Browse entries in the PDBbind-CN Database
HEADER TRANSCRIPTION 11-DEC-07 3BLH TITLE CRYSTAL STRUCTURE OF HUMAN CDK9/CYCLINT1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 9; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 2-330; COMPND 5 SYNONYM: CYCLIN-DEPENDENT KINASE 9, SERINE/THREONINE- COMPND 6 PROTEIN KINASE PITALRE, C-2K, CELL DIVISION CYCLE 2-LIKE COMPND 7 PROTEIN KINASE 4; COMPND 8 EC: 2.7.11.22, 2.7.11.23; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: CYCLIN-T1; COMPND 12 CHAIN: B; COMPND 13 FRAGMENT: UNP RESIDUES 2-259; COMPND 14 SYNONYM: CYCT1, CYCLIN-T; COMPND 15 ENGINEERED: YES; COMPND 16 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CDK9; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVL1392; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: CCNT1; SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS; SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PVL1392 KEYWDS TRANSCRIPTIONAL CDK/CYCLIN COMPLEX, PHOSPHORYLATED, KEYWDS 2 ALTERNATIVE SPLICING, ATP-BINDING, KINASE, NUCLEOTIDE- KEYWDS 3 BINDING, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, KEYWDS 4 SERINE/THREONINE-PROTEIN KINASE, TRANSCRIPTION REGULATION, KEYWDS 5 TRANSFERASE, ACETYLATION, CELL CYCLE, CELL DIVISION, COILED KEYWDS 6 COIL, HOST-VIRUS INTERACTION EXPDTA X-RAY DIFFRACTION AUTHOR S.BAUMLI,G.LOLLI,E.D.LOWE,L.N.JOHNSON REVDAT 4 19-MAY-09 3BLH 1 REMARK REVDAT 3 24-FEB-09 3BLH 1 VERSN REVDAT 2 12-AUG-08 3BLH 1 JRNL REVDAT 1 01-JUL-08 3BLH 0 JRNL AUTH S.BAUMLI,G.LOLLI,E.D.LOWE,S.TROIANI,L.RUSCONI, JRNL AUTH 2 A.N.BULLOCK,J.E.DEBRECZENI,S.KNAPP,L.N.JOHNSON JRNL TITL THE STRUCTURE OF P-TEFB (CDK9/CYCLIN T1), ITS JRNL TITL 2 COMPLEX WITH FLAVOPIRIDOL AND REGULATION BY JRNL TITL 3 PHOSPHORYLATION JRNL REF EMBO J. V. 27 1907 2008 JRNL REFN ISSN 0261-4189 JRNL PMID 18566585 JRNL DOI 10.1038/EMBOJ.2008.121 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.48 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.73 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 37490 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.221 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 3600 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 48.7360 - 12.7090 0.50 281 0 0.2910 0.0000 REMARK 3 2 12.7090 - 10.1170 0.59 325 0 0.1870 0.0000 REMARK 3 3 10.1170 - 8.8470 0.74 408 0 0.1590 0.0000 REMARK 3 4 8.8470 - 8.0420 0.85 469 0 0.1580 0.0000 REMARK 3 5 8.0420 - 7.4680 0.91 491 0 0.1510 0.0000 REMARK 3 6 7.4680 - 7.0290 0.94 523 0 0.1540 0.0000 REMARK 3 7 7.0290 - 6.6780 0.81 449 0 0.1730 0.0000 REMARK 3 8 6.6780 - 6.3880 0.79 450 0 0.1720 0.0000 REMARK 3 9 6.3880 - 6.1420 0.88 464 0 0.1630 0.0000 REMARK 3 10 6.1420 - 5.9310 0.87 483 0 0.1760 0.0000 REMARK 3 11 5.9310 - 5.7460 0.87 511 0 0.1590 0.0000 REMARK 3 12 5.7460 - 5.5820 0.91 466 0 0.1570 0.0000 REMARK 3 13 5.5820 - 5.4350 0.90 511 0 0.1590 0.0000 REMARK 3 14 5.4350 - 5.3020 0.92 506 0 0.1500 0.0000 REMARK 3 15 5.3020 - 5.1820 0.93 517 0 0.1370 0.0000 REMARK 3 16 5.1820 - 5.0720 0.90 475 0 0.1330 0.0000 REMARK 3 17 5.0720 - 4.9710 0.91 515 0 0.1320 0.0000 REMARK 3 18 4.9710 - 4.8770 0.89 514 0 0.1230 0.0000 REMARK 3 19 4.8770 - 4.7900 0.91 482 0 0.1240 0.0000 REMARK 3 20 4.7900 - 4.7090 0.92 513 0 0.1190 0.0000 REMARK 3 21 4.7090 - 4.6330 0.89 490 0 0.1300 0.0000 REMARK 3 22 4.6330 - 4.5620 0.89 470 0 0.1090 0.0000 REMARK 3 23 4.5620 - 4.4950 0.92 519 0 0.1240 0.0000 REMARK 3 24 4.4950 - 4.4310 0.90 532 0 0.1170 0.0000 REMARK 3 25 4.4310 - 4.3720 0.90 447 0 0.1210 0.0000 REMARK 3 26 4.3720 - 4.3150 0.91 525 0 0.1150 0.0000 REMARK 3 27 4.3150 - 4.2610 0.90 530 0 0.1280 0.0000 REMARK 3 28 4.2610 - 4.2090 0.93 482 0 0.1310 0.0000 REMARK 3 29 4.2090 - 4.1610 0.92 486 0 0.1270 0.0000 REMARK 3 30 4.1610 - 4.1140 0.94 544 0 0.1240 0.0000 REMARK 3 31 4.1140 - 4.0690 0.91 524 0 0.1320 0.0000 REMARK 3 32 4.0690 - 4.0260 0.91 470 0 0.1440 0.0000 REMARK 3 33 4.0260 - 3.9850 0.91 545 0 0.1370 0.0000 REMARK 3 34 3.9850 - 3.9460 0.89 438 0 0.1630 0.0000 REMARK 3 35 3.9460 - 3.9080 0.94 558 0 0.1430 0.0000 REMARK 3 36 3.9080 - 3.8720 0.91 496 0 0.1510 0.0000 REMARK 3 37 3.8720 - 3.8360 0.89 496 0 0.1650 0.0000 REMARK 3 38 3.8360 - 3.8020 0.94 518 0 0.1560 0.0000 REMARK 3 39 3.8020 - 3.7700 0.92 499 0 0.1570 0.0000 REMARK 3 40 3.7700 - 3.7380 0.94 511 0 0.1640 0.0000 REMARK 3 41 3.7380 - 3.7070 0.92 509 0 0.1720 0.0000 REMARK 3 42 3.7070 - 3.6780 0.90 489 0 0.1560 0.0000 REMARK 3 43 3.6780 - 3.6490 0.92 568 0 0.1800 0.0000 REMARK 3 44 3.6490 - 3.6210 0.92 432 0 0.1580 0.0000 REMARK 3 45 3.6210 - 3.5940 0.93 521 0 0.1570 0.0000 REMARK 3 46 3.5940 - 3.5680 0.94 542 0 0.1740 0.0000 REMARK 3 47 3.5680 - 3.5420 0.91 482 0 0.1750 0.0000 REMARK 3 48 3.5420 - 3.5180 0.90 515 0 0.1810 0.0000 REMARK 3 49 3.5180 - 3.4930 0.89 457 0 0.1640 0.0000 REMARK 3 50 3.4930 - 3.4700 0.91 540 0 0.1750 0.0000 REMARK 3 51 3.4700 - 3.4470 0.93 534 0 0.1910 0.0000 REMARK 3 52 3.4470 - 3.4250 0.92 526 0 0.1900 0.0000 REMARK 3 53 3.4250 - 3.4030 0.95 504 0 0.1710 0.0000 REMARK 3 54 3.4030 - 3.3820 0.92 475 0 0.1860 0.0000 REMARK 3 55 3.3820 - 3.3620 0.91 513 0 0.1850 0.0000 REMARK 3 56 3.3620 - 3.3420 0.92 540 0 0.1720 0.0000 REMARK 3 57 3.3420 - 3.3220 0.92 482 0 0.1770 0.0000 REMARK 3 58 3.3220 - 3.3030 0.92 491 0 0.1910 0.0000 REMARK 3 59 3.3030 - 3.2840 0.92 478 0 0.1730 0.0000 REMARK 3 60 3.2840 - 3.2660 0.94 542 0 0.1580 0.0000 REMARK 3 61 3.2660 - 3.2480 0.94 549 0 0.1690 0.0000 REMARK 3 62 3.2480 - 3.2300 0.93 502 0 0.1780 0.0000 REMARK 3 63 3.2300 - 3.2130 0.92 529 0 0.1890 0.0000 REMARK 3 64 3.2130 - 3.1960 0.93 439 0 0.1840 0.0000 REMARK 3 65 3.1960 - 3.1800 0.90 500 0 0.1700 0.0000 REMARK 3 66 3.1800 - 3.1630 0.92 579 0 0.1860 0.0000 REMARK 3 67 3.1630 - 3.1480 0.94 526 0 0.1750 0.0000 REMARK 3 68 3.1480 - 3.1320 0.92 499 0 0.1760 0.0000 REMARK 3 69 3.1320 - 3.1170 0.90 446 0 0.1820 0.0000 REMARK 3 70 3.1170 - 3.1020 0.93 568 0 0.1900 0.0000 REMARK 3 71 3.1020 - 3.0870 0.91 410 0 0.1790 0.0000 REMARK 3 72 3.0870 - 3.0730 0.91 576 0 0.1830 0.0000 REMARK 3 73 3.0730 - 3.0590 0.91 508 0 0.1760 0.0000 REMARK 3 74 3.0590 - 3.0450 0.93 517 0 0.1960 0.0000 REMARK 3 75 3.0450 - 3.0320 0.93 531 0 0.1900 0.0000 REMARK 3 76 3.0320 - 3.0180 0.90 512 0 0.1780 0.0000 REMARK 3 77 3.0180 - 3.0050 0.95 477 0 0.1940 0.0000 REMARK 3 78 3.0050 - 2.9920 0.90 450 0 0.1810 0.0000 REMARK 3 79 2.9920 - 2.9800 0.92 587 0 0.2050 0.0000 REMARK 3 80 2.9800 - 2.9670 0.94 470 0 0.1870 0.0000 REMARK 3 81 2.9670 - 2.9550 0.91 519 0 0.2000 0.0000 REMARK 3 82 2.9550 - 2.9430 0.90 517 0 0.1680 0.0000 REMARK 3 83 2.9430 - 2.9310 0.89 488 0 0.1880 0.0000 REMARK 3 84 2.9310 - 2.9190 0.93 517 0 0.1920 0.0000 REMARK 3 85 2.9190 - 2.9080 0.91 480 0 0.1830 0.0000 REMARK 3 86 2.9080 - 2.8960 0.93 504 0 0.1740 0.0000 REMARK 3 87 2.8960 - 2.8850 0.93 550 0 0.2190 0.0000 REMARK 3 88 2.8850 - 2.8740 0.94 553 0 0.2110 0.0000 REMARK 3 89 2.8740 - 2.8630 0.94 494 0 0.2020 0.0000 REMARK 3 90 2.8630 - 2.8530 0.93 526 0 0.2040 0.0000 REMARK 3 91 2.8530 - 2.8420 0.89 463 0 0.1880 0.0000 REMARK 3 92 2.8420 - 2.8320 0.94 470 0 0.2040 0.0000 REMARK 3 93 2.8320 - 2.8220 0.90 526 0 0.1780 0.0000 REMARK 3 94 2.8220 - 2.8120 0.91 527 0 0.2020 0.0000 REMARK 3 95 2.8120 - 2.8020 0.91 505 0 0.2130 0.0000 REMARK 3 96 2.8020 - 2.7920 0.92 538 0 0.2280 0.0000 REMARK 3 97 2.7920 - 2.7830 0.90 438 0 0.1910 0.0000 REMARK 3 98 2.7830 - 2.7730 0.94 537 0 0.2170 0.0000 REMARK 3 99 2.7730 - 2.7640 0.92 516 0 0.1970 0.0000 REMARK 3 100 2.7640 - 2.7540 0.92 475 0 0.2350 0.0000 REMARK 3 101 2.7540 - 2.7450 0.94 475 0 0.2290 0.0000 REMARK 3 102 2.7450 - 2.7360 0.92 614 0 0.2210 0.0000 REMARK 3 103 2.7360 - 2.7270 0.90 480 0 0.2110 0.0000 REMARK 3 104 2.7270 - 2.7190 0.91 500 0 0.2370 0.0000 REMARK 3 105 2.7190 - 2.7100 0.91 506 0 0.2300 0.0000 REMARK 3 106 2.7100 - 2.7010 0.92 457 0 0.2360 0.0000 REMARK 3 107 2.7010 - 2.6930 0.93 500 0 0.2380 0.0000 REMARK 3 108 2.6930 - 2.6850 0.93 543 0 0.2280 0.0000 REMARK 3 109 2.6850 - 2.6760 0.94 551 0 0.2160 0.0000 REMARK 3 110 2.6760 - 2.6680 0.90 503 0 0.2180 0.0000 REMARK 3 111 2.6680 - 2.6600 0.92 390 0 0.2610 0.0000 REMARK 3 112 2.6600 - 2.6520 0.92 621 0 0.2510 0.0000 REMARK 3 113 2.6520 - 2.6440 0.92 500 0 0.2440 0.0000 REMARK 3 114 2.6440 - 2.6370 0.92 450 0 0.2410 0.0000 REMARK 3 115 2.6370 - 2.6290 0.91 534 0 0.2420 0.0000 REMARK 3 116 2.6290 - 2.6210 0.93 518 0 0.2460 0.0000 REMARK 3 117 2.6210 - 2.6140 0.92 504 0 0.2500 0.0000 REMARK 3 118 2.6140 - 2.6060 0.93 531 0 0.2410 0.0000 REMARK 3 119 2.6060 - 2.5990 0.92 513 0 0.2640 0.0000 REMARK 3 120 2.5990 - 2.5920 0.94 538 0 0.2520 0.0000 REMARK 3 121 2.5920 - 2.5850 0.92 447 0 0.2610 0.0000 REMARK 3 122 2.5850 - 2.5780 0.92 507 0 0.2670 0.0000 REMARK 3 123 2.5780 - 2.5710 0.92 523 0 0.2500 0.0000 REMARK 3 124 2.5710 - 2.5640 0.93 539 0 0.2600 0.0000 REMARK 3 125 2.5640 - 2.5570 0.92 462 0 0.2690 0.0000 REMARK 3 126 2.5570 - 2.5500 0.94 581 0 0.2690 0.0000 REMARK 3 127 2.5500 - 2.5430 0.92 487 0 0.2710 0.0000 REMARK 3 128 2.5430 - 2.5370 0.93 519 0 0.2710 0.0000 REMARK 3 129 2.5370 - 2.5300 0.90 477 0 0.2740 0.0000 REMARK 3 130 2.5300 - 2.5240 0.93 516 0 0.2820 0.0000 REMARK 3 131 2.5240 - 2.5170 0.90 509 0 0.2730 0.0000 REMARK 3 132 2.5170 - 2.5110 0.88 490 0 0.2920 0.0000 REMARK 3 133 2.5110 - 2.5050 0.90 487 0 0.2880 0.0000 REMARK 3 134 2.5050 - 2.4980 0.92 521 0 0.3200 0.0000 REMARK 3 135 2.4980 - 2.4920 0.90 469 0 0.2840 0.0000 REMARK 3 136 2.4920 - 2.4860 0.90 532 0 0.3100 0.0000 REMARK 3 137 2.4860 - 2.4800 0.92 494 0 0.2990 0.0000 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : 0.37 REMARK 3 B_SOL : 80.73 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.79 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.89600 REMARK 3 B22 (A**2) : -1.89600 REMARK 3 B33 (A**2) : 3.79300 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : -0.00000 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 : 0.005 NULL REMARK 3 ANGLE : 0.646 NULL REMARK 3 CHIRALITY : 0.047 NULL REMARK 3 PLANARITY : 0.003 NULL REMARK 3 DIHEDRAL : 10.293 NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 46.9601 -17.2911 -0.5050 REMARK 3 T TENSOR REMARK 3 T11: 0.3749 T22: 0.2108 REMARK 3 T33: 0.5929 T12: -0.0163 REMARK 3 T13: -0.1239 T23: 0.0601 REMARK 3 L TENSOR REMARK 3 L11: 1.3115 L22: 1.5077 REMARK 3 L33: 2.8666 L12: 0.1496 REMARK 3 L13: 0.2240 L23: 0.1354 REMARK 3 S TENSOR REMARK 3 S11: 0.2524 S12: 0.0581 S13: -0.5822 REMARK 3 S21: 0.3049 S22: -0.0961 S23: -0.2574 REMARK 3 S31: 0.6474 S32: 0.1240 S33: -0.1515 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 21.7809 3.3575 -20.2161 REMARK 3 T TENSOR REMARK 3 T11: 0.2758 T22: 0.3630 REMARK 3 T33: 0.3137 T12: -0.0089 REMARK 3 T13: -0.0076 T23: -0.0408 REMARK 3 L TENSOR REMARK 3 L11: 2.5213 L22: 1.3274 REMARK 3 L33: 1.0365 L12: -0.5501 REMARK 3 L13: -0.3321 L23: 0.2800 REMARK 3 S TENSOR REMARK 3 S11: 0.0568 S12: 0.0801 S13: 0.1997 REMARK 3 S21: 0.0196 S22: 0.0315 S23: -0.3054 REMARK 3 S31: -0.0459 S32: 0.0420 S33: -0.0915 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 3BLH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-07. REMARK 100 THE RCSB ID CODE IS RCSB045666. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-JUN-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9756 REMARK 200 MONOCHROMATOR : SI(311) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37491 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480 REMARK 200 RESOLUTION RANGE LOW (A) : 86.460 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.06300 REMARK 200 R SYM (I) : 0.06300 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.61 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 REMARK 200 R MERGE FOR SHELL (I) : 0.47200 REMARK 200 R SYM FOR SHELL (I) : 0.47200 REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 1QMZ FOR CHAIN A, PDB ENTRY 2PK2 FOR REMARK 200 CHAIN B REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 20% PEG 1000, 0.5M NACL, REMARK 280 4MM TCEP, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 86.46000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.91770 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.92000 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 86.46000 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 49.91770 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 31.92000 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 86.46000 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 49.91770 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.92000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 99.83541 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 63.84000 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 99.83541 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 63.84000 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 99.83541 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.84000 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27190 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 GLY A 0 REMARK 465 PRO A 1 REMARK 465 ALA A 2 REMARK 465 LYS A 3 REMARK 465 GLN A 4 REMARK 465 TYR A 5 REMARK 465 ASP A 6 REMARK 465 SER A 7 REMARK 465 LEU A 51 REMARK 465 MET A 52 REMARK 465 GLU A 53 REMARK 465 ASN A 54 REMARK 465 LYS A 88 REMARK 465 ALA A 89 REMARK 465 SER A 90 REMARK 465 PRO A 91 REMARK 465 TYR A 92 REMARK 465 ASN A 93 REMARK 465 ARG A 94 REMARK 465 CYS A 95 REMARK 465 LYS A 96 REMARK 465 GLY A 97 REMARK 465 ALA A 177 REMARK 465 LYS A 178 REMARK 465 ASN A 179 REMARK 465 SER A 180 REMARK 465 GLN A 181 REMARK 465 GLU A 260 REMARK 465 LEU A 261 REMARK 465 TYR A 262 REMARK 465 GLU A 263 REMARK 465 LYS A 264 REMARK 465 LEU A 265 REMARK 465 GLU A 266 REMARK 465 GLY A 326 REMARK 465 MET A 327 REMARK 465 LEU A 328 REMARK 465 SER A 329 REMARK 465 THR A 330 REMARK 465 GLY B 0 REMARK 465 PRO B 1 REMARK 465 GLU B 2 REMARK 465 GLY B 3 REMARK 465 GLU B 4 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 CYS A 10 58.99 -154.08 REMARK 500 ASP A 149 39.81 -142.29 REMARK 500 ASP A 167 77.18 63.01 REMARK 500 SER A 175 -155.89 -158.69 REMARK 500 ARG A 184 69.25 -119.76 REMARK 500 VAL A 190 131.77 82.17 REMARK 500 ASP A 205 65.63 -112.81 REMARK 500 SER A 226 141.31 -171.78 REMARK 500 GLN A 230 67.22 -106.05 REMARK 500 ASN A 255 -0.59 86.23 REMARK 500 ASN A 258 48.59 -156.31 REMARK 500 LYS A 269 -23.85 -141.17 REMARK 500 ARG A 284 -53.37 75.04 REMARK 500 LEU A 296 49.16 -85.19 REMARK 500 ASN B 7 -141.99 -97.81 REMARK 500 THR B 121 4.92 -60.86 REMARK 500 PHE B 146 15.72 59.14 REMARK 500 ASN B 250 -7.60 76.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 260 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3BLQ RELATED DB: PDB REMARK 900 RELATED ID: 3BLR RELATED DB: PDB DBREF 3BLH A 2 330 UNP P50750 CDK9_HUMAN 2 330 DBREF 3BLH B 2 259 UNP O60563 CCNT1_HUMAN 2 259 SEQADV 3BLH GLY A 0 UNP P50750 EXPRESSION TAG SEQADV 3BLH PRO A 1 UNP P50750 EXPRESSION TAG SEQADV 3BLH GLY B 0 UNP O60563 EXPRESSION TAG SEQADV 3BLH PRO B 1 UNP O60563 EXPRESSION TAG SEQADV 3BLH ARG B 77 UNP O60563 GLN 77 ENGINEERED SEQADV 3BLH GLY B 96 UNP O60563 GLU 96 ENGINEERED SEQADV 3BLH LEU B 241 UNP O60563 PHE 241 ENGINEERED SEQRES 1 A 331 GLY PRO ALA LYS GLN TYR ASP SER VAL GLU CYS PRO PHE SEQRES 2 A 331 CYS ASP GLU VAL SER LYS TYR GLU LYS LEU ALA LYS ILE SEQRES 3 A 331 GLY GLN GLY THR PHE GLY GLU VAL PHE LYS ALA ARG HIS SEQRES 4 A 331 ARG LYS THR GLY GLN LYS VAL ALA LEU LYS LYS VAL LEU SEQRES 5 A 331 MET GLU ASN GLU LYS GLU GLY PHE PRO ILE THR ALA LEU SEQRES 6 A 331 ARG GLU ILE LYS ILE LEU GLN LEU LEU LYS HIS GLU ASN SEQRES 7 A 331 VAL VAL ASN LEU ILE GLU ILE CYS ARG THR LYS ALA SER SEQRES 8 A 331 PRO TYR ASN ARG CYS LYS GLY SER ILE TYR LEU VAL PHE SEQRES 9 A 331 ASP PHE CYS GLU HIS ASP LEU ALA GLY LEU LEU SER ASN SEQRES 10 A 331 VAL LEU VAL LYS PHE THR LEU SER GLU ILE LYS ARG VAL SEQRES 11 A 331 MET GLN MET LEU LEU ASN GLY LEU TYR TYR ILE HIS ARG SEQRES 12 A 331 ASN LYS ILE LEU HIS ARG ASP MET LYS ALA ALA ASN VAL SEQRES 13 A 331 LEU ILE THR ARG ASP GLY VAL LEU LYS LEU ALA ASP PHE SEQRES 14 A 331 GLY LEU ALA ARG ALA PHE SER LEU ALA LYS ASN SER GLN SEQRES 15 A 331 PRO ASN ARG TYR TPO ASN ARG VAL VAL THR LEU TRP TYR SEQRES 16 A 331 ARG PRO PRO GLU LEU LEU LEU GLY GLU ARG ASP TYR GLY SEQRES 17 A 331 PRO PRO ILE ASP LEU TRP GLY ALA GLY CYS ILE MET ALA SEQRES 18 A 331 GLU MET TRP THR ARG SER PRO ILE MET GLN GLY ASN THR SEQRES 19 A 331 GLU GLN HIS GLN LEU ALA LEU ILE SER GLN LEU CYS GLY SEQRES 20 A 331 SER ILE THR PRO GLU VAL TRP PRO ASN VAL ASP ASN TYR SEQRES 21 A 331 GLU LEU TYR GLU LYS LEU GLU LEU VAL LYS GLY GLN LYS SEQRES 22 A 331 ARG LYS VAL LYS ASP ARG LEU LYS ALA TYR VAL ARG ASP SEQRES 23 A 331 PRO TYR ALA LEU ASP LEU ILE ASP LYS LEU LEU VAL LEU SEQRES 24 A 331 ASP PRO ALA GLN ARG ILE ASP SER ASP ASP ALA LEU ASN SEQRES 25 A 331 HIS ASP PHE PHE TRP SER ASP PRO MET PRO SER ASP LEU SEQRES 26 A 331 LYS GLY MET LEU SER THR SEQRES 1 B 260 GLY PRO GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP SEQRES 2 B 260 TYR PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG SEQRES 3 B 260 ARG PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG SEQRES 4 B 260 GLN GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG SEQRES 5 B 260 LEU ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL SEQRES 6 B 260 TYR MET HIS ARG PHE TYR MET ILE GLN SER PHE THR ARG SEQRES 7 B 260 PHE PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU SEQRES 8 B 260 ALA ALA LYS VAL GLU GLY GLN PRO LYS LYS LEU GLU HIS SEQRES 9 B 260 VAL ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU SEQRES 10 B 260 SER LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN SEQRES 11 B 260 VAL GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN SEQRES 12 B 260 THR LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR SEQRES 13 B 260 HIS VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS SEQRES 14 B 260 ASP LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER SEQRES 15 B 260 LEU HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO SEQRES 16 B 260 VAL VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP SEQRES 17 B 260 SER ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS SEQRES 18 B 260 TRP TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU SEQRES 19 B 260 LEU ASP GLU LEU THR HIS GLU LEU LEU GLN ILE LEU GLU SEQRES 20 B 260 LYS THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG MODRES 3BLH TPO A 186 THR PHOSPHOTHREONINE HET TPO A 186 11 HET TRS B 260 8 HETNAM TPO PHOSPHOTHREONINE HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETSYN TPO PHOSPHONOTHREONINE HETSYN TRS TRIS BUFFER FORMUL 1 TPO C4 H10 N O6 P FORMUL 3 TRS C4 H12 N O3 1+ FORMUL 4 HOH *139(H2 O) HELIX 1 1 GLU A 15 SER A 17 5 3 HELIX 2 2 PRO A 60 LEU A 73 1 14 HELIX 3 3 LEU A 110 SER A 115 1 6 HELIX 4 4 THR A 122 ASN A 143 1 22 HELIX 5 5 LYS A 151 ALA A 153 5 3 HELIX 6 6 THR A 191 ARG A 195 5 5 HELIX 7 7 PRO A 196 LEU A 201 1 6 HELIX 8 8 PRO A 208 ARG A 225 1 18 HELIX 9 9 THR A 233 GLY A 246 1 14 HELIX 10 10 LYS A 274 ARG A 284 1 11 HELIX 11 11 ASP A 285 LEU A 296 1 12 HELIX 12 12 ASP A 305 HIS A 312 1 8 HELIX 13 13 ASP A 313 TRP A 316 5 4 HELIX 14 14 THR B 15 ASN B 21 1 7 HELIX 15 15 SER B 22 PHE B 27 1 6 HELIX 16 16 ASP B 30 ASN B 53 1 24 HELIX 17 17 SER B 55 GLN B 73 1 19 HELIX 18 18 PRO B 79 GLU B 95 1 17 HELIX 19 19 LYS B 100 HIS B 113 1 14 HELIX 20 20 SER B 123 LEU B 144 1 22 HELIX 21 21 HIS B 152 LEU B 163 1 12 HELIX 22 22 SER B 167 THR B 185 1 19 HELIX 23 23 THR B 186 GLN B 190 5 5 HELIX 24 24 THR B 192 ASN B 209 1 18 HELIX 25 25 HIS B 220 VAL B 225 5 6 HELIX 26 26 THR B 230 LYS B 247 1 18 HELIX 27 27 ARG B 251 TRP B 256 5 6 SHEET 1 A 5 TYR A 19 GLN A 27 0 SHEET 2 A 5 GLU A 32 HIS A 38 -1 O LYS A 35 N ALA A 23 SHEET 3 A 5 LYS A 44 LYS A 49 -1 O LEU A 47 N PHE A 34 SHEET 4 A 5 TYR A 100 ASP A 104 -1 O PHE A 103 N ALA A 46 SHEET 5 A 5 LEU A 81 CYS A 85 -1 N ILE A 82 O VAL A 102 SHEET 1 B 3 HIS A 108 ASP A 109 0 SHEET 2 B 3 VAL A 155 ILE A 157 -1 O ILE A 157 N HIS A 108 SHEET 3 B 3 LEU A 163 LEU A 165 -1 O LYS A 164 N LEU A 156 SHEET 1 C 2 ILE A 145 LEU A 146 0 SHEET 2 C 2 ARG A 172 ALA A 173 -1 O ARG A 172 N LEU A 146 LINK C TYR A 185 N TPO A 186 1555 1555 1.33 LINK C TPO A 186 N ASN A 187 1555 1555 1.33 CISPEP 1 ASP A 318 PRO A 319 0 -3.08 CISPEP 2 ASN B 7 ASN B 8 0 11.49 SITE 1 AC1 9 GLN B 46 GLN B 56 PHE B 176 THR B 179 SITE 2 AC1 9 ASN B 180 HIS B 183 ARG B 254 HOH B 339 SITE 3 AC1 9 HOH B 341 CRYST1 172.920 172.920 95.760 90.00 90.00 120.00 H 3 9 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 0.005783 0.003339 0.000000 0.00000 SCALE2 0.000000 0.006678 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010443 0.00000 ATOM 1 N VAL A 8 38.365 -4.357 -38.054 1.00115.79 N ANISOU 1 N VAL A 8 14119 17287 12589 1000 -36 -1013 N ATOM 2 CA VAL A 8 37.673 -3.858 -36.866 1.00115.57 C ANISOU 2 CA VAL A 8 14029 17153 12730 1001 -102 -876 C ATOM 3 C VAL A 8 38.654 -3.207 -35.889 1.00108.34 C ANISOU 3 C VAL A 8 13115 16091 11958 978 36 -748 C ATOM 4 O VAL A 8 39.592 -3.854 -35.418 1.00107.78 O ANISOU 4 O VAL A 8 12994 15926 12033 932 120 -832 O ATOM 5 CB VAL A 8 36.842 -4.981 -36.179 1.00 71.68 C ANISOU 5 CB VAL A 8 8350 11529 7357 954 -233 -1002 C ATOM 6 CG1 VAL A 8 36.690 -4.735 -34.688 1.00 60.19 C ANISOU 6 CG1 VAL A 8 6819 9916 6135 929 -230 -895 C ATOM 7 CG2 VAL A 8 35.481 -5.104 -36.843 1.00 75.83 C ANISOU 7 CG2 VAL A 8 8857 12207 7749 976 -403 -1038 C ATOM 8 N GLU A 9 38.433 -1.925 -35.599 1.00101.15 N ANISOU 8 N GLU A 9 12269 15162 11001 1014 52 -549 N ATOM 9 CA GLU A 9 39.327 -1.154 -34.734 1.00 98.88 C ANISOU 9 CA GLU A 9 12007 14743 10821 980 175 -416 C ATOM 10 C GLU A 9 39.383 -1.675 -33.298 1.00 89.71 C ANISOU 10 C GLU A 9 10734 13417 9934 934 161 -439 C ATOM 11 O GLU A 9 38.397 -2.191 -32.773 1.00 91.86 O ANISOU 11 O GLU A 9 10928 13666 10307 941 43 -481 O ATOM 12 CB GLU A 9 38.931 0.320 -34.732 1.00109.84 C ANISOU 12 CB GLU A 9 13515 16126 12095 1033 175 -204 C ATOM 13 CG GLU A 9 39.405 1.094 -35.944 1.00124.01 C ANISOU 13 CG GLU A 9 15458 18029 13631 1047 251 -128 C ATOM 14 CD GLU A 9 39.238 2.586 -35.757 1.00138.02 C ANISOU 14 CD GLU A 9 17377 19739 15324 1087 271 95 C ATOM 15 OE1 GLU A 9 39.154 3.022 -34.588 1.00140.54 O ANISOU 15 OE1 GLU A 9 17679 19910 15811 1081 272 179 O ATOM 16 OE2 GLU A 9 39.189 3.319 -36.771 1.00144.03 O ANISOU 16 OE2 GLU A 9 18284 20591 15849 1124 283 186 O ATOM 17 N CYS A 10 40.539 -1.529 -32.659 1.00 80.19 N ANISOU 17 N CYS A 10 9519 12109 8841 878 281 -407 N ATOM 18 CA CYS A 10 40.726 -2.086 -31.325 1.00 75.50 C ANISOU 18 CA CYS A 10 8829 11364 8495 832 269 -433 C ATOM 19 C CYS A 10 41.778 -1.370 -30.469 1.00 74.72 C ANISOU 19 C CYS A 10 8745 11154 8492 779 381 -319 C ATOM 20 O CYS A 10 42.726 -1.987 -29.995 1.00 78.98 O ANISOU 20 O CYS A 10 9212 11632 9164 734 437 -388 O ATOM 21 CB CYS A 10 41.058 -3.569 -31.423 1.00 66.58 C ANISOU 21 CB CYS A 10 7611 10223 7465 811 249 -632 C ATOM 22 SG CYS A 10 40.824 -4.391 -29.866 1.00 83.94 S ANISOU 22 SG CYS A 10 9710 12241 9942 764 180 -662 S ATOM 23 N PRO A 11 41.571 -0.070 -30.235 1.00 71.68 N ANISOU 23 N PRO A 11 8457 10737 8040 788 401 -146 N ATOM 24 CA PRO A 11 42.486 0.855 -29.557 1.00 62.50 C ANISOU 24 CA PRO A 11 7347 9477 6924 724 503 -19 C ATOM 25 C PRO A 11 42.965 0.388 -28.191 1.00 62.86 C ANISOU 25 C PRO A 11 7299 9385 7201 666 504 -40 C ATOM 26 O PRO A 11 44.059 0.757 -27.775 1.00 70.13 O ANISOU 26 O PRO A 11 8218 10256 8172 592 596 6 O ATOM 27 CB PRO A 11 41.622 2.107 -29.356 1.00 67.75 C ANISOU 27 CB PRO A 11 8136 10098 7507 775 463 145 C ATOM 28 CG PRO A 11 40.563 2.021 -30.389 1.00 69.50 C ANISOU 28 CG PRO A 11 8388 10451 7569 871 374 118 C ATOM 29 CD PRO A 11 40.293 0.574 -30.595 1.00 70.23 C ANISOU 29 CD PRO A 11 8344 10607 7733 871 308 -66 C ATOM 30 N PHE A 12 42.145 -0.384 -27.490 1.00 61.40 N ANISOU 30 N PHE A 12 7037 9145 7147 690 402 -103 N ATOM 31 CA PHE A 12 42.365 -0.607 -26.065 1.00 55.29 C ANISOU 31 CA PHE A 12 6208 8229 6571 640 388 -83 C ATOM 32 C PHE A 12 42.671 -2.060 -25.769 1.00 53.85 C ANISOU 32 C PHE A 12 5910 8015 6536 621 352 -233 C ATOM 33 O PHE A 12 42.691 -2.485 -24.613 1.00 51.23 O ANISOU 33 O PHE A 12 5530 7568 6368 586 316 -232 O ATOM 34 CB PHE A 12 41.151 -0.140 -25.250 1.00 58.58 C ANISOU 34 CB PHE A 12 6651 8583 7023 675 309 0 C ATOM 35 CG PHE A 12 40.795 1.295 -25.474 1.00 62.39 C ANISOU 35 CG PHE A 12 7265 9071 7368 720 335 147 C ATOM 36 CD1 PHE A 12 41.770 2.280 -25.410 1.00 69.97 C ANISOU 36 CD1 PHE A 12 8324 9978 8284 667 433 249 C ATOM 37 CD2 PHE A 12 39.498 1.665 -25.753 1.00 64.29 C ANISOU 37 CD2 PHE A 12 7536 9370 7523 815 257 184 C ATOM 38 CE1 PHE A 12 41.452 3.612 -25.613 1.00 71.51 C ANISOU 38 CE1 PHE A 12 8672 10149 8351 706 453 388 C ATOM 39 CE2 PHE A 12 39.173 2.996 -25.958 1.00 71.60 C ANISOU 39 CE2 PHE A 12 8600 10284 8322 880 274 322 C ATOM 40 CZ PHE A 12 40.150 3.970 -25.887 1.00 70.18 C ANISOU 40 CZ PHE A 12 8545 10022 8098 825 372 425 C ATOM 41 N CYS A 13 42.903 -2.826 -26.824 1.00 53.55 N ANISOU 41 N CYS A 13 5843 8073 6431 647 360 -362 N ATOM 42 CA CYS A 13 43.351 -4.189 -26.651 1.00 59.28 C ANISOU 42 CA CYS A 13 6483 8755 7287 642 336 -512 C ATOM 43 C CYS A 13 44.513 -4.422 -27.599 1.00 61.56 C ANISOU 43 C CYS A 13 6752 9136 7501 660 437 -597 C ATOM 44 O CYS A 13 44.310 -4.560 -28.805 1.00 63.29 O ANISOU 44 O CYS A 13 7003 9478 7566 698 448 -671 O ATOM 45 CB CYS A 13 42.210 -5.149 -26.950 1.00 62.45 C ANISOU 45 CB CYS A 13 6867 9170 7691 664 220 -622 C ATOM 46 SG CYS A 13 42.517 -6.822 -26.424 1.00 60.87 S ANISOU 46 SG CYS A 13 6599 8848 7681 647 162 -784 S ATOM 47 N ASP A 14 45.731 -4.441 -27.059 1.00 57.62 N ANISOU 47 N ASP A 14 6196 8594 7103 632 511 -588 N ATOM 48 CA ASP A 14 46.935 -4.608 -27.884 1.00 56.52 C ANISOU 48 CA ASP A 14 6011 8564 6900 649 625 -665 C ATOM 49 C ASP A 14 47.162 -6.069 -28.253 1.00 53.38 C ANISOU 49 C ASP A 14 5552 8163 6567 719 596 -864 C ATOM 50 O ASP A 14 46.776 -6.978 -27.505 1.00 54.86 O ANISOU 50 O ASP A 14 5717 8219 6908 732 496 -923 O ATOM 51 CB ASP A 14 48.173 -4.061 -27.162 1.00 60.34 C ANISOU 51 CB ASP A 14 6433 9025 7469 591 712 -582 C ATOM 52 CG ASP A 14 48.230 -2.542 -27.149 1.00 74.14 C ANISOU 52 CG ASP A 14 8265 10800 9106 513 778 -404 C ATOM 53 OD1 ASP A 14 47.494 -1.888 -27.931 1.00 78.47 O ANISOU 53 OD1 ASP A 14 8920 11411 9484 523 779 -349 O ATOM 54 OD2 ASP A 14 49.027 -2.004 -26.348 1.00 79.61 O ANISOU 54 OD2 ASP A 14 8924 11446 9879 440 821 -318 O ATOM 55 N GLU A 15 47.785 -6.293 -29.405 1.00 62.03 N ANISOU 55 N GLU A 15 6634 9397 7538 763 685 -968 N ATOM 56 CA GLU A 15 48.183 -7.644 -29.800 1.00 66.86 C ANISOU 56 CA GLU A 15 7196 10003 8204 846 677 -1171 C ATOM 57 C GLU A 15 49.356 -8.140 -28.958 1.00 60.94 C ANISOU 57 C GLU A 15 6332 9181 7640 874 710 -1201 C ATOM 58 O GLU A 15 50.310 -7.396 -28.710 1.00 57.50 O ANISOU 58 O GLU A 15 5829 8809 7210 835 809 -1110 O ATOM 59 CB GLU A 15 48.545 -7.684 -31.279 1.00 69.37 C ANISOU 59 CB GLU A 15 7535 10506 8318 893 777 -1277 C ATOM 60 CG GLU A 15 47.522 -7.020 -32.174 1.00 82.84 C ANISOU 60 CG GLU A 15 9354 12310 9811 868 750 -1224 C ATOM 61 CD GLU A 15 47.873 -7.148 -33.644 1.00103.19 C ANISOU 61 CD GLU A 15 11964 15071 12171 913 844 -1338 C ATOM 62 OE1 GLU A 15 48.456 -8.188 -34.037 1.00107.36 O ANISOU 62 OE1 GLU A 15 12447 15618 12727 988 877 -1525 O ATOM 63 OE2 GLU A 15 47.560 -6.209 -34.408 1.00112.30 O ANISOU 63 OE2 GLU A 15 13201 16348 13120 880 883 -1242 O ATOM 64 N VAL A 16 49.277 -9.399 -28.532 1.00 56.98 N ANISOU 64 N VAL A 16 5815 8548 7288 937 622 -1327 N ATOM 65 CA VAL A 16 50.275 -10.001 -27.644 1.00 57.10 C ANISOU 65 CA VAL A 16 5731 8470 7494 986 620 -1357 C ATOM 66 C VAL A 16 51.672 -10.074 -28.303 1.00 54.43 C ANISOU 66 C VAL A 16 5279 8286 7115 1064 762 -1444 C ATOM 67 O VAL A 16 52.691 -10.265 -27.633 1.00 56.59 O ANISOU 67 O VAL A 16 5438 8541 7523 1101 786 -1440 O ATOM 68 CB VAL A 16 49.810 -11.405 -27.154 1.00 54.27 C ANISOU 68 CB VAL A 16 5413 7920 7286 1044 487 -1477 C ATOM 69 CG1 VAL A 16 50.026 -12.443 -28.227 1.00 51.28 C ANISOU 69 CG1 VAL A 16 5056 7579 6850 1158 508 -1695 C ATOM 70 CG2 VAL A 16 50.531 -11.819 -25.887 1.00 52.71 C ANISOU 70 CG2 VAL A 16 5145 7585 7297 1069 442 -1439 C ATOM 71 N SER A 17 51.714 -9.897 -29.618 1.00 52.35 N ANISOU 71 N SER A 17 5042 8191 6658 1088 858 -1521 N ATOM 72 CA SER A 17 52.978 -9.841 -30.360 1.00 59.79 C ANISOU 72 CA SER A 17 5873 9320 7526 1148 1017 -1598 C ATOM 73 C SER A 17 53.934 -8.765 -29.838 1.00 62.89 C ANISOU 73 C SER A 17 6151 9804 7940 1058 1116 -1440 C ATOM 74 O SER A 17 55.116 -8.808 -30.132 1.00 74.13 O ANISOU 74 O SER A 17 7437 11371 9359 1102 1237 -1496 O ATOM 75 CB SER A 17 52.713 -9.594 -31.849 1.00 64.98 C ANISOU 75 CB SER A 17 6603 10154 7931 1153 1108 -1668 C ATOM 76 OG SER A 17 52.241 -8.267 -32.087 1.00 71.17 O ANISOU 76 OG SER A 17 7460 11017 8564 1025 1142 -1489 O ATOM 77 N LYS A 18 53.425 -7.797 -29.083 1.00 55.14 N ANISOU 77 N LYS A 18 5225 8748 6977 931 1066 -1250 N ATOM 78 CA LYS A 18 54.281 -6.781 -28.474 1.00 58.00 C ANISOU 78 CA LYS A 18 5500 9167 7371 824 1140 -1100 C ATOM 79 C LYS A 18 55.273 -7.431 -27.503 1.00 67.73 C ANISOU 79 C LYS A 18 6573 10347 8813 883 1111 -1141 C ATOM 80 O LYS A 18 56.356 -6.891 -27.216 1.00 61.61 O ANISOU 80 O LYS A 18 5664 9678 8066 827 1195 -1081 O ATOM 81 CB LYS A 18 53.438 -5.732 -27.728 1.00 46.88 C ANISOU 81 CB LYS A 18 4207 7646 5958 695 1070 -906 C ATOM 82 CG LYS A 18 52.725 -6.271 -26.501 1.00 54.66 C ANISOU 82 CG LYS A 18 5229 8416 7124 711 909 -884 C ATOM 83 CD LYS A 18 51.678 -5.289 -25.962 1.00 60.00 C ANISOU 83 CD LYS A 18 6036 8998 7762 611 847 -719 C ATOM 84 CE LYS A 18 52.321 -4.061 -25.340 1.00 54.76 C ANISOU 84 CE LYS A 18 5358 8350 7098 487 906 -556 C ATOM 85 NZ LYS A 18 51.301 -3.213 -24.662 1.00 58.05 N ANISOU 85 NZ LYS A 18 5909 8645 7501 417 835 -412 N ATOM 86 N TYR A 19 54.864 -8.585 -26.981 1.00 66.69 N ANISOU 86 N TYR A 19 6465 10048 8826 988 983 -1238 N ATOM 87 CA TYR A 19 55.681 -9.383 -26.087 1.00 58.72 C ANISOU 87 CA TYR A 19 5332 8962 8016 1077 928 -1288 C ATOM 88 C TYR A 19 56.268 -10.525 -26.892 1.00 62.90 C ANISOU 88 C TYR A 19 5793 9556 8551 1257 975 -1501 C ATOM 89 O TYR A 19 55.650 -11.024 -27.828 1.00 69.74 O ANISOU 89 O TYR A 19 6760 10427 9313 1315 981 -1621 O ATOM 90 CB TYR A 19 54.849 -9.909 -24.913 1.00 61.73 C ANISOU 90 CB TYR A 19 5808 9095 8552 1071 753 -1241 C ATOM 91 CG TYR A 19 54.247 -8.805 -24.076 1.00 62.50 C ANISOU 91 CG TYR A 19 5977 9128 8643 910 711 -1044 C ATOM 92 CD1 TYR A 19 55.021 -8.107 -23.156 1.00 64.91 C ANISOU 92 CD1 TYR A 19 6194 9449 9021 829 721 -921 C ATOM 93 CD2 TYR A 19 52.912 -8.440 -24.222 1.00 60.76 C ANISOU 93 CD2 TYR A 19 5910 8840 8337 843 662 -986 C ATOM 94 CE1 TYR A 19 54.483 -7.081 -22.397 1.00 59.18 C ANISOU 94 CE1 TYR A 19 5551 8654 8279 688 687 -752 C ATOM 95 CE2 TYR A 19 52.358 -7.408 -23.470 1.00 54.59 C ANISOU 95 CE2 TYR A 19 5196 8001 7544 718 631 -815 C ATOM 96 CZ TYR A 19 53.149 -6.734 -22.557 1.00 63.27 C ANISOU 96 CZ TYR A 19 6228 9099 8714 642 647 -701 C ATOM 97 OH TYR A 19 52.612 -5.709 -21.796 1.00 61.84 O ANISOU 97 OH TYR A 19 6132 8848 8516 524 618 -543 O ATOM 98 N GLU A 20 57.482 -10.920 -26.547 1.00 70.95 N ANISOU 98 N GLU A 20 6638 10636 9683 1351 1008 -1553 N ATOM 99 CA GLU A 20 58.135 -11.993 -27.257 1.00 69.65 C ANISOU 99 CA GLU A 20 6397 10535 9532 1549 1059 -1762 C ATOM 100 C GLU A 20 58.182 -13.219 -26.359 1.00 65.13 C ANISOU 100 C GLU A 20 5836 9741 9170 1694 907 -1835 C ATOM 101 O GLU A 20 58.767 -13.189 -25.278 1.00 62.60 O ANISOU 101 O GLU A 20 5415 9370 9000 1696 843 -1751 O ATOM 102 CB GLU A 20 59.527 -11.547 -27.657 1.00 79.76 C ANISOU 102 CB GLU A 20 7453 12081 10771 1570 1225 -1780 C ATOM 103 CG GLU A 20 60.271 -12.510 -28.543 1.00 96.78 C ANISOU 103 CG GLU A 20 9511 14356 12906 1783 1317 -2004 C ATOM 104 CD GLU A 20 61.737 -12.141 -28.641 1.00113.93 C ANISOU 104 CD GLU A 20 11413 16790 15085 1811 1462 -2010 C ATOM 105 OE1 GLU A 20 62.107 -11.046 -28.148 1.00113.97 O ANISOU 105 OE1 GLU A 20 11328 16891 15083 1630 1499 -1835 O ATOM 106 OE2 GLU A 20 62.512 -12.944 -29.202 1.00119.96 O ANISOU 106 OE2 GLU A 20 12054 17666 15859 2011 1540 -2193 O ATOM 107 N LYS A 21 57.532 -14.292 -26.792 1.00 62.35 N ANISOU 107 N LYS A 21 5623 9247 8822 1805 840 -1987 N ATOM 108 CA LYS A 21 57.463 -15.502 -25.977 1.00 70.81 C ANISOU 108 CA LYS A 21 6751 10071 10083 1933 687 -2052 C ATOM 109 C LYS A 21 58.836 -16.148 -25.805 1.00 78.68 C ANISOU 109 C LYS A 21 7568 11129 11199 2139 718 -2153 C ATOM 110 O LYS A 21 59.482 -16.522 -26.783 1.00 84.88 O ANISOU 110 O LYS A 21 8275 12063 11914 2285 835 -2320 O ATOM 111 CB LYS A 21 56.485 -16.506 -26.591 1.00 67.62 C ANISOU 111 CB LYS A 21 6547 9503 9641 1991 616 -2206 C ATOM 112 CG LYS A 21 55.047 -16.291 -26.202 1.00 57.97 C ANISOU 112 CG LYS A 21 5502 8123 8400 1817 502 -2099 C ATOM 113 CD LYS A 21 54.132 -17.025 -27.154 1.00 63.07 C ANISOU 113 CD LYS A 21 6315 8700 8948 1838 470 -2258 C ATOM 114 CE LYS A 21 52.668 -16.705 -26.861 1.00 70.46 C ANISOU 114 CE LYS A 21 7394 9531 9847 1654 368 -2150 C ATOM 115 NZ LYS A 21 51.782 -16.928 -28.050 1.00 73.41 N ANISOU 115 NZ LYS A 21 7889 9950 10054 1627 374 -2274 N ATOM 116 N LEU A 22 59.276 -16.284 -24.560 1.00 77.96 N ANISOU 116 N LEU A 22 7409 10931 11282 2159 612 -2055 N ATOM 117 CA LEU A 22 60.575 -16.887 -24.278 1.00 83.37 C ANISOU 117 CA LEU A 22 7910 11674 12094 2367 617 -2135 C ATOM 118 C LEU A 22 60.494 -18.370 -23.916 1.00 91.57 C ANISOU 118 C LEU A 22 9065 12447 13281 2578 475 -2262 C ATOM 119 O LEU A 22 61.284 -19.174 -24.405 1.00100.69 O ANISOU 119 O LEU A 22 10140 13646 14472 2814 517 -2436 O ATOM 120 CB LEU A 22 61.278 -16.133 -23.153 1.00 82.46 C ANISOU 120 CB LEU A 22 7627 11630 12073 2277 582 -1955 C ATOM 121 CG LEU A 22 61.674 -14.699 -23.464 1.00 81.60 C ANISOU 121 CG LEU A 22 7375 11794 11837 2087 730 -1840 C ATOM 122 CD1 LEU A 22 62.369 -14.080 -22.267 1.00 82.18 C ANISOU 122 CD1 LEU A 22 7300 11909 12017 1998 669 -1677 C ATOM 123 CD2 LEU A 22 62.567 -14.686 -24.679 1.00 83.29 C ANISOU 123 CD2 LEU A 22 7417 12285 11945 2194 918 -1986 C ATOM 124 N ALA A 23 59.541 -18.730 -23.059 1.00 93.20 N ANISOU 124 N ALA A 23 9467 12377 13569 2493 311 -2174 N ATOM 125 CA ALA A 23 59.498 -20.074 -22.493 1.00 89.95 C ANISOU 125 CA ALA A 23 9182 11684 13312 2663 157 -2252 C ATOM 126 C ALA A 23 58.184 -20.371 -21.770 1.00 96.69 C ANISOU 126 C ALA A 23 10281 12251 14205 2507 4 -2155 C ATOM 127 O ALA A 23 57.735 -19.574 -20.946 1.00 99.47 O ANISOU 127 O ALA A 23 10638 12595 14560 2312 -38 -1964 O ATOM 128 CB ALA A 23 60.670 -20.255 -21.533 1.00 80.63 C ANISOU 128 CB ALA A 23 7828 10520 12289 2806 94 -2196 C ATOM 129 N LYS A 24 57.576 -21.519 -22.070 1.00 98.45 N ANISOU 129 N LYS A 24 10709 12242 14455 2587 -75 -2290 N ATOM 130 CA LYS A 24 56.436 -22.001 -21.293 1.00 95.64 C ANISOU 130 CA LYS A 24 10580 11600 14160 2452 -230 -2207 C ATOM 131 C LYS A 24 56.870 -22.193 -19.852 1.00 94.42 C ANISOU 131 C LYS A 24 10407 11303 14166 2479 -360 -2059 C ATOM 132 O LYS A 24 57.993 -22.609 -19.592 1.00 97.58 O ANISOU 132 O LYS A 24 10694 11716 14665 2688 -378 -2100 O ATOM 133 CB LYS A 24 55.917 -23.338 -21.825 1.00 99.58 C ANISOU 133 CB LYS A 24 11299 11857 14679 2551 -301 -2393 C ATOM 134 CG LYS A 24 55.051 -23.249 -23.070 1.00109.15 C ANISOU 134 CG LYS A 24 12604 13143 15725 2458 -225 -2518 C ATOM 135 CD LYS A 24 54.505 -24.626 -23.453 1.00116.78 C ANISOU 135 CD LYS A 24 13813 13836 16723 2530 -320 -2697 C ATOM 136 CE LYS A 24 54.158 -24.711 -24.941 1.00117.14 C ANISOU 136 CE LYS A 24 13907 14001 16599 2542 -223 -2896 C ATOM 137 NZ LYS A 24 53.607 -26.044 -25.335 1.00113.63 N ANISOU 137 NZ LYS A 24 13715 13283 16177 2595 -321 -3082 N ATOM 138 N ILE A 25 55.981 -21.883 -18.918 1.00 95.62 N ANISOU 138 N ILE A 25 10665 11330 14335 2272 -450 -1887 N ATOM 139 CA ILE A 25 56.249 -22.126 -17.508 1.00 99.21 C ANISOU 139 CA ILE A 25 11144 11626 14924 2277 -586 -1740 C ATOM 140 C ILE A 25 55.007 -22.699 -16.841 1.00109.45 C ANISOU 140 C ILE A 25 12688 12646 16252 2121 -713 -1668 C ATOM 141 O ILE A 25 54.803 -22.539 -15.635 1.00104.23 O ANISOU 141 O ILE A 25 12069 11886 15649 2017 -806 -1497 O ATOM 142 CB ILE A 25 56.725 -20.854 -16.778 1.00 87.85 C ANISOU 142 CB ILE A 25 9521 10387 13470 2164 -549 -1559 C ATOM 143 CG1 ILE A 25 55.640 -19.778 -16.799 1.00 82.93 C ANISOU 143 CG1 ILE A 25 8938 9847 12726 1899 -492 -1443 C ATOM 144 CG2 ILE A 25 58.002 -20.331 -17.412 1.00 85.66 C ANISOU 144 CG2 ILE A 25 8989 10391 13167 2299 -423 -1628 C ATOM 145 CD1 ILE A 25 56.097 -18.435 -16.252 1.00 77.11 C ANISOU 145 CD1 ILE A 25 8038 9310 11952 1783 -436 -1286 C ATOM 146 N GLY A 26 54.183 -23.368 -17.646 1.00118.30 N ANISOU 146 N GLY A 26 13970 13653 17327 2096 -714 -1803 N ATOM 147 CA GLY A 26 52.993 -24.040 -17.157 1.00120.13 C ANISOU 147 CA GLY A 26 14435 13624 17584 1942 -829 -1761 C ATOM 148 C GLY A 26 51.834 -24.070 -18.142 1.00121.06 C ANISOU 148 C GLY A 26 14652 13761 17584 1800 -785 -1861 C ATOM 149 O GLY A 26 51.979 -23.717 -19.317 1.00111.77 O ANISOU 149 O GLY A 26 13392 12775 16302 1851 -672 -1987 O ATOM 150 N GLN A 27 50.681 -24.520 -17.652 1.00129.16 N ANISOU 150 N GLN A 27 15857 14594 18624 1616 -880 -1802 N ATOM 151 CA GLN A 27 49.425 -24.470 -18.399 1.00128.92 C ANISOU 151 CA GLN A 27 15905 14594 18483 1437 -860 -1864 C ATOM 152 C GLN A 27 48.252 -24.223 -17.457 1.00125.74 C ANISOU 152 C GLN A 27 15574 14120 18082 1182 -923 -1692 C ATOM 153 O GLN A 27 47.798 -25.140 -16.765 1.00127.76 O ANISOU 153 O GLN A 27 16003 14119 18419 1109 -1037 -1661 O ATOM 154 CB GLN A 27 49.180 -25.757 -19.188 1.00126.18 C ANISOU 154 CB GLN A 27 15745 14050 18148 1503 -916 -2073 C ATOM 155 CG GLN A 27 47.735 -25.889 -19.646 1.00125.53 C ANISOU 155 CG GLN A 27 15773 13945 17976 1272 -944 -2109 C ATOM 156 CD GLN A 27 47.615 -26.422 -21.054 1.00133.20 C ANISOU 156 CD GLN A 27 16813 14937 18859 1340 -914 -2347 C ATOM 157 OE1 GLN A 27 48.465 -27.187 -21.518 1.00143.06 O ANISOU 157 OE1 GLN A 27 18120 16086 20150 1557 -914 -2507 O ATOM 158 NE2 GLN A 27 46.556 -26.019 -21.748 1.00127.11 N ANISOU 158 NE2 GLN A 27 16035 14303 17958 1166 -891 -2377 N ATOM 159 N GLY A 28 47.765 -22.985 -17.447 1.00116.33 N ANISOU 159 N GLY A 28 14252 13155 16793 1051 -844 -1582 N ATOM 160 CA GLY A 28 46.701 -22.570 -16.549 1.00116.04 C ANISOU 160 CA GLY A 28 14246 13101 16745 828 -880 -1416 C ATOM 161 C GLY A 28 45.326 -23.166 -16.815 1.00117.75 C ANISOU 161 C GLY A 28 14592 13224 16924 643 -937 -1464 C ATOM 162 O GLY A 28 45.189 -24.173 -17.518 1.00122.46 O ANISOU 162 O GLY A 28 15310 13689 17532 674 -984 -1626 O ATOM 163 N THR A 29 44.304 -22.528 -16.248 1.00112.67 N ANISOU 163 N THR A 29 13917 12658 16235 446 -931 -1328 N ATOM 164 CA THR A 29 42.931 -23.032 -16.300 1.00111.22 C ANISOU 164 CA THR A 29 13827 12409 16022 239 -988 -1345 C ATOM 165 C THR A 29 42.299 -22.936 -17.689 1.00108.03 C ANISOU 165 C THR A 29 13390 12155 15500 212 -956 -1496 C ATOM 166 O THR A 29 41.432 -23.737 -18.040 1.00105.12 O ANISOU 166 O THR A 29 13126 11692 15121 84 -1024 -1584 O ATOM 167 CB THR A 29 42.019 -22.298 -15.287 1.00103.98 C ANISOU 167 CB THR A 29 12858 11569 15082 51 -978 -1156 C ATOM 168 OG1 THR A 29 42.590 -22.384 -13.977 1.00107.58 O ANISOU 168 OG1 THR A 29 13357 11890 15630 67 -1012 -1014 O ATOM 169 CG2 THR A 29 40.619 -22.914 -15.268 1.00 98.19 C ANISOU 169 CG2 THR A 29 12205 10775 14328 -176 -1038 -1171 C ATOM 170 N PHE A 30 42.740 -21.962 -18.479 1.00104.42 N ANISOU 170 N PHE A 30 12795 11930 14948 323 -857 -1524 N ATOM 171 CA PHE A 30 42.092 -21.666 -19.750 1.00 98.79 C ANISOU 171 CA PHE A 30 12039 11397 14098 293 -824 -1637 C ATOM 172 C PHE A 30 43.038 -21.767 -20.932 1.00 97.86 C ANISOU 172 C PHE A 30 11908 11350 13926 485 -765 -1803 C ATOM 173 O PHE A 30 42.661 -21.404 -22.047 1.00101.93 O ANISOU 173 O PHE A 30 12384 12040 14307 483 -725 -1892 O ATOM 174 CB PHE A 30 41.490 -20.260 -19.705 1.00 99.05 C ANISOU 174 CB PHE A 30 11928 11680 14027 223 -753 -1504 C ATOM 175 CG PHE A 30 40.480 -20.072 -18.609 1.00100.12 C ANISOU 175 CG PHE A 30 12059 11787 14196 42 -793 -1352 C ATOM 176 CD1 PHE A 30 39.208 -20.632 -18.719 1.00 92.42 C ANISOU 176 CD1 PHE A 30 11127 10789 13199 -137 -864 -1389 C ATOM 177 CD2 PHE A 30 40.801 -19.350 -17.464 1.00 96.37 C ANISOU 177 CD2 PHE A 30 11533 11317 13768 42 -758 -1178 C ATOM 178 CE1 PHE A 30 38.282 -20.471 -17.715 1.00 93.16 C ANISOU 178 CE1 PHE A 30 11200 10879 13318 -305 -887 -1252 C ATOM 179 CE2 PHE A 30 39.875 -19.185 -16.452 1.00 92.72 C ANISOU 179 CE2 PHE A 30 11068 10839 13324 -119 -783 -1045 C ATOM 180 CZ PHE A 30 38.612 -19.745 -16.579 1.00 93.25 C ANISOU 180 CZ PHE A 30 11165 10896 13369 -290 -842 -1081 C ATOM 181 N GLY A 31 44.256 -22.255 -20.680 1.00 92.43 N ANISOU 181 N GLY A 31 11247 10537 13336 654 -759 -1841 N ATOM 182 CA GLY A 31 45.327 -22.262 -21.667 1.00 98.32 C ANISOU 182 CA GLY A 31 11947 11373 14037 858 -680 -1983 C ATOM 183 C GLY A 31 46.726 -22.256 -21.049 1.00110.46 C ANISOU 183 C GLY A 31 13423 12863 15684 1036 -650 -1939 C ATOM 184 O GLY A 31 46.879 -22.459 -19.844 1.00122.00 O ANISOU 184 O GLY A 31 14914 14176 17266 1010 -714 -1814 O ATOM 185 N GLU A 32 47.749 -22.010 -21.868 1.00 99.83 N ANISOU 185 N GLU A 32 11982 11660 14287 1214 -551 -2040 N ATOM 186 CA GLU A 32 49.137 -22.111 -21.423 1.00 91.49 C ANISOU 186 CA GLU A 32 10846 10583 13333 1402 -524 -2029 C ATOM 187 C GLU A 32 49.708 -20.844 -20.769 1.00 82.56 C ANISOU 187 C GLU A 32 9540 9629 12200 1381 -453 -1846 C ATOM 188 O GLU A 32 49.203 -19.742 -20.971 1.00 83.07 O ANISOU 188 O GLU A 32 9534 9875 12155 1260 -387 -1755 O ATOM 189 CB GLU A 32 50.027 -22.550 -22.584 1.00101.75 C ANISOU 189 CB GLU A 32 12117 11956 14587 1610 -447 -2238 C ATOM 190 CG GLU A 32 49.753 -23.971 -23.049 1.00110.67 C ANISOU 190 CG GLU A 32 13443 12854 15753 1676 -532 -2433 C ATOM 191 CD GLU A 32 50.916 -24.575 -23.818 1.00114.80 C ANISOU 191 CD GLU A 32 13942 13394 16284 1941 -469 -2630 C ATOM 192 OE1 GLU A 32 51.218 -24.083 -24.927 1.00114.27 O ANISOU 192 OE1 GLU A 32 13780 13560 16076 2001 -343 -2732 O ATOM 193 OE2 GLU A 32 51.518 -25.551 -23.316 1.00114.49 O ANISOU 193 OE2 GLU A 32 13983 13134 16384 2095 -545 -2683 O ATOM 194 N VAL A 33 50.764 -21.019 -19.979 1.00 74.59 N ANISOU 194 N VAL A 33 8471 8559 11312 1502 -475 -1795 N ATOM 195 CA VAL A 33 51.442 -19.904 -19.327 1.00 77.98 C ANISOU 195 CA VAL A 33 8737 9144 11748 1484 -418 -1637 C ATOM 196 C VAL A 33 52.863 -19.718 -19.871 1.00 82.68 C ANISOU 196 C VAL A 33 9165 9908 12343 1673 -320 -1718 C ATOM 197 O VAL A 33 53.664 -20.653 -19.848 1.00 87.21 O ANISOU 197 O VAL A 33 9741 10382 13014 1861 -359 -1822 O ATOM 198 CB VAL A 33 51.521 -20.114 -17.808 1.00 74.74 C ANISOU 198 CB VAL A 33 8369 8560 11470 1442 -532 -1483 C ATOM 199 CG1 VAL A 33 51.943 -18.822 -17.115 1.00 69.05 C ANISOU 199 CG1 VAL A 33 7504 8003 10728 1367 -480 -1310 C ATOM 200 CG2 VAL A 33 50.188 -20.579 -17.283 1.00 75.87 C ANISOU 200 CG2 VAL A 33 8686 8515 11626 1273 -630 -1428 C ATOM 201 N PHE A 34 53.170 -18.507 -20.343 1.00 75.25 N ANISOU 201 N PHE A 34 8079 9222 11290 1624 -193 -1666 N ATOM 202 CA PHE A 34 54.476 -18.194 -20.935 1.00 67.52 C ANISOU 202 CA PHE A 34 6919 8449 10288 1766 -76 -1735 C ATOM 203 C PHE A 34 55.237 -17.108 -20.189 1.00 67.86 C ANISOU 203 C PHE A 34 6798 8636 10351 1706 -35 -1572 C ATOM 204 O PHE A 34 54.647 -16.117 -19.745 1.00 66.15 O ANISOU 204 O PHE A 34 6597 8458 10080 1526 -28 -1418 O ATOM 205 CB PHE A 34 54.300 -17.693 -22.364 1.00 66.88 C ANISOU 205 CB PHE A 34 6809 8575 10028 1752 63 -1834 C ATOM 206 CG PHE A 34 53.734 -18.704 -23.296 1.00 78.75 C ANISOU 206 CG PHE A 34 8453 9983 11486 1824 42 -2025 C ATOM 207 CD1 PHE A 34 54.559 -19.641 -23.903 1.00 86.35 C ANISOU 207 CD1 PHE A 34 9395 10933 12481 2040 70 -2217 C ATOM 208 CD2 PHE A 34 52.380 -18.718 -23.579 1.00 78.31 C ANISOU 208 CD2 PHE A 34 8546 9859 11350 1679 -8 -2021 C ATOM 209 CE1 PHE A 34 54.042 -20.578 -24.771 1.00 87.51 C ANISOU 209 CE1 PHE A 34 9692 10981 12578 2102 48 -2406 C ATOM 210 CE2 PHE A 34 51.854 -19.652 -24.447 1.00 88.89 C ANISOU 210 CE2 PHE A 34 10019 11114 12641 1727 -37 -2205 C ATOM 211 CZ PHE A 34 52.689 -20.587 -25.044 1.00 90.51 C ANISOU 211 CZ PHE A 34 10226 11288 12875 1936 -9 -2400 C ATOM 212 N LYS A 35 56.552 -17.276 -20.077 1.00 68.92 N ANISOU 212 N LYS A 35 6771 8859 10559 1857 -7 -1611 N ATOM 213 CA LYS A 35 57.411 -16.158 -19.715 1.00 65.96 C ANISOU 213 CA LYS A 35 6208 8687 10169 1792 65 -1491 C ATOM 214 C LYS A 35 57.714 -15.400 -21.001 1.00 67.86 C ANISOU 214 C LYS A 35 6344 9189 10249 1771 245 -1555 C ATOM 215 O LYS A 35 57.975 -16.012 -22.036 1.00 72.85 O ANISOU 215 O LYS A 35 6961 9882 10836 1912 314 -1728 O ATOM 216 CB LYS A 35 58.708 -16.628 -19.069 1.00 67.73 C ANISOU 216 CB LYS A 35 6275 8927 10533 1956 16 -1504 C ATOM 217 CG LYS A 35 59.594 -15.471 -18.613 1.00 69.20 C ANISOU 217 CG LYS A 35 6260 9325 10707 1859 75 -1376 C ATOM 218 CD LYS A 35 60.952 -15.943 -18.138 1.00 72.59 C ANISOU 218 CD LYS A 35 6494 9822 11264 2037 33 -1409 C ATOM 219 CE LYS A 35 61.773 -14.777 -17.594 1.00 82.49 C ANISOU 219 CE LYS A 35 7553 11283 12507 1904 74 -1274 C ATOM 220 NZ LYS A 35 63.114 -15.192 -17.073 1.00 84.89 N ANISOU 220 NZ LYS A 35 7637 11681 12936 2069 19 -1298 N ATOM 221 N ALA A 36 57.658 -14.074 -20.956 1.00 57.10 N ANISOU 221 N ALA A 36 4931 7974 8792 1594 322 -1418 N ATOM 222 CA ALA A 36 57.924 -13.302 -22.162 1.00 59.33 C ANISOU 222 CA ALA A 36 5136 8498 8908 1554 493 -1457 C ATOM 223 C ALA A 36 58.585 -11.959 -21.908 1.00 62.36 C ANISOU 223 C ALA A 36 5386 9068 9241 1406 581 -1313 C ATOM 224 O ALA A 36 58.715 -11.497 -20.769 1.00 59.24 O ANISOU 224 O ALA A 36 4970 8611 8926 1312 504 -1173 O ATOM 225 CB ALA A 36 56.657 -13.126 -22.992 1.00 56.87 C ANISOU 225 CB ALA A 36 5000 8157 8452 1473 516 -1480 C ATOM 226 N ARG A 37 58.973 -11.330 -23.007 1.00 66.49 N ANISOU 226 N ARG A 37 5832 9815 9615 1375 743 -1349 N ATOM 227 CA ARG A 37 59.831 -10.163 -22.982 1.00 65.31 C ANISOU 227 CA ARG A 37 5534 9873 9409 1244 853 -1243 C ATOM 228 C ARG A 37 59.205 -9.082 -23.834 1.00 63.33 C ANISOU 228 C ARG A 37 5388 9716 8958 1088 963 -1173 C ATOM 229 O ARG A 37 58.906 -9.307 -25.007 1.00 60.50 O ANISOU 229 O ARG A 37 5081 9435 8472 1144 1046 -1279 O ATOM 230 CB ARG A 37 61.195 -10.548 -23.563 1.00 63.26 C ANISOU 230 CB ARG A 37 5039 9833 9162 1380 965 -1370 C ATOM 231 CG ARG A 37 62.213 -9.447 -23.575 1.00 60.01 C ANISOU 231 CG ARG A 37 4440 9662 8698 1238 1086 -1276 C ATOM 232 CD ARG A 37 63.483 -9.891 -24.297 1.00 56.73 C ANISOU 232 CD ARG A 37 3778 9497 8280 1383 1216 -1420 C ATOM 233 NE ARG A 37 64.456 -8.811 -24.288 1.00 67.41 N ANISOU 233 NE ARG A 37 4938 11093 9580 1214 1334 -1322 N ATOM 234 CZ ARG A 37 64.464 -7.808 -25.157 1.00 68.35 C ANISOU 234 CZ ARG A 37 5076 11382 9514 1045 1495 -1267 C ATOM 235 NH1 ARG A 37 63.559 -7.763 -26.129 1.00 59.96 N ANISOU 235 NH1 ARG A 37 4205 10282 8294 1042 1554 -1305 N ATOM 236 NH2 ARG A 37 65.389 -6.862 -25.060 1.00 74.43 N ANISOU 236 NH2 ARG A 37 5672 12359 10248 873 1594 -1174 N ATOM 237 N HIS A 38 58.993 -7.913 -23.247 1.00 58.50 N ANISOU 237 N HIS A 38 4824 9090 8313 897 957 -997 N ATOM 238 CA HIS A 38 58.520 -6.786 -24.021 1.00 57.48 C ANISOU 238 CA HIS A 38 4796 9049 7993 753 1062 -913 C ATOM 239 C HIS A 38 59.540 -6.475 -25.110 1.00 64.55 C ANISOU 239 C HIS A 38 5545 10211 8768 747 1245 -972 C ATOM 240 O HIS A 38 60.733 -6.377 -24.826 1.00 66.91 O ANISOU 240 O HIS A 38 5643 10647 9132 735 1297 -972 O ATOM 241 CB HIS A 38 58.313 -5.573 -23.127 1.00 61.91 C ANISOU 241 CB HIS A 38 5427 9544 8552 560 1028 -719 C ATOM 242 CG HIS A 38 57.665 -4.432 -23.835 1.00 68.71 C ANISOU 242 CG HIS A 38 6436 10445 9224 429 1110 -620 C ATOM 243 ND1 HIS A 38 58.321 -3.688 -24.794 1.00 77.72 N ANISOU 243 ND1 HIS A 38 7525 11790 10214 346 1272 -602 N ATOM 244 CD2 HIS A 38 56.409 -3.930 -23.759 1.00 55.77 C ANISOU 244 CD2 HIS A 38 5000 8675 7517 378 1053 -535 C ATOM 245 CE1 HIS A 38 57.499 -2.767 -25.266 1.00 77.58 C ANISOU 245 CE1 HIS A 38 7690 11746 10041 250 1302 -502 C ATOM 246 NE2 HIS A 38 56.333 -2.893 -24.654 1.00 61.03 N ANISOU 246 NE2 HIS A 38 5742 9451 7995 278 1169 -464 N ATOM 247 N ARG A 39 59.086 -6.319 -26.352 1.00 62.30 N ANISOU 247 N ARG A 39 5352 10017 8303 753 1342 -1021 N ATOM 248 CA ARG A 39 60.023 -6.226 -27.469 1.00 56.86 C ANISOU 248 CA ARG A 39 4526 9589 7488 771 1524 -1104 C ATOM 249 C ARG A 39 60.839 -4.936 -27.502 1.00 64.42 C ANISOU 249 C ARG A 39 5397 10719 8361 568 1652 -963 C ATOM 250 O ARG A 39 61.858 -4.864 -28.197 1.00 63.22 O ANISOU 250 O ARG A 39 5075 10807 8137 565 1807 -1022 O ATOM 251 CB ARG A 39 59.332 -6.463 -28.811 1.00 63.98 C ANISOU 251 CB ARG A 39 5559 10546 8203 834 1590 -1202 C ATOM 252 CG ARG A 39 58.978 -7.930 -29.060 1.00 82.79 C ANISOU 252 CG ARG A 39 7965 12834 10657 1051 1513 -1403 C ATOM 253 CD ARG A 39 58.545 -8.208 -30.513 1.00 87.87 C ANISOU 253 CD ARG A 39 8706 13584 11096 1116 1600 -1531 C ATOM 254 NE ARG A 39 57.662 -9.375 -30.604 1.00 86.40 N ANISOU 254 NE ARG A 39 8643 13222 10962 1258 1471 -1674 N ATOM 255 CZ ARG A 39 58.058 -10.612 -30.906 1.00 92.85 C ANISOU 255 CZ ARG A 39 9404 14031 11843 1449 1469 -1880 C ATOM 256 NH1 ARG A 39 59.338 -10.867 -31.171 1.00 88.28 N ANISOU 256 NH1 ARG A 39 8627 13630 11284 1548 1596 -1975 N ATOM 257 NH2 ARG A 39 57.167 -11.600 -30.946 1.00 90.56 N ANISOU 257 NH2 ARG A 39 9257 13555 11597 1543 1341 -1995 N ATOM 258 N LYS A 40 60.412 -3.927 -26.744 1.00 66.18 N ANISOU 258 N LYS A 40 5735 10822 8590 395 1590 -783 N ATOM 259 CA LYS A 40 61.090 -2.627 -26.774 1.00 57.70 C ANISOU 259 CA LYS A 40 4622 9877 7424 174 1703 -639 C ATOM 260 C LYS A 40 61.938 -2.345 -25.540 1.00 57.24 C ANISOU 260 C LYS A 40 4415 9809 7526 78 1646 -564 C ATOM 261 O LYS A 40 62.994 -1.728 -25.637 1.00 62.91 O ANISOU 261 O LYS A 40 4979 10713 8211 -59 1757 -520 O ATOM 262 CB LYS A 40 60.084 -1.500 -26.967 1.00 60.25 C ANISOU 262 CB LYS A 40 5204 10090 7599 30 1697 -484 C ATOM 263 CG LYS A 40 59.543 -1.369 -28.383 1.00 60.52 C ANISOU 263 CG LYS A 40 5366 10217 7414 58 1797 -518 C ATOM 264 CD LYS A 40 58.246 -0.557 -28.374 1.00 62.25 C ANISOU 264 CD LYS A 40 5856 10264 7531 -6 1724 -384 C ATOM 265 CE LYS A 40 57.819 -0.187 -29.779 1.00 70.53 C ANISOU 265 CE LYS A 40 7037 11424 8335 -11 1826 -381 C ATOM 266 NZ LYS A 40 58.930 0.462 -30.535 1.00 77.24 N ANISOU 266 NZ LYS A 40 7799 12503 9044 -147 2019 -344 N ATOM 267 N THR A 41 61.473 -2.806 -24.387 1.00 56.83 N ANISOU 267 N THR A 41 4407 9548 7640 141 1472 -551 N ATOM 268 CA THR A 41 62.071 -2.457 -23.103 1.00 59.34 C ANISOU 268 CA THR A 41 4634 9819 8094 38 1388 -461 C ATOM 269 C THR A 41 62.729 -3.653 -22.429 1.00 64.95 C ANISOU 269 C THR A 41 5147 10533 8998 213 1292 -573 C ATOM 270 O THR A 41 63.546 -3.485 -21.525 1.00 67.06 O ANISOU 270 O THR A 41 5268 10838 9372 148 1240 -526 O ATOM 271 CB THR A 41 60.988 -1.978 -22.134 1.00 58.16 C ANISOU 271 CB THR A 41 4711 9410 7977 -34 1249 -339 C ATOM 272 OG1 THR A 41 60.232 -3.116 -21.691 1.00 54.30 O ANISOU 272 OG1 THR A 41 4278 8750 7604 150 1112 -420 O ATOM 273 CG2 THR A 41 60.062 -0.959 -22.822 1.00 42.40 C ANISOU 273 CG2 THR A 41 2950 7365 5795 -144 1314 -241 C ATOM 274 N GLY A 42 62.345 -4.857 -22.847 1.00 63.28 N ANISOU 274 N GLY A 42 4946 10270 8828 436 1258 -719 N ATOM 275 CA GLY A 42 62.902 -6.077 -22.296 1.00 55.56 C ANISOU 275 CA GLY A 42 3814 9268 8027 633 1163 -832 C ATOM 276 C GLY A 42 62.192 -6.507 -21.028 1.00 58.04 C ANISOU 276 C GLY A 42 4256 9314 8482 667 964 -777 C ATOM 277 O GLY A 42 62.521 -7.542 -20.445 1.00 58.07 O ANISOU 277 O GLY A 42 4178 9250 8637 830 858 -851 O ATOM 278 N GLN A 43 61.209 -5.721 -20.597 1.00 59.41 N ANISOU 278 N GLN A 43 4638 9335 8602 518 916 -646 N ATOM 279 CA GLN A 43 60.478 -6.032 -19.366 1.00 63.14 C ANISOU 279 CA GLN A 43 5238 9565 9187 527 742 -583 C ATOM 280 C GLN A 43 59.894 -7.432 -19.426 1.00 64.88 C ANISOU 280 C GLN A 43 5519 9641 9492 731 651 -706 C ATOM 281 O GLN A 43 59.164 -7.754 -20.363 1.00 62.02 O ANISOU 281 O GLN A 43 5258 9262 9045 792 696 -784 O ATOM 282 CB GLN A 43 59.368 -5.013 -19.120 1.00 58.21 C ANISOU 282 CB GLN A 43 4838 8814 8467 366 729 -448 C ATOM 283 CG GLN A 43 58.425 -5.379 -17.985 1.00 67.60 C ANISOU 283 CG GLN A 43 6173 9763 9747 381 570 -395 C ATOM 284 CD GLN A 43 57.065 -4.707 -18.125 1.00 79.33 C ANISOU 284 CD GLN A 43 7881 11137 11125 301 573 -319 C ATOM 285 OE1 GLN A 43 56.647 -4.344 -19.230 1.00 82.30 O ANISOU 285 OE1 GLN A 43 8317 11587 11367 295 670 -339 O ATOM 286 NE2 GLN A 43 56.366 -4.546 -17.008 1.00 80.63 N ANISOU 286 NE2 GLN A 43 8165 11132 11340 249 466 -231 N ATOM 287 N LYS A 44 60.230 -8.266 -18.442 1.00 67.15 N ANISOU 287 N LYS A 44 5751 9822 9940 831 517 -722 N ATOM 288 CA LYS A 44 59.729 -9.639 -18.402 1.00 62.06 C ANISOU 288 CA LYS A 44 5182 9011 9387 1016 418 -832 C ATOM 289 C LYS A 44 58.324 -9.682 -17.814 1.00 67.84 C ANISOU 289 C LYS A 44 6146 9513 10118 946 316 -758 C ATOM 290 O LYS A 44 58.030 -9.004 -16.828 1.00 71.23 O ANISOU 290 O LYS A 44 6640 9865 10558 812 255 -620 O ATOM 291 CB LYS A 44 60.642 -10.538 -17.578 1.00 58.94 C ANISOU 291 CB LYS A 44 4655 8581 9160 1160 308 -869 C ATOM 292 CG LYS A 44 62.105 -10.572 -18.022 1.00 60.60 C ANISOU 292 CG LYS A 44 4595 9038 9393 1250 397 -946 C ATOM 293 CD LYS A 44 62.259 -11.006 -19.462 1.00 63.52 C ANISOU 293 CD LYS A 44 4914 9539 9681 1378 537 -1109 C ATOM 294 CE LYS A 44 63.729 -10.981 -19.873 1.00 67.03 C ANISOU 294 CE LYS A 44 5068 10259 10142 1461 641 -1183 C ATOM 295 NZ LYS A 44 64.408 -9.713 -19.484 1.00 63.66 N ANISOU 295 NZ LYS A 44 4502 10009 9675 1245 696 -1046 N ATOM 296 N VAL A 45 57.462 -10.486 -18.427 1.00 65.74 N ANISOU 296 N VAL A 45 6001 9146 9833 1035 299 -857 N ATOM 297 CA VAL A 45 56.073 -10.607 -18.003 1.00 62.79 C ANISOU 297 CA VAL A 45 5827 8581 9451 969 212 -803 C ATOM 298 C VAL A 45 55.630 -12.071 -18.088 1.00 66.60 C ANISOU 298 C VAL A 45 6390 8898 10018 1111 120 -927 C ATOM 299 O VAL A 45 56.318 -12.899 -18.682 1.00 62.33 O ANISOU 299 O VAL A 45 5771 8396 9517 1271 141 -1067 O ATOM 300 CB VAL A 45 55.143 -9.764 -18.903 1.00 63.21 C ANISOU 300 CB VAL A 45 5978 8702 9337 869 304 -779 C ATOM 301 CG1 VAL A 45 55.593 -8.298 -18.931 1.00 60.37 C ANISOU 301 CG1 VAL A 45 5567 8489 8881 727 402 -659 C ATOM 302 CG2 VAL A 45 55.098 -10.344 -20.317 1.00 60.38 C ANISOU 302 CG2 VAL A 45 5612 8432 8897 978 381 -940 C ATOM 303 N ALA A 46 54.483 -12.391 -17.494 1.00 66.68 N ANISOU 303 N ALA A 46 6560 8722 10054 1051 21 -879 N ATOM 304 CA ALA A 46 53.877 -13.709 -17.670 1.00 61.16 C ANISOU 304 CA ALA A 46 5971 7854 9413 1143 -62 -991 C ATOM 305 C ALA A 46 52.604 -13.567 -18.484 1.00 61.21 C ANISOU 305 C ALA A 46 6093 7863 9300 1069 -32 -1025 C ATOM 306 O ALA A 46 51.763 -12.714 -18.192 1.00 61.10 O ANISOU 306 O ALA A 46 6137 7859 9218 931 -26 -910 O ATOM 307 CB ALA A 46 53.576 -14.364 -16.328 1.00 56.04 C ANISOU 307 CB ALA A 46 5413 6986 8892 1125 -210 -914 C ATOM 308 N LEU A 47 52.475 -14.400 -19.511 1.00 63.90 N ANISOU 308 N LEU A 47 6466 8200 9612 1169 -15 -1189 N ATOM 309 CA LEU A 47 51.280 -14.421 -20.336 1.00 56.27 C ANISOU 309 CA LEU A 47 5607 7240 8534 1107 -7 -1242 C ATOM 310 C LEU A 47 50.469 -15.669 -20.012 1.00 61.29 C ANISOU 310 C LEU A 47 6381 7654 9254 1112 -133 -1308 C ATOM 311 O LEU A 47 50.947 -16.791 -20.174 1.00 71.65 O ANISOU 311 O LEU A 47 7718 8859 10646 1240 -176 -1436 O ATOM 312 CB LEU A 47 51.656 -14.407 -21.819 1.00 56.35 C ANISOU 312 CB LEU A 47 5572 7420 8420 1193 106 -1385 C ATOM 313 CG LEU A 47 52.596 -13.301 -22.294 1.00 58.76 C ANISOU 313 CG LEU A 47 5739 7955 8633 1190 247 -1338 C ATOM 314 CD1 LEU A 47 52.877 -13.424 -23.788 1.00 52.71 C ANISOU 314 CD1 LEU A 47 4947 7351 7730 1273 359 -1490 C ATOM 315 CD2 LEU A 47 52.028 -11.926 -21.961 1.00 52.49 C ANISOU 315 CD2 LEU A 47 4965 7225 7753 1028 276 -1160 C ATOM 316 N LYS A 48 49.248 -15.474 -19.536 1.00 58.96 N ANISOU 316 N LYS A 48 6175 7286 8940 971 -193 -1220 N ATOM 317 CA LYS A 48 48.357 -16.589 -19.252 1.00 59.05 C ANISOU 317 CA LYS A 48 6320 7101 9017 931 -307 -1271 C ATOM 318 C LYS A 48 47.215 -16.581 -20.247 1.00 56.51 C ANISOU 318 C LYS A 48 6055 6845 8571 860 -299 -1347 C ATOM 319 O LYS A 48 46.416 -15.648 -20.271 1.00 66.32 O ANISOU 319 O LYS A 48 7281 8197 9722 754 -271 -1252 O ATOM 320 CB LYS A 48 47.827 -16.502 -17.824 1.00 58.57 C ANISOU 320 CB LYS A 48 6307 6908 9038 813 -388 -1112 C ATOM 321 CG LYS A 48 48.928 -16.510 -16.785 1.00 76.38 C ANISOU 321 CG LYS A 48 8514 9101 11407 876 -415 -1031 C ATOM 322 CD LYS A 48 48.394 -16.891 -15.418 1.00 95.97 C ANISOU 322 CD LYS A 48 11089 11398 13976 778 -521 -912 C ATOM 323 CE LYS A 48 49.493 -16.852 -14.352 1.00101.67 C ANISOU 323 CE LYS A 48 11764 12068 14797 840 -562 -822 C ATOM 324 NZ LYS A 48 48.906 -16.967 -12.979 1.00103.23 N ANISOU 324 NZ LYS A 48 12057 12122 15045 719 -649 -680 N ATOM 325 N LYS A 49 47.147 -17.615 -21.079 1.00 55.76 N ANISOU 325 N LYS A 49 6029 6687 8470 927 -327 -1524 N ATOM 326 CA LYS A 49 46.148 -17.673 -22.136 1.00 65.46 C ANISOU 326 CA LYS A 49 7309 7995 9569 866 -328 -1618 C ATOM 327 C LYS A 49 44.783 -18.046 -21.560 1.00 67.66 C ANISOU 327 C LYS A 49 7673 8157 9876 701 -434 -1567 C ATOM 328 O LYS A 49 44.719 -18.785 -20.583 1.00 63.13 O ANISOU 328 O LYS A 49 7170 7385 9434 663 -518 -1530 O ATOM 329 CB LYS A 49 46.567 -18.690 -23.188 1.00 73.25 C ANISOU 329 CB LYS A 49 8353 8944 10534 988 -327 -1837 C ATOM 330 CG LYS A 49 45.911 -18.508 -24.547 1.00 83.16 C ANISOU 330 CG LYS A 49 9629 10355 11613 963 -293 -1949 C ATOM 331 CD LYS A 49 46.205 -19.704 -25.442 1.00 95.55 C ANISOU 331 CD LYS A 49 11294 11841 13172 1070 -313 -2181 C ATOM 332 CE LYS A 49 45.632 -19.518 -26.838 1.00107.41 C ANISOU 332 CE LYS A 49 12819 13513 14478 1049 -280 -2301 C ATOM 333 NZ LYS A 49 46.366 -18.482 -27.621 1.00111.80 N ANISOU 333 NZ LYS A 49 13264 14320 14894 1132 -134 -2282 N ATOM 334 N VAL A 50 43.712 -17.499 -22.142 1.00 68.78 N ANISOU 334 N VAL A 50 7804 8437 9891 603 -430 -1556 N ATOM 335 CA VAL A 50 42.330 -17.933 -21.864 1.00 72.15 C ANISOU 335 CA VAL A 50 8291 8798 10324 443 -526 -1544 C ATOM 336 C VAL A 50 41.815 -18.732 -23.071 1.00 65.18 C ANISOU 336 C VAL A 50 7479 7926 9359 432 -571 -1736 C ATOM 337 O VAL A 50 42.543 -18.900 -24.036 1.00 77.24 O ANISOU 337 O VAL A 50 9016 9508 10826 558 -521 -1868 O ATOM 338 CB VAL A 50 41.413 -16.741 -21.580 1.00 66.23 C ANISOU 338 CB VAL A 50 7463 8208 9493 345 -502 -1392 C ATOM 339 CG1 VAL A 50 40.035 -17.220 -21.132 1.00 58.84 C ANISOU 339 CG1 VAL A 50 6560 7218 8580 176 -596 -1371 C ATOM 340 CG2 VAL A 50 42.042 -15.854 -20.533 1.00 58.13 C ANISOU 340 CG2 VAL A 50 6379 7183 8524 368 -445 -1223 C ATOM 341 N GLU A 55 34.243 -21.482 -23.167 1.00114.74 N ANISOU 341 N GLU A 55 13847 14217 15532 -647 -1114 -1890 N ATOM 342 CA GLU A 55 33.913 -22.704 -23.898 1.00107.99 C ANISOU 342 CA GLU A 55 13120 13247 14665 -751 -1215 -2084 C ATOM 343 C GLU A 55 32.520 -22.752 -24.538 1.00 94.71 C ANISOU 343 C GLU A 55 11357 11753 12874 -934 -1302 -2144 C ATOM 344 O GLU A 55 32.324 -22.308 -25.673 1.00 91.60 O ANISOU 344 O GLU A 55 10910 11564 12332 -869 -1309 -2229 O ATOM 345 CB GLU A 55 34.071 -23.878 -22.930 1.00112.24 C ANISOU 345 CB GLU A 55 13814 13467 15365 -864 -1270 -2079 C ATOM 346 CG GLU A 55 35.163 -23.640 -21.861 1.00111.05 C ANISOU 346 CG GLU A 55 13690 13169 15336 -725 -1197 -1943 C ATOM 347 CD GLU A 55 34.820 -22.550 -20.827 1.00 97.45 C ANISOU 347 CD GLU A 55 11815 11586 13627 -756 -1132 -1722 C ATOM 348 OE1 GLU A 55 33.649 -22.123 -20.728 1.00 96.90 O ANISOU 348 OE1 GLU A 55 11626 11691 13499 -903 -1148 -1661 O ATOM 349 OE2 GLU A 55 35.734 -22.124 -20.095 1.00 88.45 O ANISOU 349 OE2 GLU A 55 10673 10381 12554 -629 -1067 -1614 O ATOM 350 N LYS A 56 31.558 -23.304 -23.805 1.00 86.51 N ANISOU 350 N LYS A 56 10311 10654 11906 -1169 -1373 -2097 N ATOM 351 CA LYS A 56 30.210 -23.509 -24.332 1.00 88.06 C ANISOU 351 CA LYS A 56 10422 11021 12017 -1374 -1470 -2163 C ATOM 352 C LYS A 56 29.295 -22.296 -24.128 1.00 71.63 C ANISOU 352 C LYS A 56 8099 9256 9861 -1388 -1438 -2016 C ATOM 353 O LYS A 56 28.183 -22.241 -24.641 1.00 73.81 O ANISOU 353 O LYS A 56 8257 9740 10048 -1518 -1514 -2058 O ATOM 354 CB LYS A 56 29.578 -24.753 -23.695 1.00 96.37 C ANISOU 354 CB LYS A 56 11580 11862 13175 -1649 -1562 -2193 C ATOM 355 CG LYS A 56 30.190 -26.085 -24.138 1.00100.23 C ANISOU 355 CG LYS A 56 12326 12044 13712 -1667 -1630 -2379 C ATOM 356 CD LYS A 56 29.293 -27.248 -23.731 1.00104.59 C ANISOU 356 CD LYS A 56 12976 12432 14332 -1986 -1740 -2421 C ATOM 357 CE LYS A 56 29.517 -28.461 -24.614 1.00108.68 C ANISOU 357 CE LYS A 56 13728 12731 14834 -2035 -1838 -2657 C ATOM 358 NZ LYS A 56 28.268 -29.262 -24.764 1.00108.31 N ANISOU 358 NZ LYS A 56 13699 12686 14768 -2378 -1964 -2735 N ATOM 359 N GLU A 57 29.767 -21.325 -23.371 1.00 59.49 N ANISOU 359 N GLU A 57 6489 7756 8359 -1247 -1331 -1848 N ATOM 360 CA GLU A 57 28.948 -20.180 -23.045 1.00 56.26 C ANISOU 360 CA GLU A 57 5872 7611 7891 -1239 -1293 -1704 C ATOM 361 C GLU A 57 29.724 -18.899 -23.313 1.00 53.32 C ANISOU 361 C GLU A 57 5458 7353 7449 -981 -1191 -1624 C ATOM 362 O GLU A 57 29.783 -18.016 -22.463 1.00 51.92 O ANISOU 362 O GLU A 57 5204 7220 7301 -915 -1111 -1463 O ATOM 363 CB GLU A 57 28.517 -20.264 -21.581 1.00 47.59 C ANISOU 363 CB GLU A 57 4731 6439 6912 -1379 -1263 -1554 C ATOM 364 CG GLU A 57 27.575 -21.421 -21.295 1.00 61.14 C ANISOU 364 CG GLU A 57 6467 8083 8682 -1671 -1359 -1610 C ATOM 365 CD GLU A 57 26.213 -21.249 -21.972 1.00 73.72 C ANISOU 365 CD GLU A 57 7873 9969 10166 -1801 -1437 -1661 C ATOM 366 OE1 GLU A 57 25.706 -20.103 -22.027 1.00 68.01 O ANISOU 366 OE1 GLU A 57 6961 9517 9364 -1698 -1396 -1571 O ATOM 367 OE2 GLU A 57 25.651 -22.261 -22.450 1.00 81.92 O ANISOU 367 OE2 GLU A 57 8959 10967 11198 -2006 -1545 -1794 O ATOM 368 N GLY A 58 30.331 -18.807 -24.492 1.00 52.24 N ANISOU 368 N GLY A 58 5383 7255 7211 -843 -1191 -1738 N ATOM 369 CA GLY A 58 31.170 -17.666 -24.814 1.00 50.78 C ANISOU 369 CA GLY A 58 5181 7159 6954 -617 -1090 -1668 C ATOM 370 C GLY A 58 32.355 -17.506 -23.871 1.00 52.06 C ANISOU 370 C GLY A 58 5415 7128 7238 -520 -991 -1573 C ATOM 371 O GLY A 58 32.876 -18.489 -23.328 1.00 54.13 O ANISOU 371 O GLY A 58 5789 7152 7625 -574 -1008 -1616 O ATOM 372 N PHE A 59 32.773 -16.259 -23.670 1.00 49.72 N ANISOU 372 N PHE A 59 5058 6931 6901 -377 -897 -1442 N ATOM 373 CA PHE A 59 33.896 -15.957 -22.797 1.00 45.22 C ANISOU 373 CA PHE A 59 4537 6213 6431 -287 -807 -1345 C ATOM 374 C PHE A 59 33.649 -16.439 -21.368 1.00 51.33 C ANISOU 374 C PHE A 59 5323 6829 7353 -414 -822 -1254 C ATOM 375 O PHE A 59 32.670 -16.062 -20.752 1.00 58.91 O ANISOU 375 O PHE A 59 6190 7883 8312 -504 -830 -1159 O ATOM 376 CB PHE A 59 34.213 -14.459 -22.806 1.00 45.03 C ANISOU 376 CB PHE A 59 4449 6333 6326 -146 -712 -1213 C ATOM 377 CG PHE A 59 35.557 -14.140 -22.226 1.00 54.50 C ANISOU 377 CG PHE A 59 5702 7404 7600 -44 -622 -1147 C ATOM 378 CD1 PHE A 59 36.689 -14.113 -23.035 1.00 55.58 C ANISOU 378 CD1 PHE A 59 5890 7533 7694 78 -570 -1223 C ATOM 379 CD2 PHE A 59 35.705 -13.910 -20.871 1.00 52.36 C ANISOU 379 CD2 PHE A 59 5425 7030 7439 -79 -592 -1015 C ATOM 380 CE1 PHE A 59 37.947 -13.848 -22.507 1.00 49.41 C ANISOU 380 CE1 PHE A 59 5136 6654 6985 163 -492 -1167 C ATOM 381 CE2 PHE A 59 36.960 -13.642 -20.334 1.00 54.07 C ANISOU 381 CE2 PHE A 59 5684 7139 7723 6 -524 -959 C ATOM 382 CZ PHE A 59 38.085 -13.615 -21.158 1.00 45.80 C ANISOU 382 CZ PHE A 59 4669 6093 6639 125 -476 -1036 C ATOM 383 N PRO A 60 34.549 -17.274 -20.837 1.00 60.98 N ANISOU 383 N PRO A 60 6658 7814 8696 -412 -823 -1282 N ATOM 384 CA PRO A 60 34.385 -17.913 -19.523 1.00 56.85 C ANISOU 384 CA PRO A 60 6182 7110 8308 -540 -850 -1205 C ATOM 385 C PRO A 60 34.084 -16.921 -18.396 1.00 55.85 C ANISOU 385 C PRO A 60 5969 7057 8194 -552 -787 -1019 C ATOM 386 O PRO A 60 34.867 -16.001 -18.091 1.00 51.46 O ANISOU 386 O PRO A 60 5398 6522 7632 -420 -708 -930 O ATOM 387 CB PRO A 60 35.747 -18.587 -19.285 1.00 52.29 C ANISOU 387 CB PRO A 60 5735 6300 7833 -444 -842 -1247 C ATOM 388 CG PRO A 60 36.301 -18.775 -20.646 1.00 54.87 C ANISOU 388 CG PRO A 60 6093 6670 8084 -325 -840 -1407 C ATOM 389 CD PRO A 60 35.856 -17.585 -21.437 1.00 56.89 C ANISOU 389 CD PRO A 60 6230 7197 8190 -266 -792 -1380 C ATOM 390 N ILE A 61 32.942 -17.144 -17.759 1.00 52.19 N ANISOU 390 N ILE A 61 5452 6629 7747 -721 -820 -966 N ATOM 391 CA ILE A 61 32.475 -16.301 -16.671 1.00 41.47 C ANISOU 391 CA ILE A 61 4013 5352 6393 -746 -761 -806 C ATOM 392 C ILE A 61 33.480 -16.300 -15.526 1.00 50.16 C ANISOU 392 C ILE A 61 5206 6263 7590 -707 -719 -707 C ATOM 393 O ILE A 61 33.616 -15.322 -14.788 1.00 59.40 O ANISOU 393 O ILE A 61 6336 7488 8746 -649 -649 -583 O ATOM 394 CB ILE A 61 31.048 -16.716 -16.223 1.00 57.85 C ANISOU 394 CB ILE A 61 6004 7508 8468 -953 -802 -785 C ATOM 395 CG1 ILE A 61 30.510 -15.786 -15.138 1.00 52.46 C ANISOU 395 CG1 ILE A 61 5225 6935 7772 -962 -726 -629 C ATOM 396 CG2 ILE A 61 30.975 -18.225 -15.822 1.00 37.73 C ANISOU 396 CG2 ILE A 61 3579 4737 6022 -1144 -879 -838 C ATOM 397 CD1 ILE A 61 29.031 -15.976 -14.919 1.00 46.73 C ANISOU 397 CD1 ILE A 61 4365 6371 7019 -1136 -750 -618 C ATOM 398 N THR A 62 34.216 -17.391 -15.409 1.00 56.85 N ANISOU 398 N THR A 62 6185 6885 8529 -728 -770 -767 N ATOM 399 CA THR A 62 35.244 -17.516 -14.385 1.00 54.91 C ANISOU 399 CA THR A 62 6031 6455 8376 -680 -753 -682 C ATOM 400 C THR A 62 36.419 -16.592 -14.667 1.00 55.21 C ANISOU 400 C THR A 62 6049 6538 8391 -480 -686 -664 C ATOM 401 O THR A 62 36.977 -15.979 -13.747 1.00 54.86 O ANISOU 401 O THR A 62 6008 6465 8372 -437 -641 -547 O ATOM 402 CB THR A 62 35.701 -18.984 -14.255 1.00 62.32 C ANISOU 402 CB THR A 62 7125 7133 9420 -735 -838 -757 C ATOM 403 OG1 THR A 62 34.939 -19.604 -13.217 1.00 66.43 O ANISOU 403 OG1 THR A 62 7695 7556 9990 -932 -874 -677 O ATOM 404 CG2 THR A 62 37.143 -19.076 -13.884 1.00 75.29 C ANISOU 404 CG2 THR A 62 8848 8621 11139 -584 -830 -737 C ATOM 405 N ALA A 63 36.788 -16.479 -15.940 1.00 48.05 N ANISOU 405 N ALA A 63 5122 5711 7425 -372 -677 -780 N ATOM 406 CA ALA A 63 37.846 -15.550 -16.328 1.00 50.48 C ANISOU 406 CA ALA A 63 5398 6091 7692 -203 -603 -763 C ATOM 407 C ALA A 63 37.399 -14.086 -16.174 1.00 56.20 C ANISOU 407 C ALA A 63 6031 7001 8322 -177 -529 -649 C ATOM 408 O ALA A 63 38.180 -13.240 -15.742 1.00 52.10 O ANISOU 408 O ALA A 63 5506 6488 7802 -98 -467 -563 O ATOM 409 CB ALA A 63 38.329 -15.835 -17.750 1.00 48.29 C ANISOU 409 CB ALA A 63 5130 5860 7360 -103 -603 -918 C ATOM 410 N LEU A 64 36.142 -13.790 -16.509 1.00 57.96 N ANISOU 410 N LEU A 64 6184 7373 8466 -241 -540 -648 N ATOM 411 CA LEU A 64 35.619 -12.440 -16.302 1.00 51.64 C ANISOU 411 CA LEU A 64 5307 6734 7580 -201 -477 -539 C ATOM 412 C LEU A 64 35.730 -12.063 -14.848 1.00 49.79 C ANISOU 412 C LEU A 64 5091 6421 7404 -239 -441 -405 C ATOM 413 O LEU A 64 36.119 -10.952 -14.520 1.00 55.28 O ANISOU 413 O LEU A 64 5783 7159 8062 -160 -375 -317 O ATOM 414 CB LEU A 64 34.156 -12.320 -16.724 1.00 47.26 C ANISOU 414 CB LEU A 64 4659 6351 6947 -265 -508 -557 C ATOM 415 CG LEU A 64 33.916 -12.415 -18.226 1.00 51.66 C ANISOU 415 CG LEU A 64 5189 7034 7407 -216 -545 -677 C ATOM 416 CD1 LEU A 64 32.439 -12.539 -18.502 1.00 56.11 C ANISOU 416 CD1 LEU A 64 5649 7757 7914 -308 -602 -701 C ATOM 417 CD2 LEU A 64 34.531 -11.235 -18.976 1.00 39.16 C ANISOU 417 CD2 LEU A 64 3606 5556 5719 -55 -478 -648 C ATOM 418 N ARG A 65 35.386 -12.992 -13.969 1.00 46.53 N ANISOU 418 N ARG A 65 4713 5888 7077 -369 -487 -390 N ATOM 419 CA ARG A 65 35.422 -12.707 -12.540 1.00 48.63 C ANISOU 419 CA ARG A 65 5008 6086 7386 -419 -457 -262 C ATOM 420 C ARG A 65 36.842 -12.373 -12.086 1.00 51.38 C ANISOU 420 C ARG A 65 5424 6320 7778 -326 -431 -215 C ATOM 421 O ARG A 65 37.057 -11.386 -11.376 1.00 53.32 O ANISOU 421 O ARG A 65 5670 6594 7994 -291 -374 -115 O ATOM 422 CB ARG A 65 34.855 -13.880 -11.755 1.00 46.57 C ANISOU 422 CB ARG A 65 4789 5705 7199 -588 -514 -254 C ATOM 423 CG ARG A 65 34.662 -13.639 -10.289 1.00 58.98 C ANISOU 423 CG ARG A 65 6387 7232 8790 -663 -481 -123 C ATOM 424 CD ARG A 65 34.256 -14.946 -9.655 1.00 66.42 C ANISOU 424 CD ARG A 65 7400 8033 9806 -838 -544 -120 C ATOM 425 NE ARG A 65 35.167 -15.999 -10.094 1.00 85.64 N ANISOU 425 NE ARG A 65 9941 10277 12324 -811 -621 -204 N ATOM 426 CZ ARG A 65 35.173 -17.242 -9.625 1.00 93.20 C ANISOU 426 CZ ARG A 65 11010 11042 13359 -930 -693 -209 C ATOM 427 NH1 ARG A 65 34.299 -17.608 -8.692 1.00 92.09 N ANISOU 427 NH1 ARG A 65 10887 10883 13220 -1110 -693 -128 N ATOM 428 NH2 ARG A 65 36.059 -18.116 -10.092 1.00 93.92 N ANISOU 428 NH2 ARG A 65 11202 10958 13523 -866 -760 -294 N ATOM 429 N GLU A 66 37.807 -13.181 -12.523 1.00 47.74 N ANISOU 429 N GLU A 66 5018 5739 7383 -281 -474 -296 N ATOM 430 CA GLU A 66 39.202 -12.981 -12.146 1.00 49.78 C ANISOU 430 CA GLU A 66 5316 5906 7691 -192 -460 -263 C ATOM 431 C GLU A 66 39.717 -11.631 -12.639 1.00 52.31 C ANISOU 431 C GLU A 66 5586 6362 7929 -86 -379 -234 C ATOM 432 O GLU A 66 40.315 -10.864 -11.880 1.00 50.64 O ANISOU 432 O GLU A 66 5387 6136 7718 -66 -342 -141 O ATOM 433 CB GLU A 66 40.072 -14.101 -12.704 1.00 53.94 C ANISOU 433 CB GLU A 66 5891 6308 8297 -136 -517 -375 C ATOM 434 CG GLU A 66 41.550 -13.960 -12.373 1.00 62.82 C ANISOU 434 CG GLU A 66 7027 7362 9479 -32 -508 -352 C ATOM 435 CD GLU A 66 42.386 -15.092 -12.951 1.00 74.95 C ANISOU 435 CD GLU A 66 8601 8783 11093 51 -561 -474 C ATOM 436 OE1 GLU A 66 41.809 -15.970 -13.628 1.00 79.36 O ANISOU 436 OE1 GLU A 66 9197 9301 11656 21 -604 -581 O ATOM 437 OE2 GLU A 66 43.621 -15.106 -12.737 1.00 73.52 O ANISOU 437 OE2 GLU A 66 8409 8556 10967 150 -562 -469 O ATOM 438 N ILE A 67 39.474 -11.349 -13.916 1.00 45.00 N ANISOU 438 N ILE A 67 4613 5561 6922 -29 -354 -313 N ATOM 439 CA ILE A 67 39.837 -10.073 -14.500 1.00 49.40 C ANISOU 439 CA ILE A 67 5139 6246 7383 59 -277 -281 C ATOM 440 C ILE A 67 39.231 -8.914 -13.703 1.00 51.53 C ANISOU 440 C ILE A 67 5408 6572 7598 38 -231 -155 C ATOM 441 O ILE A 67 39.920 -7.943 -13.375 1.00 44.36 O ANISOU 441 O ILE A 67 4522 5667 6666 76 -177 -82 O ATOM 442 CB ILE A 67 39.386 -9.994 -15.975 1.00 48.60 C ANISOU 442 CB ILE A 67 5002 6282 7183 109 -269 -375 C ATOM 443 CG1 ILE A 67 40.171 -11.001 -16.811 1.00 48.48 C ANISOU 443 CG1 ILE A 67 5000 6215 7206 153 -297 -509 C ATOM 444 CG2 ILE A 67 39.561 -8.582 -16.526 1.00 38.49 C ANISOU 444 CG2 ILE A 67 3709 5132 5785 186 -191 -316 C ATOM 445 CD1 ILE A 67 39.667 -11.134 -18.238 1.00 51.87 C ANISOU 445 CD1 ILE A 67 5408 6769 7531 186 -303 -620 C ATOM 446 N LYS A 68 37.946 -9.020 -13.374 1.00 45.10 N ANISOU 446 N LYS A 68 4568 5804 6765 -27 -250 -135 N ATOM 447 CA LYS A 68 37.278 -7.947 -12.636 1.00 47.95 C ANISOU 447 CA LYS A 68 4924 6227 7068 -28 -201 -30 C ATOM 448 C LYS A 68 38.002 -7.722 -11.309 1.00 47.11 C ANISOU 448 C LYS A 68 4883 6000 7018 -61 -184 59 C ATOM 449 O LYS A 68 38.285 -6.591 -10.934 1.00 46.91 O ANISOU 449 O LYS A 68 4891 5991 6941 -19 -129 133 O ATOM 450 CB LYS A 68 35.795 -8.264 -12.406 1.00 41.00 C ANISOU 450 CB LYS A 68 3981 5427 6169 -99 -223 -30 C ATOM 451 CG LYS A 68 35.105 -7.366 -11.388 1.00 49.59 C ANISOU 451 CG LYS A 68 5064 6563 7216 -103 -169 72 C ATOM 452 CD LYS A 68 33.791 -7.970 -10.875 1.00 58.74 C ANISOU 452 CD LYS A 68 6149 7784 8385 -209 -189 73 C ATOM 453 CE LYS A 68 34.050 -9.212 -10.016 1.00 62.07 C ANISOU 453 CE LYS A 68 6621 8052 8909 -351 -235 75 C ATOM 454 NZ LYS A 68 32.822 -9.761 -9.374 1.00 60.85 N ANISOU 454 NZ LYS A 68 6405 7955 8760 -484 -240 93 N ATOM 455 N ILE A 69 38.328 -8.815 -10.626 1.00 43.83 N ANISOU 455 N ILE A 69 4499 5454 6701 -137 -240 51 N ATOM 456 CA ILE A 69 39.046 -8.754 -9.354 1.00 41.50 C ANISOU 456 CA ILE A 69 4269 5042 6456 -172 -245 133 C ATOM 457 C ILE A 69 40.494 -8.231 -9.464 1.00 46.43 C ANISOU 457 C ILE A 69 4916 5632 7095 -102 -230 143 C ATOM 458 O ILE A 69 40.913 -7.381 -8.672 1.00 45.94 O ANISOU 458 O ILE A 69 4893 5552 7009 -106 -199 225 O ATOM 459 CB ILE A 69 38.964 -10.092 -8.615 1.00 46.05 C ANISOU 459 CB ILE A 69 4887 5484 7126 -270 -319 131 C ATOM 460 CG1 ILE A 69 37.501 -10.327 -8.173 1.00 37.54 C ANISOU 460 CG1 ILE A 69 3785 4460 6017 -375 -312 156 C ATOM 461 CG2 ILE A 69 39.885 -10.079 -7.410 1.00 39.58 C ANISOU 461 CG2 ILE A 69 4141 4545 6354 -289 -342 212 C ATOM 462 CD1 ILE A 69 37.135 -11.760 -7.910 1.00 35.40 C ANISOU 462 CD1 ILE A 69 3549 4081 5822 -491 -385 127 C ATOM 463 N LEU A 70 41.247 -8.719 -10.448 1.00 50.83 N ANISOU 463 N LEU A 70 5442 6187 7684 -42 -247 57 N ATOM 464 CA LEU A 70 42.592 -8.197 -10.720 1.00 43.34 C ANISOU 464 CA LEU A 70 4482 5246 6740 22 -219 57 C ATOM 465 C LEU A 70 42.561 -6.689 -11.032 1.00 48.27 C ANISOU 465 C LEU A 70 5111 5975 7255 50 -136 112 C ATOM 466 O LEU A 70 43.439 -5.945 -10.620 1.00 46.36 O ANISOU 466 O LEU A 70 4888 5720 7005 47 -108 167 O ATOM 467 CB LEU A 70 43.229 -8.951 -11.888 1.00 48.09 C ANISOU 467 CB LEU A 70 5037 5862 7372 92 -233 -61 C ATOM 468 CG LEU A 70 44.168 -10.150 -11.644 1.00 58.22 C ANISOU 468 CG LEU A 70 6321 7024 8775 120 -303 -114 C ATOM 469 CD1 LEU A 70 44.191 -10.612 -10.206 1.00 52.26 C ANISOU 469 CD1 LEU A 70 5626 6134 8096 55 -371 -33 C ATOM 470 CD2 LEU A 70 43.814 -11.310 -12.580 1.00 41.61 C ANISOU 470 CD2 LEU A 70 4216 4896 6698 151 -342 -244 C ATOM 471 N GLN A 71 41.545 -6.228 -11.753 1.00 48.62 N ANISOU 471 N GLN A 71 5143 6119 7211 75 -101 99 N ATOM 472 CA GLN A 71 41.459 -4.805 -12.056 1.00 48.55 C ANISOU 472 CA GLN A 71 5165 6188 7095 114 -29 157 C ATOM 473 C GLN A 71 41.147 -3.944 -10.832 1.00 49.83 C ANISOU 473 C GLN A 71 5394 6306 7232 79 -6 259 C ATOM 474 O GLN A 71 41.518 -2.776 -10.784 1.00 45.04 O ANISOU 474 O GLN A 71 4844 5707 6561 96 46 316 O ATOM 475 CB GLN A 71 40.419 -4.557 -13.132 1.00 37.08 C ANISOU 475 CB GLN A 71 3684 4855 5549 169 -13 121 C ATOM 476 CG GLN A 71 40.889 -4.938 -14.521 1.00 44.83 C ANISOU 476 CG GLN A 71 4627 5903 6504 218 -10 29 C ATOM 477 CD GLN A 71 39.723 -5.059 -15.475 1.00 55.74 C ANISOU 477 CD GLN A 71 5974 7398 7807 255 -29 -22 C ATOM 478 OE1 GLN A 71 39.906 -5.091 -16.684 1.00 59.41 O ANISOU 478 OE1 GLN A 71 6423 7944 8206 304 -18 -84 O ATOM 479 NE2 GLN A 71 38.508 -5.139 -14.928 1.00 61.29 N ANISOU 479 NE2 GLN A 71 6655 8121 8510 229 -58 3 N ATOM 480 N LEU A 72 40.454 -4.529 -9.858 1.00 43.14 N ANISOU 480 N LEU A 72 4551 5411 6430 23 -42 278 N ATOM 481 CA LEU A 72 40.106 -3.839 -8.629 1.00 39.36 C ANISOU 481 CA LEU A 72 4138 4894 5923 -11 -17 363 C ATOM 482 C LEU A 72 41.301 -3.734 -7.687 1.00 45.91 C ANISOU 482 C LEU A 72 5025 5621 6799 -63 -37 410 C ATOM 483 O LEU A 72 41.533 -2.674 -7.103 1.00 46.17 O ANISOU 483 O LEU A 72 5133 5633 6776 -70 2 471 O ATOM 484 CB LEU A 72 38.964 -4.573 -7.912 1.00 44.70 C ANISOU 484 CB LEU A 72 4791 5571 6621 -68 -41 368 C ATOM 485 CG LEU A 72 38.608 -4.006 -6.528 1.00 48.83 C ANISOU 485 CG LEU A 72 5385 6059 7111 -110 -10 449 C ATOM 486 CD1 LEU A 72 37.984 -2.592 -6.637 1.00 35.55 C ANISOU 486 CD1 LEU A 72 3738 4452 5319 -26 67 483 C ATOM 487 CD2 LEU A 72 37.678 -4.944 -5.779 1.00 42.13 C ANISOU 487 CD2 LEU A 72 4508 5208 6293 -195 -34 456 C ATOM 488 N LEU A 73 42.052 -4.833 -7.549 1.00 39.18 N ANISOU 488 N LEU A 73 4142 4702 6045 -93 -103 377 N ATOM 489 CA LEU A 73 43.111 -4.942 -6.550 1.00 45.22 C ANISOU 489 CA LEU A 73 4944 5375 6862 -141 -147 422 C ATOM 490 C LEU A 73 44.458 -4.347 -6.998 1.00 50.58 C ANISOU 490 C LEU A 73 5601 6074 7543 -118 -132 417 C ATOM 491 O LEU A 73 45.153 -4.930 -7.826 1.00 52.54 O ANISOU 491 O LEU A 73 5774 6345 7843 -75 -148 352 O ATOM 492 CB LEU A 73 43.288 -6.406 -6.149 1.00 46.94 C ANISOU 492 CB LEU A 73 5146 5505 7184 -169 -234 398 C ATOM 493 CG LEU A 73 42.020 -7.060 -5.601 1.00 47.59 C ANISOU 493 CG LEU A 73 5254 5563 7265 -229 -249 414 C ATOM 494 CD1 LEU A 73 42.263 -8.525 -5.160 1.00 37.98 C ANISOU 494 CD1 LEU A 73 4055 4227 6150 -270 -343 402 C ATOM 495 CD2 LEU A 73 41.469 -6.214 -4.454 1.00 36.28 C ANISOU 495 CD2 LEU A 73 3893 4134 5757 -280 -208 500 C ATOM 496 N LYS A 74 44.822 -3.192 -6.450 1.00 44.35 N ANISOU 496 N LYS A 74 4878 5280 6695 -153 -98 480 N ATOM 497 CA LYS A 74 46.129 -2.588 -6.746 1.00 47.45 C ANISOU 497 CA LYS A 74 5247 5695 7086 -167 -84 485 C ATOM 498 C LYS A 74 46.926 -2.325 -5.475 1.00 47.99 C ANISOU 498 C LYS A 74 5362 5699 7173 -246 -135 545 C ATOM 499 O LYS A 74 46.651 -1.379 -4.747 1.00 55.50 O ANISOU 499 O LYS A 74 6418 6618 8051 -295 -109 601 O ATOM 500 CB LYS A 74 45.974 -1.302 -7.549 1.00 39.49 C ANISOU 500 CB LYS A 74 4282 4748 5974 -151 6 499 C ATOM 501 CG LYS A 74 45.209 -1.509 -8.841 1.00 52.29 C ANISOU 501 CG LYS A 74 5859 6447 7560 -70 46 444 C ATOM 502 CD LYS A 74 45.806 -2.675 -9.616 1.00 59.82 C ANISOU 502 CD LYS A 74 6698 7437 8595 -33 12 360 C ATOM 503 CE LYS A 74 45.041 -2.955 -10.896 1.00 60.82 C ANISOU 503 CE LYS A 74 6789 7644 8678 39 41 294 C ATOM 504 NZ LYS A 74 45.897 -3.716 -11.839 1.00 54.71 N ANISOU 504 NZ LYS A 74 5921 6918 7948 80 38 208 N ATOM 505 N HIS A 75 47.927 -3.160 -5.220 1.00 43.97 N ANISOU 505 N HIS A 75 4778 5172 6757 -250 -211 528 N ATOM 506 CA HIS A 75 48.615 -3.121 -3.944 1.00 44.06 C ANISOU 506 CA HIS A 75 4826 5126 6789 -320 -286 585 C ATOM 507 C HIS A 75 49.993 -3.794 -4.043 1.00 55.62 C ANISOU 507 C HIS A 75 6168 6614 8350 -298 -359 556 C ATOM 508 O HIS A 75 50.161 -4.752 -4.806 1.00 58.25 O ANISOU 508 O HIS A 75 6409 6965 8756 -213 -374 490 O ATOM 509 CB HIS A 75 47.729 -3.792 -2.897 1.00 37.47 C ANISOU 509 CB HIS A 75 4072 4204 5960 -339 -336 622 C ATOM 510 CG HIS A 75 48.294 -3.758 -1.517 1.00 52.09 C ANISOU 510 CG HIS A 75 5986 5995 7809 -412 -417 687 C ATOM 511 ND1 HIS A 75 49.162 -4.722 -1.048 1.00 54.19 N ANISOU 511 ND1 HIS A 75 6202 6224 8165 -400 -530 694 N ATOM 512 CD2 HIS A 75 48.119 -2.878 -0.503 1.00 50.92 C ANISOU 512 CD2 HIS A 75 5955 5818 7573 -490 -408 746 C ATOM 513 CE1 HIS A 75 49.498 -4.434 0.198 1.00 58.09 C ANISOU 513 CE1 HIS A 75 6774 6676 8621 -476 -592 760 C ATOM 514 NE2 HIS A 75 48.879 -3.321 0.553 1.00 60.83 N ANISOU 514 NE2 HIS A 75 7226 7027 8858 -537 -517 788 N ATOM 515 N GLU A 76 50.978 -3.288 -3.293 1.00 46.98 N ANISOU 515 N GLU A 76 5070 5527 7252 -369 -406 600 N ATOM 516 CA GLU A 76 52.342 -3.808 -3.388 1.00 52.69 C ANISOU 516 CA GLU A 76 5651 6305 8064 -342 -475 574 C ATOM 517 C GLU A 76 52.433 -5.324 -3.172 1.00 49.95 C ANISOU 517 C GLU A 76 5258 5896 7826 -245 -575 547 C ATOM 518 O GLU A 76 53.301 -5.978 -3.736 1.00 52.62 O ANISOU 518 O GLU A 76 5461 6285 8246 -160 -605 490 O ATOM 519 CB GLU A 76 53.284 -3.082 -2.419 1.00 65.71 C ANISOU 519 CB GLU A 76 7307 7971 9688 -450 -534 632 C ATOM 520 CG GLU A 76 54.182 -2.051 -3.080 1.00 91.01 C ANISOU 520 CG GLU A 76 10432 11290 12858 -519 -467 620 C ATOM 521 CD GLU A 76 55.550 -2.606 -3.457 1.00108.04 C ANISOU 521 CD GLU A 76 12382 13560 15108 -476 -515 577 C ATOM 522 OE1 GLU A 76 56.285 -3.048 -2.546 1.00114.20 O ANISOU 522 OE1 GLU A 76 13110 14337 15943 -483 -637 602 O ATOM 523 OE2 GLU A 76 55.901 -2.584 -4.660 1.00111.39 O ANISOU 523 OE2 GLU A 76 12692 14087 15545 -432 -430 518 O ATOM 524 N ASN A 77 51.537 -5.871 -2.357 1.00 41.34 N ANISOU 524 N ASN A 77 4285 4693 6730 -257 -623 588 N ATOM 525 CA ASN A 77 51.554 -7.300 -2.045 1.00 46.58 C ANISOU 525 CA ASN A 77 4945 5264 7488 -182 -726 578 C ATOM 526 C ASN A 77 50.465 -8.107 -2.749 1.00 51.56 C ANISOU 526 C ASN A 77 5610 5841 8139 -130 -687 525 C ATOM 527 O ASN A 77 50.102 -9.196 -2.317 1.00 54.71 O ANISOU 527 O ASN A 77 6067 6128 8591 -109 -762 535 O ATOM 528 CB ASN A 77 51.519 -7.517 -0.528 1.00 47.47 C ANISOU 528 CB ASN A 77 5169 5284 7585 -248 -830 672 C ATOM 529 CG ASN A 77 52.622 -6.742 0.183 1.00 55.30 C ANISOU 529 CG ASN A 77 6126 6334 8550 -309 -885 719 C ATOM 530 OD1 ASN A 77 52.355 -5.870 1.005 1.00 56.39 O ANISOU 530 OD1 ASN A 77 6367 6465 8594 -417 -873 778 O ATOM 531 ND2 ASN A 77 53.867 -7.028 -0.175 1.00 53.37 N ANISOU 531 ND2 ASN A 77 5730 6161 8387 -241 -941 682 N ATOM 532 N VAL A 78 49.952 -7.564 -3.845 1.00 47.60 N ANISOU 532 N VAL A 78 5077 5418 7591 -118 -576 470 N ATOM 533 CA VAL A 78 49.025 -8.295 -4.684 1.00 40.84 C ANISOU 533 CA VAL A 78 4228 4539 6751 -70 -545 403 C ATOM 534 C VAL A 78 49.537 -8.267 -6.105 1.00 44.15 C ANISOU 534 C VAL A 78 4533 5058 7184 15 -484 305 C ATOM 535 O VAL A 78 50.018 -7.238 -6.583 1.00 47.28 O ANISOU 535 O VAL A 78 4878 5563 7524 0 -411 306 O ATOM 536 CB VAL A 78 47.615 -7.698 -4.618 1.00 43.01 C ANISOU 536 CB VAL A 78 4587 4824 6931 -137 -471 434 C ATOM 537 CG1 VAL A 78 46.698 -8.408 -5.597 1.00 40.06 C ANISOU 537 CG1 VAL A 78 4197 4454 6570 -97 -445 356 C ATOM 538 CG2 VAL A 78 47.076 -7.817 -3.195 1.00 44.69 C ANISOU 538 CG2 VAL A 78 4910 4947 7122 -222 -520 525 C ATOM 539 N VAL A 79 49.471 -9.413 -6.767 1.00 47.67 N ANISOU 539 N VAL A 79 4951 5462 7698 100 -514 219 N ATOM 540 CA VAL A 79 49.986 -9.535 -8.122 1.00 48.67 C ANISOU 540 CA VAL A 79 4975 5685 7834 193 -457 111 C ATOM 541 C VAL A 79 49.308 -8.491 -8.987 1.00 51.65 C ANISOU 541 C VAL A 79 5354 6173 8096 155 -342 104 C ATOM 542 O VAL A 79 48.145 -8.130 -8.764 1.00 52.53 O ANISOU 542 O VAL A 79 5548 6264 8145 93 -320 147 O ATOM 543 CB VAL A 79 49.775 -10.961 -8.687 1.00 55.66 C ANISOU 543 CB VAL A 79 5868 6484 8796 285 -508 9 C ATOM 544 CG1 VAL A 79 48.340 -11.162 -9.132 1.00 48.79 C ANISOU 544 CG1 VAL A 79 5075 5588 7874 236 -480 -17 C ATOM 545 CG2 VAL A 79 50.730 -11.233 -9.817 1.00 62.55 C ANISOU 545 CG2 VAL A 79 6623 7447 9696 406 -470 -104 C ATOM 546 N ASN A 80 50.059 -7.981 -9.949 1.00 47.38 N ANISOU 546 N ASN A 80 4722 5757 7522 195 -269 57 N ATOM 547 CA ASN A 80 49.593 -6.907 -10.798 1.00 43.64 C ANISOU 547 CA ASN A 80 4261 5389 6930 164 -163 63 C ATOM 548 C ASN A 80 49.331 -7.316 -12.239 1.00 48.73 C ANISOU 548 C ASN A 80 4867 6109 7540 242 -111 -47 C ATOM 549 O ASN A 80 50.247 -7.658 -12.986 1.00 55.83 O ANISOU 549 O ASN A 80 5672 7079 8461 312 -83 -126 O ATOM 550 CB ASN A 80 50.589 -5.757 -10.790 1.00 44.08 C ANISOU 550 CB ASN A 80 4270 5538 6941 113 -104 115 C ATOM 551 CG ASN A 80 50.152 -4.614 -11.686 1.00 49.67 C ANISOU 551 CG ASN A 80 5016 6337 7519 81 4 133 C ATOM 552 OD1 ASN A 80 49.077 -4.042 -11.499 1.00 55.62 O ANISOU 552 OD1 ASN A 80 5874 7057 8204 49 19 184 O ATOM 553 ND2 ASN A 80 50.977 -4.285 -12.672 1.00 44.81 N ANISOU 553 ND2 ASN A 80 4318 5843 6865 97 80 93 N ATOM 554 N LEU A 81 48.067 -7.257 -12.622 1.00 50.47 N ANISOU 554 N LEU A 81 5154 6326 7696 229 -96 -54 N ATOM 555 CA LEU A 81 47.667 -7.466 -13.998 1.00 52.67 C ANISOU 555 CA LEU A 81 5413 6689 7909 287 -50 -148 C ATOM 556 C LEU A 81 48.017 -6.203 -14.768 1.00 56.04 C ANISOU 556 C LEU A 81 5826 7248 8218 275 54 -115 C ATOM 557 O LEU A 81 47.529 -5.121 -14.451 1.00 55.45 O ANISOU 557 O LEU A 81 5817 7181 8069 218 86 -20 O ATOM 558 CB LEU A 81 46.164 -7.747 -14.069 1.00 42.11 C ANISOU 558 CB LEU A 81 4142 5320 6538 264 -81 -156 C ATOM 559 CG LEU A 81 45.555 -7.934 -15.455 1.00 46.28 C ANISOU 559 CG LEU A 81 4660 5942 6982 311 -51 -250 C ATOM 560 CD1 LEU A 81 46.022 -9.260 -16.100 1.00 40.03 C ANISOU 560 CD1 LEU A 81 3833 5118 6257 381 -87 -391 C ATOM 561 CD2 LEU A 81 44.019 -7.876 -15.363 1.00 39.20 C ANISOU 561 CD2 LEU A 81 3810 5046 6037 268 -80 -227 C ATOM 562 N ILE A 82 48.883 -6.328 -15.765 1.00 55.75 N ANISOU 562 N ILE A 82 5712 7311 8159 328 111 -191 N ATOM 563 CA ILE A 82 49.303 -5.162 -16.523 1.00 51.19 C ANISOU 563 CA ILE A 82 5128 6860 7463 300 216 -152 C ATOM 564 C ILE A 82 48.251 -4.776 -17.546 1.00 52.54 C ANISOU 564 C ILE A 82 5366 7095 7501 320 254 -165 C ATOM 565 O ILE A 82 47.875 -3.618 -17.651 1.00 54.10 O ANISOU 565 O ILE A 82 5635 7323 7596 277 300 -75 O ATOM 566 CB ILE A 82 50.641 -5.395 -17.231 1.00 50.86 C ANISOU 566 CB ILE A 82 4967 6928 7431 342 278 -226 C ATOM 567 CG1 ILE A 82 51.758 -5.530 -16.197 1.00 49.09 C ANISOU 567 CG1 ILE A 82 4660 6669 7324 317 240 -193 C ATOM 568 CG2 ILE A 82 50.933 -4.250 -18.183 1.00 36.69 C ANISOU 568 CG2 ILE A 82 3181 5270 5490 298 396 -187 C ATOM 569 CD1 ILE A 82 52.940 -6.311 -16.701 1.00 53.32 C ANISOU 569 CD1 ILE A 82 5049 7288 7922 406 262 -300 C ATOM 570 N GLU A 83 47.776 -5.758 -18.298 1.00 57.52 N ANISOU 570 N GLU A 83 5981 7742 8131 389 225 -280 N ATOM 571 CA GLU A 83 46.811 -5.510 -19.357 1.00 45.51 C ANISOU 571 CA GLU A 83 4510 6302 6480 415 246 -307 C ATOM 572 C GLU A 83 46.323 -6.841 -19.887 1.00 52.97 C ANISOU 572 C GLU A 83 5438 7228 7459 471 184 -446 C ATOM 573 O GLU A 83 46.829 -7.905 -19.503 1.00 55.53 O ANISOU 573 O GLU A 83 5723 7469 7906 500 137 -521 O ATOM 574 CB GLU A 83 47.459 -4.735 -20.507 1.00 44.59 C ANISOU 574 CB GLU A 83 4385 6330 6228 426 355 -307 C ATOM 575 CG GLU A 83 48.489 -5.564 -21.298 1.00 52.77 C ANISOU 575 CG GLU A 83 5327 7441 7281 487 398 -438 C ATOM 576 CD GLU A 83 49.126 -4.782 -22.448 1.00 62.71 C ANISOU 576 CD GLU A 83 6577 8862 8389 483 521 -433 C ATOM 577 OE1 GLU A 83 48.451 -3.909 -23.029 1.00 71.99 O ANISOU 577 OE1 GLU A 83 7841 10092 9421 461 551 -366 O ATOM 578 OE2 GLU A 83 50.302 -5.045 -22.780 1.00 60.71 O ANISOU 578 OE2 GLU A 83 6225 8687 8154 504 589 -495 O ATOM 579 N ILE A 84 45.344 -6.771 -20.782 1.00 57.51 N ANISOU 579 N ILE A 84 6051 7876 7922 489 178 -482 N ATOM 580 CA ILE A 84 44.856 -7.945 -21.495 1.00 53.09 C ANISOU 580 CA ILE A 84 5489 7319 7365 529 122 -627 C ATOM 581 C ILE A 84 45.155 -7.828 -22.987 1.00 52.46 C ANISOU 581 C ILE A 84 5405 7387 7141 586 190 -713 C ATOM 582 O ILE A 84 44.924 -6.785 -23.594 1.00 58.16 O ANISOU 582 O ILE A 84 6159 8219 7720 581 245 -643 O ATOM 583 CB ILE A 84 43.355 -8.156 -21.229 1.00 49.67 C ANISOU 583 CB ILE A 84 5091 6854 6926 486 35 -612 C ATOM 584 CG1 ILE A 84 43.185 -8.659 -19.799 1.00 45.42 C ANISOU 584 CG1 ILE A 84 4555 6161 6541 428 -31 -562 C ATOM 585 CG2 ILE A 84 42.752 -9.130 -22.238 1.00 48.63 C ANISOU 585 CG2 ILE A 84 4967 6762 6749 508 -17 -761 C ATOM 586 CD1 ILE A 84 42.112 -7.961 -19.050 1.00 51.80 C ANISOU 586 CD1 ILE A 84 5386 6967 7331 372 -53 -447 C ATOM 587 N CYS A 85 45.694 -8.893 -23.570 1.00 52.43 N ANISOU 587 N CYS A 85 5375 7380 7167 645 188 -865 N ATOM 588 CA CYS A 85 46.124 -8.837 -24.956 1.00 50.48 C ANISOU 588 CA CYS A 85 5123 7280 6777 703 267 -959 C ATOM 589 C CYS A 85 45.392 -9.852 -25.812 1.00 57.17 C ANISOU 589 C CYS A 85 6010 8135 7575 736 201 -1118 C ATOM 590 O CYS A 85 44.993 -10.919 -25.339 1.00 62.14 O ANISOU 590 O CYS A 85 6657 8631 8323 728 106 -1193 O ATOM 591 CB CYS A 85 47.645 -9.019 -25.056 1.00 64.22 C ANISOU 591 CB CYS A 85 6783 9054 8563 759 357 -1010 C ATOM 592 SG CYS A 85 48.612 -7.528 -24.578 1.00 61.02 S ANISOU 592 SG CYS A 85 6330 8722 8133 695 468 -833 S ATOM 593 N ARG A 86 45.204 -9.498 -27.076 1.00 58.33 N ANISOU 593 N ARG A 86 6187 8438 7540 762 248 -1164 N ATOM 594 CA ARG A 86 44.520 -10.355 -28.032 1.00 56.67 C ANISOU 594 CA ARG A 86 6023 8261 7248 785 187 -1321 C ATOM 595 C ARG A 86 45.518 -10.971 -29.003 1.00 66.52 C ANISOU 595 C ARG A 86 7261 9576 8438 874 267 -1485 C ATOM 596 O ARG A 86 46.730 -10.795 -28.880 1.00 57.89 O ANISOU 596 O ARG A 86 6105 8508 7384 919 368 -1476 O ATOM 597 CB ARG A 86 43.511 -9.538 -28.843 1.00 49.23 C ANISOU 597 CB ARG A 86 5127 7464 6114 761 169 -1265 C ATOM 598 CG ARG A 86 44.173 -8.436 -29.654 1.00 55.98 C ANISOU 598 CG ARG A 86 5994 8478 6798 789 296 -1194 C ATOM 599 CD ARG A 86 43.190 -7.581 -30.426 1.00 68.52 C ANISOU 599 CD ARG A 86 7645 10199 8192 781 268 -1121 C ATOM 600 NE ARG A 86 43.765 -6.266 -30.715 1.00 81.50 N ANISOU 600 NE ARG A 86 9319 11935 9714 779 382 -978 N ATOM 601 CZ ARG A 86 44.132 -5.839 -31.922 1.00 87.75 C ANISOU 601 CZ ARG A 86 10158 12880 10303 805 464 -994 C ATOM 602 NH1 ARG A 86 43.979 -6.621 -32.981 1.00 89.14 N ANISOU 602 NH1 ARG A 86 10355 13147 10367 845 446 -1157 N ATOM 603 NH2 ARG A 86 44.643 -4.620 -32.071 1.00 87.75 N ANISOU 603 NH2 ARG A 86 10198 12940 10202 780 566 -845 N ATOM 604 N THR A 87 44.966 -11.665 -29.990 1.00 79.84 N ANISOU 604 N THR A 87 9006 11308 10022 896 221 -1637 N ATOM 605 CA THR A 87 45.709 -12.315 -31.043 1.00 84.69 C ANISOU 605 CA THR A 87 9633 11994 10551 987 290 -1819 C ATOM 606 C THR A 87 44.640 -13.017 -31.838 1.00 96.49 C ANISOU 606 C THR A 87 11215 13501 11946 966 185 -1956 C ATOM 607 O THR A 87 44.471 -12.792 -33.035 1.00109.37 O ANISOU 607 O THR A 87 12889 15293 13372 986 218 -2022 O ATOM 608 CB THR A 87 46.581 -13.407 -30.482 1.00 89.76 C ANISOU 608 CB THR A 87 10244 12483 11376 1062 288 -1933 C ATOM 609 OG1 THR A 87 47.614 -13.716 -31.424 1.00109.33 O ANISOU 609 OG1 THR A 87 12701 15071 13769 1174 405 -2078 O ATOM 610 CG2 THR A 87 45.743 -14.648 -30.222 1.00 73.33 C ANISOU 610 CG2 THR A 87 8244 10223 9393 1037 141 -2052 C ATOM 611 N SER A 98 42.372 -15.667 -29.626 1.00 92.62 N ANISOU 611 N SER A 98 10827 12477 11888 756 -211 -2058 N ATOM 612 CA SER A 98 42.627 -15.890 -28.202 1.00 90.12 C ANISOU 612 CA SER A 98 10485 11975 11783 728 -237 -1956 C ATOM 613 C SER A 98 42.800 -14.615 -27.369 1.00 81.23 C ANISOU 613 C SER A 98 9274 10907 10682 708 -176 -1735 C ATOM 614 O SER A 98 42.746 -13.498 -27.884 1.00 88.42 O ANISOU 614 O SER A 98 10151 11992 11452 719 -108 -1650 O ATOM 615 CB SER A 98 43.851 -16.782 -28.015 1.00 93.03 C ANISOU 615 CB SER A 98 10874 12201 12271 842 -202 -2067 C ATOM 616 OG SER A 98 43.586 -18.089 -28.481 1.00106.12 O ANISOU 616 OG SER A 98 12640 13734 13947 848 -282 -2264 O ATOM 617 N ILE A 99 43.015 -14.813 -26.073 1.00 63.07 N ANISOU 617 N ILE A 99 6959 8448 8558 678 -204 -1645 N ATOM 618 CA ILE A 99 43.178 -13.729 -25.117 1.00 57.43 C ANISOU 618 CA ILE A 99 6182 7754 7886 650 -160 -1447 C ATOM 619 C ILE A 99 44.224 -14.109 -24.067 1.00 57.43 C ANISOU 619 C ILE A 99 6162 7602 8059 690 -149 -1413 C ATOM 620 O ILE A 99 44.338 -15.274 -23.680 1.00 62.21 O ANISOU 620 O ILE A 99 6816 8036 8785 701 -220 -1498 O ATOM 621 CB ILE A 99 41.830 -13.394 -24.438 1.00 59.27 C ANISOU 621 CB ILE A 99 6415 7976 8130 529 -238 -1334 C ATOM 622 CG1 ILE A 99 40.953 -12.596 -25.398 1.00 63.90 C ANISOU 622 CG1 ILE A 99 6990 8757 8532 516 -233 -1317 C ATOM 623 CG2 ILE A 99 42.029 -12.629 -23.137 1.00 48.82 C ANISOU 623 CG2 ILE A 99 5055 6598 6897 497 -213 -1153 C ATOM 624 CD1 ILE A 99 41.624 -11.359 -25.945 1.00 59.60 C ANISOU 624 CD1 ILE A 99 6423 8360 7863 587 -119 -1237 C ATOM 625 N TYR A 100 44.993 -13.126 -23.614 1.00 52.35 N ANISOU 625 N TYR A 100 5453 7018 7421 711 -67 -1287 N ATOM 626 CA TYR A 100 46.037 -13.375 -22.635 1.00 54.85 C ANISOU 626 CA TYR A 100 5732 7222 7887 751 -62 -1246 C ATOM 627 C TYR A 100 45.936 -12.369 -21.511 1.00 56.19 C ANISOU 627 C TYR A 100 5874 7382 8093 673 -55 -1054 C ATOM 628 O TYR A 100 45.764 -11.166 -21.752 1.00 55.90 O ANISOU 628 O TYR A 100 5818 7474 7946 641 11 -958 O ATOM 629 CB TYR A 100 47.433 -13.215 -23.259 1.00 59.98 C ANISOU 629 CB TYR A 100 6306 7975 8509 866 45 -1308 C ATOM 630 CG TYR A 100 47.822 -14.218 -24.316 1.00 60.35 C ANISOU 630 CG TYR A 100 6372 8032 8525 976 59 -1512 C ATOM 631 CD1 TYR A 100 48.644 -15.293 -24.007 1.00 65.33 C ANISOU 631 CD1 TYR A 100 6997 8534 9291 1084 28 -1614 C ATOM 632 CD2 TYR A 100 47.395 -14.075 -25.627 1.00 64.40 C ANISOU 632 CD2 TYR A 100 6916 8686 8868 985 102 -1605 C ATOM 633 CE1 TYR A 100 49.019 -16.205 -24.967 1.00 64.26 C ANISOU 633 CE1 TYR A 100 6890 8399 9125 1203 47 -1813 C ATOM 634 CE2 TYR A 100 47.768 -14.988 -26.601 1.00 70.73 C ANISOU 634 CE2 TYR A 100 7747 9500 9628 1089 121 -1805 C ATOM 635 CZ TYR A 100 48.582 -16.051 -26.266 1.00 69.65 C ANISOU 635 CZ TYR A 100 7608 9225 9632 1201 97 -1913 C ATOM 636 OH TYR A 100 48.955 -16.968 -27.231 1.00 78.56 O ANISOU 636 OH TYR A 100 8777 10354 10717 1322 119 -2124 O ATOM 637 N LEU A 101 46.070 -12.852 -20.282 1.00 50.06 N ANISOU 637 N LEU A 101 5112 6446 7463 647 -123 -999 N ATOM 638 CA LEU A 101 46.256 -11.954 -19.162 1.00 48.30 C ANISOU 638 CA LEU A 101 4864 6210 7278 588 -110 -833 C ATOM 639 C LEU A 101 47.750 -11.705 -19.041 1.00 56.25 C ANISOU 639 C LEU A 101 5789 7256 8328 661 -50 -825 C ATOM 640 O LEU A 101 48.534 -12.652 -19.013 1.00 47.71 O ANISOU 640 O LEU A 101 4684 6102 7340 749 -78 -916 O ATOM 641 CB LEU A 101 45.690 -12.561 -17.875 1.00 55.71 C ANISOU 641 CB LEU A 101 5859 6973 8335 515 -211 -770 C ATOM 642 CG LEU A 101 44.181 -12.363 -17.661 1.00 51.17 C ANISOU 642 CG LEU A 101 5331 6402 7711 407 -249 -717 C ATOM 643 CD1 LEU A 101 43.410 -13.036 -18.756 1.00 42.49 C ANISOU 643 CD1 LEU A 101 4258 5337 6550 407 -278 -849 C ATOM 644 CD2 LEU A 101 43.757 -12.902 -16.315 1.00 49.45 C ANISOU 644 CD2 LEU A 101 5163 6024 7601 324 -329 -641 C ATOM 645 N VAL A 102 48.149 -10.436 -19.000 1.00 54.64 N ANISOU 645 N VAL A 102 5541 7167 8053 625 32 -720 N ATOM 646 CA VAL A 102 49.560 -10.106 -18.849 1.00 52.92 C ANISOU 646 CA VAL A 102 5227 7010 7872 665 90 -703 C ATOM 647 C VAL A 102 49.911 -9.659 -17.427 1.00 54.16 C ANISOU 647 C VAL A 102 5374 7088 8116 598 48 -567 C ATOM 648 O VAL A 102 49.392 -8.652 -16.958 1.00 59.43 O ANISOU 648 O VAL A 102 6087 7764 8727 505 63 -448 O ATOM 649 CB VAL A 102 49.995 -9.016 -19.847 1.00 49.09 C ANISOU 649 CB VAL A 102 4697 6715 7241 654 219 -687 C ATOM 650 CG1 VAL A 102 51.511 -8.879 -19.834 1.00 44.64 C ANISOU 650 CG1 VAL A 102 4006 6238 6719 693 284 -699 C ATOM 651 CG2 VAL A 102 49.505 -9.360 -21.237 1.00 45.02 C ANISOU 651 CG2 VAL A 102 4211 6286 6610 708 255 -808 C ATOM 652 N PHE A 103 50.798 -10.398 -16.755 1.00 50.73 N ANISOU 652 N PHE A 103 4887 6577 7811 656 -8 -590 N ATOM 653 CA PHE A 103 51.282 -10.010 -15.423 1.00 53.71 C ANISOU 653 CA PHE A 103 5248 6895 8264 598 -56 -468 C ATOM 654 C PHE A 103 52.777 -9.672 -15.377 1.00 59.19 C ANISOU 654 C PHE A 103 5801 7698 8990 633 -13 -465 C ATOM 655 O PHE A 103 53.587 -10.283 -16.083 1.00 58.16 O ANISOU 655 O PHE A 103 5573 7637 8888 748 18 -578 O ATOM 656 CB PHE A 103 51.063 -11.134 -14.413 1.00 56.13 C ANISOU 656 CB PHE A 103 5615 7012 8699 622 -186 -467 C ATOM 657 CG PHE A 103 49.657 -11.662 -14.358 1.00 53.03 C ANISOU 657 CG PHE A 103 5346 6508 8295 574 -238 -476 C ATOM 658 CD1 PHE A 103 48.778 -11.219 -13.384 1.00 48.09 C ANISOU 658 CD1 PHE A 103 4800 5817 7656 459 -273 -358 C ATOM 659 CD2 PHE A 103 49.231 -12.634 -15.249 1.00 54.23 C ANISOU 659 CD2 PHE A 103 5533 6625 8448 637 -254 -610 C ATOM 660 CE1 PHE A 103 47.488 -11.725 -13.308 1.00 54.71 C ANISOU 660 CE1 PHE A 103 5728 6574 8485 403 -317 -366 C ATOM 661 CE2 PHE A 103 47.936 -13.140 -15.181 1.00 63.76 C ANISOU 661 CE2 PHE A 103 6842 7739 9646 569 -308 -620 C ATOM 662 CZ PHE A 103 47.067 -12.690 -14.207 1.00 58.20 C ANISOU 662 CZ PHE A 103 6194 6987 8932 449 -337 -495 C ATOM 663 N ASP A 104 53.144 -8.723 -14.517 1.00 63.65 N ANISOU 663 N ASP A 104 6351 8283 9551 533 -13 -341 N ATOM 664 CA ASP A 104 54.543 -8.540 -14.121 1.00 63.46 C ANISOU 664 CA ASP A 104 6185 8340 9586 544 -12 -323 C ATOM 665 C ASP A 104 55.111 -9.910 -13.732 1.00 63.50 C ANISOU 665 C ASP A 104 6136 8258 9732 686 -114 -399 C ATOM 666 O ASP A 104 54.496 -10.639 -12.957 1.00 70.33 O ANISOU 666 O ASP A 104 7106 8949 10665 698 -223 -377 O ATOM 667 CB ASP A 104 54.640 -7.573 -12.932 1.00 73.14 C ANISOU 667 CB ASP A 104 7446 9537 10806 406 -47 -178 C ATOM 668 CG ASP A 104 54.602 -6.088 -13.349 1.00 85.78 C ANISOU 668 CG ASP A 104 9069 11248 12276 278 65 -106 C ATOM 669 OD1 ASP A 104 55.263 -5.719 -14.345 1.00 90.93 O ANISOU 669 OD1 ASP A 104 9625 12055 12870 283 169 -151 O ATOM 670 OD2 ASP A 104 53.931 -5.282 -12.659 1.00 81.50 O ANISOU 670 OD2 ASP A 104 8648 10634 11686 171 51 -4 O ATOM 671 N PHE A 105 56.270 -10.274 -14.273 1.00 64.40 N ANISOU 671 N PHE A 105 6091 8492 9887 799 -78 -488 N ATOM 672 CA PHE A 105 56.856 -11.597 -14.013 1.00 64.85 C ANISOU 672 CA PHE A 105 6098 8465 10077 970 -173 -574 C ATOM 673 C PHE A 105 57.451 -11.739 -12.606 1.00 72.43 C ANISOU 673 C PHE A 105 7027 9350 11142 964 -302 -478 C ATOM 674 O PHE A 105 58.045 -10.797 -12.082 1.00 74.07 O ANISOU 674 O PHE A 105 7151 9662 11328 859 -290 -386 O ATOM 675 CB PHE A 105 57.919 -11.919 -15.065 1.00 57.19 C ANISOU 675 CB PHE A 105 4951 7666 9111 1114 -83 -709 C ATOM 676 CG PHE A 105 58.592 -13.249 -14.872 1.00 54.80 C ANISOU 676 CG PHE A 105 4593 7284 8944 1324 -175 -808 C ATOM 677 CD1 PHE A 105 57.966 -14.418 -15.253 1.00 55.60 C ANISOU 677 CD1 PHE A 105 4824 7220 9083 1444 -224 -917 C ATOM 678 CD2 PHE A 105 59.878 -13.323 -14.336 1.00 60.60 C ANISOU 678 CD2 PHE A 105 5143 8114 9767 1406 -216 -796 C ATOM 679 CE1 PHE A 105 58.605 -15.652 -15.091 1.00 63.98 C ANISOU 679 CE1 PHE A 105 5856 8183 10268 1654 -311 -1012 C ATOM 680 CE2 PHE A 105 60.530 -14.553 -14.171 1.00 55.59 C ANISOU 680 CE2 PHE A 105 4456 7406 9260 1630 -307 -888 C ATOM 681 CZ PHE A 105 59.894 -15.715 -14.546 1.00 57.43 C ANISOU 681 CZ PHE A 105 4844 7448 9530 1760 -354 -995 C ATOM 682 N CYS A 106 57.273 -12.914 -11.999 1.00 72.07 N ANISOU 682 N CYS A 106 7064 9117 11202 1069 -432 -497 N ATOM 683 CA CYS A 106 57.809 -13.196 -10.666 1.00 70.32 C ANISOU 683 CA CYS A 106 6833 8810 11074 1083 -574 -406 C ATOM 684 C CYS A 106 58.537 -14.531 -10.700 1.00 79.32 C ANISOU 684 C CYS A 106 7922 9877 12340 1311 -663 -503 C ATOM 685 O CYS A 106 57.962 -15.562 -11.070 1.00 72.26 O ANISOU 685 O CYS A 106 7151 8823 11480 1408 -695 -588 O ATOM 686 CB CYS A 106 56.711 -13.213 -9.587 1.00 70.90 C ANISOU 686 CB CYS A 106 7111 8690 11138 956 -664 -287 C ATOM 687 SG CYS A 106 55.596 -11.713 -9.486 1.00 97.97 S ANISOU 687 SG CYS A 106 10640 12166 14418 714 -565 -179 S ATOM 688 N GLU A 107 59.809 -14.499 -10.312 1.00 85.91 N ANISOU 688 N GLU A 107 8574 10827 13239 1397 -708 -494 N ATOM 689 CA GLU A 107 60.692 -15.648 -10.436 1.00 80.86 C ANISOU 689 CA GLU A 107 7843 10162 12717 1647 -780 -595 C ATOM 690 C GLU A 107 60.333 -16.773 -9.462 1.00 78.33 C ANISOU 690 C GLU A 107 7705 9565 12493 1732 -961 -550 C ATOM 691 O GLU A 107 60.244 -17.941 -9.849 1.00 74.27 O ANISOU 691 O GLU A 107 7272 8902 12046 1909 -1004 -654 O ATOM 692 CB GLU A 107 62.143 -15.198 -10.230 1.00 97.95 C ANISOU 692 CB GLU A 107 9736 12560 14920 1703 -782 -585 C ATOM 693 CG GLU A 107 63.173 -16.325 -10.281 1.00108.45 C ANISOU 693 CG GLU A 107 10937 13893 16378 1990 -864 -685 C ATOM 694 CD GLU A 107 63.325 -16.924 -11.667 1.00113.93 C ANISOU 694 CD GLU A 107 11573 14646 17068 2169 -743 -875 C ATOM 695 OE1 GLU A 107 63.496 -16.150 -12.637 1.00118.86 O ANISOU 695 OE1 GLU A 107 12071 15491 17599 2094 -571 -930 O ATOM 696 OE2 GLU A 107 63.277 -18.169 -11.783 1.00109.64 O ANISOU 696 OE2 GLU A 107 11126 13923 16609 2383 -820 -968 O ATOM 697 N HIS A 108 60.113 -16.420 -8.200 1.00 81.56 N ANISOU 697 N HIS A 108 8195 9896 12898 1599 -1065 -393 N ATOM 698 CA HIS A 108 59.935 -17.428 -7.156 1.00 80.59 C ANISOU 698 CA HIS A 108 8234 9528 12857 1671 -1245 -326 C ATOM 699 C HIS A 108 58.515 -17.555 -6.609 1.00 72.53 C ANISOU 699 C HIS A 108 7478 8292 11786 1501 -1275 -239 C ATOM 700 O HIS A 108 57.669 -16.688 -6.807 1.00 67.01 O ANISOU 700 O HIS A 108 6826 7647 10986 1312 -1172 -204 O ATOM 701 CB HIS A 108 60.895 -17.153 -5.997 1.00 83.11 C ANISOU 701 CB HIS A 108 8446 9916 13216 1680 -1372 -213 C ATOM 702 CG HIS A 108 62.277 -16.807 -6.442 1.00 93.15 C ANISOU 702 CG HIS A 108 9420 11450 14524 1798 -1334 -280 C ATOM 703 ND1 HIS A 108 62.711 -15.503 -6.570 1.00 91.06 N ANISOU 703 ND1 HIS A 108 8982 11433 14184 1637 -1234 -246 N ATOM 704 CD2 HIS A 108 63.314 -17.591 -6.818 1.00 92.82 C ANISOU 704 CD2 HIS A 108 9217 11469 14582 2059 -1374 -384 C ATOM 705 CE1 HIS A 108 63.962 -15.502 -6.995 1.00 91.45 C ANISOU 705 CE1 HIS A 108 8765 11698 14285 1775 -1213 -321 C ATOM 706 NE2 HIS A 108 64.350 -16.755 -7.157 1.00 93.72 N ANISOU 706 NE2 HIS A 108 9043 11885 14679 2043 -1294 -409 N ATOM 707 N ASP A 109 58.285 -18.654 -5.902 1.00 71.10 N ANISOU 707 N ASP A 109 7469 7869 11676 1575 -1420 -201 N ATOM 708 CA ASP A 109 57.056 -18.882 -5.174 1.00 74.56 C ANISOU 708 CA ASP A 109 8151 8104 12075 1412 -1469 -100 C ATOM 709 C ASP A 109 57.359 -19.621 -3.860 1.00 74.11 C ANISOU 709 C ASP A 109 8213 7865 12079 1464 -1658 19 C ATOM 710 O ASP A 109 58.192 -20.524 -3.817 1.00 79.47 O ANISOU 710 O ASP A 109 8870 8467 12859 1681 -1765 -23 O ATOM 711 CB ASP A 109 56.083 -19.680 -6.030 1.00 84.70 C ANISOU 711 CB ASP A 109 9584 9236 13363 1420 -1422 -206 C ATOM 712 CG ASP A 109 56.497 -21.113 -6.182 1.00 99.71 C ANISOU 712 CG ASP A 109 11571 10937 15377 1638 -1531 -289 C ATOM 713 OD1 ASP A 109 57.436 -21.380 -6.964 1.00114.12 O ANISOU 713 OD1 ASP A 109 13248 12856 17257 1847 -1504 -418 O ATOM 714 OD2 ASP A 109 55.882 -21.970 -5.512 1.00103.73 O ANISOU 714 OD2 ASP A 109 12303 11194 15915 1601 -1639 -224 O ATOM 715 N LEU A 110 56.679 -19.221 -2.793 1.00 67.96 N ANISOU 715 N LEU A 110 7566 7023 11232 1271 -1697 167 N ATOM 716 CA LEU A 110 56.919 -19.762 -1.464 1.00 65.65 C ANISOU 716 CA LEU A 110 7398 6578 10966 1286 -1872 302 C ATOM 717 C LEU A 110 56.999 -21.295 -1.417 1.00 70.41 C ANISOU 717 C LEU A 110 8161 6920 11672 1462 -2002 275 C ATOM 718 O LEU A 110 57.826 -21.847 -0.691 1.00 72.45 O ANISOU 718 O LEU A 110 8429 7106 11991 1606 -2159 335 O ATOM 719 CB LEU A 110 55.859 -19.238 -0.498 1.00 65.97 C ANISOU 719 CB LEU A 110 7603 6564 10899 1035 -1862 444 C ATOM 720 CG LEU A 110 56.274 -19.006 0.949 1.00 68.44 C ANISOU 720 CG LEU A 110 7965 6865 11175 980 -1994 603 C ATOM 721 CD1 LEU A 110 57.655 -18.362 1.019 1.00 73.69 C ANISOU 721 CD1 LEU A 110 8392 7742 11865 1080 -2034 592 C ATOM 722 CD2 LEU A 110 55.229 -18.147 1.655 1.00 64.26 C ANISOU 722 CD2 LEU A 110 7546 6358 10514 724 -1923 707 C ATOM 723 N ALA A 111 56.157 -21.987 -2.181 1.00 68.41 N ANISOU 723 N ALA A 111 8039 6519 11434 1454 -1947 184 N ATOM 724 CA ALA A 111 56.210 -23.452 -2.197 1.00 67.45 C ANISOU 724 CA ALA A 111 8097 6122 11408 1615 -2067 146 C ATOM 725 C ALA A 111 57.560 -23.966 -2.717 1.00 78.15 C ANISOU 725 C ALA A 111 9298 7521 12873 1929 -2125 33 C ATOM 726 O ALA A 111 58.140 -24.912 -2.158 1.00 80.00 O ANISOU 726 O ALA A 111 9629 7578 13191 2109 -2287 70 O ATOM 727 CB ALA A 111 55.068 -24.039 -3.008 1.00 58.25 C ANISOU 727 CB ALA A 111 7092 4808 10234 1529 -1992 52 C ATOM 728 N GLY A 112 58.048 -23.341 -3.788 1.00 73.86 N ANISOU 728 N GLY A 112 8519 7220 12326 2000 -1990 -103 N ATOM 729 CA GLY A 112 59.350 -23.665 -4.346 1.00 73.60 C ANISOU 729 CA GLY A 112 8290 7293 12383 2288 -2011 -221 C ATOM 730 C GLY A 112 60.516 -23.379 -3.411 1.00 79.50 C ANISOU 730 C GLY A 112 8879 8161 13167 2389 -2134 -119 C ATOM 731 O GLY A 112 61.373 -24.247 -3.190 1.00 84.24 O ANISOU 731 O GLY A 112 9467 8673 13867 2648 -2270 -140 O ATOM 732 N LEU A 113 60.554 -22.166 -2.862 1.00 72.97 N ANISOU 732 N LEU A 113 7934 7534 12256 2192 -2095 -13 N ATOM 733 CA LEU A 113 61.636 -21.772 -1.970 1.00 74.11 C ANISOU 733 CA LEU A 113 7917 7823 12419 2250 -2213 83 C ATOM 734 C LEU A 113 61.677 -22.667 -0.724 1.00 85.35 C ANISOU 734 C LEU A 113 9548 9000 13881 2319 -2433 220 C ATOM 735 O LEU A 113 62.749 -23.021 -0.228 1.00 92.65 O ANISOU 735 O LEU A 113 10366 9961 14875 2518 -2581 249 O ATOM 736 CB LEU A 113 61.505 -20.300 -1.581 1.00 70.41 C ANISOU 736 CB LEU A 113 7339 7575 11837 1988 -2130 171 C ATOM 737 CG LEU A 113 61.415 -19.287 -2.734 1.00 71.80 C ANISOU 737 CG LEU A 113 7338 7988 11956 1888 -1915 64 C ATOM 738 CD1 LEU A 113 60.827 -17.940 -2.286 1.00 58.16 C ANISOU 738 CD1 LEU A 113 5626 6372 10102 1594 -1833 166 C ATOM 739 CD2 LEU A 113 62.771 -19.081 -3.391 1.00 71.54 C ANISOU 739 CD2 LEU A 113 6990 8211 11982 2065 -1880 -40 C ATOM 740 N LEU A 114 60.505 -23.046 -0.234 1.00 79.57 N ANISOU 740 N LEU A 114 9109 8025 13101 2156 -2455 307 N ATOM 741 CA LEU A 114 60.416 -23.862 0.965 1.00 82.04 C ANISOU 741 CA LEU A 114 9654 8091 13427 2183 -2651 455 C ATOM 742 C LEU A 114 60.781 -25.333 0.709 1.00 91.54 C ANISOU 742 C LEU A 114 10985 9042 14752 2469 -2774 390 C ATOM 743 O LEU A 114 61.232 -26.038 1.620 1.00 81.21 O ANISOU 743 O LEU A 114 9796 7578 13484 2597 -2969 497 O ATOM 744 CB LEU A 114 59.016 -23.758 1.577 1.00 81.41 C ANISOU 744 CB LEU A 114 9839 7851 13243 1892 -2617 572 C ATOM 745 CG LEU A 114 58.681 -22.455 2.302 1.00 78.83 C ANISOU 745 CG LEU A 114 9459 7707 12787 1631 -2558 686 C ATOM 746 CD1 LEU A 114 57.314 -22.545 2.959 1.00 72.85 C ANISOU 746 CD1 LEU A 114 8970 6775 11934 1382 -2535 799 C ATOM 747 CD2 LEU A 114 59.751 -22.118 3.327 1.00 81.05 C ANISOU 747 CD2 LEU A 114 9633 8103 13059 1693 -2711 794 C ATOM 748 N SER A 115 60.579 -25.795 -0.523 1.00 94.63 N ANISOU 748 N SER A 115 11370 9387 15197 2572 -2665 214 N ATOM 749 CA SER A 115 60.927 -27.164 -0.879 1.00 92.96 C ANISOU 749 CA SER A 115 11289 8931 15101 2856 -2767 125 C ATOM 750 C SER A 115 62.373 -27.225 -1.363 1.00100.65 C ANISOU 750 C SER A 115 11973 10100 16170 3182 -2795 9 C ATOM 751 O SER A 115 62.788 -28.196 -2.000 1.00105.25 O ANISOU 751 O SER A 115 12589 10552 16850 3459 -2828 -125 O ATOM 752 CB SER A 115 59.989 -27.704 -1.957 1.00 88.94 C ANISOU 752 CB SER A 115 10936 8262 14596 2809 -2646 -21 C ATOM 753 OG SER A 115 60.375 -27.238 -3.241 1.00 91.66 O ANISOU 753 OG SER A 115 11032 8846 14950 2899 -2481 -210 O ATOM 754 N ASN A 116 63.135 -26.181 -1.059 1.00100.19 N ANISOU 754 N ASN A 116 11629 10360 16080 3146 -2779 55 N ATOM 755 CA ASN A 116 64.532 -26.107 -1.465 1.00106.34 C ANISOU 755 CA ASN A 116 12085 11380 16939 3422 -2795 -45 C ATOM 756 C ASN A 116 65.472 -26.000 -0.259 1.00114.28 C ANISOU 756 C ASN A 116 12987 12470 17965 3510 -2996 103 C ATOM 757 O ASN A 116 65.547 -24.953 0.394 1.00114.76 O ANISOU 757 O ASN A 116 12935 12727 17943 3293 -2994 215 O ATOM 758 CB ASN A 116 64.740 -24.931 -2.420 1.00102.18 C ANISOU 758 CB ASN A 116 11256 11208 16358 3308 -2577 -155 C ATOM 759 CG ASN A 116 66.093 -24.962 -3.101 1.00106.41 C ANISOU 759 CG ASN A 116 11454 11999 16976 3594 -2551 -295 C ATOM 760 OD1 ASN A 116 67.107 -25.314 -2.493 1.00110.78 O ANISOU 760 OD1 ASN A 116 11884 12601 17605 3812 -2713 -254 O ATOM 761 ND2 ASN A 116 66.117 -24.584 -4.371 1.00103.83 N ANISOU 761 ND2 ASN A 116 10968 11853 16630 3596 -2346 -460 N ATOM 762 N VAL A 117 66.188 -27.086 0.028 1.00110.73 N ANISOU 762 N VAL A 117 12584 11867 17622 3834 -3177 98 N ATOM 763 CA VAL A 117 67.047 -27.148 1.206 1.00111.92 C ANISOU 763 CA VAL A 117 12668 12064 17792 3946 -3401 246 C ATOM 764 C VAL A 117 68.141 -26.077 1.217 1.00111.61 C ANISOU 764 C VAL A 117 12206 12457 17744 3944 -3374 230 C ATOM 765 O VAL A 117 68.570 -25.637 2.284 1.00115.51 O ANISOU 765 O VAL A 117 12637 13055 18196 3870 -3519 378 O ATOM 766 CB VAL A 117 67.689 -28.546 1.375 1.00115.89 C ANISOU 766 CB VAL A 117 13283 12330 18421 4345 -3600 226 C ATOM 767 CG1 VAL A 117 66.612 -29.601 1.588 1.00117.56 C ANISOU 767 CG1 VAL A 117 13953 12084 18631 4306 -3661 280 C ATOM 768 CG2 VAL A 117 68.557 -28.889 0.171 1.00111.16 C ANISOU 768 CG2 VAL A 117 12423 11882 17932 4674 -3511 0 C ATOM 769 N LEU A 118 68.586 -25.658 0.036 1.00106.01 N ANISOU 769 N LEU A 118 11213 12001 17064 4010 -3189 51 N ATOM 770 CA LEU A 118 69.630 -24.640 -0.063 1.00106.01 C ANISOU 770 CA LEU A 118 10801 12423 17056 3987 -3142 25 C ATOM 771 C LEU A 118 69.113 -23.266 0.348 1.00105.62 C ANISOU 771 C LEU A 118 10729 12532 16871 3577 -3050 131 C ATOM 772 O LEU A 118 69.870 -22.439 0.852 1.00108.98 O ANISOU 772 O LEU A 118 10912 13230 17267 3491 -3099 191 O ATOM 773 CB LEU A 118 70.209 -24.583 -1.481 1.00112.09 C ANISOU 773 CB LEU A 118 11288 13420 17881 4156 -2951 -194 C ATOM 774 CG LEU A 118 70.922 -25.839 -2.004 1.00116.13 C ANISOU 774 CG LEU A 118 11753 13841 18529 4602 -3020 -334 C ATOM 775 CD1 LEU A 118 71.402 -25.632 -3.438 1.00116.82 C ANISOU 775 CD1 LEU A 118 11561 14186 18640 4721 -2794 -554 C ATOM 776 CD2 LEU A 118 72.081 -26.252 -1.091 1.00108.83 C ANISOU 776 CD2 LEU A 118 10667 12996 17689 4868 -3266 -255 C ATOM 777 N VAL A 119 67.821 -23.034 0.121 1.00103.14 N ANISOU 777 N VAL A 119 10670 12046 16474 3329 -2920 146 N ATOM 778 CA VAL A 119 67.162 -21.785 0.489 1.00 91.89 C ANISOU 778 CA VAL A 119 9276 10723 14916 2954 -2825 241 C ATOM 779 C VAL A 119 66.974 -21.724 1.997 1.00 95.61 C ANISOU 779 C VAL A 119 9925 11076 15326 2827 -3018 442 C ATOM 780 O VAL A 119 66.470 -22.676 2.592 1.00 98.73 O ANISOU 780 O VAL A 119 10607 11169 15736 2896 -3149 522 O ATOM 781 CB VAL A 119 65.764 -21.694 -0.157 1.00 84.12 C ANISOU 781 CB VAL A 119 8528 9569 13865 2760 -2648 201 C ATOM 782 CG1 VAL A 119 65.082 -20.401 0.240 1.00 69.37 C ANISOU 782 CG1 VAL A 119 6694 7802 11861 2402 -2552 296 C ATOM 783 CG2 VAL A 119 65.854 -21.831 -1.672 1.00 83.03 C ANISOU 783 CG2 VAL A 119 8254 9523 13770 2884 -2462 1 C ATOM 784 N LYS A 120 67.358 -20.611 2.617 1.00 97.12 N ANISOU 784 N LYS A 120 9966 11497 15438 2629 -3034 523 N ATOM 785 CA LYS A 120 67.288 -20.511 4.076 1.00102.53 C ANISOU 785 CA LYS A 120 10806 12102 16051 2515 -3225 707 C ATOM 786 C LYS A 120 66.784 -19.147 4.563 1.00104.84 C ANISOU 786 C LYS A 120 11121 12517 16197 2153 -3137 785 C ATOM 787 O LYS A 120 67.338 -18.103 4.208 1.00100.92 O ANISOU 787 O LYS A 120 10369 12301 15673 2041 -3043 734 O ATOM 788 CB LYS A 120 68.656 -20.836 4.693 1.00104.34 C ANISOU 788 CB LYS A 120 10821 12474 16349 2742 -3446 744 C ATOM 789 CG LYS A 120 68.598 -21.475 6.077 1.00108.58 C ANISOU 789 CG LYS A 120 11596 12805 16853 2782 -3700 920 C ATOM 790 CD LYS A 120 69.917 -22.167 6.415 1.00114.66 C ANISOU 790 CD LYS A 120 12172 13666 17729 3113 -3927 927 C ATOM 791 CE LYS A 120 69.802 -23.058 7.652 1.00116.55 C ANISOU 791 CE LYS A 120 12698 13641 17945 3211 -4187 1100 C ATOM 792 NZ LYS A 120 71.049 -23.843 7.914 1.00117.30 N ANISOU 792 NZ LYS A 120 12618 13799 18151 3580 -4417 1103 N ATOM 793 N PHE A 121 65.729 -19.165 5.375 1.00106.39 N ANISOU 793 N PHE A 121 11631 12498 16294 1970 -3164 907 N ATOM 794 CA PHE A 121 65.184 -17.939 5.955 1.00101.86 C ANISOU 794 CA PHE A 121 11120 12009 15574 1647 -3093 985 C ATOM 795 C PHE A 121 65.668 -17.766 7.395 1.00 99.74 C ANISOU 795 C PHE A 121 10897 11769 15231 1588 -3308 1135 C ATOM 796 O PHE A 121 65.728 -18.735 8.159 1.00 99.59 O ANISOU 796 O PHE A 121 11041 11569 15230 1722 -3495 1230 O ATOM 797 CB PHE A 121 63.648 -17.965 5.967 1.00100.44 C ANISOU 797 CB PHE A 121 11245 11605 15311 1464 -2969 1021 C ATOM 798 CG PHE A 121 63.010 -18.055 4.601 1.00105.13 C ANISOU 798 CG PHE A 121 11823 12170 15953 1482 -2761 882 C ATOM 799 CD1 PHE A 121 62.736 -16.908 3.867 1.00 97.60 C ANISOU 799 CD1 PHE A 121 10750 11392 14941 1313 -2561 810 C ATOM 800 CD2 PHE A 121 62.645 -19.285 4.069 1.00105.63 C ANISOU 800 CD2 PHE A 121 12013 12016 16106 1661 -2771 827 C ATOM 801 CE1 PHE A 121 62.137 -16.990 2.624 1.00 84.33 C ANISOU 801 CE1 PHE A 121 9062 9690 13289 1331 -2382 689 C ATOM 802 CE2 PHE A 121 62.043 -19.368 2.825 1.00 96.83 C ANISOU 802 CE2 PHE A 121 10891 10879 15020 1668 -2589 695 C ATOM 803 CZ PHE A 121 61.794 -18.219 2.103 1.00 83.85 C ANISOU 803 CZ PHE A 121 9114 9430 13314 1506 -2397 628 C ATOM 804 N THR A 122 66.007 -16.533 7.760 1.00 91.73 N ANISOU 804 N THR A 122 9754 10974 14125 1382 -3285 1156 N ATOM 805 CA THR A 122 66.232 -16.189 9.159 1.00 88.96 C ANISOU 805 CA THR A 122 9495 10644 13663 1259 -3463 1296 C ATOM 806 C THR A 122 64.889 -15.873 9.809 1.00 88.65 C ANISOU 806 C THR A 122 9786 10419 13478 1020 -3389 1386 C ATOM 807 O THR A 122 63.900 -15.630 9.112 1.00 92.98 O ANISOU 807 O THR A 122 10426 10892 14010 920 -3185 1329 O ATOM 808 CB THR A 122 67.156 -14.959 9.313 1.00 92.06 C ANISOU 808 CB THR A 122 9625 11346 14009 1113 -3473 1273 C ATOM 809 OG1 THR A 122 66.524 -13.796 8.754 1.00 85.28 O ANISOU 809 OG1 THR A 122 8771 10557 13073 869 -3244 1214 O ATOM 810 CG2 THR A 122 68.502 -15.200 8.629 1.00 90.13 C ANISOU 810 CG2 THR A 122 9012 11329 13905 1333 -3526 1177 C ATOM 811 N LEU A 123 64.845 -15.868 11.137 1.00 80.69 N ANISOU 811 N LEU A 123 8949 9352 12356 932 -3552 1525 N ATOM 812 CA LEU A 123 63.623 -15.496 11.839 1.00 84.20 C ANISOU 812 CA LEU A 123 9691 9656 12646 699 -3477 1610 C ATOM 813 C LEU A 123 63.129 -14.122 11.377 1.00 86.06 C ANISOU 813 C LEU A 123 9874 10023 12803 465 -3258 1535 C ATOM 814 O LEU A 123 61.928 -13.867 11.295 1.00 86.77 O ANISOU 814 O LEU A 123 10151 9999 12818 325 -3101 1539 O ATOM 815 CB LEU A 123 63.854 -15.476 13.349 1.00 85.31 C ANISOU 815 CB LEU A 123 9983 9778 12654 622 -3684 1759 C ATOM 816 CG LEU A 123 62.670 -14.996 14.194 1.00 87.58 C ANISOU 816 CG LEU A 123 10566 9954 12757 373 -3606 1846 C ATOM 817 CD1 LEU A 123 61.487 -15.941 14.053 1.00 87.14 C ANISOU 817 CD1 LEU A 123 10760 9636 12712 396 -3525 1886 C ATOM 818 CD2 LEU A 123 63.063 -14.851 15.654 1.00 85.84 C ANISOU 818 CD2 LEU A 123 10467 9760 12389 293 -3813 1980 C ATOM 819 N SER A 124 64.076 -13.244 11.071 1.00 84.90 N ANISOU 819 N SER A 124 9468 10118 12673 427 -3253 1468 N ATOM 820 CA SER A 124 63.782 -11.865 10.727 1.00 78.86 C ANISOU 820 CA SER A 124 8659 9479 11826 202 -3074 1409 C ATOM 821 C SER A 124 63.053 -11.754 9.383 1.00 83.68 C ANISOU 821 C SER A 124 9240 10057 12499 214 -2835 1301 C ATOM 822 O SER A 124 62.179 -10.901 9.191 1.00 71.99 O ANISOU 822 O SER A 124 7866 8558 10928 39 -2666 1282 O ATOM 823 CB SER A 124 65.089 -11.074 10.678 1.00 76.03 C ANISOU 823 CB SER A 124 8017 9387 11484 160 -3142 1366 C ATOM 824 OG SER A 124 64.840 -9.698 10.461 1.00 81.77 O ANISOU 824 OG SER A 124 8737 10213 12117 -77 -2988 1322 O ATOM 825 N GLU A 125 63.431 -12.616 8.449 1.00 88.58 N ANISOU 825 N GLU A 125 9715 10672 13267 432 -2826 1226 N ATOM 826 CA GLU A 125 62.860 -12.583 7.114 1.00 87.01 C ANISOU 826 CA GLU A 125 9472 10461 13128 462 -2616 1115 C ATOM 827 C GLU A 125 61.495 -13.273 7.106 1.00 80.98 C ANISOU 827 C GLU A 125 8976 9451 12343 459 -2549 1143 C ATOM 828 O GLU A 125 60.546 -12.794 6.477 1.00 73.32 O ANISOU 828 O GLU A 125 8073 8454 11331 355 -2365 1097 O ATOM 829 CB GLU A 125 63.831 -13.222 6.119 1.00 92.42 C ANISOU 829 CB GLU A 125 9897 11250 13967 697 -2628 1011 C ATOM 830 CG GLU A 125 65.136 -12.445 5.971 1.00 95.11 C ANISOU 830 CG GLU A 125 9935 11875 14328 673 -2658 970 C ATOM 831 CD GLU A 125 66.312 -13.322 5.569 1.00102.74 C ANISOU 831 CD GLU A 125 10652 12946 15440 945 -2767 911 C ATOM 832 OE1 GLU A 125 66.433 -14.451 6.095 1.00102.03 O ANISOU 832 OE1 GLU A 125 10649 12711 15409 1137 -2934 961 O ATOM 833 OE2 GLU A 125 67.124 -12.872 4.731 1.00107.92 O ANISOU 833 OE2 GLU A 125 11027 13832 16148 970 -2683 815 O ATOM 834 N ILE A 126 61.401 -14.388 7.821 1.00 81.36 N ANISOU 834 N ILE A 126 9177 9323 12415 567 -2704 1226 N ATOM 835 CA ILE A 126 60.125 -15.058 8.006 1.00 72.36 C ANISOU 835 CA ILE A 126 8305 7949 11241 528 -2660 1274 C ATOM 836 C ILE A 126 59.115 -14.048 8.547 1.00 75.64 C ANISOU 836 C ILE A 126 8874 8368 11497 273 -2544 1325 C ATOM 837 O ILE A 126 57.972 -14.001 8.090 1.00 75.66 O ANISOU 837 O ILE A 126 8985 8289 11471 195 -2391 1297 O ATOM 838 CB ILE A 126 60.244 -16.259 8.956 1.00 70.93 C ANISOU 838 CB ILE A 126 8296 7579 11076 638 -2865 1388 C ATOM 839 CG1 ILE A 126 61.085 -17.366 8.322 1.00 78.18 C ANISOU 839 CG1 ILE A 126 9092 8452 12159 922 -2966 1325 C ATOM 840 CG2 ILE A 126 58.871 -16.806 9.315 1.00 64.28 C ANISOU 840 CG2 ILE A 126 7746 6509 10168 532 -2812 1458 C ATOM 841 CD1 ILE A 126 61.144 -18.648 9.158 1.00 74.91 C ANISOU 841 CD1 ILE A 126 8882 7811 11770 1054 -3169 1439 C ATOM 842 N LYS A 127 59.541 -13.225 9.504 1.00 78.86 N ANISOU 842 N LYS A 127 9286 8880 11799 149 -2618 1392 N ATOM 843 CA LYS A 127 58.691 -12.148 10.012 1.00 77.23 C ANISOU 843 CA LYS A 127 9216 8693 11436 -78 -2504 1423 C ATOM 844 C LYS A 127 58.230 -11.232 8.887 1.00 77.27 C ANISOU 844 C LYS A 127 9125 8789 11445 -146 -2286 1314 C ATOM 845 O LYS A 127 57.060 -10.840 8.818 1.00 76.55 O ANISOU 845 O LYS A 127 9171 8640 11275 -258 -2142 1313 O ATOM 846 CB LYS A 127 59.428 -11.309 11.054 1.00 72.09 C ANISOU 846 CB LYS A 127 8552 8163 10678 -193 -2619 1482 C ATOM 847 CG LYS A 127 59.302 -11.830 12.457 1.00 72.26 C ANISOU 847 CG LYS A 127 8781 8075 10598 -226 -2784 1617 C ATOM 848 CD LYS A 127 60.091 -10.981 13.426 1.00 71.20 C ANISOU 848 CD LYS A 127 8623 8076 10353 -340 -2907 1660 C ATOM 849 CE LYS A 127 60.204 -11.688 14.765 1.00 77.82 C ANISOU 849 CE LYS A 127 9644 8820 11105 -329 -3111 1799 C ATOM 850 NZ LYS A 127 60.615 -10.751 15.842 1.00 85.90 N ANISOU 850 NZ LYS A 127 10718 9953 11967 -493 -3203 1844 N ATOM 851 N ARG A 128 59.162 -10.882 8.009 1.00 68.55 N ANISOU 851 N ARG A 128 7781 7838 10426 -77 -2262 1224 N ATOM 852 CA ARG A 128 58.864 -9.948 6.944 1.00 70.59 C ANISOU 852 CA ARG A 128 7948 8195 10678 -145 -2067 1130 C ATOM 853 C ARG A 128 57.868 -10.556 5.968 1.00 68.32 C ANISOU 853 C ARG A 128 7713 7803 10445 -72 -1935 1072 C ATOM 854 O ARG A 128 56.888 -9.908 5.584 1.00 60.39 O ANISOU 854 O ARG A 128 6786 6788 9372 -173 -1779 1048 O ATOM 855 CB ARG A 128 60.146 -9.537 6.227 1.00 73.67 C ANISOU 855 CB ARG A 128 8065 8781 11144 -92 -2073 1055 C ATOM 856 CG ARG A 128 59.949 -8.439 5.213 1.00 67.70 C ANISOU 856 CG ARG A 128 7228 8135 10359 -189 -1880 976 C ATOM 857 CD ARG A 128 59.510 -7.140 5.861 1.00 68.42 C ANISOU 857 CD ARG A 128 7455 8240 10302 -406 -1824 1019 C ATOM 858 NE ARG A 128 59.180 -6.157 4.831 1.00 67.48 N ANISOU 858 NE ARG A 128 7298 8189 10154 -482 -1636 951 N ATOM 859 CZ ARG A 128 57.959 -5.689 4.598 1.00 62.99 C ANISOU 859 CZ ARG A 128 6888 7536 9508 -545 -1496 948 C ATOM 860 NH1 ARG A 128 56.931 -6.081 5.348 1.00 62.69 N ANISOU 860 NH1 ARG A 128 7049 7356 9413 -558 -1511 1004 N ATOM 861 NH2 ARG A 128 57.772 -4.812 3.622 1.00 56.31 N ANISOU 861 NH2 ARG A 128 6001 6757 8638 -595 -1342 892 N ATOM 862 N VAL A 129 58.124 -11.804 5.577 1.00 67.03 N ANISOU 862 N VAL A 129 7509 7559 10401 108 -2007 1045 N ATOM 863 CA VAL A 129 57.230 -12.535 4.688 1.00 65.18 C ANISOU 863 CA VAL A 129 7334 7209 10221 178 -1909 984 C ATOM 864 C VAL A 129 55.791 -12.545 5.222 1.00 68.84 C ANISOU 864 C VAL A 129 8031 7537 10588 42 -1846 1049 C ATOM 865 O VAL A 129 54.851 -12.164 4.522 1.00 66.87 O ANISOU 865 O VAL A 129 7806 7294 10307 -19 -1691 998 O ATOM 866 CB VAL A 129 57.730 -13.982 4.451 1.00 67.45 C ANISOU 866 CB VAL A 129 7598 7386 10643 391 -2029 960 C ATOM 867 CG1 VAL A 129 56.602 -14.870 3.901 1.00 70.79 C ANISOU 867 CG1 VAL A 129 8167 7631 11097 418 -1962 926 C ATOM 868 CG2 VAL A 129 58.922 -13.978 3.507 1.00 57.86 C ANISOU 868 CG2 VAL A 129 6123 6329 9532 548 -2025 853 C ATOM 869 N MET A 130 55.625 -12.970 6.469 1.00 68.44 N ANISOU 869 N MET A 130 8145 7377 10483 -6 -1966 1164 N ATOM 870 CA MET A 130 54.305 -12.996 7.085 1.00 66.71 C ANISOU 870 CA MET A 130 8137 7048 10160 -145 -1905 1233 C ATOM 871 C MET A 130 53.665 -11.607 7.147 1.00 72.59 C ANISOU 871 C MET A 130 8897 7902 10780 -303 -1756 1223 C ATOM 872 O MET A 130 52.440 -11.464 7.060 1.00 72.41 O ANISOU 872 O MET A 130 8975 7840 10696 -388 -1635 1223 O ATOM 873 CB MET A 130 54.380 -13.616 8.478 1.00 64.76 C ANISOU 873 CB MET A 130 8062 6685 9857 -176 -2064 1367 C ATOM 874 CG MET A 130 54.656 -15.113 8.454 1.00 76.09 C ANISOU 874 CG MET A 130 9554 7953 11404 -27 -2200 1393 C ATOM 875 SD MET A 130 53.676 -15.957 7.191 1.00 77.23 S ANISOU 875 SD MET A 130 9722 7978 11643 22 -2077 1296 S ATOM 876 CE MET A 130 52.011 -15.556 7.718 1.00 52.82 C ANISOU 876 CE MET A 130 6812 4850 8406 -211 -1936 1358 C ATOM 877 N GLN A 131 54.499 -10.586 7.293 1.00 68.89 N ANISOU 877 N GLN A 131 8328 7571 10274 -340 -1768 1211 N ATOM 878 CA GLN A 131 54.020 -9.218 7.372 1.00 56.59 C ANISOU 878 CA GLN A 131 6804 6100 8599 -479 -1640 1199 C ATOM 879 C GLN A 131 53.445 -8.791 6.028 1.00 56.16 C ANISOU 879 C GLN A 131 6665 6096 8576 -457 -1467 1101 C ATOM 880 O GLN A 131 52.354 -8.220 5.956 1.00 51.90 O ANISOU 880 O GLN A 131 6216 5550 7955 -535 -1339 1096 O ATOM 881 CB GLN A 131 55.153 -8.282 7.784 1.00 64.36 C ANISOU 881 CB GLN A 131 7704 7207 9545 -534 -1708 1204 C ATOM 882 CG GLN A 131 54.700 -6.877 8.122 1.00 68.08 C ANISOU 882 CG GLN A 131 8262 7730 9876 -688 -1602 1204 C ATOM 883 CD GLN A 131 55.810 -6.046 8.725 1.00 67.29 C ANISOU 883 CD GLN A 131 8112 7729 9725 -771 -1696 1218 C ATOM 884 OE1 GLN A 131 56.864 -5.859 8.116 1.00 64.40 O ANISOU 884 OE1 GLN A 131 7558 7472 9438 -736 -1728 1171 O ATOM 885 NE2 GLN A 131 55.581 -5.544 9.929 1.00 59.10 N ANISOU 885 NE2 GLN A 131 7243 6664 8550 -891 -1739 1280 N ATOM 886 N MET A 132 54.175 -9.070 4.957 1.00 55.31 N ANISOU 886 N MET A 132 6383 6049 8582 -343 -1464 1021 N ATOM 887 CA MET A 132 53.696 -8.712 3.634 1.00 55.65 C ANISOU 887 CA MET A 132 6349 6148 8647 -316 -1310 929 C ATOM 888 C MET A 132 52.416 -9.499 3.308 1.00 60.15 C ANISOU 888 C MET A 132 7018 6608 9228 -296 -1251 918 C ATOM 889 O MET A 132 51.446 -8.936 2.813 1.00 55.32 O ANISOU 889 O MET A 132 6439 6021 8559 -346 -1119 889 O ATOM 890 CB MET A 132 54.781 -8.966 2.587 1.00 54.91 C ANISOU 890 CB MET A 132 6051 6149 8664 -193 -1320 845 C ATOM 891 CG MET A 132 55.999 -8.053 2.718 1.00 62.69 C ANISOU 891 CG MET A 132 6904 7280 9635 -239 -1350 845 C ATOM 892 SD MET A 132 57.362 -8.526 1.614 1.00 66.04 S ANISOU 892 SD MET A 132 7060 7838 10193 -83 -1370 749 S ATOM 893 CE MET A 132 57.133 -7.331 0.305 1.00 92.26 C ANISOU 893 CE MET A 132 10309 11288 13459 -155 -1167 675 C ATOM 894 N LEU A 133 52.423 -10.797 3.601 1.00 54.19 N ANISOU 894 N LEU A 133 6314 5730 8545 -226 -1356 942 N ATOM 895 CA LEU A 133 51.287 -11.656 3.312 1.00 55.40 C ANISOU 895 CA LEU A 133 6562 5770 8717 -227 -1317 931 C ATOM 896 C LEU A 133 50.039 -11.139 4.018 1.00 58.22 C ANISOU 896 C LEU A 133 7058 6111 8949 -374 -1237 995 C ATOM 897 O LEU A 133 49.008 -10.920 3.387 1.00 59.30 O ANISOU 897 O LEU A 133 7199 6275 9059 -407 -1116 951 O ATOM 898 CB LEU A 133 51.590 -13.101 3.715 1.00 57.89 C ANISOU 898 CB LEU A 133 6947 5930 9120 -145 -1462 966 C ATOM 899 CG LEU A 133 50.640 -14.207 3.247 1.00 68.96 C ANISOU 899 CG LEU A 133 8437 7194 10570 -134 -1444 937 C ATOM 900 CD1 LEU A 133 51.376 -15.525 3.133 1.00 71.41 C ANISOU 900 CD1 LEU A 133 8761 7367 11003 13 -1581 921 C ATOM 901 CD2 LEU A 133 49.466 -14.346 4.193 1.00 73.75 C ANISOU 901 CD2 LEU A 133 9220 7719 11083 -290 -1424 1034 C ATOM 902 N LEU A 134 50.146 -10.921 5.323 1.00 56.98 N ANISOU 902 N LEU A 134 7011 5927 8712 -455 -1304 1094 N ATOM 903 CA LEU A 134 49.032 -10.416 6.114 1.00 50.50 C ANISOU 903 CA LEU A 134 6323 5104 7760 -588 -1225 1154 C ATOM 904 C LEU A 134 48.584 -9.035 5.641 1.00 48.50 C ANISOU 904 C LEU A 134 6024 4973 7429 -628 -1077 1102 C ATOM 905 O LEU A 134 47.393 -8.703 5.684 1.00 51.05 O ANISOU 905 O LEU A 134 6405 5314 7677 -689 -965 1104 O ATOM 906 CB LEU A 134 49.396 -10.395 7.602 1.00 52.15 C ANISOU 906 CB LEU A 134 6660 5271 7883 -661 -1332 1264 C ATOM 907 CG LEU A 134 49.458 -11.783 8.257 1.00 57.75 C ANISOU 907 CG LEU A 134 7477 5832 8634 -646 -1466 1345 C ATOM 908 CD1 LEU A 134 50.024 -11.702 9.655 1.00 57.26 C ANISOU 908 CD1 LEU A 134 7528 5746 8481 -701 -1591 1453 C ATOM 909 CD2 LEU A 134 48.072 -12.449 8.268 1.00 50.72 C ANISOU 909 CD2 LEU A 134 6690 4861 7718 -725 -1386 1368 C ATOM 910 N ASN A 135 49.534 -8.242 5.166 1.00 45.12 N ANISOU 910 N ASN A 135 5490 4632 7019 -590 -1075 1057 N ATOM 911 CA ASN A 135 49.216 -6.920 4.640 1.00 43.90 C ANISOU 911 CA ASN A 135 5310 4575 6796 -621 -943 1011 C ATOM 912 C ASN A 135 48.458 -7.002 3.310 1.00 47.34 C ANISOU 912 C ASN A 135 5669 5045 7272 -561 -831 932 C ATOM 913 O ASN A 135 47.566 -6.204 3.043 1.00 50.23 O ANISOU 913 O ASN A 135 6065 5458 7562 -587 -713 916 O ATOM 914 CB ASN A 135 50.482 -6.080 4.476 1.00 43.74 C ANISOU 914 CB ASN A 135 5202 4634 6781 -622 -975 990 C ATOM 915 CG ASN A 135 50.177 -4.593 4.332 1.00 54.88 C ANISOU 915 CG ASN A 135 6656 6108 8088 -688 -859 973 C ATOM 916 OD1 ASN A 135 49.248 -4.076 4.954 1.00 55.87 O ANISOU 916 OD1 ASN A 135 6911 6208 8108 -746 -795 1001 O ATOM 917 ND2 ASN A 135 50.944 -3.908 3.498 1.00 48.55 N ANISOU 917 ND2 ASN A 135 5750 5385 7312 -676 -826 925 N ATOM 918 N GLY A 136 48.822 -7.968 2.476 1.00 47.79 N ANISOU 918 N GLY A 136 5631 5081 7444 -470 -872 881 N ATOM 919 CA GLY A 136 48.073 -8.244 1.268 1.00 47.77 C ANISOU 919 CA GLY A 136 5571 5102 7476 -419 -786 804 C ATOM 920 C GLY A 136 46.641 -8.661 1.593 1.00 54.16 C ANISOU 920 C GLY A 136 6472 5865 8241 -480 -742 830 C ATOM 921 O GLY A 136 45.679 -8.135 1.023 1.00 54.48 O ANISOU 921 O GLY A 136 6498 5972 8231 -489 -633 797 O ATOM 922 N LEU A 137 46.494 -9.602 2.519 1.00 43.00 N ANISOU 922 N LEU A 137 5150 4345 6843 -524 -827 895 N ATOM 923 CA LEU A 137 45.174 -10.049 2.939 1.00 48.35 C ANISOU 923 CA LEU A 137 5912 4985 7474 -609 -784 930 C ATOM 924 C LEU A 137 44.321 -8.898 3.470 1.00 53.18 C ANISOU 924 C LEU A 137 6569 5685 7953 -680 -673 961 C ATOM 925 O LEU A 137 43.147 -8.779 3.133 1.00 56.01 O ANISOU 925 O LEU A 137 6910 6097 8272 -707 -578 939 O ATOM 926 CB LEU A 137 45.288 -11.156 3.987 1.00 50.77 C ANISOU 926 CB LEU A 137 6335 5155 7800 -662 -897 1015 C ATOM 927 CG LEU A 137 45.739 -12.490 3.387 1.00 54.59 C ANISOU 927 CG LEU A 137 6802 5525 8416 -587 -994 976 C ATOM 928 CD1 LEU A 137 45.910 -13.539 4.480 1.00 54.72 C ANISOU 928 CD1 LEU A 137 6961 5385 8445 -633 -1118 1076 C ATOM 929 CD2 LEU A 137 44.763 -12.966 2.291 1.00 47.96 C ANISOU 929 CD2 LEU A 137 5914 4693 7614 -590 -922 892 C ATOM 930 N TYR A 138 44.913 -8.043 4.293 1.00 51.15 N ANISOU 930 N TYR A 138 6366 5444 7624 -706 -687 1007 N ATOM 931 CA TYR A 138 44.175 -6.924 4.849 1.00 41.91 C ANISOU 931 CA TYR A 138 5260 4340 6322 -757 -584 1028 C ATOM 932 C TYR A 138 43.604 -6.095 3.710 1.00 49.55 C ANISOU 932 C TYR A 138 6144 5405 7278 -695 -466 953 C ATOM 933 O TYR A 138 42.450 -5.661 3.750 1.00 47.14 O ANISOU 933 O TYR A 138 5854 5159 6898 -708 -364 948 O ATOM 934 CB TYR A 138 45.097 -6.055 5.704 1.00 47.18 C ANISOU 934 CB TYR A 138 5997 5006 6922 -787 -627 1065 C ATOM 935 CG TYR A 138 44.486 -4.726 6.070 1.00 53.29 C ANISOU 935 CG TYR A 138 6843 5840 7565 -813 -515 1061 C ATOM 936 CD1 TYR A 138 43.750 -4.572 7.251 1.00 55.20 C ANISOU 936 CD1 TYR A 138 7209 6077 7688 -887 -478 1114 C ATOM 937 CD2 TYR A 138 44.639 -3.618 5.236 1.00 49.40 C ANISOU 937 CD2 TYR A 138 6306 5404 7059 -760 -442 1004 C ATOM 938 CE1 TYR A 138 43.183 -3.343 7.588 1.00 54.56 C ANISOU 938 CE1 TYR A 138 7202 6045 7482 -890 -370 1098 C ATOM 939 CE2 TYR A 138 44.071 -2.388 5.563 1.00 57.97 C ANISOU 939 CE2 TYR A 138 7480 6522 8024 -768 -343 997 C ATOM 940 CZ TYR A 138 43.343 -2.259 6.741 1.00 64.80 C ANISOU 940 CZ TYR A 138 8464 7380 8777 -824 -307 1038 C ATOM 941 OH TYR A 138 42.779 -1.043 7.071 1.00 80.67 O ANISOU 941 OH TYR A 138 10569 9417 10666 -810 -205 1019 O ATOM 942 N TYR A 139 44.429 -5.872 2.692 1.00 42.21 N ANISOU 942 N TYR A 139 5122 4499 6416 -622 -481 896 N ATOM 943 CA TYR A 139 44.016 -5.091 1.537 1.00 39.91 C ANISOU 943 CA TYR A 139 4763 4294 6107 -558 -382 832 C ATOM 944 C TYR A 139 42.897 -5.755 0.730 1.00 49.35 C ANISOU 944 C TYR A 139 5893 5526 7332 -531 -336 788 C ATOM 945 O TYR A 139 41.905 -5.106 0.405 1.00 50.37 O ANISOU 945 O TYR A 139 6013 5732 7394 -510 -243 771 O ATOM 946 CB TYR A 139 45.205 -4.807 0.617 1.00 39.42 C ANISOU 946 CB TYR A 139 4616 4257 6104 -501 -406 787 C ATOM 947 CG TYR A 139 44.789 -4.119 -0.644 1.00 37.53 C ANISOU 947 CG TYR A 139 4318 4101 5841 -437 -310 729 C ATOM 948 CD1 TYR A 139 44.553 -2.748 -0.654 1.00 36.20 C ANISOU 948 CD1 TYR A 139 4209 3970 5574 -437 -229 741 C ATOM 949 CD2 TYR A 139 44.596 -4.834 -1.826 1.00 27.90 C ANISOU 949 CD2 TYR A 139 3000 2914 4688 -373 -306 662 C ATOM 950 CE1 TYR A 139 44.153 -2.091 -1.817 1.00 33.49 C ANISOU 950 CE1 TYR A 139 3829 3696 5198 -370 -148 700 C ATOM 951 CE2 TYR A 139 44.189 -4.187 -2.999 1.00 35.76 C ANISOU 951 CE2 TYR A 139 3950 3993 5644 -314 -224 615 C ATOM 952 CZ TYR A 139 43.964 -2.816 -2.982 1.00 44.88 C ANISOU 952 CZ TYR A 139 5166 5186 6700 -310 -147 641 C ATOM 953 OH TYR A 139 43.572 -2.154 -4.127 1.00 48.28 O ANISOU 953 OH TYR A 139 5570 5691 7084 -244 -76 607 O ATOM 954 N ILE A 140 43.052 -7.033 0.388 1.00 50.63 N ANISOU 954 N ILE A 140 6012 5633 7591 -527 -408 765 N ATOM 955 CA ILE A 140 42.044 -7.676 -0.453 1.00 57.05 C ANISOU 955 CA ILE A 140 6763 6480 8431 -517 -375 711 C ATOM 956 C ILE A 140 40.706 -7.782 0.288 1.00 55.60 C ANISOU 956 C ILE A 140 6622 6323 8181 -602 -324 754 C ATOM 957 O ILE A 140 39.649 -7.581 -0.298 1.00 50.03 O ANISOU 957 O ILE A 140 5855 5713 7442 -591 -253 718 O ATOM 958 CB ILE A 140 42.487 -9.051 -1.052 1.00 48.95 C ANISOU 958 CB ILE A 140 5702 5373 7524 -494 -464 661 C ATOM 959 CG1 ILE A 140 42.450 -10.155 -0.018 1.00 46.36 C ANISOU 959 CG1 ILE A 140 5465 4918 7233 -575 -548 725 C ATOM 960 CG2 ILE A 140 43.883 -8.988 -1.678 1.00 52.19 C ANISOU 960 CG2 ILE A 140 6056 5773 7999 -402 -509 617 C ATOM 961 CD1 ILE A 140 42.404 -11.521 -0.652 1.00 56.40 C ANISOU 961 CD1 ILE A 140 6727 6100 8605 -565 -616 669 C ATOM 962 N HIS A 141 40.756 -8.058 1.585 1.00 50.00 N ANISOU 962 N HIS A 141 6011 5545 7442 -685 -358 834 N ATOM 963 CA HIS A 141 39.536 -8.154 2.374 1.00 48.72 C ANISOU 963 CA HIS A 141 5886 5421 7203 -777 -297 880 C ATOM 964 C HIS A 141 38.832 -6.798 2.513 1.00 49.56 C ANISOU 964 C HIS A 141 5985 5651 7196 -740 -177 876 C ATOM 965 O HIS A 141 37.621 -6.695 2.392 1.00 54.15 O ANISOU 965 O HIS A 141 6512 6332 7731 -754 -96 862 O ATOM 966 CB HIS A 141 39.854 -8.728 3.745 1.00 42.59 C ANISOU 966 CB HIS A 141 5234 4543 6405 -875 -361 973 C ATOM 967 CG HIS A 141 40.301 -10.152 3.705 1.00 52.93 C ANISOU 967 CG HIS A 141 6574 5719 7819 -910 -477 987 C ATOM 968 ND1 HIS A 141 41.046 -10.725 4.714 1.00 52.63 N ANISOU 968 ND1 HIS A 141 6651 5559 7788 -954 -579 1068 N ATOM 969 CD2 HIS A 141 40.130 -11.113 2.765 1.00 44.34 C ANISOU 969 CD2 HIS A 141 5430 4590 6828 -900 -514 928 C ATOM 970 CE1 HIS A 141 41.292 -11.989 4.407 1.00 51.61 C ANISOU 970 CE1 HIS A 141 6539 5308 7760 -960 -672 1063 C ATOM 971 NE2 HIS A 141 40.752 -12.247 3.229 1.00 46.55 N ANISOU 971 NE2 HIS A 141 5801 4711 7177 -931 -632 973 N ATOM 972 N ARG A 142 39.617 -5.766 2.777 1.00 49.45 N ANISOU 972 N ARG A 142 6027 5624 7137 -692 -172 886 N ATOM 973 CA ARG A 142 39.133 -4.402 2.858 1.00 45.54 C ANISOU 973 CA ARG A 142 5555 5211 6537 -637 -69 876 C ATOM 974 C ARG A 142 38.382 -4.057 1.579 1.00 48.94 C ANISOU 974 C ARG A 142 5874 5746 6977 -545 -4 811 C ATOM 975 O ARG A 142 37.486 -3.216 1.585 1.00 50.97 O ANISOU 975 O ARG A 142 6125 6092 7151 -491 89 801 O ATOM 976 CB ARG A 142 40.334 -3.476 3.052 1.00 51.12 C ANISOU 976 CB ARG A 142 6339 5864 7222 -610 -98 884 C ATOM 977 CG ARG A 142 40.010 -2.053 3.350 1.00 60.84 C ANISOU 977 CG ARG A 142 7648 7131 8338 -566 -8 881 C ATOM 978 CD ARG A 142 41.291 -1.251 3.502 1.00 85.56 C ANISOU 978 CD ARG A 142 10857 10196 11457 -574 -53 888 C ATOM 979 NE ARG A 142 41.026 0.172 3.679 1.00109.75 N ANISOU 979 NE ARG A 142 14022 13268 14412 -530 31 877 N ATOM 980 CZ ARG A 142 41.859 1.020 4.274 1.00122.41 C ANISOU 980 CZ ARG A 142 15746 14807 15959 -572 8 890 C ATOM 981 NH1 ARG A 142 43.017 0.583 4.753 1.00123.08 N ANISOU 981 NH1 ARG A 142 15841 14837 16086 -657 -100 918 N ATOM 982 NH2 ARG A 142 41.531 2.303 4.393 1.00124.56 N ANISOU 982 NH2 ARG A 142 16130 15067 16129 -526 87 874 N ATOM 983 N ASN A 143 38.745 -4.730 0.489 1.00 47.27 N ANISOU 983 N ASN A 143 5576 5524 6860 -518 -58 763 N ATOM 984 CA ASN A 143 38.122 -4.515 -0.810 1.00 45.68 C ANISOU 984 CA ASN A 143 5270 5421 6663 -435 -16 700 C ATOM 985 C ASN A 143 37.084 -5.563 -1.135 1.00 48.19 C ANISOU 985 C ASN A 143 5497 5794 7017 -486 -22 672 C ATOM 986 O ASN A 143 36.719 -5.732 -2.298 1.00 45.22 O ANISOU 986 O ASN A 143 5028 5488 6666 -436 -23 610 O ATOM 987 CB ASN A 143 39.177 -4.509 -1.913 1.00 45.67 C ANISOU 987 CB ASN A 143 5234 5394 6726 -374 -61 653 C ATOM 988 CG ASN A 143 39.894 -3.192 -2.012 1.00 51.79 C ANISOU 988 CG ASN A 143 6068 6165 7445 -316 -25 666 C ATOM 989 OD1 ASN A 143 39.405 -2.263 -2.655 1.00 58.58 O ANISOU 989 OD1 ASN A 143 6921 7096 8241 -237 41 649 O ATOM 990 ND2 ASN A 143 41.066 -3.094 -1.373 1.00 45.59 N ANISOU 990 ND2 ASN A 143 5347 5294 6680 -360 -75 698 N ATOM 991 N LYS A 144 36.636 -6.284 -0.108 1.00 49.92 N ANISOU 991 N LYS A 144 5752 5983 7234 -599 -31 720 N ATOM 992 CA LYS A 144 35.505 -7.194 -0.231 1.00 49.94 C ANISOU 992 CA LYS A 144 5675 6047 7254 -682 -23 706 C ATOM 993 C LYS A 144 35.825 -8.359 -1.137 1.00 52.73 C ANISOU 993 C LYS A 144 5988 6335 7714 -709 -112 651 C ATOM 994 O LYS A 144 34.966 -8.861 -1.846 1.00 57.43 O ANISOU 994 O LYS A 144 6489 7007 8324 -738 -109 600 O ATOM 995 CB LYS A 144 34.272 -6.452 -0.751 1.00 52.24 C ANISOU 995 CB LYS A 144 5856 6519 7474 -616 68 671 C ATOM 996 CG LYS A 144 33.895 -5.275 0.109 1.00 55.71 C ANISOU 996 CG LYS A 144 6343 7020 7804 -565 162 711 C ATOM 997 CD LYS A 144 33.802 -5.723 1.546 1.00 73.95 C ANISOU 997 CD LYS A 144 8738 9279 10081 -693 175 782 C ATOM 998 CE LYS A 144 33.723 -4.548 2.501 1.00 88.42 C ANISOU 998 CE LYS A 144 10659 11136 11799 -639 259 816 C ATOM 999 NZ LYS A 144 33.730 -5.008 3.926 1.00 95.12 N ANISOU 999 NZ LYS A 144 11608 11933 12599 -770 266 887 N ATOM 1000 N ILE A 145 37.072 -8.798 -1.107 1.00 52.49 N ANISOU 1000 N ILE A 145 6027 6164 7753 -696 -194 655 N ATOM 1001 CA ILE A 145 37.452 -9.980 -1.855 1.00 43.61 C ANISOU 1001 CA ILE A 145 4887 4953 6731 -709 -280 598 C ATOM 1002 C ILE A 145 37.954 -11.068 -0.924 1.00 47.99 C ANISOU 1002 C ILE A 145 5550 5341 7344 -801 -365 656 C ATOM 1003 O ILE A 145 38.683 -10.790 0.024 1.00 52.10 O ANISOU 1003 O ILE A 145 6154 5795 7847 -801 -388 727 O ATOM 1004 CB ILE A 145 38.536 -9.674 -2.889 1.00 38.42 C ANISOU 1004 CB ILE A 145 4199 4283 6117 -581 -307 533 C ATOM 1005 CG1 ILE A 145 38.095 -8.533 -3.820 1.00 40.04 C ANISOU 1005 CG1 ILE A 145 4321 4641 6251 -488 -226 490 C ATOM 1006 CG2 ILE A 145 38.877 -10.929 -3.657 1.00 44.13 C ANISOU 1006 CG2 ILE A 145 4912 4918 6939 -581 -389 459 C ATOM 1007 CD1 ILE A 145 36.886 -8.852 -4.645 1.00 44.58 C ANISOU 1007 CD1 ILE A 145 4804 5326 6810 -504 -206 430 C ATOM 1008 N LEU A 146 37.524 -12.299 -1.187 1.00 51.59 N ANISOU 1008 N LEU A 146 6014 5727 7861 -885 -418 629 N ATOM 1009 CA LEU A 146 38.085 -13.488 -0.568 1.00 47.98 C ANISOU 1009 CA LEU A 146 5677 5079 7476 -950 -519 672 C ATOM 1010 C LEU A 146 38.967 -14.144 -1.610 1.00 55.17 C ANISOU 1010 C LEU A 146 6577 5897 8489 -847 -599 579 C ATOM 1011 O LEU A 146 38.574 -14.276 -2.774 1.00 57.84 O ANISOU 1011 O LEU A 146 6834 6299 8845 -817 -583 478 O ATOM 1012 CB LEU A 146 36.974 -14.457 -0.186 1.00 56.80 C ANISOU 1012 CB LEU A 146 6830 6162 8590 -1126 -522 701 C ATOM 1013 CG LEU A 146 35.867 -13.912 0.709 1.00 52.15 C ANISOU 1013 CG LEU A 146 6220 5704 7892 -1240 -422 776 C ATOM 1014 CD1 LEU A 146 34.867 -15.012 1.003 1.00 49.41 C ANISOU 1014 CD1 LEU A 146 5903 5320 7552 -1436 -430 803 C ATOM 1015 CD2 LEU A 146 36.443 -13.347 2.001 1.00 50.89 C ANISOU 1015 CD2 LEU A 146 6160 5508 7669 -1234 -413 880 C ATOM 1016 N HIS A 147 40.167 -14.537 -1.205 1.00 52.90 N ANISOU 1016 N HIS A 147 6366 5470 8262 -784 -685 607 N ATOM 1017 CA HIS A 147 41.102 -15.155 -2.129 1.00 53.73 C ANISOU 1017 CA HIS A 147 6457 5493 8465 -663 -756 514 C ATOM 1018 C HIS A 147 40.734 -16.614 -2.402 1.00 53.18 C ANISOU 1018 C HIS A 147 6470 5267 8470 -727 -831 472 C ATOM 1019 O HIS A 147 40.771 -17.067 -3.544 1.00 49.01 O ANISOU 1019 O HIS A 147 5902 4730 7988 -667 -845 354 O ATOM 1020 CB HIS A 147 42.530 -15.074 -1.598 1.00 56.04 C ANISOU 1020 CB HIS A 147 6783 5708 8800 -560 -827 556 C ATOM 1021 CG HIS A 147 43.532 -15.736 -2.490 1.00 47.81 C ANISOU 1021 CG HIS A 147 5714 4594 7859 -418 -893 458 C ATOM 1022 ND1 HIS A 147 43.625 -17.106 -2.613 1.00 48.84 N ANISOU 1022 ND1 HIS A 147 5937 4545 8077 -410 -987 423 N ATOM 1023 CD2 HIS A 147 44.470 -15.218 -3.318 1.00 45.66 C ANISOU 1023 CD2 HIS A 147 5334 4407 7608 -278 -872 382 C ATOM 1024 CE1 HIS A 147 44.581 -17.404 -3.475 1.00 56.09 C ANISOU 1024 CE1 HIS A 147 6802 5443 9067 -252 -1019 322 C ATOM 1025 NE2 HIS A 147 45.115 -16.275 -3.910 1.00 55.98 N ANISOU 1025 NE2 HIS A 147 6657 5600 9014 -175 -947 298 N ATOM 1026 N ARG A 148 40.407 -17.346 -1.342 1.00 57.46 N ANISOU 1026 N ARG A 148 7141 5677 9014 -853 -882 569 N ATOM 1027 CA ARG A 148 39.835 -18.690 -1.459 1.00 59.66 C ANISOU 1027 CA ARG A 148 7525 5797 9346 -964 -945 548 C ATOM 1028 C ARG A 148 40.783 -19.757 -2.005 1.00 64.31 C ANISOU 1028 C ARG A 148 8196 6189 10050 -844 -1058 472 C ATOM 1029 O ARG A 148 40.379 -20.889 -2.222 1.00 78.09 O ANISOU 1029 O ARG A 148 10047 7778 11844 -924 -1117 437 O ATOM 1030 CB ARG A 148 38.563 -18.666 -2.312 1.00 58.50 C ANISOU 1030 CB ARG A 148 7286 5778 9164 -1067 -874 467 C ATOM 1031 CG ARG A 148 37.462 -17.816 -1.741 1.00 56.56 C ANISOU 1031 CG ARG A 148 6962 5717 8811 -1189 -767 538 C ATOM 1032 CD ARG A 148 36.109 -18.326 -2.174 1.00 60.90 C ANISOU 1032 CD ARG A 148 7468 6329 9342 -1356 -739 495 C ATOM 1033 NE ARG A 148 35.891 -18.188 -3.605 1.00 62.74 N ANISOU 1033 NE ARG A 148 7584 6666 9587 -1281 -728 353 N ATOM 1034 CZ ARG A 148 34.766 -18.548 -4.209 1.00 63.33 C ANISOU 1034 CZ ARG A 148 7592 6827 9644 -1407 -713 291 C ATOM 1035 NH1 ARG A 148 33.781 -19.062 -3.489 1.00 64.90 N ANISOU 1035 NH1 ARG A 148 7820 7021 9818 -1621 -701 359 N ATOM 1036 NH2 ARG A 148 34.626 -18.396 -5.520 1.00 60.77 N ANISOU 1036 NH2 ARG A 148 7169 6603 9319 -1329 -713 162 N ATOM 1037 N ASP A 149 42.037 -19.408 -2.236 1.00 59.38 N ANISOU 1037 N ASP A 149 7523 5572 9467 -655 -1087 441 N ATOM 1038 CA ASP A 149 42.987 -20.403 -2.683 1.00 59.28 C ANISOU 1038 CA ASP A 149 7579 5383 9563 -514 -1190 368 C ATOM 1039 C ASP A 149 44.366 -20.175 -2.050 1.00 60.86 C ANISOU 1039 C ASP A 149 7776 5549 9799 -362 -1256 428 C ATOM 1040 O ASP A 149 45.401 -20.342 -2.695 1.00 59.41 O ANISOU 1040 O ASP A 149 7536 5353 9686 -178 -1292 341 O ATOM 1041 CB ASP A 149 43.058 -20.440 -4.211 1.00 63.71 C ANISOU 1041 CB ASP A 149 8040 6016 10151 -410 -1152 195 C ATOM 1042 CG ASP A 149 43.621 -21.757 -4.739 1.00 72.97 C ANISOU 1042 CG ASP A 149 9323 6973 11429 -306 -1254 97 C ATOM 1043 OD1 ASP A 149 43.618 -22.762 -3.988 1.00 68.19 O ANISOU 1043 OD1 ASP A 149 8894 6142 10873 -358 -1353 163 O ATOM 1044 OD2 ASP A 149 44.071 -21.780 -5.905 1.00 76.11 O ANISOU 1044 OD2 ASP A 149 9643 7424 11853 -168 -1232 -48 O ATOM 1045 N MET A 150 44.358 -19.809 -0.772 1.00 59.55 N ANISOU 1045 N MET A 150 7667 5381 9580 -443 -1273 575 N ATOM 1046 CA MET A 150 45.589 -19.617 -0.015 1.00 61.66 C ANISOU 1046 CA MET A 150 7939 5619 9868 -327 -1354 647 C ATOM 1047 C MET A 150 46.427 -20.885 0.019 1.00 75.15 C ANISOU 1047 C MET A 150 9760 7105 11690 -196 -1498 632 C ATOM 1048 O MET A 150 45.993 -21.919 0.538 1.00 82.24 O ANISOU 1048 O MET A 150 10841 7798 12608 -279 -1575 691 O ATOM 1049 CB MET A 150 45.273 -19.178 1.422 1.00 58.25 C ANISOU 1049 CB MET A 150 7590 5198 9344 -464 -1358 809 C ATOM 1050 CG MET A 150 44.853 -17.712 1.568 1.00 53.91 C ANISOU 1050 CG MET A 150 6925 4874 8684 -530 -1230 829 C ATOM 1051 SD MET A 150 46.206 -16.551 1.244 1.00 74.96 S ANISOU 1051 SD MET A 150 9426 7698 11356 -367 -1219 787 S ATOM 1052 CE MET A 150 45.978 -16.247 -0.494 1.00 66.75 C ANISOU 1052 CE MET A 150 8233 6782 10347 -289 -1114 622 C ATOM 1053 N LYS A 151 47.627 -20.803 -0.547 1.00 76.33 N ANISOU 1053 N LYS A 151 9799 7294 11909 11 -1532 551 N ATOM 1054 CA LYS A 151 48.620 -21.864 -0.408 1.00 76.17 C ANISOU 1054 CA LYS A 151 9861 7086 11996 183 -1676 542 C ATOM 1055 C LYS A 151 50.000 -21.347 -0.786 1.00 71.44 C ANISOU 1055 C LYS A 151 9076 6624 11443 393 -1689 482 C ATOM 1056 O LYS A 151 50.118 -20.361 -1.508 1.00 73.58 O ANISOU 1056 O LYS A 151 9170 7110 11679 406 -1575 410 O ATOM 1057 CB LYS A 151 48.246 -23.096 -1.238 1.00 80.21 C ANISOU 1057 CB LYS A 151 10486 7406 12584 220 -1708 431 C ATOM 1058 CG LYS A 151 48.120 -22.858 -2.734 1.00 75.54 C ANISOU 1058 CG LYS A 151 9756 6941 12003 285 -1604 250 C ATOM 1059 CD LYS A 151 47.406 -24.032 -3.409 1.00 75.28 C ANISOU 1059 CD LYS A 151 9873 6714 12015 245 -1630 152 C ATOM 1060 CE LYS A 151 47.721 -24.094 -4.902 1.00 77.19 C ANISOU 1060 CE LYS A 151 10004 7035 12290 393 -1572 -48 C ATOM 1061 NZ LYS A 151 46.682 -24.844 -5.669 1.00 73.01 N ANISOU 1061 NZ LYS A 151 9586 6397 11757 280 -1558 -152 N ATOM 1062 N ALA A 152 51.039 -22.009 -0.290 1.00 72.48 N ANISOU 1062 N ALA A 152 9248 6639 11652 554 -1830 516 N ATOM 1063 CA ALA A 152 52.413 -21.561 -0.507 1.00 74.92 C ANISOU 1063 CA ALA A 152 9364 7094 12008 749 -1856 472 C ATOM 1064 C ALA A 152 52.713 -21.285 -1.978 1.00 69.67 C ANISOU 1064 C ALA A 152 8520 6577 11375 863 -1743 294 C ATOM 1065 O ALA A 152 53.395 -20.317 -2.309 1.00 69.70 O ANISOU 1065 O ALA A 152 8322 6804 11357 906 -1675 262 O ATOM 1066 CB ALA A 152 53.400 -22.571 0.055 1.00 81.85 C ANISOU 1066 CB ALA A 152 10317 7802 12982 941 -2034 510 C ATOM 1067 N ALA A 153 52.193 -22.125 -2.860 1.00 66.61 N ANISOU 1067 N ALA A 153 8215 6064 11028 897 -1721 178 N ATOM 1068 CA ALA A 153 52.468 -21.967 -4.284 1.00 72.58 C ANISOU 1068 CA ALA A 153 8823 6951 11802 1012 -1618 1 C ATOM 1069 C ALA A 153 51.770 -20.748 -4.910 1.00 72.41 C ANISOU 1069 C ALA A 153 8683 7154 11674 861 -1455 -24 C ATOM 1070 O ALA A 153 52.149 -20.301 -5.993 1.00 76.78 O ANISOU 1070 O ALA A 153 9084 7873 12216 944 -1358 -143 O ATOM 1071 CB ALA A 153 52.121 -23.243 -5.037 1.00 65.33 C ANISOU 1071 CB ALA A 153 8048 5825 10949 1092 -1652 -125 C ATOM 1072 N ASN A 154 50.762 -20.211 -4.226 1.00 67.06 N ANISOU 1072 N ASN A 154 8080 6486 10912 648 -1423 90 N ATOM 1073 CA ASN A 154 50.078 -18.998 -4.691 1.00 63.07 C ANISOU 1073 CA ASN A 154 7475 6186 10303 518 -1280 83 C ATOM 1074 C ASN A 154 50.642 -17.718 -4.088 1.00 64.60 C ANISOU 1074 C ASN A 154 7551 6555 10439 483 -1244 175 C ATOM 1075 O ASN A 154 50.133 -16.630 -4.349 1.00 66.55 O ANISOU 1075 O ASN A 154 7735 6957 10596 383 -1133 185 O ATOM 1076 CB ASN A 154 48.585 -19.071 -4.399 1.00 57.66 C ANISOU 1076 CB ASN A 154 6918 5439 9554 316 -1249 136 C ATOM 1077 CG ASN A 154 47.873 -20.003 -5.328 1.00 68.55 C ANISOU 1077 CG ASN A 154 8372 6714 10961 310 -1244 17 C ATOM 1078 OD1 ASN A 154 48.401 -20.346 -6.387 1.00 75.70 O ANISOU 1078 OD1 ASN A 154 9218 7636 11909 455 -1231 -123 O ATOM 1079 ND2 ASN A 154 46.668 -20.432 -4.946 1.00 62.92 N ANISOU 1079 ND2 ASN A 154 7789 5901 10218 135 -1254 66 N ATOM 1080 N VAL A 155 51.671 -17.860 -3.255 1.00 53.57 N ANISOU 1080 N VAL A 155 6138 5126 9091 564 -1348 243 N ATOM 1081 CA VAL A 155 52.394 -16.716 -2.721 1.00 53.53 C ANISOU 1081 CA VAL A 155 6014 5286 9038 538 -1332 314 C ATOM 1082 C VAL A 155 53.672 -16.528 -3.532 1.00 64.99 C ANISOU 1082 C VAL A 155 7267 6881 10545 704 -1312 215 C ATOM 1083 O VAL A 155 54.549 -17.394 -3.539 1.00 72.29 O ANISOU 1083 O VAL A 155 8161 7739 11567 874 -1408 176 O ATOM 1084 CB VAL A 155 52.731 -16.926 -1.235 1.00 58.35 C ANISOU 1084 CB VAL A 155 6720 5798 9652 505 -1467 457 C ATOM 1085 CG1 VAL A 155 53.499 -15.746 -0.680 1.00 52.30 C ANISOU 1085 CG1 VAL A 155 5835 5202 8832 464 -1461 520 C ATOM 1086 CG2 VAL A 155 51.463 -17.169 -0.437 1.00 57.36 C ANISOU 1086 CG2 VAL A 155 6791 5540 9464 334 -1474 554 C ATOM 1087 N LEU A 156 53.771 -15.407 -4.235 1.00 59.81 N ANISOU 1087 N LEU A 156 6478 6424 9824 659 -1183 176 N ATOM 1088 CA LEU A 156 54.945 -15.138 -5.058 1.00 60.37 C ANISOU 1088 CA LEU A 156 6347 6660 9930 788 -1140 84 C ATOM 1089 C LEU A 156 55.931 -14.221 -4.354 1.00 73.94 C ANISOU 1089 C LEU A 156 7943 8520 11630 748 -1166 164 C ATOM 1090 O LEU A 156 55.552 -13.424 -3.493 1.00 77.17 O ANISOU 1090 O LEU A 156 8419 8936 11964 593 -1170 273 O ATOM 1091 CB LEU A 156 54.535 -14.511 -6.386 1.00 61.40 C ANISOU 1091 CB LEU A 156 6408 6929 9993 761 -979 -12 C ATOM 1092 CG LEU A 156 53.552 -15.356 -7.196 1.00 68.06 C ANISOU 1092 CG LEU A 156 7359 7658 10842 788 -952 -106 C ATOM 1093 CD1 LEU A 156 53.362 -14.779 -8.584 1.00 64.04 C ANISOU 1093 CD1 LEU A 156 6763 7307 10262 792 -807 -210 C ATOM 1094 CD2 LEU A 156 54.040 -16.785 -7.270 1.00 68.34 C ANISOU 1094 CD2 LEU A 156 7433 7541 10994 963 -1056 -182 C ATOM 1095 N ILE A 157 57.202 -14.343 -4.724 1.00 82.33 N ANISOU 1095 N ILE A 157 8821 9702 12759 889 -1185 102 N ATOM 1096 CA ILE A 157 58.232 -13.433 -4.243 1.00 76.48 C ANISOU 1096 CA ILE A 157 7925 9134 12000 841 -1201 158 C ATOM 1097 C ILE A 157 59.066 -12.956 -5.423 1.00 74.90 C ANISOU 1097 C ILE A 157 7503 9154 11800 901 -1081 51 C ATOM 1098 O ILE A 157 59.544 -13.767 -6.211 1.00 88.11 O ANISOU 1098 O ILE A 157 9087 10846 13547 1084 -1071 -63 O ATOM 1099 CB ILE A 157 59.110 -14.094 -3.181 1.00 68.32 C ANISOU 1099 CB ILE A 157 6865 8044 11048 941 -1383 219 C ATOM 1100 CG1 ILE A 157 58.229 -14.612 -2.045 1.00 65.77 C ANISOU 1100 CG1 ILE A 157 6784 7496 10709 871 -1493 330 C ATOM 1101 CG2 ILE A 157 60.120 -13.102 -2.641 1.00 65.43 C ANISOU 1101 CG2 ILE A 157 6336 7869 10655 862 -1409 277 C ATOM 1102 CD1 ILE A 157 58.978 -14.962 -0.794 1.00 71.72 C ANISOU 1102 CD1 ILE A 157 7545 8205 11500 915 -1676 430 C ATOM 1103 N THR A 158 59.203 -11.640 -5.566 1.00 65.78 N ANISOU 1103 N THR A 158 6277 8160 10557 745 -982 87 N ATOM 1104 CA THR A 158 59.940 -11.066 -6.695 1.00 73.76 C ANISOU 1104 CA THR A 158 7090 9389 11545 763 -850 2 C ATOM 1105 C THR A 158 61.441 -11.084 -6.451 1.00 82.39 C ANISOU 1105 C THR A 158 7947 10649 12708 838 -911 -9 C ATOM 1106 O THR A 158 61.893 -11.239 -5.310 1.00 73.57 O ANISOU 1106 O THR A 158 6825 9494 11634 836 -1058 71 O ATOM 1107 CB THR A 158 59.531 -9.606 -6.989 1.00 67.36 C ANISOU 1107 CB THR A 158 6308 8679 10606 555 -718 51 C ATOM 1108 OG1 THR A 158 59.788 -8.786 -5.838 1.00 65.98 O ANISOU 1108 OG1 THR A 158 6158 8514 10397 402 -786 167 O ATOM 1109 CG2 THR A 158 58.085 -9.530 -7.345 1.00 59.46 C ANISOU 1109 CG2 THR A 158 5505 7553 9535 499 -651 53 C ATOM 1110 N ARG A 159 62.206 -10.909 -7.527 1.00 92.02 N ANISOU 1110 N ARG A 159 8965 12069 13929 901 -796 -107 N ATOM 1111 CA ARG A 159 63.661 -10.866 -7.436 1.00 94.44 C ANISOU 1111 CA ARG A 159 9003 12582 14297 969 -831 -130 C ATOM 1112 C ARG A 159 64.088 -9.858 -6.383 1.00 83.13 C ANISOU 1112 C ARG A 159 7538 11223 12827 770 -899 -6 C ATOM 1113 O ARG A 159 65.182 -9.961 -5.836 1.00 90.46 O ANISOU 1113 O ARG A 159 8280 12273 13818 815 -1000 8 O ATOM 1114 CB ARG A 159 64.299 -10.510 -8.785 1.00113.97 C ANISOU 1114 CB ARG A 159 11271 15294 16739 997 -655 -239 C ATOM 1115 CG ARG A 159 64.410 -11.673 -9.775 1.00135.90 C ANISOU 1115 CG ARG A 159 13994 18062 19578 1253 -613 -392 C ATOM 1116 CD ARG A 159 65.107 -11.242 -11.068 1.00154.31 C ANISOU 1116 CD ARG A 159 16112 20660 21858 1267 -427 -495 C ATOM 1117 NE ARG A 159 64.595 -11.956 -12.239 1.00168.87 N ANISOU 1117 NE ARG A 159 18025 22455 23683 1415 -329 -631 N ATOM 1118 CZ ARG A 159 64.850 -11.613 -13.500 1.00177.96 C ANISOU 1118 CZ ARG A 159 19066 23798 24754 1416 -149 -724 C ATOM 1119 NH1 ARG A 159 65.620 -10.563 -13.764 1.00181.48 N ANISOU 1119 NH1 ARG A 159 19325 24496 25135 1267 -40 -688 N ATOM 1120 NH2 ARG A 159 64.335 -12.320 -14.501 1.00177.42 N ANISOU 1120 NH2 ARG A 159 19083 23669 24661 1552 -77 -852 N ATOM 1121 N ASP A 160 63.221 -8.893 -6.092 1.00 65.97 N ANISOU 1121 N ASP A 160 5546 8974 10546 556 -851 78 N ATOM 1122 CA ASP A 160 63.553 -7.842 -5.138 1.00 71.77 C ANISOU 1122 CA ASP A 160 6282 9762 11225 348 -903 185 C ATOM 1123 C ASP A 160 62.964 -8.066 -3.747 1.00 77.43 C ANISOU 1123 C ASP A 160 7200 10280 11938 307 -1060 288 C ATOM 1124 O ASP A 160 62.987 -7.169 -2.902 1.00 78.43 O ANISOU 1124 O ASP A 160 7391 10412 11996 123 -1100 376 O ATOM 1125 CB ASP A 160 63.136 -6.484 -5.686 1.00 84.63 C ANISOU 1125 CB ASP A 160 7977 11451 12727 134 -745 211 C ATOM 1126 CG ASP A 160 63.753 -6.200 -7.036 1.00107.16 C ANISOU 1126 CG ASP A 160 10640 14512 15563 151 -585 124 C ATOM 1127 OD1 ASP A 160 64.430 -7.104 -7.580 1.00107.06 O ANISOU 1127 OD1 ASP A 160 10444 14596 15637 343 -587 29 O ATOM 1128 OD2 ASP A 160 63.566 -5.078 -7.555 1.00118.76 O ANISOU 1128 OD2 ASP A 160 12151 16046 16927 -23 -455 149 O ATOM 1129 N GLY A 161 62.434 -9.264 -3.517 1.00 74.69 N ANISOU 1129 N GLY A 161 6965 9756 11658 470 -1145 275 N ATOM 1130 CA GLY A 161 61.986 -9.658 -2.196 1.00 67.78 C ANISOU 1130 CA GLY A 161 6268 8701 10784 450 -1300 374 C ATOM 1131 C GLY A 161 60.630 -9.106 -1.816 1.00 68.11 C ANISOU 1131 C GLY A 161 6565 8593 10721 291 -1246 441 C ATOM 1132 O GLY A 161 60.321 -8.978 -0.632 1.00 75.79 O ANISOU 1132 O GLY A 161 7678 9466 11651 203 -1346 538 O ATOM 1133 N VAL A 162 59.823 -8.764 -2.814 1.00 60.83 N ANISOU 1133 N VAL A 162 5699 7664 9749 260 -1089 390 N ATOM 1134 CA VAL A 162 58.449 -8.340 -2.559 1.00 59.73 C ANISOU 1134 CA VAL A 162 5785 7391 9518 144 -1032 441 C ATOM 1135 C VAL A 162 57.478 -9.515 -2.732 1.00 61.51 C ANISOU 1135 C VAL A 162 6139 7445 9788 254 -1052 412 C ATOM 1136 O VAL A 162 57.417 -10.128 -3.800 1.00 61.38 O ANISOU 1136 O VAL A 162 6064 7439 9818 374 -993 314 O ATOM 1137 CB VAL A 162 58.032 -7.180 -3.477 1.00 59.63 C ANISOU 1137 CB VAL A 162 5777 7469 9410 34 -860 416 C ATOM 1138 CG1 VAL A 162 56.654 -6.687 -3.102 1.00 47.83 C ANISOU 1138 CG1 VAL A 162 4501 5851 7821 -69 -813 473 C ATOM 1139 CG2 VAL A 162 59.048 -6.040 -3.394 1.00 58.01 C ANISOU 1139 CG2 VAL A 162 5451 7428 9163 -93 -835 441 C ATOM 1140 N LEU A 163 56.743 -9.831 -1.666 1.00 65.88 N ANISOU 1140 N LEU A 163 6870 7842 10318 203 -1135 496 N ATOM 1141 CA LEU A 163 55.729 -10.894 -1.672 1.00 59.42 C ANISOU 1141 CA LEU A 163 6197 6850 9531 260 -1158 487 C ATOM 1142 C LEU A 163 54.418 -10.426 -2.315 1.00 58.72 C ANISOU 1142 C LEU A 163 6204 6746 9363 178 -1020 464 C ATOM 1143 O LEU A 163 53.930 -9.333 -2.020 1.00 52.74 O ANISOU 1143 O LEU A 163 5505 6030 8505 46 -952 516 O ATOM 1144 CB LEU A 163 55.469 -11.377 -0.247 1.00 50.95 C ANISOU 1144 CB LEU A 163 5276 5632 8450 217 -1294 597 C ATOM 1145 CG LEU A 163 54.445 -12.500 -0.063 1.00 55.51 C ANISOU 1145 CG LEU A 163 6021 6016 9052 241 -1331 610 C ATOM 1146 CD1 LEU A 163 54.782 -13.337 1.175 1.00 57.18 C ANISOU 1146 CD1 LEU A 163 6333 6095 9298 271 -1504 705 C ATOM 1147 CD2 LEU A 163 53.031 -11.949 0.016 1.00 46.64 C ANISOU 1147 CD2 LEU A 163 5030 4863 7827 95 -1224 641 C ATOM 1148 N LYS A 164 53.867 -11.250 -3.203 1.00 60.13 N ANISOU 1148 N LYS A 164 6397 6867 9583 264 -984 381 N ATOM 1149 CA LYS A 164 52.616 -10.924 -3.893 1.00 55.60 C ANISOU 1149 CA LYS A 164 5894 6293 8939 202 -869 351 C ATOM 1150 C LYS A 164 51.663 -12.078 -3.749 1.00 56.19 C ANISOU 1150 C LYS A 164 6096 6204 9051 216 -918 343 C ATOM 1151 O LYS A 164 52.037 -13.231 -4.008 1.00 56.50 O ANISOU 1151 O LYS A 164 6129 6155 9183 333 -990 285 O ATOM 1152 CB LYS A 164 52.832 -10.706 -5.392 1.00 51.11 C ANISOU 1152 CB LYS A 164 5207 5848 8366 273 -759 237 C ATOM 1153 CG LYS A 164 54.036 -9.875 -5.765 1.00 54.71 C ANISOU 1153 CG LYS A 164 5505 6471 8812 283 -713 221 C ATOM 1154 CD LYS A 164 53.735 -8.410 -5.671 1.00 54.60 C ANISOU 1154 CD LYS A 164 5521 6540 8683 141 -623 284 C ATOM 1155 CE LYS A 164 54.755 -7.594 -6.440 1.00 54.63 C ANISOU 1155 CE LYS A 164 5375 6719 8663 134 -543 250 C ATOM 1156 NZ LYS A 164 54.482 -6.124 -6.258 1.00 59.38 N ANISOU 1156 NZ LYS A 164 6041 7369 9151 -15 -466 321 N ATOM 1157 N LEU A 165 50.430 -11.781 -3.351 1.00 51.06 N ANISOU 1157 N LEU A 165 5562 5512 8325 97 -878 397 N ATOM 1158 CA LEU A 165 49.369 -12.777 -3.429 1.00 51.85 C ANISOU 1158 CA LEU A 165 5767 5487 8447 78 -897 379 C ATOM 1159 C LEU A 165 49.031 -12.958 -4.906 1.00 52.21 C ANISOU 1159 C LEU A 165 5748 5592 8499 141 -819 252 C ATOM 1160 O LEU A 165 48.893 -11.985 -5.638 1.00 58.64 O ANISOU 1160 O LEU A 165 6492 6546 9244 128 -715 222 O ATOM 1161 CB LEU A 165 48.141 -12.328 -2.651 1.00 59.62 C ANISOU 1161 CB LEU A 165 6860 6452 9341 -68 -859 465 C ATOM 1162 CG LEU A 165 48.324 -12.025 -1.167 1.00 64.95 C ANISOU 1162 CG LEU A 165 7619 7083 9977 -149 -920 590 C ATOM 1163 CD1 LEU A 165 47.025 -11.503 -0.553 1.00 66.07 C ANISOU 1163 CD1 LEU A 165 7852 7235 10015 -282 -851 655 C ATOM 1164 CD2 LEU A 165 48.801 -13.271 -0.461 1.00 70.53 C ANISOU 1164 CD2 LEU A 165 8401 7630 10765 -110 -1061 630 C ATOM 1165 N ALA A 166 48.925 -14.202 -5.348 1.00 49.96 N ANISOU 1165 N ALA A 166 5500 5193 8289 209 -873 177 N ATOM 1166 CA ALA A 166 48.742 -14.488 -6.764 1.00 49.38 C ANISOU 1166 CA ALA A 166 5372 5171 8220 280 -813 42 C ATOM 1167 C ALA A 166 47.578 -15.440 -6.973 1.00 55.60 C ANISOU 1167 C ALA A 166 6270 5837 9019 221 -838 2 C ATOM 1168 O ALA A 166 47.045 -15.997 -6.004 1.00 53.51 O ANISOU 1168 O ALA A 166 6122 5436 8772 133 -907 82 O ATOM 1169 CB ALA A 166 50.018 -15.087 -7.341 1.00 49.19 C ANISOU 1169 CB ALA A 166 5263 5146 8282 451 -849 -52 C ATOM 1170 N ASP A 167 47.188 -15.636 -8.233 1.00 53.97 N ANISOU 1170 N ASP A 167 6030 5684 8793 257 -786 -120 N ATOM 1171 CA ASP A 167 46.167 -16.634 -8.559 1.00 65.04 C ANISOU 1171 CA ASP A 167 7529 6972 10209 197 -821 -179 C ATOM 1172 C ASP A 167 44.807 -16.342 -7.943 1.00 57.99 C ANISOU 1172 C ASP A 167 6694 6088 9252 20 -801 -91 C ATOM 1173 O ASP A 167 44.412 -16.980 -6.971 1.00 56.88 O ANISOU 1173 O ASP A 167 6661 5806 9144 -71 -868 -14 O ATOM 1174 CB ASP A 167 46.617 -18.025 -8.120 1.00 74.45 C ANISOU 1174 CB ASP A 167 8834 7940 11513 253 -941 -198 C ATOM 1175 CG ASP A 167 47.692 -18.588 -9.015 1.00102.76 C ANISOU 1175 CG ASP A 167 12370 11510 15164 445 -956 -333 C ATOM 1176 OD1 ASP A 167 47.424 -18.729 -10.229 1.00108.32 O ANISOU 1176 OD1 ASP A 167 13044 12275 15837 482 -904 -465 O ATOM 1177 OD2 ASP A 167 48.802 -18.881 -8.509 1.00114.13 O ANISOU 1177 OD2 ASP A 167 13796 12889 16680 565 -1020 -309 O ATOM 1178 N PHE A 168 44.089 -15.400 -8.540 1.00 48.64 N ANISOU 1178 N PHE A 168 5435 5073 7972 -23 -708 -102 N ATOM 1179 CA PHE A 168 42.768 -15.018 -8.064 1.00 58.69 C ANISOU 1179 CA PHE A 168 6729 6394 9177 -168 -675 -31 C ATOM 1180 C PHE A 168 41.645 -15.701 -8.840 1.00 54.73 C ANISOU 1180 C PHE A 168 6239 5895 8660 -240 -683 -119 C ATOM 1181 O PHE A 168 40.499 -15.266 -8.796 1.00 58.26 O ANISOU 1181 O PHE A 168 6655 6443 9038 -339 -640 -88 O ATOM 1182 CB PHE A 168 42.627 -13.485 -8.092 1.00 56.33 C ANISOU 1182 CB PHE A 168 6349 6276 8778 -162 -577 25 C ATOM 1183 CG PHE A 168 43.371 -12.807 -6.986 1.00 55.96 C ANISOU 1183 CG PHE A 168 6319 6213 8730 -161 -578 136 C ATOM 1184 CD1 PHE A 168 42.711 -12.407 -5.832 1.00 39.50 C ANISOU 1184 CD1 PHE A 168 4287 4120 6600 -265 -566 246 C ATOM 1185 CD2 PHE A 168 44.756 -12.635 -7.065 1.00 54.08 C ANISOU 1185 CD2 PHE A 168 6042 5972 8534 -59 -594 124 C ATOM 1186 CE1 PHE A 168 43.415 -11.794 -4.786 1.00 45.33 C ANISOU 1186 CE1 PHE A 168 5056 4841 7327 -270 -575 341 C ATOM 1187 CE2 PHE A 168 45.463 -12.030 -6.027 1.00 45.26 C ANISOU 1187 CE2 PHE A 168 4938 4845 7413 -72 -610 222 C ATOM 1188 CZ PHE A 168 44.792 -11.605 -4.887 1.00 45.42 C ANISOU 1188 CZ PHE A 168 5029 4847 7381 -179 -604 329 C ATOM 1189 N GLY A 169 41.979 -16.783 -9.533 1.00 50.22 N ANISOU 1189 N GLY A 169 5712 5215 8154 -188 -742 -232 N ATOM 1190 CA GLY A 169 41.027 -17.463 -10.394 1.00 42.70 C ANISOU 1190 CA GLY A 169 4777 4263 7185 -257 -760 -338 C ATOM 1191 C GLY A 169 39.893 -18.141 -9.655 1.00 48.28 C ANISOU 1191 C GLY A 169 5561 4879 7903 -445 -804 -282 C ATOM 1192 O GLY A 169 38.877 -18.486 -10.251 1.00 70.87 O ANISOU 1192 O GLY A 169 8409 7787 10731 -545 -810 -348 O ATOM 1193 N LEU A 170 40.071 -18.345 -8.357 1.00 53.38 N ANISOU 1193 N LEU A 170 6287 5405 8590 -505 -837 -159 N ATOM 1194 CA LEU A 170 39.016 -18.895 -7.519 1.00 56.16 C ANISOU 1194 CA LEU A 170 6714 5687 8939 -703 -863 -82 C ATOM 1195 C LEU A 170 38.524 -17.847 -6.531 1.00 57.72 C ANISOU 1195 C LEU A 170 6854 6016 9062 -772 -789 55 C ATOM 1196 O LEU A 170 37.652 -18.124 -5.706 1.00 54.38 O ANISOU 1196 O LEU A 170 6473 5571 8618 -938 -787 136 O ATOM 1197 CB LEU A 170 39.508 -20.112 -6.744 1.00 61.05 C ANISOU 1197 CB LEU A 170 7507 6039 9651 -735 -966 -41 C ATOM 1198 CG LEU A 170 39.940 -21.373 -7.497 1.00 73.41 C ANISOU 1198 CG LEU A 170 9180 7411 11301 -676 -1054 -170 C ATOM 1199 CD1 LEU A 170 39.992 -22.561 -6.533 1.00 72.68 C ANISOU 1199 CD1 LEU A 170 9288 7047 11281 -768 -1156 -95 C ATOM 1200 CD2 LEU A 170 39.018 -21.671 -8.659 1.00 69.84 C ANISOU 1200 CD2 LEU A 170 8690 7033 10816 -753 -1042 -305 C ATOM 1201 N ALA A 171 39.090 -16.643 -6.598 1.00 47.41 N ANISOU 1201 N ALA A 171 5460 4843 7710 -651 -725 79 N ATOM 1202 CA ALA A 171 38.652 -15.590 -5.695 1.00 45.67 C ANISOU 1202 CA ALA A 171 5203 4739 7413 -700 -652 194 C ATOM 1203 C ALA A 171 37.214 -15.141 -6.011 1.00 57.90 C ANISOU 1203 C ALA A 171 6656 6464 8880 -793 -583 183 C ATOM 1204 O ALA A 171 36.649 -15.464 -7.053 1.00 57.53 O ANISOU 1204 O ALA A 171 6553 6479 8828 -805 -592 84 O ATOM 1205 CB ALA A 171 39.595 -14.425 -5.741 1.00 41.86 C ANISOU 1205 CB ALA A 171 4667 4338 6899 -562 -606 216 C ATOM 1206 N ARG A 172 36.639 -14.374 -5.101 1.00 54.75 N ANISOU 1206 N ARG A 172 6234 6155 8411 -849 -518 282 N ATOM 1207 CA ARG A 172 35.248 -14.011 -5.191 1.00 51.46 C ANISOU 1207 CA ARG A 172 5720 5910 7922 -935 -454 284 C ATOM 1208 C ARG A 172 34.981 -12.781 -4.322 1.00 51.69 C ANISOU 1208 C ARG A 172 5722 6055 7865 -910 -363 378 C ATOM 1209 O ARG A 172 35.505 -12.672 -3.216 1.00 53.99 O ANISOU 1209 O ARG A 172 6103 6256 8153 -930 -363 466 O ATOM 1210 CB ARG A 172 34.398 -15.197 -4.712 1.00 57.68 C ANISOU 1210 CB ARG A 172 6552 6623 8739 -1135 -493 302 C ATOM 1211 CG ARG A 172 33.154 -14.799 -3.977 1.00 66.75 C ANISOU 1211 CG ARG A 172 7629 7924 9810 -1257 -413 372 C ATOM 1212 CD ARG A 172 32.305 -15.978 -3.596 1.00 77.45 C ANISOU 1212 CD ARG A 172 9019 9221 11190 -1480 -446 389 C ATOM 1213 NE ARG A 172 30.908 -15.569 -3.460 1.00 86.48 N ANISOU 1213 NE ARG A 172 10013 10590 12255 -1581 -363 403 N ATOM 1214 CZ ARG A 172 30.037 -15.532 -4.466 1.00 87.36 C ANISOU 1214 CZ ARG A 172 9976 10869 12347 -1597 -361 313 C ATOM 1215 NH1 ARG A 172 30.406 -15.887 -5.688 1.00 88.79 N ANISOU 1215 NH1 ARG A 172 10155 11008 12572 -1528 -434 201 N ATOM 1216 NH2 ARG A 172 28.793 -15.142 -4.251 1.00 92.94 N ANISOU 1216 NH2 ARG A 172 10531 11797 12984 -1678 -286 333 N ATOM 1217 N ALA A 173 34.169 -11.855 -4.822 1.00 54.16 N ANISOU 1217 N ALA A 173 5916 6562 8100 -858 -290 355 N ATOM 1218 CA ALA A 173 33.667 -10.751 -3.996 1.00 54.94 C ANISOU 1218 CA ALA A 173 5990 6774 8109 -837 -197 432 C ATOM 1219 C ALA A 173 32.702 -11.258 -2.921 1.00 51.33 C ANISOU 1219 C ALA A 173 5535 6341 7629 -1005 -167 497 C ATOM 1220 O ALA A 173 31.991 -12.239 -3.128 1.00 52.67 O ANISOU 1220 O ALA A 173 5666 6516 7830 -1140 -199 469 O ATOM 1221 CB ALA A 173 32.974 -9.717 -4.867 1.00 44.92 C ANISOU 1221 CB ALA A 173 4599 5701 6767 -723 -137 388 C ATOM 1222 N PHE A 174 32.672 -10.595 -1.772 1.00 53.04 N ANISOU 1222 N PHE A 174 5800 6573 7782 -1009 -101 582 N ATOM 1223 CA PHE A 174 31.728 -10.973 -0.724 1.00 54.58 C ANISOU 1223 CA PHE A 174 5990 6816 7931 -1167 -51 648 C ATOM 1224 C PHE A 174 30.991 -9.755 -0.186 1.00 66.06 C ANISOU 1224 C PHE A 174 7378 8448 9274 -1100 70 678 C ATOM 1225 O PHE A 174 31.292 -8.620 -0.568 1.00 67.68 O ANISOU 1225 O PHE A 174 7571 8704 9442 -931 104 655 O ATOM 1226 CB PHE A 174 32.426 -11.746 0.410 1.00 59.74 C ANISOU 1226 CB PHE A 174 6811 7276 8612 -1280 -102 734 C ATOM 1227 CG PHE A 174 33.305 -10.893 1.302 1.00 69.93 C ANISOU 1227 CG PHE A 174 8210 8506 9853 -1196 -83 799 C ATOM 1228 CD1 PHE A 174 34.629 -10.627 0.959 1.00 67.25 C ANISOU 1228 CD1 PHE A 174 7935 8052 9564 -1074 -150 780 C ATOM 1229 CD2 PHE A 174 32.819 -10.384 2.497 1.00 68.35 C ANISOU 1229 CD2 PHE A 174 8046 8373 9551 -1248 3 873 C ATOM 1230 CE1 PHE A 174 35.447 -9.862 1.789 1.00 59.79 C ANISOU 1230 CE1 PHE A 174 7087 7058 8573 -1019 -144 837 C ATOM 1231 CE2 PHE A 174 33.635 -9.613 3.327 1.00 65.69 C ANISOU 1231 CE2 PHE A 174 7824 7977 9160 -1183 11 924 C ATOM 1232 CZ PHE A 174 34.951 -9.357 2.969 1.00 63.52 C ANISOU 1232 CZ PHE A 174 7611 7584 8941 -1075 -68 907 C ATOM 1233 N SER A 175 30.027 -9.996 0.699 1.00 86.88 N ANISOU 1233 N SER A 175 9980 11175 11854 -1232 139 728 N ATOM 1234 CA SER A 175 29.191 -8.928 1.243 1.00 98.05 C ANISOU 1234 CA SER A 175 11320 12777 13160 -1165 265 745 C ATOM 1235 C SER A 175 28.544 -9.321 2.564 1.00107.29 C ANISOU 1235 C SER A 175 12515 13988 14263 -1333 338 823 C ATOM 1236 O SER A 175 29.045 -10.186 3.287 1.00102.97 O ANISOU 1236 O SER A 175 12104 13281 13740 -1477 288 888 O ATOM 1237 CB SER A 175 28.096 -8.570 0.245 1.00 95.46 C ANISOU 1237 CB SER A 175 10784 12670 12815 -1094 301 672 C ATOM 1238 OG SER A 175 27.347 -9.725 -0.085 1.00 93.82 O ANISOU 1238 OG SER A 175 10477 12516 12655 -1274 264 649 O ATOM 1239 N LEU A 176 27.426 -8.665 2.868 1.00124.29 N ANISOU 1239 N LEU A 176 14538 16362 16325 -1303 460 817 N ATOM 1240 CA LEU A 176 26.609 -8.986 4.036 1.00136.59 C ANISOU 1240 CA LEU A 176 16078 18017 17801 -1465 557 881 C ATOM 1241 C LEU A 176 25.129 -8.840 3.704 1.00139.06 C ANISOU 1241 C LEU A 176 16145 18617 18074 -1480 650 837 C ATOM 1242 O LEU A 176 24.677 -7.747 3.376 1.00141.58 O ANISOU 1242 O LEU A 176 16356 19096 18343 -1284 717 788 O ATOM 1243 CB LEU A 176 26.955 -8.068 5.211 1.00139.42 C ANISOU 1243 CB LEU A 176 16569 18353 18049 -1386 641 931 C ATOM 1244 CG LEU A 176 28.175 -8.416 6.064 1.00142.00 C ANISOU 1244 CG LEU A 176 17135 18438 18380 -1452 569 1007 C ATOM 1245 CD1 LEU A 176 28.137 -7.637 7.367 1.00140.22 C ANISOU 1245 CD1 LEU A 176 17013 18249 18013 -1429 674 1055 C ATOM 1246 CD2 LEU A 176 28.218 -9.908 6.346 1.00146.55 C ANISOU 1246 CD2 LEU A 176 17770 18898 19013 -1689 495 1068 C ATOM 1247 N PRO A 182 21.666 -13.852 4.052 1.00133.24 N ANISOU 1247 N PRO A 182 15047 18151 17426 -2660 640 926 N ATOM 1248 CA PRO A 182 22.243 -15.170 4.337 1.00132.58 C ANISOU 1248 CA PRO A 182 15180 17788 17405 -2892 540 990 C ATOM 1249 C PRO A 182 22.983 -15.703 3.110 1.00129.22 C ANISOU 1249 C PRO A 182 14826 17161 17111 -2832 371 910 C ATOM 1250 O PRO A 182 22.366 -16.354 2.265 1.00135.17 O ANISOU 1250 O PRO A 182 15460 17980 17919 -2960 316 843 O ATOM 1251 CB PRO A 182 21.011 -16.038 4.634 1.00134.85 C ANISOU 1251 CB PRO A 182 15334 18239 17663 -3214 601 1021 C ATOM 1252 CG PRO A 182 19.858 -15.069 4.804 1.00134.55 C ANISOU 1252 CG PRO A 182 15011 18586 17526 -3135 761 990 C ATOM 1253 CD PRO A 182 20.199 -13.904 3.943 1.00133.50 C ANISOU 1253 CD PRO A 182 14795 18514 17413 -2787 735 896 C ATOM 1254 N ASN A 183 24.282 -15.426 3.013 1.00115.42 N ANISOU 1254 N ASN A 183 13264 15184 15407 -2645 292 911 N ATOM 1255 CA ASN A 183 25.063 -15.781 1.827 1.00103.61 C ANISOU 1255 CA ASN A 183 11826 13519 14024 -2544 150 825 C ATOM 1256 C ASN A 183 25.213 -17.287 1.611 1.00 99.96 C ANISOU 1256 C ASN A 183 11495 12835 13648 -2770 35 828 C ATOM 1257 O ASN A 183 25.423 -18.042 2.560 1.00100.27 O ANISOU 1257 O ASN A 183 11711 12707 13681 -2941 24 929 O ATOM 1258 CB ASN A 183 26.452 -15.138 1.888 1.00100.72 C ANISOU 1258 CB ASN A 183 11618 12973 13678 -2306 105 834 C ATOM 1259 CG ASN A 183 26.404 -13.620 1.832 1.00 92.86 C ANISOU 1259 CG ASN A 183 10514 12158 12610 -2065 196 809 C ATOM 1260 OD1 ASN A 183 25.534 -13.037 1.187 1.00 87.06 O ANISOU 1260 OD1 ASN A 183 9575 11658 11845 -1995 248 744 O ATOM 1261 ND2 ASN A 183 27.355 -12.975 2.502 1.00 88.09 N ANISOU 1261 ND2 ASN A 183 10055 11439 11975 -1935 206 861 N ATOM 1262 N ARG A 184 25.111 -17.715 0.356 1.00 94.11 N ANISOU 1262 N ARG A 184 10688 12088 12983 -2764 -55 715 N ATOM 1263 CA ARG A 184 25.320 -19.116 0.009 1.00100.51 C ANISOU 1263 CA ARG A 184 11645 12664 13882 -2950 -176 694 C ATOM 1264 C ARG A 184 26.472 -19.240 -0.967 1.00102.74 C ANISOU 1264 C ARG A 184 12036 12746 14254 -2752 -296 604 C ATOM 1265 O ARG A 184 26.267 -19.569 -2.135 1.00107.62 O ANISOU 1265 O ARG A 184 12584 13389 14917 -2749 -364 485 O ATOM 1266 CB ARG A 184 24.072 -19.729 -0.630 1.00102.97 C ANISOU 1266 CB ARG A 184 11787 13139 14196 -3175 -183 625 C ATOM 1267 CG ARG A 184 23.017 -20.210 0.340 1.00109.27 C ANISOU 1267 CG ARG A 184 12536 14048 14932 -3477 -96 720 C ATOM 1268 CD ARG A 184 21.796 -20.692 -0.420 1.00120.43 C ANISOU 1268 CD ARG A 184 13743 15665 16351 -3687 -109 636 C ATOM 1269 NE ARG A 184 20.694 -21.046 0.468 1.00136.65 N ANISOU 1269 NE ARG A 184 15700 17883 18336 -3984 -6 723 N ATOM 1270 CZ ARG A 184 19.531 -21.539 0.050 1.00151.37 C ANISOU 1270 CZ ARG A 184 17374 19946 20195 -4230 -3 673 C ATOM 1271 NH1 ARG A 184 19.319 -21.734 -1.246 1.00155.93 N ANISOU 1271 NH1 ARG A 184 17847 20573 20826 -4207 -107 535 N ATOM 1272 NH2 ARG A 184 18.577 -21.839 0.924 1.00154.32 N ANISOU 1272 NH2 ARG A 184 17656 20480 20500 -4508 105 761 N ATOM 1273 N TYR A 185 27.684 -18.976 -0.493 1.00 97.39 N ANISOU 1273 N TYR A 185 11523 11885 13595 -2589 -322 656 N ATOM 1274 CA TYR A 185 28.860 -19.106 -1.341 1.00 89.38 C ANISOU 1274 CA TYR A 185 10606 10690 12665 -2398 -425 575 C ATOM 1275 C TYR A 185 29.190 -20.579 -1.508 1.00 88.05 C ANISOU 1275 C TYR A 185 10627 10241 12586 -2540 -547 556 C ATOM 1276 O TYR A 185 28.790 -21.405 -0.694 1.00 93.70 O ANISOU 1276 O TYR A 185 11453 10851 13296 -2767 -553 644 O ATOM 1277 CB TYR A 185 30.051 -18.347 -0.751 1.00 83.65 C ANISOU 1277 CB TYR A 185 9976 9877 11930 -2190 -416 637 C ATOM 1278 CG TYR A 185 29.782 -16.880 -0.493 1.00 82.44 C ANISOU 1278 CG TYR A 185 9678 9961 11684 -2052 -298 660 C ATOM 1279 CD1 TYR A 185 28.965 -16.143 -1.347 1.00 79.42 C ANISOU 1279 CD1 TYR A 185 9087 9828 11262 -1984 -241 579 C ATOM 1280 CD2 TYR A 185 30.355 -16.225 0.597 1.00 80.52 C ANISOU 1280 CD2 TYR A 185 9520 9684 11388 -1982 -252 759 C ATOM 1281 CE1 TYR A 185 28.720 -14.796 -1.122 1.00 77.69 C ANISOU 1281 CE1 TYR A 185 8758 9803 10958 -1840 -138 598 C ATOM 1282 CE2 TYR A 185 30.117 -14.876 0.834 1.00 74.99 C ANISOU 1282 CE2 TYR A 185 8714 9179 10600 -1853 -146 770 C ATOM 1283 CZ TYR A 185 29.300 -14.168 -0.032 1.00 76.66 C ANISOU 1283 CZ TYR A 185 8728 9619 10779 -1776 -88 690 C ATOM 1284 OH TYR A 185 29.050 -12.834 0.189 1.00 72.72 O ANISOU 1284 OH TYR A 185 8144 9293 10194 -1632 13 699 O HETATM 1285 N TPO A 186 29.918 -20.902 -2.568 1.00 84.95 N ANISOU 1285 N TPO A 186 10281 9725 12270 -2405 -639 442 N HETATM 1286 CA TPO A 186 30.295 -22.314 -2.873 1.00 86.63 C ANISOU 1286 CA TPO A 186 10691 9651 12575 -2503 -763 397 C HETATM 1287 CB TPO A 186 30.765 -22.285 -4.321 1.00 82.32 C ANISOU 1287 CB TPO A 186 10097 9105 12076 -2327 -821 231 C HETATM 1288 CG2 TPO A 186 31.801 -23.357 -4.638 1.00 71.45 C ANISOU 1288 CG2 TPO A 186 8941 7406 10800 -2261 -943 174 C HETATM 1289 OG1 TPO A 186 31.309 -20.982 -4.506 1.00 91.79 O ANISOU 1289 OG1 TPO A 186 11174 10466 13237 -2084 -756 229 O HETATM 1290 P TPO A 186 31.017 -20.067 -5.798 1.00 84.75 P ANISOU 1290 P TPO A 186 10078 9823 12300 -1937 -719 107 P HETATM 1291 O1P TPO A 186 32.198 -20.328 -6.716 1.00 71.11 O ANISOU 1291 O1P TPO A 186 8436 7946 10636 -1746 -791 1 O HETATM 1292 O2P TPO A 186 29.701 -20.589 -6.322 1.00106.18 O ANISOU 1292 O2P TPO A 186 12692 12660 14991 -2146 -731 42 O HETATM 1293 O3P TPO A 186 30.929 -18.691 -5.183 1.00 77.23 O ANISOU 1293 O3P TPO A 186 9008 9066 11270 -1830 -609 197 O HETATM 1294 C TPO A 186 31.300 -22.892 -1.898 1.00 91.82 C ANISOU 1294 C TPO A 186 11587 10022 13277 -2479 -824 504 C HETATM 1295 O TPO A 186 32.189 -22.191 -1.403 1.00 83.48 O ANISOU 1295 O TPO A 186 10551 8958 12211 -2296 -808 563 O ATOM 1296 N ASN A 187 31.087 -24.151 -1.533 1.00 95.68 N ANISOU 1296 N ASN A 187 12268 10271 13813 -2671 -905 532 N ATOM 1297 CA ASN A 187 31.914 -24.807 -0.530 1.00100.57 C ANISOU 1297 CA ASN A 187 13135 10615 14462 -2691 -972 659 C ATOM 1298 C ASN A 187 33.043 -25.534 -1.228 1.00105.79 C ANISOU 1298 C ASN A 187 13976 10985 15233 -2503 -1105 590 C ATOM 1299 O ASN A 187 33.932 -26.101 -0.591 1.00104.40 O ANISOU 1299 O ASN A 187 13958 10626 15083 -2400 -1164 683 O ATOM 1300 CB ASN A 187 31.081 -25.793 0.290 1.00110.35 C ANISOU 1300 CB ASN A 187 14502 11748 15676 -3026 -977 754 C ATOM 1301 CG ASN A 187 31.806 -26.277 1.531 1.00111.02 C ANISOU 1301 CG ASN A 187 14808 11635 15738 -3079 -1006 933 C ATOM 1302 OD1 ASN A 187 33.002 -26.566 1.493 1.00114.50 O ANISOU 1302 OD1 ASN A 187 15198 12202 16105 -3006 -935 1034 O ATOM 1303 ND2 ASN A 187 31.082 -26.367 2.641 1.00108.62 N ANISOU 1303 ND2 ASN A 187 14766 11014 15490 -3210 -1115 975 N ATOM 1304 N ARG A 188 33.015 -25.522 -2.555 1.00115.50 N ANISOU 1304 N ARG A 188 15179 12185 16521 -2450 -1154 423 N ATOM 1305 CA ARG A 188 34.092 -26.118 -3.336 1.00122.39 C ANISOU 1305 CA ARG A 188 16206 12804 17495 -2255 -1268 329 C ATOM 1306 C ARG A 188 35.252 -25.132 -3.393 1.00112.62 C ANISOU 1306 C ARG A 188 14889 11628 16273 -1941 -1257 318 C ATOM 1307 O ARG A 188 35.715 -24.764 -4.473 1.00115.58 O ANISOU 1307 O ARG A 188 15264 11943 16709 -1738 -1304 188 O ATOM 1308 CB ARG A 188 33.610 -26.445 -4.750 1.00133.83 C ANISOU 1308 CB ARG A 188 17614 14259 18976 -2265 -1302 135 C ATOM 1309 CG ARG A 188 34.731 -26.669 -5.752 1.00137.97 C ANISOU 1309 CG ARG A 188 17865 15115 19443 -2149 -1213 31 C ATOM 1310 CD ARG A 188 34.531 -25.828 -7.002 1.00143.43 C ANISOU 1310 CD ARG A 188 18548 15771 20180 -1952 -1261 -158 C ATOM 1311 NE ARG A 188 35.379 -26.274 -8.103 1.00146.52 N ANISOU 1311 NE ARG A 188 18981 16068 20622 -1665 -1284 -162 N ATOM 1312 CZ ARG A 188 36.484 -25.648 -8.495 1.00143.90 C ANISOU 1312 CZ ARG A 188 18606 15756 20315 -1445 -1295 -308 C ATOM 1313 NH1 ARG A 188 36.879 -24.544 -7.876 1.00146.28 N ANISOU 1313 NH1 ARG A 188 18835 16158 20586 -1473 -1291 -463 N ATOM 1314 NH2 ARG A 188 37.195 -26.126 -9.508 1.00137.23 N ANISOU 1314 NH2 ARG A 188 17781 14842 19517 -1201 -1310 -300 N ATOM 1315 N VAL A 189 35.711 -24.700 -2.222 1.00101.54 N ANISOU 1315 N VAL A 189 13420 10351 14810 -1906 -1193 449 N ATOM 1316 CA VAL A 189 36.738 -23.670 -2.144 1.00 88.42 C ANISOU 1316 CA VAL A 189 11645 8804 13147 -1645 -1166 433 C ATOM 1317 C VAL A 189 37.956 -24.039 -1.300 1.00 82.24 C ANISOU 1317 C VAL A 189 11009 7830 12409 -1512 -1249 531 C ATOM 1318 O VAL A 189 37.836 -24.592 -0.207 1.00 77.34 O ANISOU 1318 O VAL A 189 10552 7058 11775 -1640 -1293 667 O ATOM 1319 CB VAL A 189 36.161 -22.335 -1.637 1.00 88.06 C ANISOU 1319 CB VAL A 189 11399 9062 12997 -1663 -1034 482 C ATOM 1320 CG1 VAL A 189 35.322 -21.675 -2.720 1.00 83.16 C ANISOU 1320 CG1 VAL A 189 10598 8655 12342 -1695 -968 357 C ATOM 1321 CG2 VAL A 189 35.339 -22.557 -0.377 1.00 90.40 C ANISOU 1321 CG2 VAL A 189 11751 9379 13219 -1875 -989 640 C ATOM 1322 N VAL A 190 39.128 -23.712 -1.833 1.00 83.43 N ANISOU 1322 N VAL A 190 11095 7999 12606 -1258 -1272 462 N ATOM 1323 CA VAL A 190 40.412 -23.867 -1.139 1.00 82.29 C ANISOU 1323 CA VAL A 190 11047 7711 12511 -1094 -1360 535 C ATOM 1324 C VAL A 190 40.947 -25.290 -1.233 1.00 82.67 C ANISOU 1324 C VAL A 190 11305 7444 12662 -1040 -1498 505 C ATOM 1325 O VAL A 190 40.223 -26.246 -0.975 1.00 82.09 O ANISOU 1325 O VAL A 190 11398 7197 12596 -1225 -1541 540 O ATOM 1326 CB VAL A 190 40.322 -23.485 0.362 1.00 71.29 C ANISOU 1326 CB VAL A 190 9716 6331 11042 -1197 -1352 724 C ATOM 1327 CG1 VAL A 190 41.714 -23.530 1.020 1.00 61.37 C ANISOU 1327 CG1 VAL A 190 8529 4960 9827 -1010 -1454 793 C ATOM 1328 CG2 VAL A 190 39.639 -22.117 0.551 1.00 55.17 C ANISOU 1328 CG2 VAL A 190 7493 4581 8888 -1266 -1209 755 C ATOM 1329 N THR A 191 42.219 -25.427 -1.592 1.00 86.78 N ANISOU 1329 N THR A 191 11820 7891 13261 -786 -1567 442 N ATOM 1330 CA THR A 191 42.867 -26.732 -1.592 1.00 84.38 C ANISOU 1330 CA THR A 191 11723 7278 13059 -685 -1706 418 C ATOM 1331 C THR A 191 42.668 -27.413 -0.247 1.00 89.88 C ANISOU 1331 C THR A 191 12646 7764 13740 -827 -1792 601 C ATOM 1332 O THR A 191 42.708 -26.764 0.801 1.00 88.77 O ANISOU 1332 O THR A 191 12481 7720 13528 -882 -1772 749 O ATOM 1333 CB THR A 191 44.365 -26.615 -1.880 1.00 89.52 C ANISOU 1333 CB THR A 191 12306 7923 13786 -373 -1764 358 C ATOM 1334 OG1 THR A 191 44.555 -26.422 -3.284 1.00 90.14 O ANISOU 1334 OG1 THR A 191 12243 8116 13892 -244 -1704 165 O ATOM 1335 CG2 THR A 191 45.101 -27.877 -1.443 1.00 98.87 C ANISOU 1335 CG2 THR A 191 13721 8782 15064 -252 -1925 391 C ATOM 1336 N LEU A 192 42.455 -28.725 -0.286 1.00 90.83 N ANISOU 1336 N LEU A 192 13003 7590 13919 -890 -1889 591 N ATOM 1337 CA LEU A 192 42.132 -29.497 0.909 1.00 90.28 C ANISOU 1337 CA LEU A 192 13184 7293 13827 -1061 -1970 768 C ATOM 1338 C LEU A 192 43.053 -29.251 2.120 1.00 84.98 C ANISOU 1338 C LEU A 192 12565 6587 13135 -942 -2047 933 C ATOM 1339 O LEU A 192 42.573 -29.086 3.243 1.00 92.64 O ANISOU 1339 O LEU A 192 13613 7572 14013 -1127 -2033 1104 O ATOM 1340 CB LEU A 192 42.087 -30.994 0.579 1.00 87.60 C ANISOU 1340 CB LEU A 192 13117 6593 13574 -1079 -2089 716 C ATOM 1341 CG LEU A 192 41.634 -31.873 1.746 1.00 92.88 C ANISOU 1341 CG LEU A 192 14078 7003 14210 -1294 -2170 904 C ATOM 1342 CD1 LEU A 192 40.134 -31.714 2.011 1.00 87.48 C ANISOU 1342 CD1 LEU A 192 13375 6440 13426 -1670 -2056 967 C ATOM 1343 CD2 LEU A 192 42.006 -33.335 1.508 1.00105.76 C ANISOU 1343 CD2 LEU A 192 16012 8227 15944 -1220 -2322 863 C ATOM 1344 N TRP A 193 44.365 -29.235 1.902 1.00 65.37 N ANISOU 1344 N TRP A 193 10035 4072 10731 -640 -2130 882 N ATOM 1345 CA TRP A 193 45.302 -29.128 3.022 1.00 75.63 C ANISOU 1345 CA TRP A 193 11393 5324 12019 -517 -2233 1033 C ATOM 1346 C TRP A 193 45.240 -27.766 3.710 1.00 83.41 C ANISOU 1346 C TRP A 193 12194 6608 12892 -586 -2138 1125 C ATOM 1347 O TRP A 193 45.634 -27.609 4.875 1.00 76.99 O ANISOU 1347 O TRP A 193 11456 5776 12022 -591 -2206 1284 O ATOM 1348 CB TRP A 193 46.732 -29.401 2.562 1.00 83.16 C ANISOU 1348 CB TRP A 193 12300 6208 13087 -168 -2341 942 C ATOM 1349 CG TRP A 193 46.947 -30.782 2.032 1.00 87.64 C ANISOU 1349 CG TRP A 193 13084 6450 13765 -55 -2454 859 C ATOM 1350 CD1 TRP A 193 46.093 -31.852 2.134 1.00 89.39 C ANISOU 1350 CD1 TRP A 193 13577 6396 13991 -247 -2496 891 C ATOM 1351 CD2 TRP A 193 48.104 -31.257 1.342 1.00 87.23 C ANISOU 1351 CD2 TRP A 193 13006 6306 13834 277 -2540 727 C ATOM 1352 NE1 TRP A 193 46.647 -32.956 1.532 1.00 90.26 N ANISOU 1352 NE1 TRP A 193 13850 6227 14217 -50 -2608 783 N ATOM 1353 CE2 TRP A 193 47.883 -32.620 1.041 1.00 92.48 C ANISOU 1353 CE2 TRP A 193 13948 6619 14571 285 -2634 678 C ATOM 1354 CE3 TRP A 193 49.304 -30.664 0.943 1.00 83.99 C ANISOU 1354 CE3 TRP A 193 12360 6078 13473 564 -2542 643 C ATOM 1355 CZ2 TRP A 193 48.821 -33.396 0.365 1.00 88.10 C ANISOU 1355 CZ2 TRP A 193 13448 5889 14136 595 -2729 541 C ATOM 1356 CZ3 TRP A 193 50.235 -31.438 0.269 1.00 90.54 C ANISOU 1356 CZ3 TRP A 193 13220 6758 14422 864 -2629 510 C ATOM 1357 CH2 TRP A 193 49.990 -32.789 -0.009 1.00 87.05 C ANISOU 1357 CH2 TRP A 193 13064 5963 14050 889 -2721 458 C ATOM 1358 N TYR A 194 44.743 -26.777 2.979 1.00 79.45 N ANISOU 1358 N TYR A 194 11463 6374 12351 -635 -1986 1023 N ATOM 1359 CA TYR A 194 44.679 -25.435 3.509 1.00 76.54 C ANISOU 1359 CA TYR A 194 10925 6278 11879 -685 -1889 1087 C ATOM 1360 C TYR A 194 43.256 -25.063 3.905 1.00 75.88 C ANISOU 1360 C TYR A 194 10847 6305 11681 -972 -1764 1152 C ATOM 1361 O TYR A 194 43.022 -23.994 4.473 1.00 67.66 O ANISOU 1361 O TYR A 194 9701 5471 10538 -1039 -1676 1216 O ATOM 1362 CB TYR A 194 45.253 -24.451 2.494 1.00 76.62 C ANISOU 1362 CB TYR A 194 10673 6521 11918 -511 -1810 941 C ATOM 1363 CG TYR A 194 46.744 -24.606 2.289 1.00 82.35 C ANISOU 1363 CG TYR A 194 11349 7203 12738 -231 -1917 895 C ATOM 1364 CD1 TYR A 194 47.642 -23.797 2.979 1.00 89.71 C ANISOU 1364 CD1 TYR A 194 12183 8265 13637 -139 -1948 970 C ATOM 1365 CD2 TYR A 194 47.256 -25.556 1.414 1.00 77.46 C ANISOU 1365 CD2 TYR A 194 10773 6422 12237 -59 -1988 771 C ATOM 1366 CE1 TYR A 194 49.009 -23.928 2.803 1.00 89.95 C ANISOU 1366 CE1 TYR A 194 12138 8285 13754 112 -2047 928 C ATOM 1367 CE2 TYR A 194 48.624 -25.696 1.230 1.00 80.79 C ANISOU 1367 CE2 TYR A 194 11126 6827 12745 213 -2079 723 C ATOM 1368 CZ TYR A 194 49.497 -24.876 1.926 1.00 87.03 C ANISOU 1368 CZ TYR A 194 11795 7768 13504 295 -2108 805 C ATOM 1369 OH TYR A 194 50.864 -24.986 1.753 1.00 86.04 O ANISOU 1369 OH TYR A 194 11569 7658 13464 559 -2198 758 O ATOM 1370 N ARG A 195 42.309 -25.959 3.630 1.00 76.93 N ANISOU 1370 N ARG A 195 11104 6298 11828 -1145 -1758 1135 N ATOM 1371 CA ARG A 195 40.899 -25.650 3.857 1.00 81.02 C ANISOU 1371 CA ARG A 195 11589 6949 12245 -1419 -1631 1176 C ATOM 1372 C ARG A 195 40.537 -25.612 5.339 1.00 78.57 C ANISOU 1372 C ARG A 195 11413 6619 11820 -1595 -1628 1374 C ATOM 1373 O ARG A 195 40.850 -26.534 6.076 1.00 87.67 O ANISOU 1373 O ARG A 195 12798 7528 12985 -1625 -1747 1488 O ATOM 1374 CB ARG A 195 39.988 -26.621 3.107 1.00 82.01 C ANISOU 1374 CB ARG A 195 11795 6949 12416 -1576 -1628 1094 C ATOM 1375 CG ARG A 195 38.514 -26.259 3.228 1.00 84.54 C ANISOU 1375 CG ARG A 195 12032 7453 12638 -1854 -1491 1119 C ATOM 1376 CD ARG A 195 37.654 -27.269 2.516 1.00 81.26 C ANISOU 1376 CD ARG A 195 11697 6910 12267 -2030 -1505 1039 C ATOM 1377 NE ARG A 195 38.143 -27.463 1.162 1.00 82.70 N ANISOU 1377 NE ARG A 195 11813 7060 12551 -1843 -1544 850 N ATOM 1378 CZ ARG A 195 38.061 -28.604 0.493 1.00 84.72 C ANISOU 1378 CZ ARG A 195 12218 7084 12887 -1876 -1627 758 C ATOM 1379 NH1 ARG A 195 37.506 -29.673 1.055 1.00 89.07 N ANISOU 1379 NH1 ARG A 195 13003 7401 13437 -2101 -1686 846 N ATOM 1380 NH2 ARG A 195 38.545 -28.675 -0.739 1.00 79.72 N ANISOU 1380 NH2 ARG A 195 11513 6450 12329 -1688 -1649 576 N ATOM 1381 N PRO A 196 39.879 -24.527 5.775 1.00 80.37 N ANISOU 1381 N PRO A 196 11502 7103 11930 -1704 -1491 1415 N ATOM 1382 CA PRO A 196 39.482 -24.310 7.172 1.00 79.99 C ANISOU 1382 CA PRO A 196 11556 7089 11748 -1869 -1459 1590 C ATOM 1383 C PRO A 196 38.328 -25.228 7.594 1.00 81.72 C ANISOU 1383 C PRO A 196 11930 7199 11919 -2160 -1432 1675 C ATOM 1384 O PRO A 196 37.581 -25.690 6.735 1.00 74.75 O ANISOU 1384 O PRO A 196 11006 6307 11089 -2263 -1396 1579 O ATOM 1385 CB PRO A 196 38.999 -22.856 7.155 1.00 72.87 C ANISOU 1385 CB PRO A 196 10428 6509 10750 -1876 -1299 1553 C ATOM 1386 CG PRO A 196 38.498 -22.675 5.753 1.00 71.66 C ANISOU 1386 CG PRO A 196 10093 6469 10667 -1844 -1227 1383 C ATOM 1387 CD PRO A 196 39.558 -23.354 4.944 1.00 73.46 C ANISOU 1387 CD PRO A 196 10365 6510 11035 -1645 -1359 1292 C ATOM 1388 N PRO A 197 38.181 -25.468 8.910 1.00 88.43 N ANISOU 1388 N PRO A 197 12957 7980 12662 -2305 -1449 1854 N ATOM 1389 CA PRO A 197 37.126 -26.293 9.511 1.00 90.56 C ANISOU 1389 CA PRO A 197 13391 8157 12861 -2610 -1415 1966 C ATOM 1390 C PRO A 197 35.745 -25.945 8.969 1.00 94.38 C ANISOU 1390 C PRO A 197 13685 8870 13307 -2808 -1245 1887 C ATOM 1391 O PRO A 197 35.027 -26.853 8.544 1.00 89.71 O ANISOU 1391 O PRO A 197 13161 8168 12758 -2992 -1251 1864 O ATOM 1392 CB PRO A 197 37.185 -25.906 10.987 1.00 94.24 C ANISOU 1392 CB PRO A 197 13964 8675 13169 -2690 -1395 2146 C ATOM 1393 CG PRO A 197 38.574 -25.444 11.212 1.00 90.11 C ANISOU 1393 CG PRO A 197 13444 8119 12674 -2412 -1510 2151 C ATOM 1394 CD PRO A 197 39.067 -24.867 9.924 1.00 85.43 C ANISOU 1394 CD PRO A 197 12622 7630 12206 -2185 -1500 1960 C ATOM 1395 N GLU A 198 35.391 -24.656 8.992 1.00 92.79 N ANISOU 1395 N GLU A 198 13254 8978 13025 -2767 -1104 1845 N ATOM 1396 CA GLU A 198 34.087 -24.174 8.521 1.00 89.05 C ANISOU 1396 CA GLU A 198 12568 8762 12505 -2919 -941 1770 C ATOM 1397 C GLU A 198 33.677 -24.848 7.221 1.00 86.69 C ANISOU 1397 C GLU A 198 12208 8403 12327 -2957 -971 1631 C ATOM 1398 O GLU A 198 32.598 -25.429 7.119 1.00 92.25 O ANISOU 1398 O GLU A 198 12910 9128 13012 -3208 -920 1636 O ATOM 1399 CB GLU A 198 34.090 -22.653 8.283 1.00 95.04 C ANISOU 1399 CB GLU A 198 13078 9819 13213 -2753 -825 1690 C ATOM 1400 CG GLU A 198 34.757 -21.796 9.352 1.00 98.05 C ANISOU 1400 CG GLU A 198 13504 10260 13491 -2648 -813 1783 C ATOM 1401 CD GLU A 198 36.179 -21.399 8.991 1.00 96.41 C ANISOU 1401 CD GLU A 198 13291 9973 13366 -2367 -926 1729 C ATOM 1402 OE1 GLU A 198 37.080 -22.240 9.159 1.00102.11 O ANISOU 1402 OE1 GLU A 198 14188 10450 14159 -2302 -1080 1777 O ATOM 1403 OE2 GLU A 198 36.400 -20.246 8.551 1.00 91.29 O ANISOU 1403 OE2 GLU A 198 12467 9510 12711 -2211 -861 1640 O ATOM 1404 N LEU A 199 34.539 -24.752 6.218 1.00 85.89 N ANISOU 1404 N LEU A 199 12052 8242 12342 -2713 -1051 1500 N ATOM 1405 CA LEU A 199 34.224 -25.312 4.915 1.00 89.55 C ANISOU 1405 CA LEU A 199 12457 8660 12909 -2722 -1081 1349 C ATOM 1406 C LEU A 199 34.046 -26.830 4.991 1.00 91.33 C ANISOU 1406 C LEU A 199 12932 8577 13191 -2905 -1188 1390 C ATOM 1407 O LEU A 199 33.105 -27.374 4.420 1.00 91.57 O ANISOU 1407 O LEU A 199 12936 8619 13238 -3103 -1163 1328 O ATOM 1408 CB LEU A 199 35.282 -24.919 3.883 1.00 84.19 C ANISOU 1408 CB LEU A 199 11686 7973 12330 -2415 -1142 1207 C ATOM 1409 CG LEU A 199 35.448 -23.405 3.723 1.00 81.72 C ANISOU 1409 CG LEU A 199 11141 7949 11961 -2250 -1037 1164 C ATOM 1410 CD1 LEU A 199 36.412 -23.084 2.598 1.00 86.17 C ANISOU 1410 CD1 LEU A 199 11610 8512 12617 -1982 -1086 1021 C ATOM 1411 CD2 LEU A 199 34.110 -22.737 3.483 1.00 72.05 C ANISOU 1411 CD2 LEU A 199 9714 7006 10654 -2394 -889 1129 C ATOM 1412 N LEU A 200 34.940 -27.502 5.709 1.00 89.75 N ANISOU 1412 N LEU A 200 12981 8102 13016 -2842 -1313 1498 N ATOM 1413 CA LEU A 200 34.866 -28.950 5.865 1.00 92.94 C ANISOU 1413 CA LEU A 200 13670 8173 13472 -2997 -1428 1554 C ATOM 1414 C LEU A 200 33.573 -29.393 6.565 1.00 95.69 C ANISOU 1414 C LEU A 200 14088 8551 13719 -3379 -1345 1672 C ATOM 1415 O LEU A 200 33.103 -30.509 6.370 1.00 96.47 O ANISOU 1415 O LEU A 200 14359 8438 13858 -3583 -1401 1676 O ATOM 1416 CB LEU A 200 36.091 -29.456 6.623 1.00 90.13 C ANISOU 1416 CB LEU A 200 13561 7540 13145 -2831 -1578 1668 C ATOM 1417 CG LEU A 200 37.407 -29.259 5.877 1.00 84.15 C ANISOU 1417 CG LEU A 200 12747 6721 12504 -2466 -1676 1546 C ATOM 1418 CD1 LEU A 200 38.580 -29.290 6.846 1.00 87.41 C ANISOU 1418 CD1 LEU A 200 13308 6997 12908 -2286 -1793 1678 C ATOM 1419 CD2 LEU A 200 37.565 -30.303 4.775 1.00 79.69 C ANISOU 1419 CD2 LEU A 200 12288 5918 12074 -2412 -1773 1403 C ATOM 1420 N LEU A 201 33.000 -28.510 7.374 1.00 94.64 N ANISOU 1420 N LEU A 201 13822 8685 13452 -3479 -1207 1763 N ATOM 1421 CA LEU A 201 31.735 -28.794 8.034 1.00 92.54 C ANISOU 1421 CA LEU A 201 13573 8512 13077 -3837 -1098 1868 C ATOM 1422 C LEU A 201 30.543 -28.317 7.209 1.00102.52 C ANISOU 1422 C LEU A 201 14542 10080 14329 -3967 -964 1739 C ATOM 1423 O LEU A 201 29.407 -28.369 7.675 1.00107.62 O ANISOU 1423 O LEU A 201 15126 10885 14881 -4254 -848 1806 O ATOM 1424 CB LEU A 201 31.699 -28.149 9.417 1.00 85.73 C ANISOU 1424 CB LEU A 201 12732 7783 12058 -3884 -1013 2037 C ATOM 1425 CG LEU A 201 32.457 -28.911 10.500 1.00 85.99 C ANISOU 1425 CG LEU A 201 13104 7512 12057 -3900 -1138 2220 C ATOM 1426 CD1 LEU A 201 32.370 -28.192 11.847 1.00 85.63 C ANISOU 1426 CD1 LEU A 201 13070 7633 11834 -3952 -1044 2375 C ATOM 1427 CD2 LEU A 201 31.929 -30.343 10.599 1.00 83.05 C ANISOU 1427 CD2 LEU A 201 12988 6860 11706 -4192 -1203 2298 C ATOM 1428 N GLY A 202 30.810 -27.834 5.998 1.00106.18 N ANISOU 1428 N GLY A 202 14819 10641 14882 -3752 -978 1559 N ATOM 1429 CA GLY A 202 29.761 -27.452 5.064 1.00103.64 C ANISOU 1429 CA GLY A 202 14229 10588 14561 -3844 -883 1424 C ATOM 1430 C GLY A 202 29.240 -26.019 5.116 1.00 98.61 C ANISOU 1430 C GLY A 202 13287 10347 13833 -3758 -724 1396 C ATOM 1431 O GLY A 202 28.134 -25.754 4.645 1.00102.13 O ANISOU 1431 O GLY A 202 13515 11043 14248 -3894 -630 1328 O ATOM 1432 N GLU A 203 30.020 -25.093 5.671 1.00 88.02 N ANISOU 1432 N GLU A 203 11931 9065 12448 -3532 -700 1443 N ATOM 1433 CA GLU A 203 29.605 -23.686 5.735 1.00 87.78 C ANISOU 1433 CA GLU A 203 11643 9379 12331 -3424 -555 1414 C ATOM 1434 C GLU A 203 29.597 -23.002 4.360 1.00 85.60 C ANISOU 1434 C GLU A 203 11139 9266 12120 -3228 -547 1235 C ATOM 1435 O GLU A 203 30.503 -23.198 3.551 1.00 83.72 O ANISOU 1435 O GLU A 203 10953 8873 11983 -3042 -655 1145 O ATOM 1436 CB GLU A 203 30.497 -22.901 6.698 1.00 86.75 C ANISOU 1436 CB GLU A 203 11587 9242 12134 -3247 -544 1507 C ATOM 1437 CG GLU A 203 30.262 -21.400 6.663 1.00 85.43 C ANISOU 1437 CG GLU A 203 11188 9383 11889 -3089 -412 1458 C ATOM 1438 CD GLU A 203 28.992 -20.983 7.380 1.00 92.05 C ANISOU 1438 CD GLU A 203 11902 10482 12593 -3279 -245 1517 C ATOM 1439 OE1 GLU A 203 28.944 -21.097 8.624 1.00 89.52 O ANISOU 1439 OE1 GLU A 203 11716 10132 12167 -3400 -204 1656 O ATOM 1440 OE2 GLU A 203 28.046 -20.526 6.704 1.00 95.29 O ANISOU 1440 OE2 GLU A 203 12074 11137 12993 -3299 -153 1424 O ATOM 1441 N ARG A 204 28.569 -22.200 4.104 1.00 83.16 N ANISOU 1441 N ARG A 204 10578 9275 11744 -3264 -418 1186 N ATOM 1442 CA ARG A 204 28.434 -21.511 2.822 1.00 83.77 C ANISOU 1442 CA ARG A 204 10439 9528 11863 -3090 -407 1030 C ATOM 1443 C ARG A 204 28.290 -20.016 3.038 1.00 85.80 C ANISOU 1443 C ARG A 204 10514 10054 12031 -2913 -284 1028 C ATOM 1444 O ARG A 204 28.243 -19.237 2.092 1.00 92.92 O ANISOU 1444 O ARG A 204 11247 11111 12948 -2739 -265 920 O ATOM 1445 CB ARG A 204 27.231 -22.047 2.042 1.00 84.35 C ANISOU 1445 CB ARG A 204 10367 9731 11951 -3296 -394 947 C ATOM 1446 CG ARG A 204 27.373 -23.499 1.638 1.00 90.73 C ANISOU 1446 CG ARG A 204 11364 10258 12852 -3463 -525 920 C ATOM 1447 CD ARG A 204 26.135 -23.999 0.935 1.00101.25 C ANISOU 1447 CD ARG A 204 12549 11734 14186 -3699 -514 839 C ATOM 1448 NE ARG A 204 25.964 -23.396 -0.382 1.00105.13 N ANISOU 1448 NE ARG A 204 12830 12412 14702 -3532 -524 679 N ATOM 1449 CZ ARG A 204 26.527 -23.863 -1.491 1.00110.29 C ANISOU 1449 CZ ARG A 204 13551 12911 15442 -3430 -640 551 C ATOM 1450 NH1 ARG A 204 27.310 -24.936 -1.438 1.00109.15 N ANISOU 1450 NH1 ARG A 204 13676 12417 15378 -3461 -756 557 N ATOM 1451 NH2 ARG A 204 26.316 -23.254 -2.652 1.00111.15 N ANISOU 1451 NH2 ARG A 204 13466 13214 15551 -3286 -641 416 N ATOM 1452 N ASP A 205 28.205 -19.625 4.300 1.00 83.08 N ANISOU 1452 N ASP A 205 10223 9758 11588 -2962 -200 1150 N ATOM 1453 CA ASP A 205 28.143 -18.227 4.664 1.00 88.72 C ANISOU 1453 CA ASP A 205 10813 10688 12210 -2793 -85 1155 C ATOM 1454 C ASP A 205 29.437 -17.901 5.400 1.00 88.39 C ANISOU 1454 C ASP A 205 10959 10468 12158 -2644 -138 1226 C ATOM 1455 O ASP A 205 29.436 -17.618 6.597 1.00 92.21 O ANISOU 1455 O ASP A 205 11525 10970 12539 -2694 -76 1333 O ATOM 1456 CB ASP A 205 26.934 -17.975 5.560 1.00 96.56 C ANISOU 1456 CB ASP A 205 11702 11910 13077 -2969 67 1225 C ATOM 1457 CG ASP A 205 26.499 -16.528 5.556 1.00110.14 C ANISOU 1457 CG ASP A 205 13228 13907 14711 -2789 197 1181 C ATOM 1458 OD1 ASP A 205 27.108 -15.722 4.824 1.00115.21 O ANISOU 1458 OD1 ASP A 205 13825 14558 15393 -2543 165 1101 O ATOM 1459 OD2 ASP A 205 25.543 -16.197 6.287 1.00119.12 O ANISOU 1459 OD2 ASP A 205 14264 15255 15739 -2891 334 1225 O ATOM 1460 N TYR A 206 30.546 -17.978 4.673 1.00 82.43 N ANISOU 1460 N TYR A 206 10267 9549 11504 -2466 -254 1164 N ATOM 1461 CA TYR A 206 31.870 -17.768 5.249 1.00 78.23 C ANISOU 1461 CA TYR A 206 9896 8848 10981 -2324 -328 1221 C ATOM 1462 C TYR A 206 32.454 -16.455 4.747 1.00 77.09 C ANISOU 1462 C TYR A 206 9642 8819 10830 -2075 -297 1148 C ATOM 1463 O TYR A 206 31.948 -15.870 3.783 1.00 78.78 O ANISOU 1463 O TYR A 206 9681 9200 11054 -1996 -243 1047 O ATOM 1464 CB TYR A 206 32.795 -18.924 4.872 1.00 68.48 C ANISOU 1464 CB TYR A 206 8824 7327 9869 -2308 -490 1213 C ATOM 1465 CG TYR A 206 32.829 -19.172 3.389 1.00 70.89 C ANISOU 1465 CG TYR A 206 9026 7628 10280 -2223 -538 1065 C ATOM 1466 CD1 TYR A 206 32.067 -20.188 2.809 1.00 70.30 C ANISOU 1466 CD1 TYR A 206 8950 7506 10254 -2394 -568 1018 C ATOM 1467 CD2 TYR A 206 33.602 -18.374 2.558 1.00 67.60 C ANISOU 1467 CD2 TYR A 206 8520 7263 9904 -1985 -552 972 C ATOM 1468 CE1 TYR A 206 32.093 -20.411 1.435 1.00 69.00 C ANISOU 1468 CE1 TYR A 206 8702 7343 10173 -2316 -615 874 C ATOM 1469 CE2 TYR A 206 33.633 -18.581 1.193 1.00 68.19 C ANISOU 1469 CE2 TYR A 206 8507 7346 10057 -1907 -589 837 C ATOM 1470 CZ TYR A 206 32.884 -19.598 0.634 1.00 70.30 C ANISOU 1470 CZ TYR A 206 8779 7565 10368 -2066 -624 784 C ATOM 1471 OH TYR A 206 32.938 -19.780 -0.730 1.00 68.47 O ANISOU 1471 OH TYR A 206 8469 7346 10199 -1983 -664 642 O ATOM 1472 N GLY A 207 33.520 -15.999 5.401 1.00 71.12 N ANISOU 1472 N GLY A 207 8997 7974 10054 -1961 -337 1202 N ATOM 1473 CA GLY A 207 34.137 -14.725 5.075 1.00 65.16 C ANISOU 1473 CA GLY A 207 8165 7311 9280 -1754 -307 1148 C ATOM 1474 C GLY A 207 35.650 -14.777 5.097 1.00 66.80 C ANISOU 1474 C GLY A 207 8479 7347 9554 -1619 -428 1157 C ATOM 1475 O GLY A 207 36.240 -15.838 4.874 1.00 63.24 O ANISOU 1475 O GLY A 207 8117 6711 9200 -1629 -546 1159 O ATOM 1476 N PRO A 208 36.290 -13.622 5.354 1.00 65.47 N ANISOU 1476 N PRO A 208 8299 7242 9335 -1490 -401 1157 N ATOM 1477 CA PRO A 208 37.755 -13.468 5.355 1.00 59.50 C ANISOU 1477 CA PRO A 208 7605 6370 8634 -1358 -506 1159 C ATOM 1478 C PRO A 208 38.517 -14.440 6.255 1.00 61.57 C ANISOU 1478 C PRO A 208 8037 6436 8921 -1411 -635 1256 C ATOM 1479 O PRO A 208 39.658 -14.766 5.949 1.00 60.73 O ANISOU 1479 O PRO A 208 7956 6215 8904 -1302 -748 1238 O ATOM 1480 CB PRO A 208 37.952 -12.026 5.828 1.00 52.59 C ANISOU 1480 CB PRO A 208 6711 5615 7655 -1285 -430 1167 C ATOM 1481 CG PRO A 208 36.742 -11.321 5.313 1.00 59.46 C ANISOU 1481 CG PRO A 208 7453 6671 8470 -1285 -292 1109 C ATOM 1482 CD PRO A 208 35.603 -12.316 5.404 1.00 58.41 C ANISOU 1482 CD PRO A 208 7304 6552 8338 -1444 -264 1131 C ATOM 1483 N PRO A 209 37.907 -14.892 7.357 1.00 66.64 N ANISOU 1483 N PRO A 209 8794 7048 9479 -1571 -617 1362 N ATOM 1484 CA PRO A 209 38.608 -15.865 8.199 1.00 63.98 C ANISOU 1484 CA PRO A 209 8639 6511 9159 -1619 -751 1468 C ATOM 1485 C PRO A 209 39.107 -17.115 7.468 1.00 62.61 C ANISOU 1485 C PRO A 209 8510 6145 9133 -1581 -879 1435 C ATOM 1486 O PRO A 209 40.051 -17.735 7.954 1.00 63.83 O ANISOU 1486 O PRO A 209 8795 6131 9328 -1535 -1015 1499 O ATOM 1487 CB PRO A 209 37.555 -16.233 9.243 1.00 65.58 C ANISOU 1487 CB PRO A 209 8939 6734 9243 -1829 -680 1574 C ATOM 1488 CG PRO A 209 36.775 -14.974 9.403 1.00 63.67 C ANISOU 1488 CG PRO A 209 8582 6725 8886 -1832 -516 1541 C ATOM 1489 CD PRO A 209 36.696 -14.371 8.017 1.00 61.73 C ANISOU 1489 CD PRO A 209 8147 6584 8723 -1695 -473 1401 C ATOM 1490 N ILE A 210 38.521 -17.489 6.335 1.00 59.42 N ANISOU 1490 N ILE A 210 8009 5762 8808 -1589 -846 1333 N ATOM 1491 CA ILE A 210 39.026 -18.682 5.641 1.00 70.23 C ANISOU 1491 CA ILE A 210 9441 6933 10312 -1543 -969 1288 C ATOM 1492 C ILE A 210 40.422 -18.454 5.069 1.00 67.25 C ANISOU 1492 C ILE A 210 9016 6510 10024 -1316 -1058 1221 C ATOM 1493 O ILE A 210 41.246 -19.375 5.033 1.00 67.48 O ANISOU 1493 O ILE A 210 9146 6347 10144 -1240 -1190 1229 O ATOM 1494 CB ILE A 210 38.097 -19.192 4.511 1.00 68.12 C ANISOU 1494 CB ILE A 210 9090 6692 10102 -1612 -924 1181 C ATOM 1495 CG1 ILE A 210 38.166 -18.256 3.298 1.00 59.34 C ANISOU 1495 CG1 ILE A 210 7777 5756 9014 -1464 -856 1043 C ATOM 1496 CG2 ILE A 210 36.665 -19.411 5.031 1.00 56.32 C ANISOU 1496 CG2 ILE A 210 7606 5274 8519 -1854 -829 1242 C ATOM 1497 CD1 ILE A 210 37.367 -18.749 2.092 1.00 57.53 C ANISOU 1497 CD1 ILE A 210 7462 5559 8836 -1512 -832 926 C ATOM 1498 N ASP A 211 40.687 -17.229 4.626 1.00 56.85 N ANISOU 1498 N ASP A 211 7548 5371 8681 -1207 -984 1156 N ATOM 1499 CA ASP A 211 41.997 -16.901 4.081 1.00 61.03 C ANISOU 1499 CA ASP A 211 8009 5894 9283 -1012 -1049 1094 C ATOM 1500 C ASP A 211 43.048 -16.875 5.189 1.00 65.56 C ANISOU 1500 C ASP A 211 8682 6389 9838 -969 -1154 1198 C ATOM 1501 O ASP A 211 44.221 -17.208 4.970 1.00 59.29 O ANISOU 1501 O ASP A 211 7881 5515 9131 -825 -1264 1175 O ATOM 1502 CB ASP A 211 41.966 -15.568 3.323 1.00 57.45 C ANISOU 1502 CB ASP A 211 7386 5647 8795 -933 -937 1008 C ATOM 1503 CG ASP A 211 41.266 -15.677 1.979 1.00 58.67 C ANISOU 1503 CG ASP A 211 7430 5871 8991 -918 -871 887 C ATOM 1504 OD1 ASP A 211 41.111 -16.810 1.474 1.00 58.77 O ANISOU 1504 OD1 ASP A 211 7486 5761 9082 -936 -930 843 O ATOM 1505 OD2 ASP A 211 40.872 -14.631 1.426 1.00 61.13 O ANISOU 1505 OD2 ASP A 211 7623 6355 9250 -888 -767 836 O ATOM 1506 N LEU A 212 42.618 -16.495 6.386 1.00 61.00 N ANISOU 1506 N LEU A 212 8192 5845 9140 -1090 -1123 1309 N ATOM 1507 CA LEU A 212 43.550 -16.374 7.500 1.00 64.17 C ANISOU 1507 CA LEU A 212 8691 6194 9498 -1064 -1225 1411 C ATOM 1508 C LEU A 212 43.966 -17.728 8.064 1.00 68.15 C ANISOU 1508 C LEU A 212 9366 6475 10054 -1071 -1379 1499 C ATOM 1509 O LEU A 212 45.109 -17.912 8.479 1.00 69.20 O ANISOU 1509 O LEU A 212 9539 6535 10220 -963 -1514 1541 O ATOM 1510 CB LEU A 212 42.988 -15.443 8.573 1.00 60.70 C ANISOU 1510 CB LEU A 212 8297 5872 8894 -1181 -1136 1489 C ATOM 1511 CG LEU A 212 43.294 -13.997 8.166 1.00 64.22 C ANISOU 1511 CG LEU A 212 8603 6493 9305 -1099 -1052 1411 C ATOM 1512 CD1 LEU A 212 42.279 -13.044 8.718 1.00 76.10 C ANISOU 1512 CD1 LEU A 212 10115 8136 10664 -1201 -906 1431 C ATOM 1513 CD2 LEU A 212 44.704 -13.604 8.601 1.00 62.22 C ANISOU 1513 CD2 LEU A 212 8354 6227 9060 -1003 -1168 1436 C ATOM 1514 N TRP A 213 43.035 -18.675 8.058 1.00 72.45 N ANISOU 1514 N TRP A 213 10011 6912 10606 -1200 -1364 1527 N ATOM 1515 CA TRP A 213 43.346 -20.046 8.408 1.00 68.13 C ANISOU 1515 CA TRP A 213 9646 6120 10119 -1207 -1508 1601 C ATOM 1516 C TRP A 213 44.475 -20.507 7.509 1.00 67.59 C ANISOU 1516 C TRP A 213 9518 5958 10204 -987 -1620 1505 C ATOM 1517 O TRP A 213 45.428 -21.149 7.958 1.00 67.65 O ANISOU 1517 O TRP A 213 9627 5814 10260 -880 -1776 1565 O ATOM 1518 CB TRP A 213 42.131 -20.945 8.193 1.00 70.72 C ANISOU 1518 CB TRP A 213 10061 6356 10453 -1387 -1457 1609 C ATOM 1519 CG TRP A 213 42.473 -22.393 8.344 1.00 74.84 C ANISOU 1519 CG TRP A 213 10785 6594 11056 -1381 -1608 1665 C ATOM 1520 CD1 TRP A 213 42.911 -23.239 7.367 1.00 76.60 C ANISOU 1520 CD1 TRP A 213 11019 6663 11425 -1255 -1691 1565 C ATOM 1521 CD2 TRP A 213 42.432 -23.158 9.551 1.00 74.04 C ANISOU 1521 CD2 TRP A 213 10925 6319 10888 -1497 -1699 1835 C ATOM 1522 NE1 TRP A 213 43.140 -24.485 7.891 1.00 83.34 N ANISOU 1522 NE1 TRP A 213 12110 7241 12313 -1277 -1830 1660 N ATOM 1523 CE2 TRP A 213 42.851 -24.463 9.231 1.00 81.22 C ANISOU 1523 CE2 TRP A 213 11989 6955 11915 -1429 -1840 1834 C ATOM 1524 CE3 TRP A 213 42.078 -22.868 10.871 1.00 78.60 C ANISOU 1524 CE3 TRP A 213 11614 6942 11308 -1649 -1672 1988 C ATOM 1525 CZ2 TRP A 213 42.925 -25.478 10.183 1.00 81.56 C ANISOU 1525 CZ2 TRP A 213 12303 6758 11927 -1510 -1962 1992 C ATOM 1526 CZ3 TRP A 213 42.152 -23.880 11.819 1.00 79.86 C ANISOU 1526 CZ3 TRP A 213 12035 6880 11428 -1739 -1788 2146 C ATOM 1527 CH2 TRP A 213 42.572 -25.165 11.469 1.00 79.29 C ANISOU 1527 CH2 TRP A 213 12120 6527 11479 -1670 -1935 2152 C ATOM 1528 N GLY A 214 44.357 -20.171 6.229 1.00 65.43 N ANISOU 1528 N GLY A 214 9075 5785 10000 -911 -1539 1355 N ATOM 1529 CA GLY A 214 45.396 -20.476 5.267 1.00 71.50 C ANISOU 1529 CA GLY A 214 9758 6508 10901 -697 -1614 1243 C ATOM 1530 C GLY A 214 46.703 -19.757 5.564 1.00 66.66 C ANISOU 1530 C GLY A 214 9048 5985 10293 -541 -1677 1255 C ATOM 1531 O GLY A 214 47.779 -20.278 5.279 1.00 66.35 O ANISOU 1531 O GLY A 214 8991 5864 10356 -362 -1792 1219 O ATOM 1532 N ALA A 215 46.611 -18.553 6.119 1.00 58.26 N ANISOU 1532 N ALA A 215 7920 5096 9119 -609 -1602 1297 N ATOM 1533 CA ALA A 215 47.797 -17.797 6.485 1.00 58.44 C ANISOU 1533 CA ALA A 215 7857 5215 9131 -502 -1663 1313 C ATOM 1534 C ALA A 215 48.496 -18.571 7.590 1.00 63.90 C ANISOU 1534 C ALA A 215 8701 5753 9824 -469 -1839 1439 C ATOM 1535 O ALA A 215 49.713 -18.737 7.579 1.00 62.14 O ANISOU 1535 O ALA A 215 8421 5517 9674 -307 -1962 1430 O ATOM 1536 CB ALA A 215 47.420 -16.387 6.964 1.00 49.91 C ANISOU 1536 CB ALA A 215 6724 4323 7917 -608 -1548 1339 C ATOM 1537 N GLY A 216 47.704 -19.049 8.542 1.00 65.03 N ANISOU 1537 N GLY A 216 9036 5790 9880 -625 -1851 1560 N ATOM 1538 CA GLY A 216 48.206 -19.923 9.581 1.00 75.55 C ANISOU 1538 CA GLY A 216 10555 6948 11202 -610 -2022 1695 C ATOM 1539 C GLY A 216 48.996 -21.111 9.051 1.00 78.66 C ANISOU 1539 C GLY A 216 10983 7153 11750 -423 -2168 1659 C ATOM 1540 O GLY A 216 50.142 -21.321 9.454 1.00 81.96 O ANISOU 1540 O GLY A 216 11400 7534 12207 -270 -2323 1700 O ATOM 1541 N CYS A 217 48.390 -21.892 8.155 1.00 73.65 N ANISOU 1541 N CYS A 217 10380 6402 11200 -428 -2124 1579 N ATOM 1542 CA CYS A 217 49.038 -23.098 7.639 1.00 76.26 C ANISOU 1542 CA CYS A 217 10778 6524 11673 -248 -2257 1534 C ATOM 1543 C CYS A 217 50.343 -22.759 6.927 1.00 79.94 C ANISOU 1543 C CYS A 217 11033 7099 12242 4 -2305 1421 C ATOM 1544 O CYS A 217 51.315 -23.523 6.976 1.00 82.08 O ANISOU 1544 O CYS A 217 11341 7242 12606 202 -2460 1427 O ATOM 1545 CB CYS A 217 48.112 -23.865 6.690 1.00 77.03 C ANISOU 1545 CB CYS A 217 10935 6499 11835 -315 -2185 1440 C ATOM 1546 SG CYS A 217 46.545 -24.427 7.411 1.00 83.65 S ANISOU 1546 SG CYS A 217 12007 7209 12567 -632 -2126 1563 S ATOM 1547 N ILE A 218 50.359 -21.608 6.266 1.00 71.19 N ANISOU 1547 N ILE A 218 9704 6231 11114 -1 -2170 1322 N ATOM 1548 CA ILE A 218 51.546 -21.155 5.556 1.00 69.07 C ANISOU 1548 CA ILE A 218 9213 6103 10926 203 -2187 1215 C ATOM 1549 C ILE A 218 52.616 -20.682 6.534 1.00 74.32 C ANISOU 1549 C ILE A 218 9831 6852 11556 266 -2308 1310 C ATOM 1550 O ILE A 218 53.808 -20.960 6.357 1.00 71.93 O ANISOU 1550 O ILE A 218 9425 6560 11344 472 -2420 1275 O ATOM 1551 CB ILE A 218 51.209 -20.028 4.561 1.00 53.72 C ANISOU 1551 CB ILE A 218 7068 4387 8957 157 -2003 1093 C ATOM 1552 CG1 ILE A 218 50.473 -20.602 3.363 1.00 50.32 C ANISOU 1552 CG1 ILE A 218 6643 3890 8588 162 -1916 968 C ATOM 1553 CG2 ILE A 218 52.479 -19.326 4.070 1.00 54.95 C ANISOU 1553 CG2 ILE A 218 6993 4726 9162 319 -2011 1016 C ATOM 1554 CD1 ILE A 218 49.644 -19.571 2.612 1.00 53.76 C ANISOU 1554 CD1 ILE A 218 6955 4514 8956 47 -1732 891 C ATOM 1555 N MET A 219 52.194 -19.961 7.566 1.00 71.81 N ANISOU 1555 N MET A 219 9581 6603 11099 90 -2285 1423 N ATOM 1556 CA MET A 219 53.149 -19.482 8.549 1.00 72.07 C ANISOU 1556 CA MET A 219 9585 6720 11080 123 -2407 1513 C ATOM 1557 C MET A 219 53.900 -20.670 9.139 1.00 69.23 C ANISOU 1557 C MET A 219 9350 6170 10784 275 -2622 1599 C ATOM 1558 O MET A 219 55.124 -20.691 9.146 1.00 73.55 O ANISOU 1558 O MET A 219 9768 6780 11399 456 -2746 1582 O ATOM 1559 CB MET A 219 52.473 -18.660 9.650 1.00 65.97 C ANISOU 1559 CB MET A 219 8917 6017 10133 -96 -2354 1624 C ATOM 1560 CG MET A 219 53.475 -17.954 10.547 1.00 67.82 C ANISOU 1560 CG MET A 219 9095 6375 10299 -78 -2466 1690 C ATOM 1561 SD MET A 219 52.748 -16.803 11.715 1.00 80.61 S ANISOU 1561 SD MET A 219 10823 8103 11702 -323 -2382 1783 S ATOM 1562 CE MET A 219 54.138 -16.464 12.791 1.00 97.49 C ANISOU 1562 CE MET A 219 12933 10322 13787 -264 -2591 1867 C ATOM 1563 N ALA A 220 53.154 -21.661 9.617 1.00 72.82 N ANISOU 1563 N ALA A 220 10055 6396 11218 201 -2667 1691 N ATOM 1564 CA ALA A 220 53.741 -22.862 10.204 1.00 81.97 C ANISOU 1564 CA ALA A 220 11383 7333 12429 339 -2876 1788 C ATOM 1565 C ALA A 220 54.678 -23.538 9.212 1.00 83.64 C ANISOU 1565 C ALA A 220 11471 7492 12817 620 -2950 1663 C ATOM 1566 O ALA A 220 55.673 -24.144 9.595 1.00 83.69 O ANISOU 1566 O ALA A 220 11496 7418 12883 819 -3138 1711 O ATOM 1567 CB ALA A 220 52.644 -23.831 10.643 1.00 83.79 C ANISOU 1567 CB ALA A 220 11911 7312 12615 187 -2877 1889 C ATOM 1568 N GLU A 221 54.348 -23.414 7.932 1.00 86.20 N ANISOU 1568 N GLU A 221 11665 7869 13216 644 -2802 1500 N ATOM 1569 CA GLU A 221 55.107 -24.038 6.860 1.00 84.11 C ANISOU 1569 CA GLU A 221 11284 7564 13108 901 -2837 1356 C ATOM 1570 C GLU A 221 56.465 -23.367 6.667 1.00 81.43 C ANISOU 1570 C GLU A 221 10664 7459 12817 1085 -2882 1297 C ATOM 1571 O GLU A 221 57.373 -23.954 6.078 1.00 90.12 O ANISOU 1571 O GLU A 221 11663 8536 14042 1341 -2958 1207 O ATOM 1572 CB GLU A 221 54.292 -23.995 5.564 1.00 92.97 C ANISOU 1572 CB GLU A 221 12352 8704 14268 844 -2654 1200 C ATOM 1573 CG GLU A 221 54.781 -24.917 4.460 1.00101.27 C ANISOU 1573 CG GLU A 221 13370 9642 15467 1083 -2682 1049 C ATOM 1574 CD GLU A 221 53.678 -25.283 3.472 1.00102.77 C ANISOU 1574 CD GLU A 221 13637 9741 15671 978 -2548 937 C ATOM 1575 OE1 GLU A 221 52.486 -25.116 3.816 1.00 96.30 O ANISOU 1575 OE1 GLU A 221 12944 8886 14758 723 -2470 1006 O ATOM 1576 OE2 GLU A 221 54.007 -25.748 2.358 1.00104.77 O ANISOU 1576 OE2 GLU A 221 13820 9967 16022 1150 -2523 777 O ATOM 1577 N MET A 222 56.608 -22.145 7.175 1.00 73.98 N ANISOU 1577 N MET A 222 9596 6742 11772 952 -2836 1343 N ATOM 1578 CA MET A 222 57.871 -21.408 7.062 1.00 81.93 C ANISOU 1578 CA MET A 222 10330 7991 12810 1077 -2877 1296 C ATOM 1579 C MET A 222 58.996 -22.056 7.878 1.00 86.33 C ANISOU 1579 C MET A 222 10898 8492 13413 1273 -3117 1385 C ATOM 1580 O MET A 222 60.178 -21.837 7.606 1.00 79.98 O ANISOU 1580 O MET A 222 9852 7856 12679 1449 -3179 1323 O ATOM 1581 CB MET A 222 57.690 -19.939 7.469 1.00 77.10 C ANISOU 1581 CB MET A 222 9620 7606 12067 861 -2776 1328 C ATOM 1582 CG MET A 222 56.746 -19.144 6.562 1.00 76.81 C ANISOU 1582 CG MET A 222 9526 7665 11991 708 -2543 1229 C ATOM 1583 SD MET A 222 57.397 -18.856 4.895 1.00 73.68 S ANISOU 1583 SD MET A 222 8841 7442 11711 868 -2420 1028 S ATOM 1584 CE MET A 222 58.850 -17.862 5.243 1.00 70.63 C ANISOU 1584 CE MET A 222 8194 7326 11317 913 -2489 1036 C ATOM 1585 N TRP A 223 58.616 -22.849 8.878 1.00 87.74 N ANISOU 1585 N TRP A 223 11352 8442 13544 1238 -3251 1534 N ATOM 1586 CA TRP A 223 59.577 -23.572 9.704 1.00 85.80 C ANISOU 1586 CA TRP A 223 11162 8108 13331 1431 -3497 1637 C ATOM 1587 C TRP A 223 59.558 -25.064 9.387 1.00 94.14 C ANISOU 1587 C TRP A 223 12402 8862 14503 1636 -3597 1627 C ATOM 1588 O TRP A 223 60.610 -25.677 9.237 1.00 96.65 O ANISOU 1588 O TRP A 223 12631 9159 14934 1923 -3744 1595 O ATOM 1589 CB TRP A 223 59.299 -23.359 11.194 1.00 80.14 C ANISOU 1589 CB TRP A 223 10643 7352 12454 1253 -3605 1834 C ATOM 1590 CG TRP A 223 59.683 -22.001 11.705 1.00 80.48 C ANISOU 1590 CG TRP A 223 10511 7680 12388 1114 -3580 1853 C ATOM 1591 CD1 TRP A 223 60.907 -21.617 12.167 1.00 79.25 C ANISOU 1591 CD1 TRP A 223 10172 7704 12235 1224 -3733 1876 C ATOM 1592 CD2 TRP A 223 58.831 -20.848 11.818 1.00 78.51 C ANISOU 1592 CD2 TRP A 223 10261 7561 12007 835 -3396 1847 C ATOM 1593 NE1 TRP A 223 60.872 -20.298 12.558 1.00 81.67 N ANISOU 1593 NE1 TRP A 223 10378 8233 12418 1015 -3657 1883 N ATOM 1594 CE2 TRP A 223 59.609 -19.805 12.355 1.00 78.23 C ANISOU 1594 CE2 TRP A 223 10060 7764 11899 785 -3448 1865 C ATOM 1595 CE3 TRP A 223 57.486 -20.600 11.518 1.00 73.19 C ANISOU 1595 CE3 TRP A 223 9708 6831 11271 630 -3197 1826 C ATOM 1596 CZ2 TRP A 223 59.091 -18.533 12.592 1.00 77.11 C ANISOU 1596 CZ2 TRP A 223 9895 7778 11624 545 -3306 1858 C ATOM 1597 CZ3 TRP A 223 56.971 -19.339 11.762 1.00 68.05 C ANISOU 1597 CZ3 TRP A 223 9016 6351 10490 410 -3056 1823 C ATOM 1598 CH2 TRP A 223 57.771 -18.322 12.290 1.00 72.95 C ANISOU 1598 CH2 TRP A 223 9496 7182 11041 373 -3109 1837 C ATOM 1599 N THR A 224 58.368 -25.652 9.283 1.00 95.44 N ANISOU 1599 N THR A 224 12825 8796 14644 1491 -3519 1650 N ATOM 1600 CA THR A 224 58.278 -27.088 9.018 1.00 98.14 C ANISOU 1600 CA THR A 224 13385 8815 15087 1656 -3616 1644 C ATOM 1601 C THR A 224 58.660 -27.432 7.583 1.00100.41 C ANISOU 1601 C THR A 224 13507 9117 15528 1875 -3539 1431 C ATOM 1602 O THR A 224 58.872 -28.600 7.262 1.00104.45 O ANISOU 1602 O THR A 224 14159 9381 16145 2082 -3636 1393 O ATOM 1603 CB THR A 224 56.880 -27.676 9.312 1.00 90.11 C ANISOU 1603 CB THR A 224 12700 7540 13999 1411 -3558 1730 C ATOM 1604 OG1 THR A 224 55.930 -27.168 8.367 1.00 82.15 O ANISOU 1604 OG1 THR A 224 11610 6624 12981 1235 -3328 1601 O ATOM 1605 CG2 THR A 224 56.438 -27.341 10.725 1.00 88.66 C ANISOU 1605 CG2 THR A 224 12689 7353 13646 1183 -3613 1938 C ATOM 1606 N ARG A 225 58.734 -26.424 6.720 1.00 97.73 N ANISOU 1606 N ARG A 225 12886 9055 15193 1831 -3364 1291 N ATOM 1607 CA ARG A 225 59.152 -26.655 5.343 1.00 95.56 C ANISOU 1607 CA ARG A 225 12433 8832 15042 2035 -3278 1084 C ATOM 1608 C ARG A 225 58.231 -27.651 4.634 1.00 97.73 C ANISOU 1608 C ARG A 225 12940 8828 15366 2017 -3220 1007 C ATOM 1609 O ARG A 225 58.621 -28.289 3.657 1.00 97.64 O ANISOU 1609 O ARG A 225 12882 8749 15467 2240 -3210 851 O ATOM 1610 CB ARG A 225 60.585 -27.179 5.325 1.00 91.53 C ANISOU 1610 CB ARG A 225 11781 8347 14648 2390 -3444 1048 C ATOM 1611 CG ARG A 225 61.618 -26.131 5.637 1.00 88.57 C ANISOU 1611 CG ARG A 225 11091 8312 14250 2425 -3470 1062 C ATOM 1612 CD ARG A 225 61.912 -25.300 4.407 1.00 90.28 C ANISOU 1612 CD ARG A 225 10992 8810 14499 2439 -3275 879 C ATOM 1613 NE ARG A 225 62.783 -24.176 4.723 1.00 93.13 N ANISOU 1613 NE ARG A 225 11063 9501 14821 2404 -3280 900 N ATOM 1614 CZ ARG A 225 63.663 -23.650 3.879 1.00 93.29 C ANISOU 1614 CZ ARG A 225 10754 9792 14899 2525 -3199 764 C ATOM 1615 NH1 ARG A 225 63.800 -24.158 2.658 1.00 86.85 N ANISOU 1615 NH1 ARG A 225 9859 8962 14179 2708 -3101 591 N ATOM 1616 NH2 ARG A 225 64.416 -22.621 4.264 1.00 94.15 N ANISOU 1616 NH2 ARG A 225 10619 10189 14963 2453 -3214 799 N ATOM 1617 N SER A 226 57.004 -27.773 5.125 1.00 98.72 N ANISOU 1617 N SER A 226 13311 8798 15400 1744 -3179 1109 N ATOM 1618 CA SER A 226 56.077 -28.764 4.603 1.00102.85 C ANISOU 1618 CA SER A 226 14078 9041 15958 1685 -3145 1058 C ATOM 1619 C SER A 226 54.691 -28.550 5.201 1.00100.98 C ANISOU 1619 C SER A 226 14033 8741 15595 1326 -3064 1178 C ATOM 1620 O SER A 226 54.567 -28.226 6.384 1.00104.85 O ANISOU 1620 O SER A 226 14606 9249 15982 1189 -3124 1354 O ATOM 1621 CB SER A 226 56.588 -30.170 4.933 1.00105.52 C ANISOU 1621 CB SER A 226 14657 9047 16389 1915 -3351 1103 C ATOM 1622 OG SER A 226 55.779 -31.157 4.327 1.00112.23 O ANISOU 1622 OG SER A 226 15746 9613 17284 1868 -3322 1030 O ATOM 1623 N PRO A 227 53.642 -28.731 4.385 1.00 93.56 N ANISOU 1623 N PRO A 227 13155 7740 14654 1174 -2927 1079 N ATOM 1624 CA PRO A 227 52.261 -28.503 4.833 1.00 93.64 C ANISOU 1624 CA PRO A 227 13306 7726 14546 830 -2828 1174 C ATOM 1625 C PRO A 227 51.894 -29.333 6.064 1.00 89.90 C ANISOU 1625 C PRO A 227 13154 6984 14020 714 -2964 1375 C ATOM 1626 O PRO A 227 51.839 -30.555 5.997 1.00 88.57 O ANISOU 1626 O PRO A 227 13226 6506 13920 779 -3068 1381 O ATOM 1627 CB PRO A 227 51.422 -28.915 3.619 1.00 92.43 C ANISOU 1627 CB PRO A 227 13180 7502 14439 762 -2711 1011 C ATOM 1628 CG PRO A 227 52.338 -28.734 2.453 1.00 91.40 C ANISOU 1628 CG PRO A 227 12818 7503 14407 1029 -2677 817 C ATOM 1629 CD PRO A 227 53.712 -29.084 2.957 1.00 91.16 C ANISOU 1629 CD PRO A 227 12764 7423 14449 1316 -2849 863 C ATOM 1630 N ILE A 228 51.633 -28.649 7.173 1.00 90.41 N ANISOU 1630 N ILE A 228 13235 7164 13954 535 -2957 1536 N ATOM 1631 CA ILE A 228 51.387 -29.278 8.469 1.00 88.31 C ANISOU 1631 CA ILE A 228 13258 6688 13607 420 -3084 1748 C ATOM 1632 C ILE A 228 50.283 -30.344 8.496 1.00 90.43 C ANISOU 1632 C ILE A 228 13829 6664 13867 221 -3076 1797 C ATOM 1633 O ILE A 228 50.365 -31.294 9.276 1.00105.06 O ANISOU 1633 O ILE A 228 15966 8242 15708 222 -3227 1942 O ATOM 1634 CB ILE A 228 51.074 -28.212 9.536 1.00 87.01 C ANISOU 1634 CB ILE A 228 13044 6740 13277 216 -3027 1886 C ATOM 1635 CG1 ILE A 228 49.880 -27.361 9.091 1.00 84.49 C ANISOU 1635 CG1 ILE A 228 12606 6615 12881 -39 -2798 1818 C ATOM 1636 CG2 ILE A 228 52.287 -27.329 9.760 1.00 89.65 C ANISOU 1636 CG2 ILE A 228 13143 7308 13613 403 -3088 1875 C ATOM 1637 CD1 ILE A 228 49.368 -26.402 10.141 1.00 79.58 C ANISOU 1637 CD1 ILE A 228 11977 6175 12086 -257 -2723 1947 C ATOM 1638 N MET A 229 49.263 -30.192 7.655 1.00 84.55 N ANISOU 1638 N MET A 229 13026 5976 13122 45 -2908 1682 N ATOM 1639 CA MET A 229 48.113 -31.101 7.662 1.00 94.76 C ANISOU 1639 CA MET A 229 14577 7031 14396 -195 -2883 1722 C ATOM 1640 C MET A 229 47.722 -31.584 6.261 1.00100.20 C ANISOU 1640 C MET A 229 15234 7646 15193 -169 -2814 1516 C ATOM 1641 O MET A 229 46.960 -30.914 5.558 1.00 96.68 O ANISOU 1641 O MET A 229 14608 7409 14717 -310 -2647 1409 O ATOM 1642 CB MET A 229 46.912 -30.424 8.323 1.00 96.39 C ANISOU 1642 CB MET A 229 14778 7401 14445 -542 -2738 1829 C ATOM 1643 CG MET A 229 47.085 -30.178 9.808 1.00 97.09 C ANISOU 1643 CG MET A 229 14984 7504 14402 -622 -2808 2047 C ATOM 1644 SD MET A 229 45.715 -29.235 10.499 1.00125.97 S ANISOU 1644 SD MET A 229 18589 11406 17868 -995 -2607 2139 S ATOM 1645 CE MET A 229 45.980 -27.656 9.713 1.00101.82 C ANISOU 1645 CE MET A 229 15128 8741 14816 -884 -2456 1969 C ATOM 1646 N GLN A 230 48.219 -32.759 5.876 1.00109.24 N ANISOU 1646 N GLN A 230 16568 8485 16454 13 -2949 1463 N ATOM 1647 CA GLN A 230 48.071 -33.250 4.504 1.00112.31 C ANISOU 1647 CA GLN A 230 16930 8794 16948 94 -2904 1245 C ATOM 1648 C GLN A 230 47.052 -34.375 4.353 1.00113.40 C ANISOU 1648 C GLN A 230 17370 8624 17094 -132 -2920 1251 C ATOM 1649 O GLN A 230 47.415 -35.500 4.024 1.00112.68 O ANISOU 1649 O GLN A 230 17500 8213 17101 14 -3042 1196 O ATOM 1650 CB GLN A 230 49.424 -33.713 3.960 1.00112.34 C ANISOU 1650 CB GLN A 230 16899 8699 17088 498 -3026 1130 C ATOM 1651 CG GLN A 230 50.582 -32.829 4.380 1.00110.43 C ANISOU 1651 CG GLN A 230 16414 8704 16842 721 -3063 1169 C ATOM 1652 CD GLN A 230 51.847 -33.113 3.603 1.00108.27 C ANISOU 1652 CD GLN A 230 16016 8422 16701 1113 -3136 1013 C ATOM 1653 OE1 GLN A 230 51.799 -33.638 2.493 1.00114.48 O ANISOU 1653 OE1 GLN A 230 16814 9114 17570 1214 -3101 828 O ATOM 1654 NE2 GLN A 230 52.990 -32.759 4.181 1.00101.63 N ANISOU 1654 NE2 GLN A 230 15046 7694 15876 1334 -3238 1081 N ATOM 1655 N GLY A 231 45.778 -34.060 4.566 1.00117.64 N ANISOU 1655 N GLY A 231 17908 9262 17528 -488 -2795 1308 N ATOM 1656 CA GLY A 231 44.718 -35.049 4.470 1.00122.41 C ANISOU 1656 CA GLY A 231 18775 9611 18126 -759 -2797 1323 C ATOM 1657 C GLY A 231 44.547 -35.645 3.084 1.00126.24 C ANISOU 1657 C GLY A 231 19271 9982 18712 -698 -2783 1092 C ATOM 1658 O GLY A 231 45.105 -35.148 2.106 1.00126.06 O ANISOU 1658 O GLY A 231 19014 10135 18748 -472 -2734 910 O ATOM 1659 N ASN A 232 43.769 -36.721 3.001 1.00128.03 N ANISOU 1659 N ASN A 232 19783 9912 18950 -915 -2824 1098 N ATOM 1660 CA ASN A 232 43.505 -37.378 1.726 1.00125.08 C ANISOU 1660 CA ASN A 232 19464 9403 18660 -897 -2820 878 C ATOM 1661 C ASN A 232 42.047 -37.261 1.318 1.00121.82 C ANISOU 1661 C ASN A 232 18999 9110 18176 -1284 -2691 833 C ATOM 1662 O ASN A 232 41.720 -37.285 0.132 1.00120.82 O ANISOU 1662 O ASN A 232 18773 9049 18085 -1287 -2635 627 O ATOM 1663 CB ASN A 232 43.941 -38.839 1.776 1.00130.00 C ANISOU 1663 CB ASN A 232 20480 9541 19375 -784 -2998 880 C ATOM 1664 CG ASN A 232 45.447 -38.988 1.771 1.00134.43 C ANISOU 1664 CG ASN A 232 21037 10009 20031 -327 -3122 845 C ATOM 1665 OD1 ASN A 232 46.024 -39.656 2.631 1.00136.22 O ANISOU 1665 OD1 ASN A 232 21516 9962 20281 -212 -3276 995 O ATOM 1666 ND2 ASN A 232 46.097 -38.345 0.806 1.00135.10 N ANISOU 1666 ND2 ASN A 232 20826 10338 20167 -64 -3056 651 N ATOM 1667 N THR A 233 41.176 -37.140 2.315 1.00121.27 N ANISOU 1667 N THR A 233 18993 9082 18002 -1610 -2645 1027 N ATOM 1668 CA THR A 233 39.772 -36.820 2.084 1.00119.55 C ANISOU 1668 CA THR A 233 18658 9065 17703 -1981 -2505 1009 C ATOM 1669 C THR A 233 39.331 -35.789 3.118 1.00111.75 C ANISOU 1669 C THR A 233 17495 8379 16585 -2141 -2394 1189 C ATOM 1670 O THR A 233 40.041 -35.540 4.093 1.00111.72 O ANISOU 1670 O THR A 233 17537 8361 16552 -2012 -2446 1343 O ATOM 1671 CB THR A 233 38.860 -38.070 2.179 1.00115.44 C ANISOU 1671 CB THR A 233 18463 8217 17181 -2312 -2561 1048 C ATOM 1672 OG1 THR A 233 38.768 -38.505 3.542 1.00118.01 O ANISOU 1672 OG1 THR A 233 19039 8357 17442 -2473 -2620 1301 O ATOM 1673 CG2 THR A 233 39.403 -39.203 1.320 1.00116.23 C ANISOU 1673 CG2 THR A 233 18809 7947 17406 -2134 -2696 886 C ATOM 1674 N GLU A 234 38.163 -35.192 2.903 1.00104.37 N ANISOU 1674 N GLU A 234 16361 7723 15571 -2412 -2244 1163 N ATOM 1675 CA GLU A 234 37.609 -34.236 3.858 1.00106.20 C ANISOU 1675 CA GLU A 234 16433 8245 15672 -2578 -2123 1319 C ATOM 1676 C GLU A 234 37.566 -34.787 5.290 1.00111.91 C ANISOU 1676 C GLU A 234 17434 8766 16323 -2741 -2184 1567 C ATOM 1677 O GLU A 234 37.884 -34.080 6.252 1.00106.38 O ANISOU 1677 O GLU A 234 16673 8209 15537 -2691 -2156 1708 O ATOM 1678 CB GLU A 234 36.215 -33.783 3.420 1.00107.52 C ANISOU 1678 CB GLU A 234 16393 8691 15771 -2875 -1968 1258 C ATOM 1679 CG GLU A 234 36.182 -33.126 2.050 1.00114.65 C ANISOU 1679 CG GLU A 234 17013 9828 16720 -2726 -1902 1030 C ATOM 1680 CD GLU A 234 34.927 -32.305 1.835 1.00121.42 C ANISOU 1680 CD GLU A 234 17599 11050 17486 -2956 -1740 1003 C ATOM 1681 OE1 GLU A 234 34.090 -32.258 2.761 1.00124.91 O ANISOU 1681 OE1 GLU A 234 18061 11568 17832 -3230 -1671 1155 O ATOM 1682 OE2 GLU A 234 34.779 -31.703 0.749 1.00119.43 O ANISOU 1682 OE2 GLU A 234 17112 11014 17252 -2856 -1682 833 O ATOM 1683 N GLN A 235 37.173 -36.049 5.433 1.00118.83 N ANISOU 1683 N GLN A 235 18627 9301 17221 -2944 -2271 1621 N ATOM 1684 CA GLN A 235 37.136 -36.670 6.753 1.00121.97 C ANISOU 1684 CA GLN A 235 19326 9474 17543 -3107 -2339 1864 C ATOM 1685 C GLN A 235 38.532 -36.827 7.346 1.00114.64 C ANISOU 1685 C GLN A 235 18553 8352 16655 -2768 -2495 1954 C ATOM 1686 O GLN A 235 38.730 -36.626 8.545 1.00111.17 O ANISOU 1686 O GLN A 235 18202 7924 16115 -2802 -2513 2156 O ATOM 1687 CB GLN A 235 36.411 -38.014 6.714 1.00130.87 C ANISOU 1687 CB GLN A 235 20781 10256 18688 -3412 -2401 1901 C ATOM 1688 CG GLN A 235 34.904 -37.879 6.784 1.00142.04 C ANISOU 1688 CG GLN A 235 22086 11879 20004 -3854 -2245 1928 C ATOM 1689 CD GLN A 235 34.236 -39.108 7.367 1.00159.23 C ANISOU 1689 CD GLN A 235 24630 13726 22143 -4219 -2300 2076 C ATOM 1690 OE1 GLN A 235 34.750 -40.224 7.256 1.00166.85 O ANISOU 1690 OE1 GLN A 235 25942 14262 23192 -4152 -2463 2082 O ATOM 1691 NE2 GLN A 235 33.080 -38.909 7.994 1.00163.07 N ANISOU 1691 NE2 GLN A 235 25048 14412 22499 -4608 -2161 2196 N ATOM 1692 N HIS A 236 39.497 -37.186 6.506 1.00108.62 N ANISOU 1692 N HIS A 236 17815 7424 16031 -2438 -2608 1801 N ATOM 1693 CA HIS A 236 40.880 -37.286 6.952 1.00106.12 C ANISOU 1693 CA HIS A 236 17593 6962 15765 -2079 -2759 1862 C ATOM 1694 C HIS A 236 41.391 -35.904 7.352 1.00108.96 C ANISOU 1694 C HIS A 236 17638 7702 16061 -1919 -2682 1891 C ATOM 1695 O HIS A 236 42.101 -35.752 8.352 1.00109.71 O ANISOU 1695 O HIS A 236 17808 7769 16106 -1800 -2767 2050 O ATOM 1696 CB HIS A 236 41.759 -37.900 5.859 1.00106.89 C ANISOU 1696 CB HIS A 236 17738 6848 16025 -1750 -2871 1664 C ATOM 1697 CG HIS A 236 43.156 -38.204 6.306 1.00114.93 C ANISOU 1697 CG HIS A 236 18879 7682 17109 -1379 -3045 1726 C ATOM 1698 ND1 HIS A 236 44.219 -38.284 5.431 1.00114.88 N ANISOU 1698 ND1 HIS A 236 18779 7638 17233 -990 -3116 1546 N ATOM 1699 CD2 HIS A 236 43.669 -38.430 7.540 1.00118.92 C ANISOU 1699 CD2 HIS A 236 19578 8048 17558 -1331 -3165 1949 C ATOM 1700 CE1 HIS A 236 45.322 -38.557 6.104 1.00115.12 C ANISOU 1700 CE1 HIS A 236 18927 7518 17294 -715 -3274 1653 C ATOM 1701 NE2 HIS A 236 45.017 -38.648 7.386 1.00119.24 N ANISOU 1701 NE2 HIS A 236 19629 7972 17703 -913 -3314 1899 N ATOM 1702 N GLN A 237 41.011 -34.896 6.571 1.00103.66 N ANISOU 1702 N GLN A 237 16624 7378 15383 -1925 -2527 1739 N ATOM 1703 CA GLN A 237 41.386 -33.518 6.854 1.00100.82 C ANISOU 1703 CA GLN A 237 15966 7381 14959 -1802 -2439 1750 C ATOM 1704 C GLN A 237 40.798 -33.078 8.191 1.00101.19 C ANISOU 1704 C GLN A 237 16056 7549 14843 -2047 -2374 1964 C ATOM 1705 O GLN A 237 41.496 -32.500 9.026 1.00 91.05 O ANISOU 1705 O GLN A 237 14740 6356 13498 -1919 -2411 2072 O ATOM 1706 CB GLN A 237 40.911 -32.587 5.732 1.00 97.37 C ANISOU 1706 CB GLN A 237 15193 7269 14536 -1802 -2280 1555 C ATOM 1707 CG GLN A 237 41.600 -31.231 5.714 1.00 99.80 C ANISOU 1707 CG GLN A 237 15204 7897 14818 -1589 -2215 1518 C ATOM 1708 CD GLN A 237 43.093 -31.328 5.422 1.00102.19 C ANISOU 1708 CD GLN A 237 15489 8109 15228 -1213 -2345 1454 C ATOM 1709 OE1 GLN A 237 43.915 -30.710 6.107 1.00100.08 O ANISOU 1709 OE1 GLN A 237 15152 7946 14928 -1065 -2385 1538 O ATOM 1710 NE2 GLN A 237 43.450 -32.110 4.407 1.00103.21 N ANISOU 1710 NE2 GLN A 237 15679 8054 15482 -1060 -2412 1300 N ATOM 1711 N LEU A 238 39.512 -33.361 8.391 1.00106.82 N ANISOU 1711 N LEU A 238 16839 8271 15478 -2404 -2276 2020 N ATOM 1712 CA LEU A 238 38.839 -32.987 9.632 1.00109.91 C ANISOU 1712 CA LEU A 238 17270 8790 15701 -2660 -2191 2215 C ATOM 1713 C LEU A 238 39.440 -33.716 10.826 1.00113.80 C ANISOU 1713 C LEU A 238 18092 9002 16143 -2646 -2346 2430 C ATOM 1714 O LEU A 238 39.502 -33.178 11.934 1.00113.61 O ANISOU 1714 O LEU A 238 18081 9103 15984 -2697 -2321 2587 O ATOM 1715 CB LEU A 238 37.336 -33.249 9.545 1.00110.87 C ANISOU 1715 CB LEU A 238 17391 8978 15757 -3053 -2056 2224 C ATOM 1716 CG LEU A 238 36.481 -32.034 9.179 1.00112.42 C ANISOU 1716 CG LEU A 238 17228 9600 15887 -3149 -1851 2129 C ATOM 1717 CD1 LEU A 238 35.043 -32.454 8.907 1.00117.27 C ANISOU 1717 CD1 LEU A 238 17827 10266 16464 -3516 -1741 2112 C ATOM 1718 CD2 LEU A 238 36.541 -30.978 10.279 1.00104.06 C ANISOU 1718 CD2 LEU A 238 16069 8791 14679 -3146 -1765 2258 C ATOM 1719 N ALA A 239 39.884 -34.946 10.594 1.00112.88 N ANISOU 1719 N ALA A 239 18257 8501 16131 -2569 -2510 2435 N ATOM 1720 CA ALA A 239 40.543 -35.709 11.636 1.00110.80 C ANISOU 1720 CA ALA A 239 18328 7939 15833 -2512 -2683 2636 C ATOM 1721 C ALA A 239 41.891 -35.072 11.926 1.00108.41 C ANISOU 1721 C ALA A 239 17909 7729 15552 -2142 -2786 2642 C ATOM 1722 O ALA A 239 42.228 -34.822 13.084 1.00114.11 O ANISOU 1722 O ALA A 239 18719 8482 16156 -2143 -2836 2823 O ATOM 1723 CB ALA A 239 40.713 -37.159 11.214 1.00107.68 C ANISOU 1723 CB ALA A 239 18262 7095 15555 -2487 -2838 2621 C ATOM 1724 N LEU A 240 42.659 -34.808 10.872 1.00 98.96 N ANISOU 1724 N LEU A 240 16511 6591 14500 -1835 -2815 2442 N ATOM 1725 CA LEU A 240 43.982 -34.214 11.034 1.00103.15 C ANISOU 1725 CA LEU A 240 16900 7226 15065 -1484 -2911 2428 C ATOM 1726 C LEU A 240 43.910 -32.905 11.812 1.00101.82 C ANISOU 1726 C LEU A 240 16523 7414 14752 -1551 -2805 2506 C ATOM 1727 O LEU A 240 44.693 -32.691 12.742 1.00 99.48 O ANISOU 1727 O LEU A 240 16281 7125 14392 -1428 -2914 2638 O ATOM 1728 CB LEU A 240 44.665 -34.008 9.681 1.00104.63 C ANISOU 1728 CB LEU A 240 16857 7484 15415 -1189 -2912 2184 C ATOM 1729 CG LEU A 240 45.271 -35.277 9.079 1.00113.57 C ANISOU 1729 CG LEU A 240 18210 8242 16698 -979 -3075 2111 C ATOM 1730 CD1 LEU A 240 46.017 -34.976 7.791 1.00115.42 C ANISOU 1730 CD1 LEU A 240 18192 8588 17073 -672 -3060 1868 C ATOM 1731 CD2 LEU A 240 46.195 -35.934 10.083 1.00117.03 C ANISOU 1731 CD2 LEU A 240 18906 8429 17133 -804 -3287 2290 C ATOM 1732 N ILE A 241 42.963 -32.047 11.432 1.00 98.50 N ANISOU 1732 N ILE A 241 15870 7282 14274 -1742 -2600 2422 N ATOM 1733 CA ILE A 241 42.721 -30.777 12.122 1.00101.72 C ANISOU 1733 CA ILE A 241 16090 8023 14534 -1829 -2475 2479 C ATOM 1734 C ILE A 241 42.458 -30.968 13.618 1.00103.92 C ANISOU 1734 C ILE A 241 16604 8239 14641 -2022 -2507 2721 C ATOM 1735 O ILE A 241 42.939 -30.194 14.449 1.00 99.49 O ANISOU 1735 O ILE A 241 15989 7839 13975 -1959 -2521 2804 O ATOM 1736 CB ILE A 241 41.535 -29.988 11.488 1.00 87.84 C ANISOU 1736 CB ILE A 241 14088 6549 12737 -2029 -2247 2361 C ATOM 1737 CG1 ILE A 241 41.970 -29.310 10.182 1.00 83.95 C ANISOU 1737 CG1 ILE A 241 13302 6229 12368 -1803 -2198 2137 C ATOM 1738 CG2 ILE A 241 40.989 -28.943 12.463 1.00 80.98 C ANISOU 1738 CG2 ILE A 241 13127 5957 11686 -2194 -2112 2464 C ATOM 1739 CD1 ILE A 241 40.861 -28.534 9.491 1.00 77.09 C ANISOU 1739 CD1 ILE A 241 12193 5632 11464 -1963 -1995 2019 C ATOM 1740 N SER A 242 41.691 -31.999 13.957 1.00107.88 N ANISOU 1740 N SER A 242 17377 8508 15106 -2269 -2520 2833 N ATOM 1741 CA SER A 242 41.391 -32.297 15.353 1.00111.37 C ANISOU 1741 CA SER A 242 18073 8869 15373 -2476 -2547 3073 C ATOM 1742 C SER A 242 42.633 -32.763 16.107 1.00109.91 C ANISOU 1742 C SER A 242 18105 8469 15188 -2243 -2781 3209 C ATOM 1743 O SER A 242 42.811 -32.447 17.285 1.00105.13 O ANISOU 1743 O SER A 242 17595 7929 14422 -2294 -2813 3378 O ATOM 1744 CB SER A 242 40.280 -33.345 15.458 1.00118.76 C ANISOU 1744 CB SER A 242 19254 9594 16275 -2813 -2504 3160 C ATOM 1745 OG SER A 242 39.005 -32.759 15.255 1.00120.47 O ANISOU 1745 OG SER A 242 19276 10082 16415 -3092 -2275 3103 O ATOM 1746 N GLN A 243 43.490 -33.510 15.418 1.00113.49 N ANISOU 1746 N GLN A 243 18631 8675 15816 -1979 -2946 3131 N ATOM 1747 CA GLN A 243 44.713 -34.024 16.022 1.00117.52 C ANISOU 1747 CA GLN A 243 19329 8974 16348 -1717 -3186 3246 C ATOM 1748 C GLN A 243 45.744 -32.916 16.222 1.00116.60 C ANISOU 1748 C GLN A 243 18951 9132 16218 -1460 -3224 3202 C ATOM 1749 O GLN A 243 46.811 -33.145 16.801 1.00117.96 O ANISOU 1749 O GLN A 243 19223 9204 16393 -1235 -3423 3297 O ATOM 1750 CB GLN A 243 45.295 -35.157 15.175 1.00121.21 C ANISOU 1750 CB GLN A 243 19943 9100 17012 -1492 -3342 3157 C ATOM 1751 CG GLN A 243 44.436 -36.415 15.151 1.00127.92 C ANISOU 1751 CG GLN A 243 21135 9601 17867 -1741 -3356 3233 C ATOM 1752 CD GLN A 243 44.869 -37.384 14.072 1.00131.15 C ANISOU 1752 CD GLN A 243 21643 9709 18479 -1528 -3467 3083 C ATOM 1753 OE1 GLN A 243 45.822 -37.120 13.338 1.00138.23 O ANISOU 1753 OE1 GLN A 243 22340 10672 19509 -1183 -3526 2923 O ATOM 1754 NE2 GLN A 243 44.169 -38.510 13.962 1.00122.98 N ANISOU 1754 NE2 GLN A 243 20920 8343 17462 -1738 -3491 3130 N ATOM 1755 N LEU A 244 45.419 -31.715 15.749 1.00108.24 N ANISOU 1755 N LEU A 244 17561 8421 15143 -1499 -3040 3062 N ATOM 1756 CA LEU A 244 46.301 -30.567 15.922 1.00 99.10 C ANISOU 1756 CA LEU A 244 16152 7539 13963 -1302 -3055 3014 C ATOM 1757 C LEU A 244 45.681 -29.464 16.769 1.00 99.42 C ANISOU 1757 C LEU A 244 16105 7867 13802 -1520 -2904 3086 C ATOM 1758 O LEU A 244 46.335 -28.910 17.655 1.00100.72 O ANISOU 1758 O LEU A 244 16267 8141 13861 -1450 -2983 3177 O ATOM 1759 CB LEU A 244 46.726 -29.987 14.575 1.00 94.37 C ANISOU 1759 CB LEU A 244 15229 7102 13526 -1094 -2989 2772 C ATOM 1760 CG LEU A 244 47.802 -28.903 14.710 1.00 93.45 C ANISOU 1760 CG LEU A 244 14867 7237 13404 -878 -3031 2725 C ATOM 1761 CD1 LEU A 244 49.091 -29.524 15.205 1.00 93.80 C ANISOU 1761 CD1 LEU A 244 15033 7109 13498 -616 -3285 2814 C ATOM 1762 CD2 LEU A 244 48.030 -28.177 13.396 1.00 92.97 C ANISOU 1762 CD2 LEU A 244 14478 7376 13469 -736 -2920 2495 C ATOM 1763 N CYS A 245 44.423 -29.139 16.497 1.00 99.54 N ANISOU 1763 N CYS A 245 16046 8013 13762 -1777 -2690 3038 N ATOM 1764 CA CYS A 245 43.810 -27.964 17.110 1.00108.47 C ANISOU 1764 CA CYS A 245 17045 9450 14720 -1946 -2518 3060 C ATOM 1765 C CYS A 245 42.840 -28.312 18.235 1.00107.71 C ANISOU 1765 C CYS A 245 17185 9313 14428 -2260 -2451 3250 C ATOM 1766 O CYS A 245 42.064 -27.465 18.679 1.00100.87 O ANISOU 1766 O CYS A 245 16222 8692 13413 -2438 -2273 3259 O ATOM 1767 CB CYS A 245 43.096 -27.122 16.043 1.00115.57 C ANISOU 1767 CB CYS A 245 17643 10592 15675 -1987 -2309 2864 C ATOM 1768 SG CYS A 245 44.075 -26.793 14.543 1.00104.70 S ANISOU 1768 SG CYS A 245 15994 9264 14525 -1657 -2355 2630 S ATOM 1769 N GLY A 246 42.898 -29.553 18.704 1.00113.29 N ANISOU 1769 N GLY A 246 18207 9708 15128 -2321 -2591 3404 N ATOM 1770 CA GLY A 246 41.903 -30.051 19.635 1.00115.75 C ANISOU 1770 CA GLY A 246 18761 9952 15266 -2649 -2518 3585 C ATOM 1771 C GLY A 246 40.709 -30.508 18.827 1.00120.43 C ANISOU 1771 C GLY A 246 19316 10514 15926 -2875 -2364 3503 C ATOM 1772 O GLY A 246 40.772 -30.539 17.601 1.00116.27 O ANISOU 1772 O GLY A 246 18617 9981 15579 -2752 -2348 3319 O ATOM 1773 N SER A 247 39.617 -30.859 19.493 1.00130.20 N ANISOU 1773 N SER A 247 20706 11748 17014 -3214 -2248 3635 N ATOM 1774 CA SER A 247 38.454 -31.364 18.772 1.00130.95 C ANISOU 1774 CA SER A 247 20770 11817 17168 -3460 -2112 3567 C ATOM 1775 C SER A 247 37.310 -30.360 18.716 1.00128.71 C ANISOU 1775 C SER A 247 20211 11910 16781 -3658 -1848 3489 C ATOM 1776 O SER A 247 37.160 -29.509 19.595 1.00125.93 O ANISOU 1776 O SER A 247 19804 11790 16253 -3707 -1751 3556 O ATOM 1777 CB SER A 247 37.984 -32.698 19.356 1.00135.97 C ANISOU 1777 CB SER A 247 21780 12138 17745 -3722 -2178 3759 C ATOM 1778 OG SER A 247 37.876 -32.631 20.764 1.00139.74 O ANISOU 1778 OG SER A 247 22453 12647 17996 -3877 -2169 3978 O ATOM 1779 N ILE A 248 36.512 -30.472 17.660 1.00127.94 N ANISOU 1779 N ILE A 248 19945 11872 16794 -3758 -1738 3342 N ATOM 1780 CA ILE A 248 35.397 -29.568 17.420 1.00121.02 C ANISOU 1780 CA ILE A 248 18781 11354 15849 -3916 -1497 3246 C ATOM 1781 C ILE A 248 34.359 -29.705 18.531 1.00120.76 C ANISOU 1781 C ILE A 248 18864 11417 15601 -4268 -1355 3417 C ATOM 1782 O ILE A 248 33.639 -30.701 18.604 1.00113.99 O ANISOU 1782 O ILE A 248 18176 10404 14733 -4547 -1342 3503 O ATOM 1783 CB ILE A 248 34.733 -29.866 16.059 1.00115.32 C ANISOU 1783 CB ILE A 248 17888 10642 15286 -3974 -1438 3068 C ATOM 1784 CG1 ILE A 248 35.721 -30.557 15.109 1.00110.58 C ANISOU 1784 CG1 ILE A 248 17368 9753 14895 -3723 -1635 2968 C ATOM 1785 CG2 ILE A 248 34.169 -28.599 15.441 1.00100.53 C ANISOU 1785 CG2 ILE A 248 15635 9154 13409 -3920 -1254 2899 C ATOM 1786 CD1 ILE A 248 36.718 -29.633 14.464 1.00 87.77 C ANISOU 1786 CD1 ILE A 248 14254 6992 12104 -3359 -1678 2815 C ATOM 1787 N THR A 249 34.290 -28.699 19.396 1.00126.88 N ANISOU 1787 N THR A 249 19554 12451 16202 -4260 -1247 3465 N ATOM 1788 CA THR A 249 33.409 -28.744 20.554 1.00134.00 C ANISOU 1788 CA THR A 249 20570 13469 16875 -4567 -1105 3630 C ATOM 1789 C THR A 249 32.563 -27.489 20.633 1.00128.62 C ANISOU 1789 C THR A 249 19582 13207 16082 -4613 -861 3534 C ATOM 1790 O THR A 249 33.086 -26.386 20.545 1.00124.23 O ANISOU 1790 O THR A 249 18854 12824 15525 -4369 -845 3432 O ATOM 1791 CB THR A 249 34.218 -28.850 21.855 1.00139.96 C ANISOU 1791 CB THR A 249 21609 14099 17471 -4521 -1229 3826 C ATOM 1792 OG1 THR A 249 34.991 -30.055 21.839 1.00143.30 O ANISOU 1792 OG1 THR A 249 22336 14120 17991 -4465 -1466 3930 O ATOM 1793 CG2 THR A 249 33.293 -28.860 23.059 1.00143.91 C ANISOU 1793 CG2 THR A 249 22226 14738 17712 -4843 -1066 3995 C ATOM 1794 N PRO A 250 31.245 -27.652 20.805 1.00127.77 N ANISOU 1794 N PRO A 250 19404 13264 15878 -4928 -668 3565 N ATOM 1795 CA PRO A 250 30.368 -26.489 20.967 1.00124.22 C ANISOU 1795 CA PRO A 250 18668 13222 15307 -4969 -425 3481 C ATOM 1796 C PRO A 250 30.851 -25.595 22.105 1.00120.90 C ANISOU 1796 C PRO A 250 18312 12933 14690 -4858 -394 3552 C ATOM 1797 O PRO A 250 30.461 -24.430 22.185 1.00119.02 O ANISOU 1797 O PRO A 250 17847 13005 14371 -4781 -230 3452 O ATOM 1798 CB PRO A 250 29.017 -27.119 21.313 1.00123.66 C ANISOU 1798 CB PRO A 250 18609 13247 15129 -5369 -258 3572 C ATOM 1799 CG PRO A 250 29.071 -28.473 20.686 1.00119.95 C ANISOU 1799 CG PRO A 250 18316 12444 14816 -5501 -406 3607 C ATOM 1800 CD PRO A 250 30.497 -28.921 20.823 1.00121.97 C ANISOU 1800 CD PRO A 250 18846 12350 15149 -5262 -664 3673 C ATOM 1801 N GLU A 251 31.694 -26.141 22.975 1.00120.08 N ANISOU 1801 N GLU A 251 18527 12589 14508 -4845 -559 3720 N ATOM 1802 CA GLU A 251 32.288 -25.357 24.045 1.00121.70 C ANISOU 1802 CA GLU A 251 18822 12891 14529 -4731 -568 3787 C ATOM 1803 C GLU A 251 33.401 -24.498 23.480 1.00115.72 C ANISOU 1803 C GLU A 251 17928 12141 13898 -4366 -689 3640 C ATOM 1804 O GLU A 251 33.524 -23.318 23.806 1.00113.56 O ANISOU 1804 O GLU A 251 17529 12094 13525 -4241 -604 3568 O ATOM 1805 CB GLU A 251 32.859 -26.262 25.128 1.00132.56 C ANISOU 1805 CB GLU A 251 20586 14003 15776 -4832 -727 4021 C ATOM 1806 CG GLU A 251 33.895 -25.563 25.982 1.00141.64 C ANISOU 1806 CG GLU A 251 21842 15175 16799 -4627 -836 4067 C ATOM 1807 CD GLU A 251 34.614 -26.506 26.914 1.00154.41 C ANISOU 1807 CD GLU A 251 23843 16505 18319 -4675 -1042 4293 C ATOM 1808 OE1 GLU A 251 34.019 -27.538 27.290 1.00158.67 O ANISOU 1808 OE1 GLU A 251 24597 16898 18791 -4947 -1024 4452 O ATOM 1809 OE2 GLU A 251 35.775 -26.213 27.271 1.00158.02 O ANISOU 1809 OE2 GLU A 251 24391 16885 18765 -4444 -1227 4315 O ATOM 1810 N VAL A 252 34.217 -25.112 22.634 1.00112.24 N ANISOU 1810 N VAL A 252 17523 11448 13675 -4201 -887 3596 N ATOM 1811 CA VAL A 252 35.326 -24.434 21.981 1.00105.47 C ANISOU 1811 CA VAL A 252 16531 10582 12960 -3864 -1012 3459 C ATOM 1812 C VAL A 252 34.812 -23.524 20.860 1.00110.29 C ANISOU 1812 C VAL A 252 16792 11430 13683 -3768 -861 3241 C ATOM 1813 O VAL A 252 35.262 -22.386 20.694 1.00108.74 O ANISOU 1813 O VAL A 252 16432 11396 13488 -3566 -836 3129 O ATOM 1814 CB VAL A 252 36.332 -25.478 21.432 1.00 97.75 C ANISOU 1814 CB VAL A 252 15707 9259 12175 -3719 -1264 3482 C ATOM 1815 CG1 VAL A 252 37.199 -24.896 20.353 1.00 95.82 C ANISOU 1815 CG1 VAL A 252 15247 9036 12124 -3409 -1345 3298 C ATOM 1816 CG2 VAL A 252 37.198 -26.016 22.557 1.00 99.69 C ANISOU 1816 CG2 VAL A 252 16267 9300 12308 -3696 -1452 3678 C ATOM 1817 N TRP A 253 33.833 -24.033 20.125 1.00112.44 N ANISOU 1817 N TRP A 253 16961 11722 14039 -3929 -762 3188 N ATOM 1818 CA TRP A 253 33.312 -23.393 18.927 1.00103.56 C ANISOU 1818 CA TRP A 253 15521 10787 13039 -3845 -648 2990 C ATOM 1819 C TRP A 253 31.792 -23.307 19.043 1.00104.05 C ANISOU 1819 C TRP A 253 15449 11086 12999 -4109 -418 2987 C ATOM 1820 O TRP A 253 31.072 -24.171 18.531 1.00 98.54 O ANISOU 1820 O TRP A 253 14741 10324 12375 -4301 -397 2988 O ATOM 1821 CB TRP A 253 33.695 -24.248 17.720 1.00102.05 C ANISOU 1821 CB TRP A 253 15325 10369 13080 -3764 -790 2908 C ATOM 1822 CG TRP A 253 33.267 -23.732 16.392 1.00 97.74 C ANISOU 1822 CG TRP A 253 14483 9983 12671 -3669 -708 2708 C ATOM 1823 CD1 TRP A 253 32.397 -22.713 16.141 1.00 93.31 C ANISOU 1823 CD1 TRP A 253 13660 9740 12053 -3681 -514 2606 C ATOM 1824 CD2 TRP A 253 33.663 -24.248 15.116 1.00 90.32 C ANISOU 1824 CD2 TRP A 253 13487 8888 11940 -3544 -820 2587 C ATOM 1825 NE1 TRP A 253 32.241 -22.551 14.783 1.00 89.67 N ANISOU 1825 NE1 TRP A 253 12987 9334 11751 -3573 -508 2438 N ATOM 1826 CE2 TRP A 253 33.006 -23.484 14.134 1.00 84.56 C ANISOU 1826 CE2 TRP A 253 12461 8403 11264 -3495 -689 2420 C ATOM 1827 CE3 TRP A 253 34.517 -25.276 14.710 1.00 89.55 C ANISOU 1827 CE3 TRP A 253 13569 8472 11985 -3456 -1018 2599 C ATOM 1828 CZ2 TRP A 253 33.177 -23.715 12.774 1.00 81.65 C ANISOU 1828 CZ2 TRP A 253 11975 7975 11073 -3377 -750 2269 C ATOM 1829 CZ3 TRP A 253 34.684 -25.505 13.364 1.00 89.92 C ANISOU 1829 CZ3 TRP A 253 13494 8458 12212 -3332 -1069 2440 C ATOM 1830 CH2 TRP A 253 34.018 -24.727 12.410 1.00 86.22 C ANISOU 1830 CH2 TRP A 253 12734 8244 11782 -3301 -935 2278 C ATOM 1831 N PRO A 254 31.301 -22.267 19.733 1.00106.57 N ANISOU 1831 N PRO A 254 15663 11685 13143 -4122 -245 2981 N ATOM 1832 CA PRO A 254 29.882 -22.006 20.006 1.00107.97 C ANISOU 1832 CA PRO A 254 15689 12143 13193 -4344 -5 2978 C ATOM 1833 C PRO A 254 28.974 -22.232 18.800 1.00109.95 C ANISOU 1833 C PRO A 254 15693 12494 13589 -4417 70 2851 C ATOM 1834 O PRO A 254 29.089 -21.518 17.808 1.00108.90 O ANISOU 1834 O PRO A 254 15338 12463 13576 -4205 75 2686 O ATOM 1835 CB PRO A 254 29.875 -20.524 20.386 1.00107.13 C ANISOU 1835 CB PRO A 254 15436 12305 12964 -4169 125 2895 C ATOM 1836 CG PRO A 254 31.197 -20.310 21.023 1.00108.34 C ANISOU 1836 CG PRO A 254 15799 12288 13076 -4000 -40 2958 C ATOM 1837 CD PRO A 254 32.170 -21.229 20.314 1.00107.99 C ANISOU 1837 CD PRO A 254 15869 11928 13235 -3905 -278 2968 C ATOM 1838 N ASN A 255 28.080 -23.212 18.897 1.00118.66 N ANISOU 1838 N ASN A 255 16841 13573 14671 -4726 124 2932 N ATOM 1839 CA ASN A 255 27.104 -23.493 17.841 1.00122.55 C ANISOU 1839 CA ASN A 255 17101 14182 15280 -4845 197 2820 C ATOM 1840 C ASN A 255 27.604 -24.421 16.736 1.00118.08 C ANISOU 1840 C ASN A 255 16602 13331 14934 -4807 7 2762 C ATOM 1841 O ASN A 255 26.857 -24.734 15.805 1.00115.46 O ANISOU 1841 O ASN A 255 16097 13071 14701 -4912 42 2664 O ATOM 1842 CB ASN A 255 26.559 -22.200 17.219 1.00123.47 C ANISOU 1842 CB ASN A 255 16865 14643 15406 -4666 346 2646 C ATOM 1843 CG ASN A 255 25.249 -21.761 17.836 1.00127.96 C ANISOU 1843 CG ASN A 255 17257 15558 15802 -4856 592 2665 C ATOM 1844 OD1 ASN A 255 24.914 -22.146 18.957 1.00132.74 O ANISOU 1844 OD1 ASN A 255 18017 16178 16240 -5082 669 2815 O ATOM 1845 ND2 ASN A 255 24.494 -20.952 17.100 1.00126.08 N ANISOU 1845 ND2 ASN A 255 16693 15613 15600 -4760 717 2513 N ATOM 1846 N VAL A 256 28.855 -24.863 16.834 1.00113.58 N ANISOU 1846 N VAL A 256 16277 12446 14433 -4653 -195 2816 N ATOM 1847 CA VAL A 256 29.417 -25.732 15.803 1.00110.74 C ANISOU 1847 CA VAL A 256 15995 11804 14277 -4581 -376 2750 C ATOM 1848 C VAL A 256 28.490 -26.905 15.493 1.00118.09 C ANISOU 1848 C VAL A 256 16984 12638 15248 -4909 -363 2783 C ATOM 1849 O VAL A 256 28.376 -27.334 14.345 1.00115.51 O ANISOU 1849 O VAL A 256 16574 12235 15078 -4895 -426 2658 O ATOM 1850 CB VAL A 256 30.809 -26.275 16.173 1.00101.42 C ANISOU 1850 CB VAL A 256 15112 10279 13144 -4415 -596 2841 C ATOM 1851 CG1 VAL A 256 30.751 -27.085 17.462 1.00103.02 C ANISOU 1851 CG1 VAL A 256 15630 10313 13199 -4649 -625 3067 C ATOM 1852 CG2 VAL A 256 31.345 -27.122 15.035 1.00 92.22 C ANISOU 1852 CG2 VAL A 256 14005 8844 12192 -4315 -765 2748 C ATOM 1853 N ASP A 257 27.824 -27.422 16.516 1.00129.69 N ANISOU 1853 N ASP A 257 18598 14113 16563 -5218 -281 2950 N ATOM 1854 CA ASP A 257 26.905 -28.530 16.306 1.00142.55 C ANISOU 1854 CA ASP A 257 20291 15656 18214 -5574 -259 2995 C ATOM 1855 C ASP A 257 25.634 -28.068 15.605 1.00146.29 C ANISOU 1855 C ASP A 257 20400 16486 18698 -5705 -82 2859 C ATOM 1856 O ASP A 257 24.597 -27.871 16.240 1.00151.52 O ANISOU 1856 O ASP A 257 20947 17412 19212 -5949 105 2922 O ATOM 1857 CB ASP A 257 26.595 -29.241 17.621 1.00146.24 C ANISOU 1857 CB ASP A 257 21037 16021 18506 -5883 -222 3227 C ATOM 1858 CG ASP A 257 27.666 -30.242 17.997 1.00152.76 C ANISOU 1858 CG ASP A 257 22273 16396 19373 -5837 -448 3363 C ATOM 1859 OD1 ASP A 257 28.479 -30.609 17.118 1.00148.79 O ANISOU 1859 OD1 ASP A 257 21830 15645 19056 -5621 -628 3267 O ATOM 1860 OD2 ASP A 257 27.694 -30.666 19.169 1.00162.67 O ANISOU 1860 OD2 ASP A 257 23790 17548 20469 -6010 -446 3568 O ATOM 1861 N ASN A 258 25.742 -27.895 14.289 1.00139.60 N ANISOU 1861 N ASN A 258 19367 15654 18021 -5532 -144 2671 N ATOM 1862 CA ASN A 258 24.621 -27.509 13.443 1.00130.81 C ANISOU 1862 CA ASN A 258 17904 14857 16939 -5622 -17 2526 C ATOM 1863 C ASN A 258 24.827 -27.928 11.986 1.00127.61 C ANISOU 1863 C ASN A 258 17438 14316 16731 -5525 -152 2358 C ATOM 1864 O ASN A 258 24.646 -27.116 11.084 1.00123.60 O ANISOU 1864 O ASN A 258 16646 14034 16283 -5337 -112 2194 O ATOM 1865 CB ASN A 258 24.383 -25.995 13.512 1.00121.43 C ANISOU 1865 CB ASN A 258 16412 14053 15674 -5398 139 2441 C ATOM 1866 CG ASN A 258 23.565 -25.578 14.726 1.00124.39 C ANISOU 1866 CG ASN A 258 16729 14696 15840 -5585 343 2558 C ATOM 1867 OD1 ASN A 258 22.863 -26.387 15.328 1.00136.87 O ANISOU 1867 OD1 ASN A 258 18408 16262 17336 -5936 404 2682 O ATOM 1868 ND2 ASN A 258 23.645 -24.302 15.081 1.00118.90 N ANISOU 1868 ND2 ASN A 258 15877 14245 15053 -5356 455 2516 N ATOM 1869 N TYR A 259 25.209 -29.184 11.747 1.00128.88 N ANISOU 1869 N TYR A 259 17878 14105 16987 -5645 -312 2395 N ATOM 1870 CA TYR A 259 25.343 -29.657 10.368 1.00131.69 C ANISOU 1870 CA TYR A 259 18193 14328 17517 -5577 -435 2227 C ATOM 1871 C TYR A 259 25.232 -31.158 10.148 1.00125.05 C ANISOU 1871 C TYR A 259 17630 13134 16749 -5845 -561 2266 C ATOM 1872 O TYR A 259 24.273 -31.612 9.539 1.00128.61 O ANISOU 1872 O TYR A 259 17967 13670 17228 -6103 -529 2194 O ATOM 1873 CB TYR A 259 26.629 -29.161 9.720 1.00145.99 C ANISOU 1873 CB TYR A 259 20015 16015 19441 -5149 -560 2117 C ATOM 1874 CG TYR A 259 26.687 -29.498 8.248 1.00151.91 C ANISOU 1874 CG TYR A 259 20682 16691 20347 -5064 -657 1924 C ATOM 1875 CD1 TYR A 259 26.329 -28.555 7.291 1.00148.37 C ANISOU 1875 CD1 TYR A 259 19897 16549 19928 -4908 -587 1756 C ATOM 1876 CD2 TYR A 259 27.074 -30.766 7.815 1.00153.57 C ANISOU 1876 CD2 TYR A 259 21163 16522 20666 -5141 -820 1910 C ATOM 1877 CE1 TYR A 259 26.371 -28.851 5.947 1.00148.48 C ANISOU 1877 CE1 TYR A 259 19842 16509 20066 -4835 -675 1580 C ATOM 1878 CE2 TYR A 259 27.119 -31.072 6.469 1.00153.87 C ANISOU 1878 CE2 TYR A 259 21135 16496 20833 -5064 -904 1723 C ATOM 1879 CZ TYR A 259 26.766 -30.108 5.539 1.00152.25 C ANISOU 1879 CZ TYR A 259 20587 16616 20645 -4915 -830 1559 C ATOM 1880 OH TYR A 259 26.804 -30.393 4.194 1.00151.87 O ANISOU 1880 OH TYR A 259 20477 16521 20708 -4840 -913 1372 O ATOM 1881 N LEU A 267 33.175 -37.282 13.695 1.00130.94 N ANISOU 1881 N LEU A 267 21227 10754 17771 -4925 -1958 3140 N ATOM 1882 CA LEU A 267 34.387 -36.660 14.230 1.00132.12 C ANISOU 1882 CA LEU A 267 21367 10929 17903 -4558 -2048 3190 C ATOM 1883 C LEU A 267 34.929 -37.304 15.498 1.00144.48 C ANISOU 1883 C LEU A 267 23316 12216 19365 -4580 -2180 3447 C ATOM 1884 O LEU A 267 34.287 -38.172 16.096 1.00144.50 O ANISOU 1884 O LEU A 267 23601 12021 19281 -4913 -2179 3612 O ATOM 1885 CB LEU A 267 34.141 -35.177 14.504 1.00120.95 C ANISOU 1885 CB LEU A 267 19583 9991 16381 -4505 -1869 3152 C ATOM 1886 CG LEU A 267 33.795 -34.303 13.300 1.00116.05 C ANISOU 1886 CG LEU A 267 18559 9681 15852 -4400 -1749 2906 C ATOM 1887 CD1 LEU A 267 33.357 -32.921 13.760 1.00110.90 C ANISOU 1887 CD1 LEU A 267 17600 9472 15065 -4411 -1560 2906 C ATOM 1888 CD2 LEU A 267 34.982 -34.213 12.358 1.00117.10 C ANISOU 1888 CD2 LEU A 267 18631 9702 16160 -3990 -1889 2740 C ATOM 1889 N VAL A 268 36.119 -36.856 15.897 1.00151.42 N ANISOU 1889 N VAL A 268 24198 13089 20247 -4229 -2297 3480 N ATOM 1890 CA VAL A 268 36.764 -37.310 17.126 1.00157.94 C ANISOU 1890 CA VAL A 268 25356 13692 20963 -4194 -2440 3721 C ATOM 1891 C VAL A 268 36.074 -36.671 18.323 1.00159.65 C ANISOU 1891 C VAL A 268 25538 14182 20940 -4456 -2282 3891 C ATOM 1892 O VAL A 268 35.191 -35.828 18.158 1.00159.59 O ANISOU 1892 O VAL A 268 25229 14540 20869 -4618 -2066 3806 O ATOM 1893 CB VAL A 268 38.253 -36.919 17.165 1.00151.83 C ANISOU 1893 CB VAL A 268 24543 12885 20261 -3732 -2613 3689 C ATOM 1894 CG1 VAL A 268 38.978 -37.433 15.931 1.00149.20 C ANISOU 1894 CG1 VAL A 268 24196 12333 20162 -3436 -2748 3497 C ATOM 1895 CG2 VAL A 268 38.389 -35.416 17.275 1.00143.81 C ANISOU 1895 CG2 VAL A 268 23150 12315 19178 -3604 -2481 3607 C ATOM 1896 N LYS A 269 36.483 -37.060 19.527 1.00156.09 N ANISOU 1896 N LYS A 269 25397 13562 20349 -4486 -2389 4128 N ATOM 1897 CA LYS A 269 35.830 -36.554 20.728 1.00151.03 C ANISOU 1897 CA LYS A 269 24767 13158 19458 -4750 -2240 4301 C ATOM 1898 C LYS A 269 36.793 -36.261 21.879 1.00145.89 C ANISOU 1898 C LYS A 269 24273 12489 18669 -4559 -2371 4471 C ATOM 1899 O LYS A 269 36.492 -35.444 22.748 1.00141.71 O ANISOU 1899 O LYS A 269 23652 12249 17942 -4662 -2242 4549 O ATOM 1900 CB LYS A 269 34.727 -37.518 21.177 1.00155.56 C ANISOU 1900 CB LYS A 269 25608 13573 19925 -5210 -2163 4466 C ATOM 1901 CG LYS A 269 33.686 -37.802 20.095 1.00151.75 C ANISOU 1901 CG LYS A 269 24961 13136 19561 -5444 -2032 4302 C ATOM 1902 CD LYS A 269 32.697 -38.880 20.510 1.00146.87 C ANISOU 1902 CD LYS A 269 24637 12315 18852 -5909 -1985 4469 C ATOM 1903 CE LYS A 269 31.710 -39.157 19.389 1.00142.51 C ANISOU 1903 CE LYS A 269 23906 11817 18425 -6137 -1874 4292 C ATOM 1904 NZ LYS A 269 30.646 -40.103 19.813 1.00149.80 N ANISOU 1904 NZ LYS A 269 25073 12599 19246 -6640 -1801 4450 N ATOM 1905 N GLY A 270 37.953 -36.913 21.879 1.00146.83 N ANISOU 1905 N GLY A 270 24622 12280 18888 -4273 -2628 4521 N ATOM 1906 CA GLY A 270 38.892 -36.771 22.980 1.00151.48 C ANISOU 1906 CA GLY A 270 25386 12823 19346 -4096 -2786 4696 C ATOM 1907 C GLY A 270 40.095 -35.872 22.735 1.00151.24 C ANISOU 1907 C GLY A 270 25105 12958 19400 -3671 -2890 4566 C ATOM 1908 O GLY A 270 40.797 -35.492 23.674 1.00148.43 O ANISOU 1908 O GLY A 270 24819 12664 18913 -3544 -2991 4689 O ATOM 1909 N GLN A 271 40.333 -35.526 21.474 1.00152.21 N ANISOU 1909 N GLN A 271 24937 13162 19735 -3463 -2865 4318 N ATOM 1910 CA GLN A 271 41.531 -34.783 21.092 1.00152.74 C ANISOU 1910 CA GLN A 271 24768 13358 19910 -3060 -2971 4183 C ATOM 1911 C GLN A 271 41.722 -33.490 21.889 1.00150.80 C ANISOU 1911 C GLN A 271 24331 13474 19492 -3032 -2892 4209 C ATOM 1912 O GLN A 271 40.756 -32.832 22.267 1.00152.30 O ANISOU 1912 O GLN A 271 24413 13924 19530 -3291 -2677 4222 O ATOM 1913 CB GLN A 271 41.508 -34.486 19.591 1.00153.41 C ANISOU 1913 CB GLN A 271 24542 13534 20214 -2913 -2895 3908 C ATOM 1914 CG GLN A 271 41.378 -35.725 18.713 1.00156.04 C ANISOU 1914 CG GLN A 271 25056 13511 20722 -2917 -2978 3849 C ATOM 1915 CD GLN A 271 42.658 -36.540 18.642 1.00159.64 C ANISOU 1915 CD GLN A 271 25720 13631 21304 -2573 -3251 3880 C ATOM 1916 OE1 GLN A 271 43.760 -35.995 18.695 1.00157.90 O ANISOU 1916 OE1 GLN A 271 25355 13517 21124 -2249 -3360 3839 O ATOM 1917 NE2 GLN A 271 42.515 -37.854 18.515 1.00165.42 N ANISOU 1917 NE2 GLN A 271 26793 13959 22102 -2642 -3364 3950 N ATOM 1918 N LYS A 272 42.978 -33.133 22.137 1.00147.18 N ANISOU 1918 N LYS A 272 23829 13034 19057 -2714 -3068 4211 N ATOM 1919 CA LYS A 272 43.304 -31.930 22.895 1.00143.21 C ANISOU 1919 CA LYS A 272 23169 12848 18397 -2669 -3027 4229 C ATOM 1920 C LYS A 272 44.351 -31.103 22.153 1.00140.87 C ANISOU 1920 C LYS A 272 22554 12717 18253 -2324 -3089 4036 C ATOM 1921 O LYS A 272 45.209 -31.659 21.469 1.00144.52 O ANISOU 1921 O LYS A 272 23013 12993 18906 -2058 -3255 3966 O ATOM 1922 CB LYS A 272 43.808 -32.306 24.287 1.00145.33 C ANISOU 1922 CB LYS A 272 23753 12991 18474 -2682 -3201 4481 C ATOM 1923 CG LYS A 272 42.904 -33.290 25.017 1.00149.00 C ANISOU 1923 CG LYS A 272 24581 13239 18792 -3012 -3169 4696 C ATOM 1924 CD LYS A 272 43.529 -33.751 26.317 1.00149.90 C ANISOU 1924 CD LYS A 272 25034 13194 18728 -2986 -3375 4951 C ATOM 1925 CE LYS A 272 42.602 -34.684 27.068 1.00155.54 C ANISOU 1925 CE LYS A 272 26120 13704 19276 -3342 -3328 5177 C ATOM 1926 NZ LYS A 272 43.246 -35.219 28.302 1.00159.07 N ANISOU 1926 NZ LYS A 272 26930 13964 19545 -3303 -3550 5440 N ATOM 1927 N ARG A 273 44.278 -29.781 22.299 1.00133.63 N ANISOU 1927 N ARG A 273 21379 12148 17247 -2332 -2953 3949 N ATOM 1928 CA ARG A 273 45.105 -28.853 21.519 1.00131.34 C ANISOU 1928 CA ARG A 273 20759 12052 17091 -2061 -2965 3753 C ATOM 1929 C ARG A 273 46.606 -29.111 21.620 1.00118.26 C ANISOU 1929 C ARG A 273 19128 10280 15524 -1735 -3234 3777 C ATOM 1930 O ARG A 273 47.192 -29.033 22.699 1.00112.78 O ANISOU 1930 O ARG A 273 18572 9589 14688 -1700 -3375 3926 O ATOM 1931 CB ARG A 273 44.813 -27.400 21.908 1.00143.31 C ANISOU 1931 CB ARG A 273 22063 13931 18458 -2143 -2796 3695 C ATOM 1932 CG ARG A 273 43.390 -26.951 21.639 1.00156.05 C ANISOU 1932 CG ARG A 273 23567 15717 20006 -2408 -2516 3627 C ATOM 1933 CD ARG A 273 43.177 -25.503 22.064 1.00166.29 C ANISOU 1933 CD ARG A 273 24677 17352 21154 -2451 -2363 3567 C ATOM 1934 NE ARG A 273 41.760 -25.188 22.233 1.00174.93 N ANISOU 1934 NE ARG A 273 25740 18603 22122 -2728 -2111 3566 N ATOM 1935 CZ ARG A 273 41.295 -24.013 22.647 1.00178.09 C ANISOU 1935 CZ ARG A 273 26009 19285 22372 -2803 -1941 3519 C ATOM 1936 NH1 ARG A 273 42.135 -23.028 22.937 1.00176.98 N ANISOU 1936 NH1 ARG A 273 25772 19286 22185 -2641 -1997 3470 N ATOM 1937 NH2 ARG A 273 39.988 -23.822 22.772 1.00179.73 N ANISOU 1937 NH2 ARG A 273 26180 19636 22474 -3041 -1714 3517 N ATOM 1938 N LYS A 274 47.224 -29.388 20.478 1.00112.11 N ANISOU 1938 N LYS A 274 18200 9421 14974 -1492 -3301 3622 N ATOM 1939 CA LYS A 274 48.653 -29.662 20.426 1.00109.48 C ANISOU 1939 CA LYS A 274 17848 8997 14753 -1156 -3545 3620 C ATOM 1940 C LYS A 274 49.376 -28.737 19.443 1.00102.88 C ANISOU 1940 C LYS A 274 16632 8396 14062 -932 -3506 3399 C ATOM 1941 O LYS A 274 50.493 -29.034 19.012 1.00 99.73 O ANISOU 1941 O LYS A 274 16152 7931 13809 -636 -3673 3342 O ATOM 1942 CB LYS A 274 48.899 -31.133 20.056 1.00112.85 C ANISOU 1942 CB LYS A 274 18515 9042 15323 -1031 -3708 3665 C ATOM 1943 CG LYS A 274 48.084 -32.123 20.885 1.00117.95 C ANISOU 1943 CG LYS A 274 19555 9422 15838 -1286 -3729 3879 C ATOM 1944 CD LYS A 274 48.659 -33.524 20.844 1.00125.08 C ANISOU 1944 CD LYS A 274 20749 9924 16852 -1107 -3962 3969 C ATOM 1945 CE LYS A 274 48.016 -34.393 21.923 1.00137.27 C ANISOU 1945 CE LYS A 274 22715 11219 18223 -1362 -4013 4226 C ATOM 1946 NZ LYS A 274 48.798 -35.627 22.252 1.00139.90 N ANISOU 1946 NZ LYS A 274 23375 11169 18612 -1152 -4292 4370 N ATOM 1947 N VAL A 275 48.742 -27.616 19.093 1.00 96.82 N ANISOU 1947 N VAL A 275 15634 7905 13249 -1069 -3283 3279 N ATOM 1948 CA VAL A 275 49.308 -26.706 18.097 1.00 90.27 C ANISOU 1948 CA VAL A 275 14457 7296 12546 -892 -3221 3073 C ATOM 1949 C VAL A 275 50.686 -26.231 18.509 1.00 88.56 C ANISOU 1949 C VAL A 275 14129 7189 12332 -666 -3400 3086 C ATOM 1950 O VAL A 275 51.619 -26.234 17.703 1.00 86.63 O ANISOU 1950 O VAL A 275 13693 6968 12252 -414 -3478 2963 O ATOM 1951 CB VAL A 275 48.426 -25.461 17.848 1.00 85.49 C ANISOU 1951 CB VAL A 275 13650 6975 11857 -1077 -2967 2970 C ATOM 1952 CG1 VAL A 275 49.181 -24.442 16.982 1.00 65.35 C ANISOU 1952 CG1 VAL A 275 10768 4649 9411 -891 -2929 2786 C ATOM 1953 CG2 VAL A 275 47.101 -25.852 17.201 1.00 85.18 C ANISOU 1953 CG2 VAL A 275 13643 6874 11846 -1274 -2783 2918 C ATOM 1954 N LYS A 276 50.810 -25.818 19.764 1.00 92.79 N ANISOU 1954 N LYS A 276 14775 7805 12674 -763 -3463 3231 N ATOM 1955 CA LYS A 276 52.082 -25.310 20.261 1.00104.43 C ANISOU 1955 CA LYS A 276 16144 9409 14128 -582 -3642 3251 C ATOM 1956 C LYS A 276 53.075 -26.427 20.586 1.00110.46 C ANISOU 1956 C LYS A 276 17062 9945 14964 -351 -3923 3362 C ATOM 1957 O LYS A 276 54.283 -26.228 20.488 1.00113.05 O ANISOU 1957 O LYS A 276 17222 10361 15371 -113 -4082 3319 O ATOM 1958 CB LYS A 276 51.881 -24.383 21.466 1.00106.19 C ANISOU 1958 CB LYS A 276 16425 9817 14106 -767 -3610 3348 C ATOM 1959 CG LYS A 276 51.551 -22.943 21.093 1.00 98.29 C ANISOU 1959 CG LYS A 276 15173 9107 13064 -864 -3400 3197 C ATOM 1960 CD LYS A 276 51.525 -22.026 22.307 1.00 99.76 C ANISOU 1960 CD LYS A 276 15427 9466 13011 -1012 -3396 3279 C ATOM 1961 CE LYS A 276 51.319 -20.569 21.881 1.00109.50 C ANISOU 1961 CE LYS A 276 16418 10967 14220 -1075 -3205 3117 C ATOM 1962 NZ LYS A 276 51.799 -19.552 22.875 1.00111.75 N ANISOU 1962 NZ LYS A 276 16706 11435 14320 -1133 -3260 3149 N ATOM 1963 N ASP A 277 52.566 -27.597 20.959 1.00113.38 N ANISOU 1963 N ASP A 277 17747 10024 15307 -419 -3986 3505 N ATOM 1964 CA ASP A 277 53.424 -28.747 21.247 1.00118.88 C ANISOU 1964 CA ASP A 277 18631 10463 16075 -189 -4256 3619 C ATOM 1965 C ASP A 277 54.029 -29.371 19.987 1.00111.36 C ANISOU 1965 C ASP A 277 17541 9388 15383 96 -4310 3463 C ATOM 1966 O ASP A 277 55.218 -29.692 19.947 1.00106.12 O ANISOU 1966 O ASP A 277 16809 8694 14820 394 -4520 3459 O ATOM 1967 CB ASP A 277 52.654 -29.818 22.027 1.00130.77 C ANISOU 1967 CB ASP A 277 20550 11671 17465 -367 -4302 3828 C ATOM 1968 CG ASP A 277 52.643 -29.560 23.519 1.00141.44 C ANISOU 1968 CG ASP A 277 22100 13081 18560 -516 -4388 4037 C ATOM 1969 OD1 ASP A 277 52.873 -28.399 23.925 1.00144.36 O ANISOU 1969 OD1 ASP A 277 22287 13746 18817 -565 -4341 3999 O ATOM 1970 OD2 ASP A 277 52.408 -30.521 24.284 1.00146.14 O ANISOU 1970 OD2 ASP A 277 23047 13420 19058 -588 -4505 4239 O ATOM 1971 N ARG A 278 53.205 -29.544 18.960 1.00107.83 N ANISOU 1971 N ARG A 278 17048 8882 15040 6 -4121 3329 N ATOM 1972 CA ARG A 278 53.640 -30.235 17.757 1.00108.95 C ANISOU 1972 CA ARG A 278 17105 8880 15411 253 -4156 3178 C ATOM 1973 C ARG A 278 54.552 -29.356 16.910 1.00103.03 C ANISOU 1973 C ARG A 278 15957 8408 14783 469 -4126 2982 C ATOM 1974 O ARG A 278 55.377 -29.860 16.151 1.00104.83 O ANISOU 1974 O ARG A 278 16082 8563 15186 759 -4222 2876 O ATOM 1975 CB ARG A 278 52.432 -30.712 16.944 1.00119.21 C ANISOU 1975 CB ARG A 278 18497 10032 16766 66 -3969 3097 C ATOM 1976 CG ARG A 278 52.717 -31.907 16.036 1.00129.32 C ANISOU 1976 CG ARG A 278 19877 11017 18242 282 -4059 3011 C ATOM 1977 CD ARG A 278 51.453 -32.385 15.334 1.00135.10 C ANISOU 1977 CD ARG A 278 20724 11602 19005 52 -3885 2943 C ATOM 1978 NE ARG A 278 51.747 -33.192 14.153 1.00141.32 N ANISOU 1978 NE ARG A 278 21506 12197 19992 267 -3919 2781 N ATOM 1979 CZ ARG A 278 52.000 -32.694 12.944 1.00144.47 C ANISOU 1979 CZ ARG A 278 21603 12773 20516 403 -3809 2553 C ATOM 1980 NH1 ARG A 278 52.003 -31.381 12.744 1.00137.25 N ANISOU 1980 NH1 ARG A 278 20371 12223 19555 346 -3664 2469 N ATOM 1981 NH2 ARG A 278 52.256 -33.511 11.932 1.00150.66 N ANISOU 1981 NH2 ARG A 278 22417 13363 21465 599 -3846 2410 N ATOM 1982 N LEU A 279 54.407 -28.041 17.053 1.00 97.48 N ANISOU 1982 N LEU A 279 15036 8020 13981 326 -3989 2934 N ATOM 1983 CA LEU A 279 55.216 -27.086 16.301 1.00 90.64 C ANISOU 1983 CA LEU A 279 13797 7434 13207 482 -3943 2760 C ATOM 1984 C LEU A 279 56.345 -26.516 17.155 1.00 84.24 C ANISOU 1984 C LEU A 279 12879 6801 12326 594 -4119 2834 C ATOM 1985 O LEU A 279 57.282 -25.891 16.642 1.00 80.18 O ANISOU 1985 O LEU A 279 12065 6499 11899 760 -4139 2713 O ATOM 1986 CB LEU A 279 54.340 -25.952 15.767 1.00 87.81 C ANISOU 1986 CB LEU A 279 13262 7303 12797 259 -3674 2641 C ATOM 1987 CG LEU A 279 53.438 -26.337 14.601 1.00 91.74 C ANISOU 1987 CG LEU A 279 13754 7704 13400 200 -3499 2509 C ATOM 1988 CD1 LEU A 279 52.697 -25.115 14.071 1.00 93.52 C ANISOU 1988 CD1 LEU A 279 13775 8185 13573 19 -3253 2392 C ATOM 1989 CD2 LEU A 279 54.266 -26.982 13.504 1.00 90.56 C ANISOU 1989 CD2 LEU A 279 13482 7468 13458 498 -3573 2368 C ATOM 1990 N LYS A 280 56.218 -26.716 18.463 1.00 84.75 N ANISOU 1990 N LYS A 280 13190 6787 12222 481 -4240 3035 N ATOM 1991 CA LYS A 280 57.244 -26.368 19.446 1.00103.46 C ANISOU 1991 CA LYS A 280 15524 9285 14501 576 -4449 3138 C ATOM 1992 C LYS A 280 58.654 -26.690 18.940 1.00112.93 C ANISOU 1992 C LYS A 280 16509 10521 15879 935 -4638 3061 C ATOM 1993 O LYS A 280 59.594 -25.916 19.148 1.00106.46 O ANISOU 1993 O LYS A 280 15452 9953 15046 1018 -4723 3028 O ATOM 1994 CB LYS A 280 56.973 -27.151 20.738 1.00109.59 C ANISOU 1994 CB LYS A 280 16678 9843 15117 491 -4609 3379 C ATOM 1995 CG LYS A 280 57.729 -26.693 21.973 1.00107.97 C ANISOU 1995 CG LYS A 280 16496 9782 14748 499 -4802 3514 C ATOM 1996 CD LYS A 280 57.389 -27.604 23.153 1.00107.18 C ANISOU 1996 CD LYS A 280 16802 9432 14488 419 -4953 3760 C ATOM 1997 CE LYS A 280 58.214 -27.257 24.378 1.00108.22 C ANISOU 1997 CE LYS A 280 16972 9694 14453 454 -5179 3900 C ATOM 1998 NZ LYS A 280 57.939 -28.172 25.517 1.00109.32 N ANISOU 1998 NZ LYS A 280 17520 9588 14427 389 -5339 4150 N ATOM 1999 N ALA A 281 58.787 -27.845 18.286 1.00119.45 N ANISOU 1999 N ALA A 281 17422 11097 16868 1144 -4704 3030 N ATOM 2000 CA ALA A 281 60.059 -28.291 17.723 1.00112.02 C ANISOU 2000 CA ALA A 281 16286 10169 16108 1515 -4869 2945 C ATOM 2001 C ALA A 281 60.614 -27.281 16.719 1.00104.25 C ANISOU 2001 C ALA A 281 14878 9504 15228 1583 -4735 2731 C ATOM 2002 O ALA A 281 61.633 -26.628 16.963 1.00 99.34 O ANISOU 2002 O ALA A 281 14010 9132 14601 1686 -4838 2713 O ATOM 2003 CB ALA A 281 59.892 -29.665 17.061 1.00103.46 C ANISOU 2003 CB ALA A 281 15394 8739 15177 1699 -4911 2918 C ATOM 2004 N TYR A 282 59.912 -27.148 15.599 1.00100.24 N ANISOU 2004 N TYR A 282 14293 8990 14803 1508 -4504 2574 N ATOM 2005 CA TYR A 282 60.361 -26.340 14.472 1.00 91.14 C ANISOU 2005 CA TYR A 282 12770 8099 13760 1583 -4360 2366 C ATOM 2006 C TYR A 282 60.527 -24.853 14.770 1.00 92.98 C ANISOU 2006 C TYR A 282 12777 8669 13880 1400 -4272 2344 C ATOM 2007 O TYR A 282 61.512 -24.240 14.353 1.00 94.17 O ANISOU 2007 O TYR A 282 12615 9066 14100 1529 -4291 2242 O ATOM 2008 CB TYR A 282 59.398 -26.525 13.301 1.00 86.27 C ANISOU 2008 CB TYR A 282 12173 7386 13221 1502 -4132 2225 C ATOM 2009 CG TYR A 282 59.188 -27.969 12.934 1.00 93.53 C ANISOU 2009 CG TYR A 282 13328 7959 14251 1660 -4207 2227 C ATOM 2010 CD1 TYR A 282 58.173 -28.713 13.521 1.00 98.07 C ANISOU 2010 CD1 TYR A 282 14269 8249 14745 1482 -4218 2365 C ATOM 2011 CD2 TYR A 282 60.018 -28.598 12.012 1.00100.52 C ANISOU 2011 CD2 TYR A 282 14077 8799 15317 1984 -4266 2090 C ATOM 2012 CE1 TYR A 282 57.984 -30.046 13.195 1.00104.30 C ANISOU 2012 CE1 TYR A 282 15301 8697 15633 1610 -4293 2369 C ATOM 2013 CE2 TYR A 282 59.838 -29.929 11.676 1.00105.89 C ANISOU 2013 CE2 TYR A 282 14998 9138 16096 2138 -4339 2082 C ATOM 2014 CZ TYR A 282 58.818 -30.649 12.270 1.00109.11 C ANISOU 2014 CZ TYR A 282 15787 9246 16423 1943 -4357 2224 C ATOM 2015 OH TYR A 282 58.631 -31.975 11.941 1.00115.12 O ANISOU 2015 OH TYR A 282 16813 9647 17282 2077 -4434 2217 O ATOM 2016 N VAL A 283 59.566 -24.274 15.486 1.00 97.75 N ANISOU 2016 N VAL A 283 13544 9286 14309 1099 -4172 2435 N ATOM 2017 CA VAL A 283 59.474 -22.817 15.588 1.00102.70 C ANISOU 2017 CA VAL A 283 13990 10201 14831 900 -4037 2384 C ATOM 2018 C VAL A 283 60.377 -22.217 16.665 1.00105.98 C ANISOU 2018 C VAL A 283 14341 10791 15135 895 -4216 2479 C ATOM 2019 O VAL A 283 61.171 -21.312 16.387 1.00108.27 O ANISOU 2019 O VAL A 283 14347 11339 15450 924 -4209 2386 O ATOM 2020 CB VAL A 283 58.011 -22.356 15.803 1.00100.71 C ANISOU 2020 CB VAL A 283 13916 9911 14439 589 -3827 2414 C ATOM 2021 CG1 VAL A 283 57.906 -20.834 15.742 1.00 92.71 C ANISOU 2021 CG1 VAL A 283 12715 9177 13335 414 -3672 2336 C ATOM 2022 CG2 VAL A 283 57.104 -22.993 14.766 1.00 96.73 C ANISOU 2022 CG2 VAL A 283 13474 9240 14039 581 -3669 2325 C ATOM 2023 N ARG A 284 60.234 -22.709 17.892 1.00101.02 N ANISOU 2023 N ARG A 284 13984 10026 14374 841 -4375 2664 N ATOM 2024 CA ARG A 284 61.082 -22.277 19.004 1.00104.65 C ANISOU 2024 CA ARG A 284 14420 10631 14713 842 -4578 2768 C ATOM 2025 C ARG A 284 60.739 -20.884 19.550 1.00 98.50 C ANISOU 2025 C ARG A 284 13601 10071 13752 565 -4461 2760 C ATOM 2026 O ARG A 284 60.518 -20.732 20.752 1.00 94.93 O ANISOU 2026 O ARG A 284 13354 9607 13107 421 -4545 2900 O ATOM 2027 CB ARG A 284 62.563 -22.368 18.622 1.00109.74 C ANISOU 2027 CB ARG A 284 14766 11424 15505 1128 -4756 2699 C ATOM 2028 CG ARG A 284 63.011 -23.779 18.272 1.00115.77 C ANISOU 2028 CG ARG A 284 15595 11963 16430 1438 -4911 2722 C ATOM 2029 CD ARG A 284 64.448 -23.801 17.787 1.00123.47 C ANISOU 2029 CD ARG A 284 16231 13123 17560 1733 -5055 2628 C ATOM 2030 NE ARG A 284 64.952 -25.165 17.644 1.00134.50 N ANISOU 2030 NE ARG A 284 17714 14297 19091 2060 -5239 2666 N ATOM 2031 CZ ARG A 284 66.241 -25.475 17.536 1.00140.22 C ANISOU 2031 CZ ARG A 284 18209 15137 19932 2367 -5435 2636 C ATOM 2032 NH1 ARG A 284 67.159 -24.515 17.556 1.00138.59 N ANISOU 2032 NH1 ARG A 284 17659 15277 19721 2364 -5471 2571 N ATOM 2033 NH2 ARG A 284 66.614 -26.744 17.412 1.00141.84 N ANISOU 2033 NH2 ARG A 284 18527 15111 20257 2678 -5596 2671 N ATOM 2034 N ASP A 285 60.691 -19.877 18.678 1.00 94.78 N ANISOU 2034 N ASP A 285 12886 9791 13335 494 -4268 2596 N ATOM 2035 CA ASP A 285 60.314 -18.528 19.105 1.00 87.24 C ANISOU 2035 CA ASP A 285 11911 9020 12216 240 -4140 2572 C ATOM 2036 C ASP A 285 58.898 -18.471 19.672 1.00 85.07 C ANISOU 2036 C ASP A 285 11926 8619 11776 4 -3989 2650 C ATOM 2037 O ASP A 285 57.936 -18.838 18.999 1.00 81.97 O ANISOU 2037 O ASP A 285 11601 8101 11442 -33 -3815 2609 O ATOM 2038 CB ASP A 285 60.443 -17.529 17.960 1.00 89.17 C ANISOU 2038 CB ASP A 285 11868 9457 12557 214 -3950 2387 C ATOM 2039 CG ASP A 285 60.090 -16.109 18.385 1.00 95.92 C ANISOU 2039 CG ASP A 285 12719 10480 13246 -35 -3826 2358 C ATOM 2040 OD1 ASP A 285 58.889 -15.762 18.421 1.00 83.88 O ANISOU 2040 OD1 ASP A 285 11349 8895 11626 -209 -3633 2355 O ATOM 2041 OD2 ASP A 285 61.023 -15.334 18.684 1.00108.39 O ANISOU 2041 OD2 ASP A 285 14140 12254 14790 -55 -3923 2333 O ATOM 2042 N PRO A 286 58.768 -17.998 20.917 1.00 89.67 N ANISOU 2042 N PRO A 286 12675 9252 12145 -159 -4053 2759 N ATOM 2043 CA PRO A 286 57.474 -17.901 21.599 1.00 90.73 C ANISOU 2043 CA PRO A 286 13081 9297 12095 -387 -3911 2840 C ATOM 2044 C PRO A 286 56.438 -17.132 20.775 1.00 90.04 C ANISOU 2044 C PRO A 286 12920 9269 12024 -524 -3612 2708 C ATOM 2045 O PRO A 286 55.319 -17.625 20.609 1.00 96.15 O ANISOU 2045 O PRO A 286 13840 9906 12786 -607 -3471 2733 O ATOM 2046 CB PRO A 286 57.806 -17.118 22.874 1.00 84.55 C ANISOU 2046 CB PRO A 286 12387 8649 11088 -522 -4016 2917 C ATOM 2047 CG PRO A 286 59.249 -17.325 23.086 1.00 90.02 C ANISOU 2047 CG PRO A 286 12936 9420 11846 -340 -4287 2942 C ATOM 2048 CD PRO A 286 59.865 -17.452 21.731 1.00 91.00 C ANISOU 2048 CD PRO A 286 12762 9590 12224 -146 -4257 2798 C ATOM 2049 N TYR A 287 56.803 -15.950 20.276 1.00 81.69 N ANISOU 2049 N TYR A 287 11641 8411 10988 -553 -3523 2574 N ATOM 2050 CA TYR A 287 55.850 -15.071 19.583 1.00 90.57 C ANISOU 2050 CA TYR A 287 12706 9604 12102 -681 -3251 2455 C ATOM 2051 C TYR A 287 55.291 -15.688 18.307 1.00 86.61 C ANISOU 2051 C TYR A 287 12124 9005 11781 -594 -3115 2373 C ATOM 2052 O TYR A 287 54.084 -15.639 18.060 1.00 79.10 O ANISOU 2052 O TYR A 287 11258 8004 10792 -708 -2925 2354 O ATOM 2053 CB TYR A 287 56.469 -13.703 19.278 1.00 91.59 C ANISOU 2053 CB TYR A 287 12629 9948 12223 -720 -3204 2336 C ATOM 2054 CG TYR A 287 56.828 -12.924 20.516 1.00 98.49 C ANISOU 2054 CG TYR A 287 13603 10925 12896 -851 -3303 2395 C ATOM 2055 CD1 TYR A 287 55.901 -12.745 21.536 1.00100.17 C ANISOU 2055 CD1 TYR A 287 14072 11093 12897 -1019 -3237 2477 C ATOM 2056 CD2 TYR A 287 58.092 -12.368 20.671 1.00 99.40 C ANISOU 2056 CD2 TYR A 287 13554 11191 13023 -815 -3461 2363 C ATOM 2057 CE1 TYR A 287 56.222 -12.039 22.675 1.00100.03 C ANISOU 2057 CE1 TYR A 287 14162 11166 12678 -1138 -3328 2522 C ATOM 2058 CE2 TYR A 287 58.422 -11.656 21.807 1.00 98.69 C ANISOU 2058 CE2 TYR A 287 13565 11193 12739 -947 -3562 2409 C ATOM 2059 CZ TYR A 287 57.483 -11.494 22.806 1.00 98.61 C ANISOU 2059 CZ TYR A 287 13828 11124 12514 -1105 -3496 2486 C ATOM 2060 OH TYR A 287 57.803 -10.786 23.940 1.00 97.91 O ANISOU 2060 OH TYR A 287 13857 11127 12219 -1236 -3595 2522 O ATOM 2061 N ALA A 288 56.180 -16.260 17.503 1.00 86.36 N ANISOU 2061 N ALA A 288 11919 8956 11937 -389 -3216 2317 N ATOM 2062 CA ALA A 288 55.777 -16.996 16.318 1.00 86.17 C ANISOU 2062 CA ALA A 288 11836 8821 12082 -284 -3121 2238 C ATOM 2063 C ALA A 288 54.751 -18.077 16.665 1.00 88.23 C ANISOU 2063 C ALA A 288 12359 8856 12310 -345 -3104 2341 C ATOM 2064 O ALA A 288 53.722 -18.215 15.998 1.00 87.77 O ANISOU 2064 O ALA A 288 12324 8740 12283 -417 -2929 2286 O ATOM 2065 CB ALA A 288 56.983 -17.609 15.651 1.00 81.67 C ANISOU 2065 CB ALA A 288 11083 8252 11698 -34 -3268 2185 C ATOM 2066 N LEU A 289 55.031 -18.845 17.708 1.00 90.35 N ANISOU 2066 N LEU A 289 12824 8998 12507 -326 -3292 2496 N ATOM 2067 CA LEU A 289 54.119 -19.907 18.109 1.00 91.54 C ANISOU 2067 CA LEU A 289 13244 8922 12615 -403 -3289 2612 C ATOM 2068 C LEU A 289 52.784 -19.335 18.578 1.00 88.00 C ANISOU 2068 C LEU A 289 12926 8515 11994 -665 -3088 2643 C ATOM 2069 O LEU A 289 51.728 -19.907 18.306 1.00 85.67 O ANISOU 2069 O LEU A 289 12744 8099 11709 -761 -2968 2655 O ATOM 2070 CB LEU A 289 54.742 -20.795 19.190 1.00 88.47 C ANISOU 2070 CB LEU A 289 13057 8389 12167 -329 -3543 2787 C ATOM 2071 CG LEU A 289 55.809 -21.789 18.723 1.00 89.81 C ANISOU 2071 CG LEU A 289 13165 8436 12522 -45 -3745 2780 C ATOM 2072 CD1 LEU A 289 56.609 -22.301 19.911 1.00 85.84 C ANISOU 2072 CD1 LEU A 289 12818 7867 11932 37 -4015 2950 C ATOM 2073 CD2 LEU A 289 55.191 -22.951 17.952 1.00 88.63 C ANISOU 2073 CD2 LEU A 289 13128 8040 12506 9 -3696 2760 C ATOM 2074 N ASP A 290 52.824 -18.200 19.270 1.00 82.37 N ANISOU 2074 N ASP A 290 12194 7981 11123 -780 -3048 2646 N ATOM 2075 CA ASP A 290 51.588 -17.607 19.759 1.00 83.08 C ANISOU 2075 CA ASP A 290 12400 8127 11040 -1006 -2853 2667 C ATOM 2076 C ASP A 290 50.713 -17.121 18.607 1.00 81.40 C ANISOU 2076 C ASP A 290 12035 7982 10911 -1046 -2613 2520 C ATOM 2077 O ASP A 290 49.501 -17.344 18.607 1.00 84.57 O ANISOU 2077 O ASP A 290 12534 8340 11258 -1184 -2460 2539 O ATOM 2078 CB ASP A 290 51.857 -16.462 20.726 1.00 88.91 C ANISOU 2078 CB ASP A 290 13160 9034 11587 -1105 -2863 2685 C ATOM 2079 CG ASP A 290 50.579 -15.919 21.342 1.00 93.86 C ANISOU 2079 CG ASP A 290 13928 9715 12019 -1321 -2664 2711 C ATOM 2080 OD1 ASP A 290 49.809 -16.717 21.921 1.00 91.94 O ANISOU 2080 OD1 ASP A 290 13891 9352 11688 -1426 -2644 2831 O ATOM 2081 OD2 ASP A 290 50.344 -14.696 21.245 1.00 94.29 O ANISOU 2081 OD2 ASP A 290 13891 9931 12005 -1383 -2524 2611 O ATOM 2082 N LEU A 291 51.326 -16.464 17.625 1.00 70.45 N ANISOU 2082 N LEU A 291 10406 6712 9651 -929 -2583 2377 N ATOM 2083 CA LEU A 291 50.578 -15.993 16.465 1.00 73.11 C ANISOU 2083 CA LEU A 291 10596 7116 10068 -947 -2373 2238 C ATOM 2084 C LEU A 291 49.983 -17.142 15.646 1.00 77.68 C ANISOU 2084 C LEU A 291 11199 7534 10780 -908 -2338 2221 C ATOM 2085 O LEU A 291 48.818 -17.069 15.228 1.00 74.56 O ANISOU 2085 O LEU A 291 10810 7151 10369 -1017 -2161 2181 O ATOM 2086 CB LEU A 291 51.433 -15.084 15.577 1.00 64.64 C ANISOU 2086 CB LEU A 291 9272 6194 9093 -834 -2356 2100 C ATOM 2087 CG LEU A 291 50.754 -14.548 14.305 1.00 60.90 C ANISOU 2087 CG LEU A 291 8645 5797 8699 -835 -2151 1958 C ATOM 2088 CD1 LEU A 291 49.369 -13.987 14.595 1.00 58.24 C ANISOU 2088 CD1 LEU A 291 8399 5506 8225 -1005 -1959 1964 C ATOM 2089 CD2 LEU A 291 51.624 -13.494 13.627 1.00 61.21 C ANISOU 2089 CD2 LEU A 291 8469 5996 8793 -760 -2132 1845 C ATOM 2090 N ILE A 292 50.772 -18.194 15.415 1.00 72.74 N ANISOU 2090 N ILE A 292 10588 6764 10285 -752 -2509 2246 N ATOM 2091 CA ILE A 292 50.276 -19.337 14.653 1.00 75.03 C ANISOU 2091 CA ILE A 292 10930 6876 10704 -712 -2493 2223 C ATOM 2092 C ILE A 292 49.103 -19.971 15.374 1.00 82.12 C ANISOU 2092 C ILE A 292 12068 7646 11488 -909 -2441 2344 C ATOM 2093 O ILE A 292 48.129 -20.398 14.753 1.00 87.11 O ANISOU 2093 O ILE A 292 12718 8217 12164 -991 -2320 2302 O ATOM 2094 CB ILE A 292 51.325 -20.422 14.468 1.00 73.88 C ANISOU 2094 CB ILE A 292 10806 6567 10698 -501 -2701 2245 C ATOM 2095 CG1 ILE A 292 52.498 -19.910 13.639 1.00 69.57 C ANISOU 2095 CG1 ILE A 292 9995 6160 10280 -299 -2743 2115 C ATOM 2096 CG2 ILE A 292 50.686 -21.645 13.809 1.00 75.46 C ANISOU 2096 CG2 ILE A 292 11117 6548 11006 -491 -2684 2229 C ATOM 2097 CD1 ILE A 292 53.734 -20.810 13.717 1.00 72.55 C ANISOU 2097 CD1 ILE A 292 10371 6425 10770 -65 -2973 2148 C ATOM 2098 N ASP A 293 49.210 -20.037 16.694 1.00 82.03 N ANISOU 2098 N ASP A 293 12238 7604 11323 -993 -2534 2497 N ATOM 2099 CA ASP A 293 48.131 -20.552 17.522 1.00 92.45 C ANISOU 2099 CA ASP A 293 13793 8829 12504 -1203 -2476 2629 C ATOM 2100 C ASP A 293 46.841 -19.736 17.340 1.00 90.91 C ANISOU 2100 C ASP A 293 13530 8794 12217 -1388 -2223 2564 C ATOM 2101 O ASP A 293 45.734 -20.283 17.351 1.00 89.79 O ANISOU 2101 O ASP A 293 13488 8585 12042 -1546 -2118 2603 O ATOM 2102 CB ASP A 293 48.570 -20.549 18.989 1.00102.42 C ANISOU 2102 CB ASP A 293 15247 10077 13592 -1254 -2615 2795 C ATOM 2103 CG ASP A 293 47.602 -21.275 19.892 1.00107.33 C ANISOU 2103 CG ASP A 293 16141 10573 14068 -1463 -2583 2955 C ATOM 2104 OD1 ASP A 293 46.924 -22.214 19.418 1.00115.95 O ANISOU 2104 OD1 ASP A 293 17313 11504 15238 -1522 -2541 2967 O ATOM 2105 OD2 ASP A 293 47.525 -20.903 21.081 1.00103.83 O ANISOU 2105 OD2 ASP A 293 15834 10195 13422 -1577 -2598 3067 O ATOM 2106 N LYS A 294 46.993 -18.426 17.164 1.00 87.10 N ANISOU 2106 N LYS A 294 12874 8524 11695 -1365 -2128 2465 N ATOM 2107 CA LYS A 294 45.847 -17.536 17.005 1.00 84.33 C ANISOU 2107 CA LYS A 294 12451 8337 11255 -1502 -1896 2397 C ATOM 2108 C LYS A 294 45.293 -17.529 15.580 1.00 80.15 C ANISOU 2108 C LYS A 294 11741 7838 10875 -1460 -1768 2253 C ATOM 2109 O LYS A 294 44.149 -17.134 15.361 1.00 77.48 O ANISOU 2109 O LYS A 294 11357 7600 10482 -1577 -1585 2210 O ATOM 2110 CB LYS A 294 46.206 -16.127 17.468 1.00 85.14 C ANISOU 2110 CB LYS A 294 12482 8629 11238 -1498 -1853 2356 C ATOM 2111 CG LYS A 294 46.547 -16.094 18.940 1.00 91.24 C ANISOU 2111 CG LYS A 294 13449 9390 11827 -1574 -1959 2496 C ATOM 2112 CD LYS A 294 46.831 -14.696 19.442 1.00 91.54 C ANISOU 2112 CD LYS A 294 13443 9605 11732 -1591 -1912 2447 C ATOM 2113 CE LYS A 294 47.149 -14.738 20.928 1.00 92.57 C ANISOU 2113 CE LYS A 294 13786 9722 11664 -1675 -2028 2586 C ATOM 2114 NZ LYS A 294 47.393 -13.385 21.491 1.00 96.25 N ANISOU 2114 NZ LYS A 294 14239 10349 11981 -1710 -1986 2533 N ATOM 2115 N LEU A 295 46.109 -17.968 14.622 1.00 77.06 N ANISOU 2115 N LEU A 295 11245 7371 10664 -1287 -1867 2175 N ATOM 2116 CA LEU A 295 45.659 -18.181 13.249 1.00 69.16 C ANISOU 2116 CA LEU A 295 10102 6370 9805 -1240 -1775 2044 C ATOM 2117 C LEU A 295 44.911 -19.515 13.096 1.00 79.17 C ANISOU 2117 C LEU A 295 11509 7449 11124 -1330 -1787 2091 C ATOM 2118 O LEU A 295 43.835 -19.565 12.503 1.00 80.64 O ANISOU 2118 O LEU A 295 11645 7676 11320 -1435 -1647 2033 O ATOM 2119 CB LEU A 295 46.841 -18.146 12.282 1.00 59.91 C ANISOU 2119 CB LEU A 295 8770 5199 8795 -1020 -1867 1936 C ATOM 2120 CG LEU A 295 47.531 -16.804 12.054 1.00 62.63 C ANISOU 2120 CG LEU A 295 8935 5739 9122 -940 -1829 1855 C ATOM 2121 CD1 LEU A 295 48.794 -17.007 11.250 1.00 65.61 C ANISOU 2121 CD1 LEU A 295 9171 6103 9654 -734 -1942 1774 C ATOM 2122 CD2 LEU A 295 46.603 -15.851 11.341 1.00 60.33 C ANISOU 2122 CD2 LEU A 295 8519 5605 8800 -1005 -1624 1752 C ATOM 2123 N LEU A 296 45.475 -20.596 13.630 1.00 78.41 N ANISOU 2123 N LEU A 296 11592 7143 11057 -1294 -1961 2199 N ATOM 2124 CA LEU A 296 44.836 -21.904 13.497 1.00 83.90 C ANISOU 2124 CA LEU A 296 12451 7625 11803 -1386 -1987 2248 C ATOM 2125 C LEU A 296 43.792 -22.135 14.586 1.00 88.93 C ANISOU 2125 C LEU A 296 13276 8242 12270 -1642 -1917 2395 C ATOM 2126 O LEU A 296 43.783 -23.169 15.239 1.00 94.98 O ANISOU 2126 O LEU A 296 14275 8803 13011 -1713 -2025 2530 O ATOM 2127 CB LEU A 296 45.871 -23.032 13.476 1.00 81.97 C ANISOU 2127 CB LEU A 296 12333 7135 11676 -1217 -2205 2292 C ATOM 2128 CG LEU A 296 46.892 -22.971 12.335 1.00 77.53 C ANISOU 2128 CG LEU A 296 11582 6588 11290 -958 -2268 2140 C ATOM 2129 CD1 LEU A 296 47.841 -24.158 12.387 1.00 79.52 C ANISOU 2129 CD1 LEU A 296 11972 6591 11652 -778 -2482 2186 C ATOM 2130 CD2 LEU A 296 46.194 -22.904 10.990 1.00 74.24 C ANISOU 2130 CD2 LEU A 296 11015 6226 10965 -973 -2124 1976 C ATOM 2131 N VAL A 297 42.916 -21.152 14.766 1.00 88.64 N ANISOU 2131 N VAL A 297 13140 8425 12114 -1774 -1732 2367 N ATOM 2132 CA VAL A 297 41.810 -21.244 15.713 1.00 79.44 C ANISOU 2132 CA VAL A 297 12109 7296 10779 -2022 -1623 2484 C ATOM 2133 C VAL A 297 40.581 -21.827 15.018 1.00 81.24 C ANISOU 2133 C VAL A 297 12306 7505 11055 -2182 -1500 2438 C ATOM 2134 O VAL A 297 40.272 -21.463 13.882 1.00 81.29 O ANISOU 2134 O VAL A 297 12113 7613 11163 -2122 -1413 2287 O ATOM 2135 CB VAL A 297 41.495 -19.855 16.322 1.00 78.91 C ANISOU 2135 CB VAL A 297 11950 7484 10547 -2068 -1483 2470 C ATOM 2136 CG1 VAL A 297 40.066 -19.777 16.819 1.00 79.56 C ANISOU 2136 CG1 VAL A 297 12066 7679 10486 -2307 -1296 2518 C ATOM 2137 CG2 VAL A 297 42.469 -19.538 17.437 1.00 78.52 C ANISOU 2137 CG2 VAL A 297 12024 7423 10388 -2009 -1614 2571 C ATOM 2138 N LEU A 298 39.888 -22.737 15.700 1.00 84.28 N ANISOU 2138 N LEU A 298 12893 7766 11365 -2394 -1497 2572 N ATOM 2139 CA LEU A 298 38.770 -23.473 15.110 1.00 79.41 C ANISOU 2139 CA LEU A 298 12273 7103 10796 -2577 -1407 2545 C ATOM 2140 C LEU A 298 37.562 -22.605 14.750 1.00 78.46 C ANISOU 2140 C LEU A 298 11933 7265 10615 -2695 -1180 2452 C ATOM 2141 O LEU A 298 37.087 -22.628 13.619 1.00 76.21 O ANISOU 2141 O LEU A 298 11484 7031 10439 -2682 -1120 2319 O ATOM 2142 CB LEU A 298 38.332 -24.591 16.048 1.00 78.51 C ANISOU 2142 CB LEU A 298 12441 6796 10592 -2803 -1454 2729 C ATOM 2143 CG LEU A 298 39.260 -25.797 16.120 1.00 86.33 C ANISOU 2143 CG LEU A 298 13672 7447 11681 -2708 -1682 2812 C ATOM 2144 CD1 LEU A 298 38.908 -26.651 17.334 1.00 90.14 C ANISOU 2144 CD1 LEU A 298 14462 7766 12022 -2932 -1724 3029 C ATOM 2145 CD2 LEU A 298 39.188 -26.607 14.829 1.00 82.97 C ANISOU 2145 CD2 LEU A 298 13212 6860 11452 -2659 -1726 2687 C ATOM 2146 N ASP A 299 37.046 -21.859 15.717 1.00 81.04 N ANISOU 2146 N ASP A 299 12258 7777 10758 -2804 -1057 2520 N ATOM 2147 CA ASP A 299 35.914 -20.987 15.451 1.00 86.95 C ANISOU 2147 CA ASP A 299 12794 8804 11440 -2887 -842 2433 C ATOM 2148 C ASP A 299 36.377 -19.793 14.612 1.00 94.07 C ANISOU 2148 C ASP A 299 13468 9862 12411 -2652 -809 2273 C ATOM 2149 O ASP A 299 37.167 -18.963 15.074 1.00 93.30 O ANISOU 2149 O ASP A 299 13377 9815 12257 -2516 -843 2276 O ATOM 2150 CB ASP A 299 35.282 -20.519 16.762 1.00 94.03 C ANISOU 2150 CB ASP A 299 13765 9851 12112 -3049 -714 2545 C ATOM 2151 CG ASP A 299 34.036 -19.686 16.545 1.00103.34 C ANISOU 2151 CG ASP A 299 14724 11323 13217 -3130 -486 2460 C ATOM 2152 OD1 ASP A 299 33.489 -19.718 15.421 1.00106.65 O ANISOU 2152 OD1 ASP A 299 14957 11809 13756 -3117 -434 2340 O ATOM 2153 OD2 ASP A 299 33.602 -18.999 17.497 1.00105.71 O ANISOU 2153 OD2 ASP A 299 15038 11793 13335 -3198 -361 2508 O ATOM 2154 N PRO A 300 35.888 -19.710 13.366 1.00 94.16 N ANISOU 2154 N PRO A 300 13287 9949 12541 -2613 -748 2134 N ATOM 2155 CA PRO A 300 36.239 -18.634 12.431 1.00 81.40 C ANISOU 2155 CA PRO A 300 11460 8475 10993 -2404 -712 1983 C ATOM 2156 C PRO A 300 36.083 -17.266 13.069 1.00 81.54 C ANISOU 2156 C PRO A 300 11409 8708 10866 -2361 -590 1977 C ATOM 2157 O PRO A 300 36.777 -16.326 12.691 1.00 85.27 O ANISOU 2157 O PRO A 300 11791 9242 11365 -2178 -603 1897 O ATOM 2158 CB PRO A 300 35.196 -18.795 11.315 1.00 77.38 C ANISOU 2158 CB PRO A 300 10776 8068 10559 -2467 -615 1873 C ATOM 2159 CG PRO A 300 34.107 -19.648 11.928 1.00 85.15 C ANISOU 2159 CG PRO A 300 11848 9038 11468 -2742 -552 1972 C ATOM 2160 CD PRO A 300 34.873 -20.602 12.785 1.00 91.15 C ANISOU 2160 CD PRO A 300 12877 9538 12217 -2792 -702 2114 C ATOM 2161 N ALA A 301 35.175 -17.160 14.031 1.00 83.74 N ANISOU 2161 N ALA A 301 11737 9095 10985 -2534 -469 2059 N ATOM 2162 CA ALA A 301 34.857 -15.873 14.635 1.00 83.47 C ANISOU 2162 CA ALA A 301 11642 9271 10800 -2498 -331 2039 C ATOM 2163 C ALA A 301 35.823 -15.524 15.750 1.00 81.43 C ANISOU 2163 C ALA A 301 11561 8946 10434 -2452 -416 2125 C ATOM 2164 O ALA A 301 35.905 -14.365 16.159 1.00 81.84 O ANISOU 2164 O ALA A 301 11584 9132 10379 -2376 -342 2089 O ATOM 2165 CB ALA A 301 33.430 -15.863 15.149 1.00 84.55 C ANISOU 2165 CB ALA A 301 11733 9587 10805 -2690 -147 2073 C ATOM 2166 N GLN A 302 36.545 -16.526 16.243 1.00 81.38 N ANISOU 2166 N GLN A 302 11746 8727 10450 -2497 -579 2239 N ATOM 2167 CA GLN A 302 37.545 -16.304 17.282 1.00 84.99 C ANISOU 2167 CA GLN A 302 12372 9112 10808 -2451 -694 2328 C ATOM 2168 C GLN A 302 38.951 -16.304 16.686 1.00 84.55 C ANISOU 2168 C GLN A 302 12295 8928 10902 -2246 -879 2279 C ATOM 2169 O GLN A 302 39.934 -16.021 17.376 1.00 80.92 O ANISOU 2169 O GLN A 302 11934 8426 10386 -2176 -995 2330 O ATOM 2170 CB GLN A 302 37.438 -17.360 18.378 1.00 86.23 C ANISOU 2170 CB GLN A 302 12771 9132 10861 -2629 -760 2505 C ATOM 2171 CG GLN A 302 36.174 -17.293 19.220 1.00 93.33 C ANISOU 2171 CG GLN A 302 13713 10178 11572 -2847 -574 2574 C ATOM 2172 CD GLN A 302 36.167 -18.347 20.325 1.00102.85 C ANISOU 2172 CD GLN A 302 15184 11234 12662 -3032 -649 2765 C ATOM 2173 OE1 GLN A 302 37.066 -18.383 21.171 1.00108.16 O ANISOU 2173 OE1 GLN A 302 16036 11809 13252 -2989 -786 2860 O ATOM 2174 NE2 GLN A 302 35.159 -19.215 20.313 1.00 95.84 N ANISOU 2174 NE2 GLN A 302 14325 10327 11763 -3246 -566 2827 N ATOM 2175 N ARG A 303 39.033 -16.626 15.399 1.00 80.38 N ANISOU 2175 N ARG A 303 11628 8353 10557 -2155 -903 2178 N ATOM 2176 CA ARG A 303 40.291 -16.600 14.663 1.00 73.81 C ANISOU 2176 CA ARG A 303 10736 7433 9876 -1954 -1049 2110 C ATOM 2177 C ARG A 303 40.744 -15.164 14.425 1.00 73.55 C ANISOU 2177 C ARG A 303 10566 7562 9818 -1823 -995 2011 C ATOM 2178 O ARG A 303 39.969 -14.326 13.954 1.00 83.38 O ANISOU 2178 O ARG A 303 11677 8969 11034 -1823 -836 1922 O ATOM 2179 CB ARG A 303 40.119 -17.318 13.326 1.00 71.02 C ANISOU 2179 CB ARG A 303 10276 7004 9705 -1905 -1064 2017 C ATOM 2180 CG ARG A 303 41.397 -17.523 12.531 1.00 67.52 C ANISOU 2180 CG ARG A 303 9777 6455 9422 -1701 -1213 1949 C ATOM 2181 CD ARG A 303 41.094 -18.423 11.353 1.00 68.90 C ANISOU 2181 CD ARG A 303 9896 6531 9750 -1683 -1225 1868 C ATOM 2182 NE ARG A 303 40.268 -19.548 11.782 1.00 73.92 N ANISOU 2182 NE ARG A 303 10689 7037 10360 -1872 -1228 1962 N ATOM 2183 CZ ARG A 303 39.318 -20.124 11.052 1.00 69.51 C ANISOU 2183 CZ ARG A 303 10088 6465 9857 -1977 -1159 1908 C ATOM 2184 NH1 ARG A 303 39.039 -19.691 9.828 1.00 62.57 N ANISOU 2184 NH1 ARG A 303 9012 5701 9059 -1900 -1084 1758 N ATOM 2185 NH2 ARG A 303 38.635 -21.135 11.563 1.00 71.73 N ANISOU 2185 NH2 ARG A 303 10531 6619 10103 -2174 -1169 2008 N ATOM 2186 N ILE A 304 42.002 -14.888 14.747 1.00 64.10 N ANISOU 2186 N ILE A 304 9406 6319 8630 -1711 -1134 2028 N ATOM 2187 CA ILE A 304 42.562 -13.547 14.588 1.00 64.83 C ANISOU 2187 CA ILE A 304 9394 6543 8695 -1608 -1102 1943 C ATOM 2188 C ILE A 304 42.443 -13.041 13.138 1.00 63.43 C ANISOU 2188 C ILE A 304 9009 6445 8646 -1499 -1019 1796 C ATOM 2189 O ILE A 304 42.475 -13.826 12.186 1.00 62.12 O ANISOU 2189 O ILE A 304 8774 6202 8626 -1448 -1057 1752 O ATOM 2190 CB ILE A 304 44.037 -13.511 15.062 1.00 65.91 C ANISOU 2190 CB ILE A 304 9583 6613 8847 -1515 -1292 1985 C ATOM 2191 CG1 ILE A 304 44.474 -12.082 15.372 1.00 61.14 C ANISOU 2191 CG1 ILE A 304 8939 6144 8147 -1484 -1253 1933 C ATOM 2192 CG2 ILE A 304 44.958 -14.174 14.039 1.00 66.18 C ANISOU 2192 CG2 ILE A 304 9514 6549 9081 -1365 -1418 1931 C ATOM 2193 CD1 ILE A 304 45.859 -12.001 15.961 1.00 60.83 C ANISOU 2193 CD1 ILE A 304 8945 6066 8099 -1425 -1441 1979 C ATOM 2194 N ASP A 305 42.272 -11.733 12.971 1.00 63.49 N ANISOU 2194 N ASP A 305 8934 6599 8591 -1463 -906 1721 N ATOM 2195 CA ASP A 305 42.171 -11.159 11.628 1.00 62.34 C ANISOU 2195 CA ASP A 305 8608 6532 8545 -1359 -829 1593 C ATOM 2196 C ASP A 305 43.492 -10.518 11.213 1.00 61.91 C ANISOU 2196 C ASP A 305 8485 6482 8554 -1235 -916 1540 C ATOM 2197 O ASP A 305 44.406 -10.373 12.027 1.00 59.46 O ANISOU 2197 O ASP A 305 8255 6139 8199 -1235 -1026 1596 O ATOM 2198 CB ASP A 305 41.015 -10.161 11.526 1.00 65.06 C ANISOU 2198 CB ASP A 305 8897 7032 8791 -1388 -639 1539 C ATOM 2199 CG ASP A 305 41.187 -8.957 12.448 1.00 82.31 C ANISOU 2199 CG ASP A 305 11163 9290 10822 -1397 -594 1550 C ATOM 2200 OD1 ASP A 305 42.328 -8.655 12.874 1.00 85.97 O ANISOU 2200 OD1 ASP A 305 11683 9707 11274 -1366 -708 1571 O ATOM 2201 OD2 ASP A 305 40.170 -8.295 12.739 1.00 87.22 O ANISOU 2201 OD2 ASP A 305 11789 10020 11330 -1433 -444 1531 O ATOM 2202 N SER A 306 43.601 -10.143 9.947 1.00 59.02 N ANISOU 2202 N SER A 306 7968 6168 8288 -1137 -870 1435 N ATOM 2203 CA SER A 306 44.869 -9.647 9.449 1.00 62.61 C ANISOU 2203 CA SER A 306 8340 6635 8813 -1033 -946 1386 C ATOM 2204 C SER A 306 45.313 -8.404 10.219 1.00 68.23 C ANISOU 2204 C SER A 306 9109 7414 9404 -1061 -935 1398 C ATOM 2205 O SER A 306 46.499 -8.220 10.500 1.00 73.08 O ANISOU 2205 O SER A 306 9720 8014 10034 -1034 -1051 1412 O ATOM 2206 CB SER A 306 44.789 -9.381 7.948 1.00 65.02 C ANISOU 2206 CB SER A 306 8486 7000 9219 -939 -874 1274 C ATOM 2207 OG SER A 306 43.663 -8.590 7.641 1.00 77.89 O ANISOU 2207 OG SER A 306 10090 8729 10776 -962 -717 1232 O ATOM 2208 N ASP A 307 44.358 -7.565 10.595 1.00 67.05 N ANISOU 2208 N ASP A 307 9011 7337 9126 -1116 -799 1390 N ATOM 2209 CA ASP A 307 44.707 -6.322 11.266 1.00 62.11 C ANISOU 2209 CA ASP A 307 8459 6761 8379 -1141 -777 1385 C ATOM 2210 C ASP A 307 45.349 -6.582 12.619 1.00 66.71 C ANISOU 2210 C ASP A 307 9182 7291 8873 -1216 -903 1476 C ATOM 2211 O ASP A 307 46.390 -6.009 12.941 1.00 71.15 O ANISOU 2211 O ASP A 307 9761 7859 9414 -1216 -993 1473 O ATOM 2212 CB ASP A 307 43.491 -5.407 11.416 1.00 66.98 C ANISOU 2212 CB ASP A 307 9116 7459 8873 -1163 -601 1351 C ATOM 2213 CG ASP A 307 43.883 -3.973 11.729 1.00 79.69 C ANISOU 2213 CG ASP A 307 10791 9106 10382 -1158 -566 1311 C ATOM 2214 OD1 ASP A 307 44.606 -3.344 10.912 1.00 84.96 O ANISOU 2214 OD1 ASP A 307 11380 9782 11117 -1101 -582 1254 O ATOM 2215 OD2 ASP A 307 43.471 -3.478 12.799 1.00 82.90 O ANISOU 2215 OD2 ASP A 307 11335 9527 10634 -1219 -519 1336 O ATOM 2216 N ASP A 308 44.730 -7.448 13.412 1.00 65.29 N ANISOU 2216 N ASP A 308 9106 7066 8635 -1291 -914 1560 N ATOM 2217 CA ASP A 308 45.258 -7.759 14.734 1.00 72.17 C ANISOU 2217 CA ASP A 308 10131 7887 9404 -1365 -1037 1659 C ATOM 2218 C ASP A 308 46.534 -8.579 14.630 1.00 68.62 C ANISOU 2218 C ASP A 308 9644 7354 9074 -1305 -1239 1699 C ATOM 2219 O ASP A 308 47.441 -8.465 15.462 1.00 65.61 O ANISOU 2219 O ASP A 308 9335 6961 8633 -1325 -1375 1751 O ATOM 2220 CB ASP A 308 44.217 -8.500 15.572 1.00 80.26 C ANISOU 2220 CB ASP A 308 11283 8886 10326 -1470 -984 1748 C ATOM 2221 CG ASP A 308 43.003 -7.649 15.866 1.00 86.22 C ANISOU 2221 CG ASP A 308 12072 9747 10939 -1523 -786 1711 C ATOM 2222 OD1 ASP A 308 43.165 -6.421 16.031 1.00 91.34 O ANISOU 2222 OD1 ASP A 308 12740 10460 11503 -1501 -732 1650 O ATOM 2223 OD2 ASP A 308 41.888 -8.206 15.927 1.00 83.68 O ANISOU 2223 OD2 ASP A 308 11757 9447 10591 -1586 -684 1740 O ATOM 2224 N ALA A 309 46.596 -9.406 13.597 1.00 65.51 N ANISOU 2224 N ALA A 309 9134 6910 8847 -1225 -1260 1669 N ATOM 2225 CA ALA A 309 47.750 -10.251 13.391 1.00 62.00 C ANISOU 2225 CA ALA A 309 8640 6386 8529 -1137 -1441 1694 C ATOM 2226 C ALA A 309 48.935 -9.355 13.115 1.00 61.48 C ANISOU 2226 C ALA A 309 8464 6401 8495 -1077 -1501 1634 C ATOM 2227 O ALA A 309 50.023 -9.582 13.642 1.00 63.59 O ANISOU 2227 O ALA A 309 8737 6652 8773 -1050 -1668 1681 O ATOM 2228 CB ALA A 309 47.514 -11.218 12.235 1.00 60.44 C ANISOU 2228 CB ALA A 309 8345 6123 8498 -1055 -1429 1647 C ATOM 2229 N LEU A 310 48.721 -8.330 12.292 1.00 57.91 N ANISOU 2229 N LEU A 310 7910 6040 8052 -1062 -1368 1535 N ATOM 2230 CA LEU A 310 49.789 -7.386 11.975 1.00 62.53 C ANISOU 2230 CA LEU A 310 8394 6706 8659 -1034 -1405 1478 C ATOM 2231 C LEU A 310 50.282 -6.679 13.236 1.00 65.94 C ANISOU 2231 C LEU A 310 8947 7164 8942 -1129 -1482 1528 C ATOM 2232 O LEU A 310 51.450 -6.298 13.335 1.00 57.44 O ANISOU 2232 O LEU A 310 7805 6135 7886 -1125 -1594 1517 O ATOM 2233 CB LEU A 310 49.327 -6.374 10.933 1.00 57.66 C ANISOU 2233 CB LEU A 310 7690 6165 8053 -1017 -1239 1378 C ATOM 2234 CG LEU A 310 49.293 -6.955 9.524 1.00 56.77 C ANISOU 2234 CG LEU A 310 7420 6052 8097 -909 -1200 1311 C ATOM 2235 CD1 LEU A 310 48.814 -5.912 8.522 1.00 49.90 C ANISOU 2235 CD1 LEU A 310 6481 5260 7219 -894 -1041 1224 C ATOM 2236 CD2 LEU A 310 50.665 -7.472 9.153 1.00 50.94 C ANISOU 2236 CD2 LEU A 310 6552 5318 7483 -825 -1342 1300 C ATOM 2237 N ASN A 311 49.386 -6.535 14.207 1.00 63.32 N ANISOU 2237 N ASN A 311 8789 6812 8457 -1221 -1422 1579 N ATOM 2238 CA ASN A 311 49.695 -5.826 15.438 1.00 69.30 C ANISOU 2238 CA ASN A 311 9691 7595 9047 -1319 -1477 1616 C ATOM 2239 C ASN A 311 50.409 -6.711 16.465 1.00 74.30 C ANISOU 2239 C ASN A 311 10407 8178 9648 -1338 -1679 1726 C ATOM 2240 O ASN A 311 51.032 -6.214 17.404 1.00 77.48 O ANISOU 2240 O ASN A 311 10896 8610 9932 -1407 -1780 1755 O ATOM 2241 CB ASN A 311 48.409 -5.242 16.022 1.00 73.53 C ANISOU 2241 CB ASN A 311 10376 8145 9417 -1397 -1311 1614 C ATOM 2242 CG ASN A 311 48.660 -4.381 17.242 1.00 83.40 C ANISOU 2242 CG ASN A 311 11791 9421 10475 -1496 -1345 1629 C ATOM 2243 OD1 ASN A 311 49.541 -3.517 17.240 1.00 78.47 O ANISOU 2243 OD1 ASN A 311 11146 8833 9837 -1517 -1405 1582 O ATOM 2244 ND2 ASN A 311 47.879 -4.609 18.295 1.00 86.79 N ANISOU 2244 ND2 ASN A 311 12391 9838 10746 -1570 -1304 1693 N ATOM 2245 N HIS A 312 50.319 -8.022 16.263 1.00 74.43 N ANISOU 2245 N HIS A 312 10405 8110 9766 -1275 -1744 1785 N ATOM 2246 CA HIS A 312 50.918 -9.015 17.153 1.00 71.11 C ANISOU 2246 CA HIS A 312 10077 7617 9327 -1269 -1940 1902 C ATOM 2247 C HIS A 312 52.411 -8.782 17.407 1.00 71.99 C ANISOU 2247 C HIS A 312 10105 7781 9466 -1228 -2136 1905 C ATOM 2248 O HIS A 312 53.152 -8.361 16.513 1.00 65.39 O ANISOU 2248 O HIS A 312 9079 7014 8750 -1160 -2143 1819 O ATOM 2249 CB HIS A 312 50.696 -10.421 16.591 1.00 67.83 C ANISOU 2249 CB HIS A 312 9632 7083 9056 -1181 -1977 1940 C ATOM 2250 CG HIS A 312 51.067 -11.516 17.540 1.00 77.81 C ANISOU 2250 CG HIS A 312 11039 8240 10287 -1176 -2162 2077 C ATOM 2251 ND1 HIS A 312 52.371 -11.909 17.751 1.00 79.10 N ANISOU 2251 ND1 HIS A 312 11147 8392 10513 -1077 -2380 2114 N ATOM 2252 CD2 HIS A 312 50.302 -12.307 18.332 1.00 79.19 C ANISOU 2252 CD2 HIS A 312 11410 8312 10365 -1256 -2164 2191 C ATOM 2253 CE1 HIS A 312 52.395 -12.892 18.632 1.00 86.52 C ANISOU 2253 CE1 HIS A 312 12258 9218 11399 -1084 -2517 2248 C ATOM 2254 NE2 HIS A 312 51.152 -13.154 18.998 1.00 86.82 N ANISOU 2254 NE2 HIS A 312 12458 9193 11336 -1201 -2386 2300 N ATOM 2255 N ASP A 313 52.845 -9.076 18.631 1.00 78.63 N ANISOU 2255 N ASP A 313 11087 8602 10189 -1275 -2298 2009 N ATOM 2256 CA ASP A 313 54.212 -8.784 19.064 1.00 85.29 C ANISOU 2256 CA ASP A 313 11862 9519 11025 -1259 -2497 2020 C ATOM 2257 C ASP A 313 55.282 -9.440 18.188 1.00 86.28 C ANISOU 2257 C ASP A 313 11764 9655 11364 -1095 -2625 1993 C ATOM 2258 O ASP A 313 56.433 -9.005 18.168 1.00 87.40 O ANISOU 2258 O ASP A 313 11765 9902 11539 -1074 -2747 1962 O ATOM 2259 CB ASP A 313 54.409 -9.182 20.529 1.00 96.89 C ANISOU 2259 CB ASP A 313 13533 10954 12325 -1325 -2664 2151 C ATOM 2260 CG ASP A 313 53.780 -8.191 21.494 1.00102.18 C ANISOU 2260 CG ASP A 313 14394 11670 12759 -1492 -2570 2149 C ATOM 2261 OD1 ASP A 313 53.650 -6.997 21.133 1.00 97.84 O ANISOU 2261 OD1 ASP A 313 13794 11198 12180 -1549 -2440 2039 O ATOM 2262 OD2 ASP A 313 53.424 -8.611 22.618 1.00106.72 O ANISOU 2262 OD2 ASP A 313 15179 12198 13170 -1562 -2626 2258 O ATOM 2263 N PHE A 314 54.897 -10.489 17.473 1.00 84.22 N ANISOU 2263 N PHE A 314 11469 9289 11240 -984 -2593 2001 N ATOM 2264 CA PHE A 314 55.788 -11.157 16.532 1.00 78.85 C ANISOU 2264 CA PHE A 314 10583 8610 10765 -807 -2683 1958 C ATOM 2265 C PHE A 314 56.405 -10.169 15.517 1.00 73.52 C ANISOU 2265 C PHE A 314 9670 8087 10179 -789 -2603 1824 C ATOM 2266 O PHE A 314 57.534 -10.353 15.078 1.00 75.26 O ANISOU 2266 O PHE A 314 9696 8381 10518 -676 -2717 1791 O ATOM 2267 CB PHE A 314 55.011 -12.281 15.833 1.00 73.85 C ANISOU 2267 CB PHE A 314 9984 7828 10246 -720 -2611 1961 C ATOM 2268 CG PHE A 314 55.767 -12.977 14.728 1.00 73.95 C ANISOU 2268 CG PHE A 314 9798 7830 10468 -526 -2668 1893 C ATOM 2269 CD1 PHE A 314 56.790 -13.867 15.017 1.00 78.51 C ANISOU 2269 CD1 PHE A 314 10341 8365 11125 -375 -2886 1950 C ATOM 2270 CD2 PHE A 314 55.414 -12.774 13.398 1.00 73.09 C ANISOU 2270 CD2 PHE A 314 9548 7753 10471 -482 -2501 1770 C ATOM 2271 CE1 PHE A 314 57.463 -14.521 14.004 1.00 81.31 C ANISOU 2271 CE1 PHE A 314 10515 8712 11668 -179 -2927 1876 C ATOM 2272 CE2 PHE A 314 56.081 -13.423 12.380 1.00 75.64 C ANISOU 2272 CE2 PHE A 314 9698 8070 10972 -301 -2540 1698 C ATOM 2273 CZ PHE A 314 57.109 -14.299 12.683 1.00 82.51 C ANISOU 2273 CZ PHE A 314 10529 8899 11922 -146 -2749 1746 C ATOM 2274 N PHE A 315 55.670 -9.123 15.150 1.00 61.58 N ANISOU 2274 N PHE A 315 8173 6623 8602 -898 -2408 1752 N ATOM 2275 CA PHE A 315 56.182 -8.144 14.191 1.00 71.62 C ANISOU 2275 CA PHE A 315 9251 8022 9939 -901 -2321 1637 C ATOM 2276 C PHE A 315 56.807 -6.935 14.888 1.00 78.79 C ANISOU 2276 C PHE A 315 10173 9041 10723 -1038 -2371 1629 C ATOM 2277 O PHE A 315 57.312 -6.018 14.233 1.00 78.93 O ANISOU 2277 O PHE A 315 10053 9164 10774 -1076 -2312 1545 O ATOM 2278 CB PHE A 315 55.070 -7.682 13.231 1.00 68.67 C ANISOU 2278 CB PHE A 315 8879 7632 9580 -921 -2085 1558 C ATOM 2279 CG PHE A 315 54.392 -8.807 12.520 1.00 65.38 C ANISOU 2279 CG PHE A 315 8454 7112 9275 -812 -2032 1555 C ATOM 2280 CD1 PHE A 315 53.149 -9.256 12.935 1.00 65.59 C ANISOU 2280 CD1 PHE A 315 8657 7035 9230 -864 -1956 1608 C ATOM 2281 CD2 PHE A 315 55.011 -9.445 11.458 1.00 66.77 C ANISOU 2281 CD2 PHE A 315 8446 7299 9623 -664 -2061 1497 C ATOM 2282 CE1 PHE A 315 52.522 -10.314 12.288 1.00 63.64 C ANISOU 2282 CE1 PHE A 315 8409 6688 9084 -787 -1916 1603 C ATOM 2283 CE2 PHE A 315 54.401 -10.512 10.819 1.00 65.72 C ANISOU 2283 CE2 PHE A 315 8326 7058 9589 -570 -2023 1486 C ATOM 2284 CZ PHE A 315 53.148 -10.942 11.229 1.00 56.26 C ANISOU 2284 CZ PHE A 315 7310 5747 8320 -640 -1954 1539 C ATOM 2285 N TRP A 316 56.782 -6.938 16.216 1.00 79.17 N ANISOU 2285 N TRP A 316 10399 9062 10619 -1124 -2481 1715 N ATOM 2286 CA TRP A 316 57.205 -5.762 16.965 1.00 79.52 C ANISOU 2286 CA TRP A 316 10505 9194 10517 -1277 -2519 1700 C ATOM 2287 C TRP A 316 58.208 -6.069 18.083 1.00 79.84 C ANISOU 2287 C TRP A 316 10567 9278 10489 -1297 -2771 1781 C ATOM 2288 O TRP A 316 58.393 -5.284 19.014 1.00 76.36 O ANISOU 2288 O TRP A 316 10246 8883 9884 -1439 -2828 1791 O ATOM 2289 CB TRP A 316 55.974 -5.011 17.472 1.00 71.79 C ANISOU 2289 CB TRP A 316 9754 8160 9365 -1400 -2351 1691 C ATOM 2290 CG TRP A 316 55.072 -4.586 16.333 1.00 74.45 C ANISOU 2290 CG TRP A 316 10044 8477 9768 -1373 -2119 1606 C ATOM 2291 CD1 TRP A 316 53.875 -5.146 15.980 1.00 69.34 C ANISOU 2291 CD1 TRP A 316 9457 7747 9141 -1321 -1980 1616 C ATOM 2292 CD2 TRP A 316 55.314 -3.530 15.387 1.00 73.36 C ANISOU 2292 CD2 TRP A 316 9787 8408 9679 -1399 -2008 1504 C ATOM 2293 NE1 TRP A 316 53.355 -4.499 14.888 1.00 63.67 N ANISOU 2293 NE1 TRP A 316 8660 7051 8480 -1301 -1799 1525 N ATOM 2294 CE2 TRP A 316 54.217 -3.507 14.500 1.00 70.85 C ANISOU 2294 CE2 TRP A 316 9470 8045 9406 -1344 -1811 1459 C ATOM 2295 CE3 TRP A 316 56.346 -2.600 15.209 1.00 71.70 C ANISOU 2295 CE3 TRP A 316 9476 8295 9473 -1475 -2059 1451 C ATOM 2296 CZ2 TRP A 316 54.122 -2.584 13.448 1.00 68.60 C ANISOU 2296 CZ2 TRP A 316 9100 7800 9163 -1348 -1668 1369 C ATOM 2297 CZ3 TRP A 316 56.248 -1.681 14.163 1.00 66.89 C ANISOU 2297 CZ3 TRP A 316 8789 7718 8908 -1496 -1907 1363 C ATOM 2298 CH2 TRP A 316 55.146 -1.682 13.299 1.00 68.33 C ANISOU 2298 CH2 TRP A 316 8988 7846 9129 -1425 -1716 1326 C ATOM 2299 N SER A 317 58.863 -7.216 17.965 1.00 82.45 N ANISOU 2299 N SER A 317 10785 9596 10945 -1145 -2929 1835 N ATOM 2300 CA SER A 317 59.944 -7.577 18.866 1.00 86.12 C ANISOU 2300 CA SER A 317 11225 10121 11374 -1125 -3189 1911 C ATOM 2301 C SER A 317 61.165 -7.991 18.050 1.00 89.66 C ANISOU 2301 C SER A 317 11370 10677 12020 -972 -3302 1869 C ATOM 2302 O SER A 317 61.059 -8.245 16.844 1.00 82.98 O ANISOU 2302 O SER A 317 10372 9824 11334 -864 -3179 1797 O ATOM 2303 CB SER A 317 59.511 -8.695 19.816 1.00 88.36 C ANISOU 2303 CB SER A 317 11720 10269 11583 -1073 -3305 2048 C ATOM 2304 OG SER A 317 59.121 -9.854 19.105 1.00 95.48 O ANISOU 2304 OG SER A 317 12594 11048 12637 -910 -3266 2068 O ATOM 2305 N ASP A 318 62.324 -8.032 18.704 1.00 98.73 N ANISOU 2305 N ASP A 318 12423 11941 13150 -963 -3533 1909 N ATOM 2306 CA ASP A 318 63.575 -8.394 18.039 1.00 99.74 C ANISOU 2306 CA ASP A 318 12237 12205 13453 -814 -3655 1870 C ATOM 2307 C ASP A 318 63.652 -9.898 17.825 1.00 93.36 C ANISOU 2307 C ASP A 318 11406 11285 12780 -564 -3753 1931 C ATOM 2308 O ASP A 318 63.145 -10.667 18.640 1.00 91.48 O ANISOU 2308 O ASP A 318 11398 10895 12464 -531 -3839 2043 O ATOM 2309 CB ASP A 318 64.774 -7.928 18.864 1.00103.63 C ANISOU 2309 CB ASP A 318 12625 12876 13874 -893 -3883 1893 C ATOM 2310 CG ASP A 318 64.727 -6.444 19.167 1.00115.08 C ANISOU 2310 CG ASP A 318 14133 14416 15178 -1157 -3804 1832 C ATOM 2311 OD1 ASP A 318 64.244 -5.666 18.311 1.00117.77 O ANISOU 2311 OD1 ASP A 318 14449 14752 15547 -1239 -3578 1738 O ATOM 2312 OD2 ASP A 318 65.176 -6.053 20.264 1.00121.85 O ANISOU 2312 OD2 ASP A 318 15072 15340 15884 -1280 -3973 1877 O ATOM 2313 N PRO A 319 64.279 -10.321 16.716 1.00 87.67 N ANISOU 2313 N PRO A 319 10422 10633 12258 -389 -3736 1855 N ATOM 2314 CA PRO A 319 64.821 -9.421 15.694 1.00 83.99 C ANISOU 2314 CA PRO A 319 9691 10346 11874 -442 -3611 1726 C ATOM 2315 C PRO A 319 63.681 -8.851 14.870 1.00 86.75 C ANISOU 2315 C PRO A 319 10136 10612 12214 -537 -3330 1653 C ATOM 2316 O PRO A 319 62.846 -9.620 14.394 1.00 84.94 O ANISOU 2316 O PRO A 319 10005 10225 12045 -430 -3232 1656 O ATOM 2317 CB PRO A 319 65.642 -10.368 14.815 1.00 85.74 C ANISOU 2317 CB PRO A 319 9650 10626 12303 -180 -3673 1683 C ATOM 2318 CG PRO A 319 64.945 -11.691 14.962 1.00 86.00 C ANISOU 2318 CG PRO A 319 9880 10423 12375 -8 -3710 1757 C ATOM 2319 CD PRO A 319 64.591 -11.731 16.417 1.00 87.40 C ANISOU 2319 CD PRO A 319 10329 10506 12372 -120 -3849 1891 C ATOM 2320 N MET A 320 63.641 -7.535 14.706 1.00 83.51 N ANISOU 2320 N MET A 320 9705 10299 11725 -735 -3210 1590 N ATOM 2321 CA MET A 320 62.591 -6.913 13.913 1.00 79.57 C ANISOU 2321 CA MET A 320 9292 9730 11210 -815 -2952 1522 C ATOM 2322 C MET A 320 62.640 -7.415 12.474 1.00 84.71 C ANISOU 2322 C MET A 320 9749 10396 12039 -652 -2831 1440 C ATOM 2323 O MET A 320 63.695 -7.858 12.013 1.00 82.49 O ANISOU 2323 O MET A 320 9221 10236 11885 -521 -2923 1409 O ATOM 2324 CB MET A 320 62.723 -5.393 13.958 1.00 72.31 C ANISOU 2324 CB MET A 320 8377 8913 10185 -1041 -2867 1468 C ATOM 2325 CG MET A 320 62.379 -4.814 15.304 1.00 76.69 C ANISOU 2325 CG MET A 320 9179 9419 10540 -1211 -2936 1528 C ATOM 2326 SD MET A 320 60.613 -4.815 15.623 1.00 88.69 S ANISOU 2326 SD MET A 320 11029 10732 11937 -1249 -2756 1559 S ATOM 2327 CE MET A 320 60.061 -3.611 14.413 1.00 54.04 C ANISOU 2327 CE MET A 320 6603 6362 7568 -1333 -2489 1443 C ATOM 2328 N PRO A 321 61.493 -7.354 11.762 1.00 86.85 N ANISOU 2328 N PRO A 321 10128 10556 12314 -655 -2626 1401 N ATOM 2329 CA PRO A 321 61.384 -7.838 10.375 1.00 82.71 C ANISOU 2329 CA PRO A 321 9456 10033 11938 -510 -2500 1319 C ATOM 2330 C PRO A 321 62.444 -7.215 9.465 1.00 79.71 C ANISOU 2330 C PRO A 321 8793 9856 11637 -514 -2461 1230 C ATOM 2331 O PRO A 321 62.695 -6.013 9.556 1.00 76.43 O ANISOU 2331 O PRO A 321 8359 9541 11140 -694 -2413 1210 O ATOM 2332 CB PRO A 321 59.991 -7.370 9.944 1.00 67.57 C ANISOU 2332 CB PRO A 321 7710 8008 9954 -593 -2286 1293 C ATOM 2333 CG PRO A 321 59.237 -7.168 11.212 1.00 68.49 C ANISOU 2333 CG PRO A 321 8087 8021 9914 -715 -2322 1380 C ATOM 2334 CD PRO A 321 60.227 -6.774 12.253 1.00 76.30 C ANISOU 2334 CD PRO A 321 9056 9103 10830 -799 -2502 1428 C ATOM 2335 N SER A 322 63.047 -8.016 8.594 1.00 78.51 N ANISOU 2335 N SER A 322 8434 9760 11636 -322 -2473 1175 N ATOM 2336 CA SER A 322 64.084 -7.507 7.705 1.00 84.36 C ANISOU 2336 CA SER A 322 8886 10715 12450 -321 -2427 1091 C ATOM 2337 C SER A 322 63.822 -7.880 6.250 1.00 86.93 C ANISOU 2337 C SER A 322 9106 11044 12880 -189 -2258 995 C ATOM 2338 O SER A 322 63.109 -8.841 5.971 1.00 89.53 O ANISOU 2338 O SER A 322 9540 11218 13261 -46 -2235 990 O ATOM 2339 CB SER A 322 65.475 -7.996 8.147 1.00 83.40 C ANISOU 2339 CB SER A 322 8539 10745 12403 -215 -2637 1108 C ATOM 2340 OG SER A 322 65.627 -9.399 7.979 1.00 78.69 O ANISOU 2340 OG SER A 322 7900 10070 11929 51 -2729 1109 O ATOM 2341 N ASP A 323 64.419 -7.121 5.335 1.00 87.02 N ANISOU 2341 N ASP A 323 8915 11235 12914 -249 -2144 919 N ATOM 2342 CA ASP A 323 64.235 -7.325 3.903 1.00 93.05 C ANISOU 2342 CA ASP A 323 9572 12031 13751 -146 -1972 822 C ATOM 2343 C ASP A 323 64.788 -8.644 3.366 1.00 96.75 C ANISOU 2343 C ASP A 323 9877 12518 14367 127 -2034 767 C ATOM 2344 O ASP A 323 65.625 -9.287 3.996 1.00101.45 O ANISOU 2344 O ASP A 323 10366 13157 15023 244 -2215 796 O ATOM 2345 CB ASP A 323 64.818 -6.150 3.121 1.00 99.27 C ANISOU 2345 CB ASP A 323 10190 13017 14510 -296 -1840 767 C ATOM 2346 CG ASP A 323 63.936 -4.923 3.188 1.00118.78 C ANISOU 2346 CG ASP A 323 12870 15415 16846 -520 -1711 794 C ATOM 2347 OD1 ASP A 323 62.690 -5.087 3.209 1.00123.52 O ANISOU 2347 OD1 ASP A 323 13697 15833 17402 -504 -1643 811 O ATOM 2348 OD2 ASP A 323 64.485 -3.800 3.220 1.00125.60 O ANISOU 2348 OD2 ASP A 323 13673 16403 17648 -711 -1681 796 O ATOM 2349 N LEU A 324 64.308 -9.029 2.186 1.00 97.12 N ANISOU 2349 N LEU A 324 9910 12528 14463 234 -1886 682 N ATOM 2350 CA LEU A 324 64.664 -10.298 1.568 1.00 97.32 C ANISOU 2350 CA LEU A 324 9822 12534 14619 502 -1920 611 C ATOM 2351 C LEU A 324 65.728 -10.124 0.480 1.00108.78 C ANISOU 2351 C LEU A 324 10961 14234 16138 580 -1832 504 C ATOM 2352 O LEU A 324 65.711 -9.144 -0.272 1.00101.38 O ANISOU 2352 O LEU A 324 9954 13422 15142 434 -1668 464 O ATOM 2353 CB LEU A 324 63.415 -10.962 0.985 1.00 87.74 C ANISOU 2353 CB LEU A 324 8812 11112 13412 574 -1823 577 C ATOM 2354 CG LEU A 324 62.541 -11.815 1.912 1.00 82.83 C ANISOU 2354 CG LEU A 324 8456 10234 12782 608 -1938 661 C ATOM 2355 CD1 LEU A 324 62.327 -11.153 3.253 1.00 79.66 C ANISOU 2355 CD1 LEU A 324 8197 9797 12272 421 -2030 785 C ATOM 2356 CD2 LEU A 324 61.203 -12.133 1.249 1.00 79.22 C ANISOU 2356 CD2 LEU A 324 8183 9612 12306 601 -1807 624 C ATOM 2357 N LYS A 325 66.650 -11.086 0.411 1.00121.66 N ANISOU 2357 N LYS A 325 12406 15932 17886 815 -1942 459 N ATOM 2358 CA LYS A 325 67.731 -11.078 -0.578 1.00128.29 C ANISOU 2358 CA LYS A 325 12922 17024 18797 926 -1865 350 C ATOM 2359 C LYS A 325 68.316 -12.473 -0.840 1.00126.93 C ANISOU 2359 C LYS A 325 12630 16833 18763 1263 -1958 277 C ATOM 2360 O LYS A 325 68.359 -13.331 0.045 1.00120.23 O ANISOU 2360 O LYS A 325 11879 15837 17965 1402 -2149 338 O ATOM 2361 CB LYS A 325 68.841 -10.108 -0.161 1.00132.55 C ANISOU 2361 CB LYS A 325 13224 17831 19309 765 -1911 383 C ATOM 2362 CG LYS A 325 68.525 -8.654 -0.472 1.00135.97 C ANISOU 2362 CG LYS A 325 13697 18345 19620 458 -1749 400 C ATOM 2363 CD LYS A 325 69.614 -7.712 0.011 1.00138.05 C ANISOU 2363 CD LYS A 325 13746 18853 19852 271 -1809 435 C ATOM 2364 CE LYS A 325 69.196 -6.257 -0.176 1.00135.54 C ANISOU 2364 CE LYS A 325 13538 18558 19405 -47 -1664 465 C ATOM 2365 NZ LYS A 325 70.263 -5.302 0.243 1.00136.46 N ANISOU 2365 NZ LYS A 325 13455 18907 19485 -262 -1717 493 N TER 2366 LYS A 325 ATOM 2367 N ARG B 5 38.830 -1.505 -12.569 1.00136.81 N ANISOU 2367 N ARG B 5 15734 17924 18322 284 -1177 -1196 N ATOM 2368 CA ARG B 5 38.657 -1.155 -13.978 1.00137.84 C ANISOU 2368 CA ARG B 5 15860 17976 18537 205 -1004 -1167 C ATOM 2369 C ARG B 5 39.982 -0.859 -14.705 1.00144.20 C ANISOU 2369 C ARG B 5 16485 18763 19541 174 -953 -1234 C ATOM 2370 O ARG B 5 40.782 -0.038 -14.247 1.00151.44 O ANISOU 2370 O ARG B 5 17272 19697 20571 138 -1013 -1337 O ATOM 2371 CB ARG B 5 37.723 0.053 -14.102 1.00134.83 C ANISOU 2371 CB ARG B 5 15548 17560 18122 113 -934 -1172 C ATOM 2372 CG ARG B 5 36.433 -0.070 -13.311 1.00134.21 C ANISOU 2372 CG ARG B 5 15628 17507 17858 137 -982 -1123 C ATOM 2373 CD ARG B 5 35.739 1.277 -13.143 1.00135.93 C ANISOU 2373 CD ARG B 5 15878 17700 18068 57 -949 -1164 C ATOM 2374 NE ARG B 5 34.700 1.209 -12.118 1.00138.39 N ANISOU 2374 NE ARG B 5 16314 18061 18208 92 -1019 -1146 N ATOM 2375 CZ ARG B 5 34.096 2.264 -11.581 1.00138.27 C ANISOU 2375 CZ ARG B 5 16330 18045 18161 50 -1031 -1203 C ATOM 2376 NH1 ARG B 5 34.419 3.492 -11.968 1.00139.52 N ANISOU 2376 NH1 ARG B 5 16408 18140 18464 -32 -978 -1279 N ATOM 2377 NH2 ARG B 5 33.168 2.086 -10.651 1.00135.30 N ANISOU 2377 NH2 ARG B 5 16064 17727 17616 91 -1088 -1182 N ATOM 2378 N LYS B 6 40.210 -1.532 -15.834 1.00141.09 N ANISOU 2378 N LYS B 6 16077 18338 19193 187 -840 -1183 N ATOM 2379 CA LYS B 6 41.272 -1.140 -16.761 1.00143.94 C ANISOU 2379 CA LYS B 6 16280 18678 19731 142 -741 -1227 C ATOM 2380 C LYS B 6 40.943 0.256 -17.253 1.00157.72 C ANISOU 2380 C LYS B 6 18019 20378 21532 27 -633 -1233 C ATOM 2381 O LYS B 6 40.043 0.412 -18.074 1.00160.54 O ANISOU 2381 O LYS B 6 18481 20704 21813 -6 -512 -1152 O ATOM 2382 CB LYS B 6 41.284 -2.047 -17.996 1.00133.76 C ANISOU 2382 CB LYS B 6 15011 17371 18440 174 -613 -1167 C ATOM 2383 CG LYS B 6 41.659 -3.488 -17.763 1.00127.73 C ANISOU 2383 CG LYS B 6 14246 16625 17661 289 -686 -1157 C ATOM 2384 CD LYS B 6 43.089 -3.618 -17.330 1.00124.39 C ANISOU 2384 CD LYS B 6 13639 16235 17386 334 -772 -1237 C ATOM 2385 CE LYS B 6 43.516 -5.057 -17.297 1.00115.31 C ANISOU 2385 CE LYS B 6 12479 15088 16245 456 -819 -1217 C ATOM 2386 NZ LYS B 6 44.781 -5.141 -16.526 1.00122.01 N ANISOU 2386 NZ LYS B 6 13160 15987 17212 516 -951 -1291 N ATOM 2387 N ASN B 7 41.653 1.275 -16.783 1.00164.32 N ANISOU 2387 N ASN B 7 18725 21204 22506 -33 -675 -1326 N ATOM 2388 CA ASN B 7 41.296 2.639 -17.178 1.00171.20 C ANISOU 2388 CA ASN B 7 19593 22008 23448 -141 -571 -1325 C ATOM 2389 C ASN B 7 42.141 3.225 -18.347 1.00178.16 C ANISOU 2389 C ASN B 7 20334 22840 24517 -213 -404 -1313 C ATOM 2390 O ASN B 7 42.449 2.460 -19.257 1.00176.46 O ANISOU 2390 O ASN B 7 20104 22648 24295 -175 -314 -1258 O ATOM 2391 CB ASN B 7 41.091 3.526 -15.942 1.00175.68 C ANISOU 2391 CB ASN B 7 20158 22573 24021 -174 -698 -1423 C ATOM 2392 CG ASN B 7 39.622 3.633 -15.548 1.00175.65 C ANISOU 2392 CG ASN B 7 20346 22567 23828 -164 -714 -1365 C ATOM 2393 OD1 ASN B 7 38.734 3.618 -16.406 1.00173.55 O ANISOU 2393 OD1 ASN B 7 20190 22266 23485 -179 -590 -1257 O ATOM 2394 ND2 ASN B 7 39.361 3.742 -14.250 1.00177.28 N ANISOU 2394 ND2 ASN B 7 20585 22822 23952 -134 -867 -1442 N ATOM 2395 N ASN B 8 42.529 4.509 -18.387 1.00179.29 N ANISOU 2395 N ASN B 8 20374 22915 24831 -312 -351 -1360 N ATOM 2396 CA ASN B 8 42.465 5.509 -17.316 1.00177.63 C ANISOU 2396 CA ASN B 8 20132 22671 24689 -365 -457 -1470 C ATOM 2397 C ASN B 8 41.118 6.207 -17.122 1.00166.09 C ANISOU 2397 C ASN B 8 18832 21160 23115 -395 -437 -1423 C ATOM 2398 O ASN B 8 40.101 5.802 -17.687 1.00168.88 O ANISOU 2398 O ASN B 8 19340 21522 23305 -363 -365 -1301 O ATOM 2399 CB ASN B 8 43.549 6.567 -17.532 1.00185.19 C ANISOU 2399 CB ASN B 8 20887 23555 25923 -466 -393 -1550 C ATOM 2400 CG ASN B 8 44.867 5.966 -17.965 1.00191.61 C ANISOU 2400 CG ASN B 8 21526 24410 26868 -447 -371 -1580 C ATOM 2401 OD1 ASN B 8 45.304 4.946 -17.433 1.00191.23 O ANISOU 2401 OD1 ASN B 8 21452 24453 26755 -355 -502 -1628 O ATOM 2402 ND2 ASN B 8 45.512 6.598 -18.937 1.00196.83 N ANISOU 2402 ND2 ASN B 8 22063 25005 27720 -527 -197 -1544 N ATOM 2403 N ASN B 9 41.141 7.271 -16.323 1.00152.61 N ANISOU 2403 N ASN B 9 17076 19402 21506 -455 -501 -1533 N ATOM 2404 CA ASN B 9 39.926 7.857 -15.755 1.00138.60 C ANISOU 2404 CA ASN B 9 15444 17600 19619 -463 -533 -1533 C ATOM 2405 C ASN B 9 39.007 8.639 -16.696 1.00121.82 C ANISOU 2405 C ASN B 9 13410 15376 17498 -515 -359 -1406 C ATOM 2406 O ASN B 9 37.811 8.757 -16.430 1.00124.16 O ANISOU 2406 O ASN B 9 13856 15674 17646 -492 -372 -1365 O ATOM 2407 CB ASN B 9 40.266 8.710 -14.524 1.00139.83 C ANISOU 2407 CB ASN B 9 15513 17743 19875 -501 -670 -1719 C ATOM 2408 CG ASN B 9 40.182 7.923 -13.231 1.00141.44 C ANISOU 2408 CG ASN B 9 15759 18080 19900 -407 -876 -1806 C ATOM 2409 OD1 ASN B 9 39.694 6.793 -13.210 1.00142.83 O ANISOU 2409 OD1 ASN B 9 16053 18338 19879 -318 -907 -1709 O ATOM 2410 ND2 ASN B 9 40.649 8.522 -12.142 1.00142.67 N ANISOU 2410 ND2 ASN B 9 15820 18261 20127 -425 -1016 -1989 N ATOM 2411 N LYS B 10 39.552 9.174 -17.782 1.00 97.98 N ANISOU 2411 N LYS B 10 10302 12280 14648 -579 -196 -1338 N ATOM 2412 CA LYS B 10 38.744 9.963 -18.699 1.00 77.24 C ANISOU 2412 CA LYS B 10 7754 9564 12030 -618 -29 -1202 C ATOM 2413 C LYS B 10 38.722 9.370 -20.096 1.00 64.43 C ANISOU 2413 C LYS B 10 6163 7980 10336 -590 126 -1039 C ATOM 2414 O LYS B 10 38.309 10.025 -21.065 1.00 65.88 O ANISOU 2414 O LYS B 10 6380 8103 10547 -620 287 -908 O ATOM 2415 CB LYS B 10 39.215 11.413 -18.725 1.00 88.60 C ANISOU 2415 CB LYS B 10 9072 10854 13737 -724 49 -1249 C ATOM 2416 CG LYS B 10 38.818 12.192 -17.481 1.00102.09 C ANISOU 2416 CG LYS B 10 10793 12511 15486 -750 -78 -1399 C ATOM 2417 CD LYS B 10 39.537 13.536 -17.397 1.00115.07 C ANISOU 2417 CD LYS B 10 12279 13997 17444 -862 -21 -1491 C ATOM 2418 CE LYS B 10 39.098 14.314 -16.163 1.00120.18 C ANISOU 2418 CE LYS B 10 12941 14595 18128 -883 -149 -1664 C ATOM 2419 NZ LYS B 10 40.003 15.457 -15.872 1.00128.74 N ANISOU 2419 NZ LYS B 10 13839 15537 19538 -993 -136 -1814 N ATOM 2420 N ARG B 11 39.160 8.118 -20.194 1.00 56.02 N ANISOU 2420 N ARG B 11 5088 7020 9176 -525 76 -1048 N ATOM 2421 CA ARG B 11 39.112 7.388 -21.457 1.00 54.23 C ANISOU 2421 CA ARG B 11 4897 6852 8856 -483 204 -923 C ATOM 2422 C ARG B 11 37.687 7.273 -22.017 1.00 59.10 C ANISOU 2422 C ARG B 11 5695 7492 9268 -446 261 -799 C ATOM 2423 O ARG B 11 37.473 7.417 -23.226 1.00 60.14 O ANISOU 2423 O ARG B 11 5851 7634 9367 -445 416 -676 O ATOM 2424 CB ARG B 11 39.694 5.991 -21.289 1.00 47.09 C ANISOU 2424 CB ARG B 11 3966 6047 7881 -408 116 -975 C ATOM 2425 CG ARG B 11 39.266 5.045 -22.394 1.00 52.30 C ANISOU 2425 CG ARG B 11 4712 6779 8383 -346 211 -872 C ATOM 2426 CD ARG B 11 39.874 3.682 -22.215 1.00 52.74 C ANISOU 2426 CD ARG B 11 4733 6908 8399 -270 129 -931 C ATOM 2427 NE ARG B 11 41.289 3.690 -22.532 1.00 58.12 N ANISOU 2427 NE ARG B 11 5230 7591 9261 -287 179 -980 N ATOM 2428 CZ ARG B 11 42.107 2.664 -22.320 1.00 66.47 C ANISOU 2428 CZ ARG B 11 6211 8700 10344 -224 108 -1047 C ATOM 2429 NH1 ARG B 11 41.652 1.543 -21.776 1.00 58.83 N ANISOU 2429 NH1 ARG B 11 5341 7775 9238 -140 -14 -1064 N ATOM 2430 NH2 ARG B 11 43.387 2.760 -22.650 1.00 63.80 N ANISOU 2430 NH2 ARG B 11 5693 8366 10184 -243 164 -1091 N ATOM 2431 N TRP B 12 36.722 6.998 -21.141 1.00 44.01 N ANISOU 2431 N TRP B 12 3906 5603 7215 -410 136 -833 N ATOM 2432 CA TRP B 12 35.331 6.818 -21.583 1.00 56.02 C ANISOU 2432 CA TRP B 12 5588 7153 8545 -373 173 -732 C ATOM 2433 C TRP B 12 34.435 8.028 -21.284 1.00 59.02 C ANISOU 2433 C TRP B 12 6028 7452 8945 -411 191 -705 C ATOM 2434 O TRP B 12 33.226 7.894 -21.193 1.00 55.74 O ANISOU 2434 O TRP B 12 5741 7063 8375 -377 169 -661 O ATOM 2435 CB TRP B 12 34.712 5.538 -20.997 1.00 37.01 C ANISOU 2435 CB TRP B 12 3283 4829 5950 -300 49 -761 C ATOM 2436 CG TRP B 12 35.394 4.279 -21.457 1.00 48.89 C ANISOU 2436 CG TRP B 12 4750 6402 7426 -250 49 -770 C ATOM 2437 CD1 TRP B 12 36.209 3.463 -20.717 1.00 48.64 C ANISOU 2437 CD1 TRP B 12 4656 6398 7428 -214 -66 -857 C ATOM 2438 CD2 TRP B 12 35.332 3.699 -22.771 1.00 47.29 C ANISOU 2438 CD2 TRP B 12 4564 6250 7155 -221 168 -694 C ATOM 2439 NE1 TRP B 12 36.654 2.409 -21.489 1.00 48.39 N ANISOU 2439 NE1 TRP B 12 4600 6415 7369 -166 -20 -839 N ATOM 2440 CE2 TRP B 12 36.135 2.531 -22.752 1.00 41.54 C ANISOU 2440 CE2 TRP B 12 3780 5566 6437 -172 123 -750 C ATOM 2441 CE3 TRP B 12 34.676 4.051 -23.960 1.00 41.18 C ANISOU 2441 CE3 TRP B 12 3845 5498 6305 -224 304 -587 C ATOM 2442 CZ2 TRP B 12 36.304 1.721 -23.873 1.00 39.53 C ANISOU 2442 CZ2 TRP B 12 3523 5370 6129 -131 215 -720 C ATOM 2443 CZ3 TRP B 12 34.842 3.231 -25.082 1.00 45.29 C ANISOU 2443 CZ3 TRP B 12 4363 6095 6751 -181 390 -555 C ATOM 2444 CH2 TRP B 12 35.642 2.080 -25.025 1.00 42.79 C ANISOU 2444 CH2 TRP B 12 3991 5815 6454 -138 346 -629 C ATOM 2445 N TYR B 13 35.028 9.204 -21.129 1.00 52.77 N ANISOU 2445 N TYR B 13 5136 6555 8358 -482 234 -738 N ATOM 2446 CA TYR B 13 34.230 10.424 -21.080 1.00 55.42 C ANISOU 2446 CA TYR B 13 5519 6792 8745 -516 286 -695 C ATOM 2447 C TYR B 13 34.611 11.326 -22.237 1.00 52.40 C ANISOU 2447 C TYR B 13 5071 6327 8510 -563 473 -571 C ATOM 2448 O TYR B 13 35.780 11.504 -22.528 1.00 62.69 O ANISOU 2448 O TYR B 13 6239 7597 9984 -611 532 -590 O ATOM 2449 CB TYR B 13 34.322 11.106 -19.707 1.00 48.27 C ANISOU 2449 CB TYR B 13 4577 5818 7945 -554 161 -853 C ATOM 2450 CG TYR B 13 33.669 10.239 -18.665 1.00 50.93 C ANISOU 2450 CG TYR B 13 5011 6254 8085 -491 0 -930 C ATOM 2451 CD1 TYR B 13 32.308 10.346 -18.391 1.00 51.79 C ANISOU 2451 CD1 TYR B 13 5257 6376 8045 -456 -19 -893 C ATOM 2452 CD2 TYR B 13 34.390 9.248 -18.019 1.00 56.00 C ANISOU 2452 CD2 TYR B 13 5609 6983 8685 -459 -122 -1022 C ATOM 2453 CE1 TYR B 13 31.697 9.515 -17.467 1.00 54.64 C ANISOU 2453 CE1 TYR B 13 5706 6831 8226 -400 -149 -946 C ATOM 2454 CE2 TYR B 13 33.790 8.412 -17.104 1.00 63.35 C ANISOU 2454 CE2 TYR B 13 6633 8004 9433 -396 -255 -1064 C ATOM 2455 CZ TYR B 13 32.448 8.548 -16.829 1.00 63.76 C ANISOU 2455 CZ TYR B 13 6819 8066 9342 -370 -263 -1025 C ATOM 2456 OH TYR B 13 31.875 7.710 -15.909 1.00 69.98 O ANISOU 2456 OH TYR B 13 7692 8942 9954 -311 -381 -1056 O ATOM 2457 N PHE B 14 33.611 11.843 -22.932 1.00 52.08 N ANISOU 2457 N PHE B 14 5125 6266 8398 -543 570 -432 N ATOM 2458 CA PHE B 14 33.850 12.532 -24.190 1.00 58.13 C ANISOU 2458 CA PHE B 14 5851 6983 9251 -563 761 -269 C ATOM 2459 C PHE B 14 33.281 13.952 -24.187 1.00 59.99 C ANISOU 2459 C PHE B 14 6104 7069 9620 -596 837 -198 C ATOM 2460 O PHE B 14 32.299 14.238 -23.494 1.00 57.38 O ANISOU 2460 O PHE B 14 5861 6711 9230 -575 755 -240 O ATOM 2461 CB PHE B 14 33.255 11.711 -25.342 1.00 55.66 C ANISOU 2461 CB PHE B 14 5630 6813 8705 -485 831 -134 C ATOM 2462 CG PHE B 14 33.737 10.287 -25.376 1.00 57.40 C ANISOU 2462 CG PHE B 14 5840 7166 8805 -446 762 -209 C ATOM 2463 CD1 PHE B 14 34.724 9.892 -26.272 1.00 55.13 C ANISOU 2463 CD1 PHE B 14 5463 6932 8553 -446 866 -169 C ATOM 2464 CD2 PHE B 14 33.227 9.348 -24.492 1.00 52.52 C ANISOU 2464 CD2 PHE B 14 5295 6611 8049 -408 600 -317 C ATOM 2465 CE1 PHE B 14 35.183 8.572 -26.290 1.00 45.93 C ANISOU 2465 CE1 PHE B 14 4284 5876 7293 -404 803 -247 C ATOM 2466 CE2 PHE B 14 33.673 8.034 -24.502 1.00 51.58 C ANISOU 2466 CE2 PHE B 14 5165 6593 7841 -368 539 -379 C ATOM 2467 CZ PHE B 14 34.656 7.643 -25.404 1.00 52.31 C ANISOU 2467 CZ PHE B 14 5168 6731 7977 -364 638 -351 C ATOM 2468 N THR B 15 33.912 14.837 -24.957 1.00 61.38 N ANISOU 2468 N THR B 15 6192 7144 9987 -646 1002 -88 N ATOM 2469 CA THR B 15 33.403 16.193 -25.164 1.00 58.52 C ANISOU 2469 CA THR B 15 5844 6623 9769 -669 1106 19 C ATOM 2470 C THR B 15 32.282 16.136 -26.177 1.00 60.51 C ANISOU 2470 C THR B 15 6224 6958 9810 -581 1190 219 C ATOM 2471 O THR B 15 32.137 15.148 -26.899 1.00 57.19 O ANISOU 2471 O THR B 15 5852 6707 9171 -519 1200 280 O ATOM 2472 CB THR B 15 34.473 17.104 -25.753 1.00 61.76 C ANISOU 2472 CB THR B 15 6113 6895 10458 -750 1275 101 C ATOM 2473 OG1 THR B 15 34.867 16.586 -27.034 1.00 65.82 O ANISOU 2473 OG1 THR B 15 6615 7526 10868 -714 1414 262 O ATOM 2474 CG2 THR B 15 35.691 17.184 -24.825 1.00 52.07 C ANISOU 2474 CG2 THR B 15 4731 5591 9463 -843 1196 -107 C ATOM 2475 N ARG B 16 31.494 17.198 -26.254 1.00 71.47 N ANISOU 2475 N ARG B 16 7660 8227 11268 -571 1249 317 N ATOM 2476 CA ARG B 16 30.378 17.193 -27.185 1.00 74.63 C ANISOU 2476 CA ARG B 16 8176 8714 11464 -476 1315 506 C ATOM 2477 C ARG B 16 30.880 17.088 -28.623 1.00 74.05 C ANISOU 2477 C ARG B 16 8073 8722 11340 -450 1489 705 C ATOM 2478 O ARG B 16 30.248 16.447 -29.466 1.00 76.36 O ANISOU 2478 O ARG B 16 8448 9187 11379 -363 1507 809 O ATOM 2479 CB ARG B 16 29.465 18.399 -26.965 1.00 81.01 C ANISOU 2479 CB ARG B 16 9033 9370 12377 -461 1346 576 C ATOM 2480 CG ARG B 16 28.666 18.296 -25.666 1.00 90.14 C ANISOU 2480 CG ARG B 16 10250 10511 13489 -454 1171 391 C ATOM 2481 CD ARG B 16 27.404 19.144 -25.682 1.00 96.97 C ANISOU 2481 CD ARG B 16 11198 11301 14346 -395 1193 483 C ATOM 2482 NE ARG B 16 26.654 19.025 -24.431 1.00 97.76 N ANISOU 2482 NE ARG B 16 11350 11398 14396 -386 1036 301 N ATOM 2483 CZ ARG B 16 25.860 18.001 -24.122 1.00 90.75 C ANISOU 2483 CZ ARG B 16 10548 10682 13253 -331 917 239 C ATOM 2484 NH1 ARG B 16 25.713 16.996 -24.979 1.00100.82 N ANISOU 2484 NH1 ARG B 16 11863 12135 14307 -281 928 330 N ATOM 2485 NH2 ARG B 16 25.217 17.976 -22.954 1.00 66.92 N ANISOU 2485 NH2 ARG B 16 7569 7655 10202 -325 792 83 N ATOM 2486 N GLU B 17 32.035 17.693 -28.887 1.00 70.18 N ANISOU 2486 N GLU B 17 7458 8116 11090 -526 1615 746 N ATOM 2487 CA GLU B 17 32.667 17.610 -30.200 1.00 72.18 C ANISOU 2487 CA GLU B 17 7666 8448 11311 -508 1796 929 C ATOM 2488 C GLU B 17 33.114 16.184 -30.517 1.00 72.26 C ANISOU 2488 C GLU B 17 7670 8671 11112 -475 1743 848 C ATOM 2489 O GLU B 17 32.993 15.718 -31.653 1.00 68.57 O ANISOU 2489 O GLU B 17 7240 8365 10449 -404 1836 983 O ATOM 2490 CB GLU B 17 33.852 18.569 -30.285 1.00 81.70 C ANISOU 2490 CB GLU B 17 8722 9468 12853 -611 1943 974 C ATOM 2491 CG GLU B 17 34.986 18.066 -31.162 1.00 95.84 C ANISOU 2491 CG GLU B 17 10414 11361 14641 -627 2073 1037 C ATOM 2492 CD GLU B 17 35.790 19.195 -31.766 1.00114.57 C ANISOU 2492 CD GLU B 17 12671 13569 17293 -696 2297 1208 C ATOM 2493 OE1 GLU B 17 35.267 20.333 -31.806 1.00119.56 O ANISOU 2493 OE1 GLU B 17 13331 14032 18065 -702 2374 1338 O ATOM 2494 OE2 GLU B 17 36.937 18.947 -32.206 1.00119.59 O ANISOU 2494 OE2 GLU B 17 13183 14239 18017 -743 2401 1217 O ATOM 2495 N GLN B 18 33.637 15.490 -29.513 1.00 70.40 N ANISOU 2495 N GLN B 18 7388 8440 10920 -521 1592 624 N ATOM 2496 CA GLN B 18 33.947 14.076 -29.677 1.00 66.21 C ANISOU 2496 CA GLN B 18 6864 8095 10200 -481 1521 531 C ATOM 2497 C GLN B 18 32.677 13.275 -29.947 1.00 62.97 C ANISOU 2497 C GLN B 18 6602 7842 9481 -381 1439 551 C ATOM 2498 O GLN B 18 32.693 12.307 -30.704 1.00 66.68 O ANISOU 2498 O GLN B 18 7097 8481 9758 -322 1457 567 O ATOM 2499 CB GLN B 18 34.657 13.526 -28.447 1.00 63.35 C ANISOU 2499 CB GLN B 18 6429 7699 9943 -536 1361 299 C ATOM 2500 CG GLN B 18 36.148 13.787 -28.423 1.00 62.94 C ANISOU 2500 CG GLN B 18 6202 7571 10139 -619 1434 251 C ATOM 2501 CD GLN B 18 36.754 13.414 -27.092 1.00 77.45 C ANISOU 2501 CD GLN B 18 7967 9371 12089 -667 1257 20 C ATOM 2502 OE1 GLN B 18 36.322 13.895 -26.040 1.00 79.23 O ANISOU 2502 OE1 GLN B 18 8219 9501 12382 -694 1140 -84 O ATOM 2503 NE2 GLN B 18 37.754 12.544 -27.125 1.00 85.93 N ANISOU 2503 NE2 GLN B 18 8948 10528 13174 -667 1233 -66 N ATOM 2504 N LEU B 19 31.571 13.677 -29.330 1.00 57.02 N ANISOU 2504 N LEU B 19 5940 7034 8690 -364 1350 537 N ATOM 2505 CA LEU B 19 30.307 12.992 -29.582 1.00 57.07 C ANISOU 2505 CA LEU B 19 6076 7184 8425 -276 1276 557 C ATOM 2506 C LEU B 19 29.820 13.277 -31.003 1.00 61.87 C ANISOU 2506 C LEU B 19 6727 7891 8890 -201 1420 770 C ATOM 2507 O LEU B 19 29.265 12.411 -31.670 1.00 67.74 O ANISOU 2507 O LEU B 19 7533 8813 9391 -127 1399 785 O ATOM 2508 CB LEU B 19 29.272 13.365 -28.530 1.00 47.64 C ANISOU 2508 CB LEU B 19 4955 5910 7236 -276 1151 485 C ATOM 2509 CG LEU B 19 29.615 12.756 -27.168 1.00 52.57 C ANISOU 2509 CG LEU B 19 5558 6505 7912 -322 988 268 C ATOM 2510 CD1 LEU B 19 28.781 13.367 -26.065 1.00 51.79 C ANISOU 2510 CD1 LEU B 19 5510 6308 7861 -332 890 195 C ATOM 2511 CD2 LEU B 19 29.422 11.248 -27.206 1.00 48.06 C ANISOU 2511 CD2 LEU B 19 5035 6098 7128 -276 893 189 C ATOM 2512 N GLU B 20 30.064 14.489 -31.476 1.00 70.41 N ANISOU 2512 N GLU B 20 7768 8859 10125 -219 1569 934 N ATOM 2513 CA GLU B 20 29.749 14.828 -32.853 1.00 73.26 C ANISOU 2513 CA GLU B 20 8160 9319 10356 -141 1722 1162 C ATOM 2514 C GLU B 20 30.563 13.972 -33.827 1.00 69.64 C ANISOU 2514 C GLU B 20 7656 9033 9772 -117 1807 1181 C ATOM 2515 O GLU B 20 29.999 13.331 -34.717 1.00 72.20 O ANISOU 2515 O GLU B 20 8043 9556 9834 -26 1816 1235 O ATOM 2516 CB GLU B 20 29.987 16.318 -33.100 1.00 84.93 C ANISOU 2516 CB GLU B 20 9593 10613 12063 -172 1879 1346 C ATOM 2517 CG GLU B 20 29.700 16.764 -34.525 1.00 99.17 C ANISOU 2517 CG GLU B 20 11427 12517 13735 -82 2051 1615 C ATOM 2518 CD GLU B 20 28.299 16.389 -34.987 1.00109.63 C ANISOU 2518 CD GLU B 20 12876 14016 14764 39 1975 1671 C ATOM 2519 OE1 GLU B 20 27.402 16.209 -34.124 1.00104.05 O ANISOU 2519 OE1 GLU B 20 12231 13281 14024 43 1816 1543 O ATOM 2520 OE2 GLU B 20 28.100 16.276 -36.218 1.00114.97 O ANISOU 2520 OE2 GLU B 20 13580 14867 15237 131 2076 1839 O ATOM 2521 N ASN B 21 31.884 13.950 -33.649 1.00 63.03 N ANISOU 2521 N ASN B 21 6700 8124 9123 -196 1866 1122 N ATOM 2522 CA ASN B 21 32.764 13.150 -34.504 1.00 64.79 C ANISOU 2522 CA ASN B 21 6863 8500 9254 -175 1954 1124 C ATOM 2523 C ASN B 21 32.863 11.697 -34.077 1.00 71.63 C ANISOU 2523 C ASN B 21 7741 9483 9991 -162 1800 907 C ATOM 2524 O ASN B 21 33.943 11.207 -33.725 1.00 74.94 O ANISOU 2524 O ASN B 21 8063 9880 10530 -213 1787 786 O ATOM 2525 CB ASN B 21 34.158 13.766 -34.575 1.00 72.89 C ANISOU 2525 CB ASN B 21 7742 9405 10550 -263 2099 1164 C ATOM 2526 CG ASN B 21 34.123 15.201 -35.051 1.00 86.00 C ANISOU 2526 CG ASN B 21 9382 10929 12364 -280 2274 1395 C ATOM 2527 OD1 ASN B 21 33.247 15.586 -35.837 1.00 77.46 O ANISOU 2527 OD1 ASN B 21 8390 9919 11120 -195 2342 1581 O ATOM 2528 ND2 ASN B 21 35.066 16.008 -34.572 1.00 96.82 N ANISOU 2528 ND2 ASN B 21 10630 12099 14060 -389 2345 1386 N ATOM 2529 N SER B 22 31.725 11.012 -34.124 1.00 64.65 N ANISOU 2529 N SER B 22 6972 8720 8874 -90 1687 864 N ATOM 2530 CA SER B 22 31.647 9.623 -33.716 1.00 62.19 C ANISOU 2530 CA SER B 22 6685 8503 8441 -72 1541 671 C ATOM 2531 C SER B 22 32.024 8.676 -34.862 1.00 65.48 C ANISOU 2531 C SER B 22 7085 9117 8676 -7 1616 668 C ATOM 2532 O SER B 22 32.031 9.062 -36.031 1.00 64.35 O ANISOU 2532 O SER B 22 6941 9078 8430 44 1766 825 O ATOM 2533 CB SER B 22 30.229 9.320 -33.275 1.00 54.97 C ANISOU 2533 CB SER B 22 5890 7622 7375 -31 1397 625 C ATOM 2534 OG SER B 22 29.405 9.182 -34.411 1.00 55.85 O ANISOU 2534 OG SER B 22 6067 7901 7251 59 1450 731 O ATOM 2535 N PRO B 23 32.331 7.420 -34.532 1.00 60.75 N ANISOU 2535 N PRO B 23 6474 8574 8034 -2 1515 489 N ATOM 2536 CA PRO B 23 32.602 6.469 -35.614 1.00 59.35 C ANISOU 2536 CA PRO B 23 6285 8584 7680 67 1579 459 C ATOM 2537 C PRO B 23 31.470 6.409 -36.646 1.00 57.82 C ANISOU 2537 C PRO B 23 6186 8564 7218 157 1606 547 C ATOM 2538 O PRO B 23 31.750 6.323 -37.844 1.00 61.66 O ANISOU 2538 O PRO B 23 6652 9207 7569 218 1737 621 O ATOM 2539 CB PRO B 23 32.747 5.135 -34.874 1.00 52.55 C ANISOU 2539 CB PRO B 23 5425 7720 6821 63 1426 246 C ATOM 2540 CG PRO B 23 33.236 5.530 -33.517 1.00 57.75 C ANISOU 2540 CG PRO B 23 6037 8190 7715 -21 1339 187 C ATOM 2541 CD PRO B 23 32.549 6.832 -33.200 1.00 58.67 C ANISOU 2541 CD PRO B 23 6197 8204 7890 -53 1352 312 C ATOM 2542 N SER B 24 30.219 6.454 -36.197 1.00 53.32 N ANISOU 2542 N SER B 24 5711 7979 6567 172 1485 535 N ATOM 2543 CA SER B 24 29.085 6.395 -37.114 1.00 63.71 C ANISOU 2543 CA SER B 24 7107 9466 7633 260 1490 604 C ATOM 2544 C SER B 24 29.041 7.621 -38.018 1.00 68.10 C ANISOU 2544 C SER B 24 7661 10061 8153 300 1650 844 C ATOM 2545 O SER B 24 28.674 7.520 -39.194 1.00 71.16 O ANISOU 2545 O SER B 24 8074 10646 8316 390 1721 924 O ATOM 2546 CB SER B 24 27.757 6.280 -36.352 1.00 64.33 C ANISOU 2546 CB SER B 24 7274 9505 7665 260 1330 546 C ATOM 2547 OG SER B 24 27.708 5.100 -35.586 1.00 56.21 O ANISOU 2547 OG SER B 24 6254 8450 6653 231 1192 346 O ATOM 2548 N ARG B 25 29.398 8.779 -37.461 1.00 60.58 N ANISOU 2548 N ARG B 25 6677 8920 7421 237 1707 957 N ATOM 2549 CA ARG B 25 29.407 10.013 -38.237 1.00 62.39 C ANISOU 2549 CA ARG B 25 6900 9145 7660 269 1872 1205 C ATOM 2550 C ARG B 25 30.342 9.850 -39.424 1.00 67.08 C ANISOU 2550 C ARG B 25 7430 9886 8170 308 2047 1288 C ATOM 2551 O ARG B 25 30.065 10.337 -40.515 1.00 70.77 O ANISOU 2551 O ARG B 25 7921 10487 8480 391 2170 1477 O ATOM 2552 CB ARG B 25 29.846 11.212 -37.390 1.00 63.61 C ANISOU 2552 CB ARG B 25 7008 9042 8117 177 1913 1281 C ATOM 2553 CG ARG B 25 29.490 12.574 -38.013 1.00 63.38 C ANISOU 2553 CG ARG B 25 6998 8968 8117 216 2056 1547 C ATOM 2554 CD ARG B 25 28.042 12.942 -37.766 1.00 59.65 C ANISOU 2554 CD ARG B 25 6626 8491 7549 271 1951 1589 C ATOM 2555 NE ARG B 25 27.767 13.036 -36.329 1.00 73.54 N ANISOU 2555 NE ARG B 25 8394 10059 9488 191 1803 1434 N ATOM 2556 CZ ARG B 25 27.206 12.078 -35.592 1.00 67.12 C ANISOU 2556 CZ ARG B 25 7625 9286 8592 183 1625 1233 C ATOM 2557 NH1 ARG B 25 27.020 12.262 -34.296 1.00 66.45 N ANISOU 2557 NH1 ARG B 25 7545 9035 8667 115 1510 1114 N ATOM 2558 NH2 ARG B 25 26.831 10.937 -36.144 1.00 61.74 N ANISOU 2558 NH2 ARG B 25 6979 8810 7671 243 1566 1149 N ATOM 2559 N ARG B 26 31.443 9.142 -39.206 1.00 69.08 N ANISOU 2559 N ARG B 26 7601 10125 8521 258 2057 1148 N ATOM 2560 CA ARG B 26 32.454 8.971 -40.236 1.00 71.34 C ANISOU 2560 CA ARG B 26 7811 10539 8757 287 2232 1209 C ATOM 2561 C ARG B 26 31.873 8.215 -41.423 1.00 71.79 C ANISOU 2561 C ARG B 26 7924 10878 8474 409 2247 1202 C ATOM 2562 O ARG B 26 32.320 8.389 -42.553 1.00 79.72 O ANISOU 2562 O ARG B 26 8898 12038 9355 470 2417 1330 O ATOM 2563 CB ARG B 26 33.677 8.255 -39.662 1.00 78.30 C ANISOU 2563 CB ARG B 26 8588 11348 9815 214 2213 1029 C ATOM 2564 CG ARG B 26 34.773 7.935 -40.666 1.00 96.42 C ANISOU 2564 CG ARG B 26 10790 13781 12066 245 2388 1057 C ATOM 2565 CD ARG B 26 35.822 7.010 -40.054 1.00102.14 C ANISOU 2565 CD ARG B 26 11418 14452 12940 193 2331 845 C ATOM 2566 NE ARG B 26 36.592 6.300 -41.074 1.00108.18 N ANISOU 2566 NE ARG B 26 12118 15403 13585 253 2457 809 N ATOM 2567 CZ ARG B 26 37.351 5.232 -40.834 1.00113.14 C ANISOU 2567 CZ ARG B 26 12676 16048 14265 249 2408 610 C ATOM 2568 NH1 ARG B 26 37.446 4.741 -39.603 1.00111.11 N ANISOU 2568 NH1 ARG B 26 12408 15637 14172 190 2232 444 N ATOM 2569 NH2 ARG B 26 38.014 4.653 -41.829 1.00112.36 N ANISOU 2569 NH2 ARG B 26 12517 16125 14050 312 2538 581 N ATOM 2570 N PHE B 27 30.859 7.394 -41.174 1.00 64.45 N ANISOU 2570 N PHE B 27 7075 10021 7391 445 2071 1051 N ATOM 2571 CA PHE B 27 30.232 6.630 -42.252 1.00 66.63 C ANISOU 2571 CA PHE B 27 7399 10567 7349 557 2061 1006 C ATOM 2572 C PHE B 27 28.862 7.199 -42.651 1.00 69.18 C ANISOU 2572 C PHE B 27 7815 10983 7486 635 2018 1138 C ATOM 2573 O PHE B 27 28.024 6.505 -43.223 1.00 65.89 O ANISOU 2573 O PHE B 27 7448 10763 6823 715 1937 1051 O ATOM 2574 CB PHE B 27 30.128 5.147 -41.883 1.00 71.25 C ANISOU 2574 CB PHE B 27 7990 11195 7885 551 1908 724 C ATOM 2575 CG PHE B 27 31.449 4.517 -41.550 1.00 79.14 C ANISOU 2575 CG PHE B 27 8897 12120 9053 496 1944 594 C ATOM 2576 CD1 PHE B 27 32.200 3.888 -42.528 1.00 77.64 C ANISOU 2576 CD1 PHE B 27 8649 12103 8746 553 2056 542 C ATOM 2577 CD2 PHE B 27 31.948 4.563 -40.258 1.00 82.98 C ANISOU 2577 CD2 PHE B 27 9346 12373 9810 394 1864 522 C ATOM 2578 CE1 PHE B 27 33.420 3.312 -42.218 1.00 77.83 C ANISOU 2578 CE1 PHE B 27 8578 12058 8936 509 2089 422 C ATOM 2579 CE2 PHE B 27 33.170 3.984 -39.944 1.00 81.42 C ANISOU 2579 CE2 PHE B 27 9052 12114 9768 353 1888 404 C ATOM 2580 CZ PHE B 27 33.902 3.359 -40.923 1.00 78.41 C ANISOU 2580 CZ PHE B 27 8611 11896 9285 410 2001 356 C ATOM 2581 N GLY B 28 28.640 8.467 -42.337 1.00 70.14 N ANISOU 2581 N GLY B 28 7952 10958 7742 611 2068 1338 N ATOM 2582 CA GLY B 28 27.504 9.184 -42.881 1.00 70.52 C ANISOU 2582 CA GLY B 28 8072 11099 7624 701 2068 1514 C ATOM 2583 C GLY B 28 26.204 9.028 -42.129 1.00 74.83 C ANISOU 2583 C GLY B 28 8688 11595 8148 699 1874 1418 C ATOM 2584 O GLY B 28 25.144 9.285 -42.683 1.00 85.32 O ANISOU 2584 O GLY B 28 10073 13061 9285 793 1841 1507 O ATOM 2585 N VAL B 29 26.275 8.605 -40.873 1.00 69.36 N ANISOU 2585 N VAL B 29 7990 10718 7646 599 1747 1239 N ATOM 2586 CA VAL B 29 25.091 8.584 -40.031 1.00 64.17 C ANISOU 2586 CA VAL B 29 7393 9986 7002 586 1582 1165 C ATOM 2587 C VAL B 29 24.935 9.955 -39.370 1.00 63.21 C ANISOU 2587 C VAL B 29 7280 9649 7088 547 1619 1328 C ATOM 2588 O VAL B 29 25.820 10.403 -38.643 1.00 64.01 O ANISOU 2588 O VAL B 29 7333 9549 7438 455 1664 1328 O ATOM 2589 CB VAL B 29 25.166 7.462 -38.954 1.00 52.64 C ANISOU 2589 CB VAL B 29 5929 8437 5635 505 1429 905 C ATOM 2590 CG1 VAL B 29 23.869 7.355 -38.206 1.00 49.29 C ANISOU 2590 CG1 VAL B 29 5566 7971 5191 501 1272 835 C ATOM 2591 CG2 VAL B 29 25.494 6.129 -39.593 1.00 52.78 C ANISOU 2591 CG2 VAL B 29 5926 8629 5497 536 1412 740 C ATOM 2592 N ASP B 30 23.819 10.626 -39.646 1.00 63.51 N ANISOU 2592 N ASP B 30 7372 9731 7029 622 1599 1461 N ATOM 2593 CA ASP B 30 23.495 11.904 -39.012 1.00 64.52 C ANISOU 2593 CA ASP B 30 7513 9651 7350 598 1622 1601 C ATOM 2594 C ASP B 30 23.537 11.757 -37.506 1.00 71.39 C ANISOU 2594 C ASP B 30 8379 10308 8438 487 1502 1424 C ATOM 2595 O ASP B 30 23.323 10.667 -36.985 1.00 75.51 O ANISOU 2595 O ASP B 30 8912 10873 8905 457 1371 1218 O ATOM 2596 CB ASP B 30 22.072 12.336 -39.373 1.00 79.47 C ANISOU 2596 CB ASP B 30 9467 11641 9086 704 1566 1707 C ATOM 2597 CG ASP B 30 21.897 12.623 -40.837 1.00105.92 C ANISOU 2597 CG ASP B 30 12827 15214 12203 834 1675 1908 C ATOM 2598 OD1 ASP B 30 22.813 12.304 -41.631 1.00112.30 O ANISOU 2598 OD1 ASP B 30 13601 16136 12932 846 1788 1940 O ATOM 2599 OD2 ASP B 30 20.828 13.170 -41.189 1.00119.29 O ANISOU 2599 OD2 ASP B 30 14561 16979 13786 931 1647 2036 O ATOM 2600 N PRO B 31 23.779 12.864 -36.796 1.00 70.84 N ANISOU 2600 N PRO B 31 8291 10008 8615 430 1547 1505 N ATOM 2601 CA PRO B 31 23.702 12.900 -35.335 1.00 64.42 C ANISOU 2601 CA PRO B 31 7478 9001 7995 339 1432 1347 C ATOM 2602 C PRO B 31 22.392 12.341 -34.812 1.00 73.34 C ANISOU 2602 C PRO B 31 8672 10196 8998 369 1269 1230 C ATOM 2603 O PRO B 31 22.391 11.444 -33.962 1.00 80.09 O ANISOU 2603 O PRO B 31 9532 11036 9864 314 1150 1034 O ATOM 2604 CB PRO B 31 23.770 14.391 -35.031 1.00 65.88 C ANISOU 2604 CB PRO B 31 7649 8976 8407 318 1521 1501 C ATOM 2605 CG PRO B 31 24.629 14.934 -36.123 1.00 70.74 C ANISOU 2605 CG PRO B 31 8218 9617 9043 341 1711 1699 C ATOM 2606 CD PRO B 31 24.289 14.128 -37.351 1.00 68.11 C ANISOU 2606 CD PRO B 31 7915 9567 8395 444 1725 1744 C ATOM 2607 N ASP B 32 21.284 12.877 -35.308 1.00 76.92 N ANISOU 2607 N ASP B 32 9169 10719 9339 460 1269 1357 N ATOM 2608 CA ASP B 32 19.962 12.489 -34.825 1.00 75.54 C ANISOU 2608 CA ASP B 32 9042 10599 9061 491 1126 1261 C ATOM 2609 C ASP B 32 19.656 11.005 -35.023 1.00 62.92 C ANISOU 2609 C ASP B 32 7455 9186 7268 498 1022 1089 C ATOM 2610 O ASP B 32 19.076 10.361 -34.144 1.00 54.02 O ANISOU 2610 O ASP B 32 6345 8033 6144 459 897 931 O ATOM 2611 CB ASP B 32 18.882 13.356 -35.468 1.00 83.75 C ANISOU 2611 CB ASP B 32 10113 11698 10012 602 1153 1443 C ATOM 2612 CG ASP B 32 18.717 14.683 -34.758 1.00107.93 C ANISOU 2612 CG ASP B 32 13176 14530 13302 585 1192 1539 C ATOM 2613 OD1 ASP B 32 19.372 14.875 -33.706 1.00111.15 O ANISOU 2613 OD1 ASP B 32 13562 14745 13924 483 1182 1436 O ATOM 2614 OD2 ASP B 32 17.933 15.529 -35.243 1.00120.96 O ANISOU 2614 OD2 ASP B 32 14846 16195 14919 680 1229 1709 O ATOM 2615 N LYS B 33 20.048 10.475 -36.176 1.00 56.35 N ANISOU 2615 N LYS B 33 6607 8533 6269 548 1080 1120 N ATOM 2616 CA LYS B 33 19.917 9.056 -36.467 1.00 64.70 C ANISOU 2616 CA LYS B 33 7666 9756 7162 552 997 946 C ATOM 2617 C LYS B 33 20.681 8.230 -35.415 1.00 65.80 C ANISOU 2617 C LYS B 33 7785 9768 7446 444 937 758 C ATOM 2618 O LYS B 33 20.169 7.252 -34.868 1.00 58.96 O ANISOU 2618 O LYS B 33 6935 8922 6544 418 819 594 O ATOM 2619 CB LYS B 33 20.463 8.783 -37.871 1.00 68.83 C ANISOU 2619 CB LYS B 33 8167 10477 7510 621 1097 1013 C ATOM 2620 CG LYS B 33 19.915 7.540 -38.547 1.00 80.71 C ANISOU 2620 CG LYS B 33 9676 12207 8783 671 1014 865 C ATOM 2621 CD LYS B 33 18.418 7.655 -38.813 1.00 89.44 C ANISOU 2621 CD LYS B 33 10811 13437 9736 748 923 885 C ATOM 2622 CE LYS B 33 17.912 6.465 -39.622 1.00 96.00 C ANISOU 2622 CE LYS B 33 11632 14508 10336 799 847 730 C ATOM 2623 NZ LYS B 33 16.473 6.187 -39.362 1.00 97.81 N ANISOU 2623 NZ LYS B 33 11872 14797 10493 821 709 647 N ATOM 2624 N GLU B 34 21.906 8.649 -35.120 1.00 63.26 N ANISOU 2624 N GLU B 34 7424 9312 7298 385 1020 791 N ATOM 2625 CA GLU B 34 22.739 7.919 -34.185 1.00 59.84 C ANISOU 2625 CA GLU B 34 6963 8773 6999 298 966 630 C ATOM 2626 C GLU B 34 22.117 7.915 -32.792 1.00 58.72 C ANISOU 2626 C GLU B 34 6852 8497 6960 245 844 533 C ATOM 2627 O GLU B 34 22.159 6.898 -32.093 1.00 57.98 O ANISOU 2627 O GLU B 34 6764 8391 6874 205 748 377 O ATOM 2628 CB GLU B 34 24.166 8.475 -34.158 1.00 42.70 C ANISOU 2628 CB GLU B 34 4727 6490 5005 247 1079 686 C ATOM 2629 CG GLU B 34 25.010 7.925 -33.022 1.00 51.75 C ANISOU 2629 CG GLU B 34 5838 7509 6317 160 1010 530 C ATOM 2630 CD GLU B 34 26.501 8.194 -33.181 1.00 59.00 C ANISOU 2630 CD GLU B 34 6670 8361 7386 116 1117 555 C ATOM 2631 OE1 GLU B 34 26.893 8.856 -34.161 1.00 62.74 O ANISOU 2631 OE1 GLU B 34 7114 8877 7848 145 1260 706 O ATOM 2632 OE2 GLU B 34 27.282 7.741 -32.318 1.00 59.26 O ANISOU 2632 OE2 GLU B 34 6660 8305 7551 54 1059 429 O ATOM 2633 N LEU B 35 21.538 9.042 -32.389 1.00 49.86 N ANISOU 2633 N LEU B 35 5751 7277 5917 250 853 629 N ATOM 2634 CA LEU B 35 20.868 9.098 -31.093 1.00 53.35 C ANISOU 2634 CA LEU B 35 6223 7610 6437 211 745 538 C ATOM 2635 C LEU B 35 19.730 8.095 -31.080 1.00 56.93 C ANISOU 2635 C LEU B 35 6716 8189 6726 240 640 444 C ATOM 2636 O LEU B 35 19.542 7.380 -30.089 1.00 55.19 O ANISOU 2636 O LEU B 35 6510 7924 6535 194 545 312 O ATOM 2637 CB LEU B 35 20.353 10.502 -30.761 1.00 53.60 C ANISOU 2637 CB LEU B 35 6268 7523 6577 224 780 652 C ATOM 2638 CG LEU B 35 21.487 11.526 -30.620 1.00 79.46 C ANISOU 2638 CG LEU B 35 9493 10636 10062 177 882 725 C ATOM 2639 CD1 LEU B 35 20.999 12.833 -29.997 1.00 77.27 C ANISOU 2639 CD1 LEU B 35 9226 10199 9936 175 897 788 C ATOM 2640 CD2 LEU B 35 22.660 10.937 -29.818 1.00 82.03 C ANISOU 2640 CD2 LEU B 35 9774 10886 10508 91 844 580 C ATOM 2641 N SER B 36 18.997 8.028 -32.193 1.00 48.99 N ANISOU 2641 N SER B 36 5722 7344 5548 318 660 513 N ATOM 2642 CA SER B 36 17.910 7.065 -32.330 1.00 54.76 C ANISOU 2642 CA SER B 36 6474 8206 6127 345 564 415 C ATOM 2643 C SER B 36 18.389 5.623 -32.262 1.00 52.47 C ANISOU 2643 C SER B 36 6171 7960 5803 305 514 254 C ATOM 2644 O SER B 36 17.782 4.806 -31.572 1.00 51.59 O ANISOU 2644 O SER B 36 6076 7838 5690 272 421 134 O ATOM 2645 CB SER B 36 17.153 7.290 -33.625 1.00 54.16 C ANISOU 2645 CB SER B 36 6398 8314 5865 444 591 513 C ATOM 2646 OG SER B 36 16.544 8.553 -33.574 1.00 78.96 O ANISOU 2646 OG SER B 36 9552 11402 9045 489 623 660 O ATOM 2647 N TYR B 37 19.462 5.311 -32.987 1.00 44.57 N ANISOU 2647 N TYR B 37 5141 7008 4787 310 584 255 N ATOM 2648 CA TYR B 37 20.034 3.970 -32.946 1.00 43.80 C ANISOU 2648 CA TYR B 37 5026 6934 4680 278 546 102 C ATOM 2649 C TYR B 37 20.402 3.572 -31.512 1.00 48.19 C ANISOU 2649 C TYR B 37 5588 7327 5396 201 477 9 C ATOM 2650 O TYR B 37 20.211 2.425 -31.113 1.00 56.09 O ANISOU 2650 O TYR B 37 6595 8327 6388 177 402 -118 O ATOM 2651 CB TYR B 37 21.240 3.862 -33.868 1.00 49.69 C ANISOU 2651 CB TYR B 37 5731 7742 5409 298 648 127 C ATOM 2652 CG TYR B 37 20.884 3.919 -35.334 1.00 65.53 C ANISOU 2652 CG TYR B 37 7731 9953 7213 386 706 188 C ATOM 2653 CD1 TYR B 37 19.601 3.602 -35.771 1.00 70.94 C ANISOU 2653 CD1 TYR B 37 8440 10774 7739 435 635 152 C ATOM 2654 CD2 TYR B 37 21.834 4.267 -36.291 1.00 67.27 C ANISOU 2654 CD2 TYR B 37 7918 10246 7396 422 832 278 C ATOM 2655 CE1 TYR B 37 19.267 3.648 -37.127 1.00 68.14 C ANISOU 2655 CE1 TYR B 37 8078 10633 7179 527 677 200 C ATOM 2656 CE2 TYR B 37 21.514 4.310 -37.645 1.00 66.59 C ANISOU 2656 CE2 TYR B 37 7831 10373 7099 514 887 339 C ATOM 2657 CZ TYR B 37 20.230 3.999 -38.055 1.00 72.17 C ANISOU 2657 CZ TYR B 37 8563 11223 7635 569 803 296 C ATOM 2658 OH TYR B 37 19.909 4.034 -39.392 1.00 76.31 O ANISOU 2658 OH TYR B 37 9082 11980 7932 670 845 347 O ATOM 2659 N ARG B 38 20.894 4.530 -30.733 1.00 41.24 N ANISOU 2659 N ARG B 38 4702 6306 4659 165 500 73 N ATOM 2660 CA ARG B 38 21.214 4.288 -29.334 1.00 45.15 C ANISOU 2660 CA ARG B 38 5203 6665 5286 103 429 -8 C ATOM 2661 C ARG B 38 19.956 4.012 -28.526 1.00 51.63 C ANISOU 2661 C ARG B 38 6071 7476 6070 95 337 -56 C ATOM 2662 O ARG B 38 19.919 3.076 -27.731 1.00 55.93 O ANISOU 2662 O ARG B 38 6628 7987 6636 64 264 -154 O ATOM 2663 CB ARG B 38 21.951 5.484 -28.728 1.00 43.89 C ANISOU 2663 CB ARG B 38 5019 6371 5286 69 472 56 C ATOM 2664 CG ARG B 38 23.337 5.676 -29.266 1.00 44.11 C ANISOU 2664 CG ARG B 38 4984 6380 5394 57 560 87 C ATOM 2665 CD ARG B 38 24.065 6.829 -28.597 1.00 51.45 C ANISOU 2665 CD ARG B 38 5875 7162 6510 10 596 128 C ATOM 2666 NE ARG B 38 25.320 7.083 -29.298 1.00 57.93 N ANISOU 2666 NE ARG B 38 6624 7977 7409 -1 702 177 N ATOM 2667 CZ ARG B 38 26.497 6.607 -28.910 1.00 52.78 C ANISOU 2667 CZ ARG B 38 5910 7282 6861 -40 690 93 C ATOM 2668 NH1 ARG B 38 26.583 5.865 -27.812 1.00 50.70 N ANISOU 2668 NH1 ARG B 38 5656 6978 6630 -66 572 -33 N ATOM 2669 NH2 ARG B 38 27.585 6.869 -29.620 1.00 44.67 N ANISOU 2669 NH2 ARG B 38 4808 6258 5905 -49 800 144 N ATOM 2670 N GLN B 39 18.933 4.837 -28.722 1.00 44.40 N ANISOU 2670 N GLN B 39 5176 6588 5104 128 346 22 N ATOM 2671 CA GLN B 39 17.672 4.670 -28.005 1.00 47.50 C ANISOU 2671 CA GLN B 39 5604 6981 5464 125 271 -16 C ATOM 2672 C GLN B 39 16.996 3.341 -28.347 1.00 43.67 C ANISOU 2672 C GLN B 39 5122 6599 4872 129 216 -110 C ATOM 2673 O GLN B 39 16.391 2.707 -27.491 1.00 45.80 O ANISOU 2673 O GLN B 39 5410 6836 5154 97 150 -181 O ATOM 2674 CB GLN B 39 16.726 5.837 -28.275 1.00 45.24 C ANISOU 2674 CB GLN B 39 5328 6713 5149 172 298 90 C ATOM 2675 CG GLN B 39 16.994 7.086 -27.451 1.00 59.25 C ANISOU 2675 CG GLN B 39 7107 8343 7064 155 324 144 C ATOM 2676 CD GLN B 39 16.484 8.378 -28.122 1.00 66.26 C ANISOU 2676 CD GLN B 39 7993 9235 7949 216 390 286 C ATOM 2677 OE1 GLN B 39 16.207 8.405 -29.320 1.00 78.46 O ANISOU 2677 OE1 GLN B 39 9530 10899 9381 276 429 367 O ATOM 2678 NE2 GLN B 39 16.379 9.452 -27.343 1.00 54.37 N ANISOU 2678 NE2 GLN B 39 6493 7599 6568 207 403 316 N ATOM 2679 N GLN B 40 17.121 2.899 -29.588 1.00 45.42 N ANISOU 2679 N GLN B 40 5323 6943 4993 166 246 -117 N ATOM 2680 CA GLN B 40 16.490 1.638 -29.973 1.00 48.35 C ANISOU 2680 CA GLN B 40 5688 7407 5278 167 192 -229 C ATOM 2681 C GLN B 40 17.229 0.457 -29.362 1.00 48.66 C ANISOU 2681 C GLN B 40 5725 7367 5399 116 160 -339 C ATOM 2682 O GLN B 40 16.614 -0.509 -28.946 1.00 56.03 O ANISOU 2682 O GLN B 40 6664 8289 6336 88 102 -427 O ATOM 2683 CB GLN B 40 16.401 1.492 -31.488 1.00 49.19 C ANISOU 2683 CB GLN B 40 5767 7684 5239 229 227 -226 C ATOM 2684 CG GLN B 40 15.583 2.584 -32.177 1.00 62.64 C ANISOU 2684 CG GLN B 40 7472 9487 6842 298 252 -105 C ATOM 2685 CD GLN B 40 15.815 2.634 -33.686 1.00 76.88 C ANISOU 2685 CD GLN B 40 9252 11467 8492 373 307 -68 C ATOM 2686 OE1 GLN B 40 16.111 1.610 -34.325 1.00 73.90 O ANISOU 2686 OE1 GLN B 40 8854 11181 8045 377 298 -183 O ATOM 2687 NE2 GLN B 40 15.689 3.831 -34.262 1.00 78.30 N ANISOU 2687 NE2 GLN B 40 9436 11695 8619 438 368 95 N ATOM 2688 N ALA B 41 18.552 0.543 -29.297 1.00 41.85 N ANISOU 2688 N ALA B 41 4847 6444 4612 106 202 -327 N ATOM 2689 CA ALA B 41 19.335 -0.502 -28.660 1.00 38.28 C ANISOU 2689 CA ALA B 41 4388 5909 4248 70 169 -416 C ATOM 2690 C ALA B 41 18.994 -0.608 -27.172 1.00 47.10 C ANISOU 2690 C ALA B 41 5538 6911 5445 28 104 -425 C ATOM 2691 O ALA B 41 18.841 -1.712 -26.635 1.00 51.36 O ANISOU 2691 O ALA B 41 6088 7411 6016 5 55 -497 O ATOM 2692 CB ALA B 41 20.824 -0.253 -28.856 1.00 35.83 C ANISOU 2692 CB ALA B 41 4042 5561 4010 73 226 -395 C ATOM 2693 N ALA B 42 18.875 0.540 -26.512 1.00 44.02 N ANISOU 2693 N ALA B 42 5164 6471 5093 21 109 -349 N ATOM 2694 CA ALA B 42 18.508 0.564 -25.104 1.00 50.52 C ANISOU 2694 CA ALA B 42 6018 7209 5968 -10 53 -358 C ATOM 2695 C ALA B 42 17.104 -0.027 -24.889 1.00 49.77 C ANISOU 2695 C ALA B 42 5948 7152 5811 -17 13 -387 C ATOM 2696 O ALA B 42 16.884 -0.784 -23.941 1.00 43.57 O ANISOU 2696 O ALA B 42 5184 6315 5057 -44 -31 -423 O ATOM 2697 CB ALA B 42 18.601 1.975 -24.544 1.00 40.70 C ANISOU 2697 CB ALA B 42 4780 5911 4775 -11 70 -292 C ATOM 2698 N ASN B 43 16.168 0.297 -25.780 1.00 39.27 N ANISOU 2698 N ASN B 43 4610 5917 4396 10 31 -367 N ATOM 2699 CA ASN B 43 14.826 -0.282 -25.706 1.00 42.69 C ANISOU 2699 CA ASN B 43 5046 6397 4778 0 -5 -406 C ATOM 2700 C ASN B 43 14.802 -1.800 -25.876 1.00 41.45 C ANISOU 2700 C ASN B 43 4876 6241 4631 -26 -32 -505 C ATOM 2701 O ASN B 43 14.111 -2.518 -25.128 1.00 43.74 O ANISOU 2701 O ASN B 43 5176 6491 4953 -62 -64 -539 O ATOM 2702 CB ASN B 43 13.881 0.376 -26.714 1.00 52.14 C ANISOU 2702 CB ASN B 43 6222 7712 5878 45 11 -370 C ATOM 2703 CG ASN B 43 13.563 1.817 -26.357 1.00 75.61 C ANISOU 2703 CG ASN B 43 9208 10659 8860 72 33 -271 C ATOM 2704 OD1 ASN B 43 13.864 2.286 -25.250 1.00 80.08 O ANISOU 2704 OD1 ASN B 43 9799 11124 9505 49 30 -252 O ATOM 2705 ND2 ASN B 43 12.962 2.535 -27.301 1.00 86.18 N ANISOU 2705 ND2 ASN B 43 10529 12094 10122 128 55 -211 N ATOM 2706 N LEU B 44 15.551 -2.277 -26.862 1.00 35.49 N ANISOU 2706 N LEU B 44 4097 5530 3859 -8 -12 -550 N ATOM 2707 CA LEU B 44 15.709 -3.701 -27.098 1.00 40.62 C ANISOU 2707 CA LEU B 44 4730 6164 4539 -28 -31 -657 C ATOM 2708 C LEU B 44 16.366 -4.374 -25.883 1.00 45.43 C ANISOU 2708 C LEU B 44 5364 6635 5264 -61 -53 -660 C ATOM 2709 O LEU B 44 15.948 -5.454 -25.460 1.00 41.21 O ANISOU 2709 O LEU B 44 4832 6045 4781 -91 -79 -713 O ATOM 2710 CB LEU B 44 16.525 -3.955 -28.371 1.00 39.90 C ANISOU 2710 CB LEU B 44 4606 6150 4403 9 5 -708 C ATOM 2711 CG LEU B 44 16.772 -5.435 -28.710 1.00 50.56 C ANISOU 2711 CG LEU B 44 5933 7479 5799 -4 -11 -841 C ATOM 2712 CD1 LEU B 44 15.452 -6.166 -28.961 1.00 50.75 C ANISOU 2712 CD1 LEU B 44 5938 7546 5798 -29 -50 -931 C ATOM 2713 CD2 LEU B 44 17.696 -5.575 -29.896 1.00 43.14 C ANISOU 2713 CD2 LEU B 44 4960 6621 4810 40 34 -891 C ATOM 2714 N LEU B 45 17.373 -3.731 -25.301 1.00 41.02 N ANISOU 2714 N LEU B 45 4818 6020 4749 -52 -43 -600 N ATOM 2715 CA LEU B 45 17.981 -4.288 -24.098 1.00 38.37 C ANISOU 2715 CA LEU B 45 4503 5573 4503 -69 -76 -594 C ATOM 2716 C LEU B 45 16.977 -4.408 -22.961 1.00 39.89 C ANISOU 2716 C LEU B 45 4732 5727 4698 -97 -107 -563 C ATOM 2717 O LEU B 45 16.970 -5.399 -22.232 1.00 40.44 O ANISOU 2717 O LEU B 45 4817 5724 4822 -113 -130 -573 O ATOM 2718 CB LEU B 45 19.188 -3.476 -23.660 1.00 33.17 C ANISOU 2718 CB LEU B 45 3839 4877 3888 -55 -70 -548 C ATOM 2719 CG LEU B 45 20.355 -3.687 -24.634 1.00 39.53 C ANISOU 2719 CG LEU B 45 4599 5703 4719 -32 -33 -584 C ATOM 2720 CD1 LEU B 45 21.340 -2.543 -24.537 1.00 29.69 C ANISOU 2720 CD1 LEU B 45 3328 4445 3508 -24 -7 -532 C ATOM 2721 CD2 LEU B 45 21.039 -5.017 -24.375 1.00 32.69 C ANISOU 2721 CD2 LEU B 45 3721 4770 3930 -27 -59 -644 C ATOM 2722 N GLN B 46 16.122 -3.406 -22.821 1.00 40.58 N ANISOU 2722 N GLN B 46 4830 5859 4728 -97 -100 -519 N ATOM 2723 CA GLN B 46 15.152 -3.401 -21.741 1.00 41.85 C ANISOU 2723 CA GLN B 46 5021 5998 4884 -119 -117 -489 C ATOM 2724 C GLN B 46 14.099 -4.491 -21.991 1.00 36.71 C ANISOU 2724 C GLN B 46 4355 5356 4236 -150 -119 -536 C ATOM 2725 O GLN B 46 13.727 -5.224 -21.079 1.00 38.09 O ANISOU 2725 O GLN B 46 4549 5473 4452 -176 -127 -523 O ATOM 2726 CB GLN B 46 14.523 -2.009 -21.610 1.00 41.22 C ANISOU 2726 CB GLN B 46 4947 5963 4753 -104 -104 -441 C ATOM 2727 CG GLN B 46 13.555 -1.815 -20.431 1.00 32.78 C ANISOU 2727 CG GLN B 46 3904 4881 3669 -118 -113 -413 C ATOM 2728 CD GLN B 46 14.276 -1.591 -19.108 1.00 42.45 C ANISOU 2728 CD GLN B 46 5164 6046 4919 -114 -136 -388 C ATOM 2729 OE1 GLN B 46 15.335 -0.947 -19.043 1.00 45.07 O ANISOU 2729 OE1 GLN B 46 5494 6354 5278 -98 -144 -386 O ATOM 2730 NE2 GLN B 46 13.693 -2.107 -18.041 1.00 34.81 N ANISOU 2730 NE2 GLN B 46 4224 5063 3941 -129 -144 -371 N ATOM 2731 N ASP B 47 13.636 -4.605 -23.232 1.00 40.52 N ANISOU 2731 N ASP B 47 4799 5917 4680 -145 -110 -591 N ATOM 2732 CA ASP B 47 12.662 -5.635 -23.607 1.00 39.75 C ANISOU 2732 CA ASP B 47 4670 5834 4600 -179 -117 -664 C ATOM 2733 C ASP B 47 13.236 -7.038 -23.335 1.00 43.73 C ANISOU 2733 C ASP B 47 5176 6232 5206 -205 -121 -711 C ATOM 2734 O ASP B 47 12.649 -7.826 -22.600 1.00 47.92 O ANISOU 2734 O ASP B 47 5714 6693 5803 -245 -120 -706 O ATOM 2735 CB ASP B 47 12.270 -5.469 -25.085 1.00 39.77 C ANISOU 2735 CB ASP B 47 4624 5960 4526 -156 -117 -732 C ATOM 2736 CG ASP B 47 11.082 -6.365 -25.508 1.00 51.28 C ANISOU 2736 CG ASP B 47 6031 7454 5998 -194 -135 -828 C ATOM 2737 OD1 ASP B 47 10.349 -6.884 -24.641 1.00 47.33 O ANISOU 2737 OD1 ASP B 47 5531 6886 5565 -242 -135 -820 O ATOM 2738 OD2 ASP B 47 10.874 -6.531 -26.732 1.00 54.49 O ANISOU 2738 OD2 ASP B 47 6393 7966 6347 -174 -147 -915 O ATOM 2739 N MET B 48 14.408 -7.329 -23.894 1.00 44.91 N ANISOU 2739 N MET B 48 5320 6365 5377 -178 -119 -748 N ATOM 2740 CA MET B 48 15.071 -8.601 -23.637 1.00 38.00 C ANISOU 2740 CA MET B 48 4446 5380 4612 -188 -122 -788 C ATOM 2741 C MET B 48 15.339 -8.856 -22.162 1.00 43.33 C ANISOU 2741 C MET B 48 5167 5947 5348 -195 -132 -694 C ATOM 2742 O MET B 48 15.092 -9.951 -21.663 1.00 52.52 O ANISOU 2742 O MET B 48 6336 7016 6602 -220 -130 -696 O ATOM 2743 CB MET B 48 16.372 -8.693 -24.402 1.00 34.28 C ANISOU 2743 CB MET B 48 3957 4918 4151 -147 -114 -833 C ATOM 2744 CG MET B 48 16.189 -8.732 -25.887 1.00 41.05 C ANISOU 2744 CG MET B 48 4769 5885 4943 -133 -99 -937 C ATOM 2745 SD MET B 48 17.769 -9.041 -26.703 1.00 50.23 S ANISOU 2745 SD MET B 48 5905 7051 6129 -83 -73 -996 S ATOM 2746 CE MET B 48 18.555 -7.458 -26.411 1.00 71.39 C ANISOU 2746 CE MET B 48 8603 9774 8747 -53 -54 -868 C ATOM 2747 N GLY B 49 15.848 -7.851 -21.462 1.00 37.06 N ANISOU 2747 N GLY B 49 4403 5170 4507 -169 -143 -614 N ATOM 2748 CA GLY B 49 16.210 -8.035 -20.067 1.00 31.87 C ANISOU 2748 CA GLY B 49 3788 4439 3883 -161 -162 -532 C ATOM 2749 C GLY B 49 15.013 -8.409 -19.210 1.00 39.41 C ANISOU 2749 C GLY B 49 4766 5369 4839 -197 -150 -483 C ATOM 2750 O GLY B 49 15.105 -9.246 -18.305 1.00 41.85 O ANISOU 2750 O GLY B 49 5101 5596 5204 -198 -150 -428 O ATOM 2751 N GLN B 50 13.876 -7.790 -19.492 1.00 36.91 N ANISOU 2751 N GLN B 50 4435 5126 4462 -221 -133 -494 N ATOM 2752 CA GLN B 50 12.675 -8.074 -18.721 1.00 42.50 C ANISOU 2752 CA GLN B 50 5152 5822 5173 -258 -110 -451 C ATOM 2753 C GLN B 50 12.242 -9.499 -18.976 1.00 44.43 C ANISOU 2753 C GLN B 50 5369 5984 5526 -303 -89 -491 C ATOM 2754 O GLN B 50 11.950 -10.234 -18.039 1.00 43.32 O ANISOU 2754 O GLN B 50 5251 5767 5442 -323 -66 -423 O ATOM 2755 CB GLN B 50 11.565 -7.080 -19.053 1.00 38.77 C ANISOU 2755 CB GLN B 50 4656 5451 4624 -268 -98 -464 C ATOM 2756 CG GLN B 50 11.827 -5.714 -18.436 1.00 44.85 C ANISOU 2756 CG GLN B 50 5459 6269 5313 -229 -108 -411 C ATOM 2757 CD GLN B 50 11.055 -4.578 -19.099 1.00 49.98 C ANISOU 2757 CD GLN B 50 6080 7012 5897 -218 -101 -429 C ATOM 2758 OE1 GLN B 50 11.128 -3.436 -18.649 1.00 61.16 O ANISOU 2758 OE1 GLN B 50 7516 8456 7266 -189 -102 -395 O ATOM 2759 NE2 GLN B 50 10.316 -4.884 -20.163 1.00 43.11 N ANISOU 2759 NE2 GLN B 50 5159 6192 5028 -236 -96 -488 N ATOM 2760 N ARG B 51 12.244 -9.898 -20.245 1.00 40.13 N ANISOU 2760 N ARG B 51 4776 5456 5015 -315 -94 -601 N ATOM 2761 CA ARG B 51 11.864 -11.256 -20.614 1.00 38.61 C ANISOU 2761 CA ARG B 51 4547 5177 4946 -361 -78 -673 C ATOM 2762 C ARG B 51 12.815 -12.336 -20.099 1.00 48.61 C ANISOU 2762 C ARG B 51 5841 6300 6329 -346 -73 -639 C ATOM 2763 O ARG B 51 12.385 -13.461 -19.828 1.00 45.27 O ANISOU 2763 O ARG B 51 5405 5763 6032 -388 -44 -639 O ATOM 2764 CB ARG B 51 11.738 -11.378 -22.127 1.00 35.04 C ANISOU 2764 CB ARG B 51 4034 4795 4484 -366 -92 -821 C ATOM 2765 CG ARG B 51 10.700 -10.448 -22.713 1.00 42.94 C ANISOU 2765 CG ARG B 51 4999 5940 5377 -372 -101 -853 C ATOM 2766 CD ARG B 51 10.347 -10.848 -24.128 1.00 44.62 C ANISOU 2766 CD ARG B 51 5142 6227 5586 -381 -120 -1008 C ATOM 2767 NE ARG B 51 9.880 -9.703 -24.896 1.00 51.21 N ANISOU 2767 NE ARG B 51 5953 7228 6276 -346 -140 -1019 N ATOM 2768 CZ ARG B 51 9.120 -9.795 -25.981 1.00 50.44 C ANISOU 2768 CZ ARG B 51 5788 7244 6134 -350 -164 -1136 C ATOM 2769 NH1 ARG B 51 8.721 -10.983 -26.410 1.00 46.44 N ANISOU 2769 NH1 ARG B 51 5224 6693 5727 -400 -173 -1272 N ATOM 2770 NH2 ARG B 51 8.761 -8.697 -26.636 1.00 48.82 N ANISOU 2770 NH2 ARG B 51 5567 7192 5789 -302 -182 -1118 N ATOM 2771 N LEU B 52 14.103 -12.000 -19.989 1.00 44.84 N ANISOU 2771 N LEU B 52 5393 5823 5822 -286 -99 -610 N ATOM 2772 CA LEU B 52 15.106 -12.949 -19.523 1.00 42.15 C ANISOU 2772 CA LEU B 52 5072 5358 5586 -255 -104 -574 C ATOM 2773 C LEU B 52 15.086 -12.977 -18.009 1.00 44.67 C ANISOU 2773 C LEU B 52 5448 5632 5895 -239 -102 -420 C ATOM 2774 O LEU B 52 15.718 -13.817 -17.373 1.00 43.92 O ANISOU 2774 O LEU B 52 5375 5431 5882 -208 -103 -353 O ATOM 2775 CB LEU B 52 16.502 -12.563 -20.022 1.00 41.57 C ANISOU 2775 CB LEU B 52 4992 5316 5488 -194 -135 -610 C ATOM 2776 CG LEU B 52 16.822 -12.902 -21.483 1.00 43.81 C ANISOU 2776 CG LEU B 52 5222 5623 5803 -192 -127 -758 C ATOM 2777 CD1 LEU B 52 18.041 -12.117 -21.929 1.00 35.51 C ANISOU 2777 CD1 LEU B 52 4161 4643 4690 -137 -143 -771 C ATOM 2778 CD2 LEU B 52 17.046 -14.409 -21.648 1.00 41.21 C ANISOU 2778 CD2 LEU B 52 4872 5148 5638 -197 -113 -818 C ATOM 2779 N ASN B 53 14.357 -12.034 -17.435 1.00 43.38 N ANISOU 2779 N ASN B 53 5305 5557 5620 -251 -97 -364 N ATOM 2780 CA ASN B 53 14.317 -11.882 -15.995 1.00 43.07 C ANISOU 2780 CA ASN B 53 5320 5514 5532 -228 -95 -227 C ATOM 2781 C ASN B 53 15.675 -11.523 -15.373 1.00 44.23 C ANISOU 2781 C ASN B 53 5499 5673 5634 -153 -149 -177 C ATOM 2782 O ASN B 53 16.020 -12.008 -14.294 1.00 41.00 O ANISOU 2782 O ASN B 53 5128 5219 5230 -114 -157 -70 O ATOM 2783 CB ASN B 53 13.716 -13.130 -15.326 1.00 40.99 C ANISOU 2783 CB ASN B 53 5068 5133 5374 -257 -44 -145 C ATOM 2784 CG ASN B 53 13.235 -12.849 -13.916 1.00 41.71 C ANISOU 2784 CG ASN B 53 5210 5260 5378 -243 -21 -3 C ATOM 2785 OD1 ASN B 53 13.033 -11.692 -13.553 1.00 45.76 O ANISOU 2785 OD1 ASN B 53 5738 5891 5756 -228 -38 2 O ATOM 2786 ND2 ASN B 53 13.040 -13.896 -13.120 1.00 40.41 N ANISOU 2786 ND2 ASN B 53 5070 4994 5291 -245 24 113 N ATOM 2787 N VAL B 54 16.445 -10.666 -16.037 1.00 41.77 N ANISOU 2787 N VAL B 54 5165 5426 5279 -129 -185 -250 N ATOM 2788 CA VAL B 54 17.594 -10.048 -15.359 1.00 44.49 C ANISOU 2788 CA VAL B 54 5527 5805 5573 -68 -239 -214 C ATOM 2789 C VAL B 54 17.175 -8.749 -14.676 1.00 44.42 C ANISOU 2789 C VAL B 54 5542 5897 5439 -67 -251 -190 C ATOM 2790 O VAL B 54 16.076 -8.233 -14.921 1.00 41.54 O ANISOU 2790 O VAL B 54 5175 5580 5030 -107 -215 -208 O ATOM 2791 CB VAL B 54 18.750 -9.744 -16.306 1.00 42.45 C ANISOU 2791 CB VAL B 54 5224 5557 5347 -44 -265 -298 C ATOM 2792 CG1 VAL B 54 19.281 -11.034 -16.930 1.00 36.63 C ANISOU 2792 CG1 VAL B 54 4461 4720 4737 -33 -255 -336 C ATOM 2793 CG2 VAL B 54 18.317 -8.725 -17.367 1.00 37.39 C ANISOU 2793 CG2 VAL B 54 4555 4999 4655 -78 -241 -375 C ATOM 2794 N SER B 55 18.047 -8.226 -13.817 1.00 39.96 N ANISOU 2794 N SER B 55 4992 5367 4824 -16 -305 -161 N ATOM 2795 CA SER B 55 17.756 -6.988 -13.076 1.00 40.54 C ANISOU 2795 CA SER B 55 5085 5530 4789 -9 -321 -157 C ATOM 2796 C SER B 55 17.876 -5.730 -13.944 1.00 43.26 C ANISOU 2796 C SER B 55 5394 5920 5124 -28 -319 -242 C ATOM 2797 O SER B 55 18.480 -5.763 -15.017 1.00 44.07 O ANISOU 2797 O SER B 55 5456 6000 5290 -35 -315 -294 O ATOM 2798 CB SER B 55 18.691 -6.854 -11.870 1.00 40.21 C ANISOU 2798 CB SER B 55 5063 5520 4697 55 -390 -119 C ATOM 2799 OG SER B 55 20.029 -6.606 -12.289 1.00 55.77 O ANISOU 2799 OG SER B 55 6988 7480 6722 81 -441 -177 O ATOM 2800 N GLN B 56 17.317 -4.616 -13.474 1.00 44.83 N ANISOU 2800 N GLN B 56 5605 6180 5246 -32 -316 -250 N ATOM 2801 CA GLN B 56 17.519 -3.340 -14.158 1.00 37.56 C ANISOU 2801 CA GLN B 56 4653 5287 4331 -42 -312 -313 C ATOM 2802 C GLN B 56 19.010 -2.969 -14.158 1.00 42.35 C ANISOU 2802 C GLN B 56 5226 5880 4986 -17 -362 -351 C ATOM 2803 O GLN B 56 19.523 -2.419 -15.124 1.00 38.14 O ANISOU 2803 O GLN B 56 4651 5337 4505 -29 -346 -391 O ATOM 2804 CB GLN B 56 16.694 -2.221 -13.529 1.00 37.63 C ANISOU 2804 CB GLN B 56 4681 5349 4269 -43 -301 -320 C ATOM 2805 CG GLN B 56 16.794 -0.901 -14.295 1.00 40.88 C ANISOU 2805 CG GLN B 56 5060 5767 4707 -52 -285 -369 C ATOM 2806 CD GLN B 56 16.151 -0.981 -15.660 1.00 41.77 C ANISOU 2806 CD GLN B 56 5149 5881 4842 -77 -233 -366 C ATOM 2807 OE1 GLN B 56 14.949 -1.239 -15.783 1.00 42.46 O ANISOU 2807 OE1 GLN B 56 5245 5993 4895 -92 -201 -348 O ATOM 2808 NE2 GLN B 56 16.941 -0.755 -16.697 1.00 45.84 N ANISOU 2808 NE2 GLN B 56 5628 6379 5410 -78 -224 -387 N ATOM 2809 N LEU B 57 19.696 -3.291 -13.071 1.00 37.83 N ANISOU 2809 N LEU B 57 4666 5314 4394 22 -422 -334 N ATOM 2810 CA LEU B 57 21.134 -3.111 -12.997 1.00 43.13 C ANISOU 2810 CA LEU B 57 5292 5976 5120 49 -480 -374 C ATOM 2811 C LEU B 57 21.867 -3.788 -14.169 1.00 51.65 C ANISOU 2811 C LEU B 57 6325 7002 6296 43 -458 -389 C ATOM 2812 O LEU B 57 22.751 -3.194 -14.796 1.00 48.99 O ANISOU 2812 O LEU B 57 5932 6659 6023 37 -458 -439 O ATOM 2813 CB LEU B 57 21.675 -3.634 -11.657 1.00 38.68 C ANISOU 2813 CB LEU B 57 4748 5441 4508 105 -555 -341 C ATOM 2814 CG LEU B 57 23.203 -3.803 -11.613 1.00 50.80 C ANISOU 2814 CG LEU B 57 6223 6965 6112 143 -624 -376 C ATOM 2815 CD1 LEU B 57 23.894 -2.493 -11.956 1.00 48.34 C ANISOU 2815 CD1 LEU B 57 5847 6664 5855 117 -637 -471 C ATOM 2816 CD2 LEU B 57 23.665 -4.294 -10.261 1.00 40.97 C ANISOU 2816 CD2 LEU B 57 4999 5769 4800 212 -708 -336 C ATOM 2817 N THR B 58 21.508 -5.033 -14.459 1.00 46.78 N ANISOU 2817 N THR B 58 5729 6344 5700 45 -434 -349 N ATOM 2818 CA THR B 58 22.140 -5.756 -15.556 1.00 33.75 C ANISOU 2818 CA THR B 58 4038 4647 4139 45 -411 -378 C ATOM 2819 C THR B 58 21.826 -5.088 -16.887 1.00 40.22 C ANISOU 2819 C THR B 58 4829 5489 4965 6 -350 -427 C ATOM 2820 O THR B 58 22.718 -4.893 -17.720 1.00 39.12 O ANISOU 2820 O THR B 58 4636 5347 4880 10 -334 -468 O ATOM 2821 CB THR B 58 21.681 -7.212 -15.569 1.00 37.96 C ANISOU 2821 CB THR B 58 4599 5118 4706 51 -393 -338 C ATOM 2822 OG1 THR B 58 22.084 -7.827 -14.345 1.00 45.46 O ANISOU 2822 OG1 THR B 58 5574 6048 5649 101 -447 -270 O ATOM 2823 CG2 THR B 58 22.264 -7.975 -16.759 1.00 32.06 C ANISOU 2823 CG2 THR B 58 3806 4322 4053 53 -365 -393 C ATOM 2824 N ILE B 59 20.558 -4.730 -17.089 1.00 37.68 N ANISOU 2824 N ILE B 59 4538 5195 4583 -27 -311 -415 N ATOM 2825 CA ILE B 59 20.184 -4.000 -18.292 1.00 42.22 C ANISOU 2825 CA ILE B 59 5089 5809 5145 -50 -259 -444 C ATOM 2826 C ILE B 59 20.976 -2.681 -18.432 1.00 39.17 C ANISOU 2826 C ILE B 59 4666 5439 4776 -47 -257 -458 C ATOM 2827 O ILE B 59 21.472 -2.336 -19.514 1.00 34.14 O ANISOU 2827 O ILE B 59 3989 4816 4169 -49 -215 -476 O ATOM 2828 CB ILE B 59 18.689 -3.696 -18.303 1.00 36.85 C ANISOU 2828 CB ILE B 59 4440 5164 4397 -75 -231 -425 C ATOM 2829 CG1 ILE B 59 17.894 -4.985 -18.448 1.00 37.75 C ANISOU 2829 CG1 ILE B 59 4568 5256 4520 -93 -218 -426 C ATOM 2830 CG2 ILE B 59 18.335 -2.688 -19.423 1.00 28.84 C ANISOU 2830 CG2 ILE B 59 3400 4202 3355 -83 -186 -438 C ATOM 2831 CD1 ILE B 59 16.485 -4.855 -17.962 1.00 34.86 C ANISOU 2831 CD1 ILE B 59 4229 4915 4100 -117 -202 -396 C ATOM 2832 N ASN B 60 21.076 -1.948 -17.333 1.00 36.31 N ANISOU 2832 N ASN B 60 4318 5077 4400 -42 -296 -451 N ATOM 2833 CA ASN B 60 21.793 -0.681 -17.312 1.00 46.72 C ANISOU 2833 CA ASN B 60 5598 6393 5761 -46 -297 -476 C ATOM 2834 C ASN B 60 23.249 -0.880 -17.708 1.00 46.88 C ANISOU 2834 C ASN B 60 5554 6390 5870 -37 -307 -505 C ATOM 2835 O ASN B 60 23.794 -0.149 -18.532 1.00 44.16 O ANISOU 2835 O ASN B 60 5160 6040 5581 -51 -259 -514 O ATOM 2836 CB ASN B 60 21.691 -0.031 -15.926 1.00 37.18 C ANISOU 2836 CB ASN B 60 4412 5192 4524 -38 -353 -491 C ATOM 2837 CG ASN B 60 20.307 0.530 -15.647 1.00 43.40 C ANISOU 2837 CG ASN B 60 5247 6006 5239 -48 -326 -471 C ATOM 2838 OD1 ASN B 60 19.453 0.611 -16.543 1.00 40.83 O ANISOU 2838 OD1 ASN B 60 4929 5691 4893 -61 -269 -445 O ATOM 2839 ND2 ASN B 60 20.079 0.931 -14.401 1.00 44.72 N ANISOU 2839 ND2 ASN B 60 5439 6192 5358 -34 -369 -490 N ATOM 2840 N THR B 61 23.861 -1.902 -17.131 1.00 40.06 N ANISOU 2840 N THR B 61 4686 5512 5024 -9 -361 -511 N ATOM 2841 CA THR B 61 25.234 -2.211 -17.435 1.00 33.73 C ANISOU 2841 CA THR B 61 3815 4691 4311 9 -375 -543 C ATOM 2842 C THR B 61 25.395 -2.473 -18.929 1.00 40.42 C ANISOU 2842 C THR B 61 4629 5539 5188 0 -295 -550 C ATOM 2843 O THR B 61 26.328 -1.958 -19.573 1.00 41.52 O ANISOU 2843 O THR B 61 4700 5679 5397 -7 -259 -571 O ATOM 2844 CB THR B 61 25.739 -3.394 -16.598 1.00 40.11 C ANISOU 2844 CB THR B 61 4629 5482 5129 56 -447 -534 C ATOM 2845 OG1 THR B 61 25.906 -2.960 -15.245 1.00 48.04 O ANISOU 2845 OG1 THR B 61 5644 6510 6098 75 -528 -537 O ATOM 2846 CG2 THR B 61 27.088 -3.908 -17.123 1.00 35.15 C ANISOU 2846 CG2 THR B 61 3921 4832 4601 82 -452 -568 C ATOM 2847 N ALA B 62 24.493 -3.266 -19.490 1.00 38.74 N ANISOU 2847 N ALA B 62 4459 5334 4925 -1 -263 -537 N ATOM 2848 CA ALA B 62 24.568 -3.571 -20.924 1.00 44.86 C ANISOU 2848 CA ALA B 62 5206 6133 5705 -2 -192 -560 C ATOM 2849 C ALA B 62 24.397 -2.314 -21.773 1.00 46.15 C ANISOU 2849 C ALA B 62 5350 6341 5843 -23 -124 -539 C ATOM 2850 O ALA B 62 25.009 -2.194 -22.834 1.00 48.15 O ANISOU 2850 O ALA B 62 5555 6622 6117 -17 -63 -550 O ATOM 2851 CB ALA B 62 23.538 -4.629 -21.328 1.00 31.51 C ANISOU 2851 CB ALA B 62 3558 4446 3967 -4 -180 -571 C ATOM 2852 N ILE B 63 23.551 -1.395 -21.311 1.00 38.73 N ANISOU 2852 N ILE B 63 4448 5408 4859 -42 -130 -504 N ATOM 2853 CA ILE B 63 23.345 -0.121 -22.002 1.00 41.95 C ANISOU 2853 CA ILE B 63 4841 5840 5257 -54 -66 -466 C ATOM 2854 C ILE B 63 24.618 0.752 -22.053 1.00 46.05 C ANISOU 2854 C ILE B 63 5292 6325 5880 -65 -40 -467 C ATOM 2855 O ILE B 63 24.912 1.385 -23.079 1.00 44.58 O ANISOU 2855 O ILE B 63 5070 6159 5710 -67 41 -431 O ATOM 2856 CB ILE B 63 22.171 0.681 -21.389 1.00 42.10 C ANISOU 2856 CB ILE B 63 4911 5860 5226 -65 -80 -435 C ATOM 2857 CG1 ILE B 63 20.855 -0.088 -21.611 1.00 44.99 C ANISOU 2857 CG1 ILE B 63 5325 6270 5498 -61 -85 -431 C ATOM 2858 CG2 ILE B 63 22.112 2.095 -21.995 1.00 34.11 C ANISOU 2858 CG2 ILE B 63 3879 4847 4235 -71 -15 -386 C ATOM 2859 CD1 ILE B 63 19.619 0.612 -21.112 1.00 36.54 C ANISOU 2859 CD1 ILE B 63 4295 5213 4377 -66 -90 -402 C ATOM 2860 N VAL B 64 25.367 0.787 -20.953 1.00 30.94 N ANISOU 2860 N VAL B 64 3355 4366 4035 -70 -108 -505 N ATOM 2861 CA VAL B 64 26.632 1.507 -20.937 1.00 44.97 C ANISOU 2861 CA VAL B 64 5049 6107 5931 -86 -94 -525 C ATOM 2862 C VAL B 64 27.624 0.837 -21.901 1.00 48.89 C ANISOU 2862 C VAL B 64 5481 6623 6473 -72 -44 -537 C ATOM 2863 O VAL B 64 28.313 1.530 -22.663 1.00 50.24 O ANISOU 2863 O VAL B 64 5587 6790 6712 -88 36 -516 O ATOM 2864 CB VAL B 64 27.215 1.612 -19.507 1.00 48.52 C ANISOU 2864 CB VAL B 64 5477 6523 6435 -88 -195 -583 C ATOM 2865 CG1 VAL B 64 28.627 2.176 -19.533 1.00 42.79 C ANISOU 2865 CG1 VAL B 64 4643 5764 5850 -107 -189 -625 C ATOM 2866 CG2 VAL B 64 26.312 2.459 -18.632 1.00 45.31 C ANISOU 2866 CG2 VAL B 64 5123 6105 5987 -101 -228 -585 C ATOM 2867 N TYR B 65 27.667 -0.499 -21.893 1.00 37.74 N ANISOU 2867 N TYR B 65 4085 5227 5027 -39 -80 -566 N ATOM 2868 CA TYR B 65 28.512 -1.227 -22.831 1.00 43.62 C ANISOU 2868 CA TYR B 65 4772 5993 5808 -16 -30 -591 C ATOM 2869 C TYR B 65 28.210 -0.742 -24.239 1.00 43.94 C ANISOU 2869 C TYR B 65 4807 6091 5797 -21 84 -551 C ATOM 2870 O TYR B 65 29.115 -0.362 -24.994 1.00 48.02 O ANISOU 2870 O TYR B 65 5250 6624 6371 -23 162 -543 O ATOM 2871 CB TYR B 65 28.290 -2.746 -22.774 1.00 41.83 C ANISOU 2871 CB TYR B 65 4579 5766 5549 21 -72 -628 C ATOM 2872 CG TYR B 65 28.780 -3.425 -21.521 1.00 46.11 C ANISOU 2872 CG TYR B 65 5118 6259 6143 46 -174 -650 C ATOM 2873 CD1 TYR B 65 29.644 -2.777 -20.649 1.00 43.32 C ANISOU 2873 CD1 TYR B 65 4711 5886 5864 42 -229 -661 C ATOM 2874 CD2 TYR B 65 28.410 -4.737 -21.228 1.00 44.15 C ANISOU 2874 CD2 TYR B 65 4915 5985 5877 79 -216 -659 C ATOM 2875 CE1 TYR B 65 30.107 -3.404 -19.496 1.00 44.17 C ANISOU 2875 CE1 TYR B 65 4813 5971 6000 79 -332 -676 C ATOM 2876 CE2 TYR B 65 28.868 -5.377 -20.079 1.00 40.76 C ANISOU 2876 CE2 TYR B 65 4485 5513 5488 115 -307 -655 C ATOM 2877 CZ TYR B 65 29.714 -4.702 -19.212 1.00 46.00 C ANISOU 2877 CZ TYR B 65 5098 6180 6199 120 -369 -661 C ATOM 2878 OH TYR B 65 30.170 -5.314 -18.056 1.00 39.56 O ANISOU 2878 OH TYR B 65 4281 5346 5405 169 -468 -652 O ATOM 2879 N MET B 66 26.931 -0.778 -24.591 1.00 44.72 N ANISOU 2879 N MET B 66 4979 6230 5782 -19 94 -523 N ATOM 2880 CA MET B 66 26.483 -0.382 -25.920 1.00 44.45 C ANISOU 2880 CA MET B 66 4948 6274 5666 -9 189 -479 C ATOM 2881 C MET B 66 26.923 1.047 -26.239 1.00 43.73 C ANISOU 2881 C MET B 66 4816 6170 5629 -29 266 -403 C ATOM 2882 O MET B 66 27.488 1.307 -27.299 1.00 46.49 O ANISOU 2882 O MET B 66 5119 6568 5978 -17 363 -369 O ATOM 2883 CB MET B 66 24.962 -0.510 -26.032 1.00 37.18 C ANISOU 2883 CB MET B 66 4106 5397 4625 -4 167 -463 C ATOM 2884 CG MET B 66 24.375 -0.081 -27.391 1.00 53.88 C ANISOU 2884 CG MET B 66 6225 7616 6630 21 248 -415 C ATOM 2885 SD MET B 66 23.999 1.693 -27.511 1.00 52.42 S ANISOU 2885 SD MET B 66 6047 7420 6449 12 308 -290 S ATOM 2886 CE MET B 66 22.958 1.911 -26.054 1.00 41.95 C ANISOU 2886 CE MET B 66 4783 6021 5136 -14 209 -302 C ATOM 2887 N HIS B 67 26.676 1.962 -25.310 1.00 34.41 N ANISOU 2887 N HIS B 67 3652 4921 4503 -59 228 -378 N ATOM 2888 CA HIS B 67 27.017 3.361 -25.505 1.00 40.94 C ANISOU 2888 CA HIS B 67 4440 5705 5412 -85 300 -310 C ATOM 2889 C HIS B 67 28.498 3.512 -25.777 1.00 48.54 C ANISOU 2889 C HIS B 67 5300 6640 6501 -102 354 -322 C ATOM 2890 O HIS B 67 28.898 4.204 -26.712 1.00 45.95 O ANISOU 2890 O HIS B 67 4928 6325 6204 -106 469 -248 O ATOM 2891 CB HIS B 67 26.665 4.193 -24.271 1.00 39.11 C ANISOU 2891 CB HIS B 67 4230 5388 5243 -115 234 -322 C ATOM 2892 CG HIS B 67 25.276 4.736 -24.283 1.00 45.07 C ANISOU 2892 CG HIS B 67 5059 6156 5911 -103 236 -268 C ATOM 2893 ND1 HIS B 67 24.746 5.392 -25.372 1.00 54.30 N ANISOU 2893 ND1 HIS B 67 6240 7364 7029 -82 329 -169 N ATOM 2894 CD2 HIS B 67 24.312 4.739 -23.331 1.00 46.64 C ANISOU 2894 CD2 HIS B 67 5318 6340 6062 -103 160 -295 C ATOM 2895 CE1 HIS B 67 23.509 5.763 -25.097 1.00 48.95 C ANISOU 2895 CE1 HIS B 67 5623 6692 6285 -68 302 -143 C ATOM 2896 NE2 HIS B 67 23.223 5.381 -23.864 1.00 46.41 N ANISOU 2896 NE2 HIS B 67 5330 6336 5967 -83 205 -222 N ATOM 2897 N ARG B 68 29.307 2.874 -24.940 1.00 48.37 N ANISOU 2897 N ARG B 68 5238 6584 6558 -109 275 -410 N ATOM 2898 CA ARG B 68 30.753 2.925 -25.096 1.00 39.76 C ANISOU 2898 CA ARG B 68 4035 5470 5602 -124 313 -439 C ATOM 2899 C ARG B 68 31.205 2.246 -26.377 1.00 49.42 C ANISOU 2899 C ARG B 68 5224 6774 6778 -89 407 -426 C ATOM 2900 O ARG B 68 32.048 2.776 -27.110 1.00 50.99 O ANISOU 2900 O ARG B 68 5341 6981 7053 -103 516 -386 O ATOM 2901 CB ARG B 68 31.432 2.308 -23.881 1.00 36.93 C ANISOU 2901 CB ARG B 68 3640 5073 5317 -122 189 -536 C ATOM 2902 CG ARG B 68 31.398 3.232 -22.677 1.00 42.10 C ANISOU 2902 CG ARG B 68 4290 5657 6050 -161 113 -565 C ATOM 2903 CD ARG B 68 32.021 2.595 -21.461 1.00 41.53 C ANISOU 2903 CD ARG B 68 4186 5574 6020 -145 -20 -656 C ATOM 2904 NE ARG B 68 32.012 3.512 -20.333 1.00 42.51 N ANISOU 2904 NE ARG B 68 4297 5648 6205 -178 -95 -704 N ATOM 2905 CZ ARG B 68 32.523 3.222 -19.143 1.00 46.62 C ANISOU 2905 CZ ARG B 68 4787 6172 6753 -163 -221 -787 C ATOM 2906 NH1 ARG B 68 33.089 2.045 -18.942 1.00 45.09 N ANISOU 2906 NH1 ARG B 68 4573 6017 6544 -112 -282 -812 N ATOM 2907 NH2 ARG B 68 32.476 4.106 -18.162 1.00 46.73 N ANISOU 2907 NH2 ARG B 68 4788 6155 6811 -191 -287 -847 N ATOM 2908 N PHE B 69 30.637 1.077 -26.653 1.00 52.00 N ANISOU 2908 N PHE B 69 5610 7164 6985 -45 373 -464 N ATOM 2909 CA PHE B 69 30.979 0.334 -27.858 1.00 43.12 C ANISOU 2909 CA PHE B 69 4458 6126 5801 -5 454 -480 C ATOM 2910 C PHE B 69 30.847 1.212 -29.099 1.00 46.79 C ANISOU 2910 C PHE B 69 4912 6662 6205 -1 594 -379 C ATOM 2911 O PHE B 69 31.665 1.138 -30.014 1.00 48.83 O ANISOU 2911 O PHE B 69 5102 6978 6475 17 697 -370 O ATOM 2912 CB PHE B 69 30.083 -0.889 -27.977 1.00 37.27 C ANISOU 2912 CB PHE B 69 3793 5430 4937 34 395 -538 C ATOM 2913 CG PHE B 69 30.367 -1.742 -29.171 1.00 39.18 C ANISOU 2913 CG PHE B 69 4008 5764 5113 80 466 -587 C ATOM 2914 CD1 PHE B 69 31.355 -2.719 -29.125 1.00 43.09 C ANISOU 2914 CD1 PHE B 69 4441 6242 5690 107 454 -674 C ATOM 2915 CD2 PHE B 69 29.635 -1.586 -30.339 1.00 47.67 C ANISOU 2915 CD2 PHE B 69 5120 6953 6041 105 540 -553 C ATOM 2916 CE1 PHE B 69 31.615 -3.532 -30.229 1.00 45.01 C ANISOU 2916 CE1 PHE B 69 4657 6570 5874 155 522 -739 C ATOM 2917 CE2 PHE B 69 29.882 -2.395 -31.451 1.00 54.45 C ANISOU 2917 CE2 PHE B 69 5952 7914 6822 153 603 -619 C ATOM 2918 CZ PHE B 69 30.872 -3.373 -31.394 1.00 49.85 C ANISOU 2918 CZ PHE B 69 5308 7305 6328 177 596 -718 C ATOM 2919 N TYR B 70 29.826 2.061 -29.130 1.00 44.39 N ANISOU 2919 N TYR B 70 4674 6357 5835 -11 602 -297 N ATOM 2920 CA TYR B 70 29.617 2.902 -30.309 1.00 47.44 C ANISOU 2920 CA TYR B 70 5059 6816 6151 6 733 -178 C ATOM 2921 C TYR B 70 30.385 4.233 -30.314 1.00 48.27 C ANISOU 2921 C TYR B 70 5094 6841 6407 -38 828 -81 C ATOM 2922 O TYR B 70 30.244 5.021 -31.238 1.00 52.75 O ANISOU 2922 O TYR B 70 5659 7451 6932 -22 947 45 O ATOM 2923 CB TYR B 70 28.130 3.101 -30.580 1.00 42.13 C ANISOU 2923 CB TYR B 70 4483 6201 5324 34 708 -126 C ATOM 2924 CG TYR B 70 27.463 1.843 -31.086 1.00 46.27 C ANISOU 2924 CG TYR B 70 5052 6837 5692 80 662 -210 C ATOM 2925 CD1 TYR B 70 27.763 1.335 -32.341 1.00 46.10 C ANISOU 2925 CD1 TYR B 70 5003 6947 5564 129 744 -223 C ATOM 2926 CD2 TYR B 70 26.543 1.153 -30.303 1.00 41.08 C ANISOU 2926 CD2 TYR B 70 4457 6152 5000 74 542 -285 C ATOM 2927 CE1 TYR B 70 27.154 0.181 -32.806 1.00 48.38 C ANISOU 2927 CE1 TYR B 70 5325 7332 5725 168 698 -327 C ATOM 2928 CE2 TYR B 70 25.934 0.006 -30.758 1.00 36.55 C ANISOU 2928 CE2 TYR B 70 3914 5662 4313 106 504 -373 C ATOM 2929 CZ TYR B 70 26.234 -0.471 -32.011 1.00 44.88 C ANISOU 2929 CZ TYR B 70 4939 6841 5272 152 577 -402 C ATOM 2930 OH TYR B 70 25.628 -1.613 -32.473 1.00 47.97 O ANISOU 2930 OH TYR B 70 5352 7310 5562 181 535 -513 O ATOM 2931 N MET B 71 31.206 4.474 -29.296 1.00 47.97 N ANISOU 2931 N MET B 71 4993 6686 6548 -91 777 -138 N ATOM 2932 CA MET B 71 32.203 5.534 -29.385 1.00 52.90 C ANISOU 2932 CA MET B 71 5517 7232 7349 -140 876 -78 C ATOM 2933 C MET B 71 33.447 5.037 -30.138 1.00 52.74 C ANISOU 2933 C MET B 71 5392 7270 7375 -130 971 -96 C ATOM 2934 O MET B 71 34.312 5.820 -30.506 1.00 60.96 O ANISOU 2934 O MET B 71 6339 8271 8551 -166 1088 -31 O ATOM 2935 CB MET B 71 32.585 6.054 -28.001 1.00 54.91 C ANISOU 2935 CB MET B 71 5732 7350 7783 -202 778 -151 C ATOM 2936 CG MET B 71 31.486 6.841 -27.298 1.00 60.27 C ANISOU 2936 CG MET B 71 6494 7959 8448 -218 717 -125 C ATOM 2937 SD MET B 71 30.625 7.987 -28.397 1.00 61.02 S ANISOU 2937 SD MET B 71 6640 8064 8482 -198 859 61 S ATOM 2938 CE MET B 71 31.977 9.009 -29.035 1.00 37.01 C ANISOU 2938 CE MET B 71 3465 4945 5653 -251 1031 152 C ATOM 2939 N ILE B 72 33.515 3.730 -30.371 1.00 51.31 N ANISOU 2939 N ILE B 72 5225 7178 7093 -80 926 -187 N ATOM 2940 CA ILE B 72 34.649 3.108 -31.046 1.00 53.29 C ANISOU 2940 CA ILE B 72 5378 7491 7379 -57 1007 -228 C ATOM 2941 C ILE B 72 34.230 2.495 -32.380 1.00 56.86 C ANISOU 2941 C ILE B 72 5873 8101 7630 13 1094 -204 C ATOM 2942 O ILE B 72 34.926 2.640 -33.374 1.00 60.68 O ANISOU 2942 O ILE B 72 6288 8662 8106 32 1238 -154 O ATOM 2943 CB ILE B 72 35.280 1.992 -30.184 1.00 49.54 C ANISOU 2943 CB ILE B 72 4862 6982 6980 -47 882 -377 C ATOM 2944 CG1 ILE B 72 35.663 2.524 -28.803 1.00 46.63 C ANISOU 2944 CG1 ILE B 72 4452 6484 6782 -105 774 -418 C ATOM 2945 CG2 ILE B 72 36.496 1.436 -30.870 1.00 49.05 C ANISOU 2945 CG2 ILE B 72 4685 6977 6976 -21 972 -421 C ATOM 2946 CD1 ILE B 72 36.547 3.742 -28.869 1.00 47.96 C ANISOU 2946 CD1 ILE B 72 4506 6585 7131 -170 872 -361 C ATOM 2947 N GLN B 73 33.090 1.811 -32.393 1.00 51.98 N ANISOU 2947 N GLN B 73 5363 7538 6850 53 1008 -247 N ATOM 2948 CA GLN B 73 32.579 1.184 -33.608 1.00 51.87 C ANISOU 2948 CA GLN B 73 5390 7683 6634 121 1066 -254 C ATOM 2949 C GLN B 73 31.410 1.971 -34.222 1.00 57.73 C ANISOU 2949 C GLN B 73 6215 8498 7221 142 1106 -129 C ATOM 2950 O GLN B 73 30.827 2.852 -33.589 1.00 62.94 O ANISOU 2950 O GLN B 73 6916 9068 7929 105 1067 -52 O ATOM 2951 CB GLN B 73 32.135 -0.249 -33.307 1.00 47.87 C ANISOU 2951 CB GLN B 73 4930 7194 6063 154 945 -407 C ATOM 2952 CG GLN B 73 33.132 -1.038 -32.468 1.00 55.46 C ANISOU 2952 CG GLN B 73 5825 8062 7188 142 876 -519 C ATOM 2953 CD GLN B 73 34.436 -1.310 -33.199 1.00 57.11 C ANISOU 2953 CD GLN B 73 5920 8324 7456 169 989 -552 C ATOM 2954 OE1 GLN B 73 34.568 -1.039 -34.390 1.00 55.41 O ANISOU 2954 OE1 GLN B 73 5683 8231 7140 200 1124 -500 O ATOM 2955 NE2 GLN B 73 35.399 -1.861 -32.486 1.00 60.16 N ANISOU 2955 NE2 GLN B 73 6229 8629 7999 164 934 -636 N ATOM 2956 N SER B 74 31.067 1.634 -35.457 1.00 52.98 N ANISOU 2956 N SER B 74 5635 8066 6429 209 1178 -117 N ATOM 2957 CA SER B 74 30.011 2.325 -36.180 1.00 56.04 C ANISOU 2957 CA SER B 74 6090 8554 6648 248 1218 7 C ATOM 2958 C SER B 74 28.737 1.483 -36.274 1.00 54.66 C ANISOU 2958 C SER B 74 5998 8465 6304 287 1102 -92 C ATOM 2959 O SER B 74 28.791 0.262 -36.454 1.00 54.49 O ANISOU 2959 O SER B 74 5971 8500 6231 312 1054 -247 O ATOM 2960 CB SER B 74 30.497 2.663 -37.588 1.00 58.43 C ANISOU 2960 CB SER B 74 6353 9018 6832 306 1390 108 C ATOM 2961 OG SER B 74 29.435 3.132 -38.400 1.00 60.59 O ANISOU 2961 OG SER B 74 6694 9426 6902 368 1416 216 O ATOM 2962 N PHE B 75 27.589 2.143 -36.155 1.00 56.21 N ANISOU 2962 N PHE B 75 6263 8665 6430 293 1060 -6 N ATOM 2963 CA PHE B 75 26.302 1.486 -36.373 1.00 55.21 C ANISOU 2963 CA PHE B 75 6201 8638 6138 331 963 -84 C ATOM 2964 C PHE B 75 26.216 0.916 -37.792 1.00 59.62 C ANISOU 2964 C PHE B 75 6749 9418 6484 413 1024 -127 C ATOM 2965 O PHE B 75 25.518 -0.067 -38.037 1.00 65.27 O ANISOU 2965 O PHE B 75 7488 10221 7090 439 942 -269 O ATOM 2966 CB PHE B 75 25.147 2.449 -36.106 1.00 46.73 C ANISOU 2966 CB PHE B 75 5186 7542 5027 333 927 35 C ATOM 2967 CG PHE B 75 24.783 2.581 -34.643 1.00 50.06 C ANISOU 2967 CG PHE B 75 5637 7782 5602 264 818 3 C ATOM 2968 CD1 PHE B 75 24.049 1.583 -34.001 1.00 43.26 C ANISOU 2968 CD1 PHE B 75 4811 6900 4726 246 691 -135 C ATOM 2969 CD2 PHE B 75 25.152 3.710 -33.917 1.00 46.17 C ANISOU 2969 CD2 PHE B 75 5133 7142 5267 218 847 108 C ATOM 2970 CE1 PHE B 75 23.711 1.698 -32.658 1.00 41.83 C ANISOU 2970 CE1 PHE B 75 4658 6570 4665 191 601 -156 C ATOM 2971 CE2 PHE B 75 24.819 3.836 -32.575 1.00 47.88 C ANISOU 2971 CE2 PHE B 75 5376 7212 5604 163 747 65 C ATOM 2972 CZ PHE B 75 24.086 2.828 -31.942 1.00 45.26 C ANISOU 2972 CZ PHE B 75 5084 6878 5234 153 626 -60 C ATOM 2973 N THR B 76 26.935 1.531 -38.724 1.00 56.71 N ANISOU 2973 N THR B 76 6341 9145 6061 453 1171 -9 N ATOM 2974 CA THR B 76 26.960 1.044 -40.103 1.00 65.09 C ANISOU 2974 CA THR B 76 7388 10441 6903 540 1242 -47 C ATOM 2975 C THR B 76 27.652 -0.316 -40.229 1.00 63.80 C ANISOU 2975 C THR B 76 7179 10303 6758 544 1225 -259 C ATOM 2976 O THR B 76 27.384 -1.061 -41.160 1.00 70.07 O ANISOU 2976 O THR B 76 7973 11279 7372 611 1227 -372 O ATOM 2977 CB THR B 76 27.621 2.063 -41.080 1.00 67.72 C ANISOU 2977 CB THR B 76 7686 10875 7167 588 1426 155 C ATOM 2978 OG1 THR B 76 29.049 2.053 -40.915 1.00 67.12 O ANISOU 2978 OG1 THR B 76 7531 10711 7259 546 1526 153 O ATOM 2979 CG2 THR B 76 27.076 3.478 -40.849 1.00 62.37 C ANISOU 2979 CG2 THR B 76 7046 10123 6527 580 1455 380 C ATOM 2980 N ARG B 77 28.544 -0.638 -39.301 1.00 63.02 N ANISOU 2980 N ARG B 77 7040 10026 6880 479 1204 -321 N ATOM 2981 CA ARG B 77 29.213 -1.932 -39.337 1.00 59.15 C ANISOU 2981 CA ARG B 77 6504 9536 6435 488 1183 -517 C ATOM 2982 C ARG B 77 28.596 -2.942 -38.363 1.00 63.48 C ANISOU 2982 C ARG B 77 7092 9960 7070 449 1020 -673 C ATOM 2983 O ARG B 77 28.498 -4.131 -38.674 1.00 60.20 O ANISOU 2983 O ARG B 77 6669 9591 6614 478 978 -851 O ATOM 2984 CB ARG B 77 30.709 -1.782 -39.071 1.00 61.40 C ANISOU 2984 CB ARG B 77 6701 9728 6901 459 1274 -493 C ATOM 2985 CG ARG B 77 31.445 -3.114 -39.005 1.00 72.17 C ANISOU 2985 CG ARG B 77 8012 11069 8339 475 1248 -691 C ATOM 2986 CD ARG B 77 32.879 -3.006 -39.491 1.00 93.01 C ANISOU 2986 CD ARG B 77 10546 13742 11050 493 1392 -674 C ATOM 2987 NE ARG B 77 33.639 -4.228 -39.230 1.00109.66 N ANISOU 2987 NE ARG B 77 12598 15794 13275 507 1356 -858 N ATOM 2988 CZ ARG B 77 33.390 -5.407 -39.797 1.00118.40 C ANISOU 2988 CZ ARG B 77 13713 16987 14287 565 1328 -1040 C ATOM 2989 NH1 ARG B 77 32.393 -5.538 -40.662 1.00118.26 N ANISOU 2989 NH1 ARG B 77 13755 17134 14045 611 1324 -1075 N ATOM 2990 NH2 ARG B 77 34.137 -6.461 -39.494 1.00121.61 N ANISOU 2990 NH2 ARG B 77 14062 17313 14830 580 1300 -1193 N ATOM 2991 N PHE B 78 28.186 -2.473 -37.186 1.00 56.44 N ANISOU 2991 N PHE B 78 6237 8905 6301 385 935 -607 N ATOM 2992 CA PHE B 78 27.528 -3.341 -36.216 1.00 52.45 C ANISOU 2992 CA PHE B 78 5774 8284 5871 348 792 -722 C ATOM 2993 C PHE B 78 26.140 -2.814 -35.856 1.00 56.70 C ANISOU 2993 C PHE B 78 6386 8820 6339 329 716 -656 C ATOM 2994 O PHE B 78 26.008 -1.867 -35.074 1.00 53.95 O ANISOU 2994 O PHE B 78 6057 8370 6070 289 702 -535 O ATOM 2995 CB PHE B 78 28.368 -3.484 -34.942 1.00 52.90 C ANISOU 2995 CB PHE B 78 5803 8147 6149 294 745 -730 C ATOM 2996 CG PHE B 78 29.786 -3.966 -35.181 1.00 54.65 C ANISOU 2996 CG PHE B 78 5939 8358 6467 314 814 -792 C ATOM 2997 CD1 PHE B 78 30.108 -5.307 -35.051 1.00 53.63 C ANISOU 2997 CD1 PHE B 78 5789 8189 6399 334 765 -952 C ATOM 2998 CD2 PHE B 78 30.794 -3.071 -35.509 1.00 54.60 C ANISOU 2998 CD2 PHE B 78 5866 8370 6509 311 930 -688 C ATOM 2999 CE1 PHE B 78 31.405 -5.749 -35.253 1.00 61.89 C ANISOU 2999 CE1 PHE B 78 6748 9224 7542 361 827 -1012 C ATOM 3000 CE2 PHE B 78 32.092 -3.500 -35.709 1.00 59.41 C ANISOU 3000 CE2 PHE B 78 6383 8973 7216 329 996 -747 C ATOM 3001 CZ PHE B 78 32.401 -4.842 -35.581 1.00 63.69 C ANISOU 3001 CZ PHE B 78 6905 9485 7809 358 941 -911 C ATOM 3002 N PRO B 79 25.094 -3.442 -36.413 1.00 56.66 N ANISOU 3002 N PRO B 79 6410 8925 6194 359 663 -750 N ATOM 3003 CA PRO B 79 23.700 -3.074 -36.123 1.00 53.99 C ANISOU 3003 CA PRO B 79 6128 8598 5787 346 585 -709 C ATOM 3004 C PRO B 79 23.357 -3.243 -34.644 1.00 50.76 C ANISOU 3004 C PRO B 79 5752 7998 5536 276 488 -715 C ATOM 3005 O PRO B 79 23.776 -4.218 -34.005 1.00 43.20 O ANISOU 3005 O PRO B 79 4785 6932 4699 249 441 -819 O ATOM 3006 CB PRO B 79 22.880 -4.067 -36.959 1.00 50.25 C ANISOU 3006 CB PRO B 79 5654 8268 5172 385 539 -868 C ATOM 3007 CG PRO B 79 23.865 -4.662 -37.945 1.00 54.26 C ANISOU 3007 CG PRO B 79 6110 8879 5626 436 620 -962 C ATOM 3008 CD PRO B 79 25.196 -4.617 -37.292 1.00 52.65 C ANISOU 3008 CD PRO B 79 5874 8528 5602 405 669 -926 C ATOM 3009 N GLY B 80 22.586 -2.299 -34.110 1.00 53.08 N ANISOU 3009 N GLY B 80 6084 8257 5826 256 460 -600 N ATOM 3010 CA GLY B 80 22.139 -2.385 -32.733 1.00 50.81 C ANISOU 3010 CA GLY B 80 5831 7816 5658 198 374 -602 C ATOM 3011 C GLY B 80 21.497 -3.723 -32.417 1.00 52.73 C ANISOU 3011 C GLY B 80 6086 8029 5918 178 289 -747 C ATOM 3012 O GLY B 80 21.712 -4.267 -31.332 1.00 59.11 O ANISOU 3012 O GLY B 80 6906 8698 6854 137 237 -778 O ATOM 3013 N ASN B 81 20.722 -4.260 -33.361 1.00 46.32 N ANISOU 3013 N ASN B 81 5267 7351 4981 208 277 -835 N ATOM 3014 CA ASN B 81 19.984 -5.506 -33.139 1.00 47.31 C ANISOU 3014 CA ASN B 81 5394 7443 5136 181 201 -981 C ATOM 3015 C ASN B 81 20.888 -6.719 -32.963 1.00 51.02 C ANISOU 3015 C ASN B 81 5841 7820 5726 172 200 -1101 C ATOM 3016 O ASN B 81 20.459 -7.755 -32.481 1.00 54.49 O ANISOU 3016 O ASN B 81 6284 8170 6249 139 144 -1198 O ATOM 3017 CB ASN B 81 18.989 -5.754 -34.271 1.00 56.41 C ANISOU 3017 CB ASN B 81 6529 8774 6129 217 184 -1069 C ATOM 3018 CG ASN B 81 17.828 -4.771 -34.259 1.00 55.84 C ANISOU 3018 CG ASN B 81 6479 8776 5963 225 158 -965 C ATOM 3019 OD1 ASN B 81 17.653 -3.992 -33.323 1.00 59.19 O ANISOU 3019 OD1 ASN B 81 6935 9102 6453 197 151 -843 O ATOM 3020 ND2 ASN B 81 17.033 -4.807 -35.303 1.00 53.86 N ANISOU 3020 ND2 ASN B 81 6204 8706 5555 271 142 -1021 N ATOM 3021 N SER B 82 22.147 -6.578 -33.349 1.00 51.01 N ANISOU 3021 N SER B 82 5809 7831 5743 203 268 -1087 N ATOM 3022 CA SER B 82 23.142 -7.620 -33.114 1.00 53.10 C ANISOU 3022 CA SER B 82 6042 7995 6137 205 271 -1184 C ATOM 3023 C SER B 82 23.959 -7.368 -31.851 1.00 53.54 C ANISOU 3023 C SER B 82 6105 7891 6347 176 254 -1094 C ATOM 3024 O SER B 82 24.277 -8.293 -31.118 1.00 65.17 O ANISOU 3024 O SER B 82 7577 9236 7949 164 211 -1148 O ATOM 3025 CB SER B 82 24.076 -7.740 -34.316 1.00 51.90 C ANISOU 3025 CB SER B 82 5837 7964 5918 264 358 -1246 C ATOM 3026 OG SER B 82 23.385 -8.334 -35.401 1.00 67.97 O ANISOU 3026 OG SER B 82 7861 10141 7824 296 355 -1381 O ATOM 3027 N VAL B 83 24.291 -6.114 -31.589 1.00 53.41 N ANISOU 3027 N VAL B 83 6092 7881 6320 169 287 -957 N ATOM 3028 CA VAL B 83 25.145 -5.797 -30.454 1.00 51.11 C ANISOU 3028 CA VAL B 83 5793 7459 6167 145 267 -890 C ATOM 3029 C VAL B 83 24.401 -5.941 -29.122 1.00 45.23 C ANISOU 3029 C VAL B 83 5103 6603 5481 104 176 -860 C ATOM 3030 O VAL B 83 24.960 -6.441 -28.134 1.00 50.21 O ANISOU 3030 O VAL B 83 5730 7120 6226 96 129 -866 O ATOM 3031 CB VAL B 83 25.804 -4.401 -30.620 1.00 53.54 C ANISOU 3031 CB VAL B 83 6075 7799 6470 144 336 -770 C ATOM 3032 CG1 VAL B 83 26.578 -3.999 -29.381 1.00 49.75 C ANISOU 3032 CG1 VAL B 83 5579 7191 6132 113 299 -719 C ATOM 3033 CG2 VAL B 83 26.742 -4.417 -31.814 1.00 55.87 C ANISOU 3033 CG2 VAL B 83 6307 8193 6730 186 438 -794 C ATOM 3034 N ALA B 84 23.140 -5.527 -29.099 1.00 42.61 N ANISOU 3034 N ALA B 84 4815 6312 5062 85 154 -826 N ATOM 3035 CA ALA B 84 22.349 -5.564 -27.865 1.00 44.50 C ANISOU 3035 CA ALA B 84 5104 6463 5341 47 83 -790 C ATOM 3036 C ALA B 84 22.348 -6.956 -27.221 1.00 49.06 C ANISOU 3036 C ALA B 84 5691 6939 6012 37 31 -862 C ATOM 3037 O ALA B 84 22.735 -7.109 -26.064 1.00 46.21 O ANISOU 3037 O ALA B 84 5345 6477 5736 28 -11 -822 O ATOM 3038 CB ALA B 84 20.923 -5.079 -28.123 1.00 39.83 C ANISOU 3038 CB ALA B 84 4544 5946 4643 35 73 -764 C ATOM 3039 N PRO B 85 21.915 -7.985 -27.970 1.00 48.75 N ANISOU 3039 N PRO B 85 5638 6924 5959 43 35 -971 N ATOM 3040 CA PRO B 85 21.932 -9.330 -27.383 1.00 49.31 C ANISOU 3040 CA PRO B 85 5714 6873 6147 33 -3 -1033 C ATOM 3041 C PRO B 85 23.325 -9.742 -26.856 1.00 46.87 C ANISOU 3041 C PRO B 85 5381 6470 5955 65 -7 -1024 C ATOM 3042 O PRO B 85 23.435 -10.254 -25.740 1.00 42.05 O ANISOU 3042 O PRO B 85 4795 5746 5436 60 -53 -982 O ATOM 3043 CB PRO B 85 21.491 -10.226 -28.545 1.00 49.79 C ANISOU 3043 CB PRO B 85 5746 6989 6183 41 15 -1178 C ATOM 3044 CG PRO B 85 20.697 -9.318 -29.439 1.00 49.69 C ANISOU 3044 CG PRO B 85 5732 7138 6011 43 36 -1170 C ATOM 3045 CD PRO B 85 21.344 -7.972 -29.329 1.00 49.43 C ANISOU 3045 CD PRO B 85 5703 7149 5928 60 69 -1044 C ATOM 3046 N ALA B 86 24.380 -9.526 -27.630 1.00 41.10 N ANISOU 3046 N ALA B 86 4600 5795 5221 102 41 -1057 N ATOM 3047 CA ALA B 86 25.708 -9.853 -27.120 1.00 42.67 C ANISOU 3047 CA ALA B 86 4761 5914 5538 135 33 -1050 C ATOM 3048 C ALA B 86 26.037 -9.010 -25.873 1.00 45.24 C ANISOU 3048 C ALA B 86 5104 6194 5890 121 -13 -932 C ATOM 3049 O ALA B 86 26.516 -9.542 -24.873 1.00 43.66 O ANISOU 3049 O ALA B 86 4907 5899 5784 138 -66 -906 O ATOM 3050 CB ALA B 86 26.772 -9.704 -28.205 1.00 44.54 C ANISOU 3050 CB ALA B 86 4928 6229 5766 175 105 -1106 C ATOM 3051 N ALA B 87 25.749 -7.711 -25.910 1.00 41.42 N ANISOU 3051 N ALA B 87 4632 5780 5326 95 5 -862 N ATOM 3052 CA ALA B 87 26.020 -6.847 -24.747 1.00 40.94 C ANISOU 3052 CA ALA B 87 4583 5680 5291 79 -39 -776 C ATOM 3053 C ALA B 87 25.304 -7.322 -23.484 1.00 44.44 C ANISOU 3053 C ALA B 87 5087 6050 5747 67 -113 -738 C ATOM 3054 O ALA B 87 25.859 -7.269 -22.382 1.00 41.57 O ANISOU 3054 O ALA B 87 4724 5636 5436 79 -170 -698 O ATOM 3055 CB ALA B 87 25.623 -5.432 -25.044 1.00 32.71 C ANISOU 3055 CB ALA B 87 3549 4708 4173 53 -2 -716 C ATOM 3056 N LEU B 88 24.067 -7.780 -23.652 1.00 38.08 N ANISOU 3056 N LEU B 88 4328 5249 4891 44 -112 -751 N ATOM 3057 CA LEU B 88 23.255 -8.212 -22.524 1.00 36.02 C ANISOU 3057 CA LEU B 88 4124 4926 4636 27 -162 -704 C ATOM 3058 C LEU B 88 23.773 -9.552 -21.999 1.00 48.37 C ANISOU 3058 C LEU B 88 5686 6386 6307 58 -193 -716 C ATOM 3059 O LEU B 88 23.855 -9.772 -20.780 1.00 46.64 O ANISOU 3059 O LEU B 88 5497 6111 6114 71 -242 -646 O ATOM 3060 CB LEU B 88 21.793 -8.350 -22.949 1.00 38.65 C ANISOU 3060 CB LEU B 88 4488 5292 4903 -11 -142 -722 C ATOM 3061 CG LEU B 88 20.868 -8.687 -21.780 1.00 42.48 C ANISOU 3061 CG LEU B 88 5027 5721 5391 -35 -176 -661 C ATOM 3062 CD1 LEU B 88 20.986 -7.606 -20.712 1.00 37.12 C ANISOU 3062 CD1 LEU B 88 4375 5062 4668 -33 -207 -579 C ATOM 3063 CD2 LEU B 88 19.438 -8.822 -22.258 1.00 47.65 C ANISOU 3063 CD2 LEU B 88 5693 6413 5997 -76 -155 -690 C ATOM 3064 N PHE B 89 24.114 -10.445 -22.932 1.00 37.98 N ANISOU 3064 N PHE B 89 4334 5049 5049 76 -161 -804 N ATOM 3065 CA PHE B 89 24.674 -11.744 -22.591 1.00 40.57 C ANISOU 3065 CA PHE B 89 4650 5263 5501 114 -181 -823 C ATOM 3066 C PHE B 89 25.930 -11.537 -21.742 1.00 48.36 C ANISOU 3066 C PHE B 89 5611 6224 6539 164 -227 -766 C ATOM 3067 O PHE B 89 26.123 -12.200 -20.719 1.00 47.47 O ANISOU 3067 O PHE B 89 5521 6028 6488 196 -275 -703 O ATOM 3068 CB PHE B 89 24.999 -12.546 -23.862 1.00 34.39 C ANISOU 3068 CB PHE B 89 3818 4476 4771 133 -133 -953 C ATOM 3069 CG PHE B 89 25.687 -13.853 -23.595 1.00 46.40 C ANISOU 3069 CG PHE B 89 5319 5868 6443 182 -147 -982 C ATOM 3070 CD1 PHE B 89 25.027 -14.877 -22.907 1.00 51.04 C ANISOU 3070 CD1 PHE B 89 5948 6329 7115 172 -167 -948 C ATOM 3071 CD2 PHE B 89 26.990 -14.074 -24.037 1.00 55.92 C ANISOU 3071 CD2 PHE B 89 6458 7071 7717 240 -133 -1037 C ATOM 3072 CE1 PHE B 89 25.655 -16.097 -22.661 1.00 55.66 C ANISOU 3072 CE1 PHE B 89 6515 6777 7857 225 -175 -961 C ATOM 3073 CE2 PHE B 89 27.638 -15.303 -23.792 1.00 56.08 C ANISOU 3073 CE2 PHE B 89 6454 6962 7890 298 -147 -1062 C ATOM 3074 CZ PHE B 89 26.967 -16.313 -23.105 1.00 53.43 C ANISOU 3074 CZ PHE B 89 6167 6491 7643 292 -169 -1021 C ATOM 3075 N LEU B 90 26.759 -10.582 -22.150 1.00 42.41 N ANISOU 3075 N LEU B 90 4807 5548 5760 171 -212 -781 N ATOM 3076 CA LEU B 90 27.994 -10.290 -21.429 1.00 47.05 C ANISOU 3076 CA LEU B 90 5349 6125 6403 213 -260 -748 C ATOM 3077 C LEU B 90 27.716 -9.704 -20.050 1.00 45.01 C ANISOU 3077 C LEU B 90 5136 5870 6096 206 -330 -657 C ATOM 3078 O LEU B 90 28.291 -10.155 -19.046 1.00 44.17 O ANISOU 3078 O LEU B 90 5027 5721 6036 255 -398 -612 O ATOM 3079 CB LEU B 90 28.875 -9.332 -22.234 1.00 43.22 C ANISOU 3079 CB LEU B 90 4789 5719 5915 209 -213 -788 C ATOM 3080 CG LEU B 90 30.119 -8.819 -21.528 1.00 37.48 C ANISOU 3080 CG LEU B 90 3996 4994 5251 237 -262 -767 C ATOM 3081 CD1 LEU B 90 31.024 -9.993 -21.176 1.00 43.27 C ANISOU 3081 CD1 LEU B 90 4687 5656 6098 309 -305 -786 C ATOM 3082 CD2 LEU B 90 30.847 -7.837 -22.435 1.00 37.68 C ANISOU 3082 CD2 LEU B 90 3944 5088 5285 216 -193 -801 C ATOM 3083 N ALA B 91 26.832 -8.705 -20.020 1.00 33.46 N ANISOU 3083 N ALA B 91 3713 4465 4535 153 -314 -632 N ATOM 3084 CA ALA B 91 26.446 -8.004 -18.791 1.00 39.08 C ANISOU 3084 CA ALA B 91 4469 5196 5185 143 -370 -565 C ATOM 3085 C ALA B 91 25.782 -8.918 -17.760 1.00 45.29 C ANISOU 3085 C ALA B 91 5321 5929 5957 162 -411 -497 C ATOM 3086 O ALA B 91 25.995 -8.766 -16.549 1.00 41.26 O ANISOU 3086 O ALA B 91 4830 5427 5418 192 -476 -441 O ATOM 3087 CB ALA B 91 25.526 -6.818 -19.130 1.00 39.69 C ANISOU 3087 CB ALA B 91 4572 5336 5171 87 -330 -561 C ATOM 3088 N ALA B 92 24.985 -9.879 -18.225 1.00 44.48 N ANISOU 3088 N ALA B 92 5250 5773 5878 146 -369 -503 N ATOM 3089 CA ALA B 92 24.385 -10.823 -17.285 1.00 39.72 C ANISOU 3089 CA ALA B 92 4704 5102 5287 160 -390 -424 C ATOM 3090 C ALA B 92 25.461 -11.674 -16.602 1.00 45.31 C ANISOU 3090 C ALA B 92 5392 5745 6078 238 -444 -381 C ATOM 3091 O ALA B 92 25.392 -11.926 -15.389 1.00 43.16 O ANISOU 3091 O ALA B 92 5161 5461 5776 275 -491 -283 O ATOM 3092 CB ALA B 92 23.340 -11.679 -17.957 1.00 35.65 C ANISOU 3092 CB ALA B 92 4209 4528 4807 118 -332 -453 C ATOM 3093 N LYS B 93 26.470 -12.090 -17.368 1.00 44.16 N ANISOU 3093 N LYS B 93 5181 5568 6030 272 -436 -451 N ATOM 3094 CA LYS B 93 27.625 -12.804 -16.799 1.00 44.22 C ANISOU 3094 CA LYS B 93 5152 5522 6125 358 -492 -418 C ATOM 3095 C LYS B 93 28.380 -11.926 -15.814 1.00 54.27 C ANISOU 3095 C LYS B 93 6404 6879 7338 394 -575 -380 C ATOM 3096 O LYS B 93 28.666 -12.336 -14.685 1.00 54.42 O ANISOU 3096 O LYS B 93 6443 6887 7347 459 -644 -292 O ATOM 3097 CB LYS B 93 28.568 -13.312 -17.898 1.00 38.36 C ANISOU 3097 CB LYS B 93 4331 4743 5500 387 -460 -518 C ATOM 3098 CG LYS B 93 27.927 -14.397 -18.775 1.00 44.99 C ANISOU 3098 CG LYS B 93 5187 5489 6419 367 -391 -575 C ATOM 3099 CD LYS B 93 28.939 -15.209 -19.560 1.00 51.75 C ANISOU 3099 CD LYS B 93 5970 6285 7409 423 -369 -663 C ATOM 3100 CE LYS B 93 29.357 -14.508 -20.812 1.00 55.67 C ANISOU 3100 CE LYS B 93 6402 6876 7873 397 -315 -781 C ATOM 3101 NZ LYS B 93 30.334 -15.321 -21.571 1.00 58.78 N ANISOU 3101 NZ LYS B 93 6721 7221 8393 457 -285 -876 N ATOM 3102 N VAL B 94 28.677 -10.701 -16.235 1.00 54.64 N ANISOU 3102 N VAL B 94 6407 7011 7341 354 -568 -446 N ATOM 3103 CA VAL B 94 29.454 -9.796 -15.405 1.00 46.24 C ANISOU 3103 CA VAL B 94 5303 6022 6243 377 -646 -444 C ATOM 3104 C VAL B 94 28.721 -9.463 -14.108 1.00 47.72 C ANISOU 3104 C VAL B 94 5566 6254 6311 381 -700 -366 C ATOM 3105 O VAL B 94 29.344 -9.322 -13.060 1.00 45.57 O ANISOU 3105 O VAL B 94 5278 6029 6009 438 -791 -338 O ATOM 3106 CB VAL B 94 29.801 -8.496 -16.158 1.00 43.86 C ANISOU 3106 CB VAL B 94 4942 5783 5940 320 -610 -526 C ATOM 3107 CG1 VAL B 94 30.263 -7.423 -15.180 1.00 34.00 C ANISOU 3107 CG1 VAL B 94 3665 4605 4650 322 -689 -535 C ATOM 3108 CG2 VAL B 94 30.856 -8.746 -17.249 1.00 41.07 C ANISOU 3108 CG2 VAL B 94 4493 5412 5700 334 -566 -598 C ATOM 3109 N GLU B 95 27.398 -9.326 -14.177 1.00 44.25 N ANISOU 3109 N GLU B 95 5203 5813 5797 324 -645 -336 N ATOM 3110 CA GLU B 95 26.624 -8.928 -12.993 1.00 48.81 C ANISOU 3110 CA GLU B 95 5850 6445 6252 325 -680 -269 C ATOM 3111 C GLU B 95 26.178 -10.115 -12.139 1.00 53.57 C ANISOU 3111 C GLU B 95 6517 7000 6838 375 -691 -150 C ATOM 3112 O GLU B 95 25.394 -9.943 -11.211 1.00 58.93 O ANISOU 3112 O GLU B 95 7259 7723 7408 376 -698 -80 O ATOM 3113 CB GLU B 95 25.412 -8.042 -13.365 1.00 41.59 C ANISOU 3113 CB GLU B 95 4976 5565 5263 244 -616 -293 C ATOM 3114 CG GLU B 95 25.780 -6.651 -13.937 1.00 57.63 C ANISOU 3114 CG GLU B 95 6954 7647 7296 202 -607 -383 C ATOM 3115 CD GLU B 95 26.607 -5.766 -12.971 1.00 65.97 C ANISOU 3115 CD GLU B 95 7972 8769 8325 231 -694 -415 C ATOM 3116 OE1 GLU B 95 26.754 -6.131 -11.782 1.00 66.19 O ANISOU 3116 OE1 GLU B 95 8025 8830 8293 288 -768 -367 O ATOM 3117 OE2 GLU B 95 27.101 -4.696 -13.405 1.00 59.98 O ANISOU 3117 OE2 GLU B 95 7155 8030 7605 196 -687 -489 O ATOM 3118 N GLY B 96 26.677 -11.313 -12.450 1.00 52.80 N ANISOU 3118 N GLY B 96 6400 6807 6852 420 -685 -122 N ATOM 3119 CA GLY B 96 26.361 -12.492 -11.661 1.00 51.06 C ANISOU 3119 CA GLY B 96 6236 6519 6645 475 -688 8 C ATOM 3120 C GLY B 96 24.951 -13.040 -11.861 1.00 59.35 C ANISOU 3120 C GLY B 96 7352 7499 7699 411 -598 58 C ATOM 3121 O GLY B 96 24.438 -13.765 -11.016 1.00 64.43 O ANISOU 3121 O GLY B 96 8052 8103 8324 440 -587 186 O ATOM 3122 N GLN B 97 24.318 -12.691 -12.975 1.00 50.86 N ANISOU 3122 N GLN B 97 6263 6414 6646 326 -531 -40 N ATOM 3123 CA GLN B 97 23.049 -13.298 -13.350 1.00 49.43 C ANISOU 3123 CA GLN B 97 6120 6162 6498 261 -449 -23 C ATOM 3124 C GLN B 97 23.194 -13.967 -14.704 1.00 52.48 C ANISOU 3124 C GLN B 97 6459 6460 7019 233 -403 -128 C ATOM 3125 O GLN B 97 22.458 -13.630 -15.635 1.00 53.46 O ANISOU 3125 O GLN B 97 6572 6607 7132 162 -353 -215 O ATOM 3126 CB GLN B 97 21.967 -12.244 -13.501 1.00 54.82 C ANISOU 3126 CB GLN B 97 6824 6935 7070 186 -416 -58 C ATOM 3127 CG GLN B 97 21.709 -11.391 -12.290 1.00 61.03 C ANISOU 3127 CG GLN B 97 7652 7825 7712 204 -453 9 C ATOM 3128 CD GLN B 97 20.508 -10.509 -12.505 1.00 57.17 C ANISOU 3128 CD GLN B 97 7181 7400 7140 132 -406 -25 C ATOM 3129 OE1 GLN B 97 20.514 -9.645 -13.374 1.00 55.60 O ANISOU 3129 OE1 GLN B 97 6948 7244 6933 95 -397 -122 O ATOM 3130 NE2 GLN B 97 19.457 -10.736 -11.729 1.00 61.16 N ANISOU 3130 NE2 GLN B 97 7737 7913 7588 117 -369 62 N ATOM 3131 N PRO B 98 24.136 -14.915 -14.825 1.00 43.55 N ANISOU 3131 N PRO B 98 5297 5236 6013 297 -420 -126 N ATOM 3132 CA PRO B 98 24.423 -15.536 -16.121 1.00 48.03 C ANISOU 3132 CA PRO B 98 5813 5730 6707 283 -378 -249 C ATOM 3133 C PRO B 98 23.159 -16.102 -16.755 1.00 51.16 C ANISOU 3133 C PRO B 98 6226 6059 7152 204 -305 -294 C ATOM 3134 O PRO B 98 22.411 -16.832 -16.099 1.00 45.87 O ANISOU 3134 O PRO B 98 5601 5302 6528 190 -279 -200 O ATOM 3135 CB PRO B 98 25.355 -16.705 -15.774 1.00 35.01 C ANISOU 3135 CB PRO B 98 4145 3958 5198 373 -402 -198 C ATOM 3136 CG PRO B 98 25.669 -16.595 -14.378 1.00 45.86 C ANISOU 3136 CG PRO B 98 5557 5364 6505 439 -466 -49 C ATOM 3137 CD PRO B 98 24.730 -15.650 -13.704 1.00 46.13 C ANISOU 3137 CD PRO B 98 5646 5508 6374 387 -468 6 C ATOM 3138 N LYS B 99 22.924 -15.768 -18.016 1.00 47.07 N ANISOU 3138 N LYS B 99 5670 5589 6625 154 -270 -436 N ATOM 3139 CA LYS B 99 21.880 -16.435 -18.785 1.00 45.96 C ANISOU 3139 CA LYS B 99 5524 5388 6551 87 -213 -517 C ATOM 3140 C LYS B 99 22.517 -17.252 -19.900 1.00 48.40 C ANISOU 3140 C LYS B 99 5775 5628 6985 109 -191 -658 C ATOM 3141 O LYS B 99 23.495 -16.821 -20.526 1.00 50.73 O ANISOU 3141 O LYS B 99 6026 5991 7255 149 -203 -729 O ATOM 3142 CB LYS B 99 20.897 -15.421 -19.368 1.00 37.63 C ANISOU 3142 CB LYS B 99 4470 4464 5365 16 -194 -575 C ATOM 3143 CG LYS B 99 20.128 -14.654 -18.300 1.00 45.38 C ANISOU 3143 CG LYS B 99 5504 5506 6232 -8 -205 -454 C ATOM 3144 CD LYS B 99 18.985 -15.493 -17.763 1.00 44.19 C ANISOU 3144 CD LYS B 99 5382 5262 6147 -55 -165 -391 C ATOM 3145 CE LYS B 99 18.508 -14.983 -16.410 1.00 54.01 C ANISOU 3145 CE LYS B 99 6683 6549 7291 -51 -174 -241 C ATOM 3146 NZ LYS B 99 17.372 -15.798 -15.879 1.00 50.51 N ANISOU 3146 NZ LYS B 99 6261 6016 6916 -100 -118 -166 N ATOM 3147 N LYS B 100 21.969 -18.432 -20.150 1.00 54.70 N ANISOU 3147 N LYS B 100 6567 6287 7928 83 -153 -703 N ATOM 3148 CA LYS B 100 22.528 -19.296 -21.183 1.00 52.27 C ANISOU 3148 CA LYS B 100 6203 5904 7753 107 -130 -857 C ATOM 3149 C LYS B 100 22.450 -18.679 -22.573 1.00 49.72 C ANISOU 3149 C LYS B 100 5834 5725 7333 79 -113 -1029 C ATOM 3150 O LYS B 100 21.525 -17.913 -22.907 1.00 46.95 O ANISOU 3150 O LYS B 100 5492 5492 6854 18 -107 -1052 O ATOM 3151 CB LYS B 100 21.887 -20.687 -21.159 1.00 50.44 C ANISOU 3151 CB LYS B 100 5969 5478 7717 77 -90 -885 C ATOM 3152 CG LYS B 100 22.161 -21.443 -19.872 1.00 60.11 C ANISOU 3152 CG LYS B 100 7236 6544 9058 127 -96 -700 C ATOM 3153 CD LYS B 100 21.595 -22.840 -19.929 1.00 78.74 C ANISOU 3153 CD LYS B 100 9587 8686 11645 95 -43 -727 C ATOM 3154 CE LYS B 100 21.806 -23.590 -18.623 1.00 89.13 C ANISOU 3154 CE LYS B 100 10949 9842 13073 151 -38 -510 C ATOM 3155 NZ LYS B 100 20.903 -24.784 -18.553 1.00 94.83 N ANISOU 3155 NZ LYS B 100 11669 10351 14010 89 32 -504 N ATOM 3156 N LEU B 101 23.454 -19.018 -23.369 1.00 46.11 N ANISOU 3156 N LEU B 101 5325 5263 6933 134 -103 -1143 N ATOM 3157 CA LEU B 101 23.567 -18.560 -24.741 1.00 49.25 C ANISOU 3157 CA LEU B 101 5673 5800 7238 128 -77 -1305 C ATOM 3158 C LEU B 101 22.301 -18.869 -25.577 1.00 60.32 C ANISOU 3158 C LEU B 101 7064 7230 8627 55 -54 -1441 C ATOM 3159 O LEU B 101 21.736 -17.963 -26.204 1.00 61.24 O ANISOU 3159 O LEU B 101 7177 7512 8580 22 -51 -1478 O ATOM 3160 CB LEU B 101 24.834 -19.155 -25.360 1.00 48.42 C ANISOU 3160 CB LEU B 101 5509 5657 7231 205 -59 -1408 C ATOM 3161 CG LEU B 101 25.344 -18.574 -26.673 1.00 58.04 C ANISOU 3161 CG LEU B 101 6673 7042 8337 225 -24 -1545 C ATOM 3162 CD1 LEU B 101 25.369 -17.056 -26.630 1.00 54.66 C ANISOU 3162 CD1 LEU B 101 6261 6788 7720 208 -31 -1448 C ATOM 3163 CD2 LEU B 101 26.733 -19.139 -26.943 1.00 56.67 C ANISOU 3163 CD2 LEU B 101 6440 6814 8276 312 -7 -1606 C ATOM 3164 N GLU B 102 21.847 -20.127 -25.584 1.00 60.12 N ANISOU 3164 N GLU B 102 7026 7040 8776 31 -39 -1516 N ATOM 3165 CA GLU B 102 20.610 -20.479 -26.294 1.00 59.24 C ANISOU 3165 CA GLU B 102 6890 6945 8673 -45 -25 -1659 C ATOM 3166 C GLU B 102 19.433 -19.635 -25.805 1.00 58.86 C ANISOU 3166 C GLU B 102 6878 6986 8498 -114 -40 -1553 C ATOM 3167 O GLU B 102 18.571 -19.229 -26.582 1.00 56.44 O ANISOU 3167 O GLU B 102 6546 6810 8088 -159 -44 -1655 O ATOM 3168 CB GLU B 102 20.267 -21.957 -26.121 1.00 65.50 C ANISOU 3168 CB GLU B 102 7664 7509 9714 -72 -3 -1728 C ATOM 3169 CG GLU B 102 21.210 -22.906 -26.868 1.00 98.37 C ANISOU 3169 CG GLU B 102 11776 11581 14020 -9 17 -1895 C ATOM 3170 CD GLU B 102 20.706 -24.346 -26.901 1.00111.98 C ANISOU 3170 CD GLU B 102 13468 13075 16003 -48 44 -2005 C ATOM 3171 OE1 GLU B 102 19.477 -24.560 -26.744 1.00114.85 O ANISOU 3171 OE1 GLU B 102 13830 13395 16411 -141 49 -2017 O ATOM 3172 OE2 GLU B 102 21.542 -25.260 -27.088 1.00111.09 O ANISOU 3172 OE2 GLU B 102 13328 12819 16064 13 64 -2083 O ATOM 3173 N HIS B 103 19.405 -19.384 -24.503 1.00 48.04 N ANISOU 3173 N HIS B 103 5565 5554 7134 -114 -51 -1352 N ATOM 3174 CA HIS B 103 18.329 -18.625 -23.892 1.00 50.96 C ANISOU 3174 CA HIS B 103 5969 5996 7397 -172 -59 -1243 C ATOM 3175 C HIS B 103 18.285 -17.187 -24.431 1.00 49.75 C ANISOU 3175 C HIS B 103 5817 6062 7025 -164 -77 -1248 C ATOM 3176 O HIS B 103 17.228 -16.719 -24.862 1.00 50.97 O ANISOU 3176 O HIS B 103 5957 6319 7090 -214 -78 -1293 O ATOM 3177 CB HIS B 103 18.474 -18.679 -22.370 1.00 51.97 C ANISOU 3177 CB HIS B 103 6158 6023 7564 -156 -63 -1031 C ATOM 3178 CG HIS B 103 17.278 -18.192 -21.619 1.00 55.14 C ANISOU 3178 CG HIS B 103 6592 6462 7896 -217 -56 -924 C ATOM 3179 ND1 HIS B 103 17.310 -17.932 -20.264 1.00 58.03 N ANISOU 3179 ND1 HIS B 103 7018 6802 8230 -199 -61 -732 N ATOM 3180 CD2 HIS B 103 16.022 -17.898 -22.029 1.00 54.66 C ANISOU 3180 CD2 HIS B 103 6508 6476 7785 -290 -44 -987 C ATOM 3181 CE1 HIS B 103 16.122 -17.513 -19.869 1.00 44.39 C ANISOU 3181 CE1 HIS B 103 5303 5124 6439 -260 -43 -681 C ATOM 3182 NE2 HIS B 103 15.323 -17.473 -20.921 1.00 53.89 N ANISOU 3182 NE2 HIS B 103 6453 6386 7635 -317 -34 -831 N ATOM 3183 N VAL B 104 19.428 -16.505 -24.437 1.00 43.42 N ANISOU 3183 N VAL B 104 5024 5326 6149 -100 -88 -1202 N ATOM 3184 CA VAL B 104 19.491 -15.124 -24.916 1.00 47.91 C ANISOU 3184 CA VAL B 104 5591 6078 6533 -90 -94 -1187 C ATOM 3185 C VAL B 104 19.152 -15.056 -26.406 1.00 48.69 C ANISOU 3185 C VAL B 104 5641 6303 6557 -96 -76 -1352 C ATOM 3186 O VAL B 104 18.451 -14.161 -26.866 1.00 44.44 O ANISOU 3186 O VAL B 104 5101 5907 5879 -114 -79 -1351 O ATOM 3187 CB VAL B 104 20.892 -14.500 -24.670 1.00 48.63 C ANISOU 3187 CB VAL B 104 5685 6196 6595 -26 -101 -1118 C ATOM 3188 CG1 VAL B 104 20.980 -13.106 -25.273 1.00 43.96 C ANISOU 3188 CG1 VAL B 104 5086 5776 5842 -19 -92 -1105 C ATOM 3189 CG2 VAL B 104 21.195 -14.450 -23.179 1.00 44.66 C ANISOU 3189 CG2 VAL B 104 5228 5606 6135 -11 -133 -960 C ATOM 3190 N ILE B 105 19.655 -16.016 -27.163 1.00 50.09 N ANISOU 3190 N ILE B 105 5776 6433 6824 -72 -60 -1496 N ATOM 3191 CA ILE B 105 19.340 -16.104 -28.578 1.00 54.41 C ANISOU 3191 CA ILE B 105 6271 7107 7294 -70 -47 -1674 C ATOM 3192 C ILE B 105 17.835 -16.285 -28.855 1.00 52.18 C ANISOU 3192 C ILE B 105 5973 6863 6992 -138 -66 -1751 C ATOM 3193 O ILE B 105 17.268 -15.648 -29.746 1.00 50.23 O ANISOU 3193 O ILE B 105 5702 6794 6590 -137 -73 -1814 O ATOM 3194 CB ILE B 105 20.190 -17.209 -29.241 1.00 55.89 C ANISOU 3194 CB ILE B 105 6414 7220 7601 -28 -24 -1832 C ATOM 3195 CG1 ILE B 105 21.554 -16.618 -29.610 1.00 51.26 C ANISOU 3195 CG1 ILE B 105 5815 6716 6946 46 4 -1804 C ATOM 3196 CG2 ILE B 105 19.458 -17.835 -30.456 1.00 44.93 C ANISOU 3196 CG2 ILE B 105 4970 5903 6198 -49 -23 -2059 C ATOM 3197 CD1 ILE B 105 22.460 -17.569 -30.296 1.00 69.34 C ANISOU 3197 CD1 ILE B 105 8054 8956 9335 99 34 -1958 C ATOM 3198 N LYS B 106 17.188 -17.132 -28.069 1.00 53.63 N ANISOU 3198 N LYS B 106 6163 6882 7331 -193 -72 -1734 N ATOM 3199 CA LYS B 106 15.768 -17.392 -28.244 1.00 56.81 C ANISOU 3199 CA LYS B 106 6534 7301 7749 -267 -86 -1809 C ATOM 3200 C LYS B 106 14.959 -16.127 -27.977 1.00 53.28 C ANISOU 3200 C LYS B 106 6111 6997 7135 -284 -103 -1691 C ATOM 3201 O LYS B 106 14.100 -15.751 -28.774 1.00 56.58 O ANISOU 3201 O LYS B 106 6488 7563 7446 -300 -123 -1781 O ATOM 3202 CB LYS B 106 15.317 -18.525 -27.327 1.00 66.43 C ANISOU 3202 CB LYS B 106 7756 8294 9190 -326 -71 -1781 C ATOM 3203 CG LYS B 106 13.978 -19.088 -27.698 1.00 84.71 C ANISOU 3203 CG LYS B 106 10011 10598 11577 -408 -78 -1914 C ATOM 3204 CD LYS B 106 13.726 -20.431 -27.046 1.00 96.39 C ANISOU 3204 CD LYS B 106 11477 11826 13320 -464 -46 -1923 C ATOM 3205 CE LYS B 106 12.257 -20.837 -27.204 1.00107.31 C ANISOU 3205 CE LYS B 106 12793 13195 14784 -565 -48 -2024 C ATOM 3206 NZ LYS B 106 11.751 -20.738 -28.617 1.00106.75 N ANISOU 3206 NZ LYS B 106 12641 13301 14617 -573 -91 -2268 N ATOM 3207 N VAL B 107 15.258 -15.457 -26.869 1.00 48.28 N ANISOU 3207 N VAL B 107 5539 6328 6478 -273 -99 -1497 N ATOM 3208 CA VAL B 107 14.572 -14.219 -26.498 1.00 42.89 C ANISOU 3208 CA VAL B 107 4883 5761 5654 -282 -110 -1380 C ATOM 3209 C VAL B 107 14.864 -13.052 -27.445 1.00 46.45 C ANISOU 3209 C VAL B 107 5325 6405 5918 -230 -115 -1391 C ATOM 3210 O VAL B 107 13.972 -12.279 -27.777 1.00 46.82 O ANISOU 3210 O VAL B 107 5359 6580 5850 -238 -128 -1382 O ATOM 3211 CB VAL B 107 14.925 -13.810 -25.065 1.00 43.16 C ANISOU 3211 CB VAL B 107 4982 5710 5707 -275 -105 -1190 C ATOM 3212 CG1 VAL B 107 14.604 -12.325 -24.824 1.00 37.52 C ANISOU 3212 CG1 VAL B 107 4295 5127 4834 -261 -114 -1084 C ATOM 3213 CG2 VAL B 107 14.214 -14.723 -24.072 1.00 37.90 C ANISOU 3213 CG2 VAL B 107 4326 4892 5182 -332 -90 -1139 C ATOM 3214 N ALA B 108 16.110 -12.937 -27.892 1.00 42.16 N ANISOU 3214 N ALA B 108 4785 5882 5354 -173 -99 -1404 N ATOM 3215 CA ALA B 108 16.459 -11.915 -28.871 1.00 51.45 C ANISOU 3215 CA ALA B 108 5950 7234 6366 -122 -86 -1407 C ATOM 3216 C ALA B 108 15.590 -12.099 -30.104 1.00 49.78 C ANISOU 3216 C ALA B 108 5686 7165 6064 -123 -100 -1556 C ATOM 3217 O ALA B 108 15.042 -11.151 -30.655 1.00 48.76 O ANISOU 3217 O ALA B 108 5549 7193 5783 -102 -106 -1524 O ATOM 3218 CB ALA B 108 17.957 -12.002 -29.252 1.00 42.69 C ANISOU 3218 CB ALA B 108 4833 6114 5271 -66 -54 -1423 C ATOM 3219 N HIS B 109 15.472 -13.343 -30.536 1.00 53.67 N ANISOU 3219 N HIS B 109 6136 7600 6655 -144 -108 -1723 N ATOM 3220 CA HIS B 109 14.733 -13.650 -31.745 1.00 56.82 C ANISOU 3220 CA HIS B 109 6474 8142 6975 -142 -131 -1902 C ATOM 3221 C HIS B 109 13.245 -13.322 -31.632 1.00 61.86 C ANISOU 3221 C HIS B 109 7089 8848 7569 -189 -171 -1896 C ATOM 3222 O HIS B 109 12.655 -12.752 -32.550 1.00 58.15 O ANISOU 3222 O HIS B 109 6584 8573 6937 -158 -196 -1947 O ATOM 3223 CB HIS B 109 14.917 -15.112 -32.113 1.00 53.88 C ANISOU 3223 CB HIS B 109 6055 7663 6753 -162 -132 -2101 C ATOM 3224 CG HIS B 109 14.202 -15.498 -33.362 1.00 64.09 C ANISOU 3224 CG HIS B 109 7276 9108 7968 -159 -164 -2319 C ATOM 3225 ND1 HIS B 109 12.849 -15.763 -33.389 1.00 67.90 N ANISOU 3225 ND1 HIS B 109 7710 9613 8478 -222 -210 -2401 N ATOM 3226 CD2 HIS B 109 14.645 -15.649 -34.632 1.00 63.68 C ANISOU 3226 CD2 HIS B 109 7184 9209 7802 -98 -159 -2479 C ATOM 3227 CE1 HIS B 109 12.490 -16.067 -34.622 1.00 71.58 C ANISOU 3227 CE1 HIS B 109 8107 10240 8851 -200 -243 -2613 C ATOM 3228 NE2 HIS B 109 13.562 -16.003 -35.395 1.00 70.75 N ANISOU 3228 NE2 HIS B 109 8011 10222 8650 -121 -212 -2662 N ATOM 3229 N THR B 110 12.627 -13.671 -30.509 1.00 52.90 N ANISOU 3229 N THR B 110 5968 7561 6571 -257 -176 -1829 N ATOM 3230 CA THR B 110 11.221 -13.349 -30.372 1.00 47.75 C ANISOU 3230 CA THR B 110 5283 6974 5887 -301 -207 -1823 C ATOM 3231 C THR B 110 10.990 -11.832 -30.286 1.00 52.18 C ANISOU 3231 C THR B 110 5877 7674 6274 -256 -210 -1665 C ATOM 3232 O THR B 110 9.984 -11.320 -30.787 1.00 56.16 O ANISOU 3232 O THR B 110 6339 8324 6675 -250 -243 -1692 O ATOM 3233 CB THR B 110 10.528 -14.131 -29.224 1.00 48.19 C ANISOU 3233 CB THR B 110 5336 6840 6134 -389 -197 -1790 C ATOM 3234 OG1 THR B 110 9.110 -14.124 -29.437 1.00 65.91 O ANISOU 3234 OG1 THR B 110 7511 9161 8370 -439 -229 -1861 O ATOM 3235 CG2 THR B 110 10.820 -13.521 -27.874 1.00 43.50 C ANISOU 3235 CG2 THR B 110 4820 6152 5555 -389 -168 -1571 C ATOM 3236 N CYS B 111 11.925 -11.109 -29.673 1.00 52.21 N ANISOU 3236 N CYS B 111 5951 7632 6256 -222 -178 -1508 N ATOM 3237 CA CYS B 111 11.806 -9.650 -29.587 1.00 55.24 C ANISOU 3237 CA CYS B 111 6365 8122 6502 -179 -173 -1363 C ATOM 3238 C CYS B 111 11.940 -8.993 -30.965 1.00 58.96 C ANISOU 3238 C CYS B 111 6809 8794 6798 -106 -175 -1402 C ATOM 3239 O CYS B 111 11.183 -8.079 -31.302 1.00 61.02 O ANISOU 3239 O CYS B 111 7058 9186 6941 -76 -191 -1349 O ATOM 3240 CB CYS B 111 12.822 -9.057 -28.602 1.00 50.04 C ANISOU 3240 CB CYS B 111 5776 7360 5879 -164 -141 -1208 C ATOM 3241 SG CYS B 111 12.517 -9.459 -26.865 1.00 54.39 S ANISOU 3241 SG CYS B 111 6369 7725 6572 -226 -139 -1112 S ATOM 3242 N LEU B 112 12.886 -9.483 -31.760 1.00 53.50 N ANISOU 3242 N LEU B 112 6106 8130 6090 -72 -155 -1492 N ATOM 3243 CA LEU B 112 13.155 -8.935 -33.086 1.00 58.01 C ANISOU 3243 CA LEU B 112 6656 8901 6483 4 -143 -1522 C ATOM 3244 C LEU B 112 12.204 -9.435 -34.183 1.00 68.70 C ANISOU 3244 C LEU B 112 7940 10420 7744 17 -193 -1698 C ATOM 3245 O LEU B 112 11.925 -8.714 -35.138 1.00 73.09 O ANISOU 3245 O LEU B 112 8477 11178 8117 85 -201 -1683 O ATOM 3246 CB LEU B 112 14.602 -9.224 -33.479 1.00 55.76 C ANISOU 3246 CB LEU B 112 6382 8592 6212 41 -91 -1548 C ATOM 3247 CG LEU B 112 15.595 -8.514 -32.565 1.00 55.79 C ANISOU 3247 CG LEU B 112 6441 8478 6280 43 -47 -1375 C ATOM 3248 CD1 LEU B 112 16.994 -8.988 -32.844 1.00 45.13 C ANISOU 3248 CD1 LEU B 112 5085 7083 4978 70 -1 -1418 C ATOM 3249 CD2 LEU B 112 15.463 -7.016 -32.757 1.00 43.47 C ANISOU 3249 CD2 LEU B 112 4902 7024 4590 86 -23 -1216 C ATOM 3250 N HIS B 113 11.711 -10.661 -34.040 1.00 70.15 N ANISOU 3250 N HIS B 113 8080 10517 8058 -47 -229 -1862 N ATOM 3251 CA HIS B 113 10.855 -11.286 -35.055 1.00 61.80 C ANISOU 3251 CA HIS B 113 6941 9603 6940 -46 -285 -2071 C ATOM 3252 C HIS B 113 9.661 -11.995 -34.416 1.00 54.70 C ANISOU 3252 C HIS B 113 5992 8599 6192 -140 -331 -2150 C ATOM 3253 O HIS B 113 9.566 -13.213 -34.460 1.00 58.19 O ANISOU 3253 O HIS B 113 6389 8940 6780 -196 -344 -2324 O ATOM 3254 CB HIS B 113 11.673 -12.288 -35.874 1.00 60.73 C ANISOU 3254 CB HIS B 113 6777 9475 6823 -26 -272 -2263 C ATOM 3255 CG HIS B 113 12.978 -11.738 -36.357 1.00 73.76 C ANISOU 3255 CG HIS B 113 8470 11193 8363 55 -207 -2182 C ATOM 3256 ND1 HIS B 113 13.088 -10.970 -37.499 1.00 72.54 N ANISOU 3256 ND1 HIS B 113 8305 11284 7973 147 -197 -2168 N ATOM 3257 CD2 HIS B 113 14.229 -11.829 -35.844 1.00 76.68 C ANISOU 3257 CD2 HIS B 113 8887 11419 8828 60 -146 -2103 C ATOM 3258 CE1 HIS B 113 14.349 -10.617 -37.670 1.00 76.50 C ANISOU 3258 CE1 HIS B 113 8844 11783 8439 197 -122 -2082 C ATOM 3259 NE2 HIS B 113 15.063 -11.128 -36.681 1.00 78.77 N ANISOU 3259 NE2 HIS B 113 9162 11837 8929 144 -94 -2050 N ATOM 3260 N PRO B 114 8.739 -11.228 -33.824 1.00 52.28 N ANISOU 3260 N PRO B 114 5687 8312 5864 -157 -349 -2024 N ATOM 3261 CA PRO B 114 7.606 -11.775 -33.068 1.00 59.27 C ANISOU 3261 CA PRO B 114 6526 9093 6901 -250 -374 -2062 C ATOM 3262 C PRO B 114 6.803 -12.793 -33.867 1.00 77.80 C ANISOU 3262 C PRO B 114 8764 11502 9293 -290 -433 -2316 C ATOM 3263 O PRO B 114 6.269 -13.734 -33.284 1.00 95.14 O ANISOU 3263 O PRO B 114 10918 13541 11689 -386 -432 -2395 O ATOM 3264 CB PRO B 114 6.721 -10.551 -32.814 1.00 56.74 C ANISOU 3264 CB PRO B 114 6205 8883 6469 -222 -392 -1917 C ATOM 3265 CG PRO B 114 7.591 -9.385 -33.015 1.00 64.31 C ANISOU 3265 CG PRO B 114 7239 9917 7280 -132 -358 -1755 C ATOM 3266 CD PRO B 114 8.613 -9.780 -34.038 1.00 57.05 C ANISOU 3266 CD PRO B 114 6322 9068 6286 -81 -346 -1857 C ATOM 3267 N GLN B 115 6.713 -12.600 -35.178 1.00 77.60 N ANISOU 3267 N GLN B 115 8691 11708 9087 -218 -481 -2443 N ATOM 3268 CA GLN B 115 5.856 -13.436 -36.012 1.00 90.45 C ANISOU 3268 CA GLN B 115 10201 13437 10730 -249 -554 -2705 C ATOM 3269 C GLN B 115 6.606 -14.608 -36.630 1.00 97.92 C ANISOU 3269 C GLN B 115 11125 14328 11752 -258 -547 -2924 C ATOM 3270 O GLN B 115 5.988 -15.576 -37.077 1.00101.44 O ANISOU 3270 O GLN B 115 11472 14776 12294 -313 -597 -3168 O ATOM 3271 CB GLN B 115 5.189 -12.605 -37.115 1.00 93.12 C ANISOU 3271 CB GLN B 115 10484 14087 10811 -156 -625 -2739 C ATOM 3272 CG GLN B 115 4.625 -11.269 -36.651 1.00 92.39 C ANISOU 3272 CG GLN B 115 10422 14065 10616 -114 -625 -2504 C ATOM 3273 CD GLN B 115 3.648 -11.418 -35.507 1.00 95.71 C ANISOU 3273 CD GLN B 115 10810 14331 11223 -214 -624 -2454 C ATOM 3274 OE1 GLN B 115 3.050 -12.480 -35.320 1.00 98.71 O ANISOU 3274 OE1 GLN B 115 11111 14613 11779 -311 -647 -2622 O ATOM 3275 NE2 GLN B 115 3.479 -10.352 -34.729 1.00 93.81 N ANISOU 3275 NE2 GLN B 115 10628 14063 10953 -192 -591 -2224 N ATOM 3276 N GLU B 116 7.933 -14.513 -36.674 1.00 96.38 N ANISOU 3276 N GLU B 116 11012 14085 11524 -205 -485 -2849 N ATOM 3277 CA GLU B 116 8.744 -15.625 -37.158 1.00 99.75 C ANISOU 3277 CA GLU B 116 11423 14435 12043 -208 -466 -3045 C ATOM 3278 C GLU B 116 8.827 -16.686 -36.078 1.00 97.07 C ANISOU 3278 C GLU B 116 11090 13780 12012 -313 -430 -3056 C ATOM 3279 O GLU B 116 8.243 -16.539 -35.010 1.00101.37 O ANISOU 3279 O GLU B 116 11652 14192 12673 -380 -418 -2912 O ATOM 3280 CB GLU B 116 10.149 -15.167 -37.567 1.00108.71 C ANISOU 3280 CB GLU B 116 12631 15628 13047 -112 -405 -2959 C ATOM 3281 CG GLU B 116 10.252 -14.690 -39.006 1.00118.67 C ANISOU 3281 CG GLU B 116 13861 17199 14030 -5 -430 -3055 C ATOM 3282 CD GLU B 116 9.190 -13.662 -39.350 1.00131.77 C ANISOU 3282 CD GLU B 116 15494 19080 15492 34 -489 -2972 C ATOM 3283 OE1 GLU B 116 9.182 -12.583 -38.717 1.00135.18 O ANISOU 3283 OE1 GLU B 116 15990 19494 15880 51 -459 -2716 O ATOM 3284 OE2 GLU B 116 8.363 -13.933 -40.250 1.00134.04 O ANISOU 3284 OE2 GLU B 116 15692 19561 15676 53 -568 -3170 O ATOM 3285 N SER B 117 9.546 -17.761 -36.361 1.00 95.32 N ANISOU 3285 N SER B 117 10855 13441 11922 -320 -408 -3223 N ATOM 3286 CA SER B 117 9.670 -18.852 -35.416 1.00 96.43 C ANISOU 3286 CA SER B 117 10999 13273 12366 -409 -369 -3234 C ATOM 3287 C SER B 117 11.122 -19.275 -35.400 1.00 96.78 C ANISOU 3287 C SER B 117 11100 13200 12470 -356 -310 -3224 C ATOM 3288 O SER B 117 11.761 -19.333 -36.455 1.00 97.04 O ANISOU 3288 O SER B 117 11116 13378 12379 -281 -312 -3368 O ATOM 3289 CB SER B 117 8.781 -20.016 -35.845 1.00106.19 C ANISOU 3289 CB SER B 117 12121 14452 13775 -491 -413 -3515 C ATOM 3290 OG SER B 117 8.811 -21.051 -34.883 1.00114.88 O ANISOU 3290 OG SER B 117 13225 15237 15189 -580 -365 -3499 O ATOM 3291 N LEU B 118 11.651 -19.558 -34.213 1.00 95.10 N ANISOU 3291 N LEU B 118 10951 12742 12440 -386 -258 -3052 N ATOM 3292 CA LEU B 118 13.065 -19.900 -34.086 1.00101.08 C ANISOU 3292 CA LEU B 118 11759 13386 13261 -328 -206 -3017 C ATOM 3293 C LEU B 118 13.422 -21.042 -35.026 1.00105.75 C ANISOU 3293 C LEU B 118 12284 13945 13952 -314 -206 -3306 C ATOM 3294 O LEU B 118 12.650 -21.995 -35.167 1.00103.16 O ANISOU 3294 O LEU B 118 11883 13518 13793 -387 -230 -3495 O ATOM 3295 CB LEU B 118 13.413 -20.284 -32.647 1.00102.06 C ANISOU 3295 CB LEU B 118 11944 13235 13598 -368 -163 -2821 C ATOM 3296 CG LEU B 118 14.905 -20.482 -32.347 1.00101.37 C ANISOU 3296 CG LEU B 118 11910 13037 13569 -298 -117 -2741 C ATOM 3297 CD1 LEU B 118 15.689 -19.163 -32.465 1.00 97.05 C ANISOU 3297 CD1 LEU B 118 11416 12669 12789 -218 -107 -2582 C ATOM 3298 CD2 LEU B 118 15.103 -21.112 -30.971 1.00 96.53 C ANISOU 3298 CD2 LEU B 118 11342 12147 13186 -336 -87 -2580 C ATOM 3299 N PRO B 119 14.584 -20.937 -35.693 1.00105.90 N ANISOU 3299 N PRO B 119 12317 14050 13869 -221 -177 -3353 N ATOM 3300 CA PRO B 119 15.071 -22.041 -36.529 1.00102.82 C ANISOU 3300 CA PRO B 119 11868 13618 13582 -195 -166 -3630 C ATOM 3301 C PRO B 119 15.284 -23.299 -35.695 1.00104.18 C ANISOU 3301 C PRO B 119 12036 13448 14098 -250 -136 -3654 C ATOM 3302 O PRO B 119 15.280 -23.246 -34.459 1.00100.11 O ANISOU 3302 O PRO B 119 11578 12747 13712 -290 -115 -3423 O ATOM 3303 CB PRO B 119 16.417 -21.525 -37.055 1.00 94.44 C ANISOU 3303 CB PRO B 119 10841 12683 12360 -82 -118 -3585 C ATOM 3304 CG PRO B 119 16.304 -20.036 -36.990 1.00 95.92 C ANISOU 3304 CG PRO B 119 11079 13074 12291 -51 -122 -3358 C ATOM 3305 CD PRO B 119 15.442 -19.742 -35.788 1.00 98.70 C ANISOU 3305 CD PRO B 119 11468 13296 12737 -136 -147 -3166 C ATOM 3306 N ASP B 120 15.456 -24.428 -36.371 1.00105.87 N ANISOU 3306 N ASP B 120 12183 13580 14460 -248 -132 -3931 N ATOM 3307 CA ASP B 120 15.722 -25.671 -35.676 1.00107.87 C ANISOU 3307 CA ASP B 120 12431 13497 15060 -288 -95 -3961 C ATOM 3308 C ASP B 120 17.102 -25.594 -35.043 1.00107.78 C ANISOU 3308 C ASP B 120 12489 13367 15094 -208 -40 -3767 C ATOM 3309 O ASP B 120 18.087 -25.303 -35.721 1.00109.18 O ANISOU 3309 O ASP B 120 12669 13683 15133 -113 -18 -3818 O ATOM 3310 CB ASP B 120 15.653 -26.854 -36.639 1.00113.03 C ANISOU 3310 CB ASP B 120 12990 14095 15863 -295 -103 -4328 C ATOM 3311 CG ASP B 120 15.934 -28.172 -35.951 1.00123.86 C ANISOU 3311 CG ASP B 120 14350 15091 17619 -332 -57 -4358 C ATOM 3312 OD1 ASP B 120 15.447 -28.365 -34.815 1.00127.85 O ANISOU 3312 OD1 ASP B 120 14887 15385 18304 -408 -41 -4159 O ATOM 3313 OD2 ASP B 120 16.647 -29.011 -36.539 1.00130.99 O ANISOU 3313 OD2 ASP B 120 15213 15912 18646 -280 -31 -4573 O ATOM 3314 N THR B 121 17.173 -25.858 -33.743 1.00100.81 N ANISOU 3314 N THR B 121 11660 12241 14404 -243 -16 -3542 N ATOM 3315 CA THR B 121 18.440 -25.800 -33.026 1.00 91.83 C ANISOU 3315 CA THR B 121 10582 10990 13318 -166 23 -3347 C ATOM 3316 C THR B 121 19.479 -26.786 -33.561 1.00 95.05 C ANISOU 3316 C THR B 121 10950 11279 13887 -92 59 -3531 C ATOM 3317 O THR B 121 20.570 -26.915 -32.999 1.00 95.54 O ANISOU 3317 O THR B 121 11044 11225 14030 -21 89 -3396 O ATOM 3318 CB THR B 121 18.241 -26.057 -31.542 1.00 84.99 C ANISOU 3318 CB THR B 121 9773 9882 12636 -212 38 -3092 C ATOM 3319 OG1 THR B 121 17.529 -27.287 -31.376 1.00 91.66 O ANISOU 3319 OG1 THR B 121 10573 10486 13767 -289 53 -3211 O ATOM 3320 CG2 THR B 121 17.448 -24.928 -30.928 1.00 76.64 C ANISOU 3320 CG2 THR B 121 8764 8960 11394 -261 11 -2884 C ATOM 3321 N ARG B 122 19.142 -27.477 -34.645 1.00 94.54 N ANISOU 3321 N ARG B 122 10806 11249 13866 -104 52 -3850 N ATOM 3322 CA ARG B 122 20.089 -28.378 -35.291 1.00100.68 C ANISOU 3322 CA ARG B 122 11536 11940 14779 -27 89 -4064 C ATOM 3323 C ARG B 122 20.560 -27.812 -36.629 1.00 92.07 C ANISOU 3323 C ARG B 122 10409 11164 13409 52 90 -4248 C ATOM 3324 O ARG B 122 21.554 -28.280 -37.188 1.00 84.79 O ANISOU 3324 O ARG B 122 9455 10232 12531 140 131 -4391 O ATOM 3325 CB ARG B 122 19.468 -29.762 -35.501 1.00114.34 C ANISOU 3325 CB ARG B 122 13195 13434 16813 -93 91 -4319 C ATOM 3326 CG ARG B 122 18.881 -30.399 -34.250 1.00124.68 C ANISOU 3326 CG ARG B 122 14532 14426 18414 -180 104 -4143 C ATOM 3327 CD ARG B 122 18.379 -31.803 -34.551 1.00135.73 C ANISOU 3327 CD ARG B 122 15851 15574 20147 -242 119 -4412 C ATOM 3328 NE ARG B 122 17.938 -32.515 -33.355 1.00145.10 N ANISOU 3328 NE ARG B 122 17061 16426 21643 -317 154 -4227 N ATOM 3329 CZ ARG B 122 17.725 -33.827 -33.303 1.00153.85 C ANISOU 3329 CZ ARG B 122 18114 17225 23118 -362 190 -4380 C ATOM 3330 NH1 ARG B 122 17.918 -34.575 -34.381 1.00157.17 N ANISOU 3330 NH1 ARG B 122 18449 17626 23642 -341 190 -4743 N ATOM 3331 NH2 ARG B 122 17.323 -34.395 -32.174 1.00155.55 N ANISOU 3331 NH2 ARG B 122 18358 17146 23600 -427 233 -4169 N ATOM 3332 N SER B 123 19.842 -26.809 -37.139 1.00 88.12 N ANISOU 3332 N SER B 123 9913 10946 12622 29 50 -4237 N ATOM 3333 CA SER B 123 20.167 -26.208 -38.437 1.00 88.66 C ANISOU 3333 CA SER B 123 9950 11340 12395 107 55 -4389 C ATOM 3334 C SER B 123 21.509 -25.488 -38.431 1.00 94.74 C ANISOU 3334 C SER B 123 10758 12208 13029 209 113 -4222 C ATOM 3335 O SER B 123 21.998 -25.073 -37.381 1.00 95.55 O ANISOU 3335 O SER B 123 10920 12193 13191 210 127 -3947 O ATOM 3336 CB SER B 123 19.070 -25.242 -38.888 1.00 85.34 C ANISOU 3336 CB SER B 123 9531 11193 11704 67 -2 -4371 C ATOM 3337 OG SER B 123 18.703 -24.351 -37.848 1.00 81.84 O ANISOU 3337 OG SER B 123 9158 10722 11215 20 -17 -4054 O ATOM 3338 N GLU B 124 22.107 -25.347 -39.607 1.00 98.50 N ANISOU 3338 N GLU B 124 11194 12908 13324 296 147 -4395 N ATOM 3339 CA GLU B 124 23.369 -24.635 -39.709 1.00106.58 C ANISOU 3339 CA GLU B 124 12236 14042 14215 388 214 -4249 C ATOM 3340 C GLU B 124 23.149 -23.141 -39.518 1.00100.68 C ANISOU 3340 C GLU B 124 11547 13498 13210 378 206 -3983 C ATOM 3341 O GLU B 124 24.046 -22.424 -39.077 1.00102.06 O ANISOU 3341 O GLU B 124 11754 13682 13342 417 249 -3766 O ATOM 3342 CB GLU B 124 24.064 -24.925 -41.042 1.00120.66 C ANISOU 3342 CB GLU B 124 13955 16016 15876 486 269 -4508 C ATOM 3343 CG GLU B 124 24.864 -26.230 -41.058 1.00131.05 C ANISOU 3343 CG GLU B 124 15220 17104 17470 533 309 -4704 C ATOM 3344 CD GLU B 124 25.981 -26.256 -40.019 1.00137.31 C ANISOU 3344 CD GLU B 124 16040 17682 18448 568 349 -4473 C ATOM 3345 OE1 GLU B 124 26.421 -25.168 -39.578 1.00136.49 O ANISOU 3345 OE1 GLU B 124 15980 17674 18206 579 365 -4204 O ATOM 3346 OE2 GLU B 124 26.421 -27.368 -39.648 1.00139.16 O ANISOU 3346 OE2 GLU B 124 16247 17652 18976 587 363 -4566 O ATOM 3347 N ALA B 125 21.945 -22.682 -39.835 1.00 93.35 N ANISOU 3347 N ALA B 125 10623 12721 12123 326 148 -4005 N ATOM 3348 CA ALA B 125 21.607 -21.273 -39.688 1.00101.58 C ANISOU 3348 CA ALA B 125 11717 13947 12932 318 138 -3763 C ATOM 3349 C ALA B 125 21.461 -20.869 -38.217 1.00100.41 C ANISOU 3349 C ALA B 125 11636 13599 12918 253 117 -3479 C ATOM 3350 O ALA B 125 21.728 -19.717 -37.850 1.00 93.45 O ANISOU 3350 O ALA B 125 10800 12800 11905 265 133 -3242 O ATOM 3351 CB ALA B 125 20.339 -20.949 -40.459 1.00106.45 C ANISOU 3351 CB ALA B 125 12310 14785 13350 293 77 -3877 C ATOM 3352 N TYR B 126 21.025 -21.814 -37.386 1.00 94.13 N ANISOU 3352 N TYR B 126 10842 12540 12384 185 84 -3506 N ATOM 3353 CA TYR B 126 20.944 -21.574 -35.953 1.00 83.11 C ANISOU 3353 CA TYR B 126 9508 10951 11120 133 70 -3247 C ATOM 3354 C TYR B 126 22.306 -21.740 -35.269 1.00 77.96 C ANISOU 3354 C TYR B 126 8876 10146 10601 190 113 -3120 C ATOM 3355 O TYR B 126 22.648 -20.978 -34.364 1.00 73.51 O ANISOU 3355 O TYR B 126 8363 9553 10014 188 112 -2876 O ATOM 3356 CB TYR B 126 19.910 -22.477 -35.279 1.00 76.56 C ANISOU 3356 CB TYR B 126 8673 9906 10511 40 29 -3293 C ATOM 3357 CG TYR B 126 20.028 -22.440 -33.767 1.00 74.84 C ANISOU 3357 CG TYR B 126 8519 9471 10447 5 28 -3032 C ATOM 3358 CD1 TYR B 126 19.445 -21.417 -33.028 1.00 69.64 C ANISOU 3358 CD1 TYR B 126 7915 8873 9672 -35 4 -2810 C ATOM 3359 CD2 TYR B 126 20.753 -23.406 -33.083 1.00 72.13 C ANISOU 3359 CD2 TYR B 126 8179 8871 10355 26 52 -3008 C ATOM 3360 CE1 TYR B 126 19.566 -21.370 -31.651 1.00 71.19 C ANISOU 3360 CE1 TYR B 126 8168 8896 9985 -58 3 -2582 C ATOM 3361 CE2 TYR B 126 20.873 -23.370 -31.710 1.00 67.54 C ANISOU 3361 CE2 TYR B 126 7657 8117 9889 8 49 -2764 C ATOM 3362 CZ TYR B 126 20.280 -22.349 -31.000 1.00 73.35 C ANISOU 3362 CZ TYR B 126 8447 8934 10490 -35 24 -2557 C ATOM 3363 OH TYR B 126 20.415 -22.304 -29.634 1.00 79.83 O ANISOU 3363 OH TYR B 126 9325 9604 11403 -44 19 -2324 O ATOM 3364 N LEU B 127 23.076 -22.737 -35.693 1.00 70.60 N ANISOU 3364 N LEU B 127 7896 9118 9812 243 147 -3296 N ATOM 3365 CA LEU B 127 24.404 -22.943 -35.136 1.00 69.11 C ANISOU 3365 CA LEU B 127 7709 8797 9753 309 185 -3194 C ATOM 3366 C LEU B 127 25.264 -21.720 -35.406 1.00 76.94 C ANISOU 3366 C LEU B 127 8707 9995 10533 366 223 -3061 C ATOM 3367 O LEU B 127 26.149 -21.373 -34.623 1.00 73.84 O ANISOU 3367 O LEU B 127 8331 9529 10197 396 234 -2880 O ATOM 3368 CB LEU B 127 25.062 -24.167 -35.757 1.00 74.66 C ANISOU 3368 CB LEU B 127 8346 9395 10625 369 222 -3437 C ATOM 3369 CG LEU B 127 24.581 -25.538 -35.291 1.00 81.08 C ANISOU 3369 CG LEU B 127 9148 9921 11739 326 202 -3544 C ATOM 3370 CD1 LEU B 127 25.460 -26.616 -35.912 1.00 84.52 C ANISOU 3370 CD1 LEU B 127 9516 10256 12341 406 248 -3773 C ATOM 3371 CD2 LEU B 127 24.591 -25.628 -33.767 1.00 70.06 C ANISOU 3371 CD2 LEU B 127 7812 8294 10514 296 178 -3276 C ATOM 3372 N GLN B 128 24.980 -21.067 -36.527 1.00 82.78 N ANISOU 3372 N GLN B 128 9428 10996 11030 381 244 -3149 N ATOM 3373 CA GLN B 128 25.746 -19.918 -36.967 1.00 75.33 C ANISOU 3373 CA GLN B 128 8482 10258 9884 434 298 -3035 C ATOM 3374 C GLN B 128 25.384 -18.675 -36.172 1.00 78.61 C ANISOU 3374 C GLN B 128 8958 10709 10200 387 270 -2769 C ATOM 3375 O GLN B 128 26.253 -17.858 -35.869 1.00 83.60 O ANISOU 3375 O GLN B 128 9595 11375 10793 414 306 -2606 O ATOM 3376 CB GLN B 128 25.532 -19.674 -38.462 1.00 77.87 C ANISOU 3376 CB GLN B 128 8764 10853 9969 477 335 -3210 C ATOM 3377 CG GLN B 128 26.321 -18.506 -39.038 1.00 81.85 C ANISOU 3377 CG GLN B 128 9261 11578 10261 536 412 -3087 C ATOM 3378 CD GLN B 128 27.815 -18.596 -38.749 1.00 86.02 C ANISOU 3378 CD GLN B 128 9752 12020 10911 592 480 -3029 C ATOM 3379 OE1 GLN B 128 28.452 -19.632 -38.979 1.00 92.18 O ANISOU 3379 OE1 GLN B 128 10482 12708 11835 640 506 -3200 O ATOM 3380 NE2 GLN B 128 28.382 -17.502 -38.242 1.00 78.11 N ANISOU 3380 NE2 GLN B 128 8768 11044 9865 588 507 -2795 N ATOM 3381 N GLN B 129 24.112 -18.513 -35.829 1.00 78.53 N ANISOU 3381 N GLN B 129 8988 10690 10160 314 209 -2733 N ATOM 3382 CA GLN B 129 23.741 -17.332 -35.052 1.00 75.89 C ANISOU 3382 CA GLN B 129 8711 10386 9740 274 185 -2492 C ATOM 3383 C GLN B 129 24.218 -17.449 -33.603 1.00 71.33 C ANISOU 3383 C GLN B 129 8168 9588 9345 254 162 -2321 C ATOM 3384 O GLN B 129 24.495 -16.444 -32.952 1.00 68.55 O ANISOU 3384 O GLN B 129 7850 9258 8940 247 160 -2128 O ATOM 3385 CB GLN B 129 22.249 -17.004 -35.157 1.00 74.06 C ANISOU 3385 CB GLN B 129 8503 10236 9402 213 132 -2497 C ATOM 3386 CG GLN B 129 21.308 -18.115 -34.776 1.00 88.84 C ANISOU 3386 CG GLN B 129 10368 11947 11441 149 81 -2614 C ATOM 3387 CD GLN B 129 19.853 -17.687 -34.883 1.00 96.55 C ANISOU 3387 CD GLN B 129 11353 13024 12308 90 30 -2613 C ATOM 3388 OE1 GLN B 129 19.501 -16.551 -34.557 1.00 90.13 O ANISOU 3388 OE1 GLN B 129 10579 12301 11366 79 21 -2436 O ATOM 3389 NE2 GLN B 129 19.001 -18.598 -35.338 1.00102.15 N ANISOU 3389 NE2 GLN B 129 12017 13712 13083 51 -4 -2818 N ATOM 3390 N VAL B 130 24.349 -18.679 -33.121 1.00 70.29 N ANISOU 3390 N VAL B 130 8027 9250 9431 251 145 -2397 N ATOM 3391 CA VAL B 130 24.951 -18.915 -31.823 1.00 69.70 C ANISOU 3391 CA VAL B 130 7979 8980 9524 256 124 -2242 C ATOM 3392 C VAL B 130 26.408 -18.474 -31.857 1.00 75.61 C ANISOU 3392 C VAL B 130 8695 9770 10265 328 163 -2182 C ATOM 3393 O VAL B 130 26.883 -17.819 -30.933 1.00 74.70 O ANISOU 3393 O VAL B 130 8603 9622 10157 330 143 -2001 O ATOM 3394 CB VAL B 130 24.850 -20.387 -31.408 1.00 66.51 C ANISOU 3394 CB VAL B 130 7565 8341 9364 252 110 -2331 C ATOM 3395 CG1 VAL B 130 25.585 -20.621 -30.108 1.00 59.91 C ANISOU 3395 CG1 VAL B 130 6754 7325 8682 280 89 -2156 C ATOM 3396 CG2 VAL B 130 23.396 -20.784 -31.255 1.00 68.67 C ANISOU 3396 CG2 VAL B 130 7863 8559 9672 166 77 -2374 C ATOM 3397 N GLN B 131 27.106 -18.819 -32.936 1.00 73.30 N ANISOU 3397 N GLN B 131 8340 9557 9953 388 220 -2343 N ATOM 3398 CA GLN B 131 28.498 -18.399 -33.121 1.00 71.03 C ANISOU 3398 CA GLN B 131 8002 9328 9657 456 272 -2304 C ATOM 3399 C GLN B 131 28.674 -16.897 -33.393 1.00 70.17 C ANISOU 3399 C GLN B 131 7900 9414 9350 447 305 -2173 C ATOM 3400 O GLN B 131 29.680 -16.307 -33.005 1.00 68.01 O ANISOU 3400 O GLN B 131 7598 9142 9100 472 326 -2060 O ATOM 3401 CB GLN B 131 29.181 -19.220 -34.218 1.00 73.29 C ANISOU 3401 CB GLN B 131 8215 9650 9980 527 335 -2522 C ATOM 3402 CG GLN B 131 29.889 -20.459 -33.696 1.00 93.57 C ANISOU 3402 CG GLN B 131 10751 11997 12806 576 324 -2583 C ATOM 3403 CD GLN B 131 30.916 -20.137 -32.608 1.00111.76 C ANISOU 3403 CD GLN B 131 13046 14206 15213 608 303 -2396 C ATOM 3404 OE1 GLN B 131 31.682 -19.171 -32.715 1.00111.78 O ANISOU 3404 OE1 GLN B 131 13017 14335 15121 627 337 -2307 O ATOM 3405 NE2 GLN B 131 30.931 -20.950 -31.553 1.00117.58 N ANISOU 3405 NE2 GLN B 131 13805 14722 16149 616 247 -2333 N ATOM 3406 N ASP B 132 27.701 -16.281 -34.058 1.00 68.05 N ANISOU 3406 N ASP B 132 7660 9302 8896 412 311 -2186 N ATOM 3407 CA ASP B 132 27.777 -14.855 -34.341 1.00 58.81 C ANISOU 3407 CA ASP B 132 6498 8300 7547 405 348 -2049 C ATOM 3408 C ASP B 132 27.713 -14.063 -33.047 1.00 65.83 C ANISOU 3408 C ASP B 132 7434 9097 8482 359 298 -1843 C ATOM 3409 O ASP B 132 28.397 -13.052 -32.900 1.00 71.28 O ANISOU 3409 O ASP B 132 8109 9841 9135 364 332 -1719 O ATOM 3410 CB ASP B 132 26.666 -14.422 -35.295 1.00 60.93 C ANISOU 3410 CB ASP B 132 6788 8753 7610 390 355 -2101 C ATOM 3411 CG ASP B 132 26.936 -14.843 -36.741 1.00 79.36 C ANISOU 3411 CG ASP B 132 9068 11254 9833 453 421 -2289 C ATOM 3412 OD1 ASP B 132 28.113 -15.088 -37.089 1.00 81.48 O ANISOU 3412 OD1 ASP B 132 9279 11529 10148 510 489 -2337 O ATOM 3413 OD2 ASP B 132 25.971 -14.926 -37.531 1.00 87.00 O ANISOU 3413 OD2 ASP B 132 10043 12355 10659 450 405 -2395 O ATOM 3414 N LEU B 133 26.904 -14.534 -32.101 1.00 59.91 N ANISOU 3414 N LEU B 133 6735 8208 7820 312 222 -1811 N ATOM 3415 CA LEU B 133 26.798 -13.868 -30.810 1.00 54.31 C ANISOU 3415 CA LEU B 133 6072 7417 7146 275 170 -1631 C ATOM 3416 C LEU B 133 28.122 -13.959 -30.034 1.00 60.33 C ANISOU 3416 C LEU B 133 6800 8079 8044 313 163 -1565 C ATOM 3417 O LEU B 133 28.619 -12.955 -29.526 1.00 61.96 O ANISOU 3417 O LEU B 133 7003 8313 8226 306 160 -1441 O ATOM 3418 CB LEU B 133 25.619 -14.425 -29.991 1.00 44.64 C ANISOU 3418 CB LEU B 133 4906 6076 5978 221 103 -1611 C ATOM 3419 CG LEU B 133 25.163 -13.619 -28.752 1.00 53.51 C ANISOU 3419 CG LEU B 133 6088 7159 7085 178 54 -1434 C ATOM 3420 CD1 LEU B 133 23.725 -13.927 -28.346 1.00 56.80 C ANISOU 3420 CD1 LEU B 133 6555 7532 7496 119 14 -1429 C ATOM 3421 CD2 LEU B 133 26.084 -13.858 -27.572 1.00 59.47 C ANISOU 3421 CD2 LEU B 133 6843 7782 7972 204 17 -1342 C ATOM 3422 N VAL B 134 28.677 -15.165 -29.949 1.00 54.41 N ANISOU 3422 N VAL B 134 6019 7210 7446 357 157 -1655 N ATOM 3423 CA VAL B 134 29.942 -15.400 -29.267 1.00 60.27 C ANISOU 3423 CA VAL B 134 6715 7859 8325 409 143 -1607 C ATOM 3424 C VAL B 134 31.043 -14.497 -29.830 1.00 65.92 C ANISOU 3424 C VAL B 134 7360 8701 8987 437 206 -1591 C ATOM 3425 O VAL B 134 31.822 -13.892 -29.088 1.00 60.19 O ANISOU 3425 O VAL B 134 6607 7957 8307 444 182 -1486 O ATOM 3426 CB VAL B 134 30.393 -16.870 -29.420 1.00 65.68 C ANISOU 3426 CB VAL B 134 7363 8413 9179 467 146 -1734 C ATOM 3427 CG1 VAL B 134 31.835 -17.018 -28.979 1.00 58.84 C ANISOU 3427 CG1 VAL B 134 6427 7491 8438 538 143 -1700 C ATOM 3428 CG2 VAL B 134 29.495 -17.797 -28.616 1.00 65.50 C ANISOU 3428 CG2 VAL B 134 7403 8223 9262 440 87 -1714 C ATOM 3429 N ILE B 135 31.102 -14.422 -31.151 1.00 58.32 N ANISOU 3429 N ILE B 135 6360 7871 7927 455 289 -1699 N ATOM 3430 CA ILE B 135 32.076 -13.590 -31.821 1.00 50.99 C ANISOU 3430 CA ILE B 135 5362 7071 6942 479 373 -1679 C ATOM 3431 C ILE B 135 31.877 -12.120 -31.478 1.00 50.88 C ANISOU 3431 C ILE B 135 5374 7128 6832 426 374 -1520 C ATOM 3432 O ILE B 135 32.841 -11.366 -31.303 1.00 52.41 O ANISOU 3432 O ILE B 135 5508 7342 7062 430 407 -1446 O ATOM 3433 CB ILE B 135 31.980 -13.790 -33.333 1.00 53.85 C ANISOU 3433 CB ILE B 135 5694 7585 7182 512 466 -1819 C ATOM 3434 CG1 ILE B 135 32.659 -15.114 -33.705 1.00 52.11 C ANISOU 3434 CG1 ILE B 135 5413 7296 7091 581 487 -1989 C ATOM 3435 CG2 ILE B 135 32.602 -12.612 -34.084 1.00 44.68 C ANISOU 3435 CG2 ILE B 135 4484 6591 5902 518 568 -1748 C ATOM 3436 CD1 ILE B 135 32.204 -15.681 -35.035 1.00 48.92 C ANISOU 3436 CD1 ILE B 135 5000 7011 6576 610 545 -2175 C ATOM 3437 N LEU B 136 30.621 -11.715 -31.367 1.00 47.43 N ANISOU 3437 N LEU B 136 5017 6717 6287 375 339 -1472 N ATOM 3438 CA LEU B 136 30.311 -10.325 -31.074 1.00 50.25 C ANISOU 3438 CA LEU B 136 5403 7131 6558 328 342 -1329 C ATOM 3439 C LEU B 136 30.622 -9.985 -29.616 1.00 53.22 C ANISOU 3439 C LEU B 136 5792 7386 7044 302 262 -1223 C ATOM 3440 O LEU B 136 31.068 -8.876 -29.314 1.00 57.57 O ANISOU 3440 O LEU B 136 6320 7960 7595 279 277 -1128 O ATOM 3441 CB LEU B 136 28.856 -10.033 -31.404 1.00 57.14 C ANISOU 3441 CB LEU B 136 6351 8073 7287 292 326 -1318 C ATOM 3442 CG LEU B 136 28.486 -8.605 -31.779 1.00 61.05 C ANISOU 3442 CG LEU B 136 6863 8683 7649 267 372 -1202 C ATOM 3443 CD1 LEU B 136 29.616 -7.936 -32.522 1.00 61.96 C ANISOU 3443 CD1 LEU B 136 6906 8886 7752 296 477 -1169 C ATOM 3444 CD2 LEU B 136 27.223 -8.633 -32.616 1.00 58.07 C ANISOU 3444 CD2 LEU B 136 6529 8420 7113 266 376 -1245 C ATOM 3445 N GLU B 137 30.406 -10.942 -28.716 1.00 50.21 N ANISOU 3445 N GLU B 137 5442 6876 6759 309 179 -1241 N ATOM 3446 CA GLU B 137 30.752 -10.739 -27.309 1.00 53.46 C ANISOU 3446 CA GLU B 137 5863 7190 7258 302 97 -1147 C ATOM 3447 C GLU B 137 32.239 -10.446 -27.206 1.00 57.69 C ANISOU 3447 C GLU B 137 6302 7730 7890 337 114 -1141 C ATOM 3448 O GLU B 137 32.671 -9.568 -26.457 1.00 53.99 O ANISOU 3448 O GLU B 137 5812 7257 7445 316 80 -1063 O ATOM 3449 CB GLU B 137 30.415 -11.963 -26.458 1.00 42.49 C ANISOU 3449 CB GLU B 137 4516 5667 5961 322 21 -1159 C ATOM 3450 CG GLU B 137 30.655 -11.736 -24.980 1.00 51.89 C ANISOU 3450 CG GLU B 137 5726 6785 7205 323 -68 -1051 C ATOM 3451 CD GLU B 137 30.780 -13.019 -24.171 1.00 57.48 C ANISOU 3451 CD GLU B 137 6450 7358 8030 372 -130 -1045 C ATOM 3452 OE1 GLU B 137 31.241 -14.048 -24.712 1.00 54.84 O ANISOU 3452 OE1 GLU B 137 6076 6969 7792 421 -103 -1132 O ATOM 3453 OE2 GLU B 137 30.430 -12.985 -22.973 1.00 54.94 O ANISOU 3453 OE2 GLU B 137 6181 6986 7706 366 -202 -948 O ATOM 3454 N SER B 138 33.013 -11.189 -27.988 1.00 56.91 N ANISOU 3454 N SER B 138 6134 7640 7851 390 169 -1239 N ATOM 3455 CA SER B 138 34.460 -11.079 -27.987 1.00 49.09 C ANISOU 3455 CA SER B 138 5032 6652 6967 431 194 -1252 C ATOM 3456 C SER B 138 34.915 -9.735 -28.559 1.00 47.59 C ANISOU 3456 C SER B 138 4788 6573 6723 394 279 -1203 C ATOM 3457 O SER B 138 35.853 -9.112 -28.059 1.00 50.25 O ANISOU 3457 O SER B 138 5047 6900 7145 388 268 -1160 O ATOM 3458 CB SER B 138 35.061 -12.240 -28.787 1.00 56.69 C ANISOU 3458 CB SER B 138 5935 7603 8002 501 246 -1382 C ATOM 3459 OG SER B 138 36.446 -12.357 -28.529 1.00 75.48 O ANISOU 3459 OG SER B 138 8204 9959 10518 552 246 -1393 O ATOM 3460 N ILE B 139 34.249 -9.288 -29.615 1.00 56.51 N ANISOU 3460 N ILE B 139 5951 7808 7714 371 364 -1207 N ATOM 3461 CA ILE B 139 34.532 -7.970 -30.169 1.00 55.54 C ANISOU 3461 CA ILE B 139 5789 7779 7533 335 455 -1131 C ATOM 3462 C ILE B 139 34.201 -6.867 -29.164 1.00 54.20 C ANISOU 3462 C ILE B 139 5655 7563 7374 274 393 -1018 C ATOM 3463 O ILE B 139 34.915 -5.865 -29.070 1.00 55.35 O ANISOU 3463 O ILE B 139 5734 7719 7577 244 433 -959 O ATOM 3464 CB ILE B 139 33.764 -7.735 -31.481 1.00 58.29 C ANISOU 3464 CB ILE B 139 6178 8261 7708 337 550 -1142 C ATOM 3465 CG1 ILE B 139 34.288 -8.676 -32.573 1.00 55.35 C ANISOU 3465 CG1 ILE B 139 5749 7960 7320 402 629 -1271 C ATOM 3466 CG2 ILE B 139 33.890 -6.289 -31.928 1.00 42.42 C ANISOU 3466 CG2 ILE B 139 4146 6331 5639 300 641 -1024 C ATOM 3467 CD1 ILE B 139 33.597 -8.493 -33.916 1.00 53.07 C ANISOU 3467 CD1 ILE B 139 5493 7834 6837 418 719 -1296 C ATOM 3468 N ILE B 140 33.123 -7.051 -28.405 1.00 47.40 N ANISOU 3468 N ILE B 140 4893 6648 6467 252 299 -994 N ATOM 3469 CA ILE B 140 32.750 -6.064 -27.391 1.00 47.44 C ANISOU 3469 CA ILE B 140 4936 6612 6476 201 237 -904 C ATOM 3470 C ILE B 140 33.800 -6.016 -26.276 1.00 46.86 C ANISOU 3470 C ILE B 140 4795 6466 6546 208 160 -902 C ATOM 3471 O ILE B 140 34.287 -4.952 -25.916 1.00 49.00 O ANISOU 3471 O ILE B 140 5017 6734 6868 170 164 -859 O ATOM 3472 CB ILE B 140 31.334 -6.326 -26.794 1.00 44.01 C ANISOU 3472 CB ILE B 140 4618 6145 5958 181 160 -882 C ATOM 3473 CG1 ILE B 140 30.241 -6.109 -27.852 1.00 46.80 C ANISOU 3473 CG1 ILE B 140 5027 6588 6166 168 224 -878 C ATOM 3474 CG2 ILE B 140 31.082 -5.410 -25.611 1.00 40.69 C ANISOU 3474 CG2 ILE B 140 4228 5679 5552 140 89 -807 C ATOM 3475 CD1 ILE B 140 28.860 -6.686 -27.479 1.00 38.48 C ANISOU 3475 CD1 ILE B 140 4068 5509 5044 155 159 -888 C ATOM 3476 N LEU B 141 34.154 -7.175 -25.737 1.00 46.99 N ANISOU 3476 N LEU B 141 4801 6420 6632 259 89 -952 N ATOM 3477 CA LEU B 141 35.187 -7.246 -24.714 1.00 51.12 C ANISOU 3477 CA LEU B 141 5251 6891 7279 284 5 -954 C ATOM 3478 C LEU B 141 36.448 -6.522 -25.164 1.00 48.19 C ANISOU 3478 C LEU B 141 4746 6560 7002 275 74 -971 C ATOM 3479 O LEU B 141 37.081 -5.808 -24.378 1.00 47.07 O ANISOU 3479 O LEU B 141 4542 6403 6940 253 20 -955 O ATOM 3480 CB LEU B 141 35.533 -8.700 -24.396 1.00 51.97 C ANISOU 3480 CB LEU B 141 5352 6935 7460 360 -52 -1002 C ATOM 3481 CG LEU B 141 34.519 -9.449 -23.550 1.00 44.57 C ANISOU 3481 CG LEU B 141 4527 5929 6478 372 -140 -967 C ATOM 3482 CD1 LEU B 141 34.818 -10.928 -23.543 1.00 51.87 C ANISOU 3482 CD1 LEU B 141 5443 6776 7490 447 -162 -1013 C ATOM 3483 CD2 LEU B 141 34.532 -8.902 -22.156 1.00 44.23 C ANISOU 3483 CD2 LEU B 141 4502 5868 6434 362 -248 -900 C ATOM 3484 N GLN B 142 36.821 -6.702 -26.426 1.00 46.84 N ANISOU 3484 N GLN B 142 4525 6447 6826 291 195 -1009 N ATOM 3485 CA GLN B 142 38.054 -6.073 -26.915 1.00 52.12 C ANISOU 3485 CA GLN B 142 5055 7156 7594 282 280 -1019 C ATOM 3486 C GLN B 142 37.915 -4.592 -27.231 1.00 53.67 C ANISOU 3486 C GLN B 142 5240 7387 7765 205 360 -942 C ATOM 3487 O GLN B 142 38.875 -3.838 -27.119 1.00 57.36 O ANISOU 3487 O GLN B 142 5593 7849 8351 174 392 -934 O ATOM 3488 CB GLN B 142 38.628 -6.852 -28.085 1.00 42.21 C ANISOU 3488 CB GLN B 142 3737 5954 6347 338 387 -1091 C ATOM 3489 CG GLN B 142 39.180 -8.177 -27.613 1.00 61.06 C ANISOU 3489 CG GLN B 142 6090 8279 8833 418 307 -1170 C ATOM 3490 CD GLN B 142 39.470 -9.118 -28.738 1.00 69.23 C ANISOU 3490 CD GLN B 142 7089 9354 9860 480 402 -1262 C ATOM 3491 OE1 GLN B 142 39.842 -8.702 -29.832 1.00 75.64 O ANISOU 3491 OE1 GLN B 142 7843 10261 10637 474 538 -1276 O ATOM 3492 NE2 GLN B 142 39.300 -10.400 -28.481 1.00 73.12 N ANISOU 3492 NE2 GLN B 142 7618 9775 10390 545 337 -1327 N ATOM 3493 N THR B 143 36.713 -4.170 -27.593 1.00 52.79 N ANISOU 3493 N THR B 143 5240 7303 7514 175 389 -886 N ATOM 3494 CA THR B 143 36.478 -2.762 -27.841 1.00 50.74 C ANISOU 3494 CA THR B 143 4981 7060 7236 110 461 -799 C ATOM 3495 C THR B 143 36.510 -1.990 -26.534 1.00 56.07 C ANISOU 3495 C THR B 143 5652 7655 7997 62 356 -779 C ATOM 3496 O THR B 143 37.003 -0.858 -26.481 1.00 57.55 O ANISOU 3496 O THR B 143 5770 7820 8277 8 404 -742 O ATOM 3497 CB THR B 143 35.136 -2.532 -28.509 1.00 50.86 C ANISOU 3497 CB THR B 143 5115 7129 7079 103 505 -742 C ATOM 3498 OG1 THR B 143 35.115 -3.198 -29.780 1.00 48.51 O ANISOU 3498 OG1 THR B 143 4816 6928 6687 151 601 -776 O ATOM 3499 CG2 THR B 143 34.906 -1.039 -28.698 1.00 44.86 C ANISOU 3499 CG2 THR B 143 4356 6369 6320 45 578 -636 C ATOM 3500 N LEU B 144 35.984 -2.602 -25.477 1.00 51.27 N ANISOU 3500 N LEU B 144 5116 7003 7360 82 218 -807 N ATOM 3501 CA LEU B 144 35.945 -1.946 -24.173 1.00 49.15 C ANISOU 3501 CA LEU B 144 4853 6679 7144 48 108 -802 C ATOM 3502 C LEU B 144 37.253 -2.142 -23.436 1.00 48.59 C ANISOU 3502 C LEU B 144 4657 6583 7220 67 33 -866 C ATOM 3503 O LEU B 144 37.422 -1.663 -22.317 1.00 46.66 O ANISOU 3503 O LEU B 144 4394 6309 7025 48 -71 -887 O ATOM 3504 CB LEU B 144 34.795 -2.483 -23.330 1.00 45.91 C ANISOU 3504 CB LEU B 144 4573 6248 6623 66 0 -792 C ATOM 3505 CG LEU B 144 33.458 -2.455 -24.057 1.00 50.90 C ANISOU 3505 CG LEU B 144 5317 6911 7110 55 62 -743 C ATOM 3506 CD1 LEU B 144 32.351 -3.037 -23.176 1.00 45.70 C ANISOU 3506 CD1 LEU B 144 4772 6229 6362 68 -38 -735 C ATOM 3507 CD2 LEU B 144 33.159 -1.038 -24.484 1.00 47.73 C ANISOU 3507 CD2 LEU B 144 4914 6520 6701 -1 143 -681 C ATOM 3508 N GLY B 145 38.178 -2.851 -24.074 1.00 51.30 N ANISOU 3508 N GLY B 145 4910 6950 7632 110 84 -907 N ATOM 3509 CA GLY B 145 39.460 -3.128 -23.463 1.00 49.42 C ANISOU 3509 CA GLY B 145 4539 6699 7540 140 14 -971 C ATOM 3510 C GLY B 145 39.245 -3.801 -22.128 1.00 45.69 C ANISOU 3510 C GLY B 145 4118 6198 7043 190 -158 -989 C ATOM 3511 O GLY B 145 39.946 -3.500 -21.157 1.00 41.96 O ANISOU 3511 O GLY B 145 3566 5720 6657 193 -262 -1027 O ATOM 3512 N PHE B 146 38.248 -4.690 -22.081 1.00 45.99 N ANISOU 3512 N PHE B 146 4289 6224 6961 229 -185 -960 N ATOM 3513 CA PHE B 146 37.956 -5.515 -20.901 1.00 46.21 C ANISOU 3513 CA PHE B 146 4381 6223 6955 287 -328 -952 C ATOM 3514 C PHE B 146 37.634 -4.744 -19.617 1.00 50.43 C ANISOU 3514 C PHE B 146 4949 6761 7452 259 -441 -936 C ATOM 3515 O PHE B 146 37.652 -5.320 -18.530 1.00 56.76 O ANISOU 3515 O PHE B 146 5776 7558 8231 317 -565 -928 O ATOM 3516 CB PHE B 146 39.080 -6.529 -20.656 1.00 46.90 C ANISOU 3516 CB PHE B 146 4370 6298 7151 376 -386 -995 C ATOM 3517 CG PHE B 146 39.110 -7.617 -21.677 1.00 50.86 C ANISOU 3517 CG PHE B 146 4878 6782 7666 425 -300 -1017 C ATOM 3518 CD1 PHE B 146 38.463 -8.821 -21.443 1.00 48.83 C ANISOU 3518 CD1 PHE B 146 4718 6472 7365 483 -342 -996 C ATOM 3519 CD2 PHE B 146 39.732 -7.415 -22.900 1.00 47.60 C ANISOU 3519 CD2 PHE B 146 4375 6405 7308 410 -169 -1061 C ATOM 3520 CE1 PHE B 146 38.457 -9.815 -22.402 1.00 54.30 C ANISOU 3520 CE1 PHE B 146 5413 7139 8081 525 -263 -1039 C ATOM 3521 CE2 PHE B 146 39.719 -8.407 -23.868 1.00 51.51 C ANISOU 3521 CE2 PHE B 146 4877 6895 7801 459 -88 -1101 C ATOM 3522 CZ PHE B 146 39.096 -9.610 -23.616 1.00 49.89 C ANISOU 3522 CZ PHE B 146 4764 6629 7565 515 -140 -1101 C ATOM 3523 N GLU B 147 37.332 -3.453 -19.752 1.00 45.77 N ANISOU 3523 N GLU B 147 4359 6179 6854 178 -394 -931 N ATOM 3524 CA GLU B 147 36.807 -2.657 -18.645 1.00 56.99 C ANISOU 3524 CA GLU B 147 5828 7601 8223 147 -484 -929 C ATOM 3525 C GLU B 147 35.292 -2.851 -18.532 1.00 51.52 C ANISOU 3525 C GLU B 147 5299 6903 7376 140 -477 -864 C ATOM 3526 O GLU B 147 34.528 -2.236 -19.271 1.00 57.08 O ANISOU 3526 O GLU B 147 6053 7601 8032 88 -381 -831 O ATOM 3527 CB GLU B 147 37.139 -1.179 -18.835 1.00 60.76 C ANISOU 3527 CB GLU B 147 6229 8069 8787 62 -431 -958 C ATOM 3528 CG GLU B 147 36.419 -0.264 -17.848 1.00 79.31 C ANISOU 3528 CG GLU B 147 8640 10413 11080 24 -502 -968 C ATOM 3529 CD GLU B 147 37.073 1.114 -17.689 1.00 90.25 C ANISOU 3529 CD GLU B 147 9914 11772 12604 -49 -491 -1033 C ATOM 3530 OE1 GLU B 147 37.870 1.528 -18.568 1.00 89.20 O ANISOU 3530 OE1 GLU B 147 9672 11616 12604 -89 -389 -1039 O ATOM 3531 OE2 GLU B 147 36.777 1.783 -16.672 1.00 91.74 O ANISOU 3531 OE2 GLU B 147 10122 11962 12773 -67 -579 -1081 O ATOM 3532 N LEU B 148 34.870 -3.695 -17.593 1.00 54.33 N ANISOU 3532 N LEU B 148 5727 7260 7654 197 -576 -840 N ATOM 3533 CA LEU B 148 33.480 -4.159 -17.524 1.00 52.85 C ANISOU 3533 CA LEU B 148 5682 7061 7337 197 -561 -776 C ATOM 3534 C LEU B 148 32.767 -3.739 -16.244 1.00 46.96 C ANISOU 3534 C LEU B 148 5010 6339 6495 195 -650 -756 C ATOM 3535 O LEU B 148 31.561 -3.942 -16.099 1.00 45.69 O ANISOU 3535 O LEU B 148 4958 6173 6229 186 -633 -704 O ATOM 3536 CB LEU B 148 33.437 -5.685 -17.647 1.00 45.84 C ANISOU 3536 CB LEU B 148 4828 6142 6447 265 -571 -748 C ATOM 3537 CG LEU B 148 34.145 -6.209 -18.897 1.00 54.34 C ANISOU 3537 CG LEU B 148 5830 7202 7612 279 -484 -787 C ATOM 3538 CD1 LEU B 148 34.009 -7.711 -19.016 1.00 61.59 C ANISOU 3538 CD1 LEU B 148 6786 8071 8543 344 -491 -773 C ATOM 3539 CD2 LEU B 148 33.583 -5.532 -20.136 1.00 47.06 C ANISOU 3539 CD2 LEU B 148 4926 6302 6654 214 -358 -790 C ATOM 3540 N THR B 149 33.529 -3.182 -15.313 1.00 35.42 N ANISOU 3540 N THR B 149 3480 4908 5069 207 -745 -806 N ATOM 3541 CA THR B 149 33.005 -2.743 -14.038 1.00 42.89 C ANISOU 3541 CA THR B 149 4483 5897 5918 216 -836 -808 C ATOM 3542 C THR B 149 32.403 -1.359 -14.242 1.00 53.36 C ANISOU 3542 C THR B 149 5823 7214 7237 134 -780 -839 C ATOM 3543 O THR B 149 33.118 -0.374 -14.449 1.00 56.00 O ANISOU 3543 O THR B 149 6061 7537 7679 89 -767 -909 O ATOM 3544 CB THR B 149 34.143 -2.645 -12.990 1.00 49.45 C ANISOU 3544 CB THR B 149 5217 6781 6790 266 -971 -874 C ATOM 3545 OG1 THR B 149 34.863 -3.884 -12.928 1.00 49.38 O ANISOU 3545 OG1 THR B 149 5174 6771 6816 350 -1018 -841 O ATOM 3546 CG2 THR B 149 33.601 -2.306 -11.629 1.00 34.48 C ANISOU 3546 CG2 THR B 149 3384 4952 4765 290 -1071 -881 C ATOM 3547 N ILE B 150 31.086 -1.279 -14.183 1.00 48.54 N ANISOU 3547 N ILE B 150 5325 6602 6514 117 -742 -787 N ATOM 3548 CA ILE B 150 30.399 -0.031 -14.462 1.00 46.67 C ANISOU 3548 CA ILE B 150 5110 6348 6274 51 -679 -803 C ATOM 3549 C ILE B 150 29.844 0.598 -13.192 1.00 48.79 C ANISOU 3549 C ILE B 150 5424 6656 6457 56 -756 -839 C ATOM 3550 O ILE B 150 29.252 -0.085 -12.362 1.00 47.51 O ANISOU 3550 O ILE B 150 5340 6539 6174 103 -810 -798 O ATOM 3551 CB ILE B 150 29.259 -0.284 -15.430 1.00 49.11 C ANISOU 3551 CB ILE B 150 5501 6635 6522 29 -575 -728 C ATOM 3552 CG1 ILE B 150 29.808 -0.994 -16.668 1.00 52.00 C ANISOU 3552 CG1 ILE B 150 5825 6981 6954 34 -503 -709 C ATOM 3553 CG2 ILE B 150 28.529 1.031 -15.776 1.00 44.97 C ANISOU 3553 CG2 ILE B 150 4997 6092 5999 -27 -507 -730 C ATOM 3554 CD1 ILE B 150 30.945 -0.261 -17.345 1.00 43.96 C ANISOU 3554 CD1 ILE B 150 4690 5943 6069 3 -456 -752 C ATOM 3555 N ASP B 151 30.062 1.896 -13.023 1.00 51.33 N ANISOU 3555 N ASP B 151 5694 6961 6847 10 -756 -917 N ATOM 3556 CA ASP B 151 29.413 2.623 -11.937 1.00 53.72 C ANISOU 3556 CA ASP B 151 6042 7298 7071 11 -812 -969 C ATOM 3557 C ASP B 151 28.145 3.294 -12.476 1.00 48.92 C ANISOU 3557 C ASP B 151 5509 6650 6429 -30 -711 -924 C ATOM 3558 O ASP B 151 28.188 3.958 -13.515 1.00 54.29 O ANISOU 3558 O ASP B 151 6154 7263 7209 -79 -617 -909 O ATOM 3559 CB ASP B 151 30.362 3.669 -11.347 1.00 64.48 C ANISOU 3559 CB ASP B 151 7298 8659 8542 -14 -880 -1106 C ATOM 3560 CG ASP B 151 29.785 4.357 -10.106 1.00 78.73 C ANISOU 3560 CG ASP B 151 9142 10516 10254 -1 -954 -1189 C ATOM 3561 OD1 ASP B 151 28.982 3.727 -9.377 1.00 78.36 O ANISOU 3561 OD1 ASP B 151 9193 10543 10037 53 -989 -1139 O ATOM 3562 OD2 ASP B 151 30.146 5.528 -9.854 1.00 88.13 O ANISOU 3562 OD2 ASP B 151 10263 11673 11549 -44 -970 -1309 O ATOM 3563 N HIS B 152 27.012 3.102 -11.803 1.00 40.74 N ANISOU 3563 N HIS B 152 4569 5658 5251 -4 -724 -893 N ATOM 3564 CA HIS B 152 25.751 3.698 -12.282 1.00 45.63 C ANISOU 3564 CA HIS B 152 5253 6248 5838 -33 -635 -851 C ATOM 3565 C HIS B 152 25.289 4.859 -11.400 1.00 47.84 C ANISOU 3565 C HIS B 152 5542 6534 6101 -41 -661 -937 C ATOM 3566 O HIS B 152 25.599 4.897 -10.218 1.00 52.76 O ANISOU 3566 O HIS B 152 6158 7219 6670 -9 -756 -1015 O ATOM 3567 CB HIS B 152 24.652 2.640 -12.378 1.00 39.50 C ANISOU 3567 CB HIS B 152 4569 5506 4933 -7 -605 -750 C ATOM 3568 CG HIS B 152 24.883 1.627 -13.453 1.00 46.09 C ANISOU 3568 CG HIS B 152 5397 6317 5797 -8 -558 -680 C ATOM 3569 ND1 HIS B 152 24.842 1.945 -14.795 1.00 48.83 N ANISOU 3569 ND1 HIS B 152 5719 6621 6212 -43 -467 -653 N ATOM 3570 CD2 HIS B 152 25.163 0.304 -13.387 1.00 42.55 C ANISOU 3570 CD2 HIS B 152 4962 5883 5321 27 -587 -637 C ATOM 3571 CE1 HIS B 152 25.082 0.857 -15.508 1.00 48.03 C ANISOU 3571 CE1 HIS B 152 5616 6519 6115 -30 -446 -612 C ATOM 3572 NE2 HIS B 152 25.280 -0.151 -14.678 1.00 46.88 N ANISOU 3572 NE2 HIS B 152 5492 6396 5925 10 -516 -604 N ATOM 3573 N PRO B 153 24.538 5.809 -11.971 1.00 51.39 N ANISOU 3573 N PRO B 153 6006 6925 6594 -74 -577 -925 N ATOM 3574 CA PRO B 153 24.045 6.915 -11.139 1.00 49.53 C ANISOU 3574 CA PRO B 153 5779 6684 6355 -76 -595 -1017 C ATOM 3575 C PRO B 153 23.168 6.410 -9.999 1.00 48.78 C ANISOU 3575 C PRO B 153 5764 6690 6080 -26 -645 -1019 C ATOM 3576 O PRO B 153 23.162 7.014 -8.925 1.00 52.04 O ANISOU 3576 O PRO B 153 6173 7143 6459 -8 -705 -1129 O ATOM 3577 CB PRO B 153 23.208 7.760 -12.108 1.00 48.39 C ANISOU 3577 CB PRO B 153 5651 6460 6276 -105 -483 -960 C ATOM 3578 CG PRO B 153 23.567 7.294 -13.467 1.00 56.71 C ANISOU 3578 CG PRO B 153 6682 7479 7385 -125 -414 -859 C ATOM 3579 CD PRO B 153 24.070 5.894 -13.362 1.00 53.04 C ANISOU 3579 CD PRO B 153 6226 7081 6848 -100 -466 -829 C ATOM 3580 N HIS B 154 22.456 5.309 -10.221 1.00 49.12 N ANISOU 3580 N HIS B 154 5874 6776 6014 -4 -617 -906 N ATOM 3581 CA HIS B 154 21.511 4.796 -9.231 1.00 51.83 C ANISOU 3581 CA HIS B 154 6293 7209 6193 39 -637 -881 C ATOM 3582 C HIS B 154 22.137 4.623 -7.857 1.00 61.78 C ANISOU 3582 C HIS B 154 7548 8561 7367 86 -746 -956 C ATOM 3583 O HIS B 154 21.500 4.887 -6.845 1.00 69.23 O ANISOU 3583 O HIS B 154 8531 9580 8192 120 -766 -997 O ATOM 3584 CB HIS B 154 20.915 3.470 -9.697 1.00 41.46 C ANISOU 3584 CB HIS B 154 5032 5912 4810 47 -596 -749 C ATOM 3585 CG HIS B 154 20.272 3.549 -11.038 1.00 46.19 C ANISOU 3585 CG HIS B 154 5632 6448 5469 9 -503 -685 C ATOM 3586 ND1 HIS B 154 20.993 3.792 -12.189 1.00 47.35 N ANISOU 3586 ND1 HIS B 154 5726 6529 5738 -21 -471 -681 N ATOM 3587 CD2 HIS B 154 18.974 3.431 -11.417 1.00 39.40 C ANISOU 3587 CD2 HIS B 154 4816 5597 4559 3 -435 -625 C ATOM 3588 CE1 HIS B 154 20.166 3.815 -13.221 1.00 57.29 C ANISOU 3588 CE1 HIS B 154 7000 7766 7001 -39 -392 -618 C ATOM 3589 NE2 HIS B 154 18.940 3.588 -12.782 1.00 55.96 N ANISOU 3589 NE2 HIS B 154 6886 7641 6734 -26 -375 -588 N ATOM 3590 N THR B 155 23.385 4.172 -7.829 1.00 58.11 N ANISOU 3590 N THR B 155 7028 8101 6952 97 -817 -976 N ATOM 3591 CA THR B 155 24.098 3.962 -6.576 1.00 63.76 C ANISOU 3591 CA THR B 155 7726 8918 7582 153 -936 -1045 C ATOM 3592 C THR B 155 24.148 5.237 -5.738 1.00 70.25 C ANISOU 3592 C THR B 155 8517 9774 8403 153 -985 -1211 C ATOM 3593 O THR B 155 23.911 5.218 -4.532 1.00 79.78 O ANISOU 3593 O THR B 155 9756 11099 9457 209 -1050 -1261 O ATOM 3594 CB THR B 155 25.534 3.498 -6.847 1.00 67.43 C ANISOU 3594 CB THR B 155 8108 9367 8143 159 -1004 -1061 C ATOM 3595 OG1 THR B 155 25.501 2.172 -7.379 1.00 64.07 O ANISOU 3595 OG1 THR B 155 7718 8926 7698 179 -973 -920 O ATOM 3596 CG2 THR B 155 26.353 3.507 -5.566 1.00 70.09 C ANISOU 3596 CG2 THR B 155 8407 9820 8405 221 -1143 -1159 C ATOM 3597 N HIS B 156 24.455 6.346 -6.394 1.00 66.51 N ANISOU 3597 N HIS B 156 7977 9194 8101 91 -949 -1297 N ATOM 3598 CA HIS B 156 24.592 7.621 -5.715 1.00 63.77 C ANISOU 3598 CA HIS B 156 7584 8845 7802 80 -991 -1474 C ATOM 3599 C HIS B 156 23.248 8.286 -5.405 1.00 71.65 C ANISOU 3599 C HIS B 156 8649 9845 8728 87 -925 -1492 C ATOM 3600 O HIS B 156 23.153 9.055 -4.447 1.00 73.82 O ANISOU 3600 O HIS B 156 8913 10170 8965 108 -976 -1642 O ATOM 3601 CB HIS B 156 25.483 8.535 -6.542 1.00 60.74 C ANISOU 3601 CB HIS B 156 7096 8325 7660 7 -966 -1549 C ATOM 3602 CG HIS B 156 26.758 7.881 -6.958 1.00 66.04 C ANISOU 3602 CG HIS B 156 7690 8990 8412 -2 -1013 -1526 C ATOM 3603 ND1 HIS B 156 27.910 7.952 -6.206 1.00 64.24 N ANISOU 3603 ND1 HIS B 156 7372 8822 8213 14 -1137 -1659 N ATOM 3604 CD2 HIS B 156 27.054 7.103 -8.027 1.00 67.05 C ANISOU 3604 CD2 HIS B 156 7813 9070 8592 -18 -954 -1392 C ATOM 3605 CE1 HIS B 156 28.865 7.259 -6.802 1.00 64.26 C ANISOU 3605 CE1 HIS B 156 7314 8807 8293 8 -1150 -1601 C ATOM 3606 NE2 HIS B 156 28.374 6.739 -7.911 1.00 61.13 N ANISOU 3606 NE2 HIS B 156 6971 8344 7911 -11 -1036 -1442 N ATOM 3607 N VAL B 157 22.216 7.985 -6.198 1.00 62.49 N ANISOU 3607 N VAL B 157 7552 8639 7551 74 -818 -1351 N ATOM 3608 CA VAL B 157 20.886 8.524 -5.927 1.00 68.75 C ANISOU 3608 CA VAL B 157 8403 9443 8275 88 -753 -1356 C ATOM 3609 C VAL B 157 20.381 7.940 -4.624 1.00 79.03 C ANISOU 3609 C VAL B 157 9767 10905 9357 156 -802 -1365 C ATOM 3610 O VAL B 157 20.124 8.667 -3.669 1.00 83.30 O ANISOU 3610 O VAL B 157 10309 11506 9836 186 -833 -1498 O ATOM 3611 CB VAL B 157 19.867 8.210 -7.041 1.00 62.50 C ANISOU 3611 CB VAL B 157 7657 8591 7500 66 -638 -1202 C ATOM 3612 CG1 VAL B 157 18.465 8.592 -6.590 1.00 65.40 C ANISOU 3612 CG1 VAL B 157 8078 8997 7773 94 -583 -1204 C ATOM 3613 CG2 VAL B 157 20.222 8.942 -8.309 1.00 56.34 C ANISOU 3613 CG2 VAL B 157 6822 7668 6915 12 -576 -1185 C ATOM 3614 N VAL B 158 20.243 6.620 -4.600 1.00 86.64 N ANISOU 3614 N VAL B 158 10780 11933 10205 183 -803 -1222 N ATOM 3615 CA VAL B 158 19.923 5.890 -3.381 1.00 94.44 C ANISOU 3615 CA VAL B 158 11826 13076 10982 253 -846 -1193 C ATOM 3616 C VAL B 158 20.581 6.514 -2.147 1.00 94.83 C ANISOU 3616 C VAL B 158 11843 13232 10956 300 -956 -1367 C ATOM 3617 O VAL B 158 19.904 6.835 -1.176 1.00 90.69 O ANISOU 3617 O VAL B 158 11356 12815 10286 347 -956 -1429 O ATOM 3618 CB VAL B 158 20.335 4.409 -3.501 1.00 94.69 C ANISOU 3618 CB VAL B 158 11884 13136 10960 275 -868 -1040 C ATOM 3619 CG1 VAL B 158 20.590 3.803 -2.129 1.00102.47 C ANISOU 3619 CG1 VAL B 158 12901 14283 11749 360 -952 -1033 C ATOM 3620 CG2 VAL B 158 19.268 3.632 -4.254 1.00 84.67 C ANISOU 3620 CG2 VAL B 158 10668 11816 9686 249 -757 -879 C ATOM 3621 N LYS B 159 21.896 6.700 -2.188 1.00 98.49 N ANISOU 3621 N LYS B 159 12229 13676 11518 290 -1051 -1458 N ATOM 3622 CA LYS B 159 22.588 7.306 -1.059 1.00104.86 C ANISOU 3622 CA LYS B 159 12988 14590 12263 332 -1171 -1648 C ATOM 3623 C LYS B 159 21.930 8.620 -0.679 1.00101.57 C ANISOU 3623 C LYS B 159 12566 14158 11870 320 -1140 -1813 C ATOM 3624 O LYS B 159 21.465 8.783 0.447 1.00104.69 O ANISOU 3624 O LYS B 159 12997 14697 12085 384 -1172 -1894 O ATOM 3625 CB LYS B 159 24.074 7.518 -1.360 1.00115.49 C ANISOU 3625 CB LYS B 159 14226 15885 13772 302 -1264 -1744 C ATOM 3626 CG LYS B 159 24.845 6.216 -1.527 1.00126.79 C ANISOU 3626 CG LYS B 159 15653 17355 15168 335 -1316 -1606 C ATOM 3627 CD LYS B 159 26.300 6.341 -1.093 1.00132.97 C ANISOU 3627 CD LYS B 159 16327 18190 16004 354 -1460 -1741 C ATOM 3628 CE LYS B 159 27.011 4.993 -1.189 1.00135.11 C ANISOU 3628 CE LYS B 159 16596 18506 16232 406 -1511 -1595 C ATOM 3629 NZ LYS B 159 28.279 4.961 -0.405 1.00136.00 N ANISOU 3629 NZ LYS B 159 16615 18735 16322 462 -1676 -1718 N ATOM 3630 N CYS B 160 21.871 9.542 -1.632 1.00 98.39 N ANISOU 3630 N CYS B 160 12118 13581 11687 245 -1071 -1857 N ATOM 3631 CA CYS B 160 21.361 10.883 -1.368 1.00 95.76 C ANISOU 3631 CA CYS B 160 11765 13194 11426 231 -1040 -2024 C ATOM 3632 C CYS B 160 19.896 10.933 -0.919 1.00 96.19 C ANISOU 3632 C CYS B 160 11905 13317 11328 275 -959 -1985 C ATOM 3633 O CYS B 160 19.586 11.500 0.127 1.00 93.84 O ANISOU 3633 O CYS B 160 11613 13118 10925 323 -992 -2140 O ATOM 3634 CB CYS B 160 21.554 11.788 -2.580 1.00 87.03 C ANISOU 3634 CB CYS B 160 10598 11871 10597 146 -965 -2033 C ATOM 3635 SG CYS B 160 20.805 13.410 -2.342 1.00 98.43 S ANISOU 3635 SG CYS B 160 12023 13215 12159 136 -908 -2211 S ATOM 3636 N THR B 161 19.001 10.350 -1.710 1.00 96.55 N ANISOU 3636 N THR B 161 12008 13315 11363 260 -852 -1791 N ATOM 3637 CA THR B 161 17.569 10.450 -1.435 1.00101.60 C ANISOU 3637 CA THR B 161 12710 14000 11892 293 -761 -1751 C ATOM 3638 C THR B 161 17.193 9.876 -0.079 1.00116.79 C ANISOU 3638 C THR B 161 14689 16133 13553 373 -798 -1764 C ATOM 3639 O THR B 161 16.102 10.137 0.429 1.00124.08 O ANISOU 3639 O THR B 161 15652 17122 14373 410 -732 -1781 O ATOM 3640 CB THR B 161 16.736 9.726 -2.482 1.00 92.62 C ANISOU 3640 CB THR B 161 11615 12801 10776 264 -657 -1538 C ATOM 3641 OG1 THR B 161 16.938 8.314 -2.346 1.00 96.79 O ANISOU 3641 OG1 THR B 161 12183 13417 11176 282 -681 -1391 O ATOM 3642 CG2 THR B 161 17.130 10.176 -3.877 1.00 90.63 C ANISOU 3642 CG2 THR B 161 11314 12369 10754 196 -618 -1499 C ATOM 3643 N GLN B 162 18.081 9.075 0.497 1.00120.03 N ANISOU 3643 N GLN B 162 15101 16654 13851 408 -896 -1744 N ATOM 3644 CA GLN B 162 17.878 8.608 1.861 1.00120.31 C ANISOU 3644 CA GLN B 162 15184 16904 13623 497 -942 -1760 C ATOM 3645 C GLN B 162 18.473 9.591 2.857 1.00117.27 C ANISOU 3645 C GLN B 162 14750 16610 13197 536 -1048 -2021 C ATOM 3646 O GLN B 162 17.807 9.999 3.808 1.00116.94 O ANISOU 3646 O GLN B 162 14737 16697 12998 595 -1034 -2121 O ATOM 3647 CB GLN B 162 18.441 7.204 2.058 1.00117.48 C ANISOU 3647 CB GLN B 162 14858 16633 13144 533 -993 -1590 C ATOM 3648 CG GLN B 162 17.392 6.135 1.856 1.00121.56 C ANISOU 3648 CG GLN B 162 15452 17165 13569 538 -881 -1359 C ATOM 3649 CD GLN B 162 17.973 4.835 1.363 1.00130.36 C ANISOU 3649 CD GLN B 162 16581 18243 14707 531 -900 -1173 C ATOM 3650 OE1 GLN B 162 19.188 4.703 1.219 1.00138.77 O ANISOU 3650 OE1 GLN B 162 17597 19287 15841 531 -1001 -1212 O ATOM 3651 NE2 GLN B 162 17.107 3.863 1.092 1.00128.52 N ANISOU 3651 NE2 GLN B 162 16404 17995 14431 523 -800 -978 N ATOM 3652 N LEU B 163 19.717 9.989 2.618 1.00115.75 N ANISOU 3652 N LEU B 163 14475 16350 13155 501 -1149 -2141 N ATOM 3653 CA LEU B 163 20.381 10.963 3.474 1.00120.06 C ANISOU 3653 CA LEU B 163 14953 16964 13702 525 -1260 -2417 C ATOM 3654 C LEU B 163 19.796 12.374 3.318 1.00115.32 C ANISOU 3654 C LEU B 163 14321 16238 13258 487 -1195 -2597 C ATOM 3655 O LEU B 163 20.445 13.360 3.654 1.00118.57 O ANISOU 3655 O LEU B 163 14651 16618 13780 471 -1272 -2840 O ATOM 3656 CB LEU B 163 21.893 10.959 3.219 1.00125.13 C ANISOU 3656 CB LEU B 163 15499 17560 14486 490 -1383 -2494 C ATOM 3657 CG LEU B 163 22.587 9.598 3.368 1.00126.74 C ANISOU 3657 CG LEU B 163 15721 17876 14558 538 -1458 -2327 C ATOM 3658 CD1 LEU B 163 24.075 9.698 3.058 1.00125.65 C ANISOU 3658 CD1 LEU B 163 15470 17684 14589 501 -1574 -2420 C ATOM 3659 CD2 LEU B 163 22.367 9.018 4.757 1.00128.84 C ANISOU 3659 CD2 LEU B 163 16047 18407 14498 658 -1527 -2325 C ATOM 3660 N VAL B 164 18.574 12.460 2.796 1.00110.65 N ANISOU 3660 N VAL B 164 13785 15569 12689 473 -1055 -2480 N ATOM 3661 CA VAL B 164 17.815 13.711 2.773 1.00111.98 C ANISOU 3661 CA VAL B 164 13936 15639 12971 462 -983 -2628 C ATOM 3662 C VAL B 164 16.344 13.421 3.065 1.00117.91 C ANISOU 3662 C VAL B 164 14770 16479 13553 514 -869 -2522 C ATOM 3663 O VAL B 164 15.498 14.321 3.026 1.00114.81 O ANISOU 3663 O VAL B 164 14372 16017 13234 518 -790 -2609 O ATOM 3664 CB VAL B 164 17.924 14.460 1.425 1.00108.62 C ANISOU 3664 CB VAL B 164 13460 14946 12866 370 -912 -2601 C ATOM 3665 CG1 VAL B 164 19.361 14.888 1.159 1.00106.73 C ANISOU 3665 CG1 VAL B 164 13123 14608 12822 311 -1009 -2724 C ATOM 3666 CG2 VAL B 164 17.378 13.603 0.287 1.00107.10 C ANISOU 3666 CG2 VAL B 164 13316 14680 12696 338 -814 -2320 C ATOM 3667 N ARG B 165 16.055 12.154 3.354 1.00120.66 N ANISOU 3667 N ARG B 165 15186 16974 13687 553 -857 -2330 N ATOM 3668 CA ARG B 165 14.713 11.716 3.726 1.00121.03 C ANISOU 3668 CA ARG B 165 15303 17126 13558 601 -747 -2214 C ATOM 3669 C ARG B 165 13.656 12.190 2.736 1.00124.73 C ANISOU 3669 C ARG B 165 15769 17428 14194 555 -616 -2143 C ATOM 3670 O ARG B 165 12.744 12.940 3.090 1.00129.07 O ANISOU 3670 O ARG B 165 16318 17992 14729 588 -549 -2242 O ATOM 3671 CB ARG B 165 14.378 12.155 5.152 1.00122.83 C ANISOU 3671 CB ARG B 165 15546 17556 13567 692 -772 -2394 C ATOM 3672 CG ARG B 165 15.074 11.310 6.202 1.00131.09 C ANISOU 3672 CG ARG B 165 16622 18830 14358 764 -877 -2378 C ATOM 3673 CD ARG B 165 15.298 12.069 7.493 1.00142.53 C ANISOU 3673 CD ARG B 165 18050 20457 15647 844 -960 -2648 C ATOM 3674 NE ARG B 165 16.328 11.428 8.308 1.00153.19 N ANISOU 3674 NE ARG B 165 19401 21997 16807 906 -1102 -2663 N ATOM 3675 CZ ARG B 165 16.815 11.933 9.437 1.00161.96 C ANISOU 3675 CZ ARG B 165 20484 23294 17759 982 -1215 -2902 C ATOM 3676 NH1 ARG B 165 17.753 11.277 10.109 1.00161.87 N ANISOU 3676 NH1 ARG B 165 20470 23462 17572 1046 -1351 -2891 N ATOM 3677 NH2 ARG B 165 16.365 13.095 9.895 1.00166.42 N ANISOU 3677 NH2 ARG B 165 21019 23869 18343 1000 -1197 -3158 N ATOM 3678 N ALA B 166 13.801 11.740 1.492 1.00119.87 N ANISOU 3678 N ALA B 166 15146 16665 13733 486 -584 -1974 N ATOM 3679 CA ALA B 166 12.843 12.027 0.433 1.00111.92 C ANISOU 3679 CA ALA B 166 14135 15517 12871 448 -471 -1875 C ATOM 3680 C ALA B 166 11.709 11.020 0.495 1.00105.11 C ANISOU 3680 C ALA B 166 13327 14752 11856 468 -381 -1690 C ATOM 3681 O ALA B 166 11.921 9.875 0.888 1.00103.94 O ANISOU 3681 O ALA B 166 13219 14715 11557 481 -403 -1572 O ATOM 3682 CB ALA B 166 13.525 11.953 -0.921 1.00110.49 C ANISOU 3682 CB ALA B 166 13921 15160 12899 373 -478 -1781 C ATOM 3683 N SER B 167 10.508 11.444 0.110 1.00100.48 N ANISOU 3683 N SER B 167 12735 14119 11322 470 -277 -1662 N ATOM 3684 CA SER B 167 9.368 10.535 0.058 1.00 92.52 C ANISOU 3684 CA SER B 167 11760 13187 10206 476 -183 -1492 C ATOM 3685 C SER B 167 9.719 9.345 -0.825 1.00 91.49 C ANISOU 3685 C SER B 167 11643 13007 10112 419 -191 -1299 C ATOM 3686 O SER B 167 10.649 9.425 -1.638 1.00 94.60 O ANISOU 3686 O SER B 167 12015 13285 10644 375 -248 -1294 O ATOM 3687 CB SER B 167 8.113 11.252 -0.459 1.00 86.82 C ANISOU 3687 CB SER B 167 11007 12397 9581 482 -81 -1496 C ATOM 3688 OG SER B 167 8.336 11.899 -1.701 1.00 84.02 O ANISOU 3688 OG SER B 167 10613 11861 9451 439 -84 -1488 O ATOM 3689 N LYS B 168 9.009 8.233 -0.661 1.00 86.31 N ANISOU 3689 N LYS B 168 11019 12434 9340 419 -130 -1144 N ATOM 3690 CA LYS B 168 9.268 7.099 -1.530 1.00 94.55 C ANISOU 3690 CA LYS B 168 12071 13416 10436 364 -132 -976 C ATOM 3691 C LYS B 168 9.086 7.616 -2.940 1.00 88.16 C ANISOU 3691 C LYS B 168 11218 12454 9826 314 -110 -965 C ATOM 3692 O LYS B 168 9.928 7.403 -3.813 1.00 88.95 O ANISOU 3692 O LYS B 168 11306 12459 10033 273 -157 -930 O ATOM 3693 CB LYS B 168 8.341 5.915 -1.238 1.00110.68 C ANISOU 3693 CB LYS B 168 14143 15543 12368 361 -50 -817 C ATOM 3694 CG LYS B 168 8.874 4.994 -0.144 1.00125.11 C ANISOU 3694 CG LYS B 168 16022 17496 14018 401 -83 -753 C ATOM 3695 CD LYS B 168 8.385 3.560 -0.301 1.00133.79 C ANISOU 3695 CD LYS B 168 17144 18600 15090 370 -17 -553 C ATOM 3696 CE LYS B 168 8.962 2.669 0.799 1.00138.65 C ANISOU 3696 CE LYS B 168 17815 19333 15533 423 -49 -468 C ATOM 3697 NZ LYS B 168 8.455 1.267 0.735 1.00139.15 N ANISOU 3697 NZ LYS B 168 17900 19385 15585 394 30 -264 N ATOM 3698 N ASP B 169 7.986 8.333 -3.129 1.00 80.39 N ANISOU 3698 N ASP B 169 10207 11456 8882 328 -37 -996 N ATOM 3699 CA ASP B 169 7.706 9.026 -4.368 1.00 80.97 C ANISOU 3699 CA ASP B 169 10236 11400 9128 304 -14 -991 C ATOM 3700 C ASP B 169 8.955 9.701 -4.962 1.00 77.01 C ANISOU 3700 C ASP B 169 9718 10778 8765 282 -85 -1056 C ATOM 3701 O ASP B 169 9.343 9.418 -6.106 1.00 69.39 O ANISOU 3701 O ASP B 169 8738 9727 7900 239 -93 -973 O ATOM 3702 CB ASP B 169 6.623 10.070 -4.122 1.00 96.05 C ANISOU 3702 CB ASP B 169 12117 13316 11060 350 52 -1072 C ATOM 3703 CG ASP B 169 6.067 10.638 -5.402 1.00106.35 C ANISOU 3703 CG ASP B 169 13376 14510 12522 339 89 -1027 C ATOM 3704 OD1 ASP B 169 5.309 9.912 -6.080 1.00115.49 O ANISOU 3704 OD1 ASP B 169 14518 15686 13676 316 130 -908 O ATOM 3705 OD2 ASP B 169 6.384 11.804 -5.727 1.00105.11 O ANISOU 3705 OD2 ASP B 169 13196 14247 12493 357 76 -1110 O ATOM 3706 N LEU B 170 9.580 10.599 -4.203 1.00 67.11 N ANISOU 3706 N LEU B 170 8459 9518 7521 309 -131 -1210 N ATOM 3707 CA LEU B 170 10.714 11.343 -4.741 1.00 71.15 C ANISOU 3707 CA LEU B 170 8940 9904 8192 282 -187 -1281 C ATOM 3708 C LEU B 170 11.867 10.412 -5.137 1.00 75.56 C ANISOU 3708 C LEU B 170 9504 10452 8752 239 -251 -1207 C ATOM 3709 O LEU B 170 12.427 10.532 -6.229 1.00 76.27 O ANISOU 3709 O LEU B 170 9567 10432 8980 198 -252 -1158 O ATOM 3710 CB LEU B 170 11.200 12.419 -3.767 1.00 71.84 C ANISOU 3710 CB LEU B 170 9010 9990 8298 313 -232 -1485 C ATOM 3711 CG LEU B 170 12.176 13.420 -4.398 1.00 72.06 C ANISOU 3711 CG LEU B 170 8987 9853 8542 278 -264 -1566 C ATOM 3712 CD1 LEU B 170 11.474 14.251 -5.456 1.00 70.70 C ANISOU 3712 CD1 LEU B 170 8788 9541 8536 276 -182 -1511 C ATOM 3713 CD2 LEU B 170 12.801 14.319 -3.357 1.00 73.11 C ANISOU 3713 CD2 LEU B 170 9094 9990 8694 299 -327 -1789 C ATOM 3714 N ALA B 171 12.213 9.482 -4.254 1.00 71.92 N ANISOU 3714 N ALA B 171 9079 10112 8137 255 -298 -1192 N ATOM 3715 CA ALA B 171 13.292 8.539 -4.537 1.00 68.86 C ANISOU 3715 CA ALA B 171 8694 9719 7749 227 -360 -1122 C ATOM 3716 C ALA B 171 12.984 7.651 -5.754 1.00 63.18 C ANISOU 3716 C ALA B 171 7978 8945 7081 184 -312 -959 C ATOM 3717 O ALA B 171 13.859 7.386 -6.582 1.00 57.45 O ANISOU 3717 O ALA B 171 7231 8146 6451 149 -340 -923 O ATOM 3718 CB ALA B 171 13.588 7.689 -3.311 1.00 65.12 C ANISOU 3718 CB ALA B 171 8260 9392 7090 269 -414 -1117 C ATOM 3719 N GLN B 172 11.742 7.194 -5.864 1.00 62.37 N ANISOU 3719 N GLN B 172 7896 8883 6919 188 -237 -873 N ATOM 3720 CA GLN B 172 11.347 6.366 -6.998 1.00 60.99 C ANISOU 3720 CA GLN B 172 7716 8667 6792 148 -196 -744 C ATOM 3721 C GLN B 172 11.402 7.145 -8.309 1.00 60.92 C ANISOU 3721 C GLN B 172 7666 8548 6933 124 -174 -744 C ATOM 3722 O GLN B 172 11.815 6.620 -9.335 1.00 60.12 O ANISOU 3722 O GLN B 172 7552 8399 6892 91 -178 -676 O ATOM 3723 CB GLN B 172 9.949 5.803 -6.788 1.00 59.47 C ANISOU 3723 CB GLN B 172 7536 8542 6517 153 -121 -670 C ATOM 3724 CG GLN B 172 9.896 4.578 -5.893 1.00 79.38 C ANISOU 3724 CG GLN B 172 10100 11152 8909 160 -120 -596 C ATOM 3725 CD GLN B 172 8.606 3.785 -6.087 1.00 96.71 C ANISOU 3725 CD GLN B 172 12290 13378 11078 138 -36 -496 C ATOM 3726 OE1 GLN B 172 7.967 3.855 -7.145 1.00 91.03 O ANISOU 3726 OE1 GLN B 172 11533 12609 10447 107 0 -471 O ATOM 3727 NE2 GLN B 172 8.222 3.021 -5.067 1.00105.01 N ANISOU 3727 NE2 GLN B 172 13374 14516 12009 155 -3 -435 N ATOM 3728 N THR B 173 10.983 8.401 -8.266 1.00 55.95 N ANISOU 3728 N THR B 173 7015 7881 6361 148 -149 -819 N ATOM 3729 CA THR B 173 11.035 9.254 -9.434 1.00 53.27 C ANISOU 3729 CA THR B 173 6639 7436 6166 138 -122 -805 C ATOM 3730 C THR B 173 12.493 9.506 -9.849 1.00 54.08 C ANISOU 3730 C THR B 173 6721 7456 6372 108 -169 -833 C ATOM 3731 O THR B 173 12.791 9.646 -11.035 1.00 47.55 O ANISOU 3731 O THR B 173 5870 6558 5639 87 -147 -769 O ATOM 3732 CB THR B 173 10.315 10.596 -9.163 1.00 57.19 C ANISOU 3732 CB THR B 173 7117 7894 6719 179 -82 -882 C ATOM 3733 OG1 THR B 173 8.956 10.341 -8.790 1.00 66.05 O ANISOU 3733 OG1 THR B 173 8247 9101 7749 208 -33 -857 O ATOM 3734 CG2 THR B 173 10.330 11.495 -10.393 1.00 47.01 C ANISOU 3734 CG2 THR B 173 5791 6488 5583 179 -46 -840 C ATOM 3735 N SER B 174 13.399 9.564 -8.876 1.00 43.71 N ANISOU 3735 N SER B 174 5411 6161 5036 110 -234 -930 N ATOM 3736 CA SER B 174 14.809 9.800 -9.173 1.00 48.06 C ANISOU 3736 CA SER B 174 5927 6641 5695 79 -282 -970 C ATOM 3737 C SER B 174 15.453 8.591 -9.843 1.00 50.41 C ANISOU 3737 C SER B 174 6227 6953 5974 51 -301 -871 C ATOM 3738 O SER B 174 16.213 8.728 -10.814 1.00 47.41 O ANISOU 3738 O SER B 174 5812 6497 5706 21 -292 -840 O ATOM 3739 CB SER B 174 15.569 10.164 -7.905 1.00 50.31 C ANISOU 3739 CB SER B 174 6202 6960 5954 94 -359 -1117 C ATOM 3740 OG SER B 174 14.920 11.236 -7.256 1.00 60.20 O ANISOU 3740 OG SER B 174 7452 8204 7219 124 -339 -1227 O ATOM 3741 N TYR B 175 15.136 7.407 -9.329 1.00 45.70 N ANISOU 3741 N TYR B 175 5671 6450 5244 64 -319 -819 N ATOM 3742 CA TYR B 175 15.652 6.164 -9.892 1.00 54.19 C ANISOU 3742 CA TYR B 175 6751 7532 6305 43 -334 -731 C ATOM 3743 C TYR B 175 15.172 6.062 -11.350 1.00 48.91 C ANISOU 3743 C TYR B 175 6068 6814 5700 19 -269 -646 C ATOM 3744 O TYR B 175 15.939 5.754 -12.270 1.00 50.52 O ANISOU 3744 O TYR B 175 6247 6977 5972 -4 -269 -612 O ATOM 3745 CB TYR B 175 15.212 4.988 -9.003 1.00 56.98 C ANISOU 3745 CB TYR B 175 7153 7980 6516 65 -349 -681 C ATOM 3746 CG TYR B 175 15.597 3.585 -9.456 1.00 82.93 C ANISOU 3746 CG TYR B 175 10450 11265 9795 50 -359 -589 C ATOM 3747 CD1 TYR B 175 16.621 2.875 -8.814 1.00 90.36 C ANISOU 3747 CD1 TYR B 175 11397 12232 10704 71 -429 -588 C ATOM 3748 CD2 TYR B 175 14.903 2.944 -10.490 1.00 88.89 C ANISOU 3748 CD2 TYR B 175 11205 11995 10575 22 -302 -509 C ATOM 3749 CE1 TYR B 175 16.956 1.574 -9.209 1.00 85.51 C ANISOU 3749 CE1 TYR B 175 10790 11600 10098 64 -434 -504 C ATOM 3750 CE2 TYR B 175 15.231 1.648 -10.890 1.00 84.94 C ANISOU 3750 CE2 TYR B 175 10711 11482 10082 9 -308 -443 C ATOM 3751 CZ TYR B 175 16.254 0.973 -10.247 1.00 85.18 C ANISOU 3751 CZ TYR B 175 10750 11521 10095 30 -370 -437 C ATOM 3752 OH TYR B 175 16.570 -0.300 -10.650 1.00 83.96 O ANISOU 3752 OH TYR B 175 10599 11337 9966 23 -371 -373 O ATOM 3753 N PHE B 176 13.905 6.396 -11.548 1.00 43.78 N ANISOU 3753 N PHE B 176 5428 6181 5025 30 -214 -619 N ATOM 3754 CA PHE B 176 13.288 6.466 -12.866 1.00 37.56 C ANISOU 3754 CA PHE B 176 4622 5370 4280 21 -159 -549 C ATOM 3755 C PHE B 176 14.031 7.430 -13.788 1.00 43.59 C ANISOU 3755 C PHE B 176 5348 6049 5166 15 -142 -550 C ATOM 3756 O PHE B 176 14.237 7.139 -14.968 1.00 49.89 O ANISOU 3756 O PHE B 176 6128 6835 5992 3 -118 -486 O ATOM 3757 CB PHE B 176 11.822 6.884 -12.698 1.00 43.17 C ANISOU 3757 CB PHE B 176 5336 6117 4948 46 -113 -539 C ATOM 3758 CG PHE B 176 11.119 7.230 -13.975 1.00 43.78 C ANISOU 3758 CG PHE B 176 5385 6182 5066 55 -66 -477 C ATOM 3759 CD1 PHE B 176 10.353 6.279 -14.637 1.00 42.86 C ANISOU 3759 CD1 PHE B 176 5262 6123 4899 43 -50 -418 C ATOM 3760 CD2 PHE B 176 11.189 8.518 -14.496 1.00 43.59 C ANISOU 3760 CD2 PHE B 176 5338 6090 5135 78 -38 -479 C ATOM 3761 CE1 PHE B 176 9.678 6.597 -15.802 1.00 40.26 C ANISOU 3761 CE1 PHE B 176 4901 5807 4588 61 -19 -369 C ATOM 3762 CE2 PHE B 176 10.531 8.842 -15.675 1.00 48.53 C ANISOU 3762 CE2 PHE B 176 5938 6718 5782 101 2 -405 C ATOM 3763 CZ PHE B 176 9.769 7.878 -16.328 1.00 42.48 C ANISOU 3763 CZ PHE B 176 5165 6035 4942 96 6 -354 C ATOM 3764 N MET B 177 14.432 8.580 -13.255 1.00 43.68 N ANISOU 3764 N MET B 177 5343 6001 5251 23 -149 -624 N ATOM 3765 CA MET B 177 15.188 9.554 -14.039 1.00 43.34 C ANISOU 3765 CA MET B 177 5260 5859 5350 10 -122 -620 C ATOM 3766 C MET B 177 16.527 8.941 -14.459 1.00 49.00 C ANISOU 3766 C MET B 177 5951 6559 6106 -24 -149 -611 C ATOM 3767 O MET B 177 16.921 9.015 -15.636 1.00 43.91 O ANISOU 3767 O MET B 177 5281 5880 5522 -35 -105 -541 O ATOM 3768 CB MET B 177 15.452 10.825 -13.225 1.00 50.88 C ANISOU 3768 CB MET B 177 6194 6738 6399 16 -131 -728 C ATOM 3769 CG MET B 177 14.227 11.677 -12.874 1.00 44.37 C ANISOU 3769 CG MET B 177 5382 5904 5572 58 -93 -751 C ATOM 3770 SD MET B 177 13.328 12.156 -14.344 1.00 66.70 S ANISOU 3770 SD MET B 177 8199 8697 8448 86 -9 -612 S ATOM 3771 CE MET B 177 12.110 13.272 -13.613 1.00 59.32 C ANISOU 3771 CE MET B 177 7266 7733 7538 142 22 -676 C ATOM 3772 N ALA B 178 17.213 8.340 -13.482 1.00 38.01 N ANISOU 3772 N ALA B 178 4566 5204 4674 -31 -220 -678 N ATOM 3773 CA ALA B 178 18.499 7.675 -13.702 1.00 41.85 C ANISOU 3773 CA ALA B 178 5022 5684 5195 -54 -257 -681 C ATOM 3774 C ALA B 178 18.407 6.621 -14.800 1.00 47.51 C ANISOU 3774 C ALA B 178 5747 6431 5874 -60 -225 -584 C ATOM 3775 O ALA B 178 19.199 6.625 -15.747 1.00 49.06 O ANISOU 3775 O ALA B 178 5905 6593 6145 -77 -197 -554 O ATOM 3776 CB ALA B 178 19.017 7.049 -12.402 1.00 37.57 C ANISOU 3776 CB ALA B 178 4492 5201 4582 -42 -346 -752 C ATOM 3777 N THR B 179 17.424 5.732 -14.695 1.00 45.94 N ANISOU 3777 N THR B 179 5594 6298 5565 -46 -223 -542 N ATOM 3778 CA THR B 179 17.249 4.710 -15.726 1.00 41.17 C ANISOU 3778 CA THR B 179 4992 5721 4930 -53 -197 -474 C ATOM 3779 C THR B 179 16.954 5.306 -17.102 1.00 46.05 C ANISOU 3779 C THR B 179 5587 6326 5586 -52 -130 -420 C ATOM 3780 O THR B 179 17.531 4.882 -18.107 1.00 44.87 O ANISOU 3780 O THR B 179 5413 6178 5456 -59 -108 -390 O ATOM 3781 CB THR B 179 16.188 3.692 -15.327 1.00 39.69 C ANISOU 3781 CB THR B 179 4847 5594 4641 -47 -203 -448 C ATOM 3782 OG1 THR B 179 16.662 2.988 -14.181 1.00 41.26 O ANISOU 3782 OG1 THR B 179 5067 5808 4801 -41 -259 -472 O ATOM 3783 CG2 THR B 179 15.912 2.690 -16.474 1.00 29.75 C ANISOU 3783 CG2 THR B 179 3580 4356 3366 -59 -176 -402 C ATOM 3784 N ASN B 180 16.074 6.302 -17.154 1.00 39.99 N ANISOU 3784 N ASN B 180 4824 5548 4824 -34 -95 -405 N ATOM 3785 CA ASN B 180 15.748 6.912 -18.436 1.00 37.10 C ANISOU 3785 CA ASN B 180 4437 5178 4483 -17 -33 -334 C ATOM 3786 C ASN B 180 16.878 7.723 -19.048 1.00 44.71 C ANISOU 3786 C ASN B 180 5360 6068 5558 -27 4 -313 C ATOM 3787 O ASN B 180 16.968 7.817 -20.276 1.00 46.80 O ANISOU 3787 O ASN B 180 5607 6349 5824 -15 57 -239 O ATOM 3788 CB ASN B 180 14.451 7.716 -18.364 1.00 46.01 C ANISOU 3788 CB ASN B 180 5577 6315 5592 16 -6 -311 C ATOM 3789 CG ASN B 180 13.231 6.818 -18.418 1.00 48.90 C ANISOU 3789 CG ASN B 180 5959 6772 5848 25 -17 -298 C ATOM 3790 OD1 ASN B 180 12.830 6.357 -19.492 1.00 47.58 O ANISOU 3790 OD1 ASN B 180 5779 6663 5636 35 0 -251 O ATOM 3791 ND2 ASN B 180 12.665 6.525 -17.257 1.00 43.21 N ANISOU 3791 ND2 ASN B 180 5263 6071 5085 21 -44 -344 N ATOM 3792 N SER B 181 17.747 8.281 -18.201 1.00 37.05 N ANISOU 3792 N SER B 181 4371 5025 4680 -49 -21 -381 N ATOM 3793 CA SER B 181 18.924 9.001 -18.692 1.00 38.99 C ANISOU 3793 CA SER B 181 4564 5190 5059 -72 17 -372 C ATOM 3794 C SER B 181 19.851 8.049 -19.483 1.00 45.83 C ANISOU 3794 C SER B 181 5405 6095 5913 -87 25 -345 C ATOM 3795 O SER B 181 20.472 8.466 -20.455 1.00 44.58 O ANISOU 3795 O SER B 181 5207 5908 5823 -92 92 -286 O ATOM 3796 CB SER B 181 19.672 9.703 -17.551 1.00 34.74 C ANISOU 3796 CB SER B 181 3997 4574 4629 -98 -27 -478 C ATOM 3797 OG SER B 181 20.474 8.780 -16.827 1.00 49.12 O ANISOU 3797 OG SER B 181 5810 6435 6419 -114 -104 -551 O ATOM 3798 N LEU B 182 19.915 6.774 -19.093 1.00 39.55 N ANISOU 3798 N LEU B 182 4631 5363 5034 -88 -35 -383 N ATOM 3799 CA LEU B 182 20.618 5.762 -19.904 1.00 41.03 C ANISOU 3799 CA LEU B 182 4798 5590 5203 -91 -24 -364 C ATOM 3800 C LEU B 182 19.951 5.488 -21.256 1.00 46.95 C ANISOU 3800 C LEU B 182 5557 6405 5876 -68 37 -288 C ATOM 3801 O LEU B 182 20.625 5.418 -22.291 1.00 43.25 O ANISOU 3801 O LEU B 182 5054 5953 5427 -65 90 -252 O ATOM 3802 CB LEU B 182 20.771 4.437 -19.140 1.00 36.12 C ANISOU 3802 CB LEU B 182 4197 5003 4522 -90 -100 -416 C ATOM 3803 CG LEU B 182 21.679 4.478 -17.917 1.00 46.63 C ANISOU 3803 CG LEU B 182 5508 6300 5909 -100 -172 -489 C ATOM 3804 CD1 LEU B 182 21.598 3.166 -17.144 1.00 41.67 C ANISOU 3804 CD1 LEU B 182 4915 5712 5204 -84 -241 -508 C ATOM 3805 CD2 LEU B 182 23.117 4.781 -18.376 1.00 50.63 C ANISOU 3805 CD2 LEU B 182 5937 6763 6536 -119 -153 -508 C ATOM 3806 N HIS B 183 18.631 5.323 -21.251 1.00 41.40 N ANISOU 3806 N HIS B 183 4896 5752 5081 -48 28 -270 N ATOM 3807 CA HIS B 183 17.914 5.068 -22.500 1.00 39.77 C ANISOU 3807 CA HIS B 183 4693 5628 4791 -19 70 -214 C ATOM 3808 C HIS B 183 17.924 6.267 -23.434 1.00 35.86 C ANISOU 3808 C HIS B 183 4176 5124 4325 8 147 -124 C ATOM 3809 O HIS B 183 18.001 6.120 -24.647 1.00 45.70 O ANISOU 3809 O HIS B 183 5407 6438 5518 33 194 -71 O ATOM 3810 CB HIS B 183 16.439 4.722 -22.239 1.00 38.09 C ANISOU 3810 CB HIS B 183 4512 5471 4487 -6 41 -220 C ATOM 3811 CG HIS B 183 16.215 3.386 -21.611 1.00 41.06 C ANISOU 3811 CG HIS B 183 4909 5868 4823 -28 -14 -281 C ATOM 3812 ND1 HIS B 183 16.645 3.083 -20.337 1.00 54.42 N ANISOU 3812 ND1 HIS B 183 6619 7509 6548 -49 -61 -325 N ATOM 3813 CD2 HIS B 183 15.552 2.293 -22.055 1.00 45.36 C ANISOU 3813 CD2 HIS B 183 5456 6476 5301 -31 -27 -302 C ATOM 3814 CE1 HIS B 183 16.281 1.850 -20.034 1.00 56.06 C ANISOU 3814 CE1 HIS B 183 6845 7740 6716 -62 -92 -351 C ATOM 3815 NE2 HIS B 183 15.608 1.352 -21.054 1.00 49.13 N ANISOU 3815 NE2 HIS B 183 5957 6923 5790 -57 -70 -344 N ATOM 3816 N LEU B 184 17.793 7.460 -22.876 1.00 39.41 N ANISOU 3816 N LEU B 184 4626 5491 4856 8 162 -105 N ATOM 3817 CA LEU B 184 17.408 8.607 -23.705 1.00 48.07 C ANISOU 3817 CA LEU B 184 5713 6575 5976 47 235 1 C ATOM 3818 C LEU B 184 18.554 9.556 -24.052 1.00 48.86 C ANISOU 3818 C LEU B 184 5771 6579 6214 31 308 53 C ATOM 3819 O LEU B 184 18.466 10.304 -25.023 1.00 52.89 O ANISOU 3819 O LEU B 184 6269 7090 6735 67 388 170 O ATOM 3820 CB LEU B 184 16.250 9.377 -23.043 1.00 45.91 C ANISOU 3820 CB LEU B 184 5464 6270 5710 73 219 3 C ATOM 3821 CG LEU B 184 15.006 8.535 -22.736 1.00 45.89 C ANISOU 3821 CG LEU B 184 5490 6363 5583 88 162 -38 C ATOM 3822 CD1 LEU B 184 13.849 9.397 -22.299 1.00 54.62 C ANISOU 3822 CD1 LEU B 184 6607 7449 6698 125 165 -21 C ATOM 3823 CD2 LEU B 184 14.623 7.746 -23.960 1.00 45.44 C ANISOU 3823 CD2 LEU B 184 5426 6431 5407 115 171 3 C ATOM 3824 N THR B 185 19.625 9.521 -23.261 1.00 45.71 N ANISOU 3824 N THR B 185 5344 6101 5922 -22 281 -28 N ATOM 3825 CA THR B 185 20.719 10.469 -23.423 1.00 48.90 C ANISOU 3825 CA THR B 185 5693 6396 6490 -52 348 2 C ATOM 3826 C THR B 185 22.076 9.783 -23.503 1.00 57.32 C ANISOU 3826 C THR B 185 6710 7468 7601 -91 343 -48 C ATOM 3827 O THR B 185 22.200 8.575 -23.293 1.00 52.97 O ANISOU 3827 O THR B 185 6171 6992 6962 -93 280 -113 O ATOM 3828 CB THR B 185 20.805 11.452 -22.244 1.00 47.16 C ANISOU 3828 CB THR B 185 5461 6046 6413 -82 319 -74 C ATOM 3829 OG1 THR B 185 21.416 10.796 -21.130 1.00 48.90 O ANISOU 3829 OG1 THR B 185 5670 6267 6642 -120 226 -210 O ATOM 3830 CG2 THR B 185 19.436 11.963 -21.842 1.00 39.03 C ANISOU 3830 CG2 THR B 185 4480 5013 5337 -41 302 -65 C ATOM 3831 N THR B 186 23.097 10.576 -23.803 1.00 52.70 N ANISOU 3831 N THR B 186 6060 6794 7169 -123 417 -14 N ATOM 3832 CA THR B 186 24.460 10.094 -23.744 1.00 49.38 C ANISOU 3832 CA THR B 186 5572 6363 6827 -165 413 -73 C ATOM 3833 C THR B 186 25.167 10.631 -22.494 1.00 47.42 C ANISOU 3833 C THR B 186 5274 6003 6739 -218 351 -192 C ATOM 3834 O THR B 186 26.383 10.740 -22.477 1.00 50.97 O ANISOU 3834 O THR B 186 5642 6405 7320 -261 370 -229 O ATOM 3835 CB THR B 186 25.265 10.501 -25.008 1.00 49.71 C ANISOU 3835 CB THR B 186 5555 6399 6934 -168 546 42 C ATOM 3836 OG1 THR B 186 25.215 11.920 -25.184 1.00 49.83 O ANISOU 3836 OG1 THR B 186 5547 6294 7092 -180 633 129 O ATOM 3837 CG2 THR B 186 24.711 9.832 -26.247 1.00 37.21 C ANISOU 3837 CG2 THR B 186 4012 4958 5167 -108 595 135 C ATOM 3838 N PHE B 187 24.412 10.979 -21.454 1.00 43.84 N ANISOU 3838 N PHE B 187 4864 5516 6277 -215 279 -261 N ATOM 3839 CA PHE B 187 25.029 11.481 -20.233 1.00 47.26 C ANISOU 3839 CA PHE B 187 5250 5865 6841 -258 209 -396 C ATOM 3840 C PHE B 187 26.114 10.548 -19.703 1.00 51.65 C ANISOU 3840 C PHE B 187 5757 6467 7400 -279 127 -495 C ATOM 3841 O PHE B 187 27.105 11.004 -19.119 1.00 56.46 O ANISOU 3841 O PHE B 187 6284 7009 8159 -323 97 -590 O ATOM 3842 CB PHE B 187 24.013 11.721 -19.121 1.00 53.15 C ANISOU 3842 CB PHE B 187 6057 6610 7526 -237 131 -473 C ATOM 3843 CG PHE B 187 23.133 12.912 -19.337 1.00 47.17 C ANISOU 3843 CG PHE B 187 5323 5769 6829 -221 199 -414 C ATOM 3844 CD1 PHE B 187 23.338 13.762 -20.407 1.00 41.35 C ANISOU 3844 CD1 PHE B 187 4553 4949 6208 -226 320 -291 C ATOM 3845 CD2 PHE B 187 22.096 13.185 -18.455 1.00 40.02 C ANISOU 3845 CD2 PHE B 187 4473 4868 5866 -193 147 -475 C ATOM 3846 CE1 PHE B 187 22.512 14.865 -20.602 1.00 42.58 C ANISOU 3846 CE1 PHE B 187 4731 5019 6430 -200 383 -223 C ATOM 3847 CE2 PHE B 187 21.269 14.283 -18.642 1.00 43.51 C ANISOU 3847 CE2 PHE B 187 4932 5227 6374 -168 209 -424 C ATOM 3848 CZ PHE B 187 21.483 15.125 -19.721 1.00 45.55 C ANISOU 3848 CZ PHE B 187 5158 5393 6757 -170 324 -295 C ATOM 3849 N SER B 188 25.928 9.246 -19.903 1.00 43.10 N ANISOU 3849 N SER B 188 4717 5495 6163 -245 90 -479 N ATOM 3850 CA SER B 188 26.861 8.256 -19.362 1.00 44.53 C ANISOU 3850 CA SER B 188 4860 5722 6338 -247 6 -562 C ATOM 3851 C SER B 188 28.218 8.331 -20.067 1.00 51.21 C ANISOU 3851 C SER B 188 5600 6537 7320 -279 67 -553 C ATOM 3852 O SER B 188 29.218 7.825 -19.563 1.00 48.84 O ANISOU 3852 O SER B 188 5235 6249 7071 -287 1 -635 O ATOM 3853 CB SER B 188 26.280 6.848 -19.461 1.00 40.28 C ANISOU 3853 CB SER B 188 4392 5287 5625 -203 -36 -538 C ATOM 3854 OG SER B 188 26.099 6.484 -20.822 1.00 42.90 O ANISOU 3854 OG SER B 188 4734 5661 5906 -186 56 -444 O ATOM 3855 N LEU B 189 28.241 8.979 -21.226 1.00 48.69 N ANISOU 3855 N LEU B 189 5260 6184 7056 -290 197 -447 N ATOM 3856 CA LEU B 189 29.479 9.191 -21.961 1.00 49.03 C ANISOU 3856 CA LEU B 189 5197 6195 7236 -324 282 -422 C ATOM 3857 C LEU B 189 30.092 10.558 -21.665 1.00 49.23 C ANISOU 3857 C LEU B 189 5136 6084 7485 -387 325 -449 C ATOM 3858 O LEU B 189 31.184 10.861 -22.162 1.00 56.17 O ANISOU 3858 O LEU B 189 5908 6919 8514 -428 401 -436 O ATOM 3859 CB LEU B 189 29.261 9.028 -23.485 1.00 42.76 C ANISOU 3859 CB LEU B 189 4423 5460 6365 -294 415 -278 C ATOM 3860 CG LEU B 189 28.811 7.644 -23.993 1.00 45.52 C ANISOU 3860 CG LEU B 189 4835 5941 6518 -238 388 -267 C ATOM 3861 CD1 LEU B 189 28.430 7.657 -25.472 1.00 43.84 C ANISOU 3861 CD1 LEU B 189 4646 5802 6209 -202 512 -138 C ATOM 3862 CD2 LEU B 189 29.853 6.578 -23.728 1.00 42.84 C ANISOU 3862 CD2 LEU B 189 4437 5638 6202 -236 331 -357 C ATOM 3863 N GLN B 190 29.410 11.382 -20.867 1.00 47.67 N ANISOU 3863 N GLN B 190 4975 5815 7323 -398 282 -496 N ATOM 3864 CA GLN B 190 29.859 12.773 -20.669 1.00 48.45 C ANISOU 3864 CA GLN B 190 4994 5761 7654 -460 335 -523 C ATOM 3865 C GLN B 190 30.067 13.171 -19.223 1.00 50.44 C ANISOU 3865 C GLN B 190 5211 5962 7992 -490 208 -708 C ATOM 3866 O GLN B 190 30.998 13.908 -18.917 1.00 56.94 O ANISOU 3866 O GLN B 190 5921 6684 9029 -554 214 -794 O ATOM 3867 CB GLN B 190 28.882 13.779 -21.275 1.00 38.42 C ANISOU 3867 CB GLN B 190 3781 4413 6403 -445 442 -394 C ATOM 3868 CG GLN B 190 28.416 13.469 -22.666 1.00 50.26 C ANISOU 3868 CG GLN B 190 5332 5987 7777 -396 556 -208 C ATOM 3869 CD GLN B 190 27.452 14.533 -23.165 1.00 63.90 C ANISOU 3869 CD GLN B 190 7110 7637 9530 -370 648 -78 C ATOM 3870 OE1 GLN B 190 27.785 15.728 -23.159 1.00 57.07 O ANISOU 3870 OE1 GLN B 190 6188 6616 8881 -413 724 -54 O ATOM 3871 NE2 GLN B 190 26.245 14.112 -23.586 1.00 60.55 N ANISOU 3871 NE2 GLN B 190 6789 7318 8901 -298 640 5 N ATOM 3872 N TYR B 191 29.186 12.711 -18.339 1.00 46.14 N ANISOU 3872 N TYR B 191 4758 5491 7281 -444 97 -772 N ATOM 3873 CA TYR B 191 29.234 13.127 -16.944 1.00 44.71 C ANISOU 3873 CA TYR B 191 4557 5285 7145 -458 -22 -948 C ATOM 3874 C TYR B 191 29.369 11.930 -16.027 1.00 48.58 C ANISOU 3874 C TYR B 191 5076 5915 7469 -417 -167 -1036 C ATOM 3875 O TYR B 191 28.818 10.869 -16.314 1.00 54.19 O ANISOU 3875 O TYR B 191 5868 6726 7995 -366 -176 -953 O ATOM 3876 CB TYR B 191 27.977 13.920 -16.597 1.00 47.73 C ANISOU 3876 CB TYR B 191 5022 5617 7496 -436 -9 -946 C ATOM 3877 CG TYR B 191 27.691 14.994 -17.608 1.00 57.08 C ANISOU 3877 CG TYR B 191 6197 6669 8822 -457 142 -818 C ATOM 3878 CD1 TYR B 191 28.382 16.205 -17.577 1.00 63.47 C ANISOU 3878 CD1 TYR B 191 6906 7312 9898 -523 198 -871 C ATOM 3879 CD2 TYR B 191 26.745 14.801 -18.606 1.00 53.36 C ANISOU 3879 CD2 TYR B 191 5811 6238 8226 -407 229 -641 C ATOM 3880 CE1 TYR B 191 28.130 17.200 -18.506 1.00 56.78 C ANISOU 3880 CE1 TYR B 191 6052 6331 9192 -536 347 -730 C ATOM 3881 CE2 TYR B 191 26.482 15.788 -19.539 1.00 57.27 C ANISOU 3881 CE2 TYR B 191 6299 6621 8839 -410 366 -504 C ATOM 3882 CZ TYR B 191 27.186 16.982 -19.487 1.00 57.74 C ANISOU 3882 CZ TYR B 191 6266 6506 9167 -474 430 -538 C ATOM 3883 OH TYR B 191 26.940 17.958 -20.415 1.00 57.06 O ANISOU 3883 OH TYR B 191 6174 6299 9208 -472 576 -379 O ATOM 3884 N THR B 192 30.102 12.096 -14.929 1.00 48.76 N ANISOU 3884 N THR B 192 5025 5942 7560 -435 -281 -1205 N ATOM 3885 CA THR B 192 30.283 11.011 -13.968 1.00 52.43 C ANISOU 3885 CA THR B 192 5513 6543 7865 -384 -425 -1280 C ATOM 3886 C THR B 192 28.944 10.613 -13.356 1.00 49.94 C ANISOU 3886 C THR B 192 5333 6306 7333 -324 -467 -1256 C ATOM 3887 O THR B 192 28.011 11.405 -13.336 1.00 54.42 O ANISOU 3887 O THR B 192 5953 6820 7903 -327 -418 -1246 O ATOM 3888 CB THR B 192 31.234 11.421 -12.841 1.00 55.21 C ANISOU 3888 CB THR B 192 5758 6900 8320 -407 -548 -1477 C ATOM 3889 OG1 THR B 192 30.643 12.480 -12.088 1.00 59.88 O ANISOU 3889 OG1 THR B 192 6366 7436 8949 -421 -571 -1588 O ATOM 3890 CG2 THR B 192 32.575 11.889 -13.404 1.00 51.54 C ANISOU 3890 CG2 THR B 192 5136 6347 8098 -477 -503 -1514 C ATOM 3891 N PRO B 193 28.845 9.379 -12.858 1.00 57.34 N ANISOU 3891 N PRO B 193 6325 7368 8095 -267 -552 -1241 N ATOM 3892 CA PRO B 193 27.598 8.902 -12.238 1.00 55.85 C ANISOU 3892 CA PRO B 193 6258 7259 7702 -212 -584 -1209 C ATOM 3893 C PRO B 193 27.108 9.754 -11.071 1.00 54.37 C ANISOU 3893 C PRO B 193 6087 7079 7491 -204 -644 -1338 C ATOM 3894 O PRO B 193 25.902 9.946 -10.963 1.00 63.18 O ANISOU 3894 O PRO B 193 7290 8204 8512 -183 -606 -1298 O ATOM 3895 CB PRO B 193 27.954 7.484 -11.776 1.00 54.58 C ANISOU 3895 CB PRO B 193 6119 7212 7408 -158 -673 -1186 C ATOM 3896 CG PRO B 193 28.977 7.034 -12.771 1.00 48.72 C ANISOU 3896 CG PRO B 193 5300 6437 6775 -179 -631 -1137 C ATOM 3897 CD PRO B 193 29.802 8.284 -13.082 1.00 54.85 C ANISOU 3897 CD PRO B 193 5962 7112 7769 -247 -591 -1216 C ATOM 3898 N PRO B 194 28.012 10.261 -10.215 1.00 57.85 N ANISOU 3898 N PRO B 194 6439 7524 8015 -219 -739 -1501 N ATOM 3899 CA PRO B 194 27.514 11.133 -9.138 1.00 45.96 C ANISOU 3899 CA PRO B 194 4948 6029 6487 -209 -791 -1646 C ATOM 3900 C PRO B 194 26.903 12.419 -9.709 1.00 53.77 C ANISOU 3900 C PRO B 194 5936 6869 7625 -255 -679 -1645 C ATOM 3901 O PRO B 194 25.932 12.944 -9.163 1.00 60.03 O ANISOU 3901 O PRO B 194 6788 7665 8355 -231 -673 -1691 O ATOM 3902 CB PRO B 194 28.784 11.462 -8.333 1.00 49.18 C ANISOU 3902 CB PRO B 194 5234 6459 6992 -226 -911 -1833 C ATOM 3903 CG PRO B 194 29.779 10.384 -8.705 1.00 42.02 C ANISOU 3903 CG PRO B 194 4278 5606 6081 -214 -949 -1765 C ATOM 3904 CD PRO B 194 29.472 10.042 -10.130 1.00 50.30 C ANISOU 3904 CD PRO B 194 5364 6578 7170 -238 -808 -1577 C ATOM 3905 N VAL B 195 27.463 12.923 -10.803 1.00 48.04 N ANISOU 3905 N VAL B 195 5141 6013 7097 -315 -583 -1585 N ATOM 3906 CA VAL B 195 26.886 14.091 -11.449 1.00 50.35 C ANISOU 3906 CA VAL B 195 5437 6156 7537 -349 -465 -1545 C ATOM 3907 C VAL B 195 25.549 13.757 -12.072 1.00 54.12 C ANISOU 3907 C VAL B 195 6033 6661 7870 -304 -383 -1379 C ATOM 3908 O VAL B 195 24.562 14.466 -11.845 1.00 57.56 O ANISOU 3908 O VAL B 195 6516 7054 8299 -284 -349 -1393 O ATOM 3909 CB VAL B 195 27.818 14.687 -12.514 1.00 55.36 C ANISOU 3909 CB VAL B 195 5970 6649 8415 -420 -366 -1492 C ATOM 3910 CG1 VAL B 195 27.124 15.828 -13.261 1.00 41.00 C ANISOU 3910 CG1 VAL B 195 4169 4676 6734 -440 -231 -1408 C ATOM 3911 CG2 VAL B 195 29.107 15.179 -11.850 1.00 45.94 C ANISOU 3911 CG2 VAL B 195 4640 5414 7402 -475 -446 -1683 C ATOM 3912 N VAL B 196 25.507 12.677 -12.851 1.00 54.03 N ANISOU 3912 N VAL B 196 6060 6720 7749 -285 -354 -1232 N ATOM 3913 CA VAL B 196 24.255 12.267 -13.476 1.00 44.44 C ANISOU 3913 CA VAL B 196 4944 5545 6396 -244 -287 -1086 C ATOM 3914 C VAL B 196 23.212 12.104 -12.386 1.00 47.01 C ANISOU 3914 C VAL B 196 5347 5955 6560 -196 -349 -1147 C ATOM 3915 O VAL B 196 22.051 12.476 -12.565 1.00 48.34 O ANISOU 3915 O VAL B 196 5573 6110 6685 -171 -293 -1094 O ATOM 3916 CB VAL B 196 24.380 10.972 -14.319 1.00 41.66 C ANISOU 3916 CB VAL B 196 4619 5274 5936 -228 -268 -957 C ATOM 3917 CG1 VAL B 196 22.994 10.477 -14.787 1.00 32.22 C ANISOU 3917 CG1 VAL B 196 3520 4138 4585 -186 -222 -841 C ATOM 3918 CG2 VAL B 196 25.283 11.200 -15.533 1.00 40.82 C ANISOU 3918 CG2 VAL B 196 4440 5095 5975 -269 -181 -882 C ATOM 3919 N ALA B 197 23.641 11.583 -11.242 1.00 48.61 N ANISOU 3919 N ALA B 197 5545 6250 6675 -178 -462 -1258 N ATOM 3920 CA ALA B 197 22.720 11.314 -10.143 1.00 49.36 C ANISOU 3920 CA ALA B 197 5714 6449 6593 -126 -517 -1307 C ATOM 3921 C ALA B 197 22.115 12.605 -9.616 1.00 57.16 C ANISOU 3921 C ALA B 197 6698 7372 7648 -124 -498 -1417 C ATOM 3922 O ALA B 197 20.929 12.650 -9.277 1.00 58.24 O ANISOU 3922 O ALA B 197 6903 7553 7672 -84 -473 -1399 O ATOM 3923 CB ALA B 197 23.419 10.562 -9.031 1.00 41.69 C ANISOU 3923 CB ALA B 197 4731 5596 5512 -98 -642 -1395 C ATOM 3924 N CYS B 198 22.938 13.651 -9.556 1.00 54.69 N ANISOU 3924 N CYS B 198 6299 6948 7534 -169 -504 -1536 N ATOM 3925 CA CYS B 198 22.485 14.981 -9.157 1.00 55.43 C ANISOU 3925 CA CYS B 198 6375 6941 7743 -173 -477 -1654 C ATOM 3926 C CYS B 198 21.461 15.547 -10.139 1.00 58.04 C ANISOU 3926 C CYS B 198 6746 7171 8135 -165 -349 -1516 C ATOM 3927 O CYS B 198 20.462 16.146 -9.739 1.00 55.60 O ANISOU 3927 O CYS B 198 6475 6847 7803 -129 -324 -1557 O ATOM 3928 CB CYS B 198 23.676 15.941 -9.032 1.00 59.14 C ANISOU 3928 CB CYS B 198 6729 7287 8454 -236 -501 -1805 C ATOM 3929 SG CYS B 198 24.684 15.648 -7.574 1.00 60.96 S ANISOU 3929 SG CYS B 198 6898 7646 8616 -229 -674 -2035 S ATOM 3930 N VAL B 199 21.724 15.367 -11.427 1.00 49.37 N ANISOU 3930 N VAL B 199 5635 6012 7110 -191 -270 -1354 N ATOM 3931 CA VAL B 199 20.784 15.776 -12.456 1.00 51.26 C ANISOU 3931 CA VAL B 199 5913 6185 7380 -171 -157 -1199 C ATOM 3932 C VAL B 199 19.406 15.132 -12.254 1.00 52.94 C ANISOU 3932 C VAL B 199 6216 6520 7380 -108 -159 -1136 C ATOM 3933 O VAL B 199 18.379 15.798 -12.366 1.00 48.49 O ANISOU 3933 O VAL B 199 5679 5913 6832 -72 -103 -1109 O ATOM 3934 CB VAL B 199 21.308 15.409 -13.843 1.00 51.27 C ANISOU 3934 CB VAL B 199 5892 6157 7430 -196 -84 -1031 C ATOM 3935 CG1 VAL B 199 20.304 15.819 -14.907 1.00 42.40 C ANISOU 3935 CG1 VAL B 199 4808 4990 6311 -160 24 -866 C ATOM 3936 CG2 VAL B 199 22.691 16.051 -14.077 1.00 45.82 C ANISOU 3936 CG2 VAL B 199 5100 5343 6967 -264 -65 -1084 C ATOM 3937 N CYS B 200 19.399 13.843 -11.933 1.00 43.69 N ANISOU 3937 N CYS B 200 5084 5493 6022 -94 -220 -1114 N ATOM 3938 CA CYS B 200 18.165 13.081 -11.785 1.00 42.49 C ANISOU 3938 CA CYS B 200 5007 5456 5680 -48 -215 -1044 C ATOM 3939 C CYS B 200 17.394 13.492 -10.545 1.00 48.13 C ANISOU 3939 C CYS B 200 5749 6216 6321 -9 -247 -1165 C ATOM 3940 O CYS B 200 16.194 13.705 -10.599 1.00 49.24 O ANISOU 3940 O CYS B 200 5925 6373 6411 28 -198 -1124 O ATOM 3941 CB CYS B 200 18.483 11.584 -11.714 1.00 45.74 C ANISOU 3941 CB CYS B 200 5447 5989 5944 -49 -268 -992 C ATOM 3942 SG CYS B 200 19.093 10.903 -13.259 1.00 58.51 S ANISOU 3942 SG CYS B 200 7043 7583 7606 -78 -219 -846 S ATOM 3943 N ILE B 201 18.088 13.596 -9.419 1.00 52.73 N ANISOU 3943 N ILE B 201 6311 6833 6892 -13 -330 -1319 N ATOM 3944 CA ILE B 201 17.470 14.104 -8.204 1.00 56.29 C ANISOU 3944 CA ILE B 201 6781 7334 7274 27 -359 -1460 C ATOM 3945 C ILE B 201 16.895 15.514 -8.387 1.00 54.39 C ANISOU 3945 C ILE B 201 6517 6957 7193 36 -291 -1516 C ATOM 3946 O ILE B 201 15.783 15.802 -7.943 1.00 51.79 O ANISOU 3946 O ILE B 201 6221 6663 6792 84 -260 -1541 O ATOM 3947 CB ILE B 201 18.463 14.109 -7.052 1.00 58.45 C ANISOU 3947 CB ILE B 201 7021 7667 7522 23 -468 -1634 C ATOM 3948 CG1 ILE B 201 18.774 12.667 -6.648 1.00 60.03 C ANISOU 3948 CG1 ILE B 201 7258 8022 7529 41 -536 -1569 C ATOM 3949 CG2 ILE B 201 17.924 14.936 -5.875 1.00 50.41 C ANISOU 3949 CG2 ILE B 201 6007 6681 6467 64 -491 -1815 C ATOM 3950 CD1 ILE B 201 19.727 12.565 -5.488 1.00 63.52 C ANISOU 3950 CD1 ILE B 201 7668 8555 7913 55 -656 -1725 C ATOM 3951 N HIS B 202 17.650 16.379 -9.053 1.00 54.49 N ANISOU 3951 N HIS B 202 6467 6808 7429 -9 -259 -1528 N ATOM 3952 CA HIS B 202 17.235 17.766 -9.285 1.00 55.82 C ANISOU 3952 CA HIS B 202 6607 6814 7789 -1 -187 -1570 C ATOM 3953 C HIS B 202 15.936 17.805 -10.076 1.00 53.52 C ANISOU 3953 C HIS B 202 6362 6516 7457 47 -98 -1407 C ATOM 3954 O HIS B 202 14.950 18.380 -9.624 1.00 54.48 O ANISOU 3954 O HIS B 202 6500 6631 7568 98 -70 -1461 O ATOM 3955 CB HIS B 202 18.338 18.521 -10.030 1.00 60.77 C ANISOU 3955 CB HIS B 202 7157 7263 8671 -65 -152 -1564 C ATOM 3956 CG HIS B 202 18.167 20.004 -10.033 1.00 68.03 C ANISOU 3956 CG HIS B 202 8034 7990 9826 -66 -91 -1645 C ATOM 3957 ND1 HIS B 202 18.044 20.741 -8.875 1.00 71.84 N ANISOU 3957 ND1 HIS B 202 8495 8448 10354 -52 -136 -1871 N ATOM 3958 CD2 HIS B 202 18.120 20.893 -11.054 1.00 68.16 C ANISOU 3958 CD2 HIS B 202 8021 7823 10053 -77 15 -1530 C ATOM 3959 CE1 HIS B 202 17.916 22.019 -9.181 1.00 60.80 C ANISOU 3959 CE1 HIS B 202 7055 6843 9202 -57 -60 -1901 C ATOM 3960 NE2 HIS B 202 17.962 22.139 -10.496 1.00 64.38 N ANISOU 3960 NE2 HIS B 202 7506 7195 9763 -71 34 -1684 N ATOM 3961 N LEU B 203 15.930 17.180 -11.251 1.00 51.03 N ANISOU 3961 N LEU B 203 6060 6215 7114 37 -55 -1216 N ATOM 3962 CA LEU B 203 14.709 17.086 -12.056 1.00 47.96 C ANISOU 3962 CA LEU B 203 5708 5851 6665 86 14 -1060 C ATOM 3963 C LEU B 203 13.545 16.438 -11.297 1.00 44.75 C ANISOU 3963 C LEU B 203 5350 5595 6057 134 -10 -1085 C ATOM 3964 O LEU B 203 12.401 16.870 -11.419 1.00 48.68 O ANISOU 3964 O LEU B 203 5858 6088 6549 187 40 -1051 O ATOM 3965 CB LEU B 203 14.959 16.351 -13.386 1.00 45.02 C ANISOU 3965 CB LEU B 203 5340 5507 6260 69 47 -875 C ATOM 3966 CG LEU B 203 13.779 16.315 -14.368 1.00 45.80 C ANISOU 3966 CG LEU B 203 5461 5636 6305 122 111 -717 C ATOM 3967 CD1 LEU B 203 13.198 17.702 -14.619 1.00 40.75 C ANISOU 3967 CD1 LEU B 203 4800 4859 5823 169 181 -697 C ATOM 3968 CD2 LEU B 203 14.196 15.698 -15.675 1.00 37.80 C ANISOU 3968 CD2 LEU B 203 4444 4651 5266 105 140 -562 C ATOM 3969 N ALA B 204 13.827 15.405 -10.513 1.00 44.63 N ANISOU 3969 N ALA B 204 5361 5713 5883 120 -80 -1137 N ATOM 3970 CA ALA B 204 12.753 14.725 -9.791 1.00 44.76 C ANISOU 3970 CA ALA B 204 5423 5874 5711 160 -88 -1142 C ATOM 3971 C ALA B 204 12.096 15.700 -8.817 1.00 52.94 C ANISOU 3971 C ALA B 204 6454 6894 6767 206 -75 -1285 C ATOM 3972 O ALA B 204 10.869 15.743 -8.688 1.00 53.24 O ANISOU 3972 O ALA B 204 6507 6983 6738 254 -30 -1259 O ATOM 3973 CB ALA B 204 13.273 13.492 -9.064 1.00 36.88 C ANISOU 3973 CB ALA B 204 4453 5007 4551 141 -160 -1160 C ATOM 3974 N CYS B 205 12.926 16.491 -8.146 1.00 53.79 N ANISOU 3974 N CYS B 205 6531 6929 6977 192 -115 -1447 N ATOM 3975 CA CYS B 205 12.451 17.521 -7.234 1.00 53.23 C ANISOU 3975 CA CYS B 205 6447 6826 6951 235 -106 -1617 C ATOM 3976 C CYS B 205 11.592 18.557 -7.957 1.00 55.55 C ANISOU 3976 C CYS B 205 6721 6983 7402 273 -16 -1563 C ATOM 3977 O CYS B 205 10.478 18.849 -7.525 1.00 53.70 O ANISOU 3977 O CYS B 205 6498 6791 7116 333 22 -1599 O ATOM 3978 CB CYS B 205 13.632 18.203 -6.539 1.00 49.20 C ANISOU 3978 CB CYS B 205 5892 6246 6556 202 -171 -1814 C ATOM 3979 SG CYS B 205 14.444 17.202 -5.275 1.00 61.70 S ANISOU 3979 SG CYS B 205 7494 8024 7926 194 -293 -1930 S ATOM 3980 N LYS B 206 12.110 19.113 -9.048 1.00 45.97 N ANISOU 3980 N LYS B 206 5476 5612 6380 244 24 -1471 N ATOM 3981 CA LYS B 206 11.343 20.068 -9.838 1.00 48.65 C ANISOU 3981 CA LYS B 206 5797 5818 6869 290 111 -1385 C ATOM 3982 C LYS B 206 10.018 19.459 -10.301 1.00 49.83 C ANISOU 3982 C LYS B 206 5977 6086 6871 345 148 -1239 C ATOM 3983 O LYS B 206 8.982 20.104 -10.251 1.00 53.75 O ANISOU 3983 O LYS B 206 6464 6553 7405 412 197 -1244 O ATOM 3984 CB LYS B 206 12.140 20.546 -11.054 1.00 55.22 C ANISOU 3984 CB LYS B 206 6597 6490 7895 251 154 -1258 C ATOM 3985 CG LYS B 206 13.297 21.498 -10.747 1.00 60.70 C ANISOU 3985 CG LYS B 206 7237 7010 8815 198 146 -1397 C ATOM 3986 CD LYS B 206 13.957 21.940 -12.041 1.00 72.13 C ANISOU 3986 CD LYS B 206 8653 8303 10450 164 215 -1234 C ATOM 3987 CE LYS B 206 14.929 23.079 -11.818 1.00 88.09 C ANISOU 3987 CE LYS B 206 10607 10113 12751 112 232 -1361 C ATOM 3988 NZ LYS B 206 15.570 23.509 -13.097 1.00 94.57 N ANISOU 3988 NZ LYS B 206 11393 10783 13757 79 318 -1178 N ATOM 3989 N TRP B 207 10.053 18.210 -10.741 1.00 45.22 N ANISOU 3989 N TRP B 207 5421 5633 6129 317 123 -1121 N ATOM 3990 CA TRP B 207 8.855 17.565 -11.265 1.00 52.16 C ANISOU 3990 CA TRP B 207 6314 6622 6883 358 153 -990 C ATOM 3991 C TRP B 207 7.814 17.345 -10.174 1.00 51.88 C ANISOU 3991 C TRP B 207 6291 6705 6714 400 153 -1083 C ATOM 3992 O TRP B 207 6.613 17.414 -10.434 1.00 51.22 O ANISOU 3992 O TRP B 207 6195 6664 6602 454 198 -1023 O ATOM 3993 CB TRP B 207 9.222 16.231 -11.927 1.00 47.16 C ANISOU 3993 CB TRP B 207 5702 6091 6126 309 123 -870 C ATOM 3994 CG TRP B 207 8.051 15.462 -12.460 1.00 47.38 C ANISOU 3994 CG TRP B 207 5734 6237 6031 338 144 -757 C ATOM 3995 CD1 TRP B 207 7.303 14.521 -11.796 1.00 47.36 C ANISOU 3995 CD1 TRP B 207 5749 6377 5870 338 131 -775 C ATOM 3996 CD2 TRP B 207 7.503 15.553 -13.777 1.00 43.35 C ANISOU 3996 CD2 TRP B 207 5202 5718 5549 369 180 -610 C ATOM 3997 NE1 TRP B 207 6.321 14.033 -12.623 1.00 47.50 N ANISOU 3997 NE1 TRP B 207 5748 6464 5834 359 156 -663 N ATOM 3998 CE2 TRP B 207 6.419 14.651 -13.842 1.00 47.70 C ANISOU 3998 CE2 TRP B 207 5751 6410 5963 383 179 -565 C ATOM 3999 CE3 TRP B 207 7.818 16.313 -14.904 1.00 35.48 C ANISOU 3999 CE3 TRP B 207 4186 4616 4680 390 216 -508 C ATOM 4000 CZ2 TRP B 207 5.653 14.494 -14.988 1.00 44.66 C ANISOU 4000 CZ2 TRP B 207 5339 6072 5560 417 198 -443 C ATOM 4001 CZ3 TRP B 207 7.063 16.153 -16.037 1.00 44.42 C ANISOU 4001 CZ3 TRP B 207 5300 5803 5774 434 239 -369 C ATOM 4002 CH2 TRP B 207 5.992 15.245 -16.075 1.00 46.31 C ANISOU 4002 CH2 TRP B 207 5532 6193 5871 448 223 -347 C ATOM 4003 N SER B 208 8.286 17.084 -8.958 1.00 56.51 N ANISOU 4003 N SER B 208 6897 7357 7216 380 105 -1226 N ATOM 4004 CA SER B 208 7.425 16.769 -7.815 1.00 58.36 C ANISOU 4004 CA SER B 208 7148 7729 7296 418 110 -1312 C ATOM 4005 C SER B 208 7.180 17.968 -6.929 1.00 61.72 C ANISOU 4005 C SER B 208 7555 8096 7801 470 129 -1493 C ATOM 4006 O SER B 208 6.575 17.831 -5.876 1.00 67.63 O ANISOU 4006 O SER B 208 8314 8962 8419 507 136 -1591 O ATOM 4007 CB SER B 208 8.075 15.697 -6.941 1.00 63.49 C ANISOU 4007 CB SER B 208 7836 8512 7774 380 46 -1354 C ATOM 4008 OG SER B 208 8.631 14.663 -7.724 1.00 72.12 O ANISOU 4008 OG SER B 208 8945 9627 8833 326 19 -1217 O ATOM 4009 N ASN B 209 7.671 19.134 -7.336 1.00 75.25 N ANISOU 4009 N ASN B 209 9236 9625 9730 472 141 -1542 N ATOM 4010 CA ASN B 209 7.602 20.336 -6.500 1.00 82.60 C ANISOU 4010 CA ASN B 209 10142 10470 10774 513 153 -1743 C ATOM 4011 C ASN B 209 8.106 20.111 -5.078 1.00 80.22 C ANISOU 4011 C ASN B 209 9857 10285 10338 505 88 -1944 C ATOM 4012 O ASN B 209 7.489 20.543 -4.107 1.00 85.89 O ANISOU 4012 O ASN B 209 10572 11062 11002 562 105 -2096 O ATOM 4013 CB ASN B 209 6.196 20.934 -6.500 1.00 87.44 C ANISOU 4013 CB ASN B 209 10734 11074 11414 600 230 -1738 C ATOM 4014 CG ASN B 209 5.881 21.658 -7.794 1.00106.74 C ANISOU 4014 CG ASN B 209 13148 13352 14055 628 288 -1589 C ATOM 4015 OD1 ASN B 209 5.684 21.031 -8.843 1.00108.96 O ANISOU 4015 OD1 ASN B 209 13436 13668 14297 616 297 -1391 O ATOM 4016 ND2 ASN B 209 5.846 22.987 -7.734 1.00112.86 N ANISOU 4016 ND2 ASN B 209 13889 13946 15047 671 327 -1684 N ATOM 4017 N TRP B 210 9.239 19.425 -4.983 1.00 72.60 N ANISOU 4017 N TRP B 210 8907 9364 9315 441 13 -1942 N ATOM 4018 CA TRP B 210 9.912 19.173 -3.723 1.00 74.49 C ANISOU 4018 CA TRP B 210 9157 9721 9424 435 -67 -2119 C ATOM 4019 C TRP B 210 11.152 20.042 -3.644 1.00 81.48 C ANISOU 4019 C TRP B 210 9995 10459 10506 391 -121 -2275 C ATOM 4020 O TRP B 210 11.818 20.300 -4.653 1.00 79.82 O ANISOU 4020 O TRP B 210 9755 10092 10480 338 -111 -2184 O ATOM 4021 CB TRP B 210 10.324 17.711 -3.636 1.00 84.89 C ANISOU 4021 CB TRP B 210 10517 11200 10538 401 -120 -2000 C ATOM 4022 CG TRP B 210 10.848 17.299 -2.298 1.00 97.68 C ANISOU 4022 CG TRP B 210 12156 12983 11976 417 -201 -2147 C ATOM 4023 CD1 TRP B 210 11.996 17.724 -1.697 1.00 98.82 C ANISOU 4023 CD1 TRP B 210 12271 13110 12168 397 -290 -2327 C ATOM 4024 CD2 TRP B 210 10.250 16.355 -1.399 1.00108.88 C ANISOU 4024 CD2 TRP B 210 13624 14617 13128 459 -200 -2117 C ATOM 4025 NE1 TRP B 210 12.146 17.114 -0.474 1.00103.22 N ANISOU 4025 NE1 TRP B 210 12858 13873 12488 435 -355 -2414 N ATOM 4026 CE2 TRP B 210 11.088 16.266 -0.269 1.00109.44 C ANISOU 4026 CE2 TRP B 210 13699 14803 13079 474 -294 -2277 C ATOM 4027 CE3 TRP B 210 9.084 15.580 -1.438 1.00110.56 C ANISOU 4027 CE3 TRP B 210 13872 14937 13198 485 -126 -1970 C ATOM 4028 CZ2 TRP B 210 10.799 15.433 0.810 1.00115.05 C ANISOU 4028 CZ2 TRP B 210 14457 15737 13518 523 -311 -2274 C ATOM 4029 CZ3 TRP B 210 8.799 14.754 -0.366 1.00112.31 C ANISOU 4029 CZ3 TRP B 210 14135 15363 13172 522 -133 -1969 C ATOM 4030 CH2 TRP B 210 9.652 14.687 0.743 1.00115.21 C ANISOU 4030 CH2 TRP B 210 14516 15847 13411 545 -222 -2110 C ATOM 4031 N GLU B 211 11.456 20.508 -2.440 1.00 88.12 N ANISOU 4031 N GLU B 211 10821 11354 11309 413 -176 -2517 N ATOM 4032 CA GLU B 211 12.676 21.266 -2.216 1.00 95.17 C ANISOU 4032 CA GLU B 211 11654 12125 12380 365 -243 -2701 C ATOM 4033 C GLU B 211 13.463 20.613 -1.100 1.00 95.39 C ANISOU 4033 C GLU B 211 11690 12347 12209 363 -361 -2840 C ATOM 4034 O GLU B 211 12.935 20.385 -0.012 1.00 95.36 O ANISOU 4034 O GLU B 211 11718 12526 11990 427 -381 -2946 O ATOM 4035 CB GLU B 211 12.350 22.713 -1.873 1.00102.75 C ANISOU 4035 CB GLU B 211 12567 12930 13542 397 -204 -2907 C ATOM 4036 CG GLU B 211 11.734 23.469 -3.030 1.00112.07 C ANISOU 4036 CG GLU B 211 13732 13893 14958 404 -93 -2763 C ATOM 4037 CD GLU B 211 11.072 24.758 -2.599 1.00124.40 C ANISOU 4037 CD GLU B 211 15260 15326 16682 463 -38 -2944 C ATOM 4038 OE1 GLU B 211 10.438 24.777 -1.523 1.00128.35 O ANISOU 4038 OE1 GLU B 211 15776 15971 17020 529 -48 -3107 O ATOM 4039 OE2 GLU B 211 11.179 25.752 -3.344 1.00130.87 O ANISOU 4039 OE2 GLU B 211 16036 15896 17793 449 23 -2919 O ATOM 4040 N ILE B 212 14.717 20.278 -1.384 1.00 96.68 N ANISOU 4040 N ILE B 212 11820 12480 12432 296 -436 -2826 N ATOM 4041 CA ILE B 212 15.584 19.714 -0.360 1.00101.57 C ANISOU 4041 CA ILE B 212 12434 13278 12880 300 -562 -2960 C ATOM 4042 C ILE B 212 16.247 20.873 0.382 1.00103.61 C ANISOU 4042 C ILE B 212 12613 13463 13289 291 -628 -3273 C ATOM 4043 O ILE B 212 16.900 21.716 -0.235 1.00105.60 O ANISOU 4043 O ILE B 212 12794 13497 13834 225 -615 -3329 O ATOM 4044 CB ILE B 212 16.634 18.744 -0.952 1.00 99.38 C ANISOU 4044 CB ILE B 212 12149 13019 12591 242 -620 -2809 C ATOM 4045 CG1 ILE B 212 15.972 17.752 -1.914 1.00 87.62 C ANISOU 4045 CG1 ILE B 212 10724 11548 11020 239 -541 -2512 C ATOM 4046 CG2 ILE B 212 17.337 17.974 0.155 1.00102.84 C ANISOU 4046 CG2 ILE B 212 12593 13678 12802 271 -749 -2907 C ATOM 4047 CD1 ILE B 212 16.946 16.849 -2.610 1.00 72.15 C ANISOU 4047 CD1 ILE B 212 8754 9586 9073 185 -582 -2367 C ATOM 4048 N PRO B 213 16.054 20.927 1.711 1.00106.46 N ANISOU 4048 N PRO B 213 12986 14010 13453 358 -692 -3481 N ATOM 4049 CA PRO B 213 16.469 22.063 2.542 1.00107.75 C ANISOU 4049 CA PRO B 213 13076 14129 13733 364 -753 -3819 C ATOM 4050 C PRO B 213 17.981 22.222 2.586 1.00101.85 C ANISOU 4050 C PRO B 213 12238 13331 13129 291 -873 -3958 C ATOM 4051 O PRO B 213 18.703 21.217 2.604 1.00 90.99 O ANISOU 4051 O PRO B 213 10872 12089 11613 278 -953 -3854 O ATOM 4052 CB PRO B 213 15.946 21.689 3.936 1.00109.69 C ANISOU 4052 CB PRO B 213 13371 14662 13643 464 -803 -3956 C ATOM 4053 CG PRO B 213 14.934 20.605 3.707 1.00108.90 C ANISOU 4053 CG PRO B 213 13370 14696 13311 508 -720 -3672 C ATOM 4054 CD PRO B 213 15.426 19.864 2.512 1.00107.08 C ANISOU 4054 CD PRO B 213 13147 14364 13175 434 -706 -3404 C ATOM 4055 N VAL B 214 18.447 23.470 2.601 1.00105.01 N ANISOU 4055 N VAL B 214 12546 13533 13821 244 -881 -4191 N ATOM 4056 CA VAL B 214 19.877 23.753 2.692 1.00109.02 C ANISOU 4056 CA VAL B 214 12944 13980 14500 168 -993 -4360 C ATOM 4057 C VAL B 214 20.440 23.199 3.995 1.00116.56 C ANISOU 4057 C VAL B 214 13887 15228 15171 222 -1158 -4556 C ATOM 4058 O VAL B 214 19.809 23.296 5.046 1.00114.02 O ANISOU 4058 O VAL B 214 13604 15085 14632 310 -1185 -4717 O ATOM 4059 CB VAL B 214 20.177 25.260 2.604 1.00105.91 C ANISOU 4059 CB VAL B 214 12445 13314 14482 109 -967 -4608 C ATOM 4060 CG1 VAL B 214 21.677 25.493 2.507 1.00100.52 C ANISOU 4060 CG1 VAL B 214 11635 12544 14015 11 -1066 -4745 C ATOM 4061 CG2 VAL B 214 19.458 25.876 1.411 1.00105.90 C ANISOU 4061 CG2 VAL B 214 12465 13036 14737 82 -795 -4406 C ATOM 4062 N SER B 215 21.624 22.601 3.917 1.00125.93 N ANISOU 4062 N SER B 215 15020 16475 16353 177 -1266 -4534 N ATOM 4063 CA SER B 215 22.248 22.003 5.087 1.00132.23 C ANISOU 4063 CA SER B 215 15802 17562 16878 237 -1434 -4691 C ATOM 4064 C SER B 215 22.591 23.083 6.103 1.00135.87 C ANISOU 4064 C SER B 215 16168 18042 17413 247 -1531 -5106 C ATOM 4065 O SER B 215 22.723 24.257 5.755 1.00132.77 O ANISOU 4065 O SER B 215 15693 17393 17361 175 -1484 -5271 O ATOM 4066 CB SER B 215 23.510 21.231 4.693 1.00132.27 C ANISOU 4066 CB SER B 215 15749 17597 16913 184 -1528 -4588 C ATOM 4067 OG SER B 215 24.570 22.111 4.358 1.00132.34 O ANISOU 4067 OG SER B 215 15611 17404 17268 81 -1570 -4774 O ATOM 4068 N THR B 216 22.728 22.676 7.359 1.00140.57 N ANISOU 4068 N THR B 216 16775 18944 17691 340 -1665 -5273 N ATOM 4069 CA THR B 216 23.093 23.596 8.429 1.00148.02 C ANISOU 4069 CA THR B 216 17627 19959 18656 362 -1781 -5695 C ATOM 4070 C THR B 216 24.317 24.443 8.064 1.00147.83 C ANISOU 4070 C THR B 216 17435 19710 19023 240 -1852 -5911 C ATOM 4071 O THR B 216 24.393 25.620 8.425 1.00148.44 O ANISOU 4071 O THR B 216 17424 19660 19316 210 -1868 -6237 O ATOM 4072 CB THR B 216 23.350 22.837 9.747 1.00150.08 C ANISOU 4072 CB THR B 216 17912 20618 18494 481 -1944 -5807 C ATOM 4073 OG1 THR B 216 23.985 21.583 9.463 1.00145.97 O ANISOU 4073 OG1 THR B 216 17417 20222 17825 486 -2005 -5542 O ATOM 4074 CG2 THR B 216 22.040 22.574 10.469 1.00149.43 C ANISOU 4074 CG2 THR B 216 17960 20741 18075 605 -1869 -5761 C ATOM 4075 N ASP B 217 25.257 23.841 7.335 1.00141.50 N ANISOU 4075 N ASP B 217 16586 18853 18326 169 -1886 -5732 N ATOM 4076 CA ASP B 217 26.506 24.504 6.953 1.00136.73 C ANISOU 4076 CA ASP B 217 15812 18052 18088 48 -1949 -5906 C ATOM 4077 C ASP B 217 26.282 25.593 5.905 1.00126.29 C ANISOU 4077 C ASP B 217 14446 16332 17206 -64 -1784 -5878 C ATOM 4078 O ASP B 217 27.133 26.465 5.709 1.00116.08 O ANISOU 4078 O ASP B 217 13004 14834 16267 -168 -1810 -6083 O ATOM 4079 CB ASP B 217 27.515 23.493 6.392 1.00142.04 C ANISOU 4079 CB ASP B 217 16449 18778 18744 10 -2010 -5689 C ATOM 4080 CG ASP B 217 27.571 22.200 7.187 1.00145.05 C ANISOU 4080 CG ASP B 217 16907 19526 18679 132 -2134 -5591 C ATOM 4081 OD1 ASP B 217 26.757 22.017 8.117 1.00147.18 O ANISOU 4081 OD1 ASP B 217 17272 20018 18632 246 -2156 -5650 O ATOM 4082 OD2 ASP B 217 28.436 21.356 6.869 1.00143.49 O ANISOU 4082 OD2 ASP B 217 16673 19394 18454 118 -2203 -5444 O ATOM 4083 N GLY B 218 25.141 25.527 5.225 1.00125.78 N ANISOU 4083 N GLY B 218 14507 16161 17124 -39 -1612 -5615 N ATOM 4084 CA GLY B 218 24.851 26.427 4.124 1.00124.01 C ANISOU 4084 CA GLY B 218 14260 15573 17284 -126 -1444 -5515 C ATOM 4085 C GLY B 218 25.195 25.779 2.797 1.00122.00 C ANISOU 4085 C GLY B 218 14024 15201 17130 -192 -1355 -5150 C ATOM 4086 O GLY B 218 25.240 26.439 1.760 1.00123.08 O ANISOU 4086 O GLY B 218 14124 15043 17599 -274 -1225 -5037 O ATOM 4087 N LYS B 219 25.450 24.475 2.836 1.00119.35 N ANISOU 4087 N LYS B 219 13745 15099 16504 -150 -1423 -4963 N ATOM 4088 CA LYS B 219 25.733 23.706 1.630 1.00120.58 C ANISOU 4088 CA LYS B 219 13927 15181 16705 -197 -1345 -4621 C ATOM 4089 C LYS B 219 24.449 23.185 0.979 1.00109.61 C ANISOU 4089 C LYS B 219 12693 13795 15160 -141 -1203 -4307 C ATOM 4090 O LYS B 219 23.586 22.629 1.660 1.00106.28 O ANISOU 4090 O LYS B 219 12376 13581 14426 -42 -1221 -4281 O ATOM 4091 CB LYS B 219 26.643 22.518 1.958 1.00124.30 C ANISOU 4091 CB LYS B 219 14380 15891 16959 -175 -1487 -4573 C ATOM 4092 CG LYS B 219 28.122 22.844 2.089 1.00129.87 C ANISOU 4092 CG LYS B 219 14910 16551 17882 -257 -1604 -4780 C ATOM 4093 CD LYS B 219 28.939 21.552 2.157 1.00132.43 C ANISOU 4093 CD LYS B 219 15226 17088 18004 -226 -1716 -4653 C ATOM 4094 CE LYS B 219 30.435 21.810 2.055 1.00133.04 C ANISOU 4094 CE LYS B 219 15117 17102 18331 -317 -1813 -4812 C ATOM 4095 NZ LYS B 219 31.205 20.539 1.942 1.00127.52 N ANISOU 4095 NZ LYS B 219 14408 16578 17464 -284 -1900 -4650 N ATOM 4096 N HIS B 220 24.329 23.360 -0.336 1.00100.14 N ANISOU 4096 N HIS B 220 11500 12373 14176 -202 -1061 -4070 N ATOM 4097 CA HIS B 220 23.250 22.734 -1.097 1.00 92.30 C ANISOU 4097 CA HIS B 220 10637 11395 13039 -156 -940 -3757 C ATOM 4098 C HIS B 220 23.449 21.217 -1.121 1.00 90.48 C ANISOU 4098 C HIS B 220 10471 11390 12517 -119 -1000 -3564 C ATOM 4099 O HIS B 220 24.582 20.742 -1.050 1.00 89.82 O ANISOU 4099 O HIS B 220 10318 11369 12443 -153 -1095 -3596 O ATOM 4100 CB HIS B 220 23.223 23.272 -2.525 1.00 92.52 C ANISOU 4100 CB HIS B 220 10644 11148 13359 -226 -788 -3556 C ATOM 4101 CG HIS B 220 23.069 24.758 -2.611 1.00 98.34 C ANISOU 4101 CG HIS B 220 11316 11626 14421 -264 -713 -3710 C ATOM 4102 ND1 HIS B 220 21.838 25.377 -2.682 1.00 96.49 N ANISOU 4102 ND1 HIS B 220 11148 11306 14208 -207 -613 -3681 N ATOM 4103 CD2 HIS B 220 23.992 25.749 -2.651 1.00 99.99 C ANISOU 4103 CD2 HIS B 220 11394 11632 14967 -353 -720 -3893 C ATOM 4104 CE1 HIS B 220 22.009 26.685 -2.757 1.00 97.04 C ANISOU 4104 CE1 HIS B 220 11135 11123 14614 -254 -560 -3835 C ATOM 4105 NE2 HIS B 220 23.306 26.937 -2.739 1.00101.80 N ANISOU 4105 NE2 HIS B 220 11616 11644 15417 -347 -621 -3967 N ATOM 4106 N TRP B 221 22.355 20.463 -1.232 1.00 91.07 N ANISOU 4106 N TRP B 221 10669 11579 12353 -49 -941 -3365 N ATOM 4107 CA TRP B 221 22.400 18.995 -1.161 1.00 87.15 C ANISOU 4107 CA TRP B 221 10243 11293 11578 -6 -989 -3185 C ATOM 4108 C TRP B 221 23.413 18.348 -2.115 1.00 89.75 C ANISOU 4108 C TRP B 221 10526 11565 12008 -70 -993 -3024 C ATOM 4109 O TRP B 221 24.104 17.390 -1.758 1.00 87.63 O ANISOU 4109 O TRP B 221 10251 11453 11591 -50 -1093 -3002 O ATOM 4110 CB TRP B 221 21.013 18.401 -1.419 1.00 83.13 C ANISOU 4110 CB TRP B 221 9859 10850 10876 54 -891 -2973 C ATOM 4111 CG TRP B 221 20.470 18.735 -2.772 1.00 87.30 C ANISOU 4111 CG TRP B 221 10404 11180 11586 14 -747 -2776 C ATOM 4112 CD1 TRP B 221 19.746 19.841 -3.117 1.00 84.76 C ANISOU 4112 CD1 TRP B 221 10077 10689 11439 12 -649 -2807 C ATOM 4113 CD2 TRP B 221 20.612 17.959 -3.968 1.00 83.62 C ANISOU 4113 CD2 TRP B 221 9961 10674 11138 -19 -688 -2520 C ATOM 4114 NE1 TRP B 221 19.426 19.801 -4.454 1.00 82.05 N ANISOU 4114 NE1 TRP B 221 9753 10213 11209 -16 -536 -2572 N ATOM 4115 CE2 TRP B 221 19.948 18.656 -5.000 1.00 85.55 C ANISOU 4115 CE2 TRP B 221 10213 10738 11553 -37 -558 -2402 C ATOM 4116 CE3 TRP B 221 21.233 16.744 -4.268 1.00 75.20 C ANISOU 4116 CE3 TRP B 221 8906 9708 9960 -27 -733 -2383 C ATOM 4117 CZ2 TRP B 221 19.891 18.175 -6.309 1.00 82.25 C ANISOU 4117 CZ2 TRP B 221 9816 10259 11177 -62 -477 -2159 C ATOM 4118 CZ3 TRP B 221 21.178 16.269 -5.567 1.00 72.19 C ANISOU 4118 CZ3 TRP B 221 8543 9250 9635 -58 -647 -2156 C ATOM 4119 CH2 TRP B 221 20.513 16.984 -6.571 1.00 79.71 C ANISOU 4119 CH2 TRP B 221 9504 10043 10740 -76 -523 -2049 C ATOM 4120 N TRP B 222 23.497 18.869 -3.331 1.00 85.44 N ANISOU 4120 N TRP B 222 9949 10802 11712 -138 -879 -2905 N ATOM 4121 CA TRP B 222 24.353 18.259 -4.331 1.00 80.12 C ANISOU 4121 CA TRP B 222 9238 10080 11126 -192 -859 -2738 C ATOM 4122 C TRP B 222 25.830 18.370 -3.988 1.00 86.26 C ANISOU 4122 C TRP B 222 9885 10858 12031 -244 -969 -2905 C ATOM 4123 O TRP B 222 26.647 17.605 -4.493 1.00 88.28 O ANISOU 4123 O TRP B 222 10107 11145 12291 -268 -990 -2797 O ATOM 4124 CB TRP B 222 24.080 18.860 -5.701 1.00 76.81 C ANISOU 4124 CB TRP B 222 8813 9440 10930 -244 -704 -2570 C ATOM 4125 CG TRP B 222 24.362 20.325 -5.790 1.00 76.10 C ANISOU 4125 CG TRP B 222 8633 9131 11151 -303 -656 -2720 C ATOM 4126 CD1 TRP B 222 25.583 20.918 -5.888 1.00 81.85 C ANISOU 4126 CD1 TRP B 222 9229 9735 12134 -387 -681 -2845 C ATOM 4127 CD2 TRP B 222 23.398 21.382 -5.821 1.00 71.33 C ANISOU 4127 CD2 TRP B 222 8055 8387 10658 -285 -568 -2755 C ATOM 4128 NE1 TRP B 222 25.442 22.282 -5.969 1.00 87.76 N ANISOU 4128 NE1 TRP B 222 9923 10265 13156 -427 -610 -2956 N ATOM 4129 CE2 TRP B 222 24.109 22.591 -5.932 1.00 77.67 C ANISOU 4129 CE2 TRP B 222 8744 8972 11795 -361 -541 -2901 C ATOM 4130 CE3 TRP B 222 22.003 21.421 -5.768 1.00 71.06 C ANISOU 4130 CE3 TRP B 222 8123 8387 10488 -211 -506 -2677 C ATOM 4131 CZ2 TRP B 222 23.474 23.827 -5.989 1.00 80.62 C ANISOU 4131 CZ2 TRP B 222 9109 9151 12372 -360 -454 -2968 C ATOM 4132 CZ3 TRP B 222 21.374 22.646 -5.824 1.00 74.03 C ANISOU 4132 CZ3 TRP B 222 8488 8585 11054 -205 -425 -2746 C ATOM 4133 CH2 TRP B 222 22.109 23.835 -5.929 1.00 82.17 C ANISOU 4133 CH2 TRP B 222 9411 9390 12421 -276 -400 -2888 C ATOM 4134 N GLU B 223 26.174 19.323 -3.131 1.00 95.32 N ANISOU 4134 N GLU B 223 10952 11973 13291 -261 -1040 -3180 N ATOM 4135 CA GLU B 223 27.564 19.503 -2.730 1.00 95.76 C ANISOU 4135 CA GLU B 223 10867 12037 13482 -313 -1158 -3373 C ATOM 4136 C GLU B 223 28.028 18.322 -1.885 1.00 92.95 C ANISOU 4136 C GLU B 223 10525 11949 12842 -242 -1312 -3395 C ATOM 4137 O GLU B 223 29.224 18.087 -1.730 1.00 92.15 O ANISOU 4137 O GLU B 223 10315 11892 12807 -270 -1414 -3482 O ATOM 4138 CB GLU B 223 27.746 20.825 -1.980 1.00 96.59 C ANISOU 4138 CB GLU B 223 10878 12044 13778 -347 -1202 -3688 C ATOM 4139 CG GLU B 223 27.687 22.044 -2.893 1.00104.80 C ANISOU 4139 CG GLU B 223 11861 12775 15183 -436 -1055 -3673 C ATOM 4140 CD GLU B 223 28.037 23.349 -2.187 1.00115.53 C ANISOU 4140 CD GLU B 223 13104 14007 16786 -484 -1101 -4005 C ATOM 4141 OE1 GLU B 223 27.148 23.942 -1.533 1.00115.83 O ANISOU 4141 OE1 GLU B 223 13193 14046 16770 -433 -1096 -4142 O ATOM 4142 OE2 GLU B 223 29.200 23.794 -2.309 1.00120.33 O ANISOU 4142 OE2 GLU B 223 13562 14506 17654 -576 -1137 -4135 O ATOM 4143 N TYR B 224 27.071 17.575 -1.348 1.00 86.75 N ANISOU 4143 N TYR B 224 9872 11341 11747 -146 -1324 -3305 N ATOM 4144 CA TYR B 224 27.391 16.387 -0.580 1.00 83.32 C ANISOU 4144 CA TYR B 224 9470 11158 11030 -66 -1452 -3278 C ATOM 4145 C TYR B 224 27.490 15.186 -1.499 1.00 86.84 C ANISOU 4145 C TYR B 224 9968 11612 11415 -63 -1398 -2990 C ATOM 4146 O TYR B 224 27.836 14.088 -1.067 1.00 87.63 O ANISOU 4146 O TYR B 224 10093 11886 11317 -1 -1487 -2921 O ATOM 4147 CB TYR B 224 26.326 16.130 0.485 1.00 84.51 C ANISOU 4147 CB TYR B 224 9734 11498 10876 37 -1481 -3311 C ATOM 4148 CG TYR B 224 26.326 17.148 1.601 1.00 97.30 C ANISOU 4148 CG TYR B 224 11301 13169 12498 57 -1565 -3628 C ATOM 4149 CD1 TYR B 224 25.361 18.148 1.658 1.00 99.81 C ANISOU 4149 CD1 TYR B 224 11652 13379 12894 51 -1472 -3719 C ATOM 4150 CD2 TYR B 224 27.296 17.116 2.595 1.00103.33 C ANISOU 4150 CD2 TYR B 224 11975 14095 13190 87 -1741 -3850 C ATOM 4151 CE1 TYR B 224 25.360 19.085 2.676 1.00106.13 C ANISOU 4151 CE1 TYR B 224 12400 14221 13703 72 -1547 -4031 C ATOM 4152 CE2 TYR B 224 27.303 18.049 3.616 1.00111.32 C ANISOU 4152 CE2 TYR B 224 12933 15165 14199 107 -1825 -4166 C ATOM 4153 CZ TYR B 224 26.334 19.031 3.651 1.00112.92 C ANISOU 4153 CZ TYR B 224 13172 15249 14484 97 -1724 -4261 C ATOM 4154 OH TYR B 224 26.343 19.960 4.667 1.00118.82 O ANISOU 4154 OH TYR B 224 13861 16050 15234 120 -1805 -4596 O ATOM 4155 N VAL B 225 27.176 15.390 -2.771 1.00 87.58 N ANISOU 4155 N VAL B 225 10078 11520 11677 -125 -1250 -2821 N ATOM 4156 CA VAL B 225 27.168 14.288 -3.722 1.00 79.69 C ANISOU 4156 CA VAL B 225 9131 10524 10621 -122 -1187 -2560 C ATOM 4157 C VAL B 225 28.344 14.377 -4.682 1.00 81.60 C ANISOU 4157 C VAL B 225 9259 10639 11106 -201 -1162 -2528 C ATOM 4158 O VAL B 225 28.965 13.362 -5.001 1.00 87.15 O ANISOU 4158 O VAL B 225 9951 11408 11755 -187 -1193 -2417 O ATOM 4159 CB VAL B 225 25.847 14.233 -4.517 1.00 76.62 C ANISOU 4159 CB VAL B 225 8857 10064 10191 -116 -1038 -2365 C ATOM 4160 CG1 VAL B 225 25.912 13.150 -5.590 1.00 68.25 C ANISOU 4160 CG1 VAL B 225 7836 8998 9099 -121 -975 -2124 C ATOM 4161 CG2 VAL B 225 24.678 13.999 -3.575 1.00 74.00 C ANISOU 4161 CG2 VAL B 225 8633 9874 9610 -35 -1054 -2379 C ATOM 4162 N ASP B 226 28.646 15.592 -5.136 1.00 80.49 N ANISOU 4162 N ASP B 226 9032 10311 11241 -283 -1098 -2622 N ATOM 4163 CA ASP B 226 29.769 15.827 -6.042 1.00 88.64 C ANISOU 4163 CA ASP B 226 9941 11209 12529 -367 -1055 -2597 C ATOM 4164 C ASP B 226 30.220 17.287 -6.006 1.00 95.69 C ANISOU 4164 C ASP B 226 10714 11919 13724 -452 -1030 -2786 C ATOM 4165 O ASP B 226 29.419 18.206 -6.218 1.00104.99 O ANISOU 4165 O ASP B 226 11930 12961 15001 -470 -933 -2788 O ATOM 4166 CB ASP B 226 29.422 15.405 -7.476 1.00 91.31 C ANISOU 4166 CB ASP B 226 10338 11460 12898 -386 -902 -2328 C ATOM 4167 CG ASP B 226 30.619 15.490 -8.420 1.00 97.12 C ANISOU 4167 CG ASP B 226 10949 12089 13864 -462 -849 -2283 C ATOM 4168 OD1 ASP B 226 30.956 16.613 -8.856 1.00 95.42 O ANISOU 4168 OD1 ASP B 226 10647 11693 13916 -541 -770 -2336 O ATOM 4169 OD2 ASP B 226 31.219 14.433 -8.729 1.00 99.10 O ANISOU 4169 OD2 ASP B 226 11187 12430 14037 -442 -879 -2191 O ATOM 4170 N ALA B 227 31.509 17.490 -5.749 1.00 90.63 N ANISOU 4170 N ALA B 227 9920 11268 13246 -505 -1115 -2944 N ATOM 4171 CA ALA B 227 32.044 18.826 -5.490 1.00 88.19 C ANISOU 4171 CA ALA B 227 9477 10799 13232 -589 -1120 -3172 C ATOM 4172 C ALA B 227 32.137 19.682 -6.742 1.00 90.88 C ANISOU 4172 C ALA B 227 9769 10878 13884 -684 -935 -3051 C ATOM 4173 O ALA B 227 32.079 20.910 -6.661 1.00104.11 O ANISOU 4173 O ALA B 227 11384 12372 15802 -745 -887 -3185 O ATOM 4174 CB ALA B 227 33.404 18.732 -4.819 1.00 83.38 C ANISOU 4174 CB ALA B 227 8705 10274 12703 -617 -1276 -3386 C ATOM 4175 N THR B 228 32.293 19.039 -7.895 1.00 79.45 N ANISOU 4175 N THR B 228 8347 9409 12432 -694 -830 -2800 N ATOM 4176 CA THR B 228 32.413 19.766 -9.156 1.00 84.18 C ANISOU 4176 CA THR B 228 8904 9783 13296 -773 -645 -2650 C ATOM 4177 C THR B 228 31.076 20.399 -9.568 1.00 90.35 C ANISOU 4177 C THR B 228 9810 10453 14067 -745 -519 -2528 C ATOM 4178 O THR B 228 31.039 21.449 -10.221 1.00 95.33 O ANISOU 4178 O THR B 228 10398 10864 14960 -806 -386 -2483 O ATOM 4179 CB THR B 228 32.941 18.846 -10.297 1.00 94.67 C ANISOU 4179 CB THR B 228 10228 11150 14593 -778 -566 -2417 C ATOM 4180 OG1 THR B 228 31.880 18.018 -10.805 1.00 90.45 O ANISOU 4180 OG1 THR B 228 9861 10711 13797 -697 -513 -2198 O ATOM 4181 CG2 THR B 228 34.087 17.969 -9.796 1.00 89.10 C ANISOU 4181 CG2 THR B 228 9425 10599 13831 -771 -708 -2519 C ATOM 4182 N VAL B 229 29.986 19.755 -9.157 1.00 82.98 N ANISOU 4182 N VAL B 229 9024 9670 12836 -650 -562 -2474 N ATOM 4183 CA VAL B 229 28.640 20.109 -9.586 1.00 77.46 C ANISOU 4183 CA VAL B 229 8448 8907 12076 -605 -453 -2334 C ATOM 4184 C VAL B 229 28.206 21.530 -9.222 1.00 80.28 C ANISOU 4184 C VAL B 229 8777 9080 12646 -630 -411 -2477 C ATOM 4185 O VAL B 229 28.368 21.964 -8.078 1.00 79.11 O ANISOU 4185 O VAL B 229 8581 8956 12520 -632 -521 -2738 O ATOM 4186 CB VAL B 229 27.617 19.098 -9.027 1.00 71.97 C ANISOU 4186 CB VAL B 229 7896 8425 11026 -504 -524 -2284 C ATOM 4187 CG1 VAL B 229 26.213 19.679 -9.046 1.00 67.94 C ANISOU 4187 CG1 VAL B 229 7486 7858 10470 -455 -448 -2235 C ATOM 4188 CG2 VAL B 229 27.676 17.812 -9.832 1.00 75.72 C ANISOU 4188 CG2 VAL B 229 8427 9014 11330 -476 -499 -2062 C ATOM 4189 N THR B 230 27.642 22.232 -10.207 1.00 77.94 N ANISOU 4189 N THR B 230 8510 8606 12497 -641 -251 -2306 N ATOM 4190 CA THR B 230 27.088 23.574 -10.016 1.00 77.23 C ANISOU 4190 CA THR B 230 8407 8316 12620 -652 -185 -2399 C ATOM 4191 C THR B 230 25.616 23.642 -10.437 1.00 77.88 C ANISOU 4191 C THR B 230 8625 8397 12568 -566 -98 -2223 C ATOM 4192 O THR B 230 25.172 22.886 -11.306 1.00 73.91 O ANISOU 4192 O THR B 230 8203 7981 11900 -525 -40 -1980 O ATOM 4193 CB THR B 230 27.882 24.641 -10.817 1.00 81.12 C ANISOU 4193 CB THR B 230 8779 8538 13505 -751 -57 -2361 C ATOM 4194 OG1 THR B 230 27.468 24.640 -12.192 1.00 75.68 O ANISOU 4194 OG1 THR B 230 8147 7772 12836 -734 106 -2047 O ATOM 4195 CG2 THR B 230 29.381 24.375 -10.738 1.00 80.82 C ANISOU 4195 CG2 THR B 230 8598 8514 13594 -840 -117 -2465 C ATOM 4196 N LEU B 231 24.873 24.562 -9.827 1.00 83.22 N ANISOU 4196 N LEU B 231 9318 8978 13326 -537 -92 -2358 N ATOM 4197 CA LEU B 231 23.452 24.752 -10.122 1.00 79.90 C ANISOU 4197 CA LEU B 231 9008 8547 12802 -450 -15 -2221 C ATOM 4198 C LEU B 231 23.205 25.084 -11.588 1.00 82.52 C ANISOU 4198 C LEU B 231 9358 8733 13262 -450 149 -1928 C ATOM 4199 O LEU B 231 22.201 24.664 -12.171 1.00 83.54 O ANISOU 4199 O LEU B 231 9585 8944 13212 -375 199 -1730 O ATOM 4200 CB LEU B 231 22.866 25.859 -9.248 1.00 72.84 C ANISOU 4200 CB LEU B 231 8101 7534 12040 -426 -23 -2439 C ATOM 4201 CG LEU B 231 21.352 26.045 -9.371 1.00 74.23 C ANISOU 4201 CG LEU B 231 8383 7721 12101 -325 41 -2332 C ATOM 4202 CD1 LEU B 231 20.613 24.732 -9.048 1.00 69.17 C ANISOU 4202 CD1 LEU B 231 7848 7368 11065 -251 -33 -2261 C ATOM 4203 CD2 LEU B 231 20.855 27.184 -8.490 1.00 70.16 C ANISOU 4203 CD2 LEU B 231 7842 7075 11739 -300 37 -2570 C ATOM 4204 N GLU B 232 24.120 25.848 -12.176 1.00 78.46 N ANISOU 4204 N GLU B 232 8743 8011 13057 -533 234 -1901 N ATOM 4205 CA GLU B 232 24.066 26.165 -13.599 1.00 78.41 C ANISOU 4205 CA GLU B 232 8743 7874 13174 -535 398 -1609 C ATOM 4206 C GLU B 232 24.040 24.894 -14.456 1.00 78.57 C ANISOU 4206 C GLU B 232 8829 8098 12925 -503 405 -1383 C ATOM 4207 O GLU B 232 23.170 24.722 -15.313 1.00 83.48 O ANISOU 4207 O GLU B 232 9534 8758 13428 -432 483 -1157 O ATOM 4208 CB GLU B 232 25.259 27.032 -13.990 1.00 77.38 C ANISOU 4208 CB GLU B 232 8479 7511 13412 -644 482 -1629 C ATOM 4209 CG GLU B 232 25.304 28.385 -13.277 1.00101.55 C ANISOU 4209 CG GLU B 232 11463 10327 16795 -684 495 -1848 C ATOM 4210 CD GLU B 232 25.666 28.281 -11.794 1.00109.90 C ANISOU 4210 CD GLU B 232 12470 11475 17810 -711 320 -2212 C ATOM 4211 OE1 GLU B 232 26.600 27.519 -11.450 1.00106.87 O ANISOU 4211 OE1 GLU B 232 12031 11238 17336 -761 216 -2311 O ATOM 4212 OE2 GLU B 232 25.019 28.976 -10.977 1.00109.05 O ANISOU 4212 OE2 GLU B 232 12375 11298 17759 -676 286 -2400 O ATOM 4213 N LEU B 233 24.997 24.007 -14.210 1.00 64.01 N ANISOU 4213 N LEU B 233 6942 6389 10990 -551 318 -1456 N ATOM 4214 CA LEU B 233 25.095 22.751 -14.945 1.00 64.99 C ANISOU 4214 CA LEU B 233 7116 6700 10876 -526 316 -1278 C ATOM 4215 C LEU B 233 23.864 21.866 -14.709 1.00 65.66 C ANISOU 4215 C LEU B 233 7329 6983 10634 -430 254 -1229 C ATOM 4216 O LEU B 233 23.282 21.339 -15.651 1.00 62.88 O ANISOU 4216 O LEU B 233 7046 6708 10137 -381 316 -1018 O ATOM 4217 CB LEU B 233 26.358 22.005 -14.535 1.00 56.04 C ANISOU 4217 CB LEU B 233 5902 5664 9725 -588 220 -1402 C ATOM 4218 CG LEU B 233 26.606 20.680 -15.246 1.00 62.80 C ANISOU 4218 CG LEU B 233 6797 6700 10365 -566 215 -1246 C ATOM 4219 CD1 LEU B 233 27.010 20.899 -16.707 1.00 56.54 C ANISOU 4219 CD1 LEU B 233 5972 5819 9692 -591 375 -1014 C ATOM 4220 CD2 LEU B 233 27.664 19.867 -14.491 1.00 58.79 C ANISOU 4220 CD2 LEU B 233 6222 6313 9802 -601 81 -1410 C ATOM 4221 N LEU B 234 23.482 21.712 -13.445 1.00 61.31 N ANISOU 4221 N LEU B 234 6805 6520 9971 -405 135 -1431 N ATOM 4222 CA LEU B 234 22.258 21.011 -13.092 1.00 64.82 C ANISOU 4222 CA LEU B 234 7360 7131 10137 -320 87 -1400 C ATOM 4223 C LEU B 234 21.043 21.496 -13.881 1.00 67.40 C ANISOU 4223 C LEU B 234 7752 7397 10462 -255 196 -1221 C ATOM 4224 O LEU B 234 20.269 20.692 -14.406 1.00 73.28 O ANISOU 4224 O LEU B 234 8571 8277 10996 -200 207 -1070 O ATOM 4225 CB LEU B 234 21.975 21.139 -11.600 1.00 67.05 C ANISOU 4225 CB LEU B 234 7650 7477 10349 -299 -26 -1647 C ATOM 4226 CG LEU B 234 22.782 20.226 -10.684 1.00 71.31 C ANISOU 4226 CG LEU B 234 8166 8180 10747 -319 -166 -1794 C ATOM 4227 CD1 LEU B 234 22.146 20.226 -9.310 1.00 73.23 C ANISOU 4227 CD1 LEU B 234 8450 8534 10840 -267 -263 -1986 C ATOM 4228 CD2 LEU B 234 22.835 18.815 -11.243 1.00 65.25 C ANISOU 4228 CD2 LEU B 234 7451 7577 9762 -299 -182 -1625 C ATOM 4229 N ASP B 235 20.858 22.803 -13.960 1.00 59.66 N ANISOU 4229 N ASP B 235 6736 6212 9721 -258 273 -1242 N ATOM 4230 CA ASP B 235 19.690 23.327 -14.664 1.00 57.36 C ANISOU 4230 CA ASP B 235 6500 5860 9436 -182 370 -1072 C ATOM 4231 C ASP B 235 19.813 23.101 -16.164 1.00 52.31 C ANISOU 4231 C ASP B 235 5869 5216 8789 -173 474 -797 C ATOM 4232 O ASP B 235 18.828 22.857 -16.848 1.00 58.39 O ANISOU 4232 O ASP B 235 6704 6063 9420 -97 514 -628 O ATOM 4233 CB ASP B 235 19.473 24.808 -14.345 1.00 63.05 C ANISOU 4233 CB ASP B 235 7178 6345 10434 -179 429 -1163 C ATOM 4234 CG ASP B 235 19.016 25.040 -12.904 1.00 79.42 C ANISOU 4234 CG ASP B 235 9258 8451 12467 -157 333 -1431 C ATOM 4235 OD1 ASP B 235 18.632 24.063 -12.227 1.00 83.47 O ANISOU 4235 OD1 ASP B 235 9825 9182 12710 -127 236 -1502 O ATOM 4236 OD2 ASP B 235 19.034 26.204 -12.448 1.00 83.79 O ANISOU 4236 OD2 ASP B 235 9763 8813 13262 -167 361 -1572 O ATOM 4237 N GLU B 236 21.033 23.159 -16.675 1.00 54.07 N ANISOU 4237 N GLU B 236 6023 5366 9156 -249 516 -758 N ATOM 4238 CA GLU B 236 21.262 22.932 -18.093 1.00 62.26 C ANISOU 4238 CA GLU B 236 7063 6416 10176 -241 622 -505 C ATOM 4239 C GLU B 236 20.961 21.465 -18.446 1.00 61.90 C ANISOU 4239 C GLU B 236 7084 6622 9814 -205 562 -429 C ATOM 4240 O GLU B 236 20.313 21.174 -19.450 1.00 62.30 O ANISOU 4240 O GLU B 236 7184 6750 9736 -143 620 -233 O ATOM 4241 CB GLU B 236 22.705 23.306 -18.438 1.00 79.17 C ANISOU 4241 CB GLU B 236 9102 8428 12552 -338 683 -505 C ATOM 4242 CG GLU B 236 23.124 23.027 -19.875 1.00101.66 C ANISOU 4242 CG GLU B 236 11944 11306 15377 -335 800 -253 C ATOM 4243 CD GLU B 236 24.613 23.272 -20.116 1.00114.46 C ANISOU 4243 CD GLU B 236 13452 12820 17220 -438 858 -272 C ATOM 4244 OE1 GLU B 236 25.145 24.293 -19.609 1.00115.56 O ANISOU 4244 OE1 GLU B 236 13508 12751 17650 -505 884 -388 O ATOM 4245 OE2 GLU B 236 25.244 22.442 -20.815 1.00113.30 O ANISOU 4245 OE2 GLU B 236 13291 12794 16964 -452 880 -178 O ATOM 4246 N LEU B 237 21.419 20.553 -17.593 1.00 52.07 N ANISOU 4246 N LEU B 237 5835 5502 8447 -239 443 -590 N ATOM 4247 CA LEU B 237 21.278 19.128 -17.838 1.00 52.19 C ANISOU 4247 CA LEU B 237 5903 5729 8199 -216 385 -538 C ATOM 4248 C LEU B 237 19.848 18.624 -17.584 1.00 53.82 C ANISOU 4248 C LEU B 237 6199 6065 8184 -137 341 -519 C ATOM 4249 O LEU B 237 19.353 17.782 -18.329 1.00 51.86 O ANISOU 4249 O LEU B 237 5998 5949 7759 -99 350 -392 O ATOM 4250 CB LEU B 237 22.316 18.335 -17.027 1.00 55.31 C ANISOU 4250 CB LEU B 237 6257 6200 8558 -272 278 -699 C ATOM 4251 CG LEU B 237 23.791 18.584 -17.393 1.00 55.88 C ANISOU 4251 CG LEU B 237 6226 6180 8826 -351 318 -709 C ATOM 4252 CD1 LEU B 237 24.731 17.588 -16.714 1.00 53.13 C ANISOU 4252 CD1 LEU B 237 5840 5944 8401 -386 203 -843 C ATOM 4253 CD2 LEU B 237 24.003 18.570 -18.910 1.00 47.19 C ANISOU 4253 CD2 LEU B 237 5117 5063 7748 -346 450 -483 C ATOM 4254 N THR B 238 19.186 19.146 -16.551 1.00 51.77 N ANISOU 4254 N THR B 238 5956 5772 7942 -115 296 -653 N ATOM 4255 CA THR B 238 17.796 18.789 -16.292 1.00 51.31 C ANISOU 4255 CA THR B 238 5969 5825 7702 -42 269 -636 C ATOM 4256 C THR B 238 16.901 19.217 -17.447 1.00 54.25 C ANISOU 4256 C THR B 238 6365 6171 8075 23 364 -437 C ATOM 4257 O THR B 238 15.976 18.499 -17.825 1.00 64.23 O ANISOU 4257 O THR B 238 7678 7576 9152 74 352 -353 O ATOM 4258 CB THR B 238 17.241 19.373 -14.960 1.00 56.31 C ANISOU 4258 CB THR B 238 6609 6425 8359 -23 218 -823 C ATOM 4259 OG1 THR B 238 17.453 20.788 -14.909 1.00 64.70 O ANISOU 4259 OG1 THR B 238 7623 7281 9681 -33 278 -870 O ATOM 4260 CG2 THR B 238 17.913 18.728 -13.768 1.00 50.79 C ANISOU 4260 CG2 THR B 238 5901 5817 7580 -63 106 -1009 C ATOM 4261 N HIS B 239 17.182 20.377 -18.019 1.00 51.51 N ANISOU 4261 N HIS B 239 5979 5647 7944 22 458 -359 N ATOM 4262 CA HIS B 239 16.378 20.876 -19.127 1.00 54.54 C ANISOU 4262 CA HIS B 239 6382 6005 8335 98 549 -154 C ATOM 4263 C HIS B 239 16.538 19.959 -20.340 1.00 56.83 C ANISOU 4263 C HIS B 239 6691 6438 8465 109 574 18 C ATOM 4264 O HIS B 239 15.558 19.626 -21.012 1.00 54.59 O ANISOU 4264 O HIS B 239 6445 6269 8029 183 583 138 O ATOM 4265 CB HIS B 239 16.765 22.320 -19.469 1.00 53.49 C ANISOU 4265 CB HIS B 239 6201 5632 8489 93 655 -92 C ATOM 4266 CG HIS B 239 16.107 22.845 -20.707 1.00 69.03 C ANISOU 4266 CG HIS B 239 8186 7572 10469 177 757 154 C ATOM 4267 ND1 HIS B 239 16.753 22.905 -21.926 1.00 74.31 N ANISOU 4267 ND1 HIS B 239 8837 8226 11173 172 851 350 N ATOM 4268 CD2 HIS B 239 14.858 23.329 -20.918 1.00 67.52 C ANISOU 4268 CD2 HIS B 239 8025 7379 10251 279 780 239 C ATOM 4269 CE1 HIS B 239 15.933 23.411 -22.832 1.00 68.86 C ANISOU 4269 CE1 HIS B 239 8169 7530 10466 270 924 553 C ATOM 4270 NE2 HIS B 239 14.777 23.674 -22.246 1.00 65.23 N ANISOU 4270 NE2 HIS B 239 7736 7075 9974 337 878 488 N ATOM 4271 N GLU B 240 17.771 19.534 -20.610 1.00 44.81 N ANISOU 4271 N GLU B 240 5133 4918 6975 39 582 14 N ATOM 4272 CA GLU B 240 18.019 18.568 -21.684 1.00 53.68 C ANISOU 4272 CA GLU B 240 6269 6188 7939 48 600 143 C ATOM 4273 C GLU B 240 17.281 17.252 -21.477 1.00 46.67 C ANISOU 4273 C GLU B 240 5433 5502 6796 73 507 96 C ATOM 4274 O GLU B 240 16.621 16.749 -22.390 1.00 45.60 O ANISOU 4274 O GLU B 240 5327 5492 6508 129 522 215 O ATOM 4275 CB GLU B 240 19.506 18.269 -21.820 1.00 60.30 C ANISOU 4275 CB GLU B 240 7052 6998 8862 -34 616 112 C ATOM 4276 CG GLU B 240 20.249 19.238 -22.685 1.00 80.33 C ANISOU 4276 CG GLU B 240 9535 9389 11597 -52 748 250 C ATOM 4277 CD GLU B 240 21.699 18.840 -22.857 1.00 93.90 C ANISOU 4277 CD GLU B 240 11188 11101 13389 -133 766 217 C ATOM 4278 OE1 GLU B 240 21.963 17.614 -22.961 1.00 89.64 O ANISOU 4278 OE1 GLU B 240 10662 10721 12675 -139 706 182 O ATOM 4279 OE2 GLU B 240 22.562 19.752 -22.891 1.00 96.26 O ANISOU 4279 OE2 GLU B 240 11414 11228 13932 -190 844 225 O ATOM 4280 N LEU B 241 17.435 16.672 -20.291 1.00 42.63 N ANISOU 4280 N LEU B 241 4930 5026 6243 32 410 -79 N ATOM 4281 CA LEU B 241 16.742 15.423 -19.950 1.00 47.99 C ANISOU 4281 CA LEU B 241 5655 5874 6705 49 328 -126 C ATOM 4282 C LEU B 241 15.206 15.576 -20.013 1.00 49.57 C ANISOU 4282 C LEU B 241 5893 6132 6811 123 329 -79 C ATOM 4283 O LEU B 241 14.519 14.740 -20.597 1.00 53.32 O ANISOU 4283 O LEU B 241 6391 6744 7124 155 314 -16 O ATOM 4284 CB LEU B 241 17.179 14.949 -18.567 1.00 44.51 C ANISOU 4284 CB LEU B 241 5215 5446 6250 3 234 -305 C ATOM 4285 CG LEU B 241 16.555 13.673 -18.018 1.00 44.01 C ANISOU 4285 CG LEU B 241 5198 5535 5989 13 156 -355 C ATOM 4286 CD1 LEU B 241 16.798 12.484 -18.958 1.00 37.02 C ANISOU 4286 CD1 LEU B 241 4321 4758 4988 8 156 -273 C ATOM 4287 CD2 LEU B 241 17.118 13.400 -16.630 1.00 44.62 C ANISOU 4287 CD2 LEU B 241 5273 5615 6066 -23 72 -515 C ATOM 4288 N LEU B 242 14.676 16.657 -19.444 1.00 43.44 N ANISOU 4288 N LEU B 242 5112 5249 6145 151 347 -117 N ATOM 4289 CA LEU B 242 13.250 16.924 -19.542 1.00 49.68 C ANISOU 4289 CA LEU B 242 5924 6084 6870 229 356 -69 C ATOM 4290 C LEU B 242 12.761 17.009 -20.983 1.00 50.35 C ANISOU 4290 C LEU B 242 6007 6222 6902 293 414 122 C ATOM 4291 O LEU B 242 11.671 16.539 -21.303 1.00 58.24 O ANISOU 4291 O LEU B 242 7021 7348 7761 347 392 165 O ATOM 4292 CB LEU B 242 12.855 18.180 -18.773 1.00 44.26 C ANISOU 4292 CB LEU B 242 5224 5253 6338 256 378 -141 C ATOM 4293 CG LEU B 242 11.333 18.374 -18.691 1.00 47.24 C ANISOU 4293 CG LEU B 242 5616 5689 6643 340 379 -116 C ATOM 4294 CD1 LEU B 242 10.665 17.096 -18.235 1.00 39.70 C ANISOU 4294 CD1 LEU B 242 4688 4918 5478 333 308 -175 C ATOM 4295 CD2 LEU B 242 10.970 19.530 -17.758 1.00 44.48 C ANISOU 4295 CD2 LEU B 242 5253 5201 6444 367 396 -225 C ATOM 4296 N GLN B 243 13.562 17.592 -21.858 1.00 47.88 N ANISOU 4296 N GLN B 243 5672 5823 6697 289 490 238 N ATOM 4297 CA GLN B 243 13.139 17.723 -23.247 1.00 55.86 C ANISOU 4297 CA GLN B 243 6683 6900 7641 362 549 432 C ATOM 4298 C GLN B 243 13.024 16.376 -23.947 1.00 54.83 C ANISOU 4298 C GLN B 243 6567 6973 7293 362 506 456 C ATOM 4299 O GLN B 243 12.045 16.125 -24.662 1.00 51.74 O ANISOU 4299 O GLN B 243 6182 6709 6766 435 496 538 O ATOM 4300 CB GLN B 243 14.068 18.646 -24.037 1.00 63.00 C ANISOU 4300 CB GLN B 243 7560 7669 8707 359 656 568 C ATOM 4301 CG GLN B 243 13.762 20.120 -23.871 1.00 77.55 C ANISOU 4301 CG GLN B 243 9388 9320 10759 402 724 624 C ATOM 4302 CD GLN B 243 14.229 20.936 -25.059 1.00 93.79 C ANISOU 4302 CD GLN B 243 11426 11292 12919 440 847 843 C ATOM 4303 OE1 GLN B 243 14.779 20.398 -26.022 1.00100.33 O ANISOU 4303 OE1 GLN B 243 12252 12224 13645 436 882 950 O ATOM 4304 NE2 GLN B 243 14.003 22.240 -25.004 1.00 99.67 N ANISOU 4304 NE2 GLN B 243 12155 11846 13869 481 920 915 N ATOM 4305 N ILE B 244 14.019 15.507 -23.768 1.00 52.38 N ANISOU 4305 N ILE B 244 6255 6694 6954 286 477 377 N ATOM 4306 CA ILE B 244 13.928 14.205 -24.421 1.00 51.42 C ANISOU 4306 CA ILE B 244 6144 6749 6643 286 439 383 C ATOM 4307 C ILE B 244 12.782 13.413 -23.792 1.00 43.12 C ANISOU 4307 C ILE B 244 5114 5804 5466 296 355 290 C ATOM 4308 O ILE B 244 12.060 12.724 -24.497 1.00 43.25 O ANISOU 4308 O ILE B 244 5132 5964 5338 333 332 325 O ATOM 4309 CB ILE B 244 15.284 13.404 -24.521 1.00 50.21 C ANISOU 4309 CB ILE B 244 5978 6608 6492 213 436 334 C ATOM 4310 CG1 ILE B 244 15.078 12.126 -25.335 1.00 64.16 C ANISOU 4310 CG1 ILE B 244 7753 8552 8074 227 406 342 C ATOM 4311 CG2 ILE B 244 15.813 13.004 -23.171 1.00 48.80 C ANISOU 4311 CG2 ILE B 244 5801 6372 6370 141 367 172 C ATOM 4312 CD1 ILE B 244 14.665 12.351 -26.798 1.00 68.22 C ANISOU 4312 CD1 ILE B 244 8261 9170 8490 306 464 494 C ATOM 4313 N LEU B 245 12.585 13.554 -22.478 1.00 43.38 N ANISOU 4313 N LEU B 245 5156 5769 5556 266 314 171 N ATOM 4314 CA LEU B 245 11.457 12.892 -21.800 1.00 37.19 C ANISOU 4314 CA LEU B 245 4389 5077 4666 275 252 94 C ATOM 4315 C LEU B 245 10.104 13.308 -22.381 1.00 44.75 C ANISOU 4315 C LEU B 245 5334 6100 5571 359 266 175 C ATOM 4316 O LEU B 245 9.232 12.461 -22.593 1.00 48.47 O ANISOU 4316 O LEU B 245 5799 6703 5914 373 226 162 O ATOM 4317 CB LEU B 245 11.503 13.121 -20.284 1.00 36.60 C ANISOU 4317 CB LEU B 245 4326 4926 4655 240 219 -39 C ATOM 4318 CG LEU B 245 12.472 12.192 -19.535 1.00 40.40 C ANISOU 4318 CG LEU B 245 4820 5417 5113 167 167 -140 C ATOM 4319 CD1 LEU B 245 12.732 12.680 -18.144 1.00 30.53 C ANISOU 4319 CD1 LEU B 245 3577 4089 3935 144 140 -262 C ATOM 4320 CD2 LEU B 245 11.969 10.766 -19.513 1.00 39.50 C ANISOU 4320 CD2 LEU B 245 4723 5435 4850 151 120 -161 C ATOM 4321 N GLU B 246 9.942 14.599 -22.674 1.00 47.20 N ANISOU 4321 N GLU B 246 5631 6312 5989 417 323 261 N ATOM 4322 CA GLU B 246 8.699 15.093 -23.274 1.00 45.21 C ANISOU 4322 CA GLU B 246 5361 6119 5698 514 335 354 C ATOM 4323 C GLU B 246 8.460 14.544 -24.683 1.00 50.56 C ANISOU 4323 C GLU B 246 6026 6951 6234 561 333 466 C ATOM 4324 O GLU B 246 7.323 14.439 -25.129 1.00 49.88 O ANISOU 4324 O GLU B 246 5917 6981 6056 629 307 504 O ATOM 4325 CB GLU B 246 8.668 16.618 -23.274 1.00 38.76 C ANISOU 4325 CB GLU B 246 4535 5143 5050 572 403 432 C ATOM 4326 CG GLU B 246 8.638 17.254 -21.877 1.00 49.04 C ANISOU 4326 CG GLU B 246 5841 6305 6485 545 399 297 C ATOM 4327 CD GLU B 246 8.966 18.760 -21.890 1.00 65.20 C ANISOU 4327 CD GLU B 246 7876 8150 8747 580 475 355 C ATOM 4328 OE1 GLU B 246 9.392 19.288 -22.945 1.00 64.29 O ANISOU 4328 OE1 GLU B 246 7753 7987 8688 614 540 515 O ATOM 4329 OE2 GLU B 246 8.806 19.417 -20.836 1.00 70.83 O ANISOU 4329 OE2 GLU B 246 8585 8749 9577 575 475 240 O ATOM 4330 N LYS B 247 9.538 14.179 -25.369 1.00 54.74 N ANISOU 4330 N LYS B 247 6563 7494 6742 526 358 508 N ATOM 4331 CA LYS B 247 9.452 13.641 -26.727 1.00 52.60 C ANISOU 4331 CA LYS B 247 6280 7381 6324 571 360 599 C ATOM 4332 C LYS B 247 9.244 12.127 -26.751 1.00 51.72 C ANISOU 4332 C LYS B 247 6166 7418 6069 523 286 485 C ATOM 4333 O LYS B 247 9.054 11.530 -27.808 1.00 58.31 O ANISOU 4333 O LYS B 247 6985 8403 6768 557 271 519 O ATOM 4334 CB LYS B 247 10.714 14.004 -27.518 1.00 49.47 C ANISOU 4334 CB LYS B 247 5888 6935 5974 563 438 703 C ATOM 4335 CG LYS B 247 10.779 15.476 -27.899 1.00 54.24 C ANISOU 4335 CG LYS B 247 6486 7415 6705 630 527 864 C ATOM 4336 CD LYS B 247 12.153 15.877 -28.429 1.00 66.51 C ANISOU 4336 CD LYS B 247 8038 8882 8351 598 620 955 C ATOM 4337 CE LYS B 247 12.203 17.378 -28.708 1.00 82.97 C ANISOU 4337 CE LYS B 247 10115 10810 10599 657 719 1120 C ATOM 4338 NZ LYS B 247 13.587 17.957 -28.742 1.00 93.83 N ANISOU 4338 NZ LYS B 247 11476 12023 12152 592 816 1167 N ATOM 4339 N THR B 248 9.270 11.502 -25.583 1.00 52.05 N ANISOU 4339 N THR B 248 6221 7417 6141 447 241 347 N ATOM 4340 CA THR B 248 9.118 10.056 -25.500 1.00 47.80 C ANISOU 4340 CA THR B 248 5680 6984 5499 394 180 244 C ATOM 4341 C THR B 248 7.700 9.667 -25.090 1.00 48.16 C ANISOU 4341 C THR B 248 5702 7109 5487 409 130 187 C ATOM 4342 O THR B 248 7.341 9.745 -23.915 1.00 53.84 O ANISOU 4342 O THR B 248 6431 7765 6262 380 118 120 O ATOM 4343 CB THR B 248 10.113 9.484 -24.486 1.00 51.78 C ANISOU 4343 CB THR B 248 6211 7396 6067 304 166 144 C ATOM 4344 OG1 THR B 248 11.398 10.076 -24.710 1.00 47.56 O ANISOU 4344 OG1 THR B 248 5683 6766 5620 289 217 192 O ATOM 4345 CG2 THR B 248 10.209 7.967 -24.623 1.00 37.26 C ANISOU 4345 CG2 THR B 248 4371 5647 4140 254 119 63 C ATOM 4346 N PRO B 249 6.887 9.235 -26.062 1.00 49.90 N ANISOU 4346 N PRO B 249 5884 7480 5594 456 101 207 N ATOM 4347 CA PRO B 249 5.460 8.924 -25.843 1.00 45.16 C ANISOU 4347 CA PRO B 249 5240 6970 4948 476 55 159 C ATOM 4348 C PRO B 249 5.230 8.030 -24.629 1.00 47.46 C ANISOU 4348 C PRO B 249 5538 7226 5267 389 29 38 C ATOM 4349 O PRO B 249 5.858 6.981 -24.518 1.00 52.10 O ANISOU 4349 O PRO B 249 6144 7812 5839 318 12 -27 O ATOM 4350 CB PRO B 249 5.064 8.189 -27.122 1.00 47.56 C ANISOU 4350 CB PRO B 249 5501 7450 5120 507 15 156 C ATOM 4351 CG PRO B 249 6.049 8.731 -28.185 1.00 41.69 C ANISOU 4351 CG PRO B 249 4781 6715 4344 556 60 267 C ATOM 4352 CD PRO B 249 7.336 8.928 -27.434 1.00 43.71 C ANISOU 4352 CD PRO B 249 5090 6805 4713 489 107 261 C ATOM 4353 N ASN B 250 4.366 8.473 -23.718 1.00 46.80 N ANISOU 4353 N ASN B 250 5441 7110 5229 400 33 17 N ATOM 4354 CA ASN B 250 3.974 7.712 -22.527 1.00 46.10 C ANISOU 4354 CA ASN B 250 5356 7004 5155 331 21 -78 C ATOM 4355 C ASN B 250 4.968 7.669 -21.381 1.00 52.54 C ANISOU 4355 C ASN B 250 6233 7700 6029 272 39 -117 C ATOM 4356 O ASN B 250 4.644 7.167 -20.297 1.00 57.50 O ANISOU 4356 O ASN B 250 6870 8316 6661 228 37 -178 O ATOM 4357 CB ASN B 250 3.567 6.283 -22.895 1.00 51.77 C ANISOU 4357 CB ASN B 250 6038 7821 5810 277 -18 -143 C ATOM 4358 CG ASN B 250 2.441 6.249 -23.909 1.00 65.52 C ANISOU 4358 CG ASN B 250 7702 9703 7490 332 -50 -134 C ATOM 4359 OD1 ASN B 250 1.348 6.775 -23.663 1.00 63.49 O ANISOU 4359 OD1 ASN B 250 7397 9481 7243 377 -49 -126 O ATOM 4360 ND2 ASN B 250 2.702 5.633 -25.064 1.00 68.49 N ANISOU 4360 ND2 ASN B 250 8058 10170 7795 335 -82 -145 N ATOM 4361 N ARG B 251 6.173 8.187 -21.596 1.00 48.83 N ANISOU 4361 N ARG B 251 5801 7149 5603 273 56 -82 N ATOM 4362 CA ARG B 251 7.207 8.059 -20.573 1.00 40.75 C ANISOU 4362 CA ARG B 251 4824 6028 4630 218 57 -133 C ATOM 4363 C ARG B 251 6.903 8.916 -19.338 1.00 44.52 C ANISOU 4363 C ARG B 251 5316 6436 5164 232 74 -170 C ATOM 4364 O ARG B 251 6.961 8.424 -18.205 1.00 45.90 O ANISOU 4364 O ARG B 251 5513 6601 5324 192 61 -237 O ATOM 4365 CB ARG B 251 8.593 8.353 -21.166 1.00 48.90 C ANISOU 4365 CB ARG B 251 5876 6998 5707 209 72 -95 C ATOM 4366 CG ARG B 251 9.766 7.949 -20.280 1.00 51.62 C ANISOU 4366 CG ARG B 251 6254 7268 6093 149 56 -156 C ATOM 4367 CD ARG B 251 9.765 6.462 -19.998 1.00 45.35 C ANISOU 4367 CD ARG B 251 5468 6528 5235 98 19 -207 C ATOM 4368 NE ARG B 251 9.478 5.700 -21.208 1.00 47.86 N ANISOU 4368 NE ARG B 251 5759 6933 5492 102 13 -186 N ATOM 4369 CZ ARG B 251 10.381 5.335 -22.113 1.00 49.71 C ANISOU 4369 CZ ARG B 251 5990 7178 5720 96 17 -171 C ATOM 4370 NH1 ARG B 251 11.666 5.645 -21.964 1.00 45.33 N ANISOU 4370 NH1 ARG B 251 5451 6545 5227 80 30 -166 N ATOM 4371 NH2 ARG B 251 9.991 4.652 -23.178 1.00 54.64 N ANISOU 4371 NH2 ARG B 251 6587 7898 6276 106 9 -172 N ATOM 4372 N LEU B 252 6.554 10.185 -19.546 1.00 46.24 N ANISOU 4372 N LEU B 252 5519 6609 5443 296 105 -128 N ATOM 4373 CA LEU B 252 6.259 11.070 -18.416 1.00 37.72 C ANISOU 4373 CA LEU B 252 4448 5458 4427 316 124 -182 C ATOM 4374 C LEU B 252 4.992 10.657 -17.693 1.00 41.56 C ANISOU 4374 C LEU B 252 4913 6025 4852 324 121 -230 C ATOM 4375 O LEU B 252 4.856 10.871 -16.485 1.00 40.28 O ANISOU 4375 O LEU B 252 4768 5839 4700 318 130 -304 O ATOM 4376 CB LEU B 252 6.172 12.521 -18.862 1.00 41.54 C ANISOU 4376 CB LEU B 252 4916 5855 5013 387 165 -124 C ATOM 4377 CG LEU B 252 7.545 13.093 -19.193 1.00 40.30 C ANISOU 4377 CG LEU B 252 4778 5582 4952 366 184 -94 C ATOM 4378 CD1 LEU B 252 7.439 14.468 -19.850 1.00 36.14 C ANISOU 4378 CD1 LEU B 252 4232 4960 4539 438 238 -2 C ATOM 4379 CD2 LEU B 252 8.401 13.116 -17.925 1.00 36.54 C ANISOU 4379 CD2 LEU B 252 4330 5030 4525 309 166 -212 C ATOM 4380 N LYS B 253 4.068 10.054 -18.432 1.00 41.71 N ANISOU 4380 N LYS B 253 4890 6150 4810 337 111 -192 N ATOM 4381 CA LYS B 253 2.855 9.527 -17.839 1.00 50.77 C ANISOU 4381 CA LYS B 253 6001 7379 5909 332 114 -233 C ATOM 4382 C LYS B 253 3.157 8.640 -16.619 1.00 49.59 C ANISOU 4382 C LYS B 253 5890 7231 5722 261 113 -300 C ATOM 4383 O LYS B 253 2.466 8.702 -15.604 1.00 48.08 O ANISOU 4383 O LYS B 253 5691 7061 5514 267 139 -344 O ATOM 4384 CB LYS B 253 2.062 8.760 -18.888 1.00 52.91 C ANISOU 4384 CB LYS B 253 6213 7765 6124 333 90 -201 C ATOM 4385 CG LYS B 253 0.711 8.289 -18.417 1.00 51.65 C ANISOU 4385 CG LYS B 253 5995 7692 5939 328 99 -239 C ATOM 4386 CD LYS B 253 -0.005 7.571 -19.547 1.00 65.96 C ANISOU 4386 CD LYS B 253 7736 9618 7709 327 63 -226 C ATOM 4387 CE LYS B 253 -1.395 7.114 -19.100 1.00 86.14 C ANISOU 4387 CE LYS B 253 10212 12256 10261 315 76 -269 C ATOM 4388 NZ LYS B 253 -2.265 6.747 -20.255 1.00 98.25 N ANISOU 4388 NZ LYS B 253 11653 13910 11767 337 32 -268 N ATOM 4389 N ARG B 254 4.219 7.850 -16.701 1.00 42.37 N ANISOU 4389 N ARG B 254 5015 6293 4790 204 86 -301 N ATOM 4390 CA ARG B 254 4.583 6.965 -15.594 1.00 45.33 C ANISOU 4390 CA ARG B 254 5429 6668 5125 149 81 -343 C ATOM 4391 C ARG B 254 4.866 7.689 -14.289 1.00 46.54 C ANISOU 4391 C ARG B 254 5618 6780 5284 167 94 -399 C ATOM 4392 O ARG B 254 4.705 7.113 -13.231 1.00 52.84 O ANISOU 4392 O ARG B 254 6438 7613 6026 145 103 -427 O ATOM 4393 CB ARG B 254 5.779 6.090 -15.962 1.00 53.79 C ANISOU 4393 CB ARG B 254 6532 7711 6193 99 47 -333 C ATOM 4394 CG ARG B 254 5.567 5.251 -17.215 1.00 63.69 C ANISOU 4394 CG ARG B 254 7752 9014 7433 78 32 -302 C ATOM 4395 CD ARG B 254 6.489 4.072 -17.201 1.00 80.83 C ANISOU 4395 CD ARG B 254 9952 11163 9597 23 7 -311 C ATOM 4396 NE ARG B 254 6.974 3.724 -18.533 1.00 95.23 N ANISOU 4396 NE ARG B 254 11758 13001 11425 19 -11 -296 N ATOM 4397 CZ ARG B 254 7.974 2.873 -18.737 1.00 93.73 C ANISOU 4397 CZ ARG B 254 11589 12781 11244 -16 -31 -307 C ATOM 4398 NH1 ARG B 254 8.559 2.312 -17.684 1.00 91.97 N ANISOU 4398 NH1 ARG B 254 11405 12511 11029 -46 -40 -321 N ATOM 4399 NH2 ARG B 254 8.384 2.582 -19.969 1.00 87.70 N ANISOU 4399 NH2 ARG B 254 10805 12043 10476 -13 -40 -304 N ATOM 4400 N ILE B 255 5.291 8.945 -14.346 1.00 44.02 N ANISOU 4400 N ILE B 255 5304 6386 5034 209 98 -418 N ATOM 4401 CA ILE B 255 5.601 9.658 -13.115 1.00 41.49 C ANISOU 4401 CA ILE B 255 5011 6027 4724 226 103 -500 C ATOM 4402 C ILE B 255 4.636 10.820 -12.855 1.00 47.94 C ANISOU 4402 C ILE B 255 5798 6831 5586 293 144 -533 C ATOM 4403 O ILE B 255 4.814 11.586 -11.912 1.00 47.98 O ANISOU 4403 O ILE B 255 5819 6799 5614 317 152 -620 O ATOM 4404 CB ILE B 255 7.066 10.149 -13.096 1.00 47.45 C ANISOU 4404 CB ILE B 255 5795 6687 5548 210 70 -533 C ATOM 4405 CG1 ILE B 255 7.344 11.051 -14.305 1.00 44.05 C ANISOU 4405 CG1 ILE B 255 5339 6173 5226 234 87 -476 C ATOM 4406 CG2 ILE B 255 8.029 8.947 -13.085 1.00 41.92 C ANISOU 4406 CG2 ILE B 255 5123 6008 4798 152 28 -516 C ATOM 4407 CD1 ILE B 255 8.674 11.795 -14.251 1.00 33.16 C ANISOU 4407 CD1 ILE B 255 3968 4680 3950 219 74 -514 C ATOM 4408 N TRP B 256 3.607 10.930 -13.686 1.00 45.20 N ANISOU 4408 N TRP B 256 5402 6521 5252 327 167 -473 N ATOM 4409 CA TRP B 256 2.690 12.058 -13.617 1.00 45.26 C ANISOU 4409 CA TRP B 256 5371 6508 5319 403 206 -490 C ATOM 4410 C TRP B 256 1.665 11.887 -12.511 1.00 46.38 C ANISOU 4410 C TRP B 256 5495 6730 5397 418 242 -553 C ATOM 4411 O TRP B 256 0.968 10.882 -12.452 1.00 41.77 O ANISOU 4411 O TRP B 256 4888 6245 4738 387 251 -527 O ATOM 4412 CB TRP B 256 1.965 12.225 -14.949 1.00 42.14 C ANISOU 4412 CB TRP B 256 4922 6139 4951 446 209 -394 C ATOM 4413 CG TRP B 256 1.020 13.380 -14.986 1.00 47.00 C ANISOU 4413 CG TRP B 256 5491 6730 5638 538 245 -394 C ATOM 4414 CD1 TRP B 256 1.347 14.708 -14.981 1.00 43.30 C ANISOU 4414 CD1 TRP B 256 5030 6134 5288 595 267 -403 C ATOM 4415 CD2 TRP B 256 -0.409 13.316 -15.052 1.00 47.57 C ANISOU 4415 CD2 TRP B 256 5493 6895 5685 586 265 -384 C ATOM 4416 NE1 TRP B 256 0.208 15.470 -15.047 1.00 51.12 N ANISOU 4416 NE1 TRP B 256 5965 7131 6328 684 300 -394 N ATOM 4417 CE2 TRP B 256 -0.884 14.645 -15.087 1.00 46.28 C ANISOU 4417 CE2 TRP B 256 5300 6660 5623 681 297 -384 C ATOM 4418 CE3 TRP B 256 -1.335 12.264 -15.086 1.00 46.76 C ANISOU 4418 CE3 TRP B 256 5342 6925 5501 555 262 -379 C ATOM 4419 CZ2 TRP B 256 -2.248 14.954 -15.150 1.00 41.22 C ANISOU 4419 CZ2 TRP B 256 4583 6086 4994 756 322 -378 C ATOM 4420 CZ3 TRP B 256 -2.689 12.567 -15.157 1.00 48.91 C ANISOU 4420 CZ3 TRP B 256 5531 7266 5787 619 287 -377 C ATOM 4421 CH2 TRP B 256 -3.135 13.906 -15.183 1.00 48.67 C ANISOU 4421 CH2 TRP B 256 5472 7173 5848 723 314 -376 C ATOM 4422 N ASN B 257 1.572 12.881 -11.641 1.00 43.62 N ANISOU 4422 N ASN B 257 5151 6335 5087 466 268 -642 N ATOM 4423 CA ASN B 257 0.590 12.861 -10.580 1.00 44.27 C ANISOU 4423 CA ASN B 257 5213 6501 5108 493 315 -708 C ATOM 4424 C ASN B 257 -0.802 13.223 -11.101 1.00 54.72 C ANISOU 4424 C ASN B 257 6456 7864 6469 555 355 -671 C ATOM 4425 O ASN B 257 -1.081 14.379 -11.428 1.00 53.31 O ANISOU 4425 O ASN B 257 6250 7611 6395 630 371 -680 O ATOM 4426 CB ASN B 257 1.017 13.805 -9.469 1.00 45.19 C ANISOU 4426 CB ASN B 257 5360 6563 5248 528 326 -839 C ATOM 4427 CG ASN B 257 0.060 13.800 -8.304 1.00 50.98 C ANISOU 4427 CG ASN B 257 6075 7397 5897 563 382 -918 C ATOM 4428 OD1 ASN B 257 -0.953 13.107 -8.313 1.00 59.55 O ANISOU 4428 OD1 ASN B 257 7120 8587 6920 558 421 -866 O ATOM 4429 ND2 ASN B 257 0.375 14.583 -7.295 1.00 57.00 N ANISOU 4429 ND2 ASN B 257 6862 8135 6663 599 390 -1052 N ATOM 4430 N TRP B 258 -1.667 12.213 -11.127 1.00 52.61 N ANISOU 4430 N TRP B 258 6148 7713 6126 525 373 -630 N ATOM 4431 CA TRP B 258 -2.950 12.231 -11.821 1.00 52.46 C ANISOU 4431 CA TRP B 258 6037 7759 6135 565 393 -583 C ATOM 4432 C TRP B 258 -4.083 12.605 -10.883 1.00 53.89 C ANISOU 4432 C TRP B 258 6166 8004 6306 617 463 -650 C ATOM 4433 O TRP B 258 -5.251 12.579 -11.268 1.00 57.76 O ANISOU 4433 O TRP B 258 6566 8564 6818 652 486 -625 O ATOM 4434 CB TRP B 258 -3.232 10.815 -12.339 1.00 59.47 C ANISOU 4434 CB TRP B 258 6897 8736 6962 487 374 -521 C ATOM 4435 CG TRP B 258 -3.012 9.810 -11.238 1.00 65.63 C ANISOU 4435 CG TRP B 258 7720 9564 7652 414 402 -546 C ATOM 4436 CD1 TRP B 258 -1.845 9.158 -10.946 1.00 68.84 C ANISOU 4436 CD1 TRP B 258 8209 9936 8011 352 370 -539 C ATOM 4437 CD2 TRP B 258 -3.960 9.398 -10.246 1.00 61.58 C ANISOU 4437 CD2 TRP B 258 7170 9144 7086 406 474 -573 C ATOM 4438 NE1 TRP B 258 -2.016 8.350 -9.847 1.00 76.14 N ANISOU 4438 NE1 TRP B 258 9153 10925 8850 312 414 -549 N ATOM 4439 CE2 TRP B 258 -3.305 8.477 -9.398 1.00 70.38 C ANISOU 4439 CE2 TRP B 258 8354 10275 8114 341 484 -566 C ATOM 4440 CE3 TRP B 258 -5.300 9.712 -9.994 1.00 62.80 C ANISOU 4440 CE3 TRP B 258 7233 9370 7256 453 537 -595 C ATOM 4441 CZ2 TRP B 258 -3.947 7.864 -8.316 1.00 75.85 C ANISOU 4441 CZ2 TRP B 258 9034 11056 8730 319 561 -568 C ATOM 4442 CZ3 TRP B 258 -5.940 9.105 -8.915 1.00 75.63 C ANISOU 4442 CZ3 TRP B 258 8840 11084 8813 425 617 -610 C ATOM 4443 CH2 TRP B 258 -5.262 8.187 -8.092 1.00 82.66 C ANISOU 4443 CH2 TRP B 258 9807 11990 9610 358 632 -589 C ATOM 4444 N ARG B 259 -3.749 12.922 -9.641 1.00 63.87 N ANISOU 4444 N ARG B 259 7480 9259 7530 624 496 -742 N ATOM 4445 CA ARG B 259 -4.770 13.142 -8.624 1.00 73.11 C ANISOU 4445 CA ARG B 259 8604 10510 8662 669 574 -814 C ATOM 4446 C ARG B 259 -5.347 14.555 -8.665 1.00 86.93 C ANISOU 4446 C ARG B 259 10307 12200 10522 780 602 -875 C ATOM 4447 O ARG B 259 -4.708 15.493 -9.153 1.00 94.03 O ANISOU 4447 O ARG B 259 11233 12970 11525 820 567 -883 O ATOM 4448 CB ARG B 259 -4.205 12.841 -7.236 1.00 72.76 C ANISOU 4448 CB ARG B 259 8633 10509 8502 640 599 -891 C ATOM 4449 CG ARG B 259 -3.743 11.409 -7.087 1.00 79.25 C ANISOU 4449 CG ARG B 259 9498 11392 9221 543 583 -817 C ATOM 4450 CD ARG B 259 -3.078 11.146 -5.748 1.00 81.13 C ANISOU 4450 CD ARG B 259 9814 11679 9332 530 596 -877 C ATOM 4451 NE ARG B 259 -2.399 9.859 -5.787 1.00 88.01 N ANISOU 4451 NE ARG B 259 10735 12570 10134 446 564 -790 N ATOM 4452 CZ ARG B 259 -1.215 9.667 -6.358 1.00 93.40 C ANISOU 4452 CZ ARG B 259 11471 13169 10847 407 482 -764 C ATOM 4453 NH1 ARG B 259 -0.576 10.685 -6.922 1.00 88.84 N ANISOU 4453 NH1 ARG B 259 10903 12484 10368 439 430 -812 N ATOM 4454 NH2 ARG B 259 -0.668 8.459 -6.363 1.00100.45 N ANISOU 4454 NH2 ARG B 259 12402 14080 11684 339 459 -686 N ATOM 4455 OXT ARG B 259 -6.467 14.787 -8.201 1.00 85.23 O ANISOU 4455 OXT ARG B 259 10020 12057 10305 833 668 -916 O TER 4456 ARG B 259 HETATM 4457 C TRS B 260 11.898 1.666 -17.985 1.00 74.78 C HETATM 4458 C1 TRS B 260 11.292 3.076 -17.931 1.00 88.90 C HETATM 4459 C2 TRS B 260 12.627 1.513 -19.312 1.00 71.54 C HETATM 4460 C3 TRS B 260 10.924 0.504 -17.749 1.00 81.60 C HETATM 4461 N TRS B 260 12.851 1.543 -16.890 1.00 72.25 N HETATM 4462 O1 TRS B 260 11.282 3.644 -16.637 1.00 92.56 O HETATM 4463 O2 TRS B 260 12.052 2.330 -20.303 1.00 67.41 O HETATM 4464 O3 TRS B 260 10.829 0.150 -16.374 1.00 69.96 O HETATM 4465 O HOH A 331 42.052 -19.542 0.836 1.00 61.27 O HETATM 4466 O HOH A 332 59.676 -6.244 -7.029 1.00 63.68 O HETATM 4467 O HOH A 333 41.851 -17.269 -5.989 1.00 47.71 O HETATM 4468 O HOH A 334 53.214 -8.452 -9.576 1.00 61.90 O HETATM 4469 O HOH A 335 48.924 -1.543 2.892 1.00 61.06 O HETATM 4470 O HOH A 336 48.219 -5.216 -7.390 1.00 53.37 O HETATM 4471 O HOH A 337 57.943 -2.371 -20.677 1.00 56.74 O HETATM 4472 O HOH A 338 43.788 -18.085 -14.312 1.00 66.21 O HETATM 4473 O HOH A 339 23.567 -22.198 -24.411 1.00 59.32 O HETATM 4474 O HOH A 340 46.186 -4.388 -23.953 1.00 56.81 O HETATM 4475 O HOH A 341 48.210 -14.805 -10.804 1.00 44.05 O HETATM 4476 O HOH A 342 57.150 -4.244 12.272 1.00 56.06 O HETATM 4477 O HOH A 343 53.311 -5.736 11.352 1.00 53.65 O HETATM 4478 O HOH A 344 45.262 -14.171 -10.855 1.00 43.77 O HETATM 4479 O HOH A 345 41.223 -10.105 7.583 1.00 53.20 O HETATM 4480 O HOH A 346 37.857 -15.374 -9.623 1.00 63.19 O HETATM 4481 O HOH A 347 52.048 -5.606 -7.606 1.00 57.64 O HETATM 4482 O HOH A 348 32.609 -12.274 -7.587 1.00 35.64 O HETATM 4483 O HOH A 349 59.864 -5.370 1.470 1.00 77.98 O HETATM 4484 O HOH A 350 63.618 -0.464 -27.806 1.00 61.77 O HETATM 4485 O HOH A 351 50.452 -0.688 -1.675 1.00 53.47 O HETATM 4486 O HOH A 352 56.360 -14.412 -29.461 1.00 70.36 O HETATM 4487 O HOH A 353 36.201 -6.091 4.933 1.00 72.23 O HETATM 4488 O HOH A 354 57.295 -4.744 -6.637 1.00 73.03 O HETATM 4489 O HOH A 355 31.510 -16.319 -8.541 1.00 70.64 O HETATM 4490 O HOH A 356 54.556 -3.246 -15.032 1.00 70.01 O HETATM 4491 O HOH A 357 53.872 -2.066 -17.419 1.00 71.79 O HETATM 4492 O HOH A 358 62.643 -19.414 15.468 1.00 69.04 O HETATM 4493 O HOH A 359 41.391 -7.139 9.425 1.00 63.29 O HETATM 4494 O HOH A 360 48.647 -3.845 -31.313 1.00 60.00 O HETATM 4495 O HOH A 361 50.688 -4.724 -29.553 1.00 66.16 O HETATM 4496 O HOH A 362 44.684 -40.111 11.135 1.00 77.16 O HETATM 4497 O HOH A 363 62.867 -17.728 -15.388 1.00 78.43 O HETATM 4498 O HOH A 364 25.667 -18.542 -19.911 1.00 42.91 O HETATM 4499 O HOH A 365 25.237 -20.276 -17.969 1.00 56.61 O HETATM 4500 O HOH A 366 42.729 -4.812 -23.079 1.00 54.94 O HETATM 4501 O HOH A 367 46.367 -6.662 -10.379 1.00 56.64 O HETATM 4502 O HOH A 368 40.978 -10.663 15.414 1.00 64.69 O HETATM 4503 O HOH A 369 44.158 -23.654 18.556 1.00 78.79 O HETATM 4504 O HOH A 370 53.747 -31.792 10.174 1.00 78.98 O HETATM 4505 O HOH A 371 53.807 -25.998 -0.111 1.00 83.53 O HETATM 4506 O HOH A 372 37.096 4.595 -33.829 1.00 69.22 O HETATM 4507 O HOH A 373 36.272 5.925 -36.371 1.00 81.40 O HETATM 4508 O HOH A 374 64.715 -19.929 10.926 1.00 85.82 O HETATM 4509 O HOH A 375 44.764 -18.726 -30.592 1.00 78.13 O HETATM 4510 O HOH A 376 51.053 -9.618 20.577 1.00 64.72 O HETATM 4511 O HOH A 377 54.926 -14.908 -12.731 1.00 64.25 O HETATM 4512 O HOH A 378 56.058 -4.732 0.813 1.00 64.29 O HETATM 4513 O HOH A 379 36.758 -3.420 -15.007 1.00 60.06 O HETATM 4514 O HOH A 380 51.331 -14.351 -11.811 1.00 73.12 O HETATM 4515 O HOH A 381 39.502 -12.230 8.692 1.00 61.03 O HETATM 4516 O HOH A 382 39.930 -14.230 10.541 1.00 62.69 O HETATM 4517 O HOH A 383 36.632 -1.789 -3.100 1.00 53.77 O HETATM 4518 O HOH A 384 34.469 -6.044 -4.460 1.00 65.11 O HETATM 4519 O HOH B 261 24.490 -14.266 -19.708 1.00 42.25 O HETATM 4520 O HOH B 262 17.225 21.002 -6.416 1.00 58.34 O HETATM 4521 O HOH B 263 31.447 6.228 -20.098 1.00 42.78 O HETATM 4522 O HOH B 264 39.607 -1.403 -28.162 1.00 61.15 O HETATM 4523 O HOH B 265 34.123 0.134 -20.823 1.00 53.84 O HETATM 4524 O HOH B 266 29.405 6.989 -16.837 1.00 54.83 O HETATM 4525 O HOH B 267 18.719 -18.659 -15.310 1.00 59.81 O HETATM 4526 O HOH B 268 7.999 -10.906 -37.100 1.00 60.18 O HETATM 4527 O HOH B 269 29.952 -3.894 -13.786 1.00 46.91 O HETATM 4528 O HOH B 270 33.066 -0.160 -36.599 1.00 50.65 O HETATM 4529 O HOH B 271 6.559 11.587 -22.084 1.00 48.93 O HETATM 4530 O HOH B 272 32.897 -14.704 -26.546 1.00 50.80 O HETATM 4531 O HOH B 273 18.699 -3.579 -10.336 1.00 46.89 O HETATM 4532 O HOH B 274 31.231 14.824 -14.636 1.00 56.72 O HETATM 4533 O HOH B 275 28.907 5.938 -33.479 1.00 52.42 O HETATM 4534 O HOH B 276 14.196 2.157 -13.462 1.00 61.13 O HETATM 4535 O HOH B 277 2.992 15.318 -11.755 1.00 46.51 O HETATM 4536 O HOH B 278 21.347 0.402 -12.094 1.00 60.06 O HETATM 4537 O HOH B 279 7.233 19.107 -18.780 1.00 49.41 O HETATM 4538 O HOH B 280 13.222 -0.504 -13.652 1.00 44.64 O HETATM 4539 O HOH B 281 21.443 -7.566 -10.358 1.00 54.16 O HETATM 4540 O HOH B 282 19.342 -0.596 -10.182 1.00 58.57 O HETATM 4541 O HOH B 283 0.104 8.931 -14.214 1.00 55.69 O HETATM 4542 O HOH B 284 33.178 19.835 -27.454 1.00 68.60 O HETATM 4543 O HOH B 285 22.763 -19.715 -16.729 1.00 55.03 O HETATM 4544 O HOH B 286 7.350 -6.632 -24.696 1.00 55.24 O HETATM 4545 O HOH B 287 32.091 -10.830 -12.627 1.00 62.33 O HETATM 4546 O HOH B 288 17.261 11.614 -32.266 1.00 67.50 O HETATM 4547 O HOH B 289 6.601 12.323 -8.905 1.00 75.61 O HETATM 4548 O HOH B 290 16.215 23.830 -15.977 1.00 73.40 O HETATM 4549 O HOH B 291 14.270 21.716 -16.354 1.00 62.21 O HETATM 4550 O HOH B 292 11.356 22.010 -14.966 1.00 61.51 O HETATM 4551 O HOH B 293 29.022 4.467 -16.188 1.00 55.00 O HETATM 4552 O HOH B 294 7.591 -11.748 -29.155 1.00 55.45 O HETATM 4553 O HOH B 295 14.529 -16.671 -16.582 1.00 46.53 O HETATM 4554 O HOH B 296 0.296 16.866 -11.508 1.00 58.76 O HETATM 4555 O HOH B 297 18.670 -14.183 -32.295 1.00 65.02 O HETATM 4556 O HOH B 298 4.427 15.442 -9.313 1.00 62.18 O HETATM 4557 O HOH B 299 30.791 -12.912 -11.884 1.00 76.14 O HETATM 4558 O HOH B 300 21.137 -7.570 -37.002 1.00 63.89 O HETATM 4559 O HOH B 301 -3.346 15.926 -11.386 1.00 57.30 O HETATM 4560 O HOH B 302 17.023 17.200 -25.101 1.00 59.95 O HETATM 4561 O HOH B 303 13.773 -16.616 -14.043 1.00 54.00 O HETATM 4562 O HOH B 304 15.722 16.544 -27.407 1.00 69.81 O HETATM 4563 O HOH B 305 21.510 -16.727 -13.586 1.00 58.27 O HETATM 4564 O HOH B 306 22.232 13.213 -25.351 1.00 61.86 O HETATM 4565 O HOH B 307 21.295 -12.476 -31.620 1.00 60.27 O HETATM 4566 O HOH B 308 3.891 10.754 -21.148 1.00 38.43 O HETATM 4567 O HOH B 309 9.370 -6.954 -22.129 1.00 40.99 O HETATM 4568 O HOH B 310 23.044 8.341 -18.284 1.00 43.61 O HETATM 4569 O HOH B 311 21.346 -0.136 -35.933 1.00 59.39 O HETATM 4570 O HOH B 312 19.322 -5.756 -37.872 1.00 91.68 O HETATM 4571 O HOH B 313 25.906 4.744 -15.878 1.00 46.91 O HETATM 4572 O HOH B 314 15.326 21.403 -4.785 1.00 68.12 O HETATM 4573 O HOH B 315 32.187 -9.695 -37.298 1.00 72.56 O HETATM 4574 O HOH B 316 24.944 7.325 -16.497 1.00 47.32 O HETATM 4575 O HOH B 317 23.419 7.866 -20.846 1.00 43.43 O HETATM 4576 O HOH B 318 19.897 -2.475 -35.590 1.00 52.55 O HETATM 4577 O HOH B 319 21.946 0.219 -38.584 1.00 74.84 O HETATM 4578 O HOH B 320 39.027 0.421 -20.952 1.00 58.77 O HETATM 4579 O HOH B 321 36.995 6.441 -18.458 1.00 55.77 O HETATM 4580 O HOH B 322 16.933 -14.049 -13.529 1.00 62.01 O HETATM 4581 O HOH B 323 7.052 5.046 -22.213 1.00 62.21 O HETATM 4582 O HOH B 324 20.655 7.182 -25.199 1.00 49.95 O HETATM 4583 O HOH B 325 33.165 5.684 -14.301 1.00 70.06 O HETATM 4584 O HOH B 326 31.588 3.465 -15.003 1.00 64.46 O HETATM 4585 O HOH B 327 33.760 1.991 -16.208 1.00 55.13 O HETATM 4586 O HOH B 328 20.503 -10.458 -33.207 1.00 56.53 O HETATM 4587 O HOH B 329 18.041 -9.340 -36.628 1.00 78.29 O HETATM 4588 O HOH B 330 23.828 27.762 -5.500 1.00 84.46 O HETATM 4589 O HOH B 331 42.728 6.289 -23.187 1.00 63.15 O HETATM 4590 O HOH B 332 28.301 -4.541 -10.375 1.00 72.23 O HETATM 4591 O HOH B 333 34.978 4.662 -16.280 1.00 63.23 O HETATM 4592 O HOH B 334 17.165 -7.170 -37.334 1.00 66.97 O HETATM 4593 O HOH B 335 35.617 8.780 -34.009 1.00 60.03 O HETATM 4594 O HOH B 336 27.286 -2.082 -11.778 1.00 67.88 O HETATM 4595 O HOH B 337 26.359 -4.679 -7.644 1.00 81.40 O HETATM 4596 O HOH B 338 -1.425 17.692 -9.248 1.00 69.00 O HETATM 4597 O HOH B 339 11.595 0.883 -22.452 1.00 60.34 O HETATM 4598 O HOH B 340 9.551 -2.520 -22.159 1.00 65.65 O HETATM 4599 O HOH B 341 9.006 -1.181 -15.274 1.00 75.09 O HETATM 4600 O HOH B 342 11.097 -1.256 -23.709 1.00 73.43 O HETATM 4601 O HOH B 343 7.807 -4.669 -22.683 1.00 60.40 O HETATM 4602 O HOH B 344 7.954 -9.188 -29.767 1.00 63.18 O HETATM 4603 O HOH B 345 36.827 -4.174 -11.011 1.00 47.54 O CONECT 1275 1285 CONECT 1285 1275 1286 CONECT 1286 1285 1287 1294 CONECT 1287 1286 1288 1289 CONECT 1288 1287 CONECT 1289 1287 1290 CONECT 1290 1289 1291 1292 1293 CONECT 1291 1290 CONECT 1292 1290 CONECT 1293 1290 CONECT 1294 1286 1295 1296 CONECT 1295 1294 CONECT 1296 1294 CONECT 4457 4458 4459 4460 4461 CONECT 4458 4457 4462 CONECT 4459 4457 4463 CONECT 4460 4457 4464 CONECT 4461 4457 CONECT 4462 4458 CONECT 4463 4459 CONECT 4464 4460 MASTER 477 0 2 27 10 0 3 6 4601 2 21 46 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3blh
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Cell division protein kinase 9, CDK9
Ligand Name
CycT1
EC.Number
E.C.2.7.11.22
Resolution
2.48(Å)
Affinity (Kd/Ki/IC50)
Kd=300nM
Release Year
2008
Protein/NA Sequence
Check fasta file
Primary Reference
(2008) Embo J. Vol. 27: pp. 1907-1918
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
O60563
P50750
Entrez Gene ID
NCBI Entrez Gene ID:
904
1025
ASD
Information of known allosteric effects of PDB entries
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