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*** VIRAL PROTEIN 22-JUN-15 5C69 ***elNémo ID: 2402291140011058810Job options:ID = 2402291140011058810 JOBID = VIRAL PROTEIN 22-JUN-15 5C69 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER VIRAL PROTEIN 22-JUN-15 5C69 TITLE CRYSTAL STRUCTURE OF PREFUSION-STABILIZED RSV F VARIANT PR-DM COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION GLYCOPROTEIN F0,FIBRITIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: F2 SUBUNIT, F1 SUBUNIT ECTODOMAIN; COMPND 5 SYNONYM: PROTEIN F; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN RESPIRATORY SYNCYTIAL VIRUS A, SOURCE 3 ENTEROBACTERIA PHAGE OX2; SOURCE 4 ORGANISM_TAXID: 11259, 10691; SOURCE 5 STRAIN: A2; SOURCE 6 GENE: WAC; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS CLASS I VIRAL FUSION PROTEIN, FUSION, RESPIRATORY SYNCYTIAL VIRUS, KEYWDS 2 PREFUSION, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.S.MCLELLAN,J.P.M.LANGEDIJK REVDAT 3 27-SEP-23 5C69 1 REMARK REVDAT 2 24-MAR-21 5C69 1 SOURCE REMARK REVDAT 1 23-SEP-15 5C69 0 JRNL AUTH A.KRARUP,D.TRUAN,P.FURMANOVA-HOLLENSTEIN,L.BOGAERT, JRNL AUTH 2 P.BOUCHIER,I.J.BISSCHOP,M.N.WIDJOJOATMODJO,R.ZAHN, JRNL AUTH 3 H.SCHUITEMAKER,J.S.MCLELLAN,J.P.LANGEDIJK JRNL TITL A HIGHLY STABLE PREFUSION RSV F VACCINE DERIVED FROM JRNL TITL 2 STRUCTURAL ANALYSIS OF THE FUSION MECHANISM. JRNL REF NAT COMMUN V. 6 8143 2015 JRNL REFN ESSN 2041-1723 JRNL PMID 26333350 JRNL DOI 10.1038/NCOMMS9143 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692) 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) : 46.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 36384 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.217 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1834 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 46.5544 - 5.4064 1.00 2885 159 0.1758 0.2083 REMARK 3 2 5.4064 - 4.2922 1.00 2734 139 0.1374 0.1698 REMARK 3 3 4.2922 - 3.7499 1.00 2682 155 0.1471 0.1639 REMARK 3 4 3.7499 - 3.4072 1.00 2686 129 0.1558 0.1901 REMARK 3 5 3.4072 - 3.1630 1.00 2628 150 0.1847 0.2445 REMARK 3 6 3.1630 - 2.9766 1.00 2649 132 0.1978 0.2753 REMARK 3 7 2.9766 - 2.8275 1.00 2637 125 0.2188 0.2439 REMARK 3 8 2.8275 - 2.7045 1.00 2611 155 0.2201 0.2559 REMARK 3 9 2.7045 - 2.6004 1.00 2611 153 0.2268 0.2838 REMARK 3 10 2.6004 - 2.5106 1.00 2601 140 0.2357 0.2548 REMARK 3 11 2.5106 - 2.4321 1.00 2598 151 0.2463 0.3116 REMARK 3 12 2.4321 - 2.3626 1.00 2618 115 0.2486 0.2791 REMARK 3 13 2.3626 - 2.3004 1.00 2610 131 0.2711 0.2876 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) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.700 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.62 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 : 0.005 3572 REMARK 3 ANGLE : 0.858 4839 REMARK 3 CHIRALITY : 0.032 580 REMARK 3 PLANARITY : 0.003 599 REMARK 3 DIHEDRAL : 13.827 1309 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 42 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.1054 0.0062 11.4558 REMARK 3 T TENSOR REMARK 3 T11: 0.3161 T22: 0.3697 REMARK 3 T33: 0.4639 T12: 0.0926 REMARK 3 T13: 0.0419 T23: 0.0851 REMARK 3 L TENSOR REMARK 3 L11: 6.8710 L22: 6.6826 REMARK 3 L33: 4.5894 L12: 5.8587 REMARK 3 L13: 5.4982 L23: 5.2512 REMARK 3 S TENSOR REMARK 3 S11: 0.1130 S12: 0.1410 S13: -0.4220 REMARK 3 S21: -0.2532 S22: 0.1691 S23: -0.7235 REMARK 3 S31: 0.0886 S32: 0.8015 S33: -0.3996 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 62 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.9551 6.9513 -14.2130 REMARK 3 T TENSOR REMARK 3 T11: 0.3546 T22: 0.3518 REMARK 3 T33: 0.2599 T12: -0.0452 REMARK 3 T13: 0.0574 T23: -0.0735 REMARK 3 L TENSOR REMARK 3 L11: 8.3892 L22: 1.0980 REMARK 3 L33: 2.8738 L12: 0.0279 REMARK 3 L13: 2.7712 L23: -1.0874 REMARK 3 S TENSOR REMARK 3 S11: -0.2235 S12: 1.1921 S13: 0.1791 REMARK 3 S21: -0.2435 S22: 0.0462 S23: 0.0136 REMARK 3 S31: 0.0757 S32: 0.4278 S33: 0.1102 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 67 ) REMARK 3 ORIGIN FOR THE GROUP (A): -21.1889 6.7549 -24.0065 REMARK 3 T TENSOR REMARK 3 T11: 1.1381 T22: 1.3920 REMARK 3 T33: 1.4140 T12: -0.0041 REMARK 3 T13: -0.3592 T23: 0.0572 REMARK 3 L TENSOR REMARK 3 L11: 1.7543 L22: 5.3284 REMARK 3 L33: 3.4776 L12: -3.0208 REMARK 3 L13: 0.9050 L23: -1.6012 REMARK 3 S TENSOR REMARK 3 S11: 0.5620 S12: -0.2742 S13: -0.6363 REMARK 3 S21: 0.7325 S22: -0.3216 S23: 0.5389 REMARK 3 S31: -0.2698 S32: 0.2678 S33: -0.2367 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -30.1700 -4.0693 -22.8560 REMARK 3 T TENSOR REMARK 3 T11: 0.8312 T22: 0.9821 REMARK 3 T33: 0.9680 T12: -0.2147 REMARK 3 T13: 0.0120 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 2.0630 L22: 0.2411 REMARK 3 L33: 3.1801 L12: -0.2960 REMARK 3 L13: -0.5300 L23: 0.8533 REMARK 3 S TENSOR REMARK 3 S11: -0.4845 S12: 0.7867 S13: 0.9137 REMARK 3 S21: -0.7499 S22: -0.3276 S23: -1.3969 REMARK 3 S31: -1.1831 S32: 0.4278 S33: 0.7840 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 98 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1992 3.4690 -15.6900 REMARK 3 T TENSOR REMARK 3 T11: 0.4660 T22: 0.4913 REMARK 3 T33: 0.6080 T12: -0.0291 REMARK 3 T13: -0.0441 T23: -0.0365 REMARK 3 L TENSOR REMARK 3 L11: 8.3964 L22: 5.0573 REMARK 3 L33: 3.3074 L12: 6.4995 REMARK 3 L13: 5.2475 L23: 4.0731 REMARK 3 S TENSOR REMARK 3 S11: 0.1330 S12: 0.0527 S13: 0.8478 REMARK 3 S21: 0.0824 S22: -0.3039 S23: 1.1250 REMARK 3 S31: -0.1619 S32: -0.4798 S33: 0.2027 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 103 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.8455 18.2729 -6.9703 REMARK 3 T TENSOR REMARK 3 T11: 1.1816 T22: 1.4374 REMARK 3 T33: 1.1180 T12: 0.5395 REMARK 3 T13: -0.2620 T23: 0.0587 REMARK 3 L TENSOR REMARK 3 L11: 5.6948 L22: 8.9756 REMARK 3 L33: 3.8957 L12: 3.0650 REMARK 3 L13: -3.2589 L23: 1.6097 REMARK 3 S TENSOR REMARK 3 S11: 0.7875 S12: 0.7520 S13: -0.0749 REMARK 3 S21: -1.0176 S22: -0.8574 S23: 2.0765 REMARK 3 S31: -0.4663 S32: -0.4593 S33: -0.0097 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 216 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.8666 8.7379 -22.0988 REMARK 3 T TENSOR REMARK 3 T11: 0.6137 T22: 0.5949 REMARK 3 T33: 0.3921 T12: -0.0325 REMARK 3 T13: -0.0262 T23: 0.0582 REMARK 3 L TENSOR REMARK 3 L11: 2.5302 L22: 2.9557 REMARK 3 L33: 2.2608 L12: 1.7630 REMARK 3 L13: 0.7252 L23: 0.7285 REMARK 3 S TENSOR REMARK 3 S11: -0.6147 S12: 1.0091 S13: 0.3030 REMARK 3 S21: -1.0806 S22: 0.5168 S23: 0.4703 REMARK 3 S31: -0.3934 S32: 0.2116 S33: 0.0838 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 217 THROUGH 331 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.0811 2.9293 -8.4546 REMARK 3 T TENSOR REMARK 3 T11: 0.3001 T22: 0.2556 REMARK 3 T33: 0.2496 T12: -0.0331 REMARK 3 T13: 0.0568 T23: -0.0044 REMARK 3 L TENSOR REMARK 3 L11: 3.0295 L22: 0.9616 REMARK 3 L33: 1.3426 L12: 0.2772 REMARK 3 L13: 1.4643 L23: 0.2593 REMARK 3 S TENSOR REMARK 3 S11: -0.0263 S12: 0.3813 S13: -0.1544 REMARK 3 S21: -0.1690 S22: 0.0082 S23: -0.0347 REMARK 3 S31: 0.1439 S32: 0.0203 S33: 0.0277 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 506 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.7882 5.6258 15.9772 REMARK 3 T TENSOR REMARK 3 T11: 0.2458 T22: 0.3205 REMARK 3 T33: 0.3595 T12: 0.0125 REMARK 3 T13: -0.0076 T23: 0.0289 REMARK 3 L TENSOR REMARK 3 L11: 1.0574 L22: 1.5431 REMARK 3 L33: 3.2274 L12: 0.1871 REMARK 3 L13: -0.0656 L23: -0.8792 REMARK 3 S TENSOR REMARK 3 S11: 0.0279 S12: -0.0330 S13: -0.0510 REMARK 3 S21: 0.1623 S22: -0.0283 S23: -0.3139 REMARK 3 S31: -0.1759 S32: 0.3267 S33: -0.0067 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 5C69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-15. REMARK 100 THE DEPOSITION ID IS D_1000211089. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792368 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36440 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 46.540 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 11.60 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 12.00 REMARK 200 R MERGE FOR SHELL (I) : 1.55400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4MMR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.24M K/NA TARTRATE, 0.2M LISO4, 0.1M REMARK 280 CHES PH 9.5, VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+1/2 REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4 REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4 REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4 REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4 REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4 REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4 REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4 REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4 REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4 REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4 REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4 REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4 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 83.91000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.91000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.91000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.91000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 83.91000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.91000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 83.91000 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 83.91000 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 83.91000 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 83.91000 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 83.91000 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 83.91000 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 83.91000 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 83.91000 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 83.91000 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 83.91000 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 83.91000 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 83.91000 REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 125.86500 REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 41.95500 REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 125.86500 REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 125.86500 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 125.86500 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 41.95500 REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 125.86500 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 41.95500 REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 125.86500 REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 41.95500 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 125.86500 REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 41.95500 REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 41.95500 REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 125.86500 REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 41.95500 REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 125.86500 REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 125.86500 REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 125.86500 REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 41.95500 REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 125.86500 REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 125.86500 REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 41.95500 REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 41.95500 REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 41.95500 REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 125.86500 REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 41.95500 REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 125.86500 REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 41.95500 REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 125.86500 REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 125.86500 REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 125.86500 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 46130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 95980 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -949.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 -41.95500 REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -41.95500 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -41.95500 REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 -41.95500 REMARK 350 BIOMT2 5 0.000000 0.000000 -1.000000 -41.95500 REMARK 350 BIOMT3 5 0.000000 -1.000000 0.000000 -41.95500 REMARK 350 BIOMT1 6 0.000000 0.000000 -1.000000 -41.95500 REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 -41.95500 REMARK 350 BIOMT3 6 -1.000000 0.000000 0.000000 -41.95500 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 CL CL A 610 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 843 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 865 LIES ON A SPECIAL POSITION. 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 GLN A 26 REMARK 465 ASN A 104 REMARK 465 ASN A 105 REMARK 465 ARG A 106 REMARK 465 ALA A 107 REMARK 465 ARG A 108 REMARK 465 ARG A 109 REMARK 465 ARG A 480 REMARK 465 LYS A 481 REMARK 465 SER A 482 REMARK 465 ASP A 483 REMARK 465 GLU A 484 REMARK 465 LEU A 485 REMARK 465 LEU A 486 REMARK 465 SER A 487 REMARK 465 ALA A 488 REMARK 465 ILE A 489 REMARK 465 GLY A 490 REMARK 465 GLY A 491 REMARK 465 TYR A 492 REMARK 465 ILE A 493 REMARK 465 PRO A 494 REMARK 465 GLU A 495 REMARK 465 ALA A 496 REMARK 465 PRO A 497 REMARK 465 ARG A 498 REMARK 465 ASP A 499 REMARK 465 GLY A 500 REMARK 465 GLN A 501 REMARK 465 ALA A 502 REMARK 465 TYR A 503 REMARK 465 VAL A 504 REMARK 465 ARG A 505 REMARK 465 LYS A 506 REMARK 465 ASP A 507 REMARK 465 GLY A 508 REMARK 465 GLU A 509 REMARK 465 TRP A 510 REMARK 465 VAL A 511 REMARK 465 LEU A 512 REMARK 465 LEU A 513 REMARK 465 SER A 514 REMARK 465 THR A 515 REMARK 465 PHE A 516 REMARK 465 LEU A 517 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 LYS A 65 -121.80 -88.38 REMARK 500 ASN A 250 42.99 -140.21 REMARK 500 SER A 263 -74.80 -118.57 REMARK 500 SER A 321 -169.23 -119.50 REMARK 500 SER A 335 -98.72 58.10 REMARK 500 ARG A 402 -15.77 -144.03 REMARK 500 ALA A 463 -157.37 -115.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 608 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 609 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 610 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 612 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 613 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4ZYP RELATED DB: PDB REMARK 900 RELATED ID: 5C6B RELATED DB: PDB DBREF 5C69 A 26 491 UNP P03420 FUS_HRSVA 26 518 DBREF 5C69 A 492 517 UNP Q38650 Q38650_BPOX2 459 484 SEQADV 5C69 ILE A 67 UNP P03420 ASN 67 ENGINEERED MUTATION SEQADV 5C69 ALA A 102 UNP P03420 PRO 102 CONFLICT SEQADV 5C69 A UNP P03420 ARG 108 DELETION SEQADV 5C69 A UNP P03420 ARG 109 DELETION SEQADV 5C69 A UNP P03420 GLU 110 DELETION SEQADV 5C69 A UNP P03420 LEU 111 DELETION SEQADV 5C69 A UNP P03420 PRO 112 DELETION SEQADV 5C69 A UNP P03420 ARG 113 DELETION SEQADV 5C69 A UNP P03420 PHE 114 DELETION SEQADV 5C69 A UNP P03420 MET 115 DELETION SEQADV 5C69 A UNP P03420 ASN 116 DELETION SEQADV 5C69 A UNP P03420 TYR 117 DELETION SEQADV 5C69 A UNP P03420 THR 118 DELETION SEQADV 5C69 A UNP P03420 LEU 119 DELETION SEQADV 5C69 A UNP P03420 ASN 120 DELETION SEQADV 5C69 A UNP P03420 ASN 121 DELETION SEQADV 5C69 A UNP P03420 ALA 122 DELETION SEQADV 5C69 A UNP P03420 LYS 123 DELETION SEQADV 5C69 A UNP P03420 LYS 124 DELETION SEQADV 5C69 A UNP P03420 THR 125 DELETION SEQADV 5C69 A UNP P03420 ASN 126 DELETION SEQADV 5C69 A UNP P03420 VAL 127 DELETION SEQADV 5C69 A UNP P03420 THR 128 DELETION SEQADV 5C69 A UNP P03420 LEU 129 DELETION SEQADV 5C69 A UNP P03420 SER 130 DELETION SEQADV 5C69 A UNP P03420 LYS 131 DELETION SEQADV 5C69 A UNP P03420 LYS 132 DELETION SEQADV 5C69 A UNP P03420 ARG 133 DELETION SEQADV 5C69 A UNP P03420 LYS 134 DELETION SEQADV 5C69 PRO A 188 UNP P03420 SER 215 ENGINEERED MUTATION SEQADV 5C69 VAL A 352 UNP P03420 ILE 379 ENGINEERED MUTATION SEQADV 5C69 VAL A 420 UNP P03420 MET 447 ENGINEERED MUTATION SEQADV 5C69 SER A 487 UNP P03420 HIS 514 LINKER SEQADV 5C69 ALA A 488 UNP P03420 ASN 515 LINKER SEQADV 5C69 ILE A 489 UNP P03420 VAL 516 LINKER SEQADV 5C69 GLY A 490 UNP P03420 ASN 517 LINKER SEQADV 5C69 GLY A 491 UNP P03420 ALA 518 LINKER SEQRES 1 A 492 GLN ASN ILE THR GLU GLU PHE TYR GLN SER THR CYS SER SEQRES 2 A 492 ALA VAL SER LYS GLY TYR LEU SER ALA LEU ARG THR GLY SEQRES 3 A 492 TRP TYR THR SER VAL ILE THR ILE GLU LEU SER ASN ILE SEQRES 4 A 492 LYS GLU ILE LYS CYS ASN GLY THR ASP ALA LYS VAL LYS SEQRES 5 A 492 LEU ILE LYS GLN GLU LEU ASP LYS TYR LYS ASN ALA VAL SEQRES 6 A 492 THR GLU LEU GLN LEU LEU MET GLN SER THR PRO ALA THR SEQRES 7 A 492 ASN ASN ARG ALA ARG ARG PHE LEU GLY PHE LEU LEU GLY SEQRES 8 A 492 VAL GLY SER ALA ILE ALA SER GLY VAL ALA VAL SER LYS SEQRES 9 A 492 VAL LEU HIS LEU GLU GLY GLU VAL ASN LYS ILE LYS SER SEQRES 10 A 492 ALA LEU LEU SER THR ASN LYS ALA VAL VAL SER LEU SER SEQRES 11 A 492 ASN GLY VAL SER VAL LEU THR SER LYS VAL LEU ASP LEU SEQRES 12 A 492 LYS ASN TYR ILE ASP LYS GLN LEU LEU PRO ILE VAL ASN SEQRES 13 A 492 LYS GLN SER CYS SER ILE PRO ASN ILE GLU THR VAL ILE SEQRES 14 A 492 GLU PHE GLN GLN LYS ASN ASN ARG LEU LEU GLU ILE THR SEQRES 15 A 492 ARG GLU PHE SER VAL ASN ALA GLY VAL THR THR PRO VAL SEQRES 16 A 492 SER THR TYR MET LEU THR ASN SER GLU LEU LEU SER LEU SEQRES 17 A 492 ILE ASN ASP MET PRO ILE THR ASN ASP GLN LYS LYS LEU SEQRES 18 A 492 MET SER ASN ASN VAL GLN ILE VAL ARG GLN GLN SER TYR SEQRES 19 A 492 SER ILE MET SER ILE ILE LYS GLU GLU VAL LEU ALA TYR SEQRES 20 A 492 VAL VAL GLN LEU PRO LEU TYR GLY VAL ILE ASP THR PRO SEQRES 21 A 492 CYS TRP LYS LEU HIS THR SER PRO LEU CYS THR THR ASN SEQRES 22 A 492 THR LYS GLU GLY SER ASN ILE CYS LEU THR ARG THR ASP SEQRES 23 A 492 ARG GLY TRP TYR CYS ASP ASN ALA GLY SER VAL SER PHE SEQRES 24 A 492 PHE PRO GLN ALA GLU THR CYS LYS VAL GLN SER ASN ARG SEQRES 25 A 492 VAL PHE CYS ASP THR MET ASN SER LEU THR LEU PRO SER SEQRES 26 A 492 GLU VAL ASN LEU CYS ASN VAL ASP ILE PHE ASN PRO LYS SEQRES 27 A 492 TYR ASP CYS LYS ILE MET THR SER LYS THR ASP VAL SER SEQRES 28 A 492 SER SER VAL ILE THR SER LEU GLY ALA ILE VAL SER CYS SEQRES 29 A 492 TYR GLY LYS THR LYS CYS THR ALA SER ASN LYS ASN ARG SEQRES 30 A 492 GLY ILE ILE LYS THR PHE SER ASN GLY CYS ASP TYR VAL SEQRES 31 A 492 SER ASN LYS GLY VAL ASP THR VAL SER VAL GLY ASN THR SEQRES 32 A 492 LEU TYR TYR VAL ASN LYS GLN GLU GLY LYS SER LEU TYR SEQRES 33 A 492 VAL LYS GLY GLU PRO ILE ILE ASN PHE TYR ASP PRO LEU SEQRES 34 A 492 VAL PHE PRO SER ASP GLU PHE ASP ALA SER ILE SER GLN SEQRES 35 A 492 VAL ASN GLU LYS ILE ASN GLN SER LEU ALA PHE ILE ARG SEQRES 36 A 492 LYS SER ASP GLU LEU LEU SER ALA ILE GLY GLY TYR ILE SEQRES 37 A 492 PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS SEQRES 38 A 492 ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU HET SO4 A 601 5 HET SO4 A 602 5 HET SO4 A 603 5 HET SO4 A 604 5 HET SO4 A 605 5 HET SO4 A 606 5 HET SO4 A 607 5 HET NHE A 608 13 HET NHE A 609 13 HET CL A 610 1 HET CL A 611 1 HET CL A 612 1 HET CL A 613 1 HET CL A 614 1 HETNAM SO4 SULFATE ION HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID HETNAM CL CHLORIDE ION HETSYN NHE N-CYCLOHEXYLTAURINE; CHES FORMUL 2 SO4 7(O4 S 2-) FORMUL 9 NHE 2(C8 H17 N O3 S) FORMUL 11 CL 5(CL 1-) FORMUL 16 HOH *173(H2 O) HELIX 1 AA1 ASP A 73 MET A 97 1 25 HELIX 2 AA2 PHE A 110 LEU A 115 5 6 HELIX 3 AA3 ILE A 121 LEU A 131 1 11 HELIX 4 AA4 GLY A 135 LEU A 144 1 10 HELIX 5 AA5 LEU A 168 LEU A 176 1 9 HELIX 6 AA6 LEU A 177 ASN A 181 5 5 HELIX 7 AA7 ASN A 189 ASN A 213 1 25 HELIX 8 AA8 THR A 226 ASP A 236 1 11 HELIX 9 AA9 THR A 240 ASN A 249 1 10 HELIX 10 AB1 ASN A 250 GLN A 257 1 8 HELIX 11 AB2 GLN A 327 CYS A 331 5 5 HELIX 12 AB3 MET A 343 SER A 345 5 3 HELIX 13 AB4 PRO A 349 VAL A 352 5 4 HELIX 14 AB5 ASN A 353 ASP A 358 1 6 HELIX 15 AB6 PRO A 446 TYR A 451 5 6 HELIX 16 AB7 ILE A 465 ILE A 479 1 15 SHEET 1 AA1 7 LYS A 332 GLN A 334 0 SHEET 2 AA1 7 ARG A 337 ASP A 341 -1 O PHE A 339 N LYS A 332 SHEET 3 AA1 7 SER A 38 ARG A 49 1 N ARG A 49 O CYS A 340 SHEET 4 AA1 7 VAL A 281 THR A 291 -1 O HIS A 290 N ALA A 39 SHEET 5 AA1 7 GLY A 313 ASN A 318 -1 O ASP A 317 N PRO A 285 SHEET 6 AA1 7 SER A 321 PHE A 325 -1 O PHE A 325 N TRP A 314 SHEET 7 AA1 7 LEU A 346 LEU A 348 -1 O LEU A 346 N PHE A 324 SHEET 1 AA2 5 LYS A 332 GLN A 334 0 SHEET 2 AA2 5 ARG A 337 ASP A 341 -1 O PHE A 339 N LYS A 332 SHEET 3 AA2 5 SER A 38 ARG A 49 1 N ARG A 49 O CYS A 340 SHEET 4 AA2 5 THR A 29 TYR A 33 -1 N TYR A 33 O SER A 38 SHEET 5 AA2 5 LYS A 438 VAL A 442 1 O LEU A 440 N PHE A 32 SHEET 1 AA3 6 LYS A 149 SER A 153 0 SHEET 2 AA3 6 SER A 159 ASP A 167 -1 O THR A 162 N ALA A 150 SHEET 3 AA3 6 GLY A 51 GLU A 60 1 N THR A 58 O SER A 163 SHEET 4 AA3 6 VAL A 269 LEU A 278 -1 O LEU A 276 N TYR A 53 SHEET 5 AA3 6 TYR A 259 LYS A 266 -1 N ILE A 261 O VAL A 273 SHEET 6 AA3 6 VAL A 216 THR A 217 -1 N THR A 217 O SER A 260 SHEET 1 AA4 4 LEU A 294 CYS A 295 0 SHEET 2 AA4 4 CYS A 306 ARG A 309 -1 O LEU A 307 N LEU A 294 SHEET 3 AA4 4 LYS A 367 SER A 371 -1 O SER A 371 N CYS A 306 SHEET 4 AA4 4 ALA A 463 SER A 464 -1 O ALA A 463 N ILE A 368 SHEET 1 AA5 3 SER A 377 ILE A 380 0 SHEET 2 AA5 3 GLY A 384 CYS A 389 -1 O ILE A 386 N VAL A 379 SHEET 3 AA5 3 GLY A 411 SER A 416 -1 O ASP A 413 N VAL A 387 SHEET 1 AA6 4 GLY A 403 THR A 407 0 SHEET 2 AA6 4 CYS A 395 ASN A 399 -1 N ALA A 397 O ILE A 405 SHEET 3 AA6 4 THR A 422 VAL A 425 -1 O THR A 422 N SER A 398 SHEET 4 AA6 4 THR A 428 TYR A 431 -1 O TYR A 430 N VAL A 423 SSBOND 1 CYS A 37 CYS A 412 1555 1555 2.02 SSBOND 2 CYS A 69 CYS A 185 1555 1555 2.03 SSBOND 3 CYS A 286 CYS A 316 1555 1555 2.03 SSBOND 4 CYS A 295 CYS A 306 1555 1555 2.04 SSBOND 5 CYS A 331 CYS A 340 1555 1555 2.04 SSBOND 6 CYS A 355 CYS A 366 1555 1555 2.04 SSBOND 7 CYS A 389 CYS A 395 1555 1555 2.04 CISPEP 1 THR A 218 PRO A 219 0 -2.09 SITE 1 AC1 3 PHE A 110 ARG A 312 GLN A 327 SITE 1 AC2 7 SER A 416 LYS A 418 LYS A 438 SER A 439 SITE 2 AC2 7 HOH A 747 HOH A 750 HOH A 784 SITE 1 AC3 2 ASN A 250 ARG A 337 SITE 1 AC4 3 LEU A 166 ASP A 167 LYS A 199 SITE 1 AC5 3 VAL A 212 ASN A 213 HOH A 701 SITE 1 AC6 4 ASN A 417 LYS A 418 GLY A 419 LYS A 434 SITE 1 AC7 4 PRO A 238 ASN A 399 ASN A 401 ARG A 402 SITE 1 AC8 4 PHE A 110 GLY A 112 PHE A 113 GLN A 327 SITE 1 AC9 7 PHE A 360 PHE A 450 TYR A 451 ASP A 452 SITE 2 AC9 7 VAL A 455 ASN A 469 HOH A 702 SITE 1 AD1 2 ASN A 189 ILE A 190 SITE 1 AD2 3 TRP A 52 TYR A 431 HOH A 776 SITE 1 AD3 3 LYS A 288 TRP A 314 ALA A 328 SITE 1 AD4 3 LYS A 129 GLN A 435 GLU A 436 CRYST1 167.820 167.820 167.820 90.00 90.00 90.00 P 41 3 2 24 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 0.005959 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005959 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005959 0.00000 ATOM 1 N ASN A 27 34.999 -7.271 -2.025 1.00 67.26 N ANISOU 1 N ASN A 27 7888 9381 8286 321 2260 -1906 N ATOM 2 CA ASN A 27 34.834 -7.874 -0.712 1.00 64.23 C ANISOU 2 CA ASN A 27 7333 8581 8492 961 1872 -1728 C ATOM 3 C ASN A 27 34.674 -6.819 0.374 1.00 57.00 C ANISOU 3 C ASN A 27 6654 7481 7522 942 1688 -1190 C ATOM 4 O ASN A 27 35.388 -5.814 0.403 1.00 58.39 O ANISOU 4 O ASN A 27 6800 7918 7466 587 1868 -1193 O ATOM 5 CB ASN A 27 36.015 -8.795 -0.380 1.00 73.08 C ANISOU 5 CB ASN A 27 7757 9827 10182 1290 1856 -2378 C ATOM 6 CG ASN A 27 37.359 -8.085 -0.459 1.00 82.28 C ANISOU 6 CG ASN A 27 8531 11473 11257 945 2187 -2803 C ATOM 7 OD1 ASN A 27 37.588 -7.264 -1.348 1.00 87.63 O ANISOU 7 OD1 ASN A 27 9356 12580 11360 321 2590 -2891 O ATOM 8 ND2 ASN A 27 38.258 -8.405 0.470 1.00 84.46 N ANISOU 8 ND2 ASN A 27 8373 11653 12065 1275 1942 -3011 N ATOM 9 N ILE A 28 33.727 -7.059 1.270 1.00 50.21 N ANISOU 9 N ILE A 28 6014 6199 6866 1284 1337 -769 N ATOM 10 CA ILE A 28 33.473 -6.147 2.364 1.00 47.07 C ANISOU 10 CA ILE A 28 5790 5646 6448 1275 1163 -346 C ATOM 11 C ILE A 28 34.476 -6.390 3.481 1.00 45.91 C ANISOU 11 C ILE A 28 5255 5523 6665 1499 1040 -469 C ATOM 12 O ILE A 28 34.701 -7.529 3.887 1.00 44.34 O ANISOU 12 O ILE A 28 4818 5166 6864 1839 813 -639 O ATOM 13 CB ILE A 28 32.040 -6.304 2.908 1.00 45.30 C ANISOU 13 CB ILE A 28 5900 5047 6266 1459 882 43 C ATOM 14 CG1 ILE A 28 31.033 -6.325 1.757 1.00 45.35 C ANISOU 14 CG1 ILE A 28 6246 4957 6028 1326 920 99 C ATOM 15 CG2 ILE A 28 31.721 -5.198 3.908 1.00 43.19 C ANISOU 15 CG2 ILE A 28 5772 4695 5943 1364 758 355 C ATOM 16 CD1 ILE A 28 31.169 -5.162 0.802 1.00 47.42 C ANISOU 16 CD1 ILE A 28 6765 5375 5879 849 1063 151 C ATOM 17 N THR A 29 35.094 -5.318 3.962 1.00 45.43 N ANISOU 17 N THR A 29 5152 5619 6490 1294 1123 -378 N ATOM 18 CA THR A 29 35.965 -5.406 5.125 1.00 45.81 C ANISOU 18 CA THR A 29 4891 5652 6861 1481 954 -426 C ATOM 19 C THR A 29 35.542 -4.347 6.122 1.00 43.93 C ANISOU 19 C THR A 29 4892 5324 6477 1369 843 -1 C ATOM 20 O THR A 29 34.769 -3.450 5.790 1.00 43.86 O ANISOU 20 O THR A 29 5205 5287 6174 1145 906 228 O ATOM 21 CB THR A 29 37.452 -5.222 4.764 1.00 48.16 C ANISOU 21 CB THR A 29 4733 6312 7254 1354 1200 -917 C ATOM 22 OG1 THR A 29 37.644 -3.942 4.152 1.00 50.98 O ANISOU 22 OG1 THR A 29 5260 6962 7150 867 1522 -849 O ATOM 23 CG2 THR A 29 37.908 -6.313 3.810 1.00 49.03 C ANISOU 23 CG2 THR A 29 4486 6559 7585 1468 1320 -1510 C ATOM 24 N GLU A 30 36.043 -4.446 7.345 1.00 42.84 N ANISOU 24 N GLU A 30 4587 5116 6574 1513 622 70 N ATOM 25 CA GLU A 30 35.601 -3.544 8.393 1.00 40.82 C ANISOU 25 CA GLU A 30 4512 4806 6191 1399 519 404 C ATOM 26 C GLU A 30 36.697 -3.322 9.428 1.00 40.40 C ANISOU 26 C GLU A 30 4200 4827 6322 1429 400 372 C ATOM 27 O GLU A 30 37.426 -4.241 9.779 1.00 41.70 O ANISOU 27 O GLU A 30 4124 4908 6813 1636 177 209 O ATOM 28 CB GLU A 30 34.334 -4.092 9.055 1.00 39.29 C ANISOU 28 CB GLU A 30 4570 4374 5984 1477 285 654 C ATOM 29 CG GLU A 30 33.731 -3.203 10.130 1.00 37.71 C ANISOU 29 CG GLU A 30 4497 4184 5646 1309 222 866 C ATOM 30 CD GLU A 30 32.316 -3.625 10.491 1.00 38.03 C ANISOU 30 CD GLU A 30 4757 4089 5601 1274 110 982 C ATOM 31 OE1 GLU A 30 32.120 -4.141 11.613 1.00 36.78 O ANISOU 31 OE1 GLU A 30 4632 3913 5432 1193 -85 1100 O ATOM 32 OE2 GLU A 30 31.403 -3.441 9.648 1.00 37.54 O ANISOU 32 OE2 GLU A 30 4848 3950 5467 1273 200 942 O ATOM 33 N GLU A 31 36.805 -2.084 9.899 1.00 40.58 N ANISOU 33 N GLU A 31 4272 4966 6180 1228 486 510 N ATOM 34 CA GLU A 31 37.785 -1.707 10.906 1.00 42.74 C ANISOU 34 CA GLU A 31 4330 5321 6588 1222 385 506 C ATOM 35 C GLU A 31 37.096 -1.027 12.077 1.00 40.05 C ANISOU 35 C GLU A 31 4171 4934 6110 1098 255 785 C ATOM 36 O GLU A 31 36.286 -0.125 11.883 1.00 39.25 O ANISOU 36 O GLU A 31 4249 4843 5821 949 361 867 O ATOM 37 CB GLU A 31 38.841 -0.774 10.308 1.00 47.26 C ANISOU 37 CB GLU A 31 4701 6163 7093 1037 667 302 C ATOM 38 CG GLU A 31 39.607 -1.377 9.143 1.00 53.47 C ANISOU 38 CG GLU A 31 5221 7125 7969 1047 883 -118 C ATOM 39 CD GLU A 31 40.673 -0.446 8.594 1.00 60.12 C ANISOU 39 CD GLU A 31 5859 8320 8665 727 1204 -359 C ATOM 40 OE1 GLU A 31 40.783 0.704 9.083 1.00 59.84 O ANISOU 40 OE1 GLU A 31 5936 8330 8469 526 1214 -134 O ATOM 41 OE2 GLU A 31 41.403 -0.869 7.669 1.00 65.70 O ANISOU 41 OE2 GLU A 31 6272 9282 9411 637 1451 -820 O ATOM 42 N PHE A 32 37.418 -1.463 13.290 1.00 40.35 N ANISOU 42 N PHE A 32 4155 4913 6262 1130 -20 886 N ATOM 43 CA PHE A 32 36.899 -0.821 14.489 1.00 39.96 C ANISOU 43 CA PHE A 32 4224 4919 6040 925 -102 1066 C ATOM 44 C PHE A 32 37.976 0.016 15.158 1.00 39.29 C ANISOU 44 C PHE A 32 3943 4974 6012 856 -105 1044 C ATOM 45 O PHE A 32 39.067 -0.469 15.421 1.00 40.78 O ANISOU 45 O PHE A 32 3944 5124 6426 972 -282 983 O ATOM 46 CB PHE A 32 36.365 -1.850 15.489 1.00 40.19 C ANISOU 46 CB PHE A 32 4428 4825 6016 837 -427 1248 C ATOM 47 CG PHE A 32 36.026 -1.260 16.833 1.00 38.46 C ANISOU 47 CG PHE A 32 4285 4761 5566 516 -489 1359 C ATOM 48 CD1 PHE A 32 34.882 -0.481 17.001 1.00 34.90 C ANISOU 48 CD1 PHE A 32 3892 4463 4906 319 -273 1265 C ATOM 49 CD2 PHE A 32 36.851 -1.478 17.930 1.00 38.40 C ANISOU 49 CD2 PHE A 32 4264 4748 5580 392 -792 1492 C ATOM 50 CE1 PHE A 32 34.567 0.060 18.242 1.00 34.83 C ANISOU 50 CE1 PHE A 32 3877 4671 4686 -20 -284 1240 C ATOM 51 CE2 PHE A 32 36.541 -0.940 19.172 1.00 38.28 C ANISOU 51 CE2 PHE A 32 4326 4935 5285 15 -822 1565 C ATOM 52 CZ PHE A 32 35.400 -0.168 19.329 1.00 36.03 C ANISOU 52 CZ PHE A 32 4050 4875 4766 -203 -528 1406 C ATOM 53 N TYR A 33 37.657 1.270 15.445 1.00 38.81 N ANISOU 53 N TYR A 33 3901 5040 5804 684 40 1053 N ATOM 54 CA TYR A 33 38.598 2.141 16.132 1.00 41.45 C ANISOU 54 CA TYR A 33 4063 5510 6177 601 36 1040 C ATOM 55 C TYR A 33 38.208 2.281 17.593 1.00 40.89 C ANISOU 55 C TYR A 33 4051 5511 5973 402 -130 1141 C ATOM 56 O TYR A 33 37.262 2.998 17.931 1.00 38.20 O ANISOU 56 O TYR A 33 3766 5258 5492 236 -42 1075 O ATOM 57 CB TYR A 33 38.661 3.502 15.441 1.00 43.01 C ANISOU 57 CB TYR A 33 4235 5784 6325 503 250 965 C ATOM 58 CG TYR A 33 38.865 3.355 13.955 1.00 45.44 C ANISOU 58 CG TYR A 33 4572 6072 6622 534 425 881 C ATOM 59 CD1 TYR A 33 40.092 2.960 13.443 1.00 48.50 C ANISOU 59 CD1 TYR A 33 4731 6577 7120 584 534 718 C ATOM 60 CD2 TYR A 33 37.824 3.572 13.068 1.00 45.80 C ANISOU 60 CD2 TYR A 33 4851 5998 6552 478 469 907 C ATOM 61 CE1 TYR A 33 40.280 2.804 12.086 1.00 50.83 C ANISOU 61 CE1 TYR A 33 5031 6949 7334 507 751 564 C ATOM 62 CE2 TYR A 33 38.003 3.418 11.711 1.00 48.05 C ANISOU 62 CE2 TYR A 33 5214 6295 6746 411 620 846 C ATOM 63 CZ TYR A 33 39.231 3.034 11.225 1.00 51.13 C ANISOU 63 CZ TYR A 33 5376 6881 7172 392 795 666 C ATOM 64 OH TYR A 33 39.409 2.882 9.870 1.00 55.65 O ANISOU 64 OH TYR A 33 6003 7558 7584 221 1002 531 O ATOM 65 N GLN A 34 38.943 1.571 18.449 1.00 42.57 N ANISOU 65 N GLN A 34 4242 5685 6249 385 -409 1252 N ATOM 66 CA GLN A 34 38.717 1.595 19.885 1.00 42.03 C ANISOU 66 CA GLN A 34 4282 5720 5970 77 -605 1378 C ATOM 67 C GLN A 34 38.843 3.000 20.467 1.00 43.34 C ANISOU 67 C GLN A 34 4302 6112 6052 -80 -431 1266 C ATOM 68 O GLN A 34 38.169 3.335 21.445 1.00 44.65 O ANISOU 68 O GLN A 34 4526 6468 5972 -400 -423 1225 O ATOM 69 CB GLN A 34 39.696 0.654 20.585 1.00 42.47 C ANISOU 69 CB GLN A 34 4372 5603 6163 84 -1062 1550 C ATOM 70 CG GLN A 34 39.493 0.542 22.086 1.00 43.90 C ANISOU 70 CG GLN A 34 4767 5881 6031 -363 -1344 1751 C ATOM 71 CD GLN A 34 40.606 -0.226 22.765 1.00 48.25 C ANISOU 71 CD GLN A 34 5378 6175 6781 -359 -1927 1946 C ATOM 72 OE1 GLN A 34 41.666 -0.450 22.180 1.00 51.06 O ANISOU 72 OE1 GLN A 34 5485 6324 7592 36 -2066 1821 O ATOM 73 NE2 GLN A 34 40.374 -0.633 24.008 1.00 49.21 N ANISOU 73 NE2 GLN A 34 5819 6310 6567 -847 -2305 2210 N ATOM 74 N SER A 35 39.694 3.823 19.865 1.00 40.75 N ANISOU 74 N SER A 35 3773 5793 5918 97 -287 1172 N ATOM 75 CA SER A 35 39.944 5.153 20.404 1.00 43.08 C ANISOU 75 CA SER A 35 3928 6251 6189 -31 -191 1079 C ATOM 76 C SER A 35 38.726 6.083 20.294 1.00 41.98 C ANISOU 76 C SER A 35 3804 6174 5974 -144 -39 891 C ATOM 77 O SER A 35 38.568 6.997 21.102 1.00 43.38 O ANISOU 77 O SER A 35 3866 6501 6117 -311 -31 743 O ATOM 78 CB SER A 35 41.149 5.790 19.707 1.00 46.14 C ANISOU 78 CB SER A 35 4121 6630 6779 118 -90 1029 C ATOM 79 OG SER A 35 40.868 6.066 18.350 1.00 48.66 O ANISOU 79 OG SER A 35 4485 6879 7126 193 101 965 O ATOM 80 N THR A 36 37.862 5.850 19.310 1.00 39.68 N ANISOU 80 N THR A 36 3624 5747 5706 -42 39 843 N ATOM 81 CA THR A 36 36.763 6.776 19.051 1.00 40.31 C ANISOU 81 CA THR A 36 3682 5785 5849 -87 76 606 C ATOM 82 C THR A 36 35.395 6.097 19.002 1.00 40.02 C ANISOU 82 C THR A 36 3741 5733 5731 -135 94 474 C ATOM 83 O THR A 36 34.395 6.729 18.646 1.00 39.11 O ANISOU 83 O THR A 36 3580 5524 5757 -119 71 210 O ATOM 84 CB THR A 36 36.981 7.532 17.719 1.00 40.35 C ANISOU 84 CB THR A 36 3749 5573 6009 33 72 638 C ATOM 85 OG1 THR A 36 36.975 6.599 16.632 1.00 40.93 O ANISOU 85 OG1 THR A 36 3987 5532 6034 153 140 776 O ATOM 86 CG2 THR A 36 38.306 8.290 17.734 1.00 37.89 C ANISOU 86 CG2 THR A 36 3333 5319 5744 -4 84 730 C ATOM 87 N CYS A 37 35.360 4.815 19.357 1.00 37.52 N ANISOU 87 N CYS A 37 3554 5473 5227 -203 73 641 N ATOM 88 CA CYS A 37 34.122 4.049 19.412 1.00 37.06 C ANISOU 88 CA CYS A 37 3604 5442 5034 -324 99 541 C ATOM 89 C CYS A 37 33.364 4.138 18.085 1.00 37.43 C ANISOU 89 C CYS A 37 3713 5246 5262 -87 138 449 C ATOM 90 O CYS A 37 32.190 4.510 18.041 1.00 38.68 O ANISOU 90 O CYS A 37 3798 5404 5494 -143 158 134 O ATOM 91 CB CYS A 37 33.246 4.535 20.572 1.00 32.52 C ANISOU 91 CB CYS A 37 2873 5175 4308 -690 171 182 C ATOM 92 SG CYS A 37 31.835 3.451 20.959 1.00 41.86 S ANISOU 92 SG CYS A 37 4170 6537 5196 -1036 244 24 S ATOM 93 N SER A 38 34.054 3.812 17.000 1.00 37.19 N ANISOU 93 N SER A 38 3794 5021 5316 148 132 672 N ATOM 94 CA SER A 38 33.452 3.881 15.677 1.00 36.11 C ANISOU 94 CA SER A 38 3779 4655 5285 305 140 639 C ATOM 95 C SER A 38 34.024 2.793 14.782 1.00 36.28 C ANISOU 95 C SER A 38 3928 4585 5271 465 183 844 C ATOM 96 O SER A 38 35.035 2.178 15.111 1.00 38.59 O ANISOU 96 O SER A 38 4158 4948 5557 506 165 965 O ATOM 97 CB SER A 38 33.667 5.261 15.048 1.00 33.95 C ANISOU 97 CB SER A 38 3487 4245 5166 313 68 576 C ATOM 98 OG SER A 38 35.043 5.551 14.913 1.00 32.80 O ANISOU 98 OG SER A 38 3300 4175 4987 299 126 742 O ATOM 99 N ALA A 39 33.361 2.546 13.659 1.00 35.52 N ANISOU 99 N ALA A 39 3984 4317 5195 558 198 830 N ATOM 100 CA ALA A 39 33.769 1.478 12.753 1.00 34.04 C ANISOU 100 CA ALA A 39 3879 4067 4986 698 258 928 C ATOM 101 C ALA A 39 33.425 1.835 11.320 1.00 36.88 C ANISOU 101 C ALA A 39 4410 4281 5323 697 298 912 C ATOM 102 O ALA A 39 32.364 2.413 11.046 1.00 35.09 O ANISOU 102 O ALA A 39 4308 3887 5137 658 182 848 O ATOM 103 CB ALA A 39 33.113 0.166 13.139 1.00 31.86 C ANISOU 103 CB ALA A 39 3676 3750 4679 754 185 968 C ATOM 104 N VAL A 40 34.325 1.486 10.407 1.00 37.51 N ANISOU 104 N VAL A 40 4481 4426 5346 702 430 921 N ATOM 105 CA VAL A 40 34.124 1.770 8.995 1.00 37.24 C ANISOU 105 CA VAL A 40 4659 4311 5178 571 479 926 C ATOM 106 C VAL A 40 34.063 0.469 8.204 1.00 40.33 C ANISOU 106 C VAL A 40 5068 4711 5546 703 591 851 C ATOM 107 O VAL A 40 34.939 -0.393 8.331 1.00 41.53 O ANISOU 107 O VAL A 40 4986 5001 5793 832 688 728 O ATOM 108 CB VAL A 40 35.242 2.677 8.437 1.00 38.72 C ANISOU 108 CB VAL A 40 4832 4662 5218 286 593 927 C ATOM 109 CG1 VAL A 40 35.150 2.793 6.920 1.00 38.10 C ANISOU 109 CG1 VAL A 40 5026 4570 4882 5 655 943 C ATOM 110 CG2 VAL A 40 35.184 4.057 9.091 1.00 38.33 C ANISOU 110 CG2 VAL A 40 4813 4530 5222 149 406 1012 C ATOM 111 N SER A 41 33.011 0.324 7.406 1.00 39.42 N ANISOU 111 N SER A 41 5206 4408 5363 694 520 885 N ATOM 112 CA SER A 41 32.871 -0.823 6.521 1.00 39.47 C ANISOU 112 CA SER A 41 5253 4412 5332 795 622 799 C ATOM 113 C SER A 41 33.209 -0.415 5.092 1.00 40.95 C ANISOU 113 C SER A 41 5622 4691 5245 478 755 759 C ATOM 114 O SER A 41 32.566 0.476 4.534 1.00 39.36 O ANISOU 114 O SER A 41 5746 4309 4900 243 582 909 O ATOM 115 CB SER A 41 31.452 -1.384 6.588 1.00 37.77 C ANISOU 115 CB SER A 41 5204 3951 5196 963 463 849 C ATOM 116 OG SER A 41 31.024 -1.493 7.932 1.00 39.61 O ANISOU 116 OG SER A 41 5324 4159 5567 1069 350 878 O ATOM 117 N LYS A 42 34.207 -1.076 4.505 1.00 43.23 N ANISOU 117 N LYS A 42 5697 5257 5473 426 1017 517 N ATOM 118 CA LYS A 42 34.684 -0.737 3.167 1.00 46.12 C ANISOU 118 CA LYS A 42 6197 5850 5476 -22 1230 401 C ATOM 119 C LYS A 42 34.380 -1.837 2.159 1.00 46.88 C ANISOU 119 C LYS A 42 6311 5998 5505 23 1363 190 C ATOM 120 O LYS A 42 34.026 -2.954 2.532 1.00 45.84 O ANISOU 120 O LYS A 42 6011 5731 5673 453 1295 97 O ATOM 121 CB LYS A 42 36.192 -0.484 3.177 1.00 51.20 C ANISOU 121 CB LYS A 42 6493 6903 6056 -251 1517 124 C ATOM 122 CG LYS A 42 36.666 0.505 4.208 1.00 54.34 C ANISOU 122 CG LYS A 42 6812 7288 6546 -273 1412 288 C ATOM 123 CD LYS A 42 38.152 0.800 4.021 1.00 61.35 C ANISOU 123 CD LYS A 42 7367 8612 7330 -578 1723 -26 C ATOM 124 CE LYS A 42 38.685 1.697 5.136 1.00 62.67 C ANISOU 124 CE LYS A 42 7417 8759 7636 -546 1611 123 C ATOM 125 NZ LYS A 42 40.145 1.982 4.964 1.00 68.56 N ANISOU 125 NZ LYS A 42 7803 9942 8304 -849 1921 -223 N ATOM 126 N GLY A 43 34.541 -1.518 0.877 1.00 40.60 N ANISOU 126 N GLY A 43 3746 5577 6105 599 1019 819 N ATOM 127 CA GLY A 43 34.400 -2.510 -0.169 1.00 42.04 C ANISOU 127 CA GLY A 43 3894 5586 6494 839 1078 580 C ATOM 128 C GLY A 43 33.163 -2.341 -1.025 1.00 42.10 C ANISOU 128 C GLY A 43 4098 5469 6427 842 1106 304 C ATOM 129 O GLY A 43 32.934 -3.110 -1.952 1.00 45.70 O ANISOU 129 O GLY A 43 4539 5798 7028 1035 1138 45 O ATOM 130 N TYR A 44 32.367 -1.326 -0.723 1.00 39.28 N ANISOU 130 N TYR A 44 3913 5158 5854 639 1079 333 N ATOM 131 CA TYR A 44 31.126 -1.105 -1.441 1.00 37.71 C ANISOU 131 CA TYR A 44 3894 4847 5585 621 1092 113 C ATOM 132 C TYR A 44 31.347 -0.293 -2.710 1.00 37.69 C ANISOU 132 C TYR A 44 3912 5051 5356 625 1173 -37 C ATOM 133 O TYR A 44 32.314 0.459 -2.819 1.00 40.08 O ANISOU 133 O TYR A 44 4120 5600 5510 559 1194 91 O ATOM 134 CB TYR A 44 30.110 -0.404 -0.535 1.00 37.94 C ANISOU 134 CB TYR A 44 4069 4843 5504 430 1018 201 C ATOM 135 CG TYR A 44 29.736 -1.211 0.688 1.00 38.27 C ANISOU 135 CG TYR A 44 4051 4777 5712 406 938 391 C ATOM 136 CD1 TYR A 44 28.668 -2.106 0.655 1.00 38.59 C ANISOU 136 CD1 TYR A 44 4130 4587 5947 448 897 353 C ATOM 137 CD2 TYR A 44 30.458 -1.088 1.874 1.00 37.15 C ANISOU 137 CD2 TYR A 44 3785 4798 5532 322 886 646 C ATOM 138 CE1 TYR A 44 28.323 -2.846 1.772 1.00 39.64 C ANISOU 138 CE1 TYR A 44 4158 4666 6236 396 804 613 C ATOM 139 CE2 TYR A 44 30.122 -1.823 2.995 1.00 37.60 C ANISOU 139 CE2 TYR A 44 3738 4840 5706 281 806 883 C ATOM 140 CZ TYR A 44 29.056 -2.701 2.938 1.00 39.41 C ANISOU 140 CZ TYR A 44 3987 4851 6134 312 765 890 C ATOM 141 OH TYR A 44 28.719 -3.441 4.044 1.00 40.73 O ANISOU 141 OH TYR A 44 4006 5044 6427 243 667 1206 O ATOM 142 N LEU A 45 30.443 -0.461 -3.667 1.00 38.24 N ANISOU 142 N LEU A 45 4081 5048 5402 684 1203 -274 N ATOM 143 CA LEU A 45 30.491 0.263 -4.930 1.00 39.01 C ANISOU 143 CA LEU A 45 4172 5390 5259 672 1270 -386 C ATOM 144 C LEU A 45 29.261 1.153 -5.048 1.00 37.47 C ANISOU 144 C LEU A 45 4170 5117 4950 505 1219 -401 C ATOM 145 O LEU A 45 28.165 0.748 -4.662 1.00 36.94 O ANISOU 145 O LEU A 45 4233 4805 4997 499 1174 -480 O ATOM 146 CB LEU A 45 30.568 -0.708 -6.103 1.00 39.01 C ANISOU 146 CB LEU A 45 4077 5455 5292 912 1346 -690 C ATOM 147 CG LEU A 45 31.825 -1.565 -6.167 1.00 43.18 C ANISOU 147 CG LEU A 45 4378 6089 5941 1132 1397 -739 C ATOM 148 CD1 LEU A 45 31.649 -2.670 -7.188 1.00 46.64 C ANISOU 148 CD1 LEU A 45 4739 6498 6482 1409 1428 -1151 C ATOM 149 CD2 LEU A 45 33.040 -0.711 -6.510 1.00 43.54 C ANISOU 149 CD2 LEU A 45 4242 6575 5727 1080 1474 -551 C ATOM 150 N SER A 46 29.444 2.359 -5.578 1.00 35.61 N ANISOU 150 N SER A 46 3925 5089 4515 366 1210 -296 N ATOM 151 CA SER A 46 28.375 3.355 -5.595 1.00 32.63 C ANISOU 151 CA SER A 46 3707 4613 4078 204 1129 -277 C ATOM 152 C SER A 46 27.387 3.166 -6.730 1.00 34.68 C ANISOU 152 C SER A 46 4031 4886 4261 251 1166 -464 C ATOM 153 O SER A 46 27.718 2.653 -7.799 1.00 37.13 O ANISOU 153 O SER A 46 4228 5411 4468 372 1252 -593 O ATOM 154 CB SER A 46 28.960 4.770 -5.691 1.00 32.35 C ANISOU 154 CB SER A 46 3615 4732 3945 14 1045 -48 C ATOM 155 OG SER A 46 29.672 4.952 -6.906 1.00 34.40 O ANISOU 155 OG SER A 46 3699 5328 4042 23 1109 31 O ATOM 156 N ALA A 47 26.166 3.611 -6.477 1.00 35.08 N ANISOU 156 N ALA A 47 4243 4744 4343 161 1095 -495 N ATOM 157 CA ALA A 47 25.182 3.844 -7.515 1.00 35.84 C ANISOU 157 CA ALA A 47 4400 4875 4344 139 1095 -598 C ATOM 158 C ALA A 47 24.359 5.020 -7.024 1.00 35.93 C ANISOU 158 C ALA A 47 4529 4734 4387 -19 977 -494 C ATOM 159 O ALA A 47 23.369 4.844 -6.322 1.00 35.29 O ANISOU 159 O ALA A 47 4569 4444 4398 -11 942 -576 O ATOM 160 CB ALA A 47 24.323 2.622 -7.757 1.00 35.47 C ANISOU 160 CB ALA A 47 4419 4675 4382 274 1132 -844 C ATOM 161 N LEU A 48 24.801 6.227 -7.359 1.00 35.82 N ANISOU 161 N LEU A 48 4452 4834 4322 -158 896 -303 N ATOM 162 CA LEU A 48 24.192 7.425 -6.807 1.00 33.29 C ANISOU 162 CA LEU A 48 4219 4323 4109 -287 738 -230 C ATOM 163 C LEU A 48 23.208 8.046 -7.788 1.00 34.87 C ANISOU 163 C LEU A 48 4448 4521 4281 -356 681 -204 C ATOM 164 O LEU A 48 23.563 8.297 -8.938 1.00 35.88 O ANISOU 164 O LEU A 48 4453 4894 4288 -416 694 -60 O ATOM 165 CB LEU A 48 25.268 8.449 -6.433 1.00 31.31 C ANISOU 165 CB LEU A 48 3871 4103 3922 -420 611 -16 C ATOM 166 CG LEU A 48 26.445 7.954 -5.586 1.00 31.72 C ANISOU 166 CG LEU A 48 3851 4223 3979 -379 656 19 C ATOM 167 CD1 LEU A 48 27.368 9.115 -5.185 1.00 29.23 C ANISOU 167 CD1 LEU A 48 3447 3901 3758 -544 480 226 C ATOM 168 CD2 LEU A 48 25.956 7.190 -4.359 1.00 31.17 C ANISOU 168 CD2 LEU A 48 3885 4000 3960 -274 694 -159 C ATOM 169 N ARG A 49 21.976 8.305 -7.350 1.00 33.25 N ANISOU 169 N ARG A 49 4373 4092 4169 -348 617 -321 N ATOM 170 CA ARG A 49 21.065 9.048 -8.215 1.00 33.41 C ANISOU 170 CA ARG A 49 4404 4088 4201 -426 531 -256 C ATOM 171 C ARG A 49 21.476 10.514 -8.237 1.00 33.05 C ANISOU 171 C ARG A 49 4285 3962 4312 -581 325 -29 C ATOM 172 O ARG A 49 21.483 11.189 -7.198 1.00 31.01 O ANISOU 172 O ARG A 49 4073 3473 4236 -593 188 -86 O ATOM 173 CB ARG A 49 19.600 8.937 -7.780 1.00 33.37 C ANISOU 173 CB ARG A 49 4531 3883 4264 -362 514 -436 C ATOM 174 CG ARG A 49 18.693 9.634 -8.802 1.00 35.99 C ANISOU 174 CG ARG A 49 4851 4214 4609 -439 428 -344 C ATOM 175 CD ARG A 49 17.408 10.201 -8.229 1.00 33.87 C ANISOU 175 CD ARG A 49 4669 3708 4491 -408 325 -451 C ATOM 176 NE ARG A 49 17.635 11.281 -7.280 1.00 32.72 N ANISOU 176 NE ARG A 49 4522 3360 4552 -422 155 -464 N ATOM 177 CZ ARG A 49 17.880 12.546 -7.610 1.00 33.08 C ANISOU 177 CZ ARG A 49 4495 3277 4795 -534 -54 -293 C ATOM 178 NH1 ARG A 49 17.946 12.915 -8.886 1.00 34.36 N ANISOU 178 NH1 ARG A 49 4561 3550 4944 -663 -104 -22 N ATOM 179 NH2 ARG A 49 18.066 13.446 -6.656 1.00 31.27 N ANISOU 179 NH2 ARG A 49 4268 2824 4791 -522 -236 -387 N ATOM 180 N THR A 50 21.793 11.005 -9.430 1.00 32.60 N ANISOU 180 N THR A 50 4087 4109 4191 -704 280 231 N ATOM 181 CA THR A 50 22.342 12.344 -9.592 1.00 31.79 C ANISOU 181 CA THR A 50 3860 3940 4279 -891 50 544 C ATOM 182 C THR A 50 21.402 13.262 -10.373 1.00 32.09 C ANISOU 182 C THR A 50 3860 3885 4449 -1001 -119 721 C ATOM 183 O THR A 50 21.434 14.476 -10.217 1.00 35.44 O ANISOU 183 O THR A 50 4228 4059 5178 -1132 -383 911 O ATOM 184 CB THR A 50 23.708 12.285 -10.303 1.00 33.24 C ANISOU 184 CB THR A 50 3825 4504 4299 -990 98 836 C ATOM 185 OG1 THR A 50 23.555 11.676 -11.595 1.00 32.97 O ANISOU 185 OG1 THR A 50 3680 4884 3963 -968 254 890 O ATOM 186 CG2 THR A 50 24.681 11.464 -9.486 1.00 29.89 C ANISOU 186 CG2 THR A 50 3419 4141 3796 -880 237 686 C ATOM 187 N GLY A 51 20.576 12.672 -11.226 1.00 31.32 N ANISOU 187 N GLY A 51 3777 3972 4150 -951 9 662 N ATOM 188 CA GLY A 51 19.624 13.427 -12.016 1.00 31.92 C ANISOU 188 CA GLY A 51 3803 4003 4322 -1050 -135 846 C ATOM 189 C GLY A 51 18.347 12.635 -12.210 1.00 32.69 C ANISOU 189 C GLY A 51 4034 4102 4283 -919 1 573 C ATOM 190 O GLY A 51 18.107 11.638 -11.531 1.00 32.05 O ANISOU 190 O GLY A 51 4099 3960 4119 -759 161 246 O ATOM 191 N TRP A 52 17.527 13.081 -13.150 1.00 35.10 N ANISOU 191 N TRP A 52 4267 4487 4584 -1005 -84 752 N ATOM 192 CA TRP A 52 16.242 12.454 -13.419 1.00 34.64 C ANISOU 192 CA TRP A 52 4313 4430 4418 -912 6 537 C ATOM 193 C TRP A 52 16.006 12.282 -14.917 1.00 37.54 C ANISOU 193 C TRP A 52 4525 5232 4507 -1009 42 730 C ATOM 194 O TRP A 52 16.332 13.164 -15.706 1.00 39.24 O ANISOU 194 O TRP A 52 4538 5632 4738 -1187 -100 1133 O ATOM 195 CB TRP A 52 15.102 13.293 -12.831 1.00 34.51 C ANISOU 195 CB TRP A 52 4380 4005 4728 -887 -169 497 C ATOM 196 CG TRP A 52 15.043 13.358 -11.329 1.00 32.89 C ANISOU 196 CG TRP A 52 4316 3454 4726 -748 -188 211 C ATOM 197 CD1 TRP A 52 15.310 14.441 -10.541 1.00 33.48 C ANISOU 197 CD1 TRP A 52 4378 3213 5129 -759 -400 228 C ATOM 198 CD2 TRP A 52 14.667 12.296 -10.441 1.00 31.22 C ANISOU 198 CD2 TRP A 52 4249 3218 4396 -583 -10 -129 C ATOM 199 NE1 TRP A 52 15.129 14.117 -9.215 1.00 31.96 N ANISOU 199 NE1 TRP A 52 4308 2866 4968 -595 -342 -118 N ATOM 200 CE2 TRP A 52 14.735 12.817 -9.129 1.00 32.22 C ANISOU 200 CE2 TRP A 52 4427 3088 4728 -499 -102 -295 C ATOM 201 CE3 TRP A 52 14.289 10.966 -10.632 1.00 30.58 C ANISOU 201 CE3 TRP A 52 4233 3308 4078 -508 190 -297 C ATOM 202 CZ2 TRP A 52 14.432 12.033 -8.009 1.00 30.58 C ANISOU 202 CZ2 TRP A 52 4311 2869 4439 -353 25 -572 C ATOM 203 CZ3 TRP A 52 13.989 10.198 -9.521 1.00 29.04 C ANISOU 203 CZ3 TRP A 52 4137 3020 3878 -378 287 -540 C ATOM 204 CH2 TRP A 52 14.059 10.735 -8.225 1.00 27.89 C ANISOU 204 CH2 TRP A 52 4018 2693 3885 -308 215 -649 C ATOM 205 N TYR A 53 15.417 11.157 -15.305 1.00 38.93 N ANISOU 205 N TYR A 53 4771 5584 4436 -905 207 455 N ATOM 206 CA TYR A 53 14.895 11.015 -16.658 1.00 41.55 C ANISOU 206 CA TYR A 53 4970 6316 4502 -982 216 564 C ATOM 207 C TYR A 53 13.367 11.018 -16.624 1.00 41.18 C ANISOU 207 C TYR A 53 5036 6043 4567 -958 158 461 C ATOM 208 O TYR A 53 12.759 10.353 -15.777 1.00 42.63 O ANISOU 208 O TYR A 53 5406 5941 4851 -822 227 148 O ATOM 209 CB TYR A 53 15.406 9.737 -17.321 1.00 44.08 C ANISOU 209 CB TYR A 53 5241 7068 4440 -882 412 296 C ATOM 210 CG TYR A 53 15.004 9.651 -18.774 1.00 52.87 C ANISOU 210 CG TYR A 53 6171 8705 5214 -964 411 391 C ATOM 211 CD1 TYR A 53 15.619 10.455 -19.738 1.00 57.12 C ANISOU 211 CD1 TYR A 53 6422 9724 5559 -1137 342 823 C ATOM 212 CD2 TYR A 53 13.997 8.784 -19.188 1.00 55.36 C ANISOU 212 CD2 TYR A 53 6569 9070 5394 -888 460 78 C ATOM 213 CE1 TYR A 53 15.248 10.387 -21.073 1.00 61.25 C ANISOU 213 CE1 TYR A 53 6735 10822 5713 -1221 339 932 C ATOM 214 CE2 TYR A 53 13.618 8.710 -20.522 1.00 59.97 C ANISOU 214 CE2 TYR A 53 6970 10182 5634 -965 447 138 C ATOM 215 CZ TYR A 53 14.247 9.510 -21.458 1.00 63.78 C ANISOU 215 CZ TYR A 53 7159 11195 5880 -1126 396 560 C ATOM 216 OH TYR A 53 13.863 9.430 -22.778 1.00 69.40 O ANISOU 216 OH TYR A 53 7654 12519 6196 -1207 383 633 O ATOM 217 N THR A 54 12.738 11.757 -17.532 1.00 40.61 N ANISOU 217 N THR A 54 4824 6127 4481 -1098 25 763 N ATOM 218 CA THR A 54 11.279 11.814 -17.542 1.00 43.88 C ANISOU 218 CA THR A 54 5318 6348 5007 -1078 -38 697 C ATOM 219 C THR A 54 10.677 11.176 -18.788 1.00 48.44 C ANISOU 219 C THR A 54 5804 7369 5232 -1128 15 666 C ATOM 220 O THR A 54 11.018 11.531 -19.916 1.00 50.80 O ANISOU 220 O THR A 54 5878 8129 5294 -1270 -29 958 O ATOM 221 CB THR A 54 10.768 13.255 -17.425 1.00 46.62 C ANISOU 221 CB THR A 54 5587 6402 5724 -1177 -283 1045 C ATOM 222 OG1 THR A 54 11.282 14.031 -18.512 1.00 51.76 O ANISOU 222 OG1 THR A 54 5979 7389 6298 -1383 -413 1522 O ATOM 223 CG2 THR A 54 11.218 13.867 -16.106 1.00 46.18 C ANISOU 223 CG2 THR A 54 5632 5874 6038 -1097 -365 967 C ATOM 224 N SER A 55 9.768 10.236 -18.565 1.00 47.99 N ANISOU 224 N SER A 55 5898 7198 5137 -1020 94 323 N ATOM 225 CA SER A 55 9.122 9.516 -19.648 1.00 48.35 C ANISOU 225 CA SER A 55 5880 7616 4873 -1053 125 204 C ATOM 226 C SER A 55 7.610 9.715 -19.592 1.00 43.59 C ANISOU 226 C SER A 55 5333 6800 4428 -1076 27 238 C ATOM 227 O SER A 55 7.040 9.837 -18.512 1.00 42.76 O ANISOU 227 O SER A 55 5369 6255 4622 -989 10 155 O ATOM 228 CB SER A 55 9.472 8.031 -19.569 1.00 50.87 C ANISOU 228 CB SER A 55 6302 8013 5015 -911 277 -265 C ATOM 229 OG SER A 55 9.122 7.364 -20.766 1.00 57.13 O ANISOU 229 OG SER A 55 6991 9246 5468 -937 286 -425 O ATOM 230 N VAL A 56 6.964 9.759 -20.752 1.00 42.81 N ANISOU 230 N VAL A 56 5095 7067 4104 -1189 -36 366 N ATOM 231 CA VAL A 56 5.514 9.904 -20.806 1.00 43.07 C ANISOU 231 CA VAL A 56 5153 6950 4262 -1219 -131 415 C ATOM 232 C VAL A 56 4.864 8.572 -21.171 1.00 45.33 C ANISOU 232 C VAL A 56 5514 7375 4336 -1178 -68 34 C ATOM 233 O VAL A 56 5.098 8.031 -22.255 1.00 47.21 O ANISOU 233 O VAL A 56 5639 8087 4211 -1229 -49 -79 O ATOM 234 CB VAL A 56 5.079 10.988 -21.816 1.00 45.41 C ANISOU 234 CB VAL A 56 5219 7517 4519 -1399 -297 889 C ATOM 235 CG1 VAL A 56 3.566 11.067 -21.889 1.00 45.46 C ANISOU 235 CG1 VAL A 56 5240 7385 4649 -1416 -390 926 C ATOM 236 CG2 VAL A 56 5.669 12.340 -21.442 1.00 45.88 C ANISOU 236 CG2 VAL A 56 5187 7348 4896 -1455 -425 1290 C ATOM 237 N ILE A 57 4.058 8.046 -20.252 1.00 43.39 N ANISOU 237 N ILE A 57 5432 6734 4320 -1087 -54 -169 N ATOM 238 CA ILE A 57 3.382 6.770 -20.448 1.00 43.67 C ANISOU 238 CA ILE A 57 5539 6792 4260 -1065 -41 -503 C ATOM 239 C ILE A 57 1.926 7.018 -20.803 1.00 43.30 C ANISOU 239 C ILE A 57 5440 6755 4256 -1154 -156 -353 C ATOM 240 O ILE A 57 1.241 7.769 -20.114 1.00 41.82 O ANISOU 240 O ILE A 57 5263 6295 4330 -1134 -201 -146 O ATOM 241 CB ILE A 57 3.460 5.880 -19.186 1.00 41.34 C ANISOU 241 CB ILE A 57 5419 6088 4200 -934 33 -768 C ATOM 242 CG1 ILE A 57 4.912 5.738 -18.715 1.00 40.75 C ANISOU 242 CG1 ILE A 57 5387 5973 4123 -840 141 -871 C ATOM 243 CG2 ILE A 57 2.837 4.516 -19.443 1.00 41.21 C ANISOU 243 CG2 ILE A 57 5451 6054 4153 -936 -6 -1084 C ATOM 244 CD1 ILE A 57 5.866 5.284 -19.792 1.00 42.44 C ANISOU 244 CD1 ILE A 57 5507 6601 4018 -842 182 -1038 C ATOM 245 N THR A 58 1.451 6.400 -21.880 1.00 42.95 N ANISOU 245 N THR A 58 5323 7046 3952 -1240 -213 -482 N ATOM 246 CA THR A 58 0.106 6.689 -22.342 1.00 44.67 C ANISOU 246 CA THR A 58 5461 7334 4178 -1348 -334 -300 C ATOM 247 C THR A 58 -0.789 5.460 -22.394 1.00 44.72 C ANISOU 247 C THR A 58 5536 7267 4187 -1362 -387 -608 C ATOM 248 O THR A 58 -0.338 4.350 -22.685 1.00 45.82 O ANISOU 248 O THR A 58 5724 7483 4202 -1328 -376 -992 O ATOM 249 CB THR A 58 0.112 7.345 -23.740 1.00 48.79 C ANISOU 249 CB THR A 58 5762 8399 4378 -1500 -416 -39 C ATOM 250 OG1 THR A 58 0.540 6.395 -24.722 1.00 52.56 O ANISOU 250 OG1 THR A 58 6183 9324 4464 -1522 -401 -376 O ATOM 251 CG2 THR A 58 1.035 8.554 -23.761 1.00 49.23 C ANISOU 251 CG2 THR A 58 5708 8531 4467 -1525 -408 334 C ATOM 252 N ILE A 59 -2.062 5.679 -22.085 1.00 43.69 N ANISOU 252 N ILE A 59 5392 6970 4239 -1405 -466 -435 N ATOM 253 CA ILE A 59 -3.101 4.687 -22.308 1.00 45.16 C ANISOU 253 CA ILE A 59 5590 7137 4432 -1475 -566 -617 C ATOM 254 C ILE A 59 -4.140 5.296 -23.238 1.00 47.72 C ANISOU 254 C ILE A 59 5754 7758 4621 -1618 -690 -350 C ATOM 255 O ILE A 59 -4.652 6.384 -22.976 1.00 47.22 O ANISOU 255 O ILE A 59 5613 7622 4706 -1618 -707 15 O ATOM 256 CB ILE A 59 -3.759 4.236 -20.993 1.00 43.45 C ANISOU 256 CB ILE A 59 5467 6484 4557 -1410 -553 -623 C ATOM 257 CG1 ILE A 59 -2.729 3.543 -20.099 1.00 42.42 C ANISOU 257 CG1 ILE A 59 5471 6091 4556 -1289 -451 -858 C ATOM 258 CG2 ILE A 59 -4.926 3.303 -21.269 1.00 45.58 C ANISOU 258 CG2 ILE A 59 5709 6739 4868 -1524 -696 -720 C ATOM 259 CD1 ILE A 59 -3.292 3.073 -18.787 1.00 41.68 C ANISOU 259 CD1 ILE A 59 5424 5654 4758 -1242 -439 -812 C ATOM 260 N GLU A 60 -4.429 4.612 -24.338 1.00 51.17 N ANISOU 260 N GLU A 60 6122 8535 4785 -1731 -793 -549 N ATOM 261 CA GLU A 60 -5.404 5.109 -25.300 1.00 54.47 C ANISOU 261 CA GLU A 60 6365 9298 5031 -1887 -924 -295 C ATOM 262 C GLU A 60 -6.819 4.754 -24.849 1.00 55.49 C ANISOU 262 C GLU A 60 6506 9177 5402 -1939 -1024 -230 C ATOM 263 O GLU A 60 -7.147 3.583 -24.648 1.00 56.77 O ANISOU 263 O GLU A 60 6751 9171 5647 -1957 -1088 -540 O ATOM 264 CB GLU A 60 -5.113 4.544 -26.687 1.00 58.76 C ANISOU 264 CB GLU A 60 6800 10400 5127 -1985 -1000 -559 C ATOM 265 CG GLU A 60 -5.880 5.208 -27.812 1.00 65.29 C ANISOU 265 CG GLU A 60 7399 11721 5687 -2162 -1126 -236 C ATOM 266 CD GLU A 60 -5.343 4.821 -29.177 1.00 71.51 C ANISOU 266 CD GLU A 60 8031 13201 5939 -2237 -1171 -483 C ATOM 267 OE1 GLU A 60 -6.116 4.867 -30.159 1.00 75.75 O ANISOU 267 OE1 GLU A 60 8410 14075 6298 -2344 -1258 -373 O ATOM 268 OE2 GLU A 60 -4.146 4.471 -29.267 1.00 72.10 O ANISOU 268 OE2 GLU A 60 8141 13374 5881 -2108 -1045 -766 O ATOM 269 N LEU A 61 -7.652 5.777 -24.688 1.00 54.47 N ANISOU 269 N LEU A 61 6267 9016 5414 -1962 -1058 191 N ATOM 270 CA LEU A 61 -8.989 5.597 -24.140 1.00 52.28 C ANISOU 270 CA LEU A 61 5961 8530 5372 -1985 -1129 312 C ATOM 271 C LEU A 61 -10.068 5.728 -25.203 1.00 55.50 C ANISOU 271 C LEU A 61 6193 9283 5613 -2163 -1296 498 C ATOM 272 O LEU A 61 -9.860 6.346 -26.245 1.00 59.05 O ANISOU 272 O LEU A 61 6507 10126 5804 -2255 -1349 671 O ATOM 273 CB LEU A 61 -9.242 6.608 -23.026 1.00 50.19 C ANISOU 273 CB LEU A 61 5680 7962 5428 -1830 -1047 596 C ATOM 274 CG LEU A 61 -8.288 6.551 -21.829 1.00 47.92 C ANISOU 274 CG LEU A 61 5548 7345 5315 -1651 -890 436 C ATOM 275 CD1 LEU A 61 -8.516 7.747 -20.939 1.00 47.84 C ANISOU 275 CD1 LEU A 61 5478 7126 5572 -1489 -843 681 C ATOM 276 CD2 LEU A 61 -8.458 5.264 -21.035 1.00 44.63 C ANISOU 276 CD2 LEU A 61 5240 6709 5008 -1637 -866 179 C ATOM 277 N SER A 62 -11.223 5.138 -24.932 1.00 54.81 N ANISOU 277 N SER A 62 6080 9080 5665 -2228 -1391 501 N ATOM 278 CA SER A 62 -12.356 5.227 -25.837 1.00 59.01 C ANISOU 278 CA SER A 62 6437 9916 6069 -2404 -1561 693 C ATOM 279 C SER A 62 -13.347 6.248 -25.303 1.00 58.71 C ANISOU 279 C SER A 62 6258 9764 6287 -2342 -1562 1136 C ATOM 280 O SER A 62 -13.626 6.277 -24.105 1.00 58.94 O ANISOU 280 O SER A 62 6329 9461 6604 -2198 -1474 1169 O ATOM 281 CB SER A 62 -13.025 3.857 -26.001 1.00 60.11 C ANISOU 281 CB SER A 62 6609 10022 6206 -2541 -1710 403 C ATOM 282 OG SER A 62 -14.317 3.978 -26.561 1.00 62.05 O ANISOU 282 OG SER A 62 6679 10481 6417 -2700 -1873 646 O ATOM 283 N ASN A 63 -13.868 7.096 -26.180 1.00113.38 N ANISOU 283 N ASN A 63 12085 16234 14760 26 -4431 837 N ATOM 284 CA ASN A 63 -14.886 8.047 -25.759 1.00112.44 C ANISOU 284 CA ASN A 63 12205 15944 14575 -138 -4225 735 C ATOM 285 C ASN A 63 -16.257 7.385 -25.746 1.00112.22 C ANISOU 285 C ASN A 63 12218 15715 14705 0 -4164 630 C ATOM 286 O ASN A 63 -16.829 7.096 -26.795 1.00110.98 O ANISOU 286 O ASN A 63 11951 15503 14712 281 -4165 521 O ATOM 287 CB ASN A 63 -14.896 9.277 -26.665 1.00111.49 C ANISOU 287 CB ASN A 63 12102 15850 14411 -85 -4055 672 C ATOM 288 CG ASN A 63 -14.963 10.574 -25.880 1.00111.70 C ANISOU 288 CG ASN A 63 12389 15802 14250 -406 -3930 670 C ATOM 289 OD1 ASN A 63 -16.027 10.971 -25.403 1.00110.99 O ANISOU 289 OD1 ASN A 63 12526 15543 14102 -459 -3776 576 O ATOM 290 ND2 ASN A 63 -13.819 11.240 -25.737 1.00112.87 N ANISOU 290 ND2 ASN A 63 12506 16064 14313 -612 -4007 784 N ATOM 291 N ILE A 64 -16.773 7.135 -24.548 1.00113.54 N ANISOU 291 N ILE A 64 12544 15764 14834 -187 -4122 679 N ATOM 292 CA ILE A 64 -18.047 6.448 -24.391 1.00113.82 C ANISOU 292 CA ILE A 64 12572 15602 15073 -97 -4049 644 C ATOM 293 C ILE A 64 -19.050 7.303 -23.636 1.00116.67 C ANISOU 293 C ILE A 64 13162 15827 15340 -239 -3775 634 C ATOM 294 O ILE A 64 -18.869 7.595 -22.452 1.00117.35 O ANISOU 294 O ILE A 64 13481 15899 15207 -441 -3706 729 O ATOM 295 CB ILE A 64 -17.880 5.115 -23.652 1.00112.56 C ANISOU 295 CB ILE A 64 12368 15400 14999 -123 -4205 767 C ATOM 296 CG1 ILE A 64 -17.064 4.142 -24.496 1.00111.23 C ANISOU 296 CG1 ILE A 64 11984 15337 14943 92 -4476 766 C ATOM 297 CG2 ILE A 64 -19.238 4.518 -23.320 1.00112.50 C ANISOU 297 CG2 ILE A 64 12349 15160 15234 -94 -4090 785 C ATOM 298 CD1 ILE A 64 -16.851 2.830 -23.818 1.00112.05 C ANISOU 298 CD1 ILE A 64 12066 15388 15119 84 -4644 883 C ATOM 299 N LYS A 65 -20.103 7.708 -24.336 1.00117.73 N ANISOU 299 N LYS A 65 13251 15861 15622 -95 -3627 519 N ATOM 300 CA LYS A 65 -21.195 8.446 -23.723 1.00120.34 C ANISOU 300 CA LYS A 65 13765 16062 15895 -161 -3339 520 C ATOM 301 C LYS A 65 -22.220 7.453 -23.184 1.00122.00 C ANISOU 301 C LYS A 65 13869 16112 16375 -132 -3274 623 C ATOM 302 O LYS A 65 -21.890 6.596 -22.362 1.00123.09 O ANISOU 302 O LYS A 65 14024 16234 16512 -225 -3349 767 O ATOM 303 CB LYS A 65 -21.835 9.405 -24.731 1.00121.20 C ANISOU 303 CB LYS A 65 13864 16149 16039 -7 -3207 359 C ATOM 304 CG LYS A 65 -20.851 10.378 -25.380 1.00122.06 C ANISOU 304 CG LYS A 65 14055 16396 15928 -21 -3245 286 C ATOM 305 CD LYS A 65 -20.654 11.639 -24.550 1.00124.15 C ANISOU 305 CD LYS A 65 14661 16651 15861 -241 -3076 311 C ATOM 306 CE LYS A 65 -21.865 12.559 -24.650 1.00125.08 C ANISOU 306 CE LYS A 65 14937 16647 15940 -148 -2799 220 C ATOM 307 NZ LYS A 65 -22.593 12.688 -23.356 1.00127.00 N ANISOU 307 NZ LYS A 65 15424 16779 16052 -245 -2597 315 N ATOM 308 N GLU A 66 -23.458 7.562 -23.658 1.00123.45 N ANISOU 308 N GLU A 66 13927 16169 16809 0 -3138 566 N ATOM 309 CA GLU A 66 -24.517 6.656 -23.230 1.00126.24 C ANISOU 309 CA GLU A 66 14111 16350 17505 15 -3066 695 C ATOM 310 C GLU A 66 -24.247 5.238 -23.723 1.00126.36 C ANISOU 310 C GLU A 66 13870 16303 17839 85 -3397 701 C ATOM 311 O GLU A 66 -23.602 5.031 -24.754 1.00125.02 O ANISOU 311 O GLU A 66 13608 16205 17690 225 -3664 554 O ATOM 312 CB GLU A 66 -25.881 7.139 -23.731 1.00127.63 C ANISOU 312 CB GLU A 66 14156 16413 17926 146 -2884 631 C ATOM 313 CG GLU A 66 -27.066 6.469 -23.045 1.00130.57 C ANISOU 313 CG GLU A 66 14358 16609 18645 119 -2704 836 C ATOM 314 CD GLU A 66 -28.394 6.830 -23.678 1.00131.97 C ANISOU 314 CD GLU A 66 14313 16680 19149 263 -2588 776 C ATOM 315 OE1 GLU A 66 -29.424 6.259 -23.262 1.00134.52 O ANISOU 315 OE1 GLU A 66 14408 16852 19852 246 -2456 962 O ATOM 316 OE2 GLU A 66 -28.408 7.682 -24.592 1.00130.64 O ANISOU 316 OE2 GLU A 66 14186 16577 18876 398 -2627 560 O ATOM 317 N ILE A 67 -24.736 4.265 -22.966 1.00130.08 N ANISOU 317 N ILE A 67 14252 16629 18542 10 -3365 890 N ATOM 318 CA ILE A 67 -24.590 2.866 -23.323 1.00133.29 C ANISOU 318 CA ILE A 67 14448 16922 19272 64 -3681 914 C ATOM 319 C ILE A 67 -25.976 2.329 -23.678 1.00139.26 C ANISOU 319 C ILE A 67 14918 17431 20564 121 -3687 945 C ATOM 320 O ILE A 67 -26.794 2.074 -22.797 1.00143.24 O ANISOU 320 O ILE A 67 15363 17803 21256 9 -3443 1169 O ATOM 321 CB ILE A 67 -23.954 2.063 -22.173 1.00133.20 C ANISOU 321 CB ILE A 67 14562 16914 19133 -79 -3685 1127 C ATOM 322 CG1 ILE A 67 -23.063 2.971 -21.317 1.00131.40 C ANISOU 322 CG1 ILE A 67 14663 16887 18377 -202 -3527 1163 C ATOM 323 CG2 ILE A 67 -23.165 0.907 -22.712 1.00133.72 C ANISOU 323 CG2 ILE A 67 14523 16970 19315 11 -4076 1082 C ATOM 324 CD1 ILE A 67 -22.197 2.232 -20.309 1.00131.65 C ANISOU 324 CD1 ILE A 67 14849 16957 18216 -302 -3612 1326 C ATOM 325 N LYS A 68 -26.230 2.172 -24.975 1.00126.77 N ANISOU 325 N LYS A 68 15640 14889 17639 -3719 -115 2221 N ATOM 326 CA LYS A 68 -27.579 1.936 -25.490 1.00127.89 C ANISOU 326 CA LYS A 68 16098 15197 17298 -3339 -140 2055 C ATOM 327 C LYS A 68 -28.020 0.475 -25.481 1.00126.21 C ANISOU 327 C LYS A 68 15660 15449 16845 -3086 87 1754 C ATOM 328 O LYS A 68 -27.650 -0.293 -26.367 1.00124.96 O ANISOU 328 O LYS A 68 15332 15597 16550 -3128 518 1871 O ATOM 329 CB LYS A 68 -27.683 2.480 -26.917 1.00131.71 C ANISOU 329 CB LYS A 68 16871 15664 17510 -3387 97 2407 C ATOM 330 CG LYS A 68 -27.512 3.987 -27.022 1.00136.38 C ANISOU 330 CG LYS A 68 17803 15761 18255 -3578 -140 2699 C ATOM 331 CD LYS A 68 -28.696 4.715 -26.404 1.00136.07 C ANISOU 331 CD LYS A 68 18155 15466 18078 -3282 -620 2471 C ATOM 332 CE LYS A 68 -29.316 5.700 -27.383 1.00140.06 C ANISOU 332 CE LYS A 68 19158 15772 18285 -3178 -657 2731 C ATOM 333 NZ LYS A 68 -30.639 6.189 -26.906 1.00138.60 N ANISOU 333 NZ LYS A 68 19342 15460 17862 -2794 -1082 2459 N ATOM 334 N CYS A 69 -28.828 0.101 -24.494 1.00126.53 N ANISOU 334 N CYS A 69 15711 15539 16826 -2827 -198 1364 N ATOM 335 CA CYS A 69 -29.383 -1.246 -24.442 1.00124.50 C ANISOU 335 CA CYS A 69 15295 15691 16318 -2579 -5 1053 C ATOM 336 C CYS A 69 -30.522 -1.357 -23.434 1.00122.73 C ANISOU 336 C CYS A 69 15203 15470 15957 -2280 -388 637 C ATOM 337 O CYS A 69 -30.435 -0.831 -22.324 1.00123.16 O ANISOU 337 O CYS A 69 15239 15273 16284 -2314 -764 529 O ATOM 338 CB CYS A 69 -28.293 -2.261 -24.099 1.00123.53 C ANISOU 338 CB CYS A 69 14705 15755 16477 -2738 278 1053 C ATOM 339 SG CYS A 69 -28.793 -3.978 -24.327 1.00182.42 S ANISOU 339 SG CYS A 69 21983 23701 23627 -2483 640 750 S ATOM 340 N ASN A 70 -31.594 -2.035 -23.834 1.00120.17 N ANISOU 340 N ASN A 70 15005 15453 15202 -1996 -288 394 N ATOM 341 CA ASN A 70 -32.663 -2.396 -22.913 1.00117.80 C ANISOU 341 CA ASN A 70 14772 15250 14738 -1718 -577 -34 C ATOM 342 C ASN A 70 -32.506 -3.852 -22.479 1.00114.64 C ANISOU 342 C ASN A 70 14044 15160 14354 -1668 -327 -277 C ATOM 343 O ASN A 70 -33.344 -4.397 -21.756 1.00112.62 O ANISOU 343 O ASN A 70 13800 15046 13945 -1455 -483 -643 O ATOM 344 CB ASN A 70 -34.044 -2.163 -23.548 1.00118.48 C ANISOU 344 CB ASN A 70 15218 15484 14314 -1428 -664 -188 C ATOM 345 CG ASN A 70 -34.004 -2.150 -25.070 1.00121.83 C ANISOU 345 CG ASN A 70 15760 16072 14458 -1455 -291 78 C ATOM 346 OD1 ASN A 70 -32.961 -2.379 -25.681 1.00124.21 O ANISOU 346 OD1 ASN A 70 15869 16391 14934 -1694 52 369 O ATOM 347 ND2 ASN A 70 -35.151 -1.884 -25.688 1.00121.09 N ANISOU 347 ND2 ASN A 70 15974 16125 13911 -1200 -361 -28 N ATOM 348 N GLY A 71 -31.416 -4.473 -22.922 1.00113.82 N ANISOU 348 N GLY A 71 13654 15158 14437 -1866 66 -66 N ATOM 349 CA GLY A 71 -31.161 -5.873 -22.643 1.00106.18 C ANISOU 349 CA GLY A 71 12389 14467 13489 -1819 357 -250 C ATOM 350 C GLY A 71 -30.885 -6.160 -21.183 1.00 99.51 C ANISOU 350 C GLY A 71 11329 13529 12951 -1807 107 -445 C ATOM 351 O GLY A 71 -29.962 -5.600 -20.589 1.00101.26 O ANISOU 351 O GLY A 71 11389 13521 13565 -1999 -53 -277 O ATOM 352 N THR A 72 -31.698 -7.036 -20.602 1.00 89.61 N ANISOU 352 N THR A 72 10073 12469 11505 -1586 77 -807 N ATOM 353 CA THR A 72 -31.486 -7.497 -19.238 1.00 81.79 C ANISOU 353 CA THR A 72 8870 11447 10761 -1545 -113 -1007 C ATOM 354 C THR A 72 -30.677 -8.791 -19.247 1.00 78.43 C ANISOU 354 C THR A 72 8119 11220 10459 -1580 302 -989 C ATOM 355 O THR A 72 -30.650 -9.529 -18.260 1.00 76.02 O ANISOU 355 O THR A 72 7650 10976 10258 -1486 252 -1192 O ATOM 356 CB THR A 72 -32.815 -7.729 -18.505 1.00 77.39 C ANISOU 356 CB THR A 72 8491 10983 9932 -1290 -389 -1414 C ATOM 357 OG1 THR A 72 -33.524 -8.809 -19.128 1.00 75.46 O ANISOU 357 OG1 THR A 72 8302 11055 9314 -1144 -53 -1613 O ATOM 358 CG2 THR A 72 -33.668 -6.473 -18.548 1.00 77.95 C ANISOU 358 CG2 THR A 72 8893 10880 9846 -1215 -792 -1448 C ATOM 359 N ASP A 73 -30.029 -9.067 -20.376 1.00 78.54 N ANISOU 359 N ASP A 73 8051 11341 10451 -1702 714 -743 N ATOM 360 CA ASP A 73 -29.179 -10.240 -20.492 1.00 78.26 C ANISOU 360 CA ASP A 73 7710 11487 10540 -1733 1127 -699 C ATOM 361 C ASP A 73 -27.984 -10.131 -19.540 1.00 79.68 C ANISOU 361 C ASP A 73 7566 11531 11179 -1866 1007 -566 C ATOM 362 O ASP A 73 -27.331 -9.086 -19.457 1.00 65.24 O ANISOU 362 O ASP A 73 5692 9493 9603 -2065 810 -334 O ATOM 363 CB ASP A 73 -28.701 -10.423 -21.930 1.00 63.94 C ANISOU 363 CB ASP A 73 5868 9817 8608 -1847 1570 -451 C ATOM 364 CG ASP A 73 -27.662 -11.516 -22.053 1.00 77.31 C ANISOU 364 CG ASP A 73 7224 11675 10475 -1891 1983 -370 C ATOM 365 OD1 ASP A 73 -28.052 -12.698 -22.144 1.00 75.45 O ANISOU 365 OD1 ASP A 73 6969 11647 10052 -1730 2254 -590 O ATOM 366 OD2 ASP A 73 -26.454 -11.198 -22.042 1.00 79.70 O ANISOU 366 OD2 ASP A 73 7280 11902 11102 -2086 2038 -97 O ATOM 367 N ALA A 74 -27.707 -11.221 -18.831 1.00 50.97 N ANISOU 367 N ALA A 74 4921 7329 7117 -1669 -1790 -394 N ATOM 368 CA ALA A 74 -26.705 -11.232 -17.771 1.00 59.20 C ANISOU 368 CA ALA A 74 6267 8247 7980 -1948 -1870 -313 C ATOM 369 C ALA A 74 -25.294 -10.926 -18.272 1.00 56.15 C ANISOU 369 C ALA A 74 5965 7661 7706 -1608 -2036 -288 C ATOM 370 O ALA A 74 -24.477 -10.393 -17.528 1.00 55.22 O ANISOU 370 O ALA A 74 6021 7464 7496 -1705 -1969 -273 O ATOM 371 CB ALA A 74 -26.723 -12.569 -17.055 1.00 53.33 C ANISOU 371 CB ALA A 74 5791 7405 7068 -2442 -2256 -134 C ATOM 372 N LYS A 75 -25.007 -11.261 -19.526 1.00 53.30 N ANISOU 372 N LYS A 75 5461 7269 7520 -1260 -2230 -328 N ATOM 373 CA LYS A 75 -23.690 -10.979 -20.083 1.00 50.78 C ANISOU 373 CA LYS A 75 5154 6866 7275 -1004 -2344 -407 C ATOM 374 C LYS A 75 -23.589 -9.518 -20.532 1.00 48.07 C ANISOU 374 C LYS A 75 4700 6658 6906 -783 -2011 -424 C ATOM 375 O LYS A 75 -22.539 -8.896 -20.397 1.00 46.45 O ANISOU 375 O LYS A 75 4587 6402 6659 -716 -1971 -451 O ATOM 376 CB LYS A 75 -23.371 -11.934 -21.243 1.00 50.10 C ANISOU 376 CB LYS A 75 4903 6779 7354 -817 -2668 -551 C ATOM 377 CG LYS A 75 -22.787 -13.276 -20.785 1.00 51.20 C ANISOU 377 CG LYS A 75 5198 6632 7622 -937 -3070 -587 C ATOM 378 CD LYS A 75 -22.310 -14.128 -21.955 1.00 52.20 C ANISOU 378 CD LYS A 75 5184 6779 7871 -671 -3093 -812 C ATOM 379 CE LYS A 75 -23.475 -14.666 -22.784 1.00 54.36 C ANISOU 379 CE LYS A 75 5290 7225 8141 -633 -3061 -795 C ATOM 380 NZ LYS A 75 -24.229 -15.722 -22.057 1.00 57.44 N ANISOU 380 NZ LYS A 75 5844 7410 8572 -839 -3265 -626 N ATOM 381 N VAL A 76 -24.679 -8.973 -21.065 1.00 48.78 N ANISOU 381 N VAL A 76 4591 6881 7060 -684 -1835 -400 N ATOM 382 CA VAL A 76 -24.729 -7.551 -21.385 1.00 48.69 C ANISOU 382 CA VAL A 76 4484 6900 7117 -522 -1644 -374 C ATOM 383 C VAL A 76 -24.599 -6.740 -20.091 1.00 48.85 C ANISOU 383 C VAL A 76 4601 6836 7125 -644 -1399 -426 C ATOM 384 O VAL A 76 -23.913 -5.722 -20.044 1.00 48.34 O ANISOU 384 O VAL A 76 4581 6711 7075 -544 -1320 -408 O ATOM 385 CB VAL A 76 -26.041 -7.167 -22.125 1.00 51.51 C ANISOU 385 CB VAL A 76 4584 7320 7669 -408 -1622 -351 C ATOM 386 CG1 VAL A 76 -26.140 -5.657 -22.295 1.00 51.51 C ANISOU 386 CG1 VAL A 76 4486 7227 7859 -270 -1558 -313 C ATOM 387 CG2 VAL A 76 -26.123 -7.857 -23.484 1.00 50.80 C ANISOU 387 CG2 VAL A 76 4401 7359 7540 -329 -1853 -290 C ATOM 388 N LYS A 77 -25.248 -7.224 -19.039 1.00 49.53 N ANISOU 388 N LYS A 77 4719 6956 7146 -924 -1282 -503 N ATOM 389 CA LYS A 77 -25.230 -6.570 -17.743 1.00 50.59 C ANISOU 389 CA LYS A 77 4910 7107 7207 -1158 -1011 -625 C ATOM 390 C LYS A 77 -23.814 -6.473 -17.168 1.00 48.54 C ANISOU 390 C LYS A 77 4946 6720 6776 -1227 -1079 -531 C ATOM 391 O LYS A 77 -23.424 -5.436 -16.627 1.00 47.67 O ANISOU 391 O LYS A 77 4848 6585 6679 -1210 -870 -605 O ATOM 392 CB LYS A 77 -26.150 -7.323 -16.786 1.00 56.26 C ANISOU 392 CB LYS A 77 5629 7991 7758 -1611 -905 -725 C ATOM 393 CG LYS A 77 -26.379 -6.656 -15.447 1.00 62.60 C ANISOU 393 CG LYS A 77 6402 8950 8431 -1980 -550 -962 C ATOM 394 CD LYS A 77 -27.522 -7.348 -14.714 1.00 69.06 C ANISOU 394 CD LYS A 77 7134 10062 9045 -2510 -404 -1129 C ATOM 395 CE LYS A 77 -27.761 -6.759 -13.330 1.00 74.51 C ANISOU 395 CE LYS A 77 7758 11036 9515 -3027 -6 -1457 C ATOM 396 NZ LYS A 77 -26.584 -6.955 -12.441 1.00 75.60 N ANISOU 396 NZ LYS A 77 8332 11097 9297 -3378 -129 -1212 N ATOM 397 N LEU A 78 -23.036 -7.544 -17.292 1.00 47.77 N ANISOU 397 N LEU A 78 5054 6512 6585 -1290 -1408 -406 N ATOM 398 CA LEU A 78 -21.669 -7.533 -16.772 1.00 46.86 C ANISOU 398 CA LEU A 78 5189 6231 6386 -1341 -1545 -356 C ATOM 399 C LEU A 78 -20.773 -6.595 -17.573 1.00 44.07 C ANISOU 399 C LEU A 78 4767 5864 6113 -986 -1483 -396 C ATOM 400 O LEU A 78 -19.905 -5.924 -17.017 1.00 45.07 O ANISOU 400 O LEU A 78 5030 5916 6178 -997 -1393 -397 O ATOM 401 CB LEU A 78 -21.087 -8.943 -16.767 1.00 47.29 C ANISOU 401 CB LEU A 78 5404 6092 6471 -1466 -2026 -289 C ATOM 402 CG LEU A 78 -21.738 -9.860 -15.733 1.00 50.50 C ANISOU 402 CG LEU A 78 6001 6462 6723 -1980 -2198 -150 C ATOM 403 CD1 LEU A 78 -21.472 -11.330 -16.051 1.00 50.73 C ANISOU 403 CD1 LEU A 78 6106 6241 6928 -2034 -2794 -81 C ATOM 404 CD2 LEU A 78 -21.248 -9.500 -14.340 1.00 49.23 C ANISOU 404 CD2 LEU A 78 6123 6255 6327 -2398 -2135 -59 C ATOM 405 N ILE A 79 -20.988 -6.552 -18.879 1.00 44.37 N ANISOU 405 N ILE A 79 4606 6005 6245 -736 -1544 -414 N ATOM 406 CA ILE A 79 -20.249 -5.640 -19.738 1.00 44.15 C ANISOU 406 CA ILE A 79 4522 6045 6208 -534 -1508 -418 C ATOM 407 C ILE A 79 -20.584 -4.198 -19.365 1.00 44.39 C ANISOU 407 C ILE A 79 4524 6040 6303 -485 -1261 -358 C ATOM 408 O ILE A 79 -19.694 -3.350 -19.274 1.00 44.36 O ANISOU 408 O ILE A 79 4611 5995 6248 -439 -1206 -334 O ATOM 409 CB ILE A 79 -20.562 -5.891 -21.230 1.00 45.66 C ANISOU 409 CB ILE A 79 4513 6422 6413 -420 -1643 -424 C ATOM 410 CG1 ILE A 79 -19.931 -7.208 -21.685 1.00 45.28 C ANISOU 410 CG1 ILE A 79 4423 6417 6363 -435 -1899 -615 C ATOM 411 CG2 ILE A 79 -20.058 -4.746 -22.092 1.00 45.49 C ANISOU 411 CG2 ILE A 79 4457 6524 6303 -366 -1613 -347 C ATOM 412 CD1 ILE A 79 -18.426 -7.217 -21.606 1.00 45.30 C ANISOU 412 CD1 ILE A 79 4487 6398 6327 -431 -1981 -809 C ATOM 413 N LYS A 80 -21.865 -3.930 -19.125 1.00 45.04 N ANISOU 413 N LYS A 80 4442 6124 6546 -497 -1136 -387 N ATOM 414 CA LYS A 80 -22.305 -2.584 -18.762 1.00 48.60 C ANISOU 414 CA LYS A 80 4763 6489 7214 -421 -964 -448 C ATOM 415 C LYS A 80 -21.757 -2.161 -17.398 1.00 47.24 C ANISOU 415 C LYS A 80 4729 6267 6954 -577 -733 -566 C ATOM 416 O LYS A 80 -21.405 -0.998 -17.208 1.00 45.90 O ANISOU 416 O LYS A 80 4535 5994 6912 -476 -652 -594 O ATOM 417 CB LYS A 80 -23.834 -2.486 -18.777 1.00 53.03 C ANISOU 417 CB LYS A 80 5022 7065 8060 -399 -900 -596 C ATOM 418 CG LYS A 80 -24.420 -2.367 -20.178 1.00 58.68 C ANISOU 418 CG LYS A 80 5575 7759 8964 -211 -1164 -447 C ATOM 419 CD LYS A 80 -25.958 -2.363 -20.181 1.00 65.74 C ANISOU 419 CD LYS A 80 6139 8638 10203 -172 -1138 -637 C ATOM 420 CE LYS A 80 -26.548 -0.949 -20.146 1.00 72.10 C ANISOU 420 CE LYS A 80 6658 9201 11536 4 -1203 -792 C ATOM 421 NZ LYS A 80 -26.810 -0.442 -18.764 1.00 75.67 N ANISOU 421 NZ LYS A 80 6934 9662 12154 -93 -860 -1221 N ATOM 422 N GLN A 81 -21.675 -3.099 -16.458 1.00 47.12 N ANISOU 422 N GLN A 81 4873 6314 6715 -869 -678 -608 N ATOM 423 CA GLN A 81 -21.083 -2.807 -15.155 1.00 48.04 C ANISOU 423 CA GLN A 81 5171 6417 6667 -1120 -500 -678 C ATOM 424 C GLN A 81 -19.595 -2.502 -15.291 1.00 46.97 C ANISOU 424 C GLN A 81 5263 6145 6441 -988 -619 -545 C ATOM 425 O GLN A 81 -19.077 -1.592 -14.647 1.00 47.51 O ANISOU 425 O GLN A 81 5391 6163 6499 -1003 -448 -598 O ATOM 426 CB GLN A 81 -21.303 -3.965 -14.183 1.00 49.25 C ANISOU 426 CB GLN A 81 5506 6659 6549 -1586 -538 -662 C ATOM 427 CG GLN A 81 -22.747 -4.088 -13.726 1.00 54.15 C ANISOU 427 CG GLN A 81 5890 7512 7174 -1861 -306 -884 C ATOM 428 CD GLN A 81 -23.009 -5.342 -12.921 1.00 58.69 C ANISOU 428 CD GLN A 81 6685 8206 7408 -2428 -430 -786 C ATOM 429 OE1 GLN A 81 -24.076 -5.496 -12.327 1.00 63.14 O ANISOU 429 OE1 GLN A 81 7096 9045 7849 -2822 -205 -992 O ATOM 430 NE2 GLN A 81 -22.039 -6.248 -12.898 1.00 58.61 N ANISOU 430 NE2 GLN A 81 7015 7983 7270 -2515 -836 -496 N ATOM 431 N GLU A 82 -18.909 -3.255 -16.140 1.00 46.25 N ANISOU 431 N GLU A 82 5253 6017 6304 -868 -901 -438 N ATOM 432 CA GLU A 82 -17.491 -3.014 -16.362 1.00 45.37 C ANISOU 432 CA GLU A 82 5284 5829 6125 -759 -1006 -413 C ATOM 433 C GLU A 82 -17.267 -1.658 -17.036 1.00 45.48 C ANISOU 433 C GLU A 82 5201 5876 6203 -551 -894 -376 C ATOM 434 O GLU A 82 -16.312 -0.949 -16.717 1.00 45.89 O ANISOU 434 O GLU A 82 5376 5869 6191 -532 -829 -369 O ATOM 435 CB GLU A 82 -16.879 -4.139 -17.200 1.00 44.95 C ANISOU 435 CB GLU A 82 5218 5783 6076 -695 -1327 -464 C ATOM 436 CG GLU A 82 -15.365 -4.234 -17.091 1.00 45.06 C ANISOU 436 CG GLU A 82 5354 5702 6064 -669 -1473 -570 C ATOM 437 CD GLU A 82 -14.886 -4.374 -15.654 1.00 48.09 C ANISOU 437 CD GLU A 82 6001 5864 6407 -888 -1518 -511 C ATOM 438 OE1 GLU A 82 -15.573 -5.049 -14.854 1.00 52.34 O ANISOU 438 OE1 GLU A 82 6649 6325 6914 -1153 -1604 -412 O ATOM 439 OE2 GLU A 82 -13.824 -3.802 -15.321 1.00 46.72 O ANISOU 439 OE2 GLU A 82 5938 5617 6195 -856 -1480 -549 O ATOM 440 N LEU A 83 -18.155 -1.296 -17.958 1.00 46.19 N ANISOU 440 N LEU A 83 5087 6032 6430 -430 -928 -322 N ATOM 441 CA LEU A 83 -18.073 -0.010 -18.645 1.00 47.63 C ANISOU 441 CA LEU A 83 5201 6183 6712 -310 -965 -207 C ATOM 442 C LEU A 83 -18.331 1.164 -17.709 1.00 48.77 C ANISOU 442 C LEU A 83 5303 6150 7077 -273 -790 -276 C ATOM 443 O LEU A 83 -17.738 2.228 -17.875 1.00 48.92 O ANISOU 443 O LEU A 83 5372 6073 7141 -214 -839 -182 O ATOM 444 CB LEU A 83 -19.057 0.039 -19.814 1.00 51.01 C ANISOU 444 CB LEU A 83 5435 6665 7283 -246 -1155 -96 C ATOM 445 CG LEU A 83 -18.601 -0.721 -21.059 1.00 53.39 C ANISOU 445 CG LEU A 83 5743 7208 7334 -317 -1342 -39 C ATOM 446 CD1 LEU A 83 -19.736 -0.854 -22.073 1.00 55.11 C ANISOU 446 CD1 LEU A 83 5781 7486 7672 -306 -1525 77 C ATOM 447 CD2 LEU A 83 -17.396 -0.025 -21.671 1.00 53.41 C ANISOU 447 CD2 LEU A 83 5859 7336 7097 -422 -1415 45 C ATOM 448 N ASP A 84 -19.220 0.980 -16.737 1.00 50.35 N ANISOU 448 N ASP A 84 5383 6336 7410 -351 -589 -480 N ATOM 449 CA ASP A 84 -19.448 2.009 -15.727 1.00 53.16 C ANISOU 449 CA ASP A 84 5626 6589 7982 -364 -368 -696 C ATOM 450 C ASP A 84 -18.200 2.211 -14.872 1.00 50.51 C ANISOU 450 C ASP A 84 5561 6239 7392 -478 -233 -679 C ATOM 451 O ASP A 84 -17.845 3.344 -14.552 1.00 49.70 O ANISOU 451 O ASP A 84 5430 6008 7444 -395 -165 -734 O ATOM 452 CB ASP A 84 -20.639 1.658 -14.836 1.00 58.63 C ANISOU 452 CB ASP A 84 6090 7404 8782 -550 -122 -1027 C ATOM 453 CG ASP A 84 -21.970 1.885 -15.525 1.00 66.28 C ANISOU 453 CG ASP A 84 6687 8322 10172 -382 -232 -1161 C ATOM 454 OD1 ASP A 84 -22.014 2.654 -16.514 1.00 69.82 O ANISOU 454 OD1 ASP A 84 7044 8560 10926 -123 -526 -998 O ATOM 455 OD2 ASP A 84 -22.975 1.303 -15.067 1.00 68.52 O ANISOU 455 OD2 ASP A 84 6777 8778 10480 -558 -61 -1423 O ATOM 456 N LYS A 85 -17.542 1.113 -14.500 1.00 48.89 N ANISOU 456 N LYS A 85 5606 6119 6852 -666 -253 -605 N ATOM 457 CA LYS A 85 -16.288 1.200 -13.752 1.00 47.67 C ANISOU 457 CA LYS A 85 5722 5909 6483 -775 -208 -567 C ATOM 458 C LYS A 85 -15.255 1.966 -14.566 1.00 46.64 C ANISOU 458 C LYS A 85 5656 5706 6357 -554 -327 -436 C ATOM 459 O LYS A 85 -14.533 2.805 -14.035 1.00 45.61 O ANISOU 459 O LYS A 85 5626 5495 6209 -547 -220 -447 O ATOM 460 CB LYS A 85 -15.750 -0.184 -13.401 1.00 47.25 C ANISOU 460 CB LYS A 85 5903 5859 6192 -993 -389 -494 C ATOM 461 CG LYS A 85 -16.545 -0.925 -12.347 1.00 51.48 C ANISOU 461 CG LYS A 85 6485 6479 6596 -1390 -313 -553 C ATOM 462 CD LYS A 85 -15.917 -2.280 -12.056 1.00 54.99 C ANISOU 462 CD LYS A 85 7200 6809 6883 -1624 -671 -404 C ATOM 463 CE LYS A 85 -16.741 -3.057 -11.040 1.00 62.23 C ANISOU 463 CE LYS A 85 8218 7833 7593 -2157 -676 -379 C ATOM 464 NZ LYS A 85 -15.974 -4.185 -10.435 1.00 65.58 N ANISOU 464 NZ LYS A 85 8987 8041 7888 -2497 -1134 -170 N ATOM 465 N TYR A 86 -15.207 1.669 -15.864 1.00 46.03 N ANISOU 465 N TYR A 86 5518 5705 6266 -437 -542 -326 N ATOM 466 CA TYR A 86 -14.324 2.352 -16.804 1.00 43.77 C ANISOU 466 CA TYR A 86 5276 5463 5892 -362 -668 -205 C ATOM 467 C TYR A 86 -14.603 3.856 -16.844 1.00 45.66 C ANISOU 467 C TYR A 86 5447 5551 6352 -279 -668 -105 C ATOM 468 O TYR A 86 -13.677 4.672 -16.797 1.00 44.48 O ANISOU 468 O TYR A 86 5423 5355 6120 -288 -671 -32 O ATOM 469 CB TYR A 86 -14.479 1.742 -18.204 1.00 41.79 C ANISOU 469 CB TYR A 86 4921 5412 5544 -372 -880 -147 C ATOM 470 CG TYR A 86 -13.854 2.547 -19.323 1.00 42.77 C ANISOU 470 CG TYR A 86 5062 5682 5508 -449 -1025 2 C ATOM 471 CD1 TYR A 86 -12.525 2.357 -19.680 1.00 42.95 C ANISOU 471 CD1 TYR A 86 5162 5915 5242 -569 -1027 -116 C ATOM 472 CD2 TYR A 86 -14.598 3.488 -20.034 1.00 44.38 C ANISOU 472 CD2 TYR A 86 5190 5816 5856 -465 -1211 244 C ATOM 473 CE1 TYR A 86 -11.946 3.096 -20.703 1.00 45.12 C ANISOU 473 CE1 TYR A 86 5458 6420 5266 -777 -1140 6 C ATOM 474 CE2 TYR A 86 -14.032 4.226 -21.058 1.00 46.01 C ANISOU 474 CE2 TYR A 86 5467 6172 5842 -676 -1421 458 C ATOM 475 CZ TYR A 86 -12.706 4.027 -21.390 1.00 47.87 C ANISOU 475 CZ TYR A 86 5798 6711 5680 -869 -1351 340 C ATOM 476 OH TYR A 86 -12.139 4.761 -22.412 1.00 50.88 O ANISOU 476 OH TYR A 86 6254 7336 5742 -1210 -1541 539 O ATOM 477 N LYS A 87 -15.882 4.214 -16.940 1.00 48.32 N ANISOU 477 N LYS A 87 5560 5777 7023 -196 -714 -128 N ATOM 478 CA LYS A 87 -16.285 5.616 -17.034 1.00 52.10 C ANISOU 478 CA LYS A 87 5902 6008 7888 -85 -853 -80 C ATOM 479 C LYS A 87 -16.023 6.378 -15.735 1.00 51.01 C ANISOU 479 C LYS A 87 5750 5723 7907 -57 -603 -306 C ATOM 480 O LYS A 87 -15.605 7.536 -15.757 1.00 52.47 O ANISOU 480 O LYS A 87 5953 5711 8274 8 -729 -228 O ATOM 481 CB LYS A 87 -17.766 5.726 -17.415 1.00 56.72 C ANISOU 481 CB LYS A 87 6174 6464 8913 21 -1016 -152 C ATOM 482 CG LYS A 87 -18.076 5.257 -18.827 1.00 60.52 C ANISOU 482 CG LYS A 87 6662 7052 9283 -27 -1336 123 C ATOM 483 CD LYS A 87 -19.135 6.133 -19.492 1.00 67.98 C ANISOU 483 CD LYS A 87 7368 7696 10767 74 -1746 227 C ATOM 484 CE LYS A 87 -20.424 5.367 -19.756 1.00 71.53 C ANISOU 484 CE LYS A 87 7570 8186 11422 140 -1765 92 C ATOM 485 NZ LYS A 87 -21.131 4.990 -18.498 1.00 73.67 N ANISOU 485 NZ LYS A 87 7611 8489 11892 212 -1359 -382 N ATOM 486 N ASN A 88 -16.277 5.727 -14.607 1.00 49.58 N ANISOU 486 N ASN A 88 5546 5657 7635 -166 -276 -578 N ATOM 487 CA ASN A 88 -16.009 6.334 -13.315 1.00 50.08 C ANISOU 487 CA ASN A 88 5600 5677 7751 -241 7 -831 C ATOM 488 C ASN A 88 -14.515 6.538 -13.111 1.00 47.26 C ANISOU 488 C ASN A 88 5575 5309 7073 -282 24 -648 C ATOM 489 O ASN A 88 -14.099 7.521 -12.504 1.00 47.57 O ANISOU 489 O ASN A 88 5614 5224 7237 -252 123 -741 O ATOM 490 CB ASN A 88 -16.588 5.481 -12.189 1.00 51.45 C ANISOU 490 CB ASN A 88 5724 6066 7759 -518 325 -1118 C ATOM 491 CG ASN A 88 -18.101 5.522 -12.151 1.00 57.25 C ANISOU 491 CG ASN A 88 6043 6848 8862 -512 399 -1454 C ATOM 492 OD1 ASN A 88 -18.737 6.143 -13.003 1.00 59.45 O ANISOU 492 OD1 ASN A 88 6067 6930 9592 -245 154 -1455 O ATOM 493 ND2 ASN A 88 -18.688 4.851 -11.165 1.00 59.32 N ANISOU 493 ND2 ASN A 88 6232 7376 8930 -861 698 -1742 N ATOM 494 N ALA A 89 -13.715 5.606 -13.624 1.00 44.76 N ANISOU 494 N ALA A 89 5496 5120 6392 -344 -84 -448 N ATOM 495 CA ALA A 89 -12.262 5.730 -13.565 1.00 43.83 C ANISOU 495 CA ALA A 89 5639 5007 6008 -374 -100 -339 C ATOM 496 C ALA A 89 -11.807 6.971 -14.325 1.00 44.03 C ANISOU 496 C ALA A 89 5665 4936 6127 -267 -262 -167 C ATOM 497 O ALA A 89 -11.006 7.761 -13.824 1.00 44.23 O ANISOU 497 O ALA A 89 5808 4871 6126 -266 -186 -162 O ATOM 498 CB ALA A 89 -11.591 4.485 -14.129 1.00 41.71 C ANISOU 498 CB ALA A 89 5497 4884 5465 -436 -245 -291 C ATOM 499 N VAL A 90 -12.333 7.138 -15.535 1.00 44.44 N ANISOU 499 N VAL A 90 5606 5006 6272 -232 -528 5 N ATOM 500 CA VAL A 90 -12.000 8.295 -16.356 1.00 45.51 C ANISOU 500 CA VAL A 90 5780 5045 6469 -254 -805 258 C ATOM 501 C VAL A 90 -12.410 9.597 -15.660 1.00 47.72 C ANISOU 501 C VAL A 90 5935 4973 7222 -117 -840 192 C ATOM 502 O VAL A 90 -11.627 10.540 -15.598 1.00 46.83 O ANISOU 502 O VAL A 90 5951 4744 7099 -146 -927 315 O ATOM 503 CB VAL A 90 -12.662 8.199 -17.754 1.00 46.10 C ANISOU 503 CB VAL A 90 5767 5192 6558 -337 -1159 495 C ATOM 504 CG1 VAL A 90 -12.699 9.560 -18.444 1.00 47.37 C ANISOU 504 CG1 VAL A 90 5953 5123 6922 -423 -1584 816 C ATOM 505 CG2 VAL A 90 -11.931 7.177 -18.614 1.00 41.81 C ANISOU 505 CG2 VAL A 90 5325 5053 5507 -535 -1147 513 C ATOM 506 N THR A 91 -13.627 9.635 -15.121 1.00 50.59 N ANISOU 506 N THR A 91 6011 5184 8025 17 -771 -68 N ATOM 507 CA THR A 91 -14.112 10.810 -14.394 1.00 53.08 C ANISOU 507 CA THR A 91 6082 5177 8909 164 -790 -315 C ATOM 508 C THR A 91 -13.233 11.122 -13.183 1.00 50.83 C ANISOU 508 C THR A 91 5923 4929 8462 120 -432 -509 C ATOM 509 O THR A 91 -12.934 12.278 -12.895 1.00 51.73 O ANISOU 509 O THR A 91 5990 4790 8875 203 -534 -548 O ATOM 510 CB THR A 91 -15.564 10.612 -13.925 1.00 54.79 C ANISOU 510 CB THR A 91 5883 5341 9595 262 -678 -740 C ATOM 511 OG1 THR A 91 -16.400 10.364 -15.060 1.00 57.31 O ANISOU 511 OG1 THR A 91 6082 5587 10108 318 -1049 -548 O ATOM 512 CG2 THR A 91 -16.065 11.843 -13.195 1.00 56.53 C ANISOU 512 CG2 THR A 91 5736 5240 10501 419 -707 -1156 C ATOM 513 N GLU A 92 -12.822 10.073 -12.485 1.00 48.90 N ANISOU 513 N GLU A 92 5847 4968 7765 -34 -72 -611 N ATOM 514 CA GLU A 92 -11.963 10.187 -11.313 1.00 50.02 C ANISOU 514 CA GLU A 92 6156 5171 7678 -148 241 -752 C ATOM 515 C GLU A 92 -10.624 10.832 -11.665 1.00 47.25 C ANISOU 515 C GLU A 92 6077 4740 7134 -121 104 -474 C ATOM 516 O GLU A 92 -10.181 11.771 -11.008 1.00 45.85 O ANISOU 516 O GLU A 92 5908 4420 7093 -90 190 -569 O ATOM 517 CB GLU A 92 -11.741 8.801 -10.710 1.00 51.93 C ANISOU 517 CB GLU A 92 6587 5672 7472 -381 461 -789 C ATOM 518 CG GLU A 92 -11.541 8.757 -9.214 1.00 55.56 C ANISOU 518 CG GLU A 92 7109 6226 7775 -631 801 -1042 C ATOM 519 CD GLU A 92 -11.693 7.341 -8.672 1.00 59.06 C ANISOU 519 CD GLU A 92 7710 6876 7855 -954 874 -1036 C ATOM 520 OE1 GLU A 92 -12.739 6.696 -8.937 1.00 59.05 O ANISOU 520 OE1 GLU A 92 7537 6983 7918 -1011 857 -1112 O ATOM 521 OE2 GLU A 92 -10.762 6.869 -7.988 1.00 60.42 O ANISOU 521 OE2 GLU A 92 8186 7069 7702 -1170 888 -934 O ATOM 522 N LEU A 93 -9.988 10.318 -12.713 1.00 45.28 N ANISOU 522 N LEU A 93 6019 4625 6560 -169 -94 -181 N ATOM 523 CA LEU A 93 -8.704 10.840 -13.168 1.00 43.53 C ANISOU 523 CA LEU A 93 6028 4430 6081 -229 -209 36 C ATOM 524 C LEU A 93 -8.820 12.274 -13.669 1.00 46.64 C ANISOU 524 C LEU A 93 6368 4566 6787 -183 -519 232 C ATOM 525 O LEU A 93 -7.872 13.057 -13.548 1.00 46.03 O ANISOU 525 O LEU A 93 6454 4428 6609 -233 -551 340 O ATOM 526 CB LEU A 93 -8.129 9.947 -14.269 1.00 42.63 C ANISOU 526 CB LEU A 93 6024 4607 5565 -363 -338 173 C ATOM 527 CG LEU A 93 -7.686 8.543 -13.845 1.00 41.76 C ANISOU 527 CG LEU A 93 5986 4674 5209 -406 -167 -23 C ATOM 528 CD1 LEU A 93 -7.422 7.659 -15.058 1.00 41.29 C ANISOU 528 CD1 LEU A 93 5887 4895 4907 -504 -328 -18 C ATOM 529 CD2 LEU A 93 -6.444 8.630 -12.963 1.00 40.80 C ANISOU 529 CD2 LEU A 93 6057 4521 4924 -442 -12 -121 C ATOM 530 N GLN A 94 -9.975 12.612 -14.238 1.00 50.09 N ANISOU 530 N GLN A 94 6579 4813 7638 -103 -813 289 N ATOM 531 CA GLN A 94 -10.232 13.973 -14.703 1.00 57.23 C ANISOU 531 CA GLN A 94 7408 5347 8991 -68 -1274 492 C ATOM 532 C GLN A 94 -10.233 14.962 -13.543 1.00 61.60 C ANISOU 532 C GLN A 94 7812 5592 10001 110 -1151 195 C ATOM 533 O GLN A 94 -9.815 16.103 -13.696 1.00 62.94 O ANISOU 533 O GLN A 94 8042 5479 10395 103 -1473 377 O ATOM 534 CB GLN A 94 -11.561 14.049 -15.457 1.00 60.70 C ANISOU 534 CB GLN A 94 7591 5574 9900 3 -1680 558 C ATOM 535 CG GLN A 94 -11.480 13.596 -16.905 1.00 61.85 C ANISOU 535 CG GLN A 94 7910 5941 9648 -263 -2016 988 C ATOM 536 CD GLN A 94 -12.841 13.533 -17.582 1.00 65.46 C ANISOU 536 CD GLN A 94 8119 6190 10562 -194 -2406 1048 C ATOM 537 OE1 GLN A 94 -13.848 13.213 -16.950 1.00 66.49 O ANISOU 537 OE1 GLN A 94 7934 6207 11120 59 -2218 659 O ATOM 538 NE2 GLN A 94 -12.875 13.841 -18.875 1.00 67.34 N ANISOU 538 NE2 GLN A 94 8497 6406 10683 -481 -2966 1527 N ATOM 539 N LEU A 95 -10.709 14.519 -12.384 1.00 64.68 N ANISOU 539 N LEU A 95 8001 6065 10509 208 -700 -276 N ATOM 540 CA LEU A 95 -10.641 15.326 -11.174 1.00 69.84 C ANISOU 540 CA LEU A 95 8488 6555 11494 300 -469 -666 C ATOM 541 C LEU A 95 -9.192 15.540 -10.766 1.00 70.40 C ANISOU 541 C LEU A 95 8919 6728 11102 192 -289 -496 C ATOM 542 O LEU A 95 -8.811 16.633 -10.358 1.00 72.89 O ANISOU 542 O LEU A 95 9201 6796 11697 264 -368 -558 O ATOM 543 CB LEU A 95 -11.412 14.660 -10.034 1.00 71.48 C ANISOU 543 CB LEU A 95 8434 6985 11741 254 25 -1213 C ATOM 544 CG LEU A 95 -12.740 15.291 -9.621 1.00 78.18 C ANISOU 544 CG LEU A 95 8710 7625 13372 404 -7 -1782 C ATOM 545 CD1 LEU A 95 -13.545 14.327 -8.756 1.00 78.78 C ANISOU 545 CD1 LEU A 95 8571 8091 13271 204 491 -2259 C ATOM 546 CD2 LEU A 95 -12.497 16.601 -8.884 1.00 81.92 C ANISOU 546 CD2 LEU A 95 8964 7818 14342 519 -17 -2124 C ATOM 547 N LEU A 96 -8.387 14.489 -10.884 1.00 69.85 N ANISOU 547 N LEU A 96 9159 6994 10384 32 -86 -319 N ATOM 548 CA LEU A 96 -6.985 14.545 -10.479 1.00 71.43 C ANISOU 548 CA LEU A 96 9675 7305 10161 -69 84 -218 C ATOM 549 C LEU A 96 -6.131 15.439 -11.374 1.00 76.48 C ANISOU 549 C LEU A 96 10500 7846 10713 -121 -259 149 C ATOM 550 O LEU A 96 -5.272 16.167 -10.879 1.00 79.41 O ANISOU 550 O LEU A 96 11003 8130 11038 -131 -194 161 O ATOM 551 CB LEU A 96 -6.385 13.138 -10.450 1.00 67.20 C ANISOU 551 CB LEU A 96 9352 7089 9093 -210 276 -194 C ATOM 552 CG LEU A 96 -6.672 12.346 -9.180 1.00 67.33 C ANISOU 552 CG LEU A 96 9354 7205 9023 -311 620 -481 C ATOM 553 CD1 LEU A 96 -6.183 10.919 -9.321 1.00 65.35 C ANISOU 553 CD1 LEU A 96 9295 7150 8385 -441 611 -411 C ATOM 554 CD2 LEU A 96 -6.012 13.027 -8.001 1.00 68.31 C ANISOU 554 CD2 LEU A 96 9569 7258 9127 -370 855 -630 C ATOM 555 N MET A 97 -6.357 15.388 -12.684 1.00 79.09 N ANISOU 555 N MET A 97 10854 8223 10975 -222 -633 459 N ATOM 556 CA MET A 97 -5.555 16.180 -13.613 1.00 83.14 C ANISOU 556 CA MET A 97 11575 8734 11280 -438 -992 847 C ATOM 557 C MET A 97 -5.839 17.675 -13.464 1.00 90.02 C ANISOU 557 C MET A 97 12365 9120 12716 -353 -1376 964 C ATOM 558 O MET A 97 -5.152 18.506 -14.057 1.00 91.58 O ANISOU 558 O MET A 97 12767 9253 12777 -579 -1724 1318 O ATOM 559 CB MET A 97 -5.802 15.750 -15.063 1.00 84.71 C ANISOU 559 CB MET A 97 11817 9161 11209 -695 -1323 1149 C ATOM 560 CG MET A 97 -7.026 16.392 -15.704 1.00 89.62 C ANISOU 560 CG MET A 97 12267 9418 12366 -666 -1861 1369 C ATOM 561 SD MET A 97 -6.995 16.392 -17.511 1.00 80.50 S ANISOU 561 SD MET A 97 11288 8511 10788 -1179 -2418 1907 S ATOM 562 CE MET A 97 -5.778 17.654 -17.840 1.00 85.40 C ANISOU 562 CE MET A 97 12224 9104 11120 -1581 -2748 2300 C ATOM 563 N GLN A 98 -6.854 18.011 -12.672 1.00 93.64 N ANISOU 563 N GLN A 98 12497 9250 13833 -66 -1339 622 N ATOM 564 CA GLN A 98 -7.218 19.405 -12.434 1.00 96.40 C ANISOU 564 CA GLN A 98 12655 9064 14906 81 -1743 583 C ATOM 565 C GLN A 98 -6.522 19.977 -11.202 1.00 91.95 C ANISOU 565 C GLN A 98 12095 8434 14407 190 -1385 282 C ATOM 566 O GLN A 98 -6.848 21.076 -10.751 1.00 96.22 O ANISOU 566 O GLN A 98 12392 8538 15629 364 -1625 79 O ATOM 567 CB GLN A 98 -8.733 19.542 -12.282 1.00101.76 C ANISOU 567 CB GLN A 98 12859 9415 16389 336 -1934 227 C ATOM 568 CG GLN A 98 -9.503 19.295 -13.563 1.00106.15 C ANISOU 568 CG GLN A 98 13393 9884 17054 240 -2466 580 C ATOM 569 CD GLN A 98 -10.989 19.521 -13.398 1.00112.50 C ANISOU 569 CD GLN A 98 13678 10304 18761 520 -2709 171 C ATOM 570 OE1 GLN A 98 -11.459 19.853 -12.310 1.00115.25 O ANISOU 570 OE1 GLN A 98 13634 10507 19648 764 -2432 -458 O ATOM 571 NE2 GLN A 98 -11.740 19.342 -14.479 1.00115.15 N ANISOU 571 NE2 GLN A 98 13974 10507 19272 452 -3224 472 N ATOM 572 N SER A 99 -5.563 19.230 -10.665 1.00162.93 N ANISOU 572 N SER A 99 18232 22094 21582 7151 -5678 -231 N ATOM 573 CA SER A 99 -4.797 19.678 -9.507 1.00152.75 C ANISOU 573 CA SER A 99 17131 20669 20237 6835 -4809 -57 C ATOM 574 C SER A 99 -3.298 19.563 -9.769 1.00143.67 C ANISOU 574 C SER A 99 16692 19746 18150 6722 -4569 189 C ATOM 575 O SER A 99 -2.843 18.611 -10.399 1.00145.71 O ANISOU 575 O SER A 99 17162 20221 17981 6686 -4837 73 O ATOM 576 CB SER A 99 -5.182 18.873 -8.264 1.00153.39 C ANISOU 576 CB SER A 99 16749 20613 20918 6378 -4318 -382 C ATOM 577 OG SER A 99 -6.548 19.061 -7.934 1.00160.80 O ANISOU 577 OG SER A 99 17001 21292 22806 6440 -4408 -649 O ATOM 578 N THR A 100 -2.538 20.543 -9.290 1.00133.21 N ANISOU 578 N THR A 100 15708 18349 16557 6650 -4027 492 N ATOM 579 CA THR A 100 -1.089 20.549 -9.464 1.00124.75 C ANISOU 579 CA THR A 100 15245 17472 14682 6525 -3737 709 C ATOM 580 C THR A 100 -0.430 19.598 -8.469 1.00118.34 C ANISOU 580 C THR A 100 14350 16753 13861 6064 -3285 596 C ATOM 581 O THR A 100 -0.425 19.857 -7.266 1.00114.30 O ANISOU 581 O THR A 100 13664 16132 13633 5740 -2753 609 O ATOM 582 CB THR A 100 -0.495 21.964 -9.290 1.00121.89 C ANISOU 582 CB THR A 100 15257 16998 14056 6575 -3290 1042 C ATOM 583 OG1 THR A 100 -1.179 22.887 -10.150 1.00126.62 O ANISOU 583 OG1 THR A 100 15927 17443 14740 7036 -3701 1211 O ATOM 584 CG2 THR A 100 0.994 21.966 -9.623 1.00117.45 C ANISOU 584 CG2 THR A 100 15294 16645 12686 6464 -3034 1222 C ATOM 585 N PRO A 101 0.135 18.492 -8.976 1.00118.74 N ANISOU 585 N PRO A 101 14550 16989 13577 6022 -3488 495 N ATOM 586 CA PRO A 101 0.714 17.446 -8.127 1.00115.02 C ANISOU 586 CA PRO A 101 13976 16573 13154 5649 -3154 426 C ATOM 587 C PRO A 101 1.895 17.954 -7.296 1.00110.38 C ANISOU 587 C PRO A 101 13647 16064 12230 5378 -2581 704 C ATOM 588 O PRO A 101 2.686 18.763 -7.783 1.00108.98 O ANISOU 588 O PRO A 101 13866 15971 11570 5498 -2482 906 O ATOM 589 CB PRO A 101 1.162 16.386 -9.141 1.00115.76 C ANISOU 589 CB PRO A 101 14256 16807 12920 5761 -3497 290 C ATOM 590 CG PRO A 101 1.359 17.126 -10.408 1.00103.69 C ANISOU 590 CG PRO A 101 13151 15368 10879 6097 -3822 395 C ATOM 591 CD PRO A 101 0.327 18.210 -10.409 1.00121.70 C ANISOU 591 CD PRO A 101 15256 17511 13471 6316 -4012 461 C ATOM 592 N ALA A 102 2.001 17.487 -6.054 1.00107.22 N ANISOU 592 N ALA A 102 13037 15637 12064 4990 -2215 708 N ATOM 593 CA ALA A 102 3.067 17.928 -5.156 1.00102.87 C ANISOU 593 CA ALA A 102 12681 15206 11198 4670 -1729 957 C ATOM 594 C ALA A 102 3.339 16.906 -4.053 1.00101.71 C ANISOU 594 C ALA A 102 12366 15089 11189 4282 -1525 990 C ATOM 595 O ALA A 102 2.451 16.143 -3.672 1.00102.91 O ANISOU 595 O ALA A 102 12226 15084 11793 4182 -1588 803 O ATOM 596 CB ALA A 102 2.714 19.282 -4.544 1.00101.43 C ANISOU 596 CB ALA A 102 12509 14913 11118 4548 -1364 1018 C ATOM 597 N THR A 103 4.574 16.890 -3.554 1.00100.44 N ANISOU 597 N THR A 103 12391 15125 10648 4062 -1291 1238 N ATOM 598 CA THR A 103 4.933 16.079 -2.390 1.00100.54 C ANISOU 598 CA THR A 103 12297 15186 10718 3674 -1110 1377 C ATOM 599 C THR A 103 5.822 16.872 -1.436 1.00100.92 C ANISOU 599 C THR A 103 12505 15442 10396 3298 -745 1621 C ATOM 600 O THR A 103 6.725 16.320 -0.807 1.00101.84 O ANISOU 600 O THR A 103 12639 15731 10323 3070 -708 1855 O ATOM 601 CB THR A 103 5.662 14.774 -2.783 1.00 99.73 C ANISOU 601 CB THR A 103 12175 15130 10589 3801 -1334 1458 C ATOM 602 OG1 THR A 103 6.789 15.077 -3.615 1.00 99.05 O ANISOU 602 OG1 THR A 103 12302 15215 10117 4017 -1385 1561 O ATOM 603 CG2 THR A 103 4.726 13.827 -3.517 1.00101.08 C ANISOU 603 CG2 THR A 103 12168 15088 11151 4043 -1634 1166 C ATOM 604 N PHE A 110 23.024 11.660 12.548 1.00 41.36 N ANISOU 604 N PHE A 110 4564 5712 5440 -99 -48 71 N ATOM 605 CA PHE A 110 22.884 12.822 13.423 1.00 44.72 C ANISOU 605 CA PHE A 110 5187 6130 5676 -345 -13 62 C ATOM 606 C PHE A 110 22.732 14.108 12.634 1.00 43.68 C ANISOU 606 C PHE A 110 5050 6014 5534 -406 212 -26 C ATOM 607 O PHE A 110 22.009 15.011 13.051 1.00 44.98 O ANISOU 607 O PHE A 110 5423 6098 5570 -539 334 -70 O ATOM 608 CB PHE A 110 24.094 12.972 14.350 1.00 49.07 C ANISOU 608 CB PHE A 110 5679 6774 6193 -501 -256 123 C ATOM 609 CG PHE A 110 24.094 12.035 15.515 1.00 56.13 C ANISOU 609 CG PHE A 110 6695 7621 7012 -541 -505 234 C ATOM 610 CD1 PHE A 110 25.051 11.029 15.613 1.00 61.17 C ANISOU 610 CD1 PHE A 110 7134 8299 7809 -430 -779 320 C ATOM 611 CD2 PHE A 110 23.147 12.162 16.523 1.00 59.12 C ANISOU 611 CD2 PHE A 110 7387 7913 7164 -701 -472 251 C ATOM 612 CE1 PHE A 110 25.065 10.162 16.697 1.00 65.73 C ANISOU 612 CE1 PHE A 110 7846 8812 8315 -481 -1047 452 C ATOM 613 CE2 PHE A 110 23.145 11.294 17.613 1.00 64.55 C ANISOU 613 CE2 PHE A 110 8217 8562 7746 -779 -710 371 C ATOM 614 CZ PHE A 110 24.108 10.289 17.701 1.00 67.28 C ANISOU 614 CZ PHE A 110 8386 8931 8247 -670 -1015 488 C ATOM 615 N LEU A 111 23.435 14.193 11.507 1.00 41.21 N ANISOU 615 N LEU A 111 4499 5799 5361 -320 262 -56 N ATOM 616 CA LEU A 111 23.638 15.474 10.832 1.00 42.83 C ANISOU 616 CA LEU A 111 4685 6040 5546 -434 417 -108 C ATOM 617 C LEU A 111 22.676 15.722 9.667 1.00 33.52 C ANISOU 617 C LEU A 111 3551 4789 4395 -329 633 -149 C ATOM 618 O LEU A 111 22.940 16.565 8.814 1.00 39.68 O ANISOU 618 O LEU A 111 4278 5610 5188 -393 744 -173 O ATOM 619 CB LEU A 111 25.089 15.576 10.344 1.00 36.92 C ANISOU 619 CB LEU A 111 3653 5470 4903 -470 347 -117 C ATOM 620 CG LEU A 111 26.145 15.516 11.455 1.00 39.06 C ANISOU 620 CG LEU A 111 3856 5823 5161 -598 110 -73 C ATOM 621 CD1 LEU A 111 27.553 15.479 10.883 1.00 40.83 C ANISOU 621 CD1 LEU A 111 3743 6236 5533 -603 47 -101 C ATOM 622 CD2 LEU A 111 25.996 16.680 12.445 1.00 39.57 C ANISOU 622 CD2 LEU A 111 4159 5832 5043 -855 105 -71 C ATOM 623 N GLY A 112 21.566 14.992 9.640 1.00 32.16 N ANISOU 623 N GLY A 112 3483 4510 4225 -187 677 -148 N ATOM 624 CA GLY A 112 20.532 15.200 8.639 1.00 34.68 C ANISOU 624 CA GLY A 112 3860 4749 4568 -92 853 -179 C ATOM 625 C GLY A 112 20.019 16.636 8.582 1.00 37.36 C ANISOU 625 C GLY A 112 4359 4993 4844 -227 974 -206 C ATOM 626 O GLY A 112 19.691 17.140 7.508 1.00 39.12 O ANISOU 626 O GLY A 112 4571 5190 5102 -198 1084 -212 O ATOM 627 N PHE A 113 19.977 17.308 9.731 1.00 36.41 N ANISOU 627 N PHE A 113 4391 4812 4630 -384 942 -225 N ATOM 628 CA PHE A 113 19.464 18.675 9.804 1.00 36.96 C ANISOU 628 CA PHE A 113 4622 4756 4665 -506 1049 -272 C ATOM 629 C PHE A 113 20.360 19.675 9.059 1.00 39.66 C ANISOU 629 C PHE A 113 4887 5154 5027 -626 1066 -253 C ATOM 630 O PHE A 113 19.986 20.837 8.903 1.00 41.57 O ANISOU 630 O PHE A 113 5257 5270 5266 -718 1142 -278 O ATOM 631 CB PHE A 113 19.296 19.114 11.267 1.00 36.02 C ANISOU 631 CB PHE A 113 4684 4573 4431 -666 1018 -324 C ATOM 632 CG PHE A 113 20.599 19.273 12.012 1.00 40.76 C ANISOU 632 CG PHE A 113 5234 5296 4958 -840 871 -296 C ATOM 633 CD1 PHE A 113 21.174 18.194 12.677 1.00 42.93 C ANISOU 633 CD1 PHE A 113 5435 5679 5199 -824 704 -239 C ATOM 634 CD2 PHE A 113 21.244 20.500 12.058 1.00 42.89 C ANISOU 634 CD2 PHE A 113 5533 5563 5200 -1027 879 -320 C ATOM 635 CE1 PHE A 113 22.367 18.336 13.365 1.00 45.45 C ANISOU 635 CE1 PHE A 113 5693 6111 5464 -982 539 -205 C ATOM 636 CE2 PHE A 113 22.445 20.650 12.743 1.00 45.34 C ANISOU 636 CE2 PHE A 113 5784 5996 5446 -1199 732 -296 C ATOM 637 CZ PHE A 113 23.006 19.571 13.397 1.00 46.24 C ANISOU 637 CZ PHE A 113 5809 6228 5533 -1173 557 -239 C ATOM 638 N LEU A 114 21.533 19.227 8.608 1.00 36.98 N ANISOU 638 N LEU A 114 4336 4995 4719 -631 994 -215 N ATOM 639 CA LEU A 114 22.440 20.082 7.847 1.00 36.88 C ANISOU 639 CA LEU A 114 4230 5069 4715 -769 1024 -199 C ATOM 640 C LEU A 114 22.147 20.041 6.347 1.00 36.62 C ANISOU 640 C LEU A 114 4130 5053 4730 -680 1136 -177 C ATOM 641 O LEU A 114 22.731 20.805 5.572 1.00 34.14 O ANISOU 641 O LEU A 114 3772 4797 4401 -814 1184 -155 O ATOM 642 CB LEU A 114 23.894 19.673 8.090 1.00 38.85 C ANISOU 642 CB LEU A 114 4253 5525 4983 -839 906 -191 C ATOM 643 CG LEU A 114 24.488 19.857 9.490 1.00 41.27 C ANISOU 643 CG LEU A 114 4604 5852 5226 -987 758 -193 C ATOM 644 CD1 LEU A 114 25.908 19.276 9.535 1.00 42.97 C ANISOU 644 CD1 LEU A 114 4536 6280 5509 -1008 619 -180 C ATOM 645 CD2 LEU A 114 24.499 21.327 9.881 1.00 39.82 C ANISOU 645 CD2 LEU A 114 4601 5572 4958 -1219 799 -215 C ATOM 646 N LEU A 115 21.262 19.133 5.945 1.00 35.77 N ANISOU 646 N LEU A 115 4023 4903 4664 -478 1171 -181 N ATOM 647 CA LEU A 115 20.945 18.934 4.531 1.00 35.99 C ANISOU 647 CA LEU A 115 3994 4961 4720 -393 1262 -163 C ATOM 648 C LEU A 115 20.160 20.110 3.944 1.00 37.68 C ANISOU 648 C LEU A 115 4391 5014 4914 -466 1333 -124 C ATOM 649 O LEU A 115 19.468 20.826 4.665 1.00 38.33 O ANISOU 649 O LEU A 115 4650 4915 4998 -501 1327 -136 O ATOM 650 CB LEU A 115 20.149 17.640 4.341 1.00 31.63 C ANISOU 650 CB LEU A 115 3410 4391 4219 -166 1267 -182 C ATOM 651 CG LEU A 115 20.905 16.339 4.617 1.00 34.14 C ANISOU 651 CG LEU A 115 3533 4848 4592 -59 1185 -211 C ATOM 652 CD1 LEU A 115 19.971 15.128 4.560 1.00 29.53 C ANISOU 652 CD1 LEU A 115 2969 4197 4056 147 1181 -225 C ATOM 653 CD2 LEU A 115 22.072 16.179 3.661 1.00 31.37 C ANISOU 653 CD2 LEU A 115 2948 4697 4273 -93 1219 -241 C ATOM 654 N GLY A 116 20.272 20.296 2.631 1.00 36.68 N ANISOU 654 N GLY A 116 4221 4948 4769 -496 1393 -83 N ATOM 655 CA GLY A 116 19.449 21.256 1.918 1.00 36.35 C ANISOU 655 CA GLY A 116 4353 4739 4719 -543 1424 -20 C ATOM 656 C GLY A 116 18.046 20.712 1.693 1.00 36.45 C ANISOU 656 C GLY A 116 4442 4618 4790 -340 1434 -23 C ATOM 657 O GLY A 116 17.705 19.627 2.178 1.00 35.68 O ANISOU 657 O GLY A 116 4280 4550 4726 -182 1427 -76 O ATOM 658 N VAL A 117 17.228 21.465 0.961 1.00 36.15 N ANISOU 658 N VAL A 117 4539 4424 4771 -352 1434 42 N ATOM 659 CA VAL A 117 15.844 21.077 0.696 1.00 33.58 C ANISOU 659 CA VAL A 117 4277 3963 4520 -171 1429 42 C ATOM 660 C VAL A 117 15.583 21.124 -0.810 1.00 34.94 C ANISOU 660 C VAL A 117 4463 4163 4649 -186 1424 133 C ATOM 661 O VAL A 117 15.625 22.191 -1.426 1.00 36.64 O ANISOU 661 O VAL A 117 4791 4290 4841 -325 1389 227 O ATOM 662 CB VAL A 117 14.839 21.998 1.441 1.00 40.25 C ANISOU 662 CB VAL A 117 5281 4541 5472 -145 1405 17 C ATOM 663 CG1 VAL A 117 13.397 21.516 1.245 1.00 39.45 C ANISOU 663 CG1 VAL A 117 5201 4317 5471 49 1403 -4 C ATOM 664 CG2 VAL A 117 15.163 22.070 2.929 1.00 38.16 C ANISOU 664 CG2 VAL A 117 5030 4262 5207 -185 1419 -81 C ATOM 665 N GLY A 118 15.342 19.962 -1.408 1.00 34.40 N ANISOU 665 N GLY A 118 4296 4216 4560 -62 1451 110 N ATOM 666 CA GLY A 118 15.056 19.892 -2.829 1.00 34.44 C ANISOU 666 CA GLY A 118 4323 4266 4497 -87 1447 184 C ATOM 667 C GLY A 118 13.562 19.878 -3.098 1.00 34.96 C ANISOU 667 C GLY A 118 4484 4145 4653 55 1385 218 C ATOM 668 O GLY A 118 12.749 19.942 -2.171 1.00 33.06 O ANISOU 668 O GLY A 118 4278 3743 4539 173 1366 168 O ATOM 669 N SER A 119 13.205 19.812 -4.376 1.00 36.82 N ANISOU 669 N SER A 119 4758 4412 4820 26 1353 298 N ATOM 670 CA SER A 119 11.820 19.602 -4.799 1.00 37.02 C ANISOU 670 CA SER A 119 4840 4300 4928 164 1278 330 C ATOM 671 C SER A 119 11.805 18.373 -5.705 1.00 35.72 C ANISOU 671 C SER A 119 4588 4323 4663 212 1320 297 C ATOM 672 O SER A 119 12.056 18.474 -6.907 1.00 35.28 O ANISOU 672 O SER A 119 4572 4367 4466 84 1308 370 O ATOM 673 CB SER A 119 11.274 20.836 -5.520 1.00 37.61 C ANISOU 673 CB SER A 119 5077 4190 5025 70 1152 481 C ATOM 674 OG SER A 119 9.886 20.714 -5.777 1.00 37.47 O ANISOU 674 OG SER A 119 5090 4014 5132 221 1055 506 O ATOM 675 N ALA A 120 11.524 17.216 -5.115 1.00 36.42 N ANISOU 675 N ALA A 120 4570 4454 4813 377 1368 183 N ATOM 676 CA ALA A 120 11.808 15.923 -5.746 1.00 38.84 C ANISOU 676 CA ALA A 120 4769 4948 5038 424 1431 108 C ATOM 677 C ALA A 120 11.177 15.694 -7.126 1.00 37.42 C ANISOU 677 C ALA A 120 4645 4805 4769 397 1389 164 C ATOM 678 O ALA A 120 11.773 15.025 -7.961 1.00 38.76 O ANISOU 678 O ALA A 120 4754 5163 4809 338 1458 113 O ATOM 679 CB ALA A 120 11.392 14.803 -4.807 1.00 39.00 C ANISOU 679 CB ALA A 120 4707 4945 5167 608 1454 0 C ATOM 680 N ILE A 121 9.982 16.227 -7.370 1.00 36.04 N ANISOU 680 N ILE A 121 4574 4453 4666 435 1272 255 N ATOM 681 CA ILE A 121 9.329 15.999 -8.664 1.00 35.23 C ANISOU 681 CA ILE A 121 4532 4381 4472 400 1199 322 C ATOM 682 C ILE A 121 9.220 17.256 -9.512 1.00 36.83 C ANISOU 682 C ILE A 121 4892 4503 4601 229 1078 499 C ATOM 683 O ILE A 121 8.364 17.330 -10.397 1.00 37.85 O ANISOU 683 O ILE A 121 5102 4577 4702 214 952 593 O ATOM 684 CB ILE A 121 7.896 15.406 -8.501 1.00 37.92 C ANISOU 684 CB ILE A 121 4855 4597 4957 581 1124 296 C ATOM 685 CG1 ILE A 121 7.020 16.320 -7.637 1.00 35.74 C ANISOU 685 CG1 ILE A 121 4617 4075 4890 669 1038 338 C ATOM 686 CG2 ILE A 121 7.959 13.999 -7.921 1.00 36.64 C ANISOU 686 CG2 ILE A 121 4567 4525 4830 717 1228 140 C ATOM 687 CD1 ILE A 121 5.551 15.943 -7.628 1.00 34.76 C ANISOU 687 CD1 ILE A 121 4462 3827 4918 819 952 322 C ATOM 688 N ALA A 122 10.083 18.239 -9.252 1.00 38.05 N ANISOU 688 N ALA A 122 5095 4641 4719 88 1097 554 N ATOM 689 CA ALA A 122 10.085 19.471 -10.040 1.00 37.70 C ANISOU 689 CA ALA A 122 5224 4506 4596 -104 971 739 C ATOM 690 C ALA A 122 10.311 19.177 -11.522 1.00 39.34 C ANISOU 690 C ALA A 122 5498 4899 4551 -288 963 808 C ATOM 691 O ALA A 122 9.708 19.808 -12.386 1.00 42.66 O ANISOU 691 O ALA A 122 6075 5217 4915 -390 795 978 O ATOM 692 CB ALA A 122 11.138 20.436 -9.523 1.00 37.49 C ANISOU 692 CB ALA A 122 5230 4467 4548 -255 1020 767 C ATOM 693 N SER A 123 11.175 18.211 -11.816 1.00 39.03 N ANISOU 693 N SER A 123 5341 5127 4362 -335 1139 671 N ATOM 694 CA SER A 123 11.463 17.854 -13.202 1.00 41.27 C ANISOU 694 CA SER A 123 5679 5618 4383 -529 1174 691 C ATOM 695 C SER A 123 10.252 17.170 -13.852 1.00 40.61 C ANISOU 695 C SER A 123 5636 5493 4299 -426 1063 707 C ATOM 696 O SER A 123 9.837 17.538 -14.952 1.00 41.22 O ANISOU 696 O SER A 123 5871 5574 4218 -589 936 851 O ATOM 697 CB SER A 123 12.698 16.950 -13.288 1.00 43.83 C ANISOU 697 CB SER A 123 5831 6232 4590 -579 1409 493 C ATOM 698 OG SER A 123 12.513 15.756 -12.545 1.00 45.59 O ANISOU 698 OG SER A 123 5884 6467 4973 -322 1482 315 O ATOM 699 N GLY A 124 9.682 16.182 -13.167 1.00 39.60 N ANISOU 699 N GLY A 124 5376 5328 4343 -174 1096 570 N ATOM 700 CA GLY A 124 8.502 15.502 -13.670 1.00 38.96 C ANISOU 700 CA GLY A 124 5315 5201 4287 -71 991 573 C ATOM 701 C GLY A 124 7.332 16.448 -13.867 1.00 40.67 C ANISOU 701 C GLY A 124 5665 5178 4611 -57 744 769 C ATOM 702 O GLY A 124 6.658 16.412 -14.895 1.00 43.57 O ANISOU 702 O GLY A 124 6132 5549 4872 -137 601 869 O ATOM 703 N VAL A 125 7.097 17.314 -12.886 1.00 38.92 N ANISOU 703 N VAL A 125 5441 4740 4607 41 683 818 N ATOM 704 CA VAL A 125 5.978 18.243 -12.951 1.00 38.48 C ANISOU 704 CA VAL A 125 5480 4421 4720 94 446 978 C ATOM 705 C VAL A 125 6.150 19.247 -14.092 1.00 42.28 C ANISOU 705 C VAL A 125 6167 4874 5025 -156 278 1203 C ATOM 706 O VAL A 125 5.172 19.609 -14.752 1.00 44.01 O ANISOU 706 O VAL A 125 6479 4953 5289 -158 42 1353 O ATOM 707 CB VAL A 125 5.788 18.979 -11.599 1.00 41.57 C ANISOU 707 CB VAL A 125 5820 4587 5386 244 450 943 C ATOM 708 CG1 VAL A 125 4.862 20.171 -11.740 1.00 42.59 C ANISOU 708 CG1 VAL A 125 6054 4427 5702 270 206 1107 C ATOM 709 CG2 VAL A 125 5.239 18.018 -10.561 1.00 37.81 C ANISOU 709 CG2 VAL A 125 5173 4104 5088 479 559 755 C ATOM 710 N ALA A 126 7.388 19.676 -14.348 1.00 43.09 N ANISOU 710 N ALA A 126 6338 5111 4922 -381 386 1234 N ATOM 711 CA ALA A 126 7.649 20.586 -15.461 1.00 45.38 C ANISOU 711 CA ALA A 126 6845 5399 4997 -669 243 1455 C ATOM 712 C ALA A 126 7.223 19.955 -16.788 1.00 47.24 C ANISOU 712 C ALA A 126 7165 5788 4998 -796 162 1512 C ATOM 713 O ALA A 126 6.601 20.607 -17.616 1.00 47.64 O ANISOU 713 O ALA A 126 7395 5716 4990 -918 -92 1731 O ATOM 714 CB ALA A 126 9.121 20.982 -15.511 1.00 44.32 C ANISOU 714 CB ALA A 126 6741 5439 4659 -914 421 1440 C ATOM 715 N VAL A 127 7.559 18.685 -16.984 1.00 49.11 N ANISOU 715 N VAL A 127 7276 6280 5102 -771 363 1314 N ATOM 716 CA VAL A 127 7.124 17.964 -18.173 1.00 51.54 C ANISOU 716 CA VAL A 127 7653 6741 5189 -881 308 1326 C ATOM 717 C VAL A 127 5.605 17.826 -18.179 1.00 52.13 C ANISOU 717 C VAL A 127 7725 6610 5471 -684 61 1401 C ATOM 718 O VAL A 127 4.961 18.027 -19.209 1.00 53.30 O ANISOU 718 O VAL A 127 8025 6737 5488 -819 -158 1567 O ATOM 719 CB VAL A 127 7.776 16.567 -18.267 1.00 49.18 C ANISOU 719 CB VAL A 127 7198 6728 4758 -856 587 1057 C ATOM 720 CG1 VAL A 127 7.093 15.719 -19.340 1.00 47.18 C ANISOU 720 CG1 VAL A 127 7003 6592 4331 -917 519 1035 C ATOM 721 CG2 VAL A 127 9.264 16.708 -18.557 1.00 50.52 C ANISOU 721 CG2 VAL A 127 7365 7138 4691 -1097 816 984 C ATOM 722 N SER A 128 5.038 17.499 -17.021 1.00 50.59 N ANISOU 722 N SER A 128 7357 6271 5596 -382 93 1280 N ATOM 723 CA SER A 128 3.592 17.380 -16.891 1.00 51.74 C ANISOU 723 CA SER A 128 7455 6224 5981 -182 -115 1321 C ATOM 724 C SER A 128 2.867 18.680 -17.249 1.00 56.09 C ANISOU 724 C SER A 128 8151 6513 6648 -227 -436 1580 C ATOM 725 O SER A 128 1.783 18.640 -17.831 1.00 59.34 O ANISOU 725 O SER A 128 8591 6832 7123 -190 -676 1684 O ATOM 726 CB SER A 128 3.214 16.951 -15.474 1.00 49.18 C ANISOU 726 CB SER A 128 6925 5790 5970 113 5 1143 C ATOM 727 OG SER A 128 1.806 16.842 -15.346 1.00 50.31 O ANISOU 727 OG SER A 128 6999 5764 6353 292 -177 1164 O ATOM 728 N LYS A 129 3.460 19.823 -16.905 1.00 55.79 N ANISOU 728 N LYS A 129 8201 6344 6651 -304 -456 1685 N ATOM 729 CA LYS A 129 2.888 21.121 -17.269 1.00 59.07 C ANISOU 729 CA LYS A 129 8777 6482 7184 -360 -775 1941 C ATOM 730 C LYS A 129 2.827 21.308 -18.780 1.00 61.12 C ANISOU 730 C LYS A 129 9263 6826 7135 -648 -988 2167 C ATOM 731 O LYS A 129 1.868 21.871 -19.309 1.00 62.99 O ANISOU 731 O LYS A 129 9594 6856 7482 -639 -1323 2369 O ATOM 732 CB LYS A 129 3.696 22.274 -16.668 1.00 62.78 C ANISOU 732 CB LYS A 129 9325 6811 7717 -433 -735 2002 C ATOM 733 CG LYS A 129 3.762 22.308 -15.158 1.00 65.81 C ANISOU 733 CG LYS A 129 9528 7084 8395 -186 -557 1804 C ATOM 734 CD LYS A 129 2.402 22.514 -14.519 1.00 70.38 C ANISOU 734 CD LYS A 129 9986 7382 9372 105 -718 1773 C ATOM 735 CE LYS A 129 2.548 22.904 -13.045 1.00 71.14 C ANISOU 735 CE LYS A 129 9962 7331 9735 283 -562 1607 C ATOM 736 NZ LYS A 129 3.174 24.255 -12.878 1.00 72.76 N ANISOU 736 NZ LYS A 129 10324 7348 9974 155 -632 1732 N ATOM 737 N VAL A 130 3.869 20.859 -19.470 1.00 60.72 N ANISOU 737 N VAL A 130 9296 7078 6696 -914 -798 2130 N ATOM 738 CA VAL A 130 3.934 21.006 -20.917 1.00 64.25 C ANISOU 738 CA VAL A 130 9979 7650 6784 -1243 -960 2327 C ATOM 739 C VAL A 130 2.813 20.213 -21.592 1.00 65.78 C ANISOU 739 C VAL A 130 10154 7878 6963 -1177 -1136 2336 C ATOM 740 O VAL A 130 2.249 20.659 -22.589 1.00 70.83 O ANISOU 740 O VAL A 130 10988 8449 7476 -1350 -1446 2577 O ATOM 741 CB VAL A 130 5.306 20.557 -21.472 1.00 64.64 C ANISOU 741 CB VAL A 130 10082 8058 6419 -1542 -658 2219 C ATOM 742 CG1 VAL A 130 5.355 20.712 -22.987 1.00 68.92 C ANISOU 742 CG1 VAL A 130 10889 8749 6550 -1923 -809 2414 C ATOM 743 CG2 VAL A 130 6.422 21.363 -20.833 1.00 63.68 C ANISOU 743 CG2 VAL A 130 9970 7914 6313 -1629 -498 2218 C ATOM 744 N LEU A 131 2.475 19.055 -21.033 1.00 62.23 N ANISOU 744 N LEU A 131 9478 7521 6646 -937 -959 2084 N ATOM 745 CA LEU A 131 1.434 18.206 -21.601 1.00 63.05 C ANISOU 745 CA LEU A 131 9543 7671 6744 -873 -1099 2061 C ATOM 746 C LEU A 131 0.048 18.852 -21.566 1.00 67.75 C ANISOU 746 C LEU A 131 10128 7954 7658 -709 -1484 2248 C ATOM 747 O LEU A 131 -0.870 18.398 -22.252 1.00 69.57 O ANISOU 747 O LEU A 131 10369 8201 7861 -715 -1690 2303 O ATOM 748 CB LEU A 131 1.396 16.860 -20.877 1.00 58.89 C ANISOU 748 CB LEU A 131 8773 7278 6324 -646 -821 1750 C ATOM 749 CG LEU A 131 2.627 15.983 -21.093 1.00 57.68 C ANISOU 749 CG LEU A 131 8604 7442 5869 -790 -473 1541 C ATOM 750 CD1 LEU A 131 2.421 14.605 -20.495 1.00 53.86 C ANISOU 750 CD1 LEU A 131 7908 7049 5509 -565 -270 1265 C ATOM 751 CD2 LEU A 131 2.958 15.886 -22.578 1.00 60.53 C ANISOU 751 CD2 LEU A 131 9182 8024 5794 -1148 -523 1631 C ATOM 752 N HIS A 132 -0.105 19.911 -20.773 1.00 68.61 N ANISOU 752 N HIS A 132 10208 7778 8081 -562 -1585 2333 N ATOM 753 CA HIS A 132 -1.377 20.626 -20.697 1.00 69.82 C ANISOU 753 CA HIS A 132 10329 7608 8590 -386 -1951 2493 C ATOM 754 C HIS A 132 -1.492 21.722 -21.754 1.00 73.90 C ANISOU 754 C HIS A 132 11124 7977 8979 -629 -2330 2842 C ATOM 755 O HIS A 132 -2.546 22.338 -21.904 1.00 76.13 O ANISOU 755 O HIS A 132 11401 7985 9539 -512 -2696 3011 O ATOM 756 CB HIS A 132 -1.572 21.238 -19.309 1.00 68.12 C ANISOU 756 CB HIS A 132 9939 7132 8809 -96 -1880 2388 C ATOM 757 CG HIS A 132 -1.975 20.253 -18.260 1.00 67.02 C ANISOU 757 CG HIS A 132 9520 7055 8891 181 -1633 2094 C ATOM 758 ND1 HIS A 132 -1.095 19.331 -17.723 1.00 66.21 N ANISOU 758 ND1 HIS A 132 9335 7197 8624 177 -1258 1865 N ATOM 759 CD2 HIS A 132 -3.158 20.045 -17.634 1.00 67.51 C ANISOU 759 CD2 HIS A 132 9362 6962 9325 456 -1710 1992 C ATOM 760 CE1 HIS A 132 -1.723 18.604 -16.816 1.00 64.22 C ANISOU 760 CE1 HIS A 132 8855 6930 8618 426 -1129 1657 C ATOM 761 NE2 HIS A 132 -2.972 19.013 -16.744 1.00 65.94 N ANISOU 761 NE2 HIS A 132 8982 6921 9152 589 -1381 1720 N ATOM 762 N LEU A 133 -0.409 21.970 -22.483 1.00 76.65 N ANISOU 762 N LEU A 133 11709 8502 8912 -976 -2251 2950 N ATOM 763 CA LEU A 133 -0.416 22.997 -23.519 1.00 82.67 C ANISOU 763 CA LEU A 133 12777 9140 9493 -1265 -2604 3302 C ATOM 764 C LEU A 133 -1.152 22.505 -24.763 1.00 88.48 C ANISOU 764 C LEU A 133 13598 10003 10016 -1416 -2840 3394 C ATOM 765 O LEU A 133 -1.283 21.300 -24.981 1.00 88.50 O ANISOU 765 O LEU A 133 13529 10250 9849 -1416 -2705 3251 O ATOM 766 CB LEU A 133 1.014 23.422 -23.871 1.00 81.59 C ANISOU 766 CB LEU A 133 12843 9185 8973 -1613 -2393 3344 C ATOM 767 CG LEU A 133 1.854 23.991 -22.719 1.00 78.17 C ANISOU 767 CG LEU A 133 12333 8649 8721 -1511 -2154 3242 C ATOM 768 CD1 LEU A 133 3.243 24.396 -23.193 1.00 78.20 C ANISOU 768 CD1 LEU A 133 12527 8856 8329 -1890 -1964 3290 C ATOM 769 CD2 LEU A 133 1.155 25.164 -22.047 1.00 78.37 C ANISOU 769 CD2 LEU A 133 12308 8252 9216 -1271 -2403 3329 C ATOM 770 N GLU A 134 -1.625 23.448 -25.573 1.00 92.16 N ANISOU 770 N GLU A 134 14180 10319 10517 -1536 -3152 3567 N ATOM 771 CA GLU A 134 -2.449 23.141 -26.738 1.00 97.48 C ANISOU 771 CA GLU A 134 14924 11063 11050 -1672 -3423 3663 C ATOM 772 C GLU A 134 -1.691 22.324 -27.777 1.00 97.88 C ANISOU 772 C GLU A 134 15157 11501 10532 -2046 -3246 3631 C ATOM 773 O GLU A 134 -0.540 22.625 -28.101 1.00 96.82 O ANISOU 773 O GLU A 134 15178 11524 10085 -2325 -3045 3630 O ATOM 774 CB GLU A 134 -2.970 24.430 -27.383 1.00105.76 C ANISOU 774 CB GLU A 134 16085 11859 12240 -1760 -3791 3869 C ATOM 775 CG GLU A 134 -3.504 25.465 -26.397 1.00109.33 C ANISOU 775 CG GLU A 134 16380 11936 13225 -1438 -3919 3869 C ATOM 776 CD GLU A 134 -2.402 26.320 -25.777 1.00111.95 C ANISOU 776 CD GLU A 134 16795 12193 13549 -1494 -3728 3866 C ATOM 777 OE1 GLU A 134 -1.896 27.232 -26.469 1.00116.51 O ANISOU 777 OE1 GLU A 134 17591 12735 13943 -1771 -3847 4025 O ATOM 778 OE2 GLU A 134 -2.042 26.078 -24.601 1.00108.77 O ANISOU 778 OE2 GLU A 134 16241 11765 13323 -1275 -3465 3705 O ATOM 779 N GLY A 135 -2.341 21.281 -28.286 1.00 98.47 N ANISOU 779 N GLY A 135 15194 11736 10486 -2051 -3302 3574 N ATOM 780 CA GLY A 135 -1.778 20.466 -29.347 1.00100.72 C ANISOU 780 CA GLY A 135 15635 12384 10251 -2399 -3141 3503 C ATOM 781 C GLY A 135 -0.585 19.627 -28.937 1.00100.48 C ANISOU 781 C GLY A 135 15581 12656 9942 -2470 -2672 3276 C ATOM 782 O GLY A 135 -0.018 18.901 -29.754 1.00102.98 O ANISOU 782 O GLY A 135 15989 13292 9847 -2742 -2466 3145 O ATOM 783 N GLU A 136 -0.200 19.725 -27.670 1.00 96.27 N ANISOU 783 N GLU A 136 14910 12019 9649 -2226 -2489 3205 N ATOM 784 CA GLU A 136 0.937 18.975 -27.160 1.00 90.28 C ANISOU 784 CA GLU A 136 14033 11523 8745 -2226 -1997 2905 C ATOM 785 C GLU A 136 0.593 17.495 -27.108 1.00 84.73 C ANISOU 785 C GLU A 136 13135 11019 8038 -2074 -1797 2605 C ATOM 786 O GLU A 136 1.421 16.641 -27.424 1.00 81.63 O ANISOU 786 O GLU A 136 12735 10934 7348 -2223 -1464 2376 O ATOM 787 CB GLU A 136 1.341 19.481 -25.776 1.00 86.98 C ANISOU 787 CB GLU A 136 13425 10915 8707 -1941 -1825 2810 C ATOM 788 CG GLU A 136 2.781 19.188 -25.414 1.00 86.23 C ANISOU 788 CG GLU A 136 13275 11063 8427 -2042 -1379 2588 C ATOM 789 CD GLU A 136 3.760 19.973 -26.263 1.00 92.34 C ANISOU 789 CD GLU A 136 14324 11963 8797 -2478 -1369 2767 C ATOM 790 OE1 GLU A 136 3.371 21.037 -26.794 1.00 96.89 O ANISOU 790 OE1 GLU A 136 15085 12337 9391 -2609 -1702 3042 O ATOM 791 OE2 GLU A 136 4.918 19.526 -26.402 1.00 93.25 O ANISOU 791 OE2 GLU A 136 14416 12374 8640 -2658 -1009 2575 O ATOM 792 N VAL A 137 -0.640 17.204 -26.711 1.00 83.38 N ANISOU 792 N VAL A 137 12802 10663 8216 -1780 -2005 2600 N ATOM 793 CA VAL A 137 -1.139 15.836 -26.697 1.00 81.95 C ANISOU 793 CA VAL A 137 12454 10631 8052 -1646 -1875 2349 C ATOM 794 C VAL A 137 -1.176 15.268 -28.110 1.00 84.08 C ANISOU 794 C VAL A 137 12936 11155 7855 -1995 -1952 2380 C ATOM 795 O VAL A 137 -0.848 14.102 -28.325 1.00 82.59 O ANISOU 795 O VAL A 137 12689 11214 7478 -2037 -1678 2112 O ATOM 796 CB VAL A 137 -2.546 15.756 -26.089 1.00 81.42 C ANISOU 796 CB VAL A 137 12182 10312 8441 -1308 -2124 2371 C ATOM 797 CG1 VAL A 137 -2.914 14.313 -25.793 1.00 78.33 C ANISOU 797 CG1 VAL A 137 11588 10063 8111 -1144 -1917 2074 C ATOM 798 CG2 VAL A 137 -2.618 16.595 -24.832 1.00 81.02 C ANISOU 798 CG2 VAL A 137 11975 9980 8831 -1017 -2119 2392 C ATOM 799 N ASN A 138 -1.575 16.101 -29.067 1.00 87.49 N ANISOU 799 N ASN A 138 13623 11515 8102 -2252 -2334 2708 N ATOM 800 CA ASN A 138 -1.663 15.683 -30.465 1.00 91.60 C ANISOU 800 CA ASN A 138 14388 12272 8145 -2631 -2453 2776 C ATOM 801 C ASN A 138 -0.329 15.168 -31.000 1.00 90.50 C ANISOU 801 C ASN A 138 14331 12478 7578 -2920 -2018 2539 C ATOM 802 O ASN A 138 -0.291 14.190 -31.749 1.00 90.72 O ANISOU 802 O ASN A 138 14389 12749 7330 -3079 -1882 2346 O ATOM 803 CB ASN A 138 -2.161 16.837 -31.341 1.00 97.58 C ANISOU 803 CB ASN A 138 15297 12834 8945 -2798 -2832 3058 C ATOM 804 CG ASN A 138 -3.540 17.326 -30.937 1.00 99.40 C ANISOU 804 CG ASN A 138 15402 12724 9641 -2504 -3256 3245 C ATOM 805 OD1 ASN A 138 -3.958 17.161 -29.790 1.00 97.14 O ANISOU 805 OD1 ASN A 138 14907 12284 9718 -2150 -3255 3197 O ATOM 806 ND2 ASN A 138 -4.254 17.937 -31.879 1.00103.43 N ANISOU 806 ND2 ASN A 138 16022 13112 10164 -2650 -3611 3441 N ATOM 807 N LYS A 139 0.757 15.834 -30.615 1.00 89.88 N ANISOU 807 N LYS A 139 14262 12405 7483 -2976 -1796 2530 N ATOM 808 CA LYS A 139 2.100 15.399 -30.983 1.00 90.35 C ANISOU 808 CA LYS A 139 14325 12772 7232 -3200 -1358 2268 C ATOM 809 C LYS A 139 2.325 13.961 -30.538 1.00 87.00 C ANISOU 809 C LYS A 139 13734 12568 6754 -3055 -1018 1922 C ATOM 810 O LYS A 139 2.691 13.100 -31.338 1.00 88.33 O ANISOU 810 O LYS A 139 13909 12984 6670 -3226 -805 1679 O ATOM 811 CB LYS A 139 3.157 16.309 -30.357 1.00 90.63 C ANISOU 811 CB LYS A 139 14335 12751 7348 -3209 -1184 2302 C ATOM 812 CG LYS A 139 2.987 17.778 -30.679 1.00 94.87 C ANISOU 812 CG LYS A 139 15032 13042 7971 -3334 -1508 2622 C ATOM 813 CD LYS A 139 3.983 18.618 -29.902 1.00 95.35 C ANISOU 813 CD LYS A 139 15053 13033 8145 -3311 -1335 2636 C ATOM 814 CE LYS A 139 3.864 20.086 -30.267 1.00 99.62 C ANISOU 814 CE LYS A 139 15763 13327 8761 -3453 -1650 2930 C ATOM 815 NZ LYS A 139 4.852 20.911 -29.522 1.00 99.44 N ANISOU 815 NZ LYS A 139 15707 13238 8839 -3448 -1482 2932 N ATOM 816 N ILE A 140 2.091 13.722 -29.252 1.00 83.29 N ANISOU 816 N ILE A 140 12986 11911 6750 -2627 -934 1796 N ATOM 817 CA ILE A 140 2.200 12.394 -28.654 1.00 79.91 C ANISOU 817 CA ILE A 140 12305 11577 6479 -2371 -628 1429 C ATOM 818 C ILE A 140 1.320 11.378 -29.375 1.00 81.17 C ANISOU 818 C ILE A 140 12496 11826 6518 -2412 -737 1337 C ATOM 819 O ILE A 140 1.753 10.266 -29.688 1.00 81.51 O ANISOU 819 O ILE A 140 12493 12091 6386 -2467 -460 1037 O ATOM 820 CB ILE A 140 1.796 12.416 -27.162 1.00 74.18 C ANISOU 820 CB ILE A 140 11311 10587 6288 -1920 -619 1380 C ATOM 821 CG1 ILE A 140 2.677 13.383 -26.368 1.00 72.86 C ANISOU 821 CG1 ILE A 140 11105 10327 6252 -1872 -503 1447 C ATOM 822 CG2 ILE A 140 1.852 11.018 -26.578 1.00 70.49 C ANISOU 822 CG2 ILE A 140 10614 10199 5969 -1681 -343 1032 C ATOM 823 CD1 ILE A 140 4.053 12.851 -26.074 1.00 72.35 C ANISOU 823 CD1 ILE A 140 10929 10484 6076 -1904 -76 1169 C ATOM 824 N LYS A 141 0.081 11.784 -29.634 1.00 81.80 N ANISOU 824 N LYS A 141 12648 11722 6710 -2382 -1153 1591 N ATOM 825 CA LYS A 141 -0.938 10.904 -30.193 1.00 82.20 C ANISOU 825 CA LYS A 141 12703 11813 6716 -2387 -1319 1535 C ATOM 826 C LYS A 141 -0.565 10.397 -31.582 1.00 85.01 C ANISOU 826 C LYS A 141 13300 12477 6523 -2808 -1253 1460 C ATOM 827 O LYS A 141 -0.669 9.202 -31.860 1.00 84.32 O ANISOU 827 O LYS A 141 13160 12543 6336 -2810 -1090 1190 O ATOM 828 CB LYS A 141 -2.284 11.632 -30.243 1.00 83.43 C ANISOU 828 CB LYS A 141 12887 11707 7107 -2298 -1815 1856 C ATOM 829 CG LYS A 141 -3.483 10.737 -30.499 1.00 83.68 C ANISOU 829 CG LYS A 141 12836 11727 7229 -2210 -2002 1790 C ATOM 830 CD LYS A 141 -4.773 11.530 -30.391 1.00 84.30 C ANISOU 830 CD LYS A 141 12877 11526 7626 -2071 -2484 2092 C ATOM 831 CE LYS A 141 -5.986 10.620 -30.341 1.00 83.42 C ANISOU 831 CE LYS A 141 12598 11380 7716 -1910 -2630 1991 C ATOM 832 NZ LYS A 141 -7.246 11.400 -30.204 1.00 84.21 N ANISOU 832 NZ LYS A 141 12615 11210 8172 -1755 -3096 2262 N ATOM 833 N SER A 142 -0.124 11.304 -32.449 1.00 87.21 N ANISOU 833 N SER A 142 13839 12834 6462 -3167 -1368 1685 N ATOM 834 CA SER A 142 0.202 10.929 -33.820 1.00 90.55 C ANISOU 834 CA SER A 142 14391 13464 6551 -3504 -1269 1565 C ATOM 835 C SER A 142 1.540 10.198 -33.879 1.00 90.25 C ANISOU 835 C SER A 142 14257 13676 6358 -3574 -751 1186 C ATOM 836 O SER A 142 1.764 9.375 -34.770 1.00 93.42 O ANISOU 836 O SER A 142 14686 14266 6544 -3753 -583 957 O ATOM 837 CB SER A 142 0.218 12.159 -34.737 1.00 94.33 C ANISOU 837 CB SER A 142 15072 13854 6915 -3791 -1527 1869 C ATOM 838 OG SER A 142 1.286 13.034 -34.424 1.00 94.76 O ANISOU 838 OG SER A 142 15130 13895 6979 -3849 -1356 1911 O ATOM 839 N ALA A 143 2.420 10.492 -32.926 1.00 86.95 N ANISOU 839 N ALA A 143 13708 13244 6086 -3420 -506 1112 N ATOM 840 CA ALA A 143 3.718 9.830 -32.852 1.00 88.36 C ANISOU 840 CA ALA A 143 13733 13624 6215 -3425 -31 746 C ATOM 841 C ALA A 143 3.575 8.347 -32.510 1.00 87.74 C ANISOU 841 C ALA A 143 13490 13635 6213 -3218 192 391 C ATOM 842 O ALA A 143 4.364 7.516 -32.964 1.00 89.87 O ANISOU 842 O ALA A 143 13665 14070 6411 -3275 508 66 O ATOM 843 CB ALA A 143 4.600 10.519 -31.831 1.00 88.02 C ANISOU 843 CB ALA A 143 13570 13520 6355 -3285 136 769 C ATOM 844 N LEU A 144 2.564 8.023 -31.710 1.00 84.60 N ANISOU 844 N LEU A 144 13046 13103 5995 -2970 13 452 N ATOM 845 CA LEU A 144 2.334 6.651 -31.272 1.00 81.58 C ANISOU 845 CA LEU A 144 12462 12714 5821 -2708 191 123 C ATOM 846 C LEU A 144 1.249 5.967 -32.090 1.00 84.18 C ANISOU 846 C LEU A 144 12910 13074 5999 -2823 -29 118 C ATOM 847 O LEU A 144 0.653 4.979 -31.654 1.00 81.45 O ANISOU 847 O LEU A 144 12414 12640 5894 -2582 -12 -58 O ATOM 848 CB LEU A 144 1.955 6.623 -29.796 1.00 75.38 C ANISOU 848 CB LEU A 144 11415 11649 5577 -2250 162 137 C ATOM 849 CG LEU A 144 3.036 7.078 -28.824 1.00 71.84 C ANISOU 849 CG LEU A 144 10810 11163 5321 -2092 405 85 C ATOM 850 CD1 LEU A 144 2.519 6.964 -27.401 1.00 67.29 C ANISOU 850 CD1 LEU A 144 10003 10318 5246 -1668 354 95 C ATOM 851 CD2 LEU A 144 4.290 6.244 -29.019 1.00 71.47 C ANISOU 851 CD2 LEU A 144 10683 11357 5116 -2164 825 -280 C ATOM 852 N LEU A 145 0.997 6.502 -33.278 1.00 89.30 N ANISOU 852 N LEU A 145 13800 13808 6322 -3170 -244 317 N ATOM 853 CA LEU A 145 -0.030 5.969 -34.160 1.00 93.22 C ANISOU 853 CA LEU A 145 14413 14323 6682 -3307 -489 345 C ATOM 854 C LEU A 145 0.396 4.645 -34.796 1.00 96.56 C ANISOU 854 C LEU A 145 14787 14920 6982 -3379 -172 -57 C ATOM 855 O LEU A 145 -0.410 3.721 -34.919 1.00 95.71 O ANISOU 855 O LEU A 145 14672 14808 6885 -3330 -254 -181 O ATOM 856 CB LEU A 145 -0.367 6.991 -35.246 1.00 95.77 C ANISOU 856 CB LEU A 145 14954 14617 6816 -3612 -808 680 C ATOM 857 CG LEU A 145 -1.541 6.664 -36.168 1.00 98.10 C ANISOU 857 CG LEU A 145 15377 14901 6994 -3763 -1139 788 C ATOM 858 CD1 LEU A 145 -2.834 6.524 -35.375 1.00 95.11 C ANISOU 858 CD1 LEU A 145 14912 14343 6881 -3497 -1478 927 C ATOM 859 CD2 LEU A 145 -1.675 7.727 -37.252 1.00102.23 C ANISOU 859 CD2 LEU A 145 16114 15394 7335 -4082 -1412 1104 C ATOM 860 N SER A 146 1.665 4.558 -35.191 1.00100.02 N ANISOU 860 N SER A 146 15178 15494 7332 -3492 178 -262 N ATOM 861 CA SER A 146 2.184 3.378 -35.884 1.00102.53 C ANISOU 861 CA SER A 146 15441 15956 7560 -3568 473 -635 C ATOM 862 C SER A 146 2.906 2.410 -34.944 1.00 98.87 C ANISOU 862 C SER A 146 14718 15473 7376 -3246 826 -993 C ATOM 863 O SER A 146 2.898 1.197 -35.163 1.00 99.31 O ANISOU 863 O SER A 146 14701 15556 7478 -3179 983 -1294 O ATOM 864 CB SER A 146 3.131 3.800 -37.011 1.00106.56 C ANISOU 864 CB SER A 146 16042 16627 7817 -3908 620 -656 C ATOM 865 OG SER A 146 4.282 4.450 -36.494 1.00105.76 O ANISOU 865 OG SER A 146 15826 16542 7817 -3855 829 -667 O ATOM 866 N THR A 147 3.537 2.956 -33.909 1.00 94.96 N ANISOU 866 N THR A 147 14084 14910 7086 -3046 936 -952 N ATOM 867 CA THR A 147 4.242 2.148 -32.919 1.00 90.70 C ANISOU 867 CA THR A 147 13285 14316 6860 -2718 1232 -1248 C ATOM 868 C THR A 147 3.755 2.477 -31.511 1.00 87.43 C ANISOU 868 C THR A 147 12784 13745 6690 -2431 1131 -1119 C ATOM 869 O THR A 147 3.096 3.492 -31.294 1.00 87.41 O ANISOU 869 O THR A 147 12911 13687 6613 -2494 859 -790 O ATOM 870 CB THR A 147 5.769 2.358 -32.997 1.00 90.83 C ANISOU 870 CB THR A 147 13161 14419 6930 -2745 1527 -1391 C ATOM 871 OG1 THR A 147 6.059 3.760 -33.048 1.00 89.93 O ANISOU 871 OG1 THR A 147 13148 14329 6691 -2918 1421 -1098 O ATOM 872 CG2 THR A 147 6.336 1.687 -34.242 1.00 96.83 C ANISOU 872 CG2 THR A 147 13945 15334 7510 -2973 1699 -1626 C ATOM 873 N ASN A 148 4.076 1.611 -30.558 1.00 85.02 N ANISOU 873 N ASN A 148 12258 13349 6695 -2114 1333 -1368 N ATOM 874 CA ASN A 148 3.682 1.836 -29.175 1.00 81.33 C ANISOU 874 CA ASN A 148 11654 12681 6568 -1797 1251 -1256 C ATOM 875 C ASN A 148 4.827 2.427 -28.359 1.00 79.13 C ANISOU 875 C ASN A 148 11224 12397 6444 -1674 1449 -1262 C ATOM 876 O ASN A 148 4.757 2.511 -27.130 1.00 74.17 O ANISOU 876 O ASN A 148 10427 11565 6190 -1364 1420 -1201 O ATOM 877 CB ASN A 148 3.191 0.533 -28.549 1.00 78.73 C ANISOU 877 CB ASN A 148 11175 12198 6539 -1510 1292 -1477 C ATOM 878 CG ASN A 148 2.002 -0.048 -29.284 1.00 79.86 C ANISOU 878 CG ASN A 148 11453 12333 6556 -1627 1081 -1466 C ATOM 879 OD1 ASN A 148 2.162 -0.794 -30.248 1.00 83.37 O ANISOU 879 OD1 ASN A 148 12001 12948 6729 -1831 1201 -1702 O ATOM 880 ND2 ASN A 148 0.800 0.298 -28.838 1.00 77.93 N ANISOU 880 ND2 ASN A 148 11200 11897 6513 -1505 767 -1206 N ATOM 881 N LYS A 149 5.876 2.845 -29.060 1.00 81.61 N ANISOU 881 N LYS A 149 11560 12860 6589 -1879 1592 -1291 N ATOM 882 CA LYS A 149 7.053 3.413 -28.418 1.00 80.38 C ANISOU 882 CA LYS A 149 11246 12693 6602 -1784 1754 -1290 C ATOM 883 C LYS A 149 7.745 4.391 -29.362 1.00 81.16 C ANISOU 883 C LYS A 149 11465 12934 6436 -2112 1758 -1157 C ATOM 884 O LYS A 149 8.132 4.021 -30.468 1.00 84.72 O ANISOU 884 O LYS A 149 11964 13515 6709 -2321 1842 -1289 O ATOM 885 CB LYS A 149 8.012 2.302 -27.994 1.00 81.59 C ANISOU 885 CB LYS A 149 11144 12796 7061 -1533 1991 -1605 C ATOM 886 CG LYS A 149 8.990 2.707 -26.914 1.00 82.24 C ANISOU 886 CG LYS A 149 11028 12802 7416 -1330 2096 -1593 C ATOM 887 CD LYS A 149 9.659 1.487 -26.307 1.00 84.78 C ANISOU 887 CD LYS A 149 11120 13009 8084 -1032 2228 -1843 C ATOM 888 CE LYS A 149 10.425 1.857 -25.050 1.00 84.64 C ANISOU 888 CE LYS A 149 10920 12878 8359 -803 2263 -1788 C ATOM 889 NZ LYS A 149 9.542 2.538 -24.061 1.00 82.75 N ANISOU 889 NZ LYS A 149 10721 12527 8192 -694 2131 -1584 N ATOM 890 N ALA A 150 7.893 5.638 -28.926 1.00 81.98 N ANISOU 890 N ALA A 150 11624 13006 6519 -2170 1669 -898 N ATOM 891 CA ALA A 150 8.473 6.674 -29.774 1.00 86.50 C ANISOU 891 CA ALA A 150 12332 13683 6850 -2496 1637 -736 C ATOM 892 C ALA A 150 9.142 7.769 -28.958 1.00 85.62 C ANISOU 892 C ALA A 150 12161 13512 6857 -2454 1657 -576 C ATOM 893 O ALA A 150 8.843 7.951 -27.780 1.00 82.29 O ANISOU 893 O ALA A 150 11658 12956 6651 -2212 1619 -499 O ATOM 894 CB ALA A 150 7.407 7.274 -30.670 1.00 91.09 C ANISOU 894 CB ALA A 150 13208 14265 7137 -2767 1330 -452 C ATOM 895 N VAL A 151 10.052 8.499 -29.594 1.00 87.39 N ANISOU 895 N VAL A 151 12428 13840 6936 -2708 1720 -532 N ATOM 896 CA VAL A 151 10.683 9.651 -28.964 1.00 83.74 C ANISOU 896 CA VAL A 151 11944 13325 6549 -2727 1714 -360 C ATOM 897 C VAL A 151 10.048 10.920 -29.508 1.00 84.63 C ANISOU 897 C VAL A 151 12346 13373 6436 -3001 1422 19 C ATOM 898 O VAL A 151 10.113 11.190 -30.702 1.00 86.96 O ANISOU 898 O VAL A 151 12805 13768 6467 -3317 1359 74 O ATOM 899 CB VAL A 151 12.204 9.691 -29.208 1.00 83.09 C ANISOU 899 CB VAL A 151 11701 13383 6486 -2825 1966 -560 C ATOM 900 CG1 VAL A 151 12.871 10.650 -28.231 1.00 79.21 C ANISOU 900 CG1 VAL A 151 11124 12816 6158 -2751 1985 -437 C ATOM 901 CG2 VAL A 151 12.802 8.298 -29.080 1.00 82.56 C ANISOU 901 CG2 VAL A 151 11383 13377 6610 -2608 2203 -934 C ATOM 902 N VAL A 152 9.424 11.692 -28.629 1.00 83.09 N ANISOU 902 N VAL A 152 12215 12991 6363 -2877 1226 285 N ATOM 903 CA VAL A 152 8.734 12.907 -29.039 1.00 85.56 C ANISOU 903 CA VAL A 152 12796 13168 6544 -3079 885 674 C ATOM 904 C VAL A 152 9.463 14.139 -28.527 1.00 86.79 C ANISOU 904 C VAL A 152 12959 13234 6782 -3138 880 841 C ATOM 905 O VAL A 152 9.905 14.178 -27.379 1.00 85.18 O ANISOU 905 O VAL A 152 12583 12976 6806 -2918 1022 772 O ATOM 906 CB VAL A 152 7.279 12.924 -28.527 1.00 83.65 C ANISOU 906 CB VAL A 152 12653 12725 6405 -2899 578 901 C ATOM 907 CG1 VAL A 152 6.546 14.168 -29.019 1.00 85.70 C ANISOU 907 CG1 VAL A 152 13169 12792 6601 -3073 169 1310 C ATOM 908 CG2 VAL A 152 6.553 11.663 -28.966 1.00 83.87 C ANISOU 908 CG2 VAL A 152 12664 12844 6359 -2838 585 718 C ATOM 909 N SER A 153 9.600 15.141 -29.387 1.00 91.36 N ANISOU 909 N SER A 153 13741 13796 7176 -3446 713 1052 N ATOM 910 CA SER A 153 10.148 16.422 -28.968 1.00 93.82 C ANISOU 910 CA SER A 153 14102 13985 7559 -3525 650 1247 C ATOM 911 C SER A 153 9.010 17.343 -28.553 1.00 93.75 C ANISOU 911 C SER A 153 14270 13662 7689 -3437 257 1621 C ATOM 912 O SER A 153 8.141 17.680 -29.363 1.00 96.02 O ANISOU 912 O SER A 153 14761 13852 7869 -3572 -54 1836 O ATOM 913 CB SER A 153 10.974 17.056 -30.086 1.00 99.82 C ANISOU 913 CB SER A 153 14983 14879 8066 -3914 679 1264 C ATOM 914 OG SER A 153 10.178 17.257 -31.241 1.00104.49 O ANISOU 914 OG SER A 153 15818 15447 8437 -4152 411 1445 O ATOM 915 N LEU A 154 9.009 17.734 -27.284 1.00 91.85 N ANISOU 915 N LEU A 154 13938 13247 7715 -3199 261 1690 N ATOM 916 CA LEU A 154 7.974 18.613 -26.762 1.00 92.65 C ANISOU 916 CA LEU A 154 14170 13006 8028 -3066 -106 2021 C ATOM 917 C LEU A 154 8.229 20.048 -27.206 1.00 98.44 C ANISOU 917 C LEU A 154 15086 13582 8734 -3292 -318 2268 C ATOM 918 O LEU A 154 9.317 20.365 -27.688 1.00101.86 O ANISOU 918 O LEU A 154 15528 14185 8989 -3540 -139 2178 O ATOM 919 CB LEU A 154 7.912 18.522 -25.239 1.00 87.35 C ANISOU 919 CB LEU A 154 13278 12160 7752 -2683 -18 1937 C ATOM 920 CG LEU A 154 7.651 17.120 -24.687 1.00 82.66 C ANISOU 920 CG LEU A 154 12414 11647 7346 -2355 175 1618 C ATOM 921 CD1 LEU A 154 7.531 17.165 -23.177 1.00 78.72 C ANISOU 921 CD1 LEU A 154 11684 10926 7299 -1960 219 1531 C ATOM 922 CD2 LEU A 154 6.402 16.519 -25.315 1.00 82.11 C ANISOU 922 CD2 LEU A 154 12409 11534 7254 -2299 -54 1666 C ATOM 923 N SER A 155 7.227 20.908 -27.039 1.00100.11 N ANISOU 923 N SER A 155 15428 13458 9149 -3195 -706 2564 N ATOM 924 CA SER A 155 7.292 22.283 -27.532 1.00104.74 C ANISOU 924 CA SER A 155 16205 13858 9735 -3395 -962 2806 C ATOM 925 C SER A 155 8.443 23.084 -26.922 1.00106.59 C ANISOU 925 C SER A 155 16403 14079 10018 -3467 -778 2776 C ATOM 926 O SER A 155 9.053 23.917 -27.597 1.00110.32 O ANISOU 926 O SER A 155 17011 14578 10327 -3758 -822 2856 O ATOM 927 CB SER A 155 5.968 23.002 -27.267 1.00104.42 C ANISOU 927 CB SER A 155 16243 13420 10011 -3186 -1401 3076 C ATOM 928 OG SER A 155 5.674 23.031 -25.885 1.00101.27 O ANISOU 928 OG SER A 155 15695 12806 9977 -2836 -1380 3063 O ATOM 929 N ASN A 156 8.738 22.827 -25.651 1.00103.62 N ANISOU 929 N ASN A 156 15846 13664 9860 -3218 -579 2659 N ATOM 930 CA ASN A 156 9.811 23.530 -24.953 1.00103.42 C ANISOU 930 CA ASN A 156 15763 13625 9908 -3265 -403 2616 C ATOM 931 C ASN A 156 11.201 23.082 -25.399 1.00104.00 C ANISOU 931 C ASN A 156 15729 14074 9714 -3497 -37 2362 C ATOM 932 O ASN A 156 12.194 23.751 -25.121 1.00104.84 O ANISOU 932 O ASN A 156 15807 14207 9820 -3618 84 2333 O ATOM 933 CB ASN A 156 9.673 23.338 -23.444 1.00100.35 C ANISOU 933 CB ASN A 156 15209 13080 9838 -2937 -305 2560 C ATOM 934 CG ASN A 156 9.834 21.892 -23.031 1.00 98.98 C ANISOU 934 CG ASN A 156 14797 13155 9656 -2753 -2 2264 C ATOM 935 OD1 ASN A 156 9.546 20.981 -23.807 1.00100.69 O ANISOU 935 OD1 ASN A 156 15017 13570 9672 -2809 39 2174 O ATOM 936 ND2 ASN A 156 10.301 21.671 -21.807 1.00 96.25 N ANISOU 936 ND2 ASN A 156 14206 12782 9582 -2492 202 2059 N ATOM 937 N GLY A 157 11.269 21.940 -26.076 1.00104.62 N ANISOU 937 N GLY A 157 15730 14429 9590 -3545 133 2160 N ATOM 938 CA GLY A 157 12.523 21.461 -26.627 1.00106.33 C ANISOU 938 CA GLY A 157 15825 14983 9592 -3746 458 1893 C ATOM 939 C GLY A 157 13.051 20.175 -26.017 1.00103.72 C ANISOU 939 C GLY A 157 15200 14867 9344 -3527 806 1551 C ATOM 940 O GLY A 157 13.994 19.580 -26.540 1.00105.89 O ANISOU 940 O GLY A 157 15341 15409 9484 -3645 1062 1293 O ATOM 941 N VAL A 158 12.457 19.734 -24.914 1.00100.88 N ANISOU 941 N VAL A 158 14729 14378 9224 -3204 809 1538 N ATOM 942 CA VAL A 158 12.923 18.511 -24.277 1.00 98.86 C ANISOU 942 CA VAL A 158 14186 14298 9077 -2975 1116 1211 C ATOM 943 C VAL A 158 12.408 17.292 -25.040 1.00 99.13 C ANISOU 943 C VAL A 158 14199 14487 8980 -2943 1164 1046 C ATOM 944 O VAL A 158 11.254 17.244 -25.471 1.00 98.99 O ANISOU 944 O VAL A 158 14356 14364 8891 -2950 926 1218 O ATOM 945 CB VAL A 158 12.501 18.435 -22.784 1.00 99.39 C ANISOU 945 CB VAL A 158 14142 14185 9438 -2661 1121 1237 C ATOM 946 CG1 VAL A 158 10.986 18.374 -22.639 1.00 98.23 C ANISOU 946 CG1 VAL A 158 14074 13757 9492 -2416 809 1388 C ATOM 947 CG2 VAL A 158 13.161 17.242 -22.097 1.00 96.99 C ANISOU 947 CG2 VAL A 158 13517 14054 9280 -2424 1431 881 C ATOM 948 N SER A 159 13.296 16.324 -25.236 1.00 97.42 N ANISOU 948 N SER A 159 13764 14502 8751 -2910 1452 711 N ATOM 949 CA SER A 159 12.941 15.072 -25.882 1.00 96.58 C ANISOU 949 CA SER A 159 13606 14532 8560 -2858 1533 501 C ATOM 950 C SER A 159 12.601 14.041 -24.821 1.00 91.39 C ANISOU 950 C SER A 159 12739 13828 8156 -2486 1641 322 C ATOM 951 O SER A 159 13.382 13.814 -23.898 1.00 90.62 O ANISOU 951 O SER A 159 12410 13738 8283 -2296 1815 159 O ATOM 952 CB SER A 159 14.084 14.570 -26.765 1.00 99.11 C ANISOU 952 CB SER A 159 13812 15094 8752 -3029 1763 232 C ATOM 953 OG SER A 159 14.580 15.608 -27.589 1.00102.42 O ANISOU 953 OG SER A 159 14399 15565 8952 -3385 1697 380 O ATOM 954 N VAL A 160 11.431 13.426 -24.942 1.00 85.18 N ANISOU 954 N VAL A 160 12034 12988 7341 -2387 1520 355 N ATOM 955 CA VAL A 160 11.030 12.398 -23.991 1.00 78.50 C ANISOU 955 CA VAL A 160 10994 12081 6750 -2036 1604 172 C ATOM 956 C VAL A 160 10.637 11.109 -24.701 1.00 78.59 C ANISOU 956 C VAL A 160 10983 12214 6665 -2007 1673 -50 C ATOM 957 O VAL A 160 9.960 11.128 -25.730 1.00 80.99 O ANISOU 957 O VAL A 160 11489 12556 6728 -2206 1520 56 O ATOM 958 CB VAL A 160 9.861 12.873 -23.098 1.00 76.06 C ANISOU 958 CB VAL A 160 10707 11421 6769 -1756 1300 396 C ATOM 959 CG1 VAL A 160 10.317 14.011 -22.196 1.00 76.37 C ANISOU 959 CG1 VAL A 160 10725 11309 6983 -1717 1260 549 C ATOM 960 CG2 VAL A 160 8.669 13.302 -23.940 1.00 77.92 C ANISOU 960 CG2 VAL A 160 11188 11550 6868 -1888 982 651 C ATOM 961 N LEU A 161 11.092 9.985 -24.163 1.00 74.86 N ANISOU 961 N LEU A 161 10259 11764 6422 -1747 1868 -352 N ATOM 962 CA LEU A 161 10.598 8.699 -24.614 1.00 71.27 C ANISOU 962 CA LEU A 161 9768 11346 5964 -1651 1903 -560 C ATOM 963 C LEU A 161 9.122 8.625 -24.263 1.00 66.59 C ANISOU 963 C LEU A 161 9270 10559 5471 -1499 1652 -396 C ATOM 964 O LEU A 161 8.732 8.924 -23.132 1.00 60.99 O ANISOU 964 O LEU A 161 8473 9618 5085 -1236 1533 -285 O ATOM 965 CB LEU A 161 11.364 7.548 -23.966 1.00 70.14 C ANISOU 965 CB LEU A 161 9341 11175 6135 -1354 2090 -865 C ATOM 966 CG LEU A 161 12.319 6.757 -24.859 1.00 75.18 C ANISOU 966 CG LEU A 161 9886 11944 6735 -1430 2246 -1113 C ATOM 967 CD1 LEU A 161 12.860 5.551 -24.107 1.00 75.15 C ANISOU 967 CD1 LEU A 161 9636 11844 7075 -1102 2347 -1351 C ATOM 968 CD2 LEU A 161 11.634 6.324 -26.147 1.00 77.36 C ANISOU 968 CD2 LEU A 161 10340 12321 6732 -1642 2199 -1149 C ATOM 969 N THR A 162 8.302 8.251 -25.239 1.00 67.09 N ANISOU 969 N THR A 162 9494 10670 5327 -1640 1527 -371 N ATOM 970 CA THR A 162 6.875 8.102 -25.008 1.00 65.23 C ANISOU 970 CA THR A 162 9306 10211 5266 -1466 1240 -221 C ATOM 971 C THR A 162 6.459 6.679 -25.338 1.00 65.07 C ANISOU 971 C THR A 162 9233 10249 5242 -1382 1317 -476 C ATOM 972 O THR A 162 6.987 6.058 -26.261 1.00 66.80 O ANISOU 972 O THR A 162 9496 10698 5185 -1584 1503 -689 O ATOM 973 CB THR A 162 6.054 9.102 -25.833 1.00 68.38 C ANISOU 973 CB THR A 162 9961 10560 5461 -1704 923 109 C ATOM 974 OG1 THR A 162 6.584 10.418 -25.645 1.00 69.08 O ANISOU 974 OG1 THR A 162 10123 10603 5521 -1825 871 329 O ATOM 975 CG2 THR A 162 4.615 9.100 -25.370 1.00 68.31 C ANISOU 975 CG2 THR A 162 9939 10290 5725 -1475 618 269 C ATOM 976 N SER A 163 5.512 6.166 -24.567 1.00 63.22 N ANISOU 976 N SER A 163 8904 9803 5312 -1096 1184 -467 N ATOM 977 CA SER A 163 5.150 4.765 -24.639 1.00 64.11 C ANISOU 977 CA SER A 163 8944 9927 5490 -975 1263 -716 C ATOM 978 C SER A 163 3.649 4.579 -24.469 1.00 61.91 C ANISOU 978 C SER A 163 8696 9458 5368 -853 982 -575 C ATOM 979 O SER A 163 3.056 5.124 -23.539 1.00 61.38 O ANISOU 979 O SER A 163 8561 9184 5577 -660 828 -401 O ATOM 980 CB SER A 163 5.911 3.983 -23.562 1.00 63.68 C ANISOU 980 CB SER A 163 8658 9820 5718 -700 1493 -953 C ATOM 981 OG SER A 163 5.681 2.592 -23.668 1.00 65.64 O ANISOU 981 OG SER A 163 8846 10067 6027 -596 1581 -1210 O ATOM 982 N LYS A 164 3.032 3.820 -25.370 1.00 61.94 N ANISOU 982 N LYS A 164 8795 9541 5198 -976 922 -665 N ATOM 983 CA LYS A 164 1.645 3.408 -25.172 1.00 60.81 C ANISOU 983 CA LYS A 164 8640 9235 5232 -848 688 -589 C ATOM 984 C LYS A 164 1.610 1.985 -24.618 1.00 58.30 C ANISOU 984 C LYS A 164 8180 8862 5111 -639 848 -870 C ATOM 985 O LYS A 164 2.018 1.039 -25.289 1.00 60.56 O ANISOU 985 O LYS A 164 8497 9285 5227 -737 1013 -1122 O ATOM 986 CB LYS A 164 0.848 3.506 -26.476 1.00 64.54 C ANISOU 986 CB LYS A 164 9313 9803 5405 -1121 463 -476 C ATOM 987 CG LYS A 164 -0.629 3.172 -26.325 1.00 64.34 C ANISOU 987 CG LYS A 164 9259 9619 5569 -1008 193 -382 C ATOM 988 CD LYS A 164 -1.446 3.766 -27.457 1.00 67.55 C ANISOU 988 CD LYS A 164 9861 10078 5727 -1268 -125 -151 C ATOM 989 CE LYS A 164 -0.922 3.329 -28.810 1.00 70.56 C ANISOU 989 CE LYS A 164 10440 10722 5649 -1610 -23 -289 C ATOM 990 NZ LYS A 164 -1.589 4.057 -29.923 1.00 73.26 N ANISOU 990 NZ LYS A 164 11007 11124 5704 -1907 -353 -21 N ATOM 991 N VAL A 165 1.126 1.838 -23.388 1.00 53.88 N ANISOU 991 N VAL A 165 7472 8095 4907 -362 802 -832 N ATOM 992 CA VAL A 165 1.183 0.551 -22.704 1.00 51.41 C ANISOU 992 CA VAL A 165 7033 7700 4802 -161 946 -1069 C ATOM 993 C VAL A 165 -0.137 -0.222 -22.770 1.00 53.37 C ANISOU 993 C VAL A 165 7288 7846 5145 -122 780 -1078 C ATOM 994 O VAL A 165 -0.177 -1.427 -22.506 1.00 54.64 O ANISOU 994 O VAL A 165 7394 7953 5413 -22 880 -1287 O ATOM 995 CB VAL A 165 1.579 0.728 -21.218 1.00 45.01 C ANISOU 995 CB VAL A 165 6062 6734 4308 96 1026 -1045 C ATOM 996 CG1 VAL A 165 2.986 1.292 -21.108 1.00 44.23 C ANISOU 996 CG1 VAL A 165 5929 6742 4135 65 1212 -1082 C ATOM 997 CG2 VAL A 165 0.575 1.618 -20.499 1.00 41.23 C ANISOU 997 CG2 VAL A 165 5552 6089 4025 191 810 -789 C ATOM 998 N LEU A 166 -1.215 0.469 -23.121 1.00 53.38 N ANISOU 998 N LEU A 166 7351 7811 5121 -204 515 -852 N ATOM 999 CA LEU A 166 -2.532 -0.155 -23.173 1.00 52.60 C ANISOU 999 CA LEU A 166 7234 7624 5129 -178 336 -843 C ATOM 1000 C LEU A 166 -3.447 0.599 -24.133 1.00 54.61 C ANISOU 1000 C LEU A 166 7601 7924 5223 -368 39 -623 C ATOM 1001 O LEU A 166 -3.562 1.823 -24.056 1.00 54.32 O ANISOU 1001 O LEU A 166 7579 7845 5215 -379 -110 -386 O ATOM 1002 CB LEU A 166 -3.152 -0.205 -21.771 1.00 49.99 C ANISOU 1002 CB LEU A 166 6732 7086 5176 77 306 -791 C ATOM 1003 CG LEU A 166 -4.520 -0.875 -21.602 1.00 50.45 C ANISOU 1003 CG LEU A 166 6728 7044 5397 121 150 -795 C ATOM 1004 CD1 LEU A 166 -4.469 -2.332 -22.040 1.00 52.17 C ANISOU 1004 CD1 LEU A 166 6993 7304 5526 66 257 -1044 C ATOM 1005 CD2 LEU A 166 -5.003 -0.773 -20.169 1.00 46.53 C ANISOU 1005 CD2 LEU A 166 6065 6369 5246 342 160 -745 C ATOM 1006 N ASP A 167 -4.091 -0.133 -25.039 1.00 56.04 N ANISOU 1006 N ASP A 167 7870 8181 5243 -522 -63 -699 N ATOM 1007 CA ASP A 167 -5.047 0.464 -25.966 1.00 57.84 C ANISOU 1007 CA ASP A 167 8203 8446 5325 -708 -387 -487 C ATOM 1008 C ASP A 167 -6.465 -0.019 -25.649 1.00 57.68 C ANISOU 1008 C ASP A 167 8066 8300 5550 -611 -592 -457 C ATOM 1009 O ASP A 167 -6.891 -1.081 -26.104 1.00 57.54 O ANISOU 1009 O ASP A 167 8081 8329 5453 -693 -593 -618 O ATOM 1010 CB ASP A 167 -4.678 0.125 -27.413 1.00 60.25 C ANISOU 1010 CB ASP A 167 8728 8974 5192 -1027 -373 -579 C ATOM 1011 CG ASP A 167 -5.402 0.999 -28.424 1.00 63.17 C ANISOU 1011 CG ASP A 167 9251 9400 5352 -1262 -723 -306 C ATOM 1012 OD1 ASP A 167 -6.393 1.657 -28.047 1.00 63.13 O ANISOU 1012 OD1 ASP A 167 9154 9243 5590 -1152 -1005 -76 O ATOM 1013 OD2 ASP A 167 -4.983 1.024 -29.602 1.00 65.95 O ANISOU 1013 OD2 ASP A 167 9814 9948 5297 -1564 -723 -326 O ATOM 1014 N LEU A 168 -7.188 0.765 -24.858 1.00 55.68 N ANISOU 1014 N LEU A 168 7668 7887 5601 -442 -756 -267 N ATOM 1015 CA LEU A 168 -8.560 0.422 -24.510 1.00 53.86 C ANISOU 1015 CA LEU A 168 7290 7546 5629 -352 -946 -238 C ATOM 1016 C LEU A 168 -9.507 0.929 -25.584 1.00 58.04 C ANISOU 1016 C LEU A 168 7895 8120 6038 -535 -1316 -42 C ATOM 1017 O LEU A 168 -10.583 0.369 -25.788 1.00 59.73 O ANISOU 1017 O LEU A 168 8038 8318 6338 -563 -1487 -62 O ATOM 1018 CB LEU A 168 -8.939 0.998 -23.142 1.00 49.18 C ANISOU 1018 CB LEU A 168 6483 6769 5434 -91 -933 -159 C ATOM 1019 CG LEU A 168 -8.392 0.228 -21.936 1.00 44.84 C ANISOU 1019 CG LEU A 168 5831 6150 5055 91 -623 -355 C ATOM 1020 CD1 LEU A 168 -8.758 0.904 -20.622 1.00 40.94 C ANISOU 1020 CD1 LEU A 168 5150 5495 4910 309 -610 -274 C ATOM 1021 CD2 LEU A 168 -8.906 -1.200 -21.967 1.00 45.61 C ANISOU 1021 CD2 LEU A 168 5905 6254 5170 64 -569 -550 C ATOM 1022 N LYS A 169 -9.100 1.994 -26.266 1.00 60.02 N ANISOU 1022 N LYS A 169 8292 8422 6089 -671 -1453 156 N ATOM 1023 CA LYS A 169 -9.873 2.524 -27.378 1.00 64.21 C ANISOU 1023 CA LYS A 169 8938 8998 6461 -877 -1834 371 C ATOM 1024 C LYS A 169 -10.085 1.449 -28.434 1.00 66.75 C ANISOU 1024 C LYS A 169 9402 9490 6470 -1121 -1860 225 C ATOM 1025 O LYS A 169 -11.202 1.221 -28.880 1.00 66.87 O ANISOU 1025 O LYS A 169 9382 9497 6527 -1191 -2142 290 O ATOM 1026 CB LYS A 169 -9.179 3.741 -27.992 1.00 65.93 C ANISOU 1026 CB LYS A 169 9347 9257 6445 -1033 -1937 596 C ATOM 1027 CG LYS A 169 -9.803 4.203 -29.290 1.00 70.11 C ANISOU 1027 CG LYS A 169 10061 9858 6722 -1307 -2332 823 C ATOM 1028 CD LYS A 169 -9.233 5.533 -29.747 1.00 72.25 C ANISOU 1028 CD LYS A 169 10513 10118 6820 -1445 -2476 1092 C ATOM 1029 CE LYS A 169 -9.477 5.735 -31.231 1.00 77.44 C ANISOU 1029 CE LYS A 169 11444 10919 7060 -1818 -2785 1269 C ATOM 1030 NZ LYS A 169 -10.822 5.233 -31.635 1.00 79.30 N ANISOU 1030 NZ LYS A 169 11604 11133 7393 -1840 -3111 1306 N ATOM 1031 N ASN A 170 -9.001 0.779 -28.811 1.00 67.41 N ANISOU 1031 N ASN A 170 9632 9725 6254 -1247 -1558 8 N ATOM 1032 CA ASN A 170 -9.063 -0.277 -29.809 1.00 68.54 C ANISOU 1032 CA ASN A 170 9926 10033 6082 -1487 -1530 -181 C ATOM 1033 C ASN A 170 -9.914 -1.450 -29.347 1.00 65.88 C ANISOU 1033 C ASN A 170 9436 9617 5980 -1368 -1514 -363 C ATOM 1034 O ASN A 170 -10.760 -1.927 -30.098 1.00 66.95 O ANISOU 1034 O ASN A 170 9628 9811 6000 -1538 -1729 -367 O ATOM 1035 CB ASN A 170 -7.656 -0.764 -30.169 1.00 69.26 C ANISOU 1035 CB ASN A 170 10162 10286 5867 -1605 -1161 -425 C ATOM 1036 CG ASN A 170 -7.673 -1.977 -31.084 1.00 72.41 C ANISOU 1036 CG ASN A 170 10700 10837 5978 -1824 -1075 -688 C ATOM 1037 OD1 ASN A 170 -7.824 -1.852 -32.301 1.00 74.66 O ANISOU 1037 OD1 ASN A 170 11196 11285 5887 -2141 -1237 -631 O ATOM 1038 ND2 ASN A 170 -7.510 -3.161 -30.500 1.00 72.19 N ANISOU 1038 ND2 ASN A 170 10565 10745 6119 -1668 -827 -978 N ATOM 1039 N TYR A 171 -9.699 -1.912 -28.117 1.00 63.00 N ANISOU 1039 N TYR A 171 8888 9118 5931 -1097 -1273 -504 N ATOM 1040 CA TYR A 171 -10.459 -3.056 -27.617 1.00 62.02 C ANISOU 1040 CA TYR A 171 8632 8909 6024 -1002 -1240 -674 C ATOM 1041 C TYR A 171 -11.955 -2.754 -27.574 1.00 63.15 C ANISOU 1041 C TYR A 171 8631 8975 6389 -986 -1591 -492 C ATOM 1042 O TYR A 171 -12.766 -3.511 -28.104 1.00 64.80 O ANISOU 1042 O TYR A 171 8853 9224 6546 -1118 -1732 -563 O ATOM 1043 CB TYR A 171 -9.990 -3.486 -26.221 1.00 58.03 C ANISOU 1043 CB TYR A 171 7966 8259 5823 -726 -951 -811 C ATOM 1044 CG TYR A 171 -10.754 -4.699 -25.734 1.00 57.05 C ANISOU 1044 CG TYR A 171 7738 8044 5897 -666 -919 -976 C ATOM 1045 CD1 TYR A 171 -10.394 -5.975 -26.149 1.00 58.04 C ANISOU 1045 CD1 TYR A 171 7976 8211 5867 -764 -755 -1242 C ATOM 1046 CD2 TYR A 171 -11.863 -4.568 -24.904 1.00 53.95 C ANISOU 1046 CD2 TYR A 171 7134 7523 5842 -532 -1055 -876 C ATOM 1047 CE1 TYR A 171 -11.099 -7.088 -25.734 1.00 57.37 C ANISOU 1047 CE1 TYR A 171 7817 8026 5954 -733 -741 -1383 C ATOM 1048 CE2 TYR A 171 -12.577 -5.675 -24.488 1.00 54.03 C ANISOU 1048 CE2 TYR A 171 7058 7460 6012 -516 -1025 -1021 C ATOM 1049 CZ TYR A 171 -12.189 -6.933 -24.906 1.00 55.39 C ANISOU 1049 CZ TYR A 171 7367 7661 6020 -620 -877 -1263 C ATOM 1050 OH TYR A 171 -12.886 -8.044 -24.498 1.00 54.73 O ANISOU 1050 OH TYR A 171 7218 7486 6092 -621 -856 -1399 O ATOM 1051 N ILE A 172 -12.311 -1.648 -26.934 1.00 62.62 N ANISOU 1051 N ILE A 172 8415 8794 6585 -821 -1728 -273 N ATOM 1052 CA ILE A 172 -13.706 -1.257 -26.800 1.00 64.63 C ANISOU 1052 CA ILE A 172 8482 8961 7113 -768 -2053 -111 C ATOM 1053 C ILE A 172 -14.371 -1.047 -28.160 1.00 70.17 C ANISOU 1053 C ILE A 172 9316 9773 7573 -1028 -2426 36 C ATOM 1054 O ILE A 172 -15.498 -1.485 -28.378 1.00 72.54 O ANISOU 1054 O ILE A 172 9508 10069 7985 -1079 -2646 37 O ATOM 1055 CB ILE A 172 -13.835 0.023 -25.954 1.00 62.95 C ANISOU 1055 CB ILE A 172 8102 8601 7214 -547 -2127 85 C ATOM 1056 CG1 ILE A 172 -13.452 -0.271 -24.500 1.00 59.43 C ANISOU 1056 CG1 ILE A 172 7496 8042 7043 -300 -1795 -63 C ATOM 1057 CG2 ILE A 172 -15.241 0.577 -26.033 1.00 63.89 C ANISOU 1057 CG2 ILE A 172 8031 8640 7606 -508 -2504 261 C ATOM 1058 CD1 ILE A 172 -13.403 0.952 -23.613 1.00 57.62 C ANISOU 1058 CD1 ILE A 172 7127 7674 7091 -92 -1807 85 C ATOM 1059 N ASP A 173 -13.663 -0.403 -29.084 1.00 72.93 N ANISOU 1059 N ASP A 173 9906 10231 7575 -1217 -2498 160 N ATOM 1060 CA ASP A 173 -14.231 -0.096 -30.397 1.00 77.89 C ANISOU 1060 CA ASP A 173 10696 10966 7932 -1495 -2880 337 C ATOM 1061 C ASP A 173 -14.390 -1.335 -31.279 1.00 79.32 C ANISOU 1061 C ASP A 173 11027 11307 7804 -1749 -2856 131 C ATOM 1062 O ASP A 173 -15.299 -1.396 -32.098 1.00 82.27 O ANISOU 1062 O ASP A 173 11440 11738 8080 -1935 -3201 236 O ATOM 1063 CB ASP A 173 -13.375 0.948 -31.126 1.00 80.94 C ANISOU 1063 CB ASP A 173 11328 11428 7996 -1664 -2950 534 C ATOM 1064 CG ASP A 173 -13.492 2.341 -30.514 1.00 82.41 C ANISOU 1064 CG ASP A 173 11395 11436 8482 -1466 -3117 804 C ATOM 1065 OD1 ASP A 173 -14.158 2.489 -29.465 1.00 81.32 O ANISOU 1065 OD1 ASP A 173 10971 11124 8802 -1181 -3132 805 O ATOM 1066 OD2 ASP A 173 -12.903 3.289 -31.078 1.00 84.50 O ANISOU 1066 OD2 ASP A 173 11856 11732 8517 -1607 -3221 1004 O ATOM 1067 N LYS A 174 -13.516 -2.320 -31.110 1.00 78.81 N ANISOU 1067 N LYS A 174 11040 11304 7600 -1754 -2462 -166 N ATOM 1068 CA LYS A 174 -13.528 -3.496 -31.978 1.00 81.82 C ANISOU 1068 CA LYS A 174 11588 11829 7670 -2001 -2403 -398 C ATOM 1069 C LYS A 174 -14.258 -4.694 -31.374 1.00 81.40 C ANISOU 1069 C LYS A 174 11364 11685 7880 -1891 -2327 -608 C ATOM 1070 O LYS A 174 -14.684 -5.589 -32.100 1.00 83.88 O ANISOU 1070 O LYS A 174 11779 12085 8007 -2100 -2395 -751 O ATOM 1071 CB LYS A 174 -12.097 -3.905 -32.338 1.00 83.17 C ANISOU 1071 CB LYS A 174 11967 12128 7504 -2109 -2026 -629 C ATOM 1072 CG LYS A 174 -11.290 -2.820 -33.041 1.00 86.05 C ANISOU 1072 CG LYS A 174 12534 12620 7543 -2284 -2064 -450 C ATOM 1073 CD LYS A 174 -11.900 -2.434 -34.379 1.00 91.44 C ANISOU 1073 CD LYS A 174 13428 13446 7869 -2635 -2446 -257 C ATOM 1074 CE LYS A 174 -11.124 -1.295 -35.026 1.00 93.31 C ANISOU 1074 CE LYS A 174 13879 13793 7783 -2829 -2501 -45 C ATOM 1075 NZ LYS A 174 -9.684 -1.635 -35.196 1.00 93.04 N ANISOU 1075 NZ LYS A 174 13982 13905 7465 -2918 -2054 -305 N ATOM 1076 N GLN A 175 -14.408 -4.717 -30.055 1.00 78.40 N ANISOU 1076 N GLN A 175 10739 11133 7917 -1589 -2186 -628 N ATOM 1077 CA GLN A 175 -15.028 -5.861 -29.394 1.00 78.34 C ANISOU 1077 CA GLN A 175 10581 11030 8152 -1499 -2086 -823 C ATOM 1078 C GLN A 175 -16.338 -5.506 -28.702 1.00 77.73 C ANISOU 1078 C GLN A 175 10217 10838 8479 -1358 -2324 -667 C ATOM 1079 O GLN A 175 -17.214 -6.355 -28.543 1.00 78.90 O ANISOU 1079 O GLN A 175 10255 10955 8769 -1392 -2378 -772 O ATOM 1080 CB GLN A 175 -14.064 -6.469 -28.371 1.00 77.45 C ANISOU 1080 CB GLN A 175 10436 10818 8172 -1295 -1673 -1033 C ATOM 1081 CG GLN A 175 -12.717 -6.870 -28.942 1.00 80.25 C ANISOU 1081 CG GLN A 175 11023 11276 8193 -1396 -1401 -1229 C ATOM 1082 CD GLN A 175 -12.664 -8.329 -29.345 1.00 83.68 C ANISOU 1082 CD GLN A 175 11569 11728 8500 -1522 -1261 -1536 C ATOM 1083 OE1 GLN A 175 -13.694 -8.951 -29.617 1.00 86.04 O ANISOU 1083 OE1 GLN A 175 11841 12016 8835 -1634 -1440 -1569 O ATOM 1084 NE2 GLN A 175 -11.459 -8.888 -29.376 1.00 83.79 N ANISOU 1084 NE2 GLN A 175 11696 11757 8382 -1500 -942 -1774 N ATOM 1085 N LEU A 176 -16.474 -4.252 -28.292 1.00 77.28 N ANISOU 1085 N LEU A 176 10031 10715 8617 -1207 -2459 -431 N ATOM 1086 CA LEU A 176 -17.584 -3.863 -27.428 1.00 77.72 C ANISOU 1086 CA LEU A 176 9771 10644 9113 -1022 -2609 -327 C ATOM 1087 C LEU A 176 -18.574 -2.909 -28.092 1.00 84.65 C ANISOU 1087 C LEU A 176 10563 11536 10066 -1086 -3067 -66 C ATOM 1088 O LEU A 176 -19.694 -2.748 -27.612 1.00 84.79 O ANISOU 1088 O LEU A 176 10299 11475 10441 -979 -3242 -12 O ATOM 1089 CB LEU A 176 -17.043 -3.232 -26.141 1.00 72.22 C ANISOU 1089 CB LEU A 176 8936 9816 8690 -740 -2371 -304 C ATOM 1090 CG LEU A 176 -16.793 -4.139 -24.932 1.00 67.91 C ANISOU 1090 CG LEU A 176 8290 9180 8333 -590 -2018 -521 C ATOM 1091 CD1 LEU A 176 -16.184 -5.470 -25.320 1.00 66.25 C ANISOU 1091 CD1 LEU A 176 8280 9029 7863 -729 -1809 -758 C ATOM 1092 CD2 LEU A 176 -15.900 -3.432 -23.934 1.00 65.28 C ANISOU 1092 CD2 LEU A 176 7922 8758 8125 -374 -1784 -487 C ATOM 1093 N LEU A 177 -18.159 -2.268 -29.181 1.00 90.50 N ANISOU 1093 N LEU A 177 11538 12372 10478 -1266 -3265 96 N ATOM 1094 CA LEU A 177 -19.035 -1.336 -29.891 1.00 97.11 C ANISOU 1094 CA LEU A 177 12327 13205 11363 -1344 -3746 375 C ATOM 1095 C LEU A 177 -20.336 -1.976 -30.386 1.00102.75 C ANISOU 1095 C LEU A 177 12918 13968 12153 -1480 -4048 359 C ATOM 1096 O LEU A 177 -21.401 -1.401 -30.181 1.00102.48 O ANISOU 1096 O LEU A 177 12621 13849 12468 -1372 -4356 509 O ATOM 1097 CB LEU A 177 -18.308 -0.684 -31.075 1.00 99.62 C ANISOU 1097 CB LEU A 177 12980 13636 11235 -1583 -3903 549 C ATOM 1098 CG LEU A 177 -17.692 0.699 -30.859 1.00 99.80 C ANISOU 1098 CG LEU A 177 13044 13565 11310 -1464 -3946 779 C ATOM 1099 CD1 LEU A 177 -17.411 1.364 -32.205 1.00103.24 C ANISOU 1099 CD1 LEU A 177 13792 14113 11323 -1766 -4249 1013 C ATOM 1100 CD2 LEU A 177 -18.593 1.566 -29.997 1.00 99.73 C ANISOU 1100 CD2 LEU A 177 12702 13354 11839 -1178 -4149 931 C ATOM 1101 N PRO A 178 -20.265 -3.153 -31.040 1.00108.45 N ANISOU 1101 N PRO A 178 13816 14824 12566 -1718 -3966 165 N ATOM 1102 CA PRO A 178 -21.524 -3.737 -31.521 1.00114.46 C ANISOU 1102 CA PRO A 178 14458 15636 13397 -1867 -4273 155 C ATOM 1103 C PRO A 178 -22.539 -4.005 -30.417 1.00117.40 C ANISOU 1103 C PRO A 178 14434 15888 14283 -1648 -4246 81 C ATOM 1104 O PRO A 178 -23.738 -3.834 -30.631 1.00120.21 O ANISOU 1104 O PRO A 178 14572 16241 14860 -1677 -4604 187 O ATOM 1105 CB PRO A 178 -21.077 -5.054 -32.158 1.00114.27 C ANISOU 1105 CB PRO A 178 14693 15745 12980 -2120 -4070 -106 C ATOM 1106 CG PRO A 178 -19.668 -4.826 -32.526 1.00112.73 C ANISOU 1106 CG PRO A 178 14803 15617 12412 -2185 -3822 -139 C ATOM 1107 CD PRO A 178 -19.107 -3.968 -31.452 1.00108.88 C ANISOU 1107 CD PRO A 178 14175 14991 12205 -1875 -3629 -54 C ATOM 1108 N ILE A 179 -22.061 -4.408 -29.246 1.00119.40 N ANISOU 1108 N ILE A 179 14592 16050 14725 -1445 -3833 -98 N ATOM 1109 CA ILE A 179 -22.960 -4.809 -28.176 1.00121.82 C ANISOU 1109 CA ILE A 179 14555 16266 15465 -1288 -3750 -203 C ATOM 1110 C ILE A 179 -23.664 -3.603 -27.542 1.00125.38 C ANISOU 1110 C ILE A 179 14678 16607 16355 -1052 -3941 -20 C ATOM 1111 O ILE A 179 -24.754 -3.748 -27.005 1.00127.68 O ANISOU 1111 O ILE A 179 14643 16861 17009 -981 -4025 -61 O ATOM 1112 CB ILE A 179 -22.206 -5.647 -27.099 1.00139.77 C ANISOU 1112 CB ILE A 179 16858 18470 17780 -1169 -3258 -441 C ATOM 1113 CG1 ILE A 179 -22.072 -4.889 -25.781 1.00137.17 C ANISOU 1113 CG1 ILE A 179 16303 18006 17807 -872 -3071 -400 C ATOM 1114 CG2 ILE A 179 -20.856 -6.120 -27.631 1.00137.94 C ANISOU 1114 CG2 ILE A 179 16994 18299 17119 -1279 -3021 -551 C ATOM 1115 CD1 ILE A 179 -22.811 -5.542 -24.629 1.00136.34 C ANISOU 1115 CD1 ILE A 179 15924 17832 18047 -780 -2893 -552 C ATOM 1116 N VAL A 180 -23.067 -2.415 -27.617 1.00127.21 N ANISOU 1116 N VAL A 180 14987 16783 16565 -940 -4012 169 N ATOM 1117 CA VAL A 180 -23.778 -1.211 -27.174 1.00128.84 C ANISOU 1117 CA VAL A 180 14896 16865 17192 -725 -4250 347 C ATOM 1118 C VAL A 180 -23.440 0.053 -27.959 1.00130.22 C ANISOU 1118 C VAL A 180 15229 17007 17243 -740 -4569 633 C ATOM 1119 O VAL A 180 -22.869 1.006 -27.427 1.00129.91 O ANISOU 1119 O VAL A 180 15185 16851 17323 -554 -4476 724 O ATOM 1120 CB VAL A 180 -23.548 -0.911 -25.682 1.00126.77 C ANISOU 1120 CB VAL A 180 14420 16472 17276 -439 -3899 242 C ATOM 1121 CG1 VAL A 180 -24.723 -1.426 -24.841 1.00127.06 C ANISOU 1121 CG1 VAL A 180 14074 16483 17721 -357 -3851 90 C ATOM 1122 CG2 VAL A 180 -22.223 -1.475 -25.198 1.00123.10 C ANISOU 1122 CG2 VAL A 180 14202 16020 16549 -431 -3446 90 C ATOM 1123 N ASN A 181 -23.800 0.037 -29.235 1.00130.52 N ANISOU 1123 N ASN A 181 15423 17145 17026 -986 -4955 778 N ATOM 1124 CA ASN A 181 -23.978 1.252 -30.013 1.00131.34 C ANISOU 1124 CA ASN A 181 15592 17193 17117 -1016 -5408 1094 C ATOM 1125 C ASN A 181 -25.340 1.111 -30.678 1.00133.68 C ANISOU 1125 C ASN A 181 15705 17523 17563 -1121 -5851 1181 C ATOM 1126 O ASN A 181 -25.760 1.947 -31.476 1.00137.57 O ANISOU 1126 O ASN A 181 16269 17960 18039 -1149 -6125 1407 O ATOM 1127 CB ASN A 181 -22.862 1.445 -31.043 1.00131.85 C ANISOU 1127 CB ASN A 181 16117 17364 16614 -1265 -5419 1213 C ATOM 1128 CG ASN A 181 -22.266 2.844 -31.005 1.00131.72 C ANISOU 1128 CG ASN A 181 16196 17217 16635 -1153 -5526 1461 C ATOM 1129 OD1 ASN A 181 -22.828 3.753 -30.396 1.00132.11 O ANISOU 1129 OD1 ASN A 181 15974 17081 17142 -900 -5695 1580 O ATOM 1130 ND2 ASN A 181 -21.125 3.021 -31.664 1.00131.36 N ANISOU 1130 ND2 ASN A 181 16533 17264 16112 -1350 -5423 1526 N ATOM 1131 N LYS A 182 -26.019 0.023 -30.320 1.00131.33 N ANISOU 1131 N LYS A 182 15201 17297 17401 -1155 -5754 959 N ATOM 1132 CA LYS A 182 -27.322 -0.330 -30.869 1.00133.18 C ANISOU 1132 CA LYS A 182 15263 17581 17759 -1248 -6005 966 C ATOM 1133 C LYS A 182 -28.287 -0.726 -29.754 1.00131.60 C ANISOU 1133 C LYS A 182 14604 17328 18070 -1055 -5870 777 C ATOM 1134 O LYS A 182 -27.904 -1.439 -28.826 1.00128.21 O ANISOU 1134 O LYS A 182 14097 16904 17711 -1004 -5535 557 O ATOM 1135 CB LYS A 182 -27.193 -1.483 -31.866 1.00133.18 C ANISOU 1135 CB LYS A 182 15548 17777 17277 -1609 -6046 870 C ATOM 1136 CG LYS A 182 -26.127 -1.295 -32.933 1.00132.48 C ANISOU 1136 CG LYS A 182 15938 17782 16616 -1846 -6074 986 C ATOM 1137 CD LYS A 182 -26.019 -2.537 -33.798 1.00132.46 C ANISOU 1137 CD LYS A 182 16197 17970 16162 -2188 -6032 819 C ATOM 1138 CE LYS A 182 -27.374 -2.916 -34.374 1.00135.20 C ANISOU 1138 CE LYS A 182 16375 18360 16637 -2282 -6294 833 C ATOM 1139 NZ LYS A 182 -27.330 -4.224 -35.079 1.00135.57 N1+ ANISOU 1139 NZ LYS A 182 16643 18573 16295 -2597 -6216 628 N1+ ATOM 1140 N GLN A 183 -29.535 -0.276 -29.857 1.00133.64 N ANISOU 1140 N GLN A 183 14584 17532 18660 -954 -6072 849 N ATOM 1141 CA GLN A 183 -30.562 -0.585 -28.862 1.00132.10 C ANISOU 1141 CA GLN A 183 13946 17309 18939 -792 -5931 667 C ATOM 1142 C GLN A 183 -30.736 -2.089 -28.666 1.00129.14 C ANISOU 1142 C GLN A 183 13529 17077 18460 -995 -5773 421 C ATOM 1143 O GLN A 183 -30.756 -2.574 -27.534 1.00126.44 O ANISOU 1143 O GLN A 183 12969 16712 18361 -898 -5470 216 O ATOM 1144 CB GLN A 183 -31.897 0.050 -29.256 1.00136.89 C ANISOU 1144 CB GLN A 183 14304 17867 19842 -712 -6219 783 C ATOM 1145 CG GLN A 183 -32.092 1.461 -28.719 1.00138.10 C ANISOU 1145 CG GLN A 183 14285 17814 20374 -402 -6232 896 C ATOM 1146 CD GLN A 183 -33.122 2.252 -29.507 1.00143.91 C ANISOU 1146 CD GLN A 183 14923 18476 21279 -372 -6619 1082 C ATOM 1147 OE1 GLN A 183 -34.327 2.146 -29.267 1.00146.63 O ANISOU 1147 OE1 GLN A 183 14923 18830 21960 -302 -6678 994 O ATOM 1148 NE2 GLN A 183 -32.649 3.050 -30.457 1.00145.72 N ANISOU 1148 NE2 GLN A 183 15461 18633 21275 -437 -6885 1340 N ATOM 1149 N SER A 184 -30.861 -2.826 -29.765 1.00129.01 N ANISOU 1149 N SER A 184 13740 17200 18079 -1292 -5963 435 N ATOM 1150 CA SER A 184 -30.900 -4.283 -29.692 1.00125.29 C ANISOU 1150 CA SER A 184 13309 16847 17450 -1522 -5815 198 C ATOM 1151 C SER A 184 -29.485 -4.848 -29.722 1.00119.64 C ANISOU 1151 C SER A 184 12991 16155 16313 -1641 -5548 99 C ATOM 1152 O SER A 184 -28.907 -5.066 -30.788 1.00120.31 O ANISOU 1152 O SER A 184 13453 16333 15929 -1871 -5658 154 O ATOM 1153 CB SER A 184 -31.736 -4.871 -30.828 1.00128.76 C ANISOU 1153 CB SER A 184 13816 17419 17687 -1783 -6084 218 C ATOM 1154 OG SER A 184 -33.070 -5.094 -30.405 1.00130.79 O ANISOU 1154 OG SER A 184 13664 17691 18340 -1723 -6123 137 O ATOM 1155 N CYS A 185 -28.943 -5.080 -28.532 1.00113.78 N ANISOU 1155 N CYS A 185 12196 15328 15708 -1454 -5076 -66 N ATOM 1156 CA CYS A 185 -27.567 -5.522 -28.359 1.00109.29 C ANISOU 1156 CA CYS A 185 11991 14748 14786 -1466 -4667 -178 C ATOM 1157 C CYS A 185 -27.298 -6.903 -28.943 1.00106.73 C ANISOU 1157 C CYS A 185 11945 14523 14084 -1745 -4540 -369 C ATOM 1158 O CYS A 185 -28.083 -7.831 -28.758 1.00107.77 O ANISOU 1158 O CYS A 185 11930 14683 14335 -1857 -4525 -519 O ATOM 1159 CB CYS A 185 -27.210 -5.533 -26.871 1.00107.54 C ANISOU 1159 CB CYS A 185 11609 14410 14843 -1214 -4228 -313 C ATOM 1160 SG CYS A 185 -27.638 -4.016 -25.996 1.00105.20 S ANISOU 1160 SG CYS A 185 10938 13982 15052 -877 -4318 -160 S ATOM 1161 N SER A 186 -26.180 -7.033 -29.646 1.00101.92 N ANISOU 1161 N SER A 186 11735 13965 13026 -1863 -4438 -377 N ATOM 1162 CA SER A 186 -25.662 -8.347 -29.984 1.00 97.00 C ANISOU 1162 CA SER A 186 11388 13396 12071 -2069 -4202 -614 C ATOM 1163 C SER A 186 -24.927 -8.877 -28.753 1.00 88.13 C ANISOU 1163 C SER A 186 10259 12152 11075 -1879 -3712 -802 C ATOM 1164 O SER A 186 -23.919 -8.314 -28.335 1.00 83.92 O ANISOU 1164 O SER A 186 9824 11562 10501 -1706 -3494 -765 O ATOM 1165 CB SER A 186 -24.738 -8.281 -31.199 1.00 97.83 C ANISOU 1165 CB SER A 186 11902 13611 11656 -2273 -4256 -583 C ATOM 1166 OG SER A 186 -24.555 -9.567 -31.761 1.00 98.77 O ANISOU 1166 OG SER A 186 12254 13798 11474 -2520 -4134 -821 O ATOM 1167 N ILE A 187 -25.451 -9.946 -28.165 1.00 88.54 N ANISOU 1167 N ILE A 187 10197 12162 11284 -1925 -3558 -990 N ATOM 1168 CA ILE A 187 -24.956 -10.455 -26.888 1.00 82.91 C ANISOU 1168 CA ILE A 187 9442 11319 10742 -1756 -3144 -1139 C ATOM 1169 C ILE A 187 -23.546 -11.037 -26.991 1.00 78.56 C ANISOU 1169 C ILE A 187 9242 10730 9877 -1761 -2829 -1285 C ATOM 1170 O ILE A 187 -23.299 -11.956 -27.763 1.00 68.03 O ANISOU 1170 O ILE A 187 8150 9439 8260 -1968 -2814 -1435 O ATOM 1171 CB ILE A 187 -25.914 -11.523 -26.328 1.00 82.18 C ANISOU 1171 CB ILE A 187 9170 11192 10864 -1859 -3087 -1294 C ATOM 1172 CG1 ILE A 187 -27.306 -10.914 -26.138 1.00 71.52 C ANISOU 1172 CG1 ILE A 187 7416 9887 9873 -1835 -3371 -1174 C ATOM 1173 CG2 ILE A 187 -25.377 -12.096 -25.023 1.00 66.43 C ANISOU 1173 CG2 ILE A 187 7175 9055 9011 -1719 -2677 -1431 C ATOM 1174 CD1 ILE A 187 -28.371 -11.910 -25.763 1.00 80.85 C ANISOU 1174 CD1 ILE A 187 8401 11073 11246 -1990 -3364 -1316 C ATOM 1175 N PRO A 188 -22.612 -10.498 -26.201 1.00 63.81 N ANISOU 1175 N PRO A 188 7392 8780 8073 -1531 -2575 -1254 N ATOM 1176 CA PRO A 188 -21.217 -10.949 -26.257 1.00 68.00 C ANISOU 1176 CA PRO A 188 8217 9275 8346 -1505 -2282 -1388 C ATOM 1177 C PRO A 188 -21.025 -12.324 -25.624 1.00 67.89 C ANISOU 1177 C PRO A 188 8272 9142 8380 -1529 -2012 -1622 C ATOM 1178 O PRO A 188 -21.781 -12.695 -24.727 1.00 60.70 O ANISOU 1178 O PRO A 188 7161 8153 7752 -1494 -1968 -1644 O ATOM 1179 CB PRO A 188 -20.473 -9.874 -25.463 1.00 63.96 C ANISOU 1179 CB PRO A 188 7637 8706 7959 -1245 -2134 -1260 C ATOM 1180 CG PRO A 188 -21.488 -9.386 -24.479 1.00 62.89 C ANISOU 1180 CG PRO A 188 7159 8511 8227 -1110 -2198 -1164 C ATOM 1181 CD PRO A 188 -22.825 -9.464 -25.175 1.00 65.22 C ANISOU 1181 CD PRO A 188 7302 8891 8588 -1282 -2544 -1112 C ATOM 1182 N ASN A 189 -20.034 -13.071 -26.100 1.00 67.89 N ANISOU 1182 N ASN A 189 8554 9128 8115 -1596 -1837 -1799 N ATOM 1183 CA ASN A 189 -19.696 -14.357 -25.508 1.00 60.24 C ANISOU 1183 CA ASN A 189 7680 8007 7202 -1594 -1589 -2017 C ATOM 1184 C ASN A 189 -19.101 -14.161 -24.114 1.00 62.39 C ANISOU 1184 C ASN A 189 7861 8137 7709 -1339 -1333 -1985 C ATOM 1185 O ASN A 189 -18.617 -13.080 -23.784 1.00 55.48 O ANISOU 1185 O ASN A 189 6917 7291 6873 -1168 -1298 -1840 O ATOM 1186 CB ASN A 189 -18.724 -15.128 -26.406 1.00 70.26 C ANISOU 1186 CB ASN A 189 9258 9287 8152 -1705 -1468 -2234 C ATOM 1187 CG ASN A 189 -17.452 -14.343 -26.711 1.00 69.49 C ANISOU 1187 CG ASN A 189 9283 9257 7862 -1590 -1342 -2201 C ATOM 1188 OD1 ASN A 189 -17.502 -13.164 -27.064 1.00 60.15 O ANISOU 1188 OD1 ASN A 189 8045 8200 6611 -1573 -1493 -2001 O ATOM 1189 ND2 ASN A 189 -16.306 -15.001 -26.577 1.00 68.71 N ANISOU 1189 ND2 ASN A 189 9348 9069 7690 -1516 -1072 -2401 N ATOM 1190 N ILE A 190 -19.145 -15.211 -23.299 1.00 58.19 N ANISOU 1190 N ILE A 190 7025 6651 8433 -1901 -2156 -2131 N ATOM 1191 CA ILE A 190 -18.696 -15.119 -21.913 1.00 57.33 C ANISOU 1191 CA ILE A 190 6907 6473 8401 -1959 -2032 -1910 C ATOM 1192 C ILE A 190 -17.203 -14.796 -21.826 1.00 53.34 C ANISOU 1192 C ILE A 190 6510 5978 7780 -1818 -1907 -1942 C ATOM 1193 O ILE A 190 -16.758 -14.131 -20.891 1.00 51.07 O ANISOU 1193 O ILE A 190 6226 5742 7438 -1813 -1751 -1764 O ATOM 1194 CB ILE A 190 -18.995 -16.431 -21.130 1.00 54.80 C ANISOU 1194 CB ILE A 190 6545 5896 8379 -2122 -2163 -1835 C ATOM 1195 CG1 ILE A 190 -18.782 -16.223 -19.630 1.00 52.70 C ANISOU 1195 CG1 ILE A 190 6244 5614 8164 -2213 -2031 -1566 C ATOM 1196 CG2 ILE A 190 -18.157 -17.599 -21.651 1.00 56.50 C ANISOU 1196 CG2 ILE A 190 6853 5907 8707 -2047 -2276 -2021 C ATOM 1197 CD1 ILE A 190 -19.575 -15.068 -19.064 1.00 52.26 C ANISOU 1197 CD1 ILE A 190 6089 5791 7975 -2254 -1887 -1390 C ATOM 1198 N GLU A 191 -16.436 -15.252 -22.812 1.00 53.05 N ANISOU 1198 N GLU A 191 6552 5908 7698 -1700 -1975 -2180 N ATOM 1199 CA GLU A 191 -14.991 -15.058 -22.798 1.00 51.86 C ANISOU 1199 CA GLU A 191 6489 5768 7447 -1567 -1868 -2234 C ATOM 1200 C GLU A 191 -14.623 -13.583 -22.966 1.00 49.29 C ANISOU 1200 C GLU A 191 6185 5698 6846 -1475 -1687 -2149 C ATOM 1201 O GLU A 191 -13.630 -13.114 -22.412 1.00 50.89 O ANISOU 1201 O GLU A 191 6431 5921 6984 -1414 -1551 -2064 O ATOM 1202 CB GLU A 191 -14.338 -15.908 -23.890 1.00 54.25 C ANISOU 1202 CB GLU A 191 6846 6009 7757 -1459 -1991 -2541 C ATOM 1203 CG GLU A 191 -14.500 -17.423 -23.695 1.00 55.87 C ANISOU 1203 CG GLU A 191 7044 5929 8257 -1523 -2170 -2617 C ATOM 1204 CD GLU A 191 -15.736 -17.995 -24.376 1.00 59.15 C ANISOU 1204 CD GLU A 191 7412 6333 8731 -1586 -2303 -2667 C ATOM 1205 OE1 GLU A 191 -16.558 -17.206 -24.892 1.00 60.13 O ANISOU 1205 OE1 GLU A 191 7494 6643 8710 -1611 -2298 -2669 O ATOM 1206 OE2 GLU A 191 -15.881 -19.240 -24.401 1.00 59.90 O ANISOU 1206 OE2 GLU A 191 7509 6229 9023 -1608 -2419 -2707 O ATOM 1207 N THR A 192 -15.435 -12.858 -23.726 1.00 48.92 N ANISOU 1207 N THR A 192 6103 5833 6651 -1470 -1701 -2164 N ATOM 1208 CA THR A 192 -15.240 -11.430 -23.936 1.00 48.53 C ANISOU 1208 CA THR A 192 6066 6009 6366 -1398 -1567 -2067 C ATOM 1209 C THR A 192 -15.470 -10.666 -22.639 1.00 48.59 C ANISOU 1209 C THR A 192 6027 6021 6416 -1455 -1443 -1816 C ATOM 1210 O THR A 192 -14.724 -9.743 -22.307 1.00 48.41 O ANISOU 1210 O THR A 192 6036 6085 6271 -1386 -1308 -1718 O ATOM 1211 CB THR A 192 -16.187 -10.889 -25.028 1.00 49.19 C ANISOU 1211 CB THR A 192 6115 6266 6311 -1393 -1646 -2128 C ATOM 1212 OG1 THR A 192 -15.789 -11.406 -26.302 1.00 50.05 O ANISOU 1212 OG1 THR A 192 6272 6433 6314 -1318 -1736 -2370 O ATOM 1213 CG2 THR A 192 -16.163 -9.359 -25.073 1.00 47.93 C ANISOU 1213 CG2 THR A 192 5951 6304 5955 -1344 -1534 -1978 C ATOM 1214 N VAL A 193 -16.508 -11.058 -21.908 1.00 49.12 N ANISOU 1214 N VAL A 193 6006 6004 6652 -1583 -1495 -1718 N ATOM 1215 CA VAL A 193 -16.814 -10.440 -20.627 1.00 48.31 C ANISOU 1215 CA VAL A 193 5837 5929 6590 -1644 -1383 -1502 C ATOM 1216 C VAL A 193 -15.615 -10.545 -19.699 1.00 47.70 C ANISOU 1216 C VAL A 193 5819 5764 6540 -1616 -1272 -1420 C ATOM 1217 O VAL A 193 -15.207 -9.564 -19.080 1.00 45.36 O ANISOU 1217 O VAL A 193 5524 5560 6152 -1570 -1139 -1300 O ATOM 1218 CB VAL A 193 -18.041 -11.091 -19.959 1.00 49.51 C ANISOU 1218 CB VAL A 193 5873 6009 6928 -1807 -1460 -1418 C ATOM 1219 CG1 VAL A 193 -18.278 -10.495 -18.577 1.00 48.73 C ANISOU 1219 CG1 VAL A 193 5693 5974 6850 -1868 -1333 -1209 C ATOM 1220 CG2 VAL A 193 -19.265 -10.920 -20.834 1.00 51.64 C ANISOU 1220 CG2 VAL A 193 6073 6374 7176 -1834 -1569 -1494 C ATOM 1221 N ILE A 194 -15.042 -11.743 -19.627 1.00 49.31 N ANISOU 1221 N ILE A 194 6071 5781 6882 -1638 -1345 -1496 N ATOM 1222 CA ILE A 194 -13.886 -11.983 -18.772 1.00 47.96 C ANISOU 1222 CA ILE A 194 5957 5504 6760 -1613 -1265 -1427 C ATOM 1223 C ILE A 194 -12.667 -11.207 -19.259 1.00 47.49 C ANISOU 1223 C ILE A 194 5982 5549 6515 -1456 -1157 -1492 C ATOM 1224 O ILE A 194 -11.931 -10.623 -18.464 1.00 46.49 O ANISOU 1224 O ILE A 194 5876 5446 6343 -1422 -1030 -1372 O ATOM 1225 CB ILE A 194 -13.546 -13.482 -18.701 1.00 48.01 C ANISOU 1225 CB ILE A 194 5995 5266 6981 -1662 -1402 -1513 C ATOM 1226 CG1 ILE A 194 -14.678 -14.244 -18.009 1.00 45.94 C ANISOU 1226 CG1 ILE A 194 5642 4891 6921 -1847 -1505 -1390 C ATOM 1227 CG2 ILE A 194 -12.236 -13.695 -17.962 1.00 43.92 C ANISOU 1227 CG2 ILE A 194 5543 4642 6505 -1612 -1332 -1464 C ATOM 1228 CD1 ILE A 194 -14.518 -15.735 -18.052 1.00 49.62 C ANISOU 1228 CD1 ILE A 194 6131 5092 7630 -1911 -1687 -1472 C ATOM 1229 N GLU A 195 -12.470 -11.191 -20.571 1.00 49.15 N ANISOU 1229 N GLU A 195 6232 5837 6607 -1368 -1208 -1679 N ATOM 1230 CA GLU A 195 -11.307 -10.541 -21.155 1.00 50.24 C ANISOU 1230 CA GLU A 195 6436 6095 6556 -1234 -1115 -1746 C ATOM 1231 C GLU A 195 -11.334 -9.039 -20.920 1.00 47.43 C ANISOU 1231 C GLU A 195 6067 5915 6038 -1205 -988 -1585 C ATOM 1232 O GLU A 195 -10.311 -8.435 -20.600 1.00 44.66 O ANISOU 1232 O GLU A 195 5756 5606 5605 -1138 -874 -1523 O ATOM 1233 CB GLU A 195 -11.226 -10.830 -22.651 1.00 54.72 C ANISOU 1233 CB GLU A 195 7030 6756 7005 -1163 -1202 -1978 C ATOM 1234 CG GLU A 195 -10.004 -10.230 -23.314 1.00 56.83 C ANISOU 1234 CG GLU A 195 7350 7181 7060 -1038 -1105 -2048 C ATOM 1235 CD GLU A 195 -9.950 -10.525 -24.795 1.00 62.77 C ANISOU 1235 CD GLU A 195 8113 8070 7666 -974 -1187 -2282 C ATOM 1236 OE1 GLU A 195 -8.830 -10.709 -25.311 1.00 67.05 O ANISOU 1236 OE1 GLU A 195 8687 8682 8107 -877 -1148 -2424 O ATOM 1237 OE2 GLU A 195 -11.022 -10.571 -25.440 1.00 63.65 O ANISOU 1237 OE2 GLU A 195 8193 8236 7756 -1019 -1291 -2332 O ATOM 1238 N PHE A 196 -12.507 -8.436 -21.079 1.00 48.49 N ANISOU 1238 N PHE A 196 6139 6143 6142 -1254 -1021 -1522 N ATOM 1239 CA PHE A 196 -12.632 -7.003 -20.850 1.00 48.94 C ANISOU 1239 CA PHE A 196 6173 6343 6079 -1222 -933 -1379 C ATOM 1240 C PHE A 196 -12.324 -6.639 -19.395 1.00 48.46 C ANISOU 1240 C PHE A 196 6090 6227 6097 -1244 -821 -1214 C ATOM 1241 O PHE A 196 -11.659 -5.642 -19.131 1.00 47.15 O ANISOU 1241 O PHE A 196 5946 6132 5837 -1178 -726 -1131 O ATOM 1242 CB PHE A 196 -14.027 -6.515 -21.235 1.00 48.49 C ANISOU 1242 CB PHE A 196 6037 6377 6009 -1268 -1011 -1357 C ATOM 1243 CG PHE A 196 -14.209 -5.035 -21.069 1.00 45.91 C ANISOU 1243 CG PHE A 196 5680 6178 5585 -1225 -954 -1228 C ATOM 1244 CD1 PHE A 196 -13.180 -4.161 -21.388 1.00 43.72 C ANISOU 1244 CD1 PHE A 196 5468 5982 5163 -1138 -883 -1189 C ATOM 1245 CD2 PHE A 196 -15.408 -4.516 -20.607 1.00 45.09 C ANISOU 1245 CD2 PHE A 196 5472 6113 5546 -1271 -981 -1152 C ATOM 1246 CE1 PHE A 196 -13.338 -2.798 -21.237 1.00 42.59 C ANISOU 1246 CE1 PHE A 196 5296 5927 4959 -1100 -857 -1069 C ATOM 1247 CE2 PHE A 196 -15.570 -3.148 -20.454 1.00 44.07 C ANISOU 1247 CE2 PHE A 196 5308 6081 5354 -1217 -951 -1054 C ATOM 1248 CZ PHE A 196 -14.532 -2.290 -20.771 1.00 42.90 C ANISOU 1248 CZ PHE A 196 5235 5985 5079 -1133 -897 -1009 C ATOM 1249 N GLN A 197 -12.801 -7.448 -18.455 1.00 49.73 N ANISOU 1249 N GLN A 197 6202 6267 6424 -1342 -842 -1163 N ATOM 1250 CA GLN A 197 -12.514 -7.211 -17.043 1.00 48.84 C ANISOU 1250 CA GLN A 197 6062 6122 6372 -1372 -741 -1011 C ATOM 1251 C GLN A 197 -11.011 -7.269 -16.779 1.00 46.13 C ANISOU 1251 C GLN A 197 5809 5717 6000 -1296 -662 -1011 C ATOM 1252 O GLN A 197 -10.485 -6.483 -15.992 1.00 41.85 O ANISOU 1252 O GLN A 197 5267 5216 5416 -1261 -557 -904 O ATOM 1253 CB GLN A 197 -13.255 -8.219 -16.166 1.00 51.59 C ANISOU 1253 CB GLN A 197 6341 6366 6895 -1513 -791 -946 C ATOM 1254 CG GLN A 197 -14.761 -8.053 -16.236 1.00 59.10 C ANISOU 1254 CG GLN A 197 7177 7403 7876 -1597 -849 -924 C ATOM 1255 CD GLN A 197 -15.519 -9.115 -15.466 1.00 66.25 C ANISOU 1255 CD GLN A 197 8003 8219 8951 -1758 -910 -850 C ATOM 1256 OE1 GLN A 197 -15.057 -10.249 -15.323 1.00 69.13 O ANISOU 1256 OE1 GLN A 197 8415 8413 9437 -1812 -972 -861 O ATOM 1257 NE2 GLN A 197 -16.695 -8.751 -14.965 1.00 68.04 N ANISOU 1257 NE2 GLN A 197 8096 8563 9194 -1840 -900 -770 N ATOM 1258 N GLN A 198 -10.329 -8.194 -17.451 1.00 48.85 N ANISOU 1258 N GLN A 198 6221 5967 6373 -1264 -720 -1147 N ATOM 1259 CA GLN A 198 -8.878 -8.312 -17.338 1.00 51.44 C ANISOU 1259 CA GLN A 198 6625 6244 6676 -1181 -655 -1178 C ATOM 1260 C GLN A 198 -8.177 -7.046 -17.838 1.00 48.71 C ANISOU 1260 C GLN A 198 6310 6060 6137 -1078 -560 -1163 C ATOM 1261 O GLN A 198 -7.316 -6.498 -17.151 1.00 48.06 O ANISOU 1261 O GLN A 198 6249 5982 6029 -1037 -461 -1073 O ATOM 1262 CB GLN A 198 -8.370 -9.529 -18.117 1.00 58.10 C ANISOU 1262 CB GLN A 198 7515 6974 7585 -1150 -753 -1370 C ATOM 1263 CG GLN A 198 -8.893 -10.872 -17.627 1.00 65.30 C ANISOU 1263 CG GLN A 198 8405 7682 8724 -1254 -875 -1381 C ATOM 1264 CD GLN A 198 -8.299 -11.288 -16.292 1.00 70.92 C ANISOU 1264 CD GLN A 198 9126 8250 9571 -1300 -840 -1242 C ATOM 1265 OE1 GLN A 198 -9.004 -11.787 -15.414 1.00 73.97 O ANISOU 1265 OE1 GLN A 198 9464 8545 10096 -1428 -886 -1113 O ATOM 1266 NE2 GLN A 198 -6.994 -11.095 -16.137 1.00 72.06 N ANISOU 1266 NE2 GLN A 198 9326 8384 9669 -1202 -762 -1260 N ATOM 1267 N LYS A 199 -8.557 -6.587 -19.029 1.00 48.66 N ANISOU 1267 N LYS A 199 6303 6187 5998 -1045 -600 -1241 N ATOM 1268 CA LYS A 199 -7.938 -5.416 -19.644 1.00 49.82 C ANISOU 1268 CA LYS A 199 6476 6493 5959 -967 -535 -1210 C ATOM 1269 C LYS A 199 -8.214 -4.130 -18.873 1.00 49.01 C ANISOU 1269 C LYS A 199 6338 6445 5839 -970 -471 -1033 C ATOM 1270 O LYS A 199 -7.317 -3.308 -18.670 1.00 50.22 O ANISOU 1270 O LYS A 199 6518 6644 5921 -915 -390 -958 O ATOM 1271 CB LYS A 199 -8.419 -5.252 -21.084 1.00 52.56 C ANISOU 1271 CB LYS A 199 6824 6982 6166 -952 -614 -1313 C ATOM 1272 CG LYS A 199 -7.502 -5.874 -22.102 1.00 57.81 C ANISOU 1272 CG LYS A 199 7533 7702 6729 -889 -625 -1489 C ATOM 1273 CD LYS A 199 -7.412 -5.024 -23.354 1.00 60.93 C ANISOU 1273 CD LYS A 199 7935 8324 6892 -854 -632 -1500 C ATOM 1274 CE LYS A 199 -6.234 -5.451 -24.215 1.00 63.02 C ANISOU 1274 CE LYS A 199 8230 8697 7019 -783 -600 -1657 C ATOM 1275 NZ LYS A 199 -6.310 -6.897 -24.559 1.00 66.43 N ANISOU 1275 NZ LYS A 199 8662 9032 7545 -769 -685 -1892 N ATOM 1276 N ASN A 200 -9.461 -3.963 -18.452 1.00 46.02 N ANISOU 1276 N ASN A 200 5889 6063 5534 -1032 -514 -978 N ATOM 1277 CA ASN A 200 -9.892 -2.749 -17.777 1.00 44.05 C ANISOU 1277 CA ASN A 200 5585 5873 5280 -1023 -476 -849 C ATOM 1278 C ASN A 200 -9.290 -2.635 -16.378 1.00 44.15 C ANISOU 1278 C ASN A 200 5590 5819 5365 -1022 -378 -755 C ATOM 1279 O ASN A 200 -9.136 -1.538 -15.848 1.00 43.40 O ANISOU 1279 O ASN A 200 5472 5772 5246 -981 -329 -668 O ATOM 1280 CB ASN A 200 -11.420 -2.714 -17.705 1.00 43.24 C ANISOU 1280 CB ASN A 200 5388 5800 5242 -1086 -552 -844 C ATOM 1281 CG ASN A 200 -11.954 -1.380 -17.240 1.00 43.08 C ANISOU 1281 CG ASN A 200 5296 5858 5213 -1054 -539 -752 C ATOM 1282 OD1 ASN A 200 -11.431 -0.330 -17.599 1.00 44.07 O ANISOU 1282 OD1 ASN A 200 5453 6037 5253 -984 -529 -707 O ATOM 1283 ND2 ASN A 200 -13.003 -1.415 -16.429 1.00 44.14 N ANISOU 1283 ND2 ASN A 200 5325 6004 5443 -1108 -546 -727 N ATOM 1284 N ASN A 201 -8.952 -3.780 -15.791 1.00 45.71 N ANISOU 1284 N ASN A 201 5806 5901 5659 -1068 -365 -775 N ATOM 1285 CA ASN A 201 -8.432 -3.836 -14.431 1.00 43.78 C ANISOU 1285 CA ASN A 201 5555 5597 5484 -1083 -285 -680 C ATOM 1286 C ASN A 201 -7.227 -2.924 -14.215 1.00 40.62 C ANISOU 1286 C ASN A 201 5202 5225 5007 -993 -199 -631 C ATOM 1287 O ASN A 201 -7.130 -2.254 -13.188 1.00 38.10 O ANISOU 1287 O ASN A 201 4848 4926 4702 -984 -139 -541 O ATOM 1288 CB ASN A 201 -8.058 -5.274 -14.060 1.00 44.15 C ANISOU 1288 CB ASN A 201 5633 5496 5646 -1141 -312 -708 C ATOM 1289 CG ASN A 201 -7.461 -5.375 -12.664 1.00 44.18 C ANISOU 1289 CG ASN A 201 5634 5443 5711 -1165 -239 -595 C ATOM 1290 OD1 ASN A 201 -8.174 -5.266 -11.666 1.00 44.90 O ANISOU 1290 OD1 ASN A 201 5648 5571 5842 -1237 -219 -497 O ATOM 1291 ND2 ASN A 201 -6.146 -5.576 -12.588 1.00 43.59 N ANISOU 1291 ND2 ASN A 201 5632 5297 5633 -1103 -200 -610 N ATOM 1292 N ARG A 202 -6.320 -2.890 -15.186 1.00 40.56 N ANISOU 1292 N ARG A 202 5264 5233 4914 -930 -196 -697 N ATOM 1293 CA ARG A 202 -5.125 -2.066 -15.058 1.00 40.77 C ANISOU 1293 CA ARG A 202 5330 5290 4871 -857 -120 -645 C ATOM 1294 C ARG A 202 -5.472 -0.586 -14.937 1.00 42.02 C ANISOU 1294 C ARG A 202 5450 5538 4979 -827 -113 -552 C ATOM 1295 O ARG A 202 -4.878 0.132 -14.130 1.00 41.75 O ANISOU 1295 O ARG A 202 5411 5494 4956 -792 -55 -475 O ATOM 1296 CB ARG A 202 -4.189 -2.280 -16.240 1.00 42.23 C ANISOU 1296 CB ARG A 202 5574 5519 4953 -805 -119 -736 C ATOM 1297 CG ARG A 202 -2.898 -1.516 -16.101 1.00 42.32 C ANISOU 1297 CG ARG A 202 5616 5567 4899 -743 -39 -674 C ATOM 1298 CD ARG A 202 -1.936 -1.838 -17.223 1.00 43.76 C ANISOU 1298 CD ARG A 202 5835 5822 4968 -699 -26 -774 C ATOM 1299 NE ARG A 202 -0.683 -1.120 -17.038 1.00 42.84 N ANISOU 1299 NE ARG A 202 5735 5747 4797 -652 53 -704 N ATOM 1300 CZ ARG A 202 0.353 -1.199 -17.861 1.00 43.27 C ANISOU 1300 CZ ARG A 202 5803 5898 4739 -611 90 -766 C ATOM 1301 NH1 ARG A 202 0.291 -1.973 -18.941 1.00 44.67 N ANISOU 1301 NH1 ARG A 202 5982 6150 4840 -602 54 -920 N ATOM 1302 NH2 ARG A 202 1.452 -0.505 -17.599 1.00 41.75 N ANISOU 1302 NH2 ARG A 202 5613 5740 4510 -581 161 -684 N ATOM 1303 N LEU A 203 -6.434 -0.136 -15.739 1.00 42.17 N ANISOU 1303 N LEU A 203 5436 5633 4954 -837 -187 -568 N ATOM 1304 CA LEU A 203 -6.922 1.237 -15.650 1.00 41.16 C ANISOU 1304 CA LEU A 203 5261 5568 4812 -806 -215 -490 C ATOM 1305 C LEU A 203 -7.479 1.525 -14.263 1.00 40.02 C ANISOU 1305 C LEU A 203 5038 5397 4769 -815 -186 -448 C ATOM 1306 O LEU A 203 -7.252 2.597 -13.705 1.00 41.02 O ANISOU 1306 O LEU A 203 5139 5536 4909 -765 -170 -389 O ATOM 1307 CB LEU A 203 -8.003 1.513 -16.700 1.00 41.92 C ANISOU 1307 CB LEU A 203 5325 5737 4864 -823 -321 -518 C ATOM 1308 CG LEU A 203 -8.607 2.918 -16.580 1.00 40.92 C ANISOU 1308 CG LEU A 203 5139 5652 4757 -786 -379 -444 C ATOM 1309 CD1 LEU A 203 -7.545 3.985 -16.824 1.00 37.60 C ANISOU 1309 CD1 LEU A 203 4764 5245 4276 -734 -369 -353 C ATOM 1310 CD2 LEU A 203 -9.781 3.102 -17.523 1.00 41.92 C ANISOU 1310 CD2 LEU A 203 5225 5841 4861 -806 -497 -472 C ATOM 1311 N LEU A 204 -8.206 0.563 -13.707 1.00 39.50 N ANISOU 1311 N LEU A 204 4929 5305 4775 -883 -183 -480 N ATOM 1312 CA LEU A 204 -8.814 0.753 -12.397 1.00 38.72 C ANISOU 1312 CA LEU A 204 4737 5229 4747 -906 -149 -443 C ATOM 1313 C LEU A 204 -7.761 0.826 -11.295 1.00 38.71 C ANISOU 1313 C LEU A 204 4762 5187 4758 -883 -59 -388 C ATOM 1314 O LEU A 204 -7.912 1.581 -10.336 1.00 37.37 O ANISOU 1314 O LEU A 204 4526 5066 4608 -854 -27 -359 O ATOM 1315 CB LEU A 204 -9.805 -0.368 -12.091 1.00 37.85 C ANISOU 1315 CB LEU A 204 4566 5114 4701 -1010 -170 -466 C ATOM 1316 CG LEU A 204 -11.015 -0.503 -13.014 1.00 39.59 C ANISOU 1316 CG LEU A 204 4738 5378 4926 -1045 -264 -524 C ATOM 1317 CD1 LEU A 204 -11.995 -1.515 -12.434 1.00 38.80 C ANISOU 1317 CD1 LEU A 204 4554 5280 4908 -1161 -278 -522 C ATOM 1318 CD2 LEU A 204 -11.692 0.848 -13.241 1.00 40.10 C ANISOU 1318 CD2 LEU A 204 4732 5534 4971 -978 -310 -526 C ATOM 1319 N GLU A 205 -6.700 0.039 -11.431 1.00 41.02 N ANISOU 1319 N GLU A 205 5145 5397 5045 -889 -25 -390 N ATOM 1320 CA GLU A 205 -5.666 -0.006 -10.404 1.00 41.76 C ANISOU 1320 CA GLU A 205 5266 5444 5156 -871 51 -336 C ATOM 1321 C GLU A 205 -4.790 1.235 -10.457 1.00 40.54 C ANISOU 1321 C GLU A 205 5139 5310 4956 -779 77 -305 C ATOM 1322 O GLU A 205 -4.421 1.782 -9.418 1.00 41.33 O ANISOU 1322 O GLU A 205 5214 5417 5074 -750 122 -262 O ATOM 1323 CB GLU A 205 -4.811 -1.270 -10.546 1.00 42.87 C ANISOU 1323 CB GLU A 205 5485 5477 5327 -899 60 -357 C ATOM 1324 CG GLU A 205 -5.593 -2.581 -10.440 1.00 45.08 C ANISOU 1324 CG GLU A 205 5742 5701 5686 -1001 11 -375 C ATOM 1325 CD GLU A 205 -6.098 -2.879 -9.027 1.00 49.77 C ANISOU 1325 CD GLU A 205 6263 6311 6335 -1083 38 -285 C ATOM 1326 OE1 GLU A 205 -5.885 -2.057 -8.110 1.00 48.94 O ANISOU 1326 OE1 GLU A 205 6121 6275 6198 -1051 100 -230 O ATOM 1327 OE2 GLU A 205 -6.714 -3.952 -8.832 1.00 54.14 O ANISOU 1327 OE2 GLU A 205 6790 6817 6963 -1187 -9 -268 O ATOM 1328 N ILE A 206 -4.458 1.677 -11.664 1.00 39.76 N ANISOU 1328 N ILE A 206 5087 5226 4793 -740 42 -323 N ATOM 1329 CA ILE A 206 -3.715 2.923 -11.842 1.00 39.08 C ANISOU 1329 CA ILE A 206 5019 5160 4671 -671 44 -271 C ATOM 1330 C ILE A 206 -4.476 4.071 -11.181 1.00 39.19 C ANISOU 1330 C ILE A 206 4949 5209 4731 -638 8 -247 C ATOM 1331 O ILE A 206 -3.914 4.846 -10.408 1.00 39.51 O ANISOU 1331 O ILE A 206 4977 5233 4800 -590 31 -211 O ATOM 1332 CB ILE A 206 -3.486 3.241 -13.334 1.00 39.62 C ANISOU 1332 CB ILE A 206 5130 5275 4646 -660 -4 -273 C ATOM 1333 CG1 ILE A 206 -2.447 2.288 -13.925 1.00 40.05 C ANISOU 1333 CG1 ILE A 206 5255 5317 4644 -665 43 -319 C ATOM 1334 CG2 ILE A 206 -3.055 4.688 -13.521 1.00 38.36 C ANISOU 1334 CG2 ILE A 206 4968 5140 4469 -613 -37 -188 C ATOM 1335 CD1 ILE A 206 -2.233 2.466 -15.408 1.00 39.33 C ANISOU 1335 CD1 ILE A 206 5195 5319 4431 -663 5 -336 C ATOM 1336 N THR A 207 -5.765 4.158 -11.489 1.00 39.41 N ANISOU 1336 N THR A 207 4912 5285 4775 -659 -57 -282 N ATOM 1337 CA THR A 207 -6.640 5.165 -10.900 1.00 39.79 C ANISOU 1337 CA THR A 207 4860 5377 4881 -618 -105 -293 C ATOM 1338 C THR A 207 -6.688 5.015 -9.380 1.00 40.53 C ANISOU 1338 C THR A 207 4889 5494 5018 -620 -32 -307 C ATOM 1339 O THR A 207 -6.635 5.999 -8.645 1.00 40.86 O ANISOU 1339 O THR A 207 4874 5554 5096 -554 -41 -316 O ATOM 1340 CB THR A 207 -8.063 5.061 -11.482 1.00 39.18 C ANISOU 1340 CB THR A 207 4713 5356 4818 -648 -183 -342 C ATOM 1341 OG1 THR A 207 -7.995 5.149 -12.911 1.00 40.39 O ANISOU 1341 OG1 THR A 207 4930 5505 4911 -653 -254 -326 O ATOM 1342 CG2 THR A 207 -8.961 6.165 -10.945 1.00 36.35 C ANISOU 1342 CG2 THR A 207 4236 5046 4530 -588 -245 -376 C ATOM 1343 N ARG A 208 -6.783 3.772 -8.923 1.00 40.43 N ANISOU 1343 N ARG A 208 4879 5482 4999 -698 28 -308 N ATOM 1344 CA ARG A 208 -6.788 3.456 -7.505 1.00 42.39 C ANISOU 1344 CA ARG A 208 5070 5774 5263 -726 99 -296 C ATOM 1345 C ARG A 208 -5.567 4.051 -6.812 1.00 41.33 C ANISOU 1345 C ARG A 208 4978 5602 5124 -661 145 -263 C ATOM 1346 O ARG A 208 -5.689 4.715 -5.789 1.00 43.83 O ANISOU 1346 O ARG A 208 5218 5984 5451 -621 163 -283 O ATOM 1347 CB ARG A 208 -6.823 1.946 -7.316 1.00 46.58 C ANISOU 1347 CB ARG A 208 5628 6272 5797 -835 134 -266 C ATOM 1348 CG ARG A 208 -7.451 1.466 -6.038 1.00 49.74 C ANISOU 1348 CG ARG A 208 5929 6764 6204 -911 179 -239 C ATOM 1349 CD ARG A 208 -7.925 0.027 -6.198 1.00 54.34 C ANISOU 1349 CD ARG A 208 6519 7309 6819 -1039 162 -205 C ATOM 1350 NE ARG A 208 -9.331 -0.063 -6.594 1.00 58.84 N ANISOU 1350 NE ARG A 208 6991 7960 7404 -1091 114 -245 N ATOM 1351 CZ ARG A 208 -9.807 -0.901 -7.515 1.00 61.66 C ANISOU 1351 CZ ARG A 208 7377 8253 7798 -1155 51 -264 C ATOM 1352 NH1 ARG A 208 -8.993 -1.726 -8.160 1.00 62.10 N ANISOU 1352 NH1 ARG A 208 7554 8165 7877 -1166 28 -263 N ATOM 1353 NH2 ARG A 208 -11.104 -0.912 -7.797 1.00 63.18 N ANISOU 1353 NH2 ARG A 208 7468 8529 8007 -1202 6 -299 N ATOM 1354 N GLU A 209 -4.395 3.825 -7.392 1.00 39.12 N ANISOU 1354 N GLU A 209 4810 5228 4827 -648 159 -227 N ATOM 1355 CA GLU A 209 -3.150 4.314 -6.825 1.00 38.94 C ANISOU 1355 CA GLU A 209 4829 5160 4804 -593 199 -190 C ATOM 1356 C GLU A 209 -3.081 5.837 -6.803 1.00 38.22 C ANISOU 1356 C GLU A 209 4702 5080 4739 -504 146 -200 C ATOM 1357 O GLU A 209 -2.728 6.434 -5.785 1.00 36.93 O ANISOU 1357 O GLU A 209 4502 4930 4600 -457 164 -207 O ATOM 1358 CB GLU A 209 -1.960 3.773 -7.607 1.00 39.86 C ANISOU 1358 CB GLU A 209 5056 5192 4896 -596 220 -161 C ATOM 1359 CG GLU A 209 -1.758 2.289 -7.496 1.00 43.24 C ANISOU 1359 CG GLU A 209 5525 5571 5332 -664 254 -163 C ATOM 1360 CD GLU A 209 -0.488 1.843 -8.190 1.00 48.46 C ANISOU 1360 CD GLU A 209 6277 6160 5977 -642 274 -165 C ATOM 1361 OE1 GLU A 209 0.569 2.474 -7.976 1.00 49.42 O ANISOU 1361 OE1 GLU A 209 6424 6264 6091 -588 303 -132 O ATOM 1362 OE2 GLU A 209 -0.546 0.870 -8.962 1.00 53.25 O ANISOU 1362 OE2 GLU A 209 6920 6734 6581 -675 257 -210 O ATOM 1363 N PHE A 210 -3.393 6.456 -7.938 1.00 36.78 N ANISOU 1363 N PHE A 210 4530 4886 4557 -483 68 -197 N ATOM 1364 CA PHE A 210 -3.374 7.908 -8.032 1.00 38.27 C ANISOU 1364 CA PHE A 210 4685 5058 4797 -406 -16 -191 C ATOM 1365 C PHE A 210 -4.356 8.541 -7.038 1.00 40.64 C ANISOU 1365 C PHE A 210 4861 5422 5160 -357 -48 -275 C ATOM 1366 O PHE A 210 -4.081 9.607 -6.490 1.00 41.32 O ANISOU 1366 O PHE A 210 4908 5483 5308 -279 -95 -297 O ATOM 1367 CB PHE A 210 -3.689 8.367 -9.465 1.00 37.18 C ANISOU 1367 CB PHE A 210 4574 4907 4644 -411 -111 -155 C ATOM 1368 CG PHE A 210 -2.502 8.318 -10.406 1.00 36.03 C ANISOU 1368 CG PHE A 210 4528 4726 4435 -432 -98 -70 C ATOM 1369 CD1 PHE A 210 -1.223 8.623 -9.955 1.00 34.36 C ANISOU 1369 CD1 PHE A 210 4355 4466 4233 -408 -53 -21 C ATOM 1370 CD2 PHE A 210 -2.671 7.970 -11.743 1.00 37.37 C ANISOU 1370 CD2 PHE A 210 4741 4931 4527 -477 -129 -47 C ATOM 1371 CE1 PHE A 210 -0.130 8.582 -10.817 1.00 35.85 C ANISOU 1371 CE1 PHE A 210 4615 4651 4355 -431 -33 54 C ATOM 1372 CE2 PHE A 210 -1.582 7.925 -12.619 1.00 38.49 C ANISOU 1372 CE2 PHE A 210 4955 5084 4586 -498 -107 21 C ATOM 1373 CZ PHE A 210 -0.308 8.232 -12.151 1.00 38.56 C ANISOU 1373 CZ PHE A 210 4992 5052 4606 -477 -56 73 C ATOM 1374 N SER A 211 -5.482 7.872 -6.789 1.00 39.89 N ANISOU 1374 N SER A 211 4693 5415 5049 -401 -27 -330 N ATOM 1375 CA SER A 211 -6.531 8.424 -5.927 1.00 41.64 C ANISOU 1375 CA SER A 211 4770 5738 5313 -356 -53 -428 C ATOM 1376 C SER A 211 -6.167 8.512 -4.443 1.00 40.81 C ANISOU 1376 C SER A 211 4608 5702 5197 -329 20 -468 C ATOM 1377 O SER A 211 -6.667 9.391 -3.743 1.00 41.20 O ANISOU 1377 O SER A 211 4542 5822 5290 -249 -20 -568 O ATOM 1378 CB SER A 211 -7.819 7.609 -6.062 1.00 43.48 C ANISOU 1378 CB SER A 211 4928 6070 5523 -429 -40 -466 C ATOM 1379 OG SER A 211 -8.439 7.861 -7.311 1.00 46.23 O ANISOU 1379 OG SER A 211 5286 6382 5895 -426 -138 -466 O ATOM 1380 N VAL A 212 -5.326 7.604 -3.953 1.00 38.83 N ANISOU 1380 N VAL A 212 4429 5437 4888 -391 116 -400 N ATOM 1381 CA VAL A 212 -4.916 7.670 -2.550 1.00 40.79 C ANISOU 1381 CA VAL A 212 4628 5759 5109 -373 179 -424 C ATOM 1382 C VAL A 212 -3.525 8.274 -2.374 1.00 41.08 C ANISOU 1382 C VAL A 212 4748 5687 5173 -310 173 -389 C ATOM 1383 O VAL A 212 -3.011 8.316 -1.260 1.00 42.81 O ANISOU 1383 O VAL A 212 4946 5955 5367 -293 219 -402 O ATOM 1384 CB VAL A 212 -4.932 6.282 -1.867 1.00 40.83 C ANISOU 1384 CB VAL A 212 4640 5835 5040 -491 277 -360 C ATOM 1385 CG1 VAL A 212 -6.354 5.757 -1.759 1.00 40.83 C ANISOU 1385 CG1 VAL A 212 4524 5974 5014 -564 286 -393 C ATOM 1386 CG2 VAL A 212 -4.031 5.305 -2.602 1.00 38.96 C ANISOU 1386 CG2 VAL A 212 4549 5455 4800 -554 299 -258 C ATOM 1387 N ASN A 213 -2.929 8.745 -3.469 1.00 40.55 N ANISOU 1387 N ASN A 213 4768 5489 5149 -282 112 -339 N ATOM 1388 CA ASN A 213 -1.618 9.389 -3.421 1.00 39.06 C ANISOU 1388 CA ASN A 213 4649 5198 4995 -232 96 -294 C ATOM 1389 C ASN A 213 -1.619 10.784 -4.051 1.00 40.61 C ANISOU 1389 C ASN A 213 4830 5314 5285 -154 -33 -304 C ATOM 1390 O ASN A 213 -0.559 11.322 -4.376 1.00 40.43 O ANISOU 1390 O ASN A 213 4873 5192 5298 -134 -65 -235 O ATOM 1391 CB ASN A 213 -0.570 8.523 -4.123 1.00 38.14 C ANISOU 1391 CB ASN A 213 4657 5000 4835 -293 153 -192 C ATOM 1392 CG ASN A 213 -0.227 7.275 -3.342 1.00 38.41 C ANISOU 1392 CG ASN A 213 4716 5065 4815 -356 252 -169 C ATOM 1393 OD1 ASN A 213 -0.694 6.180 -3.661 1.00 40.27 O ANISOU 1393 OD1 ASN A 213 4969 5318 5015 -432 285 -153 O ATOM 1394 ND2 ASN A 213 0.595 7.430 -2.312 1.00 35.93 N ANISOU 1394 ND2 ASN A 213 4403 4748 4502 -329 285 -162 N ATOM 1395 N ALA A 214 -2.808 11.353 -4.236 1.00 40.32 N ANISOU 1395 N ALA A 214 4702 5319 5297 -115 -117 -382 N ATOM 1396 CA ALA A 214 -2.961 12.671 -4.851 1.00 40.19 C ANISOU 1396 CA ALA A 214 4664 5213 5395 -44 -271 -386 C ATOM 1397 C ALA A 214 -2.159 12.821 -6.154 1.00 40.39 C ANISOU 1397 C ALA A 214 4803 5130 5415 -90 -315 -238 C ATOM 1398 O ALA A 214 -1.461 13.813 -6.352 1.00 43.60 O ANISOU 1398 O ALA A 214 5229 5434 5903 -54 -407 -181 O ATOM 1399 CB ALA A 214 -2.568 13.763 -3.853 1.00 38.76 C ANISOU 1399 CB ALA A 214 4420 4994 5313 59 -337 -468 C ATOM 1400 N GLY A 215 -2.253 11.826 -7.028 1.00 37.71 N ANISOU 1400 N GLY A 215 4528 4824 4976 -174 -252 -177 N ATOM 1401 CA GLY A 215 -1.673 11.919 -8.357 1.00 37.54 C ANISOU 1401 CA GLY A 215 4593 4755 4918 -223 -289 -54 C ATOM 1402 C GLY A 215 -0.170 11.719 -8.460 1.00 37.78 C ANISOU 1402 C GLY A 215 4708 4745 4903 -252 -219 38 C ATOM 1403 O GLY A 215 0.406 11.858 -9.540 1.00 38.60 O ANISOU 1403 O GLY A 215 4868 4838 4960 -295 -243 143 O ATOM 1404 N VAL A 216 0.479 11.406 -7.344 1.00 36.76 N ANISOU 1404 N VAL A 216 4579 4610 4780 -231 -134 1 N ATOM 1405 CA VAL A 216 1.912 11.137 -7.359 1.00 36.47 C ANISOU 1405 CA VAL A 216 4611 4538 4707 -253 -63 75 C ATOM 1406 C VAL A 216 2.237 9.878 -6.574 1.00 37.27 C ANISOU 1406 C VAL A 216 4735 4673 4751 -275 67 30 C ATOM 1407 O VAL A 216 2.019 9.820 -5.369 1.00 38.25 O ANISOU 1407 O VAL A 216 4814 4817 4902 -245 93 -33 O ATOM 1408 CB VAL A 216 2.720 12.293 -6.765 1.00 36.51 C ANISOU 1408 CB VAL A 216 4597 4462 4811 -199 -128 105 C ATOM 1409 CG1 VAL A 216 4.208 11.997 -6.894 1.00 36.87 C ANISOU 1409 CG1 VAL A 216 4706 4483 4818 -230 -56 188 C ATOM 1410 CG2 VAL A 216 2.357 13.599 -7.437 1.00 35.28 C ANISOU 1410 CG2 VAL A 216 4413 4245 4748 -179 -290 158 C ATOM 1411 N THR A 217 2.771 8.868 -7.245 1.00 37.64 N ANISOU 1411 N THR A 217 4847 4733 4721 -327 139 61 N ATOM 1412 CA THR A 217 3.073 7.625 -6.553 1.00 38.89 C ANISOU 1412 CA THR A 217 5030 4897 4851 -352 235 28 C ATOM 1413 C THR A 217 4.558 7.321 -6.568 1.00 38.92 C ANISOU 1413 C THR A 217 5088 4858 4843 -349 291 72 C ATOM 1414 O THR A 217 5.271 7.668 -7.510 1.00 39.31 O ANISOU 1414 O THR A 217 5163 4908 4865 -355 282 123 O ATOM 1415 CB THR A 217 2.319 6.415 -7.163 1.00 34.47 C ANISOU 1415 CB THR A 217 4488 4371 4239 -410 261 -9 C ATOM 1416 OG1 THR A 217 2.902 6.070 -8.427 1.00 35.32 O ANISOU 1416 OG1 THR A 217 4650 4482 4288 -430 270 11 O ATOM 1417 CG2 THR A 217 0.828 6.733 -7.340 1.00 34.42 C ANISOU 1417 CG2 THR A 217 4420 4415 4242 -417 200 -50 C ATOM 1418 N THR A 218 5.007 6.675 -5.497 1.00 38.43 N ANISOU 1418 N THR A 218 5031 4773 4797 -346 347 56 N ATOM 1419 CA THR A 218 6.349 6.132 -5.405 1.00 37.65 C ANISOU 1419 CA THR A 218 4977 4631 4697 -343 400 80 C ATOM 1420 C THR A 218 6.309 5.079 -4.299 1.00 37.35 C ANISOU 1420 C THR A 218 4944 4574 4673 -363 441 61 C ATOM 1421 O THR A 218 5.730 5.318 -3.249 1.00 36.79 O ANISOU 1421 O THR A 218 4831 4536 4614 -361 432 52 O ATOM 1422 CB THR A 218 7.413 7.232 -5.123 1.00 38.65 C ANISOU 1422 CB THR A 218 5095 4725 4864 -299 382 130 C ATOM 1423 OG1 THR A 218 8.726 6.657 -5.159 1.00 39.90 O ANISOU 1423 OG1 THR A 218 5287 4854 5020 -296 436 149 O ATOM 1424 CG2 THR A 218 7.181 7.930 -3.781 1.00 36.11 C ANISOU 1424 CG2 THR A 218 4729 4395 4596 -259 351 111 C ATOM 1425 N PRO A 219 6.881 3.887 -4.544 1.00 36.72 N ANISOU 1425 N PRO A 219 4909 4451 4593 -385 475 52 N ATOM 1426 CA PRO A 219 7.519 3.445 -5.786 1.00 37.32 C ANISOU 1426 CA PRO A 219 5020 4518 4643 -381 491 28 C ATOM 1427 C PRO A 219 6.558 3.299 -6.964 1.00 39.84 C ANISOU 1427 C PRO A 219 5339 4889 4911 -411 466 -11 C ATOM 1428 O PRO A 219 5.337 3.309 -6.788 1.00 41.07 O ANISOU 1428 O PRO A 219 5470 5068 5068 -440 436 -21 O ATOM 1429 CB PRO A 219 8.121 2.080 -5.412 1.00 37.37 C ANISOU 1429 CB PRO A 219 5058 4451 4692 -390 511 1 C ATOM 1430 CG PRO A 219 7.518 1.694 -4.146 1.00 37.45 C ANISOU 1430 CG PRO A 219 5055 4438 4737 -427 499 34 C ATOM 1431 CD PRO A 219 7.096 2.934 -3.445 1.00 37.09 C ANISOU 1431 CD PRO A 219 4965 4456 4672 -409 493 66 C ATOM 1432 N VAL A 220 7.117 3.199 -8.165 1.00 39.48 N ANISOU 1432 N VAL A 220 5310 4880 4813 -402 478 -36 N ATOM 1433 CA VAL A 220 6.305 2.990 -9.350 1.00 39.46 C ANISOU 1433 CA VAL A 220 5309 4940 4745 -429 451 -80 C ATOM 1434 C VAL A 220 5.938 1.509 -9.445 1.00 38.71 C ANISOU 1434 C VAL A 220 5235 4796 4676 -452 447 -170 C ATOM 1435 O VAL A 220 6.813 0.650 -9.575 1.00 40.79 O ANISOU 1435 O VAL A 220 5518 5020 4961 -429 470 -228 O ATOM 1436 CB VAL A 220 7.037 3.459 -10.616 1.00 40.01 C ANISOU 1436 CB VAL A 220 5378 5103 4722 -420 464 -71 C ATOM 1437 CG1 VAL A 220 6.252 3.089 -11.873 1.00 39.49 C ANISOU 1437 CG1 VAL A 220 5315 5120 4571 -448 435 -131 C ATOM 1438 CG2 VAL A 220 7.273 4.958 -10.544 1.00 39.25 C ANISOU 1438 CG2 VAL A 220 5258 5033 4622 -416 438 42 C ATOM 1439 N SER A 221 4.644 1.221 -9.354 1.00 37.23 N ANISOU 1439 N SER A 221 5036 4606 4505 -495 407 -184 N ATOM 1440 CA SER A 221 4.155 -0.149 -9.326 1.00 39.31 C ANISOU 1440 CA SER A 221 5314 4804 4820 -534 381 -250 C ATOM 1441 C SER A 221 4.175 -0.797 -10.707 1.00 40.82 C ANISOU 1441 C SER A 221 5522 5027 4961 -527 360 -359 C ATOM 1442 O SER A 221 4.456 -0.145 -11.709 1.00 39.13 O ANISOU 1442 O SER A 221 5304 4916 4647 -502 372 -371 O ATOM 1443 CB SER A 221 2.738 -0.193 -8.770 1.00 38.56 C ANISOU 1443 CB SER A 221 5183 4715 4753 -594 346 -221 C ATOM 1444 OG SER A 221 1.840 0.372 -9.706 1.00 39.88 O ANISOU 1444 OG SER A 221 5330 4965 4858 -602 312 -243 O ATOM 1445 N THR A 222 3.863 -2.089 -10.750 1.00 42.33 N ANISOU 1445 N THR A 222 5727 5135 5222 -553 317 -437 N ATOM 1446 CA THR A 222 3.844 -2.818 -12.006 1.00 42.45 C ANISOU 1446 CA THR A 222 5753 5176 5202 -538 283 -574 C ATOM 1447 C THR A 222 2.563 -2.513 -12.780 1.00 43.34 C ANISOU 1447 C THR A 222 5847 5371 5247 -580 239 -588 C ATOM 1448 O THR A 222 2.458 -2.833 -13.960 1.00 45.61 O ANISOU 1448 O THR A 222 6139 5727 5466 -566 211 -697 O ATOM 1449 CB THR A 222 3.989 -4.331 -11.778 1.00 43.59 C ANISOU 1449 CB THR A 222 5915 5171 5477 -545 225 -665 C ATOM 1450 OG1 THR A 222 3.152 -4.728 -10.691 1.00 44.51 O ANISOU 1450 OG1 THR A 222 6026 5189 5698 -624 186 -572 O ATOM 1451 CG2 THR A 222 5.440 -4.678 -11.427 1.00 43.93 C ANISOU 1451 CG2 THR A 222 5970 5149 5572 -479 256 -695 C ATOM 1452 N TYR A 223 1.598 -1.875 -12.117 1.00 41.95 N ANISOU 1452 N TYR A 223 5646 5206 5089 -625 230 -489 N ATOM 1453 CA TYR A 223 0.424 -1.346 -12.808 1.00 39.52 C ANISOU 1453 CA TYR A 223 5312 4986 4720 -654 186 -489 C ATOM 1454 C TYR A 223 0.780 -0.106 -13.617 1.00 40.52 C ANISOU 1454 C TYR A 223 5436 5235 4725 -616 202 -448 C ATOM 1455 O TYR A 223 0.275 0.083 -14.724 1.00 44.00 O ANISOU 1455 O TYR A 223 5873 5767 5078 -625 159 -484 O ATOM 1456 CB TYR A 223 -0.692 -1.006 -11.825 1.00 36.98 C ANISOU 1456 CB TYR A 223 4942 4652 4457 -704 170 -410 C ATOM 1457 CG TYR A 223 -1.309 -2.203 -11.154 1.00 37.54 C ANISOU 1457 CG TYR A 223 4999 4631 4632 -775 138 -422 C ATOM 1458 CD1 TYR A 223 -1.894 -3.227 -11.900 1.00 38.19 C ANISOU 1458 CD1 TYR A 223 5088 4676 4746 -816 69 -513 C ATOM 1459 CD2 TYR A 223 -1.331 -2.300 -9.773 1.00 35.02 C ANISOU 1459 CD2 TYR A 223 4655 4272 4380 -810 166 -335 C ATOM 1460 CE1 TYR A 223 -2.470 -4.322 -11.277 1.00 39.26 C ANISOU 1460 CE1 TYR A 223 5207 4714 4997 -898 22 -502 C ATOM 1461 CE2 TYR A 223 -1.898 -3.382 -9.142 1.00 35.93 C ANISOU 1461 CE2 TYR A 223 4751 4315 4586 -898 129 -313 C ATOM 1462 CZ TYR A 223 -2.467 -4.390 -9.890 1.00 39.66 C ANISOU 1462 CZ TYR A 223 5232 4730 5109 -946 53 -388 C ATOM 1463 OH TYR A 223 -3.037 -5.458 -9.227 1.00 41.73 O ANISOU 1463 OH TYR A 223 5469 4907 5479 -1050 -1 -343 O ATOM 1464 N MET A 224 1.631 0.750 -13.051 1.00 38.49 N ANISOU 1464 N MET A 224 5179 4980 4465 -582 251 -362 N ATOM 1465 CA MET A 224 2.112 1.936 -13.762 1.00 38.47 C ANISOU 1465 CA MET A 224 5173 5079 4366 -559 255 -295 C ATOM 1466 C MET A 224 3.008 1.527 -14.915 1.00 41.23 C ANISOU 1466 C MET A 224 5541 5520 4606 -542 282 -364 C ATOM 1467 O MET A 224 2.911 2.061 -16.017 1.00 44.37 O ANISOU 1467 O MET A 224 5930 6045 4882 -556 257 -346 O ATOM 1468 CB MET A 224 2.885 2.869 -12.825 1.00 35.05 C ANISOU 1468 CB MET A 224 4732 4608 3977 -530 291 -194 C ATOM 1469 CG MET A 224 2.067 3.421 -11.678 1.00 33.04 C ANISOU 1469 CG MET A 224 4443 4299 3812 -533 266 -144 C ATOM 1470 SD MET A 224 0.850 4.608 -12.286 1.00 37.24 S ANISOU 1470 SD MET A 224 4933 4894 4321 -542 172 -99 S ATOM 1471 CE MET A 224 -0.044 4.938 -10.751 1.00 33.74 C ANISOU 1471 CE MET A 224 4427 4402 3989 -530 161 -100 C ATOM 1472 N LEU A 225 3.879 0.562 -14.644 1.00 40.63 N ANISOU 1472 N LEU A 225 5480 5387 4571 -513 327 -447 N ATOM 1473 CA LEU A 225 4.870 0.118 -15.608 1.00 43.28 C ANISOU 1473 CA LEU A 225 5814 5820 4811 -479 363 -544 C ATOM 1474 C LEU A 225 5.257 -1.315 -15.265 1.00 45.64 C ANISOU 1474 C LEU A 225 6125 6003 5212 -447 364 -685 C ATOM 1475 O LEU A 225 5.891 -1.548 -14.235 1.00 47.14 O ANISOU 1475 O LEU A 225 6324 6077 5509 -426 390 -654 O ATOM 1476 CB LEU A 225 6.089 1.041 -15.572 1.00 43.73 C ANISOU 1476 CB LEU A 225 5854 5950 4812 -459 426 -448 C ATOM 1477 CG LEU A 225 6.764 1.476 -16.872 1.00 45.88 C ANISOU 1477 CG LEU A 225 6096 6430 4906 -463 455 -450 C ATOM 1478 CD1 LEU A 225 5.756 2.057 -17.853 1.00 46.58 C ANISOU 1478 CD1 LEU A 225 6181 6638 4879 -515 391 -403 C ATOM 1479 CD2 LEU A 225 7.859 2.492 -16.570 1.00 44.77 C ANISOU 1479 CD2 LEU A 225 5932 6330 4750 -464 505 -313 C ATOM 1480 N THR A 226 4.852 -2.276 -16.096 1.00 45.17 N ANISOU 1480 N THR A 226 6066 5964 5131 -442 317 -839 N ATOM 1481 CA THR A 226 5.195 -3.676 -15.846 1.00 46.55 C ANISOU 1481 CA THR A 226 6251 6005 5431 -407 286 -987 C ATOM 1482 C THR A 226 6.706 -3.863 -15.903 1.00 47.44 C ANISOU 1482 C THR A 226 6344 6148 5532 -332 347 -1055 C ATOM 1483 O THR A 226 7.426 -3.024 -16.452 1.00 45.64 O ANISOU 1483 O THR A 226 6088 6090 5165 -315 416 -1017 O ATOM 1484 CB THR A 226 4.537 -4.654 -16.865 1.00 44.79 C ANISOU 1484 CB THR A 226 6024 5802 5192 -405 208 -1171 C ATOM 1485 OG1 THR A 226 5.138 -4.498 -18.157 1.00 43.94 O ANISOU 1485 OG1 THR A 226 5886 5904 4907 -358 242 -1289 O ATOM 1486 CG2 THR A 226 3.030 -4.430 -16.959 1.00 45.20 C ANISOU 1486 CG2 THR A 226 6084 5850 5242 -480 145 -1110 C ATOM 1487 N ASN A 227 7.182 -4.965 -15.337 1.00 49.09 N ANISOU 1487 N ASN A 227 6561 6194 5898 -293 313 -1149 N ATOM 1488 CA ASN A 227 8.602 -5.268 -15.364 1.00 52.69 C ANISOU 1488 CA ASN A 227 6988 6665 6368 -210 357 -1240 C ATOM 1489 C ASN A 227 9.123 -5.316 -16.789 1.00 52.70 C ANISOU 1489 C ASN A 227 6935 6887 6201 -155 392 -1412 C ATOM 1490 O ASN A 227 10.219 -4.848 -17.076 1.00 52.89 O ANISOU 1490 O ASN A 227 6912 7053 6129 -113 474 -1419 O ATOM 1491 CB ASN A 227 8.887 -6.588 -14.654 1.00 57.45 C ANISOU 1491 CB ASN A 227 7605 7037 7186 -175 277 -1335 C ATOM 1492 CG ASN A 227 10.030 -6.474 -13.671 1.00 61.34 C ANISOU 1492 CG ASN A 227 8094 7447 7766 -137 317 -1261 C ATOM 1493 OD1 ASN A 227 9.948 -5.723 -12.689 1.00 61.44 O ANISOU 1493 OD1 ASN A 227 8130 7422 7794 -186 353 -1067 O ATOM 1494 ND2 ASN A 227 11.109 -7.210 -13.927 1.00 62.89 N ANISOU 1494 ND2 ASN A 227 8252 7620 8022 -42 306 -1429 N ATOM 1495 N SER A 228 8.315 -5.866 -17.686 1.00 53.74 N ANISOU 1495 N SER A 228 7066 7066 6286 -161 328 -1550 N ATOM 1496 CA SER A 228 8.682 -5.945 -19.090 1.00 55.23 C ANISOU 1496 CA SER A 228 7198 7499 6288 -113 354 -1729 C ATOM 1497 C SER A 228 8.784 -4.548 -19.705 1.00 53.59 C ANISOU 1497 C SER A 228 6966 7548 5847 -165 442 -1570 C ATOM 1498 O SER A 228 9.761 -4.230 -20.381 1.00 54.58 O ANISOU 1498 O SER A 228 7028 7892 5820 -132 520 -1617 O ATOM 1499 CB SER A 228 7.668 -6.799 -19.858 1.00 57.45 C ANISOU 1499 CB SER A 228 7487 7766 6574 -116 251 -1904 C ATOM 1500 OG SER A 228 7.890 -6.707 -21.256 1.00 60.42 O ANISOU 1500 OG SER A 228 7806 8426 6725 -82 280 -2059 O ATOM 1501 N GLU A 229 7.779 -3.716 -19.456 1.00 51.11 N ANISOU 1501 N GLU A 229 6696 7208 5516 -251 421 -1376 N ATOM 1502 CA GLU A 229 7.765 -2.357 -19.985 1.00 50.71 C ANISOU 1502 CA GLU A 229 6629 7359 5281 -310 469 -1200 C ATOM 1503 C GLU A 229 8.930 -1.519 -19.454 1.00 49.56 C ANISOU 1503 C GLU A 229 6458 7246 5126 -306 555 -1058 C ATOM 1504 O GLU A 229 9.551 -0.762 -20.200 1.00 49.72 O ANISOU 1504 O GLU A 229 6429 7492 4970 -329 611 -994 O ATOM 1505 CB GLU A 229 6.433 -1.680 -19.653 1.00 50.63 C ANISOU 1505 CB GLU A 229 6664 7266 5305 -386 406 -1037 C ATOM 1506 CG GLU A 229 5.244 -2.257 -20.414 1.00 52.55 C ANISOU 1506 CG GLU A 229 6919 7533 5512 -408 320 -1150 C ATOM 1507 CD GLU A 229 3.910 -1.998 -19.718 1.00 52.64 C ANISOU 1507 CD GLU A 229 6968 7389 5642 -466 251 -1035 C ATOM 1508 OE1 GLU A 229 3.909 -1.410 -18.614 1.00 49.99 O ANISOU 1508 OE1 GLU A 229 6647 6932 5414 -483 272 -882 O ATOM 1509 OE2 GLU A 229 2.861 -2.390 -20.278 1.00 53.63 O ANISOU 1509 OE2 GLU A 229 7099 7527 5751 -492 175 -1108 O ATOM 1510 N LEU A 230 9.224 -1.662 -18.164 1.00 47.17 N ANISOU 1510 N LEU A 230 6184 6728 5011 -285 559 -1000 N ATOM 1511 CA LEU A 230 10.287 -0.893 -17.532 1.00 44.80 C ANISOU 1511 CA LEU A 230 5863 6430 4729 -281 627 -868 C ATOM 1512 C LEU A 230 11.653 -1.270 -18.105 1.00 48.23 C ANISOU 1512 C LEU A 230 6223 7017 5084 -218 700 -999 C ATOM 1513 O LEU A 230 12.435 -0.398 -18.493 1.00 48.03 O ANISOU 1513 O LEU A 230 6146 7170 4934 -244 766 -900 O ATOM 1514 CB LEU A 230 10.262 -1.095 -16.016 1.00 41.03 C ANISOU 1514 CB LEU A 230 5430 5698 4461 -269 607 -801 C ATOM 1515 CG LEU A 230 11.347 -0.387 -15.198 1.00 38.97 C ANISOU 1515 CG LEU A 230 5152 5408 4247 -257 663 -678 C ATOM 1516 CD1 LEU A 230 11.439 1.086 -15.566 1.00 36.90 C ANISOU 1516 CD1 LEU A 230 4868 5285 3866 -315 687 -498 C ATOM 1517 CD2 LEU A 230 11.066 -0.542 -13.710 1.00 37.00 C ANISOU 1517 CD2 LEU A 230 4950 4930 4178 -258 630 -604 C ATOM 1518 N LEU A 231 11.931 -2.569 -18.165 1.00 50.00 N ANISOU 1518 N LEU A 231 6435 7174 5390 -138 679 -1225 N ATOM 1519 CA LEU A 231 13.156 -3.062 -18.787 1.00 51.18 C ANISOU 1519 CA LEU A 231 6495 7482 5468 -59 738 -1404 C ATOM 1520 C LEU A 231 13.274 -2.553 -20.221 1.00 51.94 C ANISOU 1520 C LEU A 231 6521 7922 5291 -90 792 -1434 C ATOM 1521 O LEU A 231 14.347 -2.141 -20.661 1.00 51.55 O ANISOU 1521 O LEU A 231 6385 8090 5113 -82 880 -1429 O ATOM 1522 CB LEU A 231 13.193 -4.593 -18.757 1.00 51.91 C ANISOU 1522 CB LEU A 231 6584 7431 5707 38 669 -1671 C ATOM 1523 CG LEU A 231 13.475 -5.179 -17.372 1.00 50.82 C ANISOU 1523 CG LEU A 231 6491 6986 5830 73 619 -1643 C ATOM 1524 CD1 LEU A 231 13.286 -6.688 -17.355 1.00 50.15 C ANISOU 1524 CD1 LEU A 231 6415 6721 5920 148 510 -1878 C ATOM 1525 CD2 LEU A 231 14.886 -4.803 -16.939 1.00 49.95 C ANISOU 1525 CD2 LEU A 231 6323 6922 5734 117 700 -1603 C ATOM 1526 N SER A 232 12.157 -2.563 -20.937 1.00 53.51 N ANISOU 1526 N SER A 232 6751 8185 5394 -135 737 -1451 N ATOM 1527 CA SER A 232 12.140 -2.096 -22.315 1.00 56.99 C ANISOU 1527 CA SER A 232 7131 8963 5559 -177 773 -1465 C ATOM 1528 C SER A 232 12.418 -0.599 -22.376 1.00 55.46 C ANISOU 1528 C SER A 232 6922 8908 5241 -281 823 -1172 C ATOM 1529 O SER A 232 13.125 -0.127 -23.253 1.00 57.12 O ANISOU 1529 O SER A 232 7046 9418 5237 -314 892 -1146 O ATOM 1530 CB SER A 232 10.798 -2.419 -22.972 1.00 59.58 C ANISOU 1530 CB SER A 232 7506 9300 5833 -206 684 -1533 C ATOM 1531 OG SER A 232 10.777 -1.980 -24.319 1.00 63.72 O ANISOU 1531 OG SER A 232 7970 10169 6073 -252 710 -1541 O ATOM 1532 N LEU A 233 11.859 0.142 -21.428 1.00 53.97 N ANISOU 1532 N LEU A 233 6810 8502 5193 -334 780 -954 N ATOM 1533 CA LEU A 233 12.078 1.578 -21.342 1.00 51.93 C ANISOU 1533 CA LEU A 233 6545 8313 4875 -426 795 -676 C ATOM 1534 C LEU A 233 13.542 1.884 -21.050 1.00 53.74 C ANISOU 1534 C LEU A 233 6702 8615 5102 -412 885 -631 C ATOM 1535 O LEU A 233 14.146 2.755 -21.680 1.00 55.02 O ANISOU 1535 O LEU A 233 6798 9004 5103 -485 928 -488 O ATOM 1536 CB LEU A 233 11.185 2.178 -20.264 1.00 49.86 C ANISOU 1536 CB LEU A 233 6369 7780 4796 -457 720 -508 C ATOM 1537 CG LEU A 233 11.196 3.692 -20.108 1.00 49.63 C ANISOU 1537 CG LEU A 233 6341 7765 4752 -544 694 -232 C ATOM 1538 CD1 LEU A 233 10.790 4.345 -21.415 1.00 51.44 C ANISOU 1538 CD1 LEU A 233 6542 8238 4764 -632 659 -133 C ATOM 1539 CD2 LEU A 233 10.247 4.090 -18.983 1.00 48.02 C ANISOU 1539 CD2 LEU A 233 6210 7293 4744 -545 616 -139 C ATOM 1540 N ILE A 234 14.106 1.161 -20.088 1.00 52.92 N ANISOU 1540 N ILE A 234 6606 8319 5182 -325 906 -742 N ATOM 1541 CA ILE A 234 15.519 1.290 -19.757 1.00 52.93 C ANISOU 1541 CA ILE A 234 6533 8373 5204 -294 986 -735 C ATOM 1542 C ILE A 234 16.398 1.010 -20.975 1.00 57.72 C ANISOU 1542 C ILE A 234 7015 9324 5590 -279 1071 -873 C ATOM 1543 O ILE A 234 17.362 1.729 -21.236 1.00 59.06 O ANISOU 1543 O ILE A 234 7098 9686 5655 -329 1141 -757 O ATOM 1544 CB ILE A 234 15.905 0.338 -18.617 1.00 50.53 C ANISOU 1544 CB ILE A 234 6258 7808 5132 -192 975 -868 C ATOM 1545 CG1 ILE A 234 15.239 0.782 -17.312 1.00 46.43 C ANISOU 1545 CG1 ILE A 234 5839 7000 4802 -220 911 -702 C ATOM 1546 CG2 ILE A 234 17.416 0.275 -18.452 1.00 51.08 C ANISOU 1546 CG2 ILE A 234 6232 7963 5212 -142 1056 -914 C ATOM 1547 CD1 ILE A 234 15.374 -0.218 -16.193 1.00 44.00 C ANISOU 1547 CD1 ILE A 234 5572 6434 4710 -140 878 -809 C ATOM 1548 N ASN A 235 16.049 -0.028 -21.726 1.00 61.08 N ANISOU 1548 N ASN A 235 7423 9842 5943 -215 1059 -1124 N ATOM 1549 CA ASN A 235 16.836 -0.429 -22.889 1.00 66.63 C ANISOU 1549 CA ASN A 235 7994 10896 6428 -181 1139 -1312 C ATOM 1550 C ASN A 235 16.767 0.591 -24.030 1.00 70.51 C ANISOU 1550 C ASN A 235 8426 11739 6624 -310 1177 -1137 C ATOM 1551 O ASN A 235 17.705 0.724 -24.816 1.00 70.18 O ANISOU 1551 O ASN A 235 8258 11997 6411 -322 1253 -1164 O ATOM 1552 CB ASN A 235 16.378 -1.799 -23.393 1.00 66.86 C ANISOU 1552 CB ASN A 235 8020 10916 6467 -72 1093 -1646 C ATOM 1553 CG ASN A 235 17.291 -2.355 -24.472 1.00 67.86 C ANISOU 1553 CG ASN A 235 7995 11388 6401 -3 1169 -1897 C ATOM 1554 OD1 ASN A 235 18.502 -2.153 -24.434 1.00 67.70 O ANISOU 1554 OD1 ASN A 235 7876 11469 6378 16 1238 -1869 O ATOM 1555 ND2 ASN A 235 16.710 -3.052 -25.446 1.00 68.93 N ANISOU 1555 ND2 ASN A 235 8118 11613 6457 34 1106 -2080 N ATOM 1556 N ASP A 236 15.652 1.309 -24.115 1.00 72.63 N ANISOU 1556 N ASP A 236 8786 11938 6872 -406 1098 -937 N ATOM 1557 CA ASP A 236 15.474 2.322 -25.149 1.00 76.05 C ANISOU 1557 CA ASP A 236 9178 12669 7047 -542 1101 -733 C ATOM 1558 C ASP A 236 15.911 3.700 -24.668 1.00 75.99 C ANISOU 1558 C ASP A 236 9170 12621 7081 -656 1099 -391 C ATOM 1559 O ASP A 236 15.799 4.681 -25.398 1.00 77.69 O ANISOU 1559 O ASP A 236 9358 13017 7142 -783 1069 -162 O ATOM 1560 CB ASP A 236 14.014 2.369 -25.608 1.00 77.34 C ANISOU 1560 CB ASP A 236 9430 12788 7167 -584 995 -705 C ATOM 1561 CG ASP A 236 13.615 1.146 -26.414 1.00 81.51 C ANISOU 1561 CG ASP A 236 9937 13444 7591 -498 988 -1028 C ATOM 1562 OD1 ASP A 236 14.216 0.069 -26.212 1.00 82.77 O ANISOU 1562 OD1 ASP A 236 10052 13566 7829 -374 1032 -1303 O ATOM 1563 OD2 ASP A 236 12.699 1.262 -27.254 1.00 84.32 O ANISOU 1563 OD2 ASP A 236 10315 13924 7798 -552 925 -1012 O ATOM 1564 N MET A 237 16.406 3.774 -23.438 1.00 77.37 N ANISOU 1564 N MET A 237 9376 12528 7494 -608 1106 -352 N ATOM 1565 CA MET A 237 16.811 5.051 -22.865 1.00 80.40 C ANISOU 1565 CA MET A 237 9762 12831 7956 -703 1087 -52 C ATOM 1566 C MET A 237 18.162 5.492 -23.408 1.00 87.24 C ANISOU 1566 C MET A 237 10485 14000 8661 -767 1185 30 C ATOM 1567 O MET A 237 19.014 4.659 -23.718 1.00 89.18 O ANISOU 1567 O MET A 237 10639 14386 8859 -682 1269 -188 O ATOM 1568 CB MET A 237 16.852 4.973 -21.336 1.00 78.10 C ANISOU 1568 CB MET A 237 9549 12161 7964 -629 1055 -49 C ATOM 1569 CG MET A 237 15.580 5.484 -20.668 1.00 77.91 C ANISOU 1569 CG MET A 237 9649 11862 8093 -652 936 76 C ATOM 1570 SD MET A 237 15.469 5.131 -18.901 1.00 73.42 S ANISOU 1570 SD MET A 237 9166 10895 7836 -555 906 25 S ATOM 1571 CE MET A 237 16.865 6.041 -18.261 1.00 55.93 C ANISOU 1571 CE MET A 237 6886 8672 5693 -587 946 193 C ATOM 1572 N PRO A 238 18.350 6.813 -23.546 1.00 89.69 N ANISOU 1572 N PRO A 238 10780 14340 8957 -902 1133 342 N ATOM 1573 CA PRO A 238 19.618 7.413 -23.975 1.00 89.47 C ANISOU 1573 CA PRO A 238 10633 14474 8887 -963 1163 464 C ATOM 1574 C PRO A 238 20.641 7.458 -22.843 1.00 85.10 C ANISOU 1574 C PRO A 238 10049 13779 8505 -920 1222 469 C ATOM 1575 O PRO A 238 20.993 8.535 -22.354 1.00 83.86 O ANISOU 1575 O PRO A 238 9893 13515 8453 -1006 1170 716 O ATOM 1576 CB PRO A 238 19.212 8.830 -24.403 1.00 91.02 C ANISOU 1576 CB PRO A 238 10850 14668 9066 -1119 1040 799 C ATOM 1577 CG PRO A 238 17.710 8.805 -24.518 1.00 90.75 C ANISOU 1577 CG PRO A 238 10929 14540 9013 -1128 953 810 C ATOM 1578 CD PRO A 238 17.269 7.811 -23.498 1.00 89.23 C ANISOU 1578 CD PRO A 238 10813 14163 8928 -1005 1008 589 C ATOM 1579 N ILE A 239 21.104 6.284 -22.428 1.00 78.84 N ANISOU 1579 N ILE A 239 9227 12973 7754 -783 1315 189 N ATOM 1580 CA ILE A 239 22.048 6.167 -21.325 1.00 72.70 C ANISOU 1580 CA ILE A 239 8417 12064 7143 -725 1372 159 C ATOM 1581 C ILE A 239 23.159 5.183 -21.681 1.00 72.85 C ANISOU 1581 C ILE A 239 8313 12245 7122 -615 1466 -101 C ATOM 1582 O ILE A 239 23.039 4.428 -22.647 1.00 73.98 O ANISOU 1582 O ILE A 239 8415 12564 7130 -563 1483 -297 O ATOM 1583 CB ILE A 239 21.348 5.708 -20.022 1.00 68.74 C ANISOU 1583 CB ILE A 239 8064 11137 6919 -615 1293 74 C ATOM 1584 CG1 ILE A 239 20.710 4.331 -20.205 1.00 66.41 C ANISOU 1584 CG1 ILE A 239 7812 10795 6623 -490 1296 -225 C ATOM 1585 CG2 ILE A 239 20.297 6.719 -19.579 1.00 69.36 C ANISOU 1585 CG2 ILE A 239 8261 10997 7094 -696 1171 309 C ATOM 1586 CD1 ILE A 239 19.943 3.852 -18.993 1.00 62.87 C ANISOU 1586 CD1 ILE A 239 7503 9960 6426 -407 1215 -284 C ATOM 1587 N THR A 240 24.237 5.195 -20.901 1.00 71.06 N ANISOU 1587 N THR A 240 8021 11955 7021 -577 1516 -107 N ATOM 1588 CA THR A 240 25.371 4.305 -21.148 1.00 71.33 C ANISOU 1588 CA THR A 240 7930 12125 7047 -466 1592 -350 C ATOM 1589 C THR A 240 24.982 2.835 -20.994 1.00 70.49 C ANISOU 1589 C THR A 240 7854 11930 7000 -296 1602 -700 C ATOM 1590 O THR A 240 23.920 2.515 -20.460 1.00 69.83 O ANISOU 1590 O THR A 240 7906 11608 7019 -262 1537 -734 O ATOM 1591 CB THR A 240 26.549 4.606 -20.197 1.00 69.03 C ANISOU 1591 CB THR A 240 7569 11750 6908 -453 1631 -286 C ATOM 1592 OG1 THR A 240 26.165 4.322 -18.846 1.00 66.16 O ANISOU 1592 OG1 THR A 240 7323 11030 6786 -374 1581 -316 O ATOM 1593 CG2 THR A 240 26.965 6.061 -20.301 1.00 67.70 C ANISOU 1593 CG2 THR A 240 7373 11632 6717 -621 1598 56 C ATOM 1594 N ASN A 241 25.846 1.941 -21.460 1.00 71.20 N ANISOU 1594 N ASN A 241 7831 12149 7072 -186 1640 -949 N ATOM 1595 CA ASN A 241 25.608 0.512 -21.306 1.00 71.56 C ANISOU 1595 CA ASN A 241 7895 12073 7220 -15 1618 -1291 C ATOM 1596 C ASN A 241 25.742 0.066 -19.851 1.00 67.94 C ANISOU 1596 C ASN A 241 7495 11292 7026 82 1599 -1360 C ATOM 1597 O ASN A 241 25.048 -0.851 -19.414 1.00 67.03 O ANISOU 1597 O ASN A 241 7487 10912 7069 177 1512 -1515 O ATOM 1598 CB ASN A 241 26.561 -0.290 -22.188 1.00 76.16 C ANISOU 1598 CB ASN A 241 8332 12868 7736 78 1640 -1535 C ATOM 1599 CG ASN A 241 26.368 -0.003 -23.662 1.00 81.80 C ANISOU 1599 CG ASN A 241 8985 13903 8192 -8 1646 -1503 C ATOM 1600 OD1 ASN A 241 25.300 -0.266 -24.221 1.00 83.16 O ANISOU 1600 OD1 ASN A 241 9230 14087 8282 -16 1599 -1556 O ATOM 1601 ND2 ASN A 241 27.404 0.533 -24.305 1.00 84.12 N ANISOU 1601 ND2 ASN A 241 9139 14467 8356 -75 1700 -1416 N ATOM 1602 N ASP A 242 26.638 0.710 -19.108 1.00 66.00 N ANISOU 1602 N ASP A 242 7211 10987 6881 49 1624 -1198 N ATOM 1603 CA ASP A 242 26.794 0.423 -17.687 1.00 64.44 C ANISOU 1603 CA ASP A 242 7105 10403 6975 122 1547 -1182 C ATOM 1604 C ASP A 242 25.521 0.778 -16.929 1.00 59.98 C ANISOU 1604 C ASP A 242 6738 9526 6525 66 1443 -1004 C ATOM 1605 O ASP A 242 25.097 0.044 -16.038 1.00 58.98 O ANISOU 1605 O ASP A 242 6716 9095 6599 147 1360 -1084 O ATOM 1606 CB ASP A 242 27.980 1.188 -17.095 1.00 67.14 C ANISOU 1606 CB ASP A 242 7361 10767 7381 82 1589 -1023 C ATOM 1607 CG ASP A 242 29.321 0.659 -17.575 1.00 73.08 C ANISOU 1607 CG ASP A 242 7909 11777 8082 167 1682 -1234 C ATOM 1608 OD1 ASP A 242 29.356 -0.039 -18.612 1.00 76.38 O ANISOU 1608 OD1 ASP A 242 8252 12405 8366 226 1708 -1450 O ATOM 1609 OD2 ASP A 242 30.343 0.951 -16.915 1.00 73.88 O ANISOU 1609 OD2 ASP A 242 7940 11836 8296 176 1699 -1171 O ATOM 1610 N GLN A 243 24.916 1.906 -17.288 1.00 56.99 N ANISOU 1610 N GLN A 243 6400 9234 6019 -75 1442 -760 N ATOM 1611 CA GLN A 243 23.702 2.358 -16.630 1.00 55.93 C ANISOU 1611 CA GLN A 243 6432 8839 5982 -128 1346 -597 C ATOM 1612 C GLN A 243 22.538 1.412 -16.921 1.00 53.21 C ANISOU 1612 C GLN A 243 6175 8407 5635 -73 1293 -766 C ATOM 1613 O GLN A 243 21.786 1.054 -16.017 1.00 51.07 O ANISOU 1613 O GLN A 243 6024 7846 5533 -41 1212 -764 O ATOM 1614 CB GLN A 243 23.358 3.784 -17.057 1.00 59.13 C ANISOU 1614 CB GLN A 243 6842 9363 6260 -285 1339 -313 C ATOM 1615 CG GLN A 243 24.070 4.861 -16.247 1.00 61.52 C ANISOU 1615 CG GLN A 243 7129 9573 6672 -349 1324 -89 C ATOM 1616 CD GLN A 243 23.903 6.254 -16.843 1.00 64.96 C ANISOU 1616 CD GLN A 243 7543 10154 6987 -510 1303 188 C ATOM 1617 OE1 GLN A 243 23.678 6.410 -18.045 1.00 67.79 O ANISOU 1617 OE1 GLN A 243 7848 10781 7131 -583 1337 215 O ATOM 1618 NE2 GLN A 243 24.017 7.273 -16.003 1.00 64.12 N ANISOU 1618 NE2 GLN A 243 7474 9867 7022 -567 1235 396 N ATOM 1619 N LYS A 244 22.401 1.008 -18.180 1.00 53.85 N ANISOU 1619 N LYS A 244 6187 8753 5521 -68 1337 -912 N ATOM 1620 CA LYS A 244 21.376 0.047 -18.576 1.00 52.36 C ANISOU 1620 CA LYS A 244 6064 8503 5327 -12 1281 -1101 C ATOM 1621 C LYS A 244 21.508 -1.250 -17.794 1.00 50.61 C ANISOU 1621 C LYS A 244 5877 8020 5334 126 1224 -1321 C ATOM 1622 O LYS A 244 20.523 -1.772 -17.278 1.00 49.84 O ANISOU 1622 O LYS A 244 5895 7674 5367 142 1133 -1343 O ATOM 1623 CB LYS A 244 21.452 -0.249 -20.073 1.00 53.33 C ANISOU 1623 CB LYS A 244 6079 8990 5193 -10 1343 -1265 C ATOM 1624 CG LYS A 244 20.882 0.840 -20.953 1.00 54.74 C ANISOU 1624 CG LYS A 244 6259 9400 5141 -158 1358 -1049 C ATOM 1625 CD LYS A 244 20.978 0.457 -22.430 1.00 58.04 C ANISOU 1625 CD LYS A 244 6563 10210 5282 -154 1420 -1228 C ATOM 1626 CE LYS A 244 20.455 1.564 -23.336 1.00 59.10 C ANISOU 1626 CE LYS A 244 6703 10548 5206 -312 1403 -970 C ATOM 1627 NZ LYS A 244 20.513 1.179 -24.778 1.00 62.58 N ANISOU 1627 NZ LYS A 244 7060 11264 5455 -305 1397 -1098 N ATOM 1628 N LYS A 245 22.731 -1.761 -17.708 1.00 50.28 N ANISOU 1628 N LYS A 245 5724 8035 5344 219 1268 -1474 N ATOM 1629 CA LYS A 245 22.997 -3.009 -17.006 1.00 52.33 C ANISOU 1629 CA LYS A 245 6001 8047 5836 354 1195 -1683 C ATOM 1630 C LYS A 245 22.676 -2.850 -15.521 1.00 48.17 C ANISOU 1630 C LYS A 245 5603 7166 5533 330 1116 -1499 C ATOM 1631 O LYS A 245 21.991 -3.680 -14.927 1.00 46.44 O ANISOU 1631 O LYS A 245 5479 6686 5479 369 1014 -1561 O ATOM 1632 CB LYS A 245 24.458 -3.439 -17.215 1.00 59.02 C ANISOU 1632 CB LYS A 245 6685 9046 6693 459 1257 -1872 C ATOM 1633 CG LYS A 245 24.813 -4.817 -16.660 1.00 64.47 C ANISOU 1633 CG LYS A 245 7371 9494 7629 615 1162 -2124 C ATOM 1634 CD LYS A 245 24.120 -5.957 -17.412 1.00 69.07 C ANISOU 1634 CD LYS A 245 7961 10068 8215 697 1090 -2406 C ATOM 1635 CE LYS A 245 24.880 -6.362 -18.668 1.00 74.07 C ANISOU 1635 CE LYS A 245 8412 11053 8679 788 1164 -2695 C ATOM 1636 NZ LYS A 245 24.358 -7.632 -19.257 1.00 75.92 N ANISOU 1636 NZ LYS A 245 8662 11192 8991 879 1036 -2950 N ATOM 1637 N LEU A 246 23.158 -1.760 -14.937 1.00 46.77 N ANISOU 1637 N LEU A 246 5423 6993 5354 259 1157 -1269 N ATOM 1638 CA LEU A 246 22.912 -1.462 -13.534 1.00 45.25 C ANISOU 1638 CA LEU A 246 5338 6513 5341 232 1090 -1093 C ATOM 1639 C LEU A 246 21.413 -1.361 -13.218 1.00 43.69 C ANISOU 1639 C LEU A 246 5278 6157 5164 168 1019 -991 C ATOM 1640 O LEU A 246 20.931 -1.944 -12.239 1.00 42.23 O ANISOU 1640 O LEU A 246 5182 5719 5146 190 937 -985 O ATOM 1641 CB LEU A 246 23.617 -0.163 -13.148 1.00 44.96 C ANISOU 1641 CB LEU A 246 5265 6546 5273 158 1142 -872 C ATOM 1642 CG LEU A 246 23.301 0.336 -11.743 1.00 44.60 C ANISOU 1642 CG LEU A 246 5324 6242 5381 125 1075 -689 C ATOM 1643 CD1 LEU A 246 24.044 -0.498 -10.711 1.00 44.96 C ANISOU 1643 CD1 LEU A 246 5369 6092 5623 219 1028 -774 C ATOM 1644 CD2 LEU A 246 23.637 1.810 -11.603 1.00 44.12 C ANISOU 1644 CD2 LEU A 246 5238 6261 5263 30 1106 -461 C ATOM 1645 N MET A 247 20.683 -0.624 -14.050 1.00 41.50 N ANISOU 1645 N MET A 247 5011 6043 4715 83 1046 -903 N ATOM 1646 CA MET A 247 19.250 -0.442 -13.846 1.00 40.21 C ANISOU 1646 CA MET A 247 4959 5759 4560 22 982 -812 C ATOM 1647 C MET A 247 18.465 -1.736 -14.079 1.00 41.84 C ANISOU 1647 C MET A 247 5209 5866 4824 75 918 -1004 C ATOM 1648 O MET A 247 17.496 -2.010 -13.376 1.00 39.46 O ANISOU 1648 O MET A 247 5000 5365 4628 52 844 -955 O ATOM 1649 CB MET A 247 18.716 0.665 -14.759 1.00 38.93 C ANISOU 1649 CB MET A 247 4786 5798 4206 -77 1011 -674 C ATOM 1650 CG MET A 247 19.247 2.056 -14.434 1.00 36.56 C ANISOU 1650 CG MET A 247 4462 5544 3886 -152 1036 -444 C ATOM 1651 SD MET A 247 18.643 3.319 -15.570 1.00 41.68 S ANISOU 1651 SD MET A 247 5095 6414 4330 -277 1038 -264 S ATOM 1652 CE MET A 247 17.069 3.775 -14.848 1.00 33.53 C ANISOU 1652 CE MET A 247 4189 5154 3397 -316 934 -148 C ATOM 1653 N SER A 248 18.891 -2.529 -15.061 1.00 43.74 N ANISOU 1653 N SER A 248 5373 6252 4996 144 940 -1228 N ATOM 1654 CA SER A 248 18.182 -3.757 -15.407 1.00 44.99 C ANISOU 1654 CA SER A 248 5561 6318 5214 197 863 -1432 C ATOM 1655 C SER A 248 18.335 -4.827 -14.332 1.00 45.97 C ANISOU 1655 C SER A 248 5729 6143 5593 266 769 -1506 C ATOM 1656 O SER A 248 17.404 -5.588 -14.065 1.00 47.35 O ANISOU 1656 O SER A 248 5977 6134 5879 258 672 -1546 O ATOM 1657 CB SER A 248 18.668 -4.301 -16.751 1.00 46.83 C ANISOU 1657 CB SER A 248 5686 6804 5304 267 905 -1683 C ATOM 1658 OG SER A 248 18.341 -3.407 -17.799 1.00 47.67 O ANISOU 1658 OG SER A 248 5760 7194 5159 186 973 -1602 O ATOM 1659 N ASN A 249 19.507 -4.880 -13.711 1.00 45.58 N ANISOU 1659 N ASN A 249 5632 6045 5642 323 788 -1508 N ATOM 1660 CA ASN A 249 19.766 -5.867 -12.674 1.00 46.86 C ANISOU 1660 CA ASN A 249 5830 5927 6049 384 686 -1558 C ATOM 1661 C ASN A 249 19.296 -5.412 -11.306 1.00 45.20 C ANISOU 1661 C ASN A 249 5719 5517 5938 305 648 -1312 C ATOM 1662 O ASN A 249 19.427 -6.147 -10.326 1.00 47.04 O ANISOU 1662 O ASN A 249 5991 5520 6362 330 556 -1301 O ATOM 1663 CB ASN A 249 21.253 -6.205 -12.627 1.00 50.26 C ANISOU 1663 CB ASN A 249 6155 6394 6549 492 709 -1690 C ATOM 1664 CG ASN A 249 21.728 -6.879 -13.895 1.00 55.48 C ANISOU 1664 CG ASN A 249 6701 7246 7135 593 732 -1986 C ATOM 1665 OD1 ASN A 249 22.763 -6.515 -14.455 1.00 58.89 O ANISOU 1665 OD1 ASN A 249 7009 7912 7455 637 830 -2061 O ATOM 1666 ND2 ASN A 249 20.961 -7.858 -14.368 1.00 55.79 N ANISOU 1666 ND2 ASN A 249 6770 7201 7229 629 639 -2163 N ATOM 1667 N ASN A 250 18.753 -4.199 -11.240 1.00 41.44 N ANISOU 1667 N ASN A 250 5277 5137 5333 211 708 -1117 N ATOM 1668 CA ASN A 250 18.229 -3.676 -9.986 1.00 39.24 C ANISOU 1668 CA ASN A 250 5078 4707 5124 141 676 -907 C ATOM 1669 C ASN A 250 16.930 -2.899 -10.171 1.00 38.43 C ANISOU 1669 C ASN A 250 5030 4659 4914 47 685 -784 C ATOM 1670 O ASN A 250 16.756 -1.836 -9.569 1.00 37.46 O ANISOU 1670 O ASN A 250 4928 4545 4761 -7 708 -612 O ATOM 1671 CB ASN A 250 19.267 -2.783 -9.307 1.00 40.04 C ANISOU 1671 CB ASN A 250 5146 4835 5232 144 728 -784 C ATOM 1672 CG ASN A 250 20.539 -3.527 -8.968 1.00 44.17 C ANISOU 1672 CG ASN A 250 5614 5288 5882 238 709 -892 C ATOM 1673 OD1 ASN A 250 20.625 -4.198 -7.935 1.00 44.98 O ANISOU 1673 OD1 ASN A 250 5759 5186 6146 257 626 -870 O ATOM 1674 ND2 ASN A 250 21.542 -3.415 -9.841 1.00 44.77 N ANISOU 1674 ND2 ASN A 250 5584 5544 5882 293 780 -1007 N ATOM 1675 N VAL A 251 16.018 -3.426 -10.993 1.00 38.86 N ANISOU 1675 N VAL A 251 5099 4744 4921 34 655 -883 N ATOM 1676 CA VAL A 251 14.781 -2.704 -11.304 1.00 38.60 C ANISOU 1676 CA VAL A 251 5105 4778 4784 -48 658 -783 C ATOM 1677 C VAL A 251 13.950 -2.417 -10.062 1.00 36.65 C ANISOU 1677 C VAL A 251 4922 4384 4621 -109 615 -625 C ATOM 1678 O VAL A 251 13.268 -1.397 -10.001 1.00 36.82 O ANISOU 1678 O VAL A 251 4956 4465 4567 -165 630 -504 O ATOM 1679 CB VAL A 251 13.882 -3.456 -12.320 1.00 43.43 C ANISOU 1679 CB VAL A 251 5724 5428 5349 -51 616 -927 C ATOM 1680 CG1 VAL A 251 14.572 -3.557 -13.653 1.00 44.61 C ANISOU 1680 CG1 VAL A 251 5799 5787 5364 1 668 -1085 C ATOM 1681 CG2 VAL A 251 13.485 -4.838 -11.802 1.00 44.07 C ANISOU 1681 CG2 VAL A 251 5843 5293 5607 -33 514 -1022 C ATOM 1682 N GLN A 252 14.007 -3.298 -9.070 1.00 37.72 N ANISOU 1682 N GLN A 252 5087 4337 4907 -100 554 -627 N ATOM 1683 CA GLN A 252 13.209 -3.085 -7.869 1.00 40.06 C ANISOU 1683 CA GLN A 252 5429 4532 5258 -166 518 -481 C ATOM 1684 C GLN A 252 13.697 -1.835 -7.142 1.00 38.92 C ANISOU 1684 C GLN A 252 5274 4437 5077 -171 569 -345 C ATOM 1685 O GLN A 252 12.889 -1.099 -6.572 1.00 39.01 O ANISOU 1685 O GLN A 252 5301 4463 5059 -222 567 -239 O ATOM 1686 CB GLN A 252 13.243 -4.312 -6.945 1.00 43.42 C ANISOU 1686 CB GLN A 252 5885 4767 5847 -171 433 -485 C ATOM 1687 CG GLN A 252 14.565 -4.562 -6.222 1.00 48.73 C ANISOU 1687 CG GLN A 252 6543 5356 6615 -112 424 -478 C ATOM 1688 CD GLN A 252 15.590 -5.285 -7.079 1.00 55.17 C ANISOU 1688 CD GLN A 252 7316 6169 7478 -17 417 -659 C ATOM 1689 OE1 GLN A 252 15.466 -5.344 -8.303 1.00 57.62 O ANISOU 1689 OE1 GLN A 252 7596 6591 7705 11 446 -791 O ATOM 1690 NE2 GLN A 252 16.607 -5.846 -6.435 1.00 58.01 N ANISOU 1690 NE2 GLN A 252 7663 6413 7966 38 374 -677 N ATOM 1691 N ILE A 253 15.005 -1.576 -7.182 1.00 37.11 N ANISOU 1691 N ILE A 253 5008 4238 4853 -115 609 -361 N ATOM 1692 CA ILE A 253 15.537 -0.344 -6.601 1.00 35.98 C ANISOU 1692 CA ILE A 253 4847 4139 4683 -121 646 -241 C ATOM 1693 C ILE A 253 15.181 0.855 -7.474 1.00 33.33 C ANISOU 1693 C ILE A 253 4491 3952 4223 -153 684 -192 C ATOM 1694 O ILE A 253 14.825 1.923 -6.963 1.00 34.64 O ANISOU 1694 O ILE A 253 4662 4125 4376 -183 676 -82 O ATOM 1695 CB ILE A 253 17.067 -0.391 -6.425 1.00 39.61 C ANISOU 1695 CB ILE A 253 5264 4594 5192 -59 672 -266 C ATOM 1696 CG1 ILE A 253 17.479 -1.599 -5.590 1.00 40.75 C ANISOU 1696 CG1 ILE A 253 5428 4578 5476 -23 613 -311 C ATOM 1697 CG2 ILE A 253 17.561 0.888 -5.768 1.00 37.61 C ANISOU 1697 CG2 ILE A 253 4994 4370 4927 -72 694 -139 C ATOM 1698 CD1 ILE A 253 16.957 -1.539 -4.187 1.00 41.62 C ANISOU 1698 CD1 ILE A 253 5587 4584 5643 -69 564 -188 C ATOM 1699 N VAL A 254 15.289 0.681 -8.790 1.00 32.03 N ANISOU 1699 N VAL A 254 4295 3906 3968 -145 715 -276 N ATOM 1700 CA VAL A 254 14.871 1.718 -9.726 1.00 33.33 C ANISOU 1700 CA VAL A 254 4440 4217 4005 -190 734 -214 C ATOM 1701 C VAL A 254 13.429 2.141 -9.424 1.00 34.85 C ANISOU 1701 C VAL A 254 4677 4367 4197 -240 684 -147 C ATOM 1702 O VAL A 254 13.135 3.335 -9.331 1.00 35.47 O ANISOU 1702 O VAL A 254 4750 4477 4252 -271 668 -36 O ATOM 1703 CB VAL A 254 14.998 1.245 -11.199 1.00 32.08 C ANISOU 1703 CB VAL A 254 4245 4215 3728 -181 767 -332 C ATOM 1704 CG1 VAL A 254 14.400 2.268 -12.153 1.00 30.90 C ANISOU 1704 CG1 VAL A 254 4084 4217 3441 -244 767 -244 C ATOM 1705 CG2 VAL A 254 16.463 0.970 -11.554 1.00 33.64 C ANISOU 1705 CG2 VAL A 254 4372 4500 3910 -128 826 -408 C ATOM 1706 N ARG A 255 12.549 1.160 -9.227 1.00 33.72 N ANISOU 1706 N ARG A 255 4570 4146 4098 -246 648 -217 N ATOM 1707 CA ARG A 255 11.143 1.437 -8.917 1.00 34.89 C ANISOU 1707 CA ARG A 255 4744 4267 4248 -293 604 -169 C ATOM 1708 C ARG A 255 10.988 2.304 -7.681 1.00 34.70 C ANISOU 1708 C ARG A 255 4719 4190 4276 -302 590 -62 C ATOM 1709 O ARG A 255 10.151 3.203 -7.640 1.00 35.27 O ANISOU 1709 O ARG A 255 4782 4295 4324 -325 562 -6 O ATOM 1710 CB ARG A 255 10.350 0.137 -8.711 1.00 35.32 C ANISOU 1710 CB ARG A 255 4827 4232 4362 -310 564 -247 C ATOM 1711 CG ARG A 255 10.025 -0.589 -9.984 1.00 37.12 C ANISOU 1711 CG ARG A 255 5053 4516 4535 -308 552 -369 C ATOM 1712 CD ARG A 255 9.044 -1.739 -9.779 1.00 38.15 C ANISOU 1712 CD ARG A 255 5209 4544 4742 -342 489 -428 C ATOM 1713 NE ARG A 255 8.882 -2.454 -11.037 1.00 39.41 N ANISOU 1713 NE ARG A 255 5364 4755 4857 -326 468 -572 N ATOM 1714 CZ ARG A 255 8.060 -2.076 -12.011 1.00 39.61 C ANISOU 1714 CZ ARG A 255 5381 4892 4775 -353 459 -593 C ATOM 1715 NH1 ARG A 255 7.298 -0.999 -11.861 1.00 38.37 N ANISOU 1715 NH1 ARG A 255 5222 4791 4568 -395 460 -475 N ATOM 1716 NH2 ARG A 255 7.991 -2.782 -13.133 1.00 40.08 N ANISOU 1716 NH2 ARG A 255 5433 5010 4786 -332 436 -743 N ATOM 1717 N GLN A 256 11.791 2.022 -6.663 1.00 35.89 N ANISOU 1717 N GLN A 256 4873 4261 4501 -276 599 -45 N ATOM 1718 CA GLN A 256 11.657 2.719 -5.391 1.00 35.78 C ANISOU 1718 CA GLN A 256 4855 4208 4530 -278 582 34 C ATOM 1719 C GLN A 256 12.147 4.153 -5.463 1.00 37.76 C ANISOU 1719 C GLN A 256 5077 4505 4765 -263 581 101 C ATOM 1720 O GLN A 256 11.718 5.000 -4.683 1.00 40.55 O ANISOU 1720 O GLN A 256 5417 4848 5142 -261 549 144 O ATOM 1721 CB GLN A 256 12.401 1.963 -4.308 1.00 35.49 C ANISOU 1721 CB GLN A 256 4832 4082 4572 -260 581 38 C ATOM 1722 CG GLN A 256 11.652 0.723 -3.897 1.00 41.64 C ANISOU 1722 CG GLN A 256 5637 4795 5389 -299 550 16 C ATOM 1723 CD GLN A 256 12.299 0.018 -2.750 1.00 46.53 C ANISOU 1723 CD GLN A 256 6270 5323 6087 -296 527 51 C ATOM 1724 OE1 GLN A 256 13.515 0.116 -2.553 1.00 49.60 O ANISOU 1724 OE1 GLN A 256 6653 5682 6511 -248 539 51 O ATOM 1725 NE2 GLN A 256 11.498 -0.709 -1.978 1.00 47.30 N ANISOU 1725 NE2 GLN A 256 6381 5382 6211 -356 488 91 N ATOM 1726 N GLN A 257 13.041 4.423 -6.404 1.00 37.47 N ANISOU 1726 N GLN A 257 5022 4525 4691 -253 609 105 N ATOM 1727 CA GLN A 257 13.572 5.763 -6.568 1.00 38.60 C ANISOU 1727 CA GLN A 257 5133 4704 4829 -257 594 192 C ATOM 1728 C GLN A 257 12.851 6.510 -7.683 1.00 40.49 C ANISOU 1728 C GLN A 257 5361 5026 4996 -297 563 234 C ATOM 1729 O GLN A 257 13.282 7.585 -8.089 1.00 46.30 O ANISOU 1729 O GLN A 257 6068 5799 5725 -318 537 325 O ATOM 1730 CB GLN A 257 15.075 5.707 -6.849 1.00 38.10 C ANISOU 1730 CB GLN A 257 5038 4671 4767 -239 640 200 C ATOM 1731 CG GLN A 257 15.888 5.114 -5.705 1.00 37.56 C ANISOU 1731 CG GLN A 257 4975 4510 4784 -196 652 173 C ATOM 1732 CD GLN A 257 17.382 5.336 -5.890 1.00 41.48 C ANISOU 1732 CD GLN A 257 5424 5040 5297 -176 687 193 C ATOM 1733 OE1 GLN A 257 18.021 4.677 -6.707 1.00 42.24 O ANISOU 1733 OE1 GLN A 257 5492 5207 5353 -162 737 129 O ATOM 1734 NE2 GLN A 257 17.940 6.287 -5.143 1.00 43.85 N ANISOU 1734 NE2 GLN A 257 5705 5300 5658 -173 657 270 N ATOM 1735 N SER A 258 11.758 5.939 -8.181 1.00 35.75 N ANISOU 1735 N SER A 258 4782 4451 4350 -315 555 179 N ATOM 1736 CA SER A 258 11.011 6.554 -9.275 1.00 33.09 C ANISOU 1736 CA SER A 258 4436 4197 3939 -354 516 217 C ATOM 1737 C SER A 258 9.683 7.127 -8.803 1.00 31.89 C ANISOU 1737 C SER A 258 4285 4000 3831 -358 444 231 C ATOM 1738 O SER A 258 9.148 6.706 -7.775 1.00 31.57 O ANISOU 1738 O SER A 258 4252 3897 3846 -339 444 183 O ATOM 1739 CB SER A 258 10.758 5.539 -10.390 1.00 33.00 C ANISOU 1739 CB SER A 258 4436 4272 3830 -369 550 131 C ATOM 1740 OG SER A 258 11.960 5.176 -11.030 1.00 33.98 O ANISOU 1740 OG SER A 258 4537 4478 3895 -360 611 104 O ATOM 1741 N TYR A 259 9.161 8.088 -9.560 1.00 32.13 N ANISOU 1741 N TYR A 259 4300 4073 3834 -386 377 299 N ATOM 1742 CA TYR A 259 7.827 8.636 -9.322 1.00 32.87 C ANISOU 1742 CA TYR A 259 4380 4137 3970 -382 297 294 C ATOM 1743 C TYR A 259 6.939 8.451 -10.538 1.00 34.59 C ANISOU 1743 C TYR A 259 4605 4436 4103 -421 266 288 C ATOM 1744 O TYR A 259 7.409 8.487 -11.676 1.00 34.53 O ANISOU 1744 O TYR A 259 4601 4518 3999 -459 275 335 O ATOM 1745 CB TYR A 259 7.884 10.125 -8.988 1.00 33.46 C ANISOU 1745 CB TYR A 259 4423 4156 4133 -367 200 378 C ATOM 1746 CG TYR A 259 8.578 10.472 -7.701 1.00 33.44 C ANISOU 1746 CG TYR A 259 4407 4073 4226 -321 205 370 C ATOM 1747 CD1 TYR A 259 9.953 10.686 -7.669 1.00 33.78 C ANISOU 1747 CD1 TYR A 259 4450 4104 4280 -327 235 432 C ATOM 1748 CD2 TYR A 259 7.859 10.620 -6.523 1.00 32.52 C ANISOU 1748 CD2 TYR A 259 4266 3912 4179 -273 178 295 C ATOM 1749 CE1 TYR A 259 10.593 11.021 -6.495 1.00 34.91 C ANISOU 1749 CE1 TYR A 259 4580 4173 4511 -284 230 421 C ATOM 1750 CE2 TYR A 259 8.490 10.954 -5.342 1.00 32.32 C ANISOU 1750 CE2 TYR A 259 4223 3831 4224 -230 178 277 C ATOM 1751 CZ TYR A 259 9.857 11.150 -5.334 1.00 34.87 C ANISOU 1751 CZ TYR A 259 4558 4125 4567 -234 199 341 C ATOM 1752 OH TYR A 259 10.498 11.481 -4.168 1.00 36.88 O ANISOU 1752 OH TYR A 259 4796 4325 4892 -191 190 320 O ATOM 1753 N SER A 260 5.650 8.257 -10.290 1.00 35.16 N ANISOU 1753 N SER A 260 4668 4493 4200 -416 229 229 N ATOM 1754 CA SER A 260 4.665 8.308 -11.355 1.00 36.55 C ANISOU 1754 CA SER A 260 4841 4732 4314 -449 172 230 C ATOM 1755 C SER A 260 3.726 9.483 -11.095 1.00 37.63 C ANISOU 1755 C SER A 260 4935 4826 4535 -430 57 266 C ATOM 1756 O SER A 260 3.088 9.571 -10.043 1.00 36.97 O ANISOU 1756 O SER A 260 4818 4694 4534 -391 44 204 O ATOM 1757 CB SER A 260 3.891 6.998 -11.455 1.00 36.66 C ANISOU 1757 CB SER A 260 4870 4768 4292 -464 213 120 C ATOM 1758 OG SER A 260 3.055 7.030 -12.592 1.00 39.48 O ANISOU 1758 OG SER A 260 5225 5198 4579 -497 156 118 O ATOM 1759 N ILE A 261 3.656 10.391 -12.060 1.00 38.47 N ANISOU 1759 N ILE A 261 5036 4961 4620 -458 -35 365 N ATOM 1760 CA ILE A 261 2.935 11.642 -11.888 1.00 38.02 C ANISOU 1760 CA ILE A 261 4935 4838 4672 -432 -175 409 C ATOM 1761 C ILE A 261 1.771 11.759 -12.870 1.00 39.76 C ANISOU 1761 C ILE A 261 5144 5108 4854 -459 -265 419 C ATOM 1762 O ILE A 261 1.973 11.866 -14.085 1.00 40.69 O ANISOU 1762 O ILE A 261 5286 5305 4871 -520 -297 512 O ATOM 1763 CB ILE A 261 3.879 12.838 -12.065 1.00 38.28 C ANISOU 1763 CB ILE A 261 4964 4822 4761 -446 -253 551 C ATOM 1764 CG1 ILE A 261 5.061 12.720 -11.101 1.00 37.67 C ANISOU 1764 CG1 ILE A 261 4893 4696 4723 -418 -168 538 C ATOM 1765 CG2 ILE A 261 3.132 14.153 -11.862 1.00 39.21 C ANISOU 1765 CG2 ILE A 261 5033 4838 5027 -409 -429 585 C ATOM 1766 CD1 ILE A 261 6.295 13.468 -11.565 1.00 38.54 C ANISOU 1766 CD1 ILE A 261 5007 4803 4834 -465 -196 690 C ATOM 1767 N MET A 262 0.554 11.725 -12.336 1.00 39.19 N ANISOU 1767 N MET A 262 5027 5010 4852 -418 -307 320 N ATOM 1768 CA MET A 262 -0.642 11.842 -13.157 1.00 40.59 C ANISOU 1768 CA MET A 262 5183 5226 5013 -436 -402 315 C ATOM 1769 C MET A 262 -0.649 13.199 -13.835 1.00 42.85 C ANISOU 1769 C MET A 262 5455 5468 5358 -444 -569 451 C ATOM 1770 O MET A 262 -0.457 14.219 -13.185 1.00 45.00 O ANISOU 1770 O MET A 262 5693 5635 5771 -396 -656 478 O ATOM 1771 CB MET A 262 -1.903 11.650 -12.311 1.00 41.69 C ANISOU 1771 CB MET A 262 5254 5352 5235 -385 -416 181 C ATOM 1772 CG MET A 262 -3.185 12.007 -13.039 1.00 42.13 C ANISOU 1772 CG MET A 262 5267 5430 5312 -387 -543 172 C ATOM 1773 SD MET A 262 -3.408 10.991 -14.509 1.00 48.70 S ANISOU 1773 SD MET A 262 6159 6375 5969 -475 -512 196 S ATOM 1774 CE MET A 262 -4.602 11.989 -15.407 1.00 52.50 C ANISOU 1774 CE MET A 262 6592 6853 6502 -471 -717 249 C ATOM 1775 N SER A 263 -0.861 13.213 -15.145 1.00 43.62 N ANISOU 1775 N SER A 263 5577 5644 5351 -510 -628 541 N ATOM 1776 CA SER A 263 -0.697 14.437 -15.913 1.00 44.00 C ANISOU 1776 CA SER A 263 5621 5661 5435 -547 -791 716 C ATOM 1777 C SER A 263 -1.990 14.897 -16.599 1.00 47.60 C ANISOU 1777 C SER A 263 6044 6115 5927 -548 -955 734 C ATOM 1778 O SER A 263 -2.621 15.860 -16.160 1.00 49.36 O ANISOU 1778 O SER A 263 6211 6216 6328 -488 -1107 728 O ATOM 1779 CB SER A 263 0.414 14.247 -16.944 1.00 43.61 C ANISOU 1779 CB SER A 263 5623 5735 5212 -643 -733 857 C ATOM 1780 OG SER A 263 0.571 15.413 -17.726 1.00 46.59 O ANISOU 1780 OG SER A 263 5993 6098 5611 -704 -899 1061 O ATOM 1781 N ILE A 264 -2.381 14.219 -17.675 1.00 48.24 N ANISOU 1781 N ILE A 264 6154 6330 5846 -610 -936 744 N ATOM 1782 CA ILE A 264 -3.553 14.634 -18.441 1.00 52.82 C ANISOU 1782 CA ILE A 264 6705 6920 6444 -621 -1100 777 C ATOM 1783 C ILE A 264 -4.439 13.479 -18.846 1.00 53.86 C ANISOU 1783 C ILE A 264 6839 7159 6465 -631 -1032 641 C ATOM 1784 O ILE A 264 -3.960 12.375 -19.108 1.00 54.99 O ANISOU 1784 O ILE A 264 7027 7409 6457 -666 -881 580 O ATOM 1785 CB ILE A 264 -3.168 15.353 -19.745 1.00 57.93 C ANISOU 1785 CB ILE A 264 7381 7636 6994 -718 -1226 1003 C ATOM 1786 CG1 ILE A 264 -2.083 14.550 -20.463 1.00 59.85 C ANISOU 1786 CG1 ILE A 264 7680 8059 7000 -801 -1069 1048 C ATOM 1787 CG2 ILE A 264 -2.723 16.771 -19.476 1.00 59.74 C ANISOU 1787 CG2 ILE A 264 7588 7716 7394 -715 -1388 1164 C ATOM 1788 CD1 ILE A 264 -1.714 15.080 -21.808 1.00 62.99 C ANISOU 1788 CD1 ILE A 264 8095 8593 7244 -915 -1164 1265 C ATOM 1789 N ILE A 265 -5.735 13.747 -18.931 1.00 55.31 N ANISOU 1789 N ILE A 265 6969 7310 6737 -598 -1158 591 N ATOM 1790 CA ILE A 265 -6.631 12.833 -19.615 1.00 59.52 C ANISOU 1790 CA ILE A 265 7503 7951 7163 -628 -1143 503 C ATOM 1791 C ILE A 265 -7.558 13.660 -20.515 1.00 64.52 C ANISOU 1791 C ILE A 265 8105 8583 7827 -643 -1359 598 C ATOM 1792 O ILE A 265 -8.522 14.278 -20.060 1.00 65.15 O ANISOU 1792 O ILE A 265 8109 8565 8082 -576 -1484 548 O ATOM 1793 CB ILE A 265 -7.404 11.932 -18.614 1.00 59.54 C ANISOU 1793 CB ILE A 265 7455 7931 7237 -575 -1040 301 C ATOM 1794 CG1 ILE A 265 -8.468 11.106 -19.331 1.00 61.50 C ANISOU 1794 CG1 ILE A 265 7690 8268 7409 -609 -1061 217 C ATOM 1795 CG2 ILE A 265 -7.990 12.736 -17.457 1.00 59.26 C ANISOU 1795 CG2 ILE A 265 7329 7777 7410 -483 -1107 238 C ATOM 1796 CD1 ILE A 265 -9.150 10.116 -18.416 1.00 61.49 C ANISOU 1796 CD1 ILE A 265 7639 8261 7465 -587 -956 46 C ATOM 1797 N LYS A 266 -7.214 13.703 -21.800 1.00 67.19 N ANISOU 1797 N LYS A 266 8496 9042 7993 -732 -1408 737 N ATOM 1798 CA LYS A 266 -7.979 14.458 -22.791 1.00 70.61 C ANISOU 1798 CA LYS A 266 8910 9492 8425 -767 -1623 862 C ATOM 1799 C LYS A 266 -7.763 13.897 -24.192 1.00 70.77 C ANISOU 1799 C LYS A 266 8987 9724 8180 -870 -1608 936 C ATOM 1800 O LYS A 266 -6.713 13.323 -24.483 1.00 69.27 O ANISOU 1800 O LYS A 266 8847 9657 7814 -920 -1460 949 O ATOM 1801 CB LYS A 266 -7.600 15.942 -22.756 1.00 73.16 C ANISOU 1801 CB LYS A 266 9220 9688 8891 -770 -1803 1063 C ATOM 1802 CG LYS A 266 -6.167 16.239 -23.166 1.00 74.94 C ANISOU 1802 CG LYS A 266 9503 9978 8990 -858 -1752 1252 C ATOM 1803 CD LYS A 266 -5.758 17.647 -22.747 1.00 77.67 C ANISOU 1803 CD LYS A 266 9826 10142 9543 -846 -1918 1417 C ATOM 1804 CE LYS A 266 -6.151 18.694 -23.779 1.00 81.64 C ANISOU 1804 CE LYS A 266 10322 10629 10070 -920 -2184 1653 C ATOM 1805 NZ LYS A 266 -5.181 18.751 -24.909 1.00 83.85 N ANISOU 1805 NZ LYS A 266 10655 11098 10108 -1074 -2169 1892 N ATOM 1806 N GLU A 267 -8.770 14.066 -25.047 1.00 72.74 N ANISOU 1806 N GLU A 267 9217 10024 8398 -895 -1766 969 N ATOM 1807 CA GLU A 267 -8.713 13.609 -26.433 1.00 74.20 C ANISOU 1807 CA GLU A 267 9443 10430 8320 -991 -1780 1032 C ATOM 1808 C GLU A 267 -8.352 12.129 -26.534 1.00 70.45 C ANISOU 1808 C GLU A 267 9003 10095 7670 -997 -1566 840 C ATOM 1809 O GLU A 267 -7.420 11.758 -27.250 1.00 70.33 O ANISOU 1809 O GLU A 267 9030 10259 7433 -1062 -1477 884 O ATOM 1810 CB GLU A 267 -7.713 14.449 -27.232 1.00 78.83 C ANISOU 1810 CB GLU A 267 10065 11114 8775 -1093 -1848 1299 C ATOM 1811 CG GLU A 267 -8.147 15.893 -27.439 1.00 84.00 C ANISOU 1811 CG GLU A 267 10690 11639 9588 -1112 -2114 1522 C ATOM 1812 CD GLU A 267 -7.078 16.732 -28.117 1.00 88.13 C ANISOU 1812 CD GLU A 267 11242 12247 9998 -1232 -2181 1815 C ATOM 1813 OE1 GLU A 267 -5.881 16.494 -27.853 1.00 88.13 O ANISOU 1813 OE1 GLU A 267 11266 12308 9913 -1259 -2012 1830 O ATOM 1814 OE2 GLU A 267 -7.431 17.628 -28.914 1.00 91.33 O ANISOU 1814 OE2 GLU A 267 11639 12660 10403 -1306 -2410 2039 O ATOM 1815 N GLU A 268 -9.090 11.300 -25.797 1.00 68.50 N ANISOU 1815 N GLU A 268 8727 9767 7532 -930 -1494 626 N ATOM 1816 CA GLU A 268 -8.917 9.845 -25.803 1.00 67.66 C ANISOU 1816 CA GLU A 268 8646 9745 7316 -929 -1325 429 C ATOM 1817 C GLU A 268 -7.528 9.374 -25.348 1.00 62.52 C ANISOU 1817 C GLU A 268 8037 9113 6604 -926 -1138 403 C ATOM 1818 O GLU A 268 -7.113 8.257 -25.661 1.00 62.31 O ANISOU 1818 O GLU A 268 8040 9189 6446 -936 -1020 270 O ATOM 1819 CB GLU A 268 -9.211 9.283 -27.200 1.00 72.57 C ANISOU 1819 CB GLU A 268 9291 10573 7710 -993 -1374 403 C ATOM 1820 CG GLU A 268 -10.667 9.367 -27.627 1.00 76.56 C ANISOU 1820 CG GLU A 268 9753 11068 8270 -991 -1538 370 C ATOM 1821 CD GLU A 268 -10.899 8.775 -29.007 1.00 81.75 C ANISOU 1821 CD GLU A 268 10434 11941 8685 -1053 -1586 332 C ATOM 1822 OE1 GLU A 268 -9.958 8.803 -29.832 1.00 84.19 O ANISOU 1822 OE1 GLU A 268 10784 12435 8768 -1111 -1547 414 O ATOM 1823 OE2 GLU A 268 -12.017 8.274 -29.267 1.00 82.90 O ANISOU 1823 OE2 GLU A 268 10549 12088 8861 -1046 -1662 214 O ATOM 1824 N VAL A 269 -6.808 10.210 -24.609 1.00 59.52 N ANISOU 1824 N VAL A 269 7656 8627 6331 -905 -1121 517 N ATOM 1825 CA VAL A 269 -5.482 9.822 -24.140 1.00 57.78 C ANISOU 1825 CA VAL A 269 7468 8418 6067 -900 -953 498 C ATOM 1826 C VAL A 269 -5.303 10.033 -22.639 1.00 53.58 C ANISOU 1826 C VAL A 269 6916 7693 5750 -829 -891 459 C ATOM 1827 O VAL A 269 -5.553 11.118 -22.119 1.00 53.51 O ANISOU 1827 O VAL A 269 6874 7561 5896 -800 -995 554 O ATOM 1828 CB VAL A 269 -4.367 10.598 -24.872 1.00 60.35 C ANISOU 1828 CB VAL A 269 7815 8865 6251 -969 -970 701 C ATOM 1829 CG1 VAL A 269 -3.003 10.160 -24.362 1.00 59.73 C ANISOU 1829 CG1 VAL A 269 7757 8802 6135 -957 -793 665 C ATOM 1830 CG2 VAL A 269 -4.461 10.395 -26.376 1.00 63.00 C ANISOU 1830 CG2 VAL A 269 8163 9441 6334 -1049 -1022 748 C ATOM 1831 N LEU A 270 -4.876 8.983 -21.947 1.00 50.78 N ANISOU 1831 N LEU A 270 6576 7311 5406 -798 -734 312 N ATOM 1832 CA LEU A 270 -4.399 9.120 -20.577 1.00 48.40 C ANISOU 1832 CA LEU A 270 6264 6867 5258 -744 -653 291 C ATOM 1833 C LEU A 270 -2.875 9.168 -20.590 1.00 48.01 C ANISOU 1833 C LEU A 270 6253 6861 5129 -759 -551 359 C ATOM 1834 O LEU A 270 -2.228 8.257 -21.098 1.00 49.40 O ANISOU 1834 O LEU A 270 6458 7146 5164 -780 -451 289 O ATOM 1835 CB LEU A 270 -4.885 7.967 -19.695 1.00 46.34 C ANISOU 1835 CB LEU A 270 5990 6542 5076 -711 -558 113 C ATOM 1836 CG LEU A 270 -4.152 7.841 -18.352 1.00 43.80 C ANISOU 1836 CG LEU A 270 5667 6114 4859 -668 -447 87 C ATOM 1837 CD1 LEU A 270 -4.346 9.093 -17.528 1.00 42.01 C ANISOU 1837 CD1 LEU A 270 5393 5786 4781 -622 -521 162 C ATOM 1838 CD2 LEU A 270 -4.616 6.616 -17.569 1.00 43.73 C ANISOU 1838 CD2 LEU A 270 5647 6061 4910 -661 -364 -59 C ATOM 1839 N ALA A 271 -2.302 10.231 -20.038 1.00 46.69 N ANISOU 1839 N ALA A 271 6074 6607 5058 -746 -585 485 N ATOM 1840 CA ALA A 271 -0.851 10.345 -19.969 1.00 45.77 C ANISOU 1840 CA ALA A 271 5982 6526 4884 -764 -493 558 C ATOM 1841 C ALA A 271 -0.377 10.645 -18.550 1.00 44.65 C ANISOU 1841 C ALA A 271 5827 6224 4912 -702 -444 540 C ATOM 1842 O ALA A 271 -0.890 11.546 -17.882 1.00 44.43 O ANISOU 1842 O ALA A 271 5766 6071 5045 -663 -543 576 O ATOM 1843 CB ALA A 271 -0.348 11.423 -20.936 1.00 45.87 C ANISOU 1843 CB ALA A 271 5993 6627 4809 -838 -593 773 C ATOM 1844 N TYR A 272 0.595 9.870 -18.085 1.00 44.12 N ANISOU 1844 N TYR A 272 5783 6167 4815 -687 -299 471 N ATOM 1845 CA TYR A 272 1.264 10.190 -16.837 1.00 43.18 C ANISOU 1845 CA TYR A 272 5655 5923 4827 -640 -252 475 C ATOM 1846 C TYR A 272 2.771 10.176 -17.046 1.00 45.03 C ANISOU 1846 C TYR A 272 5907 6220 4981 -666 -165 543 C ATOM 1847 O TYR A 272 3.293 9.450 -17.897 1.00 45.30 O ANISOU 1847 O TYR A 272 5956 6397 4858 -700 -90 512 O ATOM 1848 CB TYR A 272 0.856 9.233 -15.708 1.00 40.06 C ANISOU 1848 CB TYR A 272 5258 5449 4515 -587 -167 315 C ATOM 1849 CG TYR A 272 0.868 7.744 -16.030 1.00 40.29 C ANISOU 1849 CG TYR A 272 5316 5542 4452 -600 -69 186 C ATOM 1850 CD1 TYR A 272 -0.235 7.129 -16.619 1.00 40.37 C ANISOU 1850 CD1 TYR A 272 5322 5597 4421 -620 -108 107 C ATOM 1851 CD2 TYR A 272 1.959 6.945 -15.692 1.00 38.53 C ANISOU 1851 CD2 TYR A 272 5118 5316 4204 -587 46 134 C ATOM 1852 CE1 TYR A 272 -0.238 5.764 -16.896 1.00 40.99 C ANISOU 1852 CE1 TYR A 272 5424 5710 4441 -630 -42 -22 C ATOM 1853 CE2 TYR A 272 1.967 5.578 -15.962 1.00 38.23 C ANISOU 1853 CE2 TYR A 272 5102 5309 4114 -590 110 2 C ATOM 1854 CZ TYR A 272 0.867 4.991 -16.561 1.00 41.60 C ANISOU 1854 CZ TYR A 272 5527 5771 4508 -612 62 -76 C ATOM 1855 OH TYR A 272 0.869 3.632 -16.828 1.00 41.87 O ANISOU 1855 OH TYR A 272 5580 5814 4514 -614 103 -216 O ATOM 1856 N VAL A 273 3.462 11.008 -16.276 1.00 44.36 N ANISOU 1856 N VAL A 273 5808 6038 5007 -647 -181 625 N ATOM 1857 CA VAL A 273 4.907 11.140 -16.389 1.00 40.47 C ANISOU 1857 CA VAL A 273 5319 5598 4462 -676 -110 704 C ATOM 1858 C VAL A 273 5.579 10.220 -15.389 1.00 38.79 C ANISOU 1858 C VAL A 273 5118 5331 4290 -619 23 577 C ATOM 1859 O VAL A 273 5.300 10.293 -14.195 1.00 38.89 O ANISOU 1859 O VAL A 273 5127 5211 4440 -563 18 521 O ATOM 1860 CB VAL A 273 5.359 12.596 -16.148 1.00 38.33 C ANISOU 1860 CB VAL A 273 5022 5239 4302 -697 -222 879 C ATOM 1861 CG1 VAL A 273 6.884 12.692 -16.082 1.00 37.25 C ANISOU 1861 CG1 VAL A 273 4875 5146 4130 -727 -140 955 C ATOM 1862 CG2 VAL A 273 4.796 13.509 -17.231 1.00 38.62 C ANISOU 1862 CG2 VAL A 273 5046 5326 4300 -768 -375 1038 C ATOM 1863 N VAL A 274 6.448 9.339 -15.871 1.00 38.24 N ANISOU 1863 N VAL A 274 5056 5373 4099 -632 135 523 N ATOM 1864 CA VAL A 274 7.250 8.530 -14.964 1.00 38.30 C ANISOU 1864 CA VAL A 274 5073 5321 4159 -581 243 423 C ATOM 1865 C VAL A 274 8.657 9.108 -14.896 1.00 38.86 C ANISOU 1865 C VAL A 274 5118 5419 4226 -597 279 525 C ATOM 1866 O VAL A 274 9.321 9.297 -15.912 1.00 41.40 O ANISOU 1866 O VAL A 274 5415 5898 4418 -653 299 598 O ATOM 1867 CB VAL A 274 7.295 7.045 -15.383 1.00 39.37 C ANISOU 1867 CB VAL A 274 5225 5528 4206 -563 330 260 C ATOM 1868 CG1 VAL A 274 8.344 6.299 -14.570 1.00 37.69 C ANISOU 1868 CG1 VAL A 274 5015 5254 4051 -515 423 183 C ATOM 1869 CG2 VAL A 274 5.917 6.399 -15.193 1.00 38.32 C ANISOU 1869 CG2 VAL A 274 5113 5332 4114 -550 292 159 C ATOM 1870 N GLN A 275 9.081 9.414 -13.679 1.00 37.74 N ANISOU 1870 N GLN A 275 4976 5140 4223 -555 283 532 N ATOM 1871 CA GLN A 275 10.340 10.085 -13.421 1.00 36.16 C ANISOU 1871 CA GLN A 275 4748 4933 4058 -568 297 633 C ATOM 1872 C GLN A 275 11.338 9.054 -12.912 1.00 37.98 C ANISOU 1872 C GLN A 275 4978 5165 4286 -523 416 526 C ATOM 1873 O GLN A 275 11.205 8.551 -11.791 1.00 38.79 O ANISOU 1873 O GLN A 275 5104 5147 4489 -465 436 439 O ATOM 1874 CB GLN A 275 10.122 11.203 -12.409 1.00 34.47 C ANISOU 1874 CB GLN A 275 4527 4559 4012 -544 196 703 C ATOM 1875 CG GLN A 275 11.281 12.149 -12.175 1.00 36.02 C ANISOU 1875 CG GLN A 275 4690 4723 4274 -570 168 832 C ATOM 1876 CD GLN A 275 10.980 13.135 -11.037 1.00 36.40 C ANISOU 1876 CD GLN A 275 4730 4594 4507 -523 58 848 C ATOM 1877 OE1 GLN A 275 10.157 14.047 -11.184 1.00 36.37 O ANISOU 1877 OE1 GLN A 275 4716 4528 4574 -531 -76 906 O ATOM 1878 NE2 GLN A 275 11.636 12.939 -9.895 1.00 32.77 N ANISOU 1878 NE2 GLN A 275 4269 4055 4128 -468 104 784 N ATOM 1879 N LEU A 276 12.309 8.714 -13.755 1.00 38.11 N ANISOU 1879 N LEU A 276 4963 5334 4185 -550 490 528 N ATOM 1880 CA LEU A 276 13.279 7.665 -13.455 1.00 38.75 C ANISOU 1880 CA LEU A 276 5031 5429 4261 -499 594 406 C ATOM 1881 C LEU A 276 14.610 8.245 -12.979 1.00 38.19 C ANISOU 1881 C LEU A 276 4916 5347 4246 -503 620 491 C ATOM 1882 O LEU A 276 15.050 9.293 -13.464 1.00 37.34 O ANISOU 1882 O LEU A 276 4768 5314 4107 -572 585 647 O ATOM 1883 CB LEU A 276 13.515 6.794 -14.695 1.00 40.08 C ANISOU 1883 CB LEU A 276 5172 5793 4263 -508 663 305 C ATOM 1884 CG LEU A 276 12.317 6.028 -15.259 1.00 41.91 C ANISOU 1884 CG LEU A 276 5442 6048 4435 -501 640 191 C ATOM 1885 CD1 LEU A 276 12.700 5.337 -16.554 1.00 45.68 C ANISOU 1885 CD1 LEU A 276 5877 6747 4733 -508 700 87 C ATOM 1886 CD2 LEU A 276 11.811 5.018 -14.255 1.00 38.27 C ANISOU 1886 CD2 LEU A 276 5029 5407 4103 -435 640 58 C ATOM 1887 N PRO A 277 15.271 7.549 -12.047 1.00 36.36 N ANISOU 1887 N PRO A 277 4689 5023 4102 -437 671 398 N ATOM 1888 CA PRO A 277 16.575 8.005 -11.568 1.00 37.33 C ANISOU 1888 CA PRO A 277 4765 5135 4283 -435 696 463 C ATOM 1889 C PRO A 277 17.628 7.898 -12.647 1.00 38.40 C ANISOU 1889 C PRO A 277 4821 5482 4288 -471 772 474 C ATOM 1890 O PRO A 277 17.647 6.903 -13.362 1.00 39.85 O ANISOU 1890 O PRO A 277 4990 5783 4369 -445 835 339 O ATOM 1891 CB PRO A 277 16.882 7.042 -10.420 1.00 35.22 C ANISOU 1891 CB PRO A 277 4526 4732 4123 -351 727 340 C ATOM 1892 CG PRO A 277 16.163 5.809 -10.779 1.00 35.32 C ANISOU 1892 CG PRO A 277 4575 4756 4091 -320 751 194 C ATOM 1893 CD PRO A 277 14.902 6.248 -11.470 1.00 36.37 C ANISOU 1893 CD PRO A 277 4733 4934 4152 -370 700 237 C ATOM 1894 N LEU A 278 18.465 8.921 -12.780 1.00 39.05 N ANISOU 1894 N LEU A 278 4844 5620 4373 -534 758 629 N ATOM 1895 CA LEU A 278 19.688 8.824 -13.565 1.00 38.01 C ANISOU 1895 CA LEU A 278 4612 5700 4130 -569 844 643 C ATOM 1896 C LEU A 278 20.845 8.594 -12.610 1.00 36.46 C ANISOU 1896 C LEU A 278 4381 5418 4054 -510 882 599 C ATOM 1897 O LEU A 278 21.004 9.347 -11.655 1.00 36.01 O ANISOU 1897 O LEU A 278 4344 5199 4139 -514 816 694 O ATOM 1898 CB LEU A 278 19.937 10.091 -14.376 1.00 44.76 C ANISOU 1898 CB LEU A 278 5407 6692 4905 -698 801 870 C ATOM 1899 CG LEU A 278 19.249 10.336 -15.717 1.00 52.19 C ANISOU 1899 CG LEU A 278 6338 7828 5663 -786 783 945 C ATOM 1900 CD1 LEU A 278 19.844 11.593 -16.343 1.00 53.10 C ANISOU 1900 CD1 LEU A 278 6377 8075 5725 -929 736 1204 C ATOM 1901 CD2 LEU A 278 19.372 9.132 -16.668 1.00 56.36 C ANISOU 1901 CD2 LEU A 278 6825 8587 6001 -750 898 758 C ATOM 1902 N TYR A 279 21.650 7.564 -12.853 1.00 37.21 N ANISOU 1902 N TYR A 279 4419 5617 4101 -451 978 444 N ATOM 1903 CA TYR A 279 22.796 7.281 -11.985 1.00 37.46 C ANISOU 1903 CA TYR A 279 4409 5573 4251 -390 1008 395 C ATOM 1904 C TYR A 279 24.093 7.782 -12.608 1.00 38.79 C ANISOU 1904 C TYR A 279 4443 5951 4344 -450 1071 476 C ATOM 1905 O TYR A 279 24.749 7.060 -13.356 1.00 41.32 O ANISOU 1905 O TYR A 279 4673 6473 4555 -422 1163 351 O ATOM 1906 CB TYR A 279 22.900 5.782 -11.686 1.00 36.96 C ANISOU 1906 CB TYR A 279 4363 5451 4228 -271 1049 164 C ATOM 1907 CG TYR A 279 21.679 5.241 -10.987 1.00 37.51 C ANISOU 1907 CG TYR A 279 4554 5316 4380 -228 986 104 C ATOM 1908 CD1 TYR A 279 21.444 5.515 -9.643 1.00 35.81 C ANISOU 1908 CD1 TYR A 279 4407 4886 4314 -208 920 161 C ATOM 1909 CD2 TYR A 279 20.745 4.470 -11.670 1.00 38.63 C ANISOU 1909 CD2 TYR A 279 4735 5500 4444 -213 988 -10 C ATOM 1910 CE1 TYR A 279 20.316 5.032 -8.999 1.00 33.86 C ANISOU 1910 CE1 TYR A 279 4254 4487 4124 -183 869 118 C ATOM 1911 CE2 TYR A 279 19.609 3.976 -11.028 1.00 35.23 C ANISOU 1911 CE2 TYR A 279 4404 4893 4090 -189 929 -51 C ATOM 1912 CZ TYR A 279 19.404 4.261 -9.697 1.00 33.40 C ANISOU 1912 CZ TYR A 279 4229 4467 3994 -178 874 19 C ATOM 1913 OH TYR A 279 18.285 3.782 -9.058 1.00 33.35 O ANISOU 1913 OH TYR A 279 4303 4321 4046 -167 823 -11 O ATOM 1914 N GLY A 280 24.460 9.021 -12.298 1.00 36.71 N ANISOU 1914 N GLY A 280 4156 5646 4145 -534 1014 679 N ATOM 1915 CA GLY A 280 25.623 9.640 -12.910 1.00 37.25 C ANISOU 1915 CA GLY A 280 4090 5921 4143 -623 1060 801 C ATOM 1916 C GLY A 280 26.937 9.249 -12.265 1.00 38.31 C ANISOU 1916 C GLY A 280 4143 6042 4372 -559 1113 722 C ATOM 1917 O GLY A 280 28.007 9.545 -12.790 1.00 41.38 O ANISOU 1917 O GLY A 280 4396 6633 4694 -621 1173 784 O ATOM 1918 N VAL A 281 26.857 8.596 -11.112 1.00 37.10 N ANISOU 1918 N VAL A 281 4066 5659 4371 -443 1084 593 N ATOM 1919 CA VAL A 281 28.048 8.105 -10.427 1.00 38.67 C ANISOU 1919 CA VAL A 281 4198 5821 4674 -368 1119 502 C ATOM 1920 C VAL A 281 27.892 6.621 -10.133 1.00 38.98 C ANISOU 1920 C VAL A 281 4279 5786 4748 -230 1148 262 C ATOM 1921 O VAL A 281 26.971 6.214 -9.425 1.00 38.66 O ANISOU 1921 O VAL A 281 4363 5544 4783 -180 1087 215 O ATOM 1922 CB VAL A 281 28.318 8.867 -9.108 1.00 36.31 C ANISOU 1922 CB VAL A 281 3942 5292 4563 -368 1023 611 C ATOM 1923 CG1 VAL A 281 29.562 8.317 -8.427 1.00 36.40 C ANISOU 1923 CG1 VAL A 281 3881 5271 4678 -289 1052 516 C ATOM 1924 CG2 VAL A 281 28.474 10.357 -9.373 1.00 34.59 C ANISOU 1924 CG2 VAL A 281 3682 5111 4349 -505 964 848 C ATOM 1925 N ILE A 282 28.799 5.821 -10.686 1.00 41.06 N ANISOU 1925 N ILE A 282 4426 6216 4959 -172 1233 110 N ATOM 1926 CA ILE A 282 28.730 4.370 -10.579 1.00 45.47 C ANISOU 1926 CA ILE A 282 5004 6711 5560 -40 1245 -133 C ATOM 1927 C ILE A 282 30.116 3.794 -10.274 1.00 46.26 C ANISOU 1927 C ILE A 282 4985 6842 5751 48 1279 -257 C ATOM 1928 O ILE A 282 31.113 4.255 -10.824 1.00 47.78 O ANISOU 1928 O ILE A 282 5030 7252 5871 6 1350 -221 O ATOM 1929 CB ILE A 282 28.180 3.740 -11.883 1.00 50.35 C ANISOU 1929 CB ILE A 282 5595 7532 6003 -32 1304 -271 C ATOM 1930 CG1 ILE A 282 26.743 4.182 -12.133 1.00 51.38 C ANISOU 1930 CG1 ILE A 282 5848 7610 6063 -105 1257 -166 C ATOM 1931 CG2 ILE A 282 28.215 2.234 -11.823 1.00 50.46 C ANISOU 1931 CG2 ILE A 282 5612 7473 6088 110 1297 -539 C ATOM 1932 CD1 ILE A 282 26.194 3.685 -13.452 1.00 53.37 C ANISOU 1932 CD1 ILE A 282 6072 8078 6129 -111 1307 -284 C ATOM 1933 N ASP A 283 30.172 2.812 -9.374 1.00 44.73 N ANISOU 1933 N ASP A 283 4849 6429 5718 163 1219 -388 N ATOM 1934 CA ASP A 283 31.387 2.018 -9.135 1.00 45.44 C ANISOU 1934 CA ASP A 283 4828 6525 5911 273 1231 -549 C ATOM 1935 C ASP A 283 32.544 2.789 -8.517 1.00 42.63 C ANISOU 1935 C ASP A 283 4388 6175 5636 245 1233 -430 C ATOM 1936 O ASP A 283 33.703 2.412 -8.679 1.00 44.83 O ANISOU 1936 O ASP A 283 4521 6563 5948 309 1275 -544 O ATOM 1937 CB ASP A 283 31.880 1.372 -10.438 1.00 49.28 C ANISOU 1937 CB ASP A 283 5165 7292 6268 325 1326 -755 C ATOM 1938 CG ASP A 283 30.974 0.259 -10.917 1.00 51.80 C ANISOU 1938 CG ASP A 283 5550 7565 6565 400 1300 -950 C ATOM 1939 OD1 ASP A 283 30.299 -0.364 -10.072 1.00 49.48 O ANISOU 1939 OD1 ASP A 283 5393 6989 6416 446 1199 -968 O ATOM 1940 OD2 ASP A 283 30.944 0.001 -12.140 1.00 56.88 O ANISOU 1940 OD2 ASP A 283 6103 8465 7044 407 1376 -1083 O ATOM 1941 N THR A 284 32.241 3.874 -7.822 1.00 40.33 N ANISOU 1941 N THR A 284 4174 5770 5380 153 1182 -214 N ATOM 1942 CA THR A 284 33.252 4.529 -7.010 1.00 38.47 C ANISOU 1942 CA THR A 284 3882 5478 5258 137 1152 -110 C ATOM 1943 C THR A 284 33.213 3.895 -5.619 1.00 38.01 C ANISOU 1943 C THR A 284 3925 5136 5380 229 1049 -156 C ATOM 1944 O THR A 284 32.182 3.351 -5.204 1.00 38.04 O ANISOU 1944 O THR A 284 4065 4981 5406 258 994 -186 O ATOM 1945 CB THR A 284 33.022 6.050 -6.909 1.00 36.28 C ANISOU 1945 CB THR A 284 3627 5205 4951 -2 1124 134 C ATOM 1946 OG1 THR A 284 31.793 6.296 -6.216 1.00 33.37 O ANISOU 1946 OG1 THR A 284 3429 4632 4620 -16 1040 203 O ATOM 1947 CG2 THR A 284 32.974 6.687 -8.299 1.00 34.48 C ANISOU 1947 CG2 THR A 284 3307 5256 4538 -115 1208 217 C ATOM 1948 N PRO A 285 34.336 3.956 -4.895 1.00 36.85 N ANISOU 1948 N PRO A 285 3706 4937 5357 268 1019 -152 N ATOM 1949 CA PRO A 285 34.364 3.402 -3.538 1.00 35.97 C ANISOU 1949 CA PRO A 285 3687 4575 5407 344 911 -173 C ATOM 1950 C PRO A 285 33.361 4.076 -2.604 1.00 36.34 C ANISOU 1950 C PRO A 285 3888 4454 5466 284 832 -25 C ATOM 1951 O PRO A 285 33.254 5.304 -2.591 1.00 36.56 O ANISOU 1951 O PRO A 285 3914 4518 5458 193 829 120 O ATOM 1952 CB PRO A 285 35.803 3.677 -3.077 1.00 37.40 C ANISOU 1952 CB PRO A 285 3741 4776 5693 369 899 -162 C ATOM 1953 CG PRO A 285 36.595 3.830 -4.352 1.00 37.92 C ANISOU 1953 CG PRO A 285 3626 5123 5661 347 1018 -219 C ATOM 1954 CD PRO A 285 35.651 4.474 -5.320 1.00 36.81 C ANISOU 1954 CD PRO A 285 3521 5121 5345 239 1081 -130 C ATOM 1955 N CYS A 286 32.624 3.266 -1.849 1.00 36.15 N ANISOU 1955 N CYS A 286 3986 4256 5495 333 761 -67 N ATOM 1956 CA CYS A 286 31.771 3.750 -0.767 1.00 34.76 C ANISOU 1956 CA CYS A 286 3939 3935 5336 294 682 46 C ATOM 1957 C CYS A 286 32.147 3.078 0.543 1.00 35.58 C ANISOU 1957 C CYS A 286 4086 3870 5565 357 585 32 C ATOM 1958 O CYS A 286 32.627 1.947 0.541 1.00 38.94 O ANISOU 1958 O CYS A 286 4484 4244 6067 436 562 -75 O ATOM 1959 CB CYS A 286 30.296 3.473 -1.048 1.00 33.94 C ANISOU 1959 CB CYS A 286 3944 3807 5145 264 687 42 C ATOM 1960 SG CYS A 286 29.603 4.373 -2.407 1.00 39.48 S ANISOU 1960 SG CYS A 286 4624 4683 5694 176 770 93 S ATOM 1961 N TRP A 287 31.910 3.753 1.661 1.00 33.13 N ANISOU 1961 N TRP A 287 3839 3475 5275 326 515 135 N ATOM 1962 CA TRP A 287 32.107 3.114 2.956 1.00 34.61 C ANISOU 1962 CA TRP A 287 4080 3520 5551 371 415 142 C ATOM 1963 C TRP A 287 31.078 3.602 3.970 1.00 34.89 C ANISOU 1963 C TRP A 287 4223 3500 5534 324 358 230 C ATOM 1964 O TRP A 287 30.581 4.724 3.883 1.00 33.29 O ANISOU 1964 O TRP A 287 4030 3350 5270 271 376 285 O ATOM 1965 CB TRP A 287 33.535 3.341 3.482 1.00 33.95 C ANISOU 1965 CB TRP A 287 3906 3420 5574 411 375 145 C ATOM 1966 CG TRP A 287 33.952 4.792 3.643 1.00 35.80 C ANISOU 1966 CG TRP A 287 4091 3710 5801 358 377 232 C ATOM 1967 CD1 TRP A 287 33.977 5.519 4.803 1.00 35.90 C ANISOU 1967 CD1 TRP A 287 4141 3656 5841 341 292 303 C ATOM 1968 CD2 TRP A 287 34.419 5.678 2.608 1.00 36.72 C ANISOU 1968 CD2 TRP A 287 4105 3959 5888 308 453 257 C ATOM 1969 NE1 TRP A 287 34.426 6.798 4.553 1.00 34.99 N ANISOU 1969 NE1 TRP A 287 3958 3599 5739 291 299 361 N ATOM 1970 CE2 TRP A 287 34.702 6.917 3.221 1.00 36.30 C ANISOU 1970 CE2 TRP A 287 4037 3884 5871 261 396 351 C ATOM 1971 CE3 TRP A 287 34.619 5.538 1.231 1.00 37.95 C ANISOU 1971 CE3 TRP A 287 4173 4261 5984 293 558 211 C ATOM 1972 CZ2 TRP A 287 35.176 8.012 2.494 1.00 37.37 C ANISOU 1972 CZ2 TRP A 287 4078 4117 6004 189 430 423 C ATOM 1973 CZ3 TRP A 287 35.086 6.627 0.517 1.00 37.88 C ANISOU 1973 CZ3 TRP A 287 4067 4380 5944 217 605 289 C ATOM 1974 CH2 TRP A 287 35.362 7.848 1.152 1.00 37.97 C ANISOU 1974 CH2 TRP A 287 4070 4344 6011 160 536 405 C ATOM 1975 N LYS A 288 30.751 2.742 4.928 1.00 34.92 N ANISOU 1975 N LYS A 288 4299 3403 5565 341 282 242 N ATOM 1976 CA LYS A 288 29.771 3.093 5.942 1.00 33.32 C ANISOU 1976 CA LYS A 288 4183 3185 5293 295 234 315 C ATOM 1977 C LYS A 288 30.447 3.316 7.292 1.00 32.90 C ANISOU 1977 C LYS A 288 4129 3087 5284 312 141 364 C ATOM 1978 O LYS A 288 31.128 2.426 7.814 1.00 32.00 O ANISOU 1978 O LYS A 288 4011 2895 5252 351 74 365 O ATOM 1979 CB LYS A 288 28.690 2.013 6.064 1.00 32.82 C ANISOU 1979 CB LYS A 288 4202 3076 5191 272 216 320 C ATOM 1980 CG LYS A 288 27.467 2.484 6.857 1.00 31.90 C ANISOU 1980 CG LYS A 288 4153 3001 4966 213 199 384 C ATOM 1981 CD LYS A 288 26.381 1.418 6.905 1.00 31.85 C ANISOU 1981 CD LYS A 288 4215 2965 4924 172 184 404 C ATOM 1982 CE LYS A 288 25.233 1.861 7.810 1.00 31.83 C ANISOU 1982 CE LYS A 288 4257 3035 4802 111 170 464 C ATOM 1983 NZ LYS A 288 24.214 0.788 7.975 1.00 31.63 N ANISOU 1983 NZ LYS A 288 4287 2988 4744 52 147 509 N ATOM 1984 N LEU A 289 30.253 4.516 7.833 1.00 31.37 N ANISOU 1984 N LEU A 289 3935 2940 5044 288 125 396 N ATOM 1985 CA LEU A 289 30.783 4.887 9.139 1.00 32.27 C ANISOU 1985 CA LEU A 289 4046 3035 5178 302 34 428 C ATOM 1986 C LEU A 289 29.723 4.690 10.235 1.00 32.49 C ANISOU 1986 C LEU A 289 4152 3093 5098 269 -14 467 C ATOM 1987 O LEU A 289 28.650 5.305 10.194 1.00 31.49 O ANISOU 1987 O LEU A 289 4051 3034 4879 236 17 457 O ATOM 1988 CB LEU A 289 31.276 6.344 9.118 1.00 29.52 C ANISOU 1988 CB LEU A 289 3637 2719 4858 300 25 422 C ATOM 1989 CG LEU A 289 31.794 6.878 10.457 1.00 29.38 C ANISOU 1989 CG LEU A 289 3613 2691 4859 319 -79 434 C ATOM 1990 CD1 LEU A 289 32.839 5.938 11.055 1.00 28.66 C ANISOU 1990 CD1 LEU A 289 3507 2540 4844 358 -140 451 C ATOM 1991 CD2 LEU A 289 32.352 8.281 10.317 1.00 28.47 C ANISOU 1991 CD2 LEU A 289 3429 2580 4807 315 -104 422 C ATOM 1992 N HIS A 290 30.032 3.819 11.196 1.00 32.76 N ANISOU 1992 N HIS A 290 4215 3088 5145 274 -93 514 N ATOM 1993 CA HIS A 290 29.169 3.575 12.348 1.00 31.92 C ANISOU 1993 CA HIS A 290 4167 3042 4921 229 -144 571 C ATOM 1994 C HIS A 290 29.798 4.183 13.584 1.00 33.97 C ANISOU 1994 C HIS A 290 4405 3340 5161 247 -231 583 C ATOM 1995 O HIS A 290 30.985 4.005 13.818 1.00 37.38 O ANISOU 1995 O HIS A 290 4805 3703 5696 288 -290 591 O ATOM 1996 CB HIS A 290 28.952 2.082 12.586 1.00 32.82 C ANISOU 1996 CB HIS A 290 4331 3090 5049 198 -191 647 C ATOM 1997 CG HIS A 290 28.816 1.273 11.335 1.00 35.12 C ANISOU 1997 CG HIS A 290 4628 3298 5419 207 -137 612 C ATOM 1998 ND1 HIS A 290 27.603 0.791 10.886 1.00 36.00 N ANISOU 1998 ND1 HIS A 290 4785 3428 5466 153 -94 624 N ATOM 1999 CD2 HIS A 290 29.746 0.828 10.455 1.00 33.80 C ANISOU 1999 CD2 HIS A 290 4416 3039 5388 267 -126 551 C ATOM 2000 CE1 HIS A 290 27.792 0.091 9.782 1.00 34.52 C ANISOU 2000 CE1 HIS A 290 4588 3156 5373 182 -64 568 C ATOM 2001 NE2 HIS A 290 29.081 0.100 9.498 1.00 34.46 N ANISOU 2001 NE2 HIS A 290 4521 3089 5481 254 -79 516 N ATOM 2002 N THR A 291 29.011 4.898 14.381 1.00 34.02 N ANISOU 2002 N THR A 291 4422 3468 5037 224 -244 569 N ATOM 2003 CA THR A 291 29.530 5.516 15.593 1.00 33.64 C ANISOU 2003 CA THR A 291 4350 3479 4952 246 -332 556 C ATOM 2004 C THR A 291 28.623 5.257 16.805 1.00 34.96 C ANISOU 2004 C THR A 291 4548 3798 4936 195 -369 598 C ATOM 2005 O THR A 291 27.416 5.050 16.661 1.00 35.07 O ANISOU 2005 O THR A 291 4586 3894 4843 146 -311 607 O ATOM 2006 CB THR A 291 29.707 7.034 15.411 1.00 34.75 C ANISOU 2006 CB THR A 291 4437 3640 5128 287 -331 453 C ATOM 2007 OG1 THR A 291 28.425 7.673 15.387 1.00 34.69 O ANISOU 2007 OG1 THR A 291 4435 3734 5010 270 -290 394 O ATOM 2008 CG2 THR A 291 30.449 7.342 14.113 1.00 34.30 C ANISOU 2008 CG2 THR A 291 4339 3470 5225 310 -281 436 C ATOM 2009 N SER A 292 29.217 5.267 17.995 1.00 33.38 N ANISOU 2009 N SER A 292 4338 3652 4691 202 -466 625 N ATOM 2010 CA SER A 292 28.493 4.987 19.228 1.00 33.11 C ANISOU 2010 CA SER A 292 4321 3799 4462 145 -507 677 C ATOM 2011 C SER A 292 29.113 5.798 20.368 1.00 33.15 C ANISOU 2011 C SER A 292 4285 3902 4409 187 -599 614 C ATOM 2012 O SER A 292 30.285 6.161 20.295 1.00 32.53 O ANISOU 2012 O SER A 292 4181 3710 4470 246 -654 583 O ATOM 2013 CB SER A 292 28.529 3.488 19.523 1.00 34.19 C ANISOU 2013 CB SER A 292 4510 3892 4590 73 -554 848 C ATOM 2014 OG SER A 292 27.548 3.112 20.469 1.00 36.26 O ANISOU 2014 OG SER A 292 4785 4349 4644 -16 -567 929 O ATOM 2015 N PRO A 293 28.327 6.117 21.413 1.00 35.23 N ANISOU 2015 N PRO A 293 4530 4390 4464 159 -615 583 N ATOM 2016 CA PRO A 293 28.875 6.983 22.470 1.00 35.22 C ANISOU 2016 CA PRO A 293 4482 4497 4402 211 -707 487 C ATOM 2017 C PRO A 293 30.062 6.389 23.221 1.00 36.24 C ANISOU 2017 C PRO A 293 4624 4579 4566 208 -822 591 C ATOM 2018 O PRO A 293 30.071 5.200 23.559 1.00 35.36 O ANISOU 2018 O PRO A 293 4556 4471 4408 134 -855 761 O ATOM 2019 CB PRO A 293 27.684 7.179 23.413 1.00 35.21 C ANISOU 2019 CB PRO A 293 4453 4786 4140 171 -690 441 C ATOM 2020 CG PRO A 293 26.488 7.024 22.526 1.00 34.51 C ANISOU 2020 CG PRO A 293 4377 4703 4034 135 -572 437 C ATOM 2021 CD PRO A 293 26.876 5.915 21.578 1.00 34.75 C ANISOU 2021 CD PRO A 293 4472 4512 4219 92 -544 593 C ATOM 2022 N LEU A 294 31.058 7.242 23.461 1.00 37.22 N ANISOU 2022 N LEU A 294 4707 4648 4789 285 -897 491 N ATOM 2023 CA LEU A 294 32.269 6.891 24.199 1.00 36.79 C ANISOU 2023 CA LEU A 294 4649 4548 4780 298 -1020 559 C ATOM 2024 C LEU A 294 32.310 7.686 25.502 1.00 36.41 C ANISOU 2024 C LEU A 294 4557 4706 4571 325 -1112 454 C ATOM 2025 O LEU A 294 32.470 8.905 25.480 1.00 37.36 O ANISOU 2025 O LEU A 294 4625 4825 4745 399 -1132 278 O ATOM 2026 CB LEU A 294 33.516 7.177 23.353 1.00 37.48 C ANISOU 2026 CB LEU A 294 4710 4397 5134 364 -1038 530 C ATOM 2027 CG LEU A 294 34.905 6.939 23.966 1.00 39.80 C ANISOU 2027 CG LEU A 294 4984 4616 5524 394 -1169 577 C ATOM 2028 CD1 LEU A 294 35.218 5.455 24.081 1.00 39.34 C ANISOU 2028 CD1 LEU A 294 4975 4484 5490 346 -1212 761 C ATOM 2029 CD2 LEU A 294 35.994 7.653 23.165 1.00 38.90 C ANISOU 2029 CD2 LEU A 294 4809 4322 5649 462 -1173 497 C ATOM 2030 N CYS A 295 32.151 7.001 26.630 1.00 36.61 N ANISOU 2030 N CYS A 295 4600 4913 4398 262 -1176 563 N ATOM 2031 CA CYS A 295 32.083 7.673 27.921 1.00 37.17 C ANISOU 2031 CA CYS A 295 4623 5233 4268 281 -1257 457 C ATOM 2032 C CYS A 295 33.180 7.183 28.852 1.00 40.69 C ANISOU 2032 C CYS A 295 5076 5683 4700 270 -1404 565 C ATOM 2033 O CYS A 295 33.650 6.057 28.720 1.00 42.54 O ANISOU 2033 O CYS A 295 5361 5791 5012 215 -1441 764 O ATOM 2034 CB CYS A 295 30.714 7.449 28.576 1.00 35.69 C ANISOU 2034 CB CYS A 295 4425 5354 3781 204 -1198 471 C ATOM 2035 SG CYS A 295 29.283 7.758 27.510 1.00 39.30 S ANISOU 2035 SG CYS A 295 4876 5819 4237 199 -1029 383 S ATOM 2036 N THR A 296 33.585 8.026 29.797 1.00 41.65 N ANISOU 2036 N THR A 296 5144 5945 4734 325 -1501 425 N ATOM 2037 CA THR A 296 34.444 7.569 30.886 1.00 42.67 C ANISOU 2037 CA THR A 296 5277 6150 4785 303 -1648 528 C ATOM 2038 C THR A 296 33.644 6.604 31.748 1.00 45.07 C ANISOU 2038 C THR A 296 5610 6718 4798 178 -1652 709 C ATOM 2039 O THR A 296 32.413 6.587 31.697 1.00 45.30 O ANISOU 2039 O THR A 296 5631 6927 4654 126 -1543 693 O ATOM 2040 CB THR A 296 34.974 8.728 31.751 1.00 42.61 C ANISOU 2040 CB THR A 296 5201 6264 4726 390 -1758 317 C ATOM 2041 OG1 THR A 296 33.875 9.526 32.201 1.00 44.74 O ANISOU 2041 OG1 THR A 296 5418 6805 4775 410 -1706 127 O ATOM 2042 CG2 THR A 296 35.924 9.598 30.952 1.00 39.77 C ANISOU 2042 CG2 THR A 296 4808 5624 4678 492 -1784 183 C ATOM 2043 N THR A 297 34.337 5.796 32.538 1.00 48.36 N ANISOU 2043 N THR A 297 6052 7160 5162 121 -1783 894 N ATOM 2044 CA THR A 297 33.678 4.704 33.245 1.00 54.07 C ANISOU 2044 CA THR A 297 6811 8090 5646 -26 -1804 1134 C ATOM 2045 C THR A 297 33.921 4.719 34.756 1.00 61.09 C ANISOU 2045 C THR A 297 7668 9286 6257 -71 -1938 1179 C ATOM 2046 O THR A 297 34.085 3.670 35.374 1.00 63.28 O ANISOU 2046 O THR A 297 7984 9620 6439 -186 -2039 1441 O ATOM 2047 CB THR A 297 34.125 3.344 32.674 1.00 51.39 C ANISOU 2047 CB THR A 297 6547 7471 5509 -93 -1851 1399 C ATOM 2048 OG1 THR A 297 35.556 3.278 32.664 1.00 51.96 O ANISOU 2048 OG1 THR A 297 6623 7311 5808 -18 -1983 1411 O ATOM 2049 CG2 THR A 297 33.625 3.184 31.255 1.00 47.18 C ANISOU 2049 CG2 THR A 297 6042 6710 5176 -74 -1706 1369 C ATOM 2050 N ASN A 298 33.933 5.910 35.347 1.00 66.13 N ANISOU 2050 N ASN A 298 8233 10124 6769 17 -1951 921 N ATOM 2051 CA ASN A 298 34.053 6.044 36.795 1.00 73.45 C ANISOU 2051 CA ASN A 298 9116 11400 7393 -17 -2067 919 C ATOM 2052 C ASN A 298 32.828 5.486 37.508 1.00 78.57 C ANISOU 2052 C ASN A 298 9745 12440 7667 -164 -2007 1054 C ATOM 2053 O ASN A 298 31.715 5.525 36.982 1.00 77.21 O ANISOU 2053 O ASN A 298 9559 12340 7437 -194 -1855 1013 O ATOM 2054 CB ASN A 298 34.251 7.507 37.194 1.00 75.16 C ANISOU 2054 CB ASN A 298 9248 11739 7571 126 -2093 568 C ATOM 2055 CG ASN A 298 35.349 8.185 36.401 1.00 74.88 C ANISOU 2055 CG ASN A 298 9216 11325 7911 259 -2139 428 C ATOM 2056 OD1 ASN A 298 36.354 7.567 36.052 1.00 74.84 O ANISOU 2056 OD1 ASN A 298 9259 11044 8133 253 -2214 591 O ATOM 2057 ND2 ASN A 298 35.157 9.467 36.107 1.00 74.74 N ANISOU 2057 ND2 ASN A 298 9136 11293 7968 378 -2102 125 N ATOM 2058 N THR A 299 33.047 4.974 38.714 1.00 85.72 N ANISOU 2058 N THR A 299 10643 13612 8314 -263 -2130 1221 N ATOM 2059 CA THR A 299 31.981 4.396 39.523 1.00 92.05 C ANISOU 2059 CA THR A 299 11413 14833 8729 -429 -2091 1387 C ATOM 2060 C THR A 299 31.039 5.471 40.065 1.00 97.76 C ANISOU 2060 C THR A 299 12018 15977 9149 -375 -1989 1081 C ATOM 2061 O THR A 299 29.856 5.213 40.294 1.00 97.82 O ANISOU 2061 O THR A 299 11988 16224 8955 -472 -1847 1114 O ATOM 2062 CB THR A 299 32.562 3.580 40.689 1.00 94.23 C ANISOU 2062 CB THR A 299 11716 15232 8855 -545 -2239 1639 C ATOM 2063 OG1 THR A 299 33.739 4.233 41.181 1.00 94.53 O ANISOU 2063 OG1 THR A 299 11735 15239 8942 -427 -2396 1497 O ATOM 2064 CG2 THR A 299 32.940 2.184 40.219 1.00 93.59 C ANISOU 2064 CG2 THR A 299 11740 14818 9003 -657 -2307 1999 C ATOM 2065 N LYS A 300 31.570 6.675 40.264 1.00103.00 N ANISOU 2065 N LYS A 300 12625 16643 9867 -204 -2035 750 N ATOM 2066 CA LYS A 300 30.765 7.822 40.679 1.00108.55 C ANISOU 2066 CA LYS A 300 13209 17680 10354 -111 -1956 394 C ATOM 2067 C LYS A 300 29.738 8.162 39.595 1.00110.38 C ANISOU 2067 C LYS A 300 13425 17806 10707 -70 -1780 264 C ATOM 2068 O LYS A 300 30.102 8.511 38.471 1.00106.69 O ANISOU 2068 O LYS A 300 13008 16925 10604 28 -1751 185 O ATOM 2069 CB LYS A 300 31.667 9.022 40.978 1.00107.92 C ANISOU 2069 CB LYS A 300 13082 17537 10384 72 -2076 72 C ATOM 2070 CG LYS A 300 30.956 10.210 41.594 1.00109.57 C ANISOU 2070 CG LYS A 300 13178 18011 10442 177 -2002 -313 C ATOM 2071 CD LYS A 300 31.960 11.267 42.023 1.00111.42 C ANISOU 2071 CD LYS A 300 13376 18162 10798 333 -2152 -589 C ATOM 2072 CE LYS A 300 31.299 12.354 42.853 1.00114.56 C ANISOU 2072 CE LYS A 300 13659 18822 11048 424 -2086 -944 C ATOM 2073 NZ LYS A 300 32.306 13.262 43.469 1.00115.97 N ANISOU 2073 NZ LYS A 300 13806 18933 11322 549 -2241 -1175 N ATOM 2074 N GLU A 301 28.459 8.065 39.956 1.00115.59 N ANISOU 2074 N GLU A 301 14016 18802 11102 -148 -1643 242 N ATOM 2075 CA GLU A 301 27.344 8.030 39.004 1.00115.29 C ANISOU 2075 CA GLU A 301 13962 18744 11097 -165 -1489 219 C ATOM 2076 C GLU A 301 27.343 9.097 37.904 1.00111.83 C ANISOU 2076 C GLU A 301 13520 17987 10983 17 -1440 -78 C ATOM 2077 O GLU A 301 27.384 8.773 36.714 1.00110.30 O ANISOU 2077 O GLU A 301 13411 17417 11082 13 -1380 31 O ATOM 2078 CB GLU A 301 26.023 8.118 39.769 1.00119.86 C ANISOU 2078 CB GLU A 301 14433 19690 11418 -229 -1327 131 C ATOM 2079 CG GLU A 301 24.792 8.018 38.885 1.00120.77 C ANISOU 2079 CG GLU A 301 14521 19810 11556 -260 -1166 120 C ATOM 2080 CD GLU A 301 24.743 6.720 38.103 1.00121.72 C ANISOU 2080 CD GLU A 301 14755 19720 11774 -420 -1154 504 C ATOM 2081 OE1 GLU A 301 24.263 5.708 38.658 1.00124.41 O ANISOU 2081 OE1 GLU A 301 15095 20191 11984 -600 -1107 771 O ATOM 2082 OE2 GLU A 301 25.186 6.710 36.933 1.00120.05 O ANISOU 2082 OE2 GLU A 301 14631 19127 11855 -358 -1173 527 O ATOM 2083 N GLY A 302 27.277 10.364 38.296 1.00106.40 N ANISOU 2083 N GLY A 302 12732 17448 10248 172 -1473 -451 N ATOM 2084 CA GLY A 302 27.148 11.438 37.327 1.00 97.37 C ANISOU 2084 CA GLY A 302 11572 16026 9399 334 -1441 -732 C ATOM 2085 C GLY A 302 28.451 12.132 36.988 1.00 90.27 C ANISOU 2085 C GLY A 302 10715 14751 8830 460 -1574 -842 C ATOM 2086 O GLY A 302 28.449 13.192 36.368 1.00 90.46 O ANISOU 2086 O GLY A 302 10709 14576 9086 598 -1586 -1097 O ATOM 2087 N SER A 303 29.566 11.530 37.387 1.00 84.21 N ANISOU 2087 N SER A 303 10014 13885 8095 408 -1684 -639 N ATOM 2088 CA SER A 303 30.880 12.127 37.181 1.00 77.29 C ANISOU 2088 CA SER A 303 9166 12687 7513 514 -1819 -726 C ATOM 2089 C SER A 303 31.461 11.824 35.799 1.00 69.03 C ANISOU 2089 C SER A 303 8216 11155 6858 512 -1781 -569 C ATOM 2090 O SER A 303 32.589 12.216 35.495 1.00 68.87 O ANISOU 2090 O SER A 303 8216 10848 7104 581 -1880 -601 O ATOM 2091 CB SER A 303 31.849 11.637 38.255 1.00 78.84 C ANISOU 2091 CB SER A 303 9378 13008 7571 465 -1965 -591 C ATOM 2092 OG SER A 303 32.069 10.243 38.125 1.00 78.32 O ANISOU 2092 OG SER A 303 9405 12860 7491 314 -1947 -207 O ATOM 2093 N ASN A 304 30.697 11.130 34.962 1.00 61.93 N ANISOU 2093 N ASN A 304 7366 10178 5988 431 -1639 -404 N ATOM 2094 CA ASN A 304 31.219 10.691 33.675 1.00 55.35 C ANISOU 2094 CA ASN A 304 6618 8926 5486 418 -1596 -242 C ATOM 2095 C ASN A 304 30.903 11.645 32.544 1.00 50.29 C ANISOU 2095 C ASN A 304 5959 8062 5088 514 -1529 -432 C ATOM 2096 O ASN A 304 29.888 12.326 32.559 1.00 50.52 O ANISOU 2096 O ASN A 304 5925 8255 5016 559 -1471 -629 O ATOM 2097 CB ASN A 304 30.693 9.300 33.343 1.00 54.33 C ANISOU 2097 CB ASN A 304 6562 8798 5284 271 -1503 63 C ATOM 2098 CG ASN A 304 31.307 8.233 34.219 1.00 56.40 C ANISOU 2098 CG ASN A 304 6865 9152 5414 167 -1605 318 C ATOM 2099 OD1 ASN A 304 32.522 8.199 34.412 1.00 54.54 O ANISOU 2099 OD1 ASN A 304 6651 8750 5321 204 -1729 358 O ATOM 2100 ND2 ASN A 304 30.471 7.364 34.769 1.00 59.04 N ANISOU 2100 ND2 ASN A 304 7203 9753 5476 29 -1564 502 N ATOM 2101 N ILE A 305 31.791 11.685 31.560 1.00 43.40 N ANISOU 2101 N ILE A 305 6641 5217 4633 -663 -958 104 N ATOM 2102 CA ILE A 305 31.599 12.527 30.391 1.00 40.97 C ANISOU 2102 CA ILE A 305 6354 4822 4390 -660 -859 68 C ATOM 2103 C ILE A 305 31.599 11.679 29.127 1.00 40.10 C ANISOU 2103 C ILE A 305 5958 4801 4476 -566 -801 125 C ATOM 2104 O ILE A 305 32.224 10.616 29.077 1.00 41.26 O ANISOU 2104 O ILE A 305 5882 5074 4719 -564 -876 188 O ATOM 2105 CB ILE A 305 32.682 13.612 30.296 1.00 41.44 C ANISOU 2105 CB ILE A 305 6504 4834 4407 -890 -966 33 C ATOM 2106 CG1 ILE A 305 34.082 12.984 30.306 1.00 42.85 C ANISOU 2106 CG1 ILE A 305 6431 5180 4671 -1039 -1135 102 C ATOM 2107 CG2 ILE A 305 32.523 14.615 31.437 1.00 39.73 C ANISOU 2107 CG2 ILE A 305 6639 4483 3973 -982 -1001 -44 C ATOM 2108 CD1 ILE A 305 35.217 14.007 30.226 1.00 43.78 C ANISOU 2108 CD1 ILE A 305 6603 5286 4747 -1302 -1256 86 C ATOM 2109 N CYS A 306 30.891 12.144 28.107 1.00 38.08 N ANISOU 2109 N CYS A 306 5722 4475 4271 -479 -666 106 N ATOM 2110 CA CYS A 306 30.718 11.350 26.902 1.00 36.93 C ANISOU 2110 CA CYS A 306 5342 4403 4288 -381 -598 151 C ATOM 2111 C CYS A 306 31.004 12.134 25.653 1.00 38.57 C ANISOU 2111 C CYS A 306 5523 4568 4562 -433 -550 137 C ATOM 2112 O CYS A 306 30.886 13.357 25.615 1.00 38.89 O ANISOU 2112 O CYS A 306 5764 4489 4522 -491 -522 91 O ATOM 2113 CB CYS A 306 29.300 10.792 26.807 1.00 36.14 C ANISOU 2113 CB CYS A 306 5245 4297 4189 -190 -469 166 C ATOM 2114 SG CYS A 306 28.860 9.657 28.123 1.00 44.98 S ANISOU 2114 SG CYS A 306 6363 5482 5245 -120 -505 204 S ATOM 2115 N LEU A 307 31.320 11.386 24.612 1.00 40.59 N ANISOU 2115 N LEU A 307 5548 4914 4960 -400 -531 178 N ATOM 2116 CA LEU A 307 31.690 11.937 23.335 1.00 40.88 C ANISOU 2116 CA LEU A 307 5520 4941 5071 -449 -486 178 C ATOM 2117 C LEU A 307 31.171 10.979 22.265 1.00 37.99 C ANISOU 2117 C LEU A 307 4977 4638 4819 -310 -397 209 C ATOM 2118 O LEU A 307 31.311 9.759 22.408 1.00 38.35 O ANISOU 2118 O LEU A 307 4874 4770 4926 -249 -426 241 O ATOM 2119 CB LEU A 307 33.207 12.103 23.305 1.00 44.54 C ANISOU 2119 CB LEU A 307 5869 5483 5570 -632 -605 199 C ATOM 2120 CG LEU A 307 34.045 12.480 22.101 1.00 45.51 C ANISOU 2120 CG LEU A 307 5861 5653 5778 -729 -591 220 C ATOM 2121 CD1 LEU A 307 35.379 12.965 22.640 1.00 45.69 C ANISOU 2121 CD1 LEU A 307 5854 5736 5770 -948 -731 238 C ATOM 2122 CD2 LEU A 307 34.240 11.281 21.189 1.00 44.29 C ANISOU 2122 CD2 LEU A 307 5449 5620 5759 -616 -546 263 C ATOM 2123 N THR A 308 30.550 11.509 21.214 1.00 35.31 N ANISOU 2123 N THR A 308 4670 4247 4498 -259 -294 201 N ATOM 2124 CA THR A 308 30.125 10.668 20.092 1.00 33.26 C ANISOU 2124 CA THR A 308 4254 4048 4334 -156 -220 226 C ATOM 2125 C THR A 308 30.469 11.316 18.766 1.00 33.88 C ANISOU 2125 C THR A 308 4296 4118 4457 -205 -168 228 C ATOM 2126 O THR A 308 30.116 12.472 18.528 1.00 35.24 O ANISOU 2126 O THR A 308 4621 4196 4572 -227 -124 214 O ATOM 2127 CB THR A 308 28.603 10.380 20.111 1.00 32.43 C ANISOU 2127 CB THR A 308 4208 3918 4195 -7 -132 234 C ATOM 2128 OG1 THR A 308 28.205 9.960 21.418 1.00 34.29 O ANISOU 2128 OG1 THR A 308 4508 4154 4365 30 -167 235 O ATOM 2129 CG2 THR A 308 28.253 9.281 19.115 1.00 31.43 C ANISOU 2129 CG2 THR A 308 3920 3865 4158 68 -87 261 C ATOM 2130 N ARG A 309 31.161 10.577 17.905 1.00 33.36 N ANISOU 2130 N ARG A 309 4042 4145 4487 -212 -166 249 N ATOM 2131 CA ARG A 309 31.380 11.042 16.542 1.00 33.31 C ANISOU 2131 CA ARG A 309 3991 4147 4519 -241 -100 256 C ATOM 2132 C ARG A 309 30.027 11.186 15.848 1.00 35.43 C ANISOU 2132 C ARG A 309 4334 4365 4763 -126 -4 257 C ATOM 2133 O ARG A 309 29.246 10.228 15.798 1.00 34.83 O ANISOU 2133 O ARG A 309 4206 4323 4704 -19 21 264 O ATOM 2134 CB ARG A 309 32.275 10.081 15.766 1.00 33.11 C ANISOU 2134 CB ARG A 309 3753 4237 4589 -237 -98 276 C ATOM 2135 CG ARG A 309 33.690 9.945 16.291 1.00 34.05 C ANISOU 2135 CG ARG A 309 3752 4443 4742 -340 -188 297 C ATOM 2136 CD ARG A 309 34.494 9.070 15.350 1.00 35.76 C ANISOU 2136 CD ARG A 309 3762 4777 5050 -298 -152 322 C ATOM 2137 NE ARG A 309 34.532 9.637 13.998 1.00 37.90 N ANISOU 2137 NE ARG A 309 4020 5051 5329 -328 -61 323 N ATOM 2138 CZ ARG A 309 35.055 9.020 12.941 1.00 37.52 C ANISOU 2138 CZ ARG A 309 3826 5091 5340 -281 5 335 C ATOM 2139 NH1 ARG A 309 35.578 7.807 13.073 1.00 37.76 N ANISOU 2139 NH1 ARG A 309 3716 5201 5429 -187 -7 346 N ATOM 2140 NH2 ARG A 309 35.053 9.612 11.750 1.00 36.11 N ANISOU 2140 NH2 ARG A 309 3655 4914 5151 -318 87 339 N ATOM 2141 N THR A 310 29.747 12.380 15.329 1.00 34.40 N ANISOU 2141 N THR A 310 4328 4157 4587 -154 44 258 N ATOM 2142 CA THR A 310 28.441 12.661 14.740 1.00 34.97 C ANISOU 2142 CA THR A 310 4474 4191 4624 -37 128 273 C ATOM 2143 C THR A 310 28.385 12.401 13.241 1.00 34.16 C ANISOU 2143 C THR A 310 4268 4145 4567 -19 186 296 C ATOM 2144 O THR A 310 27.310 12.496 12.640 1.00 32.34 O ANISOU 2144 O THR A 310 4066 3912 4311 75 244 320 O ATOM 2145 CB THR A 310 28.015 14.130 14.972 1.00 36.77 C ANISOU 2145 CB THR A 310 4921 4285 4764 -40 158 271 C ATOM 2146 OG1 THR A 310 29.093 15.001 14.616 1.00 39.10 O ANISOU 2146 OG1 THR A 310 5263 4534 5060 -193 134 267 O ATOM 2147 CG2 THR A 310 27.652 14.362 16.412 1.00 36.67 C ANISOU 2147 CG2 THR A 310 5049 4208 4678 -9 128 245 C ATOM 2148 N ASP A 311 29.532 12.086 12.642 1.00 35.05 N ANISOU 2148 N ASP A 311 4257 4321 4738 -106 172 293 N ATOM 2149 CA ASP A 311 29.644 12.026 11.184 1.00 37.09 C ANISOU 2149 CA ASP A 311 4444 4627 5021 -108 235 310 C ATOM 2150 C ASP A 311 29.332 10.643 10.613 1.00 38.35 C ANISOU 2150 C ASP A 311 4477 4871 5223 -24 256 303 C ATOM 2151 O ASP A 311 29.793 10.286 9.526 1.00 38.99 O ANISOU 2151 O ASP A 311 4473 5011 5330 -36 298 304 O ATOM 2152 CB ASP A 311 31.043 12.477 10.741 1.00 37.80 C ANISOU 2152 CB ASP A 311 4469 4752 5140 -244 227 319 C ATOM 2153 CG ASP A 311 32.162 11.741 11.465 1.00 40.44 C ANISOU 2153 CG ASP A 311 4668 5167 5532 -294 160 309 C ATOM 2154 OD1 ASP A 311 31.859 10.969 12.399 1.00 39.76 O ANISOU 2154 OD1 ASP A 311 4568 5084 5455 -227 113 293 O ATOM 2155 OD2 ASP A 311 33.351 11.949 11.109 1.00 41.20 O ANISOU 2155 OD2 ASP A 311 4663 5331 5659 -400 154 328 O ATOM 2156 N ARG A 312 28.539 9.867 11.341 1.00 38.07 N ANISOU 2156 N ARG A 312 4446 4837 5184 55 231 297 N ATOM 2157 CA ARG A 312 28.115 8.566 10.843 1.00 37.74 C ANISOU 2157 CA ARG A 312 4322 4849 5167 118 245 290 C ATOM 2158 C ARG A 312 27.202 8.671 9.626 1.00 35.52 C ANISOU 2158 C ARG A 312 4060 4587 4849 151 301 309 C ATOM 2159 O ARG A 312 26.492 9.665 9.438 1.00 34.70 O ANISOU 2159 O ARG A 312 4038 4453 4695 167 326 340 O ATOM 2160 CB ARG A 312 27.408 7.778 11.932 1.00 36.84 C ANISOU 2160 CB ARG A 312 4221 4728 5048 173 203 291 C ATOM 2161 CG ARG A 312 26.160 8.404 12.510 1.00 40.39 C ANISOU 2161 CG ARG A 312 4766 5147 5433 221 214 319 C ATOM 2162 CD ARG A 312 25.726 7.464 13.610 1.00 46.05 C ANISOU 2162 CD ARG A 312 5473 5875 6150 256 173 323 C ATOM 2163 NE ARG A 312 24.578 7.879 14.392 1.00 50.95 N ANISOU 2163 NE ARG A 312 6166 6487 6705 313 188 354 N ATOM 2164 CZ ARG A 312 24.232 7.302 15.541 1.00 54.38 C ANISOU 2164 CZ ARG A 312 6612 6928 7122 335 158 364 C ATOM 2165 NH1 ARG A 312 23.162 7.724 16.195 1.00 55.90 N ANISOU 2165 NH1 ARG A 312 6864 7129 7248 399 190 397 N ATOM 2166 NH2 ARG A 312 24.964 6.310 16.041 1.00 54.74 N ANISOU 2166 NH2 ARG A 312 6610 6977 7212 304 102 348 N ATOM 2167 N GLY A 313 27.239 7.626 8.807 1.00 31.34 N ANISOU 2167 N GLY A 313 3465 4104 4338 165 319 292 N ATOM 2168 CA GLY A 313 26.440 7.562 7.603 1.00 30.19 C ANISOU 2168 CA GLY A 313 3333 3991 4147 179 358 307 C ATOM 2169 C GLY A 313 27.235 6.938 6.478 1.00 31.59 C ANISOU 2169 C GLY A 313 3460 4205 4339 159 399 273 C ATOM 2170 O GLY A 313 28.312 6.368 6.699 1.00 31.61 O ANISOU 2170 O GLY A 313 3402 4214 4395 158 399 242 O ATOM 2171 N TRP A 314 26.704 7.051 5.265 1.00 31.42 N ANISOU 2171 N TRP A 314 3462 4214 4261 152 435 285 N ATOM 2172 CA TRP A 314 27.385 6.561 4.079 1.00 31.98 C ANISOU 2172 CA TRP A 314 3509 4320 4321 137 489 251 C ATOM 2173 C TRP A 314 28.285 7.619 3.456 1.00 33.14 C ANISOU 2173 C TRP A 314 3643 4485 4464 92 543 269 C ATOM 2174 O TRP A 314 27.943 8.807 3.421 1.00 32.87 O ANISOU 2174 O TRP A 314 3660 4430 4400 65 544 317 O ATOM 2175 CB TRP A 314 26.366 6.080 3.046 1.00 32.66 C ANISOU 2175 CB TRP A 314 3641 4438 4330 134 494 253 C ATOM 2176 CG TRP A 314 25.940 4.675 3.258 1.00 31.74 C ANISOU 2176 CG TRP A 314 3538 4308 4214 148 459 215 C ATOM 2177 CD1 TRP A 314 24.753 4.242 3.779 1.00 30.56 C ANISOU 2177 CD1 TRP A 314 3407 4160 4043 141 399 241 C ATOM 2178 CD2 TRP A 314 26.700 3.497 2.949 1.00 32.52 C ANISOU 2178 CD2 TRP A 314 3642 4383 4330 169 487 149 C ATOM 2179 NE1 TRP A 314 24.729 2.866 3.815 1.00 31.30 N ANISOU 2179 NE1 TRP A 314 3530 4222 4139 135 379 195 N ATOM 2180 CE2 TRP A 314 25.909 2.386 3.313 1.00 32.81 C ANISOU 2180 CE2 TRP A 314 3726 4387 4355 163 434 134 C ATOM 2181 CE3 TRP A 314 27.969 3.280 2.399 1.00 30.99 C ANISOU 2181 CE3 TRP A 314 3419 4198 4159 199 558 107 C ATOM 2182 CZ2 TRP A 314 26.353 1.067 3.147 1.00 32.54 C ANISOU 2182 CZ2 TRP A 314 3741 4297 4326 190 447 71 C ATOM 2183 CZ3 TRP A 314 28.405 1.973 2.235 1.00 31.33 C ANISOU 2183 CZ3 TRP A 314 3492 4202 4209 250 581 46 C ATOM 2184 CH2 TRP A 314 27.595 0.882 2.608 1.00 32.66 C ANISOU 2184 CH2 TRP A 314 3738 4309 4362 247 524 25 C ATOM 2185 N TYR A 315 29.433 7.167 2.959 1.00 33.21 N ANISOU 2185 N TYR A 315 3588 4532 4499 87 595 237 N ATOM 2186 CA TYR A 315 30.385 8.006 2.246 1.00 32.15 C ANISOU 2186 CA TYR A 315 3420 4440 4356 30 659 260 C ATOM 2187 C TYR A 315 30.708 7.358 0.913 1.00 34.64 C ANISOU 2187 C TYR A 315 3725 4812 4624 50 741 229 C ATOM 2188 O TYR A 315 31.035 6.174 0.877 1.00 36.01 O ANISOU 2188 O TYR A 315 3869 4996 4817 114 760 177 O ATOM 2189 CB TYR A 315 31.679 8.178 3.039 1.00 31.75 C ANISOU 2189 CB TYR A 315 3268 4413 4382 -1 651 265 C ATOM 2190 CG TYR A 315 31.570 8.984 4.308 1.00 31.84 C ANISOU 2190 CG TYR A 315 3308 4366 4422 -47 573 292 C ATOM 2191 CD1 TYR A 315 31.059 8.424 5.474 1.00 31.58 C ANISOU 2191 CD1 TYR A 315 3292 4289 4419 3 502 274 C ATOM 2192 CD2 TYR A 315 32.009 10.303 4.349 1.00 33.26 C ANISOU 2192 CD2 TYR A 315 3519 4529 4591 -150 574 334 C ATOM 2193 CE1 TYR A 315 30.973 9.167 6.643 1.00 33.05 C ANISOU 2193 CE1 TYR A 315 3523 4420 4614 -36 437 292 C ATOM 2194 CE2 TYR A 315 31.926 11.054 5.510 1.00 33.08 C ANISOU 2194 CE2 TYR A 315 3557 4434 4577 -197 505 349 C ATOM 2195 CZ TYR A 315 31.408 10.482 6.652 1.00 34.22 C ANISOU 2195 CZ TYR A 315 3717 4542 4743 -134 439 324 C ATOM 2196 OH TYR A 315 31.323 11.230 7.803 1.00 35.80 O ANISOU 2196 OH TYR A 315 3997 4669 4934 -178 377 332 O ATOM 2197 N CYS A 316 30.621 8.117 -0.176 1.00 33.17 N ANISOU 2197 N CYS A 316 3581 4656 4367 3 793 261 N ATOM 2198 CA CYS A 316 31.058 7.620 -1.477 1.00 33.74 C ANISOU 2198 CA CYS A 316 3651 4791 4378 15 884 233 C ATOM 2199 C CYS A 316 32.011 8.612 -2.127 1.00 36.07 C ANISOU 2199 C CYS A 316 3903 5147 4657 -58 961 281 C ATOM 2200 O CYS A 316 31.765 9.820 -2.097 1.00 35.75 O ANISOU 2200 O CYS A 316 3908 5078 4599 -131 939 345 O ATOM 2201 CB CYS A 316 29.866 7.365 -2.409 1.00 31.94 C ANISOU 2201 CB CYS A 316 3535 4558 4044 18 873 226 C ATOM 2202 SG CYS A 316 28.697 6.101 -1.836 1.00 41.08 S ANISOU 2202 SG CYS A 316 4746 5661 5200 67 785 177 S ATOM 2203 N ASP A 317 33.104 8.115 -2.702 1.00 35.85 N ANISOU 2203 N ASP A 317 3791 5201 4631 -35 1057 258 N ATOM 2204 CA ASP A 317 33.952 8.980 -3.512 1.00 39.32 C ANISOU 2204 CA ASP A 317 4186 5719 5034 -115 1145 312 C ATOM 2205 C ASP A 317 33.129 9.507 -4.686 1.00 38.72 C ANISOU 2205 C ASP A 317 4241 5634 4837 -153 1169 338 C ATOM 2206 O ASP A 317 32.382 8.755 -5.315 1.00 37.19 O ANISOU 2206 O ASP A 317 4131 5430 4569 -97 1171 290 O ATOM 2207 CB ASP A 317 35.198 8.240 -4.003 1.00 42.57 C ANISOU 2207 CB ASP A 317 4474 6244 5457 -58 1262 286 C ATOM 2208 CG ASP A 317 36.231 8.049 -2.908 1.00 46.50 C ANISOU 2208 CG ASP A 317 4806 6788 6073 -44 1239 300 C ATOM 2209 OD1 ASP A 317 36.358 8.936 -2.038 1.00 47.75 O ANISOU 2209 OD1 ASP A 317 4934 6923 6287 -144 1160 352 O ATOM 2210 OD2 ASP A 317 36.919 7.009 -2.914 1.00 49.89 O ANISOU 2210 OD2 ASP A 317 5146 7277 6534 72 1300 261 O ATOM 2211 N ASN A 318 33.249 10.800 -4.966 1.00 38.16 N ANISOU 2211 N ASN A 318 4199 5562 4739 -256 1179 418 N ATOM 2212 CA ASN A 318 32.421 11.430 -5.989 1.00 37.41 C ANISOU 2212 CA ASN A 318 4233 5451 4528 -287 1187 464 C ATOM 2213 C ASN A 318 33.059 12.706 -6.525 1.00 37.49 C ANISOU 2213 C ASN A 318 4255 5484 4504 -406 1243 554 C ATOM 2214 O ASN A 318 33.092 13.724 -5.834 1.00 39.13 O ANISOU 2214 O ASN A 318 4492 5620 4757 -478 1192 610 O ATOM 2215 CB ASN A 318 31.021 11.733 -5.422 1.00 36.57 C ANISOU 2215 CB ASN A 318 4228 5247 4419 -256 1072 482 C ATOM 2216 CG ASN A 318 30.036 12.229 -6.488 1.00 36.99 C ANISOU 2216 CG ASN A 318 4402 5304 4350 -263 1066 537 C ATOM 2217 OD1 ASN A 318 30.405 12.452 -7.643 1.00 38.59 O ANISOU 2217 OD1 ASN A 318 4632 5568 4463 -305 1144 563 O ATOM 2218 ND2 ASN A 318 28.778 12.417 -6.091 1.00 33.96 N ANISOU 2218 ND2 ASN A 318 4082 4866 3956 -216 975 565 N ATOM 2219 N ALA A 319 33.577 12.635 -7.750 1.00 37.68 N ANISOU 2219 N ALA A 319 4273 5604 4439 -430 1353 566 N ATOM 2220 CA ALA A 319 34.057 13.811 -8.476 1.00 39.17 C ANISOU 2220 CA ALA A 319 4496 5820 4568 -552 1414 663 C ATOM 2221 C ALA A 319 35.114 14.635 -7.728 1.00 40.63 C ANISOU 2221 C ALA A 319 4590 6006 4841 -675 1416 719 C ATOM 2222 O ALA A 319 35.071 15.867 -7.750 1.00 41.43 O ANISOU 2222 O ALA A 319 4782 6038 4921 -789 1395 805 O ATOM 2223 CB ALA A 319 32.874 14.704 -8.839 1.00 39.20 C ANISOU 2223 CB ALA A 319 4673 5728 4492 -567 1349 730 C ATOM 2224 N GLY A 320 36.055 13.960 -7.071 1.00 39.93 N ANISOU 2224 N GLY A 320 4332 5993 4846 -657 1435 677 N ATOM 2225 CA GLY A 320 37.145 14.639 -6.392 1.00 40.81 C ANISOU 2225 CA GLY A 320 4331 6141 5034 -792 1429 735 C ATOM 2226 C GLY A 320 36.825 15.001 -4.954 1.00 41.09 C ANISOU 2226 C GLY A 320 4400 6052 5160 -818 1293 725 C ATOM 2227 O GLY A 320 37.720 15.397 -4.196 1.00 42.91 O ANISOU 2227 O GLY A 320 4532 6312 5459 -931 1263 758 O ATOM 2228 N SER A 321 35.548 14.875 -4.586 1.00 37.38 N ANISOU 2228 N SER A 321 4067 5454 4681 -721 1211 685 N ATOM 2229 CA SER A 321 35.085 15.113 -3.221 1.00 36.79 C ANISOU 2229 CA SER A 321 4043 5259 4677 -713 1093 666 C ATOM 2230 C SER A 321 34.455 13.846 -2.645 1.00 35.73 C ANISOU 2230 C SER A 321 3870 5120 4586 -554 1047 578 C ATOM 2231 O SER A 321 34.541 12.770 -3.234 1.00 35.66 O ANISOU 2231 O SER A 321 3793 5194 4563 -463 1104 529 O ATOM 2232 CB SER A 321 34.057 16.253 -3.180 1.00 39.18 C ANISOU 2232 CB SER A 321 4556 5406 4925 -736 1040 715 C ATOM 2233 OG SER A 321 34.614 17.485 -3.593 1.00 42.04 O ANISOU 2233 OG SER A 321 4990 5737 5247 -894 1071 800 O ATOM 2234 N VAL A 322 33.797 13.975 -1.502 1.00 36.55 N ANISOU 2234 N VAL A 322 4038 5117 4733 -523 947 560 N ATOM 2235 CA VAL A 322 33.079 12.845 -0.930 1.00 36.08 C ANISOU 2235 CA VAL A 322 3959 5043 4706 -389 899 490 C ATOM 2236 C VAL A 322 31.616 13.203 -0.705 1.00 36.83 C ANISOU 2236 C VAL A 322 4201 5033 4760 -327 839 501 C ATOM 2237 O VAL A 322 31.303 14.211 -0.066 1.00 38.03 O ANISOU 2237 O VAL A 322 4452 5087 4912 -364 793 538 O ATOM 2238 CB VAL A 322 33.717 12.382 0.393 1.00 36.23 C ANISOU 2238 CB VAL A 322 3876 5068 4821 -387 838 458 C ATOM 2239 CG1 VAL A 322 32.890 11.283 1.029 1.00 36.75 C ANISOU 2239 CG1 VAL A 322 3948 5101 4913 -259 785 398 C ATOM 2240 CG2 VAL A 322 35.123 11.889 0.144 1.00 37.37 C ANISOU 2240 CG2 VAL A 322 3843 5347 5008 -416 900 459 C ATOM 2241 N SER A 323 30.722 12.387 -1.259 1.00 35.52 N ANISOU 2241 N SER A 323 4053 4891 4550 -234 842 472 N ATOM 2242 CA SER A 323 29.298 12.521 -0.994 1.00 33.90 C ANISOU 2242 CA SER A 323 3941 4627 4312 -164 781 490 C ATOM 2243 C SER A 323 28.976 11.864 0.339 1.00 33.45 C ANISOU 2243 C SER A 323 3850 4535 4325 -107 712 446 C ATOM 2244 O SER A 323 29.206 10.666 0.523 1.00 32.15 O ANISOU 2244 O SER A 323 3607 4411 4196 -70 707 387 O ATOM 2245 CB SER A 323 28.466 11.898 -2.113 1.00 32.74 C ANISOU 2245 CB SER A 323 3819 4540 4082 -117 796 487 C ATOM 2246 OG SER A 323 28.461 12.729 -3.256 1.00 33.60 O ANISOU 2246 OG SER A 323 3993 4666 4106 -161 844 548 O ATOM 2247 N PHE A 324 28.459 12.659 1.269 1.00 33.72 N ANISOU 2247 N PHE A 324 3957 4486 4371 -94 664 476 N ATOM 2248 CA PHE A 324 28.175 12.186 2.617 1.00 32.09 C ANISOU 2248 CA PHE A 324 3731 4244 4217 -47 602 443 C ATOM 2249 C PHE A 324 26.681 12.158 2.892 1.00 32.34 C ANISOU 2249 C PHE A 324 3818 4259 4211 46 568 471 C ATOM 2250 O PHE A 324 26.000 13.180 2.786 1.00 32.17 O ANISOU 2250 O PHE A 324 3891 4190 4141 78 574 530 O ATOM 2251 CB PHE A 324 28.878 13.063 3.646 1.00 32.76 C ANISOU 2251 CB PHE A 324 3856 4253 4338 -111 576 448 C ATOM 2252 CG PHE A 324 28.409 12.837 5.057 1.00 34.11 C ANISOU 2252 CG PHE A 324 4049 4375 4537 -59 514 425 C ATOM 2253 CD1 PHE A 324 28.502 11.577 5.638 1.00 33.12 C ANISOU 2253 CD1 PHE A 324 3826 4298 4460 -21 481 379 C ATOM 2254 CD2 PHE A 324 27.892 13.885 5.807 1.00 34.71 C ANISOU 2254 CD2 PHE A 324 4259 4349 4581 -43 495 451 C ATOM 2255 CE1 PHE A 324 28.081 11.361 6.933 1.00 33.08 C ANISOU 2255 CE1 PHE A 324 3844 4255 4472 20 428 365 C ATOM 2256 CE2 PHE A 324 27.467 13.677 7.110 1.00 36.70 C ANISOU 2256 CE2 PHE A 324 4539 4563 4844 8 448 428 C ATOM 2257 CZ PHE A 324 27.563 12.410 7.673 1.00 35.59 C ANISOU 2257 CZ PHE A 324 4287 4485 4751 34 413 389 C ATOM 2258 N PHE A 325 26.187 10.979 3.251 1.00 30.47 N ANISOU 2258 N PHE A 325 3520 4064 3993 92 535 436 N ATOM 2259 CA PHE A 325 24.773 10.764 3.511 1.00 30.62 C ANISOU 2259 CA PHE A 325 3555 4103 3976 166 501 470 C ATOM 2260 C PHE A 325 24.571 10.498 5.008 1.00 33.43 C ANISOU 2260 C PHE A 325 3904 4421 4376 203 460 453 C ATOM 2261 O PHE A 325 24.726 9.364 5.465 1.00 32.75 O ANISOU 2261 O PHE A 325 3759 4357 4329 198 431 409 O ATOM 2262 CB PHE A 325 24.250 9.592 2.666 1.00 29.88 C ANISOU 2262 CB PHE A 325 3411 4092 3849 161 491 454 C ATOM 2263 CG PHE A 325 24.631 9.675 1.210 1.00 30.91 C ANISOU 2263 CG PHE A 325 3555 4264 3927 117 536 454 C ATOM 2264 CD1 PHE A 325 25.855 9.190 0.767 1.00 31.05 C ANISOU 2264 CD1 PHE A 325 3541 4286 3971 73 581 394 C ATOM 2265 CD2 PHE A 325 23.769 10.238 0.283 1.00 31.75 C ANISOU 2265 CD2 PHE A 325 3700 4415 3950 129 537 522 C ATOM 2266 CE1 PHE A 325 26.217 9.271 -0.570 1.00 30.00 C ANISOU 2266 CE1 PHE A 325 3425 4197 3776 37 635 394 C ATOM 2267 CE2 PHE A 325 24.126 10.320 -1.058 1.00 31.99 C ANISOU 2267 CE2 PHE A 325 3753 4486 3917 83 578 524 C ATOM 2268 CZ PHE A 325 25.351 9.837 -1.481 1.00 31.65 C ANISOU 2268 CZ PHE A 325 3689 4443 3895 35 632 457 C ATOM 2269 N PRO A 326 24.236 11.552 5.779 1.00 35.32 N ANISOU 2269 N PRO A 326 4225 4595 4602 244 460 487 N ATOM 2270 CA PRO A 326 24.148 11.474 7.245 1.00 36.41 C ANISOU 2270 CA PRO A 326 4381 4688 4764 274 428 468 C ATOM 2271 C PRO A 326 23.064 10.513 7.744 1.00 41.95 C ANISOU 2271 C PRO A 326 5025 5455 5458 334 402 482 C ATOM 2272 O PRO A 326 23.214 9.913 8.806 1.00 45.22 O ANISOU 2272 O PRO A 326 5420 5858 5903 334 370 452 O ATOM 2273 CB PRO A 326 23.830 12.918 7.655 1.00 35.05 C ANISOU 2273 CB PRO A 326 4345 4426 4548 321 452 506 C ATOM 2274 CG PRO A 326 23.248 13.542 6.448 1.00 33.46 C ANISOU 2274 CG PRO A 326 4173 4246 4296 356 490 569 C ATOM 2275 CD PRO A 326 23.940 12.907 5.283 1.00 33.57 C ANISOU 2275 CD PRO A 326 4104 4323 4327 269 495 545 C ATOM 2276 N AGLN A 327 21.990 10.384 6.972 0.50 42.58 N ANISOU 2276 N AGLN A 327 5074 5612 5491 374 410 536 N ATOM 2277 N BGLN A 327 21.975 10.369 7.006 0.50 42.56 N ANISOU 2277 N BGLN A 327 5072 5611 5490 375 409 536 N ATOM 2278 CA AGLN A 327 20.919 9.439 7.266 0.50 44.78 C ANISOU 2278 CA AGLN A 327 5282 5978 5756 399 380 564 C ATOM 2279 CA BGLN A 327 20.965 9.400 7.408 0.50 44.30 C ANISOU 2279 CA BGLN A 327 5222 5911 5699 399 378 560 C ATOM 2280 C AGLN A 327 21.139 8.151 6.467 0.50 45.45 C ANISOU 2280 C AGLN A 327 5305 6111 5851 317 352 525 C ATOM 2281 C BGLN A 327 21.088 8.146 6.546 0.50 44.44 C ANISOU 2281 C BGLN A 327 5177 5985 5724 321 351 527 C ATOM 2282 O AGLN A 327 20.588 7.995 5.376 0.50 45.44 O ANISOU 2282 O AGLN A 327 5284 6180 5803 296 349 556 O ATOM 2283 O BGLN A 327 20.435 8.012 5.508 0.50 45.48 O ANISOU 2283 O BGLN A 327 5285 6191 5806 304 346 564 O ATOM 2284 CB AGLN A 327 19.552 10.047 6.927 0.50 43.80 C ANISOU 2284 CB AGLN A 327 5146 5932 5565 484 396 661 C ATOM 2285 CB BGLN A 327 19.567 10.005 7.328 0.50 43.46 C ANISOU 2285 CB BGLN A 327 5107 5877 5530 493 395 655 C ATOM 2286 CG AGLN A 327 19.338 11.465 7.461 0.50 44.21 C ANISOU 2286 CG AGLN A 327 5295 5914 5590 592 442 702 C ATOM 2287 CG BGLN A 327 19.402 11.243 8.206 0.50 44.42 C ANISOU 2287 CG BGLN A 327 5323 5922 5632 596 436 681 C ATOM 2288 CD AGLN A 327 18.345 12.273 6.633 0.50 44.78 C ANISOU 2288 CD AGLN A 327 5369 6049 5598 684 469 803 C ATOM 2289 CD BGLN A 327 19.911 11.039 9.632 0.50 44.71 C ANISOU 2289 CD BGLN A 327 5400 5888 5701 590 426 625 C ATOM 2290 OE1AGLN A 327 18.346 12.211 5.402 0.50 44.52 O ANISOU 2290 OE1AGLN A 327 5308 6065 5542 638 458 825 O ATOM 2291 OE1BGLN A 327 19.626 10.024 10.275 0.50 44.37 O ANISOU 2291 OE1BGLN A 327 5288 5897 5673 571 396 617 O ATOM 2292 NE2AGLN A 327 17.497 13.041 7.310 0.50 45.11 N ANISOU 2292 NE2AGLN A 327 5447 6090 5602 825 508 868 N ATOM 2293 NE2BGLN A 327 20.666 12.012 10.131 0.50 43.87 N ANISOU 2293 NE2BGLN A 327 5415 5659 5594 594 444 591 N ATOM 2294 N ALA A 328 21.947 7.236 7.006 1.00 47.79 N ANISOU 2294 N ALA A 328 5589 6367 6204 277 332 459 N ATOM 2295 CA ALA A 328 22.307 5.998 6.296 1.00 49.49 C ANISOU 2295 CA ALA A 328 5781 6595 6428 217 317 410 C ATOM 2296 C ALA A 328 21.107 5.155 5.850 1.00 54.10 C ANISOU 2296 C ALA A 328 6343 7254 6957 181 281 444 C ATOM 2297 O ALA A 328 21.226 4.311 4.957 1.00 55.25 O ANISOU 2297 O ALA A 328 6505 7407 7079 123 272 406 O ATOM 2298 CB ALA A 328 23.233 5.152 7.172 1.00 45.60 C ANISOU 2298 CB ALA A 328 5281 6042 6003 212 299 352 C ATOM 2299 N GLU A 329 19.956 5.394 6.472 1.00 54.78 N ANISOU 2299 N GLU A 329 6397 7401 7017 211 261 517 N ATOM 2300 CA GLU A 329 18.722 4.731 6.092 1.00 56.94 C ANISOU 2300 CA GLU A 329 6625 7777 7231 160 219 573 C ATOM 2301 C GLU A 329 18.151 5.241 4.766 1.00 56.08 C ANISOU 2301 C GLU A 329 6502 7754 7051 145 218 622 C ATOM 2302 O GLU A 329 17.194 4.671 4.260 1.00 59.35 O ANISOU 2302 O GLU A 329 6876 8269 7406 77 170 669 O ATOM 2303 CB GLU A 329 17.681 4.888 7.205 1.00 62.80 C ANISOU 2303 CB GLU A 329 7310 8586 7964 207 210 652 C ATOM 2304 CG GLU A 329 17.392 6.338 7.612 1.00 68.12 C ANISOU 2304 CG GLU A 329 7985 9271 8626 332 261 709 C ATOM 2305 CD GLU A 329 18.400 6.897 8.616 1.00 71.83 C ANISOU 2305 CD GLU A 329 8528 9616 9149 386 293 650 C ATOM 2306 OE1 GLU A 329 19.516 6.340 8.727 1.00 71.96 O ANISOU 2306 OE1 GLU A 329 8576 9549 9217 333 279 569 O ATOM 2307 OE2 GLU A 329 18.071 7.896 9.295 1.00 73.51 O ANISOU 2307 OE2 GLU A 329 8770 9818 9343 485 332 689 O ATOM 2308 N THR A 330 18.721 6.304 4.199 1.00 54.59 N ANISOU 2308 N THR A 330 6350 7533 6860 194 264 618 N ATOM 2309 CA THR A 330 18.279 6.785 2.886 1.00 53.48 C ANISOU 2309 CA THR A 330 6209 7468 6645 180 262 667 C ATOM 2310 C THR A 330 19.024 6.087 1.747 1.00 54.98 C ANISOU 2310 C THR A 330 6450 7631 6807 90 263 589 C ATOM 2311 O THR A 330 18.761 6.343 0.569 1.00 58.51 O ANISOU 2311 O THR A 330 6913 8139 7179 60 259 618 O ATOM 2312 CB THR A 330 18.462 8.321 2.719 1.00 45.33 C ANISOU 2312 CB THR A 330 5211 6405 5605 275 315 715 C ATOM 2313 OG1 THR A 330 19.849 8.675 2.820 1.00 43.99 O ANISOU 2313 OG1 THR A 330 5108 6116 5491 268 362 638 O ATOM 2314 CG2 THR A 330 17.661 9.087 3.757 1.00 46.70 C ANISOU 2314 CG2 THR A 330 5362 6597 5786 391 328 793 C ATOM 2315 N CYS A 331 19.970 5.222 2.094 1.00 51.66 N ANISOU 2315 N CYS A 331 6063 7122 6442 60 275 494 N ATOM 2316 CA CYS A 331 20.680 4.445 1.087 1.00 48.07 C ANISOU 2316 CA CYS A 331 5669 6638 5958 -2 292 413 C ATOM 2317 C CYS A 331 20.216 2.997 1.151 1.00 48.70 C ANISOU 2317 C CYS A 331 5780 6712 6013 -81 236 377 C ATOM 2318 O CYS A 331 19.926 2.485 2.229 1.00 47.73 O ANISOU 2318 O CYS A 331 5632 6566 5938 -80 203 385 O ATOM 2319 CB CYS A 331 22.192 4.525 1.286 1.00 45.78 C ANISOU 2319 CB CYS A 331 5398 6255 5740 38 358 337 C ATOM 2320 SG CYS A 331 22.905 6.187 1.155 1.00 41.22 S ANISOU 2320 SG CYS A 331 4809 5666 5185 87 420 375 S ATOM 2321 N LYS A 332 20.144 2.343 -0.003 1.00 48.98 N ANISOU 2321 N LYS A 332 5886 6760 5963 -160 225 337 N ATOM 2322 CA LYS A 332 19.750 0.944 -0.060 1.00 50.93 C ANISOU 2322 CA LYS A 332 6205 6976 6170 -256 170 293 C ATOM 2323 C LYS A 332 20.927 0.100 -0.534 1.00 50.13 C ANISOU 2323 C LYS A 332 6219 6755 6072 -241 229 173 C ATOM 2324 O LYS A 332 21.514 0.366 -1.584 1.00 49.74 O ANISOU 2324 O LYS A 332 6217 6710 5971 -228 286 132 O ATOM 2325 CB LYS A 332 18.544 0.765 -0.985 1.00 55.58 C ANISOU 2325 CB LYS A 332 6805 7678 6634 -378 93 347 C ATOM 2326 CG LYS A 332 17.377 1.714 -0.688 1.00 59.88 C ANISOU 2326 CG LYS A 332 7214 8372 7166 -363 48 484 C ATOM 2327 CD LYS A 332 16.737 2.261 -1.971 1.00 63.40 C ANISOU 2327 CD LYS A 332 7651 8944 7494 -412 14 547 C ATOM 2328 CE LYS A 332 15.470 3.071 -1.687 1.00 64.65 C ANISOU 2328 CE LYS A 332 7665 9267 7634 -382 -36 699 C ATOM 2329 NZ LYS A 332 15.747 4.284 -0.865 1.00 65.02 N ANISOU 2329 NZ LYS A 332 7646 9288 7771 -215 35 745 N ATOM 2330 N VAL A 333 21.285 -0.912 0.247 1.00 49.05 N ANISOU 2330 N VAL A 333 6129 6515 5992 -229 222 122 N ATOM 2331 CA VAL A 333 22.394 -1.780 -0.118 1.00 49.94 C ANISOU 2331 CA VAL A 333 6353 6510 6111 -182 286 16 C ATOM 2332 C VAL A 333 21.918 -3.080 -0.765 1.00 53.17 C ANISOU 2332 C VAL A 333 6932 6851 6419 -288 244 -44 C ATOM 2333 O VAL A 333 21.107 -3.810 -0.194 1.00 54.54 O ANISOU 2333 O VAL A 333 7142 6999 6583 -378 163 -19 O ATOM 2334 CB VAL A 333 23.264 -2.111 1.102 1.00 49.06 C ANISOU 2334 CB VAL A 333 6206 6311 6122 -78 311 -4 C ATOM 2335 CG1 VAL A 333 24.344 -3.113 0.729 1.00 49.09 C ANISOU 2335 CG1 VAL A 333 6323 6200 6130 -5 379 -102 C ATOM 2336 CG2 VAL A 333 23.874 -0.844 1.652 1.00 48.58 C ANISOU 2336 CG2 VAL A 333 6006 6307 6146 6 350 41 C ATOM 2337 N GLN A 334 22.417 -3.345 -1.968 1.00 55.69 N ANISOU 2337 N GLN A 334 7367 7140 6651 -287 302 -121 N ATOM 2338 CA GLN A 334 22.187 -4.607 -2.658 1.00 61.53 C ANISOU 2338 CA GLN A 334 8317 7780 7280 -375 280 -203 C ATOM 2339 C GLN A 334 23.522 -5.319 -2.851 1.00 66.66 C ANISOU 2339 C GLN A 334 9083 8292 7954 -235 395 -312 C ATOM 2340 O GLN A 334 24.329 -4.909 -3.685 1.00 66.02 O ANISOU 2340 O GLN A 334 9004 8238 7841 -154 495 -355 O ATOM 2341 CB GLN A 334 21.500 -4.378 -4.005 1.00 64.02 C ANISOU 2341 CB GLN A 334 8703 8185 7438 -502 247 -204 C ATOM 2342 CG GLN A 334 20.142 -3.695 -3.906 1.00 66.63 C ANISOU 2342 CG GLN A 334 8905 8676 7736 -627 133 -80 C ATOM 2343 CD GLN A 334 19.021 -4.630 -3.450 1.00 68.56 C ANISOU 2343 CD GLN A 334 9202 8907 7940 -792 10 -49 C ATOM 2344 OE1 GLN A 334 18.357 -5.263 -4.272 1.00 69.96 O ANISOU 2344 OE1 GLN A 334 9512 9091 7977 -957 -63 -71 O ATOM 2345 NE2 GLN A 334 18.797 -4.703 -2.135 1.00 66.83 N ANISOU 2345 NE2 GLN A 334 8881 8677 7835 -764 -18 9 N ATOM 2346 N SER A 335 23.738 -6.384 -2.079 1.00 70.79 N ANISOU 2346 N SER A 335 9698 8672 8527 -199 383 -348 N ATOM 2347 CA SER A 335 25.017 -7.102 -2.020 1.00 72.29 C ANISOU 2347 CA SER A 335 9976 8730 8762 -26 491 -431 C ATOM 2348 C SER A 335 26.154 -6.158 -1.602 1.00 70.62 C ANISOU 2348 C SER A 335 9555 8603 8673 139 579 -397 C ATOM 2349 O SER A 335 26.332 -5.889 -0.413 1.00 70.61 O ANISOU 2349 O SER A 335 9418 8617 8793 188 547 -336 O ATOM 2350 CB SER A 335 25.334 -7.791 -3.358 1.00 74.82 C ANISOU 2350 CB SER A 335 10522 8967 8940 -20 566 -544 C ATOM 2351 OG SER A 335 25.403 -6.866 -4.433 1.00 75.86 O ANISOU 2351 OG SER A 335 10597 9231 8994 -41 615 -542 O ATOM 2352 N ASN A 336 26.924 -5.655 -2.561 1.00 66.66 N ANISOU 2352 N ASN A 336 9031 8163 8133 211 686 -432 N ATOM 2353 CA ASN A 336 27.979 -4.707 -2.221 1.00 61.25 C ANISOU 2353 CA ASN A 336 8141 7575 7554 330 762 -389 C ATOM 2354 C ASN A 336 27.845 -3.404 -3.005 1.00 53.59 C ANISOU 2354 C ASN A 336 7072 6750 6538 266 785 -345 C ATOM 2355 O ASN A 336 28.786 -2.621 -3.089 1.00 50.78 O ANISOU 2355 O ASN A 336 6584 6476 6235 340 866 -321 O ATOM 2356 CB ASN A 336 29.362 -5.327 -2.446 1.00 64.19 C ANISOU 2356 CB ASN A 336 8539 7896 7955 516 895 -452 C ATOM 2357 CG ASN A 336 29.674 -5.550 -3.913 1.00 68.94 C ANISOU 2357 CG ASN A 336 9277 8499 8420 540 1006 -532 C ATOM 2358 OD1 ASN A 336 28.782 -5.814 -4.719 1.00 70.66 O ANISOU 2358 OD1 ASN A 336 9661 8684 8503 413 965 -572 O ATOM 2359 ND2 ASN A 336 30.952 -5.439 -4.268 1.00 70.95 N ANISOU 2359 ND2 ASN A 336 9454 8803 8700 698 1148 -550 N ATOM 2360 N ARG A 337 26.660 -3.175 -3.561 1.00 49.70 N ANISOU 2360 N ARG A 337 6644 6295 5944 120 707 -325 N ATOM 2361 CA ARG A 337 26.352 -1.937 -4.268 1.00 47.45 C ANISOU 2361 CA ARG A 337 6280 6140 5607 56 710 -266 C ATOM 2362 C ARG A 337 25.440 -1.036 -3.421 1.00 44.89 C ANISOU 2362 C ARG A 337 5827 5886 5344 -9 606 -160 C ATOM 2363 O ARG A 337 24.411 -1.487 -2.913 1.00 44.89 O ANISOU 2363 O ARG A 337 5855 5868 5335 -87 505 -135 O ATOM 2364 CB ARG A 337 25.700 -2.260 -5.612 1.00 48.62 C ANISOU 2364 CB ARG A 337 6591 6303 5581 -46 699 -308 C ATOM 2365 CG ARG A 337 25.155 -1.068 -6.362 1.00 49.56 C ANISOU 2365 CG ARG A 337 6648 6554 5627 -123 677 -232 C ATOM 2366 CD ARG A 337 26.144 -0.571 -7.381 1.00 51.99 C ANISOU 2366 CD ARG A 337 6962 6910 5880 -64 809 -259 C ATOM 2367 NE ARG A 337 26.618 -1.640 -8.255 1.00 53.84 N ANISOU 2367 NE ARG A 337 7380 7073 6004 -34 890 -375 N ATOM 2368 CZ ARG A 337 27.584 -1.481 -9.151 1.00 54.88 C ANISOU 2368 CZ ARG A 337 7539 7238 6076 40 1030 -416 C ATOM 2369 NH1 ARG A 337 28.164 -0.296 -9.284 1.00 55.68 N ANISOU 2369 NH1 ARG A 337 7489 7445 6221 67 1093 -344 N ATOM 2370 NH2 ARG A 337 27.972 -2.494 -9.910 1.00 55.88 N ANISOU 2370 NH2 ARG A 337 7852 7287 6091 84 1113 -528 N ATOM 2371 N VAL A 338 25.820 0.229 -3.255 1.00 42.12 N ANISOU 2371 N VAL A 338 5341 5613 5050 23 637 -95 N ATOM 2372 CA VAL A 338 25.024 1.155 -2.452 1.00 38.47 C ANISOU 2372 CA VAL A 338 4777 5202 4638 -10 558 1 C ATOM 2373 C VAL A 338 24.273 2.143 -3.315 1.00 36.26 C ANISOU 2373 C VAL A 338 4491 5018 4268 -73 538 69 C ATOM 2374 O VAL A 338 24.884 2.927 -4.044 1.00 35.95 O ANISOU 2374 O VAL A 338 4439 5019 4202 -56 610 80 O ATOM 2375 CB VAL A 338 25.878 1.965 -1.466 1.00 40.33 C ANISOU 2375 CB VAL A 338 4889 5436 4999 63 590 34 C ATOM 2376 CG1 VAL A 338 25.008 2.468 -0.306 1.00 39.65 C ANISOU 2376 CG1 VAL A 338 4740 5358 4966 49 505 107 C ATOM 2377 CG2 VAL A 338 27.001 1.135 -0.951 1.00 42.78 C ANISOU 2377 CG2 VAL A 338 5188 5681 5386 146 638 -28 C ATOM 2378 N PHE A 339 22.948 2.116 -3.212 1.00 35.59 N ANISOU 2378 N PHE A 339 4407 4980 4135 -143 441 127 N ATOM 2379 CA PHE A 339 22.104 3.065 -3.920 1.00 36.16 C ANISOU 2379 CA PHE A 339 4457 5157 4125 -185 407 215 C ATOM 2380 C PHE A 339 21.754 4.223 -2.999 1.00 38.22 C ANISOU 2380 C PHE A 339 4610 5446 4465 -126 389 311 C ATOM 2381 O PHE A 339 21.065 4.049 -1.994 1.00 35.64 O ANISOU 2381 O PHE A 339 4231 5123 4187 -119 331 348 O ATOM 2382 CB PHE A 339 20.831 2.387 -4.440 1.00 33.71 C ANISOU 2382 CB PHE A 339 4196 4910 3702 -297 307 238 C ATOM 2383 CG PHE A 339 21.076 1.449 -5.590 1.00 34.08 C ANISOU 2383 CG PHE A 339 4391 4930 3630 -370 323 146 C ATOM 2384 CD1 PHE A 339 21.548 0.163 -5.368 1.00 32.43 C ANISOU 2384 CD1 PHE A 339 4285 4604 3433 -378 339 39 C ATOM 2385 CD2 PHE A 339 20.841 1.856 -6.896 1.00 33.29 C ANISOU 2385 CD2 PHE A 339 4345 4910 3394 -424 323 167 C ATOM 2386 CE1 PHE A 339 21.777 -0.696 -6.427 1.00 33.45 C ANISOU 2386 CE1 PHE A 339 4583 4687 3438 -433 364 -54 C ATOM 2387 CE2 PHE A 339 21.067 1.001 -7.961 1.00 33.79 C ANISOU 2387 CE2 PHE A 339 4569 4943 3329 -492 342 74 C ATOM 2388 CZ PHE A 339 21.537 -0.278 -7.726 1.00 33.95 C ANISOU 2388 CZ PHE A 339 4705 4836 3359 -495 366 -42 C ATOM 2389 N CYS A 340 22.246 5.405 -3.345 1.00 39.64 N ANISOU 2389 N CYS A 340 4772 5639 4649 -85 445 351 N ATOM 2390 CA CYS A 340 21.960 6.600 -2.573 1.00 39.41 C ANISOU 2390 CA CYS A 340 4684 5612 4677 -24 439 436 C ATOM 2391 C CYS A 340 21.405 7.683 -3.489 1.00 42.19 C ANISOU 2391 C CYS A 340 5053 6034 4944 -21 438 529 C ATOM 2392 O CYS A 340 21.474 7.572 -4.717 1.00 46.50 O ANISOU 2392 O CYS A 340 5651 6626 5392 -71 452 522 O ATOM 2393 CB CYS A 340 23.215 7.108 -1.864 1.00 39.21 C ANISOU 2393 CB CYS A 340 4640 5505 4754 20 504 402 C ATOM 2394 SG CYS A 340 23.919 6.033 -0.607 1.00 40.95 S ANISOU 2394 SG CYS A 340 4824 5649 5084 42 498 318 S ATOM 2395 N ASP A 341 20.864 8.730 -2.877 1.00 40.24 N ANISOU 2395 N ASP A 341 4776 5789 4726 48 425 619 N ATOM 2396 CA ASP A 341 20.302 9.864 -3.593 1.00 38.38 C ANISOU 2396 CA ASP A 341 4563 5602 4418 83 425 725 C ATOM 2397 C ASP A 341 21.084 11.105 -3.173 1.00 37.61 C ANISOU 2397 C ASP A 341 4509 5402 4377 135 490 745 C ATOM 2398 O ASP A 341 21.159 11.408 -1.980 1.00 37.51 O ANISOU 2398 O ASP A 341 4485 5321 4446 188 493 740 O ATOM 2399 CB ASP A 341 18.805 10.002 -3.278 1.00 37.09 C ANISOU 2399 CB ASP A 341 4336 5536 4221 135 351 830 C ATOM 2400 CG ASP A 341 18.107 11.021 -4.158 1.00 39.94 C ANISOU 2400 CG ASP A 341 4713 5971 4492 183 340 955 C ATOM 2401 OD1 ASP A 341 18.670 12.109 -4.386 1.00 43.73 O ANISOU 2401 OD1 ASP A 341 5265 6374 4975 228 398 984 O ATOM 2402 OD2 ASP A 341 16.989 10.737 -4.633 1.00 39.40 O ANISOU 2402 OD2 ASP A 341 4585 6041 4344 170 266 1032 O ATOM 2403 N THR A 342 21.668 11.825 -4.130 1.00 35.87 N ANISOU 2403 N THR A 342 4352 5169 4107 108 540 769 N ATOM 2404 CA THR A 342 22.535 12.954 -3.771 1.00 35.76 C ANISOU 2404 CA THR A 342 4395 5048 4143 119 599 783 C ATOM 2405 C THR A 342 21.770 14.099 -3.116 1.00 35.79 C ANISOU 2405 C THR A 342 4447 4997 4155 220 584 877 C ATOM 2406 O THR A 342 22.373 14.959 -2.481 1.00 36.12 O ANISOU 2406 O THR A 342 4556 4924 4246 228 618 877 O ATOM 2407 CB THR A 342 23.297 13.534 -4.982 1.00 34.93 C ANISOU 2407 CB THR A 342 4354 4946 3973 54 662 805 C ATOM 2408 OG1 THR A 342 22.367 13.994 -5.971 1.00 36.26 O ANISOU 2408 OG1 THR A 342 4565 5183 4031 81 635 904 O ATOM 2409 CG2 THR A 342 24.230 12.500 -5.585 1.00 34.46 C ANISOU 2409 CG2 THR A 342 4259 4931 3905 -25 706 707 C ATOM 2410 N MET A 343 20.447 14.110 -3.274 1.00 34.71 N ANISOU 2410 N MET A 343 4280 4946 3963 298 533 960 N ATOM 2411 CA MET A 343 19.614 15.123 -2.645 1.00 34.71 C ANISOU 2411 CA MET A 343 4318 4907 3963 433 530 1056 C ATOM 2412 C MET A 343 19.744 15.054 -1.119 1.00 36.13 C ANISOU 2412 C MET A 343 4491 5003 4234 478 536 1001 C ATOM 2413 O MET A 343 19.588 16.058 -0.429 1.00 36.26 O ANISOU 2413 O MET A 343 4594 4920 4263 572 564 1042 O ATOM 2414 CB MET A 343 18.150 14.958 -3.067 1.00 35.19 C ANISOU 2414 CB MET A 343 4301 5120 3951 511 471 1163 C ATOM 2415 CG MET A 343 17.231 16.057 -2.543 1.00 37.60 C ANISOU 2415 CG MET A 343 4640 5402 4244 689 483 1282 C ATOM 2416 SD MET A 343 17.864 17.714 -2.921 1.00 48.33 S ANISOU 2416 SD MET A 343 6201 6584 5578 742 553 1340 S ATOM 2417 CE MET A 343 17.898 17.660 -4.722 1.00 39.09 C ANISOU 2417 CE MET A 343 5033 5523 4298 653 530 1401 C ATOM 2418 N ASN A 344 20.047 13.863 -0.609 1.00 35.28 N ANISOU 2418 N ASN A 344 4299 4928 4180 411 512 908 N ATOM 2419 CA ASN A 344 20.223 13.645 0.819 1.00 36.76 C ANISOU 2419 CA ASN A 344 4473 5048 4444 438 510 854 C ATOM 2420 C ASN A 344 21.682 13.610 1.233 1.00 36.80 C ANISOU 2420 C ASN A 344 4515 4950 4518 348 538 758 C ATOM 2421 O ASN A 344 22.044 12.910 2.182 1.00 35.93 O ANISOU 2421 O ASN A 344 4360 4821 4469 328 520 690 O ATOM 2422 CB ASN A 344 19.559 12.335 1.235 1.00 39.53 C ANISOU 2422 CB ASN A 344 4709 5501 4810 425 459 828 C ATOM 2423 CG ASN A 344 18.138 12.227 0.737 1.00 43.72 C ANISOU 2423 CG ASN A 344 5169 6174 5268 479 418 931 C ATOM 2424 OD1 ASN A 344 17.340 13.157 0.897 1.00 44.93 O ANISOU 2424 OD1 ASN A 344 5338 6343 5390 602 432 1030 O ATOM 2425 ND2 ASN A 344 17.812 11.094 0.112 1.00 43.62 N ANISOU 2425 ND2 ASN A 344 5084 6268 5222 387 366 913 N ATOM 2426 N SER A 345 22.526 14.350 0.519 1.00 36.83 N ANISOU 2426 N SER A 345 4588 4899 4505 290 578 764 N ATOM 2427 CA SER A 345 23.949 14.344 0.824 1.00 35.38 C ANISOU 2427 CA SER A 345 4411 4650 4382 190 603 691 C ATOM 2428 C SER A 345 24.517 15.741 1.049 1.00 35.81 C ANISOU 2428 C SER A 345 4595 4578 4433 163 633 724 C ATOM 2429 O SER A 345 23.947 16.737 0.606 1.00 36.81 O ANISOU 2429 O SER A 345 4827 4659 4500 217 650 804 O ATOM 2430 CB SER A 345 24.740 13.653 -0.294 1.00 31.95 C ANISOU 2430 CB SER A 345 3917 4289 3934 101 632 652 C ATOM 2431 OG SER A 345 24.774 14.435 -1.474 1.00 31.46 O ANISOU 2431 OG SER A 345 3920 4236 3799 75 670 715 O ATOM 2432 N LEU A 346 25.636 15.786 1.764 1.00 33.87 N ANISOU 2432 N LEU A 346 4347 4274 4246 75 632 666 N ATOM 2433 CA LEU A 346 26.534 16.935 1.756 1.00 33.67 C ANISOU 2433 CA LEU A 346 4430 4147 4217 -22 657 686 C ATOM 2434 C LEU A 346 27.754 16.571 0.923 1.00 34.16 C ANISOU 2434 C LEU A 346 4398 4286 4296 -151 692 665 C ATOM 2435 O LEU A 346 28.129 15.403 0.833 1.00 33.59 O ANISOU 2435 O LEU A 346 4187 4314 4263 -156 691 608 O ATOM 2436 CB LEU A 346 26.971 17.320 3.168 1.00 33.38 C ANISOU 2436 CB LEU A 346 4456 4006 4221 -55 622 647 C ATOM 2437 CG LEU A 346 25.889 17.710 4.174 1.00 35.34 C ANISOU 2437 CG LEU A 346 4810 4171 4447 78 602 658 C ATOM 2438 CD1 LEU A 346 26.517 17.887 5.550 1.00 36.50 C ANISOU 2438 CD1 LEU A 346 5011 4232 4625 18 564 601 C ATOM 2439 CD2 LEU A 346 25.166 18.991 3.720 1.00 33.81 C ANISOU 2439 CD2 LEU A 346 4796 3873 4179 157 639 741 C ATOM 2440 N THR A 347 28.371 17.570 0.315 1.00 34.93 N ANISOU 2440 N THR A 347 4579 4334 4360 -248 730 714 N ATOM 2441 CA THR A 347 29.600 17.362 -0.419 1.00 36.18 C ANISOU 2441 CA THR A 347 4643 4575 4529 -377 776 707 C ATOM 2442 C THR A 347 30.759 17.822 0.452 1.00 36.25 C ANISOU 2442 C THR A 347 4645 4537 4592 -515 755 690 C ATOM 2443 O THR A 347 30.883 19.001 0.759 1.00 36.58 O ANISOU 2443 O THR A 347 4839 4452 4608 -591 743 731 O ATOM 2444 CB THR A 347 29.577 18.122 -1.751 1.00 38.15 C ANISOU 2444 CB THR A 347 4973 4825 4695 -420 835 786 C ATOM 2445 OG1 THR A 347 28.436 17.693 -2.506 1.00 38.14 O ANISOU 2445 OG1 THR A 347 4978 4880 4634 -297 835 807 O ATOM 2446 CG2 THR A 347 30.848 17.869 -2.554 1.00 37.17 C ANISOU 2446 CG2 THR A 347 4739 4812 4573 -548 901 784 C ATOM 2447 N LEU A 348 31.596 16.880 0.863 1.00 35.21 N ANISOU 2447 N LEU A 348 4344 4504 4528 -546 745 634 N ATOM 2448 CA LEU A 348 32.699 17.182 1.764 1.00 35.87 C ANISOU 2448 CA LEU A 348 4387 4578 4664 -680 706 624 C ATOM 2449 C LEU A 348 34.052 16.972 1.111 1.00 38.19 C ANISOU 2449 C LEU A 348 4520 5011 4981 -803 759 644 C ATOM 2450 O LEU A 348 34.179 16.176 0.182 1.00 39.90 O ANISOU 2450 O LEU A 348 4624 5345 5191 -743 828 634 O ATOM 2451 CB LEU A 348 32.600 16.319 3.022 1.00 34.57 C ANISOU 2451 CB LEU A 348 4149 4424 4563 -609 636 559 C ATOM 2452 CG LEU A 348 31.303 16.518 3.800 1.00 34.60 C ANISOU 2452 CG LEU A 348 4296 4308 4542 -489 592 543 C ATOM 2453 CD1 LEU A 348 31.332 15.689 5.061 1.00 34.51 C ANISOU 2453 CD1 LEU A 348 4213 4315 4586 -442 526 487 C ATOM 2454 CD2 LEU A 348 31.084 18.002 4.108 1.00 33.74 C ANISOU 2454 CD2 LEU A 348 4406 4036 4377 -551 579 584 C ATOM 2455 N PRO A 349 35.076 17.690 1.599 1.00 39.04 N ANISOU 2455 N PRO A 349 4617 5110 5107 -980 730 675 N ATOM 2456 CA PRO A 349 36.444 17.394 1.161 1.00 40.19 C ANISOU 2456 CA PRO A 349 4559 5427 5285 -1095 776 704 C ATOM 2457 C PRO A 349 36.816 15.969 1.559 1.00 39.98 C ANISOU 2457 C PRO A 349 4322 5535 5332 -978 771 647 C ATOM 2458 O PRO A 349 36.335 15.467 2.577 1.00 38.80 O ANISOU 2458 O PRO A 349 4189 5332 5219 -889 696 595 O ATOM 2459 CB PRO A 349 37.295 18.435 1.903 1.00 41.23 C ANISOU 2459 CB PRO A 349 4733 5511 5421 -1318 710 748 C ATOM 2460 CG PRO A 349 36.448 18.919 3.025 1.00 42.01 C ANISOU 2460 CG PRO A 349 5036 5420 5505 -1285 618 709 C ATOM 2461 CD PRO A 349 35.024 18.806 2.558 1.00 39.95 C ANISOU 2461 CD PRO A 349 4911 5065 5203 -1089 654 689 C ATOM 2462 N SER A 350 37.646 15.313 0.759 1.00 39.77 N ANISOU 2462 N SER A 350 4111 5678 5321 -965 858 660 N ATOM 2463 CA SER A 350 37.973 13.914 1.016 1.00 40.39 C ANISOU 2463 CA SER A 350 4014 5869 5463 -822 869 608 C ATOM 2464 C SER A 350 38.761 13.733 2.318 1.00 41.96 C ANISOU 2464 C SER A 350 4088 6117 5739 -876 775 612 C ATOM 2465 O SER A 350 38.862 12.621 2.829 1.00 41.15 O ANISOU 2465 O SER A 350 3879 6066 5692 -744 755 571 O ATOM 2466 CB SER A 350 38.759 13.331 -0.156 1.00 40.92 C ANISOU 2466 CB SER A 350 3924 6106 5518 -784 1000 626 C ATOM 2467 OG SER A 350 39.970 14.042 -0.320 1.00 45.20 O ANISOU 2467 OG SER A 350 4340 6768 6067 -960 1030 708 O ATOM 2468 N GLU A 351 39.311 14.823 2.855 1.00 42.76 N ANISOU 2468 N GLU A 351 4218 6195 5835 -1078 710 666 N ATOM 2469 CA GLU A 351 40.037 14.760 4.120 1.00 44.27 C ANISOU 2469 CA GLU A 351 4307 6433 6081 -1159 600 676 C ATOM 2470 C GLU A 351 39.146 14.332 5.292 1.00 45.33 C ANISOU 2470 C GLU A 351 4555 6439 6231 -1046 502 607 C ATOM 2471 O GLU A 351 39.654 13.922 6.333 1.00 46.49 O ANISOU 2471 O GLU A 351 4601 6639 6422 -1057 414 604 O ATOM 2472 CB GLU A 351 40.695 16.106 4.436 1.00 45.54 C ANISOU 2472 CB GLU A 351 4523 6569 6210 -1430 539 742 C ATOM 2473 CG GLU A 351 41.996 16.363 3.672 1.00 49.53 C ANISOU 2473 CG GLU A 351 4822 7274 6722 -1584 606 833 C ATOM 2474 CD GLU A 351 41.763 16.845 2.251 1.00 52.75 C ANISOU 2474 CD GLU A 351 5306 7669 7069 -1601 735 865 C ATOM 2475 OE1 GLU A 351 40.591 17.051 1.864 1.00 52.69 O ANISOU 2475 OE1 GLU A 351 5516 7492 7012 -1501 759 822 O ATOM 2476 OE2 GLU A 351 42.758 17.025 1.520 1.00 56.38 O ANISOU 2476 OE2 GLU A 351 5598 8299 7524 -1715 812 943 O ATOM 2477 N VAL A 352 37.826 14.417 5.118 1.00 43.47 N ANISOU 2477 N VAL A 352 4516 6050 5952 -938 517 561 N ATOM 2478 CA VAL A 352 36.882 13.970 6.143 1.00 41.88 C ANISOU 2478 CA VAL A 352 4414 5741 5757 -820 443 503 C ATOM 2479 C VAL A 352 37.176 12.526 6.553 1.00 42.64 C ANISOU 2479 C VAL A 352 4338 5942 5921 -682 430 473 C ATOM 2480 O VAL A 352 36.928 12.132 7.692 1.00 41.37 O ANISOU 2480 O VAL A 352 4197 5741 5780 -638 345 446 O ATOM 2481 CB VAL A 352 35.401 14.091 5.664 1.00 36.55 C ANISOU 2481 CB VAL A 352 3922 4938 5029 -698 483 475 C ATOM 2482 CG1 VAL A 352 35.121 13.189 4.459 1.00 34.64 C ANISOU 2482 CG1 VAL A 352 3603 4773 4785 -573 578 460 C ATOM 2483 CG2 VAL A 352 34.435 13.771 6.800 1.00 35.38 C ANISOU 2483 CG2 VAL A 352 3873 4691 4880 -597 411 430 C ATOM 2484 N ASN A 353 37.741 11.754 5.628 1.00 43.83 N ANISOU 2484 N ASN A 353 4331 6221 6099 -611 519 480 N ATOM 2485 CA ASN A 353 38.075 10.363 5.892 1.00 44.06 C ANISOU 2485 CA ASN A 353 4215 6336 6188 -461 523 456 C ATOM 2486 C ASN A 353 39.192 10.201 6.919 1.00 43.31 C ANISOU 2486 C ASN A 353 3956 6349 6152 -518 440 495 C ATOM 2487 O ASN A 353 39.310 9.149 7.552 1.00 43.62 O ANISOU 2487 O ASN A 353 3918 6419 6238 -393 404 479 O ATOM 2488 CB ASN A 353 38.469 9.655 4.594 1.00 46.55 C ANISOU 2488 CB ASN A 353 4427 6756 6503 -364 655 452 C ATOM 2489 CG ASN A 353 38.760 8.177 4.806 1.00 49.18 C ANISOU 2489 CG ASN A 353 4649 7147 6890 -183 672 422 C ATOM 2490 OD1 ASN A 353 37.896 7.419 5.262 1.00 48.94 O ANISOU 2490 OD1 ASN A 353 4716 7016 6863 -73 632 370 O ATOM 2491 ND2 ASN A 353 39.984 7.761 4.485 1.00 50.88 N ANISOU 2491 ND2 ASN A 353 4662 7526 7145 -147 735 462 N ATOM 2492 N LEU A 354 40.003 11.240 7.089 1.00 42.65 N ANISOU 2492 N LEU A 354 3824 6322 6059 -715 401 555 N ATOM 2493 CA LEU A 354 41.133 11.179 8.014 1.00 43.31 C ANISOU 2493 CA LEU A 354 3732 6537 6187 -803 308 608 C ATOM 2494 C LEU A 354 40.675 11.019 9.462 1.00 43.41 C ANISOU 2494 C LEU A 354 3840 6453 6199 -791 173 577 C ATOM 2495 O LEU A 354 41.438 10.544 10.305 1.00 44.37 O ANISOU 2495 O LEU A 354 3813 6684 6362 -793 90 612 O ATOM 2496 CB LEU A 354 42.008 12.426 7.885 1.00 43.46 C ANISOU 2496 CB LEU A 354 3706 6626 6180 -1061 283 681 C ATOM 2497 CG LEU A 354 42.787 12.605 6.582 1.00 46.44 C ANISOU 2497 CG LEU A 354 3931 7155 6559 -1108 411 741 C ATOM 2498 CD1 LEU A 354 43.550 13.925 6.589 1.00 46.21 C ANISOU 2498 CD1 LEU A 354 3891 7171 6495 -1403 366 819 C ATOM 2499 CD2 LEU A 354 43.737 11.438 6.347 1.00 47.43 C ANISOU 2499 CD2 LEU A 354 3768 7500 6753 -957 472 778 C ATOM 2500 N CYS A 355 39.433 11.415 9.741 1.00 41.03 N ANISOU 2500 N CYS A 355 3783 5962 5846 -772 154 519 N ATOM 2501 CA CYS A 355 38.868 11.319 11.085 1.00 41.79 C ANISOU 2501 CA CYS A 355 3997 5958 5923 -754 44 486 C ATOM 2502 C CYS A 355 38.805 9.875 11.582 1.00 42.31 C ANISOU 2502 C CYS A 355 3961 6072 6043 -568 26 471 C ATOM 2503 O CYS A 355 38.723 9.621 12.780 1.00 42.75 O ANISOU 2503 O CYS A 355 4046 6103 6093 -562 -76 466 O ATOM 2504 CB CYS A 355 37.466 11.938 11.122 1.00 40.65 C ANISOU 2504 CB CYS A 355 4115 5619 5711 -727 61 434 C ATOM 2505 SG CYS A 355 37.435 13.713 10.777 1.00 49.67 S ANISOU 2505 SG CYS A 355 5445 6651 6777 -932 67 453 S ATOM 2506 N ASN A 356 38.846 8.929 10.655 1.00 42.08 N ANISOU 2506 N ASN A 356 3831 6102 6056 -418 126 464 N ATOM 2507 CA ASN A 356 38.766 7.528 11.021 1.00 42.47 C ANISOU 2507 CA ASN A 356 3816 6169 6151 -235 119 449 C ATOM 2508 C ASN A 356 40.080 6.996 11.592 1.00 45.47 C ANISOU 2508 C ASN A 356 3973 6712 6590 -221 62 513 C ATOM 2509 O ASN A 356 40.074 6.273 12.588 1.00 47.82 O ANISOU 2509 O ASN A 356 4258 7004 6908 -145 -19 520 O ATOM 2510 CB ASN A 356 38.318 6.712 9.813 1.00 40.33 C ANISOU 2510 CB ASN A 356 3555 5880 5888 -84 247 411 C ATOM 2511 CG ASN A 356 36.903 7.048 9.392 1.00 39.16 C ANISOU 2511 CG ASN A 356 3613 5585 5680 -80 280 358 C ATOM 2512 OD1 ASN A 356 36.013 7.182 10.234 1.00 38.11 O ANISOU 2512 OD1 ASN A 356 3611 5350 5520 -85 213 338 O ATOM 2513 ND2 ASN A 356 36.688 7.209 8.094 1.00 40.18 N ANISOU 2513 ND2 ASN A 356 3765 5718 5782 -69 384 344 N ATOM 2514 N VAL A 357 41.205 7.363 10.990 1.00 46.59 N ANISOU 2514 N VAL A 357 3933 7013 6757 -296 102 572 N ATOM 2515 CA VAL A 357 42.488 6.897 11.505 1.00 50.07 C ANISOU 2515 CA VAL A 357 4129 7644 7253 -279 47 652 C ATOM 2516 C VAL A 357 43.100 7.867 12.520 1.00 50.75 C ANISOU 2516 C VAL A 357 4175 7793 7314 -510 -102 708 C ATOM 2517 O VAL A 357 43.872 7.456 13.384 1.00 53.12 O ANISOU 2517 O VAL A 357 4322 8218 7644 -503 -202 770 O ATOM 2518 CB VAL A 357 43.507 6.645 10.368 1.00 54.66 C ANISOU 2518 CB VAL A 357 4485 8409 7875 -222 174 705 C ATOM 2519 CG1 VAL A 357 43.008 5.536 9.457 1.00 54.97 C ANISOU 2519 CG1 VAL A 357 4574 8385 7928 19 313 645 C ATOM 2520 CG2 VAL A 357 43.782 7.924 9.579 1.00 56.54 C ANISOU 2520 CG2 VAL A 357 4719 8690 8073 -434 221 730 C ATOM 2521 N ASP A 358 42.755 9.146 12.421 1.00 50.47 N ANISOU 2521 N ASP A 358 4293 7668 7216 -713 -121 688 N ATOM 2522 CA ASP A 358 43.285 10.144 13.343 1.00 51.62 C ANISOU 2522 CA ASP A 358 4453 7842 7317 -959 -263 728 C ATOM 2523 C ASP A 358 42.295 11.287 13.547 1.00 48.84 C ANISOU 2523 C ASP A 358 4408 7271 6879 -1094 -286 662 C ATOM 2524 O ASP A 358 42.286 12.263 12.793 1.00 49.25 O ANISOU 2524 O ASP A 358 4535 7281 6897 -1229 -231 666 O ATOM 2525 CB ASP A 358 44.625 10.679 12.836 1.00 55.74 C ANISOU 2525 CB ASP A 358 4738 8580 7861 -1131 -258 826 C ATOM 2526 CG ASP A 358 45.217 11.733 13.749 1.00 60.34 C ANISOU 2526 CG ASP A 358 5344 9196 8387 -1425 -418 872 C ATOM 2527 OD1 ASP A 358 44.874 11.750 14.951 1.00 61.28 O ANISOU 2527 OD1 ASP A 358 5594 9227 8464 -1455 -548 841 O ATOM 2528 OD2 ASP A 358 46.034 12.545 13.264 1.00 65.11 O ANISOU 2528 OD2 ASP A 358 5844 9915 8980 -1638 -415 939 O ATOM 2529 N ILE A 359 41.471 11.158 14.583 1.00 46.53 N ANISOU 2529 N ILE A 359 4296 6839 6544 -1046 -362 608 N ATOM 2530 CA ILE A 359 40.451 12.151 14.899 1.00 44.46 C ANISOU 2530 CA ILE A 359 4335 6364 6194 -1125 -375 544 C ATOM 2531 C ILE A 359 41.051 13.522 15.252 1.00 45.42 C ANISOU 2531 C ILE A 359 4548 6463 6245 -1409 -462 568 C ATOM 2532 O ILE A 359 40.361 14.539 15.181 1.00 44.40 O ANISOU 2532 O ILE A 359 4673 6155 6043 -1487 -441 525 O ATOM 2533 CB ILE A 359 39.558 11.663 16.066 1.00 44.17 C ANISOU 2533 CB ILE A 359 4447 6216 6120 -1012 -438 493 C ATOM 2534 CG1 ILE A 359 38.292 12.515 16.178 1.00 41.55 C ANISOU 2534 CG1 ILE A 359 4416 5667 5703 -1013 -402 425 C ATOM 2535 CG2 ILE A 359 40.344 11.625 17.383 1.00 44.82 C ANISOU 2535 CG2 ILE A 359 4473 6380 6175 -1127 -599 528 C ATOM 2536 CD1 ILE A 359 37.036 11.716 16.125 1.00 39.54 C ANISOU 2536 CD1 ILE A 359 4236 5330 5458 -792 -330 381 C ATOM 2537 N PHE A 360 42.331 13.555 15.621 1.00 46.88 N ANISOU 2537 N PHE A 360 4532 6831 6448 -1566 -560 643 N ATOM 2538 CA PHE A 360 42.987 14.825 15.940 1.00 49.29 C ANISOU 2538 CA PHE A 360 4919 7128 6682 -1876 -657 673 C ATOM 2539 C PHE A 360 43.807 15.381 14.777 1.00 52.06 C ANISOU 2539 C PHE A 360 5123 7595 7061 -2025 -586 744 C ATOM 2540 O PHE A 360 44.579 16.320 14.960 1.00 55.09 O ANISOU 2540 O PHE A 360 5514 8021 7397 -2309 -672 794 O ATOM 2541 CB PHE A 360 43.888 14.676 17.166 1.00 49.64 C ANISOU 2541 CB PHE A 360 4849 7310 6704 -2015 -837 723 C ATOM 2542 CG PHE A 360 43.156 14.243 18.394 1.00 50.33 C ANISOU 2542 CG PHE A 360 5098 7284 6740 -1905 -917 661 C ATOM 2543 CD1 PHE A 360 42.272 15.104 19.027 1.00 49.87 C ANISOU 2543 CD1 PHE A 360 5392 6989 6569 -1973 -944 577 C ATOM 2544 CD2 PHE A 360 43.338 12.970 18.910 1.00 51.20 C ANISOU 2544 CD2 PHE A 360 5022 7522 6910 -1722 -954 690 C ATOM 2545 CE1 PHE A 360 41.580 14.699 20.153 1.00 50.10 C ANISOU 2545 CE1 PHE A 360 5568 6926 6540 -1866 -1003 524 C ATOM 2546 CE2 PHE A 360 42.652 12.560 20.037 1.00 51.51 C ANISOU 2546 CE2 PHE A 360 5215 7462 6895 -1628 -1022 642 C ATOM 2547 CZ PHE A 360 41.774 13.429 20.662 1.00 50.84 C ANISOU 2547 CZ PHE A 360 5467 7157 6693 -1704 -1045 558 C ATOM 2548 N ASN A 361 43.636 14.809 13.587 1.00 51.80 N ANISOU 2548 N ASN A 361 4968 7616 7097 -1846 -432 751 N ATOM 2549 CA ASN A 361 44.370 15.268 12.410 1.00 54.50 C ANISOU 2549 CA ASN A 361 5168 8080 7461 -1965 -343 821 C ATOM 2550 C ASN A 361 44.187 16.765 12.168 1.00 55.63 C ANISOU 2550 C ASN A 361 5563 8058 7516 -2215 -352 816 C ATOM 2551 O ASN A 361 43.127 17.323 12.462 1.00 54.38 O ANISOU 2551 O ASN A 361 5719 7651 7291 -2188 -355 739 O ATOM 2552 CB ASN A 361 43.941 14.481 11.168 1.00 53.44 C ANISOU 2552 CB ASN A 361 4951 7970 7383 -1717 -166 802 C ATOM 2553 CG ASN A 361 42.655 15.002 10.564 1.00 53.65 C ANISOU 2553 CG ASN A 361 5267 7760 7358 -1649 -78 728 C ATOM 2554 OD1 ASN A 361 42.671 15.935 9.757 1.00 56.35 O ANISOU 2554 OD1 ASN A 361 5701 8051 7660 -1783 -18 752 O ATOM 2555 ND2 ASN A 361 41.529 14.398 10.945 1.00 49.79 N ANISOU 2555 ND2 ASN A 361 4918 7134 6866 -1443 -70 649 N ATOM 2556 N PRO A 362 45.226 17.423 11.632 1.00 58.24 N ANISOU 2556 N PRO A 362 5759 8528 7843 -2455 -353 908 N ATOM 2557 CA PRO A 362 45.196 18.874 11.415 1.00 61.10 C ANISOU 2557 CA PRO A 362 6367 8732 8117 -2729 -372 919 C ATOM 2558 C PRO A 362 44.509 19.309 10.119 1.00 62.42 C ANISOU 2558 C PRO A 362 6677 8770 8268 -2653 -211 906 C ATOM 2559 O PRO A 362 44.316 20.508 9.919 1.00 64.69 O ANISOU 2559 O PRO A 362 7217 8884 8478 -2842 -217 910 O ATOM 2560 CB PRO A 362 46.681 19.240 11.372 1.00 63.64 C ANISOU 2560 CB PRO A 362 6433 9301 8447 -3025 -443 1042 C ATOM 2561 CG PRO A 362 47.334 18.027 10.793 1.00 62.70 C ANISOU 2561 CG PRO A 362 5916 9474 8434 -2829 -353 1104 C ATOM 2562 CD PRO A 362 46.531 16.836 11.275 1.00 60.34 C ANISOU 2562 CD PRO A 362 5628 9116 8181 -2491 -340 1017 C ATOM 2563 N LYS A 363 44.142 18.364 9.258 1.00 61.06 N ANISOU 2563 N LYS A 363 6368 8673 8159 -2386 -75 891 N ATOM 2564 CA LYS A 363 43.655 18.719 7.927 1.00 60.91 C ANISOU 2564 CA LYS A 363 6440 8584 8120 -2333 74 896 C ATOM 2565 C LYS A 363 42.134 18.808 7.862 1.00 57.70 C ANISOU 2565 C LYS A 363 6327 7922 7674 -2136 117 804 C ATOM 2566 O LYS A 363 41.587 19.487 7.002 1.00 58.20 O ANISOU 2566 O LYS A 363 6562 7862 7690 -2142 199 811 O ATOM 2567 CB LYS A 363 44.178 17.718 6.891 1.00 62.39 C ANISOU 2567 CB LYS A 363 6321 9007 8376 -2178 206 938 C ATOM 2568 CG LYS A 363 45.701 17.589 6.904 1.00 67.20 C ANISOU 2568 CG LYS A 363 6598 9907 9027 -2343 181 1046 C ATOM 2569 CD LYS A 363 46.227 16.707 5.779 1.00 70.82 C ANISOU 2569 CD LYS A 363 6778 10591 9538 -2178 341 1090 C ATOM 2570 CE LYS A 363 46.043 17.376 4.425 1.00 74.89 C ANISOU 2570 CE LYS A 363 7389 11066 9999 -2239 480 1119 C ATOM 2571 NZ LYS A 363 46.886 16.765 3.355 1.00 77.39 N ANISOU 2571 NZ LYS A 363 7414 11647 10346 -2162 633 1188 N ATOM 2572 N TYR A 364 41.450 18.128 8.775 1.00 55.08 N ANISOU 2572 N TYR A 364 6047 7523 7358 -1961 61 730 N ATOM 2573 CA TYR A 364 39.995 18.201 8.828 1.00 50.65 C ANISOU 2573 CA TYR A 364 5740 6746 6758 -1778 95 655 C ATOM 2574 C TYR A 364 39.508 18.191 10.276 1.00 49.68 C ANISOU 2574 C TYR A 364 5766 6505 6607 -1752 -19 593 C ATOM 2575 O TYR A 364 39.932 17.350 11.074 1.00 49.91 O ANISOU 2575 O TYR A 364 5633 6650 6680 -1712 -92 586 O ATOM 2576 CB TYR A 364 39.361 17.047 8.048 1.00 47.34 C ANISOU 2576 CB TYR A 364 5206 6393 6389 -1510 202 626 C ATOM 2577 CG TYR A 364 37.866 17.195 7.904 1.00 47.24 C ANISOU 2577 CG TYR A 364 5425 6192 6331 -1343 244 572 C ATOM 2578 CD1 TYR A 364 37.000 16.678 8.862 1.00 45.88 C ANISOU 2578 CD1 TYR A 364 5333 5939 6159 -1196 195 511 C ATOM 2579 CD2 TYR A 364 37.316 17.875 6.822 1.00 47.51 C ANISOU 2579 CD2 TYR A 364 5592 6142 6318 -1336 333 595 C ATOM 2580 CE1 TYR A 364 35.635 16.824 8.744 1.00 44.53 C ANISOU 2580 CE1 TYR A 364 5347 5627 5947 -1045 235 477 C ATOM 2581 CE2 TYR A 364 35.950 18.026 6.696 1.00 46.94 C ANISOU 2581 CE2 TYR A 364 5709 5923 6204 -1177 365 563 C ATOM 2582 CZ TYR A 364 35.114 17.498 7.660 1.00 46.03 C ANISOU 2582 CZ TYR A 364 5649 5747 6093 -1032 318 505 C ATOM 2583 OH TYR A 364 33.751 17.645 7.543 1.00 46.29 O ANISOU 2583 OH TYR A 364 5841 5663 6084 -872 353 488 O ATOM 2584 N ASP A 365 38.615 19.123 10.604 1.00 47.16 N ANISOU 2584 N ASP A 365 5759 5953 6206 -1760 -28 555 N ATOM 2585 CA ASP A 365 38.100 19.265 11.964 1.00 46.25 C ANISOU 2585 CA ASP A 365 5828 5707 6039 -1738 -121 494 C ATOM 2586 C ASP A 365 36.962 18.276 12.239 1.00 43.74 C ANISOU 2586 C ASP A 365 5502 5370 5746 -1454 -81 439 C ATOM 2587 O ASP A 365 35.800 18.534 11.916 1.00 42.96 O ANISOU 2587 O ASP A 365 5571 5138 5612 -1306 -7 415 O ATOM 2588 CB ASP A 365 37.634 20.705 12.195 1.00 49.07 C ANISOU 2588 CB ASP A 365 6542 5815 6288 -1850 -132 476 C ATOM 2589 CG ASP A 365 37.328 20.992 13.648 1.00 52.27 C ANISOU 2589 CG ASP A 365 7155 6087 6617 -1872 -230 413 C ATOM 2590 OD1 ASP A 365 37.835 20.254 14.519 1.00 53.53 O ANISOU 2590 OD1 ASP A 365 7163 6373 6803 -1894 -322 402 O ATOM 2591 OD2 ASP A 365 36.578 21.955 13.919 1.00 53.81 O ANISOU 2591 OD2 ASP A 365 7675 6051 6718 -1857 -212 378 O ATOM 2592 N CYS A 366 37.303 17.146 12.849 1.00 41.92 N ANISOU 2592 N CYS A 366 5073 5281 5574 -1383 -133 430 N ATOM 2593 CA CYS A 366 36.361 16.039 12.985 1.00 39.05 C ANISOU 2593 CA CYS A 366 4664 4929 5245 -1135 -93 393 C ATOM 2594 C CYS A 366 35.176 16.387 13.890 1.00 40.21 C ANISOU 2594 C CYS A 366 5060 4902 5315 -1041 -107 339 C ATOM 2595 O CYS A 366 35.345 16.967 14.967 1.00 41.56 O ANISOU 2595 O CYS A 366 5379 4993 5420 -1146 -193 317 O ATOM 2596 CB CYS A 366 37.090 14.795 13.505 1.00 38.00 C ANISOU 2596 CB CYS A 366 4284 4969 5184 -1093 -152 404 C ATOM 2597 SG CYS A 366 38.473 14.264 12.438 1.00 44.90 S ANISOU 2597 SG CYS A 366 4839 6073 6148 -1150 -111 474 S ATOM 2598 N LYS A 367 33.975 16.020 13.447 1.00 38.54 N ANISOU 2598 N LYS A 367 4893 4646 5106 -843 -22 323 N ATOM 2599 CA LYS A 367 32.760 16.419 14.142 1.00 40.42 C ANISOU 2599 CA LYS A 367 5352 4738 5270 -731 -7 288 C ATOM 2600 C LYS A 367 32.348 15.431 15.237 1.00 39.87 C ANISOU 2600 C LYS A 367 5236 4709 5205 -621 -53 260 C ATOM 2601 O LYS A 367 32.351 14.213 15.043 1.00 38.49 O ANISOU 2601 O LYS A 367 4872 4653 5101 -531 -47 268 O ATOM 2602 CB LYS A 367 31.621 16.612 13.137 1.00 41.42 C ANISOU 2602 CB LYS A 367 5541 4812 5385 -581 102 304 C ATOM 2603 CG LYS A 367 31.938 17.675 12.085 1.00 46.23 C ANISOU 2603 CG LYS A 367 6233 5360 5974 -683 149 340 C ATOM 2604 CD LYS A 367 30.692 18.210 11.410 1.00 49.82 C ANISOU 2604 CD LYS A 367 6828 5718 6382 -535 238 361 C ATOM 2605 CE LYS A 367 29.838 19.007 12.391 1.00 54.23 C ANISOU 2605 CE LYS A 367 7642 6110 6851 -456 238 336 C ATOM 2606 NZ LYS A 367 30.510 20.253 12.887 1.00 58.90 N ANISOU 2606 NZ LYS A 367 8462 6545 7374 -629 195 323 N ATOM 2607 N ILE A 368 32.007 15.988 16.394 1.00 38.70 N ANISOU 2607 N ILE A 368 5283 4450 4969 -634 -96 227 N ATOM 2608 CA ILE A 368 31.596 15.216 17.558 1.00 37.43 C ANISOU 2608 CA ILE A 368 5119 4316 4789 -546 -139 204 C ATOM 2609 C ILE A 368 30.485 15.934 18.294 1.00 36.64 C ANISOU 2609 C ILE A 368 5274 4070 4579 -452 -98 172 C ATOM 2610 O ILE A 368 30.314 17.144 18.142 1.00 38.40 O ANISOU 2610 O ILE A 368 5706 4152 4732 -490 -65 160 O ATOM 2611 CB ILE A 368 32.757 14.997 18.554 1.00 37.87 C ANISOU 2611 CB ILE A 368 5117 4434 4838 -699 -270 199 C ATOM 2612 CG1 ILE A 368 33.364 16.347 18.951 1.00 37.48 C ANISOU 2612 CG1 ILE A 368 5269 4273 4699 -898 -329 180 C ATOM 2613 CG2 ILE A 368 33.804 14.061 17.969 1.00 39.02 C ANISOU 2613 CG2 ILE A 368 4975 4755 5097 -740 -302 242 C ATOM 2614 CD1 ILE A 368 34.363 16.274 20.083 1.00 39.34 C ANISOU 2614 CD1 ILE A 368 5489 4563 4897 -1064 -474 176 C ATOM 2615 N MET A 369 29.740 15.186 19.099 1.00 36.09 N ANISOU 2615 N MET A 369 5194 4030 4489 -323 -94 163 N ATOM 2616 CA MET A 369 28.825 15.777 20.065 1.00 35.65 C ANISOU 2616 CA MET A 369 5370 3860 4316 -234 -60 133 C ATOM 2617 C MET A 369 29.253 15.334 21.464 1.00 36.12 C ANISOU 2617 C MET A 369 5455 3947 4323 -294 -158 107 C ATOM 2618 O MET A 369 29.947 14.331 21.611 1.00 35.59 O ANISOU 2618 O MET A 369 5192 4005 4327 -344 -234 127 O ATOM 2619 CB MET A 369 27.389 15.360 19.787 1.00 34.82 C ANISOU 2619 CB MET A 369 5235 3782 4212 -19 48 160 C ATOM 2620 CG MET A 369 27.178 13.863 19.899 1.00 36.60 C ANISOU 2620 CG MET A 369 5241 4154 4510 42 29 187 C ATOM 2621 SD MET A 369 25.450 13.416 20.114 1.00 62.82 S ANISOU 2621 SD MET A 369 8564 7514 7792 256 132 222 S ATOM 2622 CE MET A 369 25.117 14.255 21.666 1.00 41.41 C ANISOU 2622 CE MET A 369 6116 4691 4927 290 140 181 C ATOM 2623 N THR A 370 28.846 16.078 22.487 1.00 37.25 N ANISOU 2623 N THR A 370 5850 3971 4333 -280 -153 65 N ATOM 2624 CA THR A 370 29.228 15.750 23.854 1.00 39.89 C ANISOU 2624 CA THR A 370 6240 4324 4591 -345 -249 39 C ATOM 2625 C THR A 370 28.011 15.641 24.763 1.00 41.60 C ANISOU 2625 C THR A 370 6592 4506 4706 -170 -171 24 C ATOM 2626 O THR A 370 26.963 16.217 24.474 1.00 44.24 O ANISOU 2626 O THR A 370 7047 4764 4998 -19 -47 23 O ATOM 2627 CB THR A 370 30.196 16.799 24.432 1.00 41.83 C ANISOU 2627 CB THR A 370 6689 4464 4740 -558 -349 -8 C ATOM 2628 OG1 THR A 370 29.543 18.072 24.491 1.00 44.74 O ANISOU 2628 OG1 THR A 370 7368 4638 4994 -512 -265 -54 O ATOM 2629 CG2 THR A 370 31.442 16.917 23.562 1.00 40.40 C ANISOU 2629 CG2 THR A 370 6349 4345 4656 -749 -424 21 C ATOM 2630 N SER A 371 28.150 14.892 25.852 1.00 41.53 N ANISOU 2630 N SER A 371 6557 4568 4656 -183 -240 24 N ATOM 2631 CA SER A 371 27.084 14.780 26.846 1.00 42.91 C ANISOU 2631 CA SER A 371 6864 4724 4716 -36 -169 14 C ATOM 2632 C SER A 371 27.600 14.158 28.142 1.00 42.17 C ANISOU 2632 C SER A 371 6782 4687 4552 -117 -282 8 C ATOM 2633 O SER A 371 28.790 13.878 28.269 1.00 41.59 O ANISOU 2633 O SER A 371 6616 4667 4519 -284 -422 14 O ATOM 2634 CB SER A 371 25.914 13.950 26.305 1.00 43.19 C ANISOU 2634 CB SER A 371 6728 4856 4825 154 -56 74 C ATOM 2635 OG SER A 371 26.219 12.570 26.300 1.00 43.10 O ANISOU 2635 OG SER A 371 6480 4985 4913 131 -121 122 O ATOM 2636 N LYS A 372 26.699 13.956 29.103 1.00 42.69 N ANISOU 2636 N LYS A 372 6957 4755 4507 5 -219 6 N ATOM 2637 CA LYS A 372 27.011 13.206 30.316 1.00 44.03 C ANISOU 2637 CA LYS A 372 7125 4997 4607 -44 -313 17 C ATOM 2638 C LYS A 372 26.033 12.055 30.432 1.00 44.50 C ANISOU 2638 C LYS A 372 7031 5170 4707 109 -236 85 C ATOM 2639 O LYS A 372 25.860 11.465 31.499 1.00 48.43 O ANISOU 2639 O LYS A 372 7562 5719 5121 123 -263 104 O ATOM 2640 CB LYS A 372 26.951 14.095 31.564 1.00 45.25 C ANISOU 2640 CB LYS A 372 7604 5039 4550 -78 -323 -54 C ATOM 2641 CG LYS A 372 27.885 15.292 31.500 1.00 47.32 C ANISOU 2641 CG LYS A 372 8060 5168 4752 -260 -406 -124 C ATOM 2642 CD LYS A 372 28.100 15.947 32.853 1.00 50.07 C ANISOU 2642 CD LYS A 372 8723 5420 4882 -350 -467 -196 C ATOM 2643 CE LYS A 372 28.846 15.017 33.799 1.00 53.31 C ANISOU 2643 CE LYS A 372 9027 5962 5265 -468 -628 -162 C ATOM 2644 NZ LYS A 372 29.354 15.717 35.017 1.00 57.33 N ANISOU 2644 NZ LYS A 372 9838 6386 5561 -623 -733 -233 N ATOM 2645 N THR A 373 25.393 11.739 29.314 1.00 43.16 N ANISOU 2645 N THR A 373 6697 5042 4659 210 -144 126 N ATOM 2646 CA THR A 373 24.375 10.703 29.288 1.00 42.99 C ANISOU 2646 CA THR A 373 6531 5128 4675 336 -67 196 C ATOM 2647 C THR A 373 25.008 9.370 28.910 1.00 41.66 C ANISOU 2647 C THR A 373 6127 5056 4645 270 -163 249 C ATOM 2648 O THR A 373 25.020 8.985 27.743 1.00 42.56 O ANISOU 2648 O THR A 373 6077 5202 4891 280 -145 272 O ATOM 2649 CB THR A 373 23.235 11.061 28.302 1.00 42.62 C ANISOU 2649 CB THR A 373 6440 5086 4668 479 81 222 C ATOM 2650 OG1 THR A 373 22.653 12.313 28.685 1.00 46.21 O ANISOU 2650 OG1 THR A 373 7129 5440 4988 571 180 178 O ATOM 2651 CG2 THR A 373 22.144 9.988 28.309 1.00 39.74 C ANISOU 2651 CG2 THR A 373 5920 4849 4332 579 151 304 C ATOM 2652 N ASP A 374 25.540 8.668 29.906 1.00 41.40 N ANISOU 2652 N ASP A 374 6094 5064 4574 209 -263 268 N ATOM 2653 CA ASP A 374 26.232 7.412 29.654 1.00 42.30 C ANISOU 2653 CA ASP A 374 6011 5252 4808 164 -358 320 C ATOM 2654 C ASP A 374 25.257 6.239 29.709 1.00 44.22 C ANISOU 2654 C ASP A 374 6161 5563 5079 253 -298 392 C ATOM 2655 O ASP A 374 25.293 5.409 30.613 1.00 47.57 O ANISOU 2655 O ASP A 374 6588 6026 5462 245 -350 438 O ATOM 2656 CB ASP A 374 27.385 7.223 30.646 1.00 44.25 C ANISOU 2656 CB ASP A 374 6291 5516 5005 54 -512 321 C ATOM 2657 CG ASP A 374 26.955 7.404 32.090 1.00 47.49 C ANISOU 2657 CG ASP A 374 6891 5916 5237 62 -516 316 C ATOM 2658 OD1 ASP A 374 25.917 8.057 32.332 1.00 48.17 O ANISOU 2658 OD1 ASP A 374 7121 5960 5221 145 -392 288 O ATOM 2659 OD2 ASP A 374 27.669 6.905 32.987 1.00 50.60 O ANISOU 2659 OD2 ASP A 374 7290 6350 5584 -7 -641 344 O ATOM 2660 N VAL A 375 24.376 6.187 28.721 1.00 43.86 N ANISOU 2660 N VAL A 375 6036 5533 5098 325 -192 408 N ATOM 2661 CA VAL A 375 23.419 5.104 28.599 1.00 42.26 C ANISOU 2661 CA VAL A 375 5734 5397 4926 379 -138 480 C ATOM 2662 C VAL A 375 24.020 4.020 27.699 1.00 39.68 C ANISOU 2662 C VAL A 375 5246 5082 4746 340 -200 504 C ATOM 2663 O VAL A 375 24.872 4.310 26.852 1.00 39.22 O ANISOU 2663 O VAL A 375 5131 4997 4773 306 -237 465 O ATOM 2664 CB VAL A 375 22.071 5.627 28.042 1.00 43.03 C ANISOU 2664 CB VAL A 375 5827 5525 4998 473 4 496 C ATOM 2665 CG1 VAL A 375 22.158 5.890 26.535 1.00 38.34 C ANISOU 2665 CG1 VAL A 375 5132 4917 4518 474 28 477 C ATOM 2666 CG2 VAL A 375 20.950 4.671 28.365 1.00 46.50 C ANISOU 2666 CG2 VAL A 375 6200 6055 5413 509 61 581 C ATOM 2667 N SER A 376 23.604 2.773 27.896 1.00 37.87 N ANISOU 2667 N SER A 376 4959 4889 4540 345 -209 570 N ATOM 2668 CA SER A 376 24.172 1.652 27.150 1.00 34.99 C ANISOU 2668 CA SER A 376 4482 4513 4298 322 -265 591 C ATOM 2669 C SER A 376 23.400 1.361 25.860 1.00 34.30 C ANISOU 2669 C SER A 376 4309 4440 4282 336 -190 598 C ATOM 2670 O SER A 376 22.177 1.493 25.811 1.00 34.04 O ANISOU 2670 O SER A 376 4278 4455 4200 358 -107 631 O ATOM 2671 CB SER A 376 24.205 0.393 28.020 1.00 35.38 C ANISOU 2671 CB SER A 376 4544 4567 4332 311 -324 660 C ATOM 2672 OG SER A 376 25.093 0.542 29.115 1.00 37.79 O ANISOU 2672 OG SER A 376 4913 4867 4580 291 -417 660 O ATOM 2673 N SER A 377 24.124 0.962 24.819 1.00 33.16 N ANISOU 2673 N SER A 377 4087 4266 4246 325 -219 573 N ATOM 2674 CA SER A 377 23.498 0.559 23.562 1.00 34.31 C ANISOU 2674 CA SER A 377 4167 4420 4451 323 -165 576 C ATOM 2675 C SER A 377 24.504 -0.147 22.673 1.00 34.66 C ANISOU 2675 C SER A 377 4152 4420 4599 319 -207 549 C ATOM 2676 O SER A 377 25.698 -0.211 22.988 1.00 34.06 O ANISOU 2676 O SER A 377 4062 4323 4558 329 -272 534 O ATOM 2677 CB SER A 377 22.908 1.764 22.815 1.00 33.57 C ANISOU 2677 CB SER A 377 4064 4356 4337 344 -86 547 C ATOM 2678 OG SER A 377 23.932 2.629 22.351 1.00 34.68 O ANISOU 2678 OG SER A 377 4202 4463 4514 339 -104 487 O ATOM 2679 N SER A 378 24.011 -0.676 21.559 1.00 35.78 N ANISOU 2679 N SER A 378 4258 4556 4782 308 -169 547 N ATOM 2680 CA SER A 378 24.864 -1.309 20.566 1.00 33.82 C ANISOU 2680 CA SER A 378 3969 4261 4619 320 -183 513 C ATOM 2681 C SER A 378 24.549 -0.781 19.166 1.00 33.65 C ANISOU 2681 C SER A 378 3909 4260 4617 309 -121 474 C ATOM 2682 O SER A 378 23.415 -0.401 18.869 1.00 31.25 O ANISOU 2682 O SER A 378 3605 4001 4267 285 -76 493 O ATOM 2683 CB SER A 378 24.703 -2.829 20.611 1.00 33.63 C ANISOU 2683 CB SER A 378 3985 4177 4615 314 -211 547 C ATOM 2684 OG SER A 378 25.501 -3.460 19.622 1.00 34.31 O ANISOU 2684 OG SER A 378 4055 4207 4773 348 -210 508 O ATOM 2685 N VAL A 379 25.568 -0.746 18.316 1.00 33.28 N ANISOU 2685 N VAL A 379 3820 4193 4633 331 -119 428 N ATOM 2686 CA VAL A 379 25.380 -0.452 16.907 1.00 30.09 C ANISOU 2686 CA VAL A 379 3388 3801 4243 319 -63 392 C ATOM 2687 C VAL A 379 25.785 -1.689 16.107 1.00 31.17 C ANISOU 2687 C VAL A 379 3536 3881 4425 336 -61 369 C ATOM 2688 O VAL A 379 26.942 -2.106 16.139 1.00 32.41 O ANISOU 2688 O VAL A 379 3670 4010 4636 392 -78 353 O ATOM 2689 CB VAL A 379 26.201 0.778 16.459 1.00 29.04 C ANISOU 2689 CB VAL A 379 3209 3696 4130 325 -41 356 C ATOM 2690 CG1 VAL A 379 26.158 0.937 14.937 1.00 27.96 C ANISOU 2690 CG1 VAL A 379 3046 3569 4006 317 16 323 C ATOM 2691 CG2 VAL A 379 25.692 2.042 17.147 1.00 26.23 C ANISOU 2691 CG2 VAL A 379 2885 3366 3714 311 -33 370 C ATOM 2692 N ILE A 380 24.829 -2.290 15.410 1.00 30.73 N ANISOU 2692 N ILE A 380 3523 3813 4341 291 -41 373 N ATOM 2693 CA ILE A 380 25.138 -3.415 14.547 1.00 32.23 C ANISOU 2693 CA ILE A 380 3764 3929 4553 300 -32 338 C ATOM 2694 C ILE A 380 25.727 -2.897 13.236 1.00 33.93 C ANISOU 2694 C ILE A 380 3941 4166 4785 323 24 281 C ATOM 2695 O ILE A 380 25.108 -2.122 12.521 1.00 35.78 O ANISOU 2695 O ILE A 380 4153 4458 4983 278 54 277 O ATOM 2696 CB ILE A 380 23.894 -4.288 14.270 1.00 31.73 C ANISOU 2696 CB ILE A 380 3780 3838 4436 210 -44 362 C ATOM 2697 CG1 ILE A 380 23.281 -4.782 15.592 1.00 31.56 C ANISOU 2697 CG1 ILE A 380 3792 3808 4391 176 -91 432 C ATOM 2698 CG2 ILE A 380 24.263 -5.456 13.365 1.00 30.88 C ANISOU 2698 CG2 ILE A 380 3770 3625 4337 216 -34 313 C ATOM 2699 CD1 ILE A 380 24.246 -5.576 16.459 1.00 31.28 C ANISOU 2699 CD1 ILE A 380 3802 3684 4399 249 -130 440 C ATOM 2700 N THR A 381 26.943 -3.328 12.940 1.00 34.16 N ANISOU 2700 N THR A 381 3957 4155 4866 403 41 246 N ATOM 2701 CA THR A 381 27.659 -2.876 11.760 1.00 33.35 C ANISOU 2701 CA THR A 381 3809 4084 4778 433 105 198 C ATOM 2702 C THR A 381 27.477 -3.842 10.590 1.00 34.19 C ANISOU 2702 C THR A 381 4012 4124 4856 436 147 148 C ATOM 2703 O THR A 381 26.678 -4.779 10.659 1.00 33.42 O ANISOU 2703 O THR A 381 4023 3953 4721 390 118 152 O ATOM 2704 CB THR A 381 29.156 -2.726 12.064 1.00 32.40 C ANISOU 2704 CB THR A 381 3594 3990 4725 523 111 197 C ATOM 2705 OG1 THR A 381 29.716 -4.020 12.322 1.00 34.81 O ANISOU 2705 OG1 THR A 381 3945 4217 5063 617 101 196 O ATOM 2706 CG2 THR A 381 29.359 -1.835 13.292 1.00 29.64 C ANISOU 2706 CG2 THR A 381 3176 3696 4388 497 52 242 C ATOM 2707 N SER A 382 28.219 -3.620 9.512 1.00 34.55 N ANISOU 2707 N SER A 382 4029 4192 4906 481 216 102 N ATOM 2708 CA SER A 382 28.168 -4.545 8.389 1.00 34.78 C ANISOU 2708 CA SER A 382 4173 4149 4893 496 265 43 C ATOM 2709 C SER A 382 28.710 -5.925 8.781 1.00 36.07 C ANISOU 2709 C SER A 382 4430 4190 5085 596 261 28 C ATOM 2710 O SER A 382 28.164 -6.945 8.372 1.00 38.03 O ANISOU 2710 O SER A 382 4840 4328 5283 567 259 -4 O ATOM 2711 CB SER A 382 28.948 -3.990 7.198 1.00 35.41 C ANISOU 2711 CB SER A 382 4201 4290 4966 538 355 0 C ATOM 2712 OG SER A 382 28.328 -2.817 6.702 1.00 37.01 O ANISOU 2712 OG SER A 382 4355 4580 5127 443 358 15 O ATOM 2713 N LEU A 383 29.779 -5.956 9.574 1.00 34.96 N ANISOU 2713 N LEU A 383 4197 4066 5019 709 255 59 N ATOM 2714 CA LEU A 383 30.472 -7.212 9.844 1.00 38.18 C ANISOU 2714 CA LEU A 383 4683 4364 5458 844 265 54 C ATOM 2715 C LEU A 383 30.688 -7.491 11.325 1.00 40.13 C ANISOU 2715 C LEU A 383 4895 4596 5757 883 182 126 C ATOM 2716 O LEU A 383 31.490 -8.353 11.681 1.00 44.46 O ANISOU 2716 O LEU A 383 5466 5080 6345 1024 186 143 O ATOM 2717 CB LEU A 383 31.827 -7.229 9.133 1.00 37.41 C ANISOU 2717 CB LEU A 383 4504 4311 5398 999 360 25 C ATOM 2718 CG LEU A 383 31.777 -7.218 7.609 1.00 38.98 C ANISOU 2718 CG LEU A 383 4773 4505 5534 995 460 -52 C ATOM 2719 CD1 LEU A 383 33.180 -7.121 7.027 1.00 40.81 C ANISOU 2719 CD1 LEU A 383 4887 4815 5804 1155 565 -64 C ATOM 2720 CD2 LEU A 383 31.076 -8.467 7.101 1.00 40.68 C ANISOU 2720 CD2 LEU A 383 5236 4543 5676 984 469 -111 C ATOM 2721 N GLY A 384 29.983 -6.774 12.190 1.00 36.87 N ANISOU 2721 N GLY A 384 4432 4243 5334 770 111 173 N ATOM 2722 CA GLY A 384 30.131 -7.001 13.615 1.00 36.82 C ANISOU 2722 CA GLY A 384 4404 4228 5356 793 31 242 C ATOM 2723 C GLY A 384 29.169 -6.180 14.444 1.00 34.98 C ANISOU 2723 C GLY A 384 4144 4057 5088 663 -27 281 C ATOM 2724 O GLY A 384 28.034 -5.919 14.027 1.00 33.04 O ANISOU 2724 O GLY A 384 3948 3819 4789 553 -17 269 O ATOM 2725 N ALA A 385 29.629 -5.761 15.619 1.00 33.22 N ANISOU 2725 N ALA A 385 3844 3891 4888 681 -87 333 N ATOM 2726 CA ALA A 385 28.793 -4.980 16.520 1.00 33.92 C ANISOU 2726 CA ALA A 385 3923 4033 4932 581 -132 369 C ATOM 2727 C ALA A 385 29.641 -4.095 17.416 1.00 34.09 C ANISOU 2727 C ALA A 385 3839 4143 4973 597 -180 397 C ATOM 2728 O ALA A 385 30.595 -4.560 18.020 1.00 35.11 O ANISOU 2728 O ALA A 385 3929 4273 5140 675 -226 431 O ATOM 2729 CB ALA A 385 27.912 -5.902 17.366 1.00 33.90 C ANISOU 2729 CB ALA A 385 4034 3955 4890 544 -178 418 C ATOM 2730 N ILE A 386 29.302 -2.813 17.483 1.00 33.00 N ANISOU 2730 N ILE A 386 3662 4075 4802 521 -173 386 N ATOM 2731 CA ILE A 386 29.908 -1.929 18.466 1.00 33.32 C ANISOU 2731 CA ILE A 386 3646 4181 4834 499 -230 410 C ATOM 2732 C ILE A 386 29.053 -1.985 19.724 1.00 33.83 C ANISOU 2732 C ILE A 386 3792 4230 4833 461 -278 451 C ATOM 2733 O ILE A 386 27.823 -1.929 19.641 1.00 33.32 O ANISOU 2733 O ILE A 386 3792 4149 4719 417 -242 452 O ATOM 2734 CB ILE A 386 29.992 -0.467 17.979 1.00 32.86 C ANISOU 2734 CB ILE A 386 3542 4182 4760 434 -197 377 C ATOM 2735 CG1 ILE A 386 30.742 -0.365 16.650 1.00 32.58 C ANISOU 2735 CG1 ILE A 386 3427 4175 4778 459 -136 342 C ATOM 2736 CG2 ILE A 386 30.638 0.417 19.048 1.00 32.69 C ANISOU 2736 CG2 ILE A 386 3494 4211 4715 388 -268 397 C ATOM 2737 CD1 ILE A 386 30.807 1.061 16.106 1.00 31.19 C ANISOU 2737 CD1 ILE A 386 3223 4046 4583 384 -101 318 C ATOM 2738 N VAL A 387 29.687 -2.091 20.884 1.00 33.40 N ANISOU 2738 N VAL A 387 3727 4193 4769 475 -358 492 N ATOM 2739 CA VAL A 387 28.940 -2.128 22.134 1.00 33.76 C ANISOU 2739 CA VAL A 387 3858 4231 4739 441 -398 533 C ATOM 2740 C VAL A 387 29.393 -1.020 23.078 1.00 35.01 C ANISOU 2740 C VAL A 387 4012 4447 4843 393 -454 533 C ATOM 2741 O VAL A 387 30.550 -0.992 23.505 1.00 37.85 O ANISOU 2741 O VAL A 387 4308 4847 5226 403 -529 552 O ATOM 2742 CB VAL A 387 29.080 -3.502 22.835 1.00 33.37 C ANISOU 2742 CB VAL A 387 3854 4128 4698 494 -453 593 C ATOM 2743 CG1 VAL A 387 28.548 -3.434 24.266 1.00 33.58 C ANISOU 2743 CG1 VAL A 387 3958 4168 4635 455 -503 644 C ATOM 2744 CG2 VAL A 387 28.352 -4.579 22.035 1.00 31.77 C ANISOU 2744 CG2 VAL A 387 3713 3841 4518 509 -399 591 C ATOM 2745 N SER A 388 28.480 -0.094 23.371 1.00 34.76 N ANISOU 2745 N SER A 388 4051 4423 4733 343 -416 514 N ATOM 2746 CA SER A 388 28.710 0.936 24.379 1.00 34.32 C ANISOU 2746 CA SER A 388 4048 4394 4597 292 -462 507 C ATOM 2747 C SER A 388 28.066 0.492 25.682 1.00 34.62 C ANISOU 2747 C SER A 388 4182 4427 4547 296 -491 554 C ATOM 2748 O SER A 388 26.842 0.583 25.846 1.00 33.12 O ANISOU 2748 O SER A 388 4059 4231 4295 300 -422 562 O ATOM 2749 CB SER A 388 28.142 2.288 23.940 1.00 33.05 C ANISOU 2749 CB SER A 388 3938 4228 4392 257 -391 456 C ATOM 2750 OG SER A 388 28.791 2.760 22.774 1.00 32.55 O ANISOU 2750 OG SER A 388 3795 4173 4400 241 -366 420 O ATOM 2751 N CYS A 389 28.889 -0.005 26.600 1.00 34.72 N ANISOU 2751 N CYS A 389 4189 4456 4548 297 -593 595 N ATOM 2752 CA CYS A 389 28.376 -0.601 27.825 1.00 34.03 C ANISOU 2752 CA CYS A 389 4192 4364 4376 301 -627 652 C ATOM 2753 C CYS A 389 28.783 0.248 29.023 1.00 33.41 C ANISOU 2753 C CYS A 389 4190 4319 4186 246 -700 646 C ATOM 2754 O CYS A 389 29.969 0.418 29.301 1.00 32.60 O ANISOU 2754 O CYS A 389 4036 4253 4098 216 -802 651 O ATOM 2755 CB CYS A 389 28.889 -2.040 27.974 1.00 34.72 C ANISOU 2755 CB CYS A 389 4240 4428 4525 357 -689 720 C ATOM 2756 SG CYS A 389 28.007 -3.055 29.197 1.00 45.06 S ANISOU 2756 SG CYS A 389 5668 5711 5743 360 -705 807 S ATOM 2757 N TYR A 390 27.799 0.784 29.732 1.00 33.75 N ANISOU 2757 N TYR A 390 4356 4357 4109 231 -647 636 N ATOM 2758 CA TYR A 390 28.088 1.657 30.865 1.00 36.79 C ANISOU 2758 CA TYR A 390 4857 4758 4363 176 -704 615 C ATOM 2759 C TYR A 390 27.192 1.326 32.052 1.00 38.11 C ANISOU 2759 C TYR A 390 5148 4934 4398 192 -681 660 C ATOM 2760 O TYR A 390 26.167 0.661 31.899 1.00 37.76 O ANISOU 2760 O TYR A 390 5096 4890 4362 236 -597 701 O ATOM 2761 CB TYR A 390 27.926 3.130 30.454 1.00 37.81 C ANISOU 2761 CB TYR A 390 5053 4860 4452 142 -644 531 C ATOM 2762 CG TYR A 390 28.784 3.497 29.259 1.00 38.96 C ANISOU 2762 CG TYR A 390 5079 5004 4719 112 -658 495 C ATOM 2763 CD1 TYR A 390 30.172 3.421 29.331 1.00 38.70 C ANISOU 2763 CD1 TYR A 390 4958 5014 4733 51 -781 508 C ATOM 2764 CD2 TYR A 390 28.209 3.901 28.059 1.00 36.45 C ANISOU 2764 CD2 TYR A 390 4726 4659 4465 145 -550 460 C ATOM 2765 CE1 TYR A 390 30.961 3.737 28.245 1.00 38.52 C ANISOU 2765 CE1 TYR A 390 4811 5008 4816 23 -784 486 C ATOM 2766 CE2 TYR A 390 28.996 4.228 26.969 1.00 36.24 C ANISOU 2766 CE2 TYR A 390 4595 4636 4538 114 -556 432 C ATOM 2767 CZ TYR A 390 30.370 4.141 27.069 1.00 37.12 C ANISOU 2767 CZ TYR A 390 4617 4792 4694 53 -668 445 C ATOM 2768 OH TYR A 390 31.166 4.453 25.992 1.00 37.10 O ANISOU 2768 OH TYR A 390 4498 4812 4786 21 -664 427 O ATOM 2769 N GLY A 391 27.594 1.778 33.235 1.00 39.13 N ANISOU 2769 N GLY A 391 5391 5080 4398 143 -758 656 N ATOM 2770 CA GLY A 391 26.806 1.555 34.430 1.00 39.59 C ANISOU 2770 CA GLY A 391 5581 5154 4308 157 -731 696 C ATOM 2771 C GLY A 391 26.651 0.088 34.765 1.00 39.18 C ANISOU 2771 C GLY A 391 5480 5119 4288 186 -764 799 C ATOM 2772 O GLY A 391 27.605 -0.682 34.692 1.00 39.53 O ANISOU 2772 O GLY A 391 5439 5165 4415 185 -874 845 O ATOM 2773 N LYS A 392 25.430 -0.300 35.111 1.00 38.13 N ANISOU 2773 N LYS A 392 5400 4998 4089 216 -662 844 N ATOM 2774 CA LYS A 392 25.147 -1.655 35.562 1.00 37.98 C ANISOU 2774 CA LYS A 392 5373 4984 4073 223 -685 950 C ATOM 2775 C LYS A 392 24.599 -2.556 34.453 1.00 38.68 C ANISOU 2775 C LYS A 392 5355 5042 4300 244 -623 984 C ATOM 2776 O LYS A 392 24.042 -3.613 34.726 1.00 42.58 O ANISOU 2776 O LYS A 392 5864 5528 4785 235 -610 1070 O ATOM 2777 CB LYS A 392 24.155 -1.614 36.723 1.00 38.48 C ANISOU 2777 CB LYS A 392 5565 5094 3961 219 -616 996 C ATOM 2778 CG LYS A 392 24.610 -0.773 37.900 1.00 41.51 C ANISOU 2778 CG LYS A 392 6096 5501 4177 193 -674 959 C ATOM 2779 CD LYS A 392 23.582 -0.833 39.025 1.00 45.86 C ANISOU 2779 CD LYS A 392 6777 6104 4546 203 -586 1010 C ATOM 2780 CE LYS A 392 24.079 -0.129 40.281 1.00 49.13 C ANISOU 2780 CE LYS A 392 7367 6533 4769 169 -655 975 C ATOM 2781 NZ LYS A 392 25.263 -0.823 40.886 1.00 50.96 N ANISOU 2781 NZ LYS A 392 7597 6765 5001 115 -847 1033 N ATOM 2782 N THR A 393 24.766 -2.148 33.202 1.00 36.79 N ANISOU 2782 N THR A 393 5020 4780 4178 259 -588 917 N ATOM 2783 CA THR A 393 24.196 -2.901 32.094 1.00 35.24 C ANISOU 2783 CA THR A 393 4742 4556 4094 267 -528 936 C ATOM 2784 C THR A 393 24.916 -4.225 31.842 1.00 34.81 C ANISOU 2784 C THR A 393 4654 4433 4138 280 -613 988 C ATOM 2785 O THR A 393 26.147 -4.287 31.844 1.00 32.14 O ANISOU 2785 O THR A 393 4280 4077 3853 310 -708 977 O ATOM 2786 CB THR A 393 24.217 -2.079 30.802 1.00 34.05 C ANISOU 2786 CB THR A 393 4509 4400 4029 281 -470 850 C ATOM 2787 OG1 THR A 393 23.653 -0.789 31.063 1.00 33.59 O ANISOU 2787 OG1 THR A 393 4503 4384 3876 290 -395 802 O ATOM 2788 CG2 THR A 393 23.409 -2.776 29.708 1.00 32.71 C ANISOU 2788 CG2 THR A 393 4273 4215 3940 273 -401 870 C ATOM 2789 N LYS A 394 24.136 -5.282 31.632 1.00 35.34 N ANISOU 2789 N LYS A 394 4737 4465 4224 258 -576 1052 N ATOM 2790 CA LYS A 394 24.687 -6.548 31.168 1.00 37.34 C ANISOU 2790 CA LYS A 394 4988 4622 4577 281 -633 1091 C ATOM 2791 C LYS A 394 24.870 -6.486 29.651 1.00 35.62 C ANISOU 2791 C LYS A 394 4687 4366 4482 302 -592 1017 C ATOM 2792 O LYS A 394 23.916 -6.268 28.903 1.00 36.46 O ANISOU 2792 O LYS A 394 4767 4492 4593 257 -507 993 O ATOM 2793 CB LYS A 394 23.780 -7.729 31.559 1.00 38.85 C ANISOU 2793 CB LYS A 394 5265 4771 4728 224 -615 1190 C ATOM 2794 CG LYS A 394 24.319 -9.108 31.119 1.00 42.61 C ANISOU 2794 CG LYS A 394 5785 5110 5293 254 -671 1232 C ATOM 2795 CD LYS A 394 23.433 -10.263 31.610 1.00 46.30 C ANISOU 2795 CD LYS A 394 6367 5519 5706 173 -664 1339 C ATOM 2796 CE LYS A 394 23.955 -11.642 31.188 1.00 49.16 C ANISOU 2796 CE LYS A 394 6820 5712 6148 209 -716 1378 C ATOM 2797 NZ LYS A 394 24.934 -12.262 32.159 1.00 54.33 N ANISOU 2797 NZ LYS A 394 7545 6310 6788 299 -819 1456 N ATOM 2798 N CYS A 395 26.102 -6.665 29.201 1.00 34.81 N ANISOU 2798 N CYS A 395 4534 4223 4470 372 -652 989 N ATOM 2799 CA CYS A 395 26.398 -6.640 27.777 1.00 32.57 C ANISOU 2799 CA CYS A 395 4177 3904 4292 402 -610 920 C ATOM 2800 C CYS A 395 27.169 -7.894 27.397 1.00 34.66 C ANISOU 2800 C CYS A 395 4465 4064 4642 481 -652 949 C ATOM 2801 O CYS A 395 28.246 -8.161 27.946 1.00 32.96 O ANISOU 2801 O CYS A 395 4229 3847 4446 560 -733 986 O ATOM 2802 CB CYS A 395 27.208 -5.395 27.407 1.00 31.26 C ANISOU 2802 CB CYS A 395 3912 3809 4156 423 -614 845 C ATOM 2803 SG CYS A 395 26.537 -3.828 28.011 1.00 42.40 S ANISOU 2803 SG CYS A 395 5340 5314 5456 358 -574 807 S ATOM 2804 N THR A 396 26.616 -8.669 26.467 1.00 35.37 N ANISOU 2804 N THR A 396 4604 4065 4771 463 -600 936 N ATOM 2805 CA THR A 396 27.244 -9.918 26.055 1.00 36.84 C ANISOU 2805 CA THR A 396 4854 4119 5024 549 -623 957 C ATOM 2806 C THR A 396 27.140 -10.139 24.546 1.00 37.60 C ANISOU 2806 C THR A 396 4950 4152 5183 555 -552 879 C ATOM 2807 O THR A 396 26.376 -9.460 23.851 1.00 36.25 O ANISOU 2807 O THR A 396 4739 4039 4998 470 -492 825 O ATOM 2808 CB THR A 396 26.618 -11.137 26.779 1.00 36.71 C ANISOU 2808 CB THR A 396 4995 3997 4958 506 -652 1051 C ATOM 2809 OG1 THR A 396 25.224 -11.219 26.464 1.00 38.01 O ANISOU 2809 OG1 THR A 396 5211 4160 5071 361 -594 1051 O ATOM 2810 CG2 THR A 396 26.787 -11.034 28.294 1.00 34.79 C ANISOU 2810 CG2 THR A 396 4768 3810 4640 508 -726 1137 C ATOM 2811 N ALA A 397 27.923 -11.091 24.050 1.00 38.13 N ANISOU 2811 N ALA A 397 5070 4103 5314 668 -558 876 N ATOM 2812 CA ALA A 397 27.803 -11.557 22.679 1.00 39.52 C ANISOU 2812 CA ALA A 397 5300 4187 5529 677 -491 806 C ATOM 2813 C ALA A 397 27.656 -13.073 22.708 1.00 43.61 C ANISOU 2813 C ALA A 397 6018 4510 6041 701 -505 849 C ATOM 2814 O ALA A 397 28.363 -13.759 23.448 1.00 42.43 O ANISOU 2814 O ALA A 397 5920 4293 5907 815 -558 917 O ATOM 2815 CB ALA A 397 29.006 -11.143 21.855 1.00 39.95 C ANISOU 2815 CB ALA A 397 5236 4284 5661 812 -459 743 C ATOM 2816 N SER A 398 26.733 -13.601 21.912 1.00 46.05 N ANISOU 2816 N SER A 398 6450 4725 6321 588 -465 814 N ATOM 2817 CA SER A 398 26.457 -15.026 21.958 1.00 48.32 C ANISOU 2817 CA SER A 398 6966 4807 6586 571 -483 855 C ATOM 2818 C SER A 398 26.527 -15.703 20.606 1.00 51.16 C ANISOU 2818 C SER A 398 7460 5018 6960 593 -427 769 C ATOM 2819 O SER A 398 26.365 -15.081 19.557 1.00 49.65 O ANISOU 2819 O SER A 398 7194 4896 6774 556 -373 682 O ATOM 2820 CB SER A 398 25.079 -15.287 22.568 1.00 47.79 C ANISOU 2820 CB SER A 398 6980 4742 6435 358 -510 925 C ATOM 2821 OG SER A 398 25.060 -14.951 23.940 1.00 48.49 O ANISOU 2821 OG SER A 398 7003 4927 6492 356 -559 1016 O ATOM 2822 N ASN A 399 26.778 -17.001 20.665 1.00 56.52 N ANISOU 2822 N ASN A 399 8359 5479 7636 659 -440 797 N ATOM 2823 CA ASN A 399 26.658 -17.889 19.527 1.00 62.05 C ANISOU 2823 CA ASN A 399 9271 5985 8320 652 -394 722 C ATOM 2824 C ASN A 399 25.377 -18.700 19.709 1.00 65.80 C ANISOU 2824 C ASN A 399 9954 6338 8711 412 -435 768 C ATOM 2825 O ASN A 399 24.965 -18.957 20.843 1.00 65.36 O ANISOU 2825 O ASN A 399 9924 6284 8626 337 -493 876 O ATOM 2826 CB ASN A 399 27.887 -18.792 19.432 1.00 65.25 C ANISOU 2826 CB ASN A 399 9803 6215 8774 913 -372 720 C ATOM 2827 CG ASN A 399 27.797 -19.774 18.300 1.00 69.06 C ANISOU 2827 CG ASN A 399 10553 6464 9224 923 -316 636 C ATOM 2828 OD1 ASN A 399 27.134 -20.806 18.411 1.00 71.16 O ANISOU 2828 OD1 ASN A 399 11084 6523 9428 804 -346 663 O ATOM 2829 ND2 ASN A 399 28.475 -19.471 17.200 1.00 70.11 N ANISOU 2829 ND2 ASN A 399 10631 6622 9387 1057 -231 533 N ATOM 2830 N LYS A 400 24.735 -19.094 18.614 1.00 69.77 N ANISOU 2830 N LYS A 400 10603 6744 9164 275 -408 693 N ATOM 2831 CA LYS A 400 23.464 -19.810 18.721 1.00 74.67 C ANISOU 2831 CA LYS A 400 11402 7273 9697 5 -456 743 C ATOM 2832 C LYS A 400 23.630 -21.202 19.346 1.00 78.57 C ANISOU 2832 C LYS A 400 12187 7498 10169 30 -495 814 C ATOM 2833 O LYS A 400 22.716 -21.705 19.995 1.00 80.17 O ANISOU 2833 O LYS A 400 12489 7662 10309 -178 -550 907 O ATOM 2834 CB LYS A 400 22.789 -19.923 17.346 1.00 76.40 C ANISOU 2834 CB LYS A 400 11719 7453 9857 -160 -432 645 C ATOM 2835 CG LYS A 400 23.502 -20.834 16.357 1.00 79.84 C ANISOU 2835 CG LYS A 400 12417 7632 10285 -32 -386 543 C ATOM 2836 CD LYS A 400 22.738 -20.945 15.040 1.00 81.30 C ANISOU 2836 CD LYS A 400 12718 7786 10387 -232 -377 448 C ATOM 2837 CE LYS A 400 23.013 -19.764 14.116 1.00 80.49 C ANISOU 2837 CE LYS A 400 12382 7889 10312 -161 -316 358 C ATOM 2838 NZ LYS A 400 24.420 -19.751 13.616 1.00 81.88 N ANISOU 2838 NZ LYS A 400 12564 7995 10550 146 -228 274 N ATOM 2839 N ASN A 401 24.802 -21.809 19.173 1.00 80.70 N ANISOU 2839 N ASN A 401 12586 7591 10487 290 -462 780 N ATOM 2840 CA ASN A 401 25.032 -23.177 19.630 1.00 84.72 C ANISOU 2840 CA ASN A 401 13408 7808 10973 348 -490 841 C ATOM 2841 C ASN A 401 25.653 -23.286 21.019 1.00 84.80 C ANISOU 2841 C ASN A 401 13356 7840 11026 506 -537 970 C ATOM 2842 O ASN A 401 25.857 -24.391 21.517 1.00 86.40 O ANISOU 2842 O ASN A 401 13812 7806 11209 567 -566 1042 O ATOM 2843 CB ASN A 401 25.932 -23.925 18.637 1.00 88.82 C ANISOU 2843 CB ASN A 401 14150 8090 11508 568 -420 739 C ATOM 2844 CG ASN A 401 25.317 -24.040 17.252 1.00 90.98 C ANISOU 2844 CG ASN A 401 14564 8291 11712 402 -381 609 C ATOM 2845 OD1 ASN A 401 24.114 -24.255 17.106 1.00 91.88 O ANISOU 2845 OD1 ASN A 401 14780 8386 11744 88 -431 621 O ATOM 2846 ND2 ASN A 401 26.147 -23.900 16.224 1.00 91.39 N ANISOU 2846 ND2 ASN A 401 14616 8316 11791 606 -291 491 N ATOM 2847 N ARG A 402 25.960 -22.155 21.646 1.00 83.29 N ANISOU 2847 N ARG A 402 12845 7919 10881 569 -549 1002 N ATOM 2848 CA ARG A 402 26.737 -22.187 22.885 1.00 82.81 C ANISOU 2848 CA ARG A 402 12711 7896 10856 746 -598 1115 C ATOM 2849 C ARG A 402 26.352 -21.140 23.925 1.00 76.04 C ANISOU 2849 C ARG A 402 11599 7307 9984 643 -644 1186 C ATOM 2850 O ARG A 402 26.736 -21.253 25.091 1.00 76.40 O ANISOU 2850 O ARG A 402 11621 7379 10027 722 -703 1295 O ATOM 2851 CB ARG A 402 28.224 -22.036 22.563 1.00 86.81 C ANISOU 2851 CB ARG A 402 13115 8418 11453 1076 -558 1075 C ATOM 2852 CG ARG A 402 28.918 -23.345 22.242 1.00 92.69 C ANISOU 2852 CG ARG A 402 14143 8866 12210 1286 -531 1079 C ATOM 2853 CD ARG A 402 30.318 -23.091 21.732 1.00 96.48 C ANISOU 2853 CD ARG A 402 14477 9405 12776 1609 -468 1032 C ATOM 2854 NE ARG A 402 30.306 -22.287 20.517 1.00 98.53 N ANISOU 2854 NE ARG A 402 14596 9788 13052 1574 -387 892 N ATOM 2855 CZ ARG A 402 30.037 -22.771 19.309 1.00101.82 C ANISOU 2855 CZ ARG A 402 15215 10038 13434 1544 -311 779 C ATOM 2856 NH1 ARG A 402 29.750 -24.058 19.151 1.00104.92 N ANISOU 2856 NH1 ARG A 402 15975 10119 13772 1537 -307 781 N ATOM 2857 NH2 ARG A 402 30.051 -21.964 18.259 1.00101.50 N ANISOU 2857 NH2 ARG A 402 15029 10134 13402 1513 -243 664 N ATOM 2858 N GLY A 403 25.607 -20.123 23.511 1.00 69.58 N ANISOU 2858 N GLY A 403 10603 6686 9149 478 -617 1126 N ATOM 2859 CA GLY A 403 25.256 -19.050 24.418 1.00 63.77 C ANISOU 2859 CA GLY A 403 9640 6197 8391 403 -643 1177 C ATOM 2860 C GLY A 403 26.399 -18.060 24.544 1.00 61.22 C ANISOU 2860 C GLY A 403 9085 6037 8138 604 -640 1142 C ATOM 2861 O GLY A 403 27.175 -17.878 23.603 1.00 61.76 O ANISOU 2861 O GLY A 403 9101 6095 8272 743 -594 1054 O ATOM 2862 N ILE A 404 26.511 -17.435 25.713 1.00 57.12 N ANISOU 2862 N ILE A 404 8437 5670 7596 608 -689 1216 N ATOM 2863 CA ILE A 404 27.440 -16.328 25.924 1.00 53.07 C ANISOU 2863 CA ILE A 404 7694 5341 7128 736 -700 1187 C ATOM 2864 C ILE A 404 28.897 -16.731 25.743 1.00 51.69 C ANISOU 2864 C ILE A 404 7500 5106 7033 985 -716 1189 C ATOM 2865 O ILE A 404 29.386 -17.635 26.414 1.00 52.52 O ANISOU 2865 O ILE A 404 7719 5098 7138 1097 -768 1281 O ATOM 2866 CB ILE A 404 27.266 -15.725 27.327 1.00 52.39 C ANISOU 2866 CB ILE A 404 7526 5402 6977 682 -761 1271 C ATOM 2867 CG1 ILE A 404 25.889 -15.069 27.451 1.00 52.08 C ANISOU 2867 CG1 ILE A 404 7452 5474 6861 469 -722 1262 C ATOM 2868 CG2 ILE A 404 28.370 -14.710 27.618 1.00 51.00 C ANISOU 2868 CG2 ILE A 404 7147 5391 6840 807 -794 1250 C ATOM 2869 CD1 ILE A 404 25.483 -14.745 28.890 1.00 52.35 C ANISOU 2869 CD1 ILE A 404 7473 5615 6802 401 -765 1356 C ATOM 2870 N ILE A 405 29.592 -16.056 24.835 1.00 50.53 N ANISOU 2870 N ILE A 405 7201 5044 6952 1078 -666 1098 N ATOM 2871 CA ILE A 405 31.001 -16.351 24.619 1.00 53.10 C ANISOU 2871 CA ILE A 405 7464 5355 7355 1323 -669 1107 C ATOM 2872 C ILE A 405 31.880 -15.156 24.958 1.00 51.95 C ANISOU 2872 C ILE A 405 7051 5444 7242 1376 -704 1108 C ATOM 2873 O ILE A 405 33.088 -15.298 25.145 1.00 55.48 O ANISOU 2873 O ILE A 405 7398 5938 7744 1564 -736 1156 O ATOM 2874 CB ILE A 405 31.280 -16.791 23.173 1.00 54.37 C ANISOU 2874 CB ILE A 405 7693 5400 7565 1419 -570 1009 C ATOM 2875 CG1 ILE A 405 30.913 -15.684 22.192 1.00 51.89 C ANISOU 2875 CG1 ILE A 405 7241 5219 7257 1304 -503 895 C ATOM 2876 CG2 ILE A 405 30.539 -18.087 22.859 1.00 56.28 C ANISOU 2876 CG2 ILE A 405 8239 5380 7766 1369 -548 1009 C ATOM 2877 CD1 ILE A 405 31.247 -16.023 20.769 1.00 53.58 C ANISOU 2877 CD1 ILE A 405 7512 5342 7505 1398 -404 796 C ATOM 2878 N LYS A 406 31.277 -13.980 25.048 1.00 46.88 N ANISOU 2878 N LYS A 406 6297 4951 6565 1210 -700 1063 N ATOM 2879 CA LYS A 406 32.011 -12.815 25.509 1.00 46.61 C ANISOU 2879 CA LYS A 406 6049 5121 6540 1219 -748 1067 C ATOM 2880 C LYS A 406 31.127 -11.940 26.388 1.00 44.86 C ANISOU 2880 C LYS A 406 5816 5000 6230 1038 -783 1077 C ATOM 2881 O LYS A 406 29.979 -11.655 26.043 1.00 44.14 O ANISOU 2881 O LYS A 406 5782 4893 6098 898 -726 1029 O ATOM 2882 CB LYS A 406 32.550 -12.006 24.328 1.00 48.26 C ANISOU 2882 CB LYS A 406 6102 5422 6812 1250 -676 971 C ATOM 2883 CG LYS A 406 33.398 -10.800 24.726 1.00 50.79 C ANISOU 2883 CG LYS A 406 6208 5947 7144 1241 -728 977 C ATOM 2884 CD LYS A 406 33.807 -9.994 23.493 1.00 53.85 C ANISOU 2884 CD LYS A 406 6458 6415 7585 1243 -647 886 C ATOM 2885 CE LYS A 406 34.555 -8.707 23.855 1.00 54.52 C ANISOU 2885 CE LYS A 406 6348 6695 7671 1188 -701 890 C ATOM 2886 NZ LYS A 406 35.725 -8.945 24.752 1.00 56.25 N ANISOU 2886 NZ LYS A 406 6457 7007 7909 1291 -808 992 N ATOM 2887 N THR A 407 31.663 -11.526 27.531 1.00 42.76 N ANISOU 2887 N THR A 407 5479 4842 5927 1047 -877 1144 N ATOM 2888 CA THR A 407 30.991 -10.547 28.364 1.00 40.01 C ANISOU 2888 CA THR A 407 5119 4600 5485 897 -903 1141 C ATOM 2889 C THR A 407 31.765 -9.249 28.286 1.00 40.31 C ANISOU 2889 C THR A 407 4984 4796 5536 883 -927 1091 C ATOM 2890 O THR A 407 32.966 -9.217 28.536 1.00 41.85 O ANISOU 2890 O THR A 407 5068 5065 5768 973 -1001 1132 O ATOM 2891 CB THR A 407 30.868 -11.007 29.820 1.00 37.97 C ANISOU 2891 CB THR A 407 4953 4336 5137 882 -994 1251 C ATOM 2892 OG1 THR A 407 30.094 -12.209 29.868 1.00 37.62 O ANISOU 2892 OG1 THR A 407 5083 4135 5076 871 -968 1303 O ATOM 2893 CG2 THR A 407 30.171 -9.949 30.651 1.00 35.81 C ANISOU 2893 CG2 THR A 407 4681 4174 4753 741 -1002 1236 C ATOM 2894 N PHE A 408 31.080 -8.183 27.896 1.00 39.46 N ANISOU 2894 N PHE A 408 4852 4742 5398 769 -865 1009 N ATOM 2895 CA PHE A 408 31.719 -6.885 27.774 1.00 40.29 C ANISOU 2895 CA PHE A 408 4826 4974 5507 729 -882 957 C ATOM 2896 C PHE A 408 31.851 -6.226 29.138 1.00 42.75 C ANISOU 2896 C PHE A 408 5156 5373 5716 658 -977 995 C ATOM 2897 O PHE A 408 30.964 -6.352 29.989 1.00 44.63 O ANISOU 2897 O PHE A 408 5515 5585 5857 601 -979 1026 O ATOM 2898 CB PHE A 408 30.923 -5.979 26.838 1.00 38.36 C ANISOU 2898 CB PHE A 408 4574 4737 5263 645 -778 860 C ATOM 2899 CG PHE A 408 30.866 -6.467 25.421 1.00 40.86 C ANISOU 2899 CG PHE A 408 4872 4987 5668 699 -690 811 C ATOM 2900 CD1 PHE A 408 31.893 -6.181 24.535 1.00 43.29 C ANISOU 2900 CD1 PHE A 408 5050 5341 6056 762 -672 775 C ATOM 2901 CD2 PHE A 408 29.779 -7.204 24.971 1.00 40.23 C ANISOU 2901 CD2 PHE A 408 4904 4805 5578 673 -626 804 C ATOM 2902 CE1 PHE A 408 31.837 -6.623 23.223 1.00 44.66 C ANISOU 2902 CE1 PHE A 408 5223 5452 6292 814 -583 725 C ATOM 2903 CE2 PHE A 408 29.714 -7.646 23.668 1.00 41.82 C ANISOU 2903 CE2 PHE A 408 5111 4940 5840 708 -553 753 C ATOM 2904 CZ PHE A 408 30.745 -7.358 22.789 1.00 44.43 C ANISOU 2904 CZ PHE A 408 5329 5309 6245 786 -527 709 C ATOM 2905 N SER A 409 32.958 -5.528 29.349 1.00 41.52 N ANISOU 2905 N SER A 409 4882 5327 5569 651 -1055 997 N ATOM 2906 CA SER A 409 33.096 -4.694 30.529 1.00 43.93 C ANISOU 2906 CA SER A 409 5218 5715 5758 553 -1146 1011 C ATOM 2907 C SER A 409 32.725 -3.272 30.132 1.00 43.33 C ANISOU 2907 C SER A 409 5147 5671 5647 441 -1088 910 C ATOM 2908 O SER A 409 32.466 -3.001 28.955 1.00 44.63 O ANISOU 2908 O SER A 409 5268 5806 5883 448 -988 846 O ATOM 2909 CB SER A 409 34.512 -4.764 31.091 1.00 47.71 C ANISOU 2909 CB SER A 409 5575 6304 6250 586 -1288 1085 C ATOM 2910 OG SER A 409 35.446 -4.374 30.102 1.00 51.48 O ANISOU 2910 OG SER A 409 5878 6851 6831 610 -1275 1055 O ATOM 2911 N ASN A 410 32.684 -2.367 31.101 1.00 42.13 N ANISOU 2911 N ASN A 410 5067 5567 5373 340 -1147 897 N ATOM 2912 CA ASN A 410 32.281 -0.996 30.822 1.00 41.87 C ANISOU 2912 CA ASN A 410 5082 5537 5289 243 -1088 804 C ATOM 2913 C ASN A 410 33.258 -0.292 29.888 1.00 40.91 C ANISOU 2913 C ASN A 410 4820 5469 5254 208 -1099 763 C ATOM 2914 O ASN A 410 34.466 -0.505 29.956 1.00 41.44 O ANISOU 2914 O ASN A 410 4754 5621 5370 214 -1198 813 O ATOM 2915 CB ASN A 410 32.115 -0.209 32.121 1.00 43.80 C ANISOU 2915 CB ASN A 410 5467 5806 5369 147 -1153 795 C ATOM 2916 CG ASN A 410 30.800 -0.514 32.814 1.00 47.11 C ANISOU 2916 CG ASN A 410 6042 6172 5685 169 -1080 807 C ATOM 2917 OD1 ASN A 410 29.906 -1.118 32.226 1.00 46.76 O ANISOU 2917 OD1 ASN A 410 5997 6076 5694 228 -975 813 O ATOM 2918 ND2 ASN A 410 30.671 -0.088 34.063 1.00 51.65 N ANISOU 2918 ND2 ASN A 410 6752 6769 6104 110 -1135 814 N ATOM 2919 N GLY A 411 32.714 0.536 29.003 1.00 40.35 N ANISOU 2919 N GLY A 411 4772 5360 5201 174 -993 683 N ATOM 2920 CA GLY A 411 33.499 1.182 27.966 1.00 40.09 C ANISOU 2920 CA GLY A 411 4615 5368 5250 138 -978 647 C ATOM 2921 C GLY A 411 32.922 0.870 26.599 1.00 39.39 C ANISOU 2921 C GLY A 411 4486 5225 5256 211 -845 611 C ATOM 2922 O GLY A 411 31.838 0.296 26.497 1.00 39.12 O ANISOU 2922 O GLY A 411 4529 5122 5212 267 -771 609 O ATOM 2923 N CYS A 412 33.631 1.256 25.542 1.00 38.54 N ANISOU 2923 N CYS A 412 4256 5156 5230 198 -816 588 N ATOM 2924 CA CYS A 412 33.173 0.953 24.194 1.00 35.75 C ANISOU 2924 CA CYS A 412 3869 4759 4956 264 -696 553 C ATOM 2925 C CYS A 412 34.027 -0.142 23.588 1.00 36.78 C ANISOU 2925 C CYS A 412 3860 4923 5192 373 -696 593 C ATOM 2926 O CYS A 412 35.250 -0.057 23.573 1.00 38.68 O ANISOU 2926 O CYS A 412 3961 5261 5476 372 -755 628 O ATOM 2927 CB CYS A 412 33.203 2.186 23.289 1.00 34.22 C ANISOU 2927 CB CYS A 412 3664 4572 4767 184 -634 494 C ATOM 2928 SG CYS A 412 32.767 1.763 21.568 1.00 46.28 S ANISOU 2928 SG CYS A 412 5140 6063 6381 262 -498 459 S ATOM 2929 N ASP A 413 33.369 -1.164 23.069 1.00 35.77 N ANISOU 2929 N ASP A 413 3774 4716 5099 467 -627 591 N ATOM 2930 CA ASP A 413 34.065 -2.348 22.615 1.00 35.81 C ANISOU 2930 CA ASP A 413 3699 4718 5188 598 -620 627 C ATOM 2931 C ASP A 413 33.399 -2.840 21.337 1.00 35.46 C ANISOU 2931 C ASP A 413 3700 4592 5182 647 -502 575 C ATOM 2932 O ASP A 413 32.409 -2.258 20.883 1.00 33.75 O ANISOU 2932 O ASP A 413 3556 4341 4928 575 -441 525 O ATOM 2933 CB ASP A 413 34.041 -3.420 23.709 1.00 38.10 C ANISOU 2933 CB ASP A 413 4049 4970 5458 667 -698 700 C ATOM 2934 CG ASP A 413 35.174 -4.419 23.581 1.00 42.59 C ANISOU 2934 CG ASP A 413 4511 5566 6105 815 -727 762 C ATOM 2935 OD1 ASP A 413 35.950 -4.354 22.595 1.00 43.48 O ANISOU 2935 OD1 ASP A 413 4498 5734 6290 874 -673 745 O ATOM 2936 OD2 ASP A 413 35.279 -5.282 24.473 1.00 43.95 O ANISOU 2936 OD2 ASP A 413 4729 5709 6263 882 -798 834 O ATOM 2937 N TYR A 414 33.929 -3.918 20.771 1.00 36.06 N ANISOU 2937 N TYR A 414 3742 4636 5324 776 -472 591 N ATOM 2938 CA TYR A 414 33.493 -4.392 19.464 1.00 34.68 C ANISOU 2938 CA TYR A 414 3614 4386 5176 820 -363 534 C ATOM 2939 C TYR A 414 33.703 -5.881 19.333 1.00 36.38 C ANISOU 2939 C TYR A 414 3893 4504 5428 963 -349 559 C ATOM 2940 O TYR A 414 34.675 -6.420 19.838 1.00 37.93 O ANISOU 2940 O TYR A 414 4019 4730 5662 1075 -398 620 O ATOM 2941 CB TYR A 414 34.265 -3.663 18.363 1.00 35.30 C ANISOU 2941 CB TYR A 414 3562 4553 5297 821 -297 496 C ATOM 2942 CG TYR A 414 34.074 -4.180 16.945 1.00 33.95 C ANISOU 2942 CG TYR A 414 3429 4321 5147 883 -184 438 C ATOM 2943 CD1 TYR A 414 34.910 -5.167 16.418 1.00 34.55 C ANISOU 2943 CD1 TYR A 414 3471 4380 5276 1043 -137 446 C ATOM 2944 CD2 TYR A 414 33.082 -3.646 16.119 1.00 33.14 C ANISOU 2944 CD2 TYR A 414 3401 4187 5004 790 -121 378 C ATOM 2945 CE1 TYR A 414 34.744 -5.624 15.112 1.00 35.01 C ANISOU 2945 CE1 TYR A 414 3592 4375 5335 1098 -28 383 C ATOM 2946 CE2 TYR A 414 32.911 -4.091 14.818 1.00 33.74 C ANISOU 2946 CE2 TYR A 414 3523 4214 5082 831 -27 324 C ATOM 2947 CZ TYR A 414 33.742 -5.077 14.317 1.00 35.42 C ANISOU 2947 CZ TYR A 414 3722 4397 5337 980 21 320 C ATOM 2948 OH TYR A 414 33.561 -5.517 13.020 1.00 36.93 O ANISOU 2948 OH TYR A 414 3988 4531 5512 1018 119 257 O ATOM 2949 N VAL A 415 32.797 -6.547 18.636 1.00 36.75 N ANISOU 2949 N VAL A 415 4077 4429 5456 960 -285 516 N ATOM 2950 CA VAL A 415 32.987 -7.955 18.345 1.00 38.06 C ANISOU 2950 CA VAL A 415 4344 4469 5647 1091 -259 525 C ATOM 2951 C VAL A 415 32.654 -8.185 16.871 1.00 38.06 C ANISOU 2951 C VAL A 415 4412 4405 5645 1097 -152 441 C ATOM 2952 O VAL A 415 31.758 -7.546 16.319 1.00 35.85 O ANISOU 2952 O VAL A 415 4159 4138 5323 968 -120 392 O ATOM 2953 CB VAL A 415 32.123 -8.852 19.281 1.00 37.30 C ANISOU 2953 CB VAL A 415 4414 4252 5507 1059 -318 573 C ATOM 2954 CG1 VAL A 415 30.618 -8.672 19.005 1.00 35.60 C ANISOU 2954 CG1 VAL A 415 4312 3990 5226 897 -293 536 C ATOM 2955 CG2 VAL A 415 32.526 -10.299 19.163 1.00 38.26 C ANISOU 2955 CG2 VAL A 415 4654 4229 5656 1210 -306 598 C ATOM 2956 N SER A 416 33.408 -9.068 16.229 1.00 39.74 N ANISOU 2956 N SER A 416 4651 4553 5894 1257 -93 427 N ATOM 2957 CA SER A 416 33.181 -9.398 14.831 1.00 40.32 C ANISOU 2957 CA SER A 416 4817 4553 5949 1276 11 343 C ATOM 2958 C SER A 416 32.014 -10.383 14.694 1.00 39.17 C ANISOU 2958 C SER A 416 4914 4225 5744 1205 6 317 C ATOM 2959 O SER A 416 31.653 -11.059 15.653 1.00 37.86 O ANISOU 2959 O SER A 416 4846 3972 5568 1194 -64 374 O ATOM 2960 CB SER A 416 34.459 -9.982 14.223 1.00 43.01 C ANISOU 2960 CB SER A 416 5107 4895 6340 1493 89 337 C ATOM 2961 OG SER A 416 34.182 -11.152 13.484 1.00 44.79 O ANISOU 2961 OG SER A 416 5548 4935 6533 1572 157 283 O ATOM 2962 N ASN A 417 31.418 -10.466 13.509 1.00 39.61 N ANISOU 2962 N ASN A 417 5071 4226 5752 1140 73 237 N ATOM 2963 CA ASN A 417 30.281 -11.365 13.320 1.00 40.75 C ANISOU 2963 CA ASN A 417 5444 4209 5830 1034 57 215 C ATOM 2964 C ASN A 417 30.711 -12.813 13.113 1.00 44.03 C ANISOU 2964 C ASN A 417 6061 4424 6243 1177 88 199 C ATOM 2965 O ASN A 417 29.868 -13.704 13.021 1.00 45.88 O ANISOU 2965 O ASN A 417 6517 4497 6419 1086 66 185 O ATOM 2966 CB ASN A 417 29.405 -10.904 12.148 1.00 39.33 C ANISOU 2966 CB ASN A 417 5303 4055 5585 887 98 143 C ATOM 2967 CG ASN A 417 30.093 -11.032 10.795 1.00 41.65 C ANISOU 2967 CG ASN A 417 5628 4329 5869 991 205 58 C ATOM 2968 OD1 ASN A 417 31.297 -11.276 10.707 1.00 44.41 O ANISOU 2968 OD1 ASN A 417 5924 4680 6270 1183 261 56 O ATOM 2969 ND2 ASN A 417 29.321 -10.852 9.729 1.00 40.55 N ANISOU 2969 ND2 ASN A 417 5566 4187 5655 866 234 -5 N ATOM 2970 N LYS A 418 32.017 -13.049 13.036 1.00 44.16 N ANISOU 2970 N LYS A 418 6007 4452 6318 1400 140 206 N ATOM 2971 CA LYS A 418 32.506 -14.413 12.872 1.00 49.11 C ANISOU 2971 CA LYS A 418 6835 4880 6944 1580 183 196 C ATOM 2972 C LYS A 418 32.361 -15.164 14.189 1.00 48.57 C ANISOU 2972 C LYS A 418 6856 4710 6891 1599 86 292 C ATOM 2973 O LYS A 418 32.956 -14.782 15.197 1.00 49.05 O ANISOU 2973 O LYS A 418 6741 4888 7008 1666 26 379 O ATOM 2974 CB LYS A 418 33.961 -14.442 12.399 1.00 53.71 C ANISOU 2974 CB LYS A 418 7294 5529 7585 1842 279 190 C ATOM 2975 CG LYS A 418 34.448 -15.864 12.117 1.00 60.29 C ANISOU 2975 CG LYS A 418 8362 6140 8407 2062 346 173 C ATOM 2976 CD LYS A 418 35.861 -15.923 11.554 1.00 65.88 C ANISOU 2976 CD LYS A 418 8939 6927 9164 2346 465 170 C ATOM 2977 CE LYS A 418 36.313 -17.379 11.384 1.00 71.21 C ANISOU 2977 CE LYS A 418 9873 7361 9824 2596 535 160 C ATOM 2978 NZ LYS A 418 37.711 -17.519 10.875 1.00 73.65 N ANISOU 2978 NZ LYS A 418 10048 7756 10179 2914 666 171 N ATOM 2979 N GLY A 419 31.544 -16.213 14.179 1.00 47.65 N ANISOU 2979 N GLY A 419 7018 4375 6713 1521 65 280 N ATOM 2980 CA GLY A 419 31.282 -16.992 15.376 1.00 48.60 C ANISOU 2980 CA GLY A 419 7257 4376 6832 1513 -24 375 C ATOM 2981 C GLY A 419 30.235 -16.393 16.304 1.00 48.32 C ANISOU 2981 C GLY A 419 7146 4443 6770 1276 -123 437 C ATOM 2982 O GLY A 419 29.860 -17.016 17.301 1.00 50.83 O ANISOU 2982 O GLY A 419 7572 4671 7070 1233 -196 520 O ATOM 2983 N VAL A 420 29.767 -15.189 15.984 1.00 43.45 N ANISOU 2983 N VAL A 420 6352 4012 6143 1134 -117 403 N ATOM 2984 CA VAL A 420 28.762 -14.503 16.793 1.00 41.95 C ANISOU 2984 CA VAL A 420 6080 3938 5923 933 -190 457 C ATOM 2985 C VAL A 420 27.436 -14.411 16.034 1.00 42.92 C ANISOU 2985 C VAL A 420 6288 4051 5971 710 -180 408 C ATOM 2986 O VAL A 420 27.411 -14.085 14.848 1.00 44.48 O ANISOU 2986 O VAL A 420 6476 4273 6153 694 -119 323 O ATOM 2987 CB VAL A 420 29.238 -13.072 17.194 1.00 37.07 C ANISOU 2987 CB VAL A 420 5184 3554 5346 951 -200 472 C ATOM 2988 CG1 VAL A 420 28.121 -12.279 17.863 1.00 31.81 C ANISOU 2988 CG1 VAL A 420 4453 3002 4633 758 -249 511 C ATOM 2989 CG2 VAL A 420 30.463 -13.142 18.093 1.00 36.34 C ANISOU 2989 CG2 VAL A 420 4990 3501 5315 1132 -238 541 C ATOM 2990 N ASP A 421 26.333 -14.699 16.713 1.00 41.78 N ANISOU 2990 N ASP A 421 6218 3884 5772 535 -240 471 N ATOM 2991 CA ASP A 421 25.026 -14.601 16.086 1.00 42.10 C ANISOU 2991 CA ASP A 421 6307 3950 5739 310 -244 450 C ATOM 2992 C ASP A 421 24.207 -13.462 16.683 1.00 40.88 C ANISOU 2992 C ASP A 421 5957 4008 5567 188 -269 504 C ATOM 2993 O ASP A 421 23.460 -12.785 15.981 1.00 40.51 O ANISOU 2993 O ASP A 421 5835 4073 5486 73 -250 475 O ATOM 2994 CB ASP A 421 24.279 -15.923 16.220 1.00 44.78 C ANISOU 2994 CB ASP A 421 6902 4098 6017 177 -286 484 C ATOM 2995 CG ASP A 421 24.897 -17.015 15.377 1.00 50.66 C ANISOU 2995 CG ASP A 421 7886 4608 6753 279 -248 409 C ATOM 2996 OD1 ASP A 421 25.146 -16.775 14.175 1.00 52.43 O ANISOU 2996 OD1 ASP A 421 8115 4839 6968 313 -188 309 O ATOM 2997 OD2 ASP A 421 25.151 -18.108 15.915 1.00 54.79 O ANISOU 2997 OD2 ASP A 421 8606 4938 7275 335 -273 451 O ATOM 2998 N THR A 422 24.342 -13.253 17.987 1.00 40.18 N ANISOU 2998 N THR A 422 5797 3975 5495 223 -309 585 N ATOM 2999 CA THR A 422 23.612 -12.182 18.642 1.00 36.97 C ANISOU 2999 CA THR A 422 5230 3757 5062 135 -320 633 C ATOM 3000 C THR A 422 24.483 -11.416 19.623 1.00 36.43 C ANISOU 3000 C THR A 422 5030 3780 5034 264 -336 660 C ATOM 3001 O THR A 422 25.541 -11.881 20.049 1.00 37.44 O ANISOU 3001 O THR A 422 5185 3832 5207 403 -359 672 O ATOM 3002 CB THR A 422 22.384 -12.705 19.412 1.00 36.54 C ANISOU 3002 CB THR A 422 5244 3703 4935 -37 -360 728 C ATOM 3003 OG1 THR A 422 22.819 -13.564 20.471 1.00 38.50 O ANISOU 3003 OG1 THR A 422 5602 3838 5189 18 -405 796 O ATOM 3004 CG2 THR A 422 21.428 -13.464 18.490 1.00 34.41 C ANISOU 3004 CG2 THR A 422 5104 3359 4612 -212 -362 714 C ATOM 3005 N VAL A 423 24.005 -10.230 19.970 1.00 34.87 N ANISOU 3005 N VAL A 423 4692 3744 4811 217 -325 672 N ATOM 3006 CA VAL A 423 24.592 -9.391 20.994 1.00 33.99 C ANISOU 3006 CA VAL A 423 4477 3727 4709 291 -348 698 C ATOM 3007 C VAL A 423 23.444 -8.928 21.886 1.00 32.43 C ANISOU 3007 C VAL A 423 4255 3631 4434 185 -350 764 C ATOM 3008 O VAL A 423 22.347 -8.684 21.397 1.00 33.07 O ANISOU 3008 O VAL A 423 4315 3775 4475 81 -314 768 O ATOM 3009 CB VAL A 423 25.346 -8.199 20.363 1.00 36.42 C ANISOU 3009 CB VAL A 423 4650 4127 5062 363 -314 626 C ATOM 3010 CG1 VAL A 423 25.425 -7.022 21.313 1.00 37.66 C ANISOU 3010 CG1 VAL A 423 4713 4403 5191 365 -331 647 C ATOM 3011 CG2 VAL A 423 26.727 -8.642 19.905 1.00 36.18 C ANISOU 3011 CG2 VAL A 423 4613 4028 5106 500 -316 590 C ATOM 3012 N SER A 424 23.664 -8.851 23.191 1.00 33.85 N ANISOU 3012 N SER A 424 4439 3838 4584 213 -391 823 N ATOM 3013 CA SER A 424 22.627 -8.341 24.088 1.00 34.21 C ANISOU 3013 CA SER A 424 4462 3991 4544 134 -376 883 C ATOM 3014 C SER A 424 23.157 -7.181 24.902 1.00 32.90 C ANISOU 3014 C SER A 424 4229 3917 4355 201 -384 870 C ATOM 3015 O SER A 424 24.218 -7.281 25.518 1.00 32.93 O ANISOU 3015 O SER A 424 4243 3890 4379 276 -444 875 O ATOM 3016 CB SER A 424 22.113 -9.432 25.033 1.00 35.83 C ANISOU 3016 CB SER A 424 4778 4141 4696 68 -411 983 C ATOM 3017 OG SER A 424 21.346 -10.395 24.336 1.00 39.13 O ANISOU 3017 OG SER A 424 5273 4485 5110 -43 -402 1003 O ATOM 3018 N VAL A 425 22.415 -6.082 24.902 1.00 31.97 N ANISOU 3018 N VAL A 425 4049 3912 4188 174 -327 856 N ATOM 3019 CA VAL A 425 22.740 -4.946 25.751 1.00 32.98 C ANISOU 3019 CA VAL A 425 4154 4111 4267 219 -329 841 C ATOM 3020 C VAL A 425 21.518 -4.618 26.588 1.00 33.62 C ANISOU 3020 C VAL A 425 4253 4283 4240 177 -277 901 C ATOM 3021 O VAL A 425 20.527 -4.102 26.080 1.00 34.62 O ANISOU 3021 O VAL A 425 4328 4485 4341 153 -202 903 O ATOM 3022 CB VAL A 425 23.177 -3.729 24.927 1.00 33.11 C ANISOU 3022 CB VAL A 425 4099 4161 4321 258 -296 756 C ATOM 3023 CG1 VAL A 425 23.423 -2.528 25.834 1.00 33.29 C ANISOU 3023 CG1 VAL A 425 4136 4237 4275 284 -298 737 C ATOM 3024 CG2 VAL A 425 24.426 -4.073 24.126 1.00 32.87 C ANISOU 3024 CG2 VAL A 425 4035 4062 4391 303 -336 706 C ATOM 3025 N GLY A 426 21.583 -4.944 27.873 1.00 34.50 N ANISOU 3025 N GLY A 426 4432 4397 4281 175 -313 960 N ATOM 3026 CA GLY A 426 20.425 -4.819 28.734 1.00 33.39 C ANISOU 3026 CA GLY A 426 4312 4346 4027 137 -254 1030 C ATOM 3027 C GLY A 426 19.343 -5.767 28.256 1.00 35.00 C ANISOU 3027 C GLY A 426 4496 4566 4236 42 -221 1102 C ATOM 3028 O GLY A 426 19.612 -6.934 27.988 1.00 37.23 O ANISOU 3028 O GLY A 426 4828 4748 4569 -6 -277 1128 O ATOM 3029 N ASN A 427 18.121 -5.263 28.132 1.00 33.57 N ANISOU 3029 N ASN A 427 4246 4510 3997 14 -133 1137 N ATOM 3030 CA ASN A 427 16.999 -6.086 27.716 1.00 34.63 C ANISOU 3030 CA ASN A 427 4341 4694 4122 -104 -107 1219 C ATOM 3031 C ASN A 427 16.831 -6.147 26.196 1.00 37.13 C ANISOU 3031 C ASN A 427 4593 4995 4520 -145 -107 1173 C ATOM 3032 O ASN A 427 15.815 -6.637 25.698 1.00 39.74 O ANISOU 3032 O ASN A 427 4872 5392 4834 -257 -89 1236 O ATOM 3033 CB ASN A 427 15.713 -5.569 28.360 1.00 34.76 C ANISOU 3033 CB ASN A 427 4289 4889 4029 -114 -9 1303 C ATOM 3034 CG ASN A 427 15.722 -5.710 29.872 1.00 37.26 C ANISOU 3034 CG ASN A 427 4687 5228 4244 -99 -2 1364 C ATOM 3035 OD1 ASN A 427 16.364 -6.606 30.414 1.00 37.77 O ANISOU 3035 OD1 ASN A 427 4853 5184 4315 -137 -81 1388 O ATOM 3036 ND2 ASN A 427 15.000 -4.826 30.559 1.00 39.15 N ANISOU 3036 ND2 ASN A 427 4891 5608 4378 -34 98 1394 N ATOM 3037 N THR A 428 17.826 -5.662 25.460 1.00 35.55 N ANISOU 3037 N THR A 428 4392 4717 4398 -66 -132 1069 N ATOM 3038 CA THR A 428 17.731 -5.625 24.007 1.00 37.20 C ANISOU 3038 CA THR A 428 4549 4914 4670 -94 -127 1018 C ATOM 3039 C THR A 428 18.632 -6.648 23.319 1.00 36.89 C ANISOU 3039 C THR A 428 4591 4714 4711 -115 -194 969 C ATOM 3040 O THR A 428 19.856 -6.550 23.375 1.00 36.88 O ANISOU 3040 O THR A 428 4624 4626 4765 -23 -228 908 O ATOM 3041 CB THR A 428 18.079 -4.225 23.456 1.00 36.48 C ANISOU 3041 CB THR A 428 4393 4867 4602 10 -84 939 C ATOM 3042 OG1 THR A 428 17.200 -3.246 24.030 1.00 36.07 O ANISOU 3042 OG1 THR A 428 4286 4950 4469 54 -8 982 O ATOM 3043 CG2 THR A 428 17.936 -4.202 21.939 1.00 37.38 C ANISOU 3043 CG2 THR A 428 4457 4978 4767 -24 -78 896 C ATOM 3044 N LEU A 429 18.016 -7.617 22.651 1.00 36.17 N ANISOU 3044 N LEU A 429 4534 4590 4621 -236 -211 1000 N ATOM 3045 CA LEU A 429 18.749 -8.572 21.831 1.00 37.00 C ANISOU 3045 CA LEU A 429 4740 4531 4789 -248 -257 944 C ATOM 3046 C LEU A 429 18.879 -8.084 20.390 1.00 36.02 C ANISOU 3046 C LEU A 429 4565 4417 4704 -234 -233 860 C ATOM 3047 O LEU A 429 17.885 -7.766 19.748 1.00 35.20 O ANISOU 3047 O LEU A 429 4389 4421 4563 -319 -208 881 O ATOM 3048 CB LEU A 429 18.063 -9.936 21.845 1.00 40.17 C ANISOU 3048 CB LEU A 429 5251 4858 5156 -403 -294 1013 C ATOM 3049 CG LEU A 429 18.705 -11.016 20.974 1.00 42.17 C ANISOU 3049 CG LEU A 429 5652 4915 5455 -417 -334 953 C ATOM 3050 CD1 LEU A 429 19.808 -11.699 21.744 1.00 41.41 C ANISOU 3050 CD1 LEU A 429 5672 4666 5396 -306 -373 956 C ATOM 3051 CD2 LEU A 429 17.672 -12.031 20.521 1.00 45.40 C ANISOU 3051 CD2 LEU A 429 6153 5286 5811 -623 -361 1004 C ATOM 3052 N TYR A 430 20.113 -8.041 19.896 1.00 34.90 N ANISOU 3052 N TYR A 430 4453 4177 4631 -127 -241 774 N ATOM 3053 CA TYR A 430 20.402 -7.702 18.507 1.00 33.32 C ANISOU 3053 CA TYR A 430 4227 3969 4464 -109 -215 691 C ATOM 3054 C TYR A 430 20.924 -8.921 17.748 1.00 35.49 C ANISOU 3054 C TYR A 430 4640 4078 4766 -121 -238 644 C ATOM 3055 O TYR A 430 21.870 -9.565 18.197 1.00 36.37 O ANISOU 3055 O TYR A 430 4829 4071 4919 -32 -261 635 O ATOM 3056 CB TYR A 430 21.468 -6.602 18.403 1.00 31.56 C ANISOU 3056 CB TYR A 430 3924 3775 4292 27 -189 627 C ATOM 3057 CG TYR A 430 21.293 -5.328 19.213 1.00 31.88 C ANISOU 3057 CG TYR A 430 3873 3933 4307 70 -167 650 C ATOM 3058 CD1 TYR A 430 21.502 -5.314 20.595 1.00 33.03 C ANISOU 3058 CD1 TYR A 430 4038 4083 4431 102 -194 695 C ATOM 3059 CD2 TYR A 430 21.008 -4.115 18.578 1.00 31.75 C ANISOU 3059 CD2 TYR A 430 3773 4009 4281 88 -119 623 C ATOM 3060 CE1 TYR A 430 21.382 -4.130 21.332 1.00 34.59 C ANISOU 3060 CE1 TYR A 430 4186 4369 4589 144 -169 704 C ATOM 3061 CE2 TYR A 430 20.884 -2.928 19.297 1.00 33.15 C ANISOU 3061 CE2 TYR A 430 3904 4265 4427 139 -92 637 C ATOM 3062 CZ TYR A 430 21.067 -2.939 20.676 1.00 36.83 C ANISOU 3062 CZ TYR A 430 4402 4728 4863 165 -115 671 C ATOM 3063 OH TYR A 430 20.947 -1.762 21.398 1.00 38.55 O ANISOU 3063 OH TYR A 430 4607 5007 5032 214 -85 674 O ATOM 3064 N TYR A 431 20.338 -9.231 16.595 1.00 34.98 N ANISOU 3064 N TYR A 431 4614 4004 4673 -221 -231 615 N ATOM 3065 CA TYR A 431 20.977 -10.167 15.674 1.00 34.40 C ANISOU 3065 CA TYR A 431 4686 3768 4618 -203 -233 541 C ATOM 3066 C TYR A 431 22.027 -9.428 14.859 1.00 33.51 C ANISOU 3066 C TYR A 431 4507 3668 4556 -64 -183 452 C ATOM 3067 O TYR A 431 21.805 -8.288 14.438 1.00 32.72 O ANISOU 3067 O TYR A 431 4278 3703 4452 -62 -153 440 O ATOM 3068 CB TYR A 431 19.960 -10.833 14.740 1.00 34.26 C ANISOU 3068 CB TYR A 431 4763 3726 4529 -385 -255 539 C ATOM 3069 CG TYR A 431 19.194 -11.935 15.413 1.00 34.41 C ANISOU 3069 CG TYR A 431 4904 3671 4500 -534 -309 618 C ATOM 3070 CD1 TYR A 431 18.175 -11.643 16.309 1.00 34.32 C ANISOU 3070 CD1 TYR A 431 4787 3803 4450 -636 -327 727 C ATOM 3071 CD2 TYR A 431 19.501 -13.270 15.174 1.00 35.41 C ANISOU 3071 CD2 TYR A 431 5260 3580 4614 -568 -336 589 C ATOM 3072 CE1 TYR A 431 17.471 -12.650 16.946 1.00 35.37 C ANISOU 3072 CE1 TYR A 431 5025 3880 4535 -789 -374 812 C ATOM 3073 CE2 TYR A 431 18.800 -14.287 15.799 1.00 37.54 C ANISOU 3073 CE2 TYR A 431 5661 3768 4835 -723 -390 669 C ATOM 3074 CZ TYR A 431 17.785 -13.970 16.688 1.00 39.05 C ANISOU 3074 CZ TYR A 431 5728 4121 4990 -843 -411 784 C ATOM 3075 OH TYR A 431 17.080 -14.971 17.322 1.00 41.47 O ANISOU 3075 OH TYR A 431 6155 4358 5242 -1015 -461 876 O ATOM 3076 N VAL A 432 23.171 -10.071 14.642 1.00 32.12 N ANISOU 3076 N VAL A 432 4418 3358 4427 59 -169 399 N ATOM 3077 CA VAL A 432 24.223 -9.467 13.847 1.00 31.40 C ANISOU 3077 CA VAL A 432 4258 3291 4383 187 -113 324 C ATOM 3078 C VAL A 432 24.080 -9.921 12.394 1.00 34.32 C ANISOU 3078 C VAL A 432 4736 3594 4710 144 -76 247 C ATOM 3079 O VAL A 432 23.534 -10.999 12.119 1.00 34.13 O ANISOU 3079 O VAL A 432 4886 3447 4634 51 -101 240 O ATOM 3080 CB VAL A 432 25.631 -9.828 14.389 1.00 39.34 C ANISOU 3080 CB VAL A 432 5262 4224 5461 368 -107 319 C ATOM 3081 CG1 VAL A 432 25.763 -9.428 15.854 1.00 37.69 C ANISOU 3081 CG1 VAL A 432 4965 4080 5276 393 -158 396 C ATOM 3082 CG2 VAL A 432 25.907 -11.307 14.230 1.00 40.54 C ANISOU 3082 CG2 VAL A 432 5615 4180 5608 414 -110 303 C ATOM 3083 N ASN A 433 24.555 -9.093 11.466 1.00 34.58 N ANISOU 3083 N ASN A 433 4682 3704 4753 198 -19 190 N ATOM 3084 CA ASN A 433 24.555 -9.462 10.057 1.00 36.74 C ANISOU 3084 CA ASN A 433 5063 3921 4975 173 24 110 C ATOM 3085 C ASN A 433 25.514 -10.622 9.819 1.00 41.05 C ANISOU 3085 C ASN A 433 5769 4290 5539 303 61 55 C ATOM 3086 O ASN A 433 26.651 -10.611 10.299 1.00 42.25 O ANISOU 3086 O ASN A 433 5857 4431 5765 473 90 60 O ATOM 3087 CB ASN A 433 24.929 -8.256 9.186 1.00 36.07 C ANISOU 3087 CB ASN A 433 4843 3966 4895 212 83 74 C ATOM 3088 CG ASN A 433 23.904 -7.132 9.274 1.00 35.59 C ANISOU 3088 CG ASN A 433 4655 4063 4806 100 54 128 C ATOM 3089 OD1 ASN A 433 22.698 -7.365 9.150 1.00 38.40 O ANISOU 3089 OD1 ASN A 433 5051 4444 5096 -45 8 162 O ATOM 3090 ND2 ASN A 433 24.377 -5.913 9.506 1.00 31.33 N ANISOU 3090 ND2 ASN A 433 3963 3630 4311 166 81 144 N ATOM 3091 N LYS A 434 25.055 -11.634 9.093 1.00 43.88 N ANISOU 3091 N LYS A 434 6341 4509 5821 223 58 6 N ATOM 3092 CA LYS A 434 25.890 -12.801 8.849 1.00 46.97 C ANISOU 3092 CA LYS A 434 6928 4703 6215 360 102 -50 C ATOM 3093 C LYS A 434 26.622 -12.722 7.510 1.00 51.13 C ANISOU 3093 C LYS A 434 7499 5217 6713 464 203 -151 C ATOM 3094 O LYS A 434 27.049 -13.733 6.969 1.00 55.82 O ANISOU 3094 O LYS A 434 8306 5635 7268 549 253 -218 O ATOM 3095 CB LYS A 434 25.052 -14.078 8.922 1.00 47.45 C ANISOU 3095 CB LYS A 434 7250 4576 6200 218 43 -48 C ATOM 3096 CG LYS A 434 24.446 -14.330 10.298 1.00 46.18 C ANISOU 3096 CG LYS A 434 7067 4413 6066 131 -45 59 C ATOM 3097 CD LYS A 434 25.497 -14.243 11.399 1.00 45.52 C ANISOU 3097 CD LYS A 434 6877 4334 6085 337 -35 111 C ATOM 3098 CE LYS A 434 26.445 -15.439 11.360 1.00 46.98 C ANISOU 3098 CE LYS A 434 7265 4298 6287 520 4 78 C ATOM 3099 NZ LYS A 434 27.458 -15.408 12.456 1.00 45.16 N ANISOU 3099 NZ LYS A 434 6920 4088 6151 719 -2 146 N ATOM 3100 N GLN A 435 26.766 -11.514 6.984 1.00 52.98 N ANISOU 3100 N GLN A 435 7543 5630 6956 462 241 -159 N ATOM 3101 CA GLN A 435 27.569 -11.269 5.789 1.00 56.64 C ANISOU 3101 CA GLN A 435 8007 6118 7397 571 348 -240 C ATOM 3102 C GLN A 435 29.033 -11.693 5.989 1.00 56.71 C ANISOU 3102 C GLN A 435 7996 6072 7480 827 433 -254 C ATOM 3103 O GLN A 435 29.627 -11.435 7.033 1.00 55.62 O ANISOU 3103 O GLN A 435 7704 5990 7439 922 409 -184 O ATOM 3104 CB GLN A 435 27.489 -9.786 5.413 1.00 58.08 C ANISOU 3104 CB GLN A 435 7967 6510 7589 519 363 -219 C ATOM 3105 CG GLN A 435 28.624 -9.289 4.544 1.00 60.80 C ANISOU 3105 CG GLN A 435 8230 6925 7947 662 479 -267 C ATOM 3106 CD GLN A 435 28.263 -9.278 3.082 1.00 63.74 C ANISOU 3106 CD GLN A 435 8722 7295 8201 588 531 -344 C ATOM 3107 OE1 GLN A 435 27.380 -8.531 2.662 1.00 65.53 O ANISOU 3107 OE1 GLN A 435 8903 7622 8375 433 487 -325 O ATOM 3108 NE2 GLN A 435 28.941 -10.107 2.293 1.00 64.60 N ANISOU 3108 NE2 GLN A 435 8991 7292 8261 710 626 -427 N ATOM 3109 N GLU A 436 29.605 -12.346 4.984 1.00 58.84 N ANISOU 3109 N GLU A 436 8421 6240 7696 942 533 -341 N ATOM 3110 CA GLU A 436 31.006 -12.770 5.030 1.00 62.18 C ANISOU 3110 CA GLU A 436 8816 6629 8181 1212 634 -351 C ATOM 3111 C GLU A 436 31.981 -11.607 4.789 1.00 56.63 C ANISOU 3111 C GLU A 436 7829 6146 7542 1308 708 -326 C ATOM 3112 O GLU A 436 31.748 -10.762 3.926 1.00 55.66 O ANISOU 3112 O GLU A 436 7640 6138 7370 1211 742 -356 O ATOM 3113 CB GLU A 436 31.247 -13.874 3.998 1.00 69.63 C ANISOU 3113 CB GLU A 436 10045 7381 9028 1314 733 -456 C ATOM 3114 CG GLU A 436 32.629 -14.497 4.051 1.00 78.02 C ANISOU 3114 CG GLU A 436 11109 8388 10145 1627 849 -461 C ATOM 3115 CD GLU A 436 32.841 -15.336 5.296 1.00 84.33 C ANISOU 3115 CD GLU A 436 11963 9059 11020 1734 784 -389 C ATOM 3116 OE1 GLU A 436 32.212 -16.414 5.405 1.00 86.79 O ANISOU 3116 OE1 GLU A 436 12571 9136 11270 1680 742 -419 O ATOM 3117 OE2 GLU A 436 33.638 -14.913 6.165 1.00 86.13 O ANISOU 3117 OE2 GLU A 436 11944 9421 11361 1860 770 -298 O ATOM 3118 N GLY A 437 33.070 -11.568 5.553 1.00 53.61 N ANISOU 3118 N GLY A 437 7278 5827 7263 1489 726 -263 N ATOM 3119 CA GLY A 437 34.065 -10.516 5.414 1.00 49.82 C ANISOU 3119 CA GLY A 437 6521 5562 6845 1563 786 -225 C ATOM 3120 C GLY A 437 34.916 -10.310 6.656 1.00 49.68 C ANISOU 3120 C GLY A 437 6292 5641 6944 1669 734 -123 C ATOM 3121 O GLY A 437 34.471 -10.575 7.769 1.00 50.91 O ANISOU 3121 O GLY A 437 6475 5737 7132 1619 622 -70 O ATOM 3122 N LYS A 438 36.135 -9.810 6.469 1.00 50.22 N ANISOU 3122 N LYS A 438 6140 5873 7068 1801 811 -89 N ATOM 3123 CA LYS A 438 37.107 -9.707 7.562 1.00 50.47 C ANISOU 3123 CA LYS A 438 5961 6014 7202 1916 763 14 C ATOM 3124 C LYS A 438 36.992 -8.411 8.373 1.00 46.88 C ANISOU 3124 C LYS A 438 5298 5723 6792 1738 653 83 C ATOM 3125 O LYS A 438 36.782 -7.332 7.820 1.00 45.12 O ANISOU 3125 O LYS A 438 4993 5607 6545 1595 671 64 O ATOM 3126 CB LYS A 438 38.527 -9.834 7.008 1.00 54.57 C ANISOU 3126 CB LYS A 438 6322 6656 7758 2145 896 35 C ATOM 3127 CG LYS A 438 38.717 -10.985 6.024 1.00 60.94 C ANISOU 3127 CG LYS A 438 7345 7308 8502 2343 1038 -47 C ATOM 3128 CD LYS A 438 38.443 -12.345 6.670 1.00 66.01 C ANISOU 3128 CD LYS A 438 8222 7715 9144 2466 994 -47 C ATOM 3129 CE LYS A 438 38.429 -13.474 5.633 1.00 71.19 C ANISOU 3129 CE LYS A 438 9170 8168 9712 2627 1131 -151 C ATOM 3130 NZ LYS A 438 39.707 -13.574 4.864 1.00 75.10 N ANISOU 3130 NZ LYS A 438 9540 8778 10215 2891 1308 -151 N ATOM 3131 N SER A 439 37.133 -8.530 9.690 1.00 45.43 N ANISOU 3131 N SER A 439 5050 5548 6665 1748 540 162 N ATOM 3132 CA SER A 439 37.127 -7.373 10.578 1.00 43.49 C ANISOU 3132 CA SER A 439 4631 5444 6451 1596 433 226 C ATOM 3133 C SER A 439 38.500 -7.163 11.190 1.00 45.68 C ANISOU 3133 C SER A 439 4661 5890 6804 1707 412 319 C ATOM 3134 O SER A 439 39.210 -8.125 11.480 1.00 46.33 O ANISOU 3134 O SER A 439 4731 5949 6925 1911 427 363 O ATOM 3135 CB SER A 439 36.096 -7.540 11.689 1.00 42.11 C ANISOU 3135 CB SER A 439 4576 5165 6258 1481 307 248 C ATOM 3136 OG SER A 439 34.788 -7.503 11.168 1.00 45.06 O ANISOU 3136 OG SER A 439 5125 5434 6562 1340 313 181 O ATOM 3137 N LEU A 440 38.865 -5.905 11.399 1.00 45.41 N ANISOU 3137 N LEU A 440 4439 6028 6787 1571 371 357 N ATOM 3138 CA LEU A 440 40.127 -5.585 12.048 1.00 47.67 C ANISOU 3138 CA LEU A 440 4474 6501 7136 1626 324 457 C ATOM 3139 C LEU A 440 39.877 -4.716 13.278 1.00 46.48 C ANISOU 3139 C LEU A 440 4272 6404 6983 1442 169 506 C ATOM 3140 O LEU A 440 39.201 -3.690 13.205 1.00 45.47 O ANISOU 3140 O LEU A 440 4187 6275 6816 1248 145 469 O ATOM 3141 CB LEU A 440 41.069 -4.886 11.069 1.00 49.69 C ANISOU 3141 CB LEU A 440 4533 6941 7408 1630 430 467 C ATOM 3142 CG LEU A 440 42.368 -4.319 11.641 1.00 54.30 C ANISOU 3142 CG LEU A 440 4820 7762 8049 1626 375 580 C ATOM 3143 CD1 LEU A 440 43.179 -5.392 12.372 1.00 56.68 C ANISOU 3143 CD1 LEU A 440 5032 8098 8406 1854 340 667 C ATOM 3144 CD2 LEU A 440 43.191 -3.679 10.527 1.00 55.49 C ANISOU 3144 CD2 LEU A 440 4791 8089 8205 1617 500 589 C ATOM 3145 N TYR A 441 40.407 -5.149 14.413 1.00 46.47 N ANISOU 3145 N TYR A 441 4198 6443 7015 1514 67 591 N ATOM 3146 CA TYR A 441 40.248 -4.413 15.656 1.00 45.08 C ANISOU 3146 CA TYR A 441 3989 6317 6822 1351 -84 638 C ATOM 3147 C TYR A 441 41.459 -3.513 15.856 1.00 47.44 C ANISOU 3147 C TYR A 441 4025 6848 7151 1282 -131 714 C ATOM 3148 O TYR A 441 42.529 -3.986 16.216 1.00 50.14 O ANISOU 3148 O TYR A 441 4191 7317 7541 1412 -161 806 O ATOM 3149 CB TYR A 441 40.084 -5.383 16.833 1.00 43.39 C ANISOU 3149 CB TYR A 441 3861 6016 6609 1445 -183 693 C ATOM 3150 CG TYR A 441 39.593 -4.759 18.128 1.00 40.95 C ANISOU 3150 CG TYR A 441 3596 5711 6253 1276 -328 720 C ATOM 3151 CD1 TYR A 441 40.388 -3.870 18.850 1.00 40.80 C ANISOU 3151 CD1 TYR A 441 3405 5866 6233 1166 -434 786 C ATOM 3152 CD2 TYR A 441 38.348 -5.088 18.646 1.00 38.36 C ANISOU 3152 CD2 TYR A 441 3486 5218 5872 1221 -359 685 C ATOM 3153 CE1 TYR A 441 39.940 -3.309 20.041 1.00 39.90 C ANISOU 3153 CE1 TYR A 441 3362 5742 6056 1016 -561 801 C ATOM 3154 CE2 TYR A 441 37.893 -4.539 19.834 1.00 37.68 C ANISOU 3154 CE2 TYR A 441 3450 5137 5730 1084 -474 709 C ATOM 3155 CZ TYR A 441 38.691 -3.650 20.526 1.00 38.91 C ANISOU 3155 CZ TYR A 441 3459 5449 5876 988 -573 761 C ATOM 3156 OH TYR A 441 38.235 -3.112 21.709 1.00 38.19 O ANISOU 3156 OH TYR A 441 3446 5352 5711 855 -682 775 O ATOM 3157 N VAL A 442 41.295 -2.219 15.613 1.00 47.75 N ANISOU 3157 N VAL A 442 4038 6945 7159 1073 -138 684 N ATOM 3158 CA VAL A 442 42.403 -1.286 15.791 1.00 48.18 C ANISOU 3158 CA VAL A 442 3861 7215 7232 959 -192 757 C ATOM 3159 C VAL A 442 42.438 -0.770 17.225 1.00 49.27 C ANISOU 3159 C VAL A 442 3997 7388 7335 814 -370 807 C ATOM 3160 O VAL A 442 41.640 0.091 17.606 1.00 49.77 O ANISOU 3160 O VAL A 442 4208 7367 7336 635 -420 756 O ATOM 3161 CB VAL A 442 42.317 -0.088 14.820 1.00 45.67 C ANISOU 3161 CB VAL A 442 3527 6936 6889 789 -117 709 C ATOM 3162 CG1 VAL A 442 43.583 0.752 14.920 1.00 44.81 C ANISOU 3162 CG1 VAL A 442 3164 7059 6801 668 -165 798 C ATOM 3163 CG2 VAL A 442 42.105 -0.565 13.386 1.00 44.99 C ANISOU 3163 CG2 VAL A 442 3486 6796 6812 916 58 647 C ATOM 3164 N LYS A 443 43.357 -1.312 18.017 1.00 51.01 N ANISOU 3164 N LYS A 443 4060 7734 7589 904 -462 911 N ATOM 3165 CA LYS A 443 43.513 -0.916 19.415 1.00 52.08 C ANISOU 3165 CA LYS A 443 4186 7923 7679 772 -643 968 C ATOM 3166 C LYS A 443 43.937 0.542 19.534 1.00 52.22 C ANISOU 3166 C LYS A 443 4122 8063 7657 504 -713 977 C ATOM 3167 O LYS A 443 44.681 1.056 18.697 1.00 53.15 O ANISOU 3167 O LYS A 443 4066 8319 7808 453 -651 1000 O ATOM 3168 CB LYS A 443 44.536 -1.809 20.124 1.00 54.49 C ANISOU 3168 CB LYS A 443 4306 8368 8028 935 -729 1096 C ATOM 3169 CG LYS A 443 44.082 -3.243 20.394 1.00 56.43 C ANISOU 3169 CG LYS A 443 4684 8462 8294 1178 -704 1102 C ATOM 3170 CD LYS A 443 45.208 -4.010 21.103 1.00 62.31 C ANISOU 3170 CD LYS A 443 5228 9367 9082 1344 -796 1248 C ATOM 3171 CE LYS A 443 44.790 -5.405 21.551 1.00 64.08 C ANISOU 3171 CE LYS A 443 5609 9424 9315 1573 -795 1271 C ATOM 3172 NZ LYS A 443 45.929 -6.118 22.211 1.00 67.72 N ANISOU 3172 NZ LYS A 443 5865 10049 9817 1756 -884 1427 N ATOM 3173 N GLY A 444 43.456 1.200 20.582 1.00 51.18 N ANISOU 3173 N GLY A 444 4130 7872 7444 330 -840 959 N ATOM 3174 CA GLY A 444 43.766 2.595 20.815 1.00 50.67 C ANISOU 3174 CA GLY A 444 4051 7881 7321 60 -919 956 C ATOM 3175 C GLY A 444 43.145 3.077 22.107 1.00 51.21 C ANISOU 3175 C GLY A 444 4320 7852 7284 -81 -1053 929 C ATOM 3176 O GLY A 444 42.122 2.563 22.550 1.00 51.17 O ANISOU 3176 O GLY A 444 4511 7687 7247 8 -1039 880 O ATOM 3177 N GLU A 445 43.775 4.068 22.721 1.00 53.24 N ANISOU 3177 N GLU A 445 4535 8213 7480 -311 -1184 962 N ATOM 3178 CA GLU A 445 43.253 4.667 23.939 1.00 53.27 C ANISOU 3178 CA GLU A 445 4753 8127 7362 -464 -1308 927 C ATOM 3179 C GLU A 445 41.991 5.474 23.651 1.00 48.61 C ANISOU 3179 C GLU A 445 4444 7319 6707 -533 -1215 803 C ATOM 3180 O GLU A 445 41.996 6.341 22.777 1.00 46.41 O ANISOU 3180 O GLU A 445 4178 7019 6436 -637 -1139 764 O ATOM 3181 CB GLU A 445 44.314 5.556 24.579 1.00 58.09 C ANISOU 3181 CB GLU A 445 5258 8902 7912 -715 -1475 992 C ATOM 3182 CG GLU A 445 43.775 6.517 25.615 1.00 61.55 C ANISOU 3182 CG GLU A 445 5964 9220 8200 -923 -1582 927 C ATOM 3183 CD GLU A 445 44.056 6.063 27.027 1.00 65.76 C ANISOU 3183 CD GLU A 445 6506 9822 8657 -936 -1757 989 C ATOM 3184 OE1 GLU A 445 44.713 6.823 27.774 1.00 68.37 O ANISOU 3184 OE1 GLU A 445 6839 10245 8893 -1173 -1919 1021 O ATOM 3185 OE2 GLU A 445 43.621 4.948 27.387 1.00 66.54 O ANISOU 3185 OE2 GLU A 445 6620 9879 8781 -722 -1737 1010 O ATOM 3186 N PRO A 446 40.902 5.185 24.379 1.00 46.97 N ANISOU 3186 N PRO A 446 4456 6958 6433 -466 -1214 752 N ATOM 3187 CA PRO A 446 39.674 5.972 24.227 1.00 45.03 C ANISOU 3187 CA PRO A 446 4469 6525 6117 -515 -1129 648 C ATOM 3188 C PRO A 446 39.986 7.446 24.434 1.00 45.82 C ANISOU 3188 C PRO A 446 4668 6613 6129 -761 -1192 618 C ATOM 3189 O PRO A 446 40.531 7.803 25.482 1.00 45.99 O ANISOU 3189 O PRO A 446 4717 6692 6067 -904 -1342 646 O ATOM 3190 CB PRO A 446 38.763 5.427 25.330 1.00 44.15 C ANISOU 3190 CB PRO A 446 4532 6315 5929 -434 -1163 632 C ATOM 3191 CG PRO A 446 39.272 4.038 25.584 1.00 44.26 C ANISOU 3191 CG PRO A 446 4381 6420 6015 -275 -1205 717 C ATOM 3192 CD PRO A 446 40.766 4.138 25.405 1.00 46.85 C ANISOU 3192 CD PRO A 446 4456 6945 6398 -343 -1292 800 C ATOM 3193 N ILE A 447 39.678 8.283 23.446 1.00 44.59 N ANISOU 3193 N ILE A 447 4576 6382 5984 -819 -1087 565 N ATOM 3194 CA ILE A 447 40.128 9.672 23.490 1.00 45.45 C ANISOU 3194 CA ILE A 447 4773 6477 6019 -1064 -1143 547 C ATOM 3195 C ILE A 447 39.411 10.456 24.584 1.00 44.39 C ANISOU 3195 C ILE A 447 4944 6189 5733 -1158 -1201 480 C ATOM 3196 O ILE A 447 39.852 11.538 24.952 1.00 44.91 O ANISOU 3196 O ILE A 447 5124 6231 5710 -1380 -1285 465 O ATOM 3197 CB ILE A 447 39.935 10.393 22.131 1.00 39.49 C ANISOU 3197 CB ILE A 447 4035 5664 5307 -1095 -1009 515 C ATOM 3198 CG1 ILE A 447 38.449 10.501 21.770 1.00 35.79 C ANISOU 3198 CG1 ILE A 447 3783 5004 4813 -956 -875 435 C ATOM 3199 CG2 ILE A 447 40.739 9.694 21.026 1.00 38.98 C ANISOU 3199 CG2 ILE A 447 3674 5762 5374 -1013 -944 580 C ATOM 3200 CD1 ILE A 447 38.171 11.472 20.636 1.00 34.92 C ANISOU 3200 CD1 ILE A 447 3753 4809 4706 -1015 -767 403 C ATOM 3201 N ILE A 448 38.323 9.897 25.117 1.00 43.22 N ANISOU 3201 N ILE A 448 4934 5940 5549 -996 -1154 442 N ATOM 3202 CA ILE A 448 37.556 10.560 26.173 1.00 44.57 C ANISOU 3202 CA ILE A 448 5398 5969 5567 -1047 -1183 378 C ATOM 3203 C ILE A 448 38.394 10.709 27.447 1.00 48.72 C ANISOU 3203 C ILE A 448 5946 6574 5991 -1211 -1371 409 C ATOM 3204 O ILE A 448 38.121 11.571 28.281 1.00 51.48 O ANISOU 3204 O ILE A 448 6552 6817 6192 -1331 -1421 352 O ATOM 3205 CB ILE A 448 36.231 9.794 26.489 1.00 45.08 C ANISOU 3205 CB ILE A 448 5564 5947 5617 -831 -1087 352 C ATOM 3206 CG1 ILE A 448 35.296 10.640 27.364 1.00 43.66 C ANISOU 3206 CG1 ILE A 448 5699 5614 5277 -856 -1068 279 C ATOM 3207 CG2 ILE A 448 36.513 8.440 27.145 1.00 44.85 C ANISOU 3207 CG2 ILE A 448 5388 6028 5626 -728 -1161 420 C ATOM 3208 CD1 ILE A 448 34.886 11.950 26.743 1.00 43.43 C ANISOU 3208 CD1 ILE A 448 5851 5445 5203 -920 -981 214 C ATOM 3209 N ASN A 449 39.432 9.885 27.581 1.00 50.70 N ANISOU 3209 N ASN A 449 5934 7014 6315 -1214 -1474 502 N ATOM 3210 CA ASN A 449 40.314 9.941 28.742 1.00 53.81 C ANISOU 3210 CA ASN A 449 6306 7521 6619 -1373 -1671 552 C ATOM 3211 C ASN A 449 41.219 11.163 28.746 1.00 56.04 C ANISOU 3211 C ASN A 449 6617 7840 6834 -1668 -1779 551 C ATOM 3212 O ASN A 449 41.800 11.505 29.773 1.00 57.44 O ANISOU 3212 O ASN A 449 6857 8074 6893 -1852 -1950 570 O ATOM 3213 CB ASN A 449 41.186 8.687 28.820 1.00 56.90 C ANISOU 3213 CB ASN A 449 6385 8120 7116 -1267 -1748 670 C ATOM 3214 CG ASN A 449 40.375 7.415 28.954 1.00 57.70 C ANISOU 3214 CG ASN A 449 6481 8174 7267 -1001 -1667 681 C ATOM 3215 OD1 ASN A 449 39.200 7.446 29.319 1.00 56.39 O ANISOU 3215 OD1 ASN A 449 6544 7852 7030 -926 -1590 611 O ATOM 3216 ND2 ASN A 449 41.004 6.281 28.660 1.00 59.51 N ANISOU 3216 ND2 ASN A 449 6452 8543 7618 -857 -1679 774 N ATOM 3217 N PHE A 450 41.345 11.817 27.596 1.00 56.16 N ANISOU 3217 N PHE A 450 6595 7825 6917 -1729 -1685 533 N ATOM 3218 CA PHE A 450 42.264 12.944 27.457 1.00 58.44 C ANISOU 3218 CA PHE A 450 6892 8157 7157 -2028 -1780 547 C ATOM 3219 C PHE A 450 41.640 14.246 27.948 1.00 59.14 C ANISOU 3219 C PHE A 450 7382 8012 7078 -2187 -1785 438 C ATOM 3220 O PHE A 450 42.281 15.292 27.929 1.00 63.45 O ANISOU 3220 O PHE A 450 8013 8543 7553 -2461 -1869 435 O ATOM 3221 CB PHE A 450 42.702 13.106 25.997 1.00 57.95 C ANISOU 3221 CB PHE A 450 6625 8163 7231 -2034 -1672 583 C ATOM 3222 CG PHE A 450 43.418 11.907 25.432 1.00 59.07 C ANISOU 3222 CG PHE A 450 6380 8533 7529 -1876 -1654 688 C ATOM 3223 CD1 PHE A 450 44.218 11.107 26.239 1.00 61.89 C ANISOU 3223 CD1 PHE A 450 6532 9088 7895 -1865 -1799 781 C ATOM 3224 CD2 PHE A 450 43.290 11.578 24.089 1.00 57.91 C ANISOU 3224 CD2 PHE A 450 6088 8403 7512 -1728 -1487 695 C ATOM 3225 CE1 PHE A 450 44.875 10.002 25.714 1.00 62.36 C ANISOU 3225 CE1 PHE A 450 6251 9347 8097 -1689 -1769 881 C ATOM 3226 CE2 PHE A 450 43.942 10.476 23.559 1.00 58.10 C ANISOU 3226 CE2 PHE A 450 5785 8620 7668 -1564 -1455 783 C ATOM 3227 CZ PHE A 450 44.735 9.687 24.370 1.00 60.35 C ANISOU 3227 CZ PHE A 450 5871 9092 7967 -1535 -1590 876 C ATOM 3228 N TYR A 451 40.387 14.183 28.380 1.00 57.03 N ANISOU 3228 N TYR A 451 7367 7562 6740 -2015 -1691 354 N ATOM 3229 CA TYR A 451 39.661 15.387 28.765 1.00 56.30 C ANISOU 3229 CA TYR A 451 7673 7228 6490 -2103 -1656 247 C ATOM 3230 C TYR A 451 39.448 15.480 30.276 1.00 58.19 C ANISOU 3230 C TYR A 451 8152 7412 6546 -2159 -1768 203 C ATOM 3231 O TYR A 451 39.178 14.480 30.942 1.00 56.72 O ANISOU 3231 O TYR A 451 7888 7303 6361 -2005 -1789 231 O ATOM 3232 CB TYR A 451 38.312 15.440 28.038 1.00 53.12 C ANISOU 3232 CB TYR A 451 7400 6655 6129 -1860 -1440 185 C ATOM 3233 CG TYR A 451 38.427 15.616 26.533 1.00 51.67 C ANISOU 3233 CG TYR A 451 7061 6485 6085 -1834 -1326 211 C ATOM 3234 CD1 TYR A 451 38.499 16.884 25.967 1.00 51.68 C ANISOU 3234 CD1 TYR A 451 7245 6349 6041 -1991 -1293 175 C ATOM 3235 CD2 TYR A 451 38.463 14.516 25.681 1.00 49.46 C ANISOU 3235 CD2 TYR A 451 6476 6345 5972 -1654 -1250 271 C ATOM 3236 CE1 TYR A 451 38.605 17.054 24.600 1.00 50.86 C ANISOU 3236 CE1 TYR A 451 7008 6262 6053 -1972 -1189 206 C ATOM 3237 CE2 TYR A 451 38.566 14.677 24.313 1.00 48.45 C ANISOU 3237 CE2 TYR A 451 6222 6233 5954 -1632 -1143 292 C ATOM 3238 CZ TYR A 451 38.636 15.950 23.778 1.00 50.04 C ANISOU 3238 CZ TYR A 451 6594 6311 6107 -1793 -1114 262 C ATOM 3239 OH TYR A 451 38.740 16.126 22.417 1.00 49.88 O ANISOU 3239 OH TYR A 451 6456 6310 6185 -1776 -1007 289 O ATOM 3240 N ASP A 452 39.583 16.690 30.809 1.00 61.67 N ANISOU 3240 N ASP A 452 8903 7710 6819 -2386 -1840 135 N ATOM 3241 CA ASP A 452 39.311 16.963 32.217 1.00 64.82 C ANISOU 3241 CA ASP A 452 9600 8020 7010 -2450 -1931 72 C ATOM 3242 C ASP A 452 37.822 17.236 32.414 1.00 64.53 C ANISOU 3242 C ASP A 452 9875 7755 6889 -2219 -1746 -29 C ATOM 3243 O ASP A 452 37.287 18.197 31.863 1.00 65.30 O ANISOU 3243 O ASP A 452 10197 7657 6956 -2211 -1629 -97 O ATOM 3244 CB ASP A 452 40.145 18.152 32.697 1.00 69.24 C ANISOU 3244 CB ASP A 452 10381 8518 7410 -2813 -2095 38 C ATOM 3245 CG ASP A 452 39.762 18.619 34.091 1.00 73.59 C ANISOU 3245 CG ASP A 452 11321 8927 7714 -2885 -2169 -53 C ATOM 3246 OD1 ASP A 452 39.236 17.804 34.880 1.00 73.78 O ANISOU 3246 OD1 ASP A 452 11341 8997 7694 -2703 -2158 -51 O ATOM 3247 OD2 ASP A 452 40.000 19.806 34.401 1.00 76.55 O ANISOU 3247 OD2 ASP A 452 12020 9139 7926 -3132 -2237 -126 O ATOM 3248 N PRO A 453 37.145 16.391 33.203 1.00 64.12 N ANISOU 3248 N PRO A 453 9831 7735 6795 -2025 -1717 -28 N ATOM 3249 CA PRO A 453 35.687 16.508 33.341 1.00 64.27 C ANISOU 3249 CA PRO A 453 10083 7585 6752 -1778 -1525 -101 C ATOM 3250 C PRO A 453 35.230 17.843 33.936 1.00 66.78 C ANISOU 3250 C PRO A 453 10861 7660 6853 -1859 -1492 -219 C ATOM 3251 O PRO A 453 34.089 18.245 33.709 1.00 67.57 O ANISOU 3251 O PRO A 453 11151 7601 6921 -1660 -1308 -276 O ATOM 3252 CB PRO A 453 35.328 15.346 34.276 1.00 62.67 C ANISOU 3252 CB PRO A 453 9796 7497 6520 -1631 -1549 -61 C ATOM 3253 CG PRO A 453 36.454 14.373 34.122 1.00 62.27 C ANISOU 3253 CG PRO A 453 9375 7680 6604 -1708 -1699 52 C ATOM 3254 CD PRO A 453 37.676 15.223 33.925 1.00 63.80 C ANISOU 3254 CD PRO A 453 9559 7904 6777 -2009 -1850 57 C ATOM 3255 N LEU A 454 36.107 18.526 34.665 1.00 68.41 N ANISOU 3255 N LEU A 454 11247 7839 6909 -2145 -1669 -250 N ATOM 3256 CA LEU A 454 35.731 19.773 35.324 1.00 71.74 C ANISOU 3256 CA LEU A 454 12150 8010 7099 -2235 -1649 -371 C ATOM 3257 C LEU A 454 35.545 20.930 34.342 1.00 72.72 C ANISOU 3257 C LEU A 454 12456 7927 7246 -2272 -1542 -422 C ATOM 3258 O LEU A 454 34.887 21.920 34.664 1.00 74.75 O ANISOU 3258 O LEU A 454 13127 7935 7339 -2235 -1450 -524 O ATOM 3259 CB LEU A 454 36.776 20.160 36.376 1.00 75.18 C ANISOU 3259 CB LEU A 454 12737 8475 7353 -2567 -1889 -390 C ATOM 3260 CG LEU A 454 37.135 19.098 37.421 1.00 76.77 C ANISOU 3260 CG LEU A 454 12773 8888 7508 -2573 -2034 -328 C ATOM 3261 CD1 LEU A 454 37.946 19.713 38.560 1.00 79.70 C ANISOU 3261 CD1 LEU A 454 13401 9240 7641 -2898 -2257 -371 C ATOM 3262 CD2 LEU A 454 35.892 18.378 37.951 1.00 75.79 C ANISOU 3262 CD2 LEU A 454 12703 8745 7348 -2246 -1872 -345 C ATOM 3263 N VAL A 455 36.129 20.812 33.153 1.00 70.39 N ANISOU 3263 N VAL A 455 11867 7732 7147 -2337 -1549 -347 N ATOM 3264 CA VAL A 455 36.040 21.874 32.153 1.00 68.14 C ANISOU 3264 CA VAL A 455 11732 7265 6891 -2390 -1458 -376 C ATOM 3265 C VAL A 455 35.523 21.344 30.817 1.00 63.88 C ANISOU 3265 C VAL A 455 10901 6798 6574 -2155 -1295 -312 C ATOM 3266 O VAL A 455 35.513 22.055 29.812 1.00 65.43 O ANISOU 3266 O VAL A 455 11144 6888 6829 -2186 -1221 -310 O ATOM 3267 CB VAL A 455 37.406 22.560 31.938 1.00 69.27 C ANISOU 3267 CB VAL A 455 11865 7436 7020 -2784 -1642 -349 C ATOM 3268 CG1 VAL A 455 37.898 23.173 33.244 1.00 71.27 C ANISOU 3268 CG1 VAL A 455 12446 7602 7030 -3049 -1816 -419 C ATOM 3269 CG2 VAL A 455 38.419 21.566 31.386 1.00 68.04 C ANISOU 3269 CG2 VAL A 455 11198 7596 7060 -2865 -1747 -220 C ATOM 3270 N PHE A 456 35.086 20.092 30.820 1.00 59.82 N ANISOU 3270 N PHE A 456 10102 6455 6171 -1928 -1244 -259 N ATOM 3271 CA PHE A 456 34.553 19.458 29.623 1.00 57.18 C ANISOU 3271 CA PHE A 456 9494 6199 6032 -1707 -1099 -202 C ATOM 3272 C PHE A 456 33.168 20.003 29.274 1.00 58.10 C ANISOU 3272 C PHE A 456 9839 6126 6112 -1459 -893 -253 C ATOM 3273 O PHE A 456 32.226 19.861 30.054 1.00 59.33 O ANISOU 3273 O PHE A 456 10153 6225 6166 -1278 -815 -293 O ATOM 3274 CB PHE A 456 34.491 17.944 29.822 1.00 53.77 C ANISOU 3274 CB PHE A 456 8732 5987 5711 -1556 -1116 -133 C ATOM 3275 CG PHE A 456 34.106 17.176 28.583 1.00 51.49 C ANISOU 3275 CG PHE A 456 8149 5795 5621 -1368 -995 -72 C ATOM 3276 CD1 PHE A 456 35.002 17.032 27.536 1.00 50.92 C ANISOU 3276 CD1 PHE A 456 7819 5836 5694 -1474 -1030 -12 C ATOM 3277 CD2 PHE A 456 32.862 16.580 28.481 1.00 49.31 C ANISOU 3277 CD2 PHE A 456 7853 5508 5375 -1095 -848 -72 C ATOM 3278 CE1 PHE A 456 34.664 16.319 26.408 1.00 49.54 C ANISOU 3278 CE1 PHE A 456 7399 5742 5682 -1306 -920 35 C ATOM 3279 CE2 PHE A 456 32.514 15.860 27.358 1.00 49.00 C ANISOU 3279 CE2 PHE A 456 7562 5556 5502 -947 -751 -20 C ATOM 3280 CZ PHE A 456 33.415 15.731 26.315 1.00 49.35 C ANISOU 3280 CZ PHE A 456 7377 5694 5681 -1049 -787 28 C ATOM 3281 N PRO A 457 33.040 20.633 28.097 1.00 57.79 N ANISOU 3281 N PRO A 457 9808 5999 6149 -1444 -802 -242 N ATOM 3282 CA PRO A 457 31.735 21.138 27.655 1.00 58.61 C ANISOU 3282 CA PRO A 457 10094 5946 6231 -1191 -608 -270 C ATOM 3283 C PRO A 457 30.832 19.991 27.209 1.00 58.53 C ANISOU 3283 C PRO A 457 9803 6087 6350 -918 -494 -213 C ATOM 3284 O PRO A 457 31.056 19.411 26.145 1.00 58.60 O ANISOU 3284 O PRO A 457 9520 6222 6522 -900 -479 -149 O ATOM 3285 CB PRO A 457 32.093 22.058 26.486 1.00 57.83 C ANISOU 3285 CB PRO A 457 10047 5740 6186 -1300 -579 -254 C ATOM 3286 CG PRO A 457 33.369 21.489 25.945 1.00 57.29 C ANISOU 3286 CG PRO A 457 9645 5871 6252 -1516 -709 -186 C ATOM 3287 CD PRO A 457 34.103 20.881 27.107 1.00 57.48 C ANISOU 3287 CD PRO A 457 9595 6024 6221 -1657 -872 -190 C ATOM 3288 N SER A 458 29.827 19.664 28.015 1.00 58.75 N ANISOU 3288 N SER A 458 9924 6104 6293 -717 -415 -236 N ATOM 3289 CA SER A 458 29.025 18.469 27.769 1.00 59.60 C ANISOU 3289 CA SER A 458 9764 6373 6508 -500 -333 -176 C ATOM 3290 C SER A 458 27.621 18.770 27.248 1.00 61.09 C ANISOU 3290 C SER A 458 10021 6496 6694 -235 -142 -165 C ATOM 3291 O SER A 458 26.683 18.007 27.493 1.00 60.82 O ANISOU 3291 O SER A 458 9879 6558 6671 -46 -61 -132 O ATOM 3292 CB SER A 458 28.925 17.637 29.048 1.00 60.31 C ANISOU 3292 CB SER A 458 9837 6557 6523 -475 -389 -179 C ATOM 3293 OG SER A 458 28.377 18.402 30.108 1.00 62.27 O ANISOU 3293 OG SER A 458 10432 6658 6571 -424 -342 -250 O ATOM 3294 N ASP A 459 27.481 19.864 26.510 1.00 62.83 N ANISOU 3294 N ASP A 459 10410 6564 6901 -226 -75 -180 N ATOM 3295 CA ASP A 459 26.175 20.257 26.002 1.00 64.94 C ANISOU 3295 CA ASP A 459 10747 6769 7156 35 100 -158 C ATOM 3296 C ASP A 459 26.203 20.549 24.504 1.00 61.43 C ANISOU 3296 C ASP A 459 10185 6321 6836 41 143 -106 C ATOM 3297 O ASP A 459 25.380 21.313 24.002 1.00 63.12 O ANISOU 3297 O ASP A 459 10539 6425 7017 206 265 -92 O ATOM 3298 CB ASP A 459 25.667 21.483 26.762 1.00 71.27 C ANISOU 3298 CB ASP A 459 11967 7345 7767 118 179 -228 C ATOM 3299 CG ASP A 459 26.588 22.688 26.613 1.00 76.20 C ANISOU 3299 CG ASP A 459 12866 7761 8326 -100 106 -284 C ATOM 3300 OD1 ASP A 459 27.788 22.499 26.305 1.00 76.73 O ANISOU 3300 OD1 ASP A 459 12799 7888 8469 -362 -38 -276 O ATOM 3301 OD2 ASP A 459 26.108 23.827 26.806 1.00 79.07 O ANISOU 3301 OD2 ASP A 459 13584 7900 8557 -9 196 -331 O ATOM 3302 N GLU A 460 27.148 19.940 23.795 1.00 57.91 N ANISOU 3302 N GLU A 460 9481 5997 6524 -125 46 -73 N ATOM 3303 CA GLU A 460 27.324 20.197 22.367 1.00 56.68 C ANISOU 3303 CA GLU A 460 9214 5846 6476 -149 77 -26 C ATOM 3304 C GLU A 460 26.624 19.153 21.502 1.00 54.75 C ANISOU 3304 C GLU A 460 8668 5777 6357 10 143 43 C ATOM 3305 O GLU A 460 26.943 17.970 21.580 1.00 54.54 O ANISOU 3305 O GLU A 460 8394 5914 6414 -23 84 62 O ATOM 3306 CB GLU A 460 28.812 20.229 22.019 1.00 59.17 C ANISOU 3306 CB GLU A 460 9433 6196 6852 -429 -54 -26 C ATOM 3307 CG GLU A 460 29.633 21.205 22.838 1.00 63.14 C ANISOU 3307 CG GLU A 460 10214 6545 7231 -645 -149 -87 C ATOM 3308 CD GLU A 460 29.233 22.646 22.595 1.00 66.63 C ANISOU 3308 CD GLU A 460 11009 6738 7570 -623 -71 -115 C ATOM 3309 OE1 GLU A 460 28.988 23.016 21.421 1.00 64.26 O ANISOU 3309 OE1 GLU A 460 10674 6407 7334 -567 5 -68 O ATOM 3310 OE2 GLU A 460 29.161 23.405 23.586 1.00 70.24 O ANISOU 3310 OE2 GLU A 460 11793 7022 7872 -656 -85 -184 O ATOM 3311 N PHE A 461 25.680 19.586 20.672 1.00 53.74 N ANISOU 3311 N PHE A 461 8569 5612 6236 179 259 84 N ATOM 3312 CA PHE A 461 25.000 18.665 19.762 1.00 51.55 C ANISOU 3312 CA PHE A 461 8021 5501 6065 305 311 152 C ATOM 3313 C PHE A 461 25.668 18.664 18.393 1.00 49.73 C ANISOU 3313 C PHE A 461 7651 5309 5937 195 288 185 C ATOM 3314 O PHE A 461 25.616 17.676 17.669 1.00 50.40 O ANISOU 3314 O PHE A 461 7485 5545 6120 210 285 222 O ATOM 3315 CB PHE A 461 23.519 19.031 19.621 1.00 54.42 C ANISOU 3315 CB PHE A 461 8455 5847 6376 559 444 196 C ATOM 3316 CG PHE A 461 23.280 20.409 19.046 1.00 59.75 C ANISOU 3316 CG PHE A 461 9362 6347 6992 621 515 207 C ATOM 3317 CD1 PHE A 461 23.306 21.535 19.861 1.00 63.31 C ANISOU 3317 CD1 PHE A 461 10151 6590 7313 636 541 152 C ATOM 3318 CD2 PHE A 461 23.024 20.577 17.690 1.00 60.78 C ANISOU 3318 CD2 PHE A 461 9395 6510 7188 664 555 274 C ATOM 3319 CE1 PHE A 461 23.089 22.806 19.331 1.00 65.51 C ANISOU 3319 CE1 PHE A 461 10674 6683 7534 700 609 166 C ATOM 3320 CE2 PHE A 461 22.804 21.840 17.154 1.00 63.15 C ANISOU 3320 CE2 PHE A 461 9920 6642 7432 727 618 296 C ATOM 3321 CZ PHE A 461 22.839 22.957 17.977 1.00 65.53 C ANISOU 3321 CZ PHE A 461 10565 6722 7610 749 647 243 C ATOM 3322 N ASP A 462 26.295 19.780 18.046 1.00 48.70 N ANISOU 3322 N ASP A 462 7698 5033 5772 77 277 170 N ATOM 3323 CA ASP A 462 26.910 19.949 16.735 1.00 48.68 C ANISOU 3323 CA ASP A 462 7593 5056 5846 -29 271 208 C ATOM 3324 C ASP A 462 28.258 20.651 16.891 1.00 49.29 C ANISOU 3324 C ASP A 462 7781 5044 5903 -286 184 177 C ATOM 3325 O ASP A 462 28.419 21.809 16.507 1.00 50.58 O ANISOU 3325 O ASP A 462 8156 5049 6014 -352 206 183 O ATOM 3326 CB ASP A 462 25.985 20.750 15.806 1.00 49.76 C ANISOU 3326 CB ASP A 462 7840 5111 5956 124 377 261 C ATOM 3327 CG ASP A 462 26.575 20.967 14.410 1.00 52.21 C ANISOU 3327 CG ASP A 462 8061 5446 6330 16 379 307 C ATOM 3328 OD1 ASP A 462 27.373 20.123 13.948 1.00 49.96 O ANISOU 3328 OD1 ASP A 462 7544 5306 6134 -105 327 310 O ATOM 3329 OD2 ASP A 462 26.236 21.994 13.778 1.00 55.25 O ANISOU 3329 OD2 ASP A 462 8621 5703 6670 63 438 344 O ATOM 3330 N ALA A 463 29.223 19.955 17.475 1.00 47.15 N ANISOU 3330 N ALA A 463 7369 4877 5670 -438 80 152 N ATOM 3331 CA ALA A 463 30.542 20.544 17.661 1.00 47.31 C ANISOU 3331 CA ALA A 463 7452 4853 5671 -704 -19 136 C ATOM 3332 C ALA A 463 31.590 19.788 16.859 1.00 45.90 C ANISOU 3332 C ALA A 463 6965 4862 5613 -832 -65 179 C ATOM 3333 O ALA A 463 31.279 19.114 15.870 1.00 42.53 O ANISOU 3333 O ALA A 463 6343 4545 5271 -723 -1 217 O ATOM 3334 CB ALA A 463 30.918 20.572 19.137 1.00 46.09 C ANISOU 3334 CB ALA A 463 7421 4660 5432 -798 -116 79 C ATOM 3335 N SER A 464 32.836 19.919 17.298 1.00 45.38 N ANISOU 3335 N SER A 464 6862 4836 5544 -1066 -177 175 N ATOM 3336 CA SER A 464 33.957 19.263 16.653 1.00 43.61 C ANISOU 3336 CA SER A 464 6341 4804 5425 -1189 -220 222 C ATOM 3337 C SER A 464 35.115 19.237 17.629 1.00 43.29 C ANISOU 3337 C SER A 464 6258 4830 5361 -1405 -365 217 C ATOM 3338 O SER A 464 35.034 19.855 18.693 1.00 42.89 O ANISOU 3338 O SER A 464 6444 4652 5202 -1480 -430 171 O ATOM 3339 CB SER A 464 34.353 19.991 15.369 1.00 43.94 C ANISOU 3339 CB SER A 464 6382 4823 5490 -1294 -165 269 C ATOM 3340 OG SER A 464 34.882 21.265 15.674 1.00 46.33 O ANISOU 3340 OG SER A 464 6923 4976 5702 -1515 -220 263 O ATOM 3341 N ILE A 465 36.183 18.529 17.264 1.00 42.73 N ANISOU 3341 N ILE A 465 5890 4963 5384 -1497 -414 267 N ATOM 3342 CA ILE A 465 37.396 18.472 18.078 1.00 43.40 C ANISOU 3342 CA ILE A 465 5877 5156 5455 -1711 -561 288 C ATOM 3343 C ILE A 465 37.907 19.870 18.432 1.00 47.03 C ANISOU 3343 C ILE A 465 6589 5477 5805 -1984 -637 277 C ATOM 3344 O ILE A 465 38.172 20.165 19.601 1.00 48.73 O ANISOU 3344 O ILE A 465 6944 5644 5926 -2112 -755 244 O ATOM 3345 CB ILE A 465 38.518 17.690 17.361 1.00 42.40 C ANISOU 3345 CB ILE A 465 5383 5278 5448 -1764 -574 364 C ATOM 3346 CG1 ILE A 465 38.151 16.206 17.250 1.00 41.10 C ANISOU 3346 CG1 ILE A 465 4998 5240 5379 -1512 -526 368 C ATOM 3347 CG2 ILE A 465 39.856 17.869 18.077 1.00 42.54 C ANISOU 3347 CG2 ILE A 465 5292 5425 5446 -2022 -731 408 C ATOM 3348 CD1 ILE A 465 37.996 15.496 18.588 1.00 40.24 C ANISOU 3348 CD1 ILE A 465 4895 5153 5242 -1444 -620 344 C ATOM 3349 N SER A 466 38.026 20.734 17.430 1.00 47.85 N ANISOU 3349 N SER A 466 6770 5504 5907 -2082 -572 305 N ATOM 3350 CA SER A 466 38.571 22.071 17.653 1.00 52.36 C ANISOU 3350 CA SER A 466 7591 5931 6374 -2369 -644 303 C ATOM 3351 C SER A 466 37.629 22.983 18.434 1.00 52.79 C ANISOU 3351 C SER A 466 8076 5695 6286 -2323 -633 219 C ATOM 3352 O SER A 466 38.081 23.807 19.223 1.00 53.51 O ANISOU 3352 O SER A 466 8401 5668 6262 -2552 -740 189 O ATOM 3353 CB SER A 466 38.932 22.727 16.323 1.00 55.50 C ANISOU 3353 CB SER A 466 7962 6319 6806 -2482 -568 366 C ATOM 3354 OG SER A 466 40.087 22.117 15.780 1.00 59.00 O ANISOU 3354 OG SER A 466 8036 7033 7349 -2601 -599 449 O ATOM 3355 N GLN A 467 36.327 22.844 18.208 1.00 52.35 N ANISOU 3355 N GLN A 467 8130 5530 6231 -2030 -505 184 N ATOM 3356 CA GLN A 467 35.348 23.653 18.929 1.00 52.70 C ANISOU 3356 CA GLN A 467 8569 5313 6141 -1932 -468 110 C ATOM 3357 C GLN A 467 35.346 23.295 20.409 1.00 51.18 C ANISOU 3357 C GLN A 467 8451 5128 5868 -1939 -566 48 C ATOM 3358 O GLN A 467 35.214 24.170 21.264 1.00 52.55 O ANISOU 3358 O GLN A 467 8971 5101 5894 -2025 -607 -15 O ATOM 3359 CB GLN A 467 33.942 23.471 18.354 1.00 52.21 C ANISOU 3359 CB GLN A 467 8547 5185 6106 -1598 -308 106 C ATOM 3360 CG GLN A 467 33.735 24.036 16.963 1.00 54.06 C ANISOU 3360 CG GLN A 467 8797 5362 6380 -1570 -206 162 C ATOM 3361 CD GLN A 467 32.288 23.920 16.517 1.00 56.27 C ANISOU 3361 CD GLN A 467 9132 5581 6667 -1244 -65 165 C ATOM 3362 OE1 GLN A 467 31.997 23.458 15.410 1.00 56.20 O ANISOU 3362 OE1 GLN A 467 8925 5682 6748 -1132 10 219 O ATOM 3363 NE2 GLN A 467 31.368 24.333 17.389 1.00 57.81 N ANISOU 3363 NE2 GLN A 467 9593 5613 6758 -1089 -28 111 N ATOM 3364 N VAL A 468 35.479 22.005 20.708 1.00 49.24 N ANISOU 3364 N VAL A 468 7899 5102 5708 -1843 -602 67 N ATOM 3365 CA VAL A 468 35.553 21.562 22.093 1.00 49.50 C ANISOU 3365 CA VAL A 468 7971 5169 5666 -1856 -703 24 C ATOM 3366 C VAL A 468 36.848 22.077 22.723 1.00 54.42 C ANISOU 3366 C VAL A 468 8640 5819 6218 -2203 -880 29 C ATOM 3367 O VAL A 468 36.844 22.540 23.861 1.00 57.66 O ANISOU 3367 O VAL A 468 9310 6115 6483 -2300 -964 -33 O ATOM 3368 CB VAL A 468 35.461 20.022 22.209 1.00 46.01 C ANISOU 3368 CB VAL A 468 7188 4955 5338 -1680 -705 57 C ATOM 3369 CG1 VAL A 468 35.812 19.563 23.613 1.00 46.66 C ANISOU 3369 CG1 VAL A 468 7283 5100 5345 -1745 -838 34 C ATOM 3370 CG2 VAL A 468 34.066 19.556 21.850 1.00 44.33 C ANISOU 3370 CG2 VAL A 468 6983 4700 5159 -1364 -551 44 C ATOM 3371 N ASN A 469 37.944 22.024 21.971 1.00 56.28 N ANISOU 3371 N ASN A 469 8628 6211 6545 -2397 -934 105 N ATOM 3372 CA ASN A 469 39.229 22.532 22.456 1.00 61.41 C ANISOU 3372 CA ASN A 469 9279 6922 7134 -2757 -1108 132 C ATOM 3373 C ASN A 469 39.194 24.012 22.824 1.00 66.33 C ANISOU 3373 C ASN A 469 10348 7267 7589 -2974 -1146 72 C ATOM 3374 O ASN A 469 39.568 24.388 23.936 1.00 68.32 O ANISOU 3374 O ASN A 469 10792 7461 7705 -3165 -1285 28 O ATOM 3375 CB ASN A 469 40.331 22.304 21.416 1.00 61.05 C ANISOU 3375 CB ASN A 469 8880 7098 7217 -2911 -1127 238 C ATOM 3376 CG ASN A 469 40.854 20.884 21.422 1.00 60.35 C ANISOU 3376 CG ASN A 469 8359 7312 7261 -2798 -1161 304 C ATOM 3377 OD1 ASN A 469 40.625 20.130 22.369 1.00 60.21 O ANISOU 3377 OD1 ASN A 469 8305 7347 7223 -2680 -1218 279 O ATOM 3378 ND2 ASN A 469 41.570 20.512 20.366 1.00 59.37 N ANISOU 3378 ND2 ASN A 469 7913 7383 7263 -2827 -1121 392 N ATOM 3379 N GLU A 470 38.756 24.854 21.893 1.00 67.34 N ANISOU 3379 N GLU A 470 10657 7213 7716 -2949 -1026 70 N ATOM 3380 CA GLU A 470 38.772 26.290 22.142 1.00 71.73 C ANISOU 3380 CA GLU A 470 11660 7481 8114 -3160 -1056 20 C ATOM 3381 C GLU A 470 37.772 26.657 23.231 1.00 70.58 C ANISOU 3381 C GLU A 470 11912 7093 7812 -3000 -1026 -94 C ATOM 3382 O GLU A 470 37.958 27.637 23.947 1.00 72.26 O ANISOU 3382 O GLU A 470 12507 7092 7856 -3204 -1104 -158 O ATOM 3383 CB GLU A 470 38.494 27.081 20.856 1.00 75.65 C ANISOU 3383 CB GLU A 470 12265 7831 8647 -3144 -926 57 C ATOM 3384 CG GLU A 470 37.157 26.813 20.195 1.00 78.27 C ANISOU 3384 CG GLU A 470 12613 8087 9039 -2747 -733 45 C ATOM 3385 CD GLU A 470 36.947 27.649 18.931 1.00 83.62 C ANISOU 3385 CD GLU A 470 13409 8623 9738 -2749 -621 94 C ATOM 3386 OE1 GLU A 470 36.026 27.327 18.142 1.00 82.22 O ANISOU 3386 OE1 GLU A 470 13153 8453 9635 -2455 -475 115 O ATOM 3387 OE2 GLU A 470 37.700 28.630 18.728 1.00 87.40 O ANISOU 3387 OE2 GLU A 470 14066 8989 10154 -3057 -685 118 O ATOM 3388 N LYS A 471 36.721 25.858 23.369 1.00 69.22 N ANISOU 3388 N LYS A 471 11654 6960 7686 -2642 -912 -119 N ATOM 3389 CA LYS A 471 35.739 26.092 24.417 1.00 71.05 C ANISOU 3389 CA LYS A 471 12220 7003 7772 -2460 -866 -216 C ATOM 3390 C LYS A 471 36.334 25.760 25.783 1.00 71.19 C ANISOU 3390 C LYS A 471 12261 7101 7685 -2627 -1035 -257 C ATOM 3391 O LYS A 471 36.111 26.477 26.758 1.00 74.82 O ANISOU 3391 O LYS A 471 13116 7355 7957 -2689 -1069 -346 O ATOM 3392 CB LYS A 471 34.473 25.274 24.165 1.00 71.21 C ANISOU 3392 CB LYS A 471 12101 7082 7875 -2052 -701 -212 C ATOM 3393 CG LYS A 471 33.272 25.799 24.913 1.00 75.15 C ANISOU 3393 CG LYS A 471 12978 7352 8225 -1823 -593 -297 C ATOM 3394 CD LYS A 471 31.970 25.276 24.343 1.00 75.94 C ANISOU 3394 CD LYS A 471 12954 7489 8409 -1442 -411 -269 C ATOM 3395 CE LYS A 471 30.788 25.912 25.062 1.00 79.61 C ANISOU 3395 CE LYS A 471 13797 7733 8718 -1205 -289 -341 C ATOM 3396 NZ LYS A 471 29.484 25.383 24.579 1.00 79.46 N ANISOU 3396 NZ LYS A 471 13632 7785 8774 -839 -119 -299 N ATOM 3397 N ILE A 472 37.098 24.673 25.839 1.00 69.31 N ANISOU 3397 N ILE A 472 11611 7163 7562 -2693 -1138 -189 N ATOM 3398 CA ILE A 472 37.815 24.288 27.050 1.00 70.96 C ANISOU 3398 CA ILE A 472 11784 7492 7684 -2872 -1322 -200 C ATOM 3399 C ILE A 472 38.798 25.379 27.474 1.00 78.13 C ANISOU 3399 C ILE A 472 12945 8294 8449 -3283 -1487 -221 C ATOM 3400 O ILE A 472 38.884 25.717 28.653 1.00 81.37 O ANISOU 3400 O ILE A 472 13629 8609 8679 -3410 -1595 -292 O ATOM 3401 CB ILE A 472 38.566 22.952 26.855 1.00 66.46 C ANISOU 3401 CB ILE A 472 10699 7272 7282 -2865 -1400 -99 C ATOM 3402 CG1 ILE A 472 37.581 21.786 26.874 1.00 61.87 C ANISOU 3402 CG1 ILE A 472 9942 6777 6791 -2492 -1277 -97 C ATOM 3403 CG2 ILE A 472 39.613 22.753 27.937 1.00 68.68 C ANISOU 3403 CG2 ILE A 472 10920 7698 7476 -3131 -1624 -81 C ATOM 3404 CD1 ILE A 472 38.202 20.454 26.531 1.00 59.75 C ANISOU 3404 CD1 ILE A 472 9198 6811 6693 -2437 -1322 0 C ATOM 3405 N ASN A 473 39.521 25.941 26.510 1.00 81.78 N ANISOU 3405 N ASN A 473 13328 8767 8977 -3502 -1506 -159 N ATOM 3406 CA ASN A 473 40.476 27.010 26.795 1.00 87.39 C ANISOU 3406 CA ASN A 473 14252 9392 9559 -3900 -1652 -158 C ATOM 3407 C ASN A 473 39.808 28.278 27.321 1.00 90.94 C ANISOU 3407 C ASN A 473 15243 9501 9809 -3852 -1577 -256 C ATOM 3408 O ASN A 473 40.372 28.981 28.158 1.00 91.88 O ANISOU 3408 O ASN A 473 15560 9581 9770 -4043 -1679 -267 O ATOM 3409 CB ASN A 473 41.298 27.343 25.547 1.00 87.98 C ANISOU 3409 CB ASN A 473 14088 9583 9757 -4066 -1637 -47 C ATOM 3410 CG ASN A 473 42.347 26.291 25.243 1.00 88.84 C ANISOU 3410 CG ASN A 473 13655 10077 10024 -4173 -1740 71 C ATOM 3411 OD1 ASN A 473 42.193 25.123 25.607 1.00 89.33 O ANISOU 3411 OD1 ASN A 473 13460 10319 10162 -4002 -1762 81 O ATOM 3412 ND2 ASN A 473 43.423 26.700 24.578 1.00 90.03 N ANISOU 3412 ND2 ASN A 473 13606 10380 10223 -4386 -1776 176 N ATOM 3413 N GLN A 474 38.607 28.563 26.830 1.00 92.16 N ANISOU 3413 N GLN A 474 15631 9416 9968 -3583 -1393 -316 N ATOM 3414 CA GLN A 474 37.844 29.713 27.304 1.00 96.72 C ANISOU 3414 CA GLN A 474 16710 9678 10361 -3465 -1292 -402 C ATOM 3415 C GLN A 474 37.380 29.515 28.745 1.00 98.21 C ANISOU 3415 C GLN A 474 17116 9812 10388 -3364 -1323 -494 C ATOM 3416 O GLN A 474 37.151 30.482 29.469 1.00100.79 O ANISOU 3416 O GLN A 474 17834 9936 10525 -3364 -1300 -551 O ATOM 3417 CB GLN A 474 36.643 29.977 26.394 1.00 96.93 C ANISOU 3417 CB GLN A 474 16882 9500 10445 -3154 -1077 -422 C ATOM 3418 CG GLN A 474 36.999 30.662 25.086 1.00100.46 C ANISOU 3418 CG GLN A 474 17283 9911 10979 -3254 -1026 -341 C ATOM 3419 CD GLN A 474 35.892 30.560 24.054 1.00102.27 C ANISOU 3419 CD GLN A 474 17523 10021 11313 -2940 -830 -329 C ATOM 3420 OE1 GLN A 474 34.811 30.040 24.338 1.00102.17 O ANISOU 3420 OE1 GLN A 474 17534 9980 11307 -2609 -716 -372 O ATOM 3421 NE2 GLN A 474 36.160 31.047 22.845 1.00103.67 N ANISOU 3421 NE2 GLN A 474 17633 10185 11573 -3010 -781 -249 N ATOM 3422 N SER A 475 37.238 28.259 29.157 1.00 96.84 N ANISOU 3422 N SER A 475 16692 9822 10281 -3274 -1372 -503 N ATOM 3423 CA SER A 475 36.900 27.949 30.541 1.00 97.89 C ANISOU 3423 CA SER A 475 16986 9949 10260 -3197 -1415 -578 C ATOM 3424 C SER A 475 38.145 28.025 31.418 1.00102.40 C ANISOU 3424 C SER A 475 17484 10680 10744 -3523 -1631 -536 C ATOM 3425 O SER A 475 38.070 28.415 32.582 1.00104.12 O ANISOU 3425 O SER A 475 17979 10809 10774 -3549 -1669 -591 O ATOM 3426 CB SER A 475 36.256 26.566 30.650 1.00 93.96 C ANISOU 3426 CB SER A 475 16176 9650 9877 -2906 -1355 -561 C ATOM 3427 OG SER A 475 34.991 26.537 30.013 1.00 92.09 O ANISOU 3427 OG SER A 475 15969 9313 9710 -2527 -1121 -568 O ATOM 3428 N LEU A 476 39.290 27.655 30.851 1.00105.20 N ANISOU 3428 N LEU A 476 17456 11282 11235 -3761 -1762 -428 N ATOM 3429 CA LEU A 476 40.557 27.693 31.576 1.00110.76 C ANISOU 3429 CA LEU A 476 18032 12176 11876 -4066 -1965 -361 C ATOM 3430 C LEU A 476 41.090 29.118 31.707 1.00120.31 C ANISOU 3430 C LEU A 476 19556 13217 12939 -4300 -1994 -359 C ATOM 3431 O LEU A 476 41.757 29.453 32.688 1.00123.85 O ANISOU 3431 O LEU A 476 20115 13699 13245 -4507 -2130 -350 O ATOM 3432 CB LEU A 476 41.598 26.807 30.886 1.00107.34 C ANISOU 3432 CB LEU A 476 17055 12088 11642 -4202 -2074 -231 C ATOM 3433 CG LEU A 476 41.763 25.393 31.446 1.00103.40 C ANISOU 3433 CG LEU A 476 16214 11861 11214 -4123 -2177 -194 C ATOM 3434 CD1 LEU A 476 40.458 24.649 31.371 1.00 99.95 C ANISOU 3434 CD1 LEU A 476 15833 11330 10814 -3802 -2051 -278 C ATOM 3435 CD2 LEU A 476 42.846 24.635 30.699 1.00101.81 C ANISOU 3435 CD2 LEU A 476 15477 11999 11209 -4234 -2264 -50 C ATOM 3436 N ALA A 477 40.800 29.952 30.712 1.00124.08 N ANISOU 3436 N ALA A 477 20182 13513 13447 -4271 -1870 -361 N ATOM 3437 CA ALA A 477 41.190 31.357 30.755 1.00130.08 C ANISOU 3437 CA ALA A 477 21281 14084 14060 -4473 -1883 -362 C ATOM 3438 C ALA A 477 40.416 32.085 31.849 1.00137.82 C ANISOU 3438 C ALA A 477 22769 14783 14811 -4363 -1827 -473 C ATOM 3439 O ALA A 477 40.957 32.959 32.525 1.00139.19 O ANISOU 3439 O ALA A 477 23209 14866 14813 -4587 -1916 -477 O ATOM 3440 CB ALA A 477 40.962 32.020 29.406 1.00126.73 C ANISOU 3440 CB ALA A 477 20898 13531 13722 -4430 -1752 -334 C ATOM 3441 N PHE A 478 39.149 31.713 32.021 1.00142.76 N ANISOU 3441 N PHE A 478 23527 15281 15434 -4014 -1674 -557 N ATOM 3442 CA PHE A 478 38.328 32.258 33.098 1.00145.59 C ANISOU 3442 CA PHE A 478 24329 15403 15583 -3855 -1596 -658 C ATOM 3443 C PHE A 478 38.896 31.834 34.454 1.00145.69 C ANISOU 3443 C PHE A 478 24329 15549 15476 -4017 -1762 -667 C ATOM 3444 O PHE A 478 38.676 32.501 35.464 1.00149.14 O ANISOU 3444 O PHE A 478 25147 15813 15708 -4028 -1757 -728 O ATOM 3445 CB PHE A 478 36.867 31.805 32.962 1.00146.00 C ANISOU 3445 CB PHE A 478 24453 15346 15673 -3426 -1390 -727 C ATOM 3446 CG PHE A 478 36.136 32.420 31.790 1.00147.32 C ANISOU 3446 CG PHE A 478 24727 15333 15913 -3225 -1206 -723 C ATOM 3447 CD1 PHE A 478 36.649 33.528 31.132 1.00150.15 C ANISOU 3447 CD1 PHE A 478 25233 15570 16245 -3409 -1215 -682 C ATOM 3448 CD2 PHE A 478 34.930 31.889 31.352 1.00145.84 C ANISOU 3448 CD2 PHE A 478 24490 15106 15814 -2850 -1024 -751 C ATOM 3449 CE1 PHE A 478 35.976 34.092 30.058 1.00150.66 C ANISOU 3449 CE1 PHE A 478 25395 15478 16373 -3217 -1051 -669 C ATOM 3450 CE2 PHE A 478 34.252 32.449 30.278 1.00146.21 C ANISOU 3450 CE2 PHE A 478 24621 15003 15929 -2654 -858 -732 C ATOM 3451 CZ PHE A 478 34.777 33.552 29.631 1.00148.55 C ANISOU 3451 CZ PHE A 478 25065 15179 16199 -2835 -873 -691 C ATOM 3452 N ILE A 479 39.627 30.722 34.466 1.00139.58 N ANISOU 3452 N ILE A 479 23115 15087 14832 -4134 -1906 -598 N ATOM 3453 CA ILE A 479 40.337 30.277 35.661 1.00136.75 C ANISOU 3453 CA ILE A 479 22682 14899 14379 -4314 -2087 -578 C ATOM 3454 C ILE A 479 41.713 30.935 35.747 1.00139.68 C ANISOU 3454 C ILE A 479 23014 15361 14698 -4713 -2265 -493 C ATOM 3455 O ILE A 479 41.863 32.127 35.478 1.00142.92 O ANISOU 3455 O ILE A 479 23714 15574 15015 -4845 -2236 -501 O ATOM 3456 CB ILE A 479 40.508 28.740 35.692 1.00132.45 C ANISOU 3456 CB ILE A 479 21671 14666 13989 -4236 -2166 -528 C ATOM 3457 CG1 ILE A 479 39.364 28.084 36.470 1.00130.00 C ANISOU 3457 CG1 ILE A 479 21493 14293 13607 -3930 -2070 -619 C ATOM 3458 CG2 ILE A 479 41.835 28.361 36.326 1.00134.61 C ANISOU 3458 CG2 ILE A 479 21682 15213 14251 -4533 -2397 -431 C ATOM 3459 CD1 ILE A 479 38.228 27.576 35.608 1.00126.11 C ANISOU 3459 CD1 ILE A 479 20934 13738 13242 -3597 -1882 -660 C TER 3460 ILE A 479 HETATM 3461 S SO4 A 601 20.964 9.115 13.941 1.00120.09 S HETATM 3462 O1 SO4 A 601 22.335 9.211 13.451 1.00119.50 O HETATM 3463 O2 SO4 A 601 20.080 9.895 13.079 1.00121.33 O HETATM 3464 O3 SO4 A 601 20.547 7.716 13.919 1.00120.72 O HETATM 3465 O4 SO4 A 601 20.886 9.634 15.305 1.00120.36 O HETATM 3466 S SO4 A 602 37.100 -11.904 11.523 1.00 90.31 S HETATM 3467 O1 SO4 A 602 37.865 -10.902 10.785 1.00 90.04 O HETATM 3468 O2 SO4 A 602 35.717 -11.895 11.058 1.00 90.84 O HETATM 3469 O3 SO4 A 602 37.146 -11.615 12.957 1.00 88.38 O HETATM 3470 O4 SO4 A 602 37.670 -13.222 11.264 1.00 91.66 O HETATM 3471 S SO4 A 603 24.877 -4.983 -10.191 1.00103.07 S HETATM 3472 O1 SO4 A 603 24.868 -4.561 -11.589 1.00103.45 O HETATM 3473 O2 SO4 A 603 24.148 -6.243 -10.076 1.00103.53 O HETATM 3474 O3 SO4 A 603 26.253 -5.158 -9.731 1.00102.75 O HETATM 3475 O4 SO4 A 603 24.231 -3.967 -9.367 1.00103.53 O HETATM 3476 S SO4 A 604 -2.905 -3.454 -25.672 1.00130.86 S HETATM 3477 O1 SO4 A 604 -1.588 -2.842 -25.829 1.00130.84 O HETATM 3478 O2 SO4 A 604 -3.328 -4.028 -26.945 1.00131.43 O HETATM 3479 O3 SO4 A 604 -3.865 -2.437 -25.263 1.00130.93 O HETATM 3480 O4 SO4 A 604 -2.847 -4.503 -24.656 1.00130.57 O HETATM 3481 S SO4 A 605 -0.801 2.627 -2.495 1.00123.17 S HETATM 3482 O1 SO4 A 605 -0.535 2.717 -3.927 1.00123.20 O HETATM 3483 O2 SO4 A 605 -2.230 2.417 -2.284 1.00123.33 O HETATM 3484 O3 SO4 A 605 -0.065 1.501 -1.929 1.00123.68 O HETATM 3485 O4 SO4 A 605 -0.374 3.861 -1.839 1.00123.06 O HETATM 3486 S SO4 A 606 30.013 -17.556 10.985 1.00150.79 S HETATM 3487 O1 SO4 A 606 31.096 -18.382 10.454 1.00150.92 O HETATM 3488 O2 SO4 A 606 29.676 -16.518 10.010 1.00150.81 O HETATM 3489 O3 SO4 A 606 28.844 -18.399 11.244 1.00150.72 O HETATM 3490 O4 SO4 A 606 30.450 -16.930 12.229 1.00151.04 O HETATM 3491 S SO4 A 607 29.369 -22.329 14.856 1.00149.22 S HETATM 3492 O1 SO4 A 607 29.302 -23.456 13.924 1.00149.50 O HETATM 3493 O2 SO4 A 607 30.385 -21.379 14.403 1.00149.19 O HETATM 3494 O3 SO4 A 607 29.729 -22.826 16.179 1.00149.16 O HETATM 3495 O4 SO4 A 607 28.067 -21.660 14.905 1.00148.94 O HETATM 3496 C3' NHE A 608 20.741 16.871 17.050 1.00 89.57 C HETATM 3497 C2' NHE A 608 20.499 15.791 16.006 1.00 89.35 C HETATM 3498 C1' NHE A 608 19.238 15.006 16.302 1.00 88.93 C HETATM 3499 C6' NHE A 608 19.254 14.432 17.705 1.00 88.81 C HETATM 3500 N NHE A 608 19.094 13.951 15.339 1.00 88.65 N HETATM 3501 C1 NHE A 608 18.132 14.402 14.376 1.00 89.20 C HETATM 3502 C2 NHE A 608 17.835 13.296 13.292 1.00179.35 C HETATM 3503 S NHE A 608 18.296 13.957 11.669 1.00 89.97 S HETATM 3504 O1 NHE A 608 19.719 13.646 11.383 1.00 90.33 O HETATM 3505 O2 NHE A 608 17.385 13.422 10.576 1.00 90.09 O HETATM 3506 O3 NHE A 608 18.300 15.467 11.685 1.00 88.60 O HETATM 3507 C5' NHE A 608 19.506 15.485 18.750 1.00 88.78 C HETATM 3508 C4' NHE A 608 20.748 16.326 18.451 1.00 89.04 C HETATM 3509 C3' NHE A 609 44.416 17.575 22.510 1.00 72.62 C HETATM 3510 C2' NHE A 609 43.794 18.645 23.389 1.00 73.61 C HETATM 3511 C1' NHE A 609 43.396 18.073 24.732 1.00 74.47 C HETATM 3512 C6' NHE A 609 42.397 16.947 24.557 1.00 73.16 C HETATM 3513 N NHE A 609 42.826 19.112 25.539 1.00 76.21 N HETATM 3514 C1 NHE A 609 42.925 18.735 26.919 1.00 76.76 C HETATM 3515 C2 NHE A 609 42.640 19.995 27.824 1.00114.47 C HETATM 3516 S NHE A 609 41.913 19.452 29.391 1.00 77.50 S HETATM 3517 O1 NHE A 609 42.723 18.368 30.006 1.00 76.10 O HETATM 3518 O2 NHE A 609 40.594 18.759 29.166 1.00 77.87 O HETATM 3519 O3 NHE A 609 41.751 20.632 30.334 1.00 77.59 O HETATM 3520 C5' NHE A 609 42.973 15.852 23.705 1.00 72.51 C HETATM 3521 C4' NHE A 609 43.549 16.358 22.378 1.00 72.25 C HETATM 3522 CL CL A 610 -20.929 -17.609 -24.408 0.50 48.48 CL HETATM 3523 CL CL A 611 15.568 17.339 -8.062 1.00 41.73 CL HETATM 3524 CL CL A 612 22.538 1.078 5.274 1.00 82.77 CL HETATM 3525 CL CL A 613 27.630 -13.454 2.539 1.00 94.77 CL HETATM 3526 CL CL A 614 31.535 24.865 29.248 1.00100.95 CL HETATM 3527 O HOH A 701 1.408 3.243 -5.266 1.00 59.83 O HETATM 3528 O HOH A 702 41.800 21.246 24.957 1.00 63.46 O HETATM 3529 O HOH A 703 22.835 13.139 -13.414 1.00 42.35 O HETATM 3530 O HOH A 704 15.094 -14.876 18.755 1.00 42.77 O HETATM 3531 O HOH A 705 12.953 11.356 -3.984 1.00 45.39 O HETATM 3532 O HOH A 706 -4.151 -0.504 -7.202 1.00 51.10 O HETATM 3533 O HOH A 707 24.764 4.243 24.072 1.00 45.47 O HETATM 3534 O HOH A 708 28.818 17.431 15.146 1.00 45.47 O HETATM 3535 O HOH A 709 -5.137 10.922 -2.480 1.00 46.08 O HETATM 3536 O HOH A 710 38.837 18.489 21.561 1.00 44.00 O HETATM 3537 O HOH A 711 24.852 -12.369 24.247 1.00 45.92 O HETATM 3538 O HOH A 712 -10.676 -4.897 -11.483 1.00 57.14 O HETATM 3539 O HOH A 713 -10.142 2.695 -9.865 1.00 38.64 O HETATM 3540 O HOH A 714 -14.193 2.726 -11.505 1.00 38.78 O HETATM 3541 O HOH A 715 28.208 -3.117 32.821 1.00 45.16 O HETATM 3542 O HOH A 716 2.976 3.292 -8.310 1.00 37.98 O HETATM 3543 O HOH A 717 38.453 12.014 30.966 1.00 45.63 O HETATM 3544 O HOH A 718 -18.463 -6.873 -14.961 1.00 57.92 O HETATM 3545 O HOH A 719 16.856 -3.204 -19.908 1.00 41.95 O HETATM 3546 O HOH A 720 40.138 16.823 13.983 1.00 42.70 O HETATM 3547 O HOH A 721 33.706 -12.733 16.596 1.00 52.61 O HETATM 3548 O HOH A 722 21.177 -0.737 31.832 1.00 47.27 O HETATM 3549 O HOH A 723 8.537 18.497 -5.851 1.00 42.05 O HETATM 3550 O HOH A 724 22.798 0.706 10.189 1.00 50.07 O HETATM 3551 O HOH A 725 -10.268 4.320 -7.559 1.00 44.84 O HETATM 3552 O HOH A 726 38.411 7.493 14.608 1.00 47.10 O HETATM 3553 O HOH A 727 -4.267 -5.854 -14.422 1.00 54.90 O HETATM 3554 O HOH A 728 23.314 23.249 6.398 1.00 39.25 O HETATM 3555 O HOH A 729 21.070 7.273 17.755 1.00 50.49 O HETATM 3556 O HOH A 730 27.271 14.937 -2.400 1.00 40.38 O HETATM 3557 O HOH A 731 24.933 3.492 20.052 1.00 40.58 O HETATM 3558 O HOH A 732 22.721 -13.263 13.237 1.00 36.21 O HETATM 3559 O HOH A 733 36.740 2.441 23.494 1.00 43.75 O HETATM 3560 O HOH A 734 25.422 -1.493 8.623 1.00 45.59 O HETATM 3561 O HOH A 735 -11.661 -5.059 -14.075 1.00 43.90 O HETATM 3562 O HOH A 736 23.119 15.220 -8.211 1.00 33.48 O HETATM 3563 O HOH A 737 26.547 -6.749 6.257 1.00 53.68 O HETATM 3564 O HOH A 738 21.748 -9.197 7.451 1.00 40.33 O HETATM 3565 O HOH A 739 2.751 -2.837 -22.913 1.00 54.92 O HETATM 3566 O HOH A 740 -11.710 0.774 -5.701 1.00 55.77 O HETATM 3567 O HOH A 741 15.826 8.329 -4.545 1.00 46.18 O HETATM 3568 O HOH A 742 34.441 20.092 10.217 1.00 59.62 O HETATM 3569 O HOH A 743 25.956 18.385 -1.765 1.00 37.79 O HETATM 3570 O HOH A 744 17.658 17.112 1.252 1.00 38.35 O HETATM 3571 O HOH A 745 8.461 22.083 -11.710 1.00 32.00 O HETATM 3572 O HOH A 746 27.012 -5.417 3.414 1.00 56.64 O HETATM 3573 O HOH A 747 37.130 -12.455 15.513 1.00 60.05 O HETATM 3574 O HOH A 748 41.732 -7.474 14.741 1.00 52.21 O HETATM 3575 O HOH A 749 35.120 1.051 0.022 1.00 48.45 O HETATM 3576 O HOH A 750 33.790 -10.087 10.495 1.00 40.03 O HETATM 3577 O HOH A 751 10.466 21.345 -1.810 1.00 47.24 O HETATM 3578 O HOH A 752 -3.499 -5.543 -6.563 1.00 48.41 O HETATM 3579 O HOH A 753 34.746 -5.036 27.116 1.00 58.97 O HETATM 3580 O HOH A 754 24.672 4.045 32.869 1.00 52.63 O HETATM 3581 O HOH A 755 -13.982 5.285 -6.983 1.00 43.56 O HETATM 3582 O HOH A 756 43.910 7.341 21.134 1.00 53.19 O HETATM 3583 O HOH A 757 23.609 7.360 9.656 1.00 48.95 O HETATM 3584 O HOH A 758 9.791 5.027 -2.756 1.00 41.95 O HETATM 3585 O HOH A 759 29.880 5.443 32.351 1.00 39.08 O HETATM 3586 O HOH A 760 28.073 11.893 23.337 1.00 39.37 O HETATM 3587 O HOH A 761 22.996 -16.217 19.864 1.00 49.94 O HETATM 3588 O HOH A 762 45.492 -2.686 17.018 1.00 54.05 O HETATM 3589 O HOH A 763 22.827 -16.333 24.684 1.00 50.89 O HETATM 3590 O HOH A 764 15.235 17.658 0.055 1.00 38.12 O HETATM 3591 O HOH A 765 18.941 -0.420 20.108 1.00 42.52 O HETATM 3592 O HOH A 766 3.807 -3.561 -8.303 1.00 44.54 O HETATM 3593 O HOH A 767 22.751 -12.271 22.883 1.00 40.83 O HETATM 3594 O HOH A 768 28.287 -6.189 30.782 1.00 32.76 O HETATM 3595 O HOH A 769 34.967 -0.153 -2.515 1.00 48.82 O HETATM 3596 O HOH A 770 20.050 8.680 -0.065 1.00 53.89 O HETATM 3597 O HOH A 771 32.408 -12.773 8.683 1.00 52.08 O HETATM 3598 O HOH A 772 30.628 13.895 7.686 1.00 45.76 O HETATM 3599 O HOH A 773 25.401 11.827 10.761 1.00 35.85 O HETATM 3600 O HOH A 774 26.692 -7.213 11.961 1.00 39.83 O HETATM 3601 O HOH A 775 38.173 16.842 -1.882 1.00 38.63 O HETATM 3602 O HOH A 776 19.796 -6.477 15.024 1.00 35.07 O HETATM 3603 O HOH A 777 13.686 -7.916 26.924 1.00 38.12 O HETATM 3604 O HOH A 778 32.211 -2.498 26.241 1.00 48.69 O HETATM 3605 O HOH A 779 35.946 2.716 25.989 1.00 38.29 O HETATM 3606 O HOH A 780 35.776 4.625 27.654 1.00 47.16 O HETATM 3607 O HOH A 781 34.745 10.720 8.685 1.00 35.13 O HETATM 3608 O HOH A 782 12.766 16.715 -9.943 1.00 38.24 O HETATM 3609 O HOH A 783 37.330 -4.071 1.382 1.00 45.47 O HETATM 3610 O HOH A 784 35.125 -13.768 9.077 1.00 51.89 O HETATM 3611 O HOH A 785 20.003 15.449 -6.345 1.00 40.27 O HETATM 3612 O HOH A 786 33.764 14.808 10.930 1.00 39.01 O HETATM 3613 O HOH A 787 29.817 7.566 -13.615 1.00 42.50 O HETATM 3614 O HOH A 788 23.499 1.810 32.115 1.00 42.51 O HETATM 3615 O HOH A 789 34.320 10.292 -9.112 1.00 38.02 O HETATM 3616 O HOH A 790 8.252 0.198 -22.506 1.00 59.44 O HETATM 3617 O HOH A 791 21.251 11.201 4.275 1.00 31.67 O HETATM 3618 O HOH A 792 20.345 0.802 27.836 1.00 40.86 O HETATM 3619 O HOH A 793 31.762 7.884 18.474 1.00 32.64 O HETATM 3620 O HOH A 794 38.169 5.631 -0.796 1.00 57.24 O HETATM 3621 O HOH A 795 22.201 18.931 1.086 1.00 35.95 O HETATM 3622 O HOH A 796 11.326 -5.981 -21.952 1.00 57.27 O HETATM 3623 O HOH A 797 41.722 8.677 15.922 1.00 53.90 O HETATM 3624 O HOH A 798 34.356 12.690 13.734 1.00 42.47 O HETATM 3625 O HOH A 799 41.600 2.928 17.804 1.00 38.60 O HETATM 3626 O HOH A 800 28.293 -12.904 31.957 1.00 40.36 O HETATM 3627 O HOH A 801 26.461 5.119 34.936 1.00 60.90 O HETATM 3628 O HOH A 802 34.019 26.551 20.232 1.00 49.10 O HETATM 3629 O HOH A 803 32.229 15.726 9.016 1.00 43.87 O HETATM 3630 O HOH A 804 15.870 -9.246 18.363 1.00 39.23 O HETATM 3631 O HOH A 805 22.031 -8.386 28.531 1.00 47.76 O HETATM 3632 O HOH A 806 -12.257 4.344 -10.496 1.00 54.01 O HETATM 3633 O HOH A 807 20.972 5.821 -15.030 1.00 38.41 O HETATM 3634 O HOH A 808 21.293 -5.082 31.984 1.00 37.68 O HETATM 3635 O HOH A 809 37.124 11.503 -3.258 1.00 51.12 O HETATM 3636 O HOH A 810 2.784 5.976 -3.791 1.00 55.73 O HETATM 3637 O HOH A 811 15.121 12.886 -4.134 1.00 39.71 O HETATM 3638 O HOH A 812 36.808 11.341 -6.088 1.00 59.05 O HETATM 3639 O HOH A 813 27.848 5.118 -16.616 1.00 58.44 O HETATM 3640 O HOH A 814 17.687 -6.217 32.974 1.00 50.45 O HETATM 3641 O HOH A 815 18.875 23.574 5.423 1.00 52.10 O HETATM 3642 O HOH A 816 10.821 16.966 -2.291 1.00 47.55 O HETATM 3643 O HOH A 817 26.341 22.395 19.348 1.00 48.05 O HETATM 3644 O HOH A 818 41.951 19.960 11.938 1.00 62.71 O HETATM 3645 O HOH A 819 0.386 -4.900 -14.252 1.00 55.26 O HETATM 3646 O HOH A 820 21.732 2.070 30.055 1.00 41.74 O HETATM 3647 O HOH A 821 35.095 -14.564 27.172 1.00 40.41 O HETATM 3648 O HOH A 822 41.062 4.157 3.186 1.00 63.04 O HETATM 3649 O HOH A 823 -1.779 -3.853 -19.900 1.00 52.05 O HETATM 3650 O HOH A 824 25.741 4.776 9.943 1.00 37.49 O HETATM 3651 O HOH A 825 13.205 8.919 -5.410 1.00 50.49 O HETATM 3652 O HOH A 826 41.974 9.671 3.302 1.00 61.00 O HETATM 3653 O HOH A 827 25.203 10.137 21.245 1.00 51.72 O HETATM 3654 O HOH A 828 30.357 2.979 33.137 1.00 48.98 O HETATM 3655 O HOH A 829 20.605 23.533 7.692 1.00 56.01 O HETATM 3656 O HOH A 830 23.610 -3.039 10.054 1.00 47.80 O HETATM 3657 O HOH A 831 -2.656 15.468 -9.522 1.00 52.71 O HETATM 3658 O HOH A 832 25.971 4.436 13.883 1.00 33.65 O HETATM 3659 O HOH A 833 23.581 15.532 -12.088 1.00 47.36 O HETATM 3660 O HOH A 834 -25.534 -10.193 -14.668 1.00 56.60 O HETATM 3661 O HOH A 835 34.400 8.901 6.976 1.00 38.35 O HETATM 3662 O HOH A 836 36.100 -9.925 17.413 1.00 43.74 O HETATM 3663 O HOH A 837 16.295 19.212 4.871 1.00 46.98 O HETATM 3664 O HOH A 838 22.770 1.215 34.866 1.00 42.80 O HETATM 3665 O HOH A 839 33.781 20.460 -3.334 1.00 52.37 O HETATM 3666 O HOH A 840 29.565 2.225 -20.735 1.00 71.58 O HETATM 3667 O HOH A 841 -4.470 -4.551 -18.864 1.00 44.79 O HETATM 3668 O HOH A 842 -14.100 -1.502 -8.431 1.00 71.09 O HETATM 3669 O HOH A 843 24.288 24.288 24.288 0.33 52.92 O HETATM 3670 O HOH A 844 37.138 21.220 8.789 1.00 54.21 O HETATM 3671 O HOH A 845 -13.123 -3.325 -9.366 1.00 56.25 O HETATM 3672 O HOH A 846 25.642 2.959 37.694 1.00 52.22 O HETATM 3673 O HOH A 847 16.187 -9.803 25.217 1.00 39.18 O HETATM 3674 O HOH A 848 38.821 20.388 5.542 1.00 60.34 O HETATM 3675 O HOH A 849 41.413 21.911 10.492 1.00 57.55 O HETATM 3676 O HOH A 850 5.960 -8.083 -17.063 1.00 57.12 O HETATM 3677 O HOH A 851 46.699 4.884 21.335 1.00 65.10 O HETATM 3678 O HOH A 852 42.495 22.967 18.133 1.00 64.74 O HETATM 3679 O HOH A 853 24.176 -9.494 5.781 1.00 49.18 O HETATM 3680 O HOH A 854 -13.292 1.148 -9.602 1.00 48.75 O HETATM 3681 O HOH A 855 -11.384 16.081 -23.864 1.00 64.75 O HETATM 3682 O HOH A 856 40.034 20.134 0.277 1.00 46.64 O HETATM 3683 O HOH A 857 15.357 15.439 -5.199 1.00 67.24 O HETATM 3684 O HOH A 858 34.943 20.437 -0.866 1.00 51.47 O HETATM 3685 O HOH A 859 23.177 2.599 36.967 1.00 41.52 O HETATM 3686 O HOH A 860 35.357 8.783 -7.530 1.00 44.18 O HETATM 3687 O HOH A 861 42.090 6.364 1.713 1.00 64.38 O HETATM 3688 O HOH A 862 -4.410 0.858 -4.932 1.00 56.43 O HETATM 3689 O HOH A 863 13.956 -5.275 -23.194 1.00 60.68 O HETATM 3690 O HOH A 864 24.724 3.444 11.946 1.00 39.94 O HETATM 3691 O HOH A 865 15.156 15.156 15.156 0.33 61.38 O HETATM 3692 O HOH A 866 20.830 2.557 9.867 1.00 46.76 O HETATM 3693 O HOH A 867 37.565 -8.371 16.339 1.00 46.91 O HETATM 3694 O HOH A 868 2.432 -7.202 -14.041 1.00 52.39 O HETATM 3695 O HOH A 869 21.517 2.325 39.001 1.00 51.25 O HETATM 3696 O HOH A 870 22.317 -4.092 40.503 1.00 42.47 O HETATM 3697 O HOH A 871 37.057 7.021 -7.351 1.00 47.45 O HETATM 3698 O HOH A 872 46.962 7.207 21.570 1.00 69.89 O HETATM 3699 O HOH A 873 37.392 3.093 0.915 1.00 48.17 O CONECT 92 2928 CONECT 339 1160 CONECT 1160 339 CONECT 1960 2202 CONECT 2035 2114 CONECT 2114 2035 CONECT 2202 1960 CONECT 2320 2394 CONECT 2394 2320 CONECT 2505 2597 CONECT 2597 2505 CONECT 2756 2803 CONECT 2803 2756 CONECT 2928 92 CONECT 3461 3462 3463 3464 3465 CONECT 3462 3461 CONECT 3463 3461 CONECT 3464 3461 CONECT 3465 3461 CONECT 3466 3467 3468 3469 3470 CONECT 3467 3466 CONECT 3468 3466 CONECT 3469 3466 CONECT 3470 3466 CONECT 3471 3472 3473 3474 3475 CONECT 3472 3471 CONECT 3473 3471 CONECT 3474 3471 CONECT 3475 3471 CONECT 3476 3477 3478 3479 3480 CONECT 3477 3476 CONECT 3478 3476 CONECT 3479 3476 CONECT 3480 3476 CONECT 3481 3482 3483 3484 3485 CONECT 3482 3481 CONECT 3483 3481 CONECT 3484 3481 CONECT 3485 3481 CONECT 3486 3487 3488 3489 3490 CONECT 3487 3486 CONECT 3488 3486 CONECT 3489 3486 CONECT 3490 3486 CONECT 3491 3492 3493 3494 3495 CONECT 3492 3491 CONECT 3493 3491 CONECT 3494 3491 CONECT 3495 3491 CONECT 3496 3497 3508 CONECT 3497 3496 3498 CONECT 3498 3497 3499 3500 CONECT 3499 3498 3507 CONECT 3500 3498 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 3505 3506 CONECT 3504 3503 CONECT 3505 3503 CONECT 3506 3503 CONECT 3507 3499 3508 CONECT 3508 3496 3507 CONECT 3509 3510 3521 CONECT 3510 3509 3511 CONECT 3511 3510 3512 3513 CONECT 3512 3511 3520 CONECT 3513 3511 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 3518 3519 CONECT 3517 3516 CONECT 3518 3516 CONECT 3519 3516 CONECT 3520 3512 3521 CONECT 3521 3509 3520 MASTER 577 0 14 16 29 0 15 6 3689 1 75 38 END If you find results from this site helpful for your research, please cite one of our papers:
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