CONECT 3242 3239 3243 CONECT 3243 3242 3246 CONECT 3244 3238 3239 CONECT 3245 3237 3247 CONECT 3246 3238 3243 3247 CONECT 3247 3236 3245 3246 CONECT 3248 3249 CONECT 3249 3248 3250 3260 CONECT 3250 3249 3251 CONECT 3251 3250 3252 3257 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3237 3254 3256 CONECT 3256 3236 3255 CONECT 3257 3240 3251 CONECT 3258 3240 3241 CONECT 3259 3241 3260 CONECT 3260 3240 3249 3259 CONECT 3261 3241 3262 3265 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3261 3264 CONECT 3266 3267 3275 CONECT 3267 3266 3268 CONECT 3268 3267 3269 3293 CONECT 3269 3268 3270 CONECT 3270 3269 3271 3275 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 3279 CONECT 3274 3273 3275 3276 CONECT 3275 3266 3270 3274 3284 CONECT 3276 3274 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3279 3282 3283 CONECT 3279 3273 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3278 3281 3285 CONECT 3283 3278 CONECT 3284 3275 CONECT 3285 3282 3286 3287 CONECT 3286 3285 CONECT 3287 3285 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 3291 3292 CONECT 3291 3290 CONECT 3292 3290 CONECT 3293 3268 CONECT 3294 3295 3303 CONECT 3295 3294 3296 CONECT 3296 3295 3297 3321 CONECT 3297 3296 3298 CONECT 3298 3297 3299 3303 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 3307 CONECT 3302 3301 3303 3304 CONECT 3303 3294 3298 3302 3312 CONECT 3304 3302 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 3310 3311 CONECT 3307 3301 3306 3308 CONECT 3308 3307 3309 CONECT 3309 3308 3310 CONECT 3310 3306 3309 3313 CONECT 3311 3306 CONECT 3312 3303 CONECT 3313 3310 3314 3315 CONECT 3314 3313 CONECT 3315 3313 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 3320 CONECT 3319 3318 CONECT 3320 3318 CONECT 3321 3296 CONECT 3322 3323 3331 CONECT 3323 3322 3324 CONECT 3324 3323 3325 3349 CONECT 3325 3324 3326 CONECT 3326 3325 3327 3331 CONECT 3327 3326 3328 CONECT 3328 3327 3329 CONECT 3329 3328 3330 3335 CONECT 3330 3329 3331 3332 CONECT 3331 3322 3326 3330 3340 CONECT 3332 3330 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 3338 3339 CONECT 3335 3329 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3334 3337 3341 CONECT 3339 3334 CONECT 3340 3331 CONECT 3341 3338 3342 3343 CONECT 3342 3341 CONECT 3343 3341 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 3348 CONECT 3347 3346 CONECT 3348 3346 CONECT 3349 3324 CONECT 3350 3351 3359 CONECT 3351 3350 3352 CONECT 3352 3351 3353 3377 CONECT 3353 3352 3354 CONECT 3354 3353 3355 3359 CONECT 3355 3354 3356 CONECT 3356 3355 3357 CONECT 3357 3356 3358 3363 CONECT 3358 3357 3359 3360 CONECT 3359 3350 3354 3358 3368 CONECT 3360 3358 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 3366 3367 CONECT 3363 3357 3362 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3362 3365 3369 CONECT 3367 3362 CONECT 3368 3359 CONECT 3369 3366 3370 3371 CONECT 3370 3369 CONECT 3371 3369 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 3376 CONECT 3375 3374 CONECT 3376 3374 CONECT 3377 3352 CONECT 3378 3379 3380 3381 CONECT 3379 3378 CONECT 3380 3378 CONECT 3381 3378 3382 CONECT 3382 3381 3383 CONECT 3383 3382 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 CONECT 3398 3399 3400 3401 CONECT 3399 3398 CONECT 3400 3398 CONECT 3401 3398 3402 CONECT 3402 3401 3403 CONECT 3403 3402 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 CONECT 3413 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 CONECT 3420 3421 3422 3423 CONECT 3421 3420 CONECT 3422 3420 CONECT 3423 3420 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3430 CONECT 3430 3429 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 CONECT 3438 3439 3440 3441 CONECT 3439 3438 CONECT 3440 3438 CONECT 3441 3438 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 3449 CONECT 3449 3448 3450 CONECT 3450 3449 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 CONECT 3458 3459 3460 3461 CONECT 3459 3458 CONECT 3460 3458 CONECT 3461 3458 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 CONECT 3473 3474 3475 3476 CONECT 3474 3473 CONECT 3475 3473 CONECT 3476 3473 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 3487 3488 CONECT 3486 3485 CONECT 3487 3485 CONECT 3488 3485 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 CONECT 3493 3494 CONECT 3494 3493 3495 CONECT 3495 3494 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 CONECT 3508 3509 3510 3511 CONECT 3509 3508 CONECT 3510 3508 CONECT 3511 3508 3512 CONECT 3512 3511 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 3520 CONECT 3520 3519 3521 CONECT 3521 3520 CONECT 3522 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 CONECT 3530 3531 3532 3533 CONECT 3531 3530 CONECT 3532 3530 CONECT 3533 3530 3534 CONECT 3534 3533 3535 CONECT 3535 3534 3536 CONECT 3536 3535 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 CONECT 3549 3550 CONECT 3550 3549 3551 CONECT 3551 3550 3552 CONECT 3552 3551 3553 CONECT 3553 3552 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 CONECT 3560 3561 3562 3563 CONECT 3561 3560 CONECT 3562 3560 CONECT 3563 3560 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 CONECT 3571 3572 3573 3574 CONECT 3572 3571 CONECT 3573 3571 CONECT 3574 3571 3575 CONECT 3575 3574 3576 CONECT 3576 3575 3577 CONECT 3577 3576 3578 CONECT 3578 3577 3579 CONECT 3579 3578 3580 CONECT 3580 3579 3581 CONECT 3581 3580 CONECT 3582 3583 CONECT 3583 3582 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3587 3589 CONECT 3589 3588 3590 CONECT 3590 3589 3591 CONECT 3591 3590 CONECT 3592 3593 CONECT 3593 3592 3594 CONECT 3594 3593 3595 CONECT 3595 3594 3596 CONECT 3596 3595 3597 CONECT 3597 3596 3598 CONECT 3598 3597 3599 CONECT 3599 3598 3600 CONECT 3600 3599 3601 CONECT 3601 3600 3602 CONECT 3602 3601 3603 CONECT 3603 3602 CONECT 3604 3605 CONECT 3605 3604 3606 CONECT 3606 3605 3607 CONECT 3607 3606 3608 CONECT 3608 3607 3609 CONECT 3609 3608 3610 CONECT 3610 3609 3611 CONECT 3611 3610 CONECT 3612 3613 3617 3618 CONECT 3613 3612 3614 CONECT 3614 3613 3615 CONECT 3615 3614 3616 CONECT 3616 3615 3624 CONECT 3617 3612 CONECT 3618 3612 3619 CONECT 3619 3618 3620 CONECT 3620 3619 3621 3622 CONECT 3621 3620 CONECT 3622 3620 3623 CONECT 3623 3622 CONECT 3624 3616 3625 CONECT 3625 3624 3626 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3629 CONECT 3629 3628 3630 CONECT 3630 3629 CONECT 3631 3632 3636 3637 CONECT 3632 3631 3633 CONECT 3633 3632 3634 CONECT 3634 3633 3635 CONECT 3635 3634 3643 CONECT 3636 3631 CONECT 3637 3631 3638 CONECT 3638 3637 3639 CONECT 3639 3638 3640 3641 CONECT 3640 3639 CONECT 3641 3639 3642 CONECT 3642 3641 CONECT 3643 3635 3644 CONECT 3644 3643 3645 CONECT 3645 3644 3646 CONECT 3646 3645 CONECT 3647 3648 3652 3653 CONECT 3648 3647 3649 CONECT 3649 3648 3650 CONECT 3650 3649 3651 CONECT 3651 3650 3659 CONECT 3652 3647 CONECT 3653 3647 3654 CONECT 3654 3653 3655 CONECT 3655 3654 3656 3657 CONECT 3656 3655 CONECT 3657 3655 3658 CONECT 3658 3657 CONECT 3659 3651 3660 CONECT 3660 3659 3661 CONECT 3661 3660 3662 CONECT 3662 3661 3663 CONECT 3663 3662 3664 CONECT 3664 3663 3665 CONECT 3665 3664 3666 CONECT 3666 3665 3667 CONECT 3667 3666 3668 CONECT 3668 3667 CONECT 3669 3670 3674 3675 CONECT 3670 3669 3671 CONECT 3671 3670 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3681 CONECT 3674 3669 CONECT 3675 3669 3676 CONECT 3676 3675 3677 CONECT 3677 3676 3678 3679 CONECT 3678 3677 CONECT 3679 3677 3680 CONECT 3680 3679 CONECT 3681 3673 3682 CONECT 3682 3681 3683 CONECT 3683 3682 3684 CONECT 3684 3683 3685 CONECT 3685 3684 3686 CONECT 3686 3685 3687 CONECT 3687 3686 CONECT 3688 3689 3693 3694 CONECT 3689 3688 3690 CONECT 3690 3689 3691 CONECT 3691 3690 3692 CONECT 3692 3691 3700 CONECT 3693 3688 CONECT 3694 3688 3695 CONECT 3695 3694 3696 CONECT 3696 3695 3697 3698 CONECT 3697 3696 CONECT 3698 3696 3699 CONECT 3699 3698 CONECT 3700 3692 3701 CONECT 3701 3700 3702 CONECT 3702 3701 3703 CONECT 3703 3702 3704 CONECT 3704 3703 3705 CONECT 3705 3704 3706 CONECT 3706 3705 3707 CONECT 3707 3706 3708 CONECT 3708 3707 3709 CONECT 3709 3708 3710 CONECT 3710 3709 3711 CONECT 3711 3710 3712 CONECT 3712 3711 CONECT 3713 3714 3718 3719 CONECT 3714 3713 3715 CONECT 3715 3714 3716 CONECT 3716 3715 3717 CONECT 3717 3716 3725 CONECT 3718 3713 CONECT 3719 3713 3720 CONECT 3720 3719 3721 CONECT 3721 3720 3722 3723 CONECT 3722 3721 CONECT 3723 3721 3724 CONECT 3724 3723 CONECT 3725 3717 3726 CONECT 3726 3725 3727 CONECT 3727 3726 3728 CONECT 3728 3727 3729 CONECT 3729 3728 3730 CONECT 3730 3729 3731 CONECT 3731 3730 3732 CONECT 3732 3731 CONECT 3733 3734 3738 3739 CONECT 3734 3733 3735 CONECT 3735 3734 3736 CONECT 3736 3735 3737 CONECT 3737 3736 3745 CONECT 3738 3733 CONECT 3739 3733 3740 CONECT 3740 3739 3741 CONECT 3741 3740 3742 3743 CONECT 3742 3741 CONECT 3743 3741 3744 CONECT 3744 3743 CONECT 3745 3737 3746 CONECT 3746 3745 3747 CONECT 3747 3746 3748 CONECT 3748 3747 3749 CONECT 3749 3748 3750 CONECT 3750 3749 3751 CONECT 3751 3750 CONECT 3752 3753 3754 CONECT 3753 3752 3755 CONECT 3754 3752 3757 CONECT 3755 3753 3758 CONECT 3756 3768 3770 CONECT 3757 3754 3759 CONECT 3758 3755 3760 CONECT 3759 3757 3761 CONECT 3760 3758 3762 CONECT 3761 3759 CONECT 3762 3760 3763 CONECT 3763 3762 3764 CONECT 3764 3763 3765 CONECT 3765 3764 3767 CONECT 3766 3768 3772 CONECT 3767 3765 3769 3772 CONECT 3768 3756 3766 3771 CONECT 3769 3767 CONECT 3770 3756 CONECT 3771 3768 CONECT 3772 3766 3767 CONECT 3854 3235 CONECT 3876 3235 CONECT 3879 3235 MASTER 788 0 32 19 2 0 50 6 3726 1 552 34 END