Browse entries in the PDBbind-CN Database
HEADER DNA BINDING PROTEIN/DNA 04-FEB-14 4OWX TITLE STRUCTURAL BASIS OF SOSS1 IN COMPLEX WITH A 12NT SSDNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'); COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: INTEGRATOR COMPLEX SUBUNIT 3; COMPND 7 CHAIN: A; COMPND 8 SYNONYM: INT3,SOSS COMPLEX SUBUNIT A,SENSOR OF SINGLE-STRAND DNA COMPND 9 COMPLEX SUBUNIT A,SENSOR OF SSDNA SUBUNIT A; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: SOSS COMPLEX SUBUNIT B1; COMPND 13 CHAIN: B; COMPND 14 SYNONYM: NUCLEIC ACID-BINDING PROTEIN 2, COMPND 15 OLIGONUCLEOTIDE/OLIGOSACCHARIDE-BINDING FOLD-CONTAINING PROTEIN 2B, COMPND 16 SENSOR OF SINGLE-STRAND DNA COMPLEX SUBUNIT B1,SENSOR OF SSDNA COMPND 17 SUBUNIT B1,SOSS-B1,SINGLE-STRANDED DNA-BINDING PROTEIN 1,HSSB1; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_COMMON: HUMAN; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 GENE: INTS3, C1ORF193, C1ORF60; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: NABP2, OBFC2B, SSB1, LP3587; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SOSS1 COMPLEX, DNA DOUBLE-STRAND BREAKS, HOMOLOGOUS RECOMBINATION, KEYWDS 2 SSDNA- BINDING PROTEIN, DNA BINDING PROTEIN-DNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.REN,Q.SUN,X.TANG,H.SONG REVDAT 4 08-JAN-20 4OWX 1 REMARK REVDAT 3 06-SEP-17 4OWX 1 SOURCE REMARK REVDAT 2 03-DEC-14 4OWX 1 DBREF REVDAT 1 16-APR-14 4OWX 0 JRNL AUTH W.REN,H.CHEN,Q.SUN,X.TANG,S.C.LIM,J.HUANG,H.SONG JRNL TITL STRUCTURAL BASIS OF SOSS1 COMPLEX ASSEMBLY AND RECOGNITION JRNL TITL 2 OF SSDNA. JRNL REF CELL REP V. 6 982 2014 JRNL REFN ESSN 2211-1247 JRNL PMID 24630995 JRNL DOI 10.1016/J.CELREP.2014.02.020 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.81 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 47686 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 2413 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 41.8141 - 5.9087 0.97 2779 156 0.1838 0.2294 REMARK 3 2 5.9087 - 4.6920 1.00 2719 142 0.1763 0.2160 REMARK 3 3 4.6920 - 4.0995 1.00 2707 139 0.1487 0.1682 REMARK 3 4 4.0995 - 3.7249 1.00 2692 139 0.1564 0.1913 REMARK 3 5 3.7249 - 3.4581 1.00 2669 142 0.1727 0.2119 REMARK 3 6 3.4581 - 3.2543 1.00 2682 139 0.1824 0.2282 REMARK 3 7 3.2543 - 3.0913 1.00 2636 153 0.1914 0.2847 REMARK 3 8 3.0913 - 2.9568 1.00 2673 138 0.1955 0.2519 REMARK 3 9 2.9568 - 2.8430 1.00 2641 132 0.1901 0.2530 REMARK 3 10 2.8430 - 2.7449 1.00 2652 129 0.2012 0.2936 REMARK 3 11 2.7449 - 2.6591 1.00 2648 125 0.1975 0.2140 REMARK 3 12 2.6591 - 2.5831 1.00 2628 146 0.2052 0.2490 REMARK 3 13 2.5831 - 2.5151 1.00 2634 150 0.2162 0.2655 REMARK 3 14 2.5151 - 2.4538 1.00 2648 135 0.2367 0.2613 REMARK 3 15 2.4538 - 2.3980 1.00 2617 146 0.2472 0.3109 REMARK 3 16 2.3980 - 2.3470 1.00 2603 145 0.2622 0.3063 REMARK 3 17 2.3470 - 2.3000 1.00 2645 157 0.2749 0.3041 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.400 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 4840 REMARK 3 ANGLE : 1.119 6584 REMARK 3 CHIRALITY : 0.075 763 REMARK 3 PLANARITY : 0.004 802 REMARK 3 DIHEDRAL : 16.533 1833 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 13 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.1656 53.6205 33.0646 REMARK 3 T TENSOR REMARK 3 T11: 0.4325 T22: 0.8122 REMARK 3 T33: 0.5822 T12: 0.0331 REMARK 3 T13: 0.0393 T23: 0.1137 REMARK 3 L TENSOR REMARK 3 L11: 6.2363 L22: 9.9208 REMARK 3 L33: 8.2657 L12: 0.2996 REMARK 3 L13: -1.7609 L23: -1.8073 REMARK 3 S TENSOR REMARK 3 S11: -0.1656 S12: 0.5414 S13: -0.3164 REMARK 3 S21: -0.6182 S22: 0.4529 S23: -0.0462 REMARK 3 S31: -0.3827 S32: -1.5334 S33: -0.2994 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3044 47.6782 3.6130 REMARK 3 T TENSOR REMARK 3 T11: 0.6712 T22: 0.5398 REMARK 3 T33: 0.4088 T12: 0.0187 REMARK 3 T13: -0.0282 T23: 0.0708 REMARK 3 L TENSOR REMARK 3 L11: 5.1891 L22: 1.9810 REMARK 3 L33: 3.3357 L12: 1.1552 REMARK 3 L13: -1.6974 L23: -2.8038 REMARK 3 S TENSOR REMARK 3 S11: 0.1601 S12: 0.6876 S13: 0.4595 REMARK 3 S21: -0.2296 S22: -0.1395 S23: -0.2099 REMARK 3 S31: -0.7716 S32: 0.2098 S33: -0.0209 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 83 THROUGH 297 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8886 21.0040 11.8700 REMARK 3 T TENSOR REMARK 3 T11: 0.3700 T22: 0.3545 REMARK 3 T33: 0.3427 T12: 0.0007 REMARK 3 T13: 0.0211 T23: -0.0389 REMARK 3 L TENSOR REMARK 3 L11: 2.5050 L22: 5.5848 REMARK 3 L33: 2.7454 L12: -1.5749 REMARK 3 L13: 0.3613 L23: -0.8080 REMARK 3 S TENSOR REMARK 3 S11: 0.2461 S12: 0.3465 S13: -0.4092 REMARK 3 S21: -0.8610 S22: -0.2484 S23: -0.2554 REMARK 3 S31: 0.1684 S32: 0.2252 S33: 0.0098 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 497 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.3108 16.5975 41.4271 REMARK 3 T TENSOR REMARK 3 T11: 0.4172 T22: 0.5020 REMARK 3 T33: 0.5123 T12: -0.0120 REMARK 3 T13: -0.0731 T23: 0.2975 REMARK 3 L TENSOR REMARK 3 L11: 4.5080 L22: 3.7834 REMARK 3 L33: 2.9087 L12: -0.4682 REMARK 3 L13: 0.3325 L23: 0.5131 REMARK 3 S TENSOR REMARK 3 S11: -0.0006 S12: -0.9308 S13: -0.8969 REMARK 3 S21: 0.7083 S22: 0.1255 S23: -0.2353 REMARK 3 S31: 0.5417 S32: -0.0919 S33: -0.0637 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1313 54.2483 43.3174 REMARK 3 T TENSOR REMARK 3 T11: 0.6021 T22: 0.6325 REMARK 3 T33: 0.5993 T12: 0.0145 REMARK 3 T13: -0.0330 T23: -0.0966 REMARK 3 L TENSOR REMARK 3 L11: 2.2085 L22: 3.5141 REMARK 3 L33: 3.5403 L12: 0.0769 REMARK 3 L13: -0.8725 L23: 3.2568 REMARK 3 S TENSOR REMARK 3 S11: 0.2495 S12: -1.0286 S13: 1.1180 REMARK 3 S21: 0.2775 S22: 0.0934 S23: -0.5461 REMARK 3 S31: -1.1794 S32: 0.4228 S33: -0.3855 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 18 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.7344 59.3225 40.3458 REMARK 3 T TENSOR REMARK 3 T11: 0.5310 T22: 0.4431 REMARK 3 T33: 0.4560 T12: -0.0388 REMARK 3 T13: 0.0341 T23: -0.1790 REMARK 3 L TENSOR REMARK 3 L11: 9.2199 L22: 7.9994 REMARK 3 L33: 4.1140 L12: -3.2374 REMARK 3 L13: -0.7190 L23: 2.9947 REMARK 3 S TENSOR REMARK 3 S11: -0.3059 S12: -1.0637 S13: 0.8598 REMARK 3 S21: 0.2674 S22: 0.2813 S23: 0.0288 REMARK 3 S31: -0.7684 S32: 0.4094 S33: -0.1007 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 26 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.1392 43.1677 37.6822 REMARK 3 T TENSOR REMARK 3 T11: 0.3348 T22: 0.5337 REMARK 3 T33: 0.2706 T12: 0.0093 REMARK 3 T13: 0.0584 T23: 0.0433 REMARK 3 L TENSOR REMARK 3 L11: 8.0266 L22: 2.0433 REMARK 3 L33: 2.8575 L12: -0.5704 REMARK 3 L13: 4.1993 L23: 0.6790 REMARK 3 S TENSOR REMARK 3 S11: 0.1002 S12: -1.2010 S13: -0.5557 REMARK 3 S21: 0.6778 S22: -0.0332 S23: 0.1080 REMARK 3 S31: 0.0577 S32: 0.0461 S33: -0.3590 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 31 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.7771 39.7618 37.2940 REMARK 3 T TENSOR REMARK 3 T11: 0.3999 T22: 0.7791 REMARK 3 T33: 1.1300 T12: -0.1292 REMARK 3 T13: -0.0441 T23: 0.3855 REMARK 3 L TENSOR REMARK 3 L11: 5.3011 L22: 4.7535 REMARK 3 L33: 9.0379 L12: -0.5850 REMARK 3 L13: 2.8214 L23: 2.6759 REMARK 3 S TENSOR REMARK 3 S11: 0.2729 S12: -1.3021 S13: -1.8902 REMARK 3 S21: 0.6813 S22: 0.9959 S23: 1.2093 REMARK 3 S31: 0.6814 S32: -0.7861 S33: -0.7422 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 55 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.3777 46.0396 38.1433 REMARK 3 T TENSOR REMARK 3 T11: 0.2878 T22: 0.5142 REMARK 3 T33: 0.4539 T12: 0.0381 REMARK 3 T13: 0.0709 T23: 0.0685 REMARK 3 L TENSOR REMARK 3 L11: 5.2250 L22: 2.3262 REMARK 3 L33: 4.4045 L12: -1.6592 REMARK 3 L13: 3.7281 L23: -1.6665 REMARK 3 S TENSOR REMARK 3 S11: -0.4704 S12: -0.6853 S13: -0.1132 REMARK 3 S21: 0.1875 S22: 0.5119 S23: 0.4204 REMARK 3 S31: -0.3162 S32: -0.3871 S33: -0.4919 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 56 THROUGH 61 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3746 42.5486 27.9816 REMARK 3 T TENSOR REMARK 3 T11: 0.4216 T22: 0.5753 REMARK 3 T33: 0.6094 T12: -0.0413 REMARK 3 T13: -0.1166 T23: 0.0249 REMARK 3 L TENSOR REMARK 3 L11: 5.2031 L22: 2.8589 REMARK 3 L33: 7.2153 L12: -3.8214 REMARK 3 L13: -6.0981 L23: 4.5409 REMARK 3 S TENSOR REMARK 3 S11: -0.0526 S12: 0.6779 S13: -0.5931 REMARK 3 S21: -0.2604 S22: 0.0608 S23: 1.3626 REMARK 3 S31: 0.3270 S32: -1.4488 S33: -0.1339 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 86 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.8868 49.6741 37.7697 REMARK 3 T TENSOR REMARK 3 T11: 0.2632 T22: 0.4927 REMARK 3 T33: 0.2558 T12: 0.0421 REMARK 3 T13: -0.0007 T23: -0.0025 REMARK 3 L TENSOR REMARK 3 L11: 4.6296 L22: 5.4053 REMARK 3 L33: 2.8128 L12: -1.1037 REMARK 3 L13: -0.7912 L23: 0.0099 REMARK 3 S TENSOR REMARK 3 S11: -0.0817 S12: -0.4139 S13: 0.1421 REMARK 3 S21: 0.3830 S22: 0.1797 S23: 0.2779 REMARK 3 S31: -0.2265 S32: -0.3465 S33: 0.0238 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.9493 49.3311 28.4523 REMARK 3 T TENSOR REMARK 3 T11: 0.2707 T22: 0.4261 REMARK 3 T33: 0.3545 T12: 0.0251 REMARK 3 T13: 0.0057 T23: 0.0732 REMARK 3 L TENSOR REMARK 3 L11: 2.6230 L22: 2.4400 REMARK 3 L33: 3.9818 L12: 1.2637 REMARK 3 L13: -1.6660 L23: 1.4877 REMARK 3 S TENSOR REMARK 3 S11: 0.3022 S12: 1.0577 S13: 0.5292 REMARK 3 S21: -1.0634 S22: -0.2761 S23: 0.0416 REMARK 3 S31: -0.3094 S32: 0.1983 S33: 0.0471 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 98 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.5041 43.2302 45.1798 REMARK 3 T TENSOR REMARK 3 T11: 0.4327 T22: 0.8499 REMARK 3 T33: 0.2873 T12: 0.1115 REMARK 3 T13: -0.0048 T23: 0.0325 REMARK 3 L TENSOR REMARK 3 L11: 2.5360 L22: 1.9375 REMARK 3 L33: 0.9681 L12: -0.6599 REMARK 3 L13: -0.0854 L23: 0.4173 REMARK 3 S TENSOR REMARK 3 S11: -0.2519 S12: -0.9146 S13: 0.1512 REMARK 3 S21: 0.5221 S22: 0.3642 S23: 0.1812 REMARK 3 S31: -0.1830 S32: -0.1466 S33: 0.0619 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 4OWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-14. REMARK 100 THE DEPOSITION ID IS D_1000200164. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47747 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 41.810 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.780 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG3350, 0.1M MES PH6.0, 0.1M REMARK 280 AMMONIUM FORMATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 49.31500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.26000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.31500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.26000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, 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 DT L 10 REMARK 465 DT L 11 REMARK 465 DT L 12 REMARK 465 MET A 1 REMARK 465 GLU A 2 REMARK 465 LEU A 3 REMARK 465 GLN A 4 REMARK 465 LYS A 5 REMARK 465 GLY A 6 REMARK 465 LYS A 7 REMARK 465 GLY A 8 REMARK 465 ALA A 9 REMARK 465 ALA A 10 REMARK 465 ALA A 11 REMARK 465 ALA A 12 REMARK 465 ALA A 13 REMARK 465 ALA A 14 REMARK 465 ALA A 15 REMARK 465 SER A 16 REMARK 465 GLY A 17 REMARK 465 ALA A 18 REMARK 465 ALA A 19 REMARK 465 GLY A 20 REMARK 465 GLY A 21 REMARK 465 GLY A 22 REMARK 465 GLY A 23 REMARK 465 GLY A 24 REMARK 465 GLY A 25 REMARK 465 ALA A 26 REMARK 465 GLY A 27 REMARK 465 ALA A 28 REMARK 465 GLY A 29 REMARK 465 ALA A 30 REMARK 465 PRO A 31 REMARK 465 GLY A 32 REMARK 465 GLY A 33 REMARK 465 SER A 498 REMARK 465 SER A 499 REMARK 465 PRO A 500 REMARK 465 MET B 1 REMARK 465 THR B 2 REMARK 465 THR B 3 REMARK 465 GLU B 4 REMARK 465 ASN B 112 REMARK 465 PRO B 113 REMARK 465 GLU B 114 REMARK 465 TYR B 115 REMARK 465 SER B 116 REMARK 465 THR B 117 REMARK 465 GLN B 118 REMARK 465 GLN B 119 REMARK 465 ALA B 120 REMARK 465 PRO B 121 REMARK 465 ASN B 122 REMARK 465 LYS B 123 REMARK 465 ALA B 124 REMARK 465 VAL B 125 REMARK 465 GLN B 126 REMARK 465 ASN B 127 REMARK 465 ASP B 128 REMARK 465 SER B 129 REMARK 465 ASN B 130 REMARK 465 PRO B 131 REMARK 465 SER B 132 REMARK 465 ALA B 133 REMARK 465 SER B 134 REMARK 465 GLN B 135 REMARK 465 PRO B 136 REMARK 465 THR B 137 REMARK 465 THR B 138 REMARK 465 GLY B 139 REMARK 465 PRO B 140 REMARK 465 SER B 141 REMARK 465 ALA B 142 REMARK 465 ALA B 143 REMARK 465 SER B 144 REMARK 465 PRO B 145 REMARK 465 ALA B 146 REMARK 465 SER B 147 REMARK 465 GLU B 148 REMARK 465 ASN B 149 REMARK 465 GLN B 150 REMARK 465 ASN B 151 REMARK 465 GLY B 152 REMARK 465 ASN B 153 REMARK 465 GLY B 154 REMARK 465 LEU B 155 REMARK 465 SER B 156 REMARK 465 ALA B 157 REMARK 465 PRO B 158 REMARK 465 PRO B 159 REMARK 465 GLY B 160 REMARK 465 PRO B 161 REMARK 465 GLY B 162 REMARK 465 GLY B 163 REMARK 465 GLY B 164 REMARK 465 PRO B 165 REMARK 465 HIS B 166 REMARK 465 PRO B 167 REMARK 465 PRO B 168 REMARK 465 HIS B 169 REMARK 465 THR B 170 REMARK 465 PRO B 171 REMARK 465 SER B 172 REMARK 465 HIS B 173 REMARK 465 PRO B 174 REMARK 465 PRO B 175 REMARK 465 SER B 176 REMARK 465 THR B 177 REMARK 465 ARG B 178 REMARK 465 ILE B 179 REMARK 465 THR B 180 REMARK 465 ARG B 181 REMARK 465 SER B 182 REMARK 465 GLN B 183 REMARK 465 PRO B 184 REMARK 465 ASN B 185 REMARK 465 HIS B 186 REMARK 465 THR B 187 REMARK 465 PRO B 188 REMARK 465 ALA B 189 REMARK 465 GLY B 190 REMARK 465 PRO B 191 REMARK 465 PRO B 192 REMARK 465 GLY B 193 REMARK 465 PRO B 194 REMARK 465 SER B 195 REMARK 465 SER B 196 REMARK 465 ASN B 197 REMARK 465 PRO B 198 REMARK 465 VAL B 199 REMARK 465 SER B 200 REMARK 465 ASN B 201 REMARK 465 GLY B 202 REMARK 465 LYS B 203 REMARK 465 GLU B 204 REMARK 465 THR B 205 REMARK 465 ARG B 206 REMARK 465 ARG B 207 REMARK 465 SER B 208 REMARK 465 SER B 209 REMARK 465 LYS B 210 REMARK 465 ARG B 211 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH L 110 O HOH L 111 1.81 REMARK 500 O HOH A 652 O HOH A 663 1.97 REMARK 500 N3 DT L 8 O HOH L 101 2.00 REMARK 500 O4 DT L 8 O HOH L 102 2.13 REMARK 500 O HOH A 662 O HOH A 683 2.13 REMARK 500 O HOH A 635 O HOH A 663 2.18 REMARK 500 OD1 ASP B 45 O HOH B 327 2.18 REMARK 500 SD MET A 309 O HOH A 684 2.18 REMARK 500 OD2 ASP A 435 NH1 ARG A 439 2.18 REMARK 500 O HOH B 347 O HOH B 356 2.18 REMARK 500 OE1 GLN A 230 O HOH A 664 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 DT L 7 O3' DT L 7 C3' -0.038 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 DT L 2 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES REMARK 500 DT L 2 O4' - C1' - N1 ANGL. DEV. = 5.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 282 140.33 -175.31 REMARK 500 HIS A 426 75.46 -116.52 REMARK 500 TYR A 445 88.09 -154.52 REMARK 500 LEU A 481 -157.09 -102.89 REMARK 500 ARG A 490 6.03 -60.73 REMARK 500 GLU A 495 2.13 -61.11 REMARK 500 ASP B 56 -164.05 68.36 REMARK 500 PHE B 98 -53.09 73.98 REMARK 500 REMARK 500 REMARK: NULL DBREF 4OWX L 1 12 PDB 4OWX 4OWX 1 12 DBREF 4OWX A 1 500 UNP Q68E01 INT3_HUMAN 1 500 DBREF 4OWX B 1 211 UNP Q9BQ15 SOSB1_HUMAN 1 211 SEQRES 1 L 12 DT DT DT DT DT DT DT DT DT DT DT DT SEQRES 1 A 500 MET GLU LEU GLN LYS GLY LYS GLY ALA ALA ALA ALA ALA SEQRES 2 A 500 ALA ALA SER GLY ALA ALA GLY GLY GLY GLY GLY GLY ALA SEQRES 3 A 500 GLY ALA GLY ALA PRO GLY GLY GLY ARG LEU LEU LEU SER SEQRES 4 A 500 THR SER LEU ASP ALA LYS ASP GLU LEU GLU GLU ARG LEU SEQRES 5 A 500 GLU ARG CYS MET SER ILE VAL THR SER MET THR ALA GLY SEQRES 6 A 500 VAL SER GLU ARG GLU ALA ASN ASP ALA LEU ASN ALA TYR SEQRES 7 A 500 VAL CYS LYS GLY LEU PRO GLN HIS GLU GLU ILE CYS LEU SEQRES 8 A 500 GLY LEU PHE THR LEU ILE LEU THR GLU PRO ALA GLN ALA SEQRES 9 A 500 GLN LYS CYS TYR ARG ASP LEU ALA LEU VAL SER ARG ASP SEQRES 10 A 500 GLY MET ASN ILE VAL LEU ASN LYS ILE ASN GLN ILE LEU SEQRES 11 A 500 MET GLU LYS TYR LEU LYS LEU GLN ASP THR CYS ARG THR SEQRES 12 A 500 GLN LEU VAL TRP LEU VAL ARG GLU LEU VAL LYS SER GLY SEQRES 13 A 500 VAL LEU GLY ALA ASP GLY VAL CYS MET THR PHE MET LYS SEQRES 14 A 500 GLN ILE ALA GLY GLY ASP VAL THR ALA LYS ASN ILE TRP SEQRES 15 A 500 LEU ALA GLU SER VAL LEU ASP ILE LEU THR GLU GLN ARG SEQRES 16 A 500 GLU TRP VAL LEU LYS SER SER ILE LEU ILE ALA MET ALA SEQRES 17 A 500 VAL TYR THR TYR LEU ARG LEU ILE VAL ASP HIS HIS GLY SEQRES 18 A 500 THR ALA GLN LEU GLN ALA LEU ARG GLN LYS GLU VAL ASP SEQRES 19 A 500 PHE CYS ILE SER LEU LEU ARG GLU ARG PHE MET GLU CYS SEQRES 20 A 500 LEU MET ILE GLY ARG ASP LEU VAL ARG LEU LEU GLN ASN SEQRES 21 A 500 VAL ALA ARG ILE PRO GLU PHE GLU LEU LEU TRP LYS ASP SEQRES 22 A 500 ILE ILE HIS ASN PRO GLN ALA LEU SER PRO GLN PHE THR SEQRES 23 A 500 GLY ILE LEU GLN LEU LEU GLN SER ARG THR SER ARG LYS SEQRES 24 A 500 PHE LEU ALA CYS ARG LEU THR PRO ASP MET GLU THR LYS SEQRES 25 A 500 LEU LEU PHE MET THR SER ARG VAL ARG PHE GLY GLN GLN SEQRES 26 A 500 LYS ARG TYR GLN ASP TRP PHE GLN ARG GLN TYR LEU SER SEQRES 27 A 500 THR PRO ASP SER GLN SER LEU ARG CYS ASP LEU ILE ARG SEQRES 28 A 500 TYR ILE CYS GLY VAL VAL HIS PRO SER ASN GLU VAL LEU SEQRES 29 A 500 SER SER ASP ILE LEU PRO ARG TRP ALA ILE ILE GLY TRP SEQRES 30 A 500 LEU LEU THR THR CYS THR SER ASN VAL ALA ALA SER ASN SEQRES 31 A 500 ALA LYS LEU ALA LEU PHE TYR ASP TRP LEU PHE PHE SER SEQRES 32 A 500 PRO ASP LYS ASP SER ILE MET ASN ILE GLU PRO ALA ILE SEQRES 33 A 500 LEU VAL MET HIS HIS SER MET LYS PRO HIS PRO ALA ILE SEQRES 34 A 500 THR ALA THR LEU LEU ASP PHE MET CYS ARG ILE ILE PRO SEQRES 35 A 500 ASN PHE TYR PRO PRO LEU GLU GLY HIS VAL ARG GLN GLY SEQRES 36 A 500 VAL PHE SER SER LEU ASN HIS ILE VAL GLU LYS ARG VAL SEQRES 37 A 500 LEU ALA HIS LEU ALA PRO LEU PHE ASP ASN PRO LYS LEU SEQRES 38 A 500 ASP LYS GLU LEU ARG ALA MET LEU ARG GLU LYS PHE PRO SEQRES 39 A 500 GLU PHE CYS SER SER PRO SEQRES 1 B 211 MET THR THR GLU THR PHE VAL LYS ASP ILE LYS PRO GLY SEQRES 2 B 211 LEU LYS ASN LEU ASN LEU ILE PHE ILE VAL LEU GLU THR SEQRES 3 B 211 GLY ARG VAL THR LYS THR LYS ASP GLY HIS GLU VAL ARG SEQRES 4 B 211 THR CYS LYS VAL ALA ASP LYS THR GLY SER ILE ASN ILE SEQRES 5 B 211 SER VAL TRP ASP ASP VAL GLY ASN LEU ILE GLN PRO GLY SEQRES 6 B 211 ASP ILE ILE ARG LEU THR LYS GLY TYR ALA SER VAL PHE SEQRES 7 B 211 LYS GLY CYS LEU THR LEU TYR THR GLY ARG GLY GLY ASP SEQRES 8 B 211 LEU GLN LYS ILE GLY GLU PHE CYS MET VAL TYR SER GLU SEQRES 9 B 211 VAL PRO ASN PHE SER GLU PRO ASN PRO GLU TYR SER THR SEQRES 10 B 211 GLN GLN ALA PRO ASN LYS ALA VAL GLN ASN ASP SER ASN SEQRES 11 B 211 PRO SER ALA SER GLN PRO THR THR GLY PRO SER ALA ALA SEQRES 12 B 211 SER PRO ALA SER GLU ASN GLN ASN GLY ASN GLY LEU SER SEQRES 13 B 211 ALA PRO PRO GLY PRO GLY GLY GLY PRO HIS PRO PRO HIS SEQRES 14 B 211 THR PRO SER HIS PRO PRO SER THR ARG ILE THR ARG SER SEQRES 15 B 211 GLN PRO ASN HIS THR PRO ALA GLY PRO PRO GLY PRO SER SEQRES 16 B 211 SER ASN PRO VAL SER ASN GLY LYS GLU THR ARG ARG SER SEQRES 17 B 211 SER LYS ARG FORMUL 4 HOH *171(H2 O) HELIX 1 AA1 ASP A 46 ALA A 64 1 19 HELIX 2 AA2 SER A 67 LYS A 81 1 15 HELIX 3 AA3 GLY A 82 GLU A 100 1 19 HELIX 4 AA4 GLN A 103 SER A 115 1 13 HELIX 5 AA5 MET A 119 LYS A 133 1 15 HELIX 6 AA6 TYR A 134 LEU A 137 5 4 HELIX 7 AA7 GLN A 138 SER A 155 1 18 HELIX 8 AA8 GLY A 159 LYS A 169 1 11 HELIX 9 AA9 THR A 177 GLN A 194 1 18 HELIX 10 AB1 GLN A 194 LEU A 199 1 6 HELIX 11 AB2 SER A 201 VAL A 217 1 17 HELIX 12 AB3 THR A 222 ARG A 243 1 22 HELIX 13 AB4 ARG A 243 LEU A 248 1 6 HELIX 14 AB5 MET A 249 GLY A 251 5 3 HELIX 15 AB6 ARG A 252 ASN A 260 1 9 HELIX 16 AB7 ILE A 264 ASN A 277 1 14 HELIX 17 AB8 PRO A 278 LEU A 281 5 4 HELIX 18 AB9 GLY A 287 GLN A 293 1 7 HELIX 19 AC1 SER A 297 ARG A 304 1 8 HELIX 20 AC2 THR A 306 THR A 317 1 12 HELIX 21 AC3 GLN A 325 LEU A 337 1 13 HELIX 22 AC4 THR A 339 GLN A 343 5 5 HELIX 23 AC5 SER A 344 VAL A 356 1 13 HELIX 24 AC6 SER A 360 SER A 365 1 6 HELIX 25 AC7 PRO A 370 THR A 381 1 12 HELIX 26 AC8 SER A 384 TYR A 397 1 14 HELIX 27 AC9 SER A 408 ASN A 411 5 4 HELIX 28 AD1 ILE A 412 SER A 422 1 11 HELIX 29 AD2 HIS A 426 PHE A 444 1 19 HELIX 30 AD3 TYR A 445 PRO A 447 5 3 HELIX 31 AD4 LEU A 448 LYS A 466 1 19 HELIX 32 AD5 LEU A 472 PHE A 476 5 5 HELIX 33 AD6 ASP A 482 PHE A 493 1 12 HELIX 34 AD7 PHE B 6 ILE B 10 5 5 HELIX 35 AD8 ASP B 57 ILE B 62 1 6 SHEET 1 AA1 7 THR B 30 LYS B 31 0 SHEET 2 AA1 7 GLU B 37 ASP B 45 -1 O VAL B 38 N THR B 30 SHEET 3 AA1 7 GLY B 48 TRP B 55 -1 O ILE B 52 N CYS B 41 SHEET 4 AA1 7 CYS B 81 GLU B 97 1 O LEU B 84 N ASN B 51 SHEET 5 AA1 7 ASP B 66 PHE B 78 -1 N ILE B 67 O GLY B 96 SHEET 6 AA1 7 LEU B 17 THR B 26 -1 N PHE B 21 O ILE B 68 SHEET 7 AA1 7 GLU B 37 ASP B 45 -1 O LYS B 42 N LEU B 24 CISPEP 1 VAL B 105 PRO B 106 0 -2.47 CRYST1 98.630 162.520 65.740 90.00 90.00 90.00 P 21 21 2 4 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 0.010139 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006153 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015211 0.00000 ATOM 1 P DT L 1 -28.877 56.991 21.253 1.00149.19 P ANISOU 1 P DT L 1 19202 23623 13859 366 -1072 2222 P ATOM 2 OP1 DT L 1 -29.782 56.328 20.285 1.00153.20 O ANISOU 2 OP1 DT L 1 19680 24777 13751 11 -1651 2179 O ATOM 3 OP2 DT L 1 -29.260 57.097 22.681 1.00141.04 O ANISOU 3 OP2 DT L 1 17548 22555 13486 633 -1066 2314 O ATOM 4 O5' DT L 1 -27.427 56.310 21.183 1.00159.40 O ANISOU 4 O5' DT L 1 20929 24261 15376 -33 -467 1719 O ATOM 5 C5' DT L 1 -27.001 55.566 20.040 1.00164.42 C ANISOU 5 C5' DT L 1 22087 24878 15506 -492 -364 1379 C ATOM 6 C4' DT L 1 -25.529 55.193 20.160 1.00162.39 C ANISOU 6 C4' DT L 1 22139 23920 15642 -671 347 1013 C ATOM 7 O4' DT L 1 -25.127 54.265 19.116 1.00167.40 O ANISOU 7 O4' DT L 1 23281 24497 15828 -1132 534 593 O ATOM 8 C3' DT L 1 -24.566 56.374 20.073 1.00160.21 C ANISOU 8 C3' DT L 1 22198 23192 15484 -335 855 1268 C ATOM 9 O3' DT L 1 -23.624 56.273 21.112 1.00154.30 O ANISOU 9 O3' DT L 1 21184 21912 15531 -314 1255 1105 O ATOM 10 C2' DT L 1 -23.863 56.168 18.737 1.00164.18 C ANISOU 10 C2' DT L 1 23407 23560 15415 -593 1250 1086 C ATOM 11 C1' DT L 1 -23.855 54.649 18.636 1.00164.68 C ANISOU 11 C1' DT L 1 23430 23642 15498 -1079 1229 535 C ATOM 12 N1 DT L 1 -23.672 54.152 17.236 1.00170.04 N ANISOU 12 N1 DT L 1 24823 24401 15383 -1409 1397 266 N ATOM 13 C2 DT L 1 -23.716 52.798 16.961 1.00171.59 C ANISOU 13 C2 DT L 1 25147 24576 15472 -1873 1389 -272 C ATOM 14 O2 DT L 1 -23.901 51.945 17.813 1.00168.18 O ANISOU 14 O2 DT L 1 24245 24051 15604 -2038 1250 -510 O ATOM 15 N3 DT L 1 -23.533 52.477 15.635 1.00176.88 N ANISOU 15 N3 DT L 1 26594 25303 15311 -2146 1580 -524 N ATOM 16 C4 DT L 1 -23.316 53.350 14.581 1.00178.76 C ANISOU 16 C4 DT L 1 27472 25648 14801 -1998 1777 -253 C ATOM 17 O4 DT L 1 -23.163 52.970 13.423 1.00182.23 O ANISOU 17 O4 DT L 1 28662 26145 14432 -2268 1963 -518 O ATOM 18 C5 DT L 1 -23.281 54.745 14.941 1.00176.36 C ANISOU 18 C5 DT L 1 26964 25345 14700 -1506 1775 363 C ATOM 19 C7 DT L 1 -23.052 55.784 13.885 1.00179.77 C ANISOU 19 C7 DT L 1 28084 25835 14387 -1307 2009 760 C ATOM 20 C6 DT L 1 -23.457 55.072 16.229 1.00172.38 C ANISOU 20 C6 DT L 1 25716 24753 15027 -1244 1588 564 C ATOM 21 P DT L 2 -23.945 56.869 22.570 1.00166.33 P ANISOU 21 P DT L 2 22172 23374 17651 39 1069 1329 P ATOM 22 OP1 DT L 2 -25.409 56.896 22.789 1.00165.92 O ANISOU 22 OP1 DT L 2 21763 23921 17357 205 475 1556 O ATOM 23 OP2 DT L 2 -23.165 58.117 22.704 1.00166.05 O ANISOU 23 OP2 DT L 2 22374 22899 17819 322 1431 1571 O ATOM 24 O5' DT L 2 -23.313 55.780 23.552 1.00134.24 O ANISOU 24 O5' DT L 2 17749 19001 14256 -218 1232 948 O ATOM 25 C5' DT L 2 -22.520 54.733 22.993 1.00132.82 C ANISOU 25 C5' DT L 2 17769 18576 14120 -595 1568 555 C ATOM 26 C4' DT L 2 -21.109 54.819 23.541 1.00122.67 C ANISOU 26 C4' DT L 2 16416 16698 13495 -578 2071 446 C ATOM 27 O4' DT L 2 -20.208 53.874 22.909 1.00118.50 O ANISOU 27 O4' DT L 2 16088 15874 13064 -863 2528 91 O ATOM 28 C3' DT L 2 -20.475 56.193 23.343 1.00118.56 C ANISOU 28 C3' DT L 2 16129 15923 12997 -348 2356 727 C ATOM 29 O3' DT L 2 -19.862 56.559 24.545 1.00112.71 O ANISOU 29 O3' DT L 2 15048 14853 12925 -232 2399 764 O ATOM 30 C2' DT L 2 -19.402 55.927 22.306 1.00120.69 C ANISOU 30 C2' DT L 2 16767 15895 13195 -564 2957 542 C ATOM 31 C1' DT L 2 -18.980 54.566 22.827 1.00120.22 C ANISOU 31 C1' DT L 2 16389 15666 13625 -777 3040 167 C ATOM 32 N1 DT L 2 -17.963 53.898 21.967 1.00127.13 N ANISOU 32 N1 DT L 2 17524 16230 14551 -980 3667 -120 N ATOM 33 C2 DT L 2 -17.931 52.522 21.819 1.00130.96 C ANISOU 33 C2 DT L 2 18014 16644 15100 -1194 3761 -501 C ATOM 34 O2 DT L 2 -18.715 51.750 22.358 1.00127.06 O ANISOU 34 O2 DT L 2 17312 16331 14633 -1284 3326 -614 O ATOM 35 N3 DT L 2 -16.925 52.079 20.993 1.00135.23 N ANISOU 35 N3 DT L 2 18839 16850 15693 -1300 4453 -743 N ATOM 36 C4 DT L 2 -15.979 52.845 20.328 1.00136.98 C ANISOU 36 C4 DT L 2 19282 16849 15916 -1243 5058 -618 C ATOM 37 O4 DT L 2 -15.116 52.344 19.609 1.00139.96 O ANISOU 37 O4 DT L 2 19882 16940 16355 -1324 5740 -850 O ATOM 38 C5 DT L 2 -16.077 54.270 20.536 1.00132.93 C ANISOU 38 C5 DT L 2 18738 16423 15348 -1076 4892 -194 C ATOM 39 C7 DT L 2 -15.112 55.209 19.870 1.00134.96 C ANISOU 39 C7 DT L 2 19229 16415 15633 -1058 5533 7 C ATOM 40 C6 DT L 2 -17.050 54.718 21.335 1.00127.42 C ANISOU 40 C6 DT L 2 17813 16010 14592 -940 4209 17 C ATOM 41 P DT L 3 -20.608 57.541 25.578 1.00 77.43 P ANISOU 41 P DT L 3 10399 10496 8526 112 2017 1050 P ATOM 42 OP1 DT L 3 -21.573 58.399 24.836 1.00 66.76 O ANISOU 42 OP1 DT L 3 9343 9464 6560 361 1834 1369 O ATOM 43 OP2 DT L 3 -19.518 58.115 26.411 1.00 70.14 O ANISOU 43 OP2 DT L 3 9363 9082 8203 126 2228 1038 O ATOM 44 O5' DT L 3 -21.471 56.559 26.524 1.00 62.35 O ANISOU 44 O5' DT L 3 8051 8902 6737 88 1606 936 O ATOM 45 C5' DT L 3 -22.860 56.630 26.478 1.00 63.24 C ANISOU 45 C5' DT L 3 8065 9523 6442 247 1210 1114 C ATOM 46 C4' DT L 3 -23.403 55.444 27.228 1.00 61.61 C ANISOU 46 C4' DT L 3 7454 9526 6430 73 970 952 C ATOM 47 O4' DT L 3 -23.086 54.230 26.526 1.00 58.69 O ANISOU 47 O4' DT L 3 7169 9114 6017 -325 1085 645 O ATOM 48 C3' DT L 3 -22.857 55.270 28.639 1.00 57.52 C ANISOU 48 C3' DT L 3 6671 8710 6474 122 1008 888 C ATOM 49 O3' DT L 3 -23.972 55.309 29.460 1.00 56.25 O ANISOU 49 O3' DT L 3 6225 8900 6248 308 715 1052 O ATOM 50 C2' DT L 3 -22.263 53.858 28.651 1.00 52.19 C ANISOU 50 C2' DT L 3 5888 7847 6097 -235 1129 591 C ATOM 51 C1' DT L 3 -23.044 53.221 27.507 1.00 55.49 C ANISOU 51 C1' DT L 3 6432 8610 6041 -471 1022 494 C ATOM 52 N1 DT L 3 -22.497 51.978 26.866 1.00 59.35 N ANISOU 52 N1 DT L 3 7067 8880 6604 -844 1244 149 N ATOM 53 C2 DT L 3 -23.379 50.970 26.498 1.00 59.54 C ANISOU 53 C2 DT L 3 7059 9180 6382 -1155 1016 -5 C ATOM 54 O2 DT L 3 -24.584 51.007 26.674 1.00 67.91 O ANISOU 54 O2 DT L 3 7889 10707 7207 -1165 624 151 O ATOM 55 N3 DT L 3 -22.795 49.877 25.915 1.00 62.82 N ANISOU 55 N3 DT L 3 7710 9285 6876 -1474 1288 -364 N ATOM 56 C4 DT L 3 -21.462 49.676 25.656 1.00 61.73 C ANISOU 56 C4 DT L 3 7769 8633 7054 -1460 1788 -550 C ATOM 57 O4 DT L 3 -21.078 48.638 25.119 1.00 70.77 O ANISOU 57 O4 DT L 3 9139 9504 8248 -1712 2055 -881 O ATOM 58 C5 DT L 3 -20.589 50.768 26.053 1.00 59.23 C ANISOU 58 C5 DT L 3 7368 8115 7022 -1142 1986 -335 C ATOM 59 C7 DT L 3 -19.106 50.667 25.813 1.00 59.99 C ANISOU 59 C7 DT L 3 7540 7701 7554 -1117 2535 -474 C ATOM 60 C6 DT L 3 -21.137 51.856 26.623 1.00 57.06 C ANISOU 60 C6 DT L 3 6936 8101 6644 -883 1692 -18 C ATOM 61 P DT L 4 -24.535 56.694 30.056 1.00 52.61 P ANISOU 61 P DT L 4 5794 8514 5680 790 639 1345 P ATOM 62 OP1 DT L 4 -25.825 56.309 30.714 1.00 53.54 O ANISOU 62 OP1 DT L 4 5522 9103 5719 906 394 1479 O ATOM 63 OP2 DT L 4 -24.524 57.738 29.030 1.00 55.33 O ANISOU 63 OP2 DT L 4 6481 8833 5707 977 722 1521 O ATOM 64 O5' DT L 4 -23.484 57.075 31.212 1.00 49.91 O ANISOU 64 O5' DT L 4 5520 7675 5769 845 783 1247 O ATOM 65 C5' DT L 4 -23.376 56.235 32.362 1.00 47.76 C ANISOU 65 C5' DT L 4 4992 7373 5780 734 694 1140 C ATOM 66 C4' DT L 4 -21.929 56.132 32.829 1.00 46.25 C ANISOU 66 C4' DT L 4 4865 6690 6018 564 809 967 C ATOM 67 O4' DT L 4 -21.176 55.216 32.001 1.00 50.23 O ANISOU 67 O4' DT L 4 5329 7046 6709 248 971 795 O ATOM 68 C3' DT L 4 -21.122 57.422 32.784 1.00 47.02 C ANISOU 68 C3' DT L 4 5248 6412 6208 673 938 985 C ATOM 69 O3' DT L 4 -21.347 58.133 33.995 1.00 56.69 O ANISOU 69 O3' DT L 4 6553 7564 7422 908 804 1033 O ATOM 70 C2' DT L 4 -19.662 56.968 32.617 1.00 46.78 C ANISOU 70 C2' DT L 4 5140 6000 6635 369 1093 811 C ATOM 71 C1' DT L 4 -19.789 55.554 32.045 1.00 51.73 C ANISOU 71 C1' DT L 4 5574 6793 7288 157 1149 704 C ATOM 72 N1 DT L 4 -19.234 55.293 30.665 1.00 48.27 N ANISOU 72 N1 DT L 4 5266 6243 6831 -32 1475 600 N ATOM 73 C2 DT L 4 -19.378 56.216 29.646 1.00 50.27 C ANISOU 73 C2 DT L 4 5834 6523 6741 38 1643 700 C ATOM 74 O2 DT L 4 -19.913 57.301 29.767 1.00 50.71 O ANISOU 74 O2 DT L 4 6064 6649 6556 273 1543 887 O ATOM 75 N3 DT L 4 -18.846 55.839 28.434 1.00 52.49 N ANISOU 75 N3 DT L 4 6279 6713 6953 -153 1983 587 N ATOM 76 C4 DT L 4 -18.229 54.639 28.144 1.00 53.04 C ANISOU 76 C4 DT L 4 6225 6644 7282 -376 2196 356 C ATOM 77 O4 DT L 4 -17.802 54.389 27.023 1.00 60.00 O ANISOU 77 O4 DT L 4 7331 7437 8029 -513 2565 240 O ATOM 78 C5 DT L 4 -18.125 53.705 29.237 1.00 50.90 C ANISOU 78 C5 DT L 4 5601 6314 7423 -408 1996 275 C ATOM 79 C7 DT L 4 -17.456 52.377 29.013 1.00 52.07 C ANISOU 79 C7 DT L 4 5623 6234 7927 -583 2241 54 C ATOM 80 C6 DT L 4 -18.636 54.067 30.423 1.00 48.61 C ANISOU 80 C6 DT L 4 5157 6147 7165 -249 1634 415 C ATOM 81 P DT L 5 -21.668 59.708 33.953 1.00 60.86 P ANISOU 81 P DT L 5 7457 7932 7735 1240 885 1162 P ATOM 82 OP1 DT L 5 -22.971 59.875 33.279 1.00 68.91 O ANISOU 82 OP1 DT L 5 8449 9368 8364 1526 882 1384 O ATOM 83 OP2 DT L 5 -20.465 60.426 33.434 1.00 66.16 O ANISOU 83 OP2 DT L 5 8364 8125 8647 1050 1064 1097 O ATOM 84 O5' DT L 5 -21.787 60.110 35.488 1.00 67.30 O ANISOU 84 O5' DT L 5 8374 8636 8559 1417 748 1101 O ATOM 85 C5' DT L 5 -20.617 60.634 36.085 1.00 67.75 C ANISOU 85 C5' DT L 5 8625 8226 8890 1230 701 932 C ATOM 86 C4' DT L 5 -20.050 59.707 37.138 1.00 66.96 C ANISOU 86 C4' DT L 5 8298 8143 9002 1011 461 801 C ATOM 87 O4' DT L 5 -18.778 60.257 37.521 1.00 68.14 O ANISOU 87 O4' DT L 5 8569 7855 9468 761 357 646 O ATOM 88 C3' DT L 5 -20.854 59.598 38.434 1.00 64.49 C ANISOU 88 C3' DT L 5 8065 8039 8401 1248 321 816 C ATOM 89 O3' DT L 5 -20.742 58.300 39.000 1.00 63.76 O ANISOU 89 O3' DT L 5 7663 8148 8418 1082 157 828 O ATOM 90 C2' DT L 5 -20.236 60.662 39.329 1.00 60.60 C ANISOU 90 C2' DT L 5 7990 7144 7892 1246 206 649 C ATOM 91 C1' DT L 5 -18.784 60.547 38.902 1.00 61.48 C ANISOU 91 C1' DT L 5 7937 6938 8484 823 106 542 C ATOM 92 N1 DT L 5 -17.988 61.772 39.111 1.00 64.72 N ANISOU 92 N1 DT L 5 8702 6866 9022 676 59 387 N ATOM 93 C2 DT L 5 -16.879 61.691 39.931 1.00 72.08 C ANISOU 93 C2 DT L 5 9567 7594 10225 341 -285 226 C ATOM 94 O2 DT L 5 -16.539 60.660 40.499 1.00 65.18 O ANISOU 94 O2 DT L 5 8368 6923 9475 228 -546 246 O ATOM 95 N3 DT L 5 -16.192 62.874 40.071 1.00 76.29 N ANISOU 95 N3 DT L 5 10436 7663 10887 135 -338 62 N ATOM 96 C4 DT L 5 -16.496 64.089 39.480 1.00 74.18 C ANISOU 96 C4 DT L 5 10605 7063 10516 257 -33 62 C ATOM 97 O4 DT L 5 -15.805 65.088 39.673 1.00 76.59 O ANISOU 97 O4 DT L 5 11225 6890 10985 -1 -93 -101 O ATOM 98 C5 DT L 5 -17.667 64.096 38.627 1.00 67.35 C ANISOU 98 C5 DT L 5 9795 6439 9357 686 328 284 C ATOM 99 C7 DT L 5 -18.086 65.366 37.935 1.00 62.59 C ANISOU 99 C7 DT L 5 9663 5494 8623 916 659 376 C ATOM 100 C6 DT L 5 -18.351 62.946 38.482 1.00 64.08 C ANISOU 100 C6 DT L 5 9001 6540 8808 856 329 425 C ATOM 101 P DT L 6 -22.031 57.619 39.688 1.00 53.84 P ANISOU 101 P DT L 6 6285 7330 6843 1295 176 978 P ATOM 102 OP1 DT L 6 -22.468 58.553 40.757 1.00 69.34 O ANISOU 102 OP1 DT L 6 8633 9245 8469 1595 191 946 O ATOM 103 OP2 DT L 6 -21.698 56.220 40.048 1.00 58.23 O ANISOU 103 OP2 DT L 6 6548 7974 7605 1047 37 1015 O ATOM 104 O5' DT L 6 -23.152 57.655 38.543 1.00 47.02 O ANISOU 104 O5' DT L 6 5242 6799 5826 1457 381 1129 O ATOM 105 C5' DT L 6 -22.916 56.947 37.323 1.00 55.72 C ANISOU 105 C5' DT L 6 6103 7957 7110 1197 413 1123 C ATOM 106 C4' DT L 6 -24.152 56.168 36.939 1.00 52.14 C ANISOU 106 C4' DT L 6 5338 7983 6489 1210 436 1268 C ATOM 107 O4' DT L 6 -23.964 55.503 35.667 1.00 48.23 O ANISOU 107 O4' DT L 6 4708 7531 6086 929 458 1209 O ATOM 108 C3' DT L 6 -24.555 55.084 37.931 1.00 51.06 C ANISOU 108 C3' DT L 6 4983 8031 6385 1109 374 1329 C ATOM 109 O3' DT L 6 -25.975 55.103 38.014 1.00 47.63 O ANISOU 109 O3' DT L 6 4331 8058 5709 1307 443 1522 O ATOM 110 C2' DT L 6 -23.994 53.817 37.286 1.00 45.77 C ANISOU 110 C2' DT L 6 4128 7262 6000 708 340 1232 C ATOM 111 C1' DT L 6 -24.193 54.112 35.798 1.00 47.76 C ANISOU 111 C1' DT L 6 4383 7615 6151 652 406 1188 C ATOM 112 N1 DT L 6 -23.260 53.451 34.807 1.00 49.45 N ANISOU 112 N1 DT L 6 4627 7568 6593 335 482 1001 N ATOM 113 C2 DT L 6 -23.748 53.016 33.588 1.00 45.94 C ANISOU 113 C2 DT L 6 4145 7328 5981 150 513 948 C ATOM 114 O2 DT L 6 -24.904 53.109 33.261 1.00 47.53 O ANISOU 114 O2 DT L 6 4221 7948 5890 201 409 1068 O ATOM 115 N3 DT L 6 -22.833 52.453 32.750 1.00 46.13 N ANISOU 115 N3 DT L 6 4278 7064 6184 -101 667 745 N ATOM 116 C4 DT L 6 -21.476 52.291 32.987 1.00 45.25 C ANISOU 116 C4 DT L 6 4210 6501 6482 -155 809 629 C ATOM 117 O4 DT L 6 -20.731 51.775 32.155 1.00 46.22 O ANISOU 117 O4 DT L 6 4404 6387 6771 -339 1026 456 O ATOM 118 C5 DT L 6 -21.021 52.775 34.275 1.00 48.53 C ANISOU 118 C5 DT L 6 4578 6765 7097 23 683 726 C ATOM 119 C7 DT L 6 -19.572 52.653 34.663 1.00 43.91 C ANISOU 119 C7 DT L 6 3934 5758 6992 -36 726 650 C ATOM 120 C6 DT L 6 -21.923 53.323 35.111 1.00 43.71 C ANISOU 120 C6 DT L 6 3966 6415 6228 243 525 883 C ATOM 121 P DT L 7 -26.728 54.654 39.371 1.00 51.43 P ANISOU 121 P DT L 7 4696 8771 6073 1417 514 1674 P ATOM 122 OP1 DT L 7 -28.022 55.390 39.408 1.00 55.52 O ANISOU 122 OP1 DT L 7 5065 9681 6350 1810 674 1865 O ATOM 123 OP2 DT L 7 -25.779 54.764 40.502 1.00 53.02 O ANISOU 123 OP2 DT L 7 5236 8621 6288 1428 448 1575 O ATOM 124 O5' DT L 7 -26.995 53.089 39.159 1.00 49.96 O ANISOU 124 O5' DT L 7 4158 8745 6081 989 465 1724 O ATOM 125 C5' DT L 7 -27.577 52.615 37.939 1.00 49.68 C ANISOU 125 C5' DT L 7 3828 8963 6084 758 415 1724 C ATOM 126 C4' DT L 7 -27.762 51.113 38.070 1.00 50.34 C ANISOU 126 C4' DT L 7 3687 9072 6368 326 398 1740 C ATOM 127 O4' DT L 7 -26.470 50.491 38.199 1.00 48.91 O ANISOU 127 O4' DT L 7 3739 8395 6450 131 362 1579 O ATOM 128 C3' DT L 7 -28.539 50.629 39.290 1.00 55.45 C ANISOU 128 C3' DT L 7 4158 9933 6978 354 525 1977 C ATOM 129 O3' DT L 7 -29.212 49.485 38.909 1.00 58.42 O ANISOU 129 O3' DT L 7 4207 10489 7501 -67 514 2029 O ATOM 130 C2' DT L 7 -27.467 50.222 40.295 1.00 50.98 C ANISOU 130 C2' DT L 7 3911 8935 6525 334 514 1951 C ATOM 131 C1' DT L 7 -26.402 49.673 39.353 1.00 49.97 C ANISOU 131 C1' DT L 7 3875 8421 6691 53 394 1717 C ATOM 132 N1 DT L 7 -24.987 49.762 39.860 1.00 49.29 N ANISOU 132 N1 DT L 7 4070 7878 6781 129 299 1627 N ATOM 133 C2 DT L 7 -24.243 48.623 40.096 1.00 50.72 C ANISOU 133 C2 DT L 7 4266 7719 7287 -85 261 1636 C ATOM 134 O2 DT L 7 -24.672 47.494 39.914 1.00 52.34 O ANISOU 134 O2 DT L 7 4339 7906 7642 -362 338 1690 O ATOM 135 N3 DT L 7 -22.971 48.854 40.554 1.00 46.90 N ANISOU 135 N3 DT L 7 3946 6895 6980 31 118 1592 N ATOM 136 C4 DT L 7 -22.381 50.079 40.794 1.00 52.05 C ANISOU 136 C4 DT L 7 4768 7495 7512 254 2 1504 C ATOM 137 O4 DT L 7 -21.224 50.185 41.203 1.00 46.19 O ANISOU 137 O4 DT L 7 4101 6467 6983 281 -177 1471 O ATOM 138 C5 DT L 7 -23.216 51.226 40.529 1.00 45.67 C ANISOU 138 C5 DT L 7 4026 6978 6350 448 93 1469 C ATOM 139 C7 DT L 7 -22.690 52.616 40.750 1.00 45.44 C ANISOU 139 C7 DT L 7 4258 6825 6181 672 14 1357 C ATOM 140 C6 DT L 7 -24.453 51.015 40.074 1.00 46.69 C ANISOU 140 C6 DT L 7 3964 7461 6314 415 237 1550 C ATOM 141 P DT L 8 -30.802 49.502 38.765 1.00 62.06 P ANISOU 141 P DT L 8 4136 11576 7867 -91 564 2257 P ATOM 142 OP1 DT L 8 -31.189 48.098 38.502 1.00 63.08 O ANISOU 142 OP1 DT L 8 4021 11719 8226 -681 525 2255 O ATOM 143 OP2 DT L 8 -31.152 50.559 37.784 1.00 76.11 O ANISOU 143 OP2 DT L 8 5822 13631 9466 173 434 2229 O ATOM 144 O5' DT L 8 -31.317 49.987 40.200 1.00 81.19 O ANISOU 144 O5' DT L 8 6542 14172 10134 311 845 2523 O ATOM 145 C5' DT L 8 -31.475 49.091 41.286 1.00 92.43 C ANISOU 145 C5' DT L 8 7958 15538 11624 132 1036 2704 C ATOM 146 C4' DT L 8 -32.878 49.338 41.809 1.00102.37 C ANISOU 146 C4' DT L 8 8756 17354 12786 315 1320 3011 C ATOM 147 O4' DT L 8 -33.842 48.914 40.825 1.00107.38 O ANISOU 147 O4' DT L 8 8878 18323 13598 -23 1161 3026 O ATOM 148 C3' DT L 8 -33.321 48.678 43.114 1.00101.33 C ANISOU 148 C3' DT L 8 8598 17283 12618 249 1668 3297 C ATOM 149 O3' DT L 8 -33.123 49.709 44.105 1.00 93.71 O ANISOU 149 O3' DT L 8 8032 16281 11292 828 1889 3326 O ATOM 150 C2' DT L 8 -34.758 48.207 42.826 1.00107.49 C ANISOU 150 C2' DT L 8 8829 18436 13577 -6 1725 3436 C ATOM 151 C1' DT L 8 -35.068 48.934 41.514 1.00113.28 C ANISOU 151 C1' DT L 8 9350 19368 14325 98 1404 3260 C ATOM 152 N1 DT L 8 -36.126 48.377 40.600 1.00117.56 N ANISOU 152 N1 DT L 8 9428 20170 15071 -311 1179 3243 N ATOM 153 C2 DT L 8 -37.325 49.043 40.508 1.00129.08 C ANISOU 153 C2 DT L 8 10501 22039 16502 -22 1224 3405 C ATOM 154 O2 DT L 8 -37.565 50.049 41.151 1.00135.78 O ANISOU 154 O2 DT L 8 11414 22996 17178 563 1483 3546 O ATOM 155 N3 DT L 8 -38.241 48.485 39.647 1.00132.90 N ANISOU 155 N3 DT L 8 10529 22789 17179 -443 964 3396 N ATOM 156 C4 DT L 8 -38.081 47.352 38.869 1.00126.60 C ANISOU 156 C4 DT L 8 9686 21859 16557 -1125 678 3198 C ATOM 157 O4 DT L 8 -38.982 46.949 38.127 1.00120.34 O ANISOU 157 O4 DT L 8 8478 21346 15900 -1482 430 3186 O ATOM 158 C5 DT L 8 -36.786 46.706 39.006 1.00119.17 C ANISOU 158 C5 DT L 8 9222 20420 15635 -1374 697 3008 C ATOM 159 C7 DT L 8 -36.459 45.464 38.225 1.00114.28 C ANISOU 159 C7 DT L 8 8681 19527 15212 -2084 466 2754 C ATOM 160 C6 DT L 8 -35.886 47.245 39.847 1.00116.16 C ANISOU 160 C6 DT L 8 9221 19810 15103 -954 931 3061 C ATOM 161 P DT L 9 -34.267 50.138 45.150 1.00209.38 P ANISOU 161 P DT L 9 22481 31364 25709 1212 2416 3636 P ATOM 162 OP1 DT L 9 -35.460 50.634 44.425 1.00210.31 O ANISOU 162 OP1 DT L 9 22136 31793 25978 1340 2358 3640 O ATOM 163 OP2 DT L 9 -33.585 51.046 46.098 1.00209.29 O ANISOU 163 OP2 DT L 9 23173 31074 25273 1695 2527 3512 O ATOM 164 O5' DT L 9 -34.617 48.791 45.943 1.00120.02 O ANISOU 164 O5' DT L 9 11098 20008 14495 761 2617 3888 O ATOM 165 C5' DT L 9 -35.294 48.881 47.202 1.00112.75 C ANISOU 165 C5' DT L 9 10316 19211 13315 1009 3070 4106 C ATOM 166 C4' DT L 9 -35.086 47.622 48.031 1.00111.78 C ANISOU 166 C4' DT L 9 10388 18891 13195 599 3222 4350 C ATOM 167 O4' DT L 9 -36.221 46.746 47.825 1.00111.38 O ANISOU 167 O4' DT L 9 9823 18980 13518 173 3317 4470 O ATOM 168 C3' DT L 9 -33.836 46.793 47.711 1.00108.32 C ANISOU 168 C3' DT L 9 10230 18022 12907 213 2865 4300 C ATOM 169 O3' DT L 9 -33.266 46.228 48.905 1.00106.76 O ANISOU 169 O3' DT L 9 10606 17523 12436 201 2969 4507 O ATOM 170 C2' DT L 9 -34.369 45.716 46.766 1.00106.98 C ANISOU 170 C2' DT L 9 9536 17842 13268 -405 2716 4290 C ATOM 171 C1' DT L 9 -35.791 45.507 47.291 1.00108.05 C ANISOU 171 C1' DT L 9 9345 18265 13443 -447 3065 4464 C ATOM 172 N1 DT L 9 -36.786 45.067 46.253 1.00101.48 N ANISOU 172 N1 DT L 9 7916 17610 13033 -857 2887 4339 N ATOM 173 C2 DT L 9 -37.670 44.045 46.550 1.00 98.15 C ANISOU 173 C2 DT L 9 7233 17198 12861 -1310 3101 4505 C ATOM 174 O2 DT L 9 -37.692 43.468 47.628 1.00101.35 O ANISOU 174 O2 DT L 9 7885 17460 13162 -1381 3457 4769 O ATOM 175 N3 DT L 9 -38.529 43.722 45.529 1.00101.10 N ANISOU 175 N3 DT L 9 7072 17755 13585 -1690 2877 4356 N ATOM 176 C4 DT L 9 -38.598 44.308 44.275 1.00 98.71 C ANISOU 176 C4 DT L 9 6520 17636 13351 -1642 2456 4093 C ATOM 177 O4 DT L 9 -39.405 43.954 43.420 1.00112.99 O ANISOU 177 O4 DT L 9 7877 19630 15425 -2010 2241 3992 O ATOM 178 C5 DT L 9 -37.649 45.368 44.035 1.00 92.19 C ANISOU 178 C5 DT L 9 6019 16767 12241 -1143 2281 3955 C ATOM 179 C7 DT L 9 -37.633 46.064 42.704 1.00 89.77 C ANISOU 179 C7 DT L 9 5538 16628 11942 -1051 1858 3706 C ATOM 180 C6 DT L 9 -36.792 45.694 45.017 1.00 89.81 C ANISOU 180 C6 DT L 9 6198 16276 11651 -791 2507 4068 C TER 181 DT L 9 ATOM 182 N GLY A 34 -8.107 44.864 12.141 1.00 62.75 N ANISOU 182 N GLY A 34 9078 7619 7144 1576 -858 311 N ATOM 183 CA GLY A 34 -6.727 44.428 11.966 1.00 55.49 C ANISOU 183 CA GLY A 34 8103 6754 6228 1327 -888 169 C ATOM 184 C GLY A 34 -6.620 43.323 10.925 1.00 57.83 C ANISOU 184 C GLY A 34 8204 7248 6522 1305 -997 166 C ATOM 185 O GLY A 34 -7.472 42.433 10.865 1.00 57.24 O ANISOU 185 O GLY A 34 7963 7308 6478 1413 -1106 197 O ATOM 186 N ARG A 35 -5.569 43.353 10.113 1.00 54.94 N ANISOU 186 N ARG A 35 7861 6899 6116 1154 -956 121 N ATOM 187 CA ARG A 35 -5.444 42.364 9.048 1.00 60.83 C ANISOU 187 CA ARG A 35 8464 7814 6833 1128 -1012 81 C ATOM 188 C ARG A 35 -4.666 41.117 9.465 1.00 56.85 C ANISOU 188 C ARG A 35 7753 7384 6465 1022 -1039 -52 C ATOM 189 O ARG A 35 -4.893 40.034 8.937 1.00 57.75 O ANISOU 189 O ARG A 35 7727 7601 6614 1037 -1086 -120 O ATOM 190 CB ARG A 35 -4.815 42.994 7.801 1.00 66.71 C ANISOU 190 CB ARG A 35 9325 8571 7449 1054 -928 127 C ATOM 191 CG ARG A 35 -5.302 44.406 7.521 1.00 73.37 C ANISOU 191 CG ARG A 35 10368 9292 8216 1141 -856 307 C ATOM 192 CD ARG A 35 -5.575 44.632 6.054 1.00 86.52 C ANISOU 192 CD ARG A 35 12046 11107 9720 1170 -850 439 C ATOM 193 NE ARG A 35 -6.529 43.667 5.514 1.00 90.23 N ANISOU 193 NE ARG A 35 12370 11806 10109 1235 -977 435 N ATOM 194 CZ ARG A 35 -6.324 42.960 4.408 1.00 89.83 C ANISOU 194 CZ ARG A 35 12246 11972 9915 1143 -1010 359 C ATOM 195 NH1 ARG A 35 -5.198 43.109 3.722 1.00 89.57 N ANISOU 195 NH1 ARG A 35 12256 11965 9813 1021 -912 303 N ATOM 196 NH2 ARG A 35 -7.242 42.102 3.985 1.00 90.30 N ANISOU 196 NH2 ARG A 35 12191 12230 9890 1157 -1133 334 N ATOM 197 N LEU A 36 -3.741 41.263 10.405 1.00 54.19 N ANISOU 197 N LEU A 36 7387 6995 6209 901 -999 -77 N ATOM 198 CA LEU A 36 -2.912 40.127 10.803 1.00 49.35 C ANISOU 198 CA LEU A 36 6536 6465 5752 809 -998 -129 C ATOM 199 C LEU A 36 -3.505 39.305 11.942 1.00 49.58 C ANISOU 199 C LEU A 36 6366 6549 5925 876 -1090 -117 C ATOM 200 O LEU A 36 -3.506 38.065 11.903 1.00 48.20 O ANISOU 200 O LEU A 36 5970 6432 5910 902 -1110 -142 O ATOM 201 CB LEU A 36 -1.532 40.609 11.203 1.00 51.34 C ANISOU 201 CB LEU A 36 6791 6706 6012 614 -923 -98 C ATOM 202 CG LEU A 36 -0.753 41.129 10.012 1.00 65.77 C ANISOU 202 CG LEU A 36 8737 8512 7741 541 -824 -85 C ATOM 203 CD1 LEU A 36 0.583 41.638 10.475 1.00 65.46 C ANISOU 203 CD1 LEU A 36 8682 8477 7714 325 -767 -18 C ATOM 204 CD2 LEU A 36 -0.580 40.005 9.012 1.00 68.19 C ANISOU 204 CD2 LEU A 36 8907 8902 8098 594 -773 -150 C ATOM 205 N LEU A 37 -4.012 40.007 12.952 1.00 38.20 N ANISOU 205 N LEU A 37 5006 5076 4433 906 -1124 -78 N ATOM 206 CA LEU A 37 -4.311 39.392 14.236 1.00 41.59 C ANISOU 206 CA LEU A 37 5236 5597 4970 928 -1196 -42 C ATOM 207 C LEU A 37 -5.792 39.384 14.554 1.00 45.22 C ANISOU 207 C LEU A 37 5711 6059 5413 1132 -1271 2 C ATOM 208 O LEU A 37 -6.537 40.262 14.122 1.00 45.05 O ANISOU 208 O LEU A 37 5905 5945 5268 1242 -1244 25 O ATOM 209 CB LEU A 37 -3.575 40.136 15.350 1.00 36.38 C ANISOU 209 CB LEU A 37 4630 4957 4235 753 -1165 -39 C ATOM 210 CG LEU A 37 -2.059 40.277 15.194 1.00 44.67 C ANISOU 210 CG LEU A 37 5644 6041 5286 515 -1103 -27 C ATOM 211 CD1 LEU A 37 -1.414 40.916 16.439 1.00 44.83 C ANISOU 211 CD1 LEU A 37 5686 6141 5206 287 -1109 -19 C ATOM 212 CD2 LEU A 37 -1.429 38.922 14.927 1.00 46.59 C ANISOU 212 CD2 LEU A 37 5568 6398 5737 510 -1098 39 C ATOM 213 N LEU A 38 -6.205 38.380 15.319 1.00 48.99 N ANISOU 213 N LEU A 38 5929 6650 6033 1189 -1355 55 N ATOM 214 CA LEU A 38 -7.525 38.359 15.938 1.00 46.06 C ANISOU 214 CA LEU A 38 5531 6303 5666 1312 -1370 140 C ATOM 215 C LEU A 38 -7.529 39.266 17.156 1.00 39.27 C ANISOU 215 C LEU A 38 4777 5468 4674 1352 -1375 138 C ATOM 216 O LEU A 38 -6.687 39.123 18.031 1.00 53.82 O ANISOU 216 O LEU A 38 6511 7413 6527 1190 -1370 124 O ATOM 217 CB LEU A 38 -7.828 36.948 16.402 1.00 61.95 C ANISOU 217 CB LEU A 38 7258 8376 7903 1175 -1299 240 C ATOM 218 CG LEU A 38 -8.541 36.062 15.395 1.00 75.01 C ANISOU 218 CG LEU A 38 8860 9996 9645 1163 -1282 256 C ATOM 219 CD1 LEU A 38 -8.192 34.602 15.652 1.00 81.06 C ANISOU 219 CD1 LEU A 38 9385 10797 10618 1058 -1222 318 C ATOM 220 CD2 LEU A 38 -10.037 36.297 15.511 1.00 69.85 C ANISOU 220 CD2 LEU A 38 8244 9334 8963 1187 -1253 372 C ATOM 221 N SER A 39 -8.484 40.179 17.236 1.00 49.00 N ANISOU 221 N SER A 39 6221 6608 5790 1511 -1322 164 N ATOM 222 CA SER A 39 -8.566 41.074 18.378 1.00 60.18 C ANISOU 222 CA SER A 39 7793 7994 7079 1499 -1229 120 C ATOM 223 C SER A 39 -10.009 41.242 18.804 1.00 58.99 C ANISOU 223 C SER A 39 7651 7850 6912 1773 -1213 234 C ATOM 224 O SER A 39 -10.890 41.381 17.962 1.00 59.25 O ANISOU 224 O SER A 39 7717 7798 6999 1845 -1144 327 O ATOM 225 CB SER A 39 -7.987 42.443 18.019 1.00 69.52 C ANISOU 225 CB SER A 39 9333 8953 8130 1390 -1076 7 C ATOM 226 OG SER A 39 -6.663 42.307 17.541 1.00 80.21 O ANISOU 226 OG SER A 39 10661 10316 9497 1145 -1092 -60 O ATOM 227 N THR A 40 -10.251 41.232 20.110 1.00 47.76 N ANISOU 227 N THR A 40 6166 6544 5436 1791 -1193 230 N ATOM 228 CA THR A 40 -11.554 41.624 20.621 1.00 46.30 C ANISOU 228 CA THR A 40 6033 6334 5225 2004 -1086 323 C ATOM 229 C THR A 40 -11.534 43.130 20.800 1.00 51.20 C ANISOU 229 C THR A 40 7063 6710 5680 2076 -880 205 C ATOM 230 O THR A 40 -10.503 43.773 20.596 1.00 51.61 O ANISOU 230 O THR A 40 7324 6622 5664 1845 -809 36 O ATOM 231 CB THR A 40 -11.842 40.996 21.977 1.00 52.25 C ANISOU 231 CB THR A 40 6558 7299 5995 1934 -1088 357 C ATOM 232 OG1 THR A 40 -11.110 41.710 22.984 1.00 54.38 O ANISOU 232 OG1 THR A 40 7000 7634 6029 1883 -1055 195 O ATOM 233 CG2 THR A 40 -11.433 39.528 21.977 1.00 52.45 C ANISOU 233 CG2 THR A 40 6242 7409 6276 1597 -1148 426 C ATOM 234 N SER A 41 -12.666 43.693 21.210 1.00 46.60 N ANISOU 234 N SER A 41 6589 6053 5063 2346 -736 294 N ATOM 235 CA SER A 41 -12.741 45.121 21.420 1.00 48.71 C ANISOU 235 CA SER A 41 7256 6021 5231 2393 -456 172 C ATOM 236 C SER A 41 -11.988 45.503 22.691 1.00 45.71 C ANISOU 236 C SER A 41 7024 5671 4671 2141 -364 -100 C ATOM 237 O SER A 41 -11.704 46.676 22.917 1.00 51.40 O ANISOU 237 O SER A 41 8116 6119 5294 2057 -133 -294 O ATOM 238 CB SER A 41 -14.202 45.580 21.499 1.00 50.30 C ANISOU 238 CB SER A 41 7510 6130 5473 2790 -288 381 C ATOM 239 OG SER A 41 -14.834 45.029 22.639 1.00 58.34 O ANISOU 239 OG SER A 41 8341 7383 6444 2908 -310 431 O ATOM 240 N LEU A 42 -11.694 44.519 23.530 1.00 38.34 N ANISOU 240 N LEU A 42 5794 5079 3693 2008 -537 -101 N ATOM 241 CA LEU A 42 -10.940 44.767 24.756 1.00 45.36 C ANISOU 241 CA LEU A 42 6763 6102 4368 1717 -491 -326 C ATOM 242 C LEU A 42 -9.417 44.875 24.472 1.00 40.11 C ANISOU 242 C LEU A 42 6149 5434 3658 1304 -574 -478 C ATOM 243 O LEU A 42 -8.697 45.567 25.180 1.00 41.09 O ANISOU 243 O LEU A 42 6489 5544 3580 1008 -483 -706 O ATOM 244 CB LEU A 42 -11.223 43.656 25.768 1.00 38.15 C ANISOU 244 CB LEU A 42 5457 5608 3428 1739 -648 -197 C ATOM 245 CG LEU A 42 -10.415 43.659 27.064 1.00 40.08 C ANISOU 245 CG LEU A 42 5668 6134 3428 1402 -662 -362 C ATOM 246 CD1 LEU A 42 -10.706 44.902 27.910 1.00 43.37 C ANISOU 246 CD1 LEU A 42 6506 6396 3578 1375 -379 -632 C ATOM 247 CD2 LEU A 42 -10.661 42.392 27.876 1.00 39.69 C ANISOU 247 CD2 LEU A 42 5137 6533 3412 1440 -851 -140 C ATOM 248 N ASP A 43 -8.950 44.207 23.419 1.00 37.60 N ANISOU 248 N ASP A 43 5636 5133 3517 1276 -736 -349 N ATOM 249 CA ASP A 43 -7.514 44.126 23.122 1.00 44.85 C ANISOU 249 CA ASP A 43 6521 6098 4422 920 -822 -423 C ATOM 250 C ASP A 43 -6.911 45.460 22.698 1.00 45.73 C ANISOU 250 C ASP A 43 7050 5883 4443 743 -657 -611 C ATOM 251 O ASP A 43 -7.456 46.123 21.838 1.00 45.89 O ANISOU 251 O ASP A 43 7291 5601 4543 949 -533 -586 O ATOM 252 CB ASP A 43 -7.258 43.083 22.032 1.00 34.58 C ANISOU 252 CB ASP A 43 4931 4864 3343 982 -986 -248 C ATOM 253 CG ASP A 43 -7.398 41.678 22.544 1.00 49.51 C ANISOU 253 CG ASP A 43 6380 7078 5355 1027 -1156 -80 C ATOM 254 OD1 ASP A 43 -7.004 41.436 23.715 1.00 55.25 O ANISOU 254 OD1 ASP A 43 6952 8064 5975 853 -1195 -83 O ATOM 255 OD2 ASP A 43 -7.910 40.821 21.790 1.00 55.73 O ANISOU 255 OD2 ASP A 43 6970 7868 6338 1220 -1246 61 O ATOM 256 N ALA A 44 -5.786 45.842 23.306 1.00 41.26 N ANISOU 256 N ALA A 44 6566 5395 3714 347 -660 -767 N ATOM 257 CA ALA A 44 -5.021 47.015 22.870 1.00 41.96 C ANISOU 257 CA ALA A 44 7014 5187 3741 108 -535 -930 C ATOM 258 C ALA A 44 -4.601 46.812 21.430 1.00 40.15 C ANISOU 258 C ALA A 44 6711 4845 3701 170 -597 -781 C ATOM 259 O ALA A 44 -4.507 45.678 20.987 1.00 44.20 O ANISOU 259 O ALA A 44 6877 5574 4342 259 -758 -609 O ATOM 260 CB ALA A 44 -3.784 47.217 23.760 1.00 43.90 C ANISOU 260 CB ALA A 44 7266 5640 3775 -390 -594 -1073 C ATOM 261 N LYS A 45 -4.351 47.894 20.689 1.00 49.75 N ANISOU 261 N LYS A 45 8248 5719 4936 123 -456 -847 N ATOM 262 CA LYS A 45 -3.841 47.737 19.321 1.00 48.99 C ANISOU 262 CA LYS A 45 8074 5563 4977 147 -513 -703 C ATOM 263 C LYS A 45 -2.420 47.164 19.353 1.00 50.11 C ANISOU 263 C LYS A 45 7985 5961 5094 -200 -663 -670 C ATOM 264 O LYS A 45 -1.607 47.528 20.201 1.00 50.87 O ANISOU 264 O LYS A 45 8139 6143 5045 -555 -673 -783 O ATOM 265 CB LYS A 45 -3.897 49.044 18.517 1.00 55.07 C ANISOU 265 CB LYS A 45 9208 5927 5789 182 -322 -727 C ATOM 266 CG LYS A 45 -3.149 50.227 19.138 1.00 77.16 C ANISOU 266 CG LYS A 45 12345 8502 8471 -172 -186 -942 C ATOM 267 CD LYS A 45 -1.880 50.616 18.359 1.00 80.61 C ANISOU 267 CD LYS A 45 12814 8881 8934 -465 -223 -898 C ATOM 268 CE LYS A 45 -1.322 51.972 18.835 1.00 84.65 C ANISOU 268 CE LYS A 45 13724 9077 9364 -801 -58 -1108 C ATOM 269 NZ LYS A 45 -2.031 53.137 18.218 1.00 84.92 N ANISOU 269 NZ LYS A 45 14105 8624 9538 -574 200 -1099 N ATOM 270 N ASP A 46 -2.137 46.226 18.464 1.00 47.47 N ANISOU 270 N ASP A 46 7373 5770 4894 -105 -771 -506 N ATOM 271 CA ASP A 46 -0.828 45.611 18.462 1.00 42.04 C ANISOU 271 CA ASP A 46 6430 5323 4222 -377 -877 -425 C ATOM 272 C ASP A 46 0.148 46.466 17.661 1.00 40.67 C ANISOU 272 C ASP A 46 6437 4984 4031 -586 -813 -421 C ATOM 273 O ASP A 46 -0.094 46.751 16.497 1.00 43.83 O ANISOU 273 O ASP A 46 6945 5202 4505 -410 -749 -369 O ATOM 274 CB ASP A 46 -0.902 44.212 17.872 1.00 43.35 C ANISOU 274 CB ASP A 46 6232 5677 4562 -182 -973 -268 C ATOM 275 CG ASP A 46 0.408 43.478 17.984 1.00 54.14 C ANISOU 275 CG ASP A 46 7290 7295 5986 -418 -1041 -141 C ATOM 276 OD1 ASP A 46 1.348 43.823 17.224 1.00 57.33 O ANISOU 276 OD1 ASP A 46 7738 7646 6397 -561 -1001 -94 O ATOM 277 OD2 ASP A 46 0.498 42.571 18.842 1.00 59.36 O ANISOU 277 OD2 ASP A 46 7644 8216 6695 -451 -1125 -51 O ATOM 278 N GLU A 47 1.243 46.873 18.289 1.00 40.45 N ANISOU 278 N GLU A 47 6424 5052 3892 -980 -839 -451 N ATOM 279 CA GLU A 47 2.219 47.736 17.647 1.00 42.16 C ANISOU 279 CA GLU A 47 6806 5124 4091 -1224 -787 -430 C ATOM 280 C GLU A 47 2.823 47.096 16.390 1.00 51.54 C ANISOU 280 C GLU A 47 7769 6397 5418 -1119 -809 -231 C ATOM 281 O GLU A 47 2.958 47.750 15.358 1.00 55.68 O ANISOU 281 O GLU A 47 8463 6717 5976 -1073 -727 -195 O ATOM 282 CB GLU A 47 3.312 48.136 18.642 1.00 44.63 C ANISOU 282 CB GLU A 47 7114 5601 4241 -1715 -847 -471 C ATOM 283 CG GLU A 47 4.499 48.843 17.988 1.00 95.49 C ANISOU 283 CG GLU A 47 13635 11964 10682 -2012 -830 -386 C ATOM 284 CD GLU A 47 5.462 49.471 18.998 1.00100.50 C ANISOU 284 CD GLU A 47 14339 12725 11122 -2556 -890 -455 C ATOM 285 OE1 GLU A 47 5.605 48.928 20.119 1.00102.00 O ANISOU 285 OE1 GLU A 47 14327 13247 11181 -2738 -998 -460 O ATOM 286 OE2 GLU A 47 6.078 50.511 18.667 1.00101.86 O ANISOU 286 OE2 GLU A 47 14755 12683 11265 -2823 -835 -489 O ATOM 287 N LEU A 48 3.159 45.811 16.471 1.00 50.01 N ANISOU 287 N LEU A 48 7192 6498 5312 -1067 -896 -97 N ATOM 288 CA LEU A 48 3.734 45.118 15.331 1.00 46.53 C ANISOU 288 CA LEU A 48 6545 6133 5003 -958 -876 60 C ATOM 289 C LEU A 48 2.738 45.053 14.169 1.00 48.08 C ANISOU 289 C LEU A 48 6867 6145 5255 -603 -813 17 C ATOM 290 O LEU A 48 3.115 45.305 13.021 1.00 48.01 O ANISOU 290 O LEU A 48 6915 6069 5259 -568 -748 80 O ATOM 291 CB LEU A 48 4.286 43.733 15.725 1.00 43.58 C ANISOU 291 CB LEU A 48 5734 6071 4753 -963 -936 218 C ATOM 292 CG LEU A 48 4.785 42.794 14.606 1.00 52.02 C ANISOU 292 CG LEU A 48 6575 7200 5991 -800 -866 351 C ATOM 293 CD1 LEU A 48 5.797 41.787 15.096 1.00 51.78 C ANISOU 293 CD1 LEU A 48 6128 7450 6096 -915 -873 573 C ATOM 294 CD2 LEU A 48 3.629 42.021 14.006 1.00 55.47 C ANISOU 294 CD2 LEU A 48 7006 7545 6525 -445 -848 254 C ATOM 295 N GLU A 49 1.482 44.715 14.457 1.00 40.02 N ANISOU 295 N GLU A 49 5870 5083 4253 -357 -840 -65 N ATOM 296 CA GLU A 49 0.461 44.686 13.414 1.00 39.07 C ANISOU 296 CA GLU A 49 5851 4836 4156 -55 -804 -75 C ATOM 297 C GLU A 49 0.305 46.065 12.755 1.00 48.20 C ANISOU 297 C GLU A 49 7336 5741 5237 -57 -703 -74 C ATOM 298 O GLU A 49 0.224 46.172 11.528 1.00 49.59 O ANISOU 298 O GLU A 49 7546 5886 5410 59 -660 0 O ATOM 299 CB GLU A 49 -0.893 44.205 13.955 1.00 43.74 C ANISOU 299 CB GLU A 49 6406 5437 4774 183 -857 -124 C ATOM 300 CG GLU A 49 -2.022 44.213 12.895 1.00 39.14 C ANISOU 300 CG GLU A 49 5908 4770 4193 465 -841 -93 C ATOM 301 CD GLU A 49 -3.360 43.703 13.428 1.00 48.85 C ANISOU 301 CD GLU A 49 7067 6038 5457 691 -906 -96 C ATOM 302 OE1 GLU A 49 -3.850 44.241 14.448 1.00 48.86 O ANISOU 302 OE1 GLU A 49 7179 5965 5420 710 -882 -134 O ATOM 303 OE2 GLU A 49 -3.936 42.768 12.817 1.00 51.29 O ANISOU 303 OE2 GLU A 49 7215 6450 5822 841 -973 -63 O ATOM 304 N GLU A 50 0.274 47.114 13.573 1.00 45.80 N ANISOU 304 N GLU A 50 7269 5260 4871 -198 -652 -154 N ATOM 305 CA GLU A 50 0.156 48.483 13.070 1.00 51.47 C ANISOU 305 CA GLU A 50 8306 5680 5569 -210 -521 -142 C ATOM 306 C GLU A 50 1.324 48.854 12.129 1.00 53.98 C ANISOU 306 C GLU A 50 8619 6001 5890 -393 -493 -28 C ATOM 307 O GLU A 50 1.111 49.435 11.058 1.00 46.27 O ANISOU 307 O GLU A 50 7753 4897 4930 -271 -413 82 O ATOM 308 CB GLU A 50 0.047 49.483 14.230 1.00 46.09 C ANISOU 308 CB GLU A 50 7899 4780 4833 -380 -440 -297 C ATOM 309 CG GLU A 50 -0.237 50.919 13.802 1.00 69.25 C ANISOU 309 CG GLU A 50 11184 7323 7803 -353 -257 -289 C ATOM 310 CD GLU A 50 -0.199 51.918 14.966 1.00 92.28 C ANISOU 310 CD GLU A 50 14414 9983 10668 -576 -140 -499 C ATOM 311 OE1 GLU A 50 -1.251 52.122 15.615 1.00 98.42 O ANISOU 311 OE1 GLU A 50 15330 10623 11442 -382 -42 -599 O ATOM 312 OE2 GLU A 50 0.878 52.510 15.224 1.00 95.18 O ANISOU 312 OE2 GLU A 50 14891 10285 10987 -957 -135 -565 O ATOM 313 N ARG A 51 2.548 48.511 12.526 1.00 44.52 N ANISOU 313 N ARG A 51 7261 4980 4675 -680 -557 -12 N ATOM 314 CA ARG A 51 3.704 48.760 11.681 1.00 44.14 C ANISOU 314 CA ARG A 51 7160 4978 4633 -848 -531 130 C ATOM 315 C ARG A 51 3.664 47.990 10.335 1.00 51.93 C ANISOU 315 C ARG A 51 7968 6113 5649 -611 -514 247 C ATOM 316 O ARG A 51 3.903 48.571 9.267 1.00 50.71 O ANISOU 316 O ARG A 51 7897 5893 5476 -586 -441 361 O ATOM 317 CB ARG A 51 4.991 48.451 12.434 1.00 42.84 C ANISOU 317 CB ARG A 51 6806 5026 4447 -1196 -606 175 C ATOM 318 CG ARG A 51 6.180 48.314 11.496 1.00 65.53 C ANISOU 318 CG ARG A 51 9512 8036 7349 -1301 -581 376 C ATOM 319 CD ARG A 51 7.347 49.154 11.926 1.00 70.80 C ANISOU 319 CD ARG A 51 10233 8696 7970 -1721 -600 455 C ATOM 320 NE ARG A 51 8.404 49.159 10.917 1.00 76.36 N ANISOU 320 NE ARG A 51 10794 9512 8707 -1786 -555 683 N ATOM 321 CZ ARG A 51 8.511 50.072 9.951 1.00 76.03 C ANISOU 321 CZ ARG A 51 10932 9287 8668 -1774 -471 766 C ATOM 322 NH1 ARG A 51 7.623 51.058 9.857 1.00 75.98 N ANISOU 322 NH1 ARG A 51 11252 8954 8663 -1692 -411 655 N ATOM 323 NH2 ARG A 51 9.507 50.004 9.082 1.00 69.88 N ANISOU 323 NH2 ARG A 51 9990 8657 7906 -1831 -428 992 N ATOM 324 N LEU A 52 3.350 46.699 10.381 1.00 45.28 N ANISOU 324 N LEU A 52 6890 5469 4847 -448 -571 213 N ATOM 325 CA LEU A 52 3.237 45.916 9.151 1.00 51.55 C ANISOU 325 CA LEU A 52 7550 6390 5646 -248 -538 260 C ATOM 326 C LEU A 52 2.149 46.457 8.206 1.00 52.56 C ANISOU 326 C LEU A 52 7860 6409 5701 -28 -504 275 C ATOM 327 O LEU A 52 2.342 46.484 6.986 1.00 55.31 O ANISOU 327 O LEU A 52 8197 6834 5984 30 -448 359 O ATOM 328 CB LEU A 52 3.023 44.424 9.445 1.00 41.09 C ANISOU 328 CB LEU A 52 5961 5240 4409 -129 -586 195 C ATOM 329 CG LEU A 52 4.153 43.771 10.247 1.00 44.55 C ANISOU 329 CG LEU A 52 6144 5836 4947 -318 -598 264 C ATOM 330 CD1 LEU A 52 3.943 42.270 10.390 1.00 44.54 C ANISOU 330 CD1 LEU A 52 5868 5966 5088 -166 -604 236 C ATOM 331 CD2 LEU A 52 5.497 44.065 9.625 1.00 42.48 C ANISOU 331 CD2 LEU A 52 5820 5645 4675 -486 -514 416 C ATOM 332 N GLU A 53 1.031 46.913 8.766 1.00 48.42 N ANISOU 332 N GLU A 53 7487 5731 5179 91 -525 224 N ATOM 333 CA GLU A 53 -0.054 47.447 7.950 1.00 48.70 C ANISOU 333 CA GLU A 53 7654 5686 5163 308 -488 308 C ATOM 334 C GLU A 53 0.361 48.748 7.276 1.00 52.10 C ANISOU 334 C GLU A 53 8267 5954 5573 233 -380 458 C ATOM 335 O GLU A 53 -0.026 49.026 6.136 1.00 56.56 O ANISOU 335 O GLU A 53 8845 6573 6073 362 -341 607 O ATOM 336 CB GLU A 53 -1.337 47.623 8.776 1.00 45.17 C ANISOU 336 CB GLU A 53 7299 5112 4750 476 -508 262 C ATOM 337 CG GLU A 53 -2.070 46.305 9.052 1.00 56.98 C ANISOU 337 CG GLU A 53 8589 6800 6262 619 -624 182 C ATOM 338 CD GLU A 53 -3.207 46.442 10.073 1.00 66.92 C ANISOU 338 CD GLU A 53 9908 7958 7560 766 -642 152 C ATOM 339 OE1 GLU A 53 -3.329 47.518 10.719 1.00 64.73 O ANISOU 339 OE1 GLU A 53 9848 7449 7298 741 -543 145 O ATOM 340 OE2 GLU A 53 -3.969 45.456 10.230 1.00 64.73 O ANISOU 340 OE2 GLU A 53 9461 7827 7304 902 -740 130 O ATOM 341 N ARG A 54 1.161 49.533 7.984 1.00 49.95 N ANISOU 341 N ARG A 54 8124 5502 5353 0 -334 432 N ATOM 342 CA ARG A 54 1.666 50.787 7.456 1.00 44.70 C ANISOU 342 CA ARG A 54 7633 4641 4709 -114 -226 575 C ATOM 343 C ARG A 54 2.546 50.490 6.235 1.00 49.11 C ANISOU 343 C ARG A 54 8031 5426 5201 -160 -222 722 C ATOM 344 O ARG A 54 2.437 51.151 5.195 1.00 51.69 O ANISOU 344 O ARG A 54 8411 5728 5501 -84 -148 912 O ATOM 345 CB ARG A 54 2.448 51.511 8.556 1.00 56.26 C ANISOU 345 CB ARG A 54 9252 5899 6225 -426 -202 475 C ATOM 346 CG ARG A 54 2.891 52.928 8.251 1.00 74.23 C ANISOU 346 CG ARG A 54 11759 7877 8567 -582 -77 589 C ATOM 347 CD ARG A 54 3.570 53.549 9.479 1.00 87.06 C ANISOU 347 CD ARG A 54 13558 9308 10213 -943 -70 425 C ATOM 348 NE ARG A 54 2.692 53.522 10.650 1.00 91.33 N ANISOU 348 NE ARG A 54 14238 9716 10746 -880 -54 202 N ATOM 349 CZ ARG A 54 3.002 52.972 11.823 1.00 92.80 C ANISOU 349 CZ ARG A 54 14358 10052 10852 -1078 -156 17 C ATOM 350 NH1 ARG A 54 4.189 52.403 12.014 1.00 89.77 N ANISOU 350 NH1 ARG A 54 13754 9946 10408 -1358 -281 53 N ATOM 351 NH2 ARG A 54 2.121 53.000 12.814 1.00 93.24 N ANISOU 351 NH2 ARG A 54 14545 9999 10885 -991 -121 -170 N ATOM 352 N CYS A 55 3.384 49.464 6.357 1.00 46.99 N ANISOU 352 N CYS A 55 7549 5393 4911 -263 -283 657 N ATOM 353 CA CYS A 55 4.289 49.062 5.280 1.00 45.81 C ANISOU 353 CA CYS A 55 7236 5470 4699 -295 -245 776 C ATOM 354 C CYS A 55 3.526 48.533 4.061 1.00 46.66 C ANISOU 354 C CYS A 55 7280 5762 4686 -50 -229 803 C ATOM 355 O CYS A 55 3.779 48.940 2.922 1.00 52.63 O ANISOU 355 O CYS A 55 8036 6614 5347 -29 -162 964 O ATOM 356 CB CYS A 55 5.280 48.020 5.804 1.00 45.86 C ANISOU 356 CB CYS A 55 7012 5663 4749 -427 -277 716 C ATOM 357 SG CYS A 55 6.490 48.690 7.045 1.00 51.60 S ANISOU 357 SG CYS A 55 7755 6297 5553 -818 -313 764 S ATOM 358 N MET A 56 2.567 47.649 4.301 1.00 43.60 N ANISOU 358 N MET A 56 6835 5445 4286 114 -298 656 N ATOM 359 CA MET A 56 1.737 47.129 3.220 1.00 46.63 C ANISOU 359 CA MET A 56 7168 6023 4527 298 -309 660 C ATOM 360 C MET A 56 1.068 48.283 2.450 1.00 54.35 C ANISOU 360 C MET A 56 8278 6948 5424 387 -272 881 C ATOM 361 O MET A 56 1.029 48.288 1.211 1.00 53.52 O ANISOU 361 O MET A 56 8123 7060 5153 431 -240 999 O ATOM 362 CB MET A 56 0.702 46.150 3.778 1.00 46.16 C ANISOU 362 CB MET A 56 7043 6000 4496 429 -408 490 C ATOM 363 CG MET A 56 -0.239 45.577 2.759 1.00 51.96 C ANISOU 363 CG MET A 56 7726 6948 5067 567 -448 478 C ATOM 364 SD MET A 56 -1.262 44.228 3.407 1.00 74.17 S ANISOU 364 SD MET A 56 10424 9814 7942 670 -571 272 S ATOM 365 CE MET A 56 -2.094 45.061 4.767 1.00 62.46 C ANISOU 365 CE MET A 56 9054 8077 6603 753 -625 345 C ATOM 366 N SER A 57 0.596 49.288 3.181 1.00 49.52 N ANISOU 366 N SER A 57 7831 6051 4934 406 -253 953 N ATOM 367 CA SER A 57 -0.058 50.423 2.549 1.00 51.56 C ANISOU 367 CA SER A 57 8199 6210 5182 516 -182 1210 C ATOM 368 C SER A 57 0.949 51.275 1.750 1.00 56.63 C ANISOU 368 C SER A 57 8865 6842 5812 386 -85 1416 C ATOM 369 O SER A 57 0.586 51.879 0.728 1.00 55.18 O ANISOU 369 O SER A 57 8667 6747 5553 480 -32 1679 O ATOM 370 CB SER A 57 -0.839 51.246 3.579 1.00 53.16 C ANISOU 370 CB SER A 57 8586 6059 5552 596 -133 1218 C ATOM 371 OG SER A 57 -0.150 52.433 3.898 1.00 68.54 O ANISOU 371 OG SER A 57 10713 7694 7636 446 -15 1292 O ATOM 372 N ILE A 58 2.214 51.294 2.175 1.00 54.31 N ANISOU 372 N ILE A 58 8571 6483 5583 164 -67 1339 N ATOM 373 CA ILE A 58 3.244 51.965 1.376 1.00 53.24 C ANISOU 373 CA ILE A 58 8415 6386 5428 30 13 1552 C ATOM 374 C ILE A 58 3.458 51.220 0.047 1.00 54.96 C ANISOU 374 C ILE A 58 8445 7014 5422 103 17 1618 C ATOM 375 O ILE A 58 3.477 51.830 -1.025 1.00 55.33 O ANISOU 375 O ILE A 58 8466 7183 5374 141 79 1874 O ATOM 376 CB ILE A 58 4.578 52.100 2.137 1.00 50.86 C ANISOU 376 CB ILE A 58 8122 5971 5233 -251 16 1487 C ATOM 377 CG1 ILE A 58 4.464 53.185 3.215 1.00 56.24 C ANISOU 377 CG1 ILE A 58 9041 6234 6095 -387 46 1455 C ATOM 378 CG2 ILE A 58 5.742 52.378 1.173 1.00 52.64 C ANISOU 378 CG2 ILE A 58 8238 6363 5401 -374 80 1708 C ATOM 379 CD1 ILE A 58 5.643 53.200 4.223 1.00 52.10 C ANISOU 379 CD1 ILE A 58 8521 5636 5638 -720 4 1344 C ATOM 380 N VAL A 59 3.610 49.899 0.124 1.00 51.75 N ANISOU 380 N VAL A 59 7908 6820 4934 119 -30 1387 N ATOM 381 CA VAL A 59 3.780 49.085 -1.077 1.00 56.32 C ANISOU 381 CA VAL A 59 8345 7767 5289 177 5 1371 C ATOM 382 C VAL A 59 2.561 49.236 -1.998 1.00 58.95 C ANISOU 382 C VAL A 59 8684 8284 5430 332 -29 1482 C ATOM 383 O VAL A 59 2.695 49.387 -3.209 1.00 62.97 O ANISOU 383 O VAL A 59 9127 9070 5729 341 22 1641 O ATOM 384 CB VAL A 59 3.983 47.603 -0.701 1.00 50.50 C ANISOU 384 CB VAL A 59 7493 7141 4554 186 -13 1073 C ATOM 385 CG1 VAL A 59 3.804 46.707 -1.920 1.00 50.90 C ANISOU 385 CG1 VAL A 59 7454 7531 4355 260 37 978 C ATOM 386 CG2 VAL A 59 5.369 47.395 -0.061 1.00 54.28 C ANISOU 386 CG2 VAL A 59 7886 7552 5187 29 46 1061 C ATOM 387 N THR A 60 1.380 49.215 -1.391 1.00 49.67 N ANISOU 387 N THR A 60 7571 6983 4319 444 -117 1427 N ATOM 388 CA THR A 60 0.110 49.280 -2.099 1.00 51.81 C ANISOU 388 CA THR A 60 7814 7447 4424 584 -174 1561 C ATOM 389 C THR A 60 -0.075 50.602 -2.850 1.00 53.39 C ANISOU 389 C THR A 60 8034 7652 4601 629 -104 1965 C ATOM 390 O THR A 60 -0.639 50.634 -3.947 1.00 57.12 O ANISOU 390 O THR A 60 8407 8459 4839 684 -123 2158 O ATOM 391 CB THR A 60 -1.049 49.036 -1.101 1.00 54.62 C ANISOU 391 CB THR A 60 8217 7631 4907 702 -270 1455 C ATOM 392 OG1 THR A 60 -1.222 47.623 -0.944 1.00 60.28 O ANISOU 392 OG1 THR A 60 8847 8508 5549 689 -355 1151 O ATOM 393 CG2 THR A 60 -2.350 49.663 -1.580 1.00 62.95 C ANISOU 393 CG2 THR A 60 9259 8769 5892 859 -298 1746 C ATOM 394 N SER A 61 0.428 51.683 -2.262 1.00 57.89 N ANISOU 394 N SER A 61 8723 7858 5413 583 -17 2100 N ATOM 395 CA SER A 61 0.379 52.995 -2.891 1.00 60.86 C ANISOU 395 CA SER A 61 9121 8157 5845 619 84 2503 C ATOM 396 C SER A 61 1.155 52.993 -4.215 1.00 66.79 C ANISOU 396 C SER A 61 9730 9281 6367 542 124 2682 C ATOM 397 O SER A 61 0.874 53.803 -5.100 1.00 73.82 O ANISOU 397 O SER A 61 10553 10299 7197 603 179 3062 O ATOM 398 CB SER A 61 0.932 54.062 -1.943 1.00 57.42 C ANISOU 398 CB SER A 61 8872 7217 5729 528 183 2540 C ATOM 399 OG SER A 61 2.350 54.017 -1.887 1.00 66.08 O ANISOU 399 OG SER A 61 9960 8301 6845 310 206 2459 O ATOM 400 N MET A 62 2.109 52.070 -4.360 1.00 65.62 N ANISOU 400 N MET A 62 9519 9321 6092 422 116 2434 N ATOM 401 CA MET A 62 2.915 51.982 -5.590 1.00 70.10 C ANISOU 401 CA MET A 62 9955 10258 6422 357 184 2571 C ATOM 402 C MET A 62 2.516 50.842 -6.523 1.00 59.91 C ANISOU 402 C MET A 62 8551 9448 4765 389 144 2401 C ATOM 403 O MET A 62 2.915 50.822 -7.680 1.00 62.14 O ANISOU 403 O MET A 62 8728 10101 4782 355 207 2534 O ATOM 404 CB MET A 62 4.402 51.847 -5.253 1.00 64.79 C ANISOU 404 CB MET A 62 9275 9483 5859 200 256 2474 C ATOM 405 CG MET A 62 5.087 53.144 -4.861 1.00 68.99 C ANISOU 405 CG MET A 62 9882 9678 6653 89 317 2738 C ATOM 406 SD MET A 62 6.741 52.855 -4.162 1.00 67.40 S ANISOU 406 SD MET A 62 9652 9360 6597 -137 353 2609 S ATOM 407 CE MET A 62 6.371 52.890 -2.403 1.00 57.34 C ANISOU 407 CE MET A 62 8557 7627 5602 -208 263 2341 C ATOM 408 N THR A 63 1.749 49.876 -6.025 1.00 57.92 N ANISOU 408 N THR A 63 8325 9197 4487 435 47 2095 N ATOM 409 CA THR A 63 1.427 48.715 -6.859 1.00 67.63 C ANISOU 409 CA THR A 63 9478 10843 5377 416 19 1869 C ATOM 410 C THR A 63 -0.012 48.687 -7.414 1.00 68.16 C ANISOU 410 C THR A 63 9493 11187 5216 474 -107 1988 C ATOM 411 O THR A 63 -0.254 48.108 -8.470 1.00 67.42 O ANISOU 411 O THR A 63 9325 11539 4753 408 -122 1928 O ATOM 412 CB THR A 63 1.802 47.387 -6.166 1.00 56.12 C ANISOU 412 CB THR A 63 8044 9273 4006 382 27 1420 C ATOM 413 OG1 THR A 63 1.074 47.258 -4.936 1.00 53.98 O ANISOU 413 OG1 THR A 63 7836 8686 3986 445 -85 1308 O ATOM 414 CG2 THR A 63 3.316 47.348 -5.868 1.00 68.74 C ANISOU 414 CG2 THR A 63 9627 10726 5766 312 168 1377 C ATOM 415 N ALA A 64 -0.950 49.322 -6.712 1.00 71.52 N ANISOU 415 N ALA A 64 9955 11369 5849 585 -185 2170 N ATOM 416 CA ALA A 64 -2.361 49.364 -7.147 1.00 68.32 C ANISOU 416 CA ALA A 64 9465 11228 5267 654 -306 2366 C ATOM 417 C ALA A 64 -2.594 50.224 -8.394 1.00 66.55 C ANISOU 417 C ALA A 64 9104 11382 4802 657 -280 2834 C ATOM 418 O ALA A 64 -1.970 51.284 -8.563 1.00 66.69 O ANISOU 418 O ALA A 64 9120 11258 4961 685 -163 3141 O ATOM 419 CB ALA A 64 -3.273 49.826 -5.994 1.00 59.70 C ANISOU 419 CB ALA A 64 8438 9750 4494 808 -355 2463 C ATOM 420 N GLY A 65 -3.465 49.750 -9.287 1.00 65.95 N ANISOU 420 N GLY A 65 8896 11810 4350 601 -394 2902 N ATOM 421 CA GLY A 65 -3.847 50.515 -10.469 1.00 69.78 C ANISOU 421 CA GLY A 65 9202 12610 4703 574 -385 3290 C ATOM 422 C GLY A 65 -2.805 50.614 -11.574 1.00 72.13 C ANISOU 422 C GLY A 65 9438 13202 4764 451 -279 3309 C ATOM 423 O GLY A 65 -2.981 51.370 -12.542 1.00 75.51 O ANISOU 423 O GLY A 65 9697 13849 5146 434 -255 3642 O ATOM 424 N VAL A 66 -1.740 49.824 -11.449 1.00 82.02 N ANISOU 424 N VAL A 66 10807 14485 5873 372 -205 2958 N ATOM 425 CA VAL A 66 -0.572 49.906 -12.333 1.00 72.56 C ANISOU 425 CA VAL A 66 9569 13508 4493 283 -63 2965 C ATOM 426 C VAL A 66 -0.216 48.473 -12.811 1.00 72.80 C ANISOU 426 C VAL A 66 9654 13821 4184 139 -31 2438 C ATOM 427 O VAL A 66 -0.624 47.506 -12.166 1.00 70.66 O ANISOU 427 O VAL A 66 9480 13458 3907 123 -99 2076 O ATOM 428 CB VAL A 66 0.580 50.586 -11.529 1.00 80.44 C ANISOU 428 CB VAL A 66 10657 14061 5845 354 70 3074 C ATOM 429 CG1 VAL A 66 1.571 49.555 -10.954 1.00 68.30 C ANISOU 429 CG1 VAL A 66 9235 12311 4404 296 151 2567 C ATOM 430 CG2 VAL A 66 1.268 51.665 -12.328 1.00 74.74 C ANISOU 430 CG2 VAL A 66 9819 13482 5096 349 180 3527 C ATOM 431 N SER A 67 0.516 48.299 -13.915 1.00 75.62 N ANISOU 431 N SER A 67 9957 14494 4282 39 89 2377 N ATOM 432 CA SER A 67 0.892 46.932 -14.335 1.00 76.28 C ANISOU 432 CA SER A 67 10129 14769 4085 -83 178 1846 C ATOM 433 C SER A 67 1.994 46.326 -13.438 1.00 73.37 C ANISOU 433 C SER A 67 9882 14119 3875 -22 343 1559 C ATOM 434 O SER A 67 2.595 47.033 -12.629 1.00 71.24 O ANISOU 434 O SER A 67 9616 13439 4014 81 374 1758 O ATOM 435 CB SER A 67 1.318 46.879 -15.804 1.00 80.67 C ANISOU 435 CB SER A 67 10601 15739 4312 -199 283 1841 C ATOM 436 OG SER A 67 2.713 47.085 -15.945 1.00 92.94 O ANISOU 436 OG SER A 67 12154 17275 5884 -150 499 1894 O ATOM 437 N GLU A 68 2.250 45.024 -13.568 1.00 83.86 N ANISOU 437 N GLU A 68 11304 15491 5066 -94 452 1048 N ATOM 438 CA GLU A 68 3.248 44.351 -12.717 1.00 77.84 C ANISOU 438 CA GLU A 68 10616 14293 4667 -20 618 749 C ATOM 439 C GLU A 68 4.679 44.823 -12.996 1.00 74.01 C ANISOU 439 C GLU A 68 10067 13803 4249 30 837 941 C ATOM 440 O GLU A 68 5.485 44.935 -12.070 1.00 69.79 O ANISOU 440 O GLU A 68 9526 12870 4122 106 900 978 O ATOM 441 CB GLU A 68 3.173 42.821 -12.843 1.00 79.82 C ANISOU 441 CB GLU A 68 10973 14563 4791 -93 729 177 C ATOM 442 CG GLU A 68 2.195 42.137 -11.886 1.00 84.03 C ANISOU 442 CG GLU A 68 11571 14805 5553 -95 553 -71 C ATOM 443 CD GLU A 68 2.002 40.654 -12.199 1.00 96.84 C ANISOU 443 CD GLU A 68 13302 16481 7011 -205 663 -623 C ATOM 444 OE1 GLU A 68 3.002 39.900 -12.221 1.00 99.80 O ANISOU 444 OE1 GLU A 68 13722 16707 7493 -163 941 -895 O ATOM 445 OE2 GLU A 68 0.844 40.246 -12.435 1.00102.18 O ANISOU 445 OE2 GLU A 68 14015 17343 7464 -338 485 -768 O ATOM 446 N ARG A 69 4.988 45.108 -14.259 1.00 75.83 N ANISOU 446 N ARG A 69 10232 14510 4069 -27 944 1091 N ATOM 447 CA ARG A 69 6.301 45.652 -14.578 1.00 80.67 C ANISOU 447 CA ARG A 69 10755 15160 4736 23 1140 1346 C ATOM 448 C ARG A 69 6.436 47.056 -13.992 1.00 78.75 C ANISOU 448 C ARG A 69 10431 14660 4831 74 1011 1861 C ATOM 449 O ARG A 69 7.457 47.380 -13.384 1.00 74.22 O ANISOU 449 O ARG A 69 9825 13786 4590 114 1098 1988 O ATOM 450 CB ARG A 69 6.563 45.667 -16.091 1.00 81.63 C ANISOU 450 CB ARG A 69 10814 15804 4396 -50 1271 1391 C ATOM 451 CG ARG A 69 8.036 45.769 -16.457 1.00103.18 C ANISOU 451 CG ARG A 69 13464 18601 7139 12 1548 1514 C ATOM 452 CD ARG A 69 8.259 45.709 -17.971 1.00113.27 C ANISOU 452 CD ARG A 69 14697 20275 8066 -56 1658 1488 C ATOM 453 NE ARG A 69 9.661 45.470 -18.319 1.00119.79 N ANISOU 453 NE ARG A 69 15470 21157 8885 19 1971 1491 N ATOM 454 CZ ARG A 69 10.140 45.467 -19.562 1.00126.67 C ANISOU 454 CZ ARG A 69 16293 22356 9481 -9 2119 1508 C ATOM 455 NH1 ARG A 69 9.336 45.701 -20.591 1.00129.24 N ANISOU 455 NH1 ARG A 69 16600 23006 9498 -127 1973 1529 N ATOM 456 NH2 ARG A 69 11.429 45.236 -19.780 1.00127.92 N ANISOU 456 NH2 ARG A 69 16397 22533 9675 83 2418 1532 N ATOM 457 N GLU A 70 5.396 47.873 -14.162 1.00 78.90 N ANISOU 457 N GLU A 70 10414 14790 4776 63 814 2161 N ATOM 458 CA GLU A 70 5.398 49.239 -13.644 1.00 76.10 C ANISOU 458 CA GLU A 70 10007 14149 4757 114 723 2638 C ATOM 459 C GLU A 70 5.531 49.239 -12.134 1.00 72.27 C ANISOU 459 C GLU A 70 9633 13051 4777 156 664 2497 C ATOM 460 O GLU A 70 6.201 50.097 -11.567 1.00 73.98 O ANISOU 460 O GLU A 70 9841 12950 5317 156 685 2750 O ATOM 461 CB GLU A 70 4.124 49.980 -14.048 1.00 76.47 C ANISOU 461 CB GLU A 70 9990 14385 4682 125 552 2964 C ATOM 462 CG GLU A 70 3.908 50.050 -15.555 1.00 80.75 C ANISOU 462 CG GLU A 70 10387 15384 4910 50 557 3033 C ATOM 463 CD GLU A 70 2.585 50.714 -15.947 1.00 89.95 C ANISOU 463 CD GLU A 70 11438 16654 6086 56 378 3311 C ATOM 464 OE1 GLU A 70 2.125 51.641 -15.247 1.00 84.70 O ANISOU 464 OE1 GLU A 70 10763 15668 5750 155 310 3637 O ATOM 465 OE2 GLU A 70 2.006 50.312 -16.974 1.00 97.01 O ANISOU 465 OE2 GLU A 70 12242 17950 6667 -43 324 3212 O ATOM 466 N ALA A 71 4.887 48.269 -11.490 1.00 70.58 N ANISOU 466 N ALA A 71 9516 12689 4614 169 587 2096 N ATOM 467 CA ALA A 71 4.936 48.136 -10.041 1.00 67.57 C ANISOU 467 CA ALA A 71 9224 11787 4664 201 524 1938 C ATOM 468 C ALA A 71 6.359 47.819 -9.541 1.00 67.54 C ANISOU 468 C ALA A 71 9197 11582 4882 174 678 1843 C ATOM 469 O ALA A 71 6.852 48.455 -8.612 1.00 63.07 O ANISOU 469 O ALA A 71 8647 10663 4655 148 648 1989 O ATOM 470 CB ALA A 71 3.926 47.085 -9.560 1.00 63.59 C ANISOU 470 CB ALA A 71 8793 11227 4140 221 414 1555 C ATOM 471 N ASN A 72 7.008 46.836 -10.157 1.00 72.58 N ANISOU 471 N ASN A 72 9795 12456 5326 171 854 1607 N ATOM 472 CA ASN A 72 8.392 46.500 -9.822 1.00 75.11 C ANISOU 472 CA ASN A 72 10045 12652 5840 168 1035 1586 C ATOM 473 C ASN A 72 9.380 47.652 -10.053 1.00 75.03 C ANISOU 473 C ASN A 72 9938 12661 5909 119 1088 2030 C ATOM 474 O ASN A 72 10.258 47.888 -9.223 1.00 65.99 O ANISOU 474 O ASN A 72 8746 11252 5075 69 1107 2142 O ATOM 475 CB ASN A 72 8.831 45.225 -10.551 1.00 74.30 C ANISOU 475 CB ASN A 72 9924 12795 5510 205 1270 1257 C ATOM 476 CG ASN A 72 8.163 43.980 -9.984 1.00 78.54 C ANISOU 476 CG ASN A 72 10548 13166 6128 235 1248 806 C ATOM 477 OD1 ASN A 72 7.859 43.916 -8.789 1.00 72.74 O ANISOU 477 OD1 ASN A 72 9834 12085 5720 244 1109 758 O ATOM 478 ND2 ASN A 72 7.928 42.987 -10.838 1.00 87.42 N ANISOU 478 ND2 ASN A 72 11727 14539 6951 234 1394 469 N ATOM 479 N ASP A 73 9.219 48.373 -11.164 1.00 69.83 N ANISOU 479 N ASP A 73 9231 12332 4969 112 1101 2306 N ATOM 480 CA ASP A 73 10.004 49.586 -11.399 1.00 74.11 C ANISOU 480 CA ASP A 73 9676 12874 5609 59 1127 2777 C ATOM 481 C ASP A 73 9.814 50.578 -10.261 1.00 78.68 C ANISOU 481 C ASP A 73 10329 12979 6587 -5 964 2962 C ATOM 482 O ASP A 73 10.772 51.180 -9.784 1.00 69.61 O ANISOU 482 O ASP A 73 9136 11626 5688 -102 989 3180 O ATOM 483 CB ASP A 73 9.630 50.253 -12.723 1.00 74.72 C ANISOU 483 CB ASP A 73 9675 13382 5334 70 1139 3084 C ATOM 484 CG ASP A 73 10.031 49.428 -13.920 1.00 85.28 C ANISOU 484 CG ASP A 73 10939 15225 6237 96 1336 2932 C ATOM 485 OD1 ASP A 73 10.771 48.441 -13.733 1.00 84.19 O ANISOU 485 OD1 ASP A 73 10807 15051 6131 125 1505 2637 O ATOM 486 OD2 ASP A 73 9.617 49.772 -15.050 1.00 88.18 O ANISOU 486 OD2 ASP A 73 11237 16037 6230 88 1339 3122 O ATOM 487 N ALA A 74 8.572 50.734 -9.818 1.00 68.01 N ANISOU 487 N ALA A 74 9094 11460 5287 35 806 2871 N ATOM 488 CA ALA A 74 8.277 51.673 -8.740 1.00 66.58 C ANISOU 488 CA ALA A 74 9019 10812 5466 -11 687 3003 C ATOM 489 C ALA A 74 8.892 51.242 -7.399 1.00 66.54 C ANISOU 489 C ALA A 74 9068 10453 5762 -97 663 2769 C ATOM 490 O ALA A 74 9.422 52.078 -6.669 1.00 63.97 O ANISOU 490 O ALA A 74 8784 9816 5707 -226 634 2936 O ATOM 491 CB ALA A 74 6.783 51.889 -8.606 1.00 65.92 C ANISOU 491 CB ALA A 74 9028 10657 5360 85 558 2981 C ATOM 492 N LEU A 75 8.831 49.946 -7.088 1.00 64.75 N ANISOU 492 N LEU A 75 8831 10286 5485 -46 680 2399 N ATOM 493 CA LEU A 75 9.394 49.417 -5.839 1.00 68.20 C ANISOU 493 CA LEU A 75 9267 10455 6191 -119 661 2211 C ATOM 494 C LEU A 75 10.924 49.461 -5.870 1.00 70.86 C ANISOU 494 C LEU A 75 9456 10854 6613 -230 787 2396 C ATOM 495 O LEU A 75 11.564 49.797 -4.873 1.00 61.72 O ANISOU 495 O LEU A 75 8286 9460 5707 -382 734 2473 O ATOM 496 CB LEU A 75 8.926 47.979 -5.581 1.00 58.19 C ANISOU 496 CB LEU A 75 7994 9242 4874 -18 671 1812 C ATOM 497 CG LEU A 75 7.421 47.732 -5.459 1.00 67.29 C ANISOU 497 CG LEU A 75 9263 10357 5948 77 534 1615 C ATOM 498 CD1 LEU A 75 7.141 46.247 -5.210 1.00 55.46 C ANISOU 498 CD1 LEU A 75 7740 8897 4435 145 562 1230 C ATOM 499 CD2 LEU A 75 6.804 48.598 -4.353 1.00 62.44 C ANISOU 499 CD2 LEU A 75 8768 9380 5574 43 379 1692 C ATOM 500 N ASN A 76 11.503 49.112 -7.016 1.00 76.42 N ANISOU 500 N ASN A 76 10041 11905 7090 -166 956 2474 N ATOM 501 CA ASN A 76 12.950 49.165 -7.172 1.00 81.26 C ANISOU 501 CA ASN A 76 10482 12623 7768 -243 1100 2708 C ATOM 502 C ASN A 76 13.461 50.562 -6.852 1.00 78.19 C ANISOU 502 C ASN A 76 10095 12052 7561 -433 1006 3087 C ATOM 503 O ASN A 76 14.291 50.736 -5.952 1.00 69.46 O ANISOU 503 O ASN A 76 8929 10771 6693 -603 970 3187 O ATOM 504 CB ASN A 76 13.366 48.730 -8.578 1.00 87.28 C ANISOU 504 CB ASN A 76 11138 13808 8217 -127 1317 2754 C ATOM 505 CG ASN A 76 13.370 47.218 -8.743 1.00 97.63 C ANISOU 505 CG ASN A 76 12425 15243 9429 13 1490 2374 C ATOM 506 OD1 ASN A 76 13.707 46.482 -7.809 1.00100.35 O ANISOU 506 OD1 ASN A 76 12722 15392 10016 14 1514 2223 O ATOM 507 ND2 ASN A 76 12.993 46.746 -9.932 1.00100.14 N ANISOU 507 ND2 ASN A 76 12771 15888 9388 117 1621 2222 N ATOM 508 N ALA A 77 12.920 51.546 -7.567 1.00 77.10 N ANISOU 508 N ALA A 77 10022 11956 7318 -419 966 3305 N ATOM 509 CA ALA A 77 13.231 52.954 -7.347 1.00 77.96 C ANISOU 509 CA ALA A 77 10165 11835 7622 -591 895 3661 C ATOM 510 C ALA A 77 13.146 53.330 -5.869 1.00 78.44 C ANISOU 510 C ALA A 77 10368 11442 7993 -768 752 3544 C ATOM 511 O ALA A 77 14.109 53.838 -5.286 1.00 85.21 O ANISOU 511 O ALA A 77 11183 12151 9041 -999 728 3717 O ATOM 512 CB ALA A 77 12.297 53.819 -8.157 1.00 70.56 C ANISOU 512 CB ALA A 77 9294 10943 6572 -501 870 3860 C ATOM 513 N TYR A 78 11.997 53.055 -5.266 1.00 68.14 N ANISOU 513 N TYR A 78 9225 9948 6716 -676 657 3251 N ATOM 514 CA TYR A 78 11.735 53.433 -3.878 1.00 68.09 C ANISOU 514 CA TYR A 78 9383 9528 6962 -824 535 3107 C ATOM 515 C TYR A 78 12.745 52.833 -2.875 1.00 71.68 C ANISOU 515 C TYR A 78 9737 9956 7543 -1012 506 3006 C ATOM 516 O TYR A 78 13.180 53.514 -1.941 1.00 68.91 O ANISOU 516 O TYR A 78 9461 9345 7379 -1271 426 3061 O ATOM 517 CB TYR A 78 10.287 53.069 -3.495 1.00 61.34 C ANISOU 517 CB TYR A 78 8680 8548 6079 -646 459 2818 C ATOM 518 CG TYR A 78 9.888 53.558 -2.124 1.00 60.22 C ANISOU 518 CG TYR A 78 8730 7985 6167 -772 360 2672 C ATOM 519 CD1 TYR A 78 9.409 54.844 -1.937 1.00 61.78 C ANISOU 519 CD1 TYR A 78 9116 7842 6516 -825 361 2818 C ATOM 520 CD2 TYR A 78 9.995 52.731 -1.012 1.00 57.97 C ANISOU 520 CD2 TYR A 78 8433 7642 5949 -837 288 2393 C ATOM 521 CE1 TYR A 78 9.047 55.297 -0.677 1.00 62.05 C ANISOU 521 CE1 TYR A 78 9356 7480 6740 -946 307 2644 C ATOM 522 CE2 TYR A 78 9.630 53.170 0.249 1.00 57.99 C ANISOU 522 CE2 TYR A 78 8614 7304 6116 -967 204 2244 C ATOM 523 CZ TYR A 78 9.161 54.457 0.411 1.00 64.71 C ANISOU 523 CZ TYR A 78 9684 7813 7092 -1025 221 2347 C ATOM 524 OH TYR A 78 8.800 54.890 1.669 1.00 70.18 O ANISOU 524 OH TYR A 78 10582 8157 7927 -1159 173 2159 O ATOM 525 N VAL A 79 13.106 51.567 -3.082 1.00 61.50 N ANISOU 525 N VAL A 79 8276 8942 6151 -892 583 2872 N ATOM 526 CA VAL A 79 14.033 50.854 -2.207 1.00 64.66 C ANISOU 526 CA VAL A 79 8517 9373 6676 -1023 583 2833 C ATOM 527 C VAL A 79 15.431 51.482 -2.230 1.00 74.81 C ANISOU 527 C VAL A 79 9649 10729 8047 -1272 612 3200 C ATOM 528 O VAL A 79 16.124 51.542 -1.207 1.00 68.75 O ANISOU 528 O VAL A 79 8810 9882 7429 -1522 528 3260 O ATOM 529 CB VAL A 79 14.101 49.347 -2.582 1.00 75.61 C ANISOU 529 CB VAL A 79 9744 11016 7968 -796 722 2643 C ATOM 530 CG1 VAL A 79 15.424 48.712 -2.146 1.00 71.71 C ANISOU 530 CG1 VAL A 79 8988 10659 7601 -895 813 2794 C ATOM 531 CG2 VAL A 79 12.919 48.595 -1.973 1.00 76.51 C ANISOU 531 CG2 VAL A 79 9975 10999 8096 -659 638 2270 C ATOM 532 N CYS A 80 15.825 51.961 -3.405 1.00 83.94 N ANISOU 532 N CYS A 80 10737 12065 9090 -1219 720 3468 N ATOM 533 CA CYS A 80 17.138 52.562 -3.606 1.00 89.27 C ANISOU 533 CA CYS A 80 11240 12847 9832 -1434 758 3866 C ATOM 534 C CYS A 80 17.360 53.822 -2.771 1.00 97.01 C ANISOU 534 C CYS A 80 12354 13501 11005 -1791 597 4009 C ATOM 535 O CYS A 80 18.503 54.184 -2.486 1.00102.51 O ANISOU 535 O CYS A 80 12900 14250 11799 -2066 571 4290 O ATOM 536 CB CYS A 80 17.342 52.882 -5.086 1.00 87.18 C ANISOU 536 CB CYS A 80 10889 12848 9386 -1284 906 4124 C ATOM 537 SG CYS A 80 17.402 51.416 -6.119 1.00 89.01 S ANISOU 537 SG CYS A 80 10959 13500 9360 -937 1147 3963 S ATOM 538 N LYS A 81 16.273 54.481 -2.375 1.00 96.21 N ANISOU 538 N LYS A 81 12533 13060 10961 -1797 501 3819 N ATOM 539 CA LYS A 81 16.376 55.725 -1.615 1.00 93.38 C ANISOU 539 CA LYS A 81 12363 12326 10791 -2130 391 3897 C ATOM 540 C LYS A 81 17.091 55.520 -0.279 1.00 86.35 C ANISOU 540 C LYS A 81 11429 11379 10003 -2470 268 3816 C ATOM 541 O LYS A 81 17.733 56.429 0.240 1.00 88.47 O ANISOU 541 O LYS A 81 11754 11469 10391 -2849 189 3967 O ATOM 542 CB LYS A 81 14.999 56.376 -1.419 1.00 91.95 C ANISOU 542 CB LYS A 81 12495 11775 10667 -2017 365 3691 C ATOM 543 CG LYS A 81 14.370 56.873 -2.725 1.00 97.83 C ANISOU 543 CG LYS A 81 13257 12580 11335 -1757 470 3892 C ATOM 544 CD LYS A 81 13.378 58.017 -2.505 1.00103.82 C ANISOU 544 CD LYS A 81 14296 12891 12259 -1752 473 3886 C ATOM 545 CE LYS A 81 12.161 57.576 -1.700 1.00106.57 C ANISOU 545 CE LYS A 81 14834 13049 12609 -1596 424 3499 C ATOM 546 NZ LYS A 81 11.092 58.622 -1.663 1.00108.27 N ANISOU 546 NZ LYS A 81 15293 12864 12981 -1501 483 3538 N ATOM 547 N GLY A 82 17.005 54.316 0.266 1.00 78.93 N ANISOU 547 N GLY A 82 10371 10609 9011 -2356 253 3597 N ATOM 548 CA GLY A 82 17.698 54.044 1.505 1.00 80.73 C ANISOU 548 CA GLY A 82 10497 10865 9310 -2673 134 3575 C ATOM 549 C GLY A 82 17.261 52.781 2.214 1.00 80.95 C ANISOU 549 C GLY A 82 10440 11003 9314 -2507 114 3298 C ATOM 550 O GLY A 82 16.304 52.109 1.811 1.00 80.63 O ANISOU 550 O GLY A 82 10462 10966 9210 -2151 181 3065 O ATOM 551 N LEU A 83 17.970 52.471 3.290 1.00 82.70 N ANISOU 551 N LEU A 83 12669 7653 11101 -1928 3084 3503 N ATOM 552 CA LEU A 83 17.744 51.249 4.040 1.00 77.65 C ANISOU 552 CA LEU A 83 11861 7218 10425 -1881 2936 3267 C ATOM 553 C LEU A 83 16.413 51.174 4.833 1.00 76.20 C ANISOU 553 C LEU A 83 11907 7014 10033 -1749 2598 3037 C ATOM 554 O LEU A 83 15.864 50.080 4.999 1.00 65.99 O ANISOU 554 O LEU A 83 10619 5939 8515 -1583 2544 2861 O ATOM 555 CB LEU A 83 18.980 50.950 4.903 1.00 81.93 C ANISOU 555 CB LEU A 83 11946 7741 11444 -2198 2890 3245 C ATOM 556 CG LEU A 83 18.925 50.814 6.421 1.00 83.39 C ANISOU 556 CG LEU A 83 11961 7836 11885 -2395 2507 3032 C ATOM 557 CD1 LEU A 83 18.597 49.376 6.830 1.00 78.43 C ANISOU 557 CD1 LEU A 83 11212 7478 11110 -2250 2458 2831 C ATOM 558 CD2 LEU A 83 20.253 51.268 7.023 1.00 85.51 C ANISOU 558 CD2 LEU A 83 11886 7949 12655 -2757 2445 3079 C ATOM 559 N PRO A 84 15.885 52.320 5.322 1.00 78.21 N ANISOU 559 N PRO A 84 12356 6998 10360 -1809 2378 3031 N ATOM 560 CA PRO A 84 14.557 52.190 5.943 1.00 68.82 C ANISOU 560 CA PRO A 84 11415 5818 8914 -1619 2106 2803 C ATOM 561 C PRO A 84 13.460 51.949 4.890 1.00 70.45 C ANISOU 561 C PRO A 84 11957 6197 8612 -1255 2180 2793 C ATOM 562 O PRO A 84 12.501 51.216 5.164 1.00 63.55 O ANISOU 562 O PRO A 84 11191 5483 7471 -1065 2020 2596 O ATOM 563 CB PRO A 84 14.350 53.549 6.628 1.00 67.89 C ANISOU 563 CB PRO A 84 11435 5352 9008 -1745 1882 2802 C ATOM 564 CG PRO A 84 15.716 54.147 6.746 1.00 74.86 C ANISOU 564 CG PRO A 84 12039 6044 10360 -2087 1947 2981 C ATOM 565 CD PRO A 84 16.461 53.662 5.544 1.00 74.04 C ANISOU 565 CD PRO A 84 11811 6142 10178 -2061 2317 3183 C ATOM 566 N GLN A 85 13.605 52.545 3.706 1.00 68.97 N ANISOU 566 N GLN A 85 11929 5976 8300 -1165 2396 2999 N ATOM 567 CA GLN A 85 12.678 52.279 2.609 1.00 68.85 C ANISOU 567 CA GLN A 85 12222 6126 7813 -822 2447 2985 C ATOM 568 C GLN A 85 12.729 50.816 2.170 1.00 73.13 C ANISOU 568 C GLN A 85 12671 6979 8135 -678 2552 2882 C ATOM 569 O GLN A 85 11.712 50.236 1.786 1.00 68.15 O ANISOU 569 O GLN A 85 12239 6509 7144 -411 2425 2740 O ATOM 570 CB GLN A 85 12.950 53.188 1.410 1.00 73.60 C ANISOU 570 CB GLN A 85 13019 6616 8329 -763 2677 3235 C ATOM 571 CG GLN A 85 12.577 54.643 1.627 1.00 86.64 C ANISOU 571 CG GLN A 85 14864 7964 10090 -813 2546 3325 C ATOM 572 CD GLN A 85 13.689 55.441 2.290 1.00 86.37 C ANISOU 572 CD GLN A 85 14591 7666 10560 -1183 2581 3466 C ATOM 573 OE1 GLN A 85 14.638 54.876 2.843 1.00 82.95 O ANISOU 573 OE1 GLN A 85 13815 7282 10423 -1416 2629 3451 O ATOM 574 NE2 GLN A 85 13.579 56.761 2.229 1.00 83.04 N ANISOU 574 NE2 GLN A 85 14344 6955 10254 -1240 2532 3600 N ATOM 575 N HIS A 86 13.919 50.229 2.217 1.00 73.30 N ANISOU 575 N HIS A 86 12380 7075 8396 -851 2765 2949 N ATOM 576 CA HIS A 86 14.086 48.819 1.899 1.00 71.87 C ANISOU 576 CA HIS A 86 12085 7164 8056 -728 2871 2843 C ATOM 577 C HIS A 86 13.314 47.968 2.900 1.00 68.87 C ANISOU 577 C HIS A 86 11653 6895 7618 -695 2584 2589 C ATOM 578 O HIS A 86 12.674 46.970 2.536 1.00 63.26 O ANISOU 578 O HIS A 86 11042 6389 6604 -476 2527 2445 O ATOM 579 CB HIS A 86 15.572 48.445 1.906 1.00 68.11 C ANISOU 579 CB HIS A 86 11240 6723 7916 -933 3143 2963 C ATOM 580 CG HIS A 86 15.827 46.980 1.800 1.00 66.28 C ANISOU 580 CG HIS A 86 10850 6743 7592 -827 3233 2837 C ATOM 581 ND1 HIS A 86 15.940 46.161 2.908 1.00 65.03 N ANISOU 581 ND1 HIS A 86 10420 6662 7626 -950 3073 2676 N ATOM 582 CD2 HIS A 86 15.987 46.178 0.722 1.00 67.64 C ANISOU 582 CD2 HIS A 86 11116 7088 7498 -600 3458 2841 C ATOM 583 CE1 HIS A 86 16.153 44.919 2.512 1.00 64.92 C ANISOU 583 CE1 HIS A 86 10327 6862 7476 -805 3200 2594 C ATOM 584 NE2 HIS A 86 16.193 44.902 1.193 1.00 65.01 N ANISOU 584 NE2 HIS A 86 10562 6929 7210 -589 3430 2684 N ATOM 585 N GLU A 87 13.368 48.363 4.167 1.00 69.27 N ANISOU 585 N GLU A 87 11560 6796 7963 -914 2390 2529 N ATOM 586 CA GLU A 87 12.677 47.611 5.197 1.00 65.20 C ANISOU 586 CA GLU A 87 11005 6364 7403 -897 2133 2300 C ATOM 587 C GLU A 87 11.159 47.710 4.978 1.00 60.67 C ANISOU 587 C GLU A 87 10767 5835 6448 -621 1907 2178 C ATOM 588 O GLU A 87 10.446 46.702 5.028 1.00 55.40 O ANISOU 588 O GLU A 87 10126 5364 5559 -463 1783 2019 O ATOM 589 CB GLU A 87 13.078 48.120 6.584 1.00 70.76 C ANISOU 589 CB GLU A 87 11533 6863 8491 -1182 1957 2249 C ATOM 590 CG GLU A 87 12.525 47.282 7.731 1.00 76.27 C ANISOU 590 CG GLU A 87 12138 7674 9169 -1181 1687 1995 C ATOM 591 CD GLU A 87 12.926 47.819 9.099 1.00 80.41 C ANISOU 591 CD GLU A 87 12485 8023 10043 -1424 1440 1887 C ATOM 592 OE1 GLU A 87 14.140 48.036 9.326 1.00 81.57 O ANISOU 592 OE1 GLU A 87 12389 8042 10562 -1690 1540 1997 O ATOM 593 OE2 GLU A 87 12.021 48.027 9.942 1.00 76.17 O ANISOU 593 OE2 GLU A 87 12056 7473 9411 -1337 1142 1693 O ATOM 594 N GLU A 88 10.682 48.926 4.722 1.00 55.73 N ANISOU 594 N GLU A 88 10373 5027 5775 -563 1843 2258 N ATOM 595 CA GLU A 88 9.265 49.167 4.494 1.00 61.90 C ANISOU 595 CA GLU A 88 11434 5836 6249 -295 1616 2157 C ATOM 596 C GLU A 88 8.728 48.280 3.375 1.00 66.54 C ANISOU 596 C GLU A 88 12132 6666 6485 -30 1638 2107 C ATOM 597 O GLU A 88 7.709 47.592 3.557 1.00 52.36 O ANISOU 597 O GLU A 88 10373 5017 4506 138 1405 1931 O ATOM 598 CB GLU A 88 9.024 50.646 4.164 1.00 63.48 C ANISOU 598 CB GLU A 88 11857 5797 6465 -265 1606 2288 C ATOM 599 CG GLU A 88 9.164 51.595 5.346 1.00 60.92 C ANISOU 599 CG GLU A 88 11506 5203 6439 -461 1470 2268 C ATOM 600 CD GLU A 88 9.081 53.056 4.937 1.00 68.57 C ANISOU 600 CD GLU A 88 12685 5915 7453 -447 1493 2418 C ATOM 601 OE1 GLU A 88 9.196 53.345 3.730 1.00 75.66 O ANISOU 601 OE1 GLU A 88 13710 6836 8202 -343 1672 2584 O ATOM 602 OE2 GLU A 88 8.893 53.920 5.820 1.00 74.54 O ANISOU 602 OE2 GLU A 88 13501 6437 8385 -529 1326 2363 O ATOM 603 N ILE A 89 9.427 48.278 2.237 1.00 57.70 N ANISOU 603 N ILE A 89 11056 5578 5288 4 1904 2254 N ATOM 604 CA ILE A 89 9.021 47.470 1.094 1.00 58.35 C ANISOU 604 CA ILE A 89 11285 5854 5033 257 1923 2196 C ATOM 605 C ILE A 89 9.057 45.962 1.375 1.00 65.09 C ANISOU 605 C ILE A 89 11963 6926 5844 276 1876 2021 C ATOM 606 O ILE A 89 8.102 45.253 1.046 1.00 65.27 O ANISOU 606 O ILE A 89 12090 7087 5622 481 1660 1858 O ATOM 607 CB ILE A 89 9.824 47.804 -0.188 1.00 62.64 C ANISOU 607 CB ILE A 89 11949 6366 5486 305 2246 2394 C ATOM 608 CG1 ILE A 89 9.609 49.264 -0.580 1.00 65.68 C ANISOU 608 CG1 ILE A 89 12555 6537 5863 325 2265 2564 C ATOM 609 CG2 ILE A 89 9.435 46.873 -1.324 1.00 63.52 C ANISOU 609 CG2 ILE A 89 12239 6656 5239 575 2244 2299 C ATOM 610 CD1 ILE A 89 8.153 49.691 -0.632 1.00 86.02 C ANISOU 610 CD1 ILE A 89 15372 9090 8221 542 1936 2451 C ATOM 611 N CYS A 90 10.135 45.468 1.980 1.00 54.76 N ANISOU 611 N CYS A 90 10372 5639 4795 61 2055 2051 N ATOM 612 CA CYS A 90 10.190 44.038 2.319 1.00 58.26 C ANISOU 612 CA CYS A 90 10646 6277 5215 76 2014 1889 C ATOM 613 C CYS A 90 9.088 43.649 3.299 1.00 56.64 C ANISOU 613 C CYS A 90 10424 6124 4973 104 1669 1696 C ATOM 614 O CYS A 90 8.423 42.624 3.124 1.00 58.22 O ANISOU 614 O CYS A 90 10645 6489 4986 256 1508 1531 O ATOM 615 CB CYS A 90 11.547 43.638 2.896 1.00 52.14 C ANISOU 615 CB CYS A 90 9535 5503 4772 -165 2252 1960 C ATOM 616 SG CYS A 90 12.935 43.888 1.763 1.00 70.26 S ANISOU 616 SG CYS A 90 11769 7774 7153 -187 2684 2187 S ATOM 617 N LEU A 91 8.898 44.459 4.336 1.00 50.52 N ANISOU 617 N LEU A 91 9611 5197 4386 -39 1546 1711 N ATOM 618 CA LEU A 91 7.873 44.139 5.324 1.00 48.33 C ANISOU 618 CA LEU A 91 9246 4990 4128 0 1212 1505 C ATOM 619 C LEU A 91 6.472 44.271 4.691 1.00 54.76 C ANISOU 619 C LEU A 91 10334 5845 4629 280 992 1454 C ATOM 620 O LEU A 91 5.581 43.481 4.998 1.00 46.29 O ANISOU 620 O LEU A 91 9150 4926 3513 384 746 1266 O ATOM 621 CB LEU A 91 8.025 45.009 6.566 1.00 46.52 C ANISOU 621 CB LEU A 91 8887 4596 4193 -189 1107 1485 C ATOM 622 CG LEU A 91 9.287 44.715 7.395 1.00 52.74 C ANISOU 622 CG LEU A 91 9348 5366 5323 -464 1209 1481 C ATOM 623 CD1 LEU A 91 9.365 45.587 8.644 1.00 49.72 C ANISOU 623 CD1 LEU A 91 8896 4804 5193 -630 1040 1428 C ATOM 624 CD2 LEU A 91 9.386 43.237 7.787 1.00 44.30 C ANISOU 624 CD2 LEU A 91 8005 4539 4290 -461 1148 1313 C ATOM 625 N GLY A 92 6.315 45.228 3.769 1.00 48.24 N ANISOU 625 N GLY A 92 9722 4913 3693 389 1044 1568 N ATOM 626 CA GLY A 92 5.069 45.407 3.042 1.00 52.77 C ANISOU 626 CA GLY A 92 10482 5530 4037 651 816 1501 C ATOM 627 C GLY A 92 4.689 44.194 2.209 1.00 59.01 C ANISOU 627 C GLY A 92 11284 6517 4619 813 723 1372 C ATOM 628 O GLY A 92 3.572 43.672 2.325 1.00 58.64 O ANISOU 628 O GLY A 92 11203 6571 4505 947 426 1219 O ATOM 629 N LEU A 93 5.620 43.737 1.375 1.00 59.07 N ANISOU 629 N LEU A 93 11330 6567 4547 801 972 1433 N ATOM 630 CA LEU A 93 5.399 42.567 0.537 1.00 56.97 C ANISOU 630 CA LEU A 93 11114 6452 4079 954 902 1302 C ATOM 631 C LEU A 93 5.115 41.340 1.395 1.00 54.14 C ANISOU 631 C LEU A 93 10527 6234 3809 897 731 1119 C ATOM 632 O LEU A 93 4.236 40.530 1.081 1.00 52.47 O ANISOU 632 O LEU A 93 10332 6122 3483 1036 466 953 O ATOM 633 CB LEU A 93 6.612 42.334 -0.359 1.00 63.26 C ANISOU 633 CB LEU A 93 11979 7250 4806 946 1257 1414 C ATOM 634 CG LEU A 93 6.806 43.423 -1.420 1.00 66.58 C ANISOU 634 CG LEU A 93 12663 7545 5089 1044 1422 1593 C ATOM 635 CD1 LEU A 93 8.176 43.310 -2.059 1.00 59.54 C ANISOU 635 CD1 LEU A 93 11769 6643 4211 993 1836 1744 C ATOM 636 CD2 LEU A 93 5.705 43.347 -2.483 1.00 64.06 C ANISOU 636 CD2 LEU A 93 12623 7250 4468 1316 1166 1498 C ATOM 637 N PHE A 94 5.862 41.222 2.485 1.00 52.43 N ANISOU 637 N PHE A 94 10097 6009 3814 684 871 1153 N ATOM 638 CA PHE A 94 5.665 40.170 3.463 1.00 51.74 C ANISOU 638 CA PHE A 94 9779 6038 3841 607 730 998 C ATOM 639 C PHE A 94 4.229 40.157 4.006 1.00 55.94 C ANISOU 639 C PHE A 94 10234 6611 4409 695 355 855 C ATOM 640 O PHE A 94 3.576 39.105 4.051 1.00 49.69 O ANISOU 640 O PHE A 94 9323 5940 3615 757 141 686 O ATOM 641 CB PHE A 94 6.672 40.343 4.597 1.00 51.29 C ANISOU 641 CB PHE A 94 9411 5938 4139 342 893 1038 C ATOM 642 CG PHE A 94 6.394 39.490 5.786 1.00 50.52 C ANISOU 642 CG PHE A 94 8978 5946 4273 245 705 856 C ATOM 643 CD1 PHE A 94 6.307 38.118 5.666 1.00 50.43 C ANISOU 643 CD1 PHE A 94 8849 6076 4238 290 637 713 C ATOM 644 CD2 PHE A 94 6.232 40.059 7.034 1.00 48.16 C ANISOU 644 CD2 PHE A 94 8507 5587 4202 118 601 832 C ATOM 645 CE1 PHE A 94 6.045 37.326 6.771 1.00 51.45 C ANISOU 645 CE1 PHE A 94 8680 6286 4583 202 482 574 C ATOM 646 CE2 PHE A 94 5.976 39.273 8.137 1.00 53.63 C ANISOU 646 CE2 PHE A 94 8926 6377 5075 50 454 687 C ATOM 647 CZ PHE A 94 5.885 37.905 8.006 1.00 52.50 C ANISOU 647 CZ PHE A 94 8652 6375 4922 86 403 571 C ATOM 648 N THR A 95 3.737 41.329 4.393 1.00 53.72 N ANISOU 648 N THR A 95 10016 6215 4179 706 284 931 N ATOM 649 CA THR A 95 2.395 41.437 4.952 1.00 53.49 C ANISOU 649 CA THR A 95 9891 6217 4216 808 -24 824 C ATOM 650 C THR A 95 1.316 41.126 3.896 1.00 55.22 C ANISOU 650 C THR A 95 10280 6497 4206 1049 -277 763 C ATOM 651 O THR A 95 0.285 40.521 4.203 1.00 52.23 O ANISOU 651 O THR A 95 9740 6209 3894 1123 -553 632 O ATOM 652 CB THR A 95 2.179 42.819 5.595 1.00 52.00 C ANISOU 652 CB THR A 95 9757 5868 4131 791 -16 918 C ATOM 653 OG1 THR A 95 3.266 43.098 6.492 1.00 48.65 O ANISOU 653 OG1 THR A 95 9188 5366 3930 552 183 956 O ATOM 654 CG2 THR A 95 0.870 42.848 6.370 1.00 53.29 C ANISOU 654 CG2 THR A 95 9757 6078 4412 897 -277 806 C ATOM 655 N LEU A 96 1.572 41.523 2.654 1.00 47.88 N ANISOU 655 N LEU A 96 9578 5512 3101 1143 -183 834 N ATOM 656 CA LEU A 96 0.685 41.191 1.532 1.00 56.01 C ANISOU 656 CA LEU A 96 10734 6585 3963 1345 -420 746 C ATOM 657 C LEU A 96 0.616 39.689 1.289 1.00 58.33 C ANISOU 657 C LEU A 96 10931 7006 4225 1351 -546 575 C ATOM 658 O LEU A 96 -0.428 39.158 0.900 1.00 61.31 O ANISOU 658 O LEU A 96 11283 7430 4580 1472 -865 445 O ATOM 659 CB LEU A 96 1.164 41.870 0.256 1.00 50.32 C ANISOU 659 CB LEU A 96 10314 5772 3033 1441 -245 867 C ATOM 660 CG LEU A 96 0.747 43.325 0.096 1.00 62.76 C ANISOU 660 CG LEU A 96 12047 7208 4590 1523 -255 1001 C ATOM 661 CD1 LEU A 96 1.536 43.974 -1.031 1.00 54.88 C ANISOU 661 CD1 LEU A 96 11331 6112 3408 1570 8 1155 C ATOM 662 CD2 LEU A 96 -0.751 43.407 -0.180 1.00 63.74 C ANISOU 662 CD2 LEU A 96 12182 7357 4680 1720 -637 905 C ATOM 663 N ILE A 97 1.740 39.013 1.496 1.00 51.00 N ANISOU 663 N ILE A 97 9947 6118 3315 1220 -300 576 N ATOM 664 CA ILE A 97 1.787 37.568 1.366 1.00 49.97 C ANISOU 664 CA ILE A 97 9730 6086 3169 1217 -393 410 C ATOM 665 C ILE A 97 0.917 36.930 2.460 1.00 54.84 C ANISOU 665 C ILE A 97 10070 6780 3987 1159 -672 281 C ATOM 666 O ILE A 97 0.231 35.932 2.220 1.00 56.06 O ANISOU 666 O ILE A 97 10153 6987 4161 1212 -939 120 O ATOM 667 CB ILE A 97 3.239 37.067 1.446 1.00 47.79 C ANISOU 667 CB ILE A 97 9435 5829 2893 1099 -34 458 C ATOM 668 CG1 ILE A 97 3.982 37.395 0.145 1.00 54.55 C ANISOU 668 CG1 ILE A 97 10556 6628 3543 1203 215 560 C ATOM 669 CG2 ILE A 97 3.290 35.574 1.721 1.00 44.17 C ANISOU 669 CG2 ILE A 97 8837 5464 2480 1067 -132 279 C ATOM 670 CD1 ILE A 97 5.489 37.277 0.244 1.00 48.47 C ANISOU 670 CD1 ILE A 97 9734 5856 2828 1085 636 677 C ATOM 671 N LEU A 98 0.929 37.523 3.651 1.00 45.69 N ANISOU 671 N LEU A 98 8709 5607 3044 1035 -604 348 N ATOM 672 CA LEU A 98 0.143 36.994 4.757 1.00 48.46 C ANISOU 672 CA LEU A 98 8691 6022 3701 956 -788 241 C ATOM 673 C LEU A 98 -1.359 37.324 4.643 1.00 53.47 C ANISOU 673 C LEU A 98 9294 6659 4363 1115 -1121 209 C ATOM 674 O LEU A 98 -2.203 36.553 5.099 1.00 53.73 O ANISOU 674 O LEU A 98 9054 6755 4606 1100 -1334 102 O ATOM 675 CB LEU A 98 0.697 37.473 6.108 1.00 36.25 C ANISOU 675 CB LEU A 98 6920 4454 2401 777 -584 304 C ATOM 676 CG LEU A 98 2.055 36.902 6.554 1.00 45.81 C ANISOU 676 CG LEU A 98 8014 5682 3708 593 -327 309 C ATOM 677 CD1 LEU A 98 2.371 37.242 8.011 1.00 37.70 C ANISOU 677 CD1 LEU A 98 6750 4638 2935 433 -238 332 C ATOM 678 CD2 LEU A 98 2.112 35.391 6.355 1.00 43.27 C ANISOU 678 CD2 LEU A 98 7574 5449 3418 578 -401 172 C ATOM 679 N THR A 99 -1.686 38.449 4.018 1.00 48.90 N ANISOU 679 N THR A 99 8981 6003 3595 1269 -1163 315 N ATOM 680 CA THR A 99 -3.060 38.955 4.023 1.00 52.34 C ANISOU 680 CA THR A 99 9359 6432 4097 1433 -1456 313 C ATOM 681 C THR A 99 -3.781 38.871 2.670 1.00 58.20 C ANISOU 681 C THR A 99 10256 7159 4701 1597 -1699 256 C ATOM 682 O THR A 99 -4.997 39.069 2.598 1.00 57.94 O ANISOU 682 O THR A 99 10106 7131 4777 1721 -1983 229 O ATOM 683 CB THR A 99 -3.101 40.428 4.479 1.00 47.82 C ANISOU 683 CB THR A 99 8875 5753 3542 1478 -1324 461 C ATOM 684 OG1 THR A 99 -2.413 41.230 3.510 1.00 53.66 O ANISOU 684 OG1 THR A 99 9938 6387 4064 1509 -1143 568 O ATOM 685 CG2 THR A 99 -2.439 40.594 5.836 1.00 46.65 C ANISOU 685 CG2 THR A 99 8508 5590 3626 1277 -1065 478 C ATOM 686 N GLU A 100 -3.041 38.619 1.597 1.00 62.70 N ANISOU 686 N GLU A 100 11076 7699 5047 1607 -1577 245 N ATOM 687 CA GLU A 100 -3.650 38.575 0.259 1.00 54.31 C ANISOU 687 CA GLU A 100 10212 6603 3822 1774 -1792 188 C ATOM 688 C GLU A 100 -3.177 37.356 -0.518 1.00 58.84 C ANISOU 688 C GLU A 100 10888 7199 4269 1761 -1807 56 C ATOM 689 O GLU A 100 -2.268 37.451 -1.346 1.00 65.17 O ANISOU 689 O GLU A 100 11964 7958 4839 1798 -1572 106 O ATOM 690 CB GLU A 100 -3.357 39.855 -0.531 1.00 55.79 C ANISOU 690 CB GLU A 100 10715 6684 3798 1886 -1627 340 C ATOM 691 CG GLU A 100 -3.870 41.144 0.115 1.00 66.51 C ANISOU 691 CG GLU A 100 12023 7981 5266 1929 -1624 465 C ATOM 692 CD GLU A 100 -5.395 41.215 0.175 1.00 80.98 C ANISOU 692 CD GLU A 100 13686 9842 7243 2069 -2012 399 C ATOM 693 OE1 GLU A 100 -6.065 40.362 -0.451 1.00 89.31 O ANISOU 693 OE1 GLU A 100 14693 10944 8299 2128 -2302 263 O ATOM 694 OE2 GLU A 100 -5.928 42.127 0.849 1.00 79.39 O ANISOU 694 OE2 GLU A 100 13391 9603 7172 2123 -2028 483 O ATOM 695 N PRO A 101 -3.800 36.200 -0.245 1.00 60.48 N ANISOU 695 N PRO A 101 10870 7462 4648 1715 -2079 -108 N ATOM 696 CA PRO A 101 -3.379 34.934 -0.854 1.00 70.12 C ANISOU 696 CA PRO A 101 12175 8684 5785 1698 -2113 -255 C ATOM 697 C PRO A 101 -3.451 34.936 -2.379 1.00 66.83 C ANISOU 697 C PRO A 101 12117 8191 5086 1879 -2202 -297 C ATOM 698 O PRO A 101 -2.658 34.241 -3.003 1.00 72.56 O ANISOU 698 O PRO A 101 13033 8896 5639 1900 -2062 -354 O ATOM 699 CB PRO A 101 -4.338 33.898 -0.240 1.00 73.94 C ANISOU 699 CB PRO A 101 12317 9205 6572 1616 -2456 -409 C ATOM 700 CG PRO A 101 -5.436 34.697 0.427 1.00 67.17 C ANISOU 700 CG PRO A 101 11217 8371 5935 1641 -2636 -336 C ATOM 701 CD PRO A 101 -4.847 36.013 0.778 1.00 57.97 C ANISOU 701 CD PRO A 101 10178 7197 4649 1664 -2331 -149 C ATOM 702 N ALA A 102 -4.359 35.705 -2.970 1.00 65.38 N ANISOU 702 N ALA A 102 12036 7961 4844 2024 -2421 -267 N ATOM 703 CA ALA A 102 -4.415 35.790 -4.429 1.00 69.62 C ANISOU 703 CA ALA A 102 12955 8416 5080 2216 -2506 -297 C ATOM 704 C ALA A 102 -3.311 36.695 -5.009 1.00 71.87 C ANISOU 704 C ALA A 102 13569 8658 5079 2287 -2096 -120 C ATOM 705 O ALA A 102 -3.146 36.758 -6.219 1.00 71.54 O ANISOU 705 O ALA A 102 13879 8550 4753 2456 -2089 -122 O ATOM 706 CB ALA A 102 -5.803 36.250 -4.907 1.00 65.29 C ANISOU 706 CB ALA A 102 12406 7828 4571 2356 -2914 -333 C ATOM 707 N GLN A 103 -2.575 37.404 -4.152 1.00 74.13 N ANISOU 707 N GLN A 103 13743 8970 5453 2161 -1762 38 N ATOM 708 CA GLN A 103 -1.445 38.212 -4.614 1.00 79.77 C ANISOU 708 CA GLN A 103 14711 9632 5967 2185 -1348 220 C ATOM 709 C GLN A 103 -0.139 37.639 -4.083 1.00 72.45 C ANISOU 709 C GLN A 103 13683 8752 5094 2025 -986 249 C ATOM 710 O GLN A 103 0.936 38.171 -4.359 1.00 73.61 O ANISOU 710 O GLN A 103 13972 8861 5136 2009 -607 406 O ATOM 711 CB GLN A 103 -1.549 39.658 -4.120 1.00 82.54 C ANISOU 711 CB GLN A 103 15037 9933 6391 2162 -1231 403 C ATOM 712 CG GLN A 103 -2.856 40.368 -4.381 1.00 92.70 C ANISOU 712 CG GLN A 103 16359 11180 7683 2309 -1568 397 C ATOM 713 CD GLN A 103 -2.811 41.814 -3.903 1.00103.29 C ANISOU 713 CD GLN A 103 17712 12448 9085 2294 -1406 585 C ATOM 714 OE1 GLN A 103 -1.770 42.477 -3.991 1.00105.96 O ANISOU 714 OE1 GLN A 103 18195 12721 9346 2237 -1042 744 O ATOM 715 NE2 GLN A 103 -3.934 42.307 -3.386 1.00103.37 N ANISOU 715 NE2 GLN A 103 17560 12458 9257 2347 -1672 571 N ATOM 716 N ALA A 104 -0.240 36.564 -3.311 1.00 62.41 N ANISOU 716 N ALA A 104 12149 7556 4007 1905 -1105 107 N ATOM 717 CA ALA A 104 0.901 36.048 -2.567 1.00 68.39 C ANISOU 717 CA ALA A 104 12753 8367 4866 1739 -794 133 C ATOM 718 C ALA A 104 2.065 35.574 -3.456 1.00 73.02 C ANISOU 718 C ALA A 104 13564 8935 5244 1804 -485 156 C ATOM 719 O ALA A 104 3.215 35.942 -3.215 1.00 74.68 O ANISOU 719 O ALA A 104 13752 9146 5476 1715 -92 305 O ATOM 720 CB ALA A 104 0.458 34.951 -1.611 1.00 50.90 C ANISOU 720 CB ALA A 104 10233 6227 2879 1618 -1016 -33 C ATOM 721 N GLN A 105 1.767 34.763 -4.471 1.00 69.15 N ANISOU 721 N GLN A 105 13283 8419 4571 1963 -660 14 N ATOM 722 CA GLN A 105 2.810 34.219 -5.348 1.00 77.63 C ANISOU 722 CA GLN A 105 14590 9472 5435 2064 -376 22 C ATOM 723 C GLN A 105 3.564 35.341 -6.064 1.00 79.39 C ANISOU 723 C GLN A 105 15049 9637 5477 2147 -16 248 C ATOM 724 O GLN A 105 4.797 35.349 -6.113 1.00 72.79 O ANISOU 724 O GLN A 105 14216 8810 4630 2109 401 369 O ATOM 725 CB GLN A 105 2.217 33.232 -6.366 1.00 79.11 C ANISOU 725 CB GLN A 105 15011 9611 5435 2247 -679 -179 C ATOM 726 CG GLN A 105 3.237 32.635 -7.335 1.00 92.64 C ANISOU 726 CG GLN A 105 17007 11290 6901 2396 -394 -180 C ATOM 727 CD GLN A 105 4.346 31.843 -6.645 1.00100.78 C ANISOU 727 CD GLN A 105 17832 12385 8076 2269 -85 -187 C ATOM 728 OE1 GLN A 105 5.488 32.301 -6.547 1.00105.47 O ANISOU 728 OE1 GLN A 105 18395 13000 8677 2228 360 -6 O ATOM 729 NE2 GLN A 105 4.014 30.645 -6.176 1.00100.09 N ANISOU 729 NE2 GLN A 105 17592 12315 8122 2208 -323 -391 N ATOM 730 N LYS A 106 2.803 36.287 -6.607 1.00 77.80 N ANISOU 730 N LYS A 106 15029 9373 5157 2260 -180 309 N ATOM 731 CA LYS A 106 3.359 37.488 -7.205 1.00 67.99 C ANISOU 731 CA LYS A 106 14003 8059 3772 2326 125 534 C ATOM 732 C LYS A 106 4.228 38.289 -6.223 1.00 73.48 C ANISOU 732 C LYS A 106 14455 8763 4702 2106 473 730 C ATOM 733 O LYS A 106 5.308 38.748 -6.589 1.00 77.50 O ANISOU 733 O LYS A 106 15051 9233 5164 2097 878 909 O ATOM 734 CB LYS A 106 2.231 38.371 -7.728 1.00 70.12 C ANISOU 734 CB LYS A 106 14459 8260 3923 2466 -170 550 C ATOM 735 CG LYS A 106 2.710 39.579 -8.506 1.00 76.68 C ANISOU 735 CG LYS A 106 15571 8996 4566 2568 113 775 C ATOM 736 CD LYS A 106 1.583 40.576 -8.747 1.00 79.65 C ANISOU 736 CD LYS A 106 16070 9307 4887 2675 -177 806 C ATOM 737 CE LYS A 106 1.045 41.120 -7.435 1.00 74.42 C ANISOU 737 CE LYS A 106 15065 8670 4541 2493 -311 822 C ATOM 738 NZ LYS A 106 0.364 42.437 -7.613 1.00 74.18 N ANISOU 738 NZ LYS A 106 15162 8550 4475 2580 -414 942 N ATOM 739 N CYS A 107 3.757 38.456 -4.986 1.00 65.18 N ANISOU 739 N CYS A 107 13101 7751 3914 1933 311 699 N ATOM 740 CA CYS A 107 4.460 39.287 -4.003 1.00 69.99 C ANISOU 740 CA CYS A 107 13502 8340 4752 1725 579 872 C ATOM 741 C CYS A 107 5.741 38.647 -3.457 1.00 68.19 C ANISOU 741 C CYS A 107 13070 8166 4672 1566 912 907 C ATOM 742 O CYS A 107 6.713 39.349 -3.167 1.00 66.90 O ANISOU 742 O CYS A 107 12826 7954 4638 1433 1248 1097 O ATOM 743 CB CYS A 107 3.528 39.698 -2.852 1.00 57.08 C ANISOU 743 CB CYS A 107 11644 6715 3331 1620 301 828 C ATOM 744 SG CYS A 107 2.402 41.059 -3.295 1.00 75.56 S ANISOU 744 SG CYS A 107 14180 8950 5579 1766 77 905 S ATOM 745 N TYR A 108 5.739 37.322 -3.319 1.00 60.72 N ANISOU 745 N TYR A 108 12032 7308 3731 1576 810 727 N ATOM 746 CA TYR A 108 6.951 36.601 -2.944 1.00 64.14 C ANISOU 746 CA TYR A 108 12294 7794 4282 1469 1125 748 C ATOM 747 C TYR A 108 8.008 36.733 -4.042 1.00 69.80 C ANISOU 747 C TYR A 108 13208 8469 4846 1581 1511 887 C ATOM 748 O TYR A 108 9.191 36.905 -3.750 1.00 68.35 O ANISOU 748 O TYR A 108 12860 8283 4826 1460 1885 1038 O ATOM 749 CB TYR A 108 6.667 35.124 -2.672 1.00 56.88 C ANISOU 749 CB TYR A 108 11277 6958 3378 1487 920 515 C ATOM 750 CG TYR A 108 7.911 34.354 -2.290 1.00 63.60 C ANISOU 750 CG TYR A 108 11952 7859 4353 1401 1248 533 C ATOM 751 CD1 TYR A 108 8.459 34.473 -1.020 1.00 64.89 C ANISOU 751 CD1 TYR A 108 11800 8057 4797 1179 1383 602 C ATOM 752 CD2 TYR A 108 8.548 33.519 -3.201 1.00 63.77 C ANISOU 752 CD2 TYR A 108 12127 7883 4219 1556 1423 485 C ATOM 753 CE1 TYR A 108 9.599 33.775 -0.665 1.00 61.77 C ANISOU 753 CE1 TYR A 108 11215 7706 4548 1108 1678 626 C ATOM 754 CE2 TYR A 108 9.687 32.819 -2.856 1.00 59.51 C ANISOU 754 CE2 TYR A 108 11404 7388 3821 1498 1731 506 C ATOM 755 CZ TYR A 108 10.209 32.955 -1.591 1.00 63.20 C ANISOU 755 CZ TYR A 108 11526 7896 4590 1272 1857 580 C ATOM 756 OH TYR A 108 11.341 32.262 -1.242 1.00 69.84 O ANISOU 756 OH TYR A 108 12152 8779 5605 1221 2155 607 O ATOM 757 N ARG A 109 7.563 36.650 -5.296 1.00 64.67 N ANISOU 757 N ARG A 109 12899 7777 3895 1817 1412 839 N ATOM 758 CA ARG A 109 8.430 36.847 -6.447 1.00 68.35 C ANISOU 758 CA ARG A 109 13612 8191 4167 1968 1765 978 C ATOM 759 C ARG A 109 9.034 38.256 -6.403 1.00 73.98 C ANISOU 759 C ARG A 109 14299 8827 4984 1865 2070 1252 C ATOM 760 O ARG A 109 10.236 38.432 -6.603 1.00 76.02 O ANISOU 760 O ARG A 109 14494 9068 5323 1823 2492 1424 O ATOM 761 CB ARG A 109 7.634 36.629 -7.742 1.00 74.42 C ANISOU 761 CB ARG A 109 14792 8911 4573 2248 1532 871 C ATOM 762 CG ARG A 109 8.447 36.720 -9.025 1.00 86.03 C ANISOU 762 CG ARG A 109 16582 10322 5783 2455 1882 996 C ATOM 763 CD ARG A 109 7.550 36.610 -10.251 1.00 98.06 C ANISOU 763 CD ARG A 109 18543 11781 6935 2736 1602 889 C ATOM 764 NE ARG A 109 6.511 37.637 -10.261 1.00106.10 N ANISOU 764 NE ARG A 109 19645 12748 7921 2743 1318 923 N ATOM 765 CZ ARG A 109 6.624 38.815 -10.872 1.00115.07 C ANISOU 765 CZ ARG A 109 20998 13799 8926 2822 1493 1125 C ATOM 766 NH1 ARG A 109 7.733 39.120 -11.534 1.00123.08 N ANISOU 766 NH1 ARG A 109 22159 14770 9835 2892 1961 1321 N ATOM 767 NH2 ARG A 109 5.625 39.689 -10.824 1.00111.88 N ANISOU 767 NH2 ARG A 109 20658 13347 8505 2837 1208 1139 N ATOM 768 N ASP A 110 8.200 39.255 -6.120 1.00 71.98 N ANISOU 768 N ASP A 110 14076 8517 4756 1821 1851 1294 N ATOM 769 CA ASP A 110 8.680 40.627 -5.999 1.00 80.03 C ANISOU 769 CA ASP A 110 15075 9436 5896 1708 2094 1542 C ATOM 770 C ASP A 110 9.606 40.768 -4.788 1.00 82.13 C ANISOU 770 C ASP A 110 14949 9714 6542 1418 2313 1642 C ATOM 771 O ASP A 110 10.618 41.467 -4.856 1.00 81.78 O ANISOU 771 O ASP A 110 14830 9598 6645 1309 2667 1861 O ATOM 772 CB ASP A 110 7.512 41.613 -5.890 1.00 85.27 C ANISOU 772 CB ASP A 110 15857 10027 6513 1740 1780 1544 C ATOM 773 CG ASP A 110 6.659 41.669 -7.156 1.00 96.54 C ANISOU 773 CG ASP A 110 17677 11419 7583 2026 1577 1484 C ATOM 774 OD1 ASP A 110 7.095 41.153 -8.211 1.00103.37 O ANISOU 774 OD1 ASP A 110 18777 12289 8212 2201 1736 1483 O ATOM 775 OD2 ASP A 110 5.552 42.252 -7.093 1.00 99.33 O ANISOU 775 OD2 ASP A 110 18110 11733 7897 2086 1255 1441 O ATOM 776 N LEU A 111 9.255 40.104 -3.683 1.00 77.89 N ANISOU 776 N LEU A 111 14161 9258 6177 1291 2094 1484 N ATOM 777 CA LEU A 111 10.091 40.116 -2.479 1.00 70.29 C ANISOU 777 CA LEU A 111 12833 8305 5569 1025 2260 1554 C ATOM 778 C LEU A 111 11.497 39.598 -2.773 1.00 68.73 C ANISOU 778 C LEU A 111 12494 8139 5481 988 2667 1653 C ATOM 779 O LEU A 111 12.487 40.271 -2.495 1.00 65.27 O ANISOU 779 O LEU A 111 11866 7633 5300 814 2952 1852 O ATOM 780 CB LEU A 111 9.468 39.280 -1.362 1.00 63.22 C ANISOU 780 CB LEU A 111 11735 7503 4783 941 1965 1353 C ATOM 781 CG LEU A 111 10.256 39.216 -0.044 1.00 62.28 C ANISOU 781 CG LEU A 111 11255 7390 5019 673 2097 1406 C ATOM 782 CD1 LEU A 111 10.561 40.616 0.497 1.00 62.86 C ANISOU 782 CD1 LEU A 111 11255 7314 5313 484 2186 1599 C ATOM 783 CD2 LEU A 111 9.532 38.386 1.023 1.00 57.10 C ANISOU 783 CD2 LEU A 111 10448 6822 4424 619 1799 1209 C ATOM 784 N ALA A 112 11.571 38.401 -3.344 1.00 69.36 N ANISOU 784 N ALA A 112 12656 8310 5386 1157 2678 1512 N ATOM 785 CA ALA A 112 12.852 37.796 -3.704 1.00 80.21 C ANISOU 785 CA ALA A 112 13912 9719 6846 1176 3061 1588 C ATOM 786 C ALA A 112 13.674 38.704 -4.613 1.00 81.25 C ANISOU 786 C ALA A 112 14156 9758 6956 1218 3433 1839 C ATOM 787 O ALA A 112 14.898 38.745 -4.517 1.00 82.79 O ANISOU 787 O ALA A 112 14108 9947 7400 1114 3788 1996 O ATOM 788 CB ALA A 112 12.633 36.450 -4.372 1.00 77.22 C ANISOU 788 CB ALA A 112 13710 9417 6214 1406 2980 1385 C ATOM 789 N LEU A 113 12.990 39.438 -5.483 1.00 80.92 N ANISOU 789 N LEU A 113 14470 9642 6636 1373 3345 1883 N ATOM 790 CA LEU A 113 13.660 40.254 -6.489 1.00 92.31 C ANISOU 790 CA LEU A 113 16090 10991 7994 1457 3695 2119 C ATOM 791 C LEU A 113 14.230 41.531 -5.882 1.00 92.68 C ANISOU 791 C LEU A 113 15908 10931 8374 1193 3864 2357 C ATOM 792 O LEU A 113 15.348 41.939 -6.199 1.00 97.13 O ANISOU 792 O LEU A 113 16355 11442 9106 1129 4254 2575 O ATOM 793 CB LEU A 113 12.685 40.600 -7.622 1.00 95.61 C ANISOU 793 CB LEU A 113 16986 11355 7989 1724 3518 2081 C ATOM 794 CG LEU A 113 13.187 40.447 -9.058 1.00 98.86 C ANISOU 794 CG LEU A 113 17731 11733 8098 1993 3818 2175 C ATOM 795 CD1 LEU A 113 12.399 39.373 -9.794 1.00 98.22 C ANISOU 795 CD1 LEU A 113 17971 11702 7645 2271 3545 1926 C ATOM 796 CD2 LEU A 113 13.110 41.773 -9.797 1.00101.61 C ANISOU 796 CD2 LEU A 113 18340 11952 8315 2054 3954 2398 C ATOM 797 N VAL A 114 13.452 42.148 -4.996 1.00 85.98 N ANISOU 797 N VAL A 114 14991 10040 7638 1042 3559 2311 N ATOM 798 CA VAL A 114 13.788 43.458 -4.450 1.00 80.66 C ANISOU 798 CA VAL A 114 14174 9224 7247 807 3640 2515 C ATOM 799 C VAL A 114 14.610 43.373 -3.158 1.00 75.59 C ANISOU 799 C VAL A 114 13066 8582 7071 492 3698 2547 C ATOM 800 O VAL A 114 15.285 44.335 -2.782 1.00 76.71 O ANISOU 800 O VAL A 114 13029 8593 7523 268 3840 2740 O ATOM 801 CB VAL A 114 12.509 44.310 -4.234 1.00 77.36 C ANISOU 801 CB VAL A 114 13970 8723 6700 836 3286 2464 C ATOM 802 CG1 VAL A 114 11.879 44.008 -2.876 1.00 75.51 C ANISOU 802 CG1 VAL A 114 13519 8530 6643 687 2954 2289 C ATOM 803 CG2 VAL A 114 12.813 45.789 -4.380 1.00 76.92 C ANISOU 803 CG2 VAL A 114 13974 8480 6772 723 3437 2714 C ATOM 804 N SER A 115 14.565 42.224 -2.488 1.00 73.71 N ANISOU 804 N SER A 115 12635 8476 6896 471 3572 2358 N ATOM 805 CA SER A 115 15.319 42.056 -1.247 1.00 76.07 C ANISOU 805 CA SER A 115 12496 8777 7629 189 3597 2372 C ATOM 806 C SER A 115 16.832 42.143 -1.453 1.00 83.60 C ANISOU 806 C SER A 115 13164 9707 8895 67 3986 2569 C ATOM 807 O SER A 115 17.382 41.491 -2.335 1.00 87.76 O ANISOU 807 O SER A 115 13742 10309 9294 245 4245 2593 O ATOM 808 CB SER A 115 14.995 40.728 -0.583 1.00 70.04 C ANISOU 808 CB SER A 115 11602 8164 6847 220 3412 2140 C ATOM 809 OG SER A 115 15.762 40.586 0.599 1.00 68.42 O ANISOU 809 OG SER A 115 10975 7952 7068 -45 3434 2162 O ATOM 810 N ARG A 116 17.494 42.932 -0.610 1.00 81.86 N ANISOU 810 N ARG A 116 12635 9369 9099 -233 4005 2701 N ATOM 811 CA ARG A 116 18.939 43.104 -0.678 1.00 82.78 C ANISOU 811 CA ARG A 116 12415 9448 9590 -389 4322 2890 C ATOM 812 C ARG A 116 19.708 42.361 0.428 1.00 78.36 C ANISOU 812 C ARG A 116 11381 8956 9437 -584 4266 2813 C ATOM 813 O ARG A 116 20.932 42.275 0.377 1.00 79.97 O ANISOU 813 O ARG A 116 11263 9159 9963 -682 4506 2939 O ATOM 814 CB ARG A 116 19.286 44.592 -0.643 1.00 88.99 C ANISOU 814 CB ARG A 116 13178 10025 10609 -600 4379 3112 C ATOM 815 CG ARG A 116 18.616 45.422 -1.734 1.00100.74 C ANISOU 815 CG ARG A 116 15118 11427 11730 -413 4449 3218 C ATOM 816 CD ARG A 116 19.158 46.852 -1.754 1.00109.05 C ANISOU 816 CD ARG A 116 16116 12259 13059 -634 4562 3469 C ATOM 817 NE ARG A 116 18.557 47.675 -2.803 1.00112.44 N ANISOU 817 NE ARG A 116 16977 12596 13149 -450 4642 3590 N ATOM 818 CZ ARG A 116 19.182 48.059 -3.913 1.00111.52 C ANISOU 818 CZ ARG A 116 16976 12434 12962 -355 5011 3810 C ATOM 819 NH1 ARG A 116 20.439 47.698 -4.131 1.00114.34 N ANISOU 819 NH1 ARG A 116 17035 12830 13578 -421 5350 3938 N ATOM 820 NH2 ARG A 116 18.548 48.812 -4.805 1.00109.92 N ANISOU 820 NH2 ARG A 116 17186 12142 12436 -181 5045 3909 N ATOM 821 N ASP A 117 19.000 41.824 1.419 1.00 76.68 N ANISOU 821 N ASP A 117 11120 8797 9216 -631 3948 2612 N ATOM 822 CA ASP A 117 19.665 41.170 2.551 1.00 75.14 C ANISOU 822 CA ASP A 117 10487 8653 9410 -820 3851 2535 C ATOM 823 C ASP A 117 19.313 39.684 2.662 1.00 73.72 C ANISOU 823 C ASP A 117 10306 8658 9045 -636 3794 2331 C ATOM 824 O ASP A 117 19.207 39.130 3.774 1.00 71.01 O ANISOU 824 O ASP A 117 9741 8355 8885 -753 3576 2201 O ATOM 825 CB ASP A 117 19.359 41.907 3.871 1.00 68.00 C ANISOU 825 CB ASP A 117 9455 7610 8772 -1098 3520 2494 C ATOM 826 CG ASP A 117 17.903 41.737 4.334 1.00 77.72 C ANISOU 826 CG ASP A 117 10979 8857 9694 -1003 3222 2311 C ATOM 827 OD1 ASP A 117 17.024 41.380 3.516 1.00 80.17 O ANISOU 827 OD1 ASP A 117 11638 9254 9568 -740 3236 2242 O ATOM 828 OD2 ASP A 117 17.635 41.966 5.533 1.00 76.68 O ANISOU 828 OD2 ASP A 117 10733 8640 9761 -1188 2953 2228 O ATOM 829 N GLY A 118 19.134 39.039 1.508 1.00 68.87 N ANISOU 829 N GLY A 118 9958 8140 8070 -345 3980 2301 N ATOM 830 CA GLY A 118 18.675 37.658 1.468 1.00 66.57 C ANISOU 830 CA GLY A 118 9747 7997 7548 -146 3905 2094 C ATOM 831 C GLY A 118 17.432 37.363 2.309 1.00 68.92 C ANISOU 831 C GLY A 118 10163 8324 7700 -167 3535 1898 C ATOM 832 O GLY A 118 17.340 36.294 2.918 1.00 74.65 O ANISOU 832 O GLY A 118 10746 9146 8471 -152 3434 1748 O ATOM 833 N MET A 119 16.488 38.308 2.347 1.00 66.30 N ANISOU 833 N MET A 119 10087 7901 7202 -193 3343 1907 N ATOM 834 CA MET A 119 15.227 38.161 3.089 1.00 63.74 C ANISOU 834 CA MET A 119 9906 7591 6723 -194 2994 1738 C ATOM 835 C MET A 119 15.391 38.045 4.609 1.00 66.38 C ANISOU 835 C MET A 119 9900 7903 7418 -443 2810 1677 C ATOM 836 O MET A 119 14.501 37.549 5.305 1.00 58.83 O ANISOU 836 O MET A 119 8932 7019 6402 -417 2448 1455 O ATOM 837 CB MET A 119 14.380 37.004 2.529 1.00 59.03 C ANISOU 837 CB MET A 119 9558 7128 5742 71 2871 1533 C ATOM 838 CG MET A 119 13.897 37.266 1.103 1.00 60.67 C ANISOU 838 CG MET A 119 10158 7327 5567 321 2900 1541 C ATOM 839 SD MET A 119 12.757 36.034 0.470 1.00 92.16 S ANISOU 839 SD MET A 119 14450 11426 9140 605 2630 1270 S ATOM 840 CE MET A 119 13.678 35.381 -0.923 1.00112.99 C ANISOU 840 CE MET A 119 17220 14091 11620 828 2968 1307 C ATOM 841 N ASN A 120 16.515 38.535 5.122 1.00 70.47 N ANISOU 841 N ASN A 120 10088 8332 8356 -676 2945 1825 N ATOM 842 CA ASN A 120 16.807 38.442 6.552 1.00 62.69 C ANISOU 842 CA ASN A 120 8742 7331 7747 -901 2669 1723 C ATOM 843 C ASN A 120 15.827 39.204 7.460 1.00 55.42 C ANISOU 843 C ASN A 120 7937 6322 6797 -987 2275 1600 C ATOM 844 O ASN A 120 15.339 38.664 8.458 1.00 53.21 O ANISOU 844 O ASN A 120 7550 6117 6552 -1002 1959 1402 O ATOM 845 CB ASN A 120 18.245 38.889 6.826 1.00 66.32 C ANISOU 845 CB ASN A 120 8828 7689 8680 -1135 2869 1917 C ATOM 846 CG ASN A 120 18.577 38.877 8.296 1.00 71.55 C ANISOU 846 CG ASN A 120 9154 8314 9717 -1363 2538 1810 C ATOM 847 OD1 ASN A 120 18.667 39.928 8.929 1.00 77.29 O ANISOU 847 OD1 ASN A 120 9848 8867 10653 -1570 2370 1850 O ATOM 848 ND2 ASN A 120 18.736 37.681 8.859 1.00 69.82 N ANISOU 848 ND2 ASN A 120 8717 8247 9564 -1309 2409 1657 N ATOM 849 N ILE A 121 15.563 40.462 7.117 1.00 57.32 N ANISOU 849 N ILE A 121 8408 6395 6978 -1031 2318 1732 N ATOM 850 CA ILE A 121 14.567 41.270 7.809 1.00 51.87 C ANISOU 850 CA ILE A 121 7888 5604 6215 -1059 1990 1628 C ATOM 851 C ILE A 121 13.217 40.542 7.852 1.00 52.50 C ANISOU 851 C ILE A 121 8144 5842 5963 -836 1746 1413 C ATOM 852 O ILE A 121 12.500 40.593 8.851 1.00 57.93 O ANISOU 852 O ILE A 121 8804 6535 6672 -855 1441 1256 O ATOM 853 CB ILE A 121 14.427 42.653 7.128 1.00 57.29 C ANISOU 853 CB ILE A 121 8864 6082 6824 -1075 2127 1825 C ATOM 854 CG1 ILE A 121 15.620 43.542 7.478 1.00 62.28 C ANISOU 854 CG1 ILE A 121 9278 6498 7887 -1366 2253 2010 C ATOM 855 CG2 ILE A 121 13.144 43.357 7.547 1.00 60.05 C ANISOU 855 CG2 ILE A 121 9475 6356 6985 -993 1818 1707 C ATOM 856 CD1 ILE A 121 15.708 44.821 6.625 1.00 72.16 C ANISOU 856 CD1 ILE A 121 10748 7568 9100 -1370 2413 2222 C ATOM 857 N VAL A 122 12.884 39.838 6.774 1.00 59.36 N ANISOU 857 N VAL A 122 9189 6833 6534 -621 1881 1407 N ATOM 858 CA VAL A 122 11.645 39.083 6.740 1.00 54.59 C ANISOU 858 CA VAL A 122 8715 6362 5665 -428 1633 1208 C ATOM 859 C VAL A 122 11.699 37.901 7.697 1.00 56.02 C ANISOU 859 C VAL A 122 8602 6674 6008 -475 1465 1030 C ATOM 860 O VAL A 122 10.721 37.630 8.407 1.00 54.23 O ANISOU 860 O VAL A 122 8360 6498 5745 -437 1185 875 O ATOM 861 CB VAL A 122 11.295 38.615 5.317 1.00 58.06 C ANISOU 861 CB VAL A 122 9451 6873 5736 -184 1772 1226 C ATOM 862 CG1 VAL A 122 10.003 37.796 5.329 1.00 51.87 C ANISOU 862 CG1 VAL A 122 8757 6207 4743 -15 1459 1008 C ATOM 863 CG2 VAL A 122 11.166 39.820 4.384 1.00 56.41 C ANISOU 863 CG2 VAL A 122 9578 6527 5327 -112 1927 1421 C ATOM 864 N LEU A 123 12.837 37.207 7.727 1.00 56.83 N ANISOU 864 N LEU A 123 8466 6825 6302 -546 1652 1069 N ATOM 865 CA LEU A 123 12.996 36.056 8.624 1.00 54.97 C ANISOU 865 CA LEU A 123 7958 6699 6230 -583 1505 922 C ATOM 866 C LEU A 123 12.913 36.473 10.101 1.00 50.22 C ANISOU 866 C LEU A 123 7179 6047 5856 -752 1246 861 C ATOM 867 O LEU A 123 12.304 35.773 10.907 1.00 47.61 O ANISOU 867 O LEU A 123 6773 5795 5521 -723 1025 714 O ATOM 868 CB LEU A 123 14.296 35.285 8.349 1.00 59.19 C ANISOU 868 CB LEU A 123 8262 7283 6946 -605 1764 991 C ATOM 869 CG LEU A 123 14.435 34.442 7.073 1.00 70.98 C ANISOU 869 CG LEU A 123 9911 8855 8204 -391 2011 994 C ATOM 870 CD1 LEU A 123 15.048 33.073 7.354 1.00 65.83 C ANISOU 870 CD1 LEU A 123 9017 8299 7698 -351 2046 905 C ATOM 871 CD2 LEU A 123 13.113 34.267 6.357 1.00 77.21 C ANISOU 871 CD2 LEU A 123 11058 9677 8603 -192 1860 876 C ATOM 872 N ASN A 124 13.509 37.612 10.453 1.00 41.41 N ANISOU 872 N ASN A 124 6021 4784 4929 -923 1274 975 N ATOM 873 CA ASN A 124 13.431 38.087 11.828 1.00 46.28 C ANISOU 873 CA ASN A 124 6539 5327 5717 -1063 1008 899 C ATOM 874 C ASN A 124 11.985 38.359 12.202 1.00 50.77 C ANISOU 874 C ASN A 124 7328 5905 6056 -941 789 779 C ATOM 875 O ASN A 124 11.541 38.014 13.293 1.00 50.60 O ANISOU 875 O ASN A 124 7237 5928 6061 -940 576 655 O ATOM 876 CB ASN A 124 14.274 39.349 12.032 1.00 49.29 C ANISOU 876 CB ASN A 124 6879 5507 6342 -1270 1049 1033 C ATOM 877 CG ASN A 124 15.761 39.094 11.849 1.00 61.05 C ANISOU 877 CG ASN A 124 8061 6982 8154 -1418 1246 1165 C ATOM 878 OD1 ASN A 124 16.238 37.974 12.037 1.00 59.20 O ANISOU 878 OD1 ASN A 124 7598 6883 8010 -1388 1266 1118 O ATOM 879 ND2 ASN A 124 16.500 40.138 11.475 1.00 68.83 N ANISOU 879 ND2 ASN A 124 9025 7789 9338 -1575 1403 1346 N ATOM 880 N LYS A 125 11.248 38.956 11.273 1.00 44.41 N ANISOU 880 N LYS A 125 6788 5060 5025 -819 856 830 N ATOM 881 CA LYS A 125 9.869 39.317 11.538 1.00 44.66 C ANISOU 881 CA LYS A 125 7006 5091 4872 -688 663 740 C ATOM 882 C LYS A 125 9.008 38.056 11.651 1.00 40.12 C ANISOU 882 C LYS A 125 6363 4695 4187 -549 546 601 C ATOM 883 O LYS A 125 8.119 37.984 12.503 1.00 41.97 O ANISOU 883 O LYS A 125 6581 4960 4408 -499 364 503 O ATOM 884 CB LYS A 125 9.356 40.268 10.458 1.00 45.41 C ANISOU 884 CB LYS A 125 7396 5091 4767 -580 748 845 C ATOM 885 CG LYS A 125 8.137 41.052 10.856 1.00 57.77 C ANISOU 885 CG LYS A 125 9136 6591 6221 -473 557 789 C ATOM 886 CD LYS A 125 8.401 41.942 12.065 1.00 60.48 C ANISOU 886 CD LYS A 125 9454 6781 6745 -610 449 767 C ATOM 887 CE LYS A 125 9.579 42.863 11.840 1.00 59.92 C ANISOU 887 CE LYS A 125 9405 6513 6848 -803 590 915 C ATOM 888 NZ LYS A 125 9.745 43.833 12.954 1.00 64.08 N ANISOU 888 NZ LYS A 125 9966 6846 7534 -927 431 871 N ATOM 889 N ILE A 126 9.302 37.041 10.836 1.00 39.50 N ANISOU 889 N ILE A 126 6240 4719 4048 -487 661 595 N ATOM 890 CA ILE A 126 8.594 35.760 10.956 1.00 39.53 C ANISOU 890 CA ILE A 126 6163 4859 3998 -386 537 461 C ATOM 891 C ILE A 126 8.819 35.173 12.349 1.00 44.45 C ANISOU 891 C ILE A 126 6546 5523 4821 -486 424 392 C ATOM 892 O ILE A 126 7.859 34.825 13.044 1.00 47.39 O ANISOU 892 O ILE A 126 6884 5943 5180 -432 263 308 O ATOM 893 CB ILE A 126 9.050 34.734 9.913 1.00 41.65 C ANISOU 893 CB ILE A 126 6443 5200 4183 -307 678 451 C ATOM 894 CG1 ILE A 126 8.594 35.156 8.522 1.00 38.57 C ANISOU 894 CG1 ILE A 126 6352 4784 3517 -154 746 495 C ATOM 895 CG2 ILE A 126 8.485 33.345 10.238 1.00 30.83 C ANISOU 895 CG2 ILE A 126 4950 3929 2834 -248 531 307 C ATOM 896 CD1 ILE A 126 9.090 34.240 7.439 1.00 44.73 C ANISOU 896 CD1 ILE A 126 7216 5618 4164 -45 906 480 C ATOM 897 N ASN A 127 10.083 35.073 12.759 1.00 41.68 N ANISOU 897 N ASN A 127 6026 5149 4663 -622 512 440 N ATOM 898 CA ASN A 127 10.397 34.556 14.090 1.00 43.71 C ANISOU 898 CA ASN A 127 6085 5435 5090 -706 383 384 C ATOM 899 C ASN A 127 9.724 35.390 15.169 1.00 37.88 C ANISOU 899 C ASN A 127 5428 4633 4330 -722 211 347 C ATOM 900 O ASN A 127 9.224 34.850 16.149 1.00 39.23 O ANISOU 900 O ASN A 127 5541 4860 4507 -689 86 277 O ATOM 901 CB ASN A 127 11.914 34.505 14.332 1.00 44.38 C ANISOU 901 CB ASN A 127 5966 5485 5411 -852 468 454 C ATOM 902 CG ASN A 127 12.585 33.377 13.578 1.00 56.03 C ANISOU 902 CG ASN A 127 7313 7044 6933 -800 636 470 C ATOM 903 OD1 ASN A 127 12.016 32.289 13.415 1.00 54.77 O ANISOU 903 OD1 ASN A 127 7159 6970 6680 -685 603 385 O ATOM 904 ND2 ASN A 127 13.804 33.630 13.105 1.00 56.61 N ANISOU 904 ND2 ASN A 127 7266 7076 7168 -881 828 584 N ATOM 905 N GLN A 128 9.704 36.710 14.984 1.00 39.91 N ANISOU 905 N GLN A 128 5843 4764 4557 -758 224 401 N ATOM 906 CA GLN A 128 9.017 37.568 15.943 1.00 34.29 C ANISOU 906 CA GLN A 128 5258 3973 3799 -738 74 353 C ATOM 907 C GLN A 128 7.531 37.221 15.968 1.00 38.15 C ANISOU 907 C GLN A 128 5818 4552 4127 -556 14 292 C ATOM 908 O GLN A 128 6.949 37.040 17.048 1.00 42.78 O ANISOU 908 O GLN A 128 6386 5168 4701 -505 -86 230 O ATOM 909 CB GLN A 128 9.226 39.053 15.638 1.00 33.09 C ANISOU 909 CB GLN A 128 5287 3635 3649 -798 99 423 C ATOM 910 CG GLN A 128 8.592 39.959 16.685 1.00 38.16 C ANISOU 910 CG GLN A 128 6090 4168 4242 -759 -58 355 C ATOM 911 CD GLN A 128 8.841 41.435 16.415 1.00 50.09 C ANISOU 911 CD GLN A 128 7797 5456 5779 -827 -51 418 C ATOM 912 OE1 GLN A 128 9.452 41.799 15.403 1.00 49.73 O ANISOU 912 OE1 GLN A 128 7763 5341 5791 -907 93 539 O ATOM 913 NE2 GLN A 128 8.355 42.298 17.317 1.00 50.75 N ANISOU 913 NE2 GLN A 128 8059 5410 5816 -781 -189 345 N ATOM 914 N ILE A 129 6.923 37.090 14.787 1.00 40.53 N ANISOU 914 N ILE A 129 6196 4895 4310 -451 75 315 N ATOM 915 CA ILE A 129 5.504 36.723 14.730 1.00 43.33 C ANISOU 915 CA ILE A 129 6567 5329 4566 -290 -11 262 C ATOM 916 C ILE A 129 5.243 35.361 15.394 1.00 44.66 C ANISOU 916 C ILE A 129 6534 5619 4816 -284 -60 199 C ATOM 917 O ILE A 129 4.303 35.220 16.192 1.00 34.86 O ANISOU 917 O ILE A 129 5249 4413 3583 -208 -127 171 O ATOM 918 CB ILE A 129 4.946 36.754 13.293 1.00 42.58 C ANISOU 918 CB ILE A 129 6597 5252 4330 -177 6 286 C ATOM 919 CG1 ILE A 129 4.767 38.201 12.848 1.00 43.42 C ANISOU 919 CG1 ILE A 129 6933 5228 4338 -132 25 360 C ATOM 920 CG2 ILE A 129 3.603 36.043 13.231 1.00 37.03 C ANISOU 920 CG2 ILE A 129 5823 4643 3602 -43 -123 220 C ATOM 921 CD1 ILE A 129 4.738 38.365 11.361 1.00 50.84 C ANISOU 921 CD1 ILE A 129 8048 6154 5116 -50 85 421 C ATOM 922 N LEU A 130 6.087 34.373 15.096 1.00 39.39 N ANISOU 922 N LEU A 130 5747 5002 4219 -356 -5 193 N ATOM 923 CA LEU A 130 5.898 33.047 15.676 1.00 34.26 C ANISOU 923 CA LEU A 130 4922 4437 3657 -353 -49 146 C ATOM 924 C LEU A 130 6.082 33.069 17.196 1.00 39.95 C ANISOU 924 C LEU A 130 5576 5154 4451 -398 -95 146 C ATOM 925 O LEU A 130 5.318 32.433 17.918 1.00 36.63 O ANISOU 925 O LEU A 130 5080 4784 4053 -342 -135 133 O ATOM 926 CB LEU A 130 6.836 32.017 15.043 1.00 32.81 C ANISOU 926 CB LEU A 130 4645 4287 3533 -397 26 135 C ATOM 927 CG LEU A 130 6.689 31.715 13.557 1.00 42.41 C ANISOU 927 CG LEU A 130 5963 5512 4636 -320 74 114 C ATOM 928 CD1 LEU A 130 7.851 30.822 13.086 1.00 43.25 C ANISOU 928 CD1 LEU A 130 5993 5635 4804 -350 197 111 C ATOM 929 CD2 LEU A 130 5.357 31.053 13.276 1.00 39.11 C ANISOU 929 CD2 LEU A 130 5545 5131 4182 -221 -63 44 C ATOM 930 N MET A 131 7.085 33.793 17.689 1.00 32.27 N ANISOU 930 N MET A 131 4636 4108 3515 -496 -97 167 N ATOM 931 CA MET A 131 7.355 33.767 19.133 1.00 35.14 C ANISOU 931 CA MET A 131 4977 4458 3915 -525 -182 151 C ATOM 932 C MET A 131 6.353 34.614 19.950 1.00 39.80 C ANISOU 932 C MET A 131 5727 5010 4387 -422 -228 132 C ATOM 933 O MET A 131 6.122 34.338 21.114 1.00 43.41 O ANISOU 933 O MET A 131 6194 5487 4812 -374 -271 119 O ATOM 934 CB MET A 131 8.791 34.235 19.439 1.00 35.55 C ANISOU 934 CB MET A 131 4999 4430 4077 -671 -224 166 C ATOM 935 CG MET A 131 9.898 33.278 18.951 1.00 36.24 C ANISOU 935 CG MET A 131 4885 4566 4320 -751 -165 196 C ATOM 936 SD MET A 131 9.779 31.594 19.630 1.00 42.10 S ANISOU 936 SD MET A 131 5470 5418 5108 -691 -201 176 S ATOM 937 CE MET A 131 10.302 31.896 21.351 1.00 32.11 C ANISOU 937 CE MET A 131 4236 4106 3857 -729 -390 163 C ATOM 938 N GLU A 132 5.770 35.646 19.347 1.00 37.79 N ANISOU 938 N GLU A 132 5613 4692 4053 -366 -207 138 N ATOM 939 CA GLU A 132 5.029 36.631 20.130 1.00 38.55 C ANISOU 939 CA GLU A 132 5884 4718 4046 -259 -241 115 C ATOM 940 C GLU A 132 3.541 36.711 19.784 1.00 42.07 C ANISOU 940 C GLU A 132 6339 5215 4430 -85 -195 130 C ATOM 941 O GLU A 132 2.739 37.107 20.631 1.00 41.79 O ANISOU 941 O GLU A 132 6382 5168 4327 49 -182 120 O ATOM 942 CB GLU A 132 5.657 38.037 19.989 1.00 38.04 C ANISOU 942 CB GLU A 132 6008 4481 3966 -331 -283 110 C ATOM 943 CG GLU A 132 7.132 38.158 20.387 1.00 43.18 C ANISOU 943 CG GLU A 132 6627 5048 4733 -521 -362 100 C ATOM 944 CD GLU A 132 7.654 39.597 20.230 1.00 61.65 C ANISOU 944 CD GLU A 132 9144 7179 7101 -611 -412 104 C ATOM 945 OE1 GLU A 132 6.831 40.531 20.064 1.00 66.97 O ANISOU 945 OE1 GLU A 132 10014 7765 7667 -498 -397 100 O ATOM 946 OE2 GLU A 132 8.888 39.798 20.266 1.00 62.36 O ANISOU 946 OE2 GLU A 132 9165 7180 7349 -796 -470 121 O ATOM 947 N LYS A 133 3.181 36.351 18.550 1.00 36.02 N ANISOU 947 N LYS A 133 5498 4500 3687 -72 -177 152 N ATOM 948 CA LYS A 133 1.838 36.640 18.027 1.00 32.04 C ANISOU 948 CA LYS A 133 5005 4020 3148 87 -186 168 C ATOM 949 C LYS A 133 1.082 35.421 17.555 1.00 36.68 C ANISOU 949 C LYS A 133 5389 4725 3824 121 -210 169 C ATOM 950 O LYS A 133 -0.076 35.552 17.148 1.00 39.70 O ANISOU 950 O LYS A 133 5729 5131 4223 247 -252 183 O ATOM 951 CB LYS A 133 1.932 37.594 16.829 1.00 33.02 C ANISOU 951 CB LYS A 133 5293 4058 3193 103 -201 192 C ATOM 952 CG LYS A 133 2.830 38.816 17.047 1.00 35.82 C ANISOU 952 CG LYS A 133 5850 4256 3506 24 -183 205 C ATOM 953 CD LYS A 133 2.382 39.594 18.278 1.00 38.27 C ANISOU 953 CD LYS A 133 6274 4488 3777 116 -202 171 C ATOM 954 CE LYS A 133 3.075 40.948 18.324 1.00 34.31 C ANISOU 954 CE LYS A 133 6008 3784 3244 52 -225 173 C ATOM 955 NZ LYS A 133 2.613 41.691 19.512 1.00 37.85 N ANISOU 955 NZ LYS A 133 6617 4139 3625 171 -256 114 N ATOM 956 N TYR A 134 1.722 34.247 17.573 1.00 34.15 N ANISOU 956 N TYR A 134 4936 4459 3580 13 -204 154 N ATOM 957 CA TYR A 134 1.127 33.091 16.892 1.00 39.63 C ANISOU 957 CA TYR A 134 5471 5222 4366 23 -258 137 C ATOM 958 C TYR A 134 -0.322 32.779 17.301 1.00 40.56 C ANISOU 958 C TYR A 134 5432 5385 4594 129 -284 166 C ATOM 959 O TYR A 134 -1.157 32.479 16.447 1.00 43.93 O ANISOU 959 O TYR A 134 5780 5830 5083 179 -389 151 O ATOM 960 CB TYR A 134 1.990 31.819 16.979 1.00 40.75 C ANISOU 960 CB TYR A 134 5500 5393 4590 -91 -240 115 C ATOM 961 CG TYR A 134 1.405 30.722 16.112 1.00 39.96 C ANISOU 961 CG TYR A 134 5289 5320 4573 -80 -326 75 C ATOM 962 CD1 TYR A 134 0.621 29.714 16.661 1.00 39.64 C ANISOU 962 CD1 TYR A 134 5055 5305 4700 -81 -354 91 C ATOM 963 CD2 TYR A 134 1.573 30.745 14.734 1.00 41.65 C ANISOU 963 CD2 TYR A 134 5614 5515 4695 -61 -385 23 C ATOM 964 CE1 TYR A 134 0.048 28.737 15.863 1.00 44.20 C ANISOU 964 CE1 TYR A 134 5535 5873 5386 -87 -475 40 C ATOM 965 CE2 TYR A 134 1.009 29.764 13.917 1.00 46.01 C ANISOU 965 CE2 TYR A 134 6109 6069 5303 -40 -512 -43 C ATOM 966 CZ TYR A 134 0.245 28.767 14.491 1.00 49.07 C ANISOU 966 CZ TYR A 134 6287 6466 5893 -64 -574 -42 C ATOM 967 OH TYR A 134 -0.326 27.800 13.704 1.00 49.02 O ANISOU 967 OH TYR A 134 6222 6428 5975 -62 -737 -119 O ATOM 968 N LEU A 135 -0.616 32.874 18.594 1.00 37.00 N ANISOU 968 N LEU A 135 4940 4948 4170 173 -192 213 N ATOM 969 CA LEU A 135 -1.953 32.555 19.107 1.00 43.53 C ANISOU 969 CA LEU A 135 5585 5821 5134 279 -153 276 C ATOM 970 C LEU A 135 -3.029 33.530 18.624 1.00 44.98 C ANISOU 970 C LEU A 135 5783 5993 5315 432 -194 291 C ATOM 971 O LEU A 135 -4.213 33.190 18.626 1.00 45.91 O ANISOU 971 O LEU A 135 5686 6150 5606 512 -205 342 O ATOM 972 CB LEU A 135 -1.961 32.511 20.641 1.00 35.58 C ANISOU 972 CB LEU A 135 4586 4829 4104 326 3 338 C ATOM 973 CG LEU A 135 -1.072 31.458 21.312 1.00 41.19 C ANISOU 973 CG LEU A 135 5263 5553 4834 209 37 350 C ATOM 974 CD1 LEU A 135 -1.186 31.550 22.839 1.00 40.98 C ANISOU 974 CD1 LEU A 135 5307 5536 4726 301 183 421 C ATOM 975 CD2 LEU A 135 -1.462 30.073 20.862 1.00 33.76 C ANISOU 975 CD2 LEU A 135 4083 4639 4106 131 -1 376 C ATOM 976 N LYS A 136 -2.619 34.733 18.221 1.00 40.30 N ANISOU 976 N LYS A 136 5425 5334 4553 473 -219 259 N ATOM 977 CA LYS A 136 -3.561 35.761 17.783 1.00 44.88 C ANISOU 977 CA LYS A 136 6057 5884 5112 641 -263 279 C ATOM 978 C LYS A 136 -3.588 35.854 16.260 1.00 42.43 C ANISOU 978 C LYS A 136 5805 5556 4762 632 -434 246 C ATOM 979 O LYS A 136 -4.349 36.637 15.681 1.00 44.01 O ANISOU 979 O LYS A 136 6056 5727 4940 776 -517 265 O ATOM 980 CB LYS A 136 -3.206 37.127 18.394 1.00 44.95 C ANISOU 980 CB LYS A 136 6330 5796 4954 721 -179 275 C ATOM 981 CG LYS A 136 -3.558 37.268 19.867 1.00 53.34 C ANISOU 981 CG LYS A 136 7389 6866 6010 826 -21 305 C ATOM 982 CD LYS A 136 -2.910 38.505 20.500 1.00 66.64 C ANISOU 982 CD LYS A 136 9393 8421 7505 867 16 259 C ATOM 983 CE LYS A 136 -3.463 39.823 19.944 1.00 78.54 C ANISOU 983 CE LYS A 136 11064 9824 8952 1025 -21 261 C ATOM 984 NZ LYS A 136 -2.622 41.000 20.364 1.00 81.00 N ANISOU 984 NZ LYS A 136 11713 9962 9103 1007 -28 203 N ATOM 985 N LEU A 137 -2.757 35.050 15.611 1.00 40.64 N ANISOU 985 N LEU A 137 5591 5341 4510 487 -485 198 N ATOM 986 CA LEU A 137 -2.628 35.124 14.158 1.00 45.22 C ANISOU 986 CA LEU A 137 6298 5899 4986 496 -623 162 C ATOM 987 C LEU A 137 -3.888 34.586 13.460 1.00 50.03 C ANISOU 987 C LEU A 137 6738 6547 5723 586 -826 144 C ATOM 988 O LEU A 137 -4.341 33.470 13.746 1.00 49.40 O ANISOU 988 O LEU A 137 6414 6515 5843 529 -873 129 O ATOM 989 CB LEU A 137 -1.382 34.362 13.722 1.00 48.29 C ANISOU 989 CB LEU A 137 6749 6288 5311 345 -586 116 C ATOM 990 CG LEU A 137 -0.765 34.560 12.346 1.00 49.85 C ANISOU 990 CG LEU A 137 7168 6448 5324 349 -626 94 C ATOM 991 CD1 LEU A 137 -0.375 36.014 12.129 1.00 43.81 C ANISOU 991 CD1 LEU A 137 6646 5597 4404 393 -546 161 C ATOM 992 CD2 LEU A 137 0.452 33.633 12.218 1.00 44.53 C ANISOU 992 CD2 LEU A 137 6485 5789 4646 214 -533 56 C ATOM 993 N GLN A 138 -4.469 35.399 12.575 1.00 47.30 N ANISOU 993 N GLN A 138 6520 6169 5284 725 -961 154 N ATOM 994 CA GLN A 138 -5.680 35.012 11.844 1.00 50.92 C ANISOU 994 CA GLN A 138 6825 6653 5869 824 -1215 132 C ATOM 995 C GLN A 138 -5.454 33.773 10.988 1.00 55.76 C ANISOU 995 C GLN A 138 7420 7276 6490 727 -1385 33 C ATOM 996 O GLN A 138 -4.345 33.554 10.481 1.00 50.95 O ANISOU 996 O GLN A 138 7028 6645 5685 651 -1318 -12 O ATOM 997 CB GLN A 138 -6.186 36.158 10.961 1.00 45.31 C ANISOU 997 CB GLN A 138 6315 5893 5007 1008 -1355 162 C ATOM 998 CG GLN A 138 -6.876 37.275 11.736 1.00 52.50 C ANISOU 998 CG GLN A 138 7180 6782 5985 1160 -1258 249 C ATOM 999 CD GLN A 138 -7.447 38.346 10.835 1.00 59.49 C ANISOU 999 CD GLN A 138 8253 7606 6744 1361 -1420 287 C ATOM 1000 OE1 GLN A 138 -7.995 38.051 9.768 1.00 73.95 O ANISOU 1000 OE1 GLN A 138 10088 9449 8561 1432 -1694 254 O ATOM 1001 NE2 GLN A 138 -7.313 39.603 11.251 1.00 58.45 N ANISOU 1001 NE2 GLN A 138 8306 7393 6512 1463 -1274 351 N ATOM 1002 N ASP A 139 -6.510 32.973 10.837 1.00 53.46 N ANISOU 1002 N ASP A 139 6865 7004 6444 735 -1601 2 N ATOM 1003 CA ASP A 139 -6.445 31.707 10.115 1.00 53.27 C ANISOU 1003 CA ASP A 139 6809 6958 6471 643 -1803 -112 C ATOM 1004 C ASP A 139 -5.780 31.834 8.737 1.00 53.44 C ANISOU 1004 C ASP A 139 7212 6939 6153 699 -1927 -203 C ATOM 1005 O ASP A 139 -4.836 31.102 8.434 1.00 57.94 O ANISOU 1005 O ASP A 139 7916 7490 6607 611 -1859 -276 O ATOM 1006 CB ASP A 139 -7.851 31.114 9.983 1.00 59.88 C ANISOU 1006 CB ASP A 139 7320 7790 7640 665 -2089 -127 C ATOM 1007 CG ASP A 139 -8.335 30.468 11.268 1.00 66.11 C ANISOU 1007 CG ASP A 139 7717 8607 8795 562 -1931 -39 C ATOM 1008 OD1 ASP A 139 -7.498 29.886 11.990 1.00 75.15 O ANISOU 1008 OD1 ASP A 139 8866 9757 9931 435 -1705 -29 O ATOM 1009 OD2 ASP A 139 -9.548 30.536 11.557 1.00 76.30 O ANISOU 1009 OD2 ASP A 139 8691 9913 10386 620 -2023 34 O ATOM 1010 N THR A 140 -6.280 32.759 7.918 1.00 47.31 N ANISOU 1010 N THR A 140 6617 6145 5213 867 -2091 -186 N ATOM 1011 CA THR A 140 -5.655 33.110 6.637 1.00 56.58 C ANISOU 1011 CA THR A 140 8211 7278 6007 961 -2154 -230 C ATOM 1012 C THR A 140 -4.154 33.397 6.767 1.00 49.07 C ANISOU 1012 C THR A 140 7491 6319 4833 882 -1801 -186 C ATOM 1013 O THR A 140 -3.342 32.855 6.018 1.00 49.23 O ANISOU 1013 O THR A 140 7731 6321 4654 866 -1765 -254 O ATOM 1014 CB THR A 140 -6.345 34.331 6.000 1.00 54.67 C ANISOU 1014 CB THR A 140 8144 7013 5616 1167 -2309 -163 C ATOM 1015 OG1 THR A 140 -7.620 33.928 5.515 1.00 60.46 O ANISOU 1015 OG1 THR A 140 8710 7745 6519 1255 -2713 -229 O ATOM 1016 CG2 THR A 140 -5.530 34.903 4.824 1.00 48.22 C ANISOU 1016 CG2 THR A 140 7811 6146 4363 1271 -2264 -151 C ATOM 1017 N CYS A 141 -3.790 34.246 7.717 1.00 48.52 N ANISOU 1017 N CYS A 141 7369 6254 4810 840 -1546 -75 N ATOM 1018 CA CYS A 141 -2.384 34.551 7.939 1.00 47.42 C ANISOU 1018 CA CYS A 141 7389 6096 4534 740 -1239 -25 C ATOM 1019 C CYS A 141 -1.559 33.318 8.353 1.00 47.13 C ANISOU 1019 C CYS A 141 7217 6091 4601 582 -1125 -92 C ATOM 1020 O CYS A 141 -0.423 33.153 7.902 1.00 43.25 O ANISOU 1020 O CYS A 141 6894 5585 3956 539 -963 -94 O ATOM 1021 CB CYS A 141 -2.254 35.694 8.938 1.00 42.25 C ANISOU 1021 CB CYS A 141 6704 5413 3937 724 -1055 83 C ATOM 1022 SG CYS A 141 -3.084 37.232 8.374 1.00 51.77 S ANISOU 1022 SG CYS A 141 8123 6545 5001 935 -1163 173 S ATOM 1023 N ARG A 142 -2.129 32.435 9.173 1.00 47.84 N ANISOU 1023 N ARG A 142 7001 6217 4957 508 -1197 -133 N ATOM 1024 CA ARG A 142 -1.431 31.192 9.531 1.00 50.80 C ANISOU 1024 CA ARG A 142 7258 6604 5439 375 -1119 -192 C ATOM 1025 C ARG A 142 -1.196 30.322 8.307 1.00 55.37 C ANISOU 1025 C ARG A 142 8010 7151 5878 414 -1253 -313 C ATOM 1026 O ARG A 142 -0.081 29.846 8.077 1.00 50.67 O ANISOU 1026 O ARG A 142 7521 6546 5185 370 -1093 -340 O ATOM 1027 CB ARG A 142 -2.232 30.377 10.540 1.00 47.09 C ANISOU 1027 CB ARG A 142 6450 6158 5286 302 -1184 -194 C ATOM 1028 CG ARG A 142 -2.170 30.904 11.934 1.00 52.37 C ANISOU 1028 CG ARG A 142 6973 6859 6066 259 -987 -88 C ATOM 1029 CD ARG A 142 -3.180 30.216 12.819 1.00 50.92 C ANISOU 1029 CD ARG A 142 6473 6697 6176 230 -1031 -56 C ATOM 1030 NE ARG A 142 -3.076 30.736 14.182 1.00 61.47 N ANISOU 1030 NE ARG A 142 7732 8064 7558 223 -818 44 N ATOM 1031 CZ ARG A 142 -3.402 30.055 15.273 1.00 60.47 C ANISOU 1031 CZ ARG A 142 7385 7960 7632 174 -725 104 C ATOM 1032 NH1 ARG A 142 -3.872 28.818 15.171 1.00 62.61 N ANISOU 1032 NH1 ARG A 142 7453 8213 8122 102 -825 86 N ATOM 1033 NH2 ARG A 142 -3.262 30.616 16.463 1.00 57.96 N ANISOU 1033 NH2 ARG A 142 7071 7664 7285 202 -536 184 N ATOM 1034 N THR A 143 -2.265 30.108 7.538 1.00 53.76 N ANISOU 1034 N THR A 143 7831 6923 5674 508 -1560 -390 N ATOM 1035 CA THR A 143 -2.199 29.337 6.301 1.00 53.88 C ANISOU 1035 CA THR A 143 8071 6887 5516 579 -1753 -532 C ATOM 1036 C THR A 143 -1.143 29.923 5.365 1.00 53.77 C ANISOU 1036 C THR A 143 8447 6864 5120 679 -1565 -508 C ATOM 1037 O THR A 143 -0.315 29.194 4.815 1.00 52.15 O ANISOU 1037 O THR A 143 8407 6634 4774 691 -1475 -585 O ATOM 1038 CB THR A 143 -3.564 29.318 5.581 1.00 57.15 C ANISOU 1038 CB THR A 143 8484 7267 5963 687 -2166 -609 C ATOM 1039 OG1 THR A 143 -4.473 28.491 6.312 1.00 61.17 O ANISOU 1039 OG1 THR A 143 8608 7763 6872 576 -2336 -638 O ATOM 1040 CG2 THR A 143 -3.425 28.760 4.171 1.00 61.09 C ANISOU 1040 CG2 THR A 143 9336 7700 6177 805 -2386 -766 C ATOM 1041 N GLN A 144 -1.175 31.242 5.201 1.00 52.76 N ANISOU 1041 N GLN A 144 8463 6746 4837 759 -1483 -387 N ATOM 1042 CA GLN A 144 -0.212 31.942 4.358 1.00 54.06 C ANISOU 1042 CA GLN A 144 8984 6890 4667 846 -1263 -314 C ATOM 1043 C GLN A 144 1.224 31.831 4.866 1.00 50.09 C ANISOU 1043 C GLN A 144 8431 6401 4201 719 -885 -245 C ATOM 1044 O GLN A 144 2.141 31.642 4.069 1.00 49.81 O ANISOU 1044 O GLN A 144 8628 6349 3947 776 -705 -242 O ATOM 1045 CB GLN A 144 -0.617 33.407 4.187 1.00 46.20 C ANISOU 1045 CB GLN A 144 8131 5874 3550 943 -1262 -180 C ATOM 1046 CG GLN A 144 -1.862 33.580 3.325 1.00 46.29 C ANISOU 1046 CG GLN A 144 8283 5865 3440 1126 -1642 -238 C ATOM 1047 CD GLN A 144 -1.751 32.858 1.985 1.00 54.26 C ANISOU 1047 CD GLN A 144 9571 6837 4210 1239 -1763 -357 C ATOM 1048 OE1 GLN A 144 -2.331 31.787 1.794 1.00 54.91 O ANISOU 1048 OE1 GLN A 144 9547 6907 4410 1229 -2031 -517 O ATOM 1049 NE2 GLN A 144 -1.013 33.452 1.046 1.00 54.56 N ANISOU 1049 NE2 GLN A 144 9920 6832 3980 1331 -1528 -271 N ATOM 1050 N LEU A 145 1.413 31.930 6.183 1.00 48.23 N ANISOU 1050 N LEU A 145 7894 6193 4240 562 -770 -188 N ATOM 1051 CA LEU A 145 2.751 31.842 6.771 1.00 49.60 C ANISOU 1051 CA LEU A 145 7977 6375 4493 433 -466 -123 C ATOM 1052 C LEU A 145 3.381 30.483 6.492 1.00 53.14 C ANISOU 1052 C LEU A 145 8402 6832 4958 420 -422 -228 C ATOM 1053 O LEU A 145 4.558 30.405 6.146 1.00 54.08 O ANISOU 1053 O LEU A 145 8607 6947 4995 417 -169 -184 O ATOM 1054 CB LEU A 145 2.723 32.130 8.275 1.00 42.98 C ANISOU 1054 CB LEU A 145 6852 5556 3920 291 -418 -67 C ATOM 1055 CG LEU A 145 4.076 32.305 8.977 1.00 49.85 C ANISOU 1055 CG LEU A 145 7629 6423 4889 154 -161 13 C ATOM 1056 CD1 LEU A 145 4.950 33.345 8.274 1.00 38.41 C ANISOU 1056 CD1 LEU A 145 6394 4919 3280 167 48 130 C ATOM 1057 CD2 LEU A 145 3.912 32.675 10.466 1.00 40.78 C ANISOU 1057 CD2 LEU A 145 6267 5280 3945 48 -170 51 C ATOM 1058 N VAL A 146 2.586 29.420 6.628 1.00 46.98 N ANISOU 1058 N VAL A 146 7496 6050 4305 417 -661 -358 N ATOM 1059 CA VAL A 146 3.028 28.074 6.283 1.00 43.79 C ANISOU 1059 CA VAL A 146 7107 5619 3912 427 -668 -481 C ATOM 1060 C VAL A 146 3.441 27.997 4.814 1.00 53.50 C ANISOU 1060 C VAL A 146 8718 6815 4797 601 -626 -542 C ATOM 1061 O VAL A 146 4.481 27.427 4.476 1.00 55.50 O ANISOU 1061 O VAL A 146 9054 7057 4975 636 -411 -561 O ATOM 1062 CB VAL A 146 1.924 27.028 6.588 1.00 52.03 C ANISOU 1062 CB VAL A 146 7972 6627 5171 389 -979 -607 C ATOM 1063 CG1 VAL A 146 2.112 25.747 5.770 1.00 45.38 C ANISOU 1063 CG1 VAL A 146 7283 5707 4253 457 -1086 -777 C ATOM 1064 CG2 VAL A 146 1.890 26.718 8.072 1.00 43.38 C ANISOU 1064 CG2 VAL A 146 6522 5559 4402 228 -915 -538 C ATOM 1065 N TRP A 147 2.615 28.571 3.944 1.00 55.29 N ANISOU 1065 N TRP A 147 9184 7022 4802 734 -827 -565 N ATOM 1066 CA TRP A 147 2.947 28.656 2.532 1.00 61.80 C ANISOU 1066 CA TRP A 147 10437 7814 5231 933 -784 -603 C ATOM 1067 C TRP A 147 4.261 29.406 2.319 1.00 58.86 C ANISOU 1067 C TRP A 147 10188 7465 4713 948 -342 -429 C ATOM 1068 O TRP A 147 5.072 29.018 1.490 1.00 56.05 O ANISOU 1068 O TRP A 147 10072 7092 4131 1072 -136 -447 O ATOM 1069 CB TRP A 147 1.837 29.373 1.766 1.00 61.76 C ANISOU 1069 CB TRP A 147 10662 7788 5016 1074 -1082 -617 C ATOM 1070 CG TRP A 147 2.126 29.502 0.297 1.00 58.40 C ANISOU 1070 CG TRP A 147 10609 7312 4269 1265 -1010 -618 C ATOM 1071 CD1 TRP A 147 1.809 28.605 -0.672 1.00 56.32 C ANISOU 1071 CD1 TRP A 147 10515 6977 3907 1383 -1209 -777 C ATOM 1072 CD2 TRP A 147 2.786 30.596 -0.366 1.00 55.22 C ANISOU 1072 CD2 TRP A 147 10421 6902 3657 1349 -706 -434 C ATOM 1073 NE1 TRP A 147 2.231 29.066 -1.897 1.00 62.62 N ANISOU 1073 NE1 TRP A 147 11642 7737 4415 1555 -1045 -708 N ATOM 1074 CE2 TRP A 147 2.833 30.284 -1.736 1.00 56.78 C ANISOU 1074 CE2 TRP A 147 10923 7037 3615 1533 -729 -492 C ATOM 1075 CE3 TRP A 147 3.342 31.801 0.070 1.00 53.38 C ANISOU 1075 CE3 TRP A 147 10154 6691 3435 1280 -422 -223 C ATOM 1076 CZ2 TRP A 147 3.412 31.135 -2.681 1.00 56.15 C ANISOU 1076 CZ2 TRP A 147 11109 6925 3300 1659 -466 -339 C ATOM 1077 CZ3 TRP A 147 3.914 32.643 -0.863 1.00 62.64 C ANISOU 1077 CZ3 TRP A 147 11567 7819 4412 1382 -170 -72 C ATOM 1078 CH2 TRP A 147 3.949 32.305 -2.226 1.00 62.06 C ANISOU 1078 CH2 TRP A 147 11791 7694 4094 1574 -185 -127 C ATOM 1079 N LEU A 148 4.458 30.491 3.061 1.00 58.56 N ANISOU 1079 N LEU A 148 9985 7451 4816 828 -194 -258 N ATOM 1080 CA LEU A 148 5.652 31.304 2.888 1.00 51.63 C ANISOU 1080 CA LEU A 148 9186 6569 3863 810 200 -74 C ATOM 1081 C LEU A 148 6.900 30.533 3.305 1.00 52.70 C ANISOU 1081 C LEU A 148 9122 6727 4174 721 476 -65 C ATOM 1082 O LEU A 148 7.867 30.463 2.541 1.00 51.32 O ANISOU 1082 O LEU A 148 9115 6545 3838 815 777 0 O ATOM 1083 CB LEU A 148 5.538 32.609 3.667 1.00 49.38 C ANISOU 1083 CB LEU A 148 8765 6269 3727 684 242 82 C ATOM 1084 CG LEU A 148 6.780 33.504 3.642 1.00 50.70 C ANISOU 1084 CG LEU A 148 8952 6400 3911 608 625 286 C ATOM 1085 CD1 LEU A 148 7.244 33.742 2.213 1.00 43.15 C ANISOU 1085 CD1 LEU A 148 8385 5413 2599 793 846 372 C ATOM 1086 CD2 LEU A 148 6.496 34.829 4.338 1.00 51.39 C ANISOU 1086 CD2 LEU A 148 8971 6432 4124 501 595 409 C ATOM 1087 N VAL A 149 6.880 29.948 4.501 1.00 46.99 N ANISOU 1087 N VAL A 149 8046 6030 3777 562 385 -117 N ATOM 1088 CA VAL A 149 8.036 29.183 4.970 1.00 55.33 C ANISOU 1088 CA VAL A 149 8892 7106 5025 488 605 -108 C ATOM 1089 C VAL A 149 8.448 28.081 3.978 1.00 62.06 C ANISOU 1089 C VAL A 149 9945 7940 5694 662 692 -223 C ATOM 1090 O VAL A 149 9.635 27.924 3.673 1.00 59.87 O ANISOU 1090 O VAL A 149 9666 7671 5411 705 1021 -146 O ATOM 1091 CB VAL A 149 7.815 28.596 6.372 1.00 47.06 C ANISOU 1091 CB VAL A 149 7488 6080 4311 325 449 -157 C ATOM 1092 CG1 VAL A 149 8.984 27.711 6.774 1.00 46.04 C ANISOU 1092 CG1 VAL A 149 7165 5964 4366 283 639 -153 C ATOM 1093 CG2 VAL A 149 7.653 29.713 7.392 1.00 43.92 C ANISOU 1093 CG2 VAL A 149 6925 5692 4069 177 427 -40 C ATOM 1094 N ARG A 150 7.474 27.337 3.456 1.00 60.35 N ANISOU 1094 N ARG A 150 9904 7688 5336 772 396 -406 N ATOM 1095 CA ARG A 150 7.773 26.310 2.464 1.00 53.52 C ANISOU 1095 CA ARG A 150 9302 6777 4256 963 436 -549 C ATOM 1096 C ARG A 150 8.450 26.925 1.242 1.00 59.90 C ANISOU 1096 C ARG A 150 10475 7587 4698 1156 745 -451 C ATOM 1097 O ARG A 150 9.388 26.358 0.682 1.00 63.45 O ANISOU 1097 O ARG A 150 11044 8026 5037 1291 1030 -459 O ATOM 1098 CB ARG A 150 6.502 25.562 2.045 1.00 61.72 C ANISOU 1098 CB ARG A 150 10501 7748 5201 1037 -2 -770 C ATOM 1099 CG ARG A 150 6.654 24.775 0.726 1.00 72.45 C ANISOU 1099 CG ARG A 150 12289 9031 6206 1289 -15 -939 C ATOM 1100 CD ARG A 150 5.326 24.260 0.191 1.00 75.74 C ANISOU 1100 CD ARG A 150 12894 9361 6523 1355 -513 -1153 C ATOM 1101 NE ARG A 150 5.011 22.929 0.700 1.00 82.65 N ANISOU 1101 NE ARG A 150 13594 10147 7664 1271 -747 -1333 N ATOM 1102 CZ ARG A 150 4.220 22.695 1.743 1.00 87.77 C ANISOU 1102 CZ ARG A 150 13866 10787 8694 1060 -991 -1335 C ATOM 1103 NH1 ARG A 150 3.650 23.710 2.387 1.00 80.77 N ANISOU 1103 NH1 ARG A 150 12758 9986 7944 935 -1038 -1187 N ATOM 1104 NH2 ARG A 150 3.995 21.446 2.138 1.00 91.14 N ANISOU 1104 NH2 ARG A 150 14152 11108 9368 987 -1171 -1475 N ATOM 1105 N GLU A 151 7.977 28.098 0.842 1.00 56.20 N ANISOU 1105 N GLU A 151 10186 7125 4043 1183 712 -342 N ATOM 1106 CA GLU A 151 8.547 28.800 -0.298 1.00 60.61 C ANISOU 1106 CA GLU A 151 11031 7666 4331 1335 994 -200 C ATOM 1107 C GLU A 151 9.967 29.274 0.041 1.00 58.39 C ANISOU 1107 C GLU A 151 10567 7418 4199 1250 1489 22 C ATOM 1108 O GLU A 151 10.827 29.349 -0.825 1.00 65.02 O ANISOU 1108 O GLU A 151 11510 8239 4955 1363 1796 124 O ATOM 1109 CB GLU A 151 7.637 29.970 -0.695 1.00 57.16 C ANISOU 1109 CB GLU A 151 10731 7203 3786 1347 793 -119 C ATOM 1110 CG GLU A 151 7.472 30.167 -2.179 1.00 72.21 C ANISOU 1110 CG GLU A 151 12979 9046 5412 1558 780 -113 C ATOM 1111 CD GLU A 151 7.251 28.867 -2.931 1.00 78.64 C ANISOU 1111 CD GLU A 151 13978 9818 6085 1720 604 -331 C ATOM 1112 OE1 GLU A 151 8.068 28.557 -3.823 1.00 81.36 O ANISOU 1112 OE1 GLU A 151 14514 10134 6266 1875 871 -300 O ATOM 1113 OE2 GLU A 151 6.270 28.154 -2.631 1.00 80.88 O ANISOU 1113 OE2 GLU A 151 14208 10083 6439 1692 200 -527 O ATOM 1114 N LEU A 152 10.203 29.578 1.314 1.00 57.14 N ANISOU 1114 N LEU A 152 10017 7289 4403 1011 1497 99 N ATOM 1115 CA LEU A 152 11.532 29.964 1.800 1.00 62.17 C ANISOU 1115 CA LEU A 152 10369 7942 5311 877 1878 296 C ATOM 1116 C LEU A 152 12.520 28.788 1.803 1.00 67.56 C ANISOU 1116 C LEU A 152 10903 8650 6117 941 2096 242 C ATOM 1117 O LEU A 152 13.698 28.948 1.463 1.00 61.78 O ANISOU 1117 O LEU A 152 10110 7925 5437 978 2513 404 O ATOM 1118 CB LEU A 152 11.437 30.562 3.206 1.00 53.95 C ANISOU 1118 CB LEU A 152 8944 6907 4649 603 1725 356 C ATOM 1119 CG LEU A 152 10.895 31.988 3.270 1.00 55.39 C ANISOU 1119 CG LEU A 152 9227 7042 4777 527 1653 482 C ATOM 1120 CD1 LEU A 152 10.524 32.363 4.682 1.00 52.39 C ANISOU 1120 CD1 LEU A 152 8536 6660 4710 309 1420 466 C ATOM 1121 CD2 LEU A 152 11.926 32.949 2.731 1.00 56.12 C ANISOU 1121 CD2 LEU A 152 9381 7084 4856 509 2057 729 C ATOM 1122 N VAL A 153 12.036 27.617 2.208 1.00 65.66 N ANISOU 1122 N VAL A 153 10584 8409 5953 954 1822 29 N ATOM 1123 CA VAL A 153 12.844 26.410 2.188 1.00 62.68 C ANISOU 1123 CA VAL A 153 10106 8033 5677 1046 1983 -49 C ATOM 1124 C VAL A 153 13.292 26.084 0.761 1.00 65.11 C ANISOU 1124 C VAL A 153 10817 8318 5605 1345 2277 -67 C ATOM 1125 O VAL A 153 14.490 25.954 0.494 1.00 64.41 O ANISOU 1125 O VAL A 153 10643 8248 5582 1427 2698 57 O ATOM 1126 CB VAL A 153 12.082 25.231 2.797 1.00 58.53 C ANISOU 1126 CB VAL A 153 9488 7477 5276 1013 1605 -276 C ATOM 1127 CG1 VAL A 153 12.767 23.914 2.447 1.00 62.50 C ANISOU 1127 CG1 VAL A 153 10029 7940 5776 1183 1751 -391 C ATOM 1128 CG2 VAL A 153 11.976 25.404 4.307 1.00 43.87 C ANISOU 1128 CG2 VAL A 153 7205 5651 3814 748 1434 -222 C ATOM 1129 N LYS A 154 12.328 25.983 -0.150 1.00 64.16 N ANISOU 1129 N LYS A 154 11117 8153 5110 1509 2039 -212 N ATOM 1130 CA LYS A 154 12.605 25.675 -1.552 1.00 64.83 C ANISOU 1130 CA LYS A 154 11508 8184 4939 1742 2144 -235 C ATOM 1131 C LYS A 154 13.615 26.632 -2.176 1.00 67.44 C ANISOU 1131 C LYS A 154 11827 8532 5265 1771 2571 36 C ATOM 1132 O LYS A 154 14.438 26.225 -2.983 1.00 74.70 O ANISOU 1132 O LYS A 154 12846 9430 6108 1944 2848 75 O ATOM 1133 CB LYS A 154 11.307 25.684 -2.364 1.00 70.89 C ANISOU 1133 CB LYS A 154 12629 8888 5418 1841 1721 -390 C ATOM 1134 CG LYS A 154 10.335 24.560 -2.005 1.00 72.76 C ANISOU 1134 CG LYS A 154 12893 9071 5682 1833 1276 -674 C ATOM 1135 CD LYS A 154 8.892 24.922 -2.380 1.00 78.15 C ANISOU 1135 CD LYS A 154 13752 9712 6231 1824 804 -769 C ATOM 1136 CE LYS A 154 8.772 25.382 -3.829 1.00 83.44 C ANISOU 1136 CE LYS A 154 14786 10333 6586 2023 823 -717 C ATOM 1137 NZ LYS A 154 7.382 25.819 -4.165 1.00 84.40 N ANISOU 1137 NZ LYS A 154 15037 10414 6616 2021 371 -788 N ATOM 1138 N SER A 155 13.557 27.900 -1.787 1.00 73.83 N ANISOU 1138 N SER A 155 12514 9363 6173 1602 2620 225 N ATOM 1139 CA SER A 155 14.485 28.909 -2.294 1.00 73.06 C ANISOU 1139 CA SER A 155 12375 9255 6129 1590 3001 493 C ATOM 1140 C SER A 155 15.881 28.806 -1.675 1.00 71.06 C ANISOU 1140 C SER A 155 11707 9041 6253 1479 3382 653 C ATOM 1141 O SER A 155 16.805 29.498 -2.105 1.00 68.65 O ANISOU 1141 O SER A 155 11315 8717 6053 1468 3717 875 O ATOM 1142 CB SER A 155 13.926 30.310 -2.042 1.00 68.50 C ANISOU 1142 CB SER A 155 11804 8658 5565 1433 2891 632 C ATOM 1143 OG SER A 155 12.728 30.501 -2.760 1.00 68.76 O ANISOU 1143 OG SER A 155 12199 8649 5276 1560 2562 517 O ATOM 1144 N GLY A 156 16.026 27.964 -0.655 1.00 70.80 N ANISOU 1144 N GLY A 156 11397 9052 6452 1395 3317 547 N ATOM 1145 CA GLY A 156 17.302 27.807 0.020 1.00 69.19 C ANISOU 1145 CA GLY A 156 10746 8883 6660 1285 3613 688 C ATOM 1146 C GLY A 156 17.741 29.044 0.790 1.00 71.78 C ANISOU 1146 C GLY A 156 10744 9210 7320 1005 3697 918 C ATOM 1147 O GLY A 156 18.940 29.308 0.932 1.00 70.22 O ANISOU 1147 O GLY A 156 10215 9012 7452 919 3969 1100 O ATOM 1148 N VAL A 157 16.772 29.796 1.304 1.00 68.13 N ANISOU 1148 N VAL A 157 10364 8731 6789 859 3435 903 N ATOM 1149 CA VAL A 157 17.061 31.006 2.064 1.00 71.49 C ANISOU 1149 CA VAL A 157 10528 9121 7512 586 3455 1096 C ATOM 1150 C VAL A 157 17.820 30.698 3.362 1.00 67.24 C ANISOU 1150 C VAL A 157 9482 8609 7459 373 3446 1129 C ATOM 1151 O VAL A 157 17.495 29.748 4.072 1.00 69.68 O ANISOU 1151 O VAL A 157 9661 8959 7856 366 3162 936 O ATOM 1152 CB VAL A 157 15.765 31.775 2.374 1.00 67.45 C ANISOU 1152 CB VAL A 157 10241 8576 6813 504 3132 1044 C ATOM 1153 CG1 VAL A 157 16.047 33.006 3.242 1.00 61.88 C ANISOU 1153 CG1 VAL A 157 9272 7799 6439 217 3092 1210 C ATOM 1154 CG2 VAL A 157 15.079 32.182 1.075 1.00 61.43 C ANISOU 1154 CG2 VAL A 157 9932 7777 5630 709 3088 1025 C ATOM 1155 N LEU A 158 18.831 31.509 3.655 1.00 69.31 N ANISOU 1155 N LEU A 158 9428 8827 8080 187 3620 1340 N ATOM 1156 CA LEU A 158 19.668 31.341 4.839 1.00 68.93 C ANISOU 1156 CA LEU A 158 8875 8786 8529 -24 3573 1388 C ATOM 1157 C LEU A 158 18.873 31.597 6.120 1.00 64.50 C ANISOU 1157 C LEU A 158 8224 8206 8075 -226 3082 1250 C ATOM 1158 O LEU A 158 18.252 32.646 6.273 1.00 68.16 O ANISOU 1158 O LEU A 158 8837 8600 8461 -342 2933 1282 O ATOM 1159 CB LEU A 158 20.859 32.296 4.766 1.00 75.61 C ANISOU 1159 CB LEU A 158 9438 9566 9724 -185 3739 1606 C ATOM 1160 CG LEU A 158 21.963 32.137 5.810 1.00 81.58 C ANISOU 1160 CG LEU A 158 9659 10323 11014 -378 3664 1659 C ATOM 1161 CD1 LEU A 158 22.465 30.711 5.792 1.00 87.10 C ANISOU 1161 CD1 LEU A 158 10202 11116 11774 -192 3754 1566 C ATOM 1162 CD2 LEU A 158 23.116 33.114 5.543 1.00 81.52 C ANISOU 1162 CD2 LEU A 158 9424 10239 11313 -516 3834 1869 C ATOM 1163 N GLY A 159 18.886 30.633 7.035 1.00 55.88 N ANISOU 1163 N GLY A 159 6912 7170 7151 -246 2837 1100 N ATOM 1164 CA GLY A 159 18.155 30.759 8.282 1.00 51.69 C ANISOU 1164 CA GLY A 159 6313 6629 6699 -402 2398 972 C ATOM 1165 C GLY A 159 16.809 30.058 8.267 1.00 58.89 C ANISOU 1165 C GLY A 159 7498 7582 7295 -271 2133 759 C ATOM 1166 O GLY A 159 16.120 30.019 9.295 1.00 64.39 O ANISOU 1166 O GLY A 159 8146 8281 8039 -366 1803 656 O ATOM 1167 N ALA A 160 16.432 29.499 7.116 1.00 54.65 N ANISOU 1167 N ALA A 160 7253 7068 6445 -48 2274 695 N ATOM 1168 CA ALA A 160 15.127 28.840 6.989 1.00 55.32 C ANISOU 1168 CA ALA A 160 7591 7169 6259 66 1999 492 C ATOM 1169 C ALA A 160 14.967 27.703 7.989 1.00 52.07 C ANISOU 1169 C ALA A 160 6973 6785 6028 36 1759 355 C ATOM 1170 O ALA A 160 13.862 27.455 8.494 1.00 51.39 O ANISOU 1170 O ALA A 160 6953 6698 5875 11 1457 231 O ATOM 1171 CB ALA A 160 14.908 28.336 5.567 1.00 56.07 C ANISOU 1171 CB ALA A 160 8040 7264 5998 320 2169 430 C ATOM 1172 N ASP A 161 16.066 27.005 8.269 1.00 51.19 N ANISOU 1172 N ASP A 161 6602 6690 6157 47 1907 393 N ATOM 1173 CA ASP A 161 16.011 25.894 9.213 1.00 48.91 C ANISOU 1173 CA ASP A 161 6128 6412 6043 33 1697 287 C ATOM 1174 C ASP A 161 15.651 26.421 10.599 1.00 47.45 C ANISOU 1174 C ASP A 161 5773 6229 6027 -170 1413 303 C ATOM 1175 O ASP A 161 14.812 25.819 11.294 1.00 48.84 O ANISOU 1175 O ASP A 161 5967 6404 6186 -180 1159 197 O ATOM 1176 CB ASP A 161 17.315 25.080 9.228 1.00 47.50 C ANISOU 1176 CB ASP A 161 5699 6247 6103 110 1911 339 C ATOM 1177 CG ASP A 161 18.506 25.888 9.700 1.00 55.17 C ANISOU 1177 CG ASP A 161 6338 7229 7393 -39 2050 528 C ATOM 1178 OD1 ASP A 161 18.494 27.138 9.544 1.00 52.77 O ANISOU 1178 OD1 ASP A 161 6074 6907 7071 -162 2107 637 O ATOM 1179 OD2 ASP A 161 19.462 25.272 10.223 1.00 63.49 O ANISOU 1179 OD2 ASP A 161 7086 8297 8740 -35 2086 570 O ATOM 1180 N GLY A 162 16.245 27.559 10.976 1.00 49.72 N ANISOU 1180 N GLY A 162 5921 6504 6467 -324 1460 439 N ATOM 1181 CA GLY A 162 15.869 28.260 12.201 1.00 43.84 C ANISOU 1181 CA GLY A 162 5098 5741 5821 -495 1194 443 C ATOM 1182 C GLY A 162 14.371 28.550 12.266 1.00 46.62 C ANISOU 1182 C GLY A 162 5704 6088 5923 -475 998 347 C ATOM 1183 O GLY A 162 13.705 28.253 13.275 1.00 48.59 O ANISOU 1183 O GLY A 162 5921 6347 6193 -511 765 279 O ATOM 1184 N VAL A 163 13.832 29.109 11.185 1.00 43.29 N ANISOU 1184 N VAL A 163 5531 5650 5266 -401 1101 353 N ATOM 1185 CA VAL A 163 12.402 29.382 11.112 1.00 47.97 C ANISOU 1185 CA VAL A 163 6344 6240 5644 -358 913 269 C ATOM 1186 C VAL A 163 11.566 28.115 11.305 1.00 49.13 C ANISOU 1186 C VAL A 163 6502 6415 5751 -275 741 129 C ATOM 1187 O VAL A 163 10.532 28.155 11.985 1.00 47.89 O ANISOU 1187 O VAL A 163 6354 6262 5582 -303 534 79 O ATOM 1188 CB VAL A 163 12.017 30.074 9.789 1.00 58.17 C ANISOU 1188 CB VAL A 163 7922 7506 6673 -258 1038 301 C ATOM 1189 CG1 VAL A 163 10.501 30.203 9.667 1.00 58.95 C ANISOU 1189 CG1 VAL A 163 8214 7606 6577 -189 806 205 C ATOM 1190 CG2 VAL A 163 12.655 31.439 9.715 1.00 49.51 C ANISOU 1190 CG2 VAL A 163 6826 6349 5635 -365 1185 460 C ATOM 1191 N CYS A 164 12.004 26.992 10.728 1.00 44.09 N ANISOU 1191 N CYS A 164 5859 5782 5112 -169 838 73 N ATOM 1192 CA CYS A 164 11.228 25.755 10.870 1.00 43.73 C ANISOU 1192 CA CYS A 164 5831 5724 5059 -104 664 -61 C ATOM 1193 C CYS A 164 11.173 25.301 12.320 1.00 44.45 C ANISOU 1193 C CYS A 164 5698 5824 5368 -207 514 -49 C ATOM 1194 O CYS A 164 10.115 24.884 12.802 1.00 46.17 O ANISOU 1194 O CYS A 164 5923 6030 5590 -219 329 -106 O ATOM 1195 CB CYS A 164 11.777 24.627 10.000 1.00 48.30 C ANISOU 1195 CB CYS A 164 6477 6277 5597 42 794 -136 C ATOM 1196 SG CYS A 164 11.405 24.814 8.229 1.00 54.51 S ANISOU 1196 SG CYS A 164 7649 7038 6024 230 894 -208 S ATOM 1197 N MET A 165 12.305 25.407 13.015 1.00 37.51 N ANISOU 1197 N MET A 165 4617 4961 4675 -278 592 39 N ATOM 1198 CA MET A 165 12.363 25.072 14.442 1.00 38.35 C ANISOU 1198 CA MET A 165 4547 5074 4951 -359 440 64 C ATOM 1199 C MET A 165 11.472 25.981 15.283 1.00 41.53 C ANISOU 1199 C MET A 165 5000 5484 5294 -441 289 84 C ATOM 1200 O MET A 165 10.775 25.517 16.187 1.00 45.02 O ANISOU 1200 O MET A 165 5415 5928 5764 -449 153 70 O ATOM 1201 CB MET A 165 13.807 25.131 14.955 1.00 32.61 C ANISOU 1201 CB MET A 165 3598 4356 4435 -411 513 152 C ATOM 1202 CG MET A 165 14.698 24.155 14.222 1.00 46.51 C ANISOU 1202 CG MET A 165 5282 6110 6281 -298 687 142 C ATOM 1203 SD MET A 165 16.304 23.907 14.976 1.00 56.09 S ANISOU 1203 SD MET A 165 6162 7335 7815 -335 723 246 S ATOM 1204 CE MET A 165 17.168 25.377 14.427 1.00 44.98 C ANISOU 1204 CE MET A 165 4675 5935 6479 -440 907 367 C ATOM 1205 N THR A 166 11.493 27.275 14.986 1.00 37.27 N ANISOU 1205 N THR A 166 4545 4939 4675 -489 333 127 N ATOM 1206 CA THR A 166 10.622 28.204 15.691 1.00 36.59 C ANISOU 1206 CA THR A 166 4542 4847 4516 -535 208 135 C ATOM 1207 C THR A 166 9.166 27.863 15.388 1.00 37.66 C ANISOU 1207 C THR A 166 4787 4993 4529 -454 126 69 C ATOM 1208 O THR A 166 8.292 27.980 16.258 1.00 33.53 O ANISOU 1208 O THR A 166 4262 4478 4002 -456 19 70 O ATOM 1209 CB THR A 166 10.910 29.652 15.301 1.00 37.87 C ANISOU 1209 CB THR A 166 4799 4968 4623 -592 274 192 C ATOM 1210 OG1 THR A 166 12.308 29.917 15.477 1.00 44.81 O ANISOU 1210 OG1 THR A 166 5529 5821 5676 -687 350 264 O ATOM 1211 CG2 THR A 166 10.115 30.601 16.179 1.00 39.43 C ANISOU 1211 CG2 THR A 166 5087 5138 4758 -621 140 191 C ATOM 1212 N PHE A 167 8.902 27.424 14.160 1.00 35.57 N ANISOU 1212 N PHE A 167 4620 4724 4172 -372 172 13 N ATOM 1213 CA PHE A 167 7.543 27.029 13.802 1.00 41.18 C ANISOU 1213 CA PHE A 167 5407 5429 4810 -305 45 -59 C ATOM 1214 C PHE A 167 7.136 25.795 14.610 1.00 44.34 C ANISOU 1214 C PHE A 167 5665 5821 5362 -319 -48 -84 C ATOM 1215 O PHE A 167 6.020 25.730 15.136 1.00 43.28 O ANISOU 1215 O PHE A 167 5492 5688 5265 -322 -153 -80 O ATOM 1216 CB PHE A 167 7.418 26.752 12.299 1.00 34.95 C ANISOU 1216 CB PHE A 167 4790 4619 3871 -203 70 -134 C ATOM 1217 CG PHE A 167 6.223 27.423 11.648 1.00 44.31 C ANISOU 1217 CG PHE A 167 6131 5799 4905 -140 -51 -163 C ATOM 1218 CD1 PHE A 167 5.039 27.623 12.358 1.00 45.76 C ANISOU 1218 CD1 PHE A 167 6234 5993 5160 -159 -202 -157 C ATOM 1219 CD2 PHE A 167 6.284 27.857 10.325 1.00 45.61 C ANISOU 1219 CD2 PHE A 167 6527 5948 4854 -42 -5 -184 C ATOM 1220 CE1 PHE A 167 3.936 28.244 11.755 1.00 47.77 C ANISOU 1220 CE1 PHE A 167 6599 6242 5308 -84 -329 -177 C ATOM 1221 CE2 PHE A 167 5.189 28.475 9.719 1.00 47.40 C ANISOU 1221 CE2 PHE A 167 6906 6166 4939 34 -151 -207 C ATOM 1222 CZ PHE A 167 4.013 28.663 10.433 1.00 47.93 C ANISOU 1222 CZ PHE A 167 6854 6244 5114 11 -326 -207 C ATOM 1223 N MET A 168 8.048 24.831 14.731 1.00 39.15 N ANISOU 1223 N MET A 168 4920 5146 4808 -321 8 -92 N ATOM 1224 CA MET A 168 7.717 23.573 15.393 1.00 40.21 C ANISOU 1224 CA MET A 168 4945 5244 5088 -327 -70 -104 C ATOM 1225 C MET A 168 7.380 23.804 16.858 1.00 42.13 C ANISOU 1225 C MET A 168 5092 5514 5402 -383 -114 -12 C ATOM 1226 O MET A 168 6.565 23.085 17.435 1.00 40.28 O ANISOU 1226 O MET A 168 4795 5251 5259 -388 -176 8 O ATOM 1227 CB MET A 168 8.862 22.560 15.267 1.00 43.60 C ANISOU 1227 CB MET A 168 5311 5639 5616 -294 7 -120 C ATOM 1228 CG MET A 168 8.931 21.842 13.931 1.00 47.67 C ANISOU 1228 CG MET A 168 5950 6097 6068 -198 38 -236 C ATOM 1229 SD MET A 168 10.116 20.467 13.945 1.00 52.35 S ANISOU 1229 SD MET A 168 6459 6626 6808 -125 127 -258 S ATOM 1230 CE MET A 168 11.623 21.316 14.446 1.00 35.93 C ANISOU 1230 CE MET A 168 4223 4634 4793 -159 289 -130 C ATOM 1231 N LYS A 169 8.013 24.818 17.447 1.00 36.13 N ANISOU 1231 N LYS A 169 4336 4794 4598 -421 -79 46 N ATOM 1232 CA LYS A 169 7.799 25.154 18.854 1.00 35.83 C ANISOU 1232 CA LYS A 169 4271 4775 4569 -446 -126 119 C ATOM 1233 C LYS A 169 6.359 25.653 19.108 1.00 40.37 C ANISOU 1233 C LYS A 169 4898 5362 5078 -415 -154 133 C ATOM 1234 O LYS A 169 5.887 25.628 20.247 1.00 36.98 O ANISOU 1234 O LYS A 169 4457 4944 4651 -399 -160 198 O ATOM 1235 CB LYS A 169 8.835 26.198 19.300 1.00 38.47 C ANISOU 1235 CB LYS A 169 4624 5120 4872 -497 -126 149 C ATOM 1236 CG LYS A 169 8.813 26.598 20.776 1.00 38.54 C ANISOU 1236 CG LYS A 169 4663 5132 4846 -504 -205 200 C ATOM 1237 CD LYS A 169 9.799 27.750 21.027 1.00 34.77 C ANISOU 1237 CD LYS A 169 4222 4632 4357 -574 -254 201 C ATOM 1238 CE LYS A 169 9.749 28.271 22.482 1.00 32.28 C ANISOU 1238 CE LYS A 169 4007 4300 3957 -561 -374 219 C ATOM 1239 NZ LYS A 169 10.174 27.256 23.515 1.00 33.82 N ANISOU 1239 NZ LYS A 169 4145 4507 4197 -528 -452 264 N ATOM 1240 N GLN A 170 5.650 26.083 18.059 1.00 35.47 N ANISOU 1240 N GLN A 170 4339 4740 4396 -388 -165 81 N ATOM 1241 CA GLN A 170 4.270 26.539 18.254 1.00 40.75 C ANISOU 1241 CA GLN A 170 5016 5422 5045 -344 -199 101 C ATOM 1242 C GLN A 170 3.282 25.370 18.231 1.00 41.52 C ANISOU 1242 C GLN A 170 4986 5493 5296 -338 -248 105 C ATOM 1243 O GLN A 170 2.097 25.550 18.521 1.00 37.43 O ANISOU 1243 O GLN A 170 4405 4985 4832 -305 -262 148 O ATOM 1244 CB GLN A 170 3.860 27.580 17.210 1.00 37.64 C ANISOU 1244 CB GLN A 170 4740 5030 4531 -303 -224 58 C ATOM 1245 CG GLN A 170 4.923 28.611 16.875 1.00 37.05 C ANISOU 1245 CG GLN A 170 4790 4946 4341 -331 -165 59 C ATOM 1246 CD GLN A 170 5.456 29.305 18.109 1.00 38.35 C ANISOU 1246 CD GLN A 170 4971 5105 4494 -368 -143 110 C ATOM 1247 OE1 GLN A 170 4.694 29.697 18.993 1.00 36.04 O ANISOU 1247 OE1 GLN A 170 4698 4819 4175 -322 -157 139 O ATOM 1248 NE2 GLN A 170 6.777 29.463 18.174 1.00 32.96 N ANISOU 1248 NE2 GLN A 170 4283 4404 3838 -443 -114 118 N ATOM 1249 N ILE A 171 3.761 24.180 17.870 1.00 35.76 N ANISOU 1249 N ILE A 171 4208 4715 4664 -369 -271 65 N ATOM 1250 CA ILE A 171 2.920 22.983 17.967 1.00 39.33 C ANISOU 1250 CA ILE A 171 4534 5102 5306 -390 -329 77 C ATOM 1251 C ILE A 171 2.942 22.529 19.417 1.00 36.65 C ANISOU 1251 C ILE A 171 4110 4763 5051 -405 -244 209 C ATOM 1252 O ILE A 171 3.964 22.040 19.908 1.00 45.99 O ANISOU 1252 O ILE A 171 5307 5934 6233 -414 -209 233 O ATOM 1253 CB ILE A 171 3.435 21.825 17.103 1.00 38.83 C ANISOU 1253 CB ILE A 171 4487 4952 5313 -403 -391 -23 C ATOM 1254 CG1 ILE A 171 3.688 22.275 15.672 1.00 38.26 C ANISOU 1254 CG1 ILE A 171 4568 4884 5086 -355 -440 -150 C ATOM 1255 CG2 ILE A 171 2.448 20.687 17.123 1.00 41.72 C ANISOU 1255 CG2 ILE A 171 4732 5215 5905 -445 -488 -20 C ATOM 1256 CD1 ILE A 171 4.633 21.334 14.912 1.00 37.11 C ANISOU 1256 CD1 ILE A 171 4497 4668 4933 -323 -429 -247 C ATOM 1257 N ALA A 172 1.825 22.706 20.108 1.00 35.63 N ANISOU 1257 N ALA A 172 3898 4650 4989 -388 -202 306 N ATOM 1258 CA ALA A 172 1.769 22.464 21.539 1.00 32.27 C ANISOU 1258 CA ALA A 172 3446 4235 4580 -367 -83 452 C ATOM 1259 C ALA A 172 1.632 20.974 21.841 1.00 42.64 C ANISOU 1259 C ALA A 172 4644 5450 6108 -418 -74 525 C ATOM 1260 O ALA A 172 0.855 20.272 21.180 1.00 43.12 O ANISOU 1260 O ALA A 172 4581 5429 6373 -473 -146 500 O ATOM 1261 CB ALA A 172 0.595 23.238 22.152 1.00 29.34 C ANISOU 1261 CB ALA A 172 3038 3917 4194 -300 12 546 C ATOM 1262 N GLY A 173 2.363 20.486 22.843 1.00 36.60 N ANISOU 1262 N GLY A 173 3928 4673 5306 -399 -9 617 N ATOM 1263 CA GLY A 173 2.141 19.125 23.303 1.00 39.18 C ANISOU 1263 CA GLY A 173 4163 4890 5835 -434 28 727 C ATOM 1264 C GLY A 173 0.818 19.050 24.067 1.00 46.71 C ANISOU 1264 C GLY A 173 5005 5834 6907 -424 170 901 C ATOM 1265 O GLY A 173 0.361 20.056 24.615 1.00 45.18 O ANISOU 1265 O GLY A 173 4856 5740 6571 -346 272 955 O ATOM 1266 N GLY A 174 0.192 17.874 24.086 1.00 47.41 N ANISOU 1266 N GLY A 174 4945 5792 7276 -498 190 994 N ATOM 1267 CA GLY A 174 -1.043 17.672 24.828 1.00 41.16 C ANISOU 1267 CA GLY A 174 4003 4976 6661 -499 364 1199 C ATOM 1268 C GLY A 174 -2.202 18.507 24.320 1.00 43.84 C ANISOU 1268 C GLY A 174 4194 5379 7084 -497 362 1172 C ATOM 1269 O GLY A 174 -3.034 18.959 25.098 1.00 46.81 O ANISOU 1269 O GLY A 174 4500 5814 7471 -424 561 1333 O ATOM 1270 N ASP A 175 -2.260 18.705 23.009 1.00 45.59 N ANISOU 1270 N ASP A 175 4380 5586 7356 -554 142 974 N ATOM 1271 CA ASP A 175 -3.258 19.583 22.402 1.00 45.40 C ANISOU 1271 CA ASP A 175 4239 5626 7385 -532 85 926 C ATOM 1272 C ASP A 175 -3.667 18.940 21.079 1.00 44.83 C ANISOU 1272 C ASP A 175 4048 5435 7551 -646 -183 777 C ATOM 1273 O ASP A 175 -2.894 18.941 20.112 1.00 44.77 O ANISOU 1273 O ASP A 175 4202 5411 7399 -653 -360 581 O ATOM 1274 CB ASP A 175 -2.621 20.967 22.163 1.00 50.64 C ANISOU 1274 CB ASP A 175 5119 6427 7694 -427 62 802 C ATOM 1275 CG ASP A 175 -3.570 21.983 21.503 1.00 54.77 C ANISOU 1275 CG ASP A 175 5563 7014 8233 -373 -7 750 C ATOM 1276 OD1 ASP A 175 -4.587 21.584 20.888 1.00 50.27 O ANISOU 1276 OD1 ASP A 175 4773 6383 7947 -432 -125 749 O ATOM 1277 OD2 ASP A 175 -3.272 23.206 21.585 1.00 49.31 O ANISOU 1277 OD2 ASP A 175 5036 6420 7279 -271 33 706 O ATOM 1278 N VAL A 176 -4.864 18.366 21.040 1.00 48.68 N ANISOU 1278 N VAL A 176 4259 5827 8409 -730 -213 872 N ATOM 1279 CA VAL A 176 -5.378 17.814 19.790 1.00 56.59 C ANISOU 1279 CA VAL A 176 5153 6699 9650 -836 -525 715 C ATOM 1280 C VAL A 176 -6.545 18.627 19.225 1.00 57.88 C ANISOU 1280 C VAL A 176 5132 6923 9936 -806 -650 694 C ATOM 1281 O VAL A 176 -7.438 18.074 18.598 1.00 60.35 O ANISOU 1281 O VAL A 176 5225 7113 10592 -910 -874 660 O ATOM 1282 CB VAL A 176 -5.740 16.300 19.889 1.00 56.07 C ANISOU 1282 CB VAL A 176 4910 6407 9987 -999 -587 786 C ATOM 1283 CG1 VAL A 176 -4.494 15.485 20.178 1.00 56.81 C ANISOU 1283 CG1 VAL A 176 5223 6422 9939 -1005 -531 760 C ATOM 1284 CG2 VAL A 176 -6.819 16.034 20.954 1.00 50.68 C ANISOU 1284 CG2 VAL A 176 3924 5697 9633 -1042 -348 1075 C ATOM 1285 N THR A 177 -6.537 19.942 19.443 1.00 55.36 N ANISOU 1285 N THR A 177 4904 6778 9353 -661 -529 710 N ATOM 1286 CA THR A 177 -7.511 20.802 18.771 1.00 56.46 C ANISOU 1286 CA THR A 177 4914 6976 9563 -599 -679 666 C ATOM 1287 C THR A 177 -7.187 20.824 17.276 1.00 54.59 C ANISOU 1287 C THR A 177 4854 6690 9197 -614 -1036 410 C ATOM 1288 O THR A 177 -6.031 20.602 16.876 1.00 45.20 O ANISOU 1288 O THR A 177 3944 5483 7748 -616 -1072 276 O ATOM 1289 CB THR A 177 -7.526 22.243 19.319 1.00 48.56 C ANISOU 1289 CB THR A 177 4016 6146 8288 -420 -471 730 C ATOM 1290 OG1 THR A 177 -6.221 22.817 19.184 1.00 48.68 O ANISOU 1290 OG1 THR A 177 4389 6223 7883 -363 -449 608 O ATOM 1291 CG2 THR A 177 -7.956 22.263 20.776 1.00 44.18 C ANISOU 1291 CG2 THR A 177 3321 5638 7825 -363 -110 978 C ATOM 1292 N ALA A 178 -8.219 21.077 16.471 1.00 47.33 N ANISOU 1292 N ALA A 178 3770 5748 8464 -607 -1293 354 N ATOM 1293 CA ALA A 178 -8.119 21.114 15.016 1.00 46.20 C ANISOU 1293 CA ALA A 178 3808 5551 8194 -594 -1663 119 C ATOM 1294 C ALA A 178 -6.992 22.022 14.519 1.00 44.95 C ANISOU 1294 C ALA A 178 4050 5498 7533 -467 -1611 -1 C ATOM 1295 O ALA A 178 -6.206 21.627 13.646 1.00 50.13 O ANISOU 1295 O ALA A 178 4965 6092 7990 -473 -1755 -174 O ATOM 1296 CB ALA A 178 -9.476 21.516 14.397 1.00 41.98 C ANISOU 1296 CB ALA A 178 3027 5010 7914 -565 -1939 112 C ATOM 1297 N LYS A 179 -6.877 23.221 15.082 1.00 46.27 N ANISOU 1297 N LYS A 179 4275 5807 7499 -349 -1389 95 N ATOM 1298 CA LYS A 179 -5.809 24.132 14.638 1.00 47.63 C ANISOU 1298 CA LYS A 179 4802 6054 7240 -252 -1330 5 C ATOM 1299 C LYS A 179 -4.403 23.630 14.964 1.00 49.08 C ANISOU 1299 C LYS A 179 5177 6227 7246 -306 -1165 -24 C ATOM 1300 O LYS A 179 -3.470 23.819 14.178 1.00 46.24 O ANISOU 1300 O LYS A 179 5081 5868 6621 -272 -1202 -143 O ATOM 1301 CB LYS A 179 -6.006 25.550 15.193 1.00 46.00 C ANISOU 1301 CB LYS A 179 4629 5967 6884 -122 -1151 108 C ATOM 1302 CG LYS A 179 -7.416 26.114 14.981 1.00 51.65 C ANISOU 1302 CG LYS A 179 5123 6703 7797 -35 -1282 161 C ATOM 1303 CD LYS A 179 -7.419 27.642 14.985 1.00 61.61 C ANISOU 1303 CD LYS A 179 6552 8049 8809 132 -1194 189 C ATOM 1304 CE LYS A 179 -8.841 28.200 15.091 1.00 69.30 C ANISOU 1304 CE LYS A 179 7255 9052 10022 247 -1251 284 C ATOM 1305 NZ LYS A 179 -9.768 27.591 14.089 1.00 79.16 N ANISOU 1305 NZ LYS A 179 8304 10237 11536 209 -1619 213 N ATOM 1306 N ASN A 180 -4.237 22.989 16.116 1.00 51.67 N ANISOU 1306 N ASN A 180 5370 6541 7721 -375 -972 99 N ATOM 1307 CA ASN A 180 -2.902 22.523 16.515 1.00 42.92 C ANISOU 1307 CA ASN A 180 4417 5423 6466 -409 -831 87 C ATOM 1308 C ASN A 180 -2.476 21.340 15.638 1.00 44.31 C ANISOU 1308 C ASN A 180 4660 5471 6703 -476 -1004 -55 C ATOM 1309 O ASN A 180 -1.355 21.283 15.149 1.00 44.06 O ANISOU 1309 O ASN A 180 4841 5440 6461 -448 -982 -153 O ATOM 1310 CB ASN A 180 -2.884 22.147 18.001 1.00 40.56 C ANISOU 1310 CB ASN A 180 3989 5138 6285 -439 -600 266 C ATOM 1311 CG ASN A 180 -1.474 21.988 18.550 1.00 47.41 C ANISOU 1311 CG ASN A 180 5026 6024 6963 -440 -466 269 C ATOM 1312 OD1 ASN A 180 -0.619 22.868 18.374 1.00 44.88 O ANISOU 1312 OD1 ASN A 180 4890 5775 6387 -388 -430 214 O ATOM 1313 ND2 ASN A 180 -1.221 20.858 19.221 1.00 39.08 N ANISOU 1313 ND2 ASN A 180 3898 4892 6058 -503 -402 346 N ATOM 1314 N ILE A 181 -3.408 20.420 15.416 1.00 50.99 N ANISOU 1314 N ILE A 181 5321 6196 7857 -558 -1177 -68 N ATOM 1315 CA ILE A 181 -3.180 19.262 14.558 1.00 52.55 C ANISOU 1315 CA ILE A 181 5597 6232 8136 -615 -1386 -225 C ATOM 1316 C ILE A 181 -2.864 19.697 13.140 1.00 51.43 C ANISOU 1316 C ILE A 181 5728 6097 7717 -520 -1577 -427 C ATOM 1317 O ILE A 181 -1.989 19.131 12.483 1.00 51.97 O ANISOU 1317 O ILE A 181 6014 6095 7635 -489 -1610 -563 O ATOM 1318 CB ILE A 181 -4.432 18.392 14.513 1.00 63.35 C ANISOU 1318 CB ILE A 181 6699 7450 9922 -733 -1592 -205 C ATOM 1319 CG1 ILE A 181 -4.679 17.753 15.875 1.00 74.39 C ANISOU 1319 CG1 ILE A 181 7851 8809 11606 -829 -1368 16 C ATOM 1320 CG2 ILE A 181 -4.327 17.338 13.421 1.00 56.20 C ANISOU 1320 CG2 ILE A 181 5927 6350 9077 -777 -1891 -419 C ATOM 1321 CD1 ILE A 181 -6.089 17.218 16.000 1.00 81.01 C ANISOU 1321 CD1 ILE A 181 8344 9530 12906 -949 -1502 108 C ATOM 1322 N TRP A 182 -3.601 20.695 12.667 1.00 52.24 N ANISOU 1322 N TRP A 182 5827 6277 7744 -452 -1691 -436 N ATOM 1323 CA TRP A 182 -3.337 21.288 11.368 1.00 48.95 C ANISOU 1323 CA TRP A 182 5703 5881 7013 -333 -1845 -591 C ATOM 1324 C TRP A 182 -1.886 21.739 11.270 1.00 44.44 C ANISOU 1324 C TRP A 182 5394 5388 6101 -260 -1598 -602 C ATOM 1325 O TRP A 182 -1.227 21.497 10.258 1.00 48.99 O ANISOU 1325 O TRP A 182 6238 5920 6457 -186 -1654 -743 O ATOM 1326 CB TRP A 182 -4.274 22.477 11.102 1.00 45.87 C ANISOU 1326 CB TRP A 182 5265 5582 6582 -251 -1951 -548 C ATOM 1327 CG TRP A 182 -3.874 23.246 9.867 1.00 49.96 C ANISOU 1327 CG TRP A 182 6131 6132 6717 -108 -2049 -665 C ATOM 1328 CD1 TRP A 182 -4.273 22.995 8.581 1.00 51.42 C ANISOU 1328 CD1 TRP A 182 6503 6234 6799 -38 -2382 -835 C ATOM 1329 CD2 TRP A 182 -2.986 24.375 9.798 1.00 44.05 C ANISOU 1329 CD2 TRP A 182 5606 5493 5637 -15 -1814 -611 C ATOM 1330 NE1 TRP A 182 -3.691 23.899 7.721 1.00 46.92 N ANISOU 1330 NE1 TRP A 182 6277 5726 5824 112 -2335 -873 N ATOM 1331 CE2 TRP A 182 -2.901 24.758 8.440 1.00 48.14 C ANISOU 1331 CE2 TRP A 182 6441 5992 5857 116 -1980 -730 C ATOM 1332 CE3 TRP A 182 -2.263 25.105 10.751 1.00 48.97 C ANISOU 1332 CE3 TRP A 182 6204 6210 6191 -30 -1496 -475 C ATOM 1333 CZ2 TRP A 182 -2.117 25.839 8.013 1.00 42.14 C ANISOU 1333 CZ2 TRP A 182 5950 5303 4758 220 -1797 -687 C ATOM 1334 CZ3 TRP A 182 -1.484 26.179 10.325 1.00 40.31 C ANISOU 1334 CZ3 TRP A 182 5357 5172 4787 54 -1354 -454 C ATOM 1335 CH2 TRP A 182 -1.420 26.534 8.971 1.00 43.18 C ANISOU 1335 CH2 TRP A 182 6010 5513 4883 173 -1484 -546 C ATOM 1336 N LEU A 183 -1.383 22.398 12.309 1.00 47.11 N ANISOU 1336 N LEU A 183 5663 5835 6403 -272 -1325 -453 N ATOM 1337 CA LEU A 183 0.010 22.871 12.269 1.00 46.74 C ANISOU 1337 CA LEU A 183 5812 5853 6096 -225 -1107 -447 C ATOM 1338 C LEU A 183 0.983 21.700 12.277 1.00 49.48 C ANISOU 1338 C LEU A 183 6198 6122 6481 -255 -1041 -504 C ATOM 1339 O LEU A 183 1.947 21.701 11.503 1.00 45.62 O ANISOU 1339 O LEU A 183 5916 5630 5786 -182 -971 -584 O ATOM 1340 CB LEU A 183 0.331 23.844 13.414 1.00 43.04 C ANISOU 1340 CB LEU A 183 5268 5491 5594 -239 -885 -293 C ATOM 1341 CG LEU A 183 1.743 24.459 13.362 1.00 43.88 C ANISOU 1341 CG LEU A 183 5538 5650 5484 -215 -694 -279 C ATOM 1342 CD1 LEU A 183 1.939 25.235 12.068 1.00 44.50 C ANISOU 1342 CD1 LEU A 183 5855 5738 5313 -124 -726 -348 C ATOM 1343 CD2 LEU A 183 2.056 25.356 14.574 1.00 41.66 C ANISOU 1343 CD2 LEU A 183 5196 5442 5193 -242 -534 -151 C ATOM 1344 N ALA A 184 0.728 20.700 13.130 1.00 40.09 N ANISOU 1344 N ALA A 184 4814 4861 5558 -347 -1043 -451 N ATOM 1345 CA ALA A 184 1.608 19.520 13.173 1.00 47.89 C ANISOU 1345 CA ALA A 184 5838 5752 6607 -361 -994 -500 C ATOM 1346 C ALA A 184 1.763 18.902 11.779 1.00 47.03 C ANISOU 1346 C ALA A 184 5952 5531 6387 -286 -1156 -702 C ATOM 1347 O ALA A 184 2.865 18.616 11.334 1.00 51.23 O ANISOU 1347 O ALA A 184 6644 6049 6770 -206 -1040 -767 O ATOM 1348 CB ALA A 184 1.099 18.487 14.163 1.00 42.40 C ANISOU 1348 CB ALA A 184 4923 4958 6229 -467 -1010 -407 C ATOM 1349 N GLU A 185 0.649 18.723 11.085 1.00 48.53 N ANISOU 1349 N GLU A 185 6154 5638 6645 -296 -1429 -803 N ATOM 1350 CA GLU A 185 0.687 18.082 9.784 1.00 55.50 C ANISOU 1350 CA GLU A 185 7291 6391 7405 -213 -1634 -1018 C ATOM 1351 C GLU A 185 1.311 18.999 8.737 1.00 56.26 C ANISOU 1351 C GLU A 185 7694 6584 7099 -52 -1557 -1087 C ATOM 1352 O GLU A 185 2.065 18.551 7.873 1.00 58.25 O ANISOU 1352 O GLU A 185 8212 6775 7148 69 -1524 -1219 O ATOM 1353 CB GLU A 185 -0.714 17.660 9.348 1.00 48.19 C ANISOU 1353 CB GLU A 185 6287 5336 6687 -278 -2007 -1113 C ATOM 1354 CG GLU A 185 -0.691 16.885 8.043 1.00 59.60 C ANISOU 1354 CG GLU A 185 8036 6611 8000 -188 -2274 -1366 C ATOM 1355 CD GLU A 185 -1.918 16.009 7.853 1.00 70.54 C ANISOU 1355 CD GLU A 185 9287 7792 9721 -307 -2672 -1468 C ATOM 1356 OE1 GLU A 185 -3.024 16.437 8.255 1.00 72.53 O ANISOU 1356 OE1 GLU A 185 9258 8084 10215 -408 -2804 -1364 O ATOM 1357 OE2 GLU A 185 -1.768 14.892 7.306 1.00 73.19 O ANISOU 1357 OE2 GLU A 185 9793 7917 10100 -298 -2853 -1650 O ATOM 1358 N SER A 186 0.992 20.283 8.828 1.00 55.07 N ANISOU 1358 N SER A 186 7515 6573 6835 -37 -1508 -984 N ATOM 1359 CA SER A 186 1.480 21.255 7.867 1.00 52.77 C ANISOU 1359 CA SER A 186 7510 6361 6178 106 -1426 -1010 C ATOM 1360 C SER A 186 2.994 21.318 7.870 1.00 50.40 C ANISOU 1360 C SER A 186 7315 6111 5722 163 -1091 -966 C ATOM 1361 O SER A 186 3.608 21.228 6.807 1.00 52.12 O ANISOU 1361 O SER A 186 7823 6304 5678 306 -1029 -1061 O ATOM 1362 CB SER A 186 0.873 22.628 8.139 1.00 48.11 C ANISOU 1362 CB SER A 186 6846 5891 5545 100 -1418 -883 C ATOM 1363 OG SER A 186 -0.517 22.605 7.860 1.00 56.93 O ANISOU 1363 OG SER A 186 7886 6960 6785 91 -1747 -937 O ATOM 1364 N VAL A 187 3.590 21.462 9.059 1.00 45.61 N ANISOU 1364 N VAL A 187 6477 5573 5279 64 -879 -819 N ATOM 1365 CA VAL A 187 5.049 21.519 9.192 1.00 46.18 C ANISOU 1365 CA VAL A 187 6574 5693 5281 98 -583 -758 C ATOM 1366 C VAL A 187 5.692 20.185 8.794 1.00 51.82 C ANISOU 1366 C VAL A 187 7368 6295 6024 169 -558 -876 C ATOM 1367 O VAL A 187 6.726 20.159 8.123 1.00 55.01 O ANISOU 1367 O VAL A 187 7931 6709 6262 290 -357 -900 O ATOM 1368 CB VAL A 187 5.478 21.896 10.628 1.00 48.55 C ANISOU 1368 CB VAL A 187 6609 6072 5767 -25 -437 -591 C ATOM 1369 CG1 VAL A 187 6.984 21.907 10.755 1.00 43.94 C ANISOU 1369 CG1 VAL A 187 6005 5526 5165 1 -182 -531 C ATOM 1370 CG2 VAL A 187 4.915 23.242 11.019 1.00 42.36 C ANISOU 1370 CG2 VAL A 187 5786 5377 4934 -69 -444 -490 C ATOM 1371 N LEU A 188 5.071 19.077 9.193 1.00 50.20 N ANISOU 1371 N LEU A 188 7056 5971 6045 103 -746 -942 N ATOM 1372 CA LEU A 188 5.574 17.758 8.810 1.00 51.47 C ANISOU 1372 CA LEU A 188 7319 5987 6250 178 -757 -1071 C ATOM 1373 C LEU A 188 5.635 17.620 7.289 1.00 53.33 C ANISOU 1373 C LEU A 188 7924 6153 6184 360 -822 -1259 C ATOM 1374 O LEU A 188 6.601 17.084 6.746 1.00 59.02 O ANISOU 1374 O LEU A 188 8811 6827 6786 506 -653 -1330 O ATOM 1375 CB LEU A 188 4.707 16.650 9.407 1.00 50.06 C ANISOU 1375 CB LEU A 188 6986 5655 6381 59 -988 -1108 C ATOM 1376 CG LEU A 188 5.122 15.212 9.088 1.00 54.58 C ANISOU 1376 CG LEU A 188 7669 6028 7038 126 -1035 -1247 C ATOM 1377 CD1 LEU A 188 6.511 14.893 9.643 1.00 51.97 C ANISOU 1377 CD1 LEU A 188 7263 5737 6747 188 -742 -1155 C ATOM 1378 CD2 LEU A 188 4.085 14.220 9.613 1.00 55.02 C ANISOU 1378 CD2 LEU A 188 7572 5903 7430 -22 -1293 -1268 C ATOM 1379 N ASP A 189 4.611 18.126 6.606 1.00 52.09 N ANISOU 1379 N ASP A 189 7908 5992 5892 374 -1061 -1334 N ATOM 1380 CA ASP A 189 4.539 18.020 5.149 1.00 57.00 C ANISOU 1380 CA ASP A 189 8934 6540 6182 564 -1177 -1522 C ATOM 1381 C ASP A 189 5.691 18.764 4.470 1.00 57.62 C ANISOU 1381 C ASP A 189 9235 6732 5926 736 -822 -1459 C ATOM 1382 O ASP A 189 6.294 18.255 3.526 1.00 60.33 O ANISOU 1382 O ASP A 189 9889 7004 6031 932 -727 -1585 O ATOM 1383 CB ASP A 189 3.185 18.525 4.642 1.00 57.89 C ANISOU 1383 CB ASP A 189 9125 6639 6233 544 -1537 -1589 C ATOM 1384 CG ASP A 189 2.083 17.489 4.785 1.00 77.08 C ANISOU 1384 CG ASP A 189 11443 8887 8955 430 -1937 -1725 C ATOM 1385 OD1 ASP A 189 2.324 16.424 5.401 1.00 84.65 O ANISOU 1385 OD1 ASP A 189 12253 9730 10179 346 -1915 -1741 O ATOM 1386 OD2 ASP A 189 0.968 17.741 4.282 1.00 86.00 O ANISOU 1386 OD2 ASP A 189 12623 9979 10073 421 -2284 -1805 O ATOM 1387 N ILE A 190 5.988 19.965 4.962 1.00 51.14 N ANISOU 1387 N ILE A 190 8259 6072 5100 666 -615 -1258 N ATOM 1388 CA ILE A 190 7.158 20.719 4.523 1.00 52.67 C ANISOU 1388 CA ILE A 190 8570 6365 5075 778 -237 -1144 C ATOM 1389 C ILE A 190 8.438 19.908 4.731 1.00 57.86 C ANISOU 1389 C ILE A 190 9146 7000 5836 838 46 -1131 C ATOM 1390 O ILE A 190 9.236 19.761 3.811 1.00 63.59 O ANISOU 1390 O ILE A 190 10118 7712 6330 1035 278 -1169 O ATOM 1391 CB ILE A 190 7.289 22.053 5.291 1.00 49.30 C ANISOU 1391 CB ILE A 190 7919 6078 4735 638 -94 -925 C ATOM 1392 CG1 ILE A 190 6.131 23.002 4.950 1.00 49.01 C ANISOU 1392 CG1 ILE A 190 7995 6066 4559 629 -322 -920 C ATOM 1393 CG2 ILE A 190 8.619 22.713 4.994 1.00 42.72 C ANISOU 1393 CG2 ILE A 190 7125 5320 3787 707 310 -783 C ATOM 1394 CD1 ILE A 190 6.131 24.281 5.802 1.00 44.43 C ANISOU 1394 CD1 ILE A 190 7206 5590 4085 493 -218 -726 C ATOM 1395 N LEU A 191 8.625 19.379 5.939 1.00 54.30 N ANISOU 1395 N LEU A 191 8360 6543 5728 689 35 -1070 N ATOM 1396 CA LEU A 191 9.845 18.637 6.259 1.00 59.26 C ANISOU 1396 CA LEU A 191 8865 7152 6497 747 280 -1038 C ATOM 1397 C LEU A 191 10.041 17.390 5.390 1.00 61.85 C ANISOU 1397 C LEU A 191 9460 7326 6714 947 261 -1239 C ATOM 1398 O LEU A 191 11.151 17.129 4.923 1.00 65.36 O ANISOU 1398 O LEU A 191 9983 7775 7077 1120 561 -1229 O ATOM 1399 CB LEU A 191 9.900 18.264 7.752 1.00 53.83 C ANISOU 1399 CB LEU A 191 7804 6473 6176 565 218 -935 C ATOM 1400 CG LEU A 191 9.957 19.441 8.728 1.00 53.91 C ANISOU 1400 CG LEU A 191 7567 6625 6293 396 273 -742 C ATOM 1401 CD1 LEU A 191 10.003 18.979 10.187 1.00 50.84 C ANISOU 1401 CD1 LEU A 191 6876 6232 6208 255 200 -652 C ATOM 1402 CD2 LEU A 191 11.136 20.348 8.417 1.00 55.15 C ANISOU 1402 CD2 LEU A 191 7704 6885 6365 445 589 -615 C ATOM 1403 N THR A 192 8.972 16.626 5.170 1.00 58.79 N ANISOU 1403 N THR A 192 9208 6789 6339 929 -90 -1420 N ATOM 1404 CA THR A 192 9.081 15.377 4.410 1.00 58.06 C ANISOU 1404 CA THR A 192 9396 6506 6160 1109 -167 -1641 C ATOM 1405 C THR A 192 9.298 15.640 2.918 1.00 67.41 C ANISOU 1405 C THR A 192 11041 7679 6892 1371 -67 -1767 C ATOM 1406 O THR A 192 10.142 15.004 2.280 1.00 68.07 O ANISOU 1406 O THR A 192 11343 7692 6828 1601 151 -1855 O ATOM 1407 CB THR A 192 7.852 14.452 4.607 1.00 61.92 C ANISOU 1407 CB THR A 192 9889 6800 6839 989 -610 -1803 C ATOM 1408 OG1 THR A 192 6.690 15.062 4.035 1.00 77.49 O ANISOU 1408 OG1 THR A 192 12010 8778 8654 948 -908 -1878 O ATOM 1409 CG2 THR A 192 7.599 14.192 6.079 1.00 52.33 C ANISOU 1409 CG2 THR A 192 8248 5592 6044 748 -669 -1650 C ATOM 1410 N GLU A 193 8.529 16.577 2.368 1.00 67.74 N ANISOU 1410 N GLU A 193 11248 7789 6702 1359 -216 -1767 N ATOM 1411 CA GLU A 193 8.662 16.963 0.958 1.00 73.82 C ANISOU 1411 CA GLU A 193 12495 8559 6992 1617 -128 -1858 C ATOM 1412 C GLU A 193 10.055 17.542 0.657 1.00 68.88 C ANISOU 1412 C GLU A 193 11892 8067 6211 1771 422 -1680 C ATOM 1413 O GLU A 193 10.557 17.425 -0.453 1.00 69.92 O ANISOU 1413 O GLU A 193 12381 8174 6011 2026 621 -1734 O ATOM 1414 CB GLU A 193 7.560 17.968 0.589 1.00 74.65 C ANISOU 1414 CB GLU A 193 12718 8724 6922 1556 -404 -1847 C ATOM 1415 CG GLU A 193 7.773 18.758 -0.698 1.00 87.34 C ANISOU 1415 CG GLU A 193 14677 10400 8109 1755 -243 -1784 C ATOM 1416 CD GLU A 193 7.006 20.082 -0.703 1.00 96.55 C ANISOU 1416 CD GLU A 193 15809 11675 9199 1658 -372 -1651 C ATOM 1417 OE1 GLU A 193 7.296 20.942 -1.569 1.00 94.76 O ANISOU 1417 OE1 GLU A 193 15777 11519 8710 1778 -175 -1515 O ATOM 1418 OE2 GLU A 193 6.117 20.262 0.167 1.00 98.79 O ANISOU 1418 OE2 GLU A 193 15866 11964 9707 1468 -665 -1673 O ATOM 1419 N GLN A 194 10.679 18.151 1.659 1.00 63.82 N ANISOU 1419 N GLN A 194 10825 7565 5860 1595 658 -1441 N ATOM 1420 CA GLN A 194 11.972 18.794 1.469 1.00 63.50 C ANISOU 1420 CA GLN A 194 10719 7645 5764 1689 1158 -1241 C ATOM 1421 C GLN A 194 13.047 18.119 2.317 1.00 68.10 C ANISOU 1421 C GLN A 194 10936 8233 6705 1656 1383 -1159 C ATOM 1422 O GLN A 194 13.930 18.783 2.858 1.00 70.28 O ANISOU 1422 O GLN A 194 10900 8630 7175 1567 1666 -938 O ATOM 1423 CB GLN A 194 11.862 20.277 1.830 1.00 55.26 C ANISOU 1423 CB GLN A 194 9501 6746 4749 1513 1229 -1017 C ATOM 1424 CG GLN A 194 10.848 21.033 0.997 1.00 61.18 C ANISOU 1424 CG GLN A 194 10601 7494 5150 1565 1020 -1067 C ATOM 1425 CD GLN A 194 11.314 21.216 -0.426 1.00 73.82 C ANISOU 1425 CD GLN A 194 12669 9085 6296 1863 1291 -1082 C ATOM 1426 OE1 GLN A 194 12.509 21.357 -0.681 1.00 80.80 O ANISOU 1426 OE1 GLN A 194 13480 10019 7201 1950 1731 -924 O ATOM 1427 NE2 GLN A 194 10.375 21.210 -1.368 1.00 77.85 N ANISOU 1427 NE2 GLN A 194 13478 9529 6572 1935 963 -1191 N ATOM 1428 N ARG A 195 12.964 16.797 2.428 1.00 70.10 N ANISOU 1428 N ARG A 195 11232 8340 7061 1729 1231 -1338 N ATOM 1429 CA ARG A 195 13.849 16.041 3.305 1.00 68.29 C ANISOU 1429 CA ARG A 195 10663 8093 7190 1704 1371 -1273 C ATOM 1430 C ARG A 195 15.323 16.217 2.938 1.00 67.31 C ANISOU 1430 C ARG A 195 10462 8053 7060 1893 1882 -1128 C ATOM 1431 O ARG A 195 16.181 16.238 3.821 1.00 64.02 O ANISOU 1431 O ARG A 195 9635 7705 6983 1803 2039 -963 O ATOM 1432 CB ARG A 195 13.463 14.561 3.285 1.00 73.95 C ANISOU 1432 CB ARG A 195 11527 8596 7974 1789 1125 -1505 C ATOM 1433 CG ARG A 195 14.061 13.714 4.401 1.00 71.92 C ANISOU 1433 CG ARG A 195 10909 8291 8125 1719 1146 -1438 C ATOM 1434 CD ARG A 195 13.577 12.282 4.268 1.00 74.69 C ANISOU 1434 CD ARG A 195 11462 8391 8525 1803 888 -1672 C ATOM 1435 NE ARG A 195 14.182 11.371 5.234 1.00 73.90 N ANISOU 1435 NE ARG A 195 11076 8215 8787 1782 920 -1609 N ATOM 1436 CZ ARG A 195 15.363 10.785 5.067 1.00 73.32 C ANISOU 1436 CZ ARG A 195 10976 8112 8772 2015 1225 -1593 C ATOM 1437 NH1 ARG A 195 16.082 11.039 3.977 1.00 82.92 N ANISOU 1437 NH1 ARG A 195 12422 9377 9708 2284 1567 -1624 N ATOM 1438 NH2 ARG A 195 15.832 9.955 5.991 1.00 60.32 N ANISOU 1438 NH2 ARG A 195 9070 6385 7463 1996 1206 -1531 N ATOM 1439 N GLU A 196 15.616 16.355 1.646 1.00 71.19 N ANISOU 1439 N GLU A 196 11342 8536 7172 2161 2140 -1181 N ATOM 1440 CA GLU A 196 17.001 16.533 1.210 1.00 77.15 C ANISOU 1440 CA GLU A 196 12019 9368 7925 2362 2682 -1020 C ATOM 1441 C GLU A 196 17.578 17.797 1.838 1.00 77.05 C ANISOU 1441 C GLU A 196 11593 9529 8152 2139 2885 -720 C ATOM 1442 O GLU A 196 18.707 17.810 2.323 1.00 78.49 O ANISOU 1442 O GLU A 196 11395 9777 8652 2129 3170 -547 O ATOM 1443 CB GLU A 196 17.113 16.607 -0.314 1.00 79.75 C ANISOU 1443 CB GLU A 196 12783 9681 7836 2595 2837 -1057 C ATOM 1444 CG GLU A 196 18.563 16.579 -0.796 1.00 97.44 C ANISOU 1444 CG GLU A 196 14868 11987 10168 2751 3318 -866 C ATOM 1445 CD GLU A 196 18.738 17.056 -2.232 1.00108.55 C ANISOU 1445 CD GLU A 196 16628 13411 11205 2910 3498 -795 C ATOM 1446 OE1 GLU A 196 18.199 18.134 -2.570 1.00113.98 O ANISOU 1446 OE1 GLU A 196 17447 14154 11705 2811 3437 -705 O ATOM 1447 OE2 GLU A 196 19.424 16.358 -3.015 1.00108.27 O ANISOU 1447 OE2 GLU A 196 16745 13324 11069 3148 3708 -821 O ATOM 1448 N TRP A 197 16.780 18.857 1.842 1.00 73.31 N ANISOU 1448 N TRP A 197 11193 9114 7547 1960 2706 -666 N ATOM 1449 CA TRP A 197 17.191 20.105 2.457 1.00 69.54 C ANISOU 1449 CA TRP A 197 10370 8764 7290 1728 2834 -407 C ATOM 1450 C TRP A 197 17.338 19.957 3.986 1.00 65.08 C ANISOU 1450 C TRP A 197 9312 8226 7192 1465 2615 -343 C ATOM 1451 O TRP A 197 18.310 20.451 4.562 1.00 62.99 O ANISOU 1451 O TRP A 197 8668 8035 7229 1358 2818 -142 O ATOM 1452 CB TRP A 197 16.220 21.225 2.067 1.00 65.40 C ANISOU 1452 CB TRP A 197 10091 8267 6489 1630 2672 -385 C ATOM 1453 CG TRP A 197 16.370 22.472 2.881 1.00 64.08 C ANISOU 1453 CG TRP A 197 9593 8188 6568 1353 2677 -165 C ATOM 1454 CD1 TRP A 197 17.201 23.529 2.629 1.00 62.13 C ANISOU 1454 CD1 TRP A 197 9236 8001 6370 1316 3038 77 C ATOM 1455 CD2 TRP A 197 15.660 22.795 4.081 1.00 58.20 C ANISOU 1455 CD2 TRP A 197 8602 7458 6053 1078 2304 -169 C ATOM 1456 NE1 TRP A 197 17.049 24.489 3.607 1.00 60.36 N ANISOU 1456 NE1 TRP A 197 8725 7813 6398 1027 2874 202 N ATOM 1457 CE2 TRP A 197 16.109 24.060 4.510 1.00 56.83 C ANISOU 1457 CE2 TRP A 197 8206 7347 6042 894 2434 49 C ATOM 1458 CE3 TRP A 197 14.686 22.135 4.835 1.00 54.54 C ANISOU 1458 CE3 TRP A 197 8093 6950 5679 977 1891 -328 C ATOM 1459 CZ2 TRP A 197 15.616 24.677 5.656 1.00 61.53 C ANISOU 1459 CZ2 TRP A 197 8576 7961 6843 639 2154 88 C ATOM 1460 CZ3 TRP A 197 14.204 22.742 5.970 1.00 56.31 C ANISOU 1460 CZ3 TRP A 197 8074 7211 6111 730 1657 -262 C ATOM 1461 CH2 TRP A 197 14.665 24.001 6.373 1.00 60.04 C ANISOU 1461 CH2 TRP A 197 8366 7747 6701 576 1782 -68 C ATOM 1462 N VAL A 198 16.394 19.260 4.624 1.00 57.53 N ANISOU 1462 N VAL A 198 8366 7197 6296 1369 2203 -506 N ATOM 1463 CA VAL A 198 16.445 19.008 6.072 1.00 61.52 C ANISOU 1463 CA VAL A 198 8474 7714 7185 1156 1989 -452 C ATOM 1464 C VAL A 198 17.768 18.347 6.509 1.00 66.31 C ANISOU 1464 C VAL A 198 8768 8327 8101 1238 2215 -365 C ATOM 1465 O VAL A 198 18.316 18.660 7.571 1.00 66.73 O ANISOU 1465 O VAL A 198 8438 8441 8473 1072 2180 -219 O ATOM 1466 CB VAL A 198 15.245 18.135 6.545 1.00 53.85 C ANISOU 1466 CB VAL A 198 7600 6635 6223 1088 1572 -635 C ATOM 1467 CG1 VAL A 198 15.414 17.717 7.995 1.00 51.74 C ANISOU 1467 CG1 VAL A 198 6969 6369 6320 924 1411 -562 C ATOM 1468 CG2 VAL A 198 13.936 18.876 6.385 1.00 53.37 C ANISOU 1468 CG2 VAL A 198 7725 6587 5967 967 1311 -685 C ATOM 1469 N LEU A 199 18.279 17.450 5.672 1.00 69.19 N ANISOU 1469 N LEU A 199 9308 8620 8360 1514 2436 -458 N ATOM 1470 CA LEU A 199 19.509 16.707 5.959 1.00 72.12 C ANISOU 1470 CA LEU A 199 9403 8983 9018 1650 2665 -389 C ATOM 1471 C LEU A 199 20.762 17.593 6.039 1.00 76.24 C ANISOU 1471 C LEU A 199 9566 9633 9768 1615 3022 -134 C ATOM 1472 O LEU A 199 21.821 17.152 6.499 1.00 76.19 O ANISOU 1472 O LEU A 199 9214 9641 10092 1676 3168 -34 O ATOM 1473 CB LEU A 199 19.702 15.595 4.913 1.00 69.39 C ANISOU 1473 CB LEU A 199 9393 8515 8459 1994 2845 -565 C ATOM 1474 CG LEU A 199 18.702 14.435 5.000 1.00 70.64 C ANISOU 1474 CG LEU A 199 9818 8493 8528 2026 2471 -818 C ATOM 1475 CD1 LEU A 199 18.964 13.347 3.945 1.00 68.15 C ANISOU 1475 CD1 LEU A 199 9873 8027 7995 2385 2641 -1013 C ATOM 1476 CD2 LEU A 199 18.711 13.834 6.401 1.00 63.18 C ANISOU 1476 CD2 LEU A 199 8522 7511 7973 1855 2208 -773 C ATOM 1477 N LYS A 200 20.639 18.838 5.588 1.00 78.36 N ANISOU 1477 N LYS A 200 9906 9980 9887 1516 3150 -20 N ATOM 1478 CA LYS A 200 21.755 19.777 5.612 1.00 76.19 C ANISOU 1478 CA LYS A 200 9295 9800 9853 1445 3482 237 C ATOM 1479 C LYS A 200 21.904 20.396 6.997 1.00 73.30 C ANISOU 1479 C LYS A 200 8508 9483 9860 1127 3208 357 C ATOM 1480 O LYS A 200 22.897 21.058 7.292 1.00 77.97 O ANISOU 1480 O LYS A 200 8729 10129 10767 1023 3385 561 O ATOM 1481 CB LYS A 200 21.540 20.877 4.569 1.00 76.02 C ANISOU 1481 CB LYS A 200 9553 9813 9519 1463 3728 325 C ATOM 1482 CG LYS A 200 21.791 20.430 3.136 1.00 83.48 C ANISOU 1482 CG LYS A 200 10875 10724 10119 1793 4068 272 C ATOM 1483 CD LYS A 200 21.304 21.473 2.142 1.00 91.03 C ANISOU 1483 CD LYS A 200 12192 11690 10706 1779 4129 330 C ATOM 1484 CE LYS A 200 21.558 21.033 0.702 1.00 97.21 C ANISOU 1484 CE LYS A 200 13364 12425 11147 2066 4329 280 C ATOM 1485 NZ LYS A 200 20.958 21.981 -0.278 1.00 96.87 N ANISOU 1485 NZ LYS A 200 13710 12374 10722 2077 4333 323 N ATOM 1486 N SER A 201 20.913 20.177 7.851 1.00 65.68 N ANISOU 1486 N SER A 201 7604 8486 8865 977 2771 232 N ATOM 1487 CA SER A 201 20.899 20.842 9.145 1.00 66.43 C ANISOU 1487 CA SER A 201 7400 8620 9221 697 2493 325 C ATOM 1488 C SER A 201 20.831 19.830 10.287 1.00 61.76 C ANISOU 1488 C SER A 201 6643 7991 8830 676 2192 255 C ATOM 1489 O SER A 201 19.758 19.303 10.614 1.00 62.51 O ANISOU 1489 O SER A 201 6944 8032 8774 653 1917 114 O ATOM 1490 CB SER A 201 19.738 21.845 9.217 1.00 65.94 C ANISOU 1490 CB SER A 201 7565 8566 8923 519 2279 293 C ATOM 1491 OG SER A 201 19.674 22.474 10.486 1.00 68.59 O ANISOU 1491 OG SER A 201 7667 8923 9470 276 2008 361 O ATOM 1492 N SER A 202 21.985 19.574 10.891 1.00 54.05 N ANISOU 1492 N SER A 202 5284 7037 8215 683 2247 371 N ATOM 1493 CA SER A 202 22.098 18.586 11.954 1.00 51.49 C ANISOU 1493 CA SER A 202 4798 6673 8092 698 1989 336 C ATOM 1494 C SER A 202 21.136 18.953 13.068 1.00 54.16 C ANISOU 1494 C SER A 202 5195 7011 8374 479 1595 304 C ATOM 1495 O SER A 202 20.344 18.127 13.514 1.00 60.80 O ANISOU 1495 O SER A 202 6188 7787 9126 503 1382 201 O ATOM 1496 CB SER A 202 23.541 18.509 12.469 1.00 46.58 C ANISOU 1496 CB SER A 202 3717 6089 7892 719 2075 493 C ATOM 1497 OG SER A 202 24.440 18.304 11.398 1.00 91.34 O ANISOU 1497 OG SER A 202 9308 11770 13628 930 2503 551 O ATOM 1498 N ILE A 203 21.175 20.211 13.482 1.00 57.29 N ANISOU 1498 N ILE A 203 5487 7465 8815 272 1520 398 N ATOM 1499 CA ILE A 203 20.261 20.672 14.514 1.00 58.28 C ANISOU 1499 CA ILE A 203 5698 7591 8855 91 1184 369 C ATOM 1500 C ILE A 203 18.788 20.465 14.119 1.00 50.66 C ANISOU 1500 C ILE A 203 5098 6589 7561 110 1102 231 C ATOM 1501 O ILE A 203 17.995 20.027 14.939 1.00 49.59 O ANISOU 1501 O ILE A 203 5033 6423 7384 66 861 182 O ATOM 1502 CB ILE A 203 20.558 22.139 14.953 1.00 65.77 C ANISOU 1502 CB ILE A 203 6514 8581 9897 -123 1118 475 C ATOM 1503 CG1 ILE A 203 19.647 22.544 16.112 1.00 57.04 C ANISOU 1503 CG1 ILE A 203 5518 7467 8685 -267 779 436 C ATOM 1504 CG2 ILE A 203 20.393 23.112 13.794 1.00 73.70 C ANISOU 1504 CG2 ILE A 203 7669 9596 10738 -146 1371 503 C ATOM 1505 CD1 ILE A 203 19.885 21.716 17.350 1.00 64.06 C ANISOU 1505 CD1 ILE A 203 6277 8344 9721 -246 531 444 C ATOM 1506 N LEU A 204 18.420 20.743 12.869 1.00 56.20 N ANISOU 1506 N LEU A 204 6026 7288 8038 184 1299 177 N ATOM 1507 CA LEU A 204 17.014 20.590 12.471 1.00 54.04 C ANISOU 1507 CA LEU A 204 6075 6975 7483 196 1173 43 C ATOM 1508 C LEU A 204 16.577 19.121 12.504 1.00 55.82 C ANISOU 1508 C LEU A 204 6396 7108 7705 319 1069 -80 C ATOM 1509 O LEU A 204 15.438 18.814 12.859 1.00 51.96 O ANISOU 1509 O LEU A 204 6034 6571 7135 261 850 -156 O ATOM 1510 CB LEU A 204 16.750 21.204 11.091 1.00 51.93 C ANISOU 1510 CB LEU A 204 6060 6717 6953 273 1374 11 C ATOM 1511 CG LEU A 204 15.342 20.991 10.538 1.00 51.98 C ANISOU 1511 CG LEU A 204 6392 6674 6682 310 1213 -139 C ATOM 1512 CD1 LEU A 204 14.304 21.678 11.421 1.00 39.29 C ANISOU 1512 CD1 LEU A 204 4775 5090 5063 130 951 -125 C ATOM 1513 CD2 LEU A 204 15.246 21.482 9.100 1.00 57.97 C ANISOU 1513 CD2 LEU A 204 7434 7437 7155 435 1412 -169 C ATOM 1514 N ILE A 205 17.496 18.223 12.151 1.00 57.22 N ANISOU 1514 N ILE A 205 6496 7244 7999 487 1234 -90 N ATOM 1515 CA ILE A 205 17.255 16.782 12.243 1.00 55.57 C ANISOU 1515 CA ILE A 205 6366 6914 7834 610 1140 -198 C ATOM 1516 C ILE A 205 16.930 16.377 13.676 1.00 54.86 C ANISOU 1516 C ILE A 205 6129 6798 7917 488 872 -143 C ATOM 1517 O ILE A 205 15.889 15.772 13.928 1.00 53.60 O ANISOU 1517 O ILE A 205 6112 6550 7705 452 687 -219 O ATOM 1518 CB ILE A 205 18.478 15.970 11.767 1.00 51.77 C ANISOU 1518 CB ILE A 205 5785 6396 7490 831 1384 -191 C ATOM 1519 CG1 ILE A 205 18.710 16.185 10.274 1.00 53.72 C ANISOU 1519 CG1 ILE A 205 6252 6647 7510 1004 1685 -255 C ATOM 1520 CG2 ILE A 205 18.289 14.496 12.063 1.00 47.09 C ANISOU 1520 CG2 ILE A 205 5254 5650 6986 945 1254 -286 C ATOM 1521 CD1 ILE A 205 20.028 15.627 9.783 1.00 60.12 C ANISOU 1521 CD1 ILE A 205 6930 7450 8462 1238 2008 -211 C ATOM 1522 N ALA A 206 17.825 16.706 14.609 1.00 52.68 N ANISOU 1522 N ALA A 206 5571 6592 7852 428 849 -4 N ATOM 1523 CA ALA A 206 17.617 16.347 16.010 1.00 51.58 C ANISOU 1523 CA ALA A 206 5327 6432 7838 343 603 64 C ATOM 1524 C ALA A 206 16.311 16.958 16.545 1.00 45.49 C ANISOU 1524 C ALA A 206 4699 5681 6906 179 422 54 C ATOM 1525 O ALA A 206 15.509 16.281 17.199 1.00 46.31 O ANISOU 1525 O ALA A 206 4876 5712 7010 155 269 48 O ATOM 1526 CB ALA A 206 18.826 16.761 16.861 1.00 45.07 C ANISOU 1526 CB ALA A 206 4199 5684 7243 309 568 204 C ATOM 1527 N MET A 207 16.093 18.230 16.237 1.00 41.84 N ANISOU 1527 N MET A 207 4273 5307 6319 77 462 64 N ATOM 1528 CA MET A 207 14.900 18.944 16.695 1.00 44.64 C ANISOU 1528 CA MET A 207 4749 5686 6525 -53 319 60 C ATOM 1529 C MET A 207 13.602 18.374 16.128 1.00 47.08 C ANISOU 1529 C MET A 207 5263 5918 6705 -30 269 -49 C ATOM 1530 O MET A 207 12.592 18.279 16.838 1.00 41.75 O ANISOU 1530 O MET A 207 4628 5222 6014 -103 127 -32 O ATOM 1531 CB MET A 207 14.994 20.413 16.315 1.00 47.48 C ANISOU 1531 CB MET A 207 5126 6129 6785 -142 389 88 C ATOM 1532 CG MET A 207 15.741 21.270 17.306 1.00 67.01 C ANISOU 1532 CG MET A 207 7428 8657 9377 -248 308 193 C ATOM 1533 SD MET A 207 14.667 21.786 18.661 1.00 71.96 S ANISOU 1533 SD MET A 207 8152 9294 9894 -353 72 216 S ATOM 1534 CE MET A 207 15.737 22.997 19.437 1.00 64.61 C ANISOU 1534 CE MET A 207 7076 8401 9074 -467 -21 297 C ATOM 1535 N ALA A 208 13.616 18.023 14.847 1.00 39.89 N ANISOU 1535 N ALA A 208 4486 4962 5708 75 383 -158 N ATOM 1536 CA ALA A 208 12.415 17.482 14.208 1.00 39.44 C ANISOU 1536 CA ALA A 208 4630 4813 5543 95 284 -285 C ATOM 1537 C ALA A 208 12.090 16.112 14.794 1.00 43.87 C ANISOU 1537 C ALA A 208 5165 5237 6265 111 163 -302 C ATOM 1538 O ALA A 208 10.929 15.803 15.064 1.00 47.48 O ANISOU 1538 O ALA A 208 5670 5627 6742 34 11 -323 O ATOM 1539 CB ALA A 208 12.594 17.394 12.703 1.00 40.49 C ANISOU 1539 CB ALA A 208 4962 4914 5509 233 413 -410 C ATOM 1540 N VAL A 209 13.120 15.295 14.990 1.00 47.75 N ANISOU 1540 N VAL A 209 5566 5679 6898 214 238 -278 N ATOM 1541 CA VAL A 209 12.944 13.987 15.608 1.00 47.14 C ANISOU 1541 CA VAL A 209 5469 5452 6991 239 135 -268 C ATOM 1542 C VAL A 209 12.423 14.128 17.040 1.00 44.84 C ANISOU 1542 C VAL A 209 5067 5190 6780 108 8 -120 C ATOM 1543 O VAL A 209 11.455 13.469 17.424 1.00 50.47 O ANISOU 1543 O VAL A 209 5824 5790 7562 49 -102 -109 O ATOM 1544 CB VAL A 209 14.256 13.177 15.593 1.00 48.92 C ANISOU 1544 CB VAL A 209 5604 5626 7357 402 248 -252 C ATOM 1545 CG1 VAL A 209 14.133 11.932 16.452 1.00 44.85 C ANISOU 1545 CG1 VAL A 209 5058 4954 7028 422 132 -199 C ATOM 1546 CG2 VAL A 209 14.622 12.796 14.169 1.00 47.82 C ANISOU 1546 CG2 VAL A 209 5629 5420 7121 573 398 -410 C ATOM 1547 N TYR A 210 13.065 14.981 17.829 1.00 41.39 N ANISOU 1547 N TYR A 210 4496 4890 6338 67 24 -2 N ATOM 1548 CA TYR A 210 12.617 15.212 19.199 1.00 42.04 C ANISOU 1548 CA TYR A 210 4530 5009 6436 -24 -86 132 C ATOM 1549 C TYR A 210 11.146 15.671 19.207 1.00 45.71 C ANISOU 1549 C TYR A 210 5089 5480 6800 -131 -138 118 C ATOM 1550 O TYR A 210 10.298 15.115 19.919 1.00 45.32 O ANISOU 1550 O TYR A 210 5050 5357 6814 -173 -197 191 O ATOM 1551 CB TYR A 210 13.515 16.247 19.896 1.00 36.70 C ANISOU 1551 CB TYR A 210 3738 4470 5735 -52 -98 220 C ATOM 1552 CG TYR A 210 13.333 16.259 21.394 1.00 39.97 C ANISOU 1552 CG TYR A 210 4141 4899 6145 -86 -223 353 C ATOM 1553 CD1 TYR A 210 12.310 16.990 21.988 1.00 36.80 C ANISOU 1553 CD1 TYR A 210 3831 4547 5605 -170 -262 392 C ATOM 1554 CD2 TYR A 210 14.174 15.523 22.217 1.00 45.13 C ANISOU 1554 CD2 TYR A 210 4715 5513 6918 -6 -297 445 C ATOM 1555 CE1 TYR A 210 12.129 16.991 23.359 1.00 38.81 C ANISOU 1555 CE1 TYR A 210 4124 4813 5811 -167 -347 517 C ATOM 1556 CE2 TYR A 210 14.005 15.516 23.590 1.00 46.45 C ANISOU 1556 CE2 TYR A 210 4927 5689 7034 -9 -416 572 C ATOM 1557 CZ TYR A 210 12.976 16.241 24.155 1.00 46.28 C ANISOU 1557 CZ TYR A 210 5023 5716 6844 -86 -428 607 C ATOM 1558 OH TYR A 210 12.808 16.226 25.517 1.00 43.28 O ANISOU 1558 OH TYR A 210 4732 5343 6370 -57 -517 736 O ATOM 1559 N THR A 211 10.837 16.671 18.393 1.00 46.10 N ANISOU 1559 N THR A 211 5197 5610 6711 -166 -102 40 N ATOM 1560 CA THR A 211 9.472 17.193 18.342 1.00 43.05 C ANISOU 1560 CA THR A 211 4873 5238 6245 -247 -158 27 C ATOM 1561 C THR A 211 8.465 16.113 17.962 1.00 45.94 C ANISOU 1561 C THR A 211 5279 5454 6721 -260 -235 -31 C ATOM 1562 O THR A 211 7.487 15.900 18.677 1.00 45.25 O ANISOU 1562 O THR A 211 5148 5330 6716 -329 -284 54 O ATOM 1563 CB THR A 211 9.360 18.361 17.369 1.00 41.75 C ANISOU 1563 CB THR A 211 4787 5162 5913 -255 -118 -53 C ATOM 1564 OG1 THR A 211 10.176 19.436 17.845 1.00 43.42 O ANISOU 1564 OG1 THR A 211 4949 5485 6064 -278 -65 18 O ATOM 1565 CG2 THR A 211 7.910 18.836 17.249 1.00 36.24 C ANISOU 1565 CG2 THR A 211 4139 4470 5159 -314 -197 -69 C ATOM 1566 N TYR A 212 8.700 15.418 16.854 1.00 41.81 N ANISOU 1566 N TYR A 212 4844 4830 6212 -191 -244 -172 N ATOM 1567 CA TYR A 212 7.692 14.469 16.389 1.00 44.12 C ANISOU 1567 CA TYR A 212 5193 4952 6619 -221 -370 -257 C ATOM 1568 C TYR A 212 7.627 13.163 17.173 1.00 48.06 C ANISOU 1568 C TYR A 212 5629 5284 7347 -239 -406 -177 C ATOM 1569 O TYR A 212 6.559 12.579 17.264 1.00 46.02 O ANISOU 1569 O TYR A 212 5348 4895 7243 -326 -512 -168 O ATOM 1570 CB TYR A 212 7.737 14.275 14.865 1.00 39.94 C ANISOU 1570 CB TYR A 212 4845 4353 5978 -135 -411 -465 C ATOM 1571 CG TYR A 212 7.137 15.475 14.167 1.00 49.01 C ANISOU 1571 CG TYR A 212 6069 5620 6931 -155 -443 -518 C ATOM 1572 CD1 TYR A 212 5.755 15.620 14.070 1.00 45.93 C ANISOU 1572 CD1 TYR A 212 5662 5195 6594 -246 -612 -538 C ATOM 1573 CD2 TYR A 212 7.943 16.495 13.663 1.00 45.52 C ANISOU 1573 CD2 TYR A 212 5692 5320 6283 -86 -299 -522 C ATOM 1574 CE1 TYR A 212 5.187 16.724 13.466 1.00 48.02 C ANISOU 1574 CE1 TYR A 212 5994 5563 6688 -246 -658 -575 C ATOM 1575 CE2 TYR A 212 7.379 17.610 13.051 1.00 50.33 C ANISOU 1575 CE2 TYR A 212 6391 6021 6712 -97 -327 -551 C ATOM 1576 CZ TYR A 212 5.996 17.715 12.955 1.00 48.89 C ANISOU 1576 CZ TYR A 212 6209 5803 6563 -167 -516 -582 C ATOM 1577 OH TYR A 212 5.412 18.806 12.350 1.00 46.96 O ANISOU 1577 OH TYR A 212 6056 5641 6146 -157 -564 -605 O ATOM 1578 N LEU A 213 8.740 12.720 17.756 1.00 50.73 N ANISOU 1578 N LEU A 213 5926 5618 7731 -159 -326 -102 N ATOM 1579 CA LEU A 213 8.683 11.576 18.667 1.00 51.30 C ANISOU 1579 CA LEU A 213 5951 5537 8004 -168 -353 17 C ATOM 1580 C LEU A 213 7.734 11.900 19.817 1.00 46.00 C ANISOU 1580 C LEU A 213 5195 4911 7373 -283 -355 200 C ATOM 1581 O LEU A 213 6.955 11.053 20.250 1.00 43.80 O ANISOU 1581 O LEU A 213 4889 4473 7280 -350 -389 286 O ATOM 1582 CB LEU A 213 10.071 11.210 19.219 1.00 50.56 C ANISOU 1582 CB LEU A 213 5813 5460 7938 -45 -284 92 C ATOM 1583 CG LEU A 213 11.079 10.509 18.301 1.00 51.65 C ANISOU 1583 CG LEU A 213 6010 5505 8111 109 -240 -45 C ATOM 1584 CD1 LEU A 213 12.383 10.258 19.047 1.00 45.33 C ANISOU 1584 CD1 LEU A 213 5101 4743 7379 226 -187 71 C ATOM 1585 CD2 LEU A 213 10.542 9.206 17.720 1.00 44.47 C ANISOU 1585 CD2 LEU A 213 5223 4327 7348 128 -321 -156 C ATOM 1586 N ARG A 214 7.782 13.141 20.292 1.00 44.74 N ANISOU 1586 N ARG A 214 5003 4952 7043 -300 -305 264 N ATOM 1587 CA ARG A 214 6.937 13.559 21.411 1.00 41.72 C ANISOU 1587 CA ARG A 214 4572 4629 6650 -366 -270 435 C ATOM 1588 C ARG A 214 5.456 13.677 21.030 1.00 46.92 C ANISOU 1588 C ARG A 214 5186 5246 7397 -469 -301 419 C ATOM 1589 O ARG A 214 4.578 13.245 21.792 1.00 46.91 O ANISOU 1589 O ARG A 214 5115 5172 7538 -528 -261 572 O ATOM 1590 CB ARG A 214 7.449 14.878 22.002 1.00 42.81 C ANISOU 1590 CB ARG A 214 4724 4970 6571 -338 -227 480 C ATOM 1591 CG ARG A 214 6.452 15.612 22.887 1.00 39.76 C ANISOU 1591 CG ARG A 214 4335 4665 6106 -378 -174 605 C ATOM 1592 CD ARG A 214 6.054 14.821 24.118 1.00 42.51 C ANISOU 1592 CD ARG A 214 4680 4933 6537 -366 -112 809 C ATOM 1593 NE ARG A 214 5.115 15.599 24.916 1.00 47.82 N ANISOU 1593 NE ARG A 214 5366 5695 7109 -370 -16 928 N ATOM 1594 CZ ARG A 214 3.795 15.561 24.770 1.00 43.80 C ANISOU 1594 CZ ARG A 214 4765 5149 6727 -434 49 977 C ATOM 1595 NH1 ARG A 214 3.247 14.766 23.864 1.00 39.48 N ANISOU 1595 NH1 ARG A 214 4116 4465 6421 -521 -18 906 N ATOM 1596 NH2 ARG A 214 3.023 16.327 25.529 1.00 44.99 N ANISOU 1596 NH2 ARG A 214 4927 5393 6775 -403 170 1092 N ATOM 1597 N LEU A 215 5.178 14.259 19.861 1.00 43.59 N ANISOU 1597 N LEU A 215 4796 4864 6901 -482 -369 249 N ATOM 1598 CA LEU A 215 3.800 14.513 19.444 1.00 47.64 C ANISOU 1598 CA LEU A 215 5247 5356 7499 -566 -441 224 C ATOM 1599 C LEU A 215 3.043 13.211 19.123 1.00 54.89 C ANISOU 1599 C LEU A 215 6109 6039 8709 -648 -555 201 C ATOM 1600 O LEU A 215 1.828 13.120 19.329 1.00 54.37 O ANISOU 1600 O LEU A 215 5906 5918 8833 -745 -588 281 O ATOM 1601 CB LEU A 215 3.764 15.476 18.256 1.00 47.22 C ANISOU 1601 CB LEU A 215 5278 5399 7264 -537 -511 51 C ATOM 1602 CG LEU A 215 4.197 16.934 18.466 1.00 48.59 C ANISOU 1602 CG LEU A 215 5493 5776 7191 -492 -419 77 C ATOM 1603 CD1 LEU A 215 4.376 17.636 17.123 1.00 46.69 C ANISOU 1603 CD1 LEU A 215 5377 5586 6779 -447 -475 -90 C ATOM 1604 CD2 LEU A 215 3.202 17.708 19.333 1.00 42.66 C ANISOU 1604 CD2 LEU A 215 4653 5111 6443 -525 -366 213 C ATOM 1605 N ILE A 216 3.778 12.213 18.633 1.00 48.41 N ANISOU 1605 N ILE A 216 5382 5066 7945 -604 -611 97 N ATOM 1606 CA ILE A 216 3.233 10.898 18.299 1.00 44.63 C ANISOU 1606 CA ILE A 216 4892 4318 7749 -677 -744 51 C ATOM 1607 C ILE A 216 2.401 10.298 19.443 1.00 50.18 C ANISOU 1607 C ILE A 216 5428 4912 8726 -791 -677 293 C ATOM 1608 O ILE A 216 1.370 9.663 19.207 1.00 49.25 O ANISOU 1608 O ILE A 216 5208 4608 8896 -918 -795 296 O ATOM 1609 CB ILE A 216 4.369 9.916 17.893 1.00 42.24 C ANISOU 1609 CB ILE A 216 4739 3868 7444 -569 -758 -60 C ATOM 1610 CG1 ILE A 216 4.836 10.215 16.470 1.00 46.14 C ANISOU 1610 CG1 ILE A 216 5411 4388 7734 -466 -841 -321 C ATOM 1611 CG2 ILE A 216 3.902 8.465 17.989 1.00 42.20 C ANISOU 1611 CG2 ILE A 216 4720 3549 7763 -647 -861 -41 C ATOM 1612 CD1 ILE A 216 6.116 9.502 16.069 1.00 48.06 C ANISOU 1612 CD1 ILE A 216 5799 4546 7918 -307 -783 -423 C ATOM 1613 N VAL A 217 2.841 10.523 20.677 1.00 50.03 N ANISOU 1613 N VAL A 217 5386 5003 8621 -743 -490 503 N ATOM 1614 CA VAL A 217 2.114 10.081 21.870 1.00 50.76 C ANISOU 1614 CA VAL A 217 5356 5023 8906 -814 -361 773 C ATOM 1615 C VAL A 217 0.675 10.618 21.936 1.00 51.74 C ANISOU 1615 C VAL A 217 5295 5190 9174 -925 -339 855 C ATOM 1616 O VAL A 217 -0.222 9.959 22.454 1.00 50.56 O ANISOU 1616 O VAL A 217 4996 4893 9323 -1031 -278 1036 O ATOM 1617 CB VAL A 217 2.873 10.520 23.133 1.00 54.22 C ANISOU 1617 CB VAL A 217 5863 5621 9117 -701 -182 956 C ATOM 1618 CG1 VAL A 217 2.048 10.247 24.390 1.00 63.43 C ANISOU 1618 CG1 VAL A 217 6946 6746 10408 -741 -2 1254 C ATOM 1619 CG2 VAL A 217 4.225 9.807 23.200 1.00 51.24 C ANISOU 1619 CG2 VAL A 217 5613 5171 8685 -593 -215 919 C ATOM 1620 N ASP A 218 0.467 11.822 21.410 1.00 49.38 N ANISOU 1620 N ASP A 218 4994 5085 8682 -894 -377 737 N ATOM 1621 CA ASP A 218 -0.815 12.491 21.522 1.00 50.22 C ANISOU 1621 CA ASP A 218 4918 5265 8898 -957 -342 822 C ATOM 1622 C ASP A 218 -1.763 12.097 20.393 1.00 55.42 C ANISOU 1622 C ASP A 218 5452 5771 9836 -1079 -588 675 C ATOM 1623 O ASP A 218 -2.977 12.279 20.509 1.00 56.18 O ANISOU 1623 O ASP A 218 5320 5857 10170 -1164 -586 776 O ATOM 1624 CB ASP A 218 -0.615 14.013 21.515 1.00 48.64 C ANISOU 1624 CB ASP A 218 4790 5327 8363 -852 -282 770 C ATOM 1625 CG ASP A 218 0.051 14.531 22.779 1.00 55.35 C ANISOU 1625 CG ASP A 218 5744 6321 8967 -744 -67 930 C ATOM 1626 OD1 ASP A 218 -0.166 13.944 23.863 1.00 55.75 O ANISOU 1626 OD1 ASP A 218 5754 6310 9118 -746 93 1152 O ATOM 1627 OD2 ASP A 218 0.779 15.546 22.681 1.00 52.48 O ANISOU 1627 OD2 ASP A 218 5513 6119 8306 -657 -68 836 O ATOM 1628 N HIS A 219 -1.208 11.535 19.319 1.00 54.40 N ANISOU 1628 N HIS A 219 5471 5514 9684 -1076 -804 438 N ATOM 1629 CA HIS A 219 -1.959 11.347 18.074 1.00 53.10 C ANISOU 1629 CA HIS A 219 5273 5223 9678 -1154 -1103 232 C ATOM 1630 C HIS A 219 -2.668 9.998 17.898 1.00 55.42 C ANISOU 1630 C HIS A 219 5444 5196 10417 -1318 -1280 235 C ATOM 1631 O HIS A 219 -2.260 9.161 17.090 1.00 59.74 O ANISOU 1631 O HIS A 219 6159 5541 10997 -1319 -1484 33 O ATOM 1632 CB HIS A 219 -1.070 11.674 16.872 1.00 46.46 C ANISOU 1632 CB HIS A 219 4707 4434 8510 -1031 -1247 -49 C ATOM 1633 CG HIS A 219 -0.648 13.105 16.828 1.00 49.99 C ANISOU 1633 CG HIS A 219 5236 5163 8594 -913 -1126 -60 C ATOM 1634 ND1 HIS A 219 0.463 13.539 16.130 1.00 54.50 N ANISOU 1634 ND1 HIS A 219 6046 5829 8835 -782 -1112 -218 N ATOM 1635 CD2 HIS A 219 -1.186 14.208 17.398 1.00 48.11 C ANISOU 1635 CD2 HIS A 219 4876 5117 8289 -902 -1003 75 C ATOM 1636 CE1 HIS A 219 0.585 14.845 16.273 1.00 48.95 C ANISOU 1636 CE1 HIS A 219 5357 5349 7895 -719 -1001 -175 C ATOM 1637 NE2 HIS A 219 -0.401 15.276 17.040 1.00 48.20 N ANISOU 1637 NE2 HIS A 219 5061 5312 7940 -783 -943 -10 N ATOM 1638 N HIS A 220 -3.754 9.823 18.644 1.00 54.36 N ANISOU 1638 N HIS A 220 5074 5061 10519 -1386 -1160 459 N ATOM 1639 CA HIS A 220 -4.575 8.614 18.593 1.00 58.07 C ANISOU 1639 CA HIS A 220 5445 5305 11315 -1479 -1260 500 C ATOM 1640 C HIS A 220 -5.953 8.998 19.082 1.00 53.85 C ANISOU 1640 C HIS A 220 4629 4855 10978 -1520 -1161 691 C ATOM 1641 O HIS A 220 -6.083 9.984 19.794 1.00 59.50 O ANISOU 1641 O HIS A 220 5257 5781 11569 -1461 -931 844 O ATOM 1642 CB HIS A 220 -4.006 7.558 19.538 1.00 60.52 C ANISOU 1642 CB HIS A 220 5797 5464 11735 -1496 -1073 677 C ATOM 1643 CG HIS A 220 -3.886 8.031 20.955 1.00 61.54 C ANISOU 1643 CG HIS A 220 5846 5751 11785 -1449 -711 981 C ATOM 1644 ND1 HIS A 220 -4.832 7.753 21.918 1.00 63.80 N ANISOU 1644 ND1 HIS A 220 5941 6031 12269 -1482 -502 1249 N ATOM 1645 CD2 HIS A 220 -2.945 8.802 21.559 1.00 57.89 C ANISOU 1645 CD2 HIS A 220 5488 5458 11049 -1357 -526 1055 C ATOM 1646 CE1 HIS A 220 -4.469 8.310 23.063 1.00 64.50 C ANISOU 1646 CE1 HIS A 220 6055 6280 12171 -1394 -197 1469 C ATOM 1647 NE2 HIS A 220 -3.335 8.958 22.869 1.00 64.32 N ANISOU 1647 NE2 HIS A 220 6208 6365 11865 -1322 -220 1357 N ATOM 1648 N GLY A 221 -6.977 8.226 18.726 1.00 55.57 N ANISOU 1648 N GLY A 221 4702 4899 11512 -1614 -1327 685 N ATOM 1649 CA GLY A 221 -8.322 8.527 19.188 1.00 58.37 C ANISOU 1649 CA GLY A 221 4762 5308 12109 -1652 -1227 877 C ATOM 1650 C GLY A 221 -9.302 8.788 18.057 1.00 61.78 C ANISOU 1650 C GLY A 221 5092 5709 12673 -1687 -1557 705 C ATOM 1651 O GLY A 221 -10.496 8.572 18.214 1.00 64.60 O ANISOU 1651 O GLY A 221 5188 6000 13356 -1755 -1571 830 O ATOM 1652 N THR A 222 -8.800 9.274 16.924 1.00 62.36 N ANISOU 1652 N THR A 222 5375 5828 12492 -1628 -1821 426 N ATOM 1653 CA THR A 222 -9.613 9.435 15.715 1.00 65.40 C ANISOU 1653 CA THR A 222 5736 6160 12951 -1640 -2189 232 C ATOM 1654 C THR A 222 -8.843 8.883 14.524 1.00 60.58 C ANISOU 1654 C THR A 222 5451 5410 12155 -1611 -2504 -78 C ATOM 1655 O THR A 222 -7.623 8.761 14.583 1.00 59.90 O ANISOU 1655 O THR A 222 5601 5334 11823 -1555 -2412 -155 O ATOM 1656 CB THR A 222 -9.950 10.923 15.427 1.00 64.51 C ANISOU 1656 CB THR A 222 5578 6292 12640 -1541 -2196 205 C ATOM 1657 OG1 THR A 222 -8.748 11.639 15.118 1.00 59.87 O ANISOU 1657 OG1 THR A 222 5265 5849 11635 -1436 -2170 61 O ATOM 1658 CG2 THR A 222 -10.626 11.576 16.614 1.00 62.14 C ANISOU 1658 CG2 THR A 222 4995 6145 12470 -1530 -1854 499 C ATOM 1659 N ALA A 223 -9.554 8.564 13.449 1.00 62.31 N ANISOU 1659 N ALA A 223 5693 5495 12485 -1633 -2873 -254 N ATOM 1660 CA ALA A 223 -8.922 8.199 12.188 1.00 62.83 C ANISOU 1660 CA ALA A 223 6113 5449 12310 -1561 -3185 -569 C ATOM 1661 C ALA A 223 -7.918 9.270 11.737 1.00 62.97 C ANISOU 1661 C ALA A 223 6402 5676 11849 -1407 -3134 -712 C ATOM 1662 O ALA A 223 -6.799 8.949 11.317 1.00 72.02 O ANISOU 1662 O ALA A 223 7858 6770 12735 -1329 -3148 -882 O ATOM 1663 CB ALA A 223 -9.984 7.967 11.120 1.00 67.21 C ANISOU 1663 CB ALA A 223 6643 5871 13024 -1584 -3594 -717 C ATOM 1664 N GLN A 224 -8.311 10.540 11.835 1.00 62.49 N ANISOU 1664 N GLN A 224 6224 5840 11679 -1355 -3063 -640 N ATOM 1665 CA GLN A 224 -7.429 11.656 11.458 1.00 58.48 C ANISOU 1665 CA GLN A 224 5948 5535 10735 -1216 -3007 -750 C ATOM 1666 C GLN A 224 -6.119 11.647 12.229 1.00 58.77 C ANISOU 1666 C GLN A 224 6085 5632 10611 -1200 -2708 -692 C ATOM 1667 O GLN A 224 -5.053 11.888 11.661 1.00 61.99 O ANISOU 1667 O GLN A 224 6795 6075 10685 -1095 -2729 -868 O ATOM 1668 CB GLN A 224 -8.112 13.020 11.668 1.00 61.61 C ANISOU 1668 CB GLN A 224 6157 6158 11092 -1173 -2939 -633 C ATOM 1669 CG GLN A 224 -7.246 14.209 11.213 1.00 69.86 C ANISOU 1669 CG GLN A 224 7451 7401 11691 -1029 -2909 -747 C ATOM 1670 CD GLN A 224 -7.676 15.566 11.796 1.00 74.84 C ANISOU 1670 CD GLN A 224 7880 8265 12290 -987 -2743 -581 C ATOM 1671 OE1 GLN A 224 -8.378 15.635 12.808 1.00 73.53 O ANISOU 1671 OE1 GLN A 224 7396 8140 12404 -1056 -2544 -352 O ATOM 1672 NE2 GLN A 224 -7.239 16.651 11.154 1.00 72.57 N ANISOU 1672 NE2 GLN A 224 7805 8125 11643 -854 -2809 -692 N ATOM 1673 N LEU A 225 -6.197 11.395 13.531 1.00 60.35 N ANISOU 1673 N LEU A 225 6045 5845 11041 -1288 -2421 -435 N ATOM 1674 CA LEU A 225 -4.993 11.410 14.363 1.00 57.64 C ANISOU 1674 CA LEU A 225 5777 5556 10566 -1271 -2141 -350 C ATOM 1675 C LEU A 225 -4.078 10.223 14.039 1.00 58.31 C ANISOU 1675 C LEU A 225 6095 5422 10638 -1266 -2211 -493 C ATOM 1676 O LEU A 225 -2.864 10.392 13.935 1.00 56.80 O ANISOU 1676 O LEU A 225 6117 5257 10209 -1187 -2137 -593 O ATOM 1677 CB LEU A 225 -5.352 11.453 15.851 1.00 61.84 C ANISOU 1677 CB LEU A 225 6034 6160 11302 -1334 -1807 -23 C ATOM 1678 CG LEU A 225 -6.023 12.746 16.330 1.00 58.83 C ANISOU 1678 CG LEU A 225 5460 6015 10877 -1295 -1660 126 C ATOM 1679 CD1 LEU A 225 -6.392 12.696 17.814 1.00 60.20 C ANISOU 1679 CD1 LEU A 225 5415 6243 11215 -1322 -1304 447 C ATOM 1680 CD2 LEU A 225 -5.108 13.910 16.059 1.00 53.04 C ANISOU 1680 CD2 LEU A 225 4894 5473 9786 -1196 -1633 23 C ATOM 1681 N GLN A 226 -4.668 9.040 13.854 1.00 57.43 N ANISOU 1681 N GLN A 226 5944 5083 10796 -1343 -2360 -509 N ATOM 1682 CA GLN A 226 -3.914 7.846 13.478 1.00 62.20 C ANISOU 1682 CA GLN A 226 6778 5450 11405 -1324 -2452 -657 C ATOM 1683 C GLN A 226 -3.192 8.017 12.138 1.00 57.74 C ANISOU 1683 C GLN A 226 6585 4866 10488 -1176 -2662 -984 C ATOM 1684 O GLN A 226 -2.041 7.612 11.997 1.00 64.41 O ANISOU 1684 O GLN A 226 7671 5627 11175 -1084 -2595 -1100 O ATOM 1685 CB GLN A 226 -4.829 6.611 13.416 1.00 70.82 C ANISOU 1685 CB GLN A 226 7755 6296 12857 -1440 -2617 -627 C ATOM 1686 CG GLN A 226 -5.624 6.301 14.688 1.00 77.74 C ANISOU 1686 CG GLN A 226 8285 7161 14091 -1572 -2397 -298 C ATOM 1687 CD GLN A 226 -4.775 5.707 15.796 1.00 78.53 C ANISOU 1687 CD GLN A 226 8400 7203 14234 -1579 -2106 -115 C ATOM 1688 OE1 GLN A 226 -3.564 5.510 15.638 1.00 73.80 O ANISOU 1688 OE1 GLN A 226 8046 6560 13434 -1491 -2074 -233 O ATOM 1689 NE2 GLN A 226 -5.409 5.409 16.926 1.00 79.95 N ANISOU 1689 NE2 GLN A 226 8327 7374 14676 -1667 -1886 182 N ATOM 1690 N ALA A 227 -3.866 8.611 11.156 1.00 60.90 N ANISOU 1690 N ALA A 227 7046 5338 10756 -1129 -2900 -1125 N ATOM 1691 CA ALA A 227 -3.266 8.802 9.837 1.00 60.11 C ANISOU 1691 CA ALA A 227 7338 5233 10269 -956 -3079 -1417 C ATOM 1692 C ALA A 227 -2.073 9.747 9.929 1.00 62.55 C ANISOU 1692 C ALA A 227 7813 5723 10228 -832 -2859 -1453 C ATOM 1693 O ALA A 227 -1.049 9.531 9.281 1.00 73.28 O ANISOU 1693 O ALA A 227 9509 7027 11306 -676 -2839 -1646 O ATOM 1694 CB ALA A 227 -4.292 9.314 8.846 1.00 55.56 C ANISOU 1694 CB ALA A 227 6787 4704 9618 -921 -3370 -1518 C ATOM 1695 N LEU A 228 -2.199 10.786 10.748 1.00 57.57 N ANISOU 1695 N LEU A 228 6949 5305 9620 -888 -2677 -1263 N ATOM 1696 CA LEU A 228 -1.092 11.710 10.974 1.00 56.04 C ANISOU 1696 CA LEU A 228 6876 5367 9049 -738 -2348 -1198 C ATOM 1697 C LEU A 228 0.055 11.032 11.741 1.00 59.08 C ANISOU 1697 C LEU A 228 7287 5718 9444 -701 -2064 -1102 C ATOM 1698 O LEU A 228 1.232 11.253 11.439 1.00 54.71 O ANISOU 1698 O LEU A 228 6945 5260 8582 -537 -1881 -1161 O ATOM 1699 CB LEU A 228 -1.576 12.960 11.715 1.00 52.40 C ANISOU 1699 CB LEU A 228 6171 5163 8574 -774 -2181 -982 C ATOM 1700 CG LEU A 228 -0.490 13.854 12.325 1.00 52.35 C ANISOU 1700 CG LEU A 228 6214 5403 8274 -668 -1816 -849 C ATOM 1701 CD1 LEU A 228 0.423 14.423 11.243 1.00 54.22 C ANISOU 1701 CD1 LEU A 228 6779 5732 8091 -487 -1785 -1017 C ATOM 1702 CD2 LEU A 228 -1.092 14.987 13.162 1.00 52.85 C ANISOU 1702 CD2 LEU A 228 6049 5669 8361 -709 -1676 -645 C ATOM 1703 N ARG A 229 -0.289 10.211 12.730 1.00 58.70 N ANISOU 1703 N ARG A 229 7012 5528 9762 -846 -2021 -938 N ATOM 1704 CA ARG A 229 0.725 9.496 13.501 1.00 59.01 C ANISOU 1704 CA ARG A 229 7075 5512 9834 -804 -1789 -832 C ATOM 1705 C ARG A 229 1.586 8.605 12.613 1.00 53.74 C ANISOU 1705 C ARG A 229 6713 4655 9050 -667 -1871 -1067 C ATOM 1706 O ARG A 229 2.800 8.538 12.779 1.00 57.15 O ANISOU 1706 O ARG A 229 7255 5157 9303 -521 -1649 -1050 O ATOM 1707 CB ARG A 229 0.081 8.648 14.599 1.00 54.60 C ANISOU 1707 CB ARG A 229 6261 4783 9700 -980 -1759 -615 C ATOM 1708 CG ARG A 229 1.079 8.145 15.631 1.00 51.98 C ANISOU 1708 CG ARG A 229 5932 4449 9369 -922 -1492 -440 C ATOM 1709 CD ARG A 229 0.390 7.326 16.710 1.00 52.74 C ANISOU 1709 CD ARG A 229 5807 4369 9864 -1086 -1440 -196 C ATOM 1710 NE ARG A 229 0.244 5.931 16.319 1.00 51.62 N ANISOU 1710 NE ARG A 229 5740 3857 10016 -1157 -1634 -299 N ATOM 1711 CZ ARG A 229 -0.484 5.044 16.990 1.00 67.03 C ANISOU 1711 CZ ARG A 229 7529 5638 12303 -1290 -1615 -111 C ATOM 1712 NH1 ARG A 229 -1.134 5.429 18.080 1.00 69.09 N ANISOU 1712 NH1 ARG A 229 7543 6038 12670 -1367 -1407 183 N ATOM 1713 NH2 ARG A 229 -0.568 3.781 16.572 1.00 63.51 N ANISOU 1713 NH2 ARG A 229 7188 4922 12019 -1306 -1768 -213 N ATOM 1714 N GLN A 230 0.961 7.938 11.654 1.00 48.92 N ANISOU 1714 N GLN A 230 6243 3801 8544 -700 -2198 -1292 N ATOM 1715 CA GLN A 230 1.719 7.043 10.788 1.00 58.54 C ANISOU 1715 CA GLN A 230 7796 4808 9637 -544 -2280 -1537 C ATOM 1716 C GLN A 230 2.749 7.826 9.978 1.00 61.28 C ANISOU 1716 C GLN A 230 8412 5370 9502 -297 -2110 -1660 C ATOM 1717 O GLN A 230 3.905 7.401 9.844 1.00 63.35 O ANISOU 1717 O GLN A 230 8843 5606 9621 -120 -1919 -1710 O ATOM 1718 CB GLN A 230 0.800 6.263 9.855 1.00 54.46 C ANISOU 1718 CB GLN A 230 7411 4036 9247 -602 -2666 -1748 C ATOM 1719 CG GLN A 230 1.560 5.325 8.949 1.00 62.33 C ANISOU 1719 CG GLN A 230 8785 4838 10059 -408 -2718 -1990 C ATOM 1720 CD GLN A 230 2.198 4.180 9.713 1.00 69.01 C ANISOU 1720 CD GLN A 230 9602 5466 11154 -414 -2580 -1907 C ATOM 1721 OE1 GLN A 230 1.523 3.467 10.455 1.00 71.66 O ANISOU 1721 OE1 GLN A 230 9701 5673 11855 -604 -2627 -1735 O ATOM 1722 NE2 GLN A 230 3.505 4.003 9.542 1.00 69.22 N ANISOU 1722 NE2 GLN A 230 9864 5452 10984 -185 -2388 -2010 N ATOM 1723 N LYS A 231 2.329 8.978 9.457 1.00 57.59 N ANISOU 1723 N LYS A 231 7968 5110 8805 -280 -2161 -1688 N ATOM 1724 CA LYS A 231 3.237 9.849 8.730 1.00 57.75 C ANISOU 1724 CA LYS A 231 8220 5341 8382 -65 -1966 -1756 C ATOM 1725 C LYS A 231 4.367 10.310 9.644 1.00 54.67 C ANISOU 1725 C LYS A 231 7672 5163 7937 -17 -1569 -1537 C ATOM 1726 O LYS A 231 5.515 10.371 9.216 1.00 60.56 O ANISOU 1726 O LYS A 231 8587 5972 8451 173 -1352 -1586 O ATOM 1727 CB LYS A 231 2.483 11.035 8.116 1.00 56.69 C ANISOU 1727 CB LYS A 231 8122 5375 8044 -72 -2102 -1787 C ATOM 1728 CG LYS A 231 1.501 10.603 7.038 1.00 58.78 C ANISOU 1728 CG LYS A 231 8595 5430 8307 -76 -2541 -2039 C ATOM 1729 CD LYS A 231 0.539 11.715 6.648 1.00 70.84 C ANISOU 1729 CD LYS A 231 10074 7109 9734 -114 -2728 -2027 C ATOM 1730 CE LYS A 231 1.258 12.855 5.962 1.00 74.29 C ANISOU 1730 CE LYS A 231 10759 7777 9689 90 -2514 -2033 C ATOM 1731 NZ LYS A 231 0.402 14.074 5.895 1.00 74.52 N ANISOU 1731 NZ LYS A 231 10674 7982 9659 44 -2621 -1944 N ATOM 1732 N GLU A 232 4.052 10.597 10.907 1.00 51.30 N ANISOU 1732 N GLU A 232 6923 4834 7734 -179 -1478 -1296 N ATOM 1733 CA GLU A 232 5.078 11.047 11.848 1.00 54.54 C ANISOU 1733 CA GLU A 232 7190 5432 8099 -142 -1164 -1096 C ATOM 1734 C GLU A 232 6.033 9.914 12.211 1.00 60.98 C ANISOU 1734 C GLU A 232 8030 6099 9039 -58 -1055 -1086 C ATOM 1735 O GLU A 232 7.224 10.147 12.437 1.00 57.90 O ANISOU 1735 O GLU A 232 7628 5832 8538 63 -822 -1019 O ATOM 1736 CB GLU A 232 4.446 11.650 13.103 1.00 51.04 C ANISOU 1736 CB GLU A 232 6457 5120 7815 -306 -1112 -856 C ATOM 1737 CG GLU A 232 3.601 12.881 12.823 1.00 52.80 C ANISOU 1737 CG GLU A 232 6641 5507 7914 -357 -1181 -847 C ATOM 1738 CD GLU A 232 2.752 13.320 14.014 1.00 57.95 C ANISOU 1738 CD GLU A 232 7021 6243 8755 -503 -1144 -629 C ATOM 1739 OE1 GLU A 232 2.115 12.455 14.654 1.00 60.68 O ANISOU 1739 OE1 GLU A 232 7217 6435 9404 -617 -1206 -540 O ATOM 1740 OE2 GLU A 232 2.712 14.538 14.299 1.00 56.39 O ANISOU 1740 OE2 GLU A 232 6772 6251 8401 -493 -1039 -540 O ATOM 1741 N VAL A 233 5.500 8.693 12.271 1.00 59.41 N ANISOU 1741 N VAL A 233 7852 5621 9100 -125 -1236 -1144 N ATOM 1742 CA VAL A 233 6.307 7.512 12.557 1.00 55.87 C ANISOU 1742 CA VAL A 233 7455 4981 8790 -33 -1165 -1146 C ATOM 1743 C VAL A 233 7.322 7.304 11.437 1.00 57.24 C ANISOU 1743 C VAL A 233 7912 5125 8712 218 -1079 -1357 C ATOM 1744 O VAL A 233 8.525 7.264 11.689 1.00 62.26 O ANISOU 1744 O VAL A 233 8523 5845 9290 368 -840 -1288 O ATOM 1745 CB VAL A 233 5.430 6.240 12.746 1.00 57.30 C ANISOU 1745 CB VAL A 233 7628 4821 9323 -171 -1400 -1176 C ATOM 1746 CG1 VAL A 233 6.276 4.995 12.741 1.00 53.36 C ANISOU 1746 CG1 VAL A 233 7268 4079 8926 -33 -1356 -1236 C ATOM 1747 CG2 VAL A 233 4.648 6.307 14.043 1.00 50.81 C ANISOU 1747 CG2 VAL A 233 6504 4025 8778 -385 -1379 -902 C ATOM 1748 N ASP A 234 6.837 7.184 10.202 1.00 63.31 N ANISOU 1748 N ASP A 234 8950 5774 9329 278 -1272 -1609 N ATOM 1749 CA ASP A 234 7.712 6.971 9.050 1.00 66.41 C ANISOU 1749 CA ASP A 234 9671 6124 9436 549 -1173 -1821 C ATOM 1750 C ASP A 234 8.800 8.042 8.949 1.00 66.55 C ANISOU 1750 C ASP A 234 9646 6451 9189 693 -829 -1715 C ATOM 1751 O ASP A 234 9.969 7.737 8.719 1.00 62.86 O ANISOU 1751 O ASP A 234 9253 5989 8642 906 -588 -1732 O ATOM 1752 CB ASP A 234 6.902 6.937 7.758 1.00 65.77 C ANISOU 1752 CB ASP A 234 9916 5911 9161 590 -1460 -2097 C ATOM 1753 CG ASP A 234 6.000 5.725 7.665 1.00 75.68 C ANISOU 1753 CG ASP A 234 11257 6800 10698 475 -1825 -2250 C ATOM 1754 OD1 ASP A 234 6.425 4.620 8.067 1.00 79.94 O ANISOU 1754 OD1 ASP A 234 11804 7115 11456 508 -1795 -2250 O ATOM 1755 OD2 ASP A 234 4.857 5.887 7.188 1.00 77.40 O ANISOU 1755 OD2 ASP A 234 11526 6941 10940 346 -2158 -2365 O ATOM 1756 N PHE A 235 8.407 9.295 9.131 1.00 61.39 N ANISOU 1756 N PHE A 235 8856 6040 8431 576 -804 -1598 N ATOM 1757 CA PHE A 235 9.353 10.395 9.099 1.00 58.36 C ANISOU 1757 CA PHE A 235 8404 5927 7844 665 -501 -1477 C ATOM 1758 C PHE A 235 10.470 10.260 10.151 1.00 58.26 C ANISOU 1758 C PHE A 235 8126 5998 8012 684 -265 -1279 C ATOM 1759 O PHE A 235 11.647 10.352 9.807 1.00 62.24 O ANISOU 1759 O PHE A 235 8652 6576 8421 866 -8 -1267 O ATOM 1760 CB PHE A 235 8.609 11.721 9.259 1.00 53.27 C ANISOU 1760 CB PHE A 235 7652 5485 7104 512 -557 -1377 C ATOM 1761 CG PHE A 235 9.511 12.912 9.411 1.00 53.31 C ANISOU 1761 CG PHE A 235 7547 5742 6965 549 -271 -1224 C ATOM 1762 CD1 PHE A 235 10.122 13.483 8.305 1.00 54.58 C ANISOU 1762 CD1 PHE A 235 7924 5984 6828 724 -87 -1291 C ATOM 1763 CD2 PHE A 235 9.731 13.475 10.658 1.00 52.74 C ANISOU 1763 CD2 PHE A 235 7172 5812 7055 410 -191 -1008 C ATOM 1764 CE1 PHE A 235 10.939 14.593 8.439 1.00 51.86 C ANISOU 1764 CE1 PHE A 235 7457 5847 6401 732 176 -1132 C ATOM 1765 CE2 PHE A 235 10.549 14.594 10.798 1.00 53.78 C ANISOU 1765 CE2 PHE A 235 7201 6146 7088 421 30 -877 C ATOM 1766 CZ PHE A 235 11.150 15.149 9.686 1.00 49.97 C ANISOU 1766 CZ PHE A 235 6897 5731 6360 568 215 -933 C ATOM 1767 N CYS A 236 10.105 10.049 11.416 1.00 50.24 N ANISOU 1767 N CYS A 236 6863 4971 7257 510 -351 -1115 N ATOM 1768 CA CYS A 236 11.099 9.921 12.485 1.00 49.06 C ANISOU 1768 CA CYS A 236 6480 4894 7266 530 -188 -926 C ATOM 1769 C CYS A 236 11.988 8.704 12.276 1.00 52.41 C ANISOU 1769 C CYS A 236 6984 5137 7793 726 -108 -996 C ATOM 1770 O CYS A 236 13.199 8.754 12.522 1.00 54.86 O ANISOU 1770 O CYS A 236 7168 5538 8136 857 95 -906 O ATOM 1771 CB CYS A 236 10.429 9.799 13.855 1.00 46.51 C ANISOU 1771 CB CYS A 236 5950 4559 7162 334 -308 -743 C ATOM 1772 SG CYS A 236 9.618 11.278 14.441 1.00 53.28 S ANISOU 1772 SG CYS A 236 6666 5652 7927 143 -337 -609 S ATOM 1773 N ILE A 237 11.383 7.606 11.840 1.00 47.74 N ANISOU 1773 N ILE A 237 6588 4274 7278 748 -282 -1156 N ATOM 1774 CA ILE A 237 12.145 6.387 11.640 1.00 61.90 C ANISOU 1774 CA ILE A 237 8490 5853 9175 949 -223 -1238 C ATOM 1775 C ILE A 237 13.242 6.586 10.593 1.00 64.03 C ANISOU 1775 C ILE A 237 8908 6200 9220 1226 33 -1351 C ATOM 1776 O ILE A 237 14.380 6.160 10.804 1.00 71.45 O ANISOU 1776 O ILE A 237 9755 7138 10255 1407 229 -1288 O ATOM 1777 CB ILE A 237 11.240 5.191 11.287 1.00 66.19 C ANISOU 1777 CB ILE A 237 9253 6048 9847 911 -486 -1414 C ATOM 1778 CG1 ILE A 237 10.418 4.769 12.511 1.00 65.50 C ANISOU 1778 CG1 ILE A 237 8963 5856 10069 667 -653 -1233 C ATOM 1779 CG2 ILE A 237 12.075 4.009 10.792 1.00 55.87 C ANISOU 1779 CG2 ILE A 237 8148 4502 8579 1175 -409 -1556 C ATOM 1780 CD1 ILE A 237 11.253 4.157 13.631 1.00 66.09 C ANISOU 1780 CD1 ILE A 237 8862 5895 10354 726 -533 -1029 C ATOM 1781 N SER A 238 12.917 7.261 9.490 1.00 62.74 N ANISOU 1781 N SER A 238 8964 6111 8763 1271 48 -1496 N ATOM 1782 CA SER A 238 13.878 7.407 8.396 1.00 69.94 C ANISOU 1782 CA SER A 238 10069 7077 9428 1556 326 -1600 C ATOM 1783 C SER A 238 15.068 8.268 8.810 1.00 67.81 C ANISOU 1783 C SER A 238 9498 7076 9192 1602 651 -1379 C ATOM 1784 O SER A 238 16.200 7.993 8.416 1.00 67.60 O ANISOU 1784 O SER A 238 9469 7058 9157 1849 931 -1378 O ATOM 1785 CB SER A 238 13.222 7.964 7.131 1.00 72.62 C ANISOU 1785 CB SER A 238 10751 7432 9409 1605 261 -1787 C ATOM 1786 OG SER A 238 12.864 9.322 7.303 1.00 87.52 O ANISOU 1786 OG SER A 238 12491 9568 11193 1431 275 -1650 O ATOM 1787 N LEU A 239 14.814 9.299 9.613 1.00 59.79 N ANISOU 1787 N LEU A 239 8220 6263 8235 1370 607 -1195 N ATOM 1788 CA LEU A 239 15.898 10.157 10.097 1.00 62.50 C ANISOU 1788 CA LEU A 239 8257 6836 8654 1371 852 -988 C ATOM 1789 C LEU A 239 16.762 9.463 11.154 1.00 63.37 C ANISOU 1789 C LEU A 239 8087 6913 9078 1412 878 -848 C ATOM 1790 O LEU A 239 17.990 9.563 11.117 1.00 63.57 O ANISOU 1790 O LEU A 239 7932 7027 9197 1562 1122 -758 O ATOM 1791 CB LEU A 239 15.351 11.475 10.628 1.00 56.49 C ANISOU 1791 CB LEU A 239 7346 6270 7846 1122 769 -857 C ATOM 1792 CG LEU A 239 14.773 12.366 9.530 1.00 53.76 C ANISOU 1792 CG LEU A 239 7246 5997 7185 1122 801 -952 C ATOM 1793 CD1 LEU A 239 14.088 13.584 10.133 1.00 46.41 C ANISOU 1793 CD1 LEU A 239 6181 5220 6231 879 682 -833 C ATOM 1794 CD2 LEU A 239 15.874 12.779 8.559 1.00 53.45 C ANISOU 1794 CD2 LEU A 239 7269 6047 6993 1335 1161 -940 C ATOM 1795 N LEU A 240 16.118 8.759 12.083 1.00 57.67 N ANISOU 1795 N LEU A 240 7324 6057 8530 1285 630 -817 N ATOM 1796 CA LEU A 240 16.830 7.956 13.068 1.00 58.84 C ANISOU 1796 CA LEU A 240 7270 6134 8952 1347 615 -691 C ATOM 1797 C LEU A 240 17.757 6.927 12.414 1.00 69.54 C ANISOU 1797 C LEU A 240 8716 7336 10370 1653 789 -789 C ATOM 1798 O LEU A 240 18.909 6.794 12.812 1.00 71.97 O ANISOU 1798 O LEU A 240 8786 7705 10853 1790 933 -666 O ATOM 1799 CB LEU A 240 15.848 7.260 14.005 1.00 56.34 C ANISOU 1799 CB LEU A 240 6974 5655 8777 1181 345 -647 C ATOM 1800 CG LEU A 240 15.286 8.185 15.076 1.00 59.81 C ANISOU 1800 CG LEU A 240 7236 6265 9225 933 226 -473 C ATOM 1801 CD1 LEU A 240 14.032 7.601 15.695 1.00 54.82 C ANISOU 1801 CD1 LEU A 240 6678 5470 8682 765 8 -449 C ATOM 1802 CD2 LEU A 240 16.344 8.457 16.142 1.00 61.45 C ANISOU 1802 CD2 LEU A 240 7164 6611 9576 959 271 -271 C ATOM 1803 N ARG A 241 17.270 6.210 11.405 1.00 68.42 N ANISOU 1803 N ARG A 241 8918 6988 10089 1776 765 -1016 N ATOM 1804 CA ARG A 241 18.107 5.204 10.759 1.00 69.34 C ANISOU 1804 CA ARG A 241 9172 6935 10240 2099 939 -1132 C ATOM 1805 C ARG A 241 19.193 5.813 9.873 1.00 76.59 C ANISOU 1805 C ARG A 241 10055 8028 11019 2330 1317 -1129 C ATOM 1806 O ARG A 241 20.339 5.357 9.886 1.00 78.14 O ANISOU 1806 O ARG A 241 10103 8215 11371 2572 1541 -1069 O ATOM 1807 CB ARG A 241 17.256 4.210 9.972 1.00 67.30 C ANISOU 1807 CB ARG A 241 9334 6366 9872 2169 768 -1397 C ATOM 1808 CG ARG A 241 16.345 3.362 10.845 1.00 61.41 C ANISOU 1808 CG ARG A 241 8594 5387 9353 1972 440 -1376 C ATOM 1809 CD ARG A 241 15.721 2.216 10.063 1.00 66.54 C ANISOU 1809 CD ARG A 241 9640 5673 9970 2068 267 -1645 C ATOM 1810 NE ARG A 241 15.013 1.293 10.947 1.00 70.37 N ANISOU 1810 NE ARG A 241 10092 5899 10745 1892 -2 -1586 N ATOM 1811 CZ ARG A 241 15.615 0.373 11.698 1.00 73.93 C ANISOU 1811 CZ ARG A 241 10442 6193 11457 1996 24 -1471 C ATOM 1812 NH1 ARG A 241 16.941 0.254 11.671 1.00 72.96 N ANISOU 1812 NH1 ARG A 241 10211 6153 11358 2279 287 -1413 N ATOM 1813 NH2 ARG A 241 14.895 -0.428 12.477 1.00 71.39 N ANISOU 1813 NH2 ARG A 241 10113 5624 11390 1821 -206 -1395 N ATOM 1814 N GLU A 242 18.842 6.845 9.113 1.00 74.72 N ANISOU 1814 N GLU A 242 9940 7946 10506 2265 1401 -1173 N ATOM 1815 CA GLU A 242 19.803 7.458 8.195 1.00 77.88 C ANISOU 1815 CA GLU A 242 10335 8500 10755 2480 1798 -1148 C ATOM 1816 C GLU A 242 20.784 8.392 8.904 1.00 75.11 C ANISOU 1816 C GLU A 242 9508 8403 10626 2391 1978 -877 C ATOM 1817 O GLU A 242 21.950 8.496 8.511 1.00 74.84 O ANISOU 1817 O GLU A 242 9312 8452 10671 2605 2328 -792 O ATOM 1818 CB GLU A 242 19.086 8.199 7.061 1.00 84.39 C ANISOU 1818 CB GLU A 242 11509 9374 11180 2468 1829 -1284 C ATOM 1819 CG GLU A 242 20.033 8.914 6.105 1.00 92.95 C ANISOU 1819 CG GLU A 242 12611 10620 12085 2684 2280 -1222 C ATOM 1820 CD GLU A 242 19.381 9.291 4.791 1.00100.02 C ANISOU 1820 CD GLU A 242 13987 11494 12522 2784 2323 -1399 C ATOM 1821 OE1 GLU A 242 18.208 8.914 4.573 1.00101.30 O ANISOU 1821 OE1 GLU A 242 14466 11500 12523 2700 1969 -1600 O ATOM 1822 OE2 GLU A 242 20.052 9.958 3.974 1.00104.13 O ANISOU 1822 OE2 GLU A 242 14564 12147 12854 2953 2709 -1327 O ATOM 1823 N ARG A 243 20.316 9.062 9.953 1.00 71.51 N ANISOU 1823 N ARG A 243 8826 8059 10287 2082 1735 -740 N ATOM 1824 CA ARG A 243 21.143 10.036 10.663 1.00 67.99 C ANISOU 1824 CA ARG A 243 7959 7832 10042 1960 1829 -506 C ATOM 1825 C ARG A 243 21.092 9.839 12.186 1.00 68.60 C ANISOU 1825 C ARG A 243 7768 7911 10388 1782 1533 -371 C ATOM 1826 O ARG A 243 20.804 10.782 12.926 1.00 66.86 O ANISOU 1826 O ARG A 243 7394 7826 10185 1537 1385 -257 O ATOM 1827 CB ARG A 243 20.702 11.459 10.297 1.00 66.98 C ANISOU 1827 CB ARG A 243 7868 7876 9706 1769 1871 -465 C ATOM 1828 CG ARG A 243 20.873 11.830 8.822 1.00 74.50 C ANISOU 1828 CG ARG A 243 9080 8856 10370 1954 2198 -548 C ATOM 1829 CD ARG A 243 22.344 12.020 8.468 1.00 80.75 C ANISOU 1829 CD ARG A 243 9603 9746 11333 2149 2613 -402 C ATOM 1830 NE ARG A 243 22.580 12.142 7.029 1.00 86.83 N ANISOU 1830 NE ARG A 243 10668 10515 11810 2398 2987 -476 N ATOM 1831 CZ ARG A 243 22.713 13.299 6.384 1.00 87.11 C ANISOU 1831 CZ ARG A 243 10727 10686 11683 2351 3227 -375 C ATOM 1832 NH1 ARG A 243 22.630 14.449 7.045 1.00 82.39 N ANISOU 1832 NH1 ARG A 243 9870 10225 11212 2052 3114 -212 N ATOM 1833 NH2 ARG A 243 22.929 13.305 5.076 1.00 87.73 N ANISOU 1833 NH2 ARG A 243 11121 10750 11460 2616 3584 -436 N ATOM 1834 N PHE A 244 21.378 8.620 12.648 1.00 70.65 N ANISOU 1834 N PHE A 244 8003 8007 10835 1925 1452 -381 N ATOM 1835 CA PHE A 244 21.332 8.309 14.077 1.00 72.30 C ANISOU 1835 CA PHE A 244 8013 8193 11263 1797 1177 -244 C ATOM 1836 C PHE A 244 22.267 9.196 14.885 1.00 72.97 C ANISOU 1836 C PHE A 244 7695 8484 11548 1710 1177 -38 C ATOM 1837 O PHE A 244 21.856 9.819 15.872 1.00 71.21 O ANISOU 1837 O PHE A 244 7382 8346 11328 1482 947 61 O ATOM 1838 CB PHE A 244 21.671 6.842 14.337 1.00 73.83 C ANISOU 1838 CB PHE A 244 8247 8164 11639 2012 1132 -269 C ATOM 1839 CG PHE A 244 21.228 6.358 15.688 1.00 76.31 C ANISOU 1839 CG PHE A 244 8510 8396 12091 1877 826 -154 C ATOM 1840 CD1 PHE A 244 19.874 6.274 15.995 1.00 70.00 C ANISOU 1840 CD1 PHE A 244 7930 7503 11162 1667 615 -199 C ATOM 1841 CD2 PHE A 244 22.156 5.985 16.654 1.00 77.20 C ANISOU 1841 CD2 PHE A 244 8350 8518 12463 1972 754 15 C ATOM 1842 CE1 PHE A 244 19.450 5.832 17.243 1.00 64.41 C ANISOU 1842 CE1 PHE A 244 7190 6717 10565 1556 384 -64 C ATOM 1843 CE2 PHE A 244 21.738 5.536 17.904 1.00 71.27 C ANISOU 1843 CE2 PHE A 244 7601 7686 11793 1871 484 137 C ATOM 1844 CZ PHE A 244 20.380 5.460 18.195 1.00 65.71 C ANISOU 1844 CZ PHE A 244 7136 6891 10941 1665 323 104 C ATOM 1845 N MET A 245 23.521 9.249 14.448 1.00 72.96 N ANISOU 1845 N MET A 245 7454 8551 11719 1899 1435 24 N ATOM 1846 CA MET A 245 24.543 10.064 15.095 1.00 73.66 C ANISOU 1846 CA MET A 245 7113 8814 12061 1825 1432 215 C ATOM 1847 C MET A 245 24.101 11.501 15.333 1.00 74.48 C ANISOU 1847 C MET A 245 7177 9078 12044 1529 1342 269 C ATOM 1848 O MET A 245 24.388 12.067 16.382 1.00 78.04 O ANISOU 1848 O MET A 245 7391 9615 12645 1371 1120 395 O ATOM 1849 CB MET A 245 25.829 10.042 14.277 1.00 77.01 C ANISOU 1849 CB MET A 245 7294 9291 12677 2064 1805 267 C ATOM 1850 CG MET A 245 26.607 8.753 14.414 1.00 83.63 C ANISOU 1850 CG MET A 245 8021 9999 13757 2365 1854 279 C ATOM 1851 SD MET A 245 27.221 8.521 16.094 1.00116.16 S ANISOU 1851 SD MET A 245 11764 14137 18233 2299 1465 468 S ATOM 1852 CE MET A 245 26.201 7.175 16.637 1.00 57.96 C ANISOU 1852 CE MET A 245 4783 6520 10720 2350 1200 365 C ATOM 1853 N GLU A 246 23.398 12.088 14.369 1.00 71.32 N ANISOU 1853 N GLU A 246 7034 8704 11361 1469 1492 166 N ATOM 1854 CA GLU A 246 22.884 13.439 14.539 1.00 72.94 C ANISOU 1854 CA GLU A 246 7244 9035 11434 1205 1409 207 C ATOM 1855 C GLU A 246 21.785 13.473 15.591 1.00 67.82 C ANISOU 1855 C GLU A 246 6732 8358 10680 1007 1052 193 C ATOM 1856 O GLU A 246 21.650 14.454 16.334 1.00 67.32 O ANISOU 1856 O GLU A 246 6566 8392 10622 803 891 275 O ATOM 1857 CB GLU A 246 22.354 14.007 13.218 1.00 81.87 C ANISOU 1857 CB GLU A 246 8649 10188 12268 1219 1647 107 C ATOM 1858 CG GLU A 246 23.377 14.826 12.432 1.00 89.84 C ANISOU 1858 CG GLU A 246 9465 11308 13362 1274 2001 213 C ATOM 1859 CD GLU A 246 23.839 14.127 11.173 1.00 93.71 C ANISOU 1859 CD GLU A 246 10101 11739 13765 1581 2373 139 C ATOM 1860 OE1 GLU A 246 23.918 12.878 11.182 1.00 97.24 O ANISOU 1860 OE1 GLU A 246 10630 12060 14255 1784 2350 46 O ATOM 1861 OE2 GLU A 246 24.116 14.827 10.174 1.00 95.78 O ANISOU 1861 OE2 GLU A 246 10423 12068 13901 1634 2697 176 O ATOM 1862 N CYS A 247 21.002 12.402 15.657 1.00 57.75 N ANISOU 1862 N CYS A 247 5692 6933 9318 1074 941 92 N ATOM 1863 CA CYS A 247 19.914 12.344 16.623 1.00 63.71 C ANISOU 1863 CA CYS A 247 6571 7648 9989 904 655 102 C ATOM 1864 C CYS A 247 20.448 12.205 18.046 1.00 64.23 C ANISOU 1864 C CYS A 247 6418 7737 10251 870 443 255 C ATOM 1865 O CYS A 247 19.794 12.611 19.007 1.00 63.31 O ANISOU 1865 O CYS A 247 6347 7652 10057 712 236 314 O ATOM 1866 CB CYS A 247 18.948 11.211 16.287 1.00 61.58 C ANISOU 1866 CB CYS A 247 6585 7186 9626 966 599 -27 C ATOM 1867 SG CYS A 247 17.973 11.523 14.803 1.00 68.74 S ANISOU 1867 SG CYS A 247 7814 8063 10242 958 712 -225 S ATOM 1868 N LEU A 248 21.649 11.651 18.173 1.00 62.27 N ANISOU 1868 N LEU A 248 5941 7472 10245 1040 496 323 N ATOM 1869 CA LEU A 248 22.230 11.423 19.487 1.00 61.66 C ANISOU 1869 CA LEU A 248 5670 7404 10354 1044 259 466 C ATOM 1870 C LEU A 248 22.610 12.706 20.223 1.00 61.52 C ANISOU 1870 C LEU A 248 5457 7545 10371 866 106 563 C ATOM 1871 O LEU A 248 22.715 12.697 21.447 1.00 66.66 O ANISOU 1871 O LEU A 248 6059 8204 11064 825 -163 659 O ATOM 1872 CB LEU A 248 23.425 10.479 19.402 1.00 73.91 C ANISOU 1872 CB LEU A 248 7007 8890 12185 1294 336 514 C ATOM 1873 CG LEU A 248 23.045 9.023 19.151 1.00 82.10 C ANISOU 1873 CG LEU A 248 8264 9715 13214 1477 373 440 C ATOM 1874 CD1 LEU A 248 24.213 8.107 19.451 1.00 86.24 C ANISOU 1874 CD1 LEU A 248 8565 10168 14032 1727 370 526 C ATOM 1875 CD2 LEU A 248 21.855 8.646 19.997 1.00 83.53 C ANISOU 1875 CD2 LEU A 248 8695 9795 13246 1347 145 457 C ATOM 1876 N MET A 249 22.796 13.810 19.499 1.00 60.96 N ANISOU 1876 N MET A 249 5309 7584 10270 764 264 539 N ATOM 1877 CA MET A 249 23.116 15.087 20.147 1.00 63.43 C ANISOU 1877 CA MET A 249 5460 8012 10627 574 105 616 C ATOM 1878 C MET A 249 21.976 15.526 21.081 1.00 59.00 C ANISOU 1878 C MET A 249 5148 7454 9815 414 -138 604 C ATOM 1879 O MET A 249 22.133 16.442 21.889 1.00 57.53 O ANISOU 1879 O MET A 249 4899 7331 9629 278 -343 654 O ATOM 1880 CB MET A 249 23.416 16.184 19.113 1.00 63.64 C ANISOU 1880 CB MET A 249 5397 8123 10662 486 352 603 C ATOM 1881 CG MET A 249 22.175 16.982 18.698 1.00 75.22 C ANISOU 1881 CG MET A 249 7167 9609 11805 337 391 517 C ATOM 1882 SD MET A 249 22.439 18.468 17.683 1.00 92.72 S ANISOU 1882 SD MET A 249 9323 11909 13998 206 631 537 S ATOM 1883 CE MET A 249 22.598 17.734 16.044 1.00 83.75 C ANISOU 1883 CE MET A 249 8289 10739 12791 435 1049 468 C ATOM 1884 N ILE A 250 20.828 14.869 20.959 1.00 57.56 N ANISOU 1884 N ILE A 250 5247 7191 9431 437 -111 536 N ATOM 1885 CA ILE A 250 19.713 15.122 21.858 1.00 53.45 C ANISOU 1885 CA ILE A 250 4945 6666 8699 321 -291 550 C ATOM 1886 C ILE A 250 20.103 14.785 23.295 1.00 55.57 C ANISOU 1886 C ILE A 250 5167 6919 9028 358 -558 667 C ATOM 1887 O ILE A 250 19.799 15.545 24.226 1.00 55.50 O ANISOU 1887 O ILE A 250 5238 6963 8886 256 -742 706 O ATOM 1888 CB ILE A 250 18.467 14.323 21.448 1.00 51.70 C ANISOU 1888 CB ILE A 250 4974 6337 8331 342 -210 478 C ATOM 1889 CG1 ILE A 250 17.862 14.927 20.176 1.00 46.32 C ANISOU 1889 CG1 ILE A 250 4401 5686 7511 281 -25 356 C ATOM 1890 CG2 ILE A 250 17.435 14.315 22.580 1.00 46.95 C ANISOU 1890 CG2 ILE A 250 4545 5715 7579 262 -373 545 C ATOM 1891 CD1 ILE A 250 16.762 14.089 19.549 1.00 40.50 C ANISOU 1891 CD1 ILE A 250 3881 4827 6682 310 29 257 C ATOM 1892 N GLY A 251 20.799 13.661 23.473 1.00 53.85 N ANISOU 1892 N GLY A 251 4844 6621 8994 525 -586 720 N ATOM 1893 CA GLY A 251 21.167 13.198 24.803 1.00 49.47 C ANISOU 1893 CA GLY A 251 4280 6036 8482 598 -850 842 C ATOM 1894 C GLY A 251 20.131 12.210 25.334 1.00 56.51 C ANISOU 1894 C GLY A 251 5440 6801 9229 645 -865 889 C ATOM 1895 O GLY A 251 19.263 11.746 24.583 1.00 56.39 O ANISOU 1895 O GLY A 251 5565 6705 9157 628 -684 816 O ATOM 1896 N ARG A 252 20.203 11.912 26.630 1.00 53.69 N ANISOU 1896 N ARG A 252 5165 6417 8816 701 -1090 1018 N ATOM 1897 CA ARG A 252 19.419 10.837 27.235 1.00 49.42 C ANISOU 1897 CA ARG A 252 4850 5733 8192 771 -1091 1116 C ATOM 1898 C ARG A 252 17.892 10.942 27.123 1.00 50.71 C ANISOU 1898 C ARG A 252 5247 5863 8159 642 -948 1096 C ATOM 1899 O ARG A 252 17.200 9.915 27.141 1.00 55.28 O ANISOU 1899 O ARG A 252 5955 6285 8764 676 -865 1149 O ATOM 1900 CB ARG A 252 19.802 10.681 28.702 1.00 53.65 C ANISOU 1900 CB ARG A 252 5467 6268 8652 865 -1359 1277 C ATOM 1901 CG ARG A 252 19.454 11.904 29.552 1.00 50.73 C ANISOU 1901 CG ARG A 252 5228 6025 8022 754 -1509 1287 C ATOM 1902 CD ARG A 252 19.647 11.581 31.021 1.00 46.17 C ANISOU 1902 CD ARG A 252 4829 5417 7296 881 -1762 1449 C ATOM 1903 NE ARG A 252 21.027 11.191 31.283 1.00 54.73 N ANISOU 1903 NE ARG A 252 5703 6492 8601 1025 -2000 1492 N ATOM 1904 CZ ARG A 252 21.929 11.996 31.834 1.00 58.24 C ANISOU 1904 CZ ARG A 252 6034 7032 9063 1022 -2301 1475 C ATOM 1905 NH1 ARG A 252 21.575 13.219 32.199 1.00 55.68 N ANISOU 1905 NH1 ARG A 252 5832 6803 8520 887 -2395 1407 N ATOM 1906 NH2 ARG A 252 23.171 11.571 32.039 1.00 52.11 N ANISOU 1906 NH2 ARG A 252 5022 6241 8538 1158 -2527 1525 N ATOM 1907 N ASP A 253 17.354 12.151 27.023 1.00 47.12 N ANISOU 1907 N ASP A 253 4834 5535 7536 495 -924 1029 N ATOM 1908 CA ASP A 253 15.906 12.288 26.905 1.00 51.51 C ANISOU 1908 CA ASP A 253 5567 6066 7939 385 -791 1018 C ATOM 1909 C ASP A 253 15.377 11.634 25.634 1.00 52.31 C ANISOU 1909 C ASP A 253 5654 6061 8162 360 -613 906 C ATOM 1910 O ASP A 253 14.185 11.363 25.520 1.00 56.17 O ANISOU 1910 O ASP A 253 6259 6474 8609 285 -528 913 O ATOM 1911 CB ASP A 253 15.471 13.755 26.994 1.00 50.19 C ANISOU 1911 CB ASP A 253 5445 6049 7577 258 -801 960 C ATOM 1912 CG ASP A 253 15.233 14.203 28.430 1.00 55.96 C ANISOU 1912 CG ASP A 253 6346 6825 8091 280 -940 1081 C ATOM 1913 OD1 ASP A 253 16.219 14.564 29.120 1.00 58.62 O ANISOU 1913 OD1 ASP A 253 6648 7214 8411 335 -1150 1108 O ATOM 1914 OD2 ASP A 253 14.060 14.182 28.873 1.00 50.61 O ANISOU 1914 OD2 ASP A 253 5840 6125 7265 253 -841 1151 O ATOM 1915 N LEU A 254 16.270 11.364 24.687 1.00 48.42 N ANISOU 1915 N LEU A 254 5019 5552 7826 433 -561 805 N ATOM 1916 CA LEU A 254 15.893 10.628 23.490 1.00 54.83 C ANISOU 1916 CA LEU A 254 5868 6237 8729 453 -420 681 C ATOM 1917 C LEU A 254 15.384 9.238 23.866 1.00 57.01 C ANISOU 1917 C LEU A 254 6259 6294 9109 509 -436 760 C ATOM 1918 O LEU A 254 14.439 8.737 23.261 1.00 58.99 O ANISOU 1918 O LEU A 254 6613 6412 9387 448 -374 688 O ATOM 1919 CB LEU A 254 17.074 10.515 22.527 1.00 54.92 C ANISOU 1919 CB LEU A 254 5729 6264 8874 574 -332 581 C ATOM 1920 CG LEU A 254 16.774 9.716 21.261 1.00 55.05 C ANISOU 1920 CG LEU A 254 5840 6133 8942 640 -193 430 C ATOM 1921 CD1 LEU A 254 15.522 10.275 20.604 1.00 45.01 C ANISOU 1921 CD1 LEU A 254 4713 4879 7509 488 -153 323 C ATOM 1922 CD2 LEU A 254 17.954 9.742 20.288 1.00 56.14 C ANISOU 1922 CD2 LEU A 254 5847 6312 9173 788 -47 341 C ATOM 1923 N VAL A 255 16.009 8.619 24.867 1.00 58.45 N ANISOU 1923 N VAL A 255 6425 6420 9361 623 -539 913 N ATOM 1924 CA VAL A 255 15.558 7.316 25.346 1.00 55.85 C ANISOU 1924 CA VAL A 255 6220 5864 9137 678 -550 1028 C ATOM 1925 C VAL A 255 14.148 7.370 25.947 1.00 56.38 C ANISOU 1925 C VAL A 255 6430 5888 9103 531 -517 1135 C ATOM 1926 O VAL A 255 13.329 6.481 25.702 1.00 53.40 O ANISOU 1926 O VAL A 255 6135 5306 8849 483 -461 1149 O ATOM 1927 CB VAL A 255 16.549 6.714 26.365 1.00 54.32 C ANISOU 1927 CB VAL A 255 5997 5629 9014 852 -681 1195 C ATOM 1928 CG1 VAL A 255 16.032 5.380 26.889 1.00 45.77 C ANISOU 1928 CG1 VAL A 255 5070 4287 8032 905 -676 1342 C ATOM 1929 CG2 VAL A 255 17.920 6.537 25.722 1.00 52.71 C ANISOU 1929 CG2 VAL A 255 5603 5448 8977 1014 -690 1103 C ATOM 1930 N ARG A 256 13.867 8.418 26.718 1.00 54.07 N ANISOU 1930 N ARG A 256 6162 5776 8607 463 -548 1210 N ATOM 1931 CA ARG A 256 12.561 8.568 27.349 1.00 53.48 C ANISOU 1931 CA ARG A 256 6206 5685 8430 352 -475 1332 C ATOM 1932 C ARG A 256 11.477 8.614 26.277 1.00 50.54 C ANISOU 1932 C ARG A 256 5809 5257 8139 205 -373 1197 C ATOM 1933 O ARG A 256 10.449 7.941 26.387 1.00 54.82 O ANISOU 1933 O ARG A 256 6397 5639 8794 128 -306 1283 O ATOM 1934 CB ARG A 256 12.529 9.827 28.225 1.00 49.67 C ANISOU 1934 CB ARG A 256 5773 5415 7685 335 -519 1390 C ATOM 1935 CG ARG A 256 11.291 9.967 29.122 1.00 49.08 C ANISOU 1935 CG ARG A 256 5839 5334 7474 281 -411 1561 C ATOM 1936 CD ARG A 256 11.390 11.199 30.030 1.00 54.77 C ANISOU 1936 CD ARG A 256 6662 6248 7899 311 -469 1597 C ATOM 1937 NE ARG A 256 11.756 12.400 29.275 1.00 53.84 N ANISOU 1937 NE ARG A 256 6442 6288 7725 241 -526 1393 N ATOM 1938 CZ ARG A 256 10.898 13.198 28.645 1.00 48.90 C ANISOU 1938 CZ ARG A 256 5789 5734 7059 126 -424 1292 C ATOM 1939 NH1 ARG A 256 9.598 12.946 28.683 1.00 55.41 N ANISOU 1939 NH1 ARG A 256 6645 6497 7912 64 -269 1371 N ATOM 1940 NH2 ARG A 256 11.343 14.257 27.976 1.00 44.33 N ANISOU 1940 NH2 ARG A 256 5135 5277 6430 74 -478 1128 N ATOM 1941 N LEU A 257 11.738 9.386 25.227 1.00 50.26 N ANISOU 1941 N LEU A 257 5696 5339 8062 169 -372 993 N ATOM 1942 CA LEU A 257 10.805 9.537 24.122 1.00 49.86 C ANISOU 1942 CA LEU A 257 5641 5251 8052 53 -321 841 C ATOM 1943 C LEU A 257 10.633 8.232 23.345 1.00 51.39 C ANISOU 1943 C LEU A 257 5869 5191 8465 69 -330 758 C ATOM 1944 O LEU A 257 9.530 7.911 22.911 1.00 54.32 O ANISOU 1944 O LEU A 257 6263 5438 8938 -46 -331 719 O ATOM 1945 CB LEU A 257 11.258 10.650 23.178 1.00 43.89 C ANISOU 1945 CB LEU A 257 4834 4671 7171 43 -312 660 C ATOM 1946 CG LEU A 257 11.290 12.094 23.690 1.00 48.98 C ANISOU 1946 CG LEU A 257 5460 5538 7611 -4 -317 692 C ATOM 1947 CD1 LEU A 257 11.684 13.060 22.588 1.00 51.06 C ANISOU 1947 CD1 LEU A 257 5682 5925 7795 -24 -288 524 C ATOM 1948 CD2 LEU A 257 9.958 12.495 24.242 1.00 45.62 C ANISOU 1948 CD2 LEU A 257 5088 5135 7111 -103 -280 781 C ATOM 1949 N LEU A 258 11.714 7.483 23.164 1.00 54.22 N ANISOU 1949 N LEU A 258 6227 5458 8916 217 -352 727 N ATOM 1950 CA LEU A 258 11.637 6.226 22.411 1.00 53.00 C ANISOU 1950 CA LEU A 258 6145 5035 8959 262 -368 625 C ATOM 1951 C LEU A 258 10.910 5.141 23.200 1.00 56.65 C ANISOU 1951 C LEU A 258 6667 5254 9603 208 -387 806 C ATOM 1952 O LEU A 258 10.226 4.307 22.612 1.00 61.66 O ANISOU 1952 O LEU A 258 7365 5646 10418 140 -421 728 O ATOM 1953 CB LEU A 258 13.028 5.746 21.999 1.00 56.25 C ANISOU 1953 CB LEU A 258 6536 5414 9423 469 -356 547 C ATOM 1954 CG LEU A 258 13.658 6.548 20.867 1.00 57.02 C ANISOU 1954 CG LEU A 258 6590 5675 9402 527 -287 348 C ATOM 1955 CD1 LEU A 258 15.076 6.068 20.554 1.00 53.45 C ANISOU 1955 CD1 LEU A 258 6073 5199 9035 753 -231 309 C ATOM 1956 CD2 LEU A 258 12.769 6.470 19.635 1.00 54.23 C ANISOU 1956 CD2 LEU A 258 6365 5221 9020 453 -289 140 C ATOM 1957 N GLN A 259 11.053 5.154 24.526 1.00 59.16 N ANISOU 1957 N GLN A 259 6982 5623 9874 238 -372 1050 N ATOM 1958 CA GLN A 259 10.336 4.200 25.371 1.00 60.70 C ANISOU 1958 CA GLN A 259 7245 5596 10223 188 -345 1272 C ATOM 1959 C GLN A 259 8.843 4.445 25.236 1.00 62.29 C ANISOU 1959 C GLN A 259 7413 5764 10491 -23 -291 1295 C ATOM 1960 O GLN A 259 8.061 3.506 25.137 1.00 69.47 O ANISOU 1960 O GLN A 259 8339 6408 11650 -123 -289 1351 O ATOM 1961 CB GLN A 259 10.768 4.300 26.846 1.00 57.50 C ANISOU 1961 CB GLN A 259 6886 5280 9681 288 -330 1540 C ATOM 1962 CG GLN A 259 12.168 3.719 27.148 1.00 71.37 C ANISOU 1962 CG GLN A 259 8663 6994 11460 508 -420 1574 C ATOM 1963 CD GLN A 259 12.566 3.830 28.625 1.00 76.92 C ANISOU 1963 CD GLN A 259 9447 7780 11998 619 -458 1833 C ATOM 1964 OE1 GLN A 259 12.078 4.699 29.352 1.00 83.57 O ANISOU 1964 OE1 GLN A 259 10331 8798 12626 560 -421 1933 O ATOM 1965 NE2 GLN A 259 13.453 2.941 29.069 1.00 71.80 N ANISOU 1965 NE2 GLN A 259 8848 6997 11437 802 -541 1939 N ATOM 1966 N ASN A 260 8.456 5.716 25.207 1.00 56.87 N ANISOU 1966 N ASN A 260 6665 5334 9610 -92 -257 1252 N ATOM 1967 CA ASN A 260 7.041 6.083 25.148 1.00 56.56 C ANISOU 1967 CA ASN A 260 6558 5298 9636 -271 -199 1292 C ATOM 1968 C ASN A 260 6.328 5.696 23.857 1.00 53.90 C ANISOU 1968 C ASN A 260 6181 4795 9506 -394 -295 1081 C ATOM 1969 O ASN A 260 5.116 5.752 23.799 1.00 54.20 O ANISOU 1969 O ASN A 260 6129 4776 9689 -549 -280 1129 O ATOM 1970 CB ASN A 260 6.867 7.579 25.407 1.00 54.61 C ANISOU 1970 CB ASN A 260 6273 5358 9118 -282 -148 1283 C ATOM 1971 CG ASN A 260 7.217 7.965 26.831 1.00 55.56 C ANISOU 1971 CG ASN A 260 6468 5610 9033 -184 -69 1510 C ATOM 1972 OD1 ASN A 260 7.094 7.154 27.744 1.00 55.11 O ANISOU 1972 OD1 ASN A 260 6476 5415 9049 -148 -2 1737 O ATOM 1973 ND2 ASN A 260 7.636 9.218 27.028 1.00 53.55 N ANISOU 1973 ND2 ASN A 260 6229 5606 8512 -136 -85 1451 N ATOM 1974 N VAL A 261 7.079 5.315 22.826 1.00 60.31 N ANISOU 1974 N VAL A 261 7060 5525 10329 -311 -398 848 N ATOM 1975 CA VAL A 261 6.487 4.891 21.555 1.00 56.27 C ANISOU 1975 CA VAL A 261 6576 4833 9971 -395 -529 617 C ATOM 1976 C VAL A 261 6.922 3.476 21.173 1.00 59.59 C ANISOU 1976 C VAL A 261 7115 4923 10601 -325 -609 541 C ATOM 1977 O VAL A 261 6.676 3.028 20.054 1.00 66.30 O ANISOU 1977 O VAL A 261 8052 5596 11542 -346 -746 305 O ATOM 1978 CB VAL A 261 6.866 5.847 20.408 1.00 53.80 C ANISOU 1978 CB VAL A 261 6301 4716 9423 -335 -574 355 C ATOM 1979 CG1 VAL A 261 6.288 7.226 20.654 1.00 40.74 C ANISOU 1979 CG1 VAL A 261 4547 3339 7592 -415 -520 409 C ATOM 1980 CG2 VAL A 261 8.400 5.913 20.263 1.00 46.87 C ANISOU 1980 CG2 VAL A 261 5486 3938 8383 -126 -514 289 C ATOM 1981 N ALA A 262 7.543 2.777 22.121 1.00 51.26 N ANISOU 1981 N ALA A 262 6089 3775 9613 -230 -539 739 N ATOM 1982 CA ALA A 262 8.142 1.465 21.888 1.00 56.27 C ANISOU 1982 CA ALA A 262 6848 4101 10430 -117 -597 691 C ATOM 1983 C ALA A 262 7.193 0.382 21.364 1.00 67.07 C ANISOU 1983 C ALA A 262 8276 5081 12126 -266 -725 619 C ATOM 1984 O ALA A 262 7.641 -0.570 20.711 1.00 78.31 O ANISOU 1984 O ALA A 262 9850 6237 13667 -166 -817 455 O ATOM 1985 CB ALA A 262 8.827 0.981 23.150 1.00 51.18 C ANISOU 1985 CB ALA A 262 6217 3429 9800 3 -509 966 C ATOM 1986 N ARG A 263 5.902 0.509 21.664 1.00 62.94 N ANISOU 1986 N ARG A 263 7631 4512 11773 -498 -733 744 N ATOM 1987 CA ARG A 263 4.927 -0.513 21.266 1.00 72.29 C ANISOU 1987 CA ARG A 263 8823 5305 13339 -681 -878 708 C ATOM 1988 C ARG A 263 4.414 -0.315 19.831 1.00 75.30 C ANISOU 1988 C ARG A 263 9250 5640 13719 -752 -1103 356 C ATOM 1989 O ARG A 263 3.659 -1.138 19.318 1.00 84.84 O ANISOU 1989 O ARG A 263 10483 6664 15088 -865 -1255 250 O ATOM 1990 CB ARG A 263 3.747 -0.563 22.247 1.00 69.97 C ANISOU 1990 CB ARG A 263 8341 5061 13184 -875 -756 1005 C ATOM 1991 CG ARG A 263 4.120 -0.845 23.705 1.00 77.54 C ANISOU 1991 CG ARG A 263 9306 6047 14108 -797 -534 1364 C ATOM 1992 CD ARG A 263 4.621 -2.278 23.933 1.00 93.13 C ANISOU 1992 CD ARG A 263 11434 7731 16218 -715 -555 1414 C ATOM 1993 NE ARG A 263 3.594 -3.298 23.698 1.00100.43 N ANISOU 1993 NE ARG A 263 12321 8424 17413 -896 -628 1401 N ATOM 1994 CZ ARG A 263 3.610 -4.519 24.234 1.00 99.24 C ANISOU 1994 CZ ARG A 263 12257 8031 17420 -895 -586 1551 C ATOM 1995 NH1 ARG A 263 4.598 -4.872 25.048 1.00104.57 N ANISOU 1995 NH1 ARG A 263 13070 8678 17984 -706 -476 1727 N ATOM 1996 NH2 ARG A 263 2.637 -5.386 23.964 1.00 86.98 N ANISOU 1996 NH2 ARG A 263 10651 6259 16139 -1077 -667 1533 N ATOM 1997 N ILE A 264 4.818 0.776 19.189 1.00 67.91 N ANISOU 1997 N ILE A 264 8338 5012 12453 -651 -1099 172 N ATOM 1998 CA ILE A 264 4.500 0.978 17.781 1.00 67.13 C ANISOU 1998 CA ILE A 264 8351 4872 12282 -661 -1311 -168 C ATOM 1999 C ILE A 264 5.465 0.149 16.927 1.00 71.52 C ANISOU 1999 C ILE A 264 9184 5219 12774 -450 -1385 -421 C ATOM 2000 O ILE A 264 6.682 0.283 17.063 1.00 73.25 O ANISOU 2000 O ILE A 264 9467 5584 12781 -225 -1220 -413 O ATOM 2001 CB ILE A 264 4.587 2.465 17.397 1.00 63.96 C ANISOU 2001 CB ILE A 264 7899 4874 11528 -613 -1251 -248 C ATOM 2002 CG1 ILE A 264 3.642 3.289 18.264 1.00 54.44 C ANISOU 2002 CG1 ILE A 264 6440 3865 10379 -788 -1161 -4 C ATOM 2003 CG2 ILE A 264 4.242 2.675 15.929 1.00 65.80 C ANISOU 2003 CG2 ILE A 264 8289 5062 11649 -601 -1476 -585 C ATOM 2004 CD1 ILE A 264 3.618 4.745 17.906 1.00 49.83 C ANISOU 2004 CD1 ILE A 264 5814 3638 9481 -752 -1119 -77 C ATOM 2005 N PRO A 265 4.917 -0.706 16.042 1.00 71.20 N ANISOU 2005 N PRO A 265 9297 4871 12884 -507 -1626 -644 N ATOM 2006 CA PRO A 265 5.688 -1.713 15.292 1.00 67.31 C ANISOU 2006 CA PRO A 265 9096 4145 12334 -304 -1686 -872 C ATOM 2007 C PRO A 265 7.010 -1.197 14.715 1.00 67.54 C ANISOU 2007 C PRO A 265 9293 4318 12051 5 -1550 -1043 C ATOM 2008 O PRO A 265 8.040 -1.861 14.875 1.00 67.47 O ANISOU 2008 O PRO A 265 9388 4206 12041 220 -1429 -1033 O ATOM 2009 CB PRO A 265 4.737 -2.102 14.161 1.00 67.76 C ANISOU 2009 CB PRO A 265 9282 4086 12376 -408 -1960 -1124 C ATOM 2010 CG PRO A 265 3.375 -1.898 14.742 1.00 66.85 C ANISOU 2010 CG PRO A 265 8872 4037 12493 -704 -2030 -919 C ATOM 2011 CD PRO A 265 3.489 -0.710 15.665 1.00 63.32 C ANISOU 2011 CD PRO A 265 8187 3872 11999 -741 -1820 -680 C ATOM 2012 N GLU A 266 6.988 -0.035 14.066 1.00 66.91 N ANISOU 2012 N GLU A 266 9212 4552 11659 37 -1525 -1161 N ATOM 2013 CA GLU A 266 8.210 0.514 13.484 1.00 62.62 C ANISOU 2013 CA GLU A 266 8788 4244 10762 319 -1327 -1277 C ATOM 2014 C GLU A 266 9.275 0.734 14.548 1.00 64.95 C ANISOU 2014 C GLU A 266 8889 4747 11041 429 -1057 -1014 C ATOM 2015 O GLU A 266 10.468 0.506 14.309 1.00 66.26 O ANISOU 2015 O GLU A 266 9137 4938 11102 689 -900 -1067 O ATOM 2016 CB GLU A 266 7.921 1.810 12.727 1.00 63.94 C ANISOU 2016 CB GLU A 266 8966 4712 10617 303 -1330 -1391 C ATOM 2017 CG GLU A 266 7.190 1.608 11.392 1.00 73.38 C ANISOU 2017 CG GLU A 266 10444 5716 11719 302 -1608 -1716 C ATOM 2018 CD GLU A 266 5.672 1.558 11.528 1.00 72.42 C ANISOU 2018 CD GLU A 266 10198 5457 11860 -5 -1909 -1698 C ATOM 2019 OE1 GLU A 266 5.166 1.393 12.663 1.00 67.96 O ANISOU 2019 OE1 GLU A 266 9354 4868 11600 -209 -1881 -1432 O ATOM 2020 OE2 GLU A 266 4.984 1.696 10.489 1.00 72.18 O ANISOU 2020 OE2 GLU A 266 10340 5375 11709 -29 -2156 -1928 O ATOM 2021 N PHE A 267 8.832 1.144 15.733 1.00 51.08 N ANISOU 2021 N PHE A 267 6881 3127 9400 245 -1013 -730 N ATOM 2022 CA PHE A 267 9.748 1.442 16.822 1.00 61.75 C ANISOU 2022 CA PHE A 267 8061 4684 10715 334 -814 -479 C ATOM 2023 C PHE A 267 10.268 0.202 17.545 1.00 66.39 C ANISOU 2023 C PHE A 267 8679 5007 11538 431 -797 -343 C ATOM 2024 O PHE A 267 11.391 0.221 18.060 1.00 65.81 O ANISOU 2024 O PHE A 267 8539 5053 11412 614 -663 -230 O ATOM 2025 CB PHE A 267 9.134 2.459 17.786 1.00 60.28 C ANISOU 2025 CB PHE A 267 7653 4762 10487 144 -766 -246 C ATOM 2026 CG PHE A 267 9.135 3.869 17.246 1.00 56.44 C ANISOU 2026 CG PHE A 267 7121 4606 9718 134 -715 -337 C ATOM 2027 CD1 PHE A 267 10.311 4.605 17.199 1.00 52.25 C ANISOU 2027 CD1 PHE A 267 6546 4329 8978 297 -558 -333 C ATOM 2028 CD2 PHE A 267 7.968 4.450 16.766 1.00 61.39 C ANISOU 2028 CD2 PHE A 267 7738 5273 10316 -38 -831 -417 C ATOM 2029 CE1 PHE A 267 10.324 5.900 16.692 1.00 48.45 C ANISOU 2029 CE1 PHE A 267 6033 4121 8255 279 -502 -401 C ATOM 2030 CE2 PHE A 267 7.971 5.748 16.259 1.00 51.63 C ANISOU 2030 CE2 PHE A 267 6482 4320 8815 -34 -785 -490 C ATOM 2031 CZ PHE A 267 9.148 6.464 16.218 1.00 52.79 C ANISOU 2031 CZ PHE A 267 6610 4701 8748 120 -614 -480 C ATOM 2032 N GLU A 268 9.471 -0.870 17.566 1.00 65.29 N ANISOU 2032 N GLU A 268 8633 4498 11676 311 -947 -351 N ATOM 2033 CA GLU A 268 9.930 -2.150 18.102 1.00 67.96 C ANISOU 2033 CA GLU A 268 9051 4520 12250 415 -945 -244 C ATOM 2034 C GLU A 268 11.124 -2.646 17.310 1.00 71.19 C ANISOU 2034 C GLU A 268 9639 4844 12565 732 -893 -456 C ATOM 2035 O GLU A 268 12.129 -3.064 17.888 1.00 75.60 O ANISOU 2035 O GLU A 268 10165 5394 13165 931 -784 -324 O ATOM 2036 CB GLU A 268 8.821 -3.198 18.063 1.00 81.59 C ANISOU 2036 CB GLU A 268 10865 5820 14317 212 -1132 -251 C ATOM 2037 CG GLU A 268 8.110 -3.392 19.393 1.00 91.08 C ANISOU 2037 CG GLU A 268 11890 6990 15724 4 -1077 114 C ATOM 2038 CD GLU A 268 7.435 -4.744 19.494 1.00 98.46 C ANISOU 2038 CD GLU A 268 12907 7628 16874 -125 -1160 155 C ATOM 2039 OE1 GLU A 268 7.448 -5.494 18.491 1.00103.67 O ANISOU 2039 OE1 GLU A 268 13767 8072 17551 -74 -1301 -116 O ATOM 2040 OE2 GLU A 268 6.898 -5.058 20.579 1.00100.56 O ANISOU 2040 OE2 GLU A 268 13054 7875 17281 -265 -1074 461 O ATOM 2041 N LEU A 269 11.006 -2.598 15.984 1.00 74.65 N ANISOU 2041 N LEU A 269 10273 5219 12871 796 -969 -781 N ATOM 2042 CA LEU A 269 12.118 -2.920 15.090 1.00 79.14 C ANISOU 2042 CA LEU A 269 11031 5745 13293 1128 -866 -1002 C ATOM 2043 C LEU A 269 13.333 -2.046 15.422 1.00 81.05 C ANISOU 2043 C LEU A 269 11068 6381 13347 1312 -615 -871 C ATOM 2044 O LEU A 269 14.448 -2.552 15.570 1.00 84.36 O ANISOU 2044 O LEU A 269 11477 6758 13816 1574 -486 -833 O ATOM 2045 CB LEU A 269 11.712 -2.709 13.627 1.00 75.14 C ANISOU 2045 CB LEU A 269 10784 5189 12578 1164 -969 -1355 C ATOM 2046 CG LEU A 269 12.124 -3.728 12.553 1.00 82.06 C ANISOU 2046 CG LEU A 269 12032 5724 13425 1428 -1018 -1666 C ATOM 2047 CD1 LEU A 269 12.397 -3.027 11.217 1.00 74.01 C ANISOU 2047 CD1 LEU A 269 11222 4880 12018 1609 -940 -1943 C ATOM 2048 CD2 LEU A 269 13.307 -4.614 12.975 1.00 82.17 C ANISOU 2048 CD2 LEU A 269 12053 5611 13557 1710 -842 -1573 C ATOM 2049 N LEU A 270 13.113 -0.740 15.548 1.00 73.97 N ANISOU 2049 N LEU A 270 9994 5849 12263 1173 -559 -799 N ATOM 2050 CA LEU A 270 14.203 0.170 15.886 1.00 70.87 C ANISOU 2050 CA LEU A 270 9385 5814 11729 1300 -356 -672 C ATOM 2051 C LEU A 270 14.862 -0.194 17.219 1.00 71.92 C ANISOU 2051 C LEU A 270 9328 5959 12040 1353 -325 -389 C ATOM 2052 O LEU A 270 16.085 -0.154 17.345 1.00 77.89 O ANISOU 2052 O LEU A 270 9967 6831 12798 1577 -193 -336 O ATOM 2053 CB LEU A 270 13.724 1.619 15.915 1.00 59.55 C ANISOU 2053 CB LEU A 270 7810 4723 10094 1108 -336 -627 C ATOM 2054 CG LEU A 270 14.844 2.639 16.128 1.00 57.91 C ANISOU 2054 CG LEU A 270 7388 4861 9755 1217 -146 -524 C ATOM 2055 CD1 LEU A 270 15.775 2.682 14.916 1.00 62.55 C ANISOU 2055 CD1 LEU A 270 8075 5484 10209 1478 39 -716 C ATOM 2056 CD2 LEU A 270 14.283 4.014 16.432 1.00 51.36 C ANISOU 2056 CD2 LEU A 270 6422 4324 8769 1000 -158 -438 C ATOM 2057 N TRP A 271 14.056 -0.563 18.207 1.00 69.81 N ANISOU 2057 N TRP A 271 9030 5567 11929 1159 -447 -199 N ATOM 2058 CA TRP A 271 14.593 -0.949 19.507 1.00 68.38 C ANISOU 2058 CA TRP A 271 8726 5376 11880 1219 -439 82 C ATOM 2059 C TRP A 271 15.483 -2.197 19.463 1.00 77.25 C ANISOU 2059 C TRP A 271 9945 6223 13183 1492 -424 69 C ATOM 2060 O TRP A 271 16.568 -2.209 20.048 1.00 84.46 O ANISOU 2060 O TRP A 271 10719 7247 14124 1684 -367 209 O ATOM 2061 CB TRP A 271 13.463 -1.142 20.507 1.00 64.89 C ANISOU 2061 CB TRP A 271 8275 4830 11550 970 -531 300 C ATOM 2062 CG TRP A 271 13.174 0.091 21.244 1.00 66.64 C ANISOU 2062 CG TRP A 271 8329 5393 11599 821 -498 458 C ATOM 2063 CD1 TRP A 271 12.084 0.902 21.100 1.00 70.93 C ANISOU 2063 CD1 TRP A 271 8838 6062 12051 589 -516 432 C ATOM 2064 CD2 TRP A 271 13.996 0.692 22.240 1.00 64.12 C ANISOU 2064 CD2 TRP A 271 7864 5326 11174 908 -461 655 C ATOM 2065 NE1 TRP A 271 12.176 1.968 21.961 1.00 70.90 N ANISOU 2065 NE1 TRP A 271 8695 6366 11878 536 -468 600 N ATOM 2066 CE2 TRP A 271 13.348 1.863 22.673 1.00 61.29 C ANISOU 2066 CE2 TRP A 271 7417 5227 10642 723 -449 731 C ATOM 2067 CE3 TRP A 271 15.221 0.349 22.820 1.00 65.56 C ANISOU 2067 CE3 TRP A 271 7982 5529 11400 1134 -461 771 C ATOM 2068 CZ2 TRP A 271 13.875 2.691 23.655 1.00 61.50 C ANISOU 2068 CZ2 TRP A 271 7332 5515 10520 750 -447 899 C ATOM 2069 CZ3 TRP A 271 15.747 1.170 23.790 1.00 64.83 C ANISOU 2069 CZ3 TRP A 271 7751 5706 11178 1151 -484 944 C ATOM 2070 CH2 TRP A 271 15.077 2.327 24.201 1.00 64.01 C ANISOU 2070 CH2 TRP A 271 7597 5842 10883 958 -482 999 C ATOM 2071 N LYS A 272 15.033 -3.245 18.781 1.00 77.44 N ANISOU 2071 N LYS A 272 10206 5874 13343 1515 -496 -101 N ATOM 2072 CA LYS A 272 15.842 -4.455 18.680 1.00 87.90 C ANISOU 2072 CA LYS A 272 11656 6901 14840 1794 -479 -133 C ATOM 2073 C LYS A 272 17.168 -4.166 17.981 1.00 85.25 C ANISOU 2073 C LYS A 272 11257 6746 14387 2116 -303 -268 C ATOM 2074 O LYS A 272 18.172 -4.821 18.246 1.00 85.04 O ANISOU 2074 O LYS A 272 11193 6626 14491 2388 -243 -197 O ATOM 2075 CB LYS A 272 15.087 -5.578 17.967 1.00 98.86 C ANISOU 2075 CB LYS A 272 13347 7829 16387 1756 -610 -335 C ATOM 2076 CG LYS A 272 14.086 -6.314 18.850 1.00104.77 C ANISOU 2076 CG LYS A 272 14134 8340 17333 1497 -740 -125 C ATOM 2077 CD LYS A 272 13.600 -7.586 18.173 1.00109.57 C ANISOU 2077 CD LYS A 272 15031 8586 18014 1466 -840 -307 C ATOM 2078 CE LYS A 272 13.062 -7.300 16.778 1.00111.23 C ANISOU 2078 CE LYS A 272 15410 8768 18085 1412 -924 -665 C ATOM 2079 NZ LYS A 272 12.937 -8.555 15.974 1.00117.66 N ANISOU 2079 NZ LYS A 272 16540 9242 18925 1480 -1003 -883 N ATOM 2080 N ASP A 273 17.171 -3.175 17.097 1.00 82.81 N ANISOU 2080 N ASP A 273 10923 6695 13845 2091 -207 -441 N ATOM 2081 CA ASP A 273 18.404 -2.756 16.449 1.00 88.73 C ANISOU 2081 CA ASP A 273 11573 7651 14490 2373 11 -528 C ATOM 2082 C ASP A 273 19.279 -1.971 17.426 1.00 86.25 C ANISOU 2082 C ASP A 273 10894 7672 14207 2390 72 -268 C ATOM 2083 O ASP A 273 20.492 -2.176 17.479 1.00 83.57 O ANISOU 2083 O ASP A 273 10398 7382 13971 2663 194 -214 O ATOM 2084 CB ASP A 273 18.108 -1.944 15.182 1.00 89.36 C ANISOU 2084 CB ASP A 273 11772 7882 14298 2344 109 -773 C ATOM 2085 CG ASP A 273 17.675 -2.821 14.011 1.00 92.85 C ANISOU 2085 CG ASP A 273 12609 7983 14686 2464 65 -1082 C ATOM 2086 OD1 ASP A 273 18.161 -3.968 13.902 1.00 91.02 O ANISOU 2086 OD1 ASP A 273 12527 7451 14607 2706 81 -1145 O ATOM 2087 OD2 ASP A 273 16.850 -2.358 13.195 1.00 93.49 O ANISOU 2087 OD2 ASP A 273 12870 8084 14567 2327 -5 -1271 O ATOM 2088 N ILE A 274 18.655 -1.088 18.205 1.00 77.65 N ANISOU 2088 N ILE A 274 9670 6795 13038 2108 -28 -112 N ATOM 2089 CA ILE A 274 19.352 -0.355 19.262 1.00 77.83 C ANISOU 2089 CA ILE A 274 9393 7099 13079 2093 -42 128 C ATOM 2090 C ILE A 274 19.968 -1.295 20.312 1.00 81.27 C ANISOU 2090 C ILE A 274 9771 7376 13731 2256 -138 337 C ATOM 2091 O ILE A 274 21.123 -1.125 20.713 1.00 86.31 O ANISOU 2091 O ILE A 274 10174 8161 14457 2438 -115 449 O ATOM 2092 CB ILE A 274 18.402 0.643 19.965 1.00 74.97 C ANISOU 2092 CB ILE A 274 8979 6935 12573 1772 -148 244 C ATOM 2093 CG1 ILE A 274 18.084 1.823 19.046 1.00 72.44 C ANISOU 2093 CG1 ILE A 274 8644 6844 12037 1648 -51 82 C ATOM 2094 CG2 ILE A 274 19.003 1.146 21.263 1.00 72.58 C ANISOU 2094 CG2 ILE A 274 8453 6834 12291 1766 -233 497 C ATOM 2095 CD1 ILE A 274 17.027 2.762 19.596 1.00 67.96 C ANISOU 2095 CD1 ILE A 274 8057 6434 11328 1351 -144 164 C ATOM 2096 N ILE A 275 19.197 -2.291 20.739 1.00 78.96 N ANISOU 2096 N ILE A 275 9687 6772 13543 2191 -253 398 N ATOM 2097 CA ILE A 275 19.618 -3.204 21.798 1.00 85.13 C ANISOU 2097 CA ILE A 275 10466 7372 14507 2328 -355 626 C ATOM 2098 C ILE A 275 20.572 -4.315 21.320 1.00 96.41 C ANISOU 2098 C ILE A 275 11948 8553 16132 2679 -291 546 C ATOM 2099 O ILE A 275 21.570 -4.603 21.981 1.00 99.12 O ANISOU 2099 O ILE A 275 12142 8942 16576 2889 -325 707 O ATOM 2100 CB ILE A 275 18.392 -3.846 22.503 1.00 91.28 C ANISOU 2100 CB ILE A 275 11447 7891 15345 2112 -472 767 C ATOM 2101 CG1 ILE A 275 17.486 -2.768 23.104 1.00 82.27 C ANISOU 2101 CG1 ILE A 275 10238 7000 14020 1807 -507 879 C ATOM 2102 CG2 ILE A 275 18.836 -4.827 23.582 1.00 95.47 C ANISOU 2102 CG2 ILE A 275 12017 8212 16045 2274 -562 1025 C ATOM 2103 CD1 ILE A 275 16.132 -3.287 23.601 1.00 80.54 C ANISOU 2103 CD1 ILE A 275 10185 6542 13875 1567 -562 1004 C ATOM 2104 N HIS A 276 20.274 -4.931 20.177 1.00 97.53 N ANISOU 2104 N HIS A 276 12317 8447 16292 2749 -213 289 N ATOM 2105 CA HIS A 276 21.018 -6.119 19.738 1.00 96.03 C ANISOU 2105 CA HIS A 276 12271 8025 16189 3053 -150 197 C ATOM 2106 C HIS A 276 22.138 -5.883 18.709 1.00100.19 C ANISOU 2106 C HIS A 276 12700 8706 16664 3354 71 15 C ATOM 2107 O HIS A 276 23.209 -6.478 18.825 1.00107.31 O ANISOU 2107 O HIS A 276 13529 9615 17630 3633 130 67 O ATOM 2108 CB HIS A 276 20.053 -7.218 19.280 1.00 92.23 C ANISOU 2108 CB HIS A 276 12169 7143 15732 2960 -227 52 C ATOM 2109 CG HIS A 276 19.111 -7.674 20.351 1.00 94.35 C ANISOU 2109 CG HIS A 276 12516 7247 16084 2699 -394 277 C ATOM 2110 ND1 HIS A 276 19.502 -8.502 21.386 1.00 96.16 N ANISOU 2110 ND1 HIS A 276 12763 7373 16402 2793 -454 520 N ATOM 2111 CD2 HIS A 276 17.797 -7.413 20.559 1.00 92.46 C ANISOU 2111 CD2 HIS A 276 12339 6941 15850 2356 -493 313 C ATOM 2112 CE1 HIS A 276 18.472 -8.732 22.177 1.00 99.02 C ANISOU 2112 CE1 HIS A 276 13208 7611 16805 2521 -555 700 C ATOM 2113 NE2 HIS A 276 17.422 -8.083 21.698 1.00 97.10 N ANISOU 2113 NE2 HIS A 276 12975 7393 16526 2248 -574 584 N ATOM 2114 N ASN A 277 21.902 -5.034 17.710 1.00 99.62 N ANISOU 2114 N ASN A 277 12627 8758 16466 3309 207 -186 N ATOM 2115 CA ASN A 277 22.974 -4.645 16.781 1.00101.38 C ANISOU 2115 CA ASN A 277 12728 9183 16610 3578 472 -312 C ATOM 2116 C ASN A 277 23.016 -3.140 16.450 1.00 93.49 C ANISOU 2116 C ASN A 277 11502 8564 15457 3428 599 -318 C ATOM 2117 O ASN A 277 22.675 -2.720 15.344 1.00 90.58 O ANISOU 2117 O ASN A 277 11305 8240 14870 3410 735 -532 O ATOM 2118 CB ASN A 277 22.979 -5.509 15.507 1.00105.98 C ANISOU 2118 CB ASN A 277 13682 9514 17071 3808 594 -606 C ATOM 2119 CG ASN A 277 21.613 -5.606 14.851 1.00108.82 C ANISOU 2119 CG ASN A 277 14404 9631 17309 3596 476 -831 C ATOM 2120 OD1 ASN A 277 20.713 -4.820 15.138 1.00114.81 O ANISOU 2120 OD1 ASN A 277 15104 10510 18007 3267 351 -789 O ATOM 2121 ND2 ASN A 277 21.458 -6.571 13.956 1.00109.32 N ANISOU 2121 ND2 ASN A 277 14865 9403 17271 3760 491 -1066 N ATOM 2122 N PRO A 278 23.465 -2.327 17.417 1.00 87.70 N ANISOU 2122 N PRO A 278 10412 8121 14790 3313 532 -79 N ATOM 2123 CA PRO A 278 23.512 -0.866 17.319 1.00 86.34 C ANISOU 2123 CA PRO A 278 10017 8323 14465 3117 601 -45 C ATOM 2124 C PRO A 278 24.352 -0.391 16.145 1.00 87.67 C ANISOU 2124 C PRO A 278 10087 8644 14581 3327 929 -170 C ATOM 2125 O PRO A 278 24.166 0.730 15.658 1.00 87.37 O ANISOU 2125 O PRO A 278 9994 8842 14361 3169 1034 -211 O ATOM 2126 CB PRO A 278 24.182 -0.457 18.636 1.00 86.09 C ANISOU 2126 CB PRO A 278 9630 8482 14600 3074 444 231 C ATOM 2127 CG PRO A 278 24.916 -1.664 19.092 1.00 87.12 C ANISOU 2127 CG PRO A 278 9732 8394 14976 3363 394 321 C ATOM 2128 CD PRO A 278 24.049 -2.803 18.682 1.00 90.04 C ANISOU 2128 CD PRO A 278 10513 8385 15314 3394 365 173 C ATOM 2129 N GLN A 279 25.259 -1.253 15.700 1.00 85.41 N ANISOU 2129 N GLN A 279 9797 8222 14433 3683 1099 -218 N ATOM 2130 CA GLN A 279 26.221 -0.937 14.654 1.00 91.51 C ANISOU 2130 CA GLN A 279 10475 9180 15117 3891 1424 -303 C ATOM 2131 C GLN A 279 25.556 -0.623 13.318 1.00 99.11 C ANISOU 2131 C GLN A 279 11777 10094 15787 3903 1627 -551 C ATOM 2132 O GLN A 279 26.070 0.182 12.537 1.00105.37 O ANISOU 2132 O GLN A 279 12465 11122 16449 3947 1895 -573 O ATOM 2133 CB GLN A 279 27.187 -2.108 14.495 1.00101.18 C ANISOU 2133 CB GLN A 279 11716 10286 16443 4214 1485 -332 C ATOM 2134 CG GLN A 279 27.492 -2.837 15.804 1.00105.76 C ANISOU 2134 CG GLN A 279 12155 10774 17255 4229 1209 -137 C ATOM 2135 CD GLN A 279 28.439 -2.065 16.717 1.00110.65 C ANISOU 2135 CD GLN A 279 12283 11706 18053 4153 1136 112 C ATOM 2136 OE1 GLN A 279 28.614 -0.850 16.580 1.00104.93 O ANISOU 2136 OE1 GLN A 279 11315 11252 17303 3993 1231 164 O ATOM 2137 NE2 GLN A 279 29.063 -2.779 17.654 1.00117.23 N ANISOU 2137 NE2 GLN A 279 12989 12489 19063 4264 945 260 N ATOM 2138 N ALA A 280 24.418 -1.263 13.062 1.00 98.60 N ANISOU 2138 N ALA A 280 12129 9720 15613 3847 1477 -732 N ATOM 2139 CA ALA A 280 23.628 -0.996 11.864 1.00 99.51 C ANISOU 2139 CA ALA A 280 12630 9792 15386 3804 1552 -988 C ATOM 2140 C ALA A 280 23.203 0.463 11.830 1.00 96.47 C ANISOU 2140 C ALA A 280 12106 9735 14814 3498 1554 -920 C ATOM 2141 O ALA A 280 23.167 1.089 10.771 1.00101.12 O ANISOU 2141 O ALA A 280 12843 10435 15142 3552 1766 -1045 O ATOM 2142 CB ALA A 280 22.405 -1.894 11.828 1.00101.00 C ANISOU 2142 CB ALA A 280 13232 9630 15514 3678 1252 -1164 C ATOM 2143 N LEU A 281 22.871 0.995 13.000 1.00 90.48 N ANISOU 2143 N LEU A 281 11093 9114 14171 3195 1318 -720 N ATOM 2144 CA LEU A 281 22.492 2.393 13.122 1.00 82.09 C ANISOU 2144 CA LEU A 281 9882 8346 12960 2905 1297 -639 C ATOM 2145 C LEU A 281 23.695 3.307 12.898 1.00 85.23 C ANISOU 2145 C LEU A 281 9929 9028 13425 3013 1590 -511 C ATOM 2146 O LEU A 281 23.580 4.332 12.227 1.00 90.21 O ANISOU 2146 O LEU A 281 10577 9843 13857 2925 1745 -541 O ATOM 2147 CB LEU A 281 21.853 2.648 14.485 1.00 78.12 C ANISOU 2147 CB LEU A 281 9233 7892 12557 2594 979 -463 C ATOM 2148 CG LEU A 281 20.557 1.866 14.679 1.00 77.49 C ANISOU 2148 CG LEU A 281 9465 7542 12436 2443 722 -558 C ATOM 2149 CD1 LEU A 281 19.958 2.144 16.035 1.00 79.28 C ANISOU 2149 CD1 LEU A 281 9549 7830 12745 2166 476 -353 C ATOM 2150 CD2 LEU A 281 19.573 2.236 13.585 1.00 78.51 C ANISOU 2150 CD2 LEU A 281 9900 7644 12285 2339 723 -782 C ATOM 2151 N SER A 282 24.844 2.927 13.454 1.00 85.69 N ANISOU 2151 N SER A 282 9662 9108 13789 3204 1659 -357 N ATOM 2152 CA SER A 282 26.095 3.662 13.255 1.00 86.52 C ANISOU 2152 CA SER A 282 9370 9451 14053 3324 1941 -218 C ATOM 2153 C SER A 282 27.268 2.939 13.912 1.00 91.61 C ANISOU 2153 C SER A 282 9712 10090 15006 3511 1902 -77 C ATOM 2154 O SER A 282 27.130 2.407 15.016 1.00 87.57 O ANISOU 2154 O SER A 282 9134 9475 14664 3462 1606 22 O ATOM 2155 CB SER A 282 26.001 5.084 13.813 1.00 79.47 C ANISOU 2155 CB SER A 282 8208 8833 13152 2991 1837 -66 C ATOM 2156 OG SER A 282 27.164 5.827 13.493 1.00 81.20 O ANISOU 2156 OG SER A 282 8052 9257 13542 3076 2118 63 O ATOM 2157 N PRO A 283 28.433 2.928 13.238 1.00100.95 N ANISOU 2157 N PRO A 283 10734 11402 16222 3698 2175 -61 N ATOM 2158 CA PRO A 283 29.645 2.299 13.779 1.00106.34 C ANISOU 2158 CA PRO A 283 11117 12115 17174 3861 2131 64 C ATOM 2159 C PRO A 283 30.123 3.019 15.032 1.00110.17 C ANISOU 2159 C PRO A 283 11172 12786 17903 3641 1873 296 C ATOM 2160 O PRO A 283 30.854 2.444 15.839 1.00116.60 O ANISOU 2160 O PRO A 283 11780 13586 18934 3731 1694 406 O ATOM 2161 CB PRO A 283 30.675 2.491 12.656 1.00105.00 C ANISOU 2161 CB PRO A 283 10842 12080 16974 4045 2527 42 C ATOM 2162 CG PRO A 283 29.876 2.708 11.423 1.00106.25 C ANISOU 2162 CG PRO A 283 11414 12181 16775 4073 2758 -156 C ATOM 2163 CD PRO A 283 28.650 3.455 11.879 1.00102.65 C ANISOU 2163 CD PRO A 283 11071 11724 16208 3781 2549 -160 C ATOM 2164 N GLN A 284 29.706 4.271 15.183 1.00106.25 N ANISOU 2164 N GLN A 284 10569 12453 17350 3361 1835 355 N ATOM 2165 CA GLN A 284 30.123 5.092 16.307 1.00106.11 C ANISOU 2165 CA GLN A 284 10188 12609 17521 3127 1566 544 C ATOM 2166 C GLN A 284 29.152 4.991 17.479 1.00101.00 C ANISOU 2166 C GLN A 284 9660 11866 16848 2961 1178 584 C ATOM 2167 O GLN A 284 29.294 5.699 18.474 1.00106.18 O ANISOU 2167 O GLN A 284 10106 12650 17589 2755 907 714 O ATOM 2168 CB GLN A 284 30.256 6.546 15.858 1.00110.01 C ANISOU 2168 CB GLN A 284 10510 13317 17971 2906 1722 590 C ATOM 2169 CG GLN A 284 30.972 6.696 14.526 1.00120.57 C ANISOU 2169 CG GLN A 284 11825 14725 19261 3060 2162 551 C ATOM 2170 CD GLN A 284 31.645 8.046 14.377 1.00127.22 C ANISOU 2170 CD GLN A 284 12352 15780 20205 2847 2270 685 C ATOM 2171 OE1 GLN A 284 31.152 9.062 14.875 1.00123.78 O ANISOU 2171 OE1 GLN A 284 11860 15426 19743 2564 2090 735 O ATOM 2172 NE2 GLN A 284 32.788 8.062 13.696 1.00133.22 N ANISOU 2172 NE2 GLN A 284 12909 16615 21096 2981 2563 748 N ATOM 2173 N PHE A 285 28.168 4.108 17.360 1.00 92.99 N ANISOU 2173 N PHE A 285 9010 10612 15711 3047 1143 469 N ATOM 2174 CA PHE A 285 27.181 3.927 18.415 1.00 87.39 C ANISOU 2174 CA PHE A 285 8445 9782 14978 2895 808 523 C ATOM 2175 C PHE A 285 27.396 2.596 19.115 1.00 93.63 C ANISOU 2175 C PHE A 285 9330 10372 15872 3069 625 577 C ATOM 2176 O PHE A 285 27.002 1.551 18.597 1.00 97.88 O ANISOU 2176 O PHE A 285 10161 10663 16367 3234 714 454 O ATOM 2177 CB PHE A 285 25.767 3.983 17.839 1.00 79.87 C ANISOU 2177 CB PHE A 285 7932 8740 13677 2714 829 346 C ATOM 2178 CG PHE A 285 24.685 3.810 18.865 1.00 76.26 C ANISOU 2178 CG PHE A 285 7679 8197 13100 2489 508 398 C ATOM 2179 CD1 PHE A 285 24.599 4.659 19.961 1.00 78.01 C ANISOU 2179 CD1 PHE A 285 7745 8590 13306 2270 273 550 C ATOM 2180 CD2 PHE A 285 23.739 2.813 18.725 1.00 71.41 C ANISOU 2180 CD2 PHE A 285 7423 7319 12392 2499 452 297 C ATOM 2181 CE1 PHE A 285 23.592 4.501 20.906 1.00 74.54 C ANISOU 2181 CE1 PHE A 285 7512 8075 12734 2093 31 614 C ATOM 2182 CE2 PHE A 285 22.732 2.645 19.665 1.00 68.91 C ANISOU 2182 CE2 PHE A 285 7268 6919 11994 2293 205 377 C ATOM 2183 CZ PHE A 285 22.660 3.487 20.756 1.00 72.22 C ANISOU 2183 CZ PHE A 285 7539 7528 12375 2103 18 543 C ATOM 2184 N THR A 286 28.007 2.640 20.297 1.00 99.08 N ANISOU 2184 N THR A 286 9805 11156 16684 3031 352 752 N ATOM 2185 CA THR A 286 28.315 1.427 21.058 1.00105.29 C ANISOU 2185 CA THR A 286 10672 11774 17561 3206 168 834 C ATOM 2186 C THR A 286 27.066 0.729 21.600 1.00100.49 C ANISOU 2186 C THR A 286 10424 10908 16849 3138 -1 848 C ATOM 2187 O THR A 286 26.976 -0.500 21.578 1.00105.12 O ANISOU 2187 O THR A 286 11228 11246 17468 3310 -2 823 O ATOM 2188 CB THR A 286 29.266 1.714 22.239 1.00108.85 C ANISOU 2188 CB THR A 286 10832 12394 18132 3181 -113 1016 C ATOM 2189 OG1 THR A 286 28.618 2.583 23.180 1.00108.75 O ANISOU 2189 OG1 THR A 286 10838 12479 18005 2918 -376 1108 O ATOM 2190 CG2 THR A 286 30.555 2.359 21.751 1.00108.90 C ANISOU 2190 CG2 THR A 286 10452 12627 18297 3224 36 1019 C ATOM 2191 N GLY A 287 26.116 1.516 22.096 1.00 89.82 N ANISOU 2191 N GLY A 287 9136 9609 15381 2882 -142 895 N ATOM 2192 CA GLY A 287 24.913 0.973 22.702 1.00 82.45 C ANISOU 2192 CA GLY A 287 8551 8487 14289 2741 -295 929 C ATOM 2193 C GLY A 287 24.156 2.019 23.500 1.00 76.97 C ANISOU 2193 C GLY A 287 7895 7976 13372 2432 -464 1009 C ATOM 2194 O GLY A 287 24.587 3.171 23.598 1.00 79.06 O ANISOU 2194 O GLY A 287 7932 8497 13611 2325 -496 1025 O ATOM 2195 N ILE A 288 23.034 1.619 24.089 1.00 68.48 N ANISOU 2195 N ILE A 288 7108 6756 12155 2292 -565 1068 N ATOM 2196 CA ILE A 288 22.151 2.570 24.758 1.00 62.24 C ANISOU 2196 CA ILE A 288 6401 6120 11129 2017 -671 1129 C ATOM 2197 C ILE A 288 22.803 3.295 25.946 1.00 61.55 C ANISOU 2197 C ILE A 288 6144 6232 11012 2009 -908 1299 C ATOM 2198 O ILE A 288 22.401 4.405 26.296 1.00 63.88 O ANISOU 2198 O ILE A 288 6437 6715 11119 1810 -972 1302 O ATOM 2199 CB ILE A 288 20.834 1.883 25.206 1.00 65.45 C ANISOU 2199 CB ILE A 288 7124 6310 11435 1893 -699 1195 C ATOM 2200 CG1 ILE A 288 19.714 2.907 25.413 1.00 64.81 C ANISOU 2200 CG1 ILE A 288 7134 6381 11111 1608 -697 1187 C ATOM 2201 CG2 ILE A 288 21.050 1.051 26.453 1.00 64.87 C ANISOU 2201 CG2 ILE A 288 7133 6094 11422 2023 -874 1435 C ATOM 2202 CD1 ILE A 288 18.468 2.293 25.992 1.00 68.38 C ANISOU 2202 CD1 ILE A 288 7834 6641 11507 1486 -709 1302 C ATOM 2203 N LEU A 289 23.813 2.671 26.548 1.00 59.98 N ANISOU 2203 N LEU A 289 5815 5978 10999 2239 -1058 1428 N ATOM 2204 CA LEU A 289 24.433 3.199 27.755 1.00 66.37 C ANISOU 2204 CA LEU A 289 6504 6933 11780 2260 -1354 1590 C ATOM 2205 C LEU A 289 25.084 4.559 27.509 1.00 75.97 C ANISOU 2205 C LEU A 289 7422 8421 13024 2145 -1394 1513 C ATOM 2206 O LEU A 289 24.885 5.493 28.295 1.00 79.41 O ANISOU 2206 O LEU A 289 7892 9003 13279 1993 -1588 1562 O ATOM 2207 CB LEU A 289 25.446 2.192 28.327 1.00 69.46 C ANISOU 2207 CB LEU A 289 6836 7231 12323 2520 -1495 1701 C ATOM 2208 CG LEU A 289 26.275 2.590 29.555 1.00 65.91 C ANISOU 2208 CG LEU A 289 6304 6948 11790 2552 -1816 1817 C ATOM 2209 CD1 LEU A 289 25.421 3.204 30.657 1.00 68.08 C ANISOU 2209 CD1 LEU A 289 6829 7272 11765 2403 -2013 1933 C ATOM 2210 CD2 LEU A 289 27.012 1.388 30.097 1.00 68.24 C ANISOU 2210 CD2 LEU A 289 6646 7119 12163 2803 -1917 1916 C ATOM 2211 N GLN A 290 25.840 4.679 26.418 1.00 75.38 N ANISOU 2211 N GLN A 290 7073 8397 13171 2222 -1196 1399 N ATOM 2212 CA GLN A 290 26.528 5.935 26.121 1.00 80.77 C ANISOU 2212 CA GLN A 290 7452 9317 13921 2101 -1196 1345 C ATOM 2213 C GLN A 290 25.518 7.053 25.891 1.00 77.35 C ANISOU 2213 C GLN A 290 7173 8996 13220 1817 -1126 1255 C ATOM 2214 O GLN A 290 25.783 8.218 26.172 1.00 79.93 O ANISOU 2214 O GLN A 290 7355 9493 13521 1663 -1251 1257 O ATOM 2215 CB GLN A 290 27.485 5.794 24.927 1.00 85.56 C ANISOU 2215 CB GLN A 290 7802 9964 14745 2223 -906 1243 C ATOM 2216 CG GLN A 290 26.829 5.759 23.544 1.00 84.86 C ANISOU 2216 CG GLN A 290 7809 9805 14629 2228 -543 1095 C ATOM 2217 CD GLN A 290 27.856 5.724 22.419 1.00 88.48 C ANISOU 2217 CD GLN A 290 8034 10327 15256 2370 -238 1016 C ATOM 2218 OE1 GLN A 290 28.790 4.927 22.450 1.00104.13 O ANISOU 2218 OE1 GLN A 290 9909 12268 17386 2574 -221 1047 O ATOM 2219 NE2 GLN A 290 27.694 6.596 21.428 1.00 82.92 N ANISOU 2219 NE2 GLN A 290 7270 9727 14508 2268 16 924 N ATOM 2220 N LEU A 291 24.345 6.679 25.399 1.00 74.60 N ANISOU 2220 N LEU A 291 7131 8538 12676 1743 -943 1170 N ATOM 2221 CA LEU A 291 23.282 7.629 25.155 1.00 64.79 C ANISOU 2221 CA LEU A 291 6059 7388 11172 1491 -868 1083 C ATOM 2222 C LEU A 291 22.645 8.060 26.480 1.00 66.55 C ANISOU 2222 C LEU A 291 6464 7653 11169 1368 -1115 1197 C ATOM 2223 O LEU A 291 22.321 9.237 26.670 1.00 59.97 O ANISOU 2223 O LEU A 291 5645 6966 10174 1187 -1168 1165 O ATOM 2224 CB LEU A 291 22.254 7.019 24.207 1.00 58.39 C ANISOU 2224 CB LEU A 291 5491 6431 10263 1466 -633 958 C ATOM 2225 CG LEU A 291 20.973 7.808 23.940 1.00 61.19 C ANISOU 2225 CG LEU A 291 6042 6845 10360 1227 -566 874 C ATOM 2226 CD1 LEU A 291 21.272 9.250 23.562 1.00 53.06 C ANISOU 2226 CD1 LEU A 291 4856 6034 9271 1090 -527 815 C ATOM 2227 CD2 LEU A 291 20.144 7.130 22.854 1.00 59.71 C ANISOU 2227 CD2 LEU A 291 6050 6499 10140 1230 -374 729 C ATOM 2228 N LEU A 292 22.494 7.108 27.400 1.00 63.67 N ANISOU 2228 N LEU A 292 6258 7149 10785 1486 -1254 1337 N ATOM 2229 CA LEU A 292 21.958 7.403 28.729 1.00 61.29 C ANISOU 2229 CA LEU A 292 6168 6876 10243 1425 -1466 1471 C ATOM 2230 C LEU A 292 22.930 8.224 29.581 1.00 62.21 C ANISOU 2230 C LEU A 292 6126 7145 10366 1445 -1775 1527 C ATOM 2231 O LEU A 292 22.509 8.954 30.486 1.00 60.07 O ANISOU 2231 O LEU A 292 6028 6954 9841 1354 -1941 1573 O ATOM 2232 CB LEU A 292 21.574 6.110 29.460 1.00 61.27 C ANISOU 2232 CB LEU A 292 6395 6664 10220 1563 -1506 1635 C ATOM 2233 CG LEU A 292 20.286 5.463 28.944 1.00 55.97 C ANISOU 2233 CG LEU A 292 5945 5825 9496 1471 -1264 1606 C ATOM 2234 CD1 LEU A 292 20.172 4.011 29.368 1.00 53.72 C ANISOU 2234 CD1 LEU A 292 5817 5279 9315 1627 -1269 1756 C ATOM 2235 CD2 LEU A 292 19.079 6.260 29.423 1.00 47.84 C ANISOU 2235 CD2 LEU A 292 5111 4882 8183 1271 -1226 1634 C ATOM 2236 N GLN A 293 24.223 8.104 29.290 1.00 57.25 N ANISOU 2236 N GLN A 293 5168 6546 10036 1572 -1858 1521 N ATOM 2237 CA GLN A 293 25.242 8.821 30.053 1.00 62.76 C ANISOU 2237 CA GLN A 293 5661 7367 10819 1587 -2200 1569 C ATOM 2238 C GLN A 293 25.536 10.200 29.482 1.00 66.14 C ANISOU 2238 C GLN A 293 5864 7959 11306 1386 -2170 1446 C ATOM 2239 O GLN A 293 26.464 10.875 29.929 1.00 71.28 O ANISOU 2239 O GLN A 293 6348 8710 12023 1334 -2387 1427 O ATOM 2240 CB GLN A 293 26.535 8.019 30.110 1.00 58.99 C ANISOU 2240 CB GLN A 293 4963 6862 10588 1782 -2265 1600 C ATOM 2241 CG GLN A 293 26.467 6.841 31.044 1.00 63.25 C ANISOU 2241 CG GLN A 293 5744 7262 11027 1977 -2402 1741 C ATOM 2242 CD GLN A 293 27.686 5.965 30.943 1.00 69.67 C ANISOU 2242 CD GLN A 293 6343 8041 12089 2185 -2418 1758 C ATOM 2243 OE1 GLN A 293 28.315 5.877 29.886 1.00 75.21 O ANISOU 2243 OE1 GLN A 293 6761 8764 13052 2221 -2201 1670 O ATOM 2244 NE2 GLN A 293 28.036 5.312 32.046 1.00 68.78 N ANISOU 2244 NE2 GLN A 293 6377 7878 11877 2341 -2661 1880 N ATOM 2245 N SER A 294 24.757 10.610 28.488 1.00 57.34 N ANISOU 2245 N SER A 294 4822 6870 10094 1237 -1851 1326 N ATOM 2246 CA SER A 294 24.964 11.905 27.862 1.00 58.78 C ANISOU 2246 CA SER A 294 4824 7186 10322 1048 -1780 1224 C ATOM 2247 C SER A 294 23.798 12.828 28.211 1.00 54.16 C ANISOU 2247 C SER A 294 4547 6651 9379 853 -1794 1172 C ATOM 2248 O SER A 294 22.639 12.491 27.977 1.00 55.48 O ANISOU 2248 O SER A 294 4981 6764 9335 822 -1602 1146 O ATOM 2249 CB SER A 294 25.107 11.750 26.347 1.00 57.53 C ANISOU 2249 CB SER A 294 4500 7026 10333 1062 -1394 1131 C ATOM 2250 OG SER A 294 23.874 11.376 25.769 1.00 68.52 O ANISOU 2250 OG SER A 294 6193 8347 11494 1024 -1152 1055 O ATOM 2251 N ARG A 295 24.113 13.984 28.786 1.00 55.75 N ANISOU 2251 N ARG A 295 4703 6942 9538 726 -2036 1156 N ATOM 2252 CA ARG A 295 23.097 14.939 29.220 1.00 59.62 C ANISOU 2252 CA ARG A 295 5491 7474 9689 571 -2072 1106 C ATOM 2253 C ARG A 295 22.249 15.436 28.061 1.00 57.75 C ANISOU 2253 C ARG A 295 5307 7266 9371 433 -1727 999 C ATOM 2254 O ARG A 295 22.673 15.419 26.902 1.00 58.23 O ANISOU 2254 O ARG A 295 5143 7341 9640 421 -1500 948 O ATOM 2255 CB ARG A 295 23.749 16.123 29.935 1.00 63.38 C ANISOU 2255 CB ARG A 295 5892 8013 10179 465 -2415 1082 C ATOM 2256 CG ARG A 295 25.104 16.512 29.369 1.00 78.39 C ANISOU 2256 CG ARG A 295 7334 9950 12501 419 -2480 1071 C ATOM 2257 CD ARG A 295 25.024 17.715 28.453 1.00 79.11 C ANISOU 2257 CD ARG A 295 7312 10093 12651 208 -2291 979 C ATOM 2258 NE ARG A 295 24.726 18.937 29.195 1.00 85.04 N ANISOU 2258 NE ARG A 295 8253 10854 13202 54 -2550 920 N ATOM 2259 CZ ARG A 295 24.520 20.124 28.631 1.00 85.98 C ANISOU 2259 CZ ARG A 295 8360 10995 13315 -139 -2445 843 C ATOM 2260 NH1 ARG A 295 24.592 20.253 27.313 1.00 72.22 N ANISOU 2260 NH1 ARG A 295 6424 9278 11739 -199 -2080 831 N ATOM 2261 NH2 ARG A 295 24.238 21.184 29.382 1.00 93.84 N ANISOU 2261 NH2 ARG A 295 9575 11972 14110 -254 -2694 778 N ATOM 2262 N THR A 296 21.034 15.861 28.373 1.00 51.06 N ANISOU 2262 N THR A 296 4766 6425 8208 352 -1678 974 N ATOM 2263 CA THR A 296 20.140 16.364 27.345 1.00 45.86 C ANISOU 2263 CA THR A 296 4178 5791 7455 232 -1396 877 C ATOM 2264 C THR A 296 20.395 17.841 27.165 1.00 46.45 C ANISOU 2264 C THR A 296 4184 5945 7520 72 -1457 805 C ATOM 2265 O THR A 296 20.487 18.585 28.139 1.00 54.42 O ANISOU 2265 O THR A 296 5294 6973 8411 26 -1712 811 O ATOM 2266 CB THR A 296 18.684 16.148 27.726 1.00 43.99 C ANISOU 2266 CB THR A 296 4258 5520 6934 223 -1304 896 C ATOM 2267 OG1 THR A 296 18.434 14.738 27.779 1.00 52.80 O ANISOU 2267 OG1 THR A 296 5425 6530 8107 349 -1226 971 O ATOM 2268 CG2 THR A 296 17.740 16.797 26.676 1.00 40.86 C ANISOU 2268 CG2 THR A 296 3921 5157 6448 99 -1065 790 C ATOM 2269 N SER A 297 20.530 18.273 25.923 1.00 45.75 N ANISOU 2269 N SER A 297 3949 5885 7549 -5 -1229 737 N ATOM 2270 CA SER A 297 20.799 19.679 25.679 1.00 51.38 C ANISOU 2270 CA SER A 297 4592 6647 8285 -167 -1263 688 C ATOM 2271 C SER A 297 19.518 20.481 25.942 1.00 48.56 C ANISOU 2271 C SER A 297 4548 6300 7603 -253 -1249 634 C ATOM 2272 O SER A 297 18.419 20.037 25.593 1.00 42.26 O ANISOU 2272 O SER A 297 3926 5491 6639 -219 -1068 615 O ATOM 2273 CB SER A 297 21.300 19.884 24.259 1.00 46.19 C ANISOU 2273 CB SER A 297 3714 6011 7825 -203 -982 661 C ATOM 2274 OG SER A 297 21.353 21.260 23.967 1.00 61.93 O ANISOU 2274 OG SER A 297 5689 8028 9812 -370 -976 629 O ATOM 2275 N ARG A 298 19.669 21.658 26.547 1.00 40.55 N ANISOU 2275 N ARG A 298 3725 5004 6678 94 538 604 N ATOM 2276 CA ARG A 298 18.526 22.435 27.001 1.00 45.02 C ANISOU 2276 CA ARG A 298 4442 5609 7053 14 447 720 C ATOM 2277 C ARG A 298 17.570 22.873 25.898 1.00 42.90 C ANISOU 2277 C ARG A 298 4350 5401 6548 -24 550 707 C ATOM 2278 O ARG A 298 16.372 22.987 26.134 1.00 43.03 O ANISOU 2278 O ARG A 298 4490 5429 6431 -49 451 767 O ATOM 2279 CB ARG A 298 18.986 23.650 27.793 1.00 41.39 C ANISOU 2279 CB ARG A 298 3912 5191 6622 -57 411 792 C ATOM 2280 CG ARG A 298 19.693 23.298 29.078 1.00 37.34 C ANISOU 2280 CG ARG A 298 3252 4651 6286 -18 239 818 C ATOM 2281 CD ARG A 298 20.174 24.556 29.764 1.00 36.26 C ANISOU 2281 CD ARG A 298 3042 4560 6176 -98 195 840 C ATOM 2282 NE ARG A 298 21.184 24.233 30.770 1.00 50.31 N ANISOU 2282 NE ARG A 298 4634 6338 8143 -52 39 827 N ATOM 2283 CZ ARG A 298 21.624 25.081 31.689 1.00 48.14 C ANISOU 2283 CZ ARG A 298 4279 6104 7908 -104 -83 822 C ATOM 2284 NH1 ARG A 298 21.150 26.324 31.738 1.00 42.14 N ANISOU 2284 NH1 ARG A 298 3615 5359 7036 -206 -51 824 N ATOM 2285 NH2 ARG A 298 22.532 24.672 32.563 1.00 44.77 N ANISOU 2285 NH2 ARG A 298 3678 5694 7639 -44 -255 805 N ATOM 2286 N LYS A 299 18.092 23.117 24.703 1.00 39.55 N ANISOU 2286 N LYS A 299 3931 5033 6065 -23 748 634 N ATOM 2287 CA LYS A 299 17.243 23.591 23.620 1.00 42.40 C ANISOU 2287 CA LYS A 299 4472 5473 6165 -46 829 640 C ATOM 2288 C LYS A 299 16.200 22.531 23.264 1.00 40.22 C ANISOU 2288 C LYS A 299 4304 5177 5802 3 726 553 C ATOM 2289 O LYS A 299 15.087 22.868 22.853 1.00 44.90 O ANISOU 2289 O LYS A 299 5038 5826 6197 -17 673 585 O ATOM 2290 CB LYS A 299 18.067 23.990 22.391 1.00 37.35 C ANISOU 2290 CB LYS A 299 3828 4920 5443 -51 1082 594 C ATOM 2291 CG LYS A 299 18.779 22.815 21.738 1.00 45.68 C ANISOU 2291 CG LYS A 299 4801 5979 6576 40 1192 407 C ATOM 2292 CD LYS A 299 19.667 23.276 20.602 1.00 55.18 C ANISOU 2292 CD LYS A 299 5979 7303 7685 30 1482 371 C ATOM 2293 CE LYS A 299 20.682 24.277 21.086 1.00 63.03 C ANISOU 2293 CE LYS A 299 6806 8292 8851 -62 1585 487 C ATOM 2294 NZ LYS A 299 22.043 23.872 20.657 1.00 79.79 N ANISOU 2294 NZ LYS A 299 8712 10462 11142 -24 1806 365 N ATOM 2295 N PHE A 300 16.535 21.257 23.452 1.00 40.09 N ANISOU 2295 N PHE A 300 4209 5066 5960 66 680 442 N ATOM 2296 CA PHE A 300 15.536 20.227 23.183 1.00 46.23 C ANISOU 2296 CA PHE A 300 5077 5784 6706 87 568 352 C ATOM 2297 C PHE A 300 14.414 20.230 24.216 1.00 46.11 C ANISOU 2297 C PHE A 300 5093 5727 6702 28 380 487 C ATOM 2298 O PHE A 300 13.240 20.141 23.844 1.00 41.37 O ANISOU 2298 O PHE A 300 4588 5157 5971 -4 307 468 O ATOM 2299 CB PHE A 300 16.172 18.851 23.026 1.00 40.80 C ANISOU 2299 CB PHE A 300 4311 4964 6228 175 575 188 C ATOM 2300 CG PHE A 300 17.218 18.810 21.968 1.00 44.73 C ANISOU 2300 CG PHE A 300 4764 5530 6702 246 788 26 C ATOM 2301 CD1 PHE A 300 16.864 18.855 20.626 1.00 51.93 C ANISOU 2301 CD1 PHE A 300 5809 6561 7362 261 899 -116 C ATOM 2302 CD2 PHE A 300 18.563 18.746 22.308 1.00 46.53 C ANISOU 2302 CD2 PHE A 300 4807 5728 7146 304 881 12 C ATOM 2303 CE1 PHE A 300 17.839 18.828 19.641 1.00 59.97 C ANISOU 2303 CE1 PHE A 300 6790 7676 8322 330 1131 -264 C ATOM 2304 CE2 PHE A 300 19.542 18.713 21.330 1.00 49.12 C ANISOU 2304 CE2 PHE A 300 5062 6140 7460 370 1113 -143 C ATOM 2305 CZ PHE A 300 19.185 18.757 19.997 1.00 55.23 C ANISOU 2305 CZ PHE A 300 5983 7042 7960 381 1255 -278 C ATOM 2306 N LEU A 301 14.771 20.363 25.495 1.00 40.68 N ANISOU 2306 N LEU A 301 4313 4990 6152 16 304 615 N ATOM 2307 CA LEU A 301 13.762 20.452 26.557 1.00 38.28 C ANISOU 2307 CA LEU A 301 4035 4683 5827 -37 162 754 C ATOM 2308 C LEU A 301 12.877 21.686 26.382 1.00 41.93 C ANISOU 2308 C LEU A 301 4580 5273 6078 -84 171 814 C ATOM 2309 O LEU A 301 11.679 21.632 26.648 1.00 42.87 O ANISOU 2309 O LEU A 301 4739 5417 6131 -119 86 859 O ATOM 2310 CB LEU A 301 14.410 20.454 27.949 1.00 37.47 C ANISOU 2310 CB LEU A 301 3836 4544 5857 -27 82 874 C ATOM 2311 CG LEU A 301 15.320 19.253 28.234 1.00 45.64 C ANISOU 2311 CG LEU A 301 4778 5437 7125 47 42 846 C ATOM 2312 CD1 LEU A 301 16.048 19.382 29.588 1.00 36.77 C ANISOU 2312 CD1 LEU A 301 3559 4313 6097 74 -64 974 C ATOM 2313 CD2 LEU A 301 14.525 17.944 28.153 1.00 41.61 C ANISOU 2313 CD2 LEU A 301 4321 4785 6705 41 -32 833 C ATOM 2314 N ALA A 302 13.462 22.790 25.920 1.00 38.68 N ANISOU 2314 N ALA A 302 4184 4930 5585 -83 278 820 N ATOM 2315 CA ALA A 302 12.710 24.036 25.772 1.00 35.94 C ANISOU 2315 CA ALA A 302 3921 4664 5069 -108 279 893 C ATOM 2316 C ALA A 302 11.771 24.021 24.566 1.00 36.17 C ANISOU 2316 C ALA A 302 4066 4759 4916 -92 283 843 C ATOM 2317 O ALA A 302 10.740 24.708 24.569 1.00 33.65 O ANISOU 2317 O ALA A 302 3806 4497 4481 -92 218 902 O ATOM 2318 CB ALA A 302 13.655 25.230 25.673 1.00 27.25 C ANISOU 2318 CB ALA A 302 2806 3574 3973 -128 389 937 C ATOM 2319 N CYS A 303 12.140 23.289 23.515 1.00 34.21 N ANISOU 2319 N CYS A 303 3848 4517 4636 -65 353 720 N ATOM 2320 CA CYS A 303 11.355 23.364 22.284 1.00 38.09 C ANISOU 2320 CA CYS A 303 4462 5102 4907 -41 345 658 C ATOM 2321 C CYS A 303 9.982 22.717 22.472 1.00 43.37 C ANISOU 2321 C CYS A 303 5130 5770 5576 -59 169 618 C ATOM 2322 O CYS A 303 9.092 22.911 21.661 1.00 44.46 O ANISOU 2322 O CYS A 303 5350 6003 5541 -40 102 582 O ATOM 2323 CB CYS A 303 12.088 22.721 21.100 1.00 33.98 C ANISOU 2323 CB CYS A 303 3982 4613 4316 0 470 500 C ATOM 2324 SG CYS A 303 11.963 20.917 21.048 1.00 49.38 S ANISOU 2324 SG CYS A 303 5881 6450 6431 20 383 285 S ATOM 2325 N ARG A 304 9.808 21.953 23.543 1.00 38.03 N ANISOU 2325 N ARG A 304 4356 4995 5099 -98 91 637 N ATOM 2326 CA ARG A 304 8.514 21.320 23.786 1.00 43.22 C ANISOU 2326 CA ARG A 304 4983 5643 5795 -144 -51 617 C ATOM 2327 C ARG A 304 7.623 22.134 24.728 1.00 40.34 C ANISOU 2327 C ARG A 304 4575 5342 5410 -166 -110 763 C ATOM 2328 O ARG A 304 6.611 21.640 25.223 1.00 38.18 O ANISOU 2328 O ARG A 304 4232 5067 5208 -220 -199 780 O ATOM 2329 CB ARG A 304 8.690 19.867 24.256 1.00 37.72 C ANISOU 2329 CB ARG A 304 4219 4786 5328 -184 -94 558 C ATOM 2330 CG ARG A 304 9.156 18.929 23.129 1.00 31.40 C ANISOU 2330 CG ARG A 304 3464 3920 4547 -149 -69 344 C ATOM 2331 CD ARG A 304 8.053 18.725 22.111 1.00 36.25 C ANISOU 2331 CD ARG A 304 4135 4612 5027 -169 -171 199 C ATOM 2332 NE ARG A 304 7.892 19.778 21.095 1.00 38.08 N ANISOU 2332 NE ARG A 304 4472 5036 4961 -111 -140 185 N ATOM 2333 CZ ARG A 304 6.746 20.413 20.833 1.00 38.42 C ANISOU 2333 CZ ARG A 304 4534 5207 4857 -117 -251 226 C ATOM 2334 NH1 ARG A 304 5.655 20.145 21.532 1.00 37.39 N ANISOU 2334 NH1 ARG A 304 4300 5052 4856 -189 -378 270 N ATOM 2335 NH2 ARG A 304 6.684 21.311 19.864 1.00 36.10 N ANISOU 2335 NH2 ARG A 304 4356 5069 4291 -47 -232 234 N ATOM 2336 N LEU A 305 8.006 23.385 24.964 1.00 39.13 N ANISOU 2336 N LEU A 305 4453 5240 5175 -129 -48 857 N ATOM 2337 CA LEU A 305 7.109 24.356 25.597 1.00 34.25 C ANISOU 2337 CA LEU A 305 3815 4694 4505 -116 -96 952 C ATOM 2338 C LEU A 305 6.851 25.459 24.584 1.00 38.16 C ANISOU 2338 C LEU A 305 4413 5260 4827 -49 -90 966 C ATOM 2339 O LEU A 305 7.765 25.899 23.887 1.00 36.19 O ANISOU 2339 O LEU A 305 4248 4995 4508 -29 6 972 O ATOM 2340 CB LEU A 305 7.710 24.956 26.874 1.00 35.52 C ANISOU 2340 CB LEU A 305 3935 4826 4735 -120 -55 1042 C ATOM 2341 CG LEU A 305 7.548 24.277 28.248 1.00 38.99 C ANISOU 2341 CG LEU A 305 4284 5251 5282 -164 -90 1097 C ATOM 2342 CD1 LEU A 305 8.267 22.914 28.306 1.00 36.86 C ANISOU 2342 CD1 LEU A 305 3983 4873 5149 -201 -91 1075 C ATOM 2343 CD2 LEU A 305 8.041 25.184 29.402 1.00 38.02 C ANISOU 2343 CD2 LEU A 305 4146 5148 5150 -144 -71 1158 C ATOM 2344 N THR A 306 5.602 25.908 24.484 1.00 37.30 N ANISOU 2344 N THR A 306 4290 5232 4652 -12 -188 984 N ATOM 2345 CA THR A 306 5.297 27.031 23.604 1.00 36.07 C ANISOU 2345 CA THR A 306 4240 5128 4336 74 -207 1034 C ATOM 2346 C THR A 306 5.885 28.302 24.240 1.00 35.58 C ANISOU 2346 C THR A 306 4213 4995 4309 102 -126 1140 C ATOM 2347 O THR A 306 6.180 28.322 25.447 1.00 36.99 O ANISOU 2347 O THR A 306 4312 5129 4612 67 -97 1147 O ATOM 2348 CB THR A 306 3.777 27.175 23.423 1.00 40.45 C ANISOU 2348 CB THR A 306 4736 5785 4849 128 -360 1020 C ATOM 2349 OG1 THR A 306 3.180 27.466 24.696 1.00 38.95 O ANISOU 2349 OG1 THR A 306 4419 5598 4783 128 -369 1056 O ATOM 2350 CG2 THR A 306 3.183 25.900 22.826 1.00 31.77 C ANISOU 2350 CG2 THR A 306 3581 4740 3749 75 -462 888 C ATOM 2351 N PRO A 307 6.017 29.376 23.453 1.00 40.14 N ANISOU 2351 N PRO A 307 4917 5559 4777 165 -101 1223 N ATOM 2352 CA PRO A 307 6.547 30.610 24.044 1.00 35.31 C ANISOU 2352 CA PRO A 307 4337 4837 4242 177 -34 1310 C ATOM 2353 C PRO A 307 5.736 31.031 25.268 1.00 35.05 C ANISOU 2353 C PRO A 307 4206 4802 4310 218 -107 1289 C ATOM 2354 O PRO A 307 6.331 31.377 26.302 1.00 37.21 O ANISOU 2354 O PRO A 307 4439 5005 4693 183 -59 1273 O ATOM 2355 CB PRO A 307 6.401 31.628 22.907 1.00 34.40 C ANISOU 2355 CB PRO A 307 4379 4704 3988 252 -32 1430 C ATOM 2356 CG PRO A 307 6.480 30.786 21.667 1.00 40.15 C ANISOU 2356 CG PRO A 307 5177 5544 4536 245 -26 1396 C ATOM 2357 CD PRO A 307 5.716 29.533 22.018 1.00 32.36 C ANISOU 2357 CD PRO A 307 4059 4647 3589 225 -137 1251 C ATOM 2358 N ASP A 308 4.408 30.939 25.181 1.00 31.75 N ANISOU 2358 N ASP A 308 3732 4479 3853 292 -222 1269 N ATOM 2359 CA ASP A 308 3.545 31.326 26.303 1.00 34.13 C ANISOU 2359 CA ASP A 308 3918 4810 4238 346 -264 1236 C ATOM 2360 C ASP A 308 3.722 30.435 27.520 1.00 38.11 C ANISOU 2360 C ASP A 308 4303 5356 4820 254 -221 1178 C ATOM 2361 O ASP A 308 3.695 30.929 28.643 1.00 37.63 O ANISOU 2361 O ASP A 308 4198 5293 4809 275 -193 1155 O ATOM 2362 CB ASP A 308 2.079 31.374 25.888 1.00 34.59 C ANISOU 2362 CB ASP A 308 3903 4980 4262 447 -391 1223 C ATOM 2363 CG ASP A 308 1.173 31.933 26.990 1.00 45.36 C ANISOU 2363 CG ASP A 308 5135 6386 5714 529 -404 1181 C ATOM 2364 OD1 ASP A 308 1.224 33.160 27.262 1.00 49.60 O ANISOU 2364 OD1 ASP A 308 5731 6826 6289 632 -394 1198 O ATOM 2365 OD2 ASP A 308 0.385 31.152 27.571 1.00 42.92 O ANISOU 2365 OD2 ASP A 308 4659 6202 5446 490 -415 1125 O ATOM 2366 N MET A 309 3.918 29.134 27.314 1.00 35.81 N ANISOU 2366 N MET A 309 3973 5100 4534 160 -219 1154 N ATOM 2367 CA MET A 309 4.181 28.264 28.452 1.00 34.86 C ANISOU 2367 CA MET A 309 3763 4994 4489 76 -182 1144 C ATOM 2368 C MET A 309 5.458 28.690 29.169 1.00 38.52 C ANISOU 2368 C MET A 309 4274 5375 4986 54 -116 1156 C ATOM 2369 O MET A 309 5.486 28.770 30.399 1.00 39.21 O ANISOU 2369 O MET A 309 4311 5498 5090 48 -103 1153 O ATOM 2370 CB MET A 309 4.303 26.804 28.019 1.00 36.40 C ANISOU 2370 CB MET A 309 3928 5180 4723 -16 -197 1121 C ATOM 2371 CG MET A 309 2.988 26.128 27.812 1.00 49.66 C ANISOU 2371 CG MET A 309 5500 6943 6425 -41 -273 1091 C ATOM 2372 SD MET A 309 3.242 24.674 26.811 1.00 41.42 S ANISOU 2372 SD MET A 309 4475 5837 5427 -128 -317 1013 S ATOM 2373 CE MET A 309 4.282 23.718 27.825 1.00118.79 C ANISOU 2373 CE MET A 309 14260 15524 15352 -211 -242 1062 C ATOM 2374 N GLU A 310 6.511 28.962 28.395 1.00 32.88 N ANISOU 2374 N GLU A 310 3648 4571 4274 40 -73 1164 N ATOM 2375 CA GLU A 310 7.808 29.329 28.966 1.00 38.97 C ANISOU 2375 CA GLU A 310 4430 5262 5115 3 -20 1162 C ATOM 2376 C GLU A 310 7.734 30.625 29.742 1.00 33.87 C ANISOU 2376 C GLU A 310 3801 4584 4486 48 -30 1144 C ATOM 2377 O GLU A 310 8.230 30.718 30.866 1.00 33.90 O ANISOU 2377 O GLU A 310 3763 4592 4527 27 -42 1105 O ATOM 2378 CB GLU A 310 8.852 29.510 27.863 1.00 42.66 C ANISOU 2378 CB GLU A 310 4967 5649 5592 -26 57 1178 C ATOM 2379 CG GLU A 310 9.612 28.282 27.536 1.00 43.22 C ANISOU 2379 CG GLU A 310 4998 5718 5706 -76 93 1148 C ATOM 2380 CD GLU A 310 10.876 28.592 26.761 1.00 42.62 C ANISOU 2380 CD GLU A 310 4950 5580 5664 -107 209 1151 C ATOM 2381 OE1 GLU A 310 10.792 28.693 25.521 1.00 39.28 O ANISOU 2381 OE1 GLU A 310 4613 5176 5135 -91 270 1167 O ATOM 2382 OE2 GLU A 310 11.941 28.737 27.395 1.00 44.21 O ANISOU 2382 OE2 GLU A 310 5079 5731 5989 -148 238 1138 O ATOM 2383 N THR A 311 7.122 31.623 29.114 1.00 30.47 N ANISOU 2383 N THR A 311 3439 4114 4025 121 -39 1166 N ATOM 2384 CA THR A 311 7.029 32.944 29.701 1.00 38.40 C ANISOU 2384 CA THR A 311 4475 5038 5076 180 -51 1132 C ATOM 2385 C THR A 311 6.360 32.873 31.072 1.00 38.79 C ANISOU 2385 C THR A 311 4438 5194 5105 221 -85 1048 C ATOM 2386 O THR A 311 6.826 33.497 32.036 1.00 35.11 O ANISOU 2386 O THR A 311 3972 4691 4676 223 -91 967 O ATOM 2387 CB THR A 311 6.242 33.864 28.798 1.00 40.43 C ANISOU 2387 CB THR A 311 4815 5237 5311 282 -76 1189 C ATOM 2388 OG1 THR A 311 6.960 34.002 27.572 1.00 40.31 O ANISOU 2388 OG1 THR A 311 4902 5137 5276 237 -22 1288 O ATOM 2389 CG2 THR A 311 6.026 35.260 29.459 1.00 28.40 C ANISOU 2389 CG2 THR A 311 3323 3592 3874 367 -98 1135 C ATOM 2390 N LYS A 312 5.313 32.063 31.164 1.00 34.10 N ANISOU 2390 N LYS A 312 3765 4744 4448 242 -103 1060 N ATOM 2391 CA LYS A 312 4.588 31.905 32.422 1.00 37.23 C ANISOU 2391 CA LYS A 312 4069 5278 4800 274 -97 1005 C ATOM 2392 C LYS A 312 5.378 31.163 33.489 1.00 36.95 C ANISOU 2392 C LYS A 312 4008 5299 4734 190 -83 1004 C ATOM 2393 O LYS A 312 5.459 31.635 34.614 1.00 43.21 O ANISOU 2393 O LYS A 312 4796 6147 5476 222 -81 929 O ATOM 2394 CB LYS A 312 3.211 31.284 32.175 1.00 30.38 C ANISOU 2394 CB LYS A 312 3095 4545 3904 301 -105 1031 C ATOM 2395 CG LYS A 312 2.272 32.313 31.578 1.00 32.22 C ANISOU 2395 CG LYS A 312 3326 4757 4159 440 -145 1003 C ATOM 2396 CD LYS A 312 1.043 31.727 30.905 1.00 36.13 C ANISOU 2396 CD LYS A 312 3708 5364 4655 462 -194 1029 C ATOM 2397 CE LYS A 312 0.208 32.893 30.385 1.00 41.03 C ANISOU 2397 CE LYS A 312 4328 5954 5307 635 -259 1005 C ATOM 2398 NZ LYS A 312 -0.918 32.479 29.537 1.00 46.20 N ANISOU 2398 NZ LYS A 312 4873 6711 5969 675 -352 1024 N ATOM 2399 N LEU A 313 5.952 30.012 33.143 1.00 32.57 N ANISOU 2399 N LEU A 313 3443 4730 4203 98 -85 1079 N ATOM 2400 CA LEU A 313 6.782 29.274 34.094 1.00 34.44 C ANISOU 2400 CA LEU A 313 3659 4999 4425 37 -97 1105 C ATOM 2401 C LEU A 313 8.011 30.081 34.541 1.00 37.42 C ANISOU 2401 C LEU A 313 4079 5302 4837 36 -131 1032 C ATOM 2402 O LEU A 313 8.349 30.086 35.718 1.00 42.37 O ANISOU 2402 O LEU A 313 4694 6007 5398 39 -169 999 O ATOM 2403 CB LEU A 313 7.251 27.937 33.526 1.00 35.74 C ANISOU 2403 CB LEU A 313 3807 5116 4658 -40 -103 1186 C ATOM 2404 CG LEU A 313 6.228 26.826 33.343 1.00 44.52 C ANISOU 2404 CG LEU A 313 4861 6283 5772 -80 -91 1254 C ATOM 2405 CD1 LEU A 313 6.951 25.520 33.063 1.00 47.44 C ANISOU 2405 CD1 LEU A 313 5226 6562 6237 -148 -110 1311 C ATOM 2406 CD2 LEU A 313 5.319 26.691 34.564 1.00 49.25 C ANISOU 2406 CD2 LEU A 313 5398 7034 6281 -79 -62 1298 C ATOM 2407 N LEU A 314 8.683 30.751 33.607 1.00 38.89 N ANISOU 2407 N LEU A 314 4309 5344 5122 23 -118 1009 N ATOM 2408 CA LEU A 314 9.835 31.581 33.977 1.00 34.71 C ANISOU 2408 CA LEU A 314 3791 4723 4673 -4 -147 931 C ATOM 2409 C LEU A 314 9.391 32.689 34.937 1.00 41.64 C ANISOU 2409 C LEU A 314 4696 5624 5503 61 -183 808 C ATOM 2410 O LEU A 314 10.115 33.020 35.875 1.00 38.99 O ANISOU 2410 O LEU A 314 4345 5299 5169 44 -249 711 O ATOM 2411 CB LEU A 314 10.531 32.160 32.733 1.00 32.12 C ANISOU 2411 CB LEU A 314 3503 4234 4469 -47 -89 955 C ATOM 2412 CG LEU A 314 11.235 31.076 31.885 1.00 40.82 C ANISOU 2412 CG LEU A 314 4568 5326 5614 -104 -41 1028 C ATOM 2413 CD1 LEU A 314 11.606 31.600 30.504 1.00 35.88 C ANISOU 2413 CD1 LEU A 314 4001 4593 5040 -132 57 1075 C ATOM 2414 CD2 LEU A 314 12.473 30.521 32.594 1.00 29.96 C ANISOU 2414 CD2 LEU A 314 3098 3959 4325 -154 -87 998 C ATOM 2415 N PHE A 315 8.191 33.241 34.717 1.00 36.66 N ANISOU 2415 N PHE A 315 4092 5007 4828 148 -152 793 N ATOM 2416 CA PHE A 315 7.706 34.309 35.572 1.00 30.19 C ANISOU 2416 CA PHE A 315 3294 4197 3978 237 -173 648 C ATOM 2417 C PHE A 315 7.431 33.739 36.964 1.00 34.97 C ANISOU 2417 C PHE A 315 3854 5021 4412 257 -188 597 C ATOM 2418 O PHE A 315 7.760 34.364 37.971 1.00 35.50 O ANISOU 2418 O PHE A 315 3942 5120 4427 286 -237 445 O ATOM 2419 CB PHE A 315 6.437 34.989 35.003 1.00 29.85 C ANISOU 2419 CB PHE A 315 3269 4124 3949 355 -140 645 C ATOM 2420 CG PHE A 315 5.929 36.128 35.852 1.00 29.00 C ANISOU 2420 CG PHE A 315 3178 4004 3838 474 -154 466 C ATOM 2421 CD1 PHE A 315 6.390 37.430 35.655 1.00 35.39 C ANISOU 2421 CD1 PHE A 315 4070 4576 4802 500 -189 372 C ATOM 2422 CD2 PHE A 315 5.005 35.903 36.860 1.00 29.79 C ANISOU 2422 CD2 PHE A 315 3210 4319 3790 557 -119 384 C ATOM 2423 CE1 PHE A 315 5.929 38.504 36.441 1.00 32.12 C ANISOU 2423 CE1 PHE A 315 3676 4116 4410 624 -209 168 C ATOM 2424 CE2 PHE A 315 4.524 36.978 37.659 1.00 33.11 C ANISOU 2424 CE2 PHE A 315 3644 4738 4199 690 -117 177 C ATOM 2425 CZ PHE A 315 4.990 38.274 37.443 1.00 39.61 C ANISOU 2425 CZ PHE A 315 4557 5302 5192 731 -173 55 C ATOM 2426 N MET A 316 6.821 32.556 37.010 1.00 31.98 N ANISOU 2426 N MET A 316 3420 4791 3939 236 -146 723 N ATOM 2427 CA MET A 316 6.509 31.910 38.281 1.00 35.26 C ANISOU 2427 CA MET A 316 3803 5424 4173 243 -134 735 C ATOM 2428 C MET A 316 7.768 31.628 39.095 1.00 44.07 C ANISOU 2428 C MET A 316 4944 6562 5238 192 -228 719 C ATOM 2429 O MET A 316 7.752 31.739 40.319 1.00 39.33 O ANISOU 2429 O MET A 316 4361 6124 4459 230 -255 648 O ATOM 2430 CB MET A 316 5.709 30.615 38.066 1.00 28.29 C ANISOU 2430 CB MET A 316 2851 4645 3252 195 -68 908 C ATOM 2431 CG MET A 316 4.261 30.853 37.573 1.00 31.20 C ANISOU 2431 CG MET A 316 3149 5065 3639 256 11 901 C ATOM 2432 SD MET A 316 3.357 29.296 37.328 1.00 48.46 S ANISOU 2432 SD MET A 316 5226 7352 5833 158 74 1086 S ATOM 2433 CE MET A 316 3.138 28.792 39.042 1.00 46.22 C ANISOU 2433 CE MET A 316 4921 7309 5332 142 153 1144 C ATOM 2434 N THR A 317 8.863 31.287 38.413 1.00 37.67 N ANISOU 2434 N THR A 317 4128 5606 4577 116 -282 776 N ATOM 2435 CA THR A 317 10.059 30.808 39.109 1.00 39.16 C ANISOU 2435 CA THR A 317 4304 5827 4749 75 -391 786 C ATOM 2436 C THR A 317 11.058 31.929 39.347 1.00 36.47 C ANISOU 2436 C THR A 317 3969 5389 4498 65 -486 603 C ATOM 2437 O THR A 317 12.159 31.676 39.806 1.00 36.86 O ANISOU 2437 O THR A 317 3979 5450 4577 30 -602 584 O ATOM 2438 CB THR A 317 10.785 29.663 38.357 1.00 40.06 C ANISOU 2438 CB THR A 317 4371 5850 4999 8 -401 936 C ATOM 2439 OG1 THR A 317 11.000 30.048 36.993 1.00 37.97 O ANISOU 2439 OG1 THR A 317 4101 5411 4913 -25 -339 922 O ATOM 2440 CG2 THR A 317 9.987 28.391 38.397 1.00 38.91 C ANISOU 2440 CG2 THR A 317 4216 5785 4781 -1 -347 1109 C ATOM 2441 N SER A 318 10.667 33.164 39.040 1.00 36.16 N ANISOU 2441 N SER A 318 3970 5244 4526 97 -450 468 N ATOM 2442 CA SER A 318 11.578 34.291 39.214 1.00 35.60 C ANISOU 2442 CA SER A 318 3903 5032 4590 65 -536 286 C ATOM 2443 C SER A 318 10.913 35.490 39.880 1.00 44.28 C ANISOU 2443 C SER A 318 5067 6132 5626 153 -547 74 C ATOM 2444 O SER A 318 11.589 36.267 40.534 1.00 42.19 O ANISOU 2444 O SER A 318 4809 5819 5402 136 -657 -125 O ATOM 2445 CB SER A 318 12.182 34.706 37.867 1.00 39.86 C ANISOU 2445 CB SER A 318 4427 5329 5388 -18 -479 343 C ATOM 2446 OG SER A 318 11.191 35.212 36.983 1.00 36.87 O ANISOU 2446 OG SER A 318 4114 4855 5042 34 -372 394 O ATOM 2447 N ARG A 319 9.598 35.662 39.708 1.00 36.10 N ANISOU 2447 N ARG A 319 4064 5142 4510 251 -441 92 N ATOM 2448 CA ARG A 319 8.954 36.883 40.214 1.00 40.02 C ANISOU 2448 CA ARG A 319 4612 5601 4992 361 -439 -130 C ATOM 2449 C ARG A 319 7.872 36.619 41.264 1.00 43.10 C ANISOU 2449 C ARG A 319 4997 6271 5106 480 -380 -197 C ATOM 2450 O ARG A 319 7.514 37.509 42.025 1.00 44.30 O ANISOU 2450 O ARG A 319 5187 6455 5191 582 -391 -434 O ATOM 2451 CB ARG A 319 8.346 37.731 39.074 1.00 36.73 C ANISOU 2451 CB ARG A 319 4230 4950 4778 410 -369 -101 C ATOM 2452 CG ARG A 319 9.326 38.206 37.981 1.00 41.38 C ANISOU 2452 CG ARG A 319 4842 5250 5631 295 -388 -24 C ATOM 2453 CD ARG A 319 10.337 39.253 38.453 1.00 42.85 C ANISOU 2453 CD ARG A 319 5050 5246 5984 230 -488 -231 C ATOM 2454 NE ARG A 319 9.708 40.368 39.170 1.00 65.45 N ANISOU 2454 NE ARG A 319 7973 8045 8850 356 -521 -480 N ATOM 2455 CZ ARG A 319 8.972 41.329 38.603 1.00 75.97 C ANISOU 2455 CZ ARG A 319 9370 9166 10329 457 -476 -500 C ATOM 2456 NH1 ARG A 319 8.738 41.320 37.292 1.00 83.79 N ANISOU 2456 NH1 ARG A 319 10387 10011 11440 443 -402 -262 N ATOM 2457 NH2 ARG A 319 8.448 42.298 39.353 1.00 67.05 N ANISOU 2457 NH2 ARG A 319 8285 7975 9214 589 -511 -763 N ATOM 2458 N VAL A 320 7.342 35.404 41.290 1.00 35.35 N ANISOU 2458 N VAL A 320 3968 5485 3978 463 -304 7 N ATOM 2459 CA VAL A 320 6.250 35.090 42.190 1.00 42.08 C ANISOU 2459 CA VAL A 320 4796 6612 4581 553 -204 -11 C ATOM 2460 C VAL A 320 6.769 34.728 43.580 1.00 41.24 C ANISOU 2460 C VAL A 320 4729 6741 4200 549 -269 -72 C ATOM 2461 O VAL A 320 7.582 33.820 43.735 1.00 46.14 O ANISOU 2461 O VAL A 320 5351 7404 4775 458 -349 81 O ATOM 2462 CB VAL A 320 5.393 33.964 41.612 1.00 41.92 C ANISOU 2462 CB VAL A 320 4695 6681 4550 515 -88 240 C ATOM 2463 CG1 VAL A 320 4.334 33.536 42.615 1.00 39.29 C ANISOU 2463 CG1 VAL A 320 4312 6651 3965 574 42 254 C ATOM 2464 CG2 VAL A 320 4.747 34.444 40.297 1.00 37.84 C ANISOU 2464 CG2 VAL A 320 4144 5974 4259 551 -48 266 C ATOM 2465 N ARG A 321 6.319 35.466 44.585 1.00 45.31 N ANISOU 2465 N ARG A 321 5281 7409 4526 664 -245 -308 N ATOM 2466 CA ARG A 321 6.701 35.199 45.972 1.00 51.28 C ANISOU 2466 CA ARG A 321 6096 8437 4951 684 -308 -385 C ATOM 2467 C ARG A 321 6.100 33.873 46.465 1.00 55.78 C ANISOU 2467 C ARG A 321 6639 9290 5264 656 -183 -106 C ATOM 2468 O ARG A 321 4.924 33.573 46.200 1.00 49.49 O ANISOU 2468 O ARG A 321 5767 8574 4464 681 6 1 O ATOM 2469 CB ARG A 321 6.229 36.351 46.862 1.00 46.19 C ANISOU 2469 CB ARG A 321 5502 7899 4151 833 -284 -738 C ATOM 2470 CG ARG A 321 7.309 36.926 47.766 1.00 65.67 C ANISOU 2470 CG ARG A 321 8059 10395 6499 836 -492 -1001 C ATOM 2471 CD ARG A 321 6.965 38.317 48.295 1.00 81.58 C ANISOU 2471 CD ARG A 321 10126 12372 8498 976 -498 -1419 C ATOM 2472 NE ARG A 321 5.898 38.291 49.292 1.00 95.14 N ANISOU 2472 NE ARG A 321 11860 14441 9848 1124 -327 -1528 N ATOM 2473 CZ ARG A 321 4.635 38.645 49.055 1.00101.47 C ANISOU 2473 CZ ARG A 321 12595 15264 10695 1248 -116 -1576 C ATOM 2474 NH1 ARG A 321 4.271 39.060 47.846 1.00103.14 N ANISOU 2474 NH1 ARG A 321 12738 15160 11293 1251 -80 -1514 N ATOM 2475 NH2 ARG A 321 3.735 38.583 50.030 1.00102.17 N ANISOU 2475 NH2 ARG A 321 12679 15708 10434 1377 61 -1681 N ATOM 2476 N PHE A 322 6.900 33.078 47.175 1.00 58.10 N ANISOU 2476 N PHE A 322 6986 9724 5365 601 -296 22 N ATOM 2477 CA PHE A 322 6.406 31.822 47.757 1.00 56.12 C ANISOU 2477 CA PHE A 322 6735 9723 4864 567 -185 315 C ATOM 2478 C PHE A 322 5.288 32.105 48.749 1.00 50.62 C ANISOU 2478 C PHE A 322 6052 9347 3836 670 6 218 C ATOM 2479 O PHE A 322 5.478 32.862 49.707 1.00 60.82 O ANISOU 2479 O PHE A 322 7426 10807 4875 771 -49 -45 O ATOM 2480 CB PHE A 322 7.529 31.054 48.467 1.00 57.73 C ANISOU 2480 CB PHE A 322 7016 10022 4897 526 -374 457 C ATOM 2481 CG PHE A 322 7.187 29.619 48.764 1.00 58.42 C ANISOU 2481 CG PHE A 322 7109 10248 4839 462 -283 839 C ATOM 2482 CD1 PHE A 322 6.187 28.967 48.050 1.00 61.15 C ANISOU 2482 CD1 PHE A 322 7364 10528 5341 394 -81 1045 C ATOM 2483 CD2 PHE A 322 7.854 28.922 49.752 1.00 64.16 C ANISOU 2483 CD2 PHE A 322 7930 11158 5289 469 -413 998 C ATOM 2484 CE1 PHE A 322 5.867 27.649 48.319 1.00 59.41 C ANISOU 2484 CE1 PHE A 322 7147 10394 5032 313 5 1397 C ATOM 2485 CE2 PHE A 322 7.533 27.598 50.026 1.00 67.91 C ANISOU 2485 CE2 PHE A 322 8425 11721 5655 407 -326 1382 C ATOM 2486 CZ PHE A 322 6.540 26.967 49.311 1.00 64.34 C ANISOU 2486 CZ PHE A 322 7882 11174 5391 320 -109 1579 C ATOM 2487 N GLY A 323 4.134 31.481 48.529 1.00 48.00 N ANISOU 2487 N GLY A 323 5626 9109 3503 642 233 415 N ATOM 2488 CA GLY A 323 2.945 31.765 49.316 1.00 53.30 C ANISOU 2488 CA GLY A 323 6258 10082 3913 737 467 325 C ATOM 2489 C GLY A 323 1.929 32.540 48.487 1.00 59.14 C ANISOU 2489 C GLY A 323 6858 10694 4919 811 597 160 C ATOM 2490 O GLY A 323 0.793 32.715 48.904 1.00 64.51 O ANISOU 2490 O GLY A 323 7443 11595 5472 889 818 100 O ATOM 2491 N GLN A 324 2.336 33.002 47.308 1.00 51.92 N ANISOU 2491 N GLN A 324 5923 9432 4371 793 461 99 N ATOM 2492 CA GLN A 324 1.467 33.834 46.479 1.00 53.54 C ANISOU 2492 CA GLN A 324 6019 9490 4834 887 535 -52 C ATOM 2493 C GLN A 324 1.143 33.172 45.145 1.00 49.70 C ANISOU 2493 C GLN A 324 5427 8806 4651 782 539 184 C ATOM 2494 O GLN A 324 0.608 33.817 44.243 1.00 54.38 O ANISOU 2494 O GLN A 324 5945 9229 5485 852 540 98 O ATOM 2495 CB GLN A 324 2.126 35.202 46.238 1.00 52.28 C ANISOU 2495 CB GLN A 324 5948 9083 4833 984 375 -363 C ATOM 2496 CG GLN A 324 2.422 36.000 47.508 1.00 53.44 C ANISOU 2496 CG GLN A 324 6200 9399 4707 1100 343 -678 C ATOM 2497 CD GLN A 324 1.149 36.403 48.231 1.00 79.04 C ANISOU 2497 CD GLN A 324 9363 12913 7756 1264 568 -850 C ATOM 2498 OE1 GLN A 324 0.165 36.807 47.599 1.00 83.77 O ANISOU 2498 OE1 GLN A 324 9831 13433 8565 1355 681 -892 O ATOM 2499 NE2 GLN A 324 1.154 36.287 49.559 1.00 89.20 N ANISOU 2499 NE2 GLN A 324 10720 14542 8631 1314 636 -951 N ATOM 2500 N GLN A 325 1.436 31.880 45.031 1.00 41.60 N ANISOU 2500 N GLN A 325 4399 7801 3607 626 533 478 N ATOM 2501 CA GLN A 325 1.431 31.226 43.726 1.00 42.15 C ANISOU 2501 CA GLN A 325 4405 7647 3962 518 485 662 C ATOM 2502 C GLN A 325 0.072 30.695 43.274 1.00 43.75 C ANISOU 2502 C GLN A 325 4426 7934 4264 487 642 780 C ATOM 2503 O GLN A 325 -0.062 30.242 42.138 1.00 43.37 O ANISOU 2503 O GLN A 325 4319 7712 4448 412 590 886 O ATOM 2504 CB GLN A 325 2.448 30.071 43.695 1.00 40.36 C ANISOU 2504 CB GLN A 325 4256 7347 3733 373 382 894 C ATOM 2505 CG GLN A 325 2.065 28.853 44.566 1.00 42.49 C ANISOU 2505 CG GLN A 325 4505 7838 3801 283 500 1145 C ATOM 2506 CD GLN A 325 2.606 28.944 45.987 1.00 52.01 C ANISOU 2506 CD GLN A 325 5833 9272 4656 332 481 1120 C ATOM 2507 OE1 GLN A 325 2.932 30.030 46.473 1.00 58.78 O ANISOU 2507 OE1 GLN A 325 6757 10183 5392 450 421 855 O ATOM 2508 NE2 GLN A 325 2.719 27.796 46.656 1.00 49.66 N ANISOU 2508 NE2 GLN A 325 5575 9100 4194 243 516 1397 N ATOM 2509 N LYS A 326 -0.923 30.715 44.153 1.00 40.45 N ANISOU 2509 N LYS A 326 3908 7794 3667 537 834 754 N ATOM 2510 CA LYS A 326 -2.183 30.040 43.847 1.00 45.84 C ANISOU 2510 CA LYS A 326 4379 8583 4453 470 993 892 C ATOM 2511 C LYS A 326 -2.894 30.505 42.572 1.00 45.84 C ANISOU 2511 C LYS A 326 4240 8422 4756 528 940 805 C ATOM 2512 O LYS A 326 -3.250 29.675 41.732 1.00 48.85 O ANISOU 2512 O LYS A 326 4520 8716 5323 404 915 962 O ATOM 2513 CB LYS A 326 -3.154 30.071 45.032 1.00 52.07 C ANISOU 2513 CB LYS A 326 5057 9729 5000 521 1245 866 C ATOM 2514 CG LYS A 326 -4.493 29.426 44.691 1.00 51.75 C ANISOU 2514 CG LYS A 326 4749 9797 5114 437 1419 996 C ATOM 2515 CD LYS A 326 -5.371 29.209 45.930 1.00 61.36 C ANISOU 2515 CD LYS A 326 5846 11394 6075 437 1715 1040 C ATOM 2516 CE LYS A 326 -6.858 29.290 45.574 1.00 68.42 C ANISOU 2516 CE LYS A 326 6411 12416 7168 460 1890 992 C ATOM 2517 NZ LYS A 326 -7.209 28.404 44.427 1.00 73.47 N ANISOU 2517 NZ LYS A 326 6907 12862 8147 283 1799 1172 N ATOM 2518 N ARG A 327 -3.098 31.809 42.405 1.00 47.46 N ANISOU 2518 N ARG A 327 4444 8574 5014 719 905 556 N ATOM 2519 CA ARG A 327 -3.850 32.261 41.232 1.00 44.27 C ANISOU 2519 CA ARG A 327 3908 8036 4876 799 842 501 C ATOM 2520 C ARG A 327 -3.047 31.982 39.967 1.00 42.49 C ANISOU 2520 C ARG A 327 3796 7522 4826 707 643 608 C ATOM 2521 O ARG A 327 -3.613 31.557 38.948 1.00 41.73 O ANISOU 2521 O ARG A 327 3587 7363 4904 661 591 692 O ATOM 2522 CB ARG A 327 -4.262 33.736 41.329 1.00 41.30 C ANISOU 2522 CB ARG A 327 3515 7633 4545 1046 840 228 C ATOM 2523 CG ARG A 327 -5.067 34.093 42.577 1.00 44.59 C ANISOU 2523 CG ARG A 327 3812 8352 4777 1169 1057 70 C ATOM 2524 CD ARG A 327 -5.572 35.516 42.485 1.00 53.11 C ANISOU 2524 CD ARG A 327 4851 9355 5975 1434 1039 -213 C ATOM 2525 NE ARG A 327 -6.206 36.027 43.700 1.00 49.66 N ANISOU 2525 NE ARG A 327 4326 9191 5351 1591 1245 -434 N ATOM 2526 CZ ARG A 327 -7.513 35.982 43.935 1.00 53.67 C ANISOU 2526 CZ ARG A 327 4558 9942 5893 1684 1438 -482 C ATOM 2527 NH1 ARG A 327 -8.332 35.412 43.057 1.00 61.61 N ANISOU 2527 NH1 ARG A 327 5338 10949 7122 1620 1428 -320 N ATOM 2528 NH2 ARG A 327 -8.004 36.496 45.053 1.00 56.05 N ANISOU 2528 NH2 ARG A 327 4795 10500 6002 1840 1642 -709 N ATOM 2529 N TYR A 328 -1.734 32.178 40.039 1.00 40.06 N ANISOU 2529 N TYR A 328 3698 7060 4464 676 536 596 N ATOM 2530 CA TYR A 328 -0.876 31.903 38.880 1.00 45.89 C ANISOU 2530 CA TYR A 328 4541 7547 5348 588 382 693 C ATOM 2531 C TYR A 328 -1.001 30.450 38.461 1.00 43.29 C ANISOU 2531 C TYR A 328 4145 7237 5066 412 390 901 C ATOM 2532 O TYR A 328 -1.200 30.153 37.280 1.00 42.63 O ANISOU 2532 O TYR A 328 4027 7034 5137 374 311 952 O ATOM 2533 CB TYR A 328 0.593 32.242 39.169 1.00 36.51 C ANISOU 2533 CB TYR A 328 3546 6222 4104 563 288 650 C ATOM 2534 CG TYR A 328 0.820 33.702 39.483 1.00 39.80 C ANISOU 2534 CG TYR A 328 4042 6556 4525 713 253 425 C ATOM 2535 CD1 TYR A 328 0.884 34.645 38.462 1.00 37.01 C ANISOU 2535 CD1 TYR A 328 3735 5967 4360 792 168 365 C ATOM 2536 CD2 TYR A 328 0.971 34.141 40.800 1.00 36.39 C ANISOU 2536 CD2 TYR A 328 3649 6271 3906 777 300 270 C ATOM 2537 CE1 TYR A 328 1.092 35.989 38.739 1.00 39.62 C ANISOU 2537 CE1 TYR A 328 4144 6169 4740 922 131 164 C ATOM 2538 CE2 TYR A 328 1.182 35.485 41.091 1.00 39.76 C ANISOU 2538 CE2 TYR A 328 4151 6592 4365 912 254 25 C ATOM 2539 CZ TYR A 328 1.243 36.403 40.048 1.00 43.82 C ANISOU 2539 CZ TYR A 328 4705 6828 5118 979 170 -23 C ATOM 2540 OH TYR A 328 1.453 37.739 40.315 1.00 41.74 O ANISOU 2540 OH TYR A 328 4522 6406 4932 1104 121 -258 O ATOM 2541 N GLN A 329 -0.892 29.555 39.437 1.00 44.80 N ANISOU 2541 N GLN A 329 4329 7575 5120 308 480 1019 N ATOM 2542 CA GLN A 329 -1.100 28.130 39.199 1.00 45.75 C ANISOU 2542 CA GLN A 329 4379 7694 5309 135 505 1223 C ATOM 2543 C GLN A 329 -2.475 27.867 38.598 1.00 42.21 C ANISOU 2543 C GLN A 329 3715 7314 5010 111 559 1232 C ATOM 2544 O GLN A 329 -2.575 27.156 37.602 1.00 45.82 O ANISOU 2544 O GLN A 329 4133 7646 5633 14 475 1297 O ATOM 2545 CB GLN A 329 -0.920 27.330 40.491 1.00 41.99 C ANISOU 2545 CB GLN A 329 3930 7379 4646 47 613 1375 C ATOM 2546 CG GLN A 329 0.551 27.140 40.899 1.00 46.90 C ANISOU 2546 CG GLN A 329 4747 7905 5169 29 502 1423 C ATOM 2547 CD GLN A 329 0.699 26.459 42.253 1.00 54.34 C ANISOU 2547 CD GLN A 329 5735 9033 5878 -24 588 1585 C ATOM 2548 OE1 GLN A 329 -0.281 26.267 42.979 1.00 57.36 O ANISOU 2548 OE1 GLN A 329 6018 9638 6138 -43 764 1650 O ATOM 2549 NE2 GLN A 329 1.927 26.105 42.602 1.00 63.94 N ANISOU 2549 NE2 GLN A 329 7095 10173 7025 -43 467 1659 N ATOM 2550 N ASP A 330 -3.523 28.447 39.188 1.00 36.86 N ANISOU 2550 N ASP A 330 2884 6841 4279 208 690 1143 N ATOM 2551 CA ASP A 330 -4.882 28.270 38.654 1.00 40.47 C ANISOU 2551 CA ASP A 330 3087 7387 4903 198 733 1132 C ATOM 2552 C ASP A 330 -4.985 28.740 37.216 1.00 46.16 C ANISOU 2552 C ASP A 330 3805 7932 5803 275 544 1045 C ATOM 2553 O ASP A 330 -5.561 28.049 36.375 1.00 45.56 O ANISOU 2553 O ASP A 330 3599 7825 5887 180 476 1094 O ATOM 2554 CB ASP A 330 -5.943 28.969 39.521 1.00 50.22 C ANISOU 2554 CB ASP A 330 4139 8881 6063 329 915 1017 C ATOM 2555 CG ASP A 330 -6.034 28.380 40.929 1.00 57.80 C ANISOU 2555 CG ASP A 330 5080 10074 6808 236 1138 1133 C ATOM 2556 OD1 ASP A 330 -5.455 27.289 41.164 1.00 56.38 O ANISOU 2556 OD1 ASP A 330 4995 9843 6584 53 1142 1342 O ATOM 2557 OD2 ASP A 330 -6.680 29.015 41.800 1.00 60.42 O ANISOU 2557 OD2 ASP A 330 5309 10641 7007 360 1313 1017 O ATOM 2558 N TRP A 331 -4.396 29.896 36.917 1.00 45.47 N ANISOU 2558 N TRP A 331 3871 7720 5685 438 448 921 N ATOM 2559 CA TRP A 331 -4.469 30.420 35.557 1.00 41.62 C ANISOU 2559 CA TRP A 331 3411 7071 5331 525 275 873 C ATOM 2560 C TRP A 331 -3.721 29.512 34.588 1.00 39.88 C ANISOU 2560 C TRP A 331 3305 6690 5159 373 157 980 C ATOM 2561 O TRP A 331 -4.207 29.222 33.498 1.00 42.97 O ANISOU 2561 O TRP A 331 3628 7044 5655 357 44 986 O ATOM 2562 CB TRP A 331 -3.911 31.839 35.470 1.00 43.82 C ANISOU 2562 CB TRP A 331 3852 7213 5583 710 213 753 C ATOM 2563 CG TRP A 331 -4.622 32.840 36.333 1.00 42.26 C ANISOU 2563 CG TRP A 331 3557 7138 5360 895 311 597 C ATOM 2564 CD1 TRP A 331 -5.906 32.779 36.783 1.00 38.03 C ANISOU 2564 CD1 TRP A 331 2767 6824 4860 957 425 545 C ATOM 2565 CD2 TRP A 331 -4.061 34.051 36.861 1.00 36.15 C ANISOU 2565 CD2 TRP A 331 2931 6267 4537 1042 313 450 C ATOM 2566 NE1 TRP A 331 -6.181 33.890 37.557 1.00 43.41 N ANISOU 2566 NE1 TRP A 331 3433 7560 5499 1158 506 363 N ATOM 2567 CE2 TRP A 331 -5.061 34.681 37.617 1.00 38.68 C ANISOU 2567 CE2 TRP A 331 3090 6755 4852 1210 427 295 C ATOM 2568 CE3 TRP A 331 -2.799 34.659 36.756 1.00 45.29 C ANISOU 2568 CE3 TRP A 331 4327 7205 5676 1039 229 422 C ATOM 2569 CZ2 TRP A 331 -4.852 35.897 38.263 1.00 41.24 C ANISOU 2569 CZ2 TRP A 331 3506 7018 5148 1388 449 93 C ATOM 2570 CZ3 TRP A 331 -2.583 35.859 37.406 1.00 40.94 C ANISOU 2570 CZ3 TRP A 331 3858 6585 5114 1190 242 235 C ATOM 2571 CH2 TRP A 331 -3.609 36.470 38.149 1.00 40.66 C ANISOU 2571 CH2 TRP A 331 3678 6702 5067 1369 345 63 C ATOM 2572 N PHE A 332 -2.550 29.039 34.991 1.00 43.44 N ANISOU 2572 N PHE A 332 3920 7056 5530 272 177 1050 N ATOM 2573 CA PHE A 332 -1.794 28.140 34.135 1.00 42.16 C ANISOU 2573 CA PHE A 332 3855 6742 5422 145 87 1129 C ATOM 2574 C PHE A 332 -2.541 26.816 33.920 1.00 48.35 C ANISOU 2574 C PHE A 332 4484 7574 6313 -12 96 1207 C ATOM 2575 O PHE A 332 -2.663 26.326 32.785 1.00 42.79 O ANISOU 2575 O PHE A 332 3770 6784 5704 -61 -17 1192 O ATOM 2576 CB PHE A 332 -0.422 27.863 34.731 1.00 37.10 C ANISOU 2576 CB PHE A 332 3381 6015 4702 85 106 1185 C ATOM 2577 CG PHE A 332 0.499 27.162 33.788 1.00 35.74 C ANISOU 2577 CG PHE A 332 3313 5669 4596 1 20 1228 C ATOM 2578 CD1 PHE A 332 0.441 25.788 33.628 1.00 32.93 C ANISOU 2578 CD1 PHE A 332 2912 5278 4322 -140 16 1314 C ATOM 2579 CD2 PHE A 332 1.418 27.871 33.060 1.00 34.76 C ANISOU 2579 CD2 PHE A 332 3330 5410 4467 63 -42 1178 C ATOM 2580 CE1 PHE A 332 1.292 25.136 32.745 1.00 36.67 C ANISOU 2580 CE1 PHE A 332 3479 5591 4862 -195 -55 1317 C ATOM 2581 CE2 PHE A 332 2.281 27.225 32.183 1.00 38.75 C ANISOU 2581 CE2 PHE A 332 3920 5784 5021 -4 -91 1202 C ATOM 2582 CZ PHE A 332 2.215 25.857 32.030 1.00 33.99 C ANISOU 2582 CZ PHE A 332 3269 5154 4490 -121 -99 1256 C ATOM 2583 N GLN A 333 -3.005 26.238 35.024 1.00 45.15 N ANISOU 2583 N GLN A 333 3967 7304 5885 -98 233 1289 N ATOM 2584 CA GLN A 333 -3.749 24.990 35.005 1.00 54.41 C ANISOU 2584 CA GLN A 333 4977 8508 7190 -276 270 1385 C ATOM 2585 C GLN A 333 -4.962 25.079 34.086 1.00 51.16 C ANISOU 2585 C GLN A 333 4358 8153 6929 -261 190 1291 C ATOM 2586 O GLN A 333 -5.165 24.209 33.237 1.00 47.23 O ANISOU 2586 O GLN A 333 3810 7561 6574 -382 87 1289 O ATOM 2587 CB GLN A 333 -4.203 24.643 36.421 1.00 61.97 C ANISOU 2587 CB GLN A 333 5834 9644 8069 -346 469 1503 C ATOM 2588 CG GLN A 333 -4.983 23.359 36.512 1.00 77.91 C ANISOU 2588 CG GLN A 333 7675 11677 10250 -558 538 1635 C ATOM 2589 CD GLN A 333 -4.659 22.567 37.765 1.00 90.19 C ANISOU 2589 CD GLN A 333 9284 13276 11707 -682 695 1852 C ATOM 2590 OE1 GLN A 333 -3.938 23.037 38.655 1.00 83.53 O ANISOU 2590 OE1 GLN A 333 8596 12504 10638 -591 751 1884 O ATOM 2591 NE2 GLN A 333 -5.193 21.350 37.840 1.00 96.52 N ANISOU 2591 NE2 GLN A 333 9963 14030 12680 -895 757 2008 N ATOM 2592 N ARG A 334 -5.749 26.140 34.253 1.00 44.26 N ANISOU 2592 N ARG A 334 3361 7428 6028 -100 220 1194 N ATOM 2593 CA ARG A 334 -6.949 26.357 33.437 1.00 51.50 C ANISOU 2593 CA ARG A 334 4053 8424 7089 -47 121 1098 C ATOM 2594 C ARG A 334 -6.631 26.336 31.945 1.00 52.24 C ANISOU 2594 C ARG A 334 4260 8366 7223 -20 -110 1039 C ATOM 2595 O ARG A 334 -7.355 25.754 31.149 1.00 54.46 O ANISOU 2595 O ARG A 334 4390 8665 7638 -95 -231 996 O ATOM 2596 CB ARG A 334 -7.622 27.680 33.823 1.00 55.53 C ANISOU 2596 CB ARG A 334 4458 9079 7561 181 171 991 C ATOM 2597 CG ARG A 334 -8.690 28.194 32.843 1.00 67.67 C ANISOU 2597 CG ARG A 334 5800 10673 9237 313 11 884 C ATOM 2598 CD ARG A 334 -9.317 29.514 33.327 1.00 71.40 C ANISOU 2598 CD ARG A 334 6168 11263 9700 568 70 774 C ATOM 2599 NE ARG A 334 -10.153 30.158 32.309 1.00 84.73 N ANISOU 2599 NE ARG A 334 7719 12965 11511 745 -129 687 N ATOM 2600 CZ ARG A 334 -11.476 30.019 32.213 1.00 95.78 C ANISOU 2600 CZ ARG A 334 8764 14546 13082 772 -148 626 C ATOM 2601 NH1 ARG A 334 -12.134 29.245 33.069 1.00100.46 N ANISOU 2601 NH1 ARG A 334 9098 15320 13754 608 52 650 N ATOM 2602 NH2 ARG A 334 -12.147 30.654 31.256 1.00 95.99 N ANISOU 2602 NH2 ARG A 334 8686 14578 13207 961 -369 554 N ATOM 2603 N GLN A 335 -5.518 26.937 31.568 1.00 50.12 N ANISOU 2603 N GLN A 335 4257 7956 6831 74 -168 1032 N ATOM 2604 CA GLN A 335 -5.202 27.054 30.151 1.00 44.53 C ANISOU 2604 CA GLN A 335 3674 7136 6109 121 -358 986 C ATOM 2605 C GLN A 335 -4.520 25.811 29.582 1.00 44.80 C ANISOU 2605 C GLN A 335 3807 7043 6172 -55 -407 1008 C ATOM 2606 O GLN A 335 -4.730 25.466 28.430 1.00 45.90 O ANISOU 2606 O GLN A 335 3951 7154 6334 -70 -562 940 O ATOM 2607 CB GLN A 335 -4.319 28.285 29.940 1.00 43.40 C ANISOU 2607 CB GLN A 335 3760 6890 5838 288 -375 982 C ATOM 2608 CG GLN A 335 -3.763 28.450 28.551 1.00 46.42 C ANISOU 2608 CG GLN A 335 4322 7160 6155 329 -522 976 C ATOM 2609 CD GLN A 335 -3.269 29.859 28.348 1.00 51.69 C ANISOU 2609 CD GLN A 335 5158 7740 6742 506 -534 993 C ATOM 2610 OE1 GLN A 335 -3.062 30.583 29.321 1.00 56.19 O ANISOU 2610 OE1 GLN A 335 5741 8294 7313 569 -429 987 O ATOM 2611 NE2 GLN A 335 -3.101 30.271 27.093 1.00 51.70 N ANISOU 2611 NE2 GLN A 335 5292 7681 6670 584 -662 1013 N ATOM 2612 N TYR A 336 -3.704 25.131 30.382 1.00 37.67 N ANISOU 2612 N TYR A 336 2986 6063 5263 -173 -287 1092 N ATOM 2613 CA TYR A 336 -2.815 24.134 29.795 1.00 40.99 C ANISOU 2613 CA TYR A 336 3541 6321 5712 -287 -336 1097 C ATOM 2614 C TYR A 336 -3.000 22.710 30.299 1.00 46.09 C ANISOU 2614 C TYR A 336 4090 6911 6512 -489 -285 1164 C ATOM 2615 O TYR A 336 -2.534 21.772 29.655 1.00 45.92 O ANISOU 2615 O TYR A 336 4138 6741 6569 -580 -354 1129 O ATOM 2616 CB TYR A 336 -1.336 24.567 29.945 1.00 38.51 C ANISOU 2616 CB TYR A 336 3459 5893 5282 -226 -288 1133 C ATOM 2617 CG TYR A 336 -0.978 25.737 29.057 1.00 41.82 C ANISOU 2617 CG TYR A 336 4010 6294 5587 -71 -356 1077 C ATOM 2618 CD1 TYR A 336 -1.080 25.632 27.667 1.00 38.93 C ANISOU 2618 CD1 TYR A 336 3698 5904 5190 -47 -483 1006 C ATOM 2619 CD2 TYR A 336 -0.547 26.953 29.601 1.00 38.81 C ANISOU 2619 CD2 TYR A 336 3709 5915 5124 47 -297 1098 C ATOM 2620 CE1 TYR A 336 -0.775 26.712 26.836 1.00 34.44 C ANISOU 2620 CE1 TYR A 336 3268 5322 4498 91 -535 999 C ATOM 2621 CE2 TYR A 336 -0.226 28.039 28.776 1.00 36.03 C ANISOU 2621 CE2 TYR A 336 3485 5509 4696 173 -351 1078 C ATOM 2622 CZ TYR A 336 -0.340 27.907 27.400 1.00 41.94 C ANISOU 2622 CZ TYR A 336 4293 6241 5401 194 -462 1051 C ATOM 2623 OH TYR A 336 -0.036 28.975 26.593 1.00 43.11 O ANISOU 2623 OH TYR A 336 4584 6339 5456 314 -503 1076 O ATOM 2624 N LEU A 337 -3.679 22.544 31.432 1.00 44.64 N ANISOU 2624 N LEU A 337 3751 6837 6375 -556 -155 1261 N ATOM 2625 CA LEU A 337 -3.648 21.261 32.126 1.00 48.49 C ANISOU 2625 CA LEU A 337 4191 7243 6988 -750 -71 1392 C ATOM 2626 C LEU A 337 -5.015 20.724 32.549 1.00 50.29 C ANISOU 2626 C LEU A 337 4145 7585 7378 -894 1 1440 C ATOM 2627 O LEU A 337 -5.095 19.851 33.407 1.00 61.37 O ANISOU 2627 O LEU A 337 5502 8954 8863 -1052 124 1604 O ATOM 2628 CB LEU A 337 -2.747 21.361 33.359 1.00 44.58 C ANISOU 2628 CB LEU A 337 3831 6748 6358 -726 62 1542 C ATOM 2629 CG LEU A 337 -1.261 21.728 33.193 1.00 50.43 C ANISOU 2629 CG LEU A 337 4811 7369 6982 -621 13 1523 C ATOM 2630 CD1 LEU A 337 -0.569 21.746 34.568 1.00 44.25 C ANISOU 2630 CD1 LEU A 337 4113 6627 6074 -611 120 1671 C ATOM 2631 CD2 LEU A 337 -0.524 20.775 32.245 1.00 44.16 C ANISOU 2631 CD2 LEU A 337 4115 6352 6313 -685 -93 1479 C ATOM 2632 N SER A 338 -6.086 21.229 31.952 1.00 47.09 N ANISOU 2632 N SER A 338 3549 7314 7030 -844 -75 1313 N ATOM 2633 CA SER A 338 -7.429 20.925 32.454 1.00 52.67 C ANISOU 2633 CA SER A 338 3943 8175 7894 -963 20 1349 C ATOM 2634 C SER A 338 -8.168 19.894 31.600 1.00 53.69 C ANISOU 2634 C SER A 338 3893 8216 8293 -1152 -119 1267 C ATOM 2635 O SER A 338 -9.255 19.443 31.956 1.00 69.62 O ANISOU 2635 O SER A 338 5661 10310 10483 -1289 -42 1280 O ATOM 2636 CB SER A 338 -8.248 22.201 32.501 1.00 54.76 C ANISOU 2636 CB SER A 338 4052 8671 8083 -769 32 1252 C ATOM 2637 OG SER A 338 -8.508 22.634 31.176 1.00 61.70 O ANISOU 2637 OG SER A 338 4920 9534 8988 -658 -206 1081 O ATOM 2638 N THR A 339 -7.581 19.532 30.466 1.00 55.50 N ANISOU 2638 N THR A 339 4281 8270 8538 -1147 -317 1141 N ATOM 2639 CA THR A 339 -8.165 18.522 29.582 1.00 62.51 C ANISOU 2639 CA THR A 339 5034 9050 9669 -1322 -483 1013 C ATOM 2640 C THR A 339 -7.429 17.201 29.778 1.00 62.50 C ANISOU 2640 C THR A 339 5165 8768 9813 -1511 -446 1098 C ATOM 2641 O THR A 339 -6.255 17.190 30.165 1.00 62.74 O ANISOU 2641 O THR A 339 5446 8684 9710 -1444 -371 1201 O ATOM 2642 CB THR A 339 -8.078 18.935 28.086 1.00 69.80 C ANISOU 2642 CB THR A 339 6048 9978 10496 -1181 -748 781 C ATOM 2643 OG1 THR A 339 -6.709 18.911 27.650 1.00 69.42 O ANISOU 2643 OG1 THR A 339 6327 9768 10280 -1094 -773 764 O ATOM 2644 CG2 THR A 339 -8.652 20.328 27.870 1.00 61.91 C ANISOU 2644 CG2 THR A 339 4968 9216 9340 -953 -803 730 C ATOM 2645 N PRO A 340 -8.117 16.081 29.520 1.00 65.64 N ANISOU 2645 N PRO A 340 5386 9040 10514 -1746 -511 1050 N ATOM 2646 CA PRO A 340 -7.490 14.752 29.563 1.00 63.50 C ANISOU 2646 CA PRO A 340 5250 8447 10431 -1917 -507 1097 C ATOM 2647 C PRO A 340 -6.323 14.649 28.577 1.00 62.76 C ANISOU 2647 C PRO A 340 5432 8185 10229 -1791 -663 933 C ATOM 2648 O PRO A 340 -5.288 14.057 28.899 1.00 64.91 O ANISOU 2648 O PRO A 340 5904 8240 10521 -1799 -602 1031 O ATOM 2649 CB PRO A 340 -8.630 13.821 29.128 1.00 59.68 C ANISOU 2649 CB PRO A 340 4579 7883 10215 -2111 -588 938 C ATOM 2650 CG PRO A 340 -9.868 14.541 29.554 1.00 60.26 C ANISOU 2650 CG PRO A 340 4402 8250 10244 -2084 -496 940 C ATOM 2651 CD PRO A 340 -9.578 15.998 29.336 1.00 67.18 C ANISOU 2651 CD PRO A 340 5300 9368 10858 -1828 -546 924 C ATOM 2652 N ASP A 341 -6.503 15.226 27.391 1.00 62.31 N ANISOU 2652 N ASP A 341 5389 8244 10043 -1661 -855 687 N ATOM 2653 CA ASP A 341 -5.473 15.250 26.357 1.00 63.04 C ANISOU 2653 CA ASP A 341 5742 8236 9974 -1521 -977 512 C ATOM 2654 C ASP A 341 -4.198 15.957 26.803 1.00 58.27 C ANISOU 2654 C ASP A 341 5381 7639 9120 -1338 -839 650 C ATOM 2655 O ASP A 341 -3.111 15.651 26.316 1.00 58.11 O ANISOU 2655 O ASP A 341 5568 7469 9041 -1272 -859 576 O ATOM 2656 CB ASP A 341 -6.018 15.937 25.103 1.00 75.52 C ANISOU 2656 CB ASP A 341 7291 10009 11395 -1397 -1191 275 C ATOM 2657 CG ASP A 341 -7.369 15.377 24.670 1.00 86.96 C ANISOU 2657 CG ASP A 341 8454 11498 13087 -1566 -1362 117 C ATOM 2658 OD1 ASP A 341 -7.389 14.266 24.093 1.00 87.81 O ANISOU 2658 OD1 ASP A 341 8562 11406 13396 -1718 -1489 -62 O ATOM 2659 OD2 ASP A 341 -8.404 16.047 24.904 1.00 89.25 O ANISOU 2659 OD2 ASP A 341 8509 12015 13388 -1545 -1377 154 O ATOM 2660 N SER A 342 -4.326 16.893 27.738 1.00 56.10 N ANISOU 2660 N SER A 342 5064 7540 8712 -1257 -698 831 N ATOM 2661 CA SER A 342 -3.185 17.697 28.157 1.00 54.43 C ANISOU 2661 CA SER A 342 5058 7354 8270 -1087 -592 934 C ATOM 2662 C SER A 342 -2.216 16.974 29.087 1.00 49.74 C ANISOU 2662 C SER A 342 4577 6575 7746 -1146 -469 1108 C ATOM 2663 O SER A 342 -1.158 17.511 29.400 1.00 52.63 O ANISOU 2663 O SER A 342 5104 6942 7953 -1019 -407 1172 O ATOM 2664 CB SER A 342 -3.650 18.989 28.822 1.00 51.41 C ANISOU 2664 CB SER A 342 4601 7210 7723 -966 -504 1027 C ATOM 2665 OG SER A 342 -4.214 18.740 30.096 1.00 48.56 O ANISOU 2665 OG SER A 342 4090 6907 7451 -1075 -349 1204 O ATOM 2666 N GLN A 343 -2.559 15.765 29.522 1.00 50.86 N ANISOU 2666 N GLN A 343 4632 6551 8141 -1339 -445 1193 N ATOM 2667 CA GLN A 343 -1.748 15.063 30.526 1.00 53.46 C ANISOU 2667 CA GLN A 343 5062 6709 8543 -1388 -338 1410 C ATOM 2668 C GLN A 343 -0.292 14.867 30.115 1.00 44.23 C ANISOU 2668 C GLN A 343 4109 5368 7328 -1265 -382 1347 C ATOM 2669 O GLN A 343 0.621 15.054 30.919 1.00 46.27 O ANISOU 2669 O GLN A 343 4474 5616 7490 -1184 -306 1504 O ATOM 2670 CB GLN A 343 -2.372 13.714 30.885 1.00 61.75 C ANISOU 2670 CB GLN A 343 5997 7553 9913 -1627 -321 1516 C ATOM 2671 CG GLN A 343 -3.722 13.823 31.580 1.00 71.81 C ANISOU 2671 CG GLN A 343 7029 9004 11252 -1775 -216 1645 C ATOM 2672 CD GLN A 343 -3.689 14.703 32.821 1.00 73.22 C ANISOU 2672 CD GLN A 343 7211 9428 11181 -1686 -34 1861 C ATOM 2673 OE1 GLN A 343 -3.104 14.335 33.845 1.00 70.20 O ANISOU 2673 OE1 GLN A 343 6959 8980 10733 -1681 73 2076 O ATOM 2674 NE2 GLN A 343 -4.330 15.868 32.738 1.00 72.02 N ANISOU 2674 NE2 GLN A 343 6948 9559 10857 -1577 -14 1766 N ATOM 2675 N SER A 344 -0.077 14.503 28.855 1.00 45.85 N ANISOU 2675 N SER A 344 4367 5460 7595 -1243 -507 1101 N ATOM 2676 CA SER A 344 1.281 14.318 28.331 1.00 46.46 C ANISOU 2676 CA SER A 344 4622 5395 7636 -1116 -528 1003 C ATOM 2677 C SER A 344 2.134 15.583 28.421 1.00 47.45 C ANISOU 2677 C SER A 344 4849 5699 7481 -932 -465 1032 C ATOM 2678 O SER A 344 3.357 15.488 28.432 1.00 49.83 O ANISOU 2678 O SER A 344 5261 5904 7769 -837 -437 1034 O ATOM 2679 CB SER A 344 1.231 13.844 26.883 1.00 50.30 C ANISOU 2679 CB SER A 344 5142 5792 8177 -1112 -658 697 C ATOM 2680 OG SER A 344 0.706 14.857 26.042 1.00 48.25 O ANISOU 2680 OG SER A 344 4868 5778 7687 -1033 -718 556 O ATOM 2681 N LEU A 345 1.508 16.761 28.480 1.00 44.67 N ANISOU 2681 N LEU A 345 4445 5591 6936 -880 -446 1047 N ATOM 2682 CA LEU A 345 2.281 18.013 28.534 1.00 47.00 C ANISOU 2682 CA LEU A 345 4838 6021 6999 -721 -392 1066 C ATOM 2683 C LEU A 345 3.114 18.111 29.813 1.00 47.68 C ANISOU 2683 C LEU A 345 4965 6085 7067 -693 -301 1258 C ATOM 2684 O LEU A 345 4.135 18.802 29.859 1.00 48.42 O ANISOU 2684 O LEU A 345 5147 6205 7045 -583 -271 1255 O ATOM 2685 CB LEU A 345 1.374 19.239 28.425 1.00 40.50 C ANISOU 2685 CB LEU A 345 3950 5424 6014 -663 -399 1052 C ATOM 2686 CG LEU A 345 2.155 20.567 28.421 1.00 43.99 C ANISOU 2686 CG LEU A 345 4502 5958 6253 -511 -350 1066 C ATOM 2687 CD1 LEU A 345 3.026 20.639 27.173 1.00 33.24 C ANISOU 2687 CD1 LEU A 345 3273 4537 4820 -440 -381 931 C ATOM 2688 CD2 LEU A 345 1.250 21.798 28.535 1.00 46.82 C ANISOU 2688 CD2 LEU A 345 4797 6502 6489 -436 -353 1077 C ATOM 2689 N ARG A 346 2.666 17.394 30.839 1.00 45.28 N ANISOU 2689 N ARG A 346 4590 5737 6877 -803 -264 1428 N ATOM 2690 CA ARG A 346 3.181 17.532 32.188 1.00 42.57 C ANISOU 2690 CA ARG A 346 4278 5433 6463 -780 -192 1633 C ATOM 2691 C ARG A 346 4.648 17.082 32.362 1.00 47.42 C ANISOU 2691 C ARG A 346 5001 5887 7128 -706 -219 1670 C ATOM 2692 O ARG A 346 5.420 17.747 33.068 1.00 43.56 O ANISOU 2692 O ARG A 346 4561 5487 6504 -616 -200 1738 O ATOM 2693 CB ARG A 346 2.256 16.784 33.149 1.00 44.75 C ANISOU 2693 CB ARG A 346 4458 5710 6835 -927 -132 1829 C ATOM 2694 CG ARG A 346 2.512 17.057 34.608 1.00 53.38 C ANISOU 2694 CG ARG A 346 5581 6925 7775 -902 -47 2050 C ATOM 2695 CD ARG A 346 1.311 16.668 35.455 1.00 77.96 C ANISOU 2695 CD ARG A 346 8575 10136 10910 -1046 63 2230 C ATOM 2696 NE ARG A 346 0.107 17.389 35.050 1.00 92.22 N ANISOU 2696 NE ARG A 346 10231 12129 12680 -1064 103 2100 N ATOM 2697 CZ ARG A 346 -0.915 16.828 34.416 1.00102.53 C ANISOU 2697 CZ ARG A 346 11390 13383 14185 -1199 84 2038 C ATOM 2698 NH1 ARG A 346 -0.871 15.533 34.134 1.00105.41 N ANISOU 2698 NH1 ARG A 346 11754 13492 14804 -1342 36 2087 N ATOM 2699 NH2 ARG A 346 -1.977 17.554 34.073 1.00106.06 N ANISOU 2699 NH2 ARG A 346 11680 14020 14597 -1188 98 1918 N ATOM 2700 N CYS A 347 5.039 15.976 31.727 1.00 39.58 N ANISOU 2700 N CYS A 347 4033 4660 6345 -736 -275 1605 N ATOM 2701 CA CYS A 347 6.451 15.572 31.751 1.00 43.11 C ANISOU 2701 CA CYS A 347 4555 4956 6870 -636 -304 1605 C ATOM 2702 C CYS A 347 7.367 16.606 31.088 1.00 46.76 C ANISOU 2702 C CYS A 347 5057 5522 7187 -504 -288 1447 C ATOM 2703 O CYS A 347 8.488 16.829 31.560 1.00 45.54 O ANISOU 2703 O CYS A 347 4924 5362 7015 -415 -290 1495 O ATOM 2704 CB CYS A 347 6.635 14.210 31.100 1.00 37.93 C ANISOU 2704 CB CYS A 347 3911 4013 6486 -674 -360 1521 C ATOM 2705 SG CYS A 347 5.593 12.953 31.858 1.00 53.85 S ANISOU 2705 SG CYS A 347 5879 5850 8732 -863 -371 1733 S ATOM 2706 N ASP A 348 6.885 17.262 30.027 1.00 42.55 N ANISOU 2706 N ASP A 348 4528 5090 6550 -496 -277 1275 N ATOM 2707 CA ASP A 348 7.693 18.294 29.361 1.00 40.77 C ANISOU 2707 CA ASP A 348 4351 4958 6183 -391 -238 1161 C ATOM 2708 C ASP A 348 7.971 19.456 30.316 1.00 43.77 C ANISOU 2708 C ASP A 348 4729 5486 6417 -348 -205 1274 C ATOM 2709 O ASP A 348 9.095 19.936 30.398 1.00 42.67 O ANISOU 2709 O ASP A 348 4606 5348 6260 -279 -184 1259 O ATOM 2710 CB ASP A 348 7.007 18.838 28.093 1.00 40.61 C ANISOU 2710 CB ASP A 348 4356 5033 6040 -386 -241 1002 C ATOM 2711 CG ASP A 348 6.712 17.762 27.075 1.00 52.42 C ANISOU 2711 CG ASP A 348 5861 6407 7648 -425 -294 837 C ATOM 2712 OD1 ASP A 348 7.632 16.986 26.723 1.00 56.87 O ANISOU 2712 OD1 ASP A 348 6455 6821 8334 -386 -281 750 O ATOM 2713 OD2 ASP A 348 5.548 17.695 26.627 1.00 56.71 O ANISOU 2713 OD2 ASP A 348 6373 7007 8169 -488 -358 775 O ATOM 2714 N LEU A 349 6.928 19.907 31.013 1.00 38.46 N ANISOU 2714 N LEU A 349 4021 4939 5652 -391 -200 1363 N ATOM 2715 CA LEU A 349 7.045 20.962 32.012 1.00 38.29 C ANISOU 2715 CA LEU A 349 4001 5058 5487 -348 -175 1439 C ATOM 2716 C LEU A 349 8.048 20.556 33.090 1.00 39.67 C ANISOU 2716 C LEU A 349 4185 5190 5696 -326 -202 1555 C ATOM 2717 O LEU A 349 8.877 21.349 33.519 1.00 37.34 O ANISOU 2717 O LEU A 349 3906 4951 5330 -265 -211 1539 O ATOM 2718 CB LEU A 349 5.678 21.195 32.674 1.00 38.97 C ANISOU 2718 CB LEU A 349 4027 5283 5496 -397 -148 1511 C ATOM 2719 CG LEU A 349 4.592 21.638 31.692 1.00 37.67 C ANISOU 2719 CG LEU A 349 3823 5182 5306 -401 -154 1402 C ATOM 2720 CD1 LEU A 349 3.268 21.978 32.412 1.00 34.22 C ANISOU 2720 CD1 LEU A 349 3284 4905 4811 -429 -113 1459 C ATOM 2721 CD2 LEU A 349 5.090 22.841 30.921 1.00 38.58 C ANISOU 2721 CD2 LEU A 349 4010 5327 5322 -302 -155 1296 C ATOM 2722 N ILE A 350 7.958 19.305 33.525 1.00 38.76 N ANISOU 2722 N ILE A 350 4058 4964 5705 -378 -230 1674 N ATOM 2723 CA ILE A 350 8.809 18.828 34.592 1.00 41.30 C ANISOU 2723 CA ILE A 350 4395 5247 6048 -344 -282 1822 C ATOM 2724 C ILE A 350 10.275 18.736 34.144 1.00 43.89 C ANISOU 2724 C ILE A 350 4721 5463 6491 -253 -330 1732 C ATOM 2725 O ILE A 350 11.176 19.142 34.892 1.00 46.46 O ANISOU 2725 O ILE A 350 5039 5848 6765 -188 -384 1772 O ATOM 2726 CB ILE A 350 8.321 17.489 35.132 1.00 39.84 C ANISOU 2726 CB ILE A 350 4212 4939 5988 -423 -297 2009 C ATOM 2727 CG1 ILE A 350 6.992 17.674 35.874 1.00 35.51 C ANISOU 2727 CG1 ILE A 350 3636 4551 5305 -517 -222 2134 C ATOM 2728 CG2 ILE A 350 9.375 16.871 36.039 1.00 39.64 C ANISOU 2728 CG2 ILE A 350 4218 4833 6011 -357 -383 2171 C ATOM 2729 CD1 ILE A 350 6.373 16.351 36.350 1.00 36.25 C ANISOU 2729 CD1 ILE A 350 3720 4511 5542 -636 -206 2347 C ATOM 2730 N ARG A 351 10.522 18.227 32.932 1.00 38.77 N ANISOU 2730 N ARG A 351 4066 4672 5992 -245 -311 1593 N ATOM 2731 CA ARG A 351 11.904 18.169 32.440 1.00 38.21 C ANISOU 2731 CA ARG A 351 3964 4519 6035 -152 -320 1489 C ATOM 2732 C ARG A 351 12.398 19.598 32.249 1.00 45.10 C ANISOU 2732 C ARG A 351 4824 5542 6771 -124 -273 1398 C ATOM 2733 O ARG A 351 13.567 19.901 32.485 1.00 43.33 O ANISOU 2733 O ARG A 351 4543 5322 6599 -64 -296 1374 O ATOM 2734 CB ARG A 351 12.019 17.385 31.130 1.00 38.16 C ANISOU 2734 CB ARG A 351 3961 4358 6182 -141 -283 1326 C ATOM 2735 CG ARG A 351 11.593 15.909 31.194 1.00 41.75 C ANISOU 2735 CG ARG A 351 4428 4598 6836 -176 -338 1380 C ATOM 2736 CD ARG A 351 12.537 15.046 32.029 1.00 37.42 C ANISOU 2736 CD ARG A 351 3852 3894 6471 -96 -424 1515 C ATOM 2737 NE ARG A 351 13.923 15.136 31.572 1.00 44.46 N ANISOU 2737 NE ARG A 351 4677 4752 7464 33 -413 1380 N ATOM 2738 CZ ARG A 351 14.955 15.426 32.361 1.00 43.76 C ANISOU 2738 CZ ARG A 351 4522 4714 7392 120 -477 1463 C ATOM 2739 NH1 ARG A 351 14.755 15.643 33.658 1.00 45.58 N ANISOU 2739 NH1 ARG A 351 4776 5037 7508 100 -567 1678 N ATOM 2740 NH2 ARG A 351 16.189 15.489 31.859 1.00 42.56 N ANISOU 2740 NH2 ARG A 351 4268 4537 7366 229 -452 1323 N ATOM 2741 N TYR A 352 11.500 20.492 31.839 1.00 40.04 N ANISOU 2741 N TYR A 352 4223 5013 5978 -167 -216 1349 N ATOM 2742 CA TYR A 352 11.889 21.882 31.642 1.00 35.68 C ANISOU 2742 CA TYR A 352 3675 4561 5321 -148 -170 1281 C ATOM 2743 C TYR A 352 12.282 22.554 32.963 1.00 41.25 C ANISOU 2743 C TYR A 352 4358 5355 5960 -132 -234 1349 C ATOM 2744 O TYR A 352 13.247 23.301 33.000 1.00 39.19 O ANISOU 2744 O TYR A 352 4059 5106 5725 -112 -235 1289 O ATOM 2745 CB TYR A 352 10.765 22.664 30.952 1.00 33.51 C ANISOU 2745 CB TYR A 352 3456 4364 4910 -175 -119 1235 C ATOM 2746 CG TYR A 352 11.083 24.125 30.675 1.00 29.57 C ANISOU 2746 CG TYR A 352 2984 3924 4328 -156 -71 1185 C ATOM 2747 CD1 TYR A 352 11.591 24.532 29.444 1.00 30.21 C ANISOU 2747 CD1 TYR A 352 3095 3974 4410 -147 13 1111 C ATOM 2748 CD2 TYR A 352 10.872 25.097 31.643 1.00 30.33 C ANISOU 2748 CD2 TYR A 352 3083 4097 4344 -149 -100 1214 C ATOM 2749 CE1 TYR A 352 11.878 25.887 29.180 1.00 38.62 C ANISOU 2749 CE1 TYR A 352 4194 5058 5423 -146 67 1101 C ATOM 2750 CE2 TYR A 352 11.142 26.452 31.394 1.00 29.91 C ANISOU 2750 CE2 TYR A 352 3060 4048 4256 -138 -64 1165 C ATOM 2751 CZ TYR A 352 11.646 26.840 30.165 1.00 39.82 C ANISOU 2751 CZ TYR A 352 4346 5245 5539 -144 20 1127 C ATOM 2752 OH TYR A 352 11.922 28.179 29.933 1.00 37.38 O ANISOU 2752 OH TYR A 352 4075 4905 5221 -150 63 1113 O ATOM 2753 N ILE A 353 11.516 22.314 34.030 1.00 37.83 N ANISOU 2753 N ILE A 353 3946 4996 5434 -150 -282 1464 N ATOM 2754 CA ILE A 353 11.847 22.893 35.329 1.00 36.59 C ANISOU 2754 CA ILE A 353 3785 4953 5165 -124 -353 1509 C ATOM 2755 C ILE A 353 13.209 22.367 35.838 1.00 38.12 C ANISOU 2755 C ILE A 353 3922 5093 5469 -73 -459 1544 C ATOM 2756 O ILE A 353 14.017 23.127 36.365 1.00 42.15 O ANISOU 2756 O ILE A 353 4394 5666 5954 -46 -526 1484 O ATOM 2757 CB ILE A 353 10.739 22.633 36.388 1.00 38.99 C ANISOU 2757 CB ILE A 353 4126 5378 5311 -148 -354 1641 C ATOM 2758 CG1 ILE A 353 9.435 23.351 36.021 1.00 41.12 C ANISOU 2758 CG1 ILE A 353 4410 5733 5482 -175 -261 1582 C ATOM 2759 CG2 ILE A 353 11.173 23.108 37.752 1.00 37.48 C ANISOU 2759 CG2 ILE A 353 3949 5326 4964 -106 -438 1675 C ATOM 2760 CD1 ILE A 353 9.567 24.859 36.030 1.00 37.95 C ANISOU 2760 CD1 ILE A 353 4024 5400 4994 -133 -251 1444 C ATOM 2761 N CYS A 354 13.467 21.076 35.668 1.00 34.07 N ANISOU 2761 N CYS A 354 3391 4451 5104 -55 -489 1626 N ATOM 2762 CA CYS A 354 14.708 20.492 36.180 1.00 43.83 C ANISOU 2762 CA CYS A 354 4558 5627 6466 21 -611 1674 C ATOM 2763 C CYS A 354 15.928 20.894 35.363 1.00 39.75 C ANISOU 2763 C CYS A 354 3932 5055 6116 58 -587 1511 C ATOM 2764 O CYS A 354 16.999 21.160 35.920 1.00 43.16 O ANISOU 2764 O CYS A 354 4270 5524 6604 108 -693 1489 O ATOM 2765 CB CYS A 354 14.615 18.969 36.212 1.00 46.86 C ANISOU 2765 CB CYS A 354 4959 5848 7000 45 -651 1815 C ATOM 2766 SG CYS A 354 13.340 18.314 37.310 1.00 51.13 S ANISOU 2766 SG CYS A 354 5607 6438 7384 -18 -667 2069 S ATOM 2767 N GLY A 355 15.768 20.944 34.045 1.00 37.59 N ANISOU 2767 N GLY A 355 3660 4709 5912 31 -448 1395 N ATOM 2768 CA GLY A 355 16.923 21.025 33.159 1.00 42.99 C ANISOU 2768 CA GLY A 355 4233 5333 6768 67 -383 1261 C ATOM 2769 C GLY A 355 17.151 22.374 32.517 1.00 44.61 C ANISOU 2769 C GLY A 355 4422 5610 6916 9 -270 1149 C ATOM 2770 O GLY A 355 18.258 22.673 32.088 1.00 47.04 O ANISOU 2770 O GLY A 355 4609 5905 7360 20 -217 1062 O ATOM 2771 N VAL A 356 16.118 23.206 32.442 1.00 42.79 N ANISOU 2771 N VAL A 356 4305 5448 6506 -51 -225 1158 N ATOM 2772 CA VAL A 356 16.295 24.504 31.792 1.00 40.94 C ANISOU 2772 CA VAL A 356 4077 5243 6235 -103 -119 1080 C ATOM 2773 C VAL A 356 16.310 25.657 32.793 1.00 34.52 C ANISOU 2773 C VAL A 356 3265 4497 5352 -134 -201 1076 C ATOM 2774 O VAL A 356 17.068 26.610 32.648 1.00 37.45 O ANISOU 2774 O VAL A 356 3575 4853 5800 -177 -168 1009 O ATOM 2775 CB VAL A 356 15.217 24.735 30.725 1.00 45.15 C ANISOU 2775 CB VAL A 356 4735 5779 6641 -128 -9 1071 C ATOM 2776 CG1 VAL A 356 15.443 26.088 29.999 1.00 28.75 C ANISOU 2776 CG1 VAL A 356 2687 3708 4530 -174 102 1034 C ATOM 2777 CG2 VAL A 356 15.236 23.581 29.725 1.00 35.14 C ANISOU 2777 CG2 VAL A 356 3471 4449 5431 -97 55 1029 C ATOM 2778 N VAL A 357 15.461 25.572 33.811 1.00 37.55 N ANISOU 2778 N VAL A 357 3717 4955 5595 -117 -298 1138 N ATOM 2779 CA VAL A 357 15.388 26.634 34.806 1.00 42.84 C ANISOU 2779 CA VAL A 357 4404 5704 6169 -129 -377 1097 C ATOM 2780 C VAL A 357 16.410 26.415 35.923 1.00 40.14 C ANISOU 2780 C VAL A 357 3966 5411 5873 -101 -541 1088 C ATOM 2781 O VAL A 357 16.177 25.629 36.843 1.00 42.04 O ANISOU 2781 O VAL A 357 4230 5723 6019 -52 -646 1186 O ATOM 2782 CB VAL A 357 13.974 26.740 35.413 1.00 43.39 C ANISOU 2782 CB VAL A 357 4583 5869 6034 -113 -383 1147 C ATOM 2783 CG1 VAL A 357 13.900 27.950 36.358 1.00 36.97 C ANISOU 2783 CG1 VAL A 357 3795 5134 5118 -107 -448 1053 C ATOM 2784 CG2 VAL A 357 12.944 26.846 34.281 1.00 25.74 C ANISOU 2784 CG2 VAL A 357 2416 3595 3770 -127 -258 1156 C ATOM 2785 N HIS A 358 17.544 27.107 35.826 1.00 35.36 N ANISOU 2785 N HIS A 358 3247 4769 5419 -135 -567 983 N ATOM 2786 CA HIS A 358 18.602 26.991 36.823 1.00 41.72 C ANISOU 2786 CA HIS A 358 3929 5631 6290 -108 -753 946 C ATOM 2787 C HIS A 358 18.815 28.368 37.449 1.00 44.95 C ANISOU 2787 C HIS A 358 4332 6076 6670 -164 -831 799 C ATOM 2788 O HIS A 358 19.681 29.133 37.012 1.00 45.23 O ANISOU 2788 O HIS A 358 4252 6033 6903 -241 -803 691 O ATOM 2789 CB HIS A 358 19.886 26.438 36.181 1.00 32.72 C ANISOU 2789 CB HIS A 358 2603 4413 5417 -98 -736 924 C ATOM 2790 CG HIS A 358 19.815 24.970 35.836 1.00 42.26 C ANISOU 2790 CG HIS A 358 3809 5572 6674 -13 -716 1038 C ATOM 2791 ND1 HIS A 358 20.910 24.243 35.459 1.00 44.38 N ANISOU 2791 ND1 HIS A 358 3907 5780 7177 43 -726 1018 N ATOM 2792 CD2 HIS A 358 18.759 24.110 35.864 1.00 43.65 C ANISOU 2792 CD2 HIS A 358 4127 5738 6721 23 -693 1161 C ATOM 2793 CE1 HIS A 358 20.543 22.975 35.244 1.00 42.48 C ANISOU 2793 CE1 HIS A 358 3719 5468 6951 123 -715 1117 C ATOM 2794 NE2 HIS A 358 19.259 22.874 35.485 1.00 41.81 N ANISOU 2794 NE2 HIS A 358 3821 5408 6655 98 -698 1209 N ATOM 2795 N PRO A 359 18.005 28.696 38.472 1.00 45.99 N ANISOU 2795 N PRO A 359 4585 6325 6565 -131 -917 786 N ATOM 2796 CA PRO A 359 17.964 30.056 39.032 1.00 42.31 C ANISOU 2796 CA PRO A 359 4149 5874 6051 -171 -977 610 C ATOM 2797 C PRO A 359 19.280 30.512 39.641 1.00 50.58 C ANISOU 2797 C PRO A 359 5043 6934 7243 -208 -1164 462 C ATOM 2798 O PRO A 359 20.002 29.705 40.234 1.00 50.36 O ANISOU 2798 O PRO A 359 4918 6996 7221 -154 -1326 506 O ATOM 2799 CB PRO A 359 16.923 29.945 40.142 1.00 40.46 C ANISOU 2799 CB PRO A 359 4056 5813 5503 -94 -1038 633 C ATOM 2800 CG PRO A 359 16.090 28.739 39.769 1.00 44.40 C ANISOU 2800 CG PRO A 359 4617 6334 5917 -53 -929 845 C ATOM 2801 CD PRO A 359 17.046 27.791 39.136 1.00 43.98 C ANISOU 2801 CD PRO A 359 4445 6187 6078 -57 -942 932 C ATOM 2802 N SER A 360 19.568 31.803 39.510 1.00 56.48 N ANISOU 2802 N SER A 360 5763 7578 8118 -299 -1157 288 N ATOM 2803 CA SER A 360 20.724 32.414 40.158 1.00 67.58 C ANISOU 2803 CA SER A 360 7015 8987 9676 -360 -1354 101 C ATOM 2804 C SER A 360 20.727 32.215 41.673 1.00 70.47 C ANISOU 2804 C SER A 360 7419 9569 9787 -269 -1616 20 C ATOM 2805 O SER A 360 19.717 31.828 42.275 1.00 65.44 O ANISOU 2805 O SER A 360 6952 9074 8837 -172 -1610 98 O ATOM 2806 CB SER A 360 20.742 33.909 39.862 1.00 71.79 C ANISOU 2806 CB SER A 360 7564 9345 10368 -479 -1296 -75 C ATOM 2807 OG SER A 360 19.463 34.480 40.080 1.00 71.87 O ANISOU 2807 OG SER A 360 7785 9355 10166 -423 -1230 -107 O ATOM 2808 N ASN A 361 21.874 32.489 42.279 1.00 76.28 N ANISOU 2808 N ASN A 361 7986 10343 10653 -306 -1844 -138 N ATOM 2809 CA ASN A 361 22.039 32.398 43.725 1.00 81.03 C ANISOU 2809 CA ASN A 361 8616 11170 11000 -221 -2133 -243 C ATOM 2810 C ASN A 361 21.112 33.353 44.463 1.00 75.63 C ANISOU 2810 C ASN A 361 8130 10551 10054 -202 -2147 -425 C ATOM 2811 O ASN A 361 20.643 33.045 45.558 1.00 79.65 O ANISOU 2811 O ASN A 361 8768 11295 10201 -90 -2273 -426 O ATOM 2812 CB ASN A 361 23.495 32.693 44.116 1.00 81.59 C ANISOU 2812 CB ASN A 361 8437 11251 11313 -283 -2394 -426 C ATOM 2813 CG ASN A 361 24.475 31.669 43.561 1.00 85.35 C ANISOU 2813 CG ASN A 361 8685 11703 12039 -262 -2409 -266 C ATOM 2814 OD1 ASN A 361 24.154 30.484 43.434 1.00 81.01 O ANISOU 2814 OD1 ASN A 361 8196 11211 11374 -145 -2353 -25 O ATOM 2815 ND2 ASN A 361 25.684 32.124 43.240 1.00 93.90 N ANISOU 2815 ND2 ASN A 361 9492 12693 13493 -376 -2481 -412 N ATOM 2816 N GLU A 362 20.865 34.515 43.859 1.00 74.68 N ANISOU 2816 N GLU A 362 8035 10220 10121 -304 -2011 -573 N ATOM 2817 CA GLU A 362 20.007 35.532 44.460 1.00 81.98 C ANISOU 2817 CA GLU A 362 9131 11156 10861 -274 -2011 -784 C ATOM 2818 C GLU A 362 18.540 35.068 44.542 1.00 78.39 C ANISOU 2818 C GLU A 362 8879 10826 10077 -148 -1830 -622 C ATOM 2819 O GLU A 362 17.873 35.282 45.558 1.00 79.89 O ANISOU 2819 O GLU A 362 9203 11206 9946 -51 -1891 -742 O ATOM 2820 CB GLU A 362 20.159 36.880 43.730 1.00 86.88 C ANISOU 2820 CB GLU A 362 9724 11468 11821 -411 -1917 -957 C ATOM 2821 CG GLU A 362 18.978 37.293 42.856 1.00 90.46 C ANISOU 2821 CG GLU A 362 10332 11759 12280 -388 -1643 -851 C ATOM 2822 CD GLU A 362 19.153 38.668 42.226 1.00 98.65 C ANISOU 2822 CD GLU A 362 11364 12469 13649 -512 -1575 -1000 C ATOM 2823 OE1 GLU A 362 18.277 39.071 41.426 1.00 94.00 O ANISOU 2823 OE1 GLU A 362 10894 11723 13098 -488 -1371 -897 O ATOM 2824 OE2 GLU A 362 20.164 39.344 42.528 1.00107.80 O ANISOU 2824 OE2 GLU A 362 12396 13519 15045 -636 -1734 -1211 O ATOM 2825 N VAL A 363 18.056 34.405 43.492 1.00 69.68 N ANISOU 2825 N VAL A 363 7787 9636 9052 -151 -1610 -364 N ATOM 2826 CA VAL A 363 16.704 33.866 43.498 1.00 66.89 C ANISOU 2826 CA VAL A 363 7581 9396 8438 -53 -1444 -200 C ATOM 2827 C VAL A 363 16.591 32.723 44.510 1.00 67.83 C ANISOU 2827 C VAL A 363 7739 9793 8239 41 -1549 -56 C ATOM 2828 O VAL A 363 15.629 32.654 45.282 1.00 67.43 O ANISOU 2828 O VAL A 363 7816 9934 7869 126 -1508 -51 O ATOM 2829 CB VAL A 363 16.290 33.392 42.092 1.00 58.09 C ANISOU 2829 CB VAL A 363 6455 8120 7497 -89 -1218 21 C ATOM 2830 CG1 VAL A 363 15.070 32.468 42.160 1.00 46.15 C ANISOU 2830 CG1 VAL A 363 5041 6752 5742 -6 -1092 222 C ATOM 2831 CG2 VAL A 363 16.016 34.590 41.200 1.00 59.44 C ANISOU 2831 CG2 VAL A 363 6654 8053 7877 -148 -1090 -80 C ATOM 2832 N LEU A 364 17.588 31.843 44.512 1.00 68.24 N ANISOU 2832 N LEU A 364 7677 9865 8388 29 -1679 69 N ATOM 2833 CA LEU A 364 17.615 30.700 45.419 1.00 76.20 C ANISOU 2833 CA LEU A 364 8724 11097 9131 121 -1801 253 C ATOM 2834 C LEU A 364 17.597 31.132 46.888 1.00 76.54 C ANISOU 2834 C LEU A 364 8858 11400 8823 195 -1997 86 C ATOM 2835 O LEU A 364 17.052 30.431 47.742 1.00 76.23 O ANISOU 2835 O LEU A 364 8937 11591 8435 282 -2012 243 O ATOM 2836 CB LEU A 364 18.846 29.831 45.132 1.00 80.47 C ANISOU 2836 CB LEU A 364 9100 11575 9900 115 -1941 375 C ATOM 2837 CG LEU A 364 18.854 29.132 43.767 1.00 77.10 C ANISOU 2837 CG LEU A 364 8600 10938 9757 73 -1744 554 C ATOM 2838 CD1 LEU A 364 20.226 28.544 43.456 1.00 73.63 C ANISOU 2838 CD1 LEU A 364 7956 10422 9600 74 -1878 587 C ATOM 2839 CD2 LEU A 364 17.760 28.058 43.685 1.00 59.32 C ANISOU 2839 CD2 LEU A 364 6478 8729 7332 124 -1594 819 C ATOM 2840 N SER A 365 18.177 32.297 47.168 1.00 73.47 N ANISOU 2840 N SER A 365 8421 10972 8524 152 -2139 -235 N ATOM 2841 CA SER A 365 18.251 32.822 48.530 1.00 79.24 C ANISOU 2841 CA SER A 365 9236 11947 8927 221 -2352 -466 C ATOM 2842 C SER A 365 17.176 33.865 48.826 1.00 82.12 C ANISOU 2842 C SER A 365 9747 12342 9115 252 -2211 -695 C ATOM 2843 O SER A 365 17.296 34.630 49.783 1.00 90.42 O ANISOU 2843 O SER A 365 10856 13531 9968 293 -2375 -995 O ATOM 2844 CB SER A 365 19.626 33.433 48.780 1.00 80.58 C ANISOU 2844 CB SER A 365 9242 12061 9312 156 -2645 -726 C ATOM 2845 OG SER A 365 20.638 32.457 48.623 1.00 87.21 O ANISOU 2845 OG SER A 365 9924 12908 10306 158 -2795 -531 O ATOM 2846 N SER A 366 16.131 33.896 48.004 1.00 68.38 N ANISOU 2846 N SER A 366 8056 10473 7453 245 -1922 -575 N ATOM 2847 CA SER A 366 15.048 34.851 48.189 1.00 63.72 C ANISOU 2847 CA SER A 366 7579 9891 6739 300 -1773 -779 C ATOM 2848 C SER A 366 13.762 34.122 48.575 1.00 62.60 C ANISOU 2848 C SER A 366 7548 9987 6251 397 -1572 -571 C ATOM 2849 O SER A 366 13.760 32.901 48.749 1.00 55.32 O ANISOU 2849 O SER A 366 6630 9205 5184 406 -1564 -268 O ATOM 2850 CB SER A 366 14.817 35.619 46.895 1.00 58.04 C ANISOU 2850 CB SER A 366 6812 8824 6416 224 -1608 -820 C ATOM 2851 OG SER A 366 14.398 34.727 45.873 1.00 54.62 O ANISOU 2851 OG SER A 366 6347 8309 6099 196 -1420 -493 O ATOM 2852 N ASP A 367 12.666 34.870 48.687 1.00 58.78 N ANISOU 2852 N ASP A 367 7138 9531 5666 466 -1402 -730 N ATOM 2853 CA ASP A 367 11.364 34.279 48.980 1.00 62.24 C ANISOU 2853 CA ASP A 367 7639 10188 5821 544 -1174 -551 C ATOM 2854 C ASP A 367 10.589 33.891 47.704 1.00 59.02 C ANISOU 2854 C ASP A 367 7166 9585 5674 497 -949 -318 C ATOM 2855 O ASP A 367 9.370 33.691 47.754 1.00 54.26 O ANISOU 2855 O ASP A 367 6577 9107 4934 551 -740 -233 O ATOM 2856 CB ASP A 367 10.528 35.246 49.824 1.00 70.23 C ANISOU 2856 CB ASP A 367 8738 11372 6574 668 -1097 -862 C ATOM 2857 CG ASP A 367 10.330 36.602 49.140 1.00 77.00 C ANISOU 2857 CG ASP A 367 9573 11926 7758 681 -1061 -1154 C ATOM 2858 OD1 ASP A 367 10.702 36.748 47.950 1.00 75.03 O ANISOU 2858 OD1 ASP A 367 9249 11352 7906 585 -1058 -1063 O ATOM 2859 OD2 ASP A 367 9.787 37.525 49.788 1.00 82.12 O ANISOU 2859 OD2 ASP A 367 10286 12656 8260 795 -1028 -1470 O ATOM 2860 N ILE A 368 11.291 33.795 46.572 1.00 51.95 N ANISOU 2860 N ILE A 368 6189 8404 5146 397 -992 -227 N ATOM 2861 CA ILE A 368 10.658 33.447 45.298 1.00 46.93 C ANISOU 2861 CA ILE A 368 5502 7588 4741 354 -812 -31 C ATOM 2862 C ILE A 368 10.219 31.980 45.275 1.00 46.02 C ANISOU 2862 C ILE A 368 5372 7603 4508 331 -722 301 C ATOM 2863 O ILE A 368 10.906 31.116 45.814 1.00 51.47 O ANISOU 2863 O ILE A 368 6069 8395 5091 312 -839 443 O ATOM 2864 CB ILE A 368 11.582 33.760 44.083 1.00 45.60 C ANISOU 2864 CB ILE A 368 5262 7101 4961 255 -865 -31 C ATOM 2865 CG1 ILE A 368 11.867 35.270 43.984 1.00 40.22 C ANISOU 2865 CG1 ILE A 368 4597 6231 4452 256 -921 -330 C ATOM 2866 CG2 ILE A 368 10.973 33.237 42.754 1.00 35.65 C ANISOU 2866 CG2 ILE A 368 3966 5696 3881 218 -698 186 C ATOM 2867 CD1 ILE A 368 10.622 36.145 43.717 1.00 43.23 C ANISOU 2867 CD1 ILE A 368 5032 6549 4844 348 -769 -439 C ATOM 2868 N LEU A 369 9.053 31.720 44.680 1.00 40.98 N ANISOU 2868 N LEU A 369 4711 6955 3905 336 -528 419 N ATOM 2869 CA LEU A 369 8.532 30.362 44.467 1.00 43.33 C ANISOU 2869 CA LEU A 369 4979 7313 4171 286 -427 723 C ATOM 2870 C LEU A 369 9.638 29.419 43.985 1.00 45.36 C ANISOU 2870 C LEU A 369 5208 7427 4599 210 -548 896 C ATOM 2871 O LEU A 369 10.167 29.600 42.897 1.00 50.24 O ANISOU 2871 O LEU A 369 5779 7818 5491 164 -570 866 O ATOM 2872 CB LEU A 369 7.401 30.399 43.429 1.00 38.69 C ANISOU 2872 CB LEU A 369 4330 6627 3744 275 -257 771 C ATOM 2873 CG LEU A 369 6.689 29.084 43.104 1.00 41.69 C ANISOU 2873 CG LEU A 369 4658 7040 4140 204 -146 1043 C ATOM 2874 CD1 LEU A 369 6.087 28.505 44.388 1.00 43.87 C ANISOU 2874 CD1 LEU A 369 4958 7601 4108 217 -61 1165 C ATOM 2875 CD2 LEU A 369 5.613 29.313 42.068 1.00 42.13 C ANISOU 2875 CD2 LEU A 369 4636 7010 4360 204 -23 1028 C ATOM 2876 N PRO A 370 10.009 28.425 44.811 1.00 45.65 N ANISOU 2876 N PRO A 370 5276 7600 4467 207 -624 1079 N ATOM 2877 CA PRO A 370 11.117 27.525 44.443 1.00 41.20 C ANISOU 2877 CA PRO A 370 4675 6897 4084 167 -758 1227 C ATOM 2878 C PRO A 370 10.680 26.453 43.442 1.00 44.85 C ANISOU 2878 C PRO A 370 5094 7199 4749 102 -644 1439 C ATOM 2879 O PRO A 370 9.475 26.153 43.336 1.00 41.99 O ANISOU 2879 O PRO A 370 4736 6891 4328 75 -481 1533 O ATOM 2880 CB PRO A 370 11.514 26.864 45.774 1.00 42.39 C ANISOU 2880 CB PRO A 370 4893 7259 3955 214 -889 1367 C ATOM 2881 CG PRO A 370 10.462 27.306 46.811 1.00 44.83 C ANISOU 2881 CG PRO A 370 5288 7850 3897 263 -775 1320 C ATOM 2882 CD PRO A 370 9.362 28.032 46.076 1.00 50.14 C ANISOU 2882 CD PRO A 370 5917 8459 4675 249 -571 1185 C ATOM 2883 N ARG A 371 11.644 25.891 42.712 1.00 43.13 N ANISOU 2883 N ARG A 371 4820 6791 4778 76 -728 1490 N ATOM 2884 CA ARG A 371 11.350 24.877 41.706 1.00 35.85 C ANISOU 2884 CA ARG A 371 3863 5697 4063 22 -640 1641 C ATOM 2885 C ARG A 371 10.635 23.667 42.295 1.00 46.26 C ANISOU 2885 C ARG A 371 5224 7081 5273 -3 -590 1903 C ATOM 2886 O ARG A 371 9.728 23.115 41.666 1.00 44.78 O ANISOU 2886 O ARG A 371 5016 6817 5180 -68 -461 1988 O ATOM 2887 CB ARG A 371 12.621 24.466 40.946 1.00 36.48 C ANISOU 2887 CB ARG A 371 3870 5583 4408 23 -736 1625 C ATOM 2888 CG ARG A 371 13.167 25.569 39.974 1.00 29.23 C ANISOU 2888 CG ARG A 371 2894 4553 3659 5 -712 1404 C ATOM 2889 CD ARG A 371 14.259 25.005 39.107 1.00 32.75 C ANISOU 2889 CD ARG A 371 3249 4828 4366 0 -744 1407 C ATOM 2890 NE ARG A 371 15.384 24.514 39.912 1.00 40.15 N ANISOU 2890 NE ARG A 371 4128 5797 5331 54 -925 1454 N ATOM 2891 CZ ARG A 371 16.219 23.547 39.552 1.00 36.98 C ANISOU 2891 CZ ARG A 371 3645 5275 5130 89 -981 1527 C ATOM 2892 NH1 ARG A 371 16.099 22.937 38.377 1.00 35.65 N ANISOU 2892 NH1 ARG A 371 3454 4947 5146 69 -857 1540 N ATOM 2893 NH2 ARG A 371 17.192 23.192 40.378 1.00 37.57 N ANISOU 2893 NH2 ARG A 371 3658 5397 5220 160 -1174 1572 N ATOM 2894 N TRP A 372 11.007 23.277 43.513 1.00 41.78 N ANISOU 2894 N TRP A 372 4715 6658 4503 41 -695 2037 N ATOM 2895 CA TRP A 372 10.403 22.099 44.126 1.00 45.98 C ANISOU 2895 CA TRP A 372 5302 7236 4934 7 -642 2337 C ATOM 2896 C TRP A 372 8.901 22.273 44.367 1.00 50.37 C ANISOU 2896 C TRP A 372 5867 7946 5327 -53 -427 2377 C ATOM 2897 O TRP A 372 8.147 21.302 44.297 1.00 51.69 O ANISOU 2897 O TRP A 372 6027 8060 5553 -138 -316 2595 O ATOM 2898 CB TRP A 372 11.130 21.676 45.411 1.00 39.36 C ANISOU 2898 CB TRP A 372 4545 6540 3870 82 -810 2504 C ATOM 2899 CG TRP A 372 11.011 22.626 46.577 1.00 48.98 C ANISOU 2899 CG TRP A 372 5835 8070 4704 144 -841 2389 C ATOM 2900 CD1 TRP A 372 11.961 23.501 47.020 1.00 53.80 C ANISOU 2900 CD1 TRP A 372 6446 8776 5221 225 -1029 2169 C ATOM 2901 CD2 TRP A 372 9.896 22.760 47.477 1.00 51.66 C ANISOU 2901 CD2 TRP A 372 6250 8675 4703 132 -677 2471 C ATOM 2902 NE1 TRP A 372 11.506 24.176 48.133 1.00 53.45 N ANISOU 2902 NE1 TRP A 372 6490 9032 4785 272 -1009 2087 N ATOM 2903 CE2 TRP A 372 10.242 23.738 48.432 1.00 53.24 C ANISOU 2903 CE2 TRP A 372 6513 9128 4590 224 -780 2273 C ATOM 2904 CE3 TRP A 372 8.645 22.144 47.571 1.00 53.76 C ANISOU 2904 CE3 TRP A 372 6522 8985 4918 45 -445 2669 C ATOM 2905 CZ2 TRP A 372 9.375 24.123 49.461 1.00 52.41 C ANISOU 2905 CZ2 TRP A 372 6490 9341 4085 252 -645 2266 C ATOM 2906 CZ3 TRP A 372 7.783 22.529 48.600 1.00 53.51 C ANISOU 2906 CZ3 TRP A 372 6550 9240 4542 60 -292 2649 C ATOM 2907 CH2 TRP A 372 8.153 23.511 49.522 1.00 49.37 C ANISOU 2907 CH2 TRP A 372 6101 8987 3672 172 -385 2456 C ATOM 2908 N ALA A 373 8.472 23.504 44.643 1.00 51.04 N ANISOU 2908 N ALA A 373 5950 8205 5236 -10 -367 2156 N ATOM 2909 CA ALA A 373 7.048 23.779 44.889 1.00 50.33 C ANISOU 2909 CA ALA A 373 5835 8285 5002 -41 -156 2157 C ATOM 2910 C ALA A 373 6.257 23.696 43.588 1.00 45.53 C ANISOU 2910 C ALA A 373 5122 7503 4675 -114 -44 2110 C ATOM 2911 O ALA A 373 5.124 23.211 43.572 1.00 53.90 O ANISOU 2911 O ALA A 373 6121 8617 5742 -189 114 2230 O ATOM 2912 CB ALA A 373 6.864 25.125 45.541 1.00 40.32 C ANISOU 2912 CB ALA A 373 4594 7232 3494 54 -137 1903 C ATOM 2913 N ILE A 374 6.863 24.171 42.506 1.00 39.41 N ANISOU 2913 N ILE A 374 4320 6532 4123 -95 -128 1938 N ATOM 2914 CA ILE A 374 6.283 24.048 41.173 1.00 44.59 C ANISOU 2914 CA ILE A 374 4898 7020 5023 -150 -64 1892 C ATOM 2915 C ILE A 374 6.116 22.567 40.837 1.00 48.38 C ANISOU 2915 C ILE A 374 5356 7360 5667 -252 -50 2111 C ATOM 2916 O ILE A 374 5.049 22.135 40.391 1.00 50.86 O ANISOU 2916 O ILE A 374 5595 7657 6073 -333 54 2160 O ATOM 2917 CB ILE A 374 7.170 24.700 40.105 1.00 44.59 C ANISOU 2917 CB ILE A 374 4901 6841 5202 -113 -156 1712 C ATOM 2918 CG1 ILE A 374 7.254 26.210 40.310 1.00 49.89 C ANISOU 2918 CG1 ILE A 374 5592 7588 5775 -31 -166 1492 C ATOM 2919 CG2 ILE A 374 6.614 24.419 38.708 1.00 44.14 C ANISOU 2919 CG2 ILE A 374 4787 6631 5351 -164 -105 1686 C ATOM 2920 CD1 ILE A 374 6.162 26.945 39.606 1.00 61.38 C ANISOU 2920 CD1 ILE A 374 7001 9046 7275 -9 -68 1384 C ATOM 2921 N ILE A 375 7.171 21.791 41.070 1.00 40.34 N ANISOU 2921 N ILE A 375 4390 6230 4706 -245 -167 2231 N ATOM 2922 CA ILE A 375 7.134 20.349 40.839 1.00 47.42 C ANISOU 2922 CA ILE A 375 5284 6948 5786 -327 -173 2440 C ATOM 2923 C ILE A 375 6.030 19.685 41.661 1.00 49.71 C ANISOU 2923 C ILE A 375 5568 7355 5967 -422 -43 2673 C ATOM 2924 O ILE A 375 5.297 18.831 41.162 1.00 54.75 O ANISOU 2924 O ILE A 375 6148 7862 6793 -538 28 2770 O ATOM 2925 CB ILE A 375 8.490 19.698 41.204 1.00 50.44 C ANISOU 2925 CB ILE A 375 5725 7215 6226 -264 -335 2547 C ATOM 2926 CG1 ILE A 375 9.582 20.118 40.206 1.00 41.60 C ANISOU 2926 CG1 ILE A 375 4570 5946 5291 -199 -431 2333 C ATOM 2927 CG2 ILE A 375 8.350 18.173 41.331 1.00 45.76 C ANISOU 2927 CG2 ILE A 375 5155 6443 5790 -335 -340 2817 C ATOM 2928 CD1 ILE A 375 9.288 19.755 38.768 1.00 43.82 C ANISOU 2928 CD1 ILE A 375 4800 6029 5820 -253 -373 2229 C ATOM 2929 N GLY A 376 5.927 20.067 42.931 1.00 47.55 N ANISOU 2929 N GLY A 376 5350 7331 5386 -379 -7 2758 N ATOM 2930 CA GLY A 376 4.942 19.468 43.810 1.00 49.78 C ANISOU 2930 CA GLY A 376 5631 7741 5543 -462 144 2953 C ATOM 2931 C GLY A 376 3.554 19.771 43.265 1.00 52.27 C ANISOU 2931 C GLY A 376 5804 8128 5929 -549 323 2879 C ATOM 2932 O GLY A 376 2.692 18.903 43.224 1.00 50.96 O ANISOU 2932 O GLY A 376 5575 7882 5904 -668 421 2978 O ATOM 2933 N TRP A 377 3.348 21.008 42.829 1.00 48.37 N ANISOU 2933 N TRP A 377 5257 7739 5382 -469 337 2623 N ATOM 2934 CA TRP A 377 2.068 21.399 42.259 1.00 50.42 C ANISOU 2934 CA TRP A 377 5364 8063 5729 -513 472 2507 C ATOM 2935 C TRP A 377 1.734 20.548 41.036 1.00 50.20 C ANISOU 2935 C TRP A 377 5250 7784 6040 -631 439 2525 C ATOM 2936 O TRP A 377 0.631 20.006 40.940 1.00 49.66 O ANISOU 2936 O TRP A 377 5050 7740 6080 -757 557 2612 O ATOM 2937 CB TRP A 377 2.075 22.891 41.907 1.00 45.85 C ANISOU 2937 CB TRP A 377 4772 7568 5082 -370 444 2204 C ATOM 2938 CG TRP A 377 1.084 23.283 40.843 1.00 48.79 C ANISOU 2938 CG TRP A 377 4999 7901 5637 -381 487 2057 C ATOM 2939 CD1 TRP A 377 -0.292 23.116 40.880 1.00 44.92 C ANISOU 2939 CD1 TRP A 377 4337 7540 5190 -448 638 2091 C ATOM 2940 CD2 TRP A 377 1.371 23.925 39.600 1.00 38.49 C ANISOU 2940 CD2 TRP A 377 3698 6437 4488 -318 374 1863 C ATOM 2941 NE1 TRP A 377 -0.854 23.603 39.718 1.00 46.02 N ANISOU 2941 NE1 TRP A 377 4372 7606 5508 -416 590 1919 N ATOM 2942 CE2 TRP A 377 0.152 24.117 38.905 1.00 40.97 C ANISOU 2942 CE2 TRP A 377 3857 6789 4921 -333 430 1787 C ATOM 2943 CE3 TRP A 377 2.553 24.359 38.977 1.00 41.92 C ANISOU 2943 CE3 TRP A 377 4245 6708 4975 -253 233 1755 C ATOM 2944 CZ2 TRP A 377 0.060 24.706 37.656 1.00 45.03 C ANISOU 2944 CZ2 TRP A 377 4352 7191 5566 -273 336 1629 C ATOM 2945 CZ3 TRP A 377 2.483 24.956 37.727 1.00 44.96 C ANISOU 2945 CZ3 TRP A 377 4613 6977 5491 -209 175 1606 C ATOM 2946 CH2 TRP A 377 1.247 25.123 37.074 1.00 44.86 C ANISOU 2946 CH2 TRP A 377 4474 7010 5560 -213 217 1551 C ATOM 2947 N LEU A 378 2.686 20.427 40.111 1.00 49.42 N ANISOU 2947 N LEU A 378 5215 7456 6107 -596 282 2428 N ATOM 2948 CA LEU A 378 2.445 19.657 38.894 1.00 53.64 C ANISOU 2948 CA LEU A 378 5687 7760 6933 -688 236 2393 C ATOM 2949 C LEU A 378 2.148 18.183 39.164 1.00 61.94 C ANISOU 2949 C LEU A 378 6719 8665 8149 -846 270 2638 C ATOM 2950 O LEU A 378 1.375 17.572 38.424 1.00 60.37 O ANISOU 2950 O LEU A 378 6415 8349 8173 -968 286 2615 O ATOM 2951 CB LEU A 378 3.597 19.785 37.907 1.00 41.77 C ANISOU 2951 CB LEU A 378 4264 6063 5544 -609 91 2241 C ATOM 2952 CG LEU A 378 3.886 21.192 37.378 1.00 45.13 C ANISOU 2952 CG LEU A 378 4708 6567 5874 -484 58 2012 C ATOM 2953 CD1 LEU A 378 5.252 21.231 36.678 1.00 39.70 C ANISOU 2953 CD1 LEU A 378 4101 5709 5273 -420 -52 1919 C ATOM 2954 CD2 LEU A 378 2.771 21.658 36.450 1.00 41.51 C ANISOU 2954 CD2 LEU A 378 4146 6148 5476 -497 92 1875 C ATOM 2955 N LEU A 379 2.741 17.616 40.215 1.00 57.84 N ANISOU 2955 N LEU A 379 6308 8139 7529 -835 261 2843 N ATOM 2956 CA LEU A 379 2.516 16.207 40.518 1.00 56.28 C ANISOU 2956 CA LEU A 379 6135 7751 7497 -940 269 3007 C ATOM 2957 C LEU A 379 1.081 15.942 40.977 1.00 61.46 C ANISOU 2957 C LEU A 379 6683 8525 8143 -1066 438 3070 C ATOM 2958 O LEU A 379 0.540 14.858 40.755 1.00 62.93 O ANISOU 2958 O LEU A 379 6830 8522 8559 -1201 460 3143 O ATOM 2959 CB LEU A 379 3.501 15.695 41.575 1.00 59.57 C ANISOU 2959 CB LEU A 379 6705 8137 7792 -865 199 3182 C ATOM 2960 CG LEU A 379 4.988 15.596 41.228 1.00 59.93 C ANISOU 2960 CG LEU A 379 6839 8015 7917 -747 17 3152 C ATOM 2961 CD1 LEU A 379 5.758 14.998 42.408 1.00 58.35 C ANISOU 2961 CD1 LEU A 379 6766 7811 7594 -677 -54 3342 C ATOM 2962 CD2 LEU A 379 5.198 14.758 39.986 1.00 59.36 C ANISOU 2962 CD2 LEU A 379 6733 7617 8204 -800 -57 3086 C ATOM 2963 N THR A 380 0.473 16.929 41.627 1.00 64.17 N ANISOU 2963 N THR A 380 6974 9177 8232 -1020 564 3031 N ATOM 2964 CA THR A 380 -0.882 16.775 42.150 1.00 74.26 C ANISOU 2964 CA THR A 380 8131 10601 9485 -1123 750 3081 C ATOM 2965 C THR A 380 -1.953 16.926 41.069 1.00 71.81 C ANISOU 2965 C THR A 380 7614 10269 9403 -1210 778 2918 C ATOM 2966 O THR A 380 -3.106 16.603 41.300 1.00 78.83 O ANISOU 2966 O THR A 380 8369 11222 10360 -1323 914 2947 O ATOM 2967 CB THR A 380 -1.172 17.778 43.277 1.00 77.76 C ANISOU 2967 CB THR A 380 8581 11395 9569 -1024 888 3072 C ATOM 2968 OG1 THR A 380 -1.295 19.096 42.721 1.00 83.53 O ANISOU 2968 OG1 THR A 380 9222 12285 10229 -916 882 2851 O ATOM 2969 CG2 THR A 380 -0.052 17.760 44.305 1.00 71.88 C ANISOU 2969 CG2 THR A 380 8042 10702 8567 -921 820 3193 C ATOM 2970 N THR A 381 -1.572 17.420 39.895 1.00 69.67 N ANISOU 2970 N THR A 381 7311 9915 9245 -1159 649 2746 N ATOM 2971 CA THR A 381 -2.524 17.601 38.800 1.00 67.33 C ANISOU 2971 CA THR A 381 6821 9612 9151 -1224 633 2576 C ATOM 2972 C THR A 381 -2.674 16.344 37.949 1.00 72.84 C ANISOU 2972 C THR A 381 7490 10009 10175 -1379 539 2573 C ATOM 2973 O THR A 381 -3.477 16.315 37.014 1.00 74.76 O ANISOU 2973 O THR A 381 7571 10229 10606 -1452 494 2423 O ATOM 2974 CB THR A 381 -2.135 18.784 37.877 1.00 63.34 C ANISOU 2974 CB THR A 381 6292 9175 8598 -1089 535 2378 C ATOM 2975 OG1 THR A 381 -0.996 18.429 37.072 1.00 54.99 O ANISOU 2975 OG1 THR A 381 5393 7865 7637 -1048 364 2307 O ATOM 2976 CG2 THR A 381 -1.827 20.026 38.704 1.00 59.71 C ANISOU 2976 CG2 THR A 381 5905 8951 7829 -911 598 2328 C ATOM 2977 N CYS A 382 -1.895 15.310 38.262 1.00 71.76 N ANISOU 2977 N CYS A 382 7508 9643 10115 -1417 491 2721 N ATOM 2978 CA CYS A 382 -2.009 14.041 37.543 1.00 69.84 C ANISOU 2978 CA CYS A 382 7252 9087 10198 -1560 408 2711 C ATOM 2979 C CYS A 382 -3.340 13.374 37.856 1.00 72.55 C ANISOU 2979 C CYS A 382 7449 9439 10679 -1739 529 2764 C ATOM 2980 O CYS A 382 -3.746 13.315 39.013 1.00 72.72 O ANISOU 2980 O CYS A 382 7477 9602 10552 -1764 688 2935 O ATOM 2981 CB CYS A 382 -0.857 13.106 37.906 1.00 69.20 C ANISOU 2981 CB CYS A 382 7363 8754 10175 -1532 335 2864 C ATOM 2982 SG CYS A 382 0.774 13.718 37.411 1.00 71.88 S ANISOU 2982 SG CYS A 382 7846 9035 10429 -1341 185 2783 S ATOM 2983 N THR A 383 -4.013 12.872 36.822 1.00 77.73 N ANISOU 2983 N THR A 383 7968 9950 11614 -1868 453 2607 N ATOM 2984 CA THR A 383 -5.350 12.290 36.975 1.00 83.09 C ANISOU 2984 CA THR A 383 8467 10640 12462 -2056 556 2616 C ATOM 2985 C THR A 383 -5.407 10.799 36.641 1.00 85.83 C ANISOU 2985 C THR A 383 8842 10631 13137 -2235 494 2648 C ATOM 2986 O THR A 383 -6.488 10.253 36.413 1.00 93.28 O ANISOU 2986 O THR A 383 9616 11533 14293 -2417 531 2590 O ATOM 2987 CB THR A 383 -6.404 13.043 36.121 1.00 78.42 C ANISOU 2987 CB THR A 383 7629 10234 11931 -2072 520 2372 C ATOM 2988 OG1 THR A 383 -5.984 13.087 34.748 1.00 76.22 O ANISOU 2988 OG1 THR A 383 7355 9819 11787 -2040 300 2152 O ATOM 2989 CG2 THR A 383 -6.575 14.471 36.625 1.00 75.01 C ANISOU 2989 CG2 THR A 383 7144 10153 11202 -1901 618 2354 C ATOM 2990 N SER A 384 -4.244 10.151 36.604 1.00 80.35 N ANISOU 2990 N SER A 384 8352 9678 12499 -2179 396 2727 N ATOM 2991 CA SER A 384 -4.164 8.698 36.412 1.00 76.63 C ANISOU 2991 CA SER A 384 7939 8837 12339 -2320 340 2775 C ATOM 2992 C SER A 384 -2.823 8.173 36.903 1.00 82.81 C ANISOU 2992 C SER A 384 8957 9419 13087 -2199 287 2950 C ATOM 2993 O SER A 384 -1.841 8.926 36.995 1.00 85.49 O ANISOU 2993 O SER A 384 9401 9868 13214 -2009 238 2951 O ATOM 2994 CB SER A 384 -4.340 8.316 34.941 1.00 75.26 C ANISOU 2994 CB SER A 384 7682 8458 12453 -2393 159 2474 C ATOM 2995 OG SER A 384 -3.236 8.746 34.155 1.00 78.06 O ANISOU 2995 OG SER A 384 8146 8751 12762 -2228 8 2325 O ATOM 2996 N ASN A 385 -2.773 6.879 37.200 1.00 84.88 N ANISOU 2996 N ASN A 385 9294 9382 13574 -2305 289 3092 N ATOM 2997 CA ASN A 385 -1.549 6.271 37.704 1.00 91.65 C ANISOU 2997 CA ASN A 385 10359 10034 14429 -2183 226 3268 C ATOM 2998 C ASN A 385 -0.415 6.216 36.670 1.00 86.10 C ANISOU 2998 C ASN A 385 9736 9120 13860 -2039 33 3061 C ATOM 2999 O ASN A 385 0.755 6.337 37.024 1.00 82.08 O ANISOU 2999 O ASN A 385 9362 8589 13237 -1862 -24 3151 O ATOM 3000 CB ASN A 385 -1.846 4.896 38.299 1.00 98.17 C ANISOU 3000 CB ASN A 385 11243 10583 15473 -2334 281 3487 C ATOM 3001 CG ASN A 385 -2.673 4.987 39.569 1.00108.61 C ANISOU 3001 CG ASN A 385 12538 12134 16595 -2440 497 3756 C ATOM 3002 OD1 ASN A 385 -2.492 5.905 40.370 1.00111.00 O ANISOU 3002 OD1 ASN A 385 12874 12757 16542 -2322 582 3859 O ATOM 3003 ND2 ASN A 385 -3.596 4.044 39.753 1.00114.63 N ANISOU 3003 ND2 ASN A 385 13235 12733 17584 -2669 594 3856 N ATOM 3004 N VAL A 386 -0.769 6.051 35.399 1.00 82.79 N ANISOU 3004 N VAL A 386 9221 8560 13673 -2115 -66 2770 N ATOM 3005 CA VAL A 386 0.208 6.081 34.317 1.00 78.98 C ANISOU 3005 CA VAL A 386 8801 7904 13306 -1987 -228 2530 C ATOM 3006 C VAL A 386 0.801 7.480 34.140 1.00 79.17 C ANISOU 3006 C VAL A 386 8827 8216 13037 -1823 -236 2461 C ATOM 3007 O VAL A 386 2.014 7.630 33.974 1.00 78.20 O ANISOU 3007 O VAL A 386 8811 8013 12886 -1656 -308 2437 O ATOM 3008 CB VAL A 386 -0.396 5.574 32.992 1.00 76.32 C ANISOU 3008 CB VAL A 386 8367 7372 13260 -2117 -339 2201 C ATOM 3009 CG1 VAL A 386 0.396 6.084 31.793 1.00 74.30 C ANISOU 3009 CG1 VAL A 386 8139 7082 13009 -1985 -475 1901 C ATOM 3010 CG2 VAL A 386 -0.459 4.054 32.994 1.00 84.45 C ANISOU 3010 CG2 VAL A 386 9452 8003 14633 -2222 -380 2225 C ATOM 3011 N ALA A 387 -0.047 8.504 34.186 1.00 74.57 N ANISOU 3011 N ALA A 387 8118 7963 12252 -1864 -159 2428 N ATOM 3012 CA ALA A 387 0.447 9.877 34.124 1.00 61.95 C ANISOU 3012 CA ALA A 387 6525 6646 10369 -1715 -152 2386 C ATOM 3013 C ALA A 387 1.385 10.158 35.298 1.00 59.86 C ANISOU 3013 C ALA A 387 6397 6477 9871 -1566 -100 2627 C ATOM 3014 O ALA A 387 2.444 10.749 35.119 1.00 60.62 O ANISOU 3014 O ALA A 387 6568 6604 9860 -1414 -157 2588 O ATOM 3015 CB ALA A 387 -0.698 10.861 34.116 1.00 52.61 C ANISOU 3015 CB ALA A 387 5176 5792 9020 -1771 -72 2327 C ATOM 3016 N ALA A 388 0.981 9.727 36.491 1.00 66.01 N ANISOU 3016 N ALA A 388 7201 7309 10570 -1618 5 2867 N ATOM 3017 CA ALA A 388 1.793 9.880 37.694 1.00 59.68 C ANISOU 3017 CA ALA A 388 6530 6610 9536 -1488 32 3092 C ATOM 3018 C ALA A 388 3.163 9.235 37.515 1.00 61.13 C ANISOU 3018 C ALA A 388 6844 6523 9861 -1361 -108 3109 C ATOM 3019 O ALA A 388 4.191 9.880 37.752 1.00 67.73 O ANISOU 3019 O ALA A 388 7746 7463 10525 -1196 -163 3118 O ATOM 3020 CB ALA A 388 1.073 9.298 38.908 1.00 55.45 C ANISOU 3020 CB ALA A 388 6009 6129 8930 -1592 165 3345 C ATOM 3021 N SER A 389 3.178 7.973 37.087 1.00 62.18 N ANISOU 3021 N SER A 389 6999 6305 10320 -1433 -168 3097 N ATOM 3022 CA SER A 389 4.442 7.270 36.843 1.00 69.15 C ANISOU 3022 CA SER A 389 7986 6902 11387 -1296 -300 3083 C ATOM 3023 C SER A 389 5.336 7.978 35.818 1.00 67.68 C ANISOU 3023 C SER A 389 7788 6710 11218 -1159 -390 2841 C ATOM 3024 O SER A 389 6.543 8.121 36.042 1.00 70.92 O ANISOU 3024 O SER A 389 8265 7101 11582 -982 -462 2874 O ATOM 3025 CB SER A 389 4.192 5.827 36.417 1.00 70.33 C ANISOU 3025 CB SER A 389 8151 6657 11914 -1400 -346 3056 C ATOM 3026 OG SER A 389 3.783 5.050 37.521 1.00 85.23 O ANISOU 3026 OG SER A 389 10094 8495 13795 -1484 -276 3344 O ATOM 3027 N ASN A 390 4.751 8.418 34.701 1.00 57.96 N ANISOU 3027 N ASN A 390 6466 5501 10055 -1242 -387 2597 N ATOM 3028 CA ASN A 390 5.526 9.137 33.700 1.00 54.34 C ANISOU 3028 CA ASN A 390 6005 5053 9588 -1126 -447 2367 C ATOM 3029 C ASN A 390 6.066 10.427 34.280 1.00 52.79 C ANISOU 3029 C ASN A 390 5828 5204 9024 -983 -406 2419 C ATOM 3030 O ASN A 390 7.192 10.819 33.980 1.00 54.50 O ANISOU 3030 O ASN A 390 6086 5444 9177 -807 -453 2291 O ATOM 3031 CB ASN A 390 4.678 9.487 32.479 1.00 53.47 C ANISOU 3031 CB ASN A 390 5812 5030 9476 -1205 -450 2040 C ATOM 3032 CG ASN A 390 4.246 8.282 31.701 1.00 60.30 C ANISOU 3032 CG ASN A 390 6655 5554 10704 -1332 -524 1885 C ATOM 3033 OD1 ASN A 390 5.034 7.376 31.437 1.00 74.88 O ANISOU 3033 OD1 ASN A 390 8574 7081 12794 -1261 -594 1826 O ATOM 3034 ND2 ASN A 390 2.982 8.267 31.310 1.00 65.94 N ANISOU 3034 ND2 ASN A 390 7253 6326 11473 -1516 -520 1793 N ATOM 3035 N ALA A 391 5.247 11.104 35.085 1.00 52.03 N ANISOU 3035 N ALA A 391 5688 5378 8701 -1064 -311 2583 N ATOM 3036 CA ALA A 391 5.673 12.351 35.718 1.00 56.45 C ANISOU 3036 CA ALA A 391 6271 6258 8920 -938 -278 2614 C ATOM 3037 C ALA A 391 6.858 12.090 36.651 1.00 51.70 C ANISOU 3037 C ALA A 391 5764 5604 8275 -807 -347 2812 C ATOM 3038 O ALA A 391 7.831 12.835 36.643 1.00 51.33 O ANISOU 3038 O ALA A 391 5740 5671 8093 -654 -397 2713 O ATOM 3039 CB ALA A 391 4.523 13.012 36.472 1.00 48.19 C ANISOU 3039 CB ALA A 391 5158 5497 7654 -1037 -154 2736 C ATOM 3040 N LYS A 392 6.771 11.031 37.449 1.00 48.93 N ANISOU 3040 N LYS A 392 5465 5130 7997 -837 -355 2992 N ATOM 3041 CA LYS A 392 7.850 10.717 38.380 1.00 61.91 C ANISOU 3041 CA LYS A 392 7196 6754 9571 -696 -442 3148 C ATOM 3042 C LYS A 392 9.148 10.354 37.655 1.00 64.49 C ANISOU 3042 C LYS A 392 7530 6839 10133 -547 -573 3029 C ATOM 3043 O LYS A 392 10.229 10.774 38.070 1.00 64.63 O ANISOU 3043 O LYS A 392 7565 6946 10047 -392 -659 3046 O ATOM 3044 CB LYS A 392 7.429 9.625 39.374 1.00 61.38 C ANISOU 3044 CB LYS A 392 7197 6595 9529 -766 -414 3390 C ATOM 3045 CG LYS A 392 6.419 10.112 40.417 1.00 56.71 C ANISOU 3045 CG LYS A 392 6609 6304 8635 -860 -275 3538 C ATOM 3046 CD LYS A 392 5.896 8.972 41.315 1.00 54.80 C ANISOU 3046 CD LYS A 392 6437 5947 8436 -956 -217 3795 C ATOM 3047 CE LYS A 392 4.829 8.176 40.586 1.00 60.78 C ANISOU 3047 CE LYS A 392 7118 6488 9487 -1145 -143 3748 C ATOM 3048 NZ LYS A 392 3.814 7.571 41.499 1.00 65.60 N ANISOU 3048 NZ LYS A 392 7748 7129 10047 -1298 -1 3978 N ATOM 3049 N LEU A 393 9.039 9.596 36.566 1.00 62.38 N ANISOU 3049 N LEU A 393 7239 6274 10189 -590 -591 2882 N ATOM 3050 CA LEU A 393 10.216 9.261 35.768 1.00 65.08 C ANISOU 3050 CA LEU A 393 7572 6381 10775 -435 -689 2721 C ATOM 3051 C LEU A 393 10.880 10.524 35.222 1.00 59.95 C ANISOU 3051 C LEU A 393 6869 5973 9935 -321 -672 2490 C ATOM 3052 O LEU A 393 12.101 10.661 35.275 1.00 58.93 O ANISOU 3052 O LEU A 393 6717 5840 9833 -151 -744 2442 O ATOM 3053 CB LEU A 393 9.857 8.312 34.623 1.00 63.70 C ANISOU 3053 CB LEU A 393 7386 5868 10950 -506 -694 2528 C ATOM 3054 CG LEU A 393 11.035 7.847 33.762 1.00 59.55 C ANISOU 3054 CG LEU A 393 6847 5111 10669 -322 -766 2287 C ATOM 3055 CD1 LEU A 393 12.074 7.138 34.616 1.00 61.18 C ANISOU 3055 CD1 LEU A 393 7082 5188 10975 -162 -868 2467 C ATOM 3056 CD2 LEU A 393 10.559 6.934 32.636 1.00 53.27 C ANISOU 3056 CD2 LEU A 393 6053 4016 10171 -398 -767 2032 C ATOM 3057 N ALA A 394 10.074 11.447 34.711 1.00 49.80 N ANISOU 3057 N ALA A 394 5553 4915 8455 -412 -576 2332 N ATOM 3058 CA ALA A 394 10.597 12.715 34.215 1.00 47.05 C ANISOU 3058 CA ALA A 394 5168 4808 7900 -323 -541 2118 C ATOM 3059 C ALA A 394 11.310 13.501 35.326 1.00 49.08 C ANISOU 3059 C ALA A 394 5428 5273 7948 -232 -584 2264 C ATOM 3060 O ALA A 394 12.343 14.145 35.091 1.00 45.67 O ANISOU 3060 O ALA A 394 4954 4919 7480 -116 -608 2128 O ATOM 3061 CB ALA A 394 9.477 13.543 33.585 1.00 43.68 C ANISOU 3061 CB ALA A 394 4721 4570 7305 -430 -449 1975 C ATOM 3062 N LEU A 395 10.774 13.430 36.540 1.00 43.49 N ANISOU 3062 N LEU A 395 4764 4660 7101 -291 -592 2533 N ATOM 3063 CA LEU A 395 11.369 14.146 37.666 1.00 44.98 C ANISOU 3063 CA LEU A 395 4969 5067 7053 -206 -654 2656 C ATOM 3064 C LEU A 395 12.744 13.579 38.064 1.00 47.01 C ANISOU 3064 C LEU A 395 5218 5192 7450 -50 -810 2736 C ATOM 3065 O LEU A 395 13.666 14.316 38.416 1.00 51.24 O ANISOU 3065 O LEU A 395 5714 5880 7876 56 -890 2673 O ATOM 3066 CB LEU A 395 10.419 14.104 38.866 1.00 49.38 C ANISOU 3066 CB LEU A 395 5587 5776 7397 -301 -608 2928 C ATOM 3067 CG LEU A 395 10.932 14.735 40.164 1.00 52.75 C ANISOU 3067 CG LEU A 395 6060 6459 7524 -214 -674 3016 C ATOM 3068 CD1 LEU A 395 11.311 16.214 39.939 1.00 41.00 C ANISOU 3068 CD1 LEU A 395 4524 5189 5867 -155 -679 2797 C ATOM 3069 CD2 LEU A 395 9.901 14.586 41.276 1.00 49.18 C ANISOU 3069 CD2 LEU A 395 5674 6177 6836 -306 -572 3183 C ATOM 3070 N PHE A 396 12.865 12.261 38.005 1.00 48.25 N ANISOU 3070 N PHE A 396 5403 5059 7870 -36 -862 2857 N ATOM 3071 CA PHE A 396 14.051 11.574 38.480 1.00 50.27 C ANISOU 3071 CA PHE A 396 5654 5198 8249 118 -1004 2907 C ATOM 3072 C PHE A 396 14.978 11.227 37.338 1.00 52.02 C ANISOU 3072 C PHE A 396 5777 5185 8804 243 -1043 2704 C ATOM 3073 O PHE A 396 15.970 10.520 37.543 1.00 48.75 O ANISOU 3073 O PHE A 396 5332 4631 8558 383 -1151 2709 O ATOM 3074 CB PHE A 396 13.654 10.264 39.166 1.00 54.66 C ANISOU 3074 CB PHE A 396 6310 5577 8881 72 -1019 3116 C ATOM 3075 CG PHE A 396 13.240 10.421 40.597 1.00 57.38 C ANISOU 3075 CG PHE A 396 6753 6152 8898 30 -1017 3345 C ATOM 3076 CD1 PHE A 396 14.195 10.609 41.592 1.00 58.08 C ANISOU 3076 CD1 PHE A 396 6871 6377 8819 170 -1157 3430 C ATOM 3077 CD2 PHE A 396 11.897 10.346 40.959 1.00 58.25 C ANISOU 3077 CD2 PHE A 396 6919 6343 8870 -143 -876 3464 C ATOM 3078 CE1 PHE A 396 13.816 10.734 42.928 1.00 64.57 C ANISOU 3078 CE1 PHE A 396 7806 7414 9312 146 -1155 3632 C ATOM 3079 CE2 PHE A 396 11.506 10.469 42.291 1.00 58.58 C ANISOU 3079 CE2 PHE A 396 7055 6604 8601 -169 -848 3668 C ATOM 3080 CZ PHE A 396 12.464 10.663 43.275 1.00 62.30 C ANISOU 3080 CZ PHE A 396 7584 7208 8879 -23 -988 3754 C ATOM 3081 N TYR A 397 14.657 11.698 36.135 1.00 51.71 N ANISOU 3081 N TYR A 397 5693 5161 8792 185 -916 2432 N ATOM 3082 CA TYR A 397 15.340 11.195 34.945 1.00 50.24 C ANISOU 3082 CA TYR A 397 5436 4770 8882 279 -893 2171 C ATOM 3083 C TYR A 397 16.850 11.408 34.975 1.00 49.27 C ANISOU 3083 C TYR A 397 5187 4677 8859 470 -971 2080 C ATOM 3084 O TYR A 397 17.596 10.546 34.527 1.00 50.04 O ANISOU 3084 O TYR A 397 5222 4537 9252 605 -1012 1992 O ATOM 3085 CB TYR A 397 14.738 11.757 33.654 1.00 43.56 C ANISOU 3085 CB TYR A 397 4584 4004 7961 185 -737 1881 C ATOM 3086 CG TYR A 397 14.999 10.848 32.479 1.00 47.42 C ANISOU 3086 CG TYR A 397 5054 4234 8728 242 -704 1645 C ATOM 3087 CD1 TYR A 397 14.387 9.607 32.392 1.00 44.70 C ANISOU 3087 CD1 TYR A 397 4776 3587 8622 187 -745 1698 C ATOM 3088 CD2 TYR A 397 15.864 11.222 31.463 1.00 53.74 C ANISOU 3088 CD2 TYR A 397 5772 5090 9559 346 -622 1362 C ATOM 3089 CE1 TYR A 397 14.619 8.768 31.322 1.00 53.24 C ANISOU 3089 CE1 TYR A 397 5848 4419 9961 248 -725 1439 C ATOM 3090 CE2 TYR A 397 16.110 10.381 30.385 1.00 52.54 C ANISOU 3090 CE2 TYR A 397 5609 4723 9633 416 -578 1114 C ATOM 3091 CZ TYR A 397 15.486 9.162 30.323 1.00 56.56 C ANISOU 3091 CZ TYR A 397 6192 4926 10372 373 -640 1136 C ATOM 3092 OH TYR A 397 15.728 8.330 29.257 1.00 67.69 O ANISOU 3092 OH TYR A 397 7599 6114 12008 450 -607 848 O ATOM 3093 N ASP A 398 17.295 12.534 35.523 1.00 46.71 N ANISOU 3093 N ASP A 398 4807 4631 8310 485 -998 2090 N ATOM 3094 CA ASP A 398 18.729 12.810 35.606 1.00 44.70 C ANISOU 3094 CA ASP A 398 4393 4426 8164 644 -1083 1999 C ATOM 3095 C ASP A 398 19.387 12.170 36.814 1.00 49.93 C ANISOU 3095 C ASP A 398 5044 5029 8898 776 -1306 2245 C ATOM 3096 O ASP A 398 20.595 12.263 36.982 1.00 57.19 O ANISOU 3096 O ASP A 398 5826 5996 9909 906 -1396 2156 O ATOM 3097 CB ASP A 398 18.979 14.313 35.578 1.00 50.91 C ANISOU 3097 CB ASP A 398 5111 5509 8721 587 -1023 1867 C ATOM 3098 CG ASP A 398 18.642 14.923 34.229 1.00 58.66 C ANISOU 3098 CG ASP A 398 6088 6535 9667 500 -809 1613 C ATOM 3099 OD1 ASP A 398 19.123 14.367 33.219 1.00 67.39 O ANISOU 3099 OD1 ASP A 398 7126 7497 10983 571 -727 1438 O ATOM 3100 OD2 ASP A 398 17.894 15.929 34.174 1.00 50.39 O ANISOU 3100 OD2 ASP A 398 5108 5664 8374 376 -725 1590 O ATOM 3101 N TRP A 399 18.598 11.506 37.651 1.00 52.08 N ANISOU 3101 N TRP A 399 5489 5253 9046 699 -1342 2477 N ATOM 3102 CA TRP A 399 19.159 10.780 38.786 1.00 56.31 C ANISOU 3102 CA TRP A 399 6080 5764 9549 791 -1499 2653 C ATOM 3103 C TRP A 399 19.746 9.460 38.310 1.00 61.36 C ANISOU 3103 C TRP A 399 6691 6078 10546 917 -1538 2610 C ATOM 3104 O TRP A 399 20.707 8.945 38.885 1.00 63.58 O ANISOU 3104 O TRP A 399 6937 6317 10903 1070 -1684 2661 O ATOM 3105 CB TRP A 399 18.064 10.448 39.803 1.00 60.44 C ANISOU 3105 CB TRP A 399 6798 6340 9825 664 -1485 2924 C ATOM 3106 CG TRP A 399 17.608 11.575 40.676 1.00 60.47 C ANISOU 3106 CG TRP A 399 6856 6685 9435 584 -1479 2996 C ATOM 3107 CD1 TRP A 399 17.039 12.765 40.274 1.00 52.04 C ANISOU 3107 CD1 TRP A 399 5754 5811 8209 482 -1373 2880 C ATOM 3108 CD2 TRP A 399 17.621 11.600 42.107 1.00 49.56 C ANISOU 3108 CD2 TRP A 399 5587 5485 7757 608 -1579 3192 C ATOM 3109 NE1 TRP A 399 16.724 13.528 41.377 1.00 49.33 N ANISOU 3109 NE1 TRP A 399 5486 5754 7503 444 -1401 2970 N ATOM 3110 CE2 TRP A 399 17.075 12.835 42.514 1.00 53.12 C ANISOU 3110 CE2 TRP A 399 6059 6241 7882 521 -1525 3156 C ATOM 3111 CE3 TRP A 399 18.046 10.697 43.089 1.00 53.27 C ANISOU 3111 CE3 TRP A 399 6153 5892 8197 709 -1713 3395 C ATOM 3112 CZ2 TRP A 399 16.951 13.193 43.856 1.00 49.21 C ANISOU 3112 CZ2 TRP A 399 5676 5994 7030 534 -1594 3287 C ATOM 3113 CZ3 TRP A 399 17.925 11.052 44.420 1.00 58.71 C ANISOU 3113 CZ3 TRP A 399 6959 6831 8516 721 -1786 3551 C ATOM 3114 CH2 TRP A 399 17.378 12.291 44.792 1.00 54.17 C ANISOU 3114 CH2 TRP A 399 6402 6566 7616 634 -1723 3484 C ATOM 3115 N LEU A 400 19.134 8.898 37.269 1.00 60.29 N ANISOU 3115 N LEU A 400 6576 5705 10627 858 -1417 2505 N ATOM 3116 CA LEU A 400 19.351 7.494 36.923 1.00 58.09 C ANISOU 3116 CA LEU A 400 6323 5079 10669 940 -1446 2484 C ATOM 3117 C LEU A 400 20.809 7.170 36.590 1.00 58.84 C ANISOU 3117 C LEU A 400 6257 5091 11009 1169 -1522 2306 C ATOM 3118 O LEU A 400 21.339 6.131 37.001 1.00 65.43 O ANISOU 3118 O LEU A 400 7117 5735 12008 1292 -1632 2392 O ATOM 3119 CB LEU A 400 18.407 7.070 35.798 1.00 57.70 C ANISOU 3119 CB LEU A 400 6319 4807 10798 826 -1308 2341 C ATOM 3120 CG LEU A 400 16.908 7.189 36.133 1.00 59.66 C ANISOU 3120 CG LEU A 400 6708 5111 10851 590 -1232 2518 C ATOM 3121 CD1 LEU A 400 16.055 6.565 35.043 1.00 59.81 C ANISOU 3121 CD1 LEU A 400 6762 4866 11096 482 -1137 2356 C ATOM 3122 CD2 LEU A 400 16.583 6.534 37.474 1.00 59.89 C ANISOU 3122 CD2 LEU A 400 6866 5137 10751 542 -1307 2844 C ATOM 3123 N PHE A 401 21.463 8.084 35.881 1.00 56.44 N ANISOU 3123 N PHE A 401 5777 4944 10725 1226 -1455 2067 N ATOM 3124 CA PHE A 401 22.832 7.870 35.431 1.00 60.67 C ANISOU 3124 CA PHE A 401 6117 5438 11496 1428 -1479 1855 C ATOM 3125 C PHE A 401 23.719 9.037 35.805 1.00 62.92 C ANISOU 3125 C PHE A 401 6233 6040 11633 1465 -1524 1803 C ATOM 3126 O PHE A 401 24.753 9.273 35.179 1.00 72.25 O ANISOU 3126 O PHE A 401 7204 7269 12979 1577 -1470 1570 O ATOM 3127 CB PHE A 401 22.842 7.620 33.927 1.00 54.56 C ANISOU 3127 CB PHE A 401 5264 4500 10967 1467 -1299 1537 C ATOM 3128 CG PHE A 401 22.088 6.382 33.533 1.00 65.43 C ANISOU 3128 CG PHE A 401 6794 5533 12532 1439 -1280 1534 C ATOM 3129 CD1 PHE A 401 22.731 5.149 33.499 1.00 66.69 C ANISOU 3129 CD1 PHE A 401 6942 5430 12967 1597 -1352 1485 C ATOM 3130 CD2 PHE A 401 20.729 6.441 33.237 1.00 65.30 C ANISOU 3130 CD2 PHE A 401 6929 5454 12427 1247 -1202 1580 C ATOM 3131 CE1 PHE A 401 22.034 3.997 33.153 1.00 73.10 C ANISOU 3131 CE1 PHE A 401 7896 5909 13971 1556 -1343 1468 C ATOM 3132 CE2 PHE A 401 20.021 5.301 32.893 1.00 68.71 C ANISOU 3132 CE2 PHE A 401 7490 5568 13048 1192 -1196 1559 C ATOM 3133 CZ PHE A 401 20.674 4.073 32.849 1.00 72.86 C ANISOU 3133 CZ PHE A 401 8008 5820 13854 1343 -1266 1499 C ATOM 3134 N PHE A 402 23.309 9.749 36.849 1.00 58.53 N ANISOU 3134 N PHE A 402 5767 5705 10767 1363 -1615 2006 N ATOM 3135 CA PHE A 402 24.012 10.930 37.331 1.00 53.64 C ANISOU 3135 CA PHE A 402 5012 5388 9980 1365 -1682 1956 C ATOM 3136 C PHE A 402 25.504 10.724 37.554 1.00 61.58 C ANISOU 3136 C PHE A 402 5819 6423 11158 1549 -1807 1854 C ATOM 3137 O PHE A 402 25.916 9.914 38.376 1.00 66.63 O ANISOU 3137 O PHE A 402 6507 6985 11823 1671 -1981 2005 O ATOM 3138 CB PHE A 402 23.402 11.404 38.644 1.00 54.02 C ANISOU 3138 CB PHE A 402 5224 5633 9668 1271 -1803 2197 C ATOM 3139 CG PHE A 402 23.965 12.709 39.130 1.00 57.25 C ANISOU 3139 CG PHE A 402 5515 6346 9890 1247 -1877 2113 C ATOM 3140 CD1 PHE A 402 23.521 13.910 38.593 1.00 56.13 C ANISOU 3140 CD1 PHE A 402 5327 6357 9642 1109 -1743 1990 C ATOM 3141 CD2 PHE A 402 24.931 12.739 40.126 1.00 53.22 C ANISOU 3141 CD2 PHE A 402 4939 5963 9319 1365 -2090 2151 C ATOM 3142 CE1 PHE A 402 24.043 15.121 39.035 1.00 56.94 C ANISOU 3142 CE1 PHE A 402 5319 6711 9604 1071 -1815 1893 C ATOM 3143 CE2 PHE A 402 25.454 13.947 40.573 1.00 60.50 C ANISOU 3143 CE2 PHE A 402 5743 7153 10090 1331 -2173 2040 C ATOM 3144 CZ PHE A 402 25.012 15.135 40.029 1.00 55.19 C ANISOU 3144 CZ PHE A 402 5027 6606 9335 1176 -2033 1906 C ATOM 3145 N SER A 403 26.311 11.480 36.828 1.00 65.18 N ANISOU 3145 N SER A 403 6041 6998 11725 1565 -1709 1605 N ATOM 3146 CA SER A 403 27.718 11.583 37.158 1.00 71.43 C ANISOU 3146 CA SER A 403 6610 7894 12634 1700 -1828 1507 C ATOM 3147 C SER A 403 27.985 13.026 37.593 1.00 63.93 C ANISOU 3147 C SER A 403 5558 7247 11486 1584 -1866 1451 C ATOM 3148 O SER A 403 27.624 13.978 36.889 1.00 59.94 O ANISOU 3148 O SER A 403 5010 6834 10932 1441 -1687 1328 O ATOM 3149 CB SER A 403 28.596 11.167 35.982 1.00 80.31 C ANISOU 3149 CB SER A 403 7519 8907 14088 1816 -1670 1247 C ATOM 3150 OG SER A 403 28.944 12.282 35.186 1.00 80.95 O ANISOU 3150 OG SER A 403 7414 9166 14176 1717 -1479 1030 O ATOM 3151 N PRO A 404 28.584 13.190 38.783 1.00 65.45 N ANISOU 3151 N PRO A 404 5723 7588 11556 1648 -2108 1542 N ATOM 3152 CA PRO A 404 28.749 14.511 39.410 1.00 71.12 C ANISOU 3152 CA PRO A 404 6381 8582 12061 1536 -2193 1494 C ATOM 3153 C PRO A 404 29.657 15.475 38.635 1.00 72.49 C ANISOU 3153 C PRO A 404 6265 8868 12408 1470 -2064 1223 C ATOM 3154 O PRO A 404 29.483 16.699 38.739 1.00 71.46 O ANISOU 3154 O PRO A 404 6109 8906 12139 1313 -2037 1149 O ATOM 3155 CB PRO A 404 29.358 14.183 40.783 1.00 67.38 C ANISOU 3155 CB PRO A 404 5922 8216 11465 1673 -2497 1628 C ATOM 3156 CG PRO A 404 29.888 12.806 40.652 1.00 70.31 C ANISOU 3156 CG PRO A 404 6266 8372 12076 1872 -2548 1693 C ATOM 3157 CD PRO A 404 29.015 12.098 39.666 1.00 61.03 C ANISOU 3157 CD PRO A 404 5223 6938 11028 1831 -2329 1713 C ATOM 3158 N ASP A 405 30.601 14.936 37.868 1.00 63.04 N ANISOU 3158 N ASP A 405 4859 7579 11514 1582 -1970 1078 N ATOM 3159 CA ASP A 405 31.489 15.779 37.078 1.00 66.63 C ANISOU 3159 CA ASP A 405 5038 8142 12138 1508 -1802 836 C ATOM 3160 C ASP A 405 30.894 16.198 35.716 1.00 78.14 C ANISOU 3160 C ASP A 405 6509 9544 13635 1377 -1464 717 C ATOM 3161 O ASP A 405 31.247 17.251 35.182 1.00 82.41 O ANISOU 3161 O ASP A 405 6903 10209 14201 1236 -1303 573 O ATOM 3162 CB ASP A 405 32.847 15.108 36.936 1.00 82.63 C ANISOU 3162 CB ASP A 405 6807 10142 14445 1687 -1846 728 C ATOM 3163 CG ASP A 405 33.578 14.990 38.276 1.00 97.76 C ANISOU 3163 CG ASP A 405 8658 12177 16310 1800 -2186 820 C ATOM 3164 OD1 ASP A 405 33.270 15.787 39.194 1.00100.09 O ANISOU 3164 OD1 ASP A 405 9037 12635 16358 1698 -2349 888 O ATOM 3165 OD2 ASP A 405 34.456 14.106 38.409 1.00102.30 O ANISOU 3165 OD2 ASP A 405 9095 12690 17083 1999 -2292 816 O ATOM 3166 N LYS A 406 29.973 15.401 35.176 1.00 71.29 N ANISOU 3166 N LYS A 406 5826 8495 12764 1414 -1360 785 N ATOM 3167 CA LYS A 406 29.355 15.720 33.887 1.00 69.77 C ANISOU 3167 CA LYS A 406 5660 8265 12585 1314 -1053 673 C ATOM 3168 C LYS A 406 27.948 16.323 33.992 1.00 67.42 C ANISOU 3168 C LYS A 406 5588 7991 12035 1158 -1026 804 C ATOM 3169 O LYS A 406 27.584 17.158 33.174 1.00 66.37 O ANISOU 3169 O LYS A 406 5437 7928 11852 1026 -807 718 O ATOM 3170 CB LYS A 406 29.316 14.497 32.964 1.00 69.06 C ANISOU 3170 CB LYS A 406 5587 7964 12689 1459 -915 587 C ATOM 3171 CG LYS A 406 30.656 14.110 32.354 1.00 80.14 C ANISOU 3171 CG LYS A 406 6731 9371 14347 1592 -809 380 C ATOM 3172 CD LYS A 406 30.583 12.714 31.737 1.00 88.56 C ANISOU 3172 CD LYS A 406 7853 10195 15598 1772 -752 307 C ATOM 3173 CE LYS A 406 29.472 12.621 30.697 1.00 88.90 C ANISOU 3173 CE LYS A 406 8062 10142 15573 1705 -527 234 C ATOM 3174 NZ LYS A 406 29.031 11.215 30.455 1.00 92.48 N ANISOU 3174 NZ LYS A 406 8663 10307 16167 1848 -567 219 N ATOM 3175 N ASP A 407 27.165 15.904 34.983 1.00 67.24 N ANISOU 3175 N ASP A 407 5780 7923 11847 1172 -1233 1022 N ATOM 3176 CA ASP A 407 25.787 16.393 35.133 1.00 61.12 C ANISOU 3176 CA ASP A 407 5216 7179 10826 1035 -1209 1159 C ATOM 3177 C ASP A 407 25.683 17.558 36.117 1.00 64.77 C ANISOU 3177 C ASP A 407 5703 7856 11049 919 -1345 1216 C ATOM 3178 O ASP A 407 26.519 17.714 37.013 1.00 68.62 O ANISOU 3178 O ASP A 407 6108 8444 11522 967 -1537 1208 O ATOM 3179 CB ASP A 407 24.870 15.253 35.567 1.00 58.76 C ANISOU 3179 CB ASP A 407 5151 6707 10467 1089 -1304 1366 C ATOM 3180 CG ASP A 407 24.853 14.107 34.565 1.00 71.91 C ANISOU 3180 CG ASP A 407 6814 8124 12385 1193 -1177 1278 C ATOM 3181 OD1 ASP A 407 24.827 14.379 33.344 1.00 77.44 O ANISOU 3181 OD1 ASP A 407 7459 8823 13141 1151 -936 1073 O ATOM 3182 OD2 ASP A 407 24.875 12.934 34.994 1.00 75.71 O ANISOU 3182 OD2 ASP A 407 7388 8422 12956 1297 -1298 1388 O ATOM 3183 N SER A 408 24.662 18.391 35.939 1.00 63.24 N ANISOU 3183 N SER A 408 5672 7740 10615 756 -1224 1227 N ATOM 3184 CA SER A 408 24.432 19.511 36.850 1.00 54.77 C ANISOU 3184 CA SER A 408 4653 6852 9304 650 -1339 1250 C ATOM 3185 C SER A 408 23.620 19.049 38.054 1.00 56.66 C ANISOU 3185 C SER A 408 5101 7129 9298 684 -1530 1477 C ATOM 3186 O SER A 408 22.595 18.377 37.893 1.00 54.70 O ANISOU 3186 O SER A 408 5047 6784 8954 669 -1445 1604 O ATOM 3187 CB SER A 408 23.644 20.613 36.145 1.00 51.02 C ANISOU 3187 CB SER A 408 4299 6432 8656 472 -1109 1154 C ATOM 3188 OG SER A 408 23.180 21.566 37.088 1.00 49.89 O ANISOU 3188 OG SER A 408 4256 6434 8266 388 -1221 1179 O ATOM 3189 N ILE A 409 24.044 19.420 39.258 1.00 53.93 N ANISOU 3189 N ILE A 409 4726 6935 8829 718 -1773 1521 N ATOM 3190 CA ILE A 409 23.251 19.079 40.429 1.00 54.65 C ANISOU 3190 CA ILE A 409 5050 7106 8609 736 -1906 1728 C ATOM 3191 C ILE A 409 21.888 19.781 40.415 1.00 54.35 C ANISOU 3191 C ILE A 409 5205 7153 8293 592 -1758 1756 C ATOM 3192 O ILE A 409 20.954 19.357 41.106 1.00 53.74 O ANISOU 3192 O ILE A 409 5320 7116 7981 587 -1779 1953 O ATOM 3193 CB ILE A 409 23.952 19.427 41.730 1.00 52.46 C ANISOU 3193 CB ILE A 409 4755 7016 8164 795 -2160 1708 C ATOM 3194 CG1 ILE A 409 23.348 18.587 42.861 1.00 65.43 C ANISOU 3194 CG1 ILE A 409 6635 8697 9528 868 -2272 1957 C ATOM 3195 CG2 ILE A 409 23.827 20.904 42.022 1.00 47.98 C ANISOU 3195 CG2 ILE A 409 4152 6638 7442 675 -2196 1555 C ATOM 3196 CD1 ILE A 409 23.683 19.059 44.240 1.00 72.35 C ANISOU 3196 CD1 ILE A 409 7560 9813 10116 919 -2508 1954 C ATOM 3197 N MET A 410 21.753 20.840 39.625 1.00 50.21 N ANISOU 3197 N MET A 410 4646 6649 7783 470 -1577 1554 N ATOM 3198 CA MET A 410 20.474 21.548 39.605 1.00 49.08 C ANISOU 3198 CA MET A 410 4690 6578 7380 353 -1430 1548 C ATOM 3199 C MET A 410 19.371 20.737 38.929 1.00 47.32 C ANISOU 3199 C MET A 410 4605 6230 7146 325 -1253 1662 C ATOM 3200 O MET A 410 18.191 21.093 39.021 1.00 44.30 O ANISOU 3200 O MET A 410 4368 5912 6554 247 -1151 1697 O ATOM 3201 CB MET A 410 20.611 22.930 38.973 1.00 45.65 C ANISOU 3201 CB MET A 410 4196 6175 6975 242 -1306 1326 C ATOM 3202 CG MET A 410 21.671 23.805 39.641 1.00 51.43 C ANISOU 3202 CG MET A 410 4777 7012 7753 237 -1486 1183 C ATOM 3203 SD MET A 410 21.152 25.517 39.720 1.00 71.98 S ANISOU 3203 SD MET A 410 7456 9689 10205 101 -1412 1000 S ATOM 3204 CE MET A 410 22.368 26.271 38.653 1.00 64.38 C ANISOU 3204 CE MET A 410 6254 8610 9597 8 -1310 816 C ATOM 3205 N ASN A 411 19.753 19.642 38.269 1.00 49.67 N ANISOU 3205 N ASN A 411 4842 6345 7685 392 -1227 1702 N ATOM 3206 CA ASN A 411 18.776 18.790 37.584 1.00 50.02 C ANISOU 3206 CA ASN A 411 5003 6243 7761 359 -1085 1777 C ATOM 3207 C ASN A 411 18.113 17.795 38.528 1.00 51.52 C ANISOU 3207 C ASN A 411 5322 6398 7856 384 -1183 2041 C ATOM 3208 O ASN A 411 16.956 17.427 38.331 1.00 54.93 O ANISOU 3208 O ASN A 411 5874 6782 8216 301 -1072 2124 O ATOM 3209 CB ASN A 411 19.410 18.055 36.397 1.00 48.42 C ANISOU 3209 CB ASN A 411 4694 5845 7858 419 -998 1665 C ATOM 3210 CG ASN A 411 19.549 18.940 35.165 1.00 46.35 C ANISOU 3210 CG ASN A 411 4374 5612 7625 348 -801 1443 C ATOM 3211 OD1 ASN A 411 19.976 20.090 35.254 1.00 53.16 O ANISOU 3211 OD1 ASN A 411 5169 6602 8429 300 -791 1349 O ATOM 3212 ND2 ASN A 411 19.179 18.402 34.008 1.00 43.30 N ANISOU 3212 ND2 ASN A 411 4024 5103 7326 337 -649 1362 N ATOM 3213 N ILE A 412 18.858 17.395 39.560 1.00 44.31 N ANISOU 3213 N ILE A 412 4376 5518 6941 493 -1397 2181 N ATOM 3214 CA ILE A 412 18.422 16.401 40.530 1.00 46.35 C ANISOU 3214 CA ILE A 412 4767 5738 7107 529 -1498 2469 C ATOM 3215 C ILE A 412 17.896 17.022 41.829 1.00 52.02 C ANISOU 3215 C ILE A 412 5612 6721 7430 487 -1551 2566 C ATOM 3216 O ILE A 412 17.243 16.349 42.631 1.00 50.55 O ANISOU 3216 O ILE A 412 5582 6548 7079 465 -1535 2764 O ATOM 3217 CB ILE A 412 19.579 15.419 40.866 1.00 49.27 C ANISOU 3217 CB ILE A 412 5082 5972 7668 679 -1654 2503 C ATOM 3218 CG1 ILE A 412 20.707 16.143 41.611 1.00 50.03 C ANISOU 3218 CG1 ILE A 412 5071 6262 7678 766 -1843 2402 C ATOM 3219 CG2 ILE A 412 20.088 14.776 39.583 1.00 46.96 C ANISOU 3219 CG2 ILE A 412 4659 5422 7762 738 -1581 2375 C ATOM 3220 CD1 ILE A 412 21.875 15.234 42.059 1.00 55.37 C ANISOU 3220 CD1 ILE A 412 5683 6842 8514 937 -2023 2438 C ATOM 3221 N GLU A 413 18.197 18.302 42.033 1.00 51.22 N ANISOU 3221 N GLU A 413 5443 6829 7191 476 -1604 2410 N ATOM 3222 CA GLU A 413 17.756 19.043 43.222 1.00 55.80 C ANISOU 3222 CA GLU A 413 6132 7681 7389 454 -1663 2442 C ATOM 3223 C GLU A 413 16.223 19.103 43.488 1.00 55.02 C ANISOU 3223 C GLU A 413 6192 7679 7036 348 -1479 2565 C ATOM 3224 O GLU A 413 15.793 18.888 44.631 1.00 56.38 O ANISOU 3224 O GLU A 413 6501 7997 6924 355 -1494 2697 O ATOM 3225 CB GLU A 413 18.401 20.440 43.237 1.00 60.23 C ANISOU 3225 CB GLU A 413 6586 8391 7908 442 -1729 2160 C ATOM 3226 CG GLU A 413 17.994 21.355 44.381 1.00 77.93 C ANISOU 3226 CG GLU A 413 8930 10911 9768 429 -1796 2114 C ATOM 3227 CD GLU A 413 17.103 22.529 43.930 1.00 91.22 C ANISOU 3227 CD GLU A 413 10654 12648 11356 320 -1591 1908 C ATOM 3228 OE1 GLU A 413 17.294 23.659 44.437 1.00101.66 O ANISOU 3228 OE1 GLU A 413 11972 14122 12533 313 -1663 1707 O ATOM 3229 OE2 GLU A 413 16.198 22.320 43.090 1.00 85.99 O ANISOU 3229 OE2 GLU A 413 10029 11872 10773 249 -1376 1941 O ATOM 3230 N PRO A 414 15.396 19.382 42.452 1.00 50.24 N ANISOU 3230 N PRO A 414 5579 6984 6526 243 -1260 2445 N ATOM 3231 CA PRO A 414 13.939 19.449 42.687 1.00 48.13 C ANISOU 3231 CA PRO A 414 5418 6816 6054 146 -1086 2537 C ATOM 3232 C PRO A 414 13.356 18.192 43.338 1.00 57.83 C ANISOU 3232 C PRO A 414 6748 7994 7233 123 -1062 2844 C ATOM 3233 O PRO A 414 12.580 18.308 44.292 1.00 59.37 O ANISOU 3233 O PRO A 414 7039 8378 7141 87 -988 2936 O ATOM 3234 CB PRO A 414 13.362 19.623 41.283 1.00 43.18 C ANISOU 3234 CB PRO A 414 4739 6038 5628 63 -908 2378 C ATOM 3235 CG PRO A 414 14.459 20.372 40.528 1.00 43.35 C ANISOU 3235 CG PRO A 414 4653 6002 5814 106 -960 2131 C ATOM 3236 CD PRO A 414 15.745 19.757 41.068 1.00 50.16 C ANISOU 3236 CD PRO A 414 5458 6819 6780 214 -1164 2213 C ATOM 3237 N ALA A 415 13.725 17.011 42.847 1.00 56.40 N ANISOU 3237 N ALA A 415 6549 7542 7337 137 -1087 2928 N ATOM 3238 CA ALA A 415 13.167 15.770 43.390 1.00 50.89 C ANISOU 3238 CA ALA A 415 5953 6735 6648 92 -1035 3152 C ATOM 3239 C ALA A 415 13.458 15.598 44.878 1.00 55.27 C ANISOU 3239 C ALA A 415 6624 7457 6921 163 -1135 3302 C ATOM 3240 O ALA A 415 12.563 15.278 45.659 1.00 56.45 O ANISOU 3240 O ALA A 415 6877 7702 6871 95 -1026 3465 O ATOM 3241 CB ALA A 415 13.677 14.572 42.621 1.00 54.01 C ANISOU 3241 CB ALA A 415 6311 6794 7418 122 -1080 3185 C ATOM 3242 N ILE A 416 14.710 15.802 45.273 1.00 51.70 N ANISOU 3242 N ILE A 416 6148 7046 6451 303 -1345 3243 N ATOM 3243 CA ILE A 416 15.071 15.597 46.667 1.00 60.53 C ANISOU 3243 CA ILE A 416 7390 8318 7292 392 -1476 3381 C ATOM 3244 C ILE A 416 14.422 16.687 47.529 1.00 57.52 C ANISOU 3244 C ILE A 416 7082 8279 6494 359 -1418 3326 C ATOM 3245 O ILE A 416 13.940 16.419 48.631 1.00 59.27 O ANISOU 3245 O ILE A 416 7449 8646 6424 358 -1384 3490 O ATOM 3246 CB ILE A 416 16.624 15.489 46.872 1.00 51.45 C ANISOU 3246 CB ILE A 416 6173 7126 6249 565 -1746 3315 C ATOM 3247 CG1 ILE A 416 16.956 15.057 48.299 1.00 55.61 C ANISOU 3247 CG1 ILE A 416 6853 7780 6494 673 -1901 3495 C ATOM 3248 CG2 ILE A 416 17.321 16.789 46.541 1.00 49.43 C ANISOU 3248 CG2 ILE A 416 5773 7018 5990 598 -1846 3037 C ATOM 3249 CD1 ILE A 416 16.445 13.678 48.654 1.00 59.39 C ANISOU 3249 CD1 ILE A 416 7473 8076 7017 652 -1826 3796 C ATOM 3250 N LEU A 417 14.371 17.906 47.007 1.00 53.34 N ANISOU 3250 N LEU A 417 6456 7873 5938 333 -1394 3094 N ATOM 3251 CA LEU A 417 13.775 19.003 47.762 1.00 62.28 C ANISOU 3251 CA LEU A 417 7647 9322 6693 317 -1342 2998 C ATOM 3252 C LEU A 417 12.252 18.854 47.913 1.00 61.78 C ANISOU 3252 C LEU A 417 7650 9338 6487 199 -1069 3112 C ATOM 3253 O LEU A 417 11.700 19.181 48.968 1.00 63.26 O ANISOU 3253 O LEU A 417 7941 9777 6319 205 -1006 3144 O ATOM 3254 CB LEU A 417 14.166 20.367 47.176 1.00 56.52 C ANISOU 3254 CB LEU A 417 6794 8686 5994 327 -1406 2713 C ATOM 3255 CG LEU A 417 15.614 20.790 47.464 1.00 56.18 C ANISOU 3255 CG LEU A 417 6677 8679 5989 436 -1690 2561 C ATOM 3256 CD1 LEU A 417 15.878 22.201 46.970 1.00 51.94 C ANISOU 3256 CD1 LEU A 417 6018 8230 5488 412 -1729 2264 C ATOM 3257 CD2 LEU A 417 15.930 20.697 48.950 1.00 57.70 C ANISOU 3257 CD2 LEU A 417 7008 9080 5834 530 -1848 2616 C ATOM 3258 N VAL A 418 11.571 18.345 46.887 1.00 51.30 N ANISOU 3258 N VAL A 418 6253 7804 5435 93 -910 3160 N ATOM 3259 CA VAL A 418 10.133 18.140 47.029 1.00 56.33 C ANISOU 3259 CA VAL A 418 6913 8510 5980 -26 -664 3259 C ATOM 3260 C VAL A 418 9.846 17.022 48.030 1.00 63.21 C ANISOU 3260 C VAL A 418 7907 9365 6744 -47 -625 3527 C ATOM 3261 O VAL A 418 8.918 17.133 48.829 1.00 63.88 O ANISOU 3261 O VAL A 418 8050 9651 6569 -96 -466 3605 O ATOM 3262 CB VAL A 418 9.381 17.950 45.673 1.00 70.15 C ANISOU 3262 CB VAL A 418 8546 10063 8043 -142 -521 3212 C ATOM 3263 CG1 VAL A 418 9.769 16.652 44.996 1.00 65.54 C ANISOU 3263 CG1 VAL A 418 7946 9138 7817 -170 -575 3324 C ATOM 3264 CG2 VAL A 418 7.886 17.982 45.901 1.00 68.83 C ANISOU 3264 CG2 VAL A 418 8362 10028 7763 -255 -283 3266 C ATOM 3265 N MET A 419 10.669 15.973 48.015 1.00 63.65 N ANISOU 3265 N MET A 419 8003 9187 6993 1 -769 3666 N ATOM 3266 CA MET A 419 10.558 14.911 49.006 1.00 67.07 C ANISOU 3266 CA MET A 419 8577 9586 7319 2 -766 3943 C ATOM 3267 C MET A 419 10.733 15.448 50.417 1.00 69.58 C ANISOU 3267 C MET A 419 9036 10222 7181 92 -827 3979 C ATOM 3268 O MET A 419 9.936 15.145 51.305 1.00 69.11 O ANISOU 3268 O MET A 419 9084 10296 6880 37 -681 4154 O ATOM 3269 CB MET A 419 11.614 13.841 48.766 1.00 66.57 C ANISOU 3269 CB MET A 419 8534 9227 7533 87 -955 4053 C ATOM 3270 CG MET A 419 11.213 12.711 47.840 1.00 62.55 C ANISOU 3270 CG MET A 419 7972 8371 7424 -15 -868 4144 C ATOM 3271 SD MET A 419 12.738 11.871 47.411 1.00 90.40 S ANISOU 3271 SD MET A 419 11480 11594 11276 145 -1123 4150 S ATOM 3272 CE MET A 419 12.145 10.394 46.643 1.00 69.19 C ANISOU 3272 CE MET A 419 8785 8507 8999 28 -1019 4289 C ATOM 3273 N HIS A 420 11.789 16.233 50.616 1.00 66.14 N ANISOU 3273 N HIS A 420 8594 9906 6631 227 -1045 3803 N ATOM 3274 CA HIS A 420 12.125 16.776 51.929 1.00 67.42 C ANISOU 3274 CA HIS A 420 8891 10365 6360 330 -1162 3788 C ATOM 3275 C HIS A 420 11.033 17.702 52.454 1.00 68.48 C ANISOU 3275 C HIS A 420 9054 10811 6153 269 -953 3688 C ATOM 3276 O HIS A 420 10.529 17.517 53.555 1.00 69.71 O ANISOU 3276 O HIS A 420 9355 11155 5975 268 -867 3829 O ATOM 3277 CB HIS A 420 13.460 17.530 51.863 1.00 64.42 C ANISOU 3277 CB HIS A 420 8450 10034 5991 468 -1454 3557 C ATOM 3278 CG HIS A 420 13.773 18.324 53.090 1.00 69.89 C ANISOU 3278 CG HIS A 420 9261 11051 6244 564 -1597 3450 C ATOM 3279 ND1 HIS A 420 14.104 17.739 54.302 1.00 75.94 N ANISOU 3279 ND1 HIS A 420 10213 11910 6731 654 -1729 3639 N ATOM 3280 CD2 HIS A 420 13.824 19.660 53.305 1.00 69.21 C ANISOU 3280 CD2 HIS A 420 9143 11213 5941 588 -1646 3159 C ATOM 3281 CE1 HIS A 420 14.335 18.674 55.196 1.00 74.89 C ANISOU 3281 CE1 HIS A 420 10157 12074 6223 724 -1854 3459 C ATOM 3282 NE2 HIS A 420 14.173 19.857 54.618 1.00 75.90 N ANISOU 3282 NE2 HIS A 420 10151 12298 6392 684 -1806 3152 N ATOM 3283 N HIS A 421 10.669 18.698 51.653 1.00 62.67 N ANISOU 3283 N HIS A 421 8180 10129 5501 228 -866 3443 N ATOM 3284 CA HIS A 421 9.723 19.719 52.091 1.00 66.63 C ANISOU 3284 CA HIS A 421 8687 10933 5697 205 -685 3291 C ATOM 3285 C HIS A 421 8.272 19.233 52.147 1.00 70.10 C ANISOU 3285 C HIS A 421 9113 11397 6127 75 -368 3451 C ATOM 3286 O HIS A 421 7.405 19.957 52.629 1.00 79.32 O ANISOU 3286 O HIS A 421 10279 12827 7033 67 -189 3346 O ATOM 3287 CB HIS A 421 9.837 20.981 51.211 1.00 67.55 C ANISOU 3287 CB HIS A 421 8666 11091 5911 222 -712 2976 C ATOM 3288 CG HIS A 421 11.002 21.859 51.561 1.00 70.38 C ANISOU 3288 CG HIS A 421 9041 11565 6135 343 -988 2746 C ATOM 3289 ND1 HIS A 421 12.090 22.026 50.730 1.00 72.68 N ANISOU 3289 ND1 HIS A 421 9223 11671 6722 374 -1199 2635 N ATOM 3290 CD2 HIS A 421 11.249 22.610 52.661 1.00 71.98 C ANISOU 3290 CD2 HIS A 421 9345 12048 5956 433 -1093 2586 C ATOM 3291 CE1 HIS A 421 12.956 22.845 51.302 1.00 70.49 C ANISOU 3291 CE1 HIS A 421 8960 11551 6273 467 -1430 2418 C ATOM 3292 NE2 HIS A 421 12.473 23.208 52.475 1.00 69.35 N ANISOU 3292 NE2 HIS A 421 8952 11685 5712 506 -1382 2376 N ATOM 3293 N SER A 422 8.008 18.020 51.662 1.00 68.39 N ANISOU 3293 N SER A 422 8871 10906 6208 -24 -302 3682 N ATOM 3294 CA SER A 422 6.656 17.455 51.721 1.00 71.16 C ANISOU 3294 CA SER A 422 9189 11256 6593 -167 -21 3840 C ATOM 3295 C SER A 422 6.483 16.509 52.891 1.00 81.36 C ANISOU 3295 C SER A 422 10649 12589 7676 -186 31 4137 C ATOM 3296 O SER A 422 5.433 15.882 53.029 1.00 88.91 O ANISOU 3296 O SER A 422 11587 13520 8676 -318 256 4308 O ATOM 3297 CB SER A 422 6.286 16.728 50.424 1.00 63.13 C ANISOU 3297 CB SER A 422 8032 9912 6043 -290 36 3884 C ATOM 3298 OG SER A 422 6.376 17.598 49.313 1.00 65.16 O ANISOU 3298 OG SER A 422 8149 10135 6473 -277 3 3629 O ATOM 3299 N MET A 423 7.520 16.404 53.718 1.00 85.30 N ANISOU 3299 N MET A 423 11310 13145 7955 -57 -187 4201 N ATOM 3300 CA MET A 423 7.517 15.516 54.869 1.00 87.87 C ANISOU 3300 CA MET A 423 11832 13507 8048 -50 -178 4504 C ATOM 3301 C MET A 423 6.300 15.763 55.750 1.00 90.03 C ANISOU 3301 C MET A 423 12155 14070 7983 -126 111 4566 C ATOM 3302 O MET A 423 5.422 14.910 55.864 1.00 90.79 O ANISOU 3302 O MET A 423 12255 14078 8164 -264 323 4804 O ATOM 3303 CB MET A 423 8.793 15.726 55.679 1.00 99.02 C ANISOU 3303 CB MET A 423 13403 15025 9196 130 -481 4484 C ATOM 3304 CG MET A 423 9.716 14.518 55.753 1.00105.29 C ANISOU 3304 CG MET A 423 14299 15539 10169 193 -693 4737 C ATOM 3305 SD MET A 423 11.352 14.959 56.392 1.00179.59 S ANISOU 3305 SD MET A 423 23814 25054 19368 425 -1111 4618 S ATOM 3306 CE MET A 423 10.920 15.773 57.933 1.00103.63 C ANISOU 3306 CE MET A 423 14388 15900 9086 468 -1056 4577 C ATOM 3307 N LYS A 424 6.252 16.937 56.371 1.00 94.28 N ANISOU 3307 N LYS A 424 12724 14951 8149 -37 122 4336 N ATOM 3308 CA LYS A 424 5.129 17.310 57.229 1.00 98.25 C ANISOU 3308 CA LYS A 424 13261 15764 8305 -84 406 4341 C ATOM 3309 C LYS A 424 3.816 17.534 56.452 1.00 96.08 C ANISOU 3309 C LYS A 424 12763 15477 8266 -220 704 4252 C ATOM 3310 O LYS A 424 2.847 16.817 56.686 1.00100.74 O ANISOU 3310 O LYS A 424 13337 16048 8890 -356 947 4469 O ATOM 3311 CB LYS A 424 5.481 18.535 58.091 1.00101.72 C ANISOU 3311 CB LYS A 424 13794 16566 8287 67 321 4069 C ATOM 3312 CG LYS A 424 4.611 18.737 59.335 1.00112.19 C ANISOU 3312 CG LYS A 424 15238 18237 9150 60 567 4117 C ATOM 3313 CD LYS A 424 4.765 20.157 59.890 1.00115.11 C ANISOU 3313 CD LYS A 424 15639 18948 9152 201 518 3734 C ATOM 3314 CE LYS A 424 4.368 20.263 61.363 1.00120.54 C ANISOU 3314 CE LYS A 424 16526 19985 9290 242 654 3788 C ATOM 3315 NZ LYS A 424 2.938 19.941 61.621 1.00123.69 N ANISOU 3315 NZ LYS A 424 16861 20495 9639 116 1067 3936 N ATOM 3316 N PRO A 425 3.788 18.501 55.508 1.00 92.26 N ANISOU 3316 N PRO A 425 12104 14994 7958 -187 675 3943 N ATOM 3317 CA PRO A 425 2.500 18.931 54.944 1.00 92.06 C ANISOU 3317 CA PRO A 425 11875 15033 8071 -278 946 3819 C ATOM 3318 C PRO A 425 1.778 17.830 54.178 1.00 96.47 C ANISOU 3318 C PRO A 425 12311 15307 9036 -462 1075 4031 C ATOM 3319 O PRO A 425 0.703 17.400 54.593 1.00102.45 O ANISOU 3319 O PRO A 425 13030 16141 9756 -577 1332 4172 O ATOM 3320 CB PRO A 425 2.893 20.050 53.967 1.00 86.49 C ANISOU 3320 CB PRO A 425 11041 14310 7510 -192 817 3485 C ATOM 3321 CG PRO A 425 4.316 20.379 54.271 1.00 87.23 C ANISOU 3321 CG PRO A 425 11279 14410 7456 -54 510 3401 C ATOM 3322 CD PRO A 425 4.915 19.121 54.788 1.00 87.56 C ANISOU 3322 CD PRO A 425 11475 14292 7503 -81 394 3723 C ATOM 3323 N HIS A 426 2.362 17.389 53.068 1.00 96.00 N ANISOU 3323 N HIS A 426 12187 14924 9364 -491 900 4035 N ATOM 3324 CA HIS A 426 1.766 16.331 52.263 1.00 96.70 C ANISOU 3324 CA HIS A 426 12166 14715 9861 -660 982 4194 C ATOM 3325 C HIS A 426 2.659 15.086 52.227 1.00 94.45 C ANISOU 3325 C HIS A 426 12011 14116 9758 -676 799 4438 C ATOM 3326 O HIS A 426 3.302 14.820 51.210 1.00 89.79 O ANISOU 3326 O HIS A 426 11367 13255 9494 -666 626 4374 O ATOM 3327 CB HIS A 426 1.523 16.835 50.840 1.00 96.74 C ANISOU 3327 CB HIS A 426 11966 14588 10201 -687 955 3961 C ATOM 3328 CG HIS A 426 0.972 18.228 50.775 1.00 98.80 C ANISOU 3328 CG HIS A 426 12115 15134 10291 -612 1061 3682 C ATOM 3329 ND1 HIS A 426 -0.235 18.580 51.339 1.00105.89 N ANISOU 3329 ND1 HIS A 426 12929 16281 11023 -651 1325 3651 N ATOM 3330 CD2 HIS A 426 1.462 19.354 50.202 1.00 93.89 C ANISOU 3330 CD2 HIS A 426 11448 14575 9651 -494 944 3417 C ATOM 3331 CE1 HIS A 426 -0.465 19.864 51.119 1.00102.11 C ANISOU 3331 CE1 HIS A 426 12357 16004 10438 -543 1358 3367 C ATOM 3332 NE2 HIS A 426 0.550 20.355 50.431 1.00 97.57 N ANISOU 3332 NE2 HIS A 426 11811 15316 9945 -452 1129 3228 N ATOM 3333 N PRO A 427 2.684 14.308 53.328 1.00 96.34 N ANISOU 3333 N PRO A 427 12426 14388 9789 -694 844 4720 N ATOM 3334 CA PRO A 427 3.594 13.161 53.462 1.00 97.63 C ANISOU 3334 CA PRO A 427 12741 14272 10083 -673 657 4965 C ATOM 3335 C PRO A 427 3.290 12.061 52.454 1.00 99.86 C ANISOU 3335 C PRO A 427 12923 14162 10858 -819 673 5067 C ATOM 3336 O PRO A 427 4.072 11.125 52.287 1.00101.44 O ANISOU 3336 O PRO A 427 13211 14073 11259 -791 504 5217 O ATOM 3337 CB PRO A 427 3.317 12.658 54.883 1.00 99.47 C ANISOU 3337 CB PRO A 427 13174 14668 9953 -690 776 5256 C ATOM 3338 CG PRO A 427 1.925 13.081 55.167 1.00101.10 C ANISOU 3338 CG PRO A 427 13272 15115 10025 -811 1100 5217 C ATOM 3339 CD PRO A 427 1.758 14.406 54.471 1.00 99.11 C ANISOU 3339 CD PRO A 427 12838 15030 9790 -745 1099 4837 C ATOM 3340 N ALA A 428 2.147 12.182 51.793 1.00 99.84 N ANISOU 3340 N ALA A 428 12732 14151 11051 -967 868 4969 N ATOM 3341 CA ALA A 428 1.754 11.248 50.755 1.00 98.03 C ANISOU 3341 CA ALA A 428 12388 13568 11290 -1116 878 5004 C ATOM 3342 C ALA A 428 2.733 11.318 49.583 1.00 93.43 C ANISOU 3342 C ALA A 428 11753 12747 10997 -1026 633 4814 C ATOM 3343 O ALA A 428 3.200 10.291 49.088 1.00 89.81 O ANISOU 3343 O ALA A 428 11329 11948 10849 -1052 516 4910 O ATOM 3344 CB ALA A 428 0.341 11.559 50.292 1.00 97.48 C ANISOU 3344 CB ALA A 428 12110 13591 11336 -1272 1112 4887 C ATOM 3345 N ILE A 429 3.029 12.542 49.148 1.00 89.64 N ANISOU 3345 N ILE A 429 11194 12446 10417 -919 569 4541 N ATOM 3346 CA ILE A 429 3.981 12.796 48.073 1.00 84.87 C ANISOU 3346 CA ILE A 429 10542 11666 10039 -828 360 4348 C ATOM 3347 C ILE A 429 5.383 12.250 48.383 1.00 85.90 C ANISOU 3347 C ILE A 429 10820 11640 10179 -693 130 4456 C ATOM 3348 O ILE A 429 5.996 11.582 47.549 1.00 87.66 O ANISOU 3348 O ILE A 429 11021 11555 10733 -681 -3 4436 O ATOM 3349 CB ILE A 429 4.093 14.306 47.786 1.00 81.17 C ANISOU 3349 CB ILE A 429 9995 11454 9391 -731 344 4071 C ATOM 3350 CG1 ILE A 429 2.730 14.893 47.409 1.00 87.24 C ANISOU 3350 CG1 ILE A 429 10601 12373 10174 -835 555 3945 C ATOM 3351 CG2 ILE A 429 5.104 14.561 46.690 1.00 71.96 C ANISOU 3351 CG2 ILE A 429 8786 10104 8451 -648 147 3893 C ATOM 3352 CD1 ILE A 429 2.205 14.446 46.045 1.00 87.13 C ANISOU 3352 CD1 ILE A 429 10437 12102 10566 -955 563 3855 C ATOM 3353 N THR A 430 5.889 12.555 49.575 1.00 79.21 N ANISOU 3353 N THR A 430 10117 11012 8966 -581 76 4551 N ATOM 3354 CA THR A 430 7.208 12.096 50.002 1.00 76.65 C ANISOU 3354 CA THR A 430 9929 10579 8615 -434 -160 4655 C ATOM 3355 C THR A 430 7.305 10.578 49.907 1.00 82.42 C ANISOU 3355 C THR A 430 10726 10957 9635 -489 -190 4904 C ATOM 3356 O THR A 430 8.252 10.033 49.337 1.00 82.24 O ANISOU 3356 O THR A 430 10699 10668 9880 -406 -374 4885 O ATOM 3357 CB THR A 430 7.498 12.520 51.453 1.00 80.33 C ANISOU 3357 CB THR A 430 10564 11354 8604 -328 -195 4755 C ATOM 3358 OG1 THR A 430 7.445 13.946 51.551 1.00 83.75 O ANISOU 3358 OG1 THR A 430 10942 12102 8778 -268 -180 4495 O ATOM 3359 CG2 THR A 430 8.877 12.037 51.896 1.00 76.59 C ANISOU 3359 CG2 THR A 430 10222 10770 8107 -160 -471 4858 C ATOM 3360 N ALA A 431 6.306 9.909 50.467 1.00 84.63 N ANISOU 3360 N ALA A 431 11059 11229 9868 -631 2 5130 N ATOM 3361 CA ALA A 431 6.238 8.457 50.463 1.00 83.16 C ANISOU 3361 CA ALA A 431 10947 10701 9949 -709 2 5389 C ATOM 3362 C ALA A 431 6.312 7.858 49.054 1.00 79.98 C ANISOU 3362 C ALA A 431 10409 9930 10050 -770 -58 5252 C ATOM 3363 O ALA A 431 7.196 7.056 48.765 1.00 83.17 O ANISOU 3363 O ALA A 431 10866 10042 10694 -683 -230 5309 O ATOM 3364 CB ALA A 431 4.985 7.991 51.183 1.00 78.55 C ANISOU 3364 CB ALA A 431 10407 10190 9248 -890 260 5622 C ATOM 3365 N THR A 432 5.392 8.255 48.182 1.00 73.97 N ANISOU 3365 N THR A 432 9476 9187 9443 -905 78 5060 N ATOM 3366 CA THR A 432 5.319 7.701 46.831 1.00 70.86 C ANISOU 3366 CA THR A 432 8962 8463 9500 -978 32 4911 C ATOM 3367 C THR A 432 6.582 7.926 45.987 1.00 71.83 C ANISOU 3367 C THR A 432 9055 8449 9789 -811 -187 4707 C ATOM 3368 O THR A 432 6.994 7.036 45.238 1.00 69.07 O ANISOU 3368 O THR A 432 8694 7752 9796 -805 -284 4682 O ATOM 3369 CB THR A 432 4.064 8.204 46.070 1.00 90.41 C ANISOU 3369 CB THR A 432 11258 11027 12068 -1142 202 4726 C ATOM 3370 OG1 THR A 432 4.114 7.757 44.711 1.00 93.62 O ANISOU 3370 OG1 THR A 432 11563 11130 12877 -1189 123 4544 O ATOM 3371 CG2 THR A 432 3.988 9.716 46.083 1.00 82.33 C ANISOU 3371 CG2 THR A 432 10159 10369 10753 -1064 237 4519 C ATOM 3372 N LEU A 433 7.184 9.109 46.104 1.00 69.60 N ANISOU 3372 N LEU A 433 8755 8432 9258 -679 -258 4552 N ATOM 3373 CA LEU A 433 8.428 9.411 45.396 1.00 67.87 C ANISOU 3373 CA LEU A 433 8498 8116 9173 -522 -451 4367 C ATOM 3374 C LEU A 433 9.566 8.536 45.917 1.00 71.41 C ANISOU 3374 C LEU A 433 9064 8379 9692 -377 -633 4532 C ATOM 3375 O LEU A 433 10.412 8.086 45.143 1.00 64.30 O ANISOU 3375 O LEU A 433 8120 7223 9087 -288 -767 4432 O ATOM 3376 CB LEU A 433 8.798 10.885 45.549 1.00 60.35 C ANISOU 3376 CB LEU A 433 7508 7495 7928 -426 -484 4186 C ATOM 3377 CG LEU A 433 7.845 11.865 44.880 1.00 60.22 C ANISOU 3377 CG LEU A 433 7367 7644 7869 -526 -336 3989 C ATOM 3378 CD1 LEU A 433 8.361 13.288 45.014 1.00 53.45 C ANISOU 3378 CD1 LEU A 433 6488 7067 6754 -416 -391 3810 C ATOM 3379 CD2 LEU A 433 7.700 11.492 43.421 1.00 56.42 C ANISOU 3379 CD2 LEU A 433 6778 6890 7770 -592 -340 3834 C ATOM 3380 N LEU A 434 9.585 8.315 47.232 1.00 70.73 N ANISOU 3380 N LEU A 434 9125 8428 9322 -342 -636 4779 N ATOM 3381 CA LEU A 434 10.578 7.451 47.857 1.00 80.35 C ANISOU 3381 CA LEU A 434 10474 9483 10572 -196 -813 4976 C ATOM 3382 C LEU A 434 10.431 6.045 47.305 1.00 87.65 C ANISOU 3382 C LEU A 434 11411 9982 11910 -262 -809 5090 C ATOM 3383 O LEU A 434 11.418 5.393 46.950 1.00 84.70 O ANISOU 3383 O LEU A 434 11042 9350 11791 -125 -979 5076 O ATOM 3384 CB LEU A 434 10.407 7.439 49.383 1.00 81.89 C ANISOU 3384 CB LEU A 434 10852 9910 10353 -170 -790 5246 C ATOM 3385 CG LEU A 434 11.048 8.602 50.141 1.00 84.22 C ANISOU 3385 CG LEU A 434 11185 10572 10241 -23 -903 5148 C ATOM 3386 CD1 LEU A 434 10.582 8.657 51.590 1.00 82.18 C ANISOU 3386 CD1 LEU A 434 11112 10577 9537 -32 -828 5387 C ATOM 3387 CD2 LEU A 434 12.566 8.492 50.075 1.00 86.75 C ANISOU 3387 CD2 LEU A 434 11506 10793 10663 199 -1189 5086 C ATOM 3388 N ASP A 435 9.181 5.596 47.232 1.00 91.69 N ANISOU 3388 N ASP A 435 11917 10423 12498 -471 -612 5187 N ATOM 3389 CA ASP A 435 8.846 4.290 46.683 1.00 89.71 C ANISOU 3389 CA ASP A 435 11671 9763 12652 -574 -589 5273 C ATOM 3390 C ASP A 435 9.304 4.191 45.230 1.00 87.37 C ANISOU 3390 C ASP A 435 11235 9218 12743 -535 -680 4972 C ATOM 3391 O ASP A 435 9.838 3.165 44.809 1.00 86.71 O ANISOU 3391 O ASP A 435 11177 8773 12994 -477 -785 4989 O ATOM 3392 CB ASP A 435 7.337 4.052 46.783 1.00 87.40 C ANISOU 3392 CB ASP A 435 11353 9491 12365 -827 -351 5372 C ATOM 3393 CG ASP A 435 6.926 2.684 46.279 1.00 96.14 C ANISOU 3393 CG ASP A 435 12470 10165 13895 -958 -328 5462 C ATOM 3394 OD1 ASP A 435 5.771 2.527 45.835 1.00101.34 O ANISOU 3394 OD1 ASP A 435 13033 10775 14697 -1172 -169 5411 O ATOM 3395 OD2 ASP A 435 7.757 1.758 46.332 1.00101.64 O ANISOU 3395 OD2 ASP A 435 13264 10561 14794 -844 -476 5574 O ATOM 3396 N PHE A 436 9.112 5.268 44.474 1.00 65.96 N ANISOU 3396 N PHE A 436 8386 6699 9978 -557 -638 4696 N ATOM 3397 CA PHE A 436 9.475 5.269 43.065 1.00 68.27 C ANISOU 3397 CA PHE A 436 8556 6787 10596 -528 -703 4403 C ATOM 3398 C PHE A 436 10.991 5.239 42.902 1.00 70.11 C ANISOU 3398 C PHE A 436 8792 6927 10919 -292 -900 4321 C ATOM 3399 O PHE A 436 11.511 4.529 42.046 1.00 69.12 O ANISOU 3399 O PHE A 436 8629 6487 11146 -230 -980 4193 O ATOM 3400 CB PHE A 436 8.896 6.493 42.353 1.00 58.82 C ANISOU 3400 CB PHE A 436 7231 5834 9283 -601 -608 4158 C ATOM 3401 CG PHE A 436 9.162 6.512 40.872 1.00 66.78 C ANISOU 3401 CG PHE A 436 8133 6643 10597 -584 -656 3865 C ATOM 3402 CD1 PHE A 436 8.264 5.930 39.987 1.00 65.93 C ANISOU 3402 CD1 PHE A 436 7970 6320 10760 -744 -586 3758 C ATOM 3403 CD2 PHE A 436 10.308 7.118 40.361 1.00 56.79 C ANISOU 3403 CD2 PHE A 436 6821 5408 9346 -410 -769 3684 C ATOM 3404 CE1 PHE A 436 8.505 5.947 38.621 1.00 58.33 C ANISOU 3404 CE1 PHE A 436 6930 5179 10052 -721 -633 3471 C ATOM 3405 CE2 PHE A 436 10.557 7.134 38.991 1.00 56.88 C ANISOU 3405 CE2 PHE A 436 6749 5240 9624 -387 -793 3414 C ATOM 3406 CZ PHE A 436 9.658 6.546 38.124 1.00 58.12 C ANISOU 3406 CZ PHE A 436 6874 5185 10023 -538 -727 3305 C ATOM 3407 N MET A 437 11.687 6.020 43.723 1.00 69.72 N ANISOU 3407 N MET A 437 8776 7158 10554 -159 -979 4371 N ATOM 3408 CA MET A 437 13.142 6.078 43.700 1.00 72.54 C ANISOU 3408 CA MET A 437 9113 7476 10973 68 -1175 4295 C ATOM 3409 C MET A 437 13.758 4.697 43.890 1.00 77.09 C ANISOU 3409 C MET A 437 9769 7707 11816 174 -1294 4452 C ATOM 3410 O MET A 437 14.754 4.362 43.249 1.00 73.41 O ANISOU 3410 O MET A 437 9230 7044 11619 329 -1417 4303 O ATOM 3411 CB MET A 437 13.658 7.026 44.783 1.00 72.91 C ANISOU 3411 CB MET A 437 9205 7885 10612 174 -1254 4359 C ATOM 3412 CG MET A 437 15.148 7.273 44.713 1.00 72.50 C ANISOU 3412 CG MET A 437 9087 7839 10620 399 -1462 4236 C ATOM 3413 SD MET A 437 15.740 8.281 46.083 1.00 84.29 S ANISOU 3413 SD MET A 437 10645 9742 11637 521 -1594 4303 S ATOM 3414 CE MET A 437 15.593 7.119 47.447 1.00 82.50 C ANISOU 3414 CE MET A 437 10646 9438 11262 562 -1649 4703 C ATOM 3415 N CYS A 438 13.159 3.895 44.765 1.00 82.91 N ANISOU 3415 N CYS A 438 10652 8366 12485 95 -1247 4752 N ATOM 3416 CA CYS A 438 13.634 2.538 44.987 1.00 89.41 C ANISOU 3416 CA CYS A 438 11572 8834 13566 185 -1351 4936 C ATOM 3417 C CYS A 438 13.269 1.628 43.817 1.00 91.77 C ANISOU 3417 C CYS A 438 11810 8734 14325 95 -1301 4792 C ATOM 3418 O CYS A 438 14.127 0.950 43.255 1.00 97.79 O ANISOU 3418 O CYS A 438 12539 9209 15407 245 -1424 4685 O ATOM 3419 CB CYS A 438 13.068 1.971 46.289 1.00 92.91 C ANISOU 3419 CB CYS A 438 12208 9308 13785 118 -1302 5324 C ATOM 3420 SG CYS A 438 13.737 2.733 47.774 1.00105.51 S ANISOU 3420 SG CYS A 438 13927 11306 14857 286 -1423 5509 S ATOM 3421 N ARG A 439 11.996 1.628 43.444 1.00 85.59 N ANISOU 3421 N ARG A 439 11002 7941 13577 -143 -1125 4765 N ATOM 3422 CA ARG A 439 11.500 0.700 42.433 1.00 86.13 C ANISOU 3422 CA ARG A 439 11030 7629 14065 -256 -1084 4636 C ATOM 3423 C ARG A 439 11.970 1.007 41.002 1.00 80.67 C ANISOU 3423 C ARG A 439 10192 6837 13622 -184 -1128 4236 C ATOM 3424 O ARG A 439 11.967 0.125 40.146 1.00 87.68 O ANISOU 3424 O ARG A 439 11060 7368 14886 -195 -1152 4085 O ATOM 3425 CB ARG A 439 9.966 0.583 42.511 1.00 83.28 C ANISOU 3425 CB ARG A 439 10674 7297 13672 -539 -893 4727 C ATOM 3426 CG ARG A 439 9.477 -0.151 43.770 1.00 89.80 C ANISOU 3426 CG ARG A 439 11661 8080 14380 -625 -831 5133 C ATOM 3427 CD ARG A 439 7.995 -0.542 43.723 1.00 91.97 C ANISOU 3427 CD ARG A 439 11916 8289 14738 -916 -639 5212 C ATOM 3428 NE ARG A 439 7.721 -1.678 44.604 1.00105.01 N ANISOU 3428 NE ARG A 439 13727 9708 16462 -990 -604 5576 N ATOM 3429 CZ ARG A 439 7.549 -1.587 45.921 1.00112.69 C ANISOU 3429 CZ ARG A 439 14837 10890 17091 -1000 -533 5917 C ATOM 3430 NH1 ARG A 439 7.615 -0.411 46.525 1.00116.84 N ANISOU 3430 NH1 ARG A 439 15353 11864 17176 -938 -496 5915 N ATOM 3431 NH2 ARG A 439 7.313 -2.675 46.639 1.00116.91 N ANISOU 3431 NH2 ARG A 439 15529 11176 17714 -1072 -498 6257 N ATOM 3432 N ILE A 440 12.384 2.240 40.736 1.00 68.65 N ANISOU 3432 N ILE A 440 8576 5618 11891 -109 -1135 4057 N ATOM 3433 CA ILE A 440 12.853 2.577 39.390 1.00 69.72 C ANISOU 3433 CA ILE A 440 8583 5670 12236 -36 -1159 3693 C ATOM 3434 C ILE A 440 14.207 1.914 39.100 1.00 79.90 C ANISOU 3434 C ILE A 440 9851 6714 13791 207 -1308 3595 C ATOM 3435 O ILE A 440 14.564 1.680 37.946 1.00 80.22 O ANISOU 3435 O ILE A 440 9811 6555 14113 272 -1317 3300 O ATOM 3436 CB ILE A 440 12.928 4.114 39.160 1.00 73.04 C ANISOU 3436 CB ILE A 440 8910 6470 12372 -26 -1115 3541 C ATOM 3437 CG1 ILE A 440 13.000 4.441 37.666 1.00 72.39 C ANISOU 3437 CG1 ILE A 440 8718 6291 12496 -19 -1083 3183 C ATOM 3438 CG2 ILE A 440 14.104 4.739 39.916 1.00 65.62 C ANISOU 3438 CG2 ILE A 440 7962 5752 11218 171 -1232 3606 C ATOM 3439 CD1 ILE A 440 11.897 3.781 36.839 1.00 70.57 C ANISOU 3439 CD1 ILE A 440 8491 5826 12496 -205 -1003 3067 C ATOM 3440 N ILE A 441 14.947 1.594 40.156 1.00 76.36 N ANISOU 3440 N ILE A 441 9477 6286 13248 350 -1422 3834 N ATOM 3441 CA ILE A 441 16.281 1.034 39.991 1.00 78.18 C ANISOU 3441 CA ILE A 441 9669 6326 13712 603 -1573 3753 C ATOM 3442 C ILE A 441 16.282 -0.302 39.225 1.00 86.28 C ANISOU 3442 C ILE A 441 10712 6886 15185 626 -1588 3641 C ATOM 3443 O ILE A 441 16.990 -0.429 38.225 1.00 87.18 O ANISOU 3443 O ILE A 441 10717 6855 15551 763 -1615 3333 O ATOM 3444 CB ILE A 441 17.052 0.948 41.336 1.00 83.36 C ANISOU 3444 CB ILE A 441 10407 7104 14161 762 -1718 4044 C ATOM 3445 CG1 ILE A 441 17.305 2.352 41.891 1.00 71.40 C ANISOU 3445 CG1 ILE A 441 8843 6043 12243 783 -1732 4040 C ATOM 3446 CG2 ILE A 441 18.353 0.190 41.160 1.00 80.87 C ANISOU 3446 CG2 ILE A 441 10043 6548 14135 1027 -1879 3972 C ATOM 3447 CD1 ILE A 441 18.009 2.374 43.234 1.00 74.16 C ANISOU 3447 CD1 ILE A 441 9280 6557 12340 936 -1890 4296 C ATOM 3448 N PRO A 442 15.489 -1.298 39.673 1.00 84.45 N ANISOU 3448 N PRO A 442 10614 6416 15056 491 -1560 3873 N ATOM 3449 CA PRO A 442 15.467 -2.516 38.856 1.00 84.60 C ANISOU 3449 CA PRO A 442 10644 5981 15518 503 -1577 3719 C ATOM 3450 C PRO A 442 14.529 -2.431 37.649 1.00 86.28 C ANISOU 3450 C PRO A 442 10793 6108 15881 313 -1457 3414 C ATOM 3451 O PRO A 442 14.673 -3.228 36.723 1.00 88.22 O ANISOU 3451 O PRO A 442 11018 6021 16482 356 -1479 3161 O ATOM 3452 CB PRO A 442 14.957 -3.580 39.834 1.00 86.73 C ANISOU 3452 CB PRO A 442 11087 6025 15841 417 -1592 4101 C ATOM 3453 CG PRO A 442 14.106 -2.833 40.785 1.00 85.15 C ANISOU 3453 CG PRO A 442 10947 6175 15231 238 -1492 4371 C ATOM 3454 CD PRO A 442 14.736 -1.472 40.931 1.00 85.27 C ANISOU 3454 CD PRO A 442 10867 6617 14914 353 -1520 4273 C ATOM 3455 N ASN A 443 13.594 -1.485 37.647 1.00 87.24 N ANISOU 3455 N ASN A 443 10884 6526 15736 117 -1341 3420 N ATOM 3456 CA ASN A 443 12.555 -1.475 36.618 1.00 87.00 C ANISOU 3456 CA ASN A 443 10807 6415 15836 -84 -1243 3172 C ATOM 3457 C ASN A 443 12.815 -0.614 35.381 1.00 82.42 C ANISOU 3457 C ASN A 443 10106 5958 15253 -26 -1215 2771 C ATOM 3458 O ASN A 443 12.343 -0.948 34.299 1.00 79.92 O ANISOU 3458 O ASN A 443 9761 5455 15152 -106 -1188 2477 O ATOM 3459 CB ASN A 443 11.194 -1.110 37.219 1.00 85.66 C ANISOU 3459 CB ASN A 443 10666 6447 15434 -352 -1120 3390 C ATOM 3460 CG ASN A 443 10.730 -2.106 38.254 1.00 91.43 C ANISOU 3460 CG ASN A 443 11522 7000 16217 -452 -1109 3755 C ATOM 3461 OD1 ASN A 443 11.126 -3.271 38.235 1.00 98.13 O ANISOU 3461 OD1 ASN A 443 12441 7473 17371 -380 -1188 3795 O ATOM 3462 ND2 ASN A 443 9.882 -1.652 39.169 1.00 92.78 N ANISOU 3462 ND2 ASN A 443 11728 7436 16090 -613 -999 4023 N ATOM 3463 N PHE A 444 13.540 0.491 35.538 1.00 82.10 N ANISOU 3463 N PHE A 444 10000 6229 14964 105 -1223 2753 N ATOM 3464 CA PHE A 444 13.715 1.434 34.434 1.00 81.87 C ANISOU 3464 CA PHE A 444 9868 6345 14895 143 -1172 2416 C ATOM 3465 C PHE A 444 14.233 0.748 33.183 1.00 80.20 C ANISOU 3465 C PHE A 444 9616 5830 15025 265 -1193 2034 C ATOM 3466 O PHE A 444 13.642 0.829 32.107 1.00 80.45 O ANISOU 3466 O PHE A 444 9630 5798 15141 172 -1136 1740 O ATOM 3467 CB PHE A 444 14.673 2.562 34.800 1.00 77.81 C ANISOU 3467 CB PHE A 444 9282 6150 14133 303 -1194 2448 C ATOM 3468 CG PHE A 444 15.051 3.407 33.625 1.00 73.63 C ANISOU 3468 CG PHE A 444 8648 5715 13613 379 -1135 2103 C ATOM 3469 CD1 PHE A 444 14.120 4.257 33.043 1.00 67.31 C ANISOU 3469 CD1 PHE A 444 7839 5071 12666 215 -1038 1999 C ATOM 3470 CD2 PHE A 444 16.315 3.325 33.074 1.00 71.38 C ANISOU 3470 CD2 PHE A 444 8269 5362 13490 616 -1166 1877 C ATOM 3471 CE1 PHE A 444 14.449 5.027 31.949 1.00 62.36 C ANISOU 3471 CE1 PHE A 444 7138 4515 12043 290 -975 1695 C ATOM 3472 CE2 PHE A 444 16.655 4.094 31.978 1.00 69.79 C ANISOU 3472 CE2 PHE A 444 7972 5256 13290 690 -1080 1557 C ATOM 3473 CZ PHE A 444 15.718 4.948 31.413 1.00 68.33 C ANISOU 3473 CZ PHE A 444 7805 5209 12948 529 -985 1473 C ATOM 3474 N TYR A 445 15.359 0.078 33.341 1.00 85.04 N ANISOU 3474 N TYR A 445 10217 6274 15820 487 -1278 2022 N ATOM 3475 CA TYR A 445 15.921 -0.717 32.274 1.00 85.53 C ANISOU 3475 CA TYR A 445 10246 6042 16210 630 -1291 1662 C ATOM 3476 C TYR A 445 16.774 -1.802 32.906 1.00 88.10 C ANISOU 3476 C TYR A 445 10603 6118 16752 807 -1405 1814 C ATOM 3477 O TYR A 445 17.974 -1.618 33.097 1.00 83.99 O ANISOU 3477 O TYR A 445 10000 5680 16231 1038 -1456 1796 O ATOM 3478 CB TYR A 445 16.750 0.150 31.328 1.00 82.18 C ANISOU 3478 CB TYR A 445 9694 5796 15734 798 -1227 1319 C ATOM 3479 CG TYR A 445 17.192 -0.612 30.115 1.00 85.56 C ANISOU 3479 CG TYR A 445 10092 5966 16451 933 -1201 890 C ATOM 3480 CD1 TYR A 445 16.265 -1.060 29.185 1.00 88.29 C ANISOU 3480 CD1 TYR A 445 10501 6132 16913 788 -1163 622 C ATOM 3481 CD2 TYR A 445 18.529 -0.912 29.908 1.00 86.41 C ANISOU 3481 CD2 TYR A 445 10103 6023 16706 1207 -1218 733 C ATOM 3482 CE1 TYR A 445 16.658 -1.778 28.076 1.00 94.49 C ANISOU 3482 CE1 TYR A 445 11274 6701 17927 917 -1141 196 C ATOM 3483 CE2 TYR A 445 18.935 -1.626 28.801 1.00 90.01 C ANISOU 3483 CE2 TYR A 445 10532 6267 17401 1342 -1175 320 C ATOM 3484 CZ TYR A 445 17.995 -2.062 27.888 1.00 95.02 C ANISOU 3484 CZ TYR A 445 11251 6730 18121 1199 -1136 47 C ATOM 3485 OH TYR A 445 18.394 -2.781 26.782 1.00 94.03 O ANISOU 3485 OH TYR A 445 11113 6416 18198 1338 -1093 -394 O ATOM 3486 N PRO A 446 16.141 -2.944 33.230 1.00 92.32 N ANISOU 3486 N PRO A 446 11252 6340 17484 697 -1445 1964 N ATOM 3487 CA PRO A 446 16.712 -4.063 33.997 1.00 96.13 C ANISOU 3487 CA PRO A 446 11810 6547 18170 827 -1558 2196 C ATOM 3488 C PRO A 446 18.150 -4.498 33.671 1.00 96.27 C ANISOU 3488 C PRO A 446 11745 6429 18405 1147 -1636 2003 C ATOM 3489 O PRO A 446 18.878 -4.816 34.614 1.00 96.40 O ANISOU 3489 O PRO A 446 11786 6420 18422 1299 -1745 2274 O ATOM 3490 CB PRO A 446 15.710 -5.215 33.768 1.00 97.55 C ANISOU 3490 CB PRO A 446 12097 6349 18619 640 -1550 2196 C ATOM 3491 CG PRO A 446 14.720 -4.711 32.749 1.00 83.94 C ANISOU 3491 CG PRO A 446 10333 4713 16847 437 -1448 1897 C ATOM 3492 CD PRO A 446 14.747 -3.216 32.841 1.00 89.40 C ANISOU 3492 CD PRO A 446 10945 5860 17164 421 -1381 1917 C ATOM 3493 N PRO A 447 18.562 -4.515 32.385 1.00 97.35 N ANISOU 3493 N PRO A 447 11786 6496 18708 1258 -1578 1542 N ATOM 3494 CA PRO A 447 19.952 -4.936 32.154 1.00 95.34 C ANISOU 3494 CA PRO A 447 11432 6140 18653 1572 -1634 1372 C ATOM 3495 C PRO A 447 20.985 -3.913 32.640 1.00 88.23 C ANISOU 3495 C PRO A 447 10393 5606 17523 1736 -1654 1457 C ATOM 3496 O PRO A 447 22.187 -4.171 32.555 1.00 88.70 O ANISOU 3496 O PRO A 447 10340 5632 17730 1997 -1702 1343 O ATOM 3497 CB PRO A 447 20.031 -5.075 30.627 1.00 92.79 C ANISOU 3497 CB PRO A 447 11042 5720 18495 1629 -1527 834 C ATOM 3498 CG PRO A 447 18.614 -5.192 30.168 1.00 95.21 C ANISOU 3498 CG PRO A 447 11457 5929 18789 1344 -1475 761 C ATOM 3499 CD PRO A 447 17.829 -4.349 31.115 1.00 93.24 C ANISOU 3499 CD PRO A 447 11252 5948 18227 1128 -1470 1151 C ATOM 3500 N LEU A 448 20.523 -2.774 33.145 1.00 81.19 N ANISOU 3500 N LEU A 448 9501 5063 16286 1584 -1620 1645 N ATOM 3501 CA LEU A 448 21.424 -1.747 33.646 1.00 83.52 C ANISOU 3501 CA LEU A 448 9667 5714 16353 1709 -1649 1723 C ATOM 3502 C LEU A 448 21.097 -1.337 35.076 1.00 81.34 C ANISOU 3502 C LEU A 448 9484 5637 15782 1608 -1740 2174 C ATOM 3503 O LEU A 448 21.421 -0.215 35.483 1.00 79.92 O ANISOU 3503 O LEU A 448 9226 5814 15326 1614 -1744 2236 O ATOM 3504 CB LEU A 448 21.403 -0.512 32.735 1.00 80.64 C ANISOU 3504 CB LEU A 448 9178 5642 15820 1665 -1501 1433 C ATOM 3505 CG LEU A 448 21.895 -0.678 31.294 1.00 80.27 C ANISOU 3505 CG LEU A 448 9019 5504 15977 1797 -1378 950 C ATOM 3506 CD1 LEU A 448 21.786 0.637 30.522 1.00 76.05 C ANISOU 3506 CD1 LEU A 448 8386 5286 15222 1737 -1220 728 C ATOM 3507 CD2 LEU A 448 23.323 -1.186 31.259 1.00 82.56 C ANISOU 3507 CD2 LEU A 448 9166 5726 16478 2087 -1429 830 C ATOM 3508 N GLU A 449 20.467 -2.240 35.830 1.00 81.14 N ANISOU 3508 N GLU A 449 9630 5390 15810 1517 -1805 2474 N ATOM 3509 CA GLU A 449 20.120 -1.958 37.223 1.00 95.32 C ANISOU 3509 CA GLU A 449 11539 7374 17302 1429 -1873 2902 C ATOM 3510 C GLU A 449 21.332 -1.477 38.031 1.00 91.55 C ANISOU 3510 C GLU A 449 10980 7135 16670 1648 -2011 3018 C ATOM 3511 O GLU A 449 21.232 -0.489 38.772 1.00 86.53 O ANISOU 3511 O GLU A 449 10349 6851 15678 1585 -2024 3176 O ATOM 3512 CB GLU A 449 19.479 -3.170 37.904 1.00 95.85 C ANISOU 3512 CB GLU A 449 11796 7126 17496 1345 -1918 3208 C ATOM 3513 CG GLU A 449 18.972 -2.853 39.304 1.00 99.60 C ANISOU 3513 CG GLU A 449 12408 7824 17614 1234 -1945 3640 C ATOM 3514 CD GLU A 449 18.712 -4.082 40.148 1.00107.86 C ANISOU 3514 CD GLU A 449 13638 8565 18779 1227 -2013 3989 C ATOM 3515 OE1 GLU A 449 19.202 -4.113 41.298 1.00112.26 O ANISOU 3515 OE1 GLU A 449 14278 9233 19143 1347 -2131 4297 O ATOM 3516 OE2 GLU A 449 18.013 -5.002 39.671 1.00108.13 O ANISOU 3516 OE2 GLU A 449 13740 8252 19093 1102 -1954 3955 O ATOM 3517 N GLY A 450 22.467 -2.159 37.866 1.00 85.10 N ANISOU 3517 N GLY A 450 10079 6133 16123 1908 -2115 2914 N ATOM 3518 CA GLY A 450 23.712 -1.754 38.496 1.00 86.04 C ANISOU 3518 CA GLY A 450 10078 6465 16148 2136 -2259 2967 C ATOM 3519 C GLY A 450 24.065 -0.297 38.251 1.00 84.10 C ANISOU 3519 C GLY A 450 9661 6631 15661 2111 -2202 2785 C ATOM 3520 O GLY A 450 24.338 0.444 39.195 1.00 82.36 O ANISOU 3520 O GLY A 450 9435 6713 15146 2124 -2298 2965 O ATOM 3521 N HIS A 451 24.056 0.120 36.987 1.00 83.51 N ANISOU 3521 N HIS A 451 9456 6570 15705 2078 -2045 2422 N ATOM 3522 CA HIS A 451 24.343 1.511 36.634 1.00 79.73 C ANISOU 3522 CA HIS A 451 8817 6455 15024 2041 -1964 2241 C ATOM 3523 C HIS A 451 23.327 2.481 37.237 1.00 77.12 C ANISOU 3523 C HIS A 451 8599 6390 14314 1806 -1926 2441 C ATOM 3524 O HIS A 451 23.696 3.539 37.756 1.00 68.94 O ANISOU 3524 O HIS A 451 7486 5683 13024 1805 -1969 2481 O ATOM 3525 CB HIS A 451 24.361 1.693 35.117 1.00 72.79 C ANISOU 3525 CB HIS A 451 7814 5516 14326 2039 -1775 1832 C ATOM 3526 CG HIS A 451 25.600 1.181 34.457 1.00 75.74 C ANISOU 3526 CG HIS A 451 8004 5778 14998 2290 -1770 1557 C ATOM 3527 ND1 HIS A 451 25.776 -0.146 34.127 1.00 79.89 N ANISOU 3527 ND1 HIS A 451 8575 5935 15845 2419 -1800 1480 N ATOM 3528 CD2 HIS A 451 26.719 1.822 34.046 1.00 75.65 C ANISOU 3528 CD2 HIS A 451 7749 5979 15016 2432 -1722 1330 C ATOM 3529 CE1 HIS A 451 26.951 -0.302 33.548 1.00 82.02 C ANISOU 3529 CE1 HIS A 451 8640 6205 16318 2644 -1771 1213 C ATOM 3530 NE2 HIS A 451 27.546 0.877 33.491 1.00 82.12 N ANISOU 3530 NE2 HIS A 451 8468 6577 16158 2649 -1717 1123 N ATOM 3531 N VAL A 452 22.051 2.120 37.161 1.00 70.23 N ANISOU 3531 N VAL A 452 7897 5375 13411 1605 -1844 2549 N ATOM 3532 CA VAL A 452 20.995 2.975 37.687 1.00 71.53 C ANISOU 3532 CA VAL A 452 8164 5786 13229 1380 -1784 2728 C ATOM 3533 C VAL A 452 21.144 3.118 39.196 1.00 74.17 C ANISOU 3533 C VAL A 452 8594 6311 13278 1404 -1924 3068 C ATOM 3534 O VAL A 452 21.050 4.229 39.730 1.00 68.81 O ANISOU 3534 O VAL A 452 7901 5970 12274 1341 -1926 3123 O ATOM 3535 CB VAL A 452 19.601 2.442 37.317 1.00 71.67 C ANISOU 3535 CB VAL A 452 8323 5606 13304 1160 -1668 2772 C ATOM 3536 CG1 VAL A 452 18.516 3.339 37.886 1.00 68.47 C ANISOU 3536 CG1 VAL A 452 7999 5480 12536 939 -1591 2951 C ATOM 3537 CG2 VAL A 452 19.474 2.348 35.817 1.00 67.38 C ANISOU 3537 CG2 VAL A 452 7697 4895 13010 1152 -1548 2402 C ATOM 3538 N ARG A 453 21.389 1.992 39.870 1.00 80.83 N ANISOU 3538 N ARG A 453 9541 6931 14241 1506 -2042 3284 N ATOM 3539 CA ARG A 453 21.692 1.999 41.299 1.00 75.45 C ANISOU 3539 CA ARG A 453 8960 6409 13299 1581 -2197 3600 C ATOM 3540 C ARG A 453 22.844 2.950 41.586 1.00 78.59 C ANISOU 3540 C ARG A 453 9193 7114 13555 1743 -2318 3485 C ATOM 3541 O ARG A 453 22.750 3.797 42.475 1.00 83.66 O ANISOU 3541 O ARG A 453 9877 8074 13834 1701 -2371 3610 O ATOM 3542 CB ARG A 453 22.024 0.591 41.809 1.00 80.96 C ANISOU 3542 CB ARG A 453 9771 6780 14210 1724 -2322 3817 C ATOM 3543 CG ARG A 453 22.417 0.550 43.278 1.00 84.09 C ANISOU 3543 CG ARG A 453 10284 7338 14328 1839 -2499 4149 C ATOM 3544 CD ARG A 453 21.996 -0.747 43.963 1.00119.28 C ANISOU 3544 CD ARG A 453 14960 11492 18868 1845 -2543 4490 C ATOM 3545 NE ARG A 453 21.137 -0.489 45.119 1.00125.09 N ANISOU 3545 NE ARG A 453 15898 12433 19198 1698 -2512 4821 N ATOM 3546 CZ ARG A 453 19.915 -0.990 45.277 1.00127.51 C ANISOU 3546 CZ ARG A 453 16368 12601 19481 1476 -2364 5016 C ATOM 3547 NH1 ARG A 453 19.398 -1.796 44.358 1.00123.44 N ANISOU 3547 NH1 ARG A 453 15842 11723 19335 1371 -2257 4911 N ATOM 3548 NH2 ARG A 453 19.212 -0.690 46.362 1.00130.92 N ANISOU 3548 NH2 ARG A 453 16967 13259 19518 1359 -2320 5302 N ATOM 3549 N GLN A 454 23.918 2.825 40.813 1.00 75.11 N ANISOU 3549 N GLN A 454 8553 6584 13402 1922 -2352 3223 N ATOM 3550 CA GLN A 454 25.064 3.711 40.974 1.00 75.93 C ANISOU 3550 CA GLN A 454 8454 6969 13426 2062 -2454 3078 C ATOM 3551 C GLN A 454 24.680 5.180 40.763 1.00 69.74 C ANISOU 3551 C GLN A 454 7603 6515 12378 1893 -2347 2945 C ATOM 3552 O GLN A 454 25.140 6.059 41.488 1.00 79.71 O ANISOU 3552 O GLN A 454 8810 8081 13396 1921 -2455 2969 O ATOM 3553 CB GLN A 454 26.213 3.304 40.046 1.00 77.56 C ANISOU 3553 CB GLN A 454 8433 7022 14014 2264 -2457 2793 C ATOM 3554 CG GLN A 454 27.524 3.989 40.391 1.00 86.63 C ANISOU 3554 CG GLN A 454 9355 8436 15125 2431 -2594 2686 C ATOM 3555 CD GLN A 454 27.808 3.984 41.893 1.00 96.77 C ANISOU 3555 CD GLN A 454 10737 9885 16145 2521 -2834 2985 C ATOM 3556 OE1 GLN A 454 27.890 5.047 42.526 1.00 95.38 O ANISOU 3556 OE1 GLN A 454 10532 10044 15663 2464 -2901 3003 O ATOM 3557 NE2 GLN A 454 27.954 2.788 42.469 1.00 84.26 N ANISOU 3557 NE2 GLN A 454 9279 8063 14672 2671 -2969 3215 N ATOM 3558 N GLY A 455 23.815 5.430 39.784 1.00 70.39 N ANISOU 3558 N GLY A 455 7699 6530 12514 1723 -2145 2802 N ATOM 3559 CA GLY A 455 23.342 6.775 39.502 1.00 63.65 C ANISOU 3559 CA GLY A 455 6799 5952 11431 1565 -2031 2690 C ATOM 3560 C GLY A 455 22.586 7.393 40.664 1.00 67.44 C ANISOU 3560 C GLY A 455 7440 6682 11503 1434 -2074 2935 C ATOM 3561 O GLY A 455 22.857 8.537 41.056 1.00 64.89 O ANISOU 3561 O GLY A 455 7049 6662 10945 1415 -2115 2880 O ATOM 3562 N VAL A 456 21.638 6.638 41.214 1.00 62.72 N ANISOU 3562 N VAL A 456 7051 5958 10823 1341 -2053 3189 N ATOM 3563 CA VAL A 456 20.849 7.123 42.338 1.00 68.61 C ANISOU 3563 CA VAL A 456 7958 6942 11168 1221 -2058 3422 C ATOM 3564 C VAL A 456 21.746 7.369 43.544 1.00 64.96 C ANISOU 3564 C VAL A 456 7503 6692 10487 1380 -2272 3535 C ATOM 3565 O VAL A 456 21.601 8.374 44.242 1.00 63.77 O ANISOU 3565 O VAL A 456 7380 6856 9993 1332 -2304 3551 O ATOM 3566 CB VAL A 456 19.689 6.164 42.684 1.00 72.04 C ANISOU 3566 CB VAL A 456 8595 7189 11588 1087 -1970 3676 C ATOM 3567 CG1 VAL A 456 18.962 6.615 43.948 1.00 69.71 C ANISOU 3567 CG1 VAL A 456 8462 7164 10859 988 -1961 3920 C ATOM 3568 CG2 VAL A 456 18.713 6.087 41.519 1.00 64.49 C ANISOU 3568 CG2 VAL A 456 7618 6074 10811 910 -1773 3534 C ATOM 3569 N PHE A 457 22.699 6.470 43.765 1.00 68.69 N ANISOU 3569 N PHE A 457 7944 6993 11161 1583 -2431 3591 N ATOM 3570 CA PHE A 457 23.664 6.661 44.836 1.00 71.53 C ANISOU 3570 CA PHE A 457 8286 7551 11343 1766 -2665 3676 C ATOM 3571 C PHE A 457 24.522 7.920 44.631 1.00 73.00 C ANISOU 3571 C PHE A 457 8246 8017 11474 1809 -2729 3401 C ATOM 3572 O PHE A 457 24.699 8.709 45.556 1.00 76.13 O ANISOU 3572 O PHE A 457 8665 8713 11547 1825 -2853 3433 O ATOM 3573 CB PHE A 457 24.549 5.419 45.005 1.00 78.78 C ANISOU 3573 CB PHE A 457 9189 8213 12530 1996 -2824 3779 C ATOM 3574 CG PHE A 457 25.156 5.298 46.369 1.00 93.73 C ANISOU 3574 CG PHE A 457 11167 10273 14174 2172 -3069 3997 C ATOM 3575 CD1 PHE A 457 24.358 5.006 47.465 1.00102.82 C ANISOU 3575 CD1 PHE A 457 12589 11482 14997 2114 -3085 4322 C ATOM 3576 CD2 PHE A 457 26.519 5.475 46.563 1.00 98.16 C ANISOU 3576 CD2 PHE A 457 11530 10949 14819 2398 -3281 3875 C ATOM 3577 CE1 PHE A 457 24.907 4.891 48.733 1.00111.39 C ANISOU 3577 CE1 PHE A 457 13774 12734 15815 2295 -3319 4526 C ATOM 3578 CE2 PHE A 457 27.077 5.359 47.834 1.00105.33 C ANISOU 3578 CE2 PHE A 457 12514 12029 15479 2579 -3531 4074 C ATOM 3579 CZ PHE A 457 26.267 5.067 48.917 1.00111.58 C ANISOU 3579 CZ PHE A 457 13604 12874 15918 2535 -3555 4400 C ATOM 3580 N SER A 458 25.042 8.113 43.422 1.00 71.38 N ANISOU 3580 N SER A 458 7824 7716 11583 1822 -2639 3122 N ATOM 3581 CA SER A 458 25.848 9.297 43.132 1.00 68.16 C ANISOU 3581 CA SER A 458 7182 7550 11166 1835 -2667 2858 C ATOM 3582 C SER A 458 25.048 10.581 43.316 1.00 66.86 C ANISOU 3582 C SER A 458 7076 7648 10679 1641 -2581 2818 C ATOM 3583 O SER A 458 25.579 11.570 43.822 1.00 67.07 O ANISOU 3583 O SER A 458 7007 7944 10534 1653 -2695 2717 O ATOM 3584 CB SER A 458 26.422 9.237 41.717 1.00 65.80 C ANISOU 3584 CB SER A 458 6657 7093 11252 1866 -2529 2575 C ATOM 3585 OG SER A 458 27.302 8.140 41.572 1.00 78.39 O ANISOU 3585 OG SER A 458 8165 8473 13149 2072 -2618 2569 O ATOM 3586 N SER A 459 23.780 10.556 42.901 1.00 59.59 N ANISOU 3586 N SER A 459 6303 6645 9692 1464 -2387 2886 N ATOM 3587 CA SER A 459 22.882 11.692 43.080 1.00 58.93 C ANISOU 3587 CA SER A 459 6293 6794 9303 1287 -2290 2869 C ATOM 3588 C SER A 459 22.754 12.044 44.554 1.00 58.35 C ANISOU 3588 C SER A 459 6364 6977 8831 1307 -2442 3035 C ATOM 3589 O SER A 459 22.941 13.193 44.946 1.00 73.42 O ANISOU 3589 O SER A 459 8218 9151 10526 1279 -2504 2912 O ATOM 3590 CB SER A 459 21.485 11.381 42.521 1.00 55.68 C ANISOU 3590 CB SER A 459 6024 6243 8889 1113 -2072 2956 C ATOM 3591 OG SER A 459 21.536 11.045 41.154 1.00 56.21 O ANISOU 3591 OG SER A 459 5979 6080 9296 1104 -1941 2788 O ATOM 3592 N LEU A 460 22.421 11.035 45.356 1.00 61.38 N ANISOU 3592 N LEU A 460 6936 7268 9117 1355 -2496 3307 N ATOM 3593 CA LEU A 460 22.255 11.191 46.795 1.00 67.80 C ANISOU 3593 CA LEU A 460 7922 8311 9528 1395 -2628 3494 C ATOM 3594 C LEU A 460 23.522 11.704 47.477 1.00 66.12 C ANISOU 3594 C LEU A 460 7588 8310 9224 1573 -2896 3383 C ATOM 3595 O LEU A 460 23.476 12.703 48.199 1.00 72.01 O ANISOU 3595 O LEU A 460 8363 9353 9646 1551 -2977 3313 O ATOM 3596 CB LEU A 460 21.797 9.870 47.422 1.00 70.70 C ANISOU 3596 CB LEU A 460 8502 8495 9868 1430 -2631 3821 C ATOM 3597 CG LEU A 460 20.347 9.502 47.101 1.00 71.98 C ANISOU 3597 CG LEU A 460 8803 8530 10015 1217 -2375 3955 C ATOM 3598 CD1 LEU A 460 19.987 8.150 47.690 1.00 71.63 C ANISOU 3598 CD1 LEU A 460 8948 8271 9996 1243 -2379 4277 C ATOM 3599 CD2 LEU A 460 19.395 10.580 47.605 1.00 63.87 C ANISOU 3599 CD2 LEU A 460 7862 7812 8593 1065 -2258 3943 C ATOM 3600 N ASN A 461 24.643 11.023 47.246 1.00 68.49 N ANISOU 3600 N ASN A 461 7743 8463 9818 1753 -3036 3350 N ATOM 3601 CA ASN A 461 25.938 11.479 47.736 1.00 70.76 C ANISOU 3601 CA ASN A 461 7850 8945 10091 1923 -3288 3211 C ATOM 3602 C ASN A 461 26.215 12.939 47.391 1.00 75.96 C ANISOU 3602 C ASN A 461 8317 9834 10710 1820 -3272 2905 C ATOM 3603 O ASN A 461 26.666 13.706 48.238 1.00 75.37 O ANISOU 3603 O ASN A 461 8206 10041 10392 1869 -3460 2825 O ATOM 3604 CB ASN A 461 27.060 10.624 47.152 1.00 80.29 C ANISOU 3604 CB ASN A 461 8857 9934 11716 2100 -3366 3154 C ATOM 3605 CG ASN A 461 27.207 9.285 47.849 1.00 87.37 C ANISOU 3605 CG ASN A 461 9910 10663 12623 2280 -3501 3449 C ATOM 3606 OD1 ASN A 461 26.812 9.122 49.005 1.00 95.33 O ANISOU 3606 OD1 ASN A 461 11144 11796 13280 2318 -3609 3687 O ATOM 3607 ND2 ASN A 461 27.796 8.318 47.150 1.00 87.28 N ANISOU 3607 ND2 ASN A 461 9785 10365 13014 2400 -3492 3432 N ATOM 3608 N HIS A 462 25.946 13.325 46.147 1.00 64.04 N ANISOU 3608 N HIS A 462 6689 8204 9441 1679 -3054 2730 N ATOM 3609 CA HIS A 462 26.347 14.647 45.685 1.00 68.68 C ANISOU 3609 CA HIS A 462 7069 8959 10066 1585 -3029 2441 C ATOM 3610 C HIS A 462 25.441 15.706 46.288 1.00 64.73 C ANISOU 3610 C HIS A 462 6720 8693 9183 1444 -3006 2433 C ATOM 3611 O HIS A 462 25.864 16.836 46.528 1.00 63.07 O ANISOU 3611 O HIS A 462 6388 8696 8882 1405 -3099 2230 O ATOM 3612 CB HIS A 462 26.353 14.730 44.150 1.00 58.68 C ANISOU 3612 CB HIS A 462 5642 7495 9157 1493 -2794 2267 C ATOM 3613 CG HIS A 462 27.230 15.804 43.604 1.00 57.78 C ANISOU 3613 CG HIS A 462 5251 7499 9205 1447 -2787 1975 C ATOM 3614 ND1 HIS A 462 28.572 15.922 43.942 1.00 69.23 N ANISOU 3614 ND1 HIS A 462 6472 9052 10780 1566 -2972 1849 N ATOM 3615 CD2 HIS A 462 26.986 16.827 42.756 1.00 60.63 C ANISOU 3615 CD2 HIS A 462 5517 7890 9631 1285 -2611 1788 C ATOM 3616 CE1 HIS A 462 29.094 16.954 43.327 1.00 59.48 C ANISOU 3616 CE1 HIS A 462 5015 7897 9689 1458 -2895 1599 C ATOM 3617 NE2 HIS A 462 28.146 17.529 42.590 1.00 63.34 N ANISOU 3617 NE2 HIS A 462 5587 8335 10142 1289 -2672 1561 N ATOM 3618 N ILE A 463 24.192 15.318 46.542 1.00 65.14 N ANISOU 3618 N ILE A 463 7026 8700 9023 1362 -2875 2646 N ATOM 3619 CA ILE A 463 23.222 16.174 47.215 1.00 65.71 C ANISOU 3619 CA ILE A 463 7267 8999 8700 1247 -2832 2667 C ATOM 3620 C ILE A 463 23.698 16.508 48.638 1.00 66.63 C ANISOU 3620 C ILE A 463 7456 9388 8473 1366 -3097 2676 C ATOM 3621 O ILE A 463 23.459 17.603 49.143 1.00 65.48 O ANISOU 3621 O ILE A 463 7339 9482 8057 1305 -3145 2537 O ATOM 3622 CB ILE A 463 21.827 15.510 47.210 1.00 67.20 C ANISOU 3622 CB ILE A 463 7689 9080 8765 1140 -2616 2911 C ATOM 3623 CG1 ILE A 463 21.152 15.741 45.857 1.00 57.39 C ANISOU 3623 CG1 ILE A 463 6371 7683 7751 986 -2364 2815 C ATOM 3624 CG2 ILE A 463 20.941 16.043 48.326 1.00 68.89 C ANISOU 3624 CG2 ILE A 463 8112 9553 8509 1082 -2605 3002 C ATOM 3625 CD1 ILE A 463 20.050 14.754 45.551 1.00 52.65 C ANISOU 3625 CD1 ILE A 463 5920 6886 7199 900 -2168 3028 C ATOM 3626 N VAL A 464 24.405 15.579 49.269 1.00 75.19 N ANISOU 3626 N VAL A 464 8566 10435 9568 1549 -3284 2823 N ATOM 3627 CA VAL A 464 24.982 15.842 50.586 1.00 78.96 C ANISOU 3627 CA VAL A 464 9097 11179 9724 1695 -3569 2821 C ATOM 3628 C VAL A 464 26.238 16.714 50.473 1.00 81.16 C ANISOU 3628 C VAL A 464 9070 11617 10150 1750 -3762 2511 C ATOM 3629 O VAL A 464 26.389 17.701 51.200 1.00 81.05 O ANISOU 3629 O VAL A 464 9046 11882 9866 1746 -3916 2342 O ATOM 3630 CB VAL A 464 25.313 14.534 51.339 1.00 76.93 C ANISOU 3630 CB VAL A 464 8978 10838 9414 1891 -3717 3110 C ATOM 3631 CG1 VAL A 464 25.910 14.835 52.714 1.00 78.10 C ANISOU 3631 CG1 VAL A 464 9193 11291 9192 2064 -4032 3102 C ATOM 3632 CG2 VAL A 464 24.068 13.675 51.473 1.00 73.57 C ANISOU 3632 CG2 VAL A 464 8838 10249 8867 1801 -3507 3422 C ATOM 3633 N GLU A 465 27.132 16.343 49.560 1.00 77.53 N ANISOU 3633 N GLU A 465 8353 10979 10125 1790 -3744 2424 N ATOM 3634 CA GLU A 465 28.369 17.085 49.351 1.00 78.52 C ANISOU 3634 CA GLU A 465 8147 11232 10454 1808 -3882 2146 C ATOM 3635 C GLU A 465 28.128 18.553 48.995 1.00 77.96 C ANISOU 3635 C GLU A 465 7980 11289 10354 1604 -3799 1873 C ATOM 3636 O GLU A 465 28.942 19.409 49.334 1.00 77.83 O ANISOU 3636 O GLU A 465 7761 11475 10336 1585 -3963 1657 O ATOM 3637 CB GLU A 465 29.224 16.412 48.277 1.00 84.56 C ANISOU 3637 CB GLU A 465 8670 11749 11711 1860 -3804 2098 C ATOM 3638 CG GLU A 465 29.913 15.141 48.749 1.00100.04 C ANISOU 3638 CG GLU A 465 10630 13630 13753 2099 -3975 2296 C ATOM 3639 CD GLU A 465 31.013 15.422 49.754 1.00117.70 C ANISOU 3639 CD GLU A 465 12702 16151 15868 2244 -4294 2236 C ATOM 3640 OE1 GLU A 465 31.227 14.591 50.664 1.00126.79 O ANISOU 3640 OE1 GLU A 465 13970 17352 16852 2447 -4491 2460 O ATOM 3641 OE2 GLU A 465 31.669 16.479 49.630 1.00122.60 O ANISOU 3641 OE2 GLU A 465 13072 16943 16566 2145 -4349 1972 O ATOM 3642 N LYS A 466 27.013 18.849 48.327 1.00 67.71 N ANISOU 3642 N LYS A 466 6816 9871 9040 1442 -3548 1889 N ATOM 3643 CA LYS A 466 26.730 20.232 47.952 1.00 69.80 C ANISOU 3643 CA LYS A 466 7003 10227 9292 1257 -3466 1646 C ATOM 3644 C LYS A 466 25.837 20.960 48.963 1.00 72.01 C ANISOU 3644 C LYS A 466 7512 10741 9106 1214 -3533 1641 C ATOM 3645 O LYS A 466 25.481 22.122 48.747 1.00 71.51 O ANISOU 3645 O LYS A 466 7417 10751 9002 1066 -3477 1445 O ATOM 3646 CB LYS A 466 26.110 20.319 46.549 1.00 69.04 C ANISOU 3646 CB LYS A 466 6878 9894 9460 1109 -3160 1629 C ATOM 3647 CG LYS A 466 26.901 19.603 45.457 1.00 79.90 C ANISOU 3647 CG LYS A 466 8047 11037 11274 1155 -3056 1604 C ATOM 3648 CD LYS A 466 28.329 20.111 45.324 1.00 89.01 C ANISOU 3648 CD LYS A 466 8883 12256 12680 1172 -3175 1368 C ATOM 3649 CE LYS A 466 28.462 21.167 44.229 1.00 88.45 C ANISOU 3649 CE LYS A 466 8631 12122 12854 986 -2978 1135 C ATOM 3650 NZ LYS A 466 29.902 21.510 43.982 1.00 96.34 N ANISOU 3650 NZ LYS A 466 9306 13150 14150 985 -3040 928 N ATOM 3651 N ARG A 467 25.489 20.282 50.057 1.00 76.04 N ANISOU 3651 N ARG A 467 8261 11359 9273 1346 -3648 1850 N ATOM 3652 CA ARG A 467 24.604 20.840 51.091 1.00 79.51 C ANISOU 3652 CA ARG A 467 8961 12014 9235 1323 -3695 1856 C ATOM 3653 C ARG A 467 23.194 21.228 50.591 1.00 79.36 C ANISOU 3653 C ARG A 467 9097 11938 9117 1142 -3399 1911 C ATOM 3654 O ARG A 467 22.534 22.087 51.184 1.00 77.52 O ANISOU 3654 O ARG A 467 8999 11894 8560 1075 -3399 1810 O ATOM 3655 CB ARG A 467 25.263 22.030 51.807 1.00 84.36 C ANISOU 3655 CB ARG A 467 9459 12911 9683 1336 -3947 1540 C ATOM 3656 CG ARG A 467 26.477 21.678 52.673 1.00 93.15 C ANISOU 3656 CG ARG A 467 10436 14234 10725 1527 -4245 1528 C ATOM 3657 CD ARG A 467 27.785 22.086 52.007 1.00 99.32 C ANISOU 3657 CD ARG A 467 10793 15016 11929 1439 -4299 1353 C ATOM 3658 NE ARG A 467 28.850 22.336 52.983 1.00107.38 N ANISOU 3658 NE ARG A 467 11633 16336 12830 1471 -4598 1305 N ATOM 3659 CZ ARG A 467 29.731 21.427 53.392 1.00109.13 C ANISOU 3659 CZ ARG A 467 11759 16600 13107 1656 -4778 1458 C ATOM 3660 NH1 ARG A 467 29.690 20.188 52.914 1.00106.06 N ANISOU 3660 NH1 ARG A 467 11447 15951 12901 1826 -4684 1661 N ATOM 3661 NH2 ARG A 467 30.656 21.758 54.283 1.00114.70 N ANISOU 3661 NH2 ARG A 467 12300 17566 13715 1637 -5075 1418 N ATOM 3662 N VAL A 468 22.730 20.598 49.512 1.00 72.05 N ANISOU 3662 N VAL A 468 8145 10767 8464 1069 -3147 2055 N ATOM 3663 CA VAL A 468 21.348 20.775 49.091 1.00 67.87 C ANISOU 3663 CA VAL A 468 7755 10210 7824 925 -2862 2147 C ATOM 3664 C VAL A 468 20.426 20.230 50.180 1.00 73.81 C ANISOU 3664 C VAL A 468 8791 11085 8167 952 -2810 2385 C ATOM 3665 O VAL A 468 19.399 20.828 50.502 1.00 81.27 O ANISOU 3665 O VAL A 468 9864 12189 8824 864 -2665 2370 O ATOM 3666 CB VAL A 468 21.054 20.091 47.750 1.00 65.10 C ANISOU 3666 CB VAL A 468 7325 9569 7841 857 -2630 2248 C ATOM 3667 CG1 VAL A 468 19.555 20.042 47.497 1.00 60.90 C ANISOU 3667 CG1 VAL A 468 6952 9029 7159 734 -2355 2384 C ATOM 3668 CG2 VAL A 468 21.751 20.833 46.611 1.00 59.52 C ANISOU 3668 CG2 VAL A 468 6359 8762 7495 794 -2613 2001 C ATOM 3669 N LEU A 469 20.808 19.086 50.735 1.00 77.31 N ANISOU 3669 N LEU A 469 9325 11454 8596 1076 -2916 2605 N ATOM 3670 CA LEU A 469 20.181 18.549 51.939 1.00 83.59 C ANISOU 3670 CA LEU A 469 10388 12375 8996 1117 -2916 2840 C ATOM 3671 C LEU A 469 21.282 17.951 52.802 1.00 85.92 C ANISOU 3671 C LEU A 469 10714 12701 9232 1316 -3231 2910 C ATOM 3672 O LEU A 469 21.887 16.945 52.429 1.00 86.12 O ANISOU 3672 O LEU A 469 10666 12512 9543 1412 -3281 3044 O ATOM 3673 CB LEU A 469 19.143 17.478 51.594 1.00 82.39 C ANISOU 3673 CB LEU A 469 10355 12032 8916 1030 -2638 3137 C ATOM 3674 CG LEU A 469 18.168 17.150 52.728 1.00 88.73 C ANISOU 3674 CG LEU A 469 11422 12993 9300 1002 -2533 3366 C ATOM 3675 CD1 LEU A 469 17.218 18.320 52.945 1.00 89.87 C ANISOU 3675 CD1 LEU A 469 11606 13393 9146 887 -2367 3203 C ATOM 3676 CD2 LEU A 469 17.386 15.869 52.460 1.00 88.94 C ANISOU 3676 CD2 LEU A 469 11536 12786 9470 928 -2314 3679 C ATOM 3677 N ALA A 470 21.548 18.574 53.947 1.00 87.93 N ANISOU 3677 N ALA A 470 11075 13217 9116 1387 -3455 2807 N ATOM 3678 CA ALA A 470 22.656 18.161 54.814 1.00 90.35 C ANISOU 3678 CA ALA A 470 11402 13590 9338 1596 -3808 2831 C ATOM 3679 C ALA A 470 22.569 16.711 55.302 1.00 96.56 C ANISOU 3679 C ALA A 470 12374 14245 10071 1710 -3809 3217 C ATOM 3680 O ALA A 470 23.570 15.986 55.311 1.00 94.20 O ANISOU 3680 O ALA A 470 11977 13848 9966 1894 -4008 3281 O ATOM 3681 CB ALA A 470 22.785 19.119 56.002 1.00 86.35 C ANISOU 3681 CB ALA A 470 11027 13375 8406 1610 -4056 2648 C ATOM 3682 N HIS A 471 21.377 16.299 55.722 1.00 97.76 N ANISOU 3682 N HIS A 471 12775 14406 9965 1603 -3576 3473 N ATOM 3683 CA HIS A 471 21.205 14.983 56.327 1.00 97.44 C ANISOU 3683 CA HIS A 471 12943 14249 9831 1687 -3574 3857 C ATOM 3684 C HIS A 471 20.094 14.175 55.647 1.00 94.63 C ANISOU 3684 C HIS A 471 12634 13659 9663 1523 -3205 4099 C ATOM 3685 O HIS A 471 18.961 14.654 55.481 1.00 91.58 O ANISOU 3685 O HIS A 471 12289 13356 9153 1336 -2926 4076 O ATOM 3686 CB HIS A 471 20.945 15.134 57.826 1.00 99.02 C ANISOU 3686 CB HIS A 471 13434 14717 9470 1731 -3703 3974 C ATOM 3687 CG HIS A 471 21.986 15.945 58.537 1.00105.36 C ANISOU 3687 CG HIS A 471 14208 15742 10083 1868 -4102 3713 C ATOM 3688 ND1 HIS A 471 23.163 15.402 59.006 1.00102.59 N ANISOU 3688 ND1 HIS A 471 13843 15366 9770 2108 -4467 3759 N ATOM 3689 CD2 HIS A 471 22.027 17.263 58.851 1.00108.19 C ANISOU 3689 CD2 HIS A 471 14534 16340 10234 1788 -4209 3389 C ATOM 3690 CE1 HIS A 471 23.885 16.350 59.579 1.00106.40 C ANISOU 3690 CE1 HIS A 471 14284 16057 10086 2158 -4800 3468 C ATOM 3691 NE2 HIS A 471 23.218 17.487 59.500 1.00107.91 N ANISOU 3691 NE2 HIS A 471 14469 16396 10137 1943 -4653 3246 N ATOM 3692 N LEU A 472 20.433 12.952 55.244 1.00 87.79 N ANISOU 3692 N LEU A 472 11745 12497 9115 1596 -3214 4311 N ATOM 3693 CA LEU A 472 19.491 12.088 54.539 1.00 87.39 C ANISOU 3693 CA LEU A 472 11719 12174 9310 1440 -2911 4515 C ATOM 3694 C LEU A 472 18.723 11.172 55.484 1.00 93.11 C ANISOU 3694 C LEU A 472 12724 12880 9775 1410 -2811 4897 C ATOM 3695 O LEU A 472 17.662 10.651 55.131 1.00 90.41 O ANISOU 3695 O LEU A 472 12427 12391 9534 1233 -2526 5057 O ATOM 3696 CB LEU A 472 20.206 11.256 53.474 1.00 84.79 C ANISOU 3696 CB LEU A 472 11208 11497 9512 1508 -2952 4506 C ATOM 3697 CG LEU A 472 20.432 11.942 52.127 1.00 83.56 C ANISOU 3697 CG LEU A 472 10778 11263 9707 1427 -2868 4187 C ATOM 3698 CD1 LEU A 472 20.763 10.931 51.047 1.00 86.10 C ANISOU 3698 CD1 LEU A 472 10974 11209 10531 1445 -2817 4222 C ATOM 3699 CD2 LEU A 472 19.211 12.750 51.733 1.00 75.22 C ANISOU 3699 CD2 LEU A 472 9729 10316 8534 1200 -2591 4089 C ATOM 3700 N ALA A 473 19.269 10.981 56.681 1.00 98.04 N ANISOU 3700 N ALA A 473 13531 13654 10067 1581 -3054 5040 N ATOM 3701 CA ALA A 473 18.657 10.118 57.690 1.00101.33 C ANISOU 3701 CA ALA A 473 14239 14068 10195 1570 -2985 5429 C ATOM 3702 C ALA A 473 17.227 10.515 58.107 1.00102.27 C ANISOU 3702 C ALA A 473 14491 14381 9987 1345 -2658 5505 C ATOM 3703 O ALA A 473 16.337 9.663 58.108 1.00100.13 O ANISOU 3703 O ALA A 473 14319 13950 9777 1212 -2415 5786 O ATOM 3704 CB ALA A 473 19.581 9.969 58.922 1.00100.27 C ANISOU 3704 CB ALA A 473 14288 14093 9716 1815 -3346 5543 C ATOM 3705 N PRO A 474 16.989 11.804 58.445 1.00105.09 N ANISOU 3705 N PRO A 474 14831 15079 10019 1298 -2643 5243 N ATOM 3706 CA PRO A 474 15.657 12.156 58.963 1.00110.43 C ANISOU 3706 CA PRO A 474 15630 15974 10356 1117 -2328 5317 C ATOM 3707 C PRO A 474 14.556 12.113 57.908 1.00111.65 C ANISOU 3707 C PRO A 474 15622 15979 10822 898 -1965 5283 C ATOM 3708 O PRO A 474 13.465 12.646 58.134 1.00119.93 O ANISOU 3708 O PRO A 474 16689 17232 11645 754 -1697 5248 O ATOM 3709 CB PRO A 474 15.843 13.600 59.457 1.00111.58 C ANISOU 3709 CB PRO A 474 15763 16494 10140 1150 -2439 4980 C ATOM 3710 CG PRO A 474 17.326 13.775 59.615 1.00111.65 C ANISOU 3710 CG PRO A 474 15730 16498 10195 1364 -2873 4831 C ATOM 3711 CD PRO A 474 17.909 12.955 58.513 1.00105.62 C ANISOU 3711 CD PRO A 474 14784 15358 9988 1414 -2916 4882 C ATOM 3712 N LEU A 475 14.840 11.492 56.769 1.00107.66 N ANISOU 3712 N LEU A 475 14952 15128 10827 881 -1965 5278 N ATOM 3713 CA LEU A 475 13.868 11.378 55.695 1.00105.32 C ANISOU 3713 CA LEU A 475 14501 14662 10855 680 -1668 5234 C ATOM 3714 C LEU A 475 13.385 9.941 55.634 1.00114.00 C ANISOU 3714 C LEU A 475 15687 15452 12176 599 -1542 5580 C ATOM 3715 O LEU A 475 12.409 9.625 54.954 1.00113.88 O ANISOU 3715 O LEU A 475 15585 15290 12394 412 -1288 5609 O ATOM 3716 CB LEU A 475 14.512 11.755 54.360 1.00 94.24 C ANISOU 3716 CB LEU A 475 12849 13084 9873 703 -1755 4945 C ATOM 3717 CG LEU A 475 13.760 12.743 53.466 1.00 89.41 C ANISOU 3717 CG LEU A 475 12062 12559 9351 554 -1547 4676 C ATOM 3718 CD1 LEU A 475 14.064 12.483 51.997 1.00 85.41 C ANISOU 3718 CD1 LEU A 475 11353 11745 9353 520 -1544 4540 C ATOM 3719 CD2 LEU A 475 12.265 12.698 53.725 1.00 91.55 C ANISOU 3719 CD2 LEU A 475 12388 12934 9464 370 -1225 4799 C ATOM 3720 N PHE A 476 14.090 9.071 56.350 1.00126.95 N ANISOU 3720 N PHE A 476 17499 16986 13753 746 -1740 5836 N ATOM 3721 CA PHE A 476 13.889 7.629 56.231 1.00133.13 C ANISOU 3721 CA PHE A 476 18364 17409 14811 705 -1682 6159 C ATOM 3722 C PHE A 476 13.334 7.017 57.522 1.00142.11 C ANISOU 3722 C PHE A 476 19782 18638 15574 675 -1597 6545 C ATOM 3723 O PHE A 476 12.981 5.836 57.557 1.00146.35 O ANISOU 3723 O PHE A 476 20417 18891 16297 606 -1507 6853 O ATOM 3724 CB PHE A 476 15.202 6.926 55.840 1.00127.57 C ANISOU 3724 CB PHE A 476 17617 16418 14436 914 -1976 6169 C ATOM 3725 CG PHE A 476 15.771 7.351 54.494 1.00115.83 C ANISOU 3725 CG PHE A 476 15853 14796 13363 934 -2035 5819 C ATOM 3726 CD1 PHE A 476 15.176 8.340 53.726 1.00109.62 C ANISOU 3726 CD1 PHE A 476 14892 14139 12619 783 -1861 5532 C ATOM 3727 CD2 PHE A 476 16.903 6.733 53.997 1.00112.99 C ANISOU 3727 CD2 PHE A 476 15406 14174 13349 1112 -2257 5787 C ATOM 3728 CE1 PHE A 476 15.708 8.719 52.501 1.00107.68 C ANISOU 3728 CE1 PHE A 476 14415 13768 12730 801 -1909 5236 C ATOM 3729 CE2 PHE A 476 17.436 7.101 52.769 1.00107.12 C ANISOU 3729 CE2 PHE A 476 14411 13315 12974 1127 -2291 5473 C ATOM 3730 CZ PHE A 476 16.838 8.096 52.022 1.00104.12 C ANISOU 3730 CZ PHE A 476 13882 13067 12611 966 -2116 5205 C ATOM 3731 N ASP A 477 13.263 7.823 58.577 1.00147.08 N ANISOU 3731 N ASP A 477 20548 19661 15674 723 -1624 6523 N ATOM 3732 CA ASP A 477 12.789 7.356 59.878 1.00156.23 C ANISOU 3732 CA ASP A 477 21993 20961 16404 705 -1546 6878 C ATOM 3733 C ASP A 477 11.626 8.204 60.398 1.00156.38 C ANISOU 3733 C ASP A 477 22036 21348 16035 539 -1249 6808 C ATOM 3734 O ASP A 477 11.081 7.931 61.470 1.00157.72 O ANISOU 3734 O ASP A 477 22430 21684 15812 494 -1123 7080 O ATOM 3735 CB ASP A 477 13.931 7.366 60.899 1.00164.74 C ANISOU 3735 CB ASP A 477 23277 22181 17136 964 -1910 6965 C ATOM 3736 CG ASP A 477 15.163 6.617 60.414 1.00168.21 C ANISOU 3736 CG ASP A 477 23664 22291 17958 1170 -2223 6998 C ATOM 3737 OD1 ASP A 477 15.020 5.687 59.593 1.00168.06 O ANISOU 3737 OD1 ASP A 477 23557 21888 18412 1103 -2129 7111 O ATOM 3738 OD2 ASP A 477 16.281 6.959 60.860 1.00170.43 O ANISOU 3738 OD2 ASP A 477 23982 22701 18072 1405 -2569 6895 O ATOM 3739 N ASN A 478 11.260 9.233 59.633 1.00154.24 N ANISOU 3739 N ASN A 478 21531 21203 15869 458 -1133 6444 N ATOM 3740 CA ASN A 478 10.189 10.154 60.011 1.00154.58 C ANISOU 3740 CA ASN A 478 21551 21597 15585 329 -856 6313 C ATOM 3741 C ASN A 478 8.909 9.415 60.414 1.00164.34 C ANISOU 3741 C ASN A 478 22872 22810 16759 128 -504 6629 C ATOM 3742 O ASN A 478 8.382 8.617 59.637 1.00165.11 O ANISOU 3742 O ASN A 478 22860 22594 17281 -19 -354 6745 O ATOM 3743 CB ASN A 478 9.917 11.135 58.864 1.00138.78 C ANISOU 3743 CB ASN A 478 19263 19621 13847 262 -769 5916 C ATOM 3744 CG ASN A 478 8.952 12.240 59.251 1.00135.56 C ANISOU 3744 CG ASN A 478 18816 19592 13099 181 -525 5724 C ATOM 3745 OD1 ASN A 478 7.737 12.068 59.181 1.00135.89 O ANISOU 3745 OD1 ASN A 478 18801 19659 13171 7 -201 5811 O ATOM 3746 ND2 ASN A 478 9.490 13.390 59.645 1.00133.13 N ANISOU 3746 ND2 ASN A 478 18522 19574 12487 309 -685 5441 N ATOM 3747 N PRO A 479 8.420 9.667 61.644 1.00169.50 N ANISOU 3747 N PRO A 479 23722 23799 16883 117 -375 6762 N ATOM 3748 CA PRO A 479 7.259 8.964 62.213 1.00172.98 C ANISOU 3748 CA PRO A 479 24269 24256 17201 -69 -35 7094 C ATOM 3749 C PRO A 479 5.977 9.145 61.396 1.00170.18 C ANISOU 3749 C PRO A 479 23657 23866 17138 -295 319 6969 C ATOM 3750 O PRO A 479 5.100 8.281 61.436 1.00174.78 O ANISOU 3750 O PRO A 479 24252 24297 17859 -481 570 7244 O ATOM 3751 CB PRO A 479 7.106 9.602 63.603 1.00175.77 C ANISOU 3751 CB PRO A 479 24843 25065 16878 -4 14 7123 C ATOM 3752 CG PRO A 479 7.790 10.924 63.500 1.00172.56 C ANISOU 3752 CG PRO A 479 24348 24909 16309 154 -205 6686 C ATOM 3753 CD PRO A 479 8.936 10.703 62.558 1.00169.49 C ANISOU 3753 CD PRO A 479 23844 24195 16358 274 -541 6571 C ATOM 3754 N LYS A 480 5.884 10.250 60.660 1.00160.93 N ANISOU 3754 N LYS A 480 22256 22824 16067 -279 325 6561 N ATOM 3755 CA LYS A 480 4.716 10.546 59.831 1.00152.83 C ANISOU 3755 CA LYS A 480 20972 21782 15312 -463 619 6401 C ATOM 3756 C LYS A 480 4.727 9.791 58.495 1.00149.20 C ANISOU 3756 C LYS A 480 20331 20881 15476 -561 578 6402 C ATOM 3757 O LYS A 480 4.021 10.178 57.557 1.00147.50 O ANISOU 3757 O LYS A 480 19876 20629 15538 -672 721 6186 O ATOM 3758 CB LYS A 480 4.612 12.059 59.567 1.00142.40 C ANISOU 3758 CB LYS A 480 19493 20768 13845 -390 631 5967 C ATOM 3759 CG LYS A 480 3.686 12.826 60.511 1.00139.96 C ANISOU 3759 CG LYS A 480 19222 20887 13070 -418 904 5901 C ATOM 3760 CD LYS A 480 4.065 12.637 61.975 1.00138.79 C ANISOU 3760 CD LYS A 480 19384 20970 12379 -325 848 6122 C ATOM 3761 CE LYS A 480 3.161 13.448 62.887 1.00136.48 C ANISOU 3761 CE LYS A 480 19125 21118 11613 -343 1131 6015 C ATOM 3762 NZ LYS A 480 3.586 13.350 64.309 1.00140.97 N ANISOU 3762 NZ LYS A 480 20014 21942 11607 -241 1056 6198 N ATOM 3763 N LEU A 481 5.522 8.723 58.407 1.00145.96 N ANISOU 3763 N LEU A 481 20039 20139 15280 -510 375 6632 N ATOM 3764 CA LEU A 481 5.623 7.942 57.169 1.00141.39 C ANISOU 3764 CA LEU A 481 19310 19126 15287 -587 317 6619 C ATOM 3765 C LEU A 481 4.832 6.637 57.252 1.00148.24 C ANISOU 3765 C LEU A 481 20231 19719 16375 -784 511 6966 C ATOM 3766 O LEU A 481 3.898 6.523 58.048 1.00153.83 O ANISOU 3766 O LEU A 481 21013 20602 16831 -915 772 7161 O ATOM 3767 CB LEU A 481 7.088 7.658 56.803 1.00136.44 C ANISOU 3767 CB LEU A 481 18729 18271 14841 -386 -46 6577 C ATOM 3768 CG LEU A 481 7.933 8.726 56.087 1.00125.55 C ANISOU 3768 CG LEU A 481 17199 16983 13523 -239 -255 6185 C ATOM 3769 CD1 LEU A 481 9.416 8.486 56.332 1.00123.90 C ANISOU 3769 CD1 LEU A 481 17104 16675 13296 -8 -608 6217 C ATOM 3770 CD2 LEU A 481 7.647 8.756 54.587 1.00115.29 C ANISOU 3770 CD2 LEU A 481 15646 15444 12716 -342 -204 5953 C ATOM 3771 N ASP A 482 5.208 5.660 56.430 1.00149.93 N ANISOU 3771 N ASP A 482 20404 19497 17064 -808 388 7032 N ATOM 3772 CA ASP A 482 4.452 4.409 56.315 1.00155.76 C ANISOU 3772 CA ASP A 482 21165 19914 18103 -1015 557 7316 C ATOM 3773 C ASP A 482 5.110 3.264 57.081 1.00157.27 C ANISOU 3773 C ASP A 482 21630 19872 18254 -937 425 7715 C ATOM 3774 O ASP A 482 6.324 3.247 57.248 1.00155.65 O ANISOU 3774 O ASP A 482 21536 19621 17983 -707 134 7715 O ATOM 3775 CB ASP A 482 4.303 4.016 54.841 1.00156.95 C ANISOU 3775 CB ASP A 482 21090 19705 18838 -1114 523 7109 C ATOM 3776 CG ASP A 482 2.866 3.697 54.457 1.00156.20 C ANISOU 3776 CG ASP A 482 20843 19541 18965 -1399 820 7130 C ATOM 3777 OD1 ASP A 482 2.385 2.594 54.800 1.00156.54 O ANISOU 3777 OD1 ASP A 482 20984 19349 19145 -1554 939 7445 O ATOM 3778 OD2 ASP A 482 2.226 4.548 53.797 1.00151.56 O ANISOU 3778 OD2 ASP A 482 20033 19124 18428 -1466 925 6829 O ATOM 3779 N LYS A 483 4.297 2.314 57.541 1.00161.94 N ANISOU 3779 N LYS A 483 22324 20312 18895 -1130 637 8059 N ATOM 3780 CA LYS A 483 4.788 1.114 58.224 1.00162.67 C ANISOU 3780 CA LYS A 483 22687 20130 18991 -1083 538 8483 C ATOM 3781 C LYS A 483 5.757 0.327 57.340 1.00166.03 C ANISOU 3781 C LYS A 483 23085 20094 19906 -961 257 8435 C ATOM 3782 O LYS A 483 6.882 0.020 57.741 1.00166.08 O ANISOU 3782 O LYS A 483 23265 20013 19827 -728 -11 8560 O ATOM 3783 CB LYS A 483 3.605 0.225 58.627 1.00157.19 C ANISOU 3783 CB LYS A 483 22056 19299 18369 -1366 853 8827 C ATOM 3784 CG LYS A 483 3.926 -1.261 58.737 1.00156.36 C ANISOU 3784 CG LYS A 483 22141 18708 18560 -1391 767 9208 C ATOM 3785 CD LYS A 483 4.259 -1.665 60.159 1.00159.87 C ANISOU 3785 CD LYS A 483 22941 19259 18543 -1296 747 9653 C ATOM 3786 CE LYS A 483 4.489 -3.162 60.254 1.00162.99 C ANISOU 3786 CE LYS A 483 23529 19142 19256 -1333 680 10054 C ATOM 3787 NZ LYS A 483 4.608 -3.603 61.667 1.00171.07 N ANISOU 3787 NZ LYS A 483 24916 20269 19814 -1282 711 10540 N ATOM 3788 N GLU A 484 5.301 0.020 56.130 1.00168.93 N ANISOU 3788 N GLU A 484 23227 20178 20779 -1112 317 8235 N ATOM 3789 CA GLU A 484 6.065 -0.742 55.148 1.00169.86 C ANISOU 3789 CA GLU A 484 23287 19844 21406 -1026 93 8140 C ATOM 3790 C GLU A 484 7.228 0.060 54.568 1.00164.90 C ANISOU 3790 C GLU A 484 22554 19318 20783 -772 -178 7792 C ATOM 3791 O GLU A 484 8.341 -0.456 54.426 1.00167.55 O ANISOU 3791 O GLU A 484 22961 19415 21288 -569 -435 7822 O ATOM 3792 CB GLU A 484 5.132 -1.186 54.017 1.00168.60 C ANISOU 3792 CB GLU A 484 22914 19404 21742 -1278 248 7982 C ATOM 3793 CG GLU A 484 5.807 -1.395 52.670 1.00161.66 C ANISOU 3793 CG GLU A 484 21875 18207 21341 -1187 42 7666 C ATOM 3794 CD GLU A 484 6.204 -2.836 52.435 1.00161.87 C ANISOU 3794 CD GLU A 484 22012 17698 21793 -1178 -74 7865 C ATOM 3795 OE1 GLU A 484 5.683 -3.719 53.149 1.00166.19 O ANISOU 3795 OE1 GLU A 484 22725 18078 22341 -1314 51 8241 O ATOM 3796 OE2 GLU A 484 7.034 -3.084 51.536 1.00158.19 O ANISOU 3796 OE2 GLU A 484 21468 16973 21665 -1035 -281 7644 O ATOM 3797 N LEU A 485 6.964 1.320 54.230 1.00154.97 N ANISOU 3797 N LEU A 485 21121 18409 19353 -783 -114 7464 N ATOM 3798 CA LEU A 485 7.969 2.164 53.588 1.00147.43 C ANISOU 3798 CA LEU A 485 20041 17553 18424 -581 -338 7115 C ATOM 3799 C LEU A 485 9.145 2.515 54.506 1.00150.24 C ANISOU 3799 C LEU A 485 20565 18106 18413 -312 -579 7194 C ATOM 3800 O LEU A 485 10.299 2.337 54.111 1.00147.73 O ANISOU 3800 O LEU A 485 20227 17620 18283 -113 -837 7096 O ATOM 3801 CB LEU A 485 7.335 3.435 53.016 1.00135.66 C ANISOU 3801 CB LEU A 485 18334 16371 16839 -668 -202 6765 C ATOM 3802 CG LEU A 485 8.323 4.446 52.430 1.00124.05 C ANISOU 3802 CG LEU A 485 16745 15040 15348 -478 -407 6417 C ATOM 3803 CD1 LEU A 485 9.026 3.881 51.209 1.00114.98 C ANISOU 3803 CD1 LEU A 485 15481 13510 14697 -418 -569 6251 C ATOM 3804 CD2 LEU A 485 7.615 5.731 52.085 1.00119.91 C ANISOU 3804 CD2 LEU A 485 16054 14845 14663 -563 -255 6132 C ATOM 3805 N ARG A 486 8.854 3.008 55.716 1.00152.75 N ANISOU 3805 N ARG A 486 21040 18784 18213 -302 -498 7355 N ATOM 3806 CA ARG A 486 9.889 3.336 56.711 1.00150.00 C ANISOU 3806 CA ARG A 486 20877 18652 17463 -54 -738 7439 C ATOM 3807 C ARG A 486 10.866 2.179 56.865 1.00148.82 C ANISOU 3807 C ARG A 486 20877 18148 17519 118 -982 7686 C ATOM 3808 O ARG A 486 12.060 2.380 57.093 1.00145.80 O ANISOU 3808 O ARG A 486 20538 17816 17043 372 -1275 7624 O ATOM 3809 CB ARG A 486 9.271 3.664 58.078 1.00154.21 C ANISOU 3809 CB ARG A 486 21617 19551 17427 -101 -585 7665 C ATOM 3810 CG ARG A 486 8.848 5.118 58.271 1.00150.31 C ANISOU 3810 CG ARG A 486 21023 19521 16566 -124 -474 7370 C ATOM 3811 CD ARG A 486 7.736 5.232 59.317 1.00151.51 C ANISOU 3811 CD ARG A 486 21312 19958 16295 -275 -179 7585 C ATOM 3812 NE ARG A 486 8.128 6.012 60.487 1.00148.99 N ANISOU 3812 NE ARG A 486 21176 20052 15380 -123 -276 7580 N ATOM 3813 CZ ARG A 486 8.879 5.542 61.477 1.00149.90 C ANISOU 3813 CZ ARG A 486 21566 20188 15201 40 -483 7849 C ATOM 3814 NH1 ARG A 486 9.333 4.296 61.432 1.00151.08 N ANISOU 3814 NH1 ARG A 486 21835 19954 15612 84 -608 8156 N ATOM 3815 NH2 ARG A 486 9.186 6.320 62.505 1.00150.85 N ANISOU 3815 NH2 ARG A 486 21847 20705 14765 168 -581 7801 N ATOM 3816 N ALA A 487 10.337 0.966 56.730 1.00150.90 N ANISOU 3816 N ALA A 487 21209 18046 18082 -22 -862 7959 N ATOM 3817 CA ALA A 487 11.145 -0.245 56.699 1.00151.72 C ANISOU 3817 CA ALA A 487 21431 17734 18480 123 -1067 8184 C ATOM 3818 C ALA A 487 11.894 -0.377 55.367 1.00141.90 C ANISOU 3818 C ALA A 487 19962 16200 17754 219 -1232 7862 C ATOM 3819 O ALA A 487 13.102 -0.604 55.344 1.00132.13 O ANISOU 3819 O ALA A 487 18745 14848 16612 477 -1512 7837 O ATOM 3820 CB ALA A 487 10.266 -1.464 56.944 1.00155.99 C ANISOU 3820 CB ALA A 487 22114 17959 19198 -83 -867 8563 C ATOM 3821 N MET A 488 11.169 -0.227 54.263 1.00145.76 N ANISOU 3821 N MET A 488 20231 16582 18567 19 -1059 7609 N ATOM 3822 CA MET A 488 11.760 -0.307 52.927 1.00148.69 C ANISOU 3822 CA MET A 488 20389 16697 19410 84 -1179 7281 C ATOM 3823 C MET A 488 12.883 0.723 52.728 1.00148.67 C ANISOU 3823 C MET A 488 20272 16944 19273 315 -1396 6980 C ATOM 3824 O MET A 488 13.818 0.503 51.947 1.00141.22 O ANISOU 3824 O MET A 488 19212 15787 18659 470 -1574 6791 O ATOM 3825 CB MET A 488 10.668 -0.153 51.860 1.00145.90 C ANISOU 3825 CB MET A 488 19836 16267 19332 -180 -950 7053 C ATOM 3826 CG MET A 488 10.942 0.914 50.812 1.00141.35 C ANISOU 3826 CG MET A 488 19021 15849 18837 -145 -987 6607 C ATOM 3827 SD MET A 488 10.990 0.272 49.128 1.00198.41 S ANISOU 3827 SD MET A 488 26054 22632 26699 -203 -1009 6320 S ATOM 3828 CE MET A 488 12.306 -0.935 49.276 1.00123.80 C ANISOU 3828 CE MET A 488 16725 12787 17525 51 -1271 6483 C ATOM 3829 N LEU A 489 12.781 1.837 53.454 1.00152.95 N ANISOU 3829 N LEU A 489 20844 17935 19334 334 -1374 6930 N ATOM 3830 CA LEU A 489 13.810 2.879 53.469 1.00148.71 C ANISOU 3830 CA LEU A 489 20220 17668 18613 540 -1583 6670 C ATOM 3831 C LEU A 489 15.034 2.470 54.294 1.00150.94 C ANISOU 3831 C LEU A 489 20653 17933 18764 824 -1883 6846 C ATOM 3832 O LEU A 489 16.159 2.475 53.786 1.00151.21 O ANISOU 3832 O LEU A 489 20566 17863 19025 1022 -2106 6666 O ATOM 3833 CB LEU A 489 13.235 4.193 54.012 1.00144.60 C ANISOU 3833 CB LEU A 489 19695 17620 17625 462 -1463 6547 C ATOM 3834 CG LEU A 489 12.270 4.950 53.099 1.00137.54 C ANISOU 3834 CG LEU A 489 18600 16819 16839 249 -1227 6274 C ATOM 3835 CD1 LEU A 489 11.636 6.136 53.824 1.00135.52 C ANISOU 3835 CD1 LEU A 489 18372 17019 16099 187 -1095 6202 C ATOM 3836 CD2 LEU A 489 13.009 5.399 51.850 1.00129.31 C ANISOU 3836 CD2 LEU A 489 17334 15671 16127 325 -1347 5918 C ATOM 3837 N ARG A 490 14.813 2.096 55.556 1.00147.15 N ANISOU 3837 N ARG A 490 20433 17556 17921 850 -1887 7201 N ATOM 3838 CA ARG A 490 15.902 1.709 56.459 1.00151.42 C ANISOU 3838 CA ARG A 490 21147 18107 18277 1132 -2186 7402 C ATOM 3839 C ARG A 490 16.695 0.489 55.954 1.00153.46 C ANISOU 3839 C ARG A 490 21390 17904 19014 1289 -2354 7507 C ATOM 3840 O ARG A 490 17.571 -0.024 56.653 1.00156.72 O ANISOU 3840 O ARG A 490 21946 18264 19336 1538 -2605 7712 O ATOM 3841 CB ARG A 490 15.364 1.445 57.877 1.00153.03 C ANISOU 3841 CB ARG A 490 21667 18485 17993 1103 -2125 7799 C ATOM 3842 CG ARG A 490 16.399 1.584 58.994 1.00150.70 C ANISOU 3842 CG ARG A 490 21558 18401 17300 1397 -2449 7926 C ATOM 3843 CD ARG A 490 15.949 0.898 60.273 1.00155.14 C ANISOU 3843 CD ARG A 490 22471 18992 17481 1384 -2404 8402 C ATOM 3844 NE ARG A 490 15.921 -0.556 60.134 1.00157.89 N ANISOU 3844 NE ARG A 490 22932 18866 18191 1386 -2390 8747 N ATOM 3845 CZ ARG A 490 15.716 -1.404 61.139 1.00162.70 C ANISOU 3845 CZ ARG A 490 23859 19388 18573 1409 -2388 9214 C ATOM 3846 NH1 ARG A 490 15.521 -0.947 62.368 1.00165.05 N ANISOU 3846 NH1 ARG A 490 24398 20061 18253 1433 -2399 9390 N ATOM 3847 NH2 ARG A 490 15.709 -2.711 60.917 1.00164.36 N ANISOU 3847 NH2 ARG A 490 24155 19127 19167 1406 -2378 9504 N ATOM 3848 N GLU A 491 16.385 0.033 54.741 1.00148.14 N ANISOU 3848 N GLU A 491 20542 16899 18844 1157 -2226 7355 N ATOM 3849 CA GLU A 491 17.095 -1.082 54.119 1.00143.63 C ANISOU 3849 CA GLU A 491 19930 15875 18770 1296 -2365 7389 C ATOM 3850 C GLU A 491 17.907 -0.670 52.885 1.00140.01 C ANISOU 3850 C GLU A 491 19178 15346 18675 1396 -2464 6959 C ATOM 3851 O GLU A 491 19.110 -0.932 52.826 1.00137.07 O ANISOU 3851 O GLU A 491 18744 14878 18456 1665 -2712 6905 O ATOM 3852 CB GLU A 491 16.122 -2.239 53.798 1.00141.21 C ANISOU 3852 CB GLU A 491 19708 15160 18786 1077 -2156 7609 C ATOM 3853 CG GLU A 491 16.001 -2.672 52.319 1.00132.56 C ANISOU 3853 CG GLU A 491 18397 13700 18270 978 -2081 7326 C ATOM 3854 CD GLU A 491 17.138 -3.576 51.838 1.00126.39 C ANISOU 3854 CD GLU A 491 17573 12535 17915 1230 -2307 7289 C ATOM 3855 OE1 GLU A 491 18.170 -3.061 51.350 1.00117.00 O ANISOU 3855 OE1 GLU A 491 16203 11439 16814 1431 -2475 6997 O ATOM 3856 OE2 GLU A 491 16.986 -4.810 51.926 1.00129.72 O ANISOU 3856 OE2 GLU A 491 18132 12551 18605 1223 -2306 7544 O ATOM 3857 N LYS A 492 17.261 -0.012 51.920 1.00137.25 N ANISOU 3857 N LYS A 492 18642 15057 18449 1189 -2272 6659 N ATOM 3858 CA LYS A 492 17.808 0.108 50.564 1.00130.54 C ANISOU 3858 CA LYS A 492 17539 14038 18023 1232 -2304 6286 C ATOM 3859 C LYS A 492 19.119 0.887 50.507 1.00125.21 C ANISOU 3859 C LYS A 492 16711 13579 17286 1478 -2533 6045 C ATOM 3860 O LYS A 492 19.904 0.768 49.559 1.00 94.90 O ANISOU 3860 O LYS A 492 12680 9567 13810 1593 -2613 5792 O ATOM 3861 CB LYS A 492 16.772 0.717 49.616 1.00123.62 C ANISOU 3861 CB LYS A 492 16524 13217 17230 961 -2055 6040 C ATOM 3862 CG LYS A 492 16.644 -0.033 48.301 1.00117.76 C ANISOU 3862 CG LYS A 492 15657 12067 17018 893 -1989 5859 C ATOM 3863 CD LYS A 492 16.502 -1.519 48.559 1.00121.07 C ANISOU 3863 CD LYS A 492 16237 12068 17697 901 -2008 6152 C ATOM 3864 CE LYS A 492 16.578 -2.321 47.275 1.00118.22 C ANISOU 3864 CE LYS A 492 15758 11279 17882 884 -1991 5934 C ATOM 3865 NZ LYS A 492 16.785 -3.774 47.552 1.00119.33 N ANISOU 3865 NZ LYS A 492 16048 10982 18311 968 -2074 6195 N ATOM 3866 N PHE A 493 19.349 1.683 51.540 1.00120.74 N ANISOU 3866 N PHE A 493 16225 13396 16255 1558 -2635 6114 N ATOM 3867 CA PHE A 493 20.594 2.403 51.676 1.00118.24 C ANISOU 3867 CA PHE A 493 15772 13306 15849 1793 -2878 5912 C ATOM 3868 C PHE A 493 20.958 2.446 53.152 1.00126.62 C ANISOU 3868 C PHE A 493 17039 14608 16462 1961 -3075 6175 C ATOM 3869 O PHE A 493 20.388 3.230 53.916 1.00131.51 O ANISOU 3869 O PHE A 493 17775 15562 16629 1867 -3017 6218 O ATOM 3870 CB PHE A 493 20.452 3.818 51.134 1.00111.01 C ANISOU 3870 CB PHE A 493 14672 12694 14813 1676 -2791 5560 C ATOM 3871 CG PHE A 493 19.838 3.894 49.762 1.00103.31 C ANISOU 3871 CG PHE A 493 13539 11533 14179 1478 -2567 5330 C ATOM 3872 CD1 PHE A 493 20.635 3.863 48.629 1.00 99.28 C ANISOU 3872 CD1 PHE A 493 12803 10851 14066 1567 -2617 5048 C ATOM 3873 CD2 PHE A 493 18.467 4.018 49.608 1.00103.31 C ANISOU 3873 CD2 PHE A 493 13611 11551 14092 1212 -2308 5384 C ATOM 3874 CE1 PHE A 493 20.080 3.941 47.365 1.00 92.91 C ANISOU 3874 CE1 PHE A 493 11873 9886 13541 1401 -2425 4829 C ATOM 3875 CE2 PHE A 493 17.903 4.098 48.345 1.00103.40 C ANISOU 3875 CE2 PHE A 493 13479 11406 14401 1046 -2129 5164 C ATOM 3876 CZ PHE A 493 18.713 4.060 47.221 1.00 95.23 C ANISOU 3876 CZ PHE A 493 12248 10196 13739 1144 -2194 4888 C ATOM 3877 N PRO A 494 21.905 1.587 53.555 1.00125.32 N ANISOU 3877 N PRO A 494 16925 14274 16416 2225 -3314 6347 N ATOM 3878 CA PRO A 494 22.397 1.469 54.932 1.00133.08 C ANISOU 3878 CA PRO A 494 18113 15451 16999 2439 -3552 6614 C ATOM 3879 C PRO A 494 22.972 2.781 55.463 1.00136.37 C ANISOU 3879 C PRO A 494 18445 16337 17031 2540 -3726 6384 C ATOM 3880 O PRO A 494 22.771 3.124 56.633 1.00137.69 O ANISOU 3880 O PRO A 494 18827 16787 16700 2576 -3809 6549 O ATOM 3881 CB PRO A 494 23.514 0.425 54.810 1.00137.64 C ANISOU 3881 CB PRO A 494 18637 15728 17932 2730 -3785 6708 C ATOM 3882 CG PRO A 494 23.883 0.417 53.345 1.00128.52 C ANISOU 3882 CG PRO A 494 17175 14347 17311 2695 -3706 6357 C ATOM 3883 CD PRO A 494 22.596 0.659 52.643 1.00121.96 C ANISOU 3883 CD PRO A 494 16353 13449 16539 2351 -3376 6272 C ATOM 3884 N GLU A 495 23.664 3.508 54.589 1.00139.31 N ANISOU 3884 N GLU A 495 18509 16782 17640 2575 -3774 5996 N ATOM 3885 CA GLU A 495 24.364 4.745 54.940 1.00142.29 C ANISOU 3885 CA GLU A 495 18747 17565 17751 2676 -3960 5727 C ATOM 3886 C GLU A 495 23.467 5.872 55.472 1.00147.71 C ANISOU 3886 C GLU A 495 19555 18600 17970 2479 -3836 5654 C ATOM 3887 O GLU A 495 23.952 6.969 55.755 1.00149.63 O ANISOU 3887 O GLU A 495 19693 19172 17990 2536 -3983 5403 O ATOM 3888 CB GLU A 495 25.156 5.262 53.731 1.00132.02 C ANISOU 3888 CB GLU A 495 17077 16226 16859 2695 -3969 5330 C ATOM 3889 CG GLU A 495 26.016 4.214 53.025 1.00131.35 C ANISOU 3889 CG GLU A 495 16833 15789 17285 2869 -4049 5335 C ATOM 3890 CD GLU A 495 25.256 3.437 51.960 1.00128.65 C ANISOU 3890 CD GLU A 495 16505 15041 17337 2686 -3780 5360 C ATOM 3891 OE1 GLU A 495 24.008 3.462 51.977 1.00132.63 O ANISOU 3891 OE1 GLU A 495 17181 15516 17695 2442 -3549 5476 O ATOM 3892 OE2 GLU A 495 25.904 2.800 51.103 1.00123.28 O ANISOU 3892 OE2 GLU A 495 15649 14079 17113 2790 -3800 5246 O ATOM 3893 N PHE A 496 22.169 5.611 55.604 1.00147.46 N ANISOU 3893 N PHE A 496 19725 18499 17805 2248 -3566 5857 N ATOM 3894 CA PHE A 496 21.248 6.628 56.096 1.00139.77 C ANISOU 3894 CA PHE A 496 18856 17848 16401 2060 -3415 5793 C ATOM 3895 C PHE A 496 20.358 6.128 57.246 1.00143.75 C ANISOU 3895 C PHE A 496 19702 18417 16500 1991 -3320 6175 C ATOM 3896 O PHE A 496 19.138 5.997 57.099 1.00145.06 O ANISOU 3896 O PHE A 496 19946 18531 16639 1745 -3009 6289 O ATOM 3897 CB PHE A 496 20.429 7.192 54.938 1.00128.88 C ANISOU 3897 CB PHE A 496 17303 16413 15253 1799 -3116 5558 C ATOM 3898 CG PHE A 496 21.250 7.464 53.698 1.00127.40 C ANISOU 3898 CG PHE A 496 16803 16091 15510 1849 -3171 5235 C ATOM 3899 CD1 PHE A 496 22.254 8.423 53.698 1.00124.37 C ANISOU 3899 CD1 PHE A 496 16238 15940 15078 1983 -3384 4943 C ATOM 3900 CD2 PHE A 496 21.016 6.761 52.528 1.00123.84 C ANISOU 3900 CD2 PHE A 496 16239 15285 15528 1754 -3007 5211 C ATOM 3901 CE1 PHE A 496 23.010 8.668 52.548 1.00115.17 C ANISOU 3901 CE1 PHE A 496 14776 14656 14327 2013 -3406 4656 C ATOM 3902 CE2 PHE A 496 21.769 7.002 51.375 1.00112.89 C ANISOU 3902 CE2 PHE A 496 14577 13781 14533 1799 -3040 4912 C ATOM 3903 CZ PHE A 496 22.765 7.953 51.387 1.00105.84 C ANISOU 3903 CZ PHE A 496 13501 13125 13588 1924 -3227 4646 C ATOM 3904 N CYS A 497 20.997 5.841 58.381 1.00139.25 N ANISOU 3904 N CYS A 497 19323 17968 15617 2216 -3593 6372 N ATOM 3905 CA CYS A 497 20.300 5.558 59.632 1.00137.77 C ANISOU 3905 CA CYS A 497 19481 17922 14944 2175 -3543 6715 C ATOM 3906 C CYS A 497 20.801 6.509 60.716 1.00134.84 C ANISOU 3906 C CYS A 497 19221 17973 14040 2317 -3811 6591 C ATOM 3907 O CYS A 497 21.725 7.296 60.489 1.00126.25 O ANISOU 3907 O CYS A 497 17928 17035 13004 2456 -4049 6252 O ATOM 3908 CB CYS A 497 20.513 4.105 60.070 1.00143.15 C ANISOU 3908 CB CYS A 497 20367 18299 15723 2311 -3629 7148 C ATOM 3909 SG CYS A 497 22.080 3.780 60.920 1.00145.25 S ANISOU 3909 SG CYS A 497 20707 18638 15845 2744 -4138 7234 S TER 3910 CYS A 497 ATOM 3911 N THR B 5 -0.253 56.662 38.395 1.00 63.95 N ANISOU 3911 N THR B 5 8712 6603 8983 -401 454 -551 N ATOM 3912 CA THR B 5 -1.265 56.428 39.421 1.00 66.53 C ANISOU 3912 CA THR B 5 8977 7200 9101 -123 290 -619 C ATOM 3913 C THR B 5 -1.343 54.947 39.814 1.00 60.69 C ANISOU 3913 C THR B 5 7895 6999 8165 -4 74 -459 C ATOM 3914 O THR B 5 -1.220 54.058 38.959 1.00 55.88 O ANISOU 3914 O THR B 5 7178 6481 7571 45 63 -165 O ATOM 3915 CB THR B 5 -2.631 56.921 38.956 1.00 70.01 C ANISOU 3915 CB THR B 5 9735 7352 9515 232 366 -477 C ATOM 3916 OG1 THR B 5 -2.495 58.251 38.448 1.00 83.09 O ANISOU 3916 OG1 THR B 5 11767 8450 11352 136 570 -572 O ATOM 3917 CG2 THR B 5 -3.617 56.927 40.103 1.00 64.01 C ANISOU 3917 CG2 THR B 5 8921 6821 8578 451 252 -659 C ATOM 3918 N PHE B 6 -1.517 54.688 41.112 1.00 53.46 N ANISOU 3918 N PHE B 6 6832 6423 7056 31 -87 -659 N ATOM 3919 CA PHE B 6 -1.591 53.320 41.621 1.00 44.85 C ANISOU 3919 CA PHE B 6 5484 5814 5742 139 -283 -522 C ATOM 3920 C PHE B 6 -2.933 53.093 42.300 1.00 51.76 C ANISOU 3920 C PHE B 6 6434 6845 6389 417 -310 -515 C ATOM 3921 O PHE B 6 -3.666 54.052 42.588 1.00 48.49 O ANISOU 3921 O PHE B 6 6216 6215 5992 502 -215 -696 O ATOM 3922 CB PHE B 6 -0.485 53.061 42.643 1.00 48.62 C ANISOU 3922 CB PHE B 6 5727 6608 6138 -81 -472 -774 C ATOM 3923 CG PHE B 6 0.887 53.027 42.058 1.00 52.46 C ANISOU 3923 CG PHE B 6 6041 7049 6842 -355 -474 -822 C ATOM 3924 CD1 PHE B 6 1.302 51.942 41.299 1.00 50.77 C ANISOU 3924 CD1 PHE B 6 5640 6981 6668 -334 -532 -548 C ATOM 3925 CD2 PHE B 6 1.779 54.065 42.287 1.00 53.04 C ANISOU 3925 CD2 PHE B 6 6116 6945 7093 -652 -404 -1182 C ATOM 3926 CE1 PHE B 6 2.587 51.903 40.762 1.00 52.28 C ANISOU 3926 CE1 PHE B 6 5640 7145 7078 -602 -522 -640 C ATOM 3927 CE2 PHE B 6 3.065 54.023 41.753 1.00 53.54 C ANISOU 3927 CE2 PHE B 6 5986 6984 7374 -935 -380 -1285 C ATOM 3928 CZ PHE B 6 3.459 52.947 40.989 1.00 50.99 C ANISOU 3928 CZ PHE B 6 5469 6811 7093 -907 -441 -1018 C ATOM 3929 N VAL B 7 -3.237 51.828 42.583 1.00 44.70 N ANISOU 3929 N VAL B 7 5383 6316 5284 545 -423 -335 N ATOM 3930 CA VAL B 7 -4.525 51.471 43.166 1.00 40.75 C ANISOU 3930 CA VAL B 7 4938 5982 4562 777 -404 -333 C ATOM 3931 C VAL B 7 -4.743 52.203 44.491 1.00 46.74 C ANISOU 3931 C VAL B 7 5779 6807 5174 719 -431 -695 C ATOM 3932 O VAL B 7 -5.808 52.763 44.734 1.00 46.13 O ANISOU 3932 O VAL B 7 5835 6624 5070 867 -325 -831 O ATOM 3933 CB VAL B 7 -4.633 49.956 43.319 1.00 46.65 C ANISOU 3933 CB VAL B 7 5527 7098 5101 860 -497 -96 C ATOM 3934 CG1 VAL B 7 -5.783 49.573 44.257 1.00 46.37 C ANISOU 3934 CG1 VAL B 7 5550 7286 4784 1009 -463 -181 C ATOM 3935 CG2 VAL B 7 -4.805 49.311 41.930 1.00 36.32 C ANISOU 3935 CG2 VAL B 7 4157 5698 3946 973 -421 244 C ATOM 3936 N LYS B 8 -3.695 52.245 45.307 1.00 51.32 N ANISOU 3936 N LYS B 8 6266 7557 5676 505 -577 -882 N ATOM 3937 CA LYS B 8 -3.735 52.895 46.611 1.00 52.00 C ANISOU 3937 CA LYS B 8 6410 7746 5600 418 -624 -1246 C ATOM 3938 C LYS B 8 -4.000 54.398 46.552 1.00 56.56 C ANISOU 3938 C LYS B 8 7157 7945 6390 369 -470 -1520 C ATOM 3939 O LYS B 8 -4.366 55.000 47.562 1.00 53.79 O ANISOU 3939 O LYS B 8 6877 7644 5918 345 -462 -1827 O ATOM 3940 CB LYS B 8 -2.429 52.634 47.381 1.00 50.68 C ANISOU 3940 CB LYS B 8 6085 7846 5324 210 -847 -1405 C ATOM 3941 CG LYS B 8 -1.263 53.520 46.949 1.00 56.42 C ANISOU 3941 CG LYS B 8 6741 8340 6354 -37 -833 -1597 C ATOM 3942 CD LYS B 8 0.010 53.186 47.728 1.00 65.61 C ANISOU 3942 CD LYS B 8 7693 9824 7412 -212 -1086 -1805 C ATOM 3943 CE LYS B 8 0.873 54.425 47.960 1.00 69.33 C ANISOU 3943 CE LYS B 8 8125 10119 8098 -488 -1044 -2226 C ATOM 3944 NZ LYS B 8 1.200 55.185 46.719 1.00 66.00 N ANISOU 3944 NZ LYS B 8 7759 9248 8069 -635 -806 -2189 N ATOM 3945 N ASP B 9 -3.805 55.008 45.386 1.00 56.57 N ANISOU 3945 N ASP B 9 7246 7553 6696 351 -341 -1414 N ATOM 3946 CA ASP B 9 -4.030 56.445 45.256 1.00 59.33 C ANISOU 3946 CA ASP B 9 7813 7478 7253 317 -184 -1648 C ATOM 3947 C ASP B 9 -5.493 56.782 44.945 1.00 63.88 C ANISOU 3947 C ASP B 9 8571 7858 7842 631 -68 -1601 C ATOM 3948 O ASP B 9 -5.890 57.947 44.982 1.00 70.07 O ANISOU 3948 O ASP B 9 9556 8302 8765 671 43 -1815 O ATOM 3949 CB ASP B 9 -3.109 57.030 44.189 1.00 62.94 C ANISOU 3949 CB ASP B 9 8348 7559 8009 131 -75 -1580 C ATOM 3950 CG ASP B 9 -1.628 56.855 44.531 1.00 71.24 C ANISOU 3950 CG ASP B 9 9180 8793 9095 -201 -175 -1736 C ATOM 3951 OD1 ASP B 9 -1.247 57.167 45.682 1.00 69.10 O ANISOU 3951 OD1 ASP B 9 8821 8717 8719 -344 -269 -2079 O ATOM 3952 OD2 ASP B 9 -0.859 56.396 43.649 1.00 66.64 O ANISOU 3952 OD2 ASP B 9 8499 8177 8645 -312 -166 -1541 O ATOM 3953 N ILE B 10 -6.294 55.762 44.659 1.00 58.01 N ANISOU 3953 N ILE B 10 7407 9017 5617 353 113 -1726 N ATOM 3954 CA ILE B 10 -7.685 55.973 44.252 1.00 58.11 C ANISOU 3954 CA ILE B 10 7543 8706 5831 315 354 -1581 C ATOM 3955 C ILE B 10 -8.547 56.447 45.429 1.00 61.73 C ANISOU 3955 C ILE B 10 8114 9358 5985 564 461 -1726 C ATOM 3956 O ILE B 10 -8.504 55.855 46.514 1.00 60.86 O ANISOU 3956 O ILE B 10 8052 9646 5426 872 528 -1605 O ATOM 3957 CB ILE B 10 -8.275 54.697 43.629 1.00 52.00 C ANISOU 3957 CB ILE B 10 6746 7771 5239 351 574 -1114 C ATOM 3958 CG1 ILE B 10 -7.470 54.299 42.387 1.00 47.33 C ANISOU 3958 CG1 ILE B 10 6049 7005 4930 125 475 -1044 C ATOM 3959 CG2 ILE B 10 -9.733 54.894 43.285 1.00 44.30 C ANISOU 3959 CG2 ILE B 10 5822 6496 4513 343 782 -1043 C ATOM 3960 CD1 ILE B 10 -7.829 52.945 41.822 1.00 42.85 C ANISOU 3960 CD1 ILE B 10 5412 6311 4558 184 629 -682 C ATOM 3961 N LYS B 11 -9.300 57.531 45.210 1.00 57.93 N ANISOU 3961 N LYS B 11 7686 8601 5724 462 483 -1982 N ATOM 3962 CA LYS B 11 -10.122 58.157 46.244 1.00 56.73 C ANISOU 3962 CA LYS B 11 7611 8607 5338 684 586 -2227 C ATOM 3963 C LYS B 11 -11.508 58.483 45.677 1.00 63.45 C ANISOU 3963 C LYS B 11 8478 9065 6564 642 788 -2167 C ATOM 3964 O LYS B 11 -11.640 58.776 44.478 1.00 57.80 O ANISOU 3964 O LYS B 11 7755 7928 6278 419 706 -2117 O ATOM 3965 CB LYS B 11 -9.454 59.438 46.754 1.00 67.91 C ANISOU 3965 CB LYS B 11 9016 10102 6684 643 302 -2824 C ATOM 3966 CG LYS B 11 -8.046 59.257 47.329 1.00 77.69 C ANISOU 3966 CG LYS B 11 10163 11744 7612 697 17 -3030 C ATOM 3967 CD LYS B 11 -8.067 58.701 48.750 1.00 87.77 C ANISOU 3967 CD LYS B 11 11521 13641 8186 1143 42 -3024 C ATOM 3968 CE LYS B 11 -6.672 58.257 49.211 1.00 86.08 C ANISOU 3968 CE LYS B 11 11202 13852 7654 1271 -292 -3140 C ATOM 3969 NZ LYS B 11 -6.146 57.114 48.390 1.00 71.88 N ANISOU 3969 NZ LYS B 11 9327 11933 6052 1153 -249 -2633 N ATOM 3970 N PRO B 12 -12.547 58.422 46.532 1.00 64.94 N ANISOU 3970 N PRO B 12 8682 9416 6575 887 1059 -2174 N ATOM 3971 CA PRO B 12 -13.913 58.760 46.103 1.00 62.69 C ANISOU 3971 CA PRO B 12 8342 8790 6689 888 1237 -2198 C ATOM 3972 C PRO B 12 -13.935 60.116 45.392 1.00 60.67 C ANISOU 3972 C PRO B 12 8126 8125 6799 727 964 -2563 C ATOM 3973 O PRO B 12 -13.407 61.088 45.942 1.00 62.37 O ANISOU 3973 O PRO B 12 8398 8413 6885 733 789 -2976 O ATOM 3974 CB PRO B 12 -14.679 58.887 47.426 1.00 64.56 C ANISOU 3974 CB PRO B 12 8587 9367 6575 1187 1536 -2345 C ATOM 3975 CG PRO B 12 -13.920 58.071 48.418 1.00 55.41 C ANISOU 3975 CG PRO B 12 7520 8732 4801 1381 1623 -2135 C ATOM 3976 CD PRO B 12 -12.475 58.040 47.956 1.00 65.69 C ANISOU 3976 CD PRO B 12 8846 10054 6061 1210 1221 -2167 C ATOM 3977 N GLY B 13 -14.509 60.184 44.193 1.00 53.86 N ANISOU 3977 N GLY B 13 7241 6830 6393 608 912 -2424 N ATOM 3978 CA GLY B 13 -14.665 61.464 43.524 1.00 56.81 C ANISOU 3978 CA GLY B 13 7705 6770 7109 520 692 -2678 C ATOM 3979 C GLY B 13 -13.567 61.814 42.534 1.00 63.53 C ANISOU 3979 C GLY B 13 8676 7375 8088 251 464 -2592 C ATOM 3980 O GLY B 13 -13.736 62.723 41.718 1.00 65.99 O ANISOU 3980 O GLY B 13 9106 7249 8718 175 327 -2641 O ATOM 3981 N LEU B 14 -12.445 61.104 42.596 1.00 59.47 N ANISOU 3981 N LEU B 14 8130 7129 7337 125 448 -2445 N ATOM 3982 CA LEU B 14 -11.383 61.327 41.630 1.00 56.43 C ANISOU 3982 CA LEU B 14 7810 6542 7090 -145 313 -2349 C ATOM 3983 C LEU B 14 -11.839 60.860 40.260 1.00 53.09 C ANISOU 3983 C LEU B 14 7453 5861 6859 -182 322 -1999 C ATOM 3984 O LEU B 14 -12.520 59.835 40.140 1.00 48.51 O ANISOU 3984 O LEU B 14 6778 5401 6254 -48 415 -1799 O ATOM 3985 CB LEU B 14 -10.113 60.571 42.021 1.00 53.31 C ANISOU 3985 CB LEU B 14 7301 6527 6427 -231 289 -2309 C ATOM 3986 CG LEU B 14 -9.348 61.038 43.252 1.00 57.34 C ANISOU 3986 CG LEU B 14 7731 7347 6708 -190 174 -2715 C ATOM 3987 CD1 LEU B 14 -7.935 60.471 43.184 1.00 53.58 C ANISOU 3987 CD1 LEU B 14 7119 7113 6126 -327 70 -2685 C ATOM 3988 CD2 LEU B 14 -9.340 62.564 43.341 1.00 48.94 C ANISOU 3988 CD2 LEU B 14 6716 5943 5937 -303 60 -3147 C ATOM 3989 N LYS B 15 -11.448 61.611 39.233 1.00 57.26 N ANISOU 3989 N LYS B 15 8141 6031 7584 -351 237 -1936 N ATOM 3990 CA LYS B 15 -11.689 61.224 37.846 1.00 58.93 C ANISOU 3990 CA LYS B 15 8465 6062 7865 -354 211 -1621 C ATOM 3991 C LYS B 15 -10.413 61.371 37.007 1.00 54.30 C ANISOU 3991 C LYS B 15 7973 5399 7260 -622 246 -1470 C ATOM 3992 O LYS B 15 -9.368 61.777 37.515 1.00 56.04 O ANISOU 3992 O LYS B 15 8120 5673 7501 -829 283 -1635 O ATOM 3993 CB LYS B 15 -12.841 62.044 37.253 1.00 60.61 C ANISOU 3993 CB LYS B 15 8846 5885 8299 -176 101 -1619 C ATOM 3994 CG LYS B 15 -12.706 63.536 37.466 1.00 69.84 C ANISOU 3994 CG LYS B 15 10177 6678 9681 -242 58 -1803 C ATOM 3995 CD LYS B 15 -13.820 64.301 36.758 1.00 78.80 C ANISOU 3995 CD LYS B 15 11504 7394 11041 -9 -86 -1743 C ATOM 3996 CE LYS B 15 -13.889 63.932 35.282 1.00 83.40 C ANISOU 3996 CE LYS B 15 12287 7881 11521 57 -167 -1367 C ATOM 3997 NZ LYS B 15 -14.822 64.823 34.533 1.00 87.13 N ANISOU 3997 NZ LYS B 15 13008 7928 12170 329 -363 -1279 N ATOM 3998 N ASN B 16 -10.508 61.043 35.723 1.00 59.90 N ANISOU 3998 N ASN B 16 8821 6006 7934 -603 240 -1195 N ATOM 3999 CA ASN B 16 -9.344 60.994 34.848 1.00 62.36 C ANISOU 3999 CA ASN B 16 9208 6310 8176 -833 353 -1016 C ATOM 4000 C ASN B 16 -8.261 60.067 35.408 1.00 57.97 C ANISOU 4000 C ASN B 16 8371 6142 7513 -976 429 -1100 C ATOM 4001 O ASN B 16 -7.067 60.316 35.262 1.00 55.75 O ANISOU 4001 O ASN B 16 8030 5874 7279 -1228 540 -1126 O ATOM 4002 CB ASN B 16 -8.821 62.409 34.554 1.00 61.67 C ANISOU 4002 CB ASN B 16 9331 5811 8291 -1038 443 -994 C ATOM 4003 CG ASN B 16 -9.861 63.278 33.831 1.00 64.50 C ANISOU 4003 CG ASN B 16 10022 5748 8737 -832 349 -824 C ATOM 4004 OD1 ASN B 16 -10.531 62.820 32.901 1.00 62.89 O ANISOU 4004 OD1 ASN B 16 9965 5576 8354 -601 252 -613 O ATOM 4005 ND2 ASN B 16 -10.006 64.528 34.269 1.00 61.52 N ANISOU 4005 ND2 ASN B 16 9748 4974 8653 -880 341 -957 N ATOM 4006 N LEU B 17 -8.699 58.986 36.048 1.00 54.07 N ANISOU 4006 N LEU B 17 7688 5940 6916 -800 381 -1134 N ATOM 4007 CA LEU B 17 -7.782 57.966 36.565 1.00 56.62 C ANISOU 4007 CA LEU B 17 7769 6620 7123 -845 418 -1158 C ATOM 4008 C LEU B 17 -7.197 57.101 35.444 1.00 54.71 C ANISOU 4008 C LEU B 17 7491 6460 6837 -901 481 -985 C ATOM 4009 O LEU B 17 -7.934 56.454 34.676 1.00 49.96 O ANISOU 4009 O LEU B 17 6938 5819 6226 -752 453 -861 O ATOM 4010 CB LEU B 17 -8.479 57.073 37.592 1.00 45.72 C ANISOU 4010 CB LEU B 17 6247 5467 5659 -613 406 -1163 C ATOM 4011 CG LEU B 17 -8.993 57.827 38.817 1.00 46.32 C ANISOU 4011 CG LEU B 17 6341 5568 5690 -515 384 -1371 C ATOM 4012 CD1 LEU B 17 -9.738 56.886 39.757 1.00 44.44 C ANISOU 4012 CD1 LEU B 17 5994 5558 5332 -273 477 -1289 C ATOM 4013 CD2 LEU B 17 -7.852 58.526 39.544 1.00 43.14 C ANISOU 4013 CD2 LEU B 17 5874 5299 5217 -656 313 -1638 C ATOM 4014 N ASN B 18 -5.871 57.106 35.356 1.00 46.20 N ANISOU 4014 N ASN B 18 6288 5504 5761 -1106 556 -1040 N ATOM 4015 CA ASN B 18 -5.153 56.273 34.401 1.00 53.40 C ANISOU 4015 CA ASN B 18 7117 6547 6628 -1158 651 -938 C ATOM 4016 C ASN B 18 -4.228 55.324 35.142 1.00 50.85 C ANISOU 4016 C ASN B 18 6476 6544 6301 -1138 615 -1043 C ATOM 4017 O ASN B 18 -3.299 55.760 35.833 1.00 46.34 O ANISOU 4017 O ASN B 18 5739 6083 5784 -1271 591 -1232 O ATOM 4018 CB ASN B 18 -4.313 57.144 33.460 1.00 58.20 C ANISOU 4018 CB ASN B 18 7837 6998 7281 -1423 843 -890 C ATOM 4019 CG ASN B 18 -5.139 58.190 32.745 1.00 65.50 C ANISOU 4019 CG ASN B 18 9131 7566 8189 -1405 875 -723 C ATOM 4020 OD1 ASN B 18 -6.208 57.894 32.194 1.00 62.55 O ANISOU 4020 OD1 ASN B 18 8934 7139 7692 -1163 762 -605 O ATOM 4021 ND2 ASN B 18 -4.658 59.427 32.760 1.00 70.02 N ANISOU 4021 ND2 ASN B 18 9803 7866 8936 -1642 1011 -732 N ATOM 4022 N LEU B 19 -4.470 54.029 35.001 1.00 46.73 N ANISOU 4022 N LEU B 19 5641 6631 5482 -532 -819 -1039 N ATOM 4023 CA LEU B 19 -3.609 53.053 35.650 1.00 45.78 C ANISOU 4023 CA LEU B 19 5489 6798 5107 -472 -682 -933 C ATOM 4024 C LEU B 19 -3.709 51.685 35.009 1.00 40.42 C ANISOU 4024 C LEU B 19 4776 6246 4336 -431 -395 -710 C ATOM 4025 O LEU B 19 -4.580 51.425 34.179 1.00 37.28 O ANISOU 4025 O LEU B 19 4387 5742 4035 -417 -266 -673 O ATOM 4026 CB LEU B 19 -3.928 52.926 37.143 1.00 47.83 C ANISOU 4026 CB LEU B 19 5809 7237 5127 -284 -655 -1173 C ATOM 4027 CG LEU B 19 -5.288 52.360 37.553 1.00 51.90 C ANISOU 4027 CG LEU B 19 6372 7849 5500 -123 -411 -1278 C ATOM 4028 CD1 LEU B 19 -5.161 51.663 38.901 1.00 58.93 C ANISOU 4028 CD1 LEU B 19 7263 9092 6035 10 -301 -1292 C ATOM 4029 CD2 LEU B 19 -6.300 53.477 37.682 1.00 49.19 C ANISOU 4029 CD2 LEU B 19 6051 7343 5295 -57 -556 -1624 C ATOM 4030 N ILE B 20 -2.804 50.817 35.436 1.00 36.49 N ANISOU 4030 N ILE B 20 4230 5958 3679 -393 -338 -592 N ATOM 4031 CA ILE B 20 -2.701 49.463 34.956 1.00 41.83 C ANISOU 4031 CA ILE B 20 4845 6736 4314 -324 -153 -420 C ATOM 4032 C ILE B 20 -2.934 48.521 36.152 1.00 41.31 C ANISOU 4032 C ILE B 20 4837 6801 4060 -182 -52 -400 C ATOM 4033 O ILE B 20 -2.526 48.815 37.288 1.00 42.75 O ANISOU 4033 O ILE B 20 5059 7112 4070 -156 -143 -470 O ATOM 4034 CB ILE B 20 -1.292 49.270 34.348 1.00 51.06 C ANISOU 4034 CB ILE B 20 5858 8046 5494 -412 -238 -287 C ATOM 4035 CG1 ILE B 20 -1.188 50.006 33.007 1.00 46.28 C ANISOU 4035 CG1 ILE B 20 5151 7400 5033 -576 -294 -212 C ATOM 4036 CG2 ILE B 20 -0.959 47.818 34.159 1.00 57.06 C ANISOU 4036 CG2 ILE B 20 6532 8931 6216 -283 -131 -193 C ATOM 4037 CD1 ILE B 20 0.290 50.245 32.551 1.00 44.31 C ANISOU 4037 CD1 ILE B 20 4703 7367 4766 -725 -417 -80 C ATOM 4038 N PHE B 21 -3.601 47.396 35.910 1.00 35.97 N ANISOU 4038 N PHE B 21 4149 6097 3420 -98 110 -287 N ATOM 4039 CA PHE B 21 -3.829 46.407 36.961 1.00 35.63 C ANISOU 4039 CA PHE B 21 4132 6173 3231 -10 180 -160 C ATOM 4040 C PHE B 21 -4.001 45.022 36.343 1.00 32.32 C ANISOU 4040 C PHE B 21 3637 5655 2986 53 240 18 C ATOM 4041 O PHE B 21 -4.188 44.892 35.133 1.00 30.84 O ANISOU 4041 O PHE B 21 3386 5335 2997 63 264 -26 O ATOM 4042 CB PHE B 21 -5.049 46.793 37.820 1.00 38.22 C ANISOU 4042 CB PHE B 21 4534 6574 3413 23 290 -251 C ATOM 4043 CG PHE B 21 -6.264 47.202 37.010 1.00 39.55 C ANISOU 4043 CG PHE B 21 4714 6554 3757 19 393 -372 C ATOM 4044 CD1 PHE B 21 -6.953 46.275 36.239 1.00 37.77 C ANISOU 4044 CD1 PHE B 21 4447 6181 3723 44 513 -242 C ATOM 4045 CD2 PHE B 21 -6.719 48.513 37.025 1.00 37.34 C ANISOU 4045 CD2 PHE B 21 4479 6217 3490 5 325 -639 C ATOM 4046 CE1 PHE B 21 -8.064 46.647 35.491 1.00 38.13 C ANISOU 4046 CE1 PHE B 21 4502 6053 3933 50 593 -364 C ATOM 4047 CE2 PHE B 21 -7.839 48.885 36.287 1.00 40.56 C ANISOU 4047 CE2 PHE B 21 4898 6435 4079 10 389 -756 C ATOM 4048 CZ PHE B 21 -8.507 47.947 35.519 1.00 39.56 C ANISOU 4048 CZ PHE B 21 4736 6189 4104 30 538 -611 C ATOM 4049 N ILE B 22 -3.950 43.985 37.171 1.00 30.86 N ANISOU 4049 N ILE B 22 3446 5537 2743 99 229 218 N ATOM 4050 CA ILE B 22 -4.135 42.629 36.671 1.00 33.63 C ANISOU 4050 CA ILE B 22 3710 5728 3340 168 205 383 C ATOM 4051 C ILE B 22 -5.418 42.137 37.315 1.00 38.89 C ANISOU 4051 C ILE B 22 4407 6373 3997 146 329 566 C ATOM 4052 O ILE B 22 -5.652 42.421 38.491 1.00 36.66 O ANISOU 4052 O ILE B 22 4179 6318 3432 101 386 653 O ATOM 4053 CB ILE B 22 -2.923 41.718 37.035 1.00 32.51 C ANISOU 4053 CB ILE B 22 3499 5627 3228 222 6 516 C ATOM 4054 CG1 ILE B 22 -3.190 40.251 36.646 1.00 38.61 C ANISOU 4054 CG1 ILE B 22 4169 6173 4328 313 -100 674 C ATOM 4055 CG2 ILE B 22 -2.596 41.817 38.525 1.00 32.66 C ANISOU 4055 CG2 ILE B 22 3599 5863 2949 178 -35 671 C ATOM 4056 CD1 ILE B 22 -1.893 39.421 36.464 1.00 32.32 C ANISOU 4056 CD1 ILE B 22 3247 5350 3682 423 -357 660 C ATOM 4057 N VAL B 23 -6.292 41.452 36.581 1.00 38.51 N ANISOU 4057 N VAL B 23 4300 6102 4232 178 375 616 N ATOM 4058 CA VAL B 23 -7.511 41.003 37.246 1.00 31.93 C ANISOU 4058 CA VAL B 23 3458 5282 3391 122 496 833 C ATOM 4059 C VAL B 23 -7.354 39.675 37.956 1.00 38.63 C ANISOU 4059 C VAL B 23 4239 6098 4339 94 360 1226 C ATOM 4060 O VAL B 23 -6.783 38.733 37.412 1.00 43.84 O ANISOU 4060 O VAL B 23 4823 6519 5313 167 151 1284 O ATOM 4061 CB VAL B 23 -8.817 41.095 36.376 1.00 53.13 C ANISOU 4061 CB VAL B 23 6114 7769 6303 135 631 719 C ATOM 4062 CG1 VAL B 23 -8.529 41.592 35.021 1.00 26.94 C ANISOU 4062 CG1 VAL B 23 2798 4294 3145 208 595 428 C ATOM 4063 CG2 VAL B 23 -9.605 39.786 36.362 1.00 40.92 C ANISOU 4063 CG2 VAL B 23 4461 6022 5067 120 595 1007 C ATOM 4064 N LEU B 24 -7.859 39.619 39.184 1.00 36.07 N ANISOU 4064 N LEU B 24 3920 6043 3742 -10 454 1490 N ATOM 4065 CA LEU B 24 -7.707 38.448 40.027 1.00 39.36 C ANISOU 4065 CA LEU B 24 4271 6482 4199 -88 306 1959 C ATOM 4066 C LEU B 24 -8.948 37.563 39.963 1.00 41.67 C ANISOU 4066 C LEU B 24 4446 6613 4773 -185 344 2282 C ATOM 4067 O LEU B 24 -8.864 36.335 40.114 1.00 43.80 O ANISOU 4067 O LEU B 24 4628 6662 5353 -240 117 2669 O ATOM 4068 CB LEU B 24 -7.466 38.888 41.476 1.00 42.00 C ANISOU 4068 CB LEU B 24 4648 7307 4002 -162 374 2117 C ATOM 4069 CG LEU B 24 -6.375 39.920 41.744 1.00 50.15 C ANISOU 4069 CG LEU B 24 5787 8545 4724 -80 339 1787 C ATOM 4070 CD1 LEU B 24 -6.171 40.091 43.247 1.00 44.42 C ANISOU 4070 CD1 LEU B 24 5072 8313 3494 -130 354 1981 C ATOM 4071 CD2 LEU B 24 -5.047 39.518 41.057 1.00 42.65 C ANISOU 4071 CD2 LEU B 24 4846 7310 4050 8 85 1695 C ATOM 4072 N GLU B 25 -10.104 38.200 39.759 1.00 43.26 N ANISOU 4072 N GLU B 25 4631 6907 4899 -211 600 2126 N ATOM 4073 CA GLU B 25 -11.390 37.517 39.808 1.00 50.02 C ANISOU 4073 CA GLU B 25 5349 7688 5968 -328 680 2428 C ATOM 4074 C GLU B 25 -12.449 38.275 39.028 1.00 49.32 C ANISOU 4074 C GLU B 25 5256 7533 5951 -275 898 2067 C ATOM 4075 O GLU B 25 -12.440 39.507 38.991 1.00 45.98 O ANISOU 4075 O GLU B 25 4925 7312 5233 -203 1049 1677 O ATOM 4076 CB GLU B 25 -11.857 37.361 41.260 1.00 50.67 C ANISOU 4076 CB GLU B 25 5341 8271 5640 -508 807 2866 C ATOM 4077 CG GLU B 25 -11.399 36.090 41.911 1.00 67.69 C ANISOU 4077 CG GLU B 25 7422 10357 7942 -643 547 3462 C ATOM 4078 CD GLU B 25 -11.477 36.170 43.407 1.00 86.15 C ANISOU 4078 CD GLU B 25 9706 13298 9729 -785 646 3796 C ATOM 4079 OE1 GLU B 25 -12.093 37.138 43.903 1.00 87.80 O ANISOU 4079 OE1 GLU B 25 9912 13928 9522 -748 906 3472 O ATOM 4080 OE2 GLU B 25 -10.925 35.274 44.085 1.00 97.73 O ANISOU 4080 OE2 GLU B 25 11140 14736 11256 -877 394 4200 O ATOM 4081 N THR B 26 -13.367 37.530 38.423 1.00 53.74 N ANISOU 4081 N THR B 26 5698 7781 6940 -309 872 2202 N ATOM 4082 CA THR B 26 -14.508 38.115 37.728 1.00 50.54 C ANISOU 4082 CA THR B 26 5265 7301 6637 -269 1062 1910 C ATOM 4083 C THR B 26 -15.747 37.631 38.478 1.00 46.31 C ANISOU 4083 C THR B 26 4540 6972 6085 -452 1212 2297 C ATOM 4084 O THR B 26 -15.882 36.439 38.730 1.00 54.80 O ANISOU 4084 O THR B 26 5485 7886 7452 -585 1053 2779 O ATOM 4085 CB THR B 26 -14.575 37.636 36.280 1.00 45.14 C ANISOU 4085 CB THR B 26 4570 6088 6491 -139 891 1704 C ATOM 4086 OG1 THR B 26 -14.456 36.205 36.265 1.00 52.46 O ANISOU 4086 OG1 THR B 26 5374 6702 7856 -184 623 2079 O ATOM 4087 CG2 THR B 26 -13.443 38.234 35.446 1.00 44.55 C ANISOU 4087 CG2 THR B 26 4633 5923 6369 29 790 1309 C ATOM 4088 N GLY B 27 -16.647 38.540 38.837 1.00 63.55 N ANISOU 4088 N GLY B 27 5383 8524 10240 66 -1684 812 N ATOM 4089 CA GLY B 27 -17.811 38.165 39.625 1.00 61.44 C ANISOU 4089 CA GLY B 27 5143 8083 10118 28 -1549 1774 C ATOM 4090 C GLY B 27 -18.982 37.738 38.763 1.00 61.60 C ANISOU 4090 C GLY B 27 5022 7681 10700 -324 -1614 2168 C ATOM 4091 O GLY B 27 -18.873 37.686 37.542 1.00 64.92 O ANISOU 4091 O GLY B 27 5366 7906 11395 -498 -1807 1692 O ATOM 4092 N ARG B 28 -20.113 37.429 39.387 1.00 69.45 N ANISOU 4092 N ARG B 28 5959 8579 11849 -448 -1450 3023 N ATOM 4093 CA ARG B 28 -21.285 37.050 38.609 1.00 81.47 C ANISOU 4093 CA ARG B 28 7282 9754 13917 -812 -1510 3394 C ATOM 4094 C ARG B 28 -21.941 38.275 37.980 1.00 75.27 C ANISOU 4094 C ARG B 28 6353 9272 12974 -948 -1114 3210 C ATOM 4095 O ARG B 28 -21.819 39.395 38.484 1.00 69.58 O ANISOU 4095 O ARG B 28 5699 9022 11717 -783 -701 3083 O ATOM 4096 CB ARG B 28 -22.293 36.271 39.453 1.00 93.36 C ANISOU 4096 CB ARG B 28 8719 11094 15660 -977 -1460 4367 C ATOM 4097 CG ARG B 28 -22.544 36.873 40.818 1.00103.65 C ANISOU 4097 CG ARG B 28 10050 12933 16398 -801 -960 4846 C ATOM 4098 CD ARG B 28 -23.640 36.129 41.560 1.00119.03 C ANISOU 4098 CD ARG B 28 11880 14787 18557 -1064 -843 5835 C ATOM 4099 NE ARG B 28 -24.961 36.439 41.018 1.00126.07 N ANISOU 4099 NE ARG B 28 12381 15770 19751 -1404 -585 6118 N ATOM 4100 CZ ARG B 28 -25.673 37.511 41.356 1.00124.84 C ANISOU 4100 CZ ARG B 28 11998 16204 19234 -1329 -41 6226 C ATOM 4101 NH1 ARG B 28 -25.189 38.380 42.236 1.00123.30 N ANISOU 4101 NH1 ARG B 28 11961 16525 18362 -954 309 6080 N ATOM 4102 NH2 ARG B 28 -26.866 37.716 40.814 1.00124.77 N ANISOU 4102 NH2 ARG B 28 11768 16269 19372 -1420 29 6151 N ATOM 4103 N VAL B 29 -22.615 38.053 36.858 1.00 68.89 N ANISOU 4103 N VAL B 29 5385 8160 12629 -1223 -1293 3165 N ATOM 4104 CA VAL B 29 -23.310 39.122 36.156 1.00 73.87 C ANISOU 4104 CA VAL B 29 5916 8997 13154 -1328 -1016 3011 C ATOM 4105 C VAL B 29 -24.637 39.412 36.851 1.00 65.97 C ANISOU 4105 C VAL B 29 4686 8239 12142 -1366 -646 3718 C ATOM 4106 O VAL B 29 -25.359 38.488 37.202 1.00 70.44 O ANISOU 4106 O VAL B 29 5150 8610 13004 -1483 -748 4257 O ATOM 4107 CB VAL B 29 -23.617 38.700 34.709 1.00 81.08 C ANISOU 4107 CB VAL B 29 6916 9508 14383 -1480 -1347 2645 C ATOM 4108 CG1 VAL B 29 -24.140 39.867 33.908 1.00 76.88 C ANISOU 4108 CG1 VAL B 29 6510 9169 13533 -1463 -1103 2332 C ATOM 4109 CG2 VAL B 29 -22.376 38.155 34.059 1.00 78.82 C ANISOU 4109 CG2 VAL B 29 6780 9000 14170 -1444 -1730 2000 C ATOM 4110 N THR B 30 -24.939 40.689 37.076 1.00 63.62 N ANISOU 4110 N THR B 30 4407 8371 11396 -1201 -229 3629 N ATOM 4111 CA THR B 30 -26.306 41.113 37.404 1.00 63.89 C ANISOU 4111 CA THR B 30 4325 8638 11313 -1117 59 4003 C ATOM 4112 C THR B 30 -26.838 42.037 36.296 1.00 61.98 C ANISOU 4112 C THR B 30 4159 8372 11017 -1093 55 3591 C ATOM 4113 O THR B 30 -26.061 42.543 35.467 1.00 57.02 O ANISOU 4113 O THR B 30 3728 7632 10303 -1137 -61 3054 O ATOM 4114 CB THR B 30 -26.415 41.813 38.783 1.00 64.08 C ANISOU 4114 CB THR B 30 4294 9215 10839 -856 542 4327 C ATOM 4115 OG1 THR B 30 -25.486 42.898 38.860 1.00 67.42 O ANISOU 4115 OG1 THR B 30 4954 9872 10790 -649 722 3839 O ATOM 4116 CG2 THR B 30 -26.135 40.840 39.919 1.00 70.22 C ANISOU 4116 CG2 THR B 30 5001 10039 11641 -892 562 4885 C ATOM 4117 N LYS B 31 -28.150 42.239 36.286 1.00 61.18 N ANISOU 4117 N LYS B 31 3874 8400 10973 -1044 167 3852 N ATOM 4118 CA LYS B 31 -28.820 43.075 35.290 1.00 72.82 C ANISOU 4118 CA LYS B 31 5339 9868 12461 -1002 133 3585 C ATOM 4119 C LYS B 31 -29.429 44.314 35.940 1.00 72.29 C ANISOU 4119 C LYS B 31 5143 10286 12038 -698 536 3705 C ATOM 4120 O LYS B 31 -30.119 44.216 36.948 1.00 64.61 O ANISOU 4120 O LYS B 31 3963 9639 10947 -568 784 4089 O ATOM 4121 CB LYS B 31 -29.952 42.298 34.605 1.00 71.61 C ANISOU 4121 CB LYS B 31 4995 9490 12722 -1159 -123 3740 C ATOM 4122 CG LYS B 31 -29.546 41.494 33.373 1.00 74.30 C ANISOU 4122 CG LYS B 31 5531 9335 13363 -1360 -565 3399 C ATOM 4123 CD LYS B 31 -29.486 42.374 32.131 1.00 77.29 C ANISOU 4123 CD LYS B 31 6076 9634 13655 -1335 -690 2929 C ATOM 4124 CE LYS B 31 -29.327 41.547 30.851 1.00 80.87 C ANISOU 4124 CE LYS B 31 6711 9677 14340 -1483 -1097 2598 C ATOM 4125 NZ LYS B 31 -30.623 41.069 30.281 1.00 83.44 N ANISOU 4125 NZ LYS B 31 6812 9902 14991 -1545 -1276 2773 N ATOM 4126 N THR B 32 -29.171 45.480 35.361 1.00 52.75 N ANISOU 4126 N THR B 32 3356 8363 8323 352 665 2640 N ATOM 4127 CA THR B 32 -29.826 46.697 35.814 1.00 50.18 C ANISOU 4127 CA THR B 32 2943 8320 7802 738 754 2543 C ATOM 4128 C THR B 32 -31.265 46.698 35.318 1.00 52.68 C ANISOU 4128 C THR B 32 3055 8700 8262 682 677 2765 C ATOM 4129 O THR B 32 -31.596 46.034 34.332 1.00 54.70 O ANISOU 4129 O THR B 32 3300 8690 8794 337 499 2900 O ATOM 4130 CB THR B 32 -29.139 47.937 35.243 1.00 53.10 C ANISOU 4130 CB THR B 32 3707 8408 8061 833 619 2086 C ATOM 4131 OG1 THR B 32 -29.293 47.941 33.813 1.00 45.72 O ANISOU 4131 OG1 THR B 32 2902 7118 7351 527 400 2036 O ATOM 4132 CG2 THR B 32 -27.647 47.975 35.632 1.00 44.89 C ANISOU 4132 CG2 THR B 32 2973 7226 6856 829 641 1824 C ATOM 4133 N LYS B 33 -32.114 47.475 35.966 1.00 54.33 N ANISOU 4133 N LYS B 33 3136 9243 8263 1038 782 2763 N ATOM 4134 CA LYS B 33 -33.503 47.510 35.567 1.00 56.95 C ANISOU 4134 CA LYS B 33 3264 9673 8703 1006 725 2977 C ATOM 4135 C LYS B 33 -33.746 47.971 34.114 1.00 55.34 C ANISOU 4135 C LYS B 33 3101 9143 8782 830 490 2878 C ATOM 4136 O LYS B 33 -34.784 47.659 33.532 1.00 57.02 O ANISOU 4136 O LYS B 33 3171 9326 9168 659 388 3095 O ATOM 4137 CB LYS B 33 -34.334 48.327 36.571 1.00 60.62 C ANISOU 4137 CB LYS B 33 3590 10590 8851 1468 885 2952 C ATOM 4138 CG LYS B 33 -34.011 49.804 36.593 1.00 65.14 C ANISOU 4138 CG LYS B 33 4319 11162 9269 1888 842 2525 C ATOM 4139 CD LYS B 33 -34.627 50.470 37.808 1.00 73.71 C ANISOU 4139 CD LYS B 33 5335 12691 9979 2378 992 2442 C ATOM 4140 CE LYS B 33 -34.143 51.906 37.930 1.00 83.77 C ANISOU 4140 CE LYS B 33 6856 13878 11095 2823 878 1958 C ATOM 4141 NZ LYS B 33 -34.463 52.490 39.264 1.00 94.74 N ANISOU 4141 NZ LYS B 33 8262 15667 12068 3314 1000 1805 N ATOM 4142 N ASP B 34 -32.799 48.686 33.515 1.00 52.38 N ANISOU 4142 N ASP B 34 2988 8487 8428 839 373 2550 N ATOM 4143 CA ASP B 34 -32.958 49.047 32.101 1.00 51.01 C ANISOU 4143 CA ASP B 34 3010 7931 8441 602 115 2420 C ATOM 4144 C ASP B 34 -32.171 48.153 31.125 1.00 54.47 C ANISOU 4144 C ASP B 34 3677 7977 9041 158 -39 2382 C ATOM 4145 O ASP B 34 -31.928 48.550 29.981 1.00 48.58 O ANISOU 4145 O ASP B 34 3181 6924 8352 -7 -239 2194 O ATOM 4146 CB ASP B 34 -32.627 50.520 31.852 1.00 50.29 C ANISOU 4146 CB ASP B 34 3224 7684 8201 840 3 2040 C ATOM 4147 CG ASP B 34 -31.185 50.865 32.198 1.00 49.57 C ANISOU 4147 CG ASP B 34 3490 7422 7920 870 15 1734 C ATOM 4148 OD1 ASP B 34 -30.491 50.051 32.871 1.00 52.00 O ANISOU 4148 OD1 ASP B 34 3782 7821 8156 809 168 1793 O ATOM 4149 OD2 ASP B 34 -30.745 51.976 31.812 1.00 47.85 O ANISOU 4149 OD2 ASP B 34 3561 6978 7642 948 -152 1456 O ATOM 4150 N GLY B 35 -31.775 46.958 31.568 1.00 52.35 N ANISOU 4150 N GLY B 35 3323 7737 8831 -9 37 2560 N ATOM 4151 CA GLY B 35 -31.245 45.957 30.654 1.00 50.38 C ANISOU 4151 CA GLY B 35 3238 7145 8759 -379 -147 2547 C ATOM 4152 C GLY B 35 -29.737 45.849 30.483 1.00 59.26 C ANISOU 4152 C GLY B 35 4724 8057 9736 -448 -148 2241 C ATOM 4153 O GLY B 35 -29.275 45.177 29.559 1.00 61.18 O ANISOU 4153 O GLY B 35 5137 8031 10078 -692 -321 2158 O ATOM 4154 N HIS B 36 -28.954 46.487 31.348 1.00 50.44 N ANISOU 4154 N HIS B 36 3721 7072 8374 -219 24 2068 N ATOM 4155 CA HIS B 36 -27.502 46.346 31.224 1.00 53.97 C ANISOU 4155 CA HIS B 36 4464 7351 8690 -298 24 1820 C ATOM 4156 C HIS B 36 -26.933 45.270 32.142 1.00 53.79 C ANISOU 4156 C HIS B 36 4366 7418 8655 -313 151 1942 C ATOM 4157 O HIS B 36 -27.308 45.177 33.318 1.00 56.99 O ANISOU 4157 O HIS B 36 4550 8106 8997 -130 326 2129 O ATOM 4158 CB HIS B 36 -26.775 47.668 31.487 1.00 44.32 C ANISOU 4158 CB HIS B 36 3462 6139 7238 -99 59 1542 C ATOM 4159 CG HIS B 36 -27.099 48.750 30.507 1.00 48.50 C ANISOU 4159 CG HIS B 36 4122 6519 7787 -119 -115 1415 C ATOM 4160 ND1 HIS B 36 -26.255 49.101 29.484 1.00 43.55 N ANISOU 4160 ND1 HIS B 36 3751 5679 7117 -302 -258 1243 N ATOM 4161 CD2 HIS B 36 -28.175 49.577 30.426 1.00 46.29 C ANISOU 4161 CD2 HIS B 36 3736 6297 7554 37 -174 1456 C ATOM 4162 CE1 HIS B 36 -26.800 50.100 28.799 1.00 44.98 C ANISOU 4162 CE1 HIS B 36 3989 5770 7332 -288 -411 1204 C ATOM 4163 NE2 HIS B 36 -27.958 50.395 29.345 1.00 41.25 N ANISOU 4163 NE2 HIS B 36 3313 5436 6925 -78 -372 1312 N ATOM 4164 N GLU B 37 -26.021 44.471 31.599 1.00 49.20 N ANISOU 4164 N GLU B 37 3961 6620 8111 -505 58 1836 N ATOM 4165 CA GLU B 37 -25.270 43.509 32.404 1.00 51.57 C ANISOU 4165 CA GLU B 37 4248 6955 8392 -513 146 1901 C ATOM 4166 C GLU B 37 -24.184 44.252 33.170 1.00 52.89 C ANISOU 4166 C GLU B 37 4568 7242 8284 -320 306 1685 C ATOM 4167 O GLU B 37 -23.520 45.123 32.613 1.00 43.32 O ANISOU 4167 O GLU B 37 3575 5940 6945 -311 257 1428 O ATOM 4168 CB GLU B 37 -24.620 42.463 31.501 1.00 54.38 C ANISOU 4168 CB GLU B 37 4767 7030 8866 -725 -44 1803 C ATOM 4169 CG GLU B 37 -25.588 41.457 30.855 1.00 53.86 C ANISOU 4169 CG GLU B 37 4571 6781 9113 -929 -279 2018 C ATOM 4170 CD GLU B 37 -24.844 40.381 30.078 1.00 65.79 C ANISOU 4170 CD GLU B 37 6281 8005 10709 -1059 -504 1857 C ATOM 4171 OE1 GLU B 37 -23.877 40.719 29.354 1.00 65.15 O ANISOU 4171 OE1 GLU B 37 6449 7871 10434 -1020 -520 1533 O ATOM 4172 OE2 GLU B 37 -25.211 39.196 30.212 1.00 71.64 O ANISOU 4172 OE2 GLU B 37 6922 8589 11709 -1186 -682 2065 O ATOM 4173 N VAL B 38 -24.013 43.934 34.450 1.00 54.42 N ANISOU 4173 N VAL B 38 4639 7649 8389 -175 474 1814 N ATOM 4174 CA VAL B 38 -22.928 44.523 35.226 1.00 43.76 C ANISOU 4174 CA VAL B 38 3444 6395 6790 3 588 1605 C ATOM 4175 C VAL B 38 -22.171 43.412 35.951 1.00 48.17 C ANISOU 4175 C VAL B 38 3976 6985 7341 -32 659 1703 C ATOM 4176 O VAL B 38 -22.781 42.496 36.521 1.00 47.00 O ANISOU 4176 O VAL B 38 3598 6948 7311 -62 704 2017 O ATOM 4177 CB VAL B 38 -23.441 45.530 36.277 1.00 43.51 C ANISOU 4177 CB VAL B 38 3314 6652 6567 330 722 1604 C ATOM 4178 CG1 VAL B 38 -22.277 46.292 36.889 1.00 43.56 C ANISOU 4178 CG1 VAL B 38 3542 6673 6337 496 747 1327 C ATOM 4179 CG2 VAL B 38 -24.411 46.516 35.664 1.00 49.81 C ANISOU 4179 CG2 VAL B 38 4088 7431 7407 400 636 1557 C ATOM 4180 N ARG B 39 -20.844 43.474 35.922 1.00 51.56 N ANISOU 4180 N ARG B 39 4619 7324 7647 -41 652 1470 N ATOM 4181 CA ARG B 39 -20.072 42.575 36.775 1.00 57.23 C ANISOU 4181 CA ARG B 39 5317 8101 8324 -18 728 1543 C ATOM 4182 C ARG B 39 -18.893 43.239 37.452 1.00 54.57 C ANISOU 4182 C ARG B 39 5135 7854 7744 133 803 1322 C ATOM 4183 O ARG B 39 -18.247 44.144 36.899 1.00 48.37 O ANISOU 4183 O ARG B 39 4533 6978 6869 118 733 1076 O ATOM 4184 CB ARG B 39 -19.650 41.283 36.063 1.00 54.42 C ANISOU 4184 CB ARG B 39 5012 7505 8161 -225 585 1568 C ATOM 4185 CG ARG B 39 -18.692 41.445 34.935 1.00 57.84 C ANISOU 4185 CG ARG B 39 5671 7759 8546 -312 472 1270 C ATOM 4186 CD ARG B 39 -18.100 40.079 34.590 1.00 61.32 C ANISOU 4186 CD ARG B 39 6163 8022 9113 -400 345 1258 C ATOM 4187 NE ARG B 39 -18.853 39.338 33.571 1.00 55.48 N ANISOU 4187 NE ARG B 39 5416 7056 8608 -545 127 1310 N ATOM 4188 CZ ARG B 39 -19.014 38.020 33.597 1.00 60.87 C ANISOU 4188 CZ ARG B 39 6062 7548 9517 -621 -45 1444 C ATOM 4189 NH1 ARG B 39 -18.501 37.318 34.602 1.00 63.23 N ANISOU 4189 NH1 ARG B 39 6314 7879 9833 -570 4 1567 N ATOM 4190 NH2 ARG B 39 -19.691 37.403 32.636 1.00 62.57 N ANISOU 4190 NH2 ARG B 39 6297 7522 9955 -747 -302 1461 N ATOM 4191 N THR B 40 -18.652 42.786 38.678 1.00 48.04 N ANISOU 4191 N THR B 40 4217 7216 6819 267 926 1449 N ATOM 4192 CA THR B 40 -17.576 43.306 39.497 1.00 47.85 C ANISOU 4192 CA THR B 40 4321 7294 6566 426 981 1266 C ATOM 4193 C THR B 40 -16.342 42.438 39.318 1.00 45.42 C ANISOU 4193 C THR B 40 4111 6853 6295 298 938 1201 C ATOM 4194 O THR B 40 -16.410 41.219 39.378 1.00 51.39 O ANISOU 4194 O THR B 40 4777 7555 7194 207 927 1386 O ATOM 4195 CB THR B 40 -17.998 43.373 40.958 1.00 50.86 C ANISOU 4195 CB THR B 40 4552 8008 6766 693 1135 1421 C ATOM 4196 OG1 THR B 40 -19.145 44.223 41.054 1.00 58.99 O ANISOU 4196 OG1 THR B 40 5481 9196 7738 866 1170 1448 O ATOM 4197 CG2 THR B 40 -16.896 43.959 41.811 1.00 57.05 C ANISOU 4197 CG2 THR B 40 5491 8877 7306 875 1148 1201 C ATOM 4198 N CYS B 41 -15.215 43.083 39.062 1.00 42.15 N ANISOU 4198 N CYS B 41 3872 6377 5765 289 884 950 N ATOM 4199 CA CYS B 41 -13.947 42.390 38.917 1.00 43.65 C ANISOU 4199 CA CYS B 41 4136 6502 5948 214 854 867 C ATOM 4200 C CYS B 41 -13.004 42.892 39.986 1.00 44.88 C ANISOU 4200 C CYS B 41 4352 6796 5903 361 896 770 C ATOM 4201 O CYS B 41 -12.892 44.103 40.213 1.00 47.54 O ANISOU 4201 O CYS B 41 4775 7170 6118 443 852 633 O ATOM 4202 CB CYS B 41 -13.345 42.671 37.537 1.00 46.48 C ANISOU 4202 CB CYS B 41 4605 6722 6333 54 743 690 C ATOM 4203 SG CYS B 41 -14.368 42.088 36.173 1.00 58.32 S ANISOU 4203 SG CYS B 41 6071 8048 8040 -100 646 751 S ATOM 4204 N LYS B 42 -12.335 41.965 40.653 1.00 46.83 N ANISOU 4204 N LYS B 42 4566 7096 6131 398 941 839 N ATOM 4205 CA LYS B 42 -11.337 42.337 41.631 1.00 38.70 C ANISOU 4205 CA LYS B 42 3596 6191 4915 527 957 743 C ATOM 4206 C LYS B 42 -10.022 42.474 40.881 1.00 37.81 C ANISOU 4206 C LYS B 42 3577 5994 4796 402 865 567 C ATOM 4207 O LYS B 42 -9.590 41.543 40.195 1.00 41.66 O ANISOU 4207 O LYS B 42 4043 6405 5380 310 847 571 O ATOM 4208 CB LYS B 42 -11.252 41.271 42.723 1.00 43.30 C ANISOU 4208 CB LYS B 42 4081 6897 5475 628 1044 935 C ATOM 4209 CG LYS B 42 -10.122 41.485 43.742 1.00 47.60 C ANISOU 4209 CG LYS B 42 4689 7571 5827 762 1046 840 C ATOM 4210 CD LYS B 42 -10.084 40.339 44.767 1.00 51.68 C ANISOU 4210 CD LYS B 42 5098 8211 6328 847 1124 1074 C ATOM 4211 CE LYS B 42 -9.211 40.691 45.979 1.00 51.54 C ANISOU 4211 CE LYS B 42 5133 8379 6070 1031 1133 996 C ATOM 4212 NZ LYS B 42 -9.881 41.705 46.854 1.00 45.23 N ANISOU 4212 NZ LYS B 42 4343 7804 5038 1269 1179 957 N ATOM 4213 N VAL B 43 -9.403 43.650 40.975 1.00 38.53 N ANISOU 4213 N VAL B 43 3760 6105 4773 407 781 419 N ATOM 4214 CA VAL B 43 -8.147 43.894 40.285 1.00 36.90 C ANISOU 4214 CA VAL B 43 3588 5883 4550 268 693 316 C ATOM 4215 C VAL B 43 -7.096 44.408 41.266 1.00 40.35 C ANISOU 4215 C VAL B 43 4070 6403 4856 342 623 245 C ATOM 4216 O VAL B 43 -7.437 44.917 42.335 1.00 41.92 O ANISOU 4216 O VAL B 43 4326 6642 4961 510 603 216 O ATOM 4217 CB VAL B 43 -8.332 44.899 39.122 1.00 40.03 C ANISOU 4217 CB VAL B 43 4027 6193 4989 103 584 266 C ATOM 4218 CG1 VAL B 43 -9.510 44.477 38.203 1.00 31.37 C ANISOU 4218 CG1 VAL B 43 2897 5008 4013 48 630 327 C ATOM 4219 CG2 VAL B 43 -8.526 46.323 39.653 1.00 32.57 C ANISOU 4219 CG2 VAL B 43 3187 5195 3994 152 443 194 C ATOM 4220 N ALA B 44 -5.822 44.291 40.898 1.00 36.44 N ANISOU 4220 N ALA B 44 3542 5961 4342 236 574 215 N ATOM 4221 CA ALA B 44 -4.737 44.602 41.832 1.00 39.68 C ANISOU 4221 CA ALA B 44 3971 6452 4652 289 490 170 C ATOM 4222 C ALA B 44 -3.467 45.149 41.188 1.00 45.59 C ANISOU 4222 C ALA B 44 4667 7257 5397 101 361 164 C ATOM 4223 O ALA B 44 -3.228 44.950 39.981 1.00 42.50 O ANISOU 4223 O ALA B 44 4186 6919 5041 -39 393 206 O ATOM 4224 CB ALA B 44 -4.407 43.390 42.676 1.00 37.26 C ANISOU 4224 CB ALA B 44 3612 6239 4306 436 606 219 C ATOM 4225 N ASP B 45 -2.683 45.817 42.044 1.00 55.44 N ANISOU 4225 N ASP B 45 5957 8519 6586 116 204 127 N ATOM 4226 CA ASP B 45 -1.407 46.495 41.782 1.00 52.54 C ANISOU 4226 CA ASP B 45 5522 8213 6227 -73 20 170 C ATOM 4227 C ASP B 45 -0.492 45.902 42.812 1.00 52.39 C ANISOU 4227 C ASP B 45 5466 8310 6129 51 31 151 C ATOM 4228 O ASP B 45 -0.981 45.200 43.706 1.00 44.12 O ANISOU 4228 O ASP B 45 4477 7267 5020 271 150 106 O ATOM 4229 CB ASP B 45 -1.511 47.947 42.272 1.00 54.14 C ANISOU 4229 CB ASP B 45 5877 8233 6462 -119 -277 111 C ATOM 4230 CG ASP B 45 -1.345 48.949 41.188 1.00 55.62 C ANISOU 4230 CG ASP B 45 6030 8342 6759 -402 -465 217 C ATOM 4231 OD1 ASP B 45 -0.981 48.556 40.063 1.00 73.87 O ANISOU 4231 OD1 ASP B 45 8169 10817 9080 -566 -345 352 O ATOM 4232 OD2 ASP B 45 -1.590 50.145 41.463 1.00 53.95 O ANISOU 4232 OD2 ASP B 45 5969 7911 6617 -442 -755 165 O ATOM 4233 N LYS B 46 0.798 46.271 42.772 1.00 36.67 N ANISOU 4233 N LYS B 46 3370 6422 4141 -94 -120 213 N ATOM 4234 CA LYS B 46 1.693 45.995 43.897 1.00 49.68 C ANISOU 4234 CA LYS B 46 5007 8149 5720 15 -188 185 C ATOM 4235 C LYS B 46 1.301 46.784 45.164 1.00 48.06 C ANISOU 4235 C LYS B 46 5019 7781 5461 161 -389 52 C ATOM 4236 O LYS B 46 1.835 46.522 46.229 1.00 50.97 O ANISOU 4236 O LYS B 46 5415 8211 5739 304 -440 5 O ATOM 4237 CB LYS B 46 3.151 46.318 43.547 1.00 41.62 C ANISOU 4237 CB LYS B 46 3794 7290 4730 -195 -338 312 C ATOM 4238 CG LYS B 46 3.439 47.809 43.590 1.00 50.64 C ANISOU 4238 CG LYS B 46 4999 8276 5967 -418 -699 359 C ATOM 4239 CD LYS B 46 4.722 48.169 42.871 1.00 54.54 C ANISOU 4239 CD LYS B 46 5229 8971 6525 -711 -831 591 C ATOM 4240 CE LYS B 46 4.933 49.678 42.866 1.00 58.59 C ANISOU 4240 CE LYS B 46 5809 9265 7190 -983 -1258 688 C ATOM 4241 NZ LYS B 46 6.311 50.035 42.388 1.00 65.21 N ANISOU 4241 NZ LYS B 46 6343 10331 8102 -1295 -1431 985 N ATOM 4242 N THR B 47 0.390 47.749 45.046 1.00 45.26 N ANISOU 4242 N THR B 47 4819 7234 5144 158 -520 -23 N ATOM 4243 CA THR B 47 -0.028 48.537 46.206 1.00 47.51 C ANISOU 4243 CA THR B 47 5325 7384 5342 370 -735 -200 C ATOM 4244 C THR B 47 -1.357 48.087 46.814 1.00 44.54 C ANISOU 4244 C THR B 47 5041 7053 4830 685 -516 -286 C ATOM 4245 O THR B 47 -1.827 48.674 47.785 1.00 54.92 O ANISOU 4245 O THR B 47 6523 8330 6012 941 -653 -449 O ATOM 4246 CB THR B 47 -0.119 50.056 45.903 1.00 45.91 C ANISOU 4246 CB THR B 47 5265 6918 5261 227 -1121 -263 C ATOM 4247 OG1 THR B 47 -1.266 50.326 45.084 1.00 52.18 O ANISOU 4247 OG1 THR B 47 6097 7611 6119 207 -1028 -259 O ATOM 4248 CG2 THR B 47 1.135 50.556 45.207 1.00 43.27 C ANISOU 4248 CG2 THR B 47 4790 6565 5088 -144 -1355 -85 C ATOM 4249 N GLY B 48 -1.964 47.052 46.248 1.00 46.54 N ANISOU 4249 N GLY B 48 5171 7402 5108 680 -199 -169 N ATOM 4250 CA GLY B 48 -3.206 46.528 46.792 1.00 45.63 C ANISOU 4250 CA GLY B 48 5079 7368 4890 932 12 -164 C ATOM 4251 C GLY B 48 -4.302 46.255 45.767 1.00 43.94 C ANISOU 4251 C GLY B 48 4803 7098 4792 847 183 -78 C ATOM 4252 O GLY B 48 -4.078 46.295 44.549 1.00 38.59 O ANISOU 4252 O GLY B 48 4065 6338 4261 602 174 -28 O ATOM 4253 N SER B 49 -5.509 45.997 46.254 1.00 41.27 N ANISOU 4253 N SER B 49 4464 6841 4376 1056 331 -45 N ATOM 4254 CA SER B 49 -6.573 45.579 45.362 1.00 37.36 C ANISOU 4254 CA SER B 49 3886 6304 4005 974 488 67 C ATOM 4255 C SER B 49 -7.784 46.486 45.466 1.00 43.64 C ANISOU 4255 C SER B 49 4751 7077 4754 1130 447 -6 C ATOM 4256 O SER B 49 -7.977 47.171 46.483 1.00 46.87 O ANISOU 4256 O SER B 49 5258 7569 4982 1399 354 -135 O ATOM 4257 CB SER B 49 -6.958 44.119 45.642 1.00 41.72 C ANISOU 4257 CB SER B 49 4296 6982 4575 1022 717 270 C ATOM 4258 OG SER B 49 -7.653 43.987 46.865 1.00 46.80 O ANISOU 4258 OG SER B 49 4912 7830 5041 1292 811 343 O ATOM 4259 N ILE B 50 -8.607 46.478 44.421 1.00 45.90 N ANISOU 4259 N ILE B 50 4988 7265 5188 995 503 61 N ATOM 4260 CA ILE B 50 -9.833 47.260 44.410 1.00 41.95 C ANISOU 4260 CA ILE B 50 4525 6751 4665 1147 477 10 C ATOM 4261 C ILE B 50 -10.830 46.623 43.430 1.00 42.97 C ANISOU 4261 C ILE B 50 4522 6848 4958 1005 628 179 C ATOM 4262 O ILE B 50 -10.428 45.905 42.511 1.00 44.83 O ANISOU 4262 O ILE B 50 4702 6995 5338 761 667 261 O ATOM 4263 CB ILE B 50 -9.534 48.730 44.035 1.00 45.18 C ANISOU 4263 CB ILE B 50 5114 6942 5112 1099 174 -191 C ATOM 4264 CG1 ILE B 50 -10.674 49.655 44.483 1.00 46.86 C ANISOU 4264 CG1 ILE B 50 5408 7167 5230 1401 91 -322 C ATOM 4265 CG2 ILE B 50 -9.268 48.859 42.549 1.00 40.95 C ANISOU 4265 CG2 ILE B 50 4557 6221 4782 746 112 -124 C ATOM 4266 CD1 ILE B 50 -10.451 51.131 44.145 1.00 41.69 C ANISOU 4266 CD1 ILE B 50 4961 6230 4650 1371 -280 -523 C ATOM 4267 N ASN B 51 -12.122 46.857 43.634 1.00 46.54 N ANISOU 4267 N ASN B 51 4915 7393 5376 1181 698 227 N ATOM 4268 CA ASN B 51 -13.126 46.332 42.709 1.00 46.00 C ANISOU 4268 CA ASN B 51 4718 7278 5483 1037 798 394 C ATOM 4269 C ASN B 51 -13.367 47.304 41.577 1.00 45.90 C ANISOU 4269 C ASN B 51 4805 7046 5590 895 635 279 C ATOM 4270 O ASN B 51 -13.420 48.522 41.803 1.00 55.35 O ANISOU 4270 O ASN B 51 6136 8178 6716 1030 465 103 O ATOM 4271 CB ASN B 51 -14.460 46.096 43.424 1.00 41.67 C ANISOU 4271 CB ASN B 51 4000 6979 4852 1276 955 561 C ATOM 4272 CG ASN B 51 -14.377 45.020 44.475 1.00 51.37 C ANISOU 4272 CG ASN B 51 5081 8460 5979 1380 1126 775 C ATOM 4273 OD1 ASN B 51 -13.448 44.209 44.485 1.00 55.06 O ANISOU 4273 OD1 ASN B 51 5562 8856 6501 1232 1132 820 O ATOM 4274 ND2 ASN B 51 -15.356 44.999 45.365 1.00 57.61 N ANISOU 4274 ND2 ASN B 51 5708 9573 6609 1648 1262 929 N ATOM 4275 N ILE B 52 -13.521 46.786 40.365 1.00 40.35 N ANISOU 4275 N ILE B 52 4050 6217 5064 638 652 371 N ATOM 4276 CA ILE B 52 -14.015 47.613 39.264 1.00 42.55 C ANISOU 4276 CA ILE B 52 4388 6329 5450 512 521 320 C ATOM 4277 C ILE B 52 -15.342 47.015 38.783 1.00 41.62 C ANISOU 4277 C ILE B 52 4123 6235 5456 492 625 485 C ATOM 4278 O ILE B 52 -15.462 45.794 38.660 1.00 38.92 O ANISOU 4278 O ILE B 52 3664 5925 5197 403 733 637 O ATOM 4279 CB ILE B 52 -12.979 47.728 38.094 1.00 41.60 C ANISOU 4279 CB ILE B 52 4338 6070 5399 222 408 280 C ATOM 4280 CG1 ILE B 52 -13.507 48.638 36.977 1.00 44.33 C ANISOU 4280 CG1 ILE B 52 4740 6266 5838 88 259 265 C ATOM 4281 CG2 ILE B 52 -12.638 46.359 37.508 1.00 40.04 C ANISOU 4281 CG2 ILE B 52 4046 5905 5263 83 527 373 C ATOM 4282 CD1 ILE B 52 -12.489 48.872 35.853 1.00 42.37 C ANISOU 4282 CD1 ILE B 52 4526 5964 5609 -185 150 275 C ATOM 4283 N SER B 53 -16.350 47.852 38.549 1.00 38.99 N ANISOU 4283 N SER B 53 3791 5872 5150 580 561 462 N ATOM 4284 CA SER B 53 -17.610 47.346 38.016 1.00 41.59 C ANISOU 4284 CA SER B 53 3963 6223 5618 535 630 636 C ATOM 4285 C SER B 53 -17.662 47.674 36.543 1.00 35.40 C ANISOU 4285 C SER B 53 3256 5224 4971 289 490 598 C ATOM 4286 O SER B 53 -17.444 48.822 36.148 1.00 40.53 O ANISOU 4286 O SER B 53 4044 5753 5601 272 329 465 O ATOM 4287 CB SER B 53 -18.825 47.922 38.756 1.00 45.05 C ANISOU 4287 CB SER B 53 4292 6844 5980 833 681 676 C ATOM 4288 OG SER B 53 -18.759 47.586 40.132 1.00 46.97 O ANISOU 4288 OG SER B 53 4444 7360 6042 1086 826 731 O ATOM 4289 N VAL B 54 -17.923 46.655 35.729 1.00 37.09 N ANISOU 4289 N VAL B 54 3388 5383 5324 101 518 719 N ATOM 4290 CA VAL B 54 -17.859 46.807 34.283 1.00 38.32 C ANISOU 4290 CA VAL B 54 3617 5379 5563 -119 390 676 C ATOM 4291 C VAL B 54 -19.191 46.486 33.652 1.00 37.84 C ANISOU 4291 C VAL B 54 3442 5272 5665 -171 363 809 C ATOM 4292 O VAL B 54 -19.715 45.378 33.825 1.00 37.73 O ANISOU 4292 O VAL B 54 3290 5280 5764 -196 418 964 O ATOM 4293 CB VAL B 54 -16.771 45.907 33.686 1.00 42.25 C ANISOU 4293 CB VAL B 54 4160 5849 6045 -273 389 634 C ATOM 4294 CG1 VAL B 54 -16.734 46.060 32.168 1.00 39.10 C ANISOU 4294 CG1 VAL B 54 3821 5363 5672 -454 266 591 C ATOM 4295 CG2 VAL B 54 -15.399 46.270 34.291 1.00 40.71 C ANISOU 4295 CG2 VAL B 54 4048 5723 5697 -237 406 527 C ATOM 4296 N TRP B 55 -19.738 47.464 32.934 1.00 40.39 N ANISOU 4296 N TRP B 55 3815 5513 6017 -202 245 769 N ATOM 4297 CA TRP B 55 -21.026 47.301 32.268 1.00 41.46 C ANISOU 4297 CA TRP B 55 3841 5602 6309 -254 191 890 C ATOM 4298 C TRP B 55 -20.835 46.685 30.890 1.00 43.83 C ANISOU 4298 C TRP B 55 4200 5774 6681 -486 79 874 C ATOM 4299 O TRP B 55 -19.786 46.877 30.259 1.00 42.67 O ANISOU 4299 O TRP B 55 4188 5603 6422 -585 29 754 O ATOM 4300 CB TRP B 55 -21.685 48.670 32.073 1.00 40.03 C ANISOU 4300 CB TRP B 55 3704 5382 6124 -160 85 839 C ATOM 4301 CG TRP B 55 -22.527 49.128 33.210 1.00 38.71 C ANISOU 4301 CG TRP B 55 3416 5373 5921 134 167 878 C ATOM 4302 CD1 TRP B 55 -23.886 49.316 33.193 1.00 38.43 C ANISOU 4302 CD1 TRP B 55 3211 5417 5975 249 167 998 C ATOM 4303 CD2 TRP B 55 -22.090 49.487 34.531 1.00 42.39 C ANISOU 4303 CD2 TRP B 55 3904 5983 6219 394 254 789 C ATOM 4304 NE1 TRP B 55 -24.307 49.758 34.411 1.00 39.02 N ANISOU 4304 NE1 TRP B 55 3187 5714 5924 588 269 988 N ATOM 4305 CE2 TRP B 55 -23.234 49.880 35.251 1.00 44.03 C ANISOU 4305 CE2 TRP B 55 3952 6385 6391 692 315 847 C ATOM 4306 CE3 TRP B 55 -20.844 49.522 35.168 1.00 42.48 C ANISOU 4306 CE3 TRP B 55 4047 6000 6093 421 275 663 C ATOM 4307 CZ2 TRP B 55 -23.179 50.294 36.585 1.00 46.03 C ANISOU 4307 CZ2 TRP B 55 4189 6857 6443 1048 398 760 C ATOM 4308 CZ3 TRP B 55 -20.790 49.932 36.489 1.00 48.02 C ANISOU 4308 CZ3 TRP B 55 4746 6871 6628 738 336 582 C ATOM 4309 CH2 TRP B 55 -21.955 50.313 37.185 1.00 44.18 C ANISOU 4309 CH2 TRP B 55 4114 6595 6077 1064 397 619 C ATOM 4310 N ASP B 56 -21.853 45.960 30.426 1.00 54.08 N ANISOU 4310 N ASP B 56 4625 7922 8000 358 -740 968 N ATOM 4311 CA ASP B 56 -21.984 45.580 29.011 1.00 50.74 C ANISOU 4311 CA ASP B 56 4131 7729 7417 312 -1093 775 C ATOM 4312 C ASP B 56 -20.939 44.575 28.505 1.00 47.17 C ANISOU 4312 C ASP B 56 4000 7025 6896 43 -1170 578 C ATOM 4313 O ASP B 56 -20.285 43.907 29.309 1.00 48.79 O ANISOU 4313 O ASP B 56 4430 6903 7206 -143 -948 569 O ATOM 4314 CB ASP B 56 -22.051 46.831 28.132 1.00 49.87 C ANISOU 4314 CB ASP B 56 4099 7853 6998 790 -1210 918 C ATOM 4315 CG ASP B 56 -23.135 47.801 28.595 1.00 62.21 C ANISOU 4315 CG ASP B 56 5354 9684 8597 1110 -1123 1125 C ATOM 4316 OD1 ASP B 56 -24.277 47.340 28.845 1.00 55.34 O ANISOU 4316 OD1 ASP B 56 3987 9121 7919 962 -1234 1014 O ATOM 4317 OD2 ASP B 56 -22.850 49.018 28.726 1.00 59.21 O ANISOU 4317 OD2 ASP B 56 5229 9193 8075 1490 -893 1369 O ATOM 4318 N ASP B 57 -20.818 44.460 27.185 1.00 48.56 N ANISOU 4318 N ASP B 57 4198 7390 6862 81 -1477 428 N ATOM 4319 CA ASP B 57 -20.096 43.355 26.566 1.00 47.93 C ANISOU 4319 CA ASP B 57 4316 7146 6750 -226 -1602 193 C ATOM 4320 C ASP B 57 -18.631 43.202 26.969 1.00 45.55 C ANISOU 4320 C ASP B 57 4538 6418 6353 -251 -1412 234 C ATOM 4321 O ASP B 57 -18.162 42.070 27.156 1.00 48.17 O ANISOU 4321 O ASP B 57 5018 6518 6766 -537 -1349 102 O ATOM 4322 CB ASP B 57 -20.215 43.404 25.040 1.00 86.01 C ANISOU 4322 CB ASP B 57 9062 12308 11312 -102 -1982 27 C ATOM 4323 CG ASP B 57 -21.628 43.097 24.544 1.00104.82 C ANISOU 4323 CG ASP B 57 10817 15237 13774 -161 -2230 -216 C ATOM 4324 OD1 ASP B 57 -22.392 42.410 25.260 1.00107.49 O ANISOU 4324 OD1 ASP B 57 10805 15578 14459 -513 -2086 -367 O ATOM 4325 OD2 ASP B 57 -21.970 43.543 23.425 1.00112.56 O ANISOU 4325 OD2 ASP B 57 11648 16674 14447 175 -2542 -293 O ATOM 4326 N VAL B 58 -17.904 44.310 27.104 1.00 44.62 N ANISOU 4326 N VAL B 58 4693 6205 6057 56 -1276 372 N ATOM 4327 CA VAL B 58 -16.503 44.198 27.487 1.00 46.32 C ANISOU 4327 CA VAL B 58 5313 6125 6164 39 -1100 289 C ATOM 4328 C VAL B 58 -16.401 43.394 28.784 1.00 50.39 C ANISOU 4328 C VAL B 58 5820 6491 6836 -90 -877 294 C ATOM 4329 O VAL B 58 -15.489 42.583 28.949 1.00 48.85 O ANISOU 4329 O VAL B 58 5889 6124 6547 -173 -828 169 O ATOM 4330 CB VAL B 58 -15.755 45.564 27.574 1.00 50.89 C ANISOU 4330 CB VAL B 58 6125 6619 6592 328 -865 322 C ATOM 4331 CG1 VAL B 58 -16.435 46.505 28.538 1.00 42.92 C ANISOU 4331 CG1 VAL B 58 4909 5678 5722 519 -614 510 C ATOM 4332 CG2 VAL B 58 -14.290 45.342 27.995 1.00 48.72 C ANISOU 4332 CG2 VAL B 58 6161 6148 6203 276 -697 88 C ATOM 4333 N GLY B 59 -17.392 43.557 29.659 1.00 48.29 N ANISOU 4333 N GLY B 59 5264 6302 6781 -66 -732 453 N ATOM 4334 CA GLY B 59 -17.473 42.754 30.868 1.00 42.85 C ANISOU 4334 CA GLY B 59 4586 5460 6234 -134 -466 507 C ATOM 4335 C GLY B 59 -17.378 41.248 30.664 1.00 48.23 C ANISOU 4335 C GLY B 59 5405 5937 6982 -418 -442 395 C ATOM 4336 O GLY B 59 -16.878 40.548 31.549 1.00 42.39 O ANISOU 4336 O GLY B 59 4910 4994 6203 -342 -164 439 O ATOM 4337 N ASN B 60 -17.861 40.735 29.526 1.00 41.88 N ANISOU 4337 N ASN B 60 4453 5201 6258 -700 -687 237 N ATOM 4338 CA ASN B 60 -17.746 39.303 29.231 1.00 46.57 C ANISOU 4338 CA ASN B 60 5187 5559 6947 -1024 -607 75 C ATOM 4339 C ASN B 60 -16.407 38.893 28.625 1.00 49.22 C ANISOU 4339 C ASN B 60 5945 5753 7002 -988 -730 -38 C ATOM 4340 O ASN B 60 -16.087 37.708 28.565 1.00 51.78 O ANISOU 4340 O ASN B 60 6500 5817 7356 -1176 -583 -128 O ATOM 4341 CB ASN B 60 -18.862 38.876 28.282 1.00 51.48 C ANISOU 4341 CB ASN B 60 5386 6379 7794 -1383 -799 -166 C ATOM 4342 CG ASN B 60 -20.227 39.071 28.888 1.00 58.34 C ANISOU 4342 CG ASN B 60 5793 7404 8969 -1476 -643 -144 C ATOM 4343 OD1 ASN B 60 -20.428 38.804 30.077 1.00 56.93 O ANISOU 4343 OD1 ASN B 60 5693 6975 8961 -1467 -236 21 O ATOM 4344 ND2 ASN B 60 -21.173 39.567 28.084 1.00 54.70 N ANISOU 4344 ND2 ASN B 60 4845 7399 8540 -1506 -959 -314 N ATOM 4345 N LEU B 61 -15.653 39.871 28.133 1.00 38.32 N ANISOU 4345 N LEU B 61 4677 4519 5363 -758 -952 -50 N ATOM 4346 CA LEU B 61 -14.362 39.590 27.517 1.00 45.70 C ANISOU 4346 CA LEU B 61 5982 5351 6030 -729 -1073 -200 C ATOM 4347 C LEU B 61 -13.262 39.467 28.584 1.00 46.95 C ANISOU 4347 C LEU B 61 6453 5397 5989 -460 -813 -190 C ATOM 4348 O LEU B 61 -12.359 38.649 28.449 1.00 53.42 O ANISOU 4348 O LEU B 61 7585 6083 6630 -455 -796 -305 O ATOM 4349 CB LEU B 61 -14.013 40.663 26.486 1.00 37.58 C ANISOU 4349 CB LEU B 61 4967 4492 4821 -606 -1333 -260 C ATOM 4350 CG LEU B 61 -15.024 40.788 25.351 1.00 46.67 C ANISOU 4350 CG LEU B 61 5820 5874 6039 -716 -1627 -288 C ATOM 4351 CD1 LEU B 61 -14.671 41.949 24.433 1.00 42.39 C ANISOU 4351 CD1 LEU B 61 5392 5459 5257 -449 -1771 -263 C ATOM 4352 CD2 LEU B 61 -15.115 39.478 24.567 1.00 40.68 C ANISOU 4352 CD2 LEU B 61 5048 5069 5341 -1064 -1795 -505 C ATOM 4353 N ILE B 62 -13.376 40.236 29.669 1.00 38.53 N ANISOU 4353 N ILE B 62 3911 6031 4697 -503 -502 -221 N ATOM 4354 CA ILE B 62 -12.362 40.250 30.740 1.00 39.95 C ANISOU 4354 CA ILE B 62 4141 6152 4886 -441 -358 -105 C ATOM 4355 C ILE B 62 -12.166 38.877 31.406 1.00 42.96 C ANISOU 4355 C ILE B 62 4492 6376 5455 -513 -270 -57 C ATOM 4356 O ILE B 62 -13.143 38.189 31.748 1.00 42.66 O ANISOU 4356 O ILE B 62 4331 6296 5583 -608 -255 -21 O ATOM 4357 CB ILE B 62 -12.724 41.294 31.804 1.00 43.47 C ANISOU 4357 CB ILE B 62 4527 6712 5278 -353 -314 22 C ATOM 4358 CG1 ILE B 62 -12.780 42.683 31.162 1.00 40.64 C ANISOU 4358 CG1 ILE B 62 4216 6457 4770 -265 -381 -8 C ATOM 4359 CG2 ILE B 62 -11.714 41.276 32.940 1.00 40.95 C ANISOU 4359 CG2 ILE B 62 4266 6358 4936 -288 -217 115 C ATOM 4360 CD1 ILE B 62 -13.328 43.763 32.080 1.00 47.53 C ANISOU 4360 CD1 ILE B 62 5026 7420 5612 -173 -341 76 C ATOM 4361 N GLN B 63 -10.910 38.470 31.581 1.00 38.11 N ANISOU 4361 N GLN B 63 3973 5660 4848 -466 -201 -41 N ATOM 4362 CA GLN B 63 -10.607 37.176 32.200 1.00 39.01 C ANISOU 4362 CA GLN B 63 4076 5599 5145 -498 -115 35 C ATOM 4363 C GLN B 63 -9.620 37.343 33.358 1.00 35.99 C ANISOU 4363 C GLN B 63 3727 5230 4717 -376 -55 195 C ATOM 4364 O GLN B 63 -8.737 38.197 33.298 1.00 40.61 O ANISOU 4364 O GLN B 63 4356 5893 5181 -290 -85 167 O ATOM 4365 CB GLN B 63 -10.008 36.195 31.168 1.00 39.94 C ANISOU 4365 CB GLN B 63 4271 5537 5366 -545 -108 -125 C ATOM 4366 CG GLN B 63 -10.883 35.845 29.979 1.00 35.62 C ANISOU 4366 CG GLN B 63 3721 4966 4846 -668 -204 -330 C ATOM 4367 CD GLN B 63 -12.204 35.193 30.388 1.00 60.55 C ANISOU 4367 CD GLN B 63 6728 8066 8211 -808 -224 -296 C ATOM 4368 OE1 GLN B 63 -12.224 34.189 31.106 1.00 66.79 O ANISOU 4368 OE1 GLN B 63 7478 8674 9227 -857 -116 -189 O ATOM 4369 NE2 GLN B 63 -13.316 35.771 29.934 1.00 65.48 N ANISOU 4369 NE2 GLN B 63 7255 8839 8787 -867 -354 -367 N ATOM 4370 N PRO B 64 -9.741 36.498 34.393 1.00 36.49 N ANISOU 4370 N PRO B 64 3768 5209 4888 -368 24 366 N ATOM 4371 CA PRO B 64 -8.734 36.498 35.464 1.00 36.93 C ANISOU 4371 CA PRO B 64 3869 5282 4879 -232 38 518 C ATOM 4372 C PRO B 64 -7.351 36.289 34.844 1.00 41.19 C ANISOU 4372 C PRO B 64 4445 5728 5478 -172 7 426 C ATOM 4373 O PRO B 64 -7.222 35.448 33.942 1.00 39.30 O ANISOU 4373 O PRO B 64 4220 5317 5395 -230 47 321 O ATOM 4374 CB PRO B 64 -9.121 35.279 36.309 1.00 37.39 C ANISOU 4374 CB PRO B 64 3923 5200 5085 -244 147 721 C ATOM 4375 CG PRO B 64 -10.610 35.113 36.065 1.00 41.23 C ANISOU 4375 CG PRO B 64 4320 5676 5671 -393 207 702 C ATOM 4376 CD PRO B 64 -10.827 35.520 34.630 1.00 38.84 C ANISOU 4376 CD PRO B 64 3991 5390 5376 -484 101 441 C ATOM 4377 N GLY B 65 -6.359 37.058 35.296 1.00 33.70 N ANISOU 4377 N GLY B 65 3498 4885 4423 -62 -58 443 N ATOM 4378 CA GLY B 65 -5.011 36.980 34.759 1.00 35.21 C ANISOU 4378 CA GLY B 65 3673 5003 4704 -1 -69 365 C ATOM 4379 C GLY B 65 -4.733 38.089 33.746 1.00 42.46 C ANISOU 4379 C GLY B 65 4591 5998 5543 -35 -76 195 C ATOM 4380 O GLY B 65 -3.567 38.386 33.466 1.00 40.02 O ANISOU 4380 O GLY B 65 4239 5671 5294 19 -70 146 O ATOM 4381 N ASP B 66 -5.787 38.696 33.191 1.00 38.06 N ANISOU 4381 N ASP B 66 4070 5520 4872 -116 -81 124 N ATOM 4382 CA ASP B 66 -5.636 39.790 32.220 1.00 35.97 C ANISOU 4382 CA ASP B 66 3835 5324 4510 -132 -78 8 C ATOM 4383 C ASP B 66 -4.932 41.000 32.829 1.00 35.30 C ANISOU 4383 C ASP B 66 3710 5328 4375 -74 -121 31 C ATOM 4384 O ASP B 66 -5.267 41.422 33.943 1.00 35.51 O ANISOU 4384 O ASP B 66 3718 5443 4330 -42 -190 99 O ATOM 4385 CB ASP B 66 -7.007 40.240 31.671 1.00 34.65 C ANISOU 4385 CB ASP B 66 3700 5239 4228 -199 -113 -35 C ATOM 4386 CG ASP B 66 -7.590 39.267 30.646 1.00 44.93 C ANISOU 4386 CG ASP B 66 5042 6456 5572 -279 -105 -140 C ATOM 4387 OD1 ASP B 66 -6.870 38.353 30.176 1.00 42.54 O ANISOU 4387 OD1 ASP B 66 4776 6017 5369 -279 -40 -206 O ATOM 4388 OD2 ASP B 66 -8.782 39.421 30.298 1.00 46.58 O ANISOU 4388 OD2 ASP B 66 5238 6734 5727 -339 -174 -174 O ATOM 4389 N ILE B 67 -3.954 41.556 32.111 1.00 33.85 N ANISOU 4389 N ILE B 67 3514 5111 4235 -64 -68 -37 N ATOM 4390 CA ILE B 67 -3.332 42.811 32.546 1.00 33.35 C ANISOU 4390 CA ILE B 67 3398 5099 4173 -44 -106 -45 C ATOM 4391 C ILE B 67 -4.017 43.923 31.758 1.00 31.76 C ANISOU 4391 C ILE B 67 3275 4937 3856 -78 -68 -78 C ATOM 4392 O ILE B 67 -4.025 43.914 30.526 1.00 36.97 O ANISOU 4392 O ILE B 67 4005 5562 4480 -96 28 -111 O ATOM 4393 CB ILE B 67 -1.807 42.850 32.314 1.00 32.15 C ANISOU 4393 CB ILE B 67 3141 4869 4205 -22 -52 -77 C ATOM 4394 CG1 ILE B 67 -1.121 41.742 33.104 1.00 35.12 C ANISOU 4394 CG1 ILE B 67 3426 5207 4711 46 -115 -23 C ATOM 4395 CG2 ILE B 67 -1.222 44.237 32.705 1.00 27.96 C ANISOU 4395 CG2 ILE B 67 2535 4363 3723 -38 -99 -113 C ATOM 4396 CD1 ILE B 67 0.368 41.652 32.842 1.00 37.50 C ANISOU 4396 CD1 ILE B 67 3574 5430 5245 83 -61 -53 C ATOM 4397 N ILE B 68 -4.626 44.864 32.462 1.00 36.03 N ANISOU 4397 N ILE B 68 3822 5550 4319 -66 -140 -65 N ATOM 4398 CA ILE B 68 -5.508 45.821 31.804 1.00 33.60 C ANISOU 4398 CA ILE B 68 3585 5272 3909 -69 -119 -66 C ATOM 4399 C ILE B 68 -5.088 47.262 32.109 1.00 39.45 C ANISOU 4399 C ILE B 68 4316 5980 4693 -56 -116 -89 C ATOM 4400 O ILE B 68 -4.741 47.584 33.256 1.00 37.28 O ANISOU 4400 O ILE B 68 3989 5721 4456 -42 -193 -127 O ATOM 4401 CB ILE B 68 -6.994 45.531 32.170 1.00 34.59 C ANISOU 4401 CB ILE B 68 3721 5489 3933 -60 -179 -31 C ATOM 4402 CG1 ILE B 68 -7.434 44.212 31.502 1.00 36.53 C ANISOU 4402 CG1 ILE B 68 3977 5719 4182 -107 -173 -36 C ATOM 4403 CG2 ILE B 68 -7.889 46.709 31.778 1.00 36.19 C ANISOU 4403 CG2 ILE B 68 3960 5731 4059 -25 -187 -19 C ATOM 4404 CD1 ILE B 68 -8.897 43.873 31.601 1.00 44.04 C ANISOU 4404 CD1 ILE B 68 4896 6741 5098 -129 -225 -13 C ATOM 4405 N ARG B 69 -5.072 48.112 31.075 1.00 37.04 N ANISOU 4405 N ARG B 69 4074 5619 4382 -59 -27 -69 N ATOM 4406 CA ARG B 69 -4.887 49.556 31.264 1.00 33.46 C ANISOU 4406 CA ARG B 69 3626 5089 3999 -52 -4 -78 C ATOM 4407 C ARG B 69 -6.252 50.249 31.227 1.00 37.59 C ANISOU 4407 C ARG B 69 4218 5658 4405 14 -38 -37 C ATOM 4408 O ARG B 69 -7.011 50.076 30.255 1.00 32.35 O ANISOU 4408 O ARG B 69 3623 5041 3626 46 -26 32 O ATOM 4409 CB ARG B 69 -4.008 50.151 30.163 1.00 33.98 C ANISOU 4409 CB ARG B 69 3719 5030 4160 -83 156 -35 C ATOM 4410 CG ARG B 69 -3.736 51.639 30.339 1.00 46.39 C ANISOU 4410 CG ARG B 69 5289 6466 5873 -96 205 -38 C ATOM 4411 CD ARG B 69 -3.035 52.257 29.114 1.00 58.87 C ANISOU 4411 CD ARG B 69 6919 7909 7541 -122 418 63 C ATOM 4412 NE ARG B 69 -1.853 51.508 28.698 1.00 72.54 N ANISOU 4412 NE ARG B 69 8563 9617 9381 -177 533 51 N ATOM 4413 CZ ARG B 69 -0.649 51.660 29.243 1.00 83.68 C ANISOU 4413 CZ ARG B 69 9795 10934 11068 -257 552 -24 C ATOM 4414 NH1 ARG B 69 -0.472 52.536 30.229 1.00 85.16 N ANISOU 4414 NH1 ARG B 69 9893 11042 11422 -304 440 -118 N ATOM 4415 NH2 ARG B 69 0.380 50.941 28.803 1.00 82.33 N ANISOU 4415 NH2 ARG B 69 9521 10744 11016 -285 676 -23 N ATOM 4416 N LEU B 70 -6.548 51.032 32.271 1.00 33.97 N ANISOU 4416 N LEU B 70 3741 5190 3978 47 -90 -93 N ATOM 4417 CA LEU B 70 -7.767 51.847 32.337 1.00 40.70 C ANISOU 4417 CA LEU B 70 4635 6059 4771 134 -98 -63 C ATOM 4418 C LEU B 70 -7.384 53.298 32.045 1.00 41.48 C ANISOU 4418 C LEU B 70 4783 5980 4998 150 -22 -62 C ATOM 4419 O LEU B 70 -6.405 53.797 32.589 1.00 34.21 O ANISOU 4419 O LEU B 70 3831 4947 4221 90 -14 -160 O ATOM 4420 CB LEU B 70 -8.397 51.757 33.735 1.00 36.16 C ANISOU 4420 CB LEU B 70 4023 5575 4141 180 -160 -137 C ATOM 4421 CG LEU B 70 -9.471 52.789 34.108 1.00 37.79 C ANISOU 4421 CG LEU B 70 4251 5770 4338 289 -137 -148 C ATOM 4422 CD1 LEU B 70 -10.627 52.748 33.129 1.00 29.12 C ANISOU 4422 CD1 LEU B 70 3137 4725 3201 353 -131 -22 C ATOM 4423 CD2 LEU B 70 -10.005 52.573 35.551 1.00 33.45 C ANISOU 4423 CD2 LEU B 70 3682 5331 3697 342 -152 -227 C ATOM 4424 N THR B 71 -8.139 53.972 31.183 1.00 37.88 N ANISOU 4424 N THR B 71 4396 5486 4510 231 23 52 N ATOM 4425 CA THR B 71 -7.910 55.401 30.938 1.00 39.05 C ANISOU 4425 CA THR B 71 4606 5427 4804 265 116 86 C ATOM 4426 C THR B 71 -9.199 56.164 31.253 1.00 39.11 C ANISOU 4426 C THR B 71 4631 5433 4795 410 89 108 C ATOM 4427 O THR B 71 -10.299 55.643 31.025 1.00 44.51 O ANISOU 4427 O THR B 71 5286 6281 5346 489 18 175 O ATOM 4428 CB THR B 71 -7.412 55.679 29.489 1.00 47.57 C ANISOU 4428 CB THR B 71 5778 6411 5885 258 244 255 C ATOM 4429 OG1 THR B 71 -8.339 55.117 28.560 1.00 66.01 O ANISOU 4429 OG1 THR B 71 8174 8907 8001 343 188 377 O ATOM 4430 CG2 THR B 71 -6.086 55.013 29.257 1.00 39.89 C ANISOU 4430 CG2 THR B 71 4762 5419 4976 127 316 218 C ATOM 4431 N LYS B 72 -9.064 57.369 31.809 1.00 39.90 N ANISOU 4431 N LYS B 72 4759 5339 5062 441 143 34 N ATOM 4432 CA LYS B 72 -10.220 58.158 32.265 1.00 41.60 C ANISOU 4432 CA LYS B 72 4982 5522 5301 598 144 23 C ATOM 4433 C LYS B 72 -11.181 57.414 33.201 1.00 44.02 C ANISOU 4433 C LYS B 72 5203 6053 5468 656 71 -60 C ATOM 4434 O LYS B 72 -12.409 57.503 33.065 1.00 43.61 O ANISOU 4434 O LYS B 72 5103 6082 5383 792 63 21 O ATOM 4435 CB LYS B 72 -10.975 58.776 31.082 1.00 45.01 C ANISOU 4435 CB LYS B 72 5473 5895 5735 739 182 250 C ATOM 4436 CG LYS B 72 -10.406 60.122 30.685 1.00 58.44 C ANISOU 4436 CG LYS B 72 7277 7279 7650 756 315 316 C ATOM 4437 CD LYS B 72 -10.787 60.526 29.275 1.00 67.92 C ANISOU 4437 CD LYS B 72 8576 8433 8797 876 359 605 C ATOM 4438 CE LYS B 72 -10.083 61.823 28.890 1.00 76.97 C ANISOU 4438 CE LYS B 72 9835 9224 10188 873 538 704 C ATOM 4439 NZ LYS B 72 -10.323 62.209 27.470 1.00 87.73 N ANISOU 4439 NZ LYS B 72 11334 10541 11458 1000 606 1033 N ATOM 4440 N GLY B 73 -10.612 56.691 34.155 1.00 44.93 N ANISOU 4440 N GLY B 73 5289 6265 5519 559 25 -206 N ATOM 4441 CA GLY B 73 -11.404 56.052 35.180 1.00 38.88 C ANISOU 4441 CA GLY B 73 4467 5685 4621 612 3 -270 C ATOM 4442 C GLY B 73 -11.877 57.081 36.186 1.00 45.46 C ANISOU 4442 C GLY B 73 5343 6437 5493 730 68 -417 C ATOM 4443 O GLY B 73 -11.372 58.203 36.230 1.00 51.43 O ANISOU 4443 O GLY B 73 6173 6972 6394 736 99 -514 O ATOM 4444 N TYR B 74 -12.865 56.701 36.988 1.00 40.07 N ANISOU 4444 N TYR B 74 4612 5915 4698 824 111 -437 N ATOM 4445 CA TYR B 74 -13.294 57.530 38.089 1.00 46.61 C ANISOU 4445 CA TYR B 74 5500 6698 5513 949 200 -608 C ATOM 4446 C TYR B 74 -13.696 56.583 39.193 1.00 51.52 C ANISOU 4446 C TYR B 74 6104 7553 5919 967 236 -641 C ATOM 4447 O TYR B 74 -13.914 55.398 38.948 1.00 46.16 O ANISOU 4447 O TYR B 74 5335 7033 5171 901 211 -495 O ATOM 4448 CB TYR B 74 -14.471 58.450 37.707 1.00 37.95 C ANISOU 4448 CB TYR B 74 4355 5508 4558 1132 306 -540 C ATOM 4449 CG TYR B 74 -15.762 57.722 37.418 1.00 42.34 C ANISOU 4449 CG TYR B 74 4738 6261 5090 1211 339 -366 C ATOM 4450 CD1 TYR B 74 -16.024 57.228 36.143 1.00 42.25 C ANISOU 4450 CD1 TYR B 74 4627 6299 5126 1170 239 -165 C ATOM 4451 CD2 TYR B 74 -16.731 57.546 38.403 1.00 41.25 C ANISOU 4451 CD2 TYR B 74 4529 6257 4888 1327 474 -413 C ATOM 4452 CE1 TYR B 74 -17.216 56.583 35.856 1.00 42.07 C ANISOU 4452 CE1 TYR B 74 4414 6448 5123 1224 231 -37 C ATOM 4453 CE2 TYR B 74 -17.924 56.880 38.129 1.00 38.25 C ANISOU 4453 CE2 TYR B 74 3939 6041 4553 1378 512 -254 C ATOM 4454 CZ TYR B 74 -18.151 56.405 36.854 1.00 42.43 C ANISOU 4454 CZ TYR B 74 4350 6609 5165 1316 369 -78 C ATOM 4455 OH TYR B 74 -19.306 55.745 36.558 1.00 45.50 O ANISOU 4455 OH TYR B 74 4505 7153 5632 1344 364 48 O ATOM 4456 N ALA B 75 -13.804 57.109 40.405 1.00 48.13 N ANISOU 4456 N ALA B 75 5777 7129 5381 1062 310 -835 N ATOM 4457 CA ALA B 75 -14.060 56.270 41.556 1.00 42.18 C ANISOU 4457 CA ALA B 75 5057 6598 4373 1094 367 -857 C ATOM 4458 C ALA B 75 -15.206 56.838 42.367 1.00 52.92 C ANISOU 4458 C ALA B 75 6434 8000 5674 1290 579 -933 C ATOM 4459 O ALA B 75 -15.418 58.056 42.419 1.00 59.04 O ANISOU 4459 O ALA B 75 7265 8601 6566 1401 643 -1082 O ATOM 4460 CB ALA B 75 -12.840 56.159 42.402 1.00 40.33 C ANISOU 4460 CB ALA B 75 4970 6388 3964 1020 229 -1036 C ATOM 4461 N SER B 76 -15.937 55.948 43.017 1.00 48.17 N ANISOU 4461 N SER B 76 5784 7610 4910 1337 716 -825 N ATOM 4462 CA SER B 76 -17.108 56.353 43.761 1.00 50.66 C ANISOU 4462 CA SER B 76 6080 7988 5180 1531 973 -863 C ATOM 4463 C SER B 76 -17.453 55.225 44.723 1.00 48.54 C ANISOU 4463 C SER B 76 5828 7960 4653 1541 1117 -754 C ATOM 4464 O SER B 76 -17.002 54.092 44.551 1.00 54.49 O ANISOU 4464 O SER B 76 6551 8804 5349 1398 1014 -598 O ATOM 4465 CB SER B 76 -18.250 56.621 42.781 1.00 51.56 C ANISOU 4465 CB SER B 76 5949 8043 5599 1601 1055 -703 C ATOM 4466 OG SER B 76 -19.441 56.936 43.472 1.00 58.47 O ANISOU 4466 OG SER B 76 6750 8986 6481 1796 1330 -718 O ATOM 4467 N VAL B 77 -18.233 55.533 45.745 1.00 54.55 N ANISOU 4467 N VAL B 77 6651 8813 5262 1719 1380 -828 N ATOM 4468 CA VAL B 77 -18.592 54.549 46.759 1.00 56.90 C ANISOU 4468 CA VAL B 77 6999 9335 5285 1755 1578 -703 C ATOM 4469 C VAL B 77 -19.970 53.960 46.435 1.00 62.23 C ANISOU 4469 C VAL B 77 7374 10081 6191 1777 1828 -452 C ATOM 4470 O VAL B 77 -20.954 54.699 46.331 1.00 63.25 O ANISOU 4470 O VAL B 77 7360 10163 6510 1923 2014 -488 O ATOM 4471 CB VAL B 77 -18.595 55.209 48.144 1.00 60.78 C ANISOU 4471 CB VAL B 77 7767 9907 5421 1947 1748 -941 C ATOM 4472 CG1 VAL B 77 -19.182 54.283 49.207 1.00 53.14 C ANISOU 4472 CG1 VAL B 77 6858 9178 4154 2030 2040 -769 C ATOM 4473 CG2 VAL B 77 -17.174 55.648 48.513 1.00 59.01 C ANISOU 4473 CG2 VAL B 77 7814 9631 4975 1894 1445 -1204 C ATOM 4474 N PHE B 78 -20.027 52.641 46.251 1.00 60.13 N ANISOU 4474 N PHE B 78 6990 9906 5950 1631 1823 -205 N ATOM 4475 CA PHE B 78 -21.284 51.941 46.001 1.00 59.24 C ANISOU 4475 CA PHE B 78 6567 9855 6087 1610 2047 27 C ATOM 4476 C PHE B 78 -21.508 50.882 47.088 1.00 62.32 C ANISOU 4476 C PHE B 78 7030 10405 6243 1612 2313 209 C ATOM 4477 O PHE B 78 -20.685 49.973 47.258 1.00 66.27 O ANISOU 4477 O PHE B 78 7668 10935 6576 1494 2184 309 O ATOM 4478 CB PHE B 78 -21.268 51.294 44.607 1.00 54.49 C ANISOU 4478 CB PHE B 78 5722 9170 5810 1408 1801 162 C ATOM 4479 CG PHE B 78 -22.540 50.544 44.258 1.00 56.92 C ANISOU 4479 CG PHE B 78 5672 9526 6430 1350 1969 368 C ATOM 4480 CD1 PHE B 78 -23.724 51.227 44.001 1.00 57.80 C ANISOU 4480 CD1 PHE B 78 5516 9634 6809 1477 2108 361 C ATOM 4481 CD2 PHE B 78 -22.546 49.159 44.169 1.00 45.44 C ANISOU 4481 CD2 PHE B 78 4124 8098 5043 1165 1977 561 C ATOM 4482 CE1 PHE B 78 -24.916 50.534 43.685 1.00 59.71 C ANISOU 4482 CE1 PHE B 78 5373 9926 7390 1411 2242 537 C ATOM 4483 CE2 PHE B 78 -23.704 48.462 43.839 1.00 52.57 C ANISOU 4483 CE2 PHE B 78 4669 9019 6285 1080 2116 726 C ATOM 4484 CZ PHE B 78 -24.903 49.151 43.604 1.00 58.42 C ANISOU 4484 CZ PHE B 78 5114 9782 7301 1197 2243 710 C ATOM 4485 N LYS B 79 -22.626 50.998 47.804 1.00 72.76 N ANISOU 4485 N LYS B 79 8267 11786 7594 1733 2671 265 N ATOM 4486 CA LYS B 79 -22.944 50.129 48.949 1.00 74.40 C ANISOU 4486 CA LYS B 79 8598 12050 7619 1703 2911 432 C ATOM 4487 C LYS B 79 -21.798 50.066 49.970 1.00 70.49 C ANISOU 4487 C LYS B 79 8534 11627 6624 1753 2806 347 C ATOM 4488 O LYS B 79 -21.359 48.975 50.348 1.00 66.72 O ANISOU 4488 O LYS B 79 8160 11192 6000 1663 2785 542 O ATOM 4489 CB LYS B 79 -23.342 48.714 48.485 1.00 69.66 C ANISOU 4489 CB LYS B 79 7746 11433 7287 1501 2956 731 C ATOM 4490 CG LYS B 79 -24.575 48.665 47.573 1.00 76.61 C ANISOU 4490 CG LYS B 79 8176 12246 8686 1425 3026 805 C ATOM 4491 CD LYS B 79 -25.048 47.225 47.334 1.00 81.05 C ANISOU 4491 CD LYS B 79 8515 12762 9520 1205 3096 1063 C ATOM 4492 CE LYS B 79 -26.168 47.136 46.293 1.00 79.76 C ANISOU 4492 CE LYS B 79 7886 12530 9888 1096 3057 1091 C ATOM 4493 NZ LYS B 79 -27.435 47.825 46.683 1.00 86.90 N ANISOU 4493 NZ LYS B 79 8604 13438 10977 1214 3298 1037 N ATOM 4494 N GLY B 80 -21.309 51.232 50.396 1.00 67.94 N ANISOU 4494 N GLY B 80 8449 11298 6066 1892 2715 50 N ATOM 4495 CA GLY B 80 -20.189 51.302 51.322 1.00 70.83 C ANISOU 4495 CA GLY B 80 9199 11728 5985 1930 2539 -85 C ATOM 4496 C GLY B 80 -18.816 50.978 50.731 1.00 72.97 C ANISOU 4496 C GLY B 80 9544 12003 6180 1828 2150 -116 C ATOM 4497 O GLY B 80 -17.796 51.101 51.420 1.00 72.18 O ANISOU 4497 O GLY B 80 9724 11945 5758 1850 1934 -255 O ATOM 4498 N CYS B 81 -18.778 50.579 49.460 1.00 65.01 N ANISOU 4498 N CYS B 81 8269 10955 5478 1712 2048 -1 N ATOM 4499 CA CYS B 81 -17.533 50.095 48.855 1.00 58.79 C ANISOU 4499 CA CYS B 81 7515 10103 4717 1554 1675 6 C ATOM 4500 C CYS B 81 -16.923 51.025 47.812 1.00 57.42 C ANISOU 4500 C CYS B 81 7275 9751 4792 1473 1379 -218 C ATOM 4501 O CYS B 81 -17.537 51.305 46.768 1.00 51.40 O ANISOU 4501 O CYS B 81 6274 8870 4387 1415 1390 -189 O ATOM 4502 CB CYS B 81 -17.726 48.690 48.265 1.00 48.54 C ANISOU 4502 CB CYS B 81 6019 8776 3648 1385 1696 325 C ATOM 4503 SG CYS B 81 -18.178 47.481 49.539 1.00 65.14 S ANISOU 4503 SG CYS B 81 8245 11030 5477 1451 2021 638 S ATOM 4504 N LEU B 82 -15.709 51.494 48.104 1.00 56.99 N ANISOU 4504 N LEU B 82 7427 9678 4548 1471 1112 -431 N ATOM 4505 CA LEU B 82 -14.942 52.288 47.151 1.00 49.28 C ANISOU 4505 CA LEU B 82 6397 8513 3815 1371 844 -615 C ATOM 4506 C LEU B 82 -14.779 51.451 45.901 1.00 50.30 C ANISOU 4506 C LEU B 82 6310 8555 4246 1191 731 -407 C ATOM 4507 O LEU B 82 -14.248 50.344 45.952 1.00 58.81 O ANISOU 4507 O LEU B 82 7394 9689 5263 1108 648 -248 O ATOM 4508 CB LEU B 82 -13.569 52.689 47.724 1.00 47.91 C ANISOU 4508 CB LEU B 82 6437 8344 3424 1363 562 -852 C ATOM 4509 CG LEU B 82 -12.649 53.414 46.726 1.00 54.99 C ANISOU 4509 CG LEU B 82 7254 9024 4615 1228 308 -1010 C ATOM 4510 CD1 LEU B 82 -13.310 54.681 46.183 1.00 57.10 C ANISOU 4510 CD1 LEU B 82 7464 9109 5123 1279 421 -1152 C ATOM 4511 CD2 LEU B 82 -11.253 53.744 47.308 1.00 53.12 C ANISOU 4511 CD2 LEU B 82 7169 8790 4226 1194 11 -1251 C ATOM 4512 N THR B 83 -15.258 51.971 44.781 1.00 47.12 N ANISOU 4512 N THR B 83 5731 8014 4159 1147 730 -408 N ATOM 4513 CA THR B 83 -15.301 51.198 43.538 1.00 41.19 C ANISOU 4513 CA THR B 83 4785 7198 3666 994 643 -230 C ATOM 4514 C THR B 83 -14.738 52.017 42.390 1.00 44.01 C ANISOU 4514 C THR B 83 5107 7381 4232 930 465 -333 C ATOM 4515 O THR B 83 -14.837 53.248 42.396 1.00 47.03 O ANISOU 4515 O THR B 83 5538 7666 4664 1017 481 -490 O ATOM 4516 CB THR B 83 -16.746 50.754 43.206 1.00 43.04 C ANISOU 4516 CB THR B 83 4797 7479 4076 1008 846 -53 C ATOM 4517 OG1 THR B 83 -17.316 50.077 44.342 1.00 45.20 O ANISOU 4517 OG1 THR B 83 5105 7899 4171 1074 1079 62 O ATOM 4518 CG2 THR B 83 -16.767 49.822 42.002 1.00 38.92 C ANISOU 4518 CG2 THR B 83 4100 6905 3781 840 726 95 C ATOM 4519 N LEU B 84 -14.136 51.330 41.418 1.00 35.95 N ANISOU 4519 N LEU B 84 4017 6308 3336 785 319 -239 N ATOM 4520 CA LEU B 84 -13.509 51.971 40.275 1.00 32.29 C ANISOU 4520 CA LEU B 84 3537 5689 3044 719 181 -295 C ATOM 4521 C LEU B 84 -14.420 51.754 39.061 1.00 41.14 C ANISOU 4521 C LEU B 84 4493 6792 4347 693 198 -157 C ATOM 4522 O LEU B 84 -15.141 50.753 38.999 1.00 46.30 O ANISOU 4522 O LEU B 84 5028 7540 5025 654 250 -28 O ATOM 4523 CB LEU B 84 -12.138 51.326 40.043 1.00 34.48 C ANISOU 4523 CB LEU B 84 3859 5935 3307 593 23 -299 C ATOM 4524 CG LEU B 84 -11.210 51.810 38.936 1.00 38.88 C ANISOU 4524 CG LEU B 84 4409 6336 4027 505 -86 -340 C ATOM 4525 CD1 LEU B 84 -10.797 53.256 39.171 1.00 44.65 C ANISOU 4525 CD1 LEU B 84 5221 6932 4812 550 -103 -519 C ATOM 4526 CD2 LEU B 84 -9.963 50.919 38.887 1.00 36.59 C ANISOU 4526 CD2 LEU B 84 4122 6049 3731 402 -200 -324 C ATOM 4527 N TYR B 85 -14.384 52.678 38.103 1.00 38.69 N ANISOU 4527 N TYR B 85 4176 6357 4169 714 144 -179 N ATOM 4528 CA TYR B 85 -15.292 52.651 36.954 1.00 37.02 C ANISOU 4528 CA TYR B 85 3826 6148 4091 729 119 -58 C ATOM 4529 C TYR B 85 -14.604 53.235 35.725 1.00 39.16 C ANISOU 4529 C TYR B 85 4163 6284 4432 695 15 -43 C ATOM 4530 O TYR B 85 -13.649 53.997 35.862 1.00 42.69 O ANISOU 4530 O TYR B 85 4732 6599 4890 686 12 -134 O ATOM 4531 CB TYR B 85 -16.542 53.503 37.235 1.00 39.76 C ANISOU 4531 CB TYR B 85 4079 6505 4521 899 231 -55 C ATOM 4532 CG TYR B 85 -17.355 53.075 38.421 1.00 39.08 C ANISOU 4532 CG TYR B 85 3921 6551 4377 960 400 -56 C ATOM 4533 CD1 TYR B 85 -18.313 52.087 38.303 1.00 32.99 C ANISOU 4533 CD1 TYR B 85 2949 5902 3683 916 445 73 C ATOM 4534 CD2 TYR B 85 -17.175 53.670 39.657 1.00 37.25 C ANISOU 4534 CD2 TYR B 85 3824 6315 4013 1059 528 -191 C ATOM 4535 CE1 TYR B 85 -19.087 51.699 39.402 1.00 47.07 C ANISOU 4535 CE1 TYR B 85 4656 7797 5433 972 657 105 C ATOM 4536 CE2 TYR B 85 -17.946 53.296 40.758 1.00 40.00 C ANISOU 4536 CE2 TYR B 85 4132 6798 4267 1137 730 -174 C ATOM 4537 CZ TYR B 85 -18.888 52.307 40.618 1.00 41.97 C ANISOU 4537 CZ TYR B 85 4172 7163 4614 1092 812 -6 C ATOM 4538 OH TYR B 85 -19.629 51.927 41.701 1.00 49.92 O ANISOU 4538 OH TYR B 85 5134 8290 5542 1163 1059 41 O ATOM 4539 N THR B 86 -15.134 52.924 34.539 1.00 35.75 N ANISOU 4539 N THR B 86 3649 5886 4049 683 -64 70 N ATOM 4540 CA THR B 86 -14.640 53.486 33.283 1.00 38.10 C ANISOU 4540 CA THR B 86 4031 6079 4368 683 -134 127 C ATOM 4541 C THR B 86 -15.436 54.756 32.985 1.00 41.61 C ANISOU 4541 C THR B 86 4459 6446 4906 858 -112 183 C ATOM 4542 O THR B 86 -16.662 54.713 32.915 1.00 38.55 O ANISOU 4542 O THR B 86 3921 6157 4571 956 -135 243 O ATOM 4543 CB THR B 86 -14.870 52.502 32.119 1.00 44.42 C ANISOU 4543 CB THR B 86 4784 6977 5119 607 -253 208 C ATOM 4544 OG1 THR B 86 -14.282 51.234 32.430 1.00 44.59 O ANISOU 4544 OG1 THR B 86 4802 7048 5092 462 -258 160 O ATOM 4545 CG2 THR B 86 -14.296 53.039 30.812 1.00 40.46 C ANISOU 4545 CG2 THR B 86 4414 6389 4572 623 -297 281 C ATOM 4546 N GLY B 87 -14.763 55.888 32.804 1.00 41.16 N ANISOU 4546 N GLY B 87 3920 4273 7445 29 -271 1002 N ATOM 4547 CA GLY B 87 -15.483 57.144 32.633 1.00 36.99 C ANISOU 4547 CA GLY B 87 3425 3498 7133 174 -270 1203 C ATOM 4548 C GLY B 87 -15.942 57.369 31.200 1.00 45.33 C ANISOU 4548 C GLY B 87 4649 4676 7898 527 -459 1470 C ATOM 4549 O GLY B 87 -15.644 56.572 30.305 1.00 47.61 O ANISOU 4549 O GLY B 87 5036 5254 7800 625 -567 1493 O ATOM 4550 N ARG B 88 -16.692 58.442 30.983 1.00 43.55 N ANISOU 4550 N ARG B 88 4460 4233 7855 723 -503 1669 N ATOM 4551 CA ARG B 88 -17.022 58.872 29.627 1.00 48.37 C ANISOU 4551 CA ARG B 88 5268 4928 8183 1067 -659 2002 C ATOM 4552 C ARG B 88 -15.711 59.268 28.923 1.00 56.71 C ANISOU 4552 C ARG B 88 6602 5983 8964 1001 -386 2312 C ATOM 4553 O ARG B 88 -14.845 59.915 29.520 1.00 51.85 O ANISOU 4553 O ARG B 88 6031 5138 8531 762 -47 2375 O ATOM 4554 CB ARG B 88 -18.014 60.038 29.659 1.00 43.99 C ANISOU 4554 CB ARG B 88 4703 4092 7918 1299 -727 2168 C ATOM 4555 CG ARG B 88 -18.338 60.609 28.284 1.00 58.47 C ANISOU 4555 CG ARG B 88 6792 6015 9407 1647 -873 2505 C ATOM 4556 CD ARG B 88 -19.582 61.477 28.298 1.00 65.44 C ANISOU 4556 CD ARG B 88 7649 6767 10448 1888 -1013 2485 C ATOM 4557 NE ARG B 88 -20.756 60.699 28.676 1.00 73.65 N ANISOU 4557 NE ARG B 88 8395 8028 11558 1945 -1296 2108 N ATOM 4558 CZ ARG B 88 -21.321 60.742 29.877 1.00 69.86 C ANISOU 4558 CZ ARG B 88 7678 7410 11455 1761 -1228 1788 C ATOM 4559 NH1 ARG B 88 -20.821 61.544 30.813 1.00 67.57 N ANISOU 4559 NH1 ARG B 88 7396 6765 11512 1524 -906 1803 N ATOM 4560 NH2 ARG B 88 -22.384 59.987 30.138 1.00 61.25 N ANISOU 4560 NH2 ARG B 88 6357 6557 10359 1777 -1452 1439 N ATOM 4561 N GLY B 89 -15.543 58.831 27.679 1.00 55.19 N ANISOU 4561 N GLY B 89 6582 6071 8319 1174 -520 2469 N ATOM 4562 CA GLY B 89 -14.309 59.074 26.947 1.00 47.31 C ANISOU 4562 CA GLY B 89 5841 5116 7018 1091 -261 2719 C ATOM 4563 C GLY B 89 -13.152 58.184 27.383 1.00 45.44 C ANISOU 4563 C GLY B 89 5519 5048 6699 795 -64 2483 C ATOM 4564 O GLY B 89 -12.048 58.313 26.871 1.00 52.33 O ANISOU 4564 O GLY B 89 6555 5982 7344 689 178 2631 O ATOM 4565 N GLY B 90 -13.402 57.286 28.329 1.00 40.52 N ANISOU 4565 N GLY B 90 4642 4498 6258 666 -161 2117 N ATOM 4566 CA GLY B 90 -12.369 56.387 28.805 1.00 39.21 C ANISOU 4566 CA GLY B 90 4382 4487 6030 430 -9 1898 C ATOM 4567 C GLY B 90 -12.517 54.983 28.239 1.00 40.20 C ANISOU 4567 C GLY B 90 4488 4948 5838 524 -222 1697 C ATOM 4568 O GLY B 90 -13.438 54.727 27.494 1.00 42.75 O ANISOU 4568 O GLY B 90 4858 5405 5981 739 -487 1710 O ATOM 4569 N ASP B 91 -11.587 54.085 28.560 1.00 36.41 N ANISOU 4569 N ASP B 91 3942 4612 5282 366 -97 1511 N ATOM 4570 CA ASP B 91 -11.743 52.685 28.185 1.00 36.59 C ANISOU 4570 CA ASP B 91 3945 4901 5057 434 -265 1276 C ATOM 4571 C ASP B 91 -10.819 51.740 28.935 1.00 35.12 C ANISOU 4571 C ASP B 91 3643 4782 4918 264 -128 1045 C ATOM 4572 O ASP B 91 -9.917 52.164 29.656 1.00 40.63 O ANISOU 4572 O ASP B 91 4263 5380 5794 89 99 1080 O ATOM 4573 CB ASP B 91 -11.639 52.448 26.662 1.00 55.13 C ANISOU 4573 CB ASP B 91 6497 7495 6953 609 -322 1428 C ATOM 4574 CG ASP B 91 -10.271 52.779 26.093 1.00 67.67 C ANISOU 4574 CG ASP B 91 8219 9143 8349 530 -22 1621 C ATOM 4575 OD1 ASP B 91 -10.114 52.641 24.860 1.00 78.91 O ANISOU 4575 OD1 ASP B 91 9827 10761 9393 638 -34 1748 O ATOM 4576 OD2 ASP B 91 -9.360 53.179 26.853 1.00 67.69 O ANISOU 4576 OD2 ASP B 91 8138 9019 8561 345 229 1631 O ATOM 4577 N LEU B 92 -11.093 50.452 28.766 1.00 37.43 N ANISOU 4577 N LEU B 92 3925 5248 5047 320 -272 802 N ATOM 4578 CA LEU B 92 -10.299 49.384 29.333 1.00 35.07 C ANISOU 4578 CA LEU B 92 3553 5021 4751 225 -175 589 C ATOM 4579 C LEU B 92 -9.601 48.746 28.158 1.00 37.42 C ANISOU 4579 C LEU B 92 3983 5560 4676 331 -97 618 C ATOM 4580 O LEU B 92 -10.221 48.492 27.133 1.00 40.10 O ANISOU 4580 O LEU B 92 4448 6041 4748 464 -236 628 O ATOM 4581 CB LEU B 92 -11.215 48.345 29.965 1.00 36.01 C ANISOU 4581 CB LEU B 92 3609 5120 4953 211 -374 276 C ATOM 4582 CG LEU B 92 -11.922 48.813 31.225 1.00 41.20 C ANISOU 4582 CG LEU B 92 4127 5548 5980 71 -440 182 C ATOM 4583 CD1 LEU B 92 -12.951 47.802 31.674 1.00 38.83 C ANISOU 4583 CD1 LEU B 92 3798 5243 5713 47 -633 -136 C ATOM 4584 CD2 LEU B 92 -10.891 49.007 32.300 1.00 39.61 C ANISOU 4584 CD2 LEU B 92 3817 5246 5989 -114 -240 193 C ATOM 4585 N GLN B 93 -8.314 48.476 28.290 1.00 34.97 N ANISOU 4585 N GLN B 93 3630 5317 4338 268 127 616 N ATOM 4586 CA GLN B 93 -7.602 47.830 27.205 1.00 39.24 C ANISOU 4586 CA GLN B 93 4281 6083 4546 358 234 610 C ATOM 4587 C GLN B 93 -6.653 46.793 27.750 1.00 42.42 C ANISOU 4587 C GLN B 93 4575 6547 4995 338 358 414 C ATOM 4588 O GLN B 93 -5.812 47.097 28.588 1.00 41.91 O ANISOU 4588 O GLN B 93 4359 6432 5134 234 502 439 O ATOM 4589 CB GLN B 93 -6.858 48.863 26.353 1.00 42.81 C ANISOU 4589 CB GLN B 93 4832 6595 4840 336 436 891 C ATOM 4590 CG GLN B 93 -7.767 49.620 25.394 1.00 50.20 C ANISOU 4590 CG GLN B 93 5954 7529 5592 434 297 1104 C ATOM 4591 CD GLN B 93 -7.006 50.578 24.513 1.00 66.05 C ANISOU 4591 CD GLN B 93 8117 9577 7404 402 518 1391 C ATOM 4592 OE1 GLN B 93 -5.775 50.558 24.471 1.00 72.41 O ANISOU 4592 OE1 GLN B 93 8884 10458 8169 298 788 1390 O ATOM 4593 NE2 GLN B 93 -7.735 51.430 23.799 1.00 78.96 N ANISOU 4593 NE2 GLN B 93 9930 11163 8908 492 408 1639 N ATOM 4594 N LYS B 94 -6.811 45.560 27.286 1.00 40.61 N ANISOU 4594 N LYS B 94 4425 6430 4576 443 300 212 N ATOM 4595 CA LYS B 94 -5.936 44.499 27.710 1.00 37.97 C ANISOU 4595 CA LYS B 94 4016 6136 4275 477 417 35 C ATOM 4596 C LYS B 94 -4.591 44.655 27.001 1.00 37.55 C ANISOU 4596 C LYS B 94 3938 6260 4069 500 679 132 C ATOM 4597 O LYS B 94 -4.527 44.758 25.773 1.00 42.24 O ANISOU 4597 O LYS B 94 4674 7001 4375 543 746 199 O ATOM 4598 CB LYS B 94 -6.569 43.141 27.415 1.00 39.02 C ANISOU 4598 CB LYS B 94 4270 6294 4261 572 307 -223 C ATOM 4599 CG LYS B 94 -5.574 41.978 27.455 1.00 43.10 C ANISOU 4599 CG LYS B 94 4772 6867 4738 669 470 -383 C ATOM 4600 CD LYS B 94 -6.308 40.640 27.497 1.00 38.09 C ANISOU 4600 CD LYS B 94 4273 6165 4035 727 372 -660 C ATOM 4601 CE LYS B 94 -5.301 39.500 27.346 1.00 39.09 C ANISOU 4601 CE LYS B 94 4418 6331 4102 863 563 -802 C ATOM 4602 NZ LYS B 94 -5.937 38.187 27.657 1.00 41.32 N ANISOU 4602 NZ LYS B 94 4847 6472 4379 903 502 -1071 N ATOM 4603 N ILE B 95 -3.516 44.696 27.776 1.00 35.01 N ANISOU 4603 N ILE B 95 3427 5946 3929 457 829 131 N ATOM 4604 CA ILE B 95 -2.174 44.913 27.215 1.00 33.93 C ANISOU 4604 CA ILE B 95 3213 5997 3684 454 1099 194 C ATOM 4605 C ILE B 95 -1.257 43.733 27.477 1.00 34.80 C ANISOU 4605 C ILE B 95 3200 6201 3819 585 1198 2 C ATOM 4606 O ILE B 95 -0.123 43.715 27.033 1.00 41.21 O ANISOU 4606 O ILE B 95 3914 7191 4553 608 1422 -2 O ATOM 4607 CB ILE B 95 -1.524 46.191 27.778 1.00 43.60 C ANISOU 4607 CB ILE B 95 4280 7204 5083 274 1240 371 C ATOM 4608 CG1 ILE B 95 -1.484 46.150 29.317 1.00 45.64 C ANISOU 4608 CG1 ILE B 95 4333 7344 5665 199 1152 305 C ATOM 4609 CG2 ILE B 95 -2.314 47.424 27.308 1.00 40.87 C ANISOU 4609 CG2 ILE B 95 4096 6747 4686 177 1197 593 C ATOM 4610 CD1 ILE B 95 -0.569 47.241 29.943 1.00 39.69 C ANISOU 4610 CD1 ILE B 95 3420 6577 5083 -8 1311 396 C ATOM 4611 N GLY B 96 -1.740 42.755 28.231 1.00 41.23 N ANISOU 4611 N GLY B 96 4023 6889 4755 672 1039 -160 N ATOM 4612 CA GLY B 96 -0.959 41.552 28.479 1.00 35.30 C ANISOU 4612 CA GLY B 96 3195 6184 4031 842 1117 -329 C ATOM 4613 C GLY B 96 -1.715 40.617 29.401 1.00 35.75 C ANISOU 4613 C GLY B 96 3327 6034 4222 900 924 -474 C ATOM 4614 O GLY B 96 -2.898 40.841 29.682 1.00 33.20 O ANISOU 4614 O GLY B 96 3118 5562 3936 798 740 -478 O ATOM 4615 N GLU B 97 -1.048 39.558 29.858 1.00 41.37 N ANISOU 4615 N GLU B 97 3984 6731 5003 1070 973 -596 N ATOM 4616 CA GLU B 97 -1.646 38.653 30.835 1.00 41.02 C ANISOU 4616 CA GLU B 97 4035 6466 5085 1118 816 -716 C ATOM 4617 C GLU B 97 -0.618 37.974 31.734 1.00 41.97 C ANISOU 4617 C GLU B 97 4064 6513 5371 1218 826 -697 C ATOM 4618 O GLU B 97 0.550 37.806 31.351 1.00 38.66 O ANISOU 4618 O GLU B 97 3551 6190 4947 1300 960 -661 O ATOM 4619 CB GLU B 97 -2.533 37.610 30.151 1.00 35.09 C ANISOU 4619 CB GLU B 97 3569 5602 4160 1190 787 -913 C ATOM 4620 CG GLU B 97 -1.791 36.597 29.332 1.00 41.13 C ANISOU 4620 CG GLU B 97 4412 6418 4796 1380 970 -1026 C ATOM 4621 CD GLU B 97 -2.740 35.621 28.616 1.00 59.10 C ANISOU 4621 CD GLU B 97 6985 8580 6889 1385 960 -1233 C ATOM 4622 OE1 GLU B 97 -3.856 36.038 28.225 1.00 58.03 O ANISOU 4622 OE1 GLU B 97 6950 8479 6620 1259 849 -1281 O ATOM 4623 OE2 GLU B 97 -2.370 34.439 28.439 1.00 67.19 O ANISOU 4623 OE2 GLU B 97 8145 9461 7922 1476 1056 -1327 O ATOM 4624 N PHE B 98 -1.067 37.619 32.934 1.00 38.03 N ANISOU 4624 N PHE B 98 3783 6828 3837 -168 -518 802 N ATOM 4625 CA PHE B 98 -0.343 36.722 33.834 1.00 37.96 C ANISOU 4625 CA PHE B 98 3745 6889 3791 -145 -521 827 C ATOM 4626 C PHE B 98 0.872 37.362 34.501 1.00 37.23 C ANISOU 4626 C PHE B 98 3701 6831 3613 -122 -551 699 C ATOM 4627 O PHE B 98 0.985 37.346 35.748 1.00 38.76 O ANISOU 4627 O PHE B 98 3892 7130 3704 -31 -541 702 O ATOM 4628 CB PHE B 98 0.040 35.440 33.078 1.00 29.03 C ANISOU 4628 CB PHE B 98 2565 5704 2760 -226 -549 875 C ATOM 4629 CG PHE B 98 0.498 34.307 33.951 1.00 33.69 C ANISOU 4629 CG PHE B 98 3108 6349 3342 -192 -547 949 C ATOM 4630 CD1 PHE B 98 -0.355 33.254 34.245 1.00 33.98 C ANISOU 4630 CD1 PHE B 98 3072 6399 3441 -172 -507 1099 C ATOM 4631 CD2 PHE B 98 1.800 34.259 34.421 1.00 37.55 C ANISOU 4631 CD2 PHE B 98 3619 6868 3780 -184 -589 872 C ATOM 4632 CE1 PHE B 98 0.081 32.189 35.019 1.00 42.28 C ANISOU 4632 CE1 PHE B 98 4085 7487 4494 -138 -501 1188 C ATOM 4633 CE2 PHE B 98 2.241 33.198 35.183 1.00 35.49 C ANISOU 4633 CE2 PHE B 98 3318 6655 3512 -143 -598 950 C ATOM 4634 CZ PHE B 98 1.382 32.162 35.492 1.00 40.60 C ANISOU 4634 CZ PHE B 98 3904 7309 4212 -117 -551 1117 C ATOM 4635 N CYS B 99 1.761 37.941 33.691 1.00 37.51 N ANISOU 4635 N CYS B 99 3779 6784 3688 -200 -586 586 N ATOM 4636 CA CYS B 99 3.090 38.367 34.171 1.00 39.86 C ANISOU 4636 CA CYS B 99 4098 7098 3950 -203 -625 451 C ATOM 4637 C CYS B 99 3.131 39.739 34.850 1.00 42.51 C ANISOU 4637 C CYS B 99 4480 7450 4221 -145 -623 333 C ATOM 4638 O CYS B 99 3.749 40.684 34.342 1.00 47.43 O ANISOU 4638 O CYS B 99 5140 7987 4893 -202 -633 217 O ATOM 4639 CB CYS B 99 4.115 38.329 33.026 1.00 39.40 C ANISOU 4639 CB CYS B 99 4049 6942 3982 -319 -647 378 C ATOM 4640 SG CYS B 99 4.363 36.674 32.359 1.00 43.07 S ANISOU 4640 SG CYS B 99 4451 7391 4525 -379 -662 467 S ATOM 4641 N MET B 100 2.488 39.847 36.004 1.00 43.34 N ANISOU 4641 N MET B 100 4580 7663 4224 -32 -604 359 N ATOM 4642 CA MET B 100 2.522 41.083 36.775 1.00 42.48 C ANISOU 4642 CA MET B 100 4509 7583 4048 39 -608 226 C ATOM 4643 C MET B 100 2.455 40.707 38.249 1.00 41.87 C ANISOU 4643 C MET B 100 4415 7674 3819 166 -611 237 C ATOM 4644 O MET B 100 1.665 39.836 38.620 1.00 40.29 O ANISOU 4644 O MET B 100 4186 7552 3573 217 -565 394 O ATOM 4645 CB MET B 100 1.356 41.993 36.375 1.00 40.19 C ANISOU 4645 CB MET B 100 4247 7230 3791 59 -557 246 C ATOM 4646 CG MET B 100 1.234 43.274 37.204 1.00 41.53 C ANISOU 4646 CG MET B 100 4451 7422 3906 145 -553 104 C ATOM 4647 SD MET B 100 0.051 44.474 36.520 1.00 43.11 S ANISOU 4647 SD MET B 100 4686 7504 4190 157 -505 111 S ATOM 4648 CE MET B 100 0.072 45.693 37.852 1.00 33.80 C ANISOU 4648 CE MET B 100 3530 6384 2929 281 -507 -78 C ATOM 4649 N VAL B 101 3.316 41.301 39.074 1.00 39.14 N ANISOU 4649 N VAL B 101 4086 7387 3400 215 -667 75 N ATOM 4650 CA VAL B 101 3.244 41.054 40.505 1.00 41.97 C ANISOU 4650 CA VAL B 101 4442 7926 3580 355 -676 74 C ATOM 4651 C VAL B 101 2.184 41.988 41.092 1.00 44.72 C ANISOU 4651 C VAL B 101 4817 8323 3851 452 -616 36 C ATOM 4652 O VAL B 101 1.922 43.066 40.547 1.00 46.54 O ANISOU 4652 O VAL B 101 5072 8438 4172 416 -603 -59 O ATOM 4653 CB VAL B 101 4.601 41.255 41.209 1.00 51.39 C ANISOU 4653 CB VAL B 101 5632 9183 4710 384 -779 -100 C ATOM 4654 CG1 VAL B 101 5.700 40.513 40.464 1.00 42.48 C ANISOU 4654 CG1 VAL B 101 4467 7977 3697 275 -836 -93 C ATOM 4655 CG2 VAL B 101 4.936 42.715 41.281 1.00 56.93 C ANISOU 4655 CG2 VAL B 101 6360 9823 5448 379 -812 -328 C ATOM 4656 N TYR B 102 1.564 41.573 42.190 1.00 41.40 N ANISOU 4656 N TYR B 102 4393 8070 3268 581 -570 118 N ATOM 4657 CA TYR B 102 0.500 42.362 42.772 1.00 45.47 C ANISOU 4657 CA TYR B 102 4923 8646 3706 683 -498 89 C ATOM 4658 C TYR B 102 0.411 42.011 44.246 1.00 45.21 C ANISOU 4658 C TYR B 102 4899 8838 3441 840 -478 107 C ATOM 4659 O TYR B 102 0.866 40.947 44.663 1.00 51.25 O ANISOU 4659 O TYR B 102 5652 9696 4125 863 -498 220 O ATOM 4660 CB TYR B 102 -0.847 42.051 42.067 1.00 41.25 C ANISOU 4660 CB TYR B 102 4356 8046 3271 650 -396 270 C ATOM 4661 CG TYR B 102 -1.336 40.642 42.361 1.00 41.23 C ANISOU 4661 CG TYR B 102 4307 8134 3225 672 -334 500 C ATOM 4662 CD1 TYR B 102 -0.959 39.567 41.561 1.00 40.79 C ANISOU 4662 CD1 TYR B 102 4219 7996 3283 564 -360 622 C ATOM 4663 CD2 TYR B 102 -2.140 40.386 43.458 1.00 46.28 C ANISOU 4663 CD2 TYR B 102 4933 8938 3714 801 -241 593 C ATOM 4664 CE1 TYR B 102 -1.386 38.276 41.844 1.00 40.94 C ANISOU 4664 CE1 TYR B 102 4191 8075 3291 581 -302 830 C ATOM 4665 CE2 TYR B 102 -2.558 39.106 43.758 1.00 52.52 C ANISOU 4665 CE2 TYR B 102 5678 9797 4480 817 -171 817 C ATOM 4666 CZ TYR B 102 -2.176 38.052 42.953 1.00 49.40 C ANISOU 4666 CZ TYR B 102 5249 9299 4222 705 -205 935 C ATOM 4667 OH TYR B 102 -2.618 36.778 43.262 1.00 52.89 O ANISOU 4667 OH TYR B 102 5640 9788 4668 719 -132 1159 O ATOM 4668 N SER B 103 -0.203 42.893 45.026 1.00 43.55 N ANISOU 4668 N SER B 103 4711 8717 3120 956 -435 3 N ATOM 4669 CA SER B 103 -0.593 42.557 46.385 1.00 46.35 C ANISOU 4669 CA SER B 103 5075 9302 3232 1120 -379 54 C ATOM 4670 C SER B 103 -2.122 42.564 46.523 1.00 50.87 C ANISOU 4670 C SER B 103 5620 9915 3794 1179 -226 192 C ATOM 4671 O SER B 103 -2.793 43.449 45.983 1.00 50.88 O ANISOU 4671 O SER B 103 5613 9804 3917 1154 -192 119 O ATOM 4672 CB SER B 103 0.021 43.545 47.373 1.00 44.74 C ANISOU 4672 CB SER B 103 4915 9212 2872 1233 -457 -211 C ATOM 4673 OG SER B 103 -0.588 43.404 48.646 1.00 52.59 O ANISOU 4673 OG SER B 103 5927 10438 3616 1407 -380 -171 O ATOM 4674 N GLU B 104 -2.669 41.592 47.254 1.00 48.97 N ANISOU 4674 N GLU B 104 5359 9829 3416 1261 -129 394 N ATOM 4675 CA GLU B 104 -4.116 41.509 47.453 1.00 57.91 C ANISOU 4675 CA GLU B 104 6447 11012 4545 1318 33 536 C ATOM 4676 C GLU B 104 -4.552 42.542 48.480 1.00 58.20 C ANISOU 4676 C GLU B 104 6514 11197 4401 1476 83 370 C ATOM 4677 O GLU B 104 -5.713 42.969 48.507 1.00 56.92 O ANISOU 4677 O GLU B 104 6313 11039 4275 1521 199 393 O ATOM 4678 CB GLU B 104 -4.524 40.117 47.954 1.00 69.28 C ANISOU 4678 CB GLU B 104 7851 12566 5906 1352 137 817 C ATOM 4679 CG GLU B 104 -4.188 38.962 47.015 1.00 81.02 C ANISOU 4679 CG GLU B 104 9297 13910 7578 1207 100 991 C ATOM 4680 CD GLU B 104 -5.413 38.146 46.651 1.00 77.95 C ANISOU 4680 CD GLU B 104 8819 13474 7326 1163 240 1232 C ATOM 4681 OE1 GLU B 104 -6.488 38.429 47.213 1.00 76.55 O ANISOU 4681 OE1 GLU B 104 8609 13392 7085 1252 375 1279 O ATOM 4682 OE2 GLU B 104 -5.301 37.233 45.802 1.00 79.91 O ANISOU 4682 OE2 GLU B 104 9021 13588 7753 1041 216 1360 O ATOM 4683 N VAL B 105 -3.604 42.923 49.331 1.00 57.50 N ANISOU 4683 N VAL B 105 6489 11235 4124 1566 -11 191 N ATOM 4684 CA VAL B 105 -3.876 43.769 50.480 1.00 59.65 C ANISOU 4684 CA VAL B 105 6797 11689 4178 1738 24 18 C ATOM 4685 C VAL B 105 -3.132 45.102 50.346 1.00 61.20 C ANISOU 4685 C VAL B 105 7030 11792 4432 1727 -113 -316 C ATOM 4686 O VAL B 105 -2.019 45.153 49.830 1.00 62.02 O ANISOU 4686 O VAL B 105 7147 11781 4635 1627 -254 -412 O ATOM 4687 CB VAL B 105 -3.504 43.058 51.807 1.00 60.29 C ANISOU 4687 CB VAL B 105 6916 11989 4004 1870 37 88 C ATOM 4688 CG1 VAL B 105 -4.364 41.826 52.000 1.00 52.79 C ANISOU 4688 CG1 VAL B 105 5921 11075 3063 1873 196 419 C ATOM 4689 CG2 VAL B 105 -2.033 42.676 51.816 1.00 61.78 C ANISOU 4689 CG2 VAL B 105 7134 12122 4216 1814 -134 20 C ATOM 4690 N PRO B 106 -3.757 46.196 50.793 1.00 57.19 N ANISOU 4690 N PRO B 106 6529 11320 3882 1829 -64 -497 N ATOM 4691 CA PRO B 106 -5.113 46.234 51.353 1.00 54.22 C ANISOU 4691 CA PRO B 106 6123 11069 3409 1948 114 -402 C ATOM 4692 C PRO B 106 -6.148 46.056 50.257 1.00 56.32 C ANISOU 4692 C PRO B 106 6317 11152 3930 1837 210 -219 C ATOM 4693 O PRO B 106 -5.830 46.237 49.075 1.00 48.49 O ANISOU 4693 O PRO B 106 5315 9930 3179 1686 127 -228 O ATOM 4694 CB PRO B 106 -5.214 47.656 51.914 1.00 58.26 C ANISOU 4694 CB PRO B 106 6661 11609 3867 2062 91 -720 C ATOM 4695 CG PRO B 106 -3.749 48.130 52.041 1.00 54.45 C ANISOU 4695 CG PRO B 106 6230 11095 3364 2036 -107 -972 C ATOM 4696 CD PRO B 106 -3.082 47.504 50.875 1.00 52.80 C ANISOU 4696 CD PRO B 106 6005 10689 3370 1843 -186 -834 C ATOM 4697 N ASN B 107 -7.358 45.679 50.645 1.00 56.54 N ANISOU 4697 N ASN B 107 6292 11289 3902 1914 383 -53 N ATOM 4698 CA ASN B 107 -8.477 45.655 49.726 1.00 53.96 C ANISOU 4698 CA ASN B 107 5881 10809 3811 1837 472 82 C ATOM 4699 C ASN B 107 -9.205 46.974 49.909 1.00 54.18 C ANISOU 4699 C ASN B 107 5896 10815 3876 1934 515 -122 C ATOM 4700 O ASN B 107 -9.977 47.146 50.848 1.00 56.13 O ANISOU 4700 O ASN B 107 6120 11241 3967 2082 649 -136 O ATOM 4701 CB ASN B 107 -9.405 44.477 50.043 1.00 55.26 C ANISOU 4701 CB ASN B 107 5973 11094 3929 1860 643 378 C ATOM 4702 CG ASN B 107 -10.663 44.459 49.179 1.00 57.64 C ANISOU 4702 CG ASN B 107 6166 11259 4478 1795 736 501 C ATOM 4703 OD1 ASN B 107 -10.857 45.306 48.302 1.00 58.52 O ANISOU 4703 OD1 ASN B 107 6265 11187 4785 1739 667 382 O ATOM 4704 ND2 ASN B 107 -11.518 43.477 49.419 1.00 57.39 N ANISOU 4704 ND2 ASN B 107 6050 11310 4444 1804 890 747 N ATOM 4705 N PHE B 108 -8.960 47.904 49.003 1.00 53.38 N ANISOU 4705 N PHE B 108 5808 10491 3984 1853 409 -275 N ATOM 4706 CA PHE B 108 -9.512 49.238 49.136 1.00 51.55 C ANISOU 4706 CA PHE B 108 5570 10202 3812 1943 427 -490 C ATOM 4707 C PHE B 108 -11.038 49.281 48.976 1.00 52.09 C ANISOU 4707 C PHE B 108 5540 10269 3981 1995 579 -369 C ATOM 4708 O PHE B 108 -11.656 50.276 49.336 1.00 54.22 O ANISOU 4708 O PHE B 108 5792 10544 4263 2109 629 -533 O ATOM 4709 CB PHE B 108 -8.767 50.205 48.192 1.00 55.69 C ANISOU 4709 CB PHE B 108 6140 10470 4549 1838 274 -665 C ATOM 4710 CG PHE B 108 -7.308 50.408 48.569 1.00 61.47 C ANISOU 4710 CG PHE B 108 6951 11221 5182 1817 134 -850 C ATOM 4711 CD1 PHE B 108 -6.965 51.154 49.697 1.00 61.22 C ANISOU 4711 CD1 PHE B 108 6960 11325 4978 1957 111 -1111 C ATOM 4712 CD2 PHE B 108 -6.286 49.842 47.818 1.00 58.06 C ANISOU 4712 CD2 PHE B 108 6545 10683 4833 1663 25 -778 C ATOM 4713 CE1 PHE B 108 -5.631 51.340 50.061 1.00 56.38 C ANISOU 4713 CE1 PHE B 108 6403 10734 4285 1941 -31 -1298 C ATOM 4714 CE2 PHE B 108 -4.941 50.022 48.181 1.00 61.22 C ANISOU 4714 CE2 PHE B 108 6999 11103 5158 1646 -104 -956 C ATOM 4715 CZ PHE B 108 -4.620 50.771 49.309 1.00 58.80 C ANISOU 4715 CZ PHE B 108 6725 10929 4688 1784 -137 -1217 C ATOM 4716 N SER B 109 -11.641 48.194 48.483 1.00 51.47 N ANISOU 4716 N SER B 109 5388 10187 3981 1918 653 -96 N ATOM 4717 CA SER B 109 -13.097 48.102 48.351 1.00 51.75 C ANISOU 4717 CA SER B 109 5306 10232 4124 1960 799 31 C ATOM 4718 C SER B 109 -13.800 47.460 49.556 1.00 56.66 C ANISOU 4718 C SER B 109 5877 11116 4537 2089 992 147 C ATOM 4719 O SER B 109 -15.001 47.172 49.482 1.00 56.89 O ANISOU 4719 O SER B 109 5787 11166 4661 2111 1132 286 O ATOM 4720 CB SER B 109 -13.517 47.337 47.089 1.00 49.84 C ANISOU 4720 CB SER B 109 4988 9828 4120 1806 776 249 C ATOM 4721 OG SER B 109 -13.032 47.931 45.899 1.00 53.64 O ANISOU 4721 OG SER B 109 5512 10074 4793 1696 621 169 O ATOM 4722 N GLU B 110 -13.101 47.218 50.661 1.00 61.16 N ANISOU 4722 N GLU B 110 6524 11889 4823 2177 1006 100 N ATOM 4723 CA GLU B 110 -13.840 46.674 51.814 1.00 74.79 C ANISOU 4723 CA GLU B 110 8207 13874 6336 2313 1210 222 C ATOM 4724 C GLU B 110 -14.658 47.760 52.514 1.00 73.22 C ANISOU 4724 C GLU B 110 7979 13773 6069 2484 1318 27 C ATOM 4725 O GLU B 110 -14.173 48.871 52.729 1.00 75.76 O ANISOU 4725 O GLU B 110 8372 14068 6347 2552 1218 -257 O ATOM 4726 CB GLU B 110 -12.954 45.879 52.788 1.00 81.13 C ANISOU 4726 CB GLU B 110 9099 14890 6838 2366 1210 293 C ATOM 4727 CG GLU B 110 -11.838 46.653 53.467 1.00 98.40 C ANISOU 4727 CG GLU B 110 11412 17165 8812 2456 1071 11 C ATOM 4728 CD GLU B 110 -10.760 45.728 54.048 1.00109.78 C ANISOU 4728 CD GLU B 110 12937 18706 10070 2441 988 109 C ATOM 4729 OE1 GLU B 110 -9.993 46.176 54.931 1.00114.64 O ANISOU 4729 OE1 GLU B 110 13639 19401 10520 2526 884 -84 O ATOM 4730 OE2 GLU B 110 -10.671 44.555 53.613 1.00108.97 O ANISOU 4730 OE2 GLU B 110 12805 18552 10047 2332 1003 375 O ATOM 4731 N PRO B 111 -15.926 47.453 52.829 1.00 75.94 N ANISOU 4731 N PRO B 111 8206 14216 6431 2551 1525 172 N ATOM 4732 CA PRO B 111 -16.803 48.414 53.522 1.00 81.17 C ANISOU 4732 CA PRO B 111 8823 14986 7033 2724 1654 -3 C ATOM 4733 C PRO B 111 -16.271 48.810 54.892 1.00 83.57 C ANISOU 4733 C PRO B 111 9244 15492 7018 2872 1654 -184 C ATOM 4734 O PRO B 111 -15.934 49.981 55.058 1.00 88.95 O ANISOU 4734 O PRO B 111 9977 16157 7662 2960 1570 -491 O ATOM 4735 CB PRO B 111 -18.133 47.658 53.662 1.00 72.20 C ANISOU 4735 CB PRO B 111 7535 13928 5970 2737 1883 250 C ATOM 4736 CG PRO B 111 -17.793 46.205 53.471 1.00 74.95 C ANISOU 4736 CG PRO B 111 7887 14265 6327 2599 1883 552 C ATOM 4737 CD PRO B 111 -16.622 46.192 52.513 1.00 73.69 C ANISOU 4737 CD PRO B 111 7811 13933 6256 2462 1653 500 C TER 4738 PRO B 111 HETATM 4739 O HOH L 101 -40.027 48.371 40.541 1.00 59.33 O HETATM 4740 O HOH L 102 -39.021 45.792 36.341 1.00 48.90 O HETATM 4741 O HOH L 103 -30.303 54.168 40.681 1.00 56.88 O HETATM 4742 O HOH L 104 -36.030 43.169 50.039 1.00 53.35 O HETATM 4743 O HOH L 105 -17.476 60.175 33.656 1.00 56.58 O HETATM 4744 O HOH L 106 -26.172 53.204 29.833 1.00 49.02 O HETATM 4745 O HOH L 107 -31.082 53.945 38.149 1.00 58.55 O HETATM 4746 O HOH L 108 -18.560 50.039 32.430 1.00 35.49 O HETATM 4747 O HOH L 109 -21.628 46.339 41.079 1.00 51.76 O HETATM 4748 O HOH L 110 -29.381 46.065 40.675 1.00 66.79 O HETATM 4749 O HOH L 111 -30.408 45.909 42.158 1.00 73.19 O HETATM 4750 O HOH L 112 -21.458 59.617 43.160 1.00 65.06 O HETATM 4751 O HOH A 601 12.678 -8.369 13.695 1.00 68.31 O HETATM 4752 O HOH A 602 0.706 39.974 -14.977 1.00 69.19 O HETATM 4753 O HOH A 603 27.199 18.291 39.418 1.00 57.47 O HETATM 4754 O HOH A 604 -0.305 7.714 19.955 1.00 57.44 O HETATM 4755 O HOH A 605 -1.846 52.619 -14.624 1.00 54.08 O HETATM 4756 O HOH A 606 15.682 25.761 42.273 1.00 62.86 O HETATM 4757 O HOH A 607 20.816 23.888 24.339 1.00 44.68 O HETATM 4758 O HOH A 608 14.569 25.328 21.761 1.00 49.77 O HETATM 4759 O HOH A 609 10.180 42.240 20.437 1.00 76.71 O HETATM 4760 O HOH A 610 18.716 27.644 30.667 1.00 51.77 O HETATM 4761 O HOH A 611 -0.872 39.324 48.188 1.00 55.75 O HETATM 4762 O HOH A 612 8.752 35.560 31.929 1.00 38.77 O HETATM 4763 O HOH A 613 5.344 34.971 25.397 1.00 51.53 O HETATM 4764 O HOH A 614 15.374 25.393 45.712 1.00 67.92 O HETATM 4765 O HOH A 615 4.248 -4.119 19.765 1.00 73.71 O HETATM 4766 O HOH A 616 14.644 31.864 38.191 1.00 47.65 O HETATM 4767 O HOH A 617 13.179 31.812 35.991 1.00 41.54 O HETATM 4768 O HOH A 618 3.592 43.533 -16.376 1.00 55.54 O HETATM 4769 O HOH A 619 22.520 22.750 27.059 1.00 50.92 O HETATM 4770 O HOH A 620 8.819 -4.735 13.938 1.00 70.23 O HETATM 4771 O HOH A 621 10.870 36.156 33.840 1.00 46.03 O HETATM 4772 O HOH A 622 -2.314 37.555 50.947 1.00 74.41 O HETATM 4773 O HOH A 623 4.153 22.619 23.851 1.00 37.78 O HETATM 4774 O HOH A 624 5.286 19.272 24.148 1.00 35.53 O HETATM 4775 O HOH A 625 2.394 30.318 22.823 1.00 35.45 O HETATM 4776 O HOH A 626 3.673 32.821 20.001 1.00 36.78 O HETATM 4777 O HOH A 627 2.364 38.594 42.772 1.00 35.32 O HETATM 4778 O HOH A 628 0.661 28.421 24.023 1.00 36.53 O HETATM 4779 O HOH A 629 -0.033 17.651 20.839 1.00 43.52 O HETATM 4780 O HOH A 630 6.248 23.414 22.051 1.00 35.02 O HETATM 4781 O HOH A 631 9.455 21.702 18.740 1.00 40.10 O HETATM 4782 O HOH A 632 2.304 29.468 20.153 1.00 36.70 O HETATM 4783 O HOH A 633 -2.084 24.465 23.729 1.00 39.23 O HETATM 4784 O HOH A 634 10.797 19.577 28.107 1.00 38.22 O HETATM 4785 O HOH A 635 1.349 33.961 20.948 1.00 45.16 O HETATM 4786 O HOH A 636 0.632 27.182 19.912 1.00 42.07 O HETATM 4787 O HOH A 637 -1.794 26.230 14.745 1.00 46.49 O HETATM 4788 O HOH A 638 14.208 27.549 43.173 1.00 49.40 O HETATM 4789 O HOH A 639 15.995 14.672 36.923 1.00 43.10 O HETATM 4790 O HOH A 640 -0.707 25.140 17.489 1.00 53.76 O HETATM 4791 O HOH A 641 15.093 16.158 40.083 1.00 52.95 O HETATM 4792 O HOH A 642 -6.361 43.046 15.062 1.00 49.60 O HETATM 4793 O HOH A 643 13.867 24.061 44.397 1.00 52.52 O HETATM 4794 O HOH A 644 -4.145 25.218 20.444 1.00 57.16 O HETATM 4795 O HOH A 645 20.560 20.674 31.999 1.00 47.33 O HETATM 4796 O HOH A 646 -1.080 22.490 25.420 1.00 42.52 O HETATM 4797 O HOH A 647 -0.810 26.647 22.565 1.00 38.36 O HETATM 4798 O HOH A 648 12.413 29.477 41.373 1.00 41.90 O HETATM 4799 O HOH A 649 -2.893 21.757 27.033 1.00 42.90 O HETATM 4800 O HOH A 650 4.869 38.025 43.835 1.00 52.08 O HETATM 4801 O HOH A 651 7.591 46.678 15.337 1.00 66.01 O HETATM 4802 O HOH A 652 3.884 34.516 23.163 1.00 51.68 O HETATM 4803 O HOH A 653 7.568 14.227 27.016 1.00 58.08 O HETATM 4804 O HOH A 654 -7.064 19.874 11.437 1.00 47.20 O HETATM 4805 O HOH A 655 -1.160 31.570 47.077 1.00 63.80 O HETATM 4806 O HOH A 656 -9.498 39.417 24.698 1.00 55.53 O HETATM 4807 O HOH A 657 11.495 51.562 7.866 1.00 59.10 O HETATM 4808 O HOH A 658 7.706 10.221 22.936 1.00 52.68 O HETATM 4809 O HOH A 659 10.273 17.182 26.796 1.00 43.78 O HETATM 4810 O HOH A 660 -2.181 13.057 27.089 1.00 58.14 O HETATM 4811 O HOH A 661 -2.868 31.380 31.631 1.00 57.76 O HETATM 4812 O HOH A 662 -2.395 44.029 21.911 1.00 53.35 O HETATM 4813 O HOH A 663 2.243 33.474 22.871 1.00 50.17 O HETATM 4814 O HOH A 664 2.263 2.962 12.456 1.00 61.18 O HETATM 4815 O HOH A 665 11.483 23.565 17.989 1.00 45.02 O HETATM 4816 O HOH A 666 28.862 11.520 27.927 1.00 59.73 O HETATM 4817 O HOH A 667 -15.014 41.861 20.604 1.00 58.61 O HETATM 4818 O HOH A 668 15.336 42.695 12.266 1.00 66.38 O HETATM 4819 O HOH A 669 7.619 38.340 31.796 1.00 51.82 O HETATM 4820 O HOH A 670 -0.988 17.574 18.674 1.00 49.03 O HETATM 4821 O HOH A 671 -7.813 31.584 41.271 1.00 67.91 O HETATM 4822 O HOH A 672 23.935 18.827 21.725 1.00 61.87 O HETATM 4823 O HOH A 673 -9.215 14.530 15.020 1.00 54.14 O HETATM 4824 O HOH A 674 -4.322 12.917 22.985 1.00 59.51 O HETATM 4825 O HOH A 675 2.798 35.061 27.141 1.00 56.05 O HETATM 4826 O HOH A 676 1.998 43.898 -8.455 1.00 51.34 O HETATM 4827 O HOH A 677 -7.149 29.828 5.426 1.00 60.31 O HETATM 4828 O HOH A 678 -1.665 5.101 13.183 1.00 53.18 O HETATM 4829 O HOH A 679 1.809 46.216 21.264 1.00 55.10 O HETATM 4830 O HOH A 680 7.150 45.675 18.332 1.00 73.08 O HETATM 4831 O HOH A 681 6.976 11.057 25.095 1.00 52.41 O HETATM 4832 O HOH A 682 16.198 47.816 5.060 1.00 60.18 O HETATM 4833 O HOH A 683 -0.286 44.295 22.086 1.00 54.31 O HETATM 4834 O HOH A 684 1.502 24.170 25.602 1.00 59.52 O HETATM 4835 O HOH A 685 3.277 37.287 23.526 1.00 61.11 O HETATM 4836 O HOH A 686 -7.076 18.810 22.847 1.00 60.15 O HETATM 4837 O HOH A 687 11.707 37.981 34.884 1.00 75.50 O HETATM 4838 O HOH A 688 -1.052 8.174 6.771 1.00 60.01 O HETATM 4839 O HOH A 689 -5.776 19.361 9.349 1.00 61.70 O HETATM 4840 O HOH A 690 2.906 40.409 22.008 1.00 66.13 O HETATM 4841 O HOH A 691 -6.535 23.305 29.713 1.00 61.03 O HETATM 4842 O HOH A 692 13.026 26.548 49.281 1.00 69.36 O HETATM 4843 O HOH A 693 22.132 6.417 10.744 1.00 71.14 O HETATM 4844 O HOH A 694 -6.881 36.900 -1.769 1.00 70.57 O HETATM 4845 O HOH A 695 8.184 40.419 33.508 1.00 64.11 O HETATM 4846 O HOH A 696 6.292 56.484 1.341 1.00 67.90 O HETATM 4847 O HOH A 697 -2.510 34.544 50.095 1.00 76.81 O HETATM 4848 O HOH A 698 9.635 47.439 11.793 1.00 74.26 O HETATM 4849 O HOH A 699 3.245 53.139 -9.414 1.00 58.00 O HETATM 4850 O HOH A 700 2.064 25.489 45.517 1.00 77.19 O HETATM 4851 O HOH A 701 10.415 56.599 -5.142 1.00 71.12 O HETATM 4852 O HOH A 702 9.203 54.655 -6.599 1.00 64.71 O HETATM 4853 O HOH A 703 -6.713 6.623 9.547 1.00 72.18 O HETATM 4854 O HOH B 301 -35.725 52.409 41.310 1.00 58.94 O HETATM 4855 O HOH B 302 -36.067 47.294 31.306 1.00 43.34 O HETATM 4856 O HOH B 303 -22.496 45.859 24.498 1.00 63.90 O HETATM 4857 O HOH B 304 -28.278 52.877 32.138 1.00 47.69 O HETATM 4858 O HOH B 305 1.189 42.616 50.483 1.00 50.15 O HETATM 4859 O HOH B 306 -25.452 44.711 28.615 1.00 58.44 O HETATM 4860 O HOH B 307 -26.887 51.107 34.390 1.00 51.11 O HETATM 4861 O HOH B 308 3.934 44.481 46.749 1.00 59.00 O HETATM 4862 O HOH B 309 -24.638 53.337 47.317 1.00 62.89 O HETATM 4863 O HOH B 310 -3.727 54.638 50.676 1.00 63.09 O HETATM 4864 O HOH B 311 -34.725 45.334 30.158 1.00 50.36 O HETATM 4865 O HOH B 312 -33.589 45.695 27.485 1.00 58.79 O HETATM 4866 O HOH B 313 -10.982 44.185 45.795 1.00 44.37 O HETATM 4867 O HOH B 314 -16.467 50.357 34.070 1.00 30.65 O HETATM 4868 O HOH B 315 -20.547 54.439 38.339 1.00 42.03 O HETATM 4869 O HOH B 316 1.864 39.993 29.040 1.00 47.26 O HETATM 4870 O HOH B 317 -20.637 43.377 32.187 1.00 40.08 O HETATM 4871 O HOH B 318 -20.326 40.327 32.001 1.00 57.24 O HETATM 4872 O HOH B 319 -5.935 35.897 31.085 1.00 45.21 O HETATM 4873 O HOH B 320 -23.708 51.276 30.132 1.00 41.98 O HETATM 4874 O HOH B 321 -18.185 49.110 29.900 1.00 41.68 O HETATM 4875 O HOH B 322 -7.031 52.272 28.257 1.00 45.44 O HETATM 4876 O HOH B 323 -15.335 49.522 29.927 1.00 39.99 O HETATM 4877 O HOH B 324 -9.331 38.210 27.607 1.00 48.17 O HETATM 4878 O HOH B 325 -15.648 37.868 32.410 1.00 49.74 O HETATM 4879 O HOH B 326 -20.202 40.690 39.970 1.00 47.80 O HETATM 4880 O HOH B 327 -0.568 50.162 38.653 1.00 38.86 O HETATM 4881 O HOH B 328 -7.893 41.442 49.097 1.00 53.50 O HETATM 4882 O HOH B 329 -0.454 52.281 36.857 1.00 52.97 O HETATM 4883 O HOH B 330 -3.499 33.879 31.719 1.00 48.15 O HETATM 4884 O HOH B 331 -14.107 50.972 50.591 1.00 56.76 O HETATM 4885 O HOH B 332 -4.176 59.077 36.910 1.00 50.04 O HETATM 4886 O HOH B 333 -17.830 47.431 44.426 1.00 56.68 O HETATM 4887 O HOH B 334 -8.105 33.708 40.034 1.00 64.68 O HETATM 4888 O HOH B 335 -29.848 40.604 38.347 1.00 64.59 O HETATM 4889 O HOH B 336 -8.314 32.609 33.471 1.00 56.92 O HETATM 4890 O HOH B 337 -7.612 53.792 46.726 1.00 63.73 O HETATM 4891 O HOH B 338 -23.591 42.801 27.602 1.00 54.50 O HETATM 4892 O HOH B 339 -7.915 44.828 53.515 1.00 62.08 O HETATM 4893 O HOH B 340 2.182 47.565 40.078 1.00 54.73 O HETATM 4894 O HOH B 341 3.737 45.167 39.653 1.00 51.74 O HETATM 4895 O HOH B 342 6.372 49.675 39.468 1.00 69.70 O HETATM 4896 O HOH B 343 -4.306 50.678 21.939 1.00 60.98 O HETATM 4897 O HOH B 344 -20.622 55.198 42.680 1.00 58.09 O HETATM 4898 O HOH B 345 -10.444 52.441 50.799 1.00 58.02 O HETATM 4899 O HOH B 346 -20.591 50.758 29.403 1.00 48.83 O HETATM 4900 O HOH B 347 -14.149 50.035 27.312 1.00 47.91 O HETATM 4901 O HOH B 348 -8.290 54.216 49.624 1.00 55.10 O HETATM 4902 O HOH B 349 2.723 36.846 29.340 1.00 62.26 O HETATM 4903 O HOH B 350 -2.447 51.049 26.202 1.00 59.90 O HETATM 4904 O HOH B 351 -21.942 44.167 40.040 1.00 64.43 O HETATM 4905 O HOH B 352 -2.894 57.259 49.969 1.00 66.31 O HETATM 4906 O HOH B 353 -2.136 33.214 26.299 1.00 60.40 O HETATM 4907 O HOH B 354 -9.726 51.015 53.355 1.00 69.75 O HETATM 4908 O HOH B 355 -34.091 42.358 31.149 1.00 79.34 O HETATM 4909 O HOH B 356 -13.053 48.833 25.854 1.00 63.80 O MASTER 637 0 0 35 7 0 0 6 4906 3 0 57 END
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Related entries of code: 4owx
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
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RCSB PDB
PDBbind
15aa, >2CCZ_2|Chain... at 100%
2ltt
RCSB PDB
PDBbind
17aa, >2LTT_2|Chain... at 100%
4ljr
RCSB PDB
PDBbind
35aa, >4LJR_2|Chains... *
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RCSB PDB
PDBbind
11aa, >6FWR_2|Chain... at 100%
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RCSB PDB
PDBbind
12aa, >5ZKL_2|Chain... at 100%
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
4owx
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
N-terminal half of SOSSA (SOSSAN/B1)
Ligand Name
12nt ssDNA
EC.Number
E.C.-.-.-.-
Resolution
2.3(Å)
Affinity (Kd/Ki/IC50)
Kd=8.2uM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) Cell Rep Vol. 6: pp. 982-991
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):
Q68E01
Q9BQ15
Entrez Gene ID
NCBI Entrez Gene ID:
65123
79035
ASD
Information of known allosteric effects of PDB entries
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