HEADER SIGNALING PROTEIN, HYDROLASE 24-DEC-14 4XES TITLE STRUCTURE OF ACTIVE-LIKE NEUROTENSIN RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1, ENDOLYSIN CHIMERA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 43-396 (P20789), RESIDUES 2-161 (P00720); COMPND 5 SYNONYM: NTR1, HIGH-AFFINITY LEVOCABASTINE-INSENSITIVE NEUROTENSIN COMPND 6 RECEPTOR, NTRH,LYSIS PROTEIN, LYSOZYME, MURAMIDASE; COMPND 7 EC: 3.2.1.17; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: NEUROTENSIN/NEUROMEDIN N; COMPND 12 CHAIN: B; COMPND 13 FRAGMENT: UNP RESIDUES 157-162; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: RAT; SOURCE 4 ORGANISM_TAXID: 10116, 10665; SOURCE 5 GENE: NTSR1, NTSR; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: CABBAGE LOOPER; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 14 ORGANISM_COMMON: RAT; SOURCE 15 ORGANISM_TAXID: 10116 KEYWDS MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, NEUROTENSIN KEYWDS 2 RECEPTOR, NTSR1, SIGNALING PROTEIN, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR B.E.KRUMM,J.F.WHITE,P.SHAH,R.GRISSHAMMER REVDAT 3 27-NOV-19 4XES 1 REMARK REVDAT 2 05-AUG-15 4XES 1 JRNL REVDAT 1 29-JUL-15 4XES 0 JRNL AUTH B.E.KRUMM,J.F.WHITE,P.SHAH,R.GRISSHAMMER JRNL TITL STRUCTURAL PREREQUISITES FOR G-PROTEIN ACTIVATION BY THE JRNL TITL 2 NEUROTENSIN RECEPTOR. JRNL REF NAT COMMUN V. 6 7895 2015 JRNL REFN ESSN 2041-1723 JRNL PMID 26205105 JRNL DOI 10.1038/NCOMMS8895 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0073 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 21352 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.232 REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400 REMARK 3 FREE R VALUE TEST SET COUNT : 1209 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1510 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70 REMARK 3 BIN R VALUE (WORKING SET) : 0.3810 REMARK 3 BIN FREE R VALUE SET COUNT : 89 REMARK 3 BIN FREE R VALUE : 0.3560 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3772 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 96 REMARK 3 SOLVENT ATOMS : 55 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 42.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.63 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.20000 REMARK 3 B22 (A**2) : -3.39000 REMARK 3 B33 (A**2) : 3.58000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.474 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.312 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.287 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.246 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3793 ; 0.007 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3639 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5137 ; 1.185 ; 1.965 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8267 ; 0.768 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 473 ; 5.208 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;32.142 ;22.254 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 567 ;15.549 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;14.373 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 599 ; 0.064 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4208 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 902 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1904 ; 0.864 ; 2.531 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1903 ; 0.849 ; 2.528 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2372 ; 1.477 ; 3.789 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2373 ; 1.484 ; 3.792 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1888 ; 1.104 ; 2.776 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1888 ; 1.103 ; 2.776 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2765 ; 1.773 ; 4.065 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4361 ; 4.312 ;20.756 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4362 ; 4.312 ;20.772 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 50 A 90 REMARK 3 ORIGIN FOR THE GROUP (A): -8.8253 2.0564 -13.1266 REMARK 3 T TENSOR REMARK 3 T11: 0.7165 T22: 0.3467 REMARK 3 T33: 0.5376 T12: 0.0424 REMARK 3 T13: 0.1290 T23: 0.0340 REMARK 3 L TENSOR REMARK 3 L11: 1.0278 L22: 2.8850 REMARK 3 L33: 1.2978 L12: -0.6071 REMARK 3 L13: 0.8158 L23: -1.3279 REMARK 3 S TENSOR REMARK 3 S11: 0.1016 S12: 0.1525 S13: -0.0196 REMARK 3 S21: 0.0105 S22: -0.0601 S23: 0.7641 REMARK 3 S31: 0.1347 S32: -0.1263 S33: -0.0415 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 91 A 104 REMARK 3 ORIGIN FOR THE GROUP (A): 7.7512 -24.0533 -7.8499 REMARK 3 T TENSOR REMARK 3 T11: 0.7037 T22: 0.5767 REMARK 3 T33: 0.7320 T12: 0.0320 REMARK 3 T13: -0.0546 T23: 0.0901 REMARK 3 L TENSOR REMARK 3 L11: 0.3390 L22: 3.5267 REMARK 3 L33: 0.0354 L12: -0.8428 REMARK 3 L13: 0.0234 L23: 0.1530 REMARK 3 S TENSOR REMARK 3 S11: 0.1033 S12: -0.1032 S13: -0.3321 REMARK 3 S21: 0.0904 S22: 0.0022 S23: 0.1583 REMARK 3 S31: 0.0498 S32: -0.0131 S33: -0.1056 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 105 A 171 REMARK 3 ORIGIN FOR THE GROUP (A): 3.5521 0.1781 -10.7872 REMARK 3 T TENSOR REMARK 3 T11: 0.8002 T22: 0.2124 REMARK 3 T33: 0.3633 T12: 0.0195 REMARK 3 T13: -0.0658 T23: 0.0166 REMARK 3 L TENSOR REMARK 3 L11: 1.0458 L22: 3.4753 REMARK 3 L33: 0.4542 L12: -0.3246 REMARK 3 L13: -0.2196 L23: 0.7504 REMARK 3 S TENSOR REMARK 3 S11: -0.1803 S12: 0.3837 S13: 0.1723 REMARK 3 S21: 0.5115 S22: 0.0625 S23: -0.0149 REMARK 3 S31: -0.0150 S32: 0.0211 S33: 0.1178 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 172 A 188 REMARK 3 ORIGIN FOR THE GROUP (A): 20.5926 -23.0752 -13.2165 REMARK 3 T TENSOR REMARK 3 T11: 0.6692 T22: 0.6624 REMARK 3 T33: 0.6342 T12: -0.0500 REMARK 3 T13: 0.0187 T23: 0.0305 REMARK 3 L TENSOR REMARK 3 L11: 1.3567 L22: 4.4223 REMARK 3 L33: 7.5022 L12: 0.3780 REMARK 3 L13: 1.6917 L23: 5.2868 REMARK 3 S TENSOR REMARK 3 S11: -0.3289 S12: 0.4486 S13: 0.0559 REMARK 3 S21: 0.2122 S22: 0.4002 S23: -0.1380 REMARK 3 S31: -0.1555 S32: 0.9209 S33: -0.0713 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 189 A 250 REMARK 3 ORIGIN FOR THE GROUP (A): 10.9827 10.2558 -12.6295 REMARK 3 T TENSOR REMARK 3 T11: 0.7495 T22: 0.2504 REMARK 3 T33: 0.5245 T12: -0.0347 REMARK 3 T13: -0.1274 T23: -0.0047 REMARK 3 L TENSOR REMARK 3 L11: 2.0001 L22: 2.7941 REMARK 3 L33: 1.7761 L12: -0.4202 REMARK 3 L13: -0.1054 L23: -1.1537 REMARK 3 S TENSOR REMARK 3 S11: -0.1544 S12: 0.0993 S13: 0.2712 REMARK 3 S21: 0.0935 S22: 0.1611 S23: -0.5322 REMARK 3 S31: -0.1287 S32: 0.2497 S33: -0.0068 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 251 A 339 REMARK 3 ORIGIN FOR THE GROUP (A): 6.2679 -9.6101 -26.2894 REMARK 3 T TENSOR REMARK 3 T11: 0.5912 T22: 0.3064 REMARK 3 T33: 0.3780 T12: -0.0083 REMARK 3 T13: 0.0090 T23: 0.0424 REMARK 3 L TENSOR REMARK 3 L11: 0.6639 L22: 4.8145 REMARK 3 L33: 0.6674 L12: -0.8051 REMARK 3 L13: -0.0829 L23: 1.6447 REMARK 3 S TENSOR REMARK 3 S11: -0.0027 S12: 0.2608 S13: 0.1205 REMARK 3 S21: 0.3350 S22: 0.0071 S23: -0.2248 REMARK 3 S31: -0.0039 S32: 0.0735 S33: -0.0044 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 340 A 371 REMARK 3 ORIGIN FOR THE GROUP (A): -3.2711 3.2578 -21.6352 REMARK 3 T TENSOR REMARK 3 T11: 0.5338 T22: 0.3312 REMARK 3 T33: 0.4059 T12: -0.0194 REMARK 3 T13: -0.0341 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 0.7435 L22: 7.2487 REMARK 3 L33: 0.8359 L12: -0.4708 REMARK 3 L13: 0.0947 L23: -2.3584 REMARK 3 S TENSOR REMARK 3 S11: -0.0254 S12: 0.1187 S13: -0.1197 REMARK 3 S21: 0.1165 S22: 0.1836 S23: 0.4280 REMARK 3 S31: 0.1253 S32: -0.1420 S33: -0.1582 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 372 A 382 REMARK 3 ORIGIN FOR THE GROUP (A): -6.0175 -23.3878 -14.2584 REMARK 3 T TENSOR REMARK 3 T11: 0.5167 T22: 0.6383 REMARK 3 T33: 0.5563 T12: -0.0611 REMARK 3 T13: -0.0443 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 1.4079 L22: 7.7423 REMARK 3 L33: 4.6044 L12: -3.0816 REMARK 3 L13: -1.4870 L23: 1.5292 REMARK 3 S TENSOR REMARK 3 S11: -0.0390 S12: 0.0262 S13: -0.0818 REMARK 3 S21: 0.2202 S22: 0.0396 S23: 0.1641 REMARK 3 S31: -0.0663 S32: -0.2584 S33: -0.0005 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 383 A 1053 REMARK 3 ORIGIN FOR THE GROUP (A): 15.3127 -49.3280 -23.8539 REMARK 3 T TENSOR REMARK 3 T11: 0.2202 T22: 0.4076 REMARK 3 T33: 0.3258 T12: -0.0508 REMARK 3 T13: 0.0014 T23: 0.1190 REMARK 3 L TENSOR REMARK 3 L11: 3.5355 L22: 4.5980 REMARK 3 L33: 0.3820 L12: -2.5343 REMARK 3 L13: -0.1397 L23: 0.2820 REMARK 3 S TENSOR REMARK 3 S11: -0.0831 S12: -0.5532 S13: -0.5249 REMARK 3 S21: 0.3612 S22: 0.0769 S23: 0.0520 REMARK 3 S31: -0.0619 S32: 0.2341 S33: 0.0062 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1054 A 1165 REMARK 3 ORIGIN FOR THE GROUP (A): 16.1192 -38.2474 -38.5566 REMARK 3 T TENSOR REMARK 3 T11: 0.0206 T22: 0.0990 REMARK 3 T33: 0.2479 T12: 0.0188 REMARK 3 T13: 0.0196 T23: -0.0197 REMARK 3 L TENSOR REMARK 3 L11: 3.9164 L22: 3.1909 REMARK 3 L33: 3.2105 L12: 0.7820 REMARK 3 L13: -0.5772 L23: -0.9325 REMARK 3 S TENSOR REMARK 3 S11: -0.0286 S12: -0.0169 S13: 0.1262 REMARK 3 S21: 0.1089 S22: 0.0210 S23: -0.1379 REMARK 3 S31: -0.1770 S32: 0.0585 S33: 0.0076 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 4XES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000205522. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-MAR-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0-7.4 REMARK 200 NUMBER OF CRYSTALS USED : 6 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 10 JAN 2014 BUILT=20140307 REMARK 200 DATA SCALING SOFTWARE : XSCALE 4 JUL 2012, REMARK 200 BUILT=20131111 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22591 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 34.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.75000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.5.6 REMARK 200 STARTING MODEL: PDB ENTRY 4GRV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 19.8-23.4% PEG400, 80 MM HEPES, 50 MM REMARK 280 LITHIUM CITRATE, 2 MM TCEP, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 24.92000 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.66500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 24.92000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.66500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4380 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23150 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 33 REMARK 465 TYR A 34 REMARK 465 LYS A 35 REMARK 465 ASP A 36 REMARK 465 ASP A 37 REMARK 465 ASP A 38 REMARK 465 ASP A 39 REMARK 465 ALA A 40 REMARK 465 THR A 41 REMARK 465 SER A 42 REMARK 465 THR A 43 REMARK 465 SER A 44 REMARK 465 GLU A 45 REMARK 465 SER A 46 REMARK 465 ASP A 47 REMARK 465 THR A 48 REMARK 465 HIS A 269 REMARK 465 GLN A 270 REMARK 465 ALA A 271 REMARK 465 ALA A 272 REMARK 465 GLU A 273 REMARK 465 GLN A 274 REMARK 465 GLY A 275 REMARK 465 ARG A 276 REMARK 465 VAL A 277 REMARK 465 CYS A 278 REMARK 465 THR A 279 REMARK 465 VAL A 280 REMARK 465 GLY A 281 REMARK 465 THR A 282 REMARK 465 HIS A 283 REMARK 465 ASN A 284 REMARK 465 GLY A 285 REMARK 465 LEU A 286 REMARK 465 GLU A 287 REMARK 465 HIS A 288 REMARK 465 SER A 289 REMARK 465 THR A 290 REMARK 465 PHE A 291 REMARK 465 ASN A 292 REMARK 465 MET A 293 REMARK 465 THR A 294 REMARK 465 ILE A 295 REMARK 465 GLU A 296 REMARK 465 LEU A 976 REMARK 465 ALA A 977 REMARK 465 CYS A 978 REMARK 465 LEU A 979 REMARK 465 CYS A 980 REMARK 465 PRO A 981 REMARK 465 GLY A 982 REMARK 465 TRP A 983 REMARK 465 ARG A 984 REMARK 465 HIS A 985 REMARK 465 ARG A 986 REMARK 465 ARG A 987 REMARK 465 LYS A 988 REMARK 465 ALA A 989 REMARK 465 HIS A 990 REMARK 465 HIS A 991 REMARK 465 HIS A 992 REMARK 465 HIS A 993 REMARK 465 HIS A 994 REMARK 465 HIS A 995 REMARK 465 HIS A 996 REMARK 465 HIS A 997 REMARK 465 HIS A 998 REMARK 465 HIS A 999 REMARK 465 GLY A 1000 REMARK 465 GLY A 1001 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 SER A 53 CB OG REMARK 480 ASN A 58 OD1 ND2 REMARK 480 ILE A 61 CD1 REMARK 480 TYR A 62 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LYS A 64 NZ REMARK 480 VAL A 65 CG1 CG2 REMARK 480 LEU A 89 CD1 CD2 REMARK 480 ARG A 91 NH1 NH2 REMARK 480 LYS A 92 CD CE NZ REMARK 480 LYS A 93 CB CG CD CE NZ REMARK 480 SER A 94 CB OG REMARK 480 LEU A 95 CB CG CD1 CD2 REMARK 480 GLN A 96 CB CG CD OE1 NE2 REMARK 480 SER A 97 CB OG REMARK 480 LEU A 98 CB CG CD1 CD2 REMARK 480 GLN A 99 CB CG CD OE1 NE2 REMARK 480 TYR A 104 OH REMARK 480 TYR A 126 OH REMARK 480 PHE A 175 CG CD1 CD2 CE1 CE2 CZ REMARK 480 LYS A 176 CG CD CE NZ REMARK 480 LYS A 178 CG CD CE NZ REMARK 480 THR A 179 OG1 CG2 REMARK 480 LEU A 180 CB CG CD1 CD2 REMARK 480 MET A 181 CB CG SD CE REMARK 480 SER A 182 CB OG REMARK 480 ARG A 183 CB CG CD NE CZ NH1 NH2 REMARK 480 SER A 184 OG REMARK 480 ARG A 185 CG CD NE CZ NH1 NH2 REMARK 480 LYS A 187 CG CD CE NZ REMARK 480 LYS A 188 CB CG CD CE NZ REMARK 480 LEU A 210 CD2 REMARK 480 THR A 218 CG2 REMARK 480 ASP A 230 CG OD1 OD2 REMARK 480 LYS A 235 NZ REMARK 480 ILE A 238 CD1 REMARK 480 LEU A 247 CD1 CD2 REMARK 480 LEU A 251 CD1 CD2 REMARK 480 ILE A 334 CD1 REMARK 480 GLU A 337 CB CG CD OE1 OE2 REMARK 480 LEU A 353 CD1 CD2 REMARK 480 ILE A 367 CD1 REMARK 480 ALA A 374 CB REMARK 480 ASN A 375 CB CG OD1 ND2 REMARK 480 ARG A 377 CZ REMARK 480 GLN A 378 CB CG CD OE1 NE2 REMARK 480 VAL A 379 CG1 CG2 REMARK 480 PHE A 380 CB CG CD1 CD2 CE1 CE2 CZ REMARK 480 LEU A 381 CB CG CD1 CD2 REMARK 480 SER A 382 OG REMARK 480 LYS A 1016 CD CE NZ REMARK 480 SER A 1044 OG REMARK 480 LYS A 1048 CD CE NZ REMARK 480 ASN A 1053 CB CG OD1 ND2 REMARK 480 ASN A 1055 OD1 ND2 REMARK 480 LYS A 1065 CD CE NZ REMARK 480 GLN A 1069 CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 C VAL A 268 N ASN A 1002 1.31 REMARK 500 N PRO A 297 C SER A 1165 1.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 58 76.30 -109.37 REMARK 500 MET A 181 122.26 -172.75 REMARK 500 ASP A 216 152.34 -47.88 REMARK 500 THR A 218 92.74 -160.61 REMARK 500 PHE A 246 -61.09 -137.62 REMARK 500 ILE A1029 76.76 -105.81 REMARK 500 ARG A1052 140.84 -174.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A1352 DISTANCE = 5.89 ANGSTROMS REMARK 525 HOH A1353 DISTANCE = 6.15 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 1211 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XEE RELATED DB: PDB DBREF 4XES A 43 988 UNP P20789 NTR1_RAT 43 396 DBREF 4XES A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 4XES B 8 13 UNP P20068 NEUT_RAT 157 162 SEQADV 4XES ASP A 33 UNP P20789 EXPRESSION TAG SEQADV 4XES TYR A 34 UNP P20789 EXPRESSION TAG SEQADV 4XES LYS A 35 UNP P20789 EXPRESSION TAG SEQADV 4XES ASP A 36 UNP P20789 EXPRESSION TAG SEQADV 4XES ASP A 37 UNP P20789 EXPRESSION TAG SEQADV 4XES ASP A 38 UNP P20789 EXPRESSION TAG SEQADV 4XES ASP A 39 UNP P20789 EXPRESSION TAG SEQADV 4XES ALA A 40 UNP P20789 EXPRESSION TAG SEQADV 4XES THR A 41 UNP P20789 EXPRESSION TAG SEQADV 4XES SER A 42 UNP P20789 EXPRESSION TAG SEQADV 4XES LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4XES ALA A 166 UNP P20789 GLU 166 ENGINEERED MUTATION SEQADV 4XES ALA A 215 UNP P20789 GLY 215 ENGINEERED MUTATION SEQADV 4XES ALA A 360 UNP P20789 VAL 360 ENGINEERED MUTATION SEQADV 4XES ALA A 989 UNP P20789 LINKER SEQADV 4XES HIS A 990 UNP P20789 LINKER SEQADV 4XES HIS A 991 UNP P20789 LINKER SEQADV 4XES HIS A 992 UNP P20789 LINKER SEQADV 4XES HIS A 993 UNP P20789 LINKER SEQADV 4XES HIS A 994 UNP P20789 LINKER SEQADV 4XES HIS A 995 UNP P20789 LINKER SEQADV 4XES HIS A 996 UNP P20789 LINKER SEQADV 4XES HIS A 997 UNP P20789 LINKER SEQADV 4XES HIS A 998 UNP P20789 LINKER SEQADV 4XES HIS A 999 UNP P20789 LINKER SEQADV 4XES GLY A 1000 UNP P20789 LINKER SEQADV 4XES GLY A 1001 UNP P20789 LINKER SEQADV 4XES GLY A 1012 UNP P00720 ARG 12 CONFLICT SEQADV 4XES THR A 1054 UNP P00720 CYS 54 CONFLICT SEQADV 4XES ALA A 1097 UNP P00720 CYS 97 CONFLICT SEQADV 4XES ASN A 1122 UNP P00720 GLN 122 CONFLICT SEQADV 4XES ASN A 1123 UNP P00720 GLN 123 CONFLICT SEQADV 4XES ARG A 1137 UNP P00720 ILE 137 CONFLICT SEQADV 4XES GLY A 1162 UNP P00720 EXPRESSION TAG SEQADV 4XES SER A 1163 UNP P00720 EXPRESSION TAG SEQADV 4XES GLY A 1164 UNP P00720 EXPRESSION TAG SEQADV 4XES SER A 1165 UNP P00720 EXPRESSION TAG SEQRES 1 A 541 ASP TYR LYS ASP ASP ASP ASP ALA THR SER THR SER GLU SEQRES 2 A 541 SER ASP THR ALA GLY PRO ASN SER ASP LEU ASP VAL ASN SEQRES 3 A 541 THR ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR SEQRES 4 A 541 LEU ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL SEQRES 5 A 541 THR LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER SEQRES 6 A 541 LEU GLN SER THR VAL HIS TYR HIS LEU GLY SER LEU ALA SEQRES 7 A 541 LEU SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL SEQRES 8 A 541 GLU LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA SEQRES 9 A 541 PHE GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG SEQRES 10 A 541 ASP ALA CYS THR TYR ALA THR ALA LEU ASN VAL ALA SER SEQRES 11 A 541 LEU SER VAL ALA ARG TYR LEU ALA ILE CYS HIS PRO PHE SEQRES 12 A 541 LYS ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS SEQRES 13 A 541 PHE ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA SEQRES 14 A 541 ILE PRO MET LEU PHE THR MET GLY LEU GLN ASN ARG SER SEQRES 15 A 541 ALA ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO SEQRES 16 A 541 ILE VAL ASP THR ALA THR VAL LYS VAL VAL ILE GLN VAL SEQRES 17 A 541 ASN THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ILE SEQRES 18 A 541 SER ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL SEQRES 19 A 541 MET VAL HIS GLN ALA ALA GLU GLN GLY ARG VAL CYS THR SEQRES 20 A 541 VAL GLY THR HIS ASN GLY LEU GLU HIS SER THR PHE ASN SEQRES 21 A 541 MET THR ILE GLU PRO GLY ARG VAL GLN ALA LEU ARG HIS SEQRES 22 A 541 GLY VAL LEU VAL LEU ARG ALA VAL VAL ILE ALA PHE VAL SEQRES 23 A 541 VAL CYS TRP LEU PRO TYR HIS VAL ARG ARG LEU MET PHE SEQRES 24 A 541 CYS TYR ILE SER ASP GLU GLN TRP THR THR PHE LEU PHE SEQRES 25 A 541 ASP PHE TYR HIS TYR PHE TYR MET LEU THR ASN ALA LEU SEQRES 26 A 541 PHE TYR ALA SER SER ALA ILE ASN PRO ILE LEU TYR ASN SEQRES 27 A 541 LEU VAL SER ALA ASN PHE ARG GLN VAL PHE LEU SER THR SEQRES 28 A 541 LEU ALA CYS LEU CYS PRO GLY TRP ARG HIS ARG ARG LYS SEQRES 29 A 541 ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY GLY SEQRES 30 A 541 ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG SEQRES 31 A 541 LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE SEQRES 32 A 541 GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN SEQRES 33 A 541 ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN SEQRES 34 A 541 THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU SEQRES 35 A 541 PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU SEQRES 36 A 541 ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP SEQRES 37 A 541 ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN SEQRES 38 A 541 MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU SEQRES 39 A 541 ARG MET LEU ASN ASN LYS ARG TRP ASP GLU ALA ALA VAL SEQRES 40 A 541 ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN SEQRES 41 A 541 ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR SEQRES 42 A 541 TRP ASP ALA TYR GLY SER GLY SER SEQRES 1 B 6 ARG ARG PRO TYR ILE LEU HET CIT A1201 13 HET PEG A1202 7 HET PEG A1203 7 HET PEG A1204 7 HET PEG A1205 7 HET PEG A1206 7 HET GOL A1207 6 HET GOL A1208 6 HET GOL A1209 6 HET EPE A1210 15 HET EPE A1211 15 HETNAM CIT CITRIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM GOL GLYCEROL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EPE HEPES FORMUL 3 CIT C6 H8 O7 FORMUL 4 PEG 5(C4 H10 O3) FORMUL 9 GOL 3(C3 H8 O3) FORMUL 12 EPE 2(C8 H18 N2 O4 S) FORMUL 14 HOH *55(H2 O) HELIX 1 AA1 ASP A 60 LYS A 93 1 34 HELIX 2 AA2 GLN A 96 ALA A 120 1 25 HELIX 3 AA3 ALA A 120 PHE A 128 1 9 HELIX 4 AA4 PHE A 137 HIS A 173 1 37 HELIX 5 AA5 HIS A 173 MET A 181 1 9 HELIX 6 AA6 SER A 182 ALA A 201 1 20 HELIX 7 AA7 ILE A 202 THR A 207 1 6 HELIX 8 AA8 HIS A 219 GLY A 221 5 3 HELIX 9 AA9 ASP A 230 PHE A 246 1 17 HELIX 10 AB1 PHE A 246 VAL A 268 1 23 HELIX 11 AB2 PRO A 297 ARG A 299 5 3 HELIX 12 AB3 VAL A 300 ILE A 334 1 35 HELIX 13 AB4 SER A 335 TRP A 339 5 5 HELIX 14 AB5 THR A 340 TYR A 369 1 30 HELIX 15 AB6 ASN A 375 SER A 382 1 8 HELIX 16 AB7 ILE A 1003 GLU A 1011 1 9 HELIX 17 AB8 SER A 1038 GLY A 1051 1 14 HELIX 18 AB9 THR A 1059 ARG A 1080 1 22 HELIX 19 AC1 LEU A 1084 SER A 1090 1 7 HELIX 20 AC2 ASP A 1092 GLY A 1107 1 16 HELIX 21 AC3 GLY A 1107 ALA A 1112 1 6 HELIX 22 AC4 PHE A 1114 ASN A 1123 1 10 HELIX 23 AC5 ARG A 1125 ALA A 1134 1 10 HELIX 24 AC6 SER A 1136 THR A 1142 1 7 HELIX 25 AC7 THR A 1142 GLY A 1156 1 15 SHEET 1 AA1 2 MET A 208 ASN A 212 0 SHEET 2 AA1 2 LEU A 223 PRO A 227 -1 O VAL A 224 N GLN A 211 SHEET 1 AA2 3 ARG A1014 LYS A1019 0 SHEET 2 AA2 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA2 3 HIS A1031 LEU A1032 -1 O HIS A1031 N ILE A1027 SSBOND 1 CYS A 142 CYS A 225 1555 1555 2.05 CISPEP 1 HIS A 133 PRO A 134 0 -0.90 SITE 1 AC1 10 ARG A 299 ARG A1008 ILE A1009 PHE A1114 SITE 2 AC1 10 THR A1115 ASN A1116 SER A1117 ASN A1132 SITE 3 AC1 10 SER A1163 SER A1165 SITE 1 AC2 4 CYS A 172 LYS A 263 LEU A1079 PEG A1203 SITE 1 AC3 6 LYS A 263 MET A 267 VAL A1075 TYR A1088 SITE 2 AC3 6 ARG A1096 PEG A1202 SITE 1 AC4 3 LEU A 303 PHE A1004 ASN A1068 SITE 1 AC5 8 ARG A1080 ASN A1081 ALA A1082 GLU A1108 SITE 2 AC5 8 THR A1109 TYR A1139 PRO A1143 ASN A1144 SITE 1 AC6 2 ARG A1125 ARG B 8 SITE 1 AC7 1 TYR A 349 SITE 1 AC8 5 LYS A1083 THR A1142 PRO A1143 ASN A1144 SITE 2 AC8 5 ARG A1145 SITE 1 AC9 8 GLY A1030 HIS A1031 LEU A1032 LYS A1035 SITE 2 AC9 8 ASP A1070 PHE A1104 MET A1106 ASP A1159 SITE 1 AD1 5 ASP A 56 VAL A 57 TRP A 130 HIS A 132 SITE 2 AD1 5 HIS A 133 CRYST1 49.840 88.440 161.330 90.00 90.00 90.00 P 21 2 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.020064 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011307 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006198 0.00000 ATOM 1 N ALA A 49 -13.354 31.982 -16.139 1.00 77.79 N ATOM 2 CA ALA A 49 -11.936 32.423 -16.341 1.00 77.39 C ATOM 3 C ALA A 49 -11.327 33.038 -15.063 1.00 71.53 C ATOM 4 O ALA A 49 -11.432 34.247 -14.819 1.00 71.42 O ATOM 5 CB ALA A 49 -11.841 33.398 -17.514 1.00 77.91 C ATOM 6 N GLY A 50 -10.701 32.181 -14.256 1.00117.60 N ANISOU 6 N GLY A 50 16955 11505 16221 1208 -87 1108 N ATOM 7 CA GLY A 50 -9.993 32.590 -13.042 1.00110.79 C ANISOU 7 CA GLY A 50 16389 10473 15231 1215 -110 1058 C ATOM 8 C GLY A 50 -8.501 32.303 -13.147 1.00103.60 C ANISOU 8 C GLY A 50 15544 9644 14174 1059 -270 1172 C ATOM 9 O GLY A 50 -7.997 32.022 -14.238 1.00101.42 O ANISOU 9 O GLY A 50 15086 9544 13902 960 -373 1306 O ATOM 10 N PRO A 51 -7.779 32.356 -12.013 1.00 97.68 N ANISOU 10 N PRO A 51 15057 8763 13291 1041 -289 1128 N ATOM 11 CA PRO A 51 -6.324 32.231 -12.081 1.00 94.41 C ANISOU 11 CA PRO A 51 14698 8400 12772 890 -471 1263 C ATOM 12 C PRO A 51 -5.836 30.809 -12.391 1.00 90.78 C ANISOU 12 C PRO A 51 14107 8170 12215 812 -360 1296 C ATOM 13 O PRO A 51 -4.676 30.641 -12.783 1.00 90.45 O ANISOU 13 O PRO A 51 14027 8221 12116 692 -499 1446 O ATOM 14 CB PRO A 51 -5.852 32.687 -10.688 1.00 95.51 C ANISOU 14 CB PRO A 51 15178 8303 12805 907 -527 1187 C ATOM 15 CG PRO A 51 -7.084 32.946 -9.877 1.00 97.37 C ANISOU 15 CG PRO A 51 15550 8383 13063 1088 -332 999 C ATOM 16 CD PRO A 51 -8.258 32.393 -10.622 1.00 97.46 C ANISOU 16 CD PRO A 51 15284 8551 13194 1162 -129 961 C ATOM 17 N ASN A 52 -6.702 29.808 -12.212 1.00 87.08 N ANISOU 17 N ASN A 52 13567 7782 11735 884 -115 1170 N ATOM 18 CA ASN A 52 -6.391 28.424 -12.582 1.00 83.58 C ANISOU 18 CA ASN A 52 12993 7548 11212 824 -9 1187 C ATOM 19 C ASN A 52 -7.271 27.923 -13.721 1.00 81.68 C ANISOU 19 C ASN A 52 12492 7468 11072 855 64 1190 C ATOM 20 O ASN A 52 -7.522 26.732 -13.821 1.00 80.74 O ANISOU 20 O ASN A 52 12288 7473 10914 853 207 1140 O ATOM 21 CB ASN A 52 -6.573 27.498 -11.379 1.00 83.39 C ANISOU 21 CB ASN A 52 13118 7482 11082 862 196 1046 C ATOM 22 CG ASN A 52 -5.958 28.057 -10.114 1.00 84.32 C ANISOU 22 CG ASN A 52 13540 7399 11099 861 133 1008 C ATOM 23 OD1 ASN A 52 -4.855 28.609 -10.132 1.00 84.54 O ANISOU 23 OD1 ASN A 52 13653 7381 11088 767 -85 1124 O ATOM 24 ND2 ASN A 52 -6.667 27.915 -9.004 1.00 84.83 N ANISOU 24 ND2 ASN A 52 13774 7335 11120 968 318 856 N ATOM 25 N SER A 53 -7.705 28.831 -14.589 1.00 81.86 N ANISOU 25 N SER A 53 12400 7476 11227 880 -49 1251 N ATOM 26 CA SER A 53 -8.529 28.461 -15.735 1.00 80.08 C ANISOU 26 CA SER A 53 11939 7388 11100 901 -28 1271 C ATOM 27 C SER A 53 -7.725 27.718 -16.802 1.00 77.51 C ANISOU 27 C SER A 53 11498 7275 10675 814 -98 1389 C ATOM 28 O SER A 53 -8.284 26.971 -17.604 1.00 76.56 O ANISOU 28 O SER A 53 11232 7282 10573 828 -45 1371 O ATOM 29 CB SER A 53 -9.188 29.701 -16.343 0.00 20.00 C ATOM 30 OG SER A 53 -8.325 30.332 -17.274 0.00 20.00 O ATOM 31 N ASP A 54 -6.412 27.929 -16.806 1.00 75.95 N ANISOU 31 N ASP A 54 11372 7109 10376 732 -221 1516 N ATOM 32 CA ASP A 54 -5.529 27.296 -17.783 1.00 74.42 C ANISOU 32 CA ASP A 54 11078 7116 10081 670 -274 1653 C ATOM 33 C ASP A 54 -5.198 25.856 -17.465 1.00 72.84 C ANISOU 33 C ASP A 54 10897 7025 9752 657 -128 1590 C ATOM 34 O ASP A 54 -4.904 25.075 -18.369 1.00 72.51 O ANISOU 34 O ASP A 54 10757 7156 9635 649 -119 1649 O ATOM 35 CB ASP A 54 -4.224 28.076 -17.905 1.00 74.87 C ANISOU 35 CB ASP A 54 11177 7165 10102 589 -449 1844 C ATOM 36 CG ASP A 54 -4.341 29.254 -18.828 1.00 75.88 C ANISOU 36 CG ASP A 54 11218 7278 10335 586 -619 1975 C ATOM 37 OD1 ASP A 54 -5.478 29.568 -19.253 1.00 76.25 O ANISOU 37 OD1 ASP A 54 11190 7292 10487 651 -607 1901 O ATOM 38 OD2 ASP A 54 -3.292 29.863 -19.127 1.00 76.45 O ANISOU 38 OD2 ASP A 54 11284 7367 10395 514 -769 2167 O ATOM 39 N LEU A 55 -5.221 25.508 -16.184 1.00 71.98 N ANISOU 39 N LEU A 55 10930 6810 9607 661 -18 1472 N ATOM 40 CA LEU A 55 -4.909 24.149 -15.760 1.00 69.72 C ANISOU 40 CA LEU A 55 10677 6609 9204 645 118 1409 C ATOM 41 C LEU A 55 -6.041 23.198 -16.120 1.00 69.45 C ANISOU 41 C LEU A 55 10531 6642 9212 700 254 1292 C ATOM 42 O LEU A 55 -5.815 21.993 -16.232 1.00 69.37 O ANISOU 42 O LEU A 55 10501 6742 9112 686 334 1266 O ATOM 43 CB LEU A 55 -4.613 24.109 -14.260 1.00 69.16 C ANISOU 43 CB LEU A 55 10808 6392 9077 633 185 1326 C ATOM 44 CG LEU A 55 -3.461 25.010 -13.784 1.00 69.21 C ANISOU 44 CG LEU A 55 10949 6299 9047 565 17 1442 C ATOM 45 CD1 LEU A 55 -3.287 24.889 -12.281 1.00 69.34 C ANISOU 45 CD1 LEU A 55 11197 6158 8992 564 78 1337 C ATOM 46 CD2 LEU A 55 -2.152 24.698 -14.494 1.00 68.43 C ANISOU 46 CD2 LEU A 55 10768 6354 8878 485 -87 1628 C ATOM 47 N ASP A 56 -7.244 23.741 -16.321 1.00 70.35 N ANISOU 47 N ASP A 56 10570 6683 9476 761 267 1232 N ATOM 48 CA ASP A 56 -8.419 22.946 -16.707 1.00 70.97 C ANISOU 48 CA ASP A 56 10519 6805 9641 805 365 1143 C ATOM 49 C ASP A 56 -8.173 22.027 -17.915 1.00 70.15 C ANISOU 49 C ASP A 56 10310 6880 9464 780 309 1196 C ATOM 50 O ASP A 56 -7.712 22.475 -18.965 1.00 70.77 O ANISOU 50 O ASP A 56 10336 7043 9510 768 168 1313 O ATOM 51 CB ASP A 56 -9.630 23.851 -17.001 1.00 72.66 C ANISOU 51 CB ASP A 56 10633 6923 10050 869 338 1121 C ATOM 52 CG ASP A 56 -10.212 24.505 -15.741 1.00 74.55 C ANISOU 52 CG ASP A 56 10976 6978 10371 935 454 1031 C ATOM 53 OD1 ASP A 56 -10.134 23.906 -14.645 1.00 75.08 O ANISOU 53 OD1 ASP A 56 11159 6997 10368 944 608 948 O ATOM 54 OD2 ASP A 56 -10.767 25.624 -15.845 1.00 76.48 O ANISOU 54 OD2 ASP A 56 11196 7117 10743 988 396 1043 O ATOM 55 N VAL A 57 -8.474 20.741 -17.741 1.00 69.23 N ANISOU 55 N VAL A 57 10178 6811 9312 780 420 1112 N ATOM 56 CA VAL A 57 -8.454 19.767 -18.824 1.00 68.12 C ANISOU 56 CA VAL A 57 9964 6810 9107 776 370 1129 C ATOM 57 C VAL A 57 -9.896 19.549 -19.266 1.00 68.50 C ANISOU 57 C VAL A 57 9878 6818 9328 808 366 1063 C ATOM 58 O VAL A 57 -10.783 19.426 -18.425 1.00 68.20 O ANISOU 58 O VAL A 57 9813 6676 9421 826 487 977 O ATOM 59 CB VAL A 57 -7.833 18.434 -18.356 1.00 67.33 C ANISOU 59 CB VAL A 57 9941 6775 8866 750 471 1083 C ATOM 60 CG1 VAL A 57 -7.874 17.385 -19.462 1.00 67.14 C ANISOU 60 CG1 VAL A 57 9868 6873 8767 762 415 1084 C ATOM 61 CG2 VAL A 57 -6.401 18.650 -17.882 1.00 66.65 C ANISOU 61 CG2 VAL A 57 9970 6719 8633 714 465 1165 C ATOM 62 N ASN A 58 -10.079 19.457 -20.564 1.00 69.19 N ANISOU 62 N ASN A 58 9887 6984 9417 818 223 1115 N ATOM 63 CA ASN A 58 -11.379 19.351 -21.167 1.00 70.25 C ANISOU 63 CA ASN A 58 9886 7074 9730 839 164 1077 C ATOM 64 C ASN A 58 -11.661 17.978 -21.756 1.00 70.90 C ANISOU 64 C ASN A 58 9957 7224 9757 828 131 1030 C ATOM 65 O ASN A 58 -11.600 17.788 -22.948 1.00 71.33 O ANISOU 65 O ASN A 58 10010 7356 9736 840 -18 1072 O ATOM 66 CB ASN A 58 -11.460 20.415 -22.236 1.00 70.91 C ANISOU 66 CB ASN A 58 9903 7165 9875 859 -8 1169 C ATOM 67 CG ASN A 58 -12.823 20.544 -22.825 1.00 71.86 C ANISOU 67 CG ASN A 58 9872 7207 10223 878 -80 1142 C ATOM 68 OD1 ASN A 58 -13.817 20.368 -22.144 0.00 20.00 O ATOM 69 ND2 ASN A 58 -12.882 20.864 -24.106 0.00 20.00 N ATOM 70 N THR A 59 -11.955 17.021 -20.891 1.00 71.39 N ANISOU 70 N THR A 59 10030 7247 9845 809 268 943 N ATOM 71 CA THR A 59 -12.403 15.691 -21.288 1.00 72.49 C ANISOU 71 CA THR A 59 10147 7407 9985 792 233 888 C ATOM 72 C THR A 59 -13.890 15.577 -20.947 1.00 74.14 C ANISOU 72 C THR A 59 10199 7496 10473 784 264 848 C ATOM 73 O THR A 59 -14.284 15.838 -19.807 1.00 74.62 O ANISOU 73 O THR A 59 10225 7475 10651 791 435 820 O ATOM 74 CB THR A 59 -11.615 14.568 -20.560 1.00 72.26 C ANISOU 74 CB THR A 59 10236 7421 9799 769 358 836 C ATOM 75 OG1 THR A 59 -11.672 14.750 -19.134 1.00 71.38 O ANISOU 75 OG1 THR A 59 10141 7230 9749 757 547 798 O ATOM 76 CG2 THR A 59 -10.154 14.549 -21.010 1.00 71.75 C ANISOU 76 CG2 THR A 59 10302 7482 9475 784 322 896 C ATOM 77 N ASP A 60 -14.712 15.193 -21.924 1.00 75.32 N ANISOU 77 N ASP A 60 10256 7631 10730 775 98 854 N ATOM 78 CA ASP A 60 -16.161 15.060 -21.712 1.00 77.16 C ANISOU 78 CA ASP A 60 10305 7748 11263 762 101 846 C ATOM 79 C ASP A 60 -16.519 14.057 -20.604 1.00 77.12 C ANISOU 79 C ASP A 60 10271 7691 11339 731 282 793 C ATOM 80 O ASP A 60 -15.762 13.117 -20.317 1.00 76.21 O ANISOU 80 O ASP A 60 10283 7630 11043 707 335 748 O ATOM 81 CB ASP A 60 -16.874 14.675 -23.020 1.00 79.33 C ANISOU 81 CB ASP A 60 10509 8009 11623 742 -153 869 C ATOM 82 CG ASP A 60 -16.477 13.295 -23.529 1.00 80.21 C ANISOU 82 CG ASP A 60 10738 8168 11567 713 -251 820 C ATOM 83 OD1 ASP A 60 -15.423 12.788 -23.097 1.00 80.45 O ANISOU 83 OD1 ASP A 60 10916 8275 11373 718 -139 783 O ATOM 84 OD2 ASP A 60 -17.214 12.715 -24.362 1.00 82.24 O ANISOU 84 OD2 ASP A 60 10948 8376 11921 687 -454 821 O ATOM 85 N ILE A 61 -17.683 14.260 -19.993 1.00 77.95 N ANISOU 85 N ILE A 61 10202 7690 11723 739 382 811 N ATOM 86 CA ILE A 61 -18.154 13.379 -18.927 1.00 78.56 C ANISOU 86 CA ILE A 61 10228 7713 11908 716 570 786 C ATOM 87 C ILE A 61 -18.324 11.921 -19.409 1.00 79.73 C ANISOU 87 C ILE A 61 10371 7867 12056 643 443 766 C ATOM 88 O ILE A 61 -18.058 10.982 -18.651 1.00 80.64 O ANISOU 88 O ILE A 61 10546 7985 12109 613 571 728 O ATOM 89 CB ILE A 61 -19.462 13.904 -18.276 1.00 79.53 C ANISOU 89 CB ILE A 61 10138 7724 12355 754 711 837 C ATOM 90 CG1 ILE A 61 -19.659 13.273 -16.893 1.00 79.44 C ANISOU 90 CG1 ILE A 61 10124 7671 12385 759 986 820 C ATOM 91 CG2 ILE A 61 -20.673 13.660 -19.174 1.00 80.98 C ANISOU 91 CG2 ILE A 61 10102 7844 12823 719 516 903 C ATOM 92 CD1 ILE A 61 -18.559 13.226 -16.059 0.00 20.00 C ATOM 93 N TYR A 62 -18.754 11.731 -20.634 1.00 80.53 N ANISOU 93 N TYR A 62 10418 7958 12218 617 179 789 N ATOM 94 CA TYR A 62 -18.849 10.404 -21.154 1.00 80.83 C ANISOU 94 CA TYR A 62 10485 7981 12245 554 13 763 C ATOM 95 C TYR A 62 -17.552 9.643 -20.968 1.00 79.76 C ANISOU 95 C TYR A 62 10583 7939 11782 555 60 690 C ATOM 96 O TYR A 62 -17.481 8.679 -20.222 1.00 78.73 O ANISOU 96 O TYR A 62 10474 7784 11653 514 157 658 O ATOM 97 CB TYR A 62 -19.129 10.478 -22.637 1.00 81.79 C ANISOU 97 CB TYR A 62 10585 8082 12407 544 -307 790 C ATOM 98 CG TYR A 62 -20.495 11.019 -22.985 0.00 20.00 C ATOM 99 CD1 TYR A 62 -21.303 11.632 -22.028 0.00 20.00 C ATOM 100 CD2 TYR A 62 -20.982 10.915 -24.275 0.00 20.00 C ATOM 101 CE1 TYR A 62 -22.555 12.121 -22.358 0.00 20.00 C ATOM 102 CE2 TYR A 62 -22.229 11.399 -24.614 0.00 20.00 C ATOM 103 CZ TYR A 62 -23.010 11.998 -23.658 0.00 20.00 C ATOM 104 OH TYR A 62 -24.241 12.466 -24.041 0.00 20.00 O ATOM 105 N SER A 63 -16.520 10.104 -21.653 1.00 79.24 N ANISOU 105 N SER A 63 10678 7978 11451 603 0 679 N ATOM 106 CA SER A 63 -15.212 9.438 -21.654 1.00 78.12 C ANISOU 106 CA SER A 63 10747 7936 10999 621 41 630 C ATOM 107 C SER A 63 -14.718 9.164 -20.244 1.00 76.69 C ANISOU 107 C SER A 63 10605 7758 10773 607 298 603 C ATOM 108 O SER A 63 -14.218 8.076 -19.964 1.00 76.86 O ANISOU 108 O SER A 63 10729 7799 10674 586 331 557 O ATOM 109 CB SER A 63 -14.164 10.299 -22.363 1.00 77.74 C ANISOU 109 CB SER A 63 10818 8001 10717 684 -9 663 C ATOM 110 OG SER A 63 -14.517 10.509 -23.718 1.00 79.63 O ANISOU 110 OG SER A 63 11057 8246 10952 706 -247 690 O ATOM 111 N LYS A 64 -14.862 10.138 -19.382 1.00 75.92 N ANISOU 111 N LYS A 64 10447 7636 10760 624 469 628 N ATOM 112 CA LYS A 64 -14.309 10.023 -18.073 1.00 74.95 C ANISOU 112 CA LYS A 64 10393 7506 10579 618 705 602 C ATOM 113 C LYS A 64 -14.918 8.861 -17.334 1.00 75.38 C ANISOU 113 C LYS A 64 10386 7490 10764 568 796 577 C ATOM 114 O LYS A 64 -14.248 8.195 -16.569 1.00 74.26 O ANISOU 114 O LYS A 64 10362 7372 10482 547 894 540 O ATOM 115 CB LYS A 64 -14.496 11.321 -17.319 1.00 74.99 C ANISOU 115 CB LYS A 64 10362 7468 10664 660 857 628 C ATOM 116 CG LYS A 64 -13.285 12.209 -17.400 1.00 74.11 C ANISOU 116 CG LYS A 64 10382 7427 10349 692 831 649 C ATOM 117 CD LYS A 64 -13.146 13.066 -16.167 1.00 73.90 C ANISOU 117 CD LYS A 64 10409 7341 10329 725 1007 649 C ATOM 118 CE LYS A 64 -14.174 14.164 -16.197 1.00 74.79 C ANISOU 118 CE LYS A 64 10409 7382 10626 775 995 684 C ATOM 119 NZ LYS A 64 -13.570 15.502 -16.010 0.00 20.00 N ATOM 120 N VAL A 65 -16.186 8.598 -17.574 1.00 76.85 N ANISOU 120 N VAL A 65 10381 7588 11229 544 752 612 N ATOM 121 CA VAL A 65 -16.838 7.501 -16.896 1.00 78.20 C ANISOU 121 CA VAL A 65 10459 7684 11568 486 820 618 C ATOM 122 C VAL A 65 -16.492 6.182 -17.559 1.00 77.51 C ANISOU 122 C VAL A 65 10469 7612 11368 434 639 575 C ATOM 123 O VAL A 65 -16.030 5.263 -16.906 1.00 76.83 O ANISOU 123 O VAL A 65 10458 7521 11211 400 735 545 O ATOM 124 CB VAL A 65 -18.354 7.694 -16.831 1.00 80.47 C ANISOU 124 CB VAL A 65 10486 7868 12218 472 799 696 C ATOM 125 CG1 VAL A 65 -18.945 6.835 -15.725 0.00 20.00 C ATOM 126 CG2 VAL A 65 -18.675 9.150 -16.571 0.00 20.00 C ATOM 127 N LEU A 66 -16.686 6.108 -18.864 1.00 77.12 N ANISOU 127 N LEU A 66 10438 7576 11288 437 375 569 N ATOM 128 CA LEU A 66 -16.317 4.939 -19.628 1.00 76.56 C ANISOU 128 CA LEU A 66 10507 7515 11066 417 181 516 C ATOM 129 C LEU A 66 -14.934 4.500 -19.252 1.00 74.63 C ANISOU 129 C LEU A 66 10470 7360 10525 443 300 459 C ATOM 130 O LEU A 66 -14.630 3.336 -19.243 1.00 74.75 O ANISOU 130 O LEU A 66 10569 7351 10479 412 268 417 O ATOM 131 CB LEU A 66 -16.365 5.248 -21.115 1.00 76.94 C ANISOU 131 CB LEU A 66 10616 7593 11024 457 -86 514 C ATOM 132 CG LEU A 66 -15.571 4.326 -22.027 1.00 76.95 C ANISOU 132 CG LEU A 66 10835 7631 10771 486 -275 449 C ATOM 133 CD1 LEU A 66 -16.129 2.921 -22.021 1.00 78.12 C ANISOU 133 CD1 LEU A 66 10976 7659 11047 414 -421 420 C ATOM 134 CD2 LEU A 66 -15.529 4.867 -23.431 1.00 77.49 C ANISOU 134 CD2 LEU A 66 10975 7740 10724 549 -492 461 C ATOM 135 N VAL A 67 -14.093 5.450 -18.928 1.00 73.02 N ANISOU 135 N VAL A 67 10344 7250 10150 499 422 466 N ATOM 136 CA VAL A 67 -12.729 5.104 -18.558 1.00 71.54 C ANISOU 136 CA VAL A 67 10339 7151 9691 527 518 434 C ATOM 137 C VAL A 67 -12.668 4.624 -17.106 1.00 70.83 C ANISOU 137 C VAL A 67 10252 7021 9638 483 738 421 C ATOM 138 O VAL A 67 -11.917 3.702 -16.783 1.00 69.14 O ANISOU 138 O VAL A 67 10164 6832 9274 475 774 385 O ATOM 139 CB VAL A 67 -11.786 6.301 -18.834 1.00 70.75 C ANISOU 139 CB VAL A 67 10305 7154 9423 590 542 472 C ATOM 140 CG1 VAL A 67 -10.528 6.259 -17.984 1.00 69.38 C ANISOU 140 CG1 VAL A 67 10261 7045 9055 601 700 472 C ATOM 141 CG2 VAL A 67 -11.430 6.331 -20.317 1.00 71.32 C ANISOU 141 CG2 VAL A 67 10449 7294 9352 647 334 482 C ATOM 142 N THR A 68 -13.463 5.249 -16.242 1.00 71.37 N ANISOU 142 N THR A 68 10191 7024 9901 466 888 454 N ATOM 143 CA THR A 68 -13.545 4.846 -14.842 1.00 71.32 C ANISOU 143 CA THR A 68 10192 6971 9935 436 1111 450 C ATOM 144 C THR A 68 -14.055 3.399 -14.729 1.00 71.85 C ANISOU 144 C THR A 68 10225 6975 10100 369 1073 437 C ATOM 145 O THR A 68 -13.438 2.560 -14.064 1.00 70.86 O ANISOU 145 O THR A 68 10213 6857 9853 345 1157 409 O ATOM 146 CB THR A 68 -14.468 5.793 -14.044 1.00 72.50 C ANISOU 146 CB THR A 68 10206 7053 10287 455 1282 495 C ATOM 147 OG1 THR A 68 -14.000 7.143 -14.164 1.00 72.36 O ANISOU 147 OG1 THR A 68 10233 7075 10183 515 1292 504 O ATOM 148 CG2 THR A 68 -14.496 5.417 -12.574 1.00 72.84 C ANISOU 148 CG2 THR A 68 10290 7051 10332 442 1531 495 C ATOM 149 N ALA A 69 -15.179 3.123 -15.391 1.00 72.61 N ANISOU 149 N ALA A 69 10164 7000 10425 334 929 467 N ATOM 150 CA ALA A 69 -15.769 1.791 -15.418 1.00 73.02 C ANISOU 150 CA ALA A 69 10166 6969 10607 259 842 471 C ATOM 151 C ALA A 69 -14.766 0.744 -15.911 1.00 72.48 C ANISOU 151 C ALA A 69 10301 6940 10295 260 709 396 C ATOM 152 O ALA A 69 -14.604 -0.309 -15.293 1.00 72.25 O ANISOU 152 O ALA A 69 10327 6876 10249 214 763 380 O ATOM 153 CB ALA A 69 -17.006 1.794 -16.295 1.00 74.56 C ANISOU 153 CB ALA A 69 10176 7080 11072 223 637 521 C ATOM 154 N ILE A 70 -14.091 1.042 -17.019 1.00 72.21 N ANISOU 154 N ILE A 70 10384 6979 10071 321 543 357 N ATOM 155 CA ILE A 70 -13.006 0.193 -17.513 1.00 71.56 C ANISOU 155 CA ILE A 70 10513 6951 9725 359 449 292 C ATOM 156 C ILE A 70 -11.934 -0.004 -16.445 1.00 70.98 C ANISOU 156 C ILE A 70 10553 6938 9477 369 661 278 C ATOM 157 O ILE A 70 -11.574 -1.133 -16.121 1.00 72.04 O ANISOU 157 O ILE A 70 10781 7046 9543 346 665 243 O ATOM 158 CB ILE A 70 -12.338 0.791 -18.761 1.00 70.73 C ANISOU 158 CB ILE A 70 10514 6939 9419 451 304 277 C ATOM 159 CG1 ILE A 70 -13.258 0.636 -19.968 1.00 72.37 C ANISOU 159 CG1 ILE A 70 10678 7074 9744 445 35 273 C ATOM 160 CG2 ILE A 70 -11.000 0.114 -19.037 1.00 69.59 C ANISOU 160 CG2 ILE A 70 10586 6879 8976 521 296 231 C ATOM 161 CD1 ILE A 70 -12.898 1.543 -21.126 1.00 72.44 C ANISOU 161 CD1 ILE A 70 10746 7166 9610 531 -85 285 C ATOM 162 N TYR A 71 -11.416 1.096 -15.914 1.00 70.38 N ANISOU 162 N TYR A 71 10478 6930 9330 402 818 308 N ATOM 163 CA TYR A 71 -10.369 1.028 -14.904 1.00 69.33 C ANISOU 163 CA TYR A 71 10462 6844 9034 408 993 304 C ATOM 164 C TYR A 71 -10.821 0.153 -13.739 1.00 70.13 C ANISOU 164 C TYR A 71 10541 6861 9244 336 1127 300 C ATOM 165 O TYR A 71 -10.157 -0.820 -13.400 1.00 70.52 O ANISOU 165 O TYR A 71 10706 6914 9174 322 1143 271 O ATOM 166 CB TYR A 71 -10.005 2.429 -14.415 1.00 69.16 C ANISOU 166 CB TYR A 71 10431 6868 8976 438 1118 345 C ATOM 167 CG TYR A 71 -8.943 3.158 -15.232 1.00 68.29 C ANISOU 167 CG TYR A 71 10401 6868 8675 507 1036 368 C ATOM 168 CD1 TYR A 71 -8.901 3.067 -16.620 1.00 68.29 C ANISOU 168 CD1 TYR A 71 10411 6917 8616 556 851 365 C ATOM 169 CD2 TYR A 71 -7.999 3.970 -14.602 1.00 66.96 C ANISOU 169 CD2 TYR A 71 10303 6748 8389 523 1139 406 C ATOM 170 CE1 TYR A 71 -7.936 3.742 -17.350 1.00 67.73 C ANISOU 170 CE1 TYR A 71 10404 6954 8373 626 800 409 C ATOM 171 CE2 TYR A 71 -7.034 4.646 -15.325 1.00 66.19 C ANISOU 171 CE2 TYR A 71 10255 6750 8144 577 1067 456 C ATOM 172 CZ TYR A 71 -7.005 4.532 -16.697 1.00 66.63 C ANISOU 172 CZ TYR A 71 10304 6867 8143 632 912 463 C ATOM 173 OH TYR A 71 -6.044 5.214 -17.415 1.00 65.91 O ANISOU 173 OH TYR A 71 10253 6882 7906 694 861 536 O ATOM 174 N LEU A 72 -11.962 0.482 -13.145 1.00 71.43 N ANISOU 174 N LEU A 72 10552 6948 9639 296 1227 339 N ATOM 175 CA LEU A 72 -12.500 -0.310 -12.029 1.00 72.43 C ANISOU 175 CA LEU A 72 10638 6994 9887 232 1375 360 C ATOM 176 C LEU A 72 -12.715 -1.796 -12.369 1.00 72.89 C ANISOU 176 C LEU A 72 10707 6993 9993 173 1235 340 C ATOM 177 O LEU A 72 -12.588 -2.642 -11.490 1.00 73.48 O ANISOU 177 O LEU A 72 10828 7029 10059 127 1339 345 O ATOM 178 CB LEU A 72 -13.801 0.305 -11.477 1.00 74.29 C ANISOU 178 CB LEU A 72 10678 7159 10387 218 1509 429 C ATOM 179 CG LEU A 72 -13.731 1.062 -10.138 1.00 74.47 C ANISOU 179 CG LEU A 72 10737 7177 10380 252 1784 453 C ATOM 180 CD1 LEU A 72 -12.561 2.036 -10.056 1.00 73.14 C ANISOU 180 CD1 LEU A 72 10734 7085 9970 312 1806 416 C ATOM 181 CD2 LEU A 72 -15.044 1.790 -9.882 1.00 76.10 C ANISOU 181 CD2 LEU A 72 10742 7322 10850 273 1899 524 C ATOM 182 N ALA A 73 -13.036 -2.123 -13.621 1.00 73.01 N ANISOU 182 N ALA A 73 10696 6989 10053 174 990 318 N ATOM 183 CA ALA A 73 -13.110 -3.532 -14.033 1.00 73.10 C ANISOU 183 CA ALA A 73 10767 6931 10076 129 819 285 C ATOM 184 C ALA A 73 -11.721 -4.177 -13.981 1.00 71.21 C ANISOU 184 C ALA A 73 10751 6757 9546 176 824 219 C ATOM 185 O ALA A 73 -11.550 -5.243 -13.395 1.00 71.39 O ANISOU 185 O ALA A 73 10835 6729 9560 130 854 208 O ATOM 186 CB ALA A 73 -13.711 -3.664 -15.423 1.00 74.16 C ANISOU 186 CB ALA A 73 10866 7019 10293 134 532 268 C ATOM 187 N LEU A 74 -10.728 -3.519 -14.575 1.00 69.18 N ANISOU 187 N LEU A 74 10605 6612 9067 268 801 191 N ATOM 188 CA LEU A 74 -9.345 -3.988 -14.489 1.00 67.51 C ANISOU 188 CA LEU A 74 10580 6475 8594 326 833 154 C ATOM 189 C LEU A 74 -8.877 -4.124 -13.038 1.00 66.32 C ANISOU 189 C LEU A 74 10460 6323 8411 281 1052 178 C ATOM 190 O LEU A 74 -8.094 -5.005 -12.724 1.00 65.86 O ANISOU 190 O LEU A 74 10528 6269 8226 287 1065 153 O ATOM 191 CB LEU A 74 -8.396 -3.043 -15.230 1.00 66.30 C ANISOU 191 CB LEU A 74 10496 6450 8242 428 813 162 C ATOM 192 CG LEU A 74 -8.520 -2.953 -16.755 1.00 67.24 C ANISOU 192 CG LEU A 74 10648 6594 8303 503 600 137 C ATOM 193 CD1 LEU A 74 -7.666 -1.810 -17.300 1.00 66.53 C ANISOU 193 CD1 LEU A 74 10589 6637 8050 593 628 179 C ATOM 194 CD2 LEU A 74 -8.135 -4.263 -17.422 1.00 67.49 C ANISOU 194 CD2 LEU A 74 10842 6596 8205 553 452 71 C ATOM 195 N PHE A 75 -9.349 -3.242 -12.163 1.00 66.04 N ANISOU 195 N PHE A 75 10327 6278 8485 248 1220 225 N ATOM 196 CA PHE A 75 -8.918 -3.240 -10.761 1.00 65.32 C ANISOU 196 CA PHE A 75 10296 6179 8342 216 1426 247 C ATOM 197 C PHE A 75 -9.392 -4.468 -9.975 1.00 66.10 C ANISOU 197 C PHE A 75 10390 6184 8540 138 1481 253 C ATOM 198 O PHE A 75 -8.668 -4.973 -9.120 1.00 64.60 O ANISOU 198 O PHE A 75 10318 5994 8233 121 1576 251 O ATOM 199 CB PHE A 75 -9.394 -1.965 -10.056 1.00 64.77 C ANISOU 199 CB PHE A 75 10149 6106 8355 220 1588 290 C ATOM 200 CG PHE A 75 -8.834 -1.793 -8.672 1.00 64.01 C ANISOU 200 CG PHE A 75 10162 5999 8157 207 1782 306 C ATOM 201 CD1 PHE A 75 -7.549 -1.301 -8.482 1.00 62.71 C ANISOU 201 CD1 PHE A 75 10140 5900 7785 243 1789 304 C ATOM 202 CD2 PHE A 75 -9.585 -2.134 -7.559 1.00 64.94 C ANISOU 202 CD2 PHE A 75 10247 6036 8391 161 1953 336 C ATOM 203 CE1 PHE A 75 -7.032 -1.148 -7.204 1.00 62.26 C ANISOU 203 CE1 PHE A 75 10206 5816 7633 226 1935 319 C ATOM 204 CE2 PHE A 75 -9.072 -1.979 -6.280 1.00 64.52 C ANISOU 204 CE2 PHE A 75 10328 5965 8220 157 2124 347 C ATOM 205 CZ PHE A 75 -7.795 -1.483 -6.105 1.00 63.04 C ANISOU 205 CZ PHE A 75 10299 5831 7821 187 2102 332 C ATOM 206 N VAL A 76 -10.609 -4.928 -10.259 1.00 67.83 N ANISOU 206 N VAL A 76 10467 6317 8987 84 1411 274 N ATOM 207 CA VAL A 76 -11.137 -6.121 -9.607 1.00 69.15 C ANISOU 207 CA VAL A 76 10607 6387 9280 0 1441 300 C ATOM 208 C VAL A 76 -10.471 -7.353 -10.216 1.00 68.80 C ANISOU 208 C VAL A 76 10699 6324 9116 2 1256 238 C ATOM 209 O VAL A 76 -9.869 -8.144 -9.493 1.00 68.67 O ANISOU 209 O VAL A 76 10792 6291 9006 -21 1322 231 O ATOM 210 CB VAL A 76 -12.696 -6.203 -9.639 1.00 71.36 C ANISOU 210 CB VAL A 76 10661 6569 9881 -67 1429 374 C ATOM 211 CG1 VAL A 76 -13.313 -4.918 -9.091 1.00 71.61 C ANISOU 211 CG1 VAL A 76 10567 6623 10018 -38 1625 434 C ATOM 212 CG2 VAL A 76 -13.253 -6.492 -11.027 1.00 72.38 C ANISOU 212 CG2 VAL A 76 10723 6654 10123 -75 1144 352 C ATOM 213 N VAL A 77 -10.519 -7.466 -11.545 1.00 68.71 N ANISOU 213 N VAL A 77 10703 6316 9088 44 1027 190 N ATOM 214 CA VAL A 77 -9.998 -8.632 -12.256 1.00 68.64 C ANISOU 214 CA VAL A 77 10840 6273 8965 69 833 122 C ATOM 215 C VAL A 77 -8.525 -8.831 -11.929 1.00 67.79 C ANISOU 215 C VAL A 77 10915 6252 8589 139 916 87 C ATOM 216 O VAL A 77 -8.090 -9.936 -11.573 1.00 68.92 O ANISOU 216 O VAL A 77 11164 6347 8675 121 899 65 O ATOM 217 CB VAL A 77 -10.170 -8.479 -13.778 1.00 68.72 C ANISOU 217 CB VAL A 77 10877 6287 8944 137 589 72 C ATOM 218 CG1 VAL A 77 -9.384 -9.546 -14.535 1.00 68.62 C ANISOU 218 CG1 VAL A 77 11074 6258 8740 210 415 -10 C ATOM 219 CG2 VAL A 77 -11.646 -8.539 -14.144 1.00 70.35 C ANISOU 219 CG2 VAL A 77 10909 6376 9442 52 449 113 C ATOM 220 N GLY A 78 -7.774 -7.744 -12.032 1.00 66.56 N ANISOU 220 N GLY A 78 10784 6217 8287 213 1002 96 N ATOM 221 CA GLY A 78 -6.348 -7.757 -11.777 1.00 65.70 C ANISOU 221 CA GLY A 78 10819 6198 7946 281 1074 91 C ATOM 222 C GLY A 78 -5.951 -8.008 -10.337 1.00 65.46 C ANISOU 222 C GLY A 78 10827 6146 7898 217 1252 125 C ATOM 223 O GLY A 78 -5.001 -8.730 -10.089 1.00 65.87 O ANISOU 223 O GLY A 78 11003 6210 7814 242 1254 113 O ATOM 224 N THR A 79 -6.644 -7.416 -9.374 1.00 65.92 N ANISOU 224 N THR A 79 10792 6171 8083 147 1404 172 N ATOM 225 CA THR A 79 -6.242 -7.606 -7.978 1.00 66.26 C ANISOU 225 CA THR A 79 10905 6190 8079 97 1574 205 C ATOM 226 C THR A 79 -6.588 -9.007 -7.479 1.00 67.45 C ANISOU 226 C THR A 79 11080 6241 8307 24 1563 203 C ATOM 227 O THR A 79 -5.845 -9.584 -6.684 1.00 66.98 O ANISOU 227 O THR A 79 11137 6170 8143 6 1626 211 O ATOM 228 CB THR A 79 -6.861 -6.565 -7.029 1.00 66.27 C ANISOU 228 CB THR A 79 10836 6177 8164 65 1759 253 C ATOM 229 OG1 THR A 79 -8.286 -6.549 -7.184 1.00 67.10 O ANISOU 229 OG1 THR A 79 10774 6217 8503 23 1767 277 O ATOM 230 CG2 THR A 79 -6.283 -5.193 -7.318 1.00 65.90 C ANISOU 230 CG2 THR A 79 10804 6218 8014 131 1770 260 C ATOM 231 N VAL A 80 -7.720 -9.534 -7.943 1.00 68.64 N ANISOU 231 N VAL A 80 11117 6310 8651 -23 1468 203 N ATOM 232 CA VAL A 80 -8.102 -10.913 -7.678 1.00 69.39 C ANISOU 232 CA VAL A 80 11224 6296 8844 -97 1407 208 C ATOM 233 C VAL A 80 -7.089 -11.869 -8.304 1.00 68.72 C ANISOU 233 C VAL A 80 11303 6215 8591 -39 1248 138 C ATOM 234 O VAL A 80 -6.458 -12.669 -7.603 1.00 67.73 O ANISOU 234 O VAL A 80 11284 6062 8385 -61 1292 141 O ATOM 235 CB VAL A 80 -9.501 -11.220 -8.246 1.00 71.01 C ANISOU 235 CB VAL A 80 11264 6405 9311 -160 1285 234 C ATOM 236 CG1 VAL A 80 -9.747 -12.724 -8.302 1.00 72.43 C ANISOU 236 CG1 VAL A 80 11480 6461 9577 -229 1138 229 C ATOM 237 CG2 VAL A 80 -10.566 -10.541 -7.402 1.00 71.59 C ANISOU 237 CG2 VAL A 80 11161 6455 9582 -220 1479 329 C ATOM 238 N GLY A 81 -6.942 -11.763 -9.623 1.00 68.37 N ANISOU 238 N GLY A 81 11284 6203 8487 43 1070 79 N ATOM 239 CA GLY A 81 -6.064 -12.641 -10.389 1.00 68.24 C ANISOU 239 CA GLY A 81 11432 6188 8306 131 918 9 C ATOM 240 C GLY A 81 -4.676 -12.786 -9.797 1.00 66.87 C ANISOU 240 C GLY A 81 11389 6087 7930 186 1027 15 C ATOM 241 O GLY A 81 -4.174 -13.902 -9.634 1.00 67.69 O ANISOU 241 O GLY A 81 11607 6136 7974 195 976 -9 O ATOM 242 N ASN A 82 -4.056 -11.658 -9.473 1.00 65.20 N ANISOU 242 N ASN A 82 11158 5988 7625 219 1162 57 N ATOM 243 CA ASN A 82 -2.709 -11.652 -8.905 1.00 64.02 C ANISOU 243 CA ASN A 82 11114 5907 7304 263 1251 85 C ATOM 244 C ASN A 82 -2.667 -12.221 -7.476 1.00 63.57 C ANISOU 244 C ASN A 82 11094 5776 7281 160 1368 122 C ATOM 245 O ASN A 82 -1.645 -12.771 -7.046 1.00 63.02 O ANISOU 245 O ASN A 82 11133 5714 7095 183 1384 135 O ATOM 246 CB ASN A 82 -2.127 -10.230 -8.925 1.00 63.18 C ANISOU 246 CB ASN A 82 10970 5919 7114 308 1337 135 C ATOM 247 CG ASN A 82 -1.795 -9.744 -10.334 1.00 63.61 C ANISOU 247 CG ASN A 82 11019 6068 7082 431 1232 119 C ATOM 248 OD1 ASN A 82 -0.858 -10.234 -10.965 1.00 64.87 O ANISOU 248 OD1 ASN A 82 11269 6277 7100 539 1175 111 O ATOM 249 ND2 ASN A 82 -2.549 -8.766 -10.827 1.00 63.57 N ANISOU 249 ND2 ASN A 82 10909 6087 7157 426 1217 122 N ATOM 250 N SER A 83 -3.770 -12.082 -6.744 1.00 63.31 N ANISOU 250 N SER A 83 10971 5673 7411 54 1454 150 N ATOM 251 CA SER A 83 -3.843 -12.567 -5.372 1.00 63.11 C ANISOU 251 CA SER A 83 10985 5578 7414 -38 1583 196 C ATOM 252 C SER A 83 -4.018 -14.074 -5.351 1.00 63.66 C ANISOU 252 C SER A 83 11103 5543 7541 -81 1485 177 C ATOM 253 O SER A 83 -3.204 -14.796 -4.780 1.00 62.25 O ANISOU 253 O SER A 83 11042 5343 7266 -86 1497 184 O ATOM 254 CB SER A 83 -4.989 -11.889 -4.636 1.00 63.57 C ANISOU 254 CB SER A 83 10929 5602 7622 -113 1732 247 C ATOM 255 OG SER A 83 -4.689 -10.525 -4.469 1.00 63.34 O ANISOU 255 OG SER A 83 10896 5653 7517 -71 1826 262 O ATOM 256 N VAL A 84 -5.100 -14.516 -5.985 1.00 64.87 N ANISOU 256 N VAL A 84 11161 5620 7864 -118 1373 159 N ATOM 257 CA VAL A 84 -5.335 -15.916 -6.307 1.00 66.02 C ANISOU 257 CA VAL A 84 11353 5650 8079 -148 1212 129 C ATOM 258 C VAL A 84 -4.051 -16.604 -6.778 1.00 65.29 C ANISOU 258 C VAL A 84 11435 5582 7789 -44 1109 66 C ATOM 259 O VAL A 84 -3.731 -17.714 -6.342 1.00 65.90 O ANISOU 259 O VAL A 84 11605 5579 7854 -72 1072 64 O ATOM 260 CB VAL A 84 -6.414 -16.030 -7.408 1.00 67.53 C ANISOU 260 CB VAL A 84 11444 5778 8435 -158 1030 99 C ATOM 261 CG1 VAL A 84 -6.373 -17.385 -8.111 1.00 68.87 C ANISOU 261 CG1 VAL A 84 11721 5831 8612 -145 794 36 C ATOM 262 CG2 VAL A 84 -7.792 -15.776 -6.819 1.00 68.79 C ANISOU 262 CG2 VAL A 84 11413 5873 8850 -281 1118 189 C ATOM 263 N THR A 85 -3.327 -15.946 -7.672 1.00 64.08 N ANISOU 263 N THR A 85 11319 5538 7487 84 1070 25 N ATOM 264 CA THR A 85 -2.065 -16.477 -8.153 1.00 63.51 C ANISOU 264 CA THR A 85 11396 5508 7225 210 1006 -14 C ATOM 265 C THR A 85 -1.098 -16.681 -6.991 1.00 62.79 C ANISOU 265 C THR A 85 11373 5435 7048 184 1135 41 C ATOM 266 O THR A 85 -0.551 -17.763 -6.840 1.00 63.37 O ANISOU 266 O THR A 85 11555 5447 7073 206 1078 24 O ATOM 267 CB THR A 85 -1.466 -15.591 -9.269 1.00 62.41 C ANISOU 267 CB THR A 85 11262 5500 6948 356 978 -35 C ATOM 268 OG1 THR A 85 -2.280 -15.717 -10.441 1.00 63.48 O ANISOU 268 OG1 THR A 85 11387 5591 7138 394 811 -101 O ATOM 269 CG2 THR A 85 -0.031 -15.998 -9.614 1.00 61.66 C ANISOU 269 CG2 THR A 85 11298 5472 6655 502 969 -40 C ATOM 270 N LEU A 86 -0.913 -15.664 -6.158 1.00 62.38 N ANISOU 270 N LEU A 86 11270 5451 6979 137 1292 107 N ATOM 271 CA LEU A 86 -0.026 -15.787 -5.002 1.00 62.61 C ANISOU 271 CA LEU A 86 11377 5483 6926 102 1395 166 C ATOM 272 C LEU A 86 -0.449 -16.934 -4.084 1.00 63.75 C ANISOU 272 C LEU A 86 11570 5498 7153 -5 1405 178 C ATOM 273 O LEU A 86 0.380 -17.739 -3.663 1.00 63.31 O ANISOU 273 O LEU A 86 11620 5409 7023 5 1384 190 O ATOM 274 CB LEU A 86 0.013 -14.484 -4.205 1.00 62.11 C ANISOU 274 CB LEU A 86 11272 5479 6845 55 1541 227 C ATOM 275 CG LEU A 86 0.791 -13.359 -4.881 1.00 61.60 C ANISOU 275 CG LEU A 86 11182 5543 6679 153 1534 246 C ATOM 276 CD1 LEU A 86 0.443 -12.016 -4.255 1.00 60.80 C ANISOU 276 CD1 LEU A 86 11030 5470 6599 100 1648 288 C ATOM 277 CD2 LEU A 86 2.288 -13.642 -4.806 1.00 61.37 C ANISOU 277 CD2 LEU A 86 11241 5562 6513 224 1509 290 C ATOM 278 N PHE A 87 -1.745 -16.988 -3.789 1.00 65.17 N ANISOU 278 N PHE A 87 11658 5603 7498 -107 1438 190 N ATOM 279 CA PHE A 87 -2.341 -18.059 -2.997 1.00 66.83 C ANISOU 279 CA PHE A 87 11883 5686 7821 -218 1448 222 C ATOM 280 C PHE A 87 -2.094 -19.428 -3.630 1.00 67.79 C ANISOU 280 C PHE A 87 12088 5721 7948 -185 1260 167 C ATOM 281 O PHE A 87 -1.727 -20.381 -2.938 1.00 67.82 O ANISOU 281 O PHE A 87 12182 5649 7938 -229 1255 190 O ATOM 282 CB PHE A 87 -3.851 -17.823 -2.851 1.00 67.96 C ANISOU 282 CB PHE A 87 11873 5774 8173 -314 1501 261 C ATOM 283 CG PHE A 87 -4.558 -18.872 -2.032 1.00 69.64 C ANISOU 283 CG PHE A 87 12071 5858 8529 -437 1525 326 C ATOM 284 CD1 PHE A 87 -4.657 -18.746 -0.650 1.00 69.84 C ANISOU 284 CD1 PHE A 87 12120 5870 8546 -512 1725 413 C ATOM 285 CD2 PHE A 87 -5.128 -19.978 -2.641 1.00 71.06 C ANISOU 285 CD2 PHE A 87 12226 5923 8850 -475 1340 306 C ATOM 286 CE1 PHE A 87 -5.313 -19.696 0.107 1.00 70.93 C ANISOU 286 CE1 PHE A 87 12238 5896 8817 -623 1762 493 C ATOM 287 CE2 PHE A 87 -5.785 -20.939 -1.888 1.00 72.53 C ANISOU 287 CE2 PHE A 87 12384 5985 9188 -598 1355 386 C ATOM 288 CZ PHE A 87 -5.878 -20.794 -0.512 1.00 72.57 C ANISOU 288 CZ PHE A 87 12393 5991 9186 -671 1577 486 C ATOM 289 N THR A 88 -2.292 -19.503 -4.947 1.00 67.87 N ANISOU 289 N THR A 88 12084 5733 7967 -101 1101 91 N ATOM 290 CA THR A 88 -2.203 -20.758 -5.689 1.00 68.33 C ANISOU 290 CA THR A 88 12243 5689 8030 -53 898 22 C ATOM 291 C THR A 88 -0.764 -21.245 -5.850 1.00 68.16 C ANISOU 291 C THR A 88 12378 5707 7812 76 872 -10 C ATOM 292 O THR A 88 -0.525 -22.448 -5.874 1.00 69.15 O ANISOU 292 O THR A 88 12613 5725 7935 90 760 -41 O ATOM 293 CB THR A 88 -2.900 -20.628 -7.061 1.00 68.68 C ANISOU 293 CB THR A 88 12253 5714 8128 4 725 -51 C ATOM 294 OG1 THR A 88 -4.309 -20.482 -6.855 1.00 69.23 O ANISOU 294 OG1 THR A 88 12167 5707 8429 -133 717 -3 O ATOM 295 CG2 THR A 88 -2.663 -21.843 -7.939 1.00 69.73 C ANISOU 295 CG2 THR A 88 12541 5737 8216 90 498 -141 C ATOM 296 N LEU A 89 0.195 -20.331 -5.946 1.00 67.49 N ANISOU 296 N LEU A 89 12296 5767 7579 172 971 8 N ATOM 297 CA LEU A 89 1.600 -20.733 -6.074 1.00 67.73 C ANISOU 297 CA LEU A 89 12444 5844 7446 302 963 8 C ATOM 298 C LEU A 89 2.216 -21.099 -4.730 1.00 68.08 C ANISOU 298 C LEU A 89 12532 5858 7476 219 1057 83 C ATOM 299 O LEU A 89 3.266 -21.731 -4.684 1.00 67.96 O ANISOU 299 O LEU A 89 12613 5839 7367 303 1031 91 O ATOM 300 CB LEU A 89 2.440 -19.625 -6.714 1.00 66.97 C ANISOU 300 CB LEU A 89 12314 5913 7216 434 1025 29 C ATOM 301 CG LEU A 89 2.105 -19.181 -8.140 1.00 67.70 C ANISOU 301 CG LEU A 89 12388 6061 7271 552 939 -35 C ATOM 302 CD1 LEU A 89 3.066 -18.083 -8.566 0.00 67.12 C ANISOU 302 CD1 LEU A 89 12274 6157 7071 668 1027 22 C ATOM 303 CD2 LEU A 89 2.157 -20.340 -9.126 0.00 69.31 C ANISOU 303 CD2 LEU A 89 12732 6180 7422 677 772 -130 C ATOM 304 N ALA A 90 1.594 -20.673 -3.635 1.00 68.61 N ANISOU 304 N ALA A 90 12537 5903 7629 67 1172 144 N ATOM 305 CA ALA A 90 2.130 -20.969 -2.315 1.00 69.21 C ANISOU 305 CA ALA A 90 12677 5942 7675 -14 1259 218 C ATOM 306 C ALA A 90 1.863 -22.437 -1.973 1.00 71.22 C ANISOU 306 C ALA A 90 13008 6047 8003 -74 1171 207 C ATOM 307 O ALA A 90 2.746 -23.152 -1.486 1.00 71.71 O ANISOU 307 O ALA A 90 13172 6072 8000 -57 1151 232 O ATOM 308 CB ALA A 90 1.510 -20.049 -1.271 1.00 68.65 C ANISOU 308 CB ALA A 90 12547 5887 7647 -138 1417 284 C ATOM 309 N ARG A 91 0.675 -22.906 -2.258 1.00 84.39 N ANISOU 309 N ARG A 91 10996 9517 11551 225 169 1409 N ATOM 310 CA ARG A 91 0.356 -24.240 -1.858 1.00 86.19 C ANISOU 310 CA ARG A 91 11178 9631 11939 219 218 1483 C ATOM 311 C ARG A 91 0.783 -25.319 -2.832 1.00 87.27 C ANISOU 311 C ARG A 91 11225 9749 12184 213 60 1423 C ATOM 312 O ARG A 91 0.740 -26.489 -2.505 1.00 88.17 O ANISOU 312 O ARG A 91 11330 9790 12379 212 75 1479 O ATOM 313 CB ARG A 91 -1.109 -24.331 -1.647 1.00 86.76 C ANISOU 313 CB ARG A 91 11147 9585 12232 203 366 1542 C ATOM 314 CG ARG A 91 -1.886 -23.711 -2.765 1.00 86.16 C ANISOU 314 CG ARG A 91 10909 9484 12341 187 284 1455 C ATOM 315 CD ARG A 91 -3.289 -24.258 -2.779 1.00 87.38 C ANISOU 315 CD ARG A 91 10908 9474 12818 170 379 1507 C ATOM 316 NE ARG A 91 -3.821 -24.284 -1.435 1.00 88.27 N ANISOU 316 NE ARG A 91 11075 9508 12954 171 632 1635 N ATOM 317 CZ ARG A 91 -5.020 -24.711 -1.119 1.00 89.36 C ANISOU 317 CZ ARG A 91 11091 9480 13381 159 777 1707 C ATOM 318 NH1 ARG A 91 -5.391 -24.692 0.141 0.00 20.00 N ATOM 319 NH2 ARG A 91 -5.840 -25.147 -2.059 0.00 20.00 N ATOM 320 N LYS A 92 1.194 -24.942 -4.020 1.00 88.02 N ANISOU 320 N LYS A 92 11270 9900 12273 216 -82 1311 N ATOM 321 CA LYS A 92 1.648 -25.934 -4.949 1.00 88.89 C ANISOU 321 CA LYS A 92 11326 9990 12457 221 -231 1248 C ATOM 322 C LYS A 92 2.749 -26.743 -4.311 1.00 90.59 C ANISOU 322 C LYS A 92 11618 10224 12576 228 -253 1286 C ATOM 323 O LYS A 92 2.614 -27.946 -4.149 1.00 92.56 O ANISOU 323 O LYS A 92 11825 10396 12946 223 -264 1327 O ATOM 324 CB LYS A 92 2.136 -25.294 -6.232 1.00 87.45 C ANISOU 324 CB LYS A 92 11146 9870 12209 241 -357 1127 C ATOM 325 CG LYS A 92 1.102 -25.301 -7.336 1.00 87.12 C ANISOU 325 CG LYS A 92 11009 9757 12334 247 -428 1063 C ATOM 326 CD LYS A 92 1.620 -24.537 -8.538 0.00 20.00 C ATOM 327 CE LYS A 92 0.687 -24.663 -9.725 0.00 20.00 C ATOM 328 NZ LYS A 92 0.892 -23.583 -10.719 0.00 20.00 N ATOM 329 N LYS A 93 3.844 -26.098 -3.948 1.00 90.75 N ANISOU 329 N LYS A 93 11746 10335 12399 241 -266 1271 N ATOM 330 CA LYS A 93 4.957 -26.835 -3.388 1.00 91.50 C ANISOU 330 CA LYS A 93 11919 10439 12407 253 -306 1300 C ATOM 331 C LYS A 93 5.414 -27.969 -4.278 1.00 92.21 C ANISOU 331 C LYS A 93 11943 10495 12594 254 -422 1256 C ATOM 332 O LYS A 93 5.236 -29.134 -3.964 1.00 91.81 O ANISOU 332 O LYS A 93 11871 10372 12638 249 -418 1312 O ATOM 333 CB LYS A 93 4.587 -27.442 -2.042 0.00 92.58 C ANISOU 333 CB LYS A 93 12141 10514 12521 257 -194 1419 C ATOM 334 CG LYS A 93 5.589 -28.484 -1.542 0.00 20.00 C ATOM 335 CD LYS A 93 4.961 -29.854 -1.261 0.00 20.00 C ATOM 336 CE LYS A 93 5.765 -30.657 -0.237 0.00 20.00 C ATOM 337 NZ LYS A 93 5.148 -31.965 0.134 0.00 20.00 N ATOM 338 N SER A 94 6.005 -27.614 -5.403 1.00 92.91 N ANISOU 338 N SER A 94 12011 10630 12657 266 -511 1159 N ATOM 339 CA SER A 94 6.670 -28.594 -6.269 1.00 93.32 C ANISOU 339 CA SER A 94 12021 10652 12785 277 -613 1106 C ATOM 340 C SER A 94 7.980 -29.153 -5.703 1.00 93.85 C ANISOU 340 C SER A 94 12133 10725 12797 284 -656 1123 C ATOM 341 O SER A 94 8.563 -28.583 -4.778 1.00 93.55 O ANISOU 341 O SER A 94 12170 10724 12650 287 -633 1153 O ATOM 342 CB SER A 94 6.924 -27.984 -7.656 0.00 92.50 C ANISOU 342 CB SER A 94 11911 10575 12658 300 -667 1000 C ATOM 343 OG SER A 94 5.730 -28.204 -8.434 0.00 20.00 O ATOM 344 N LEU A 95 8.425 -30.275 -6.275 1.00 94.76 N ANISOU 344 N LEU A 95 12208 10796 13000 290 -731 1098 N ATOM 345 CA LEU A 95 9.658 -30.954 -5.867 1.00 94.64 C ANISOU 345 CA LEU A 95 12216 10770 12972 298 -788 1106 C ATOM 346 C LEU A 95 10.848 -30.553 -6.743 1.00 94.33 C ANISOU 346 C LEU A 95 12173 10758 12910 319 -832 1017 C ATOM 347 O LEU A 95 11.920 -30.246 -6.222 1.00 95.17 O ANISOU 347 O LEU A 95 12308 10880 12971 325 -854 1011 O ATOM 348 CB LEU A 95 9.514 -32.436 -5.899 0.00 20.00 C ATOM 349 CG LEU A 95 8.240 -32.997 -5.263 0.00 20.00 C ATOM 350 CD1 LEU A 95 8.079 -34.473 -5.593 0.00 20.00 C ATOM 351 CD2 LEU A 95 8.249 -32.778 -3.758 0.00 20.00 C ATOM 352 N GLN A 96 10.655 -30.561 -8.066 1.00 93.38 N ANISOU 352 N GLN A 96 12025 10625 12829 336 -844 946 N ATOM 353 CA GLN A 96 11.709 -30.186 -9.020 1.00 91.66 C ANISOU 353 CA GLN A 96 11819 10411 12596 365 -847 864 C ATOM 354 C GLN A 96 12.194 -28.747 -8.807 1.00 90.24 C ANISOU 354 C GLN A 96 11672 10291 12322 367 -791 842 C ATOM 355 O GLN A 96 11.387 -27.853 -8.541 1.00 89.63 O ANISOU 355 O GLN A 96 11617 10259 12177 357 -748 857 O ATOM 356 CB GLN A 96 11.250 -30.294 -10.410 0.00 20.00 C ATOM 357 CG GLN A 96 10.975 -31.724 -10.832 0.00 20.00 C ATOM 358 CD GLN A 96 10.439 -31.820 -12.244 0.00 20.00 C ATOM 359 OE1 GLN A 96 9.843 -30.872 -12.763 0.00 20.00 O ATOM 360 NE2 GLN A 96 10.643 -32.975 -12.875 0.00 20.00 N ATOM 361 N SER A 97 13.508 -28.537 -8.920 1.00 89.30 N ANISOU 361 N SER A 97 11545 10162 12220 382 -789 805 N ATOM 362 CA SER A 97 14.127 -27.221 -8.684 1.00 88.15 C ANISOU 362 CA SER A 97 11415 10057 12022 384 -745 780 C ATOM 363 C SER A 97 14.020 -26.291 -9.896 1.00 87.61 C ANISOU 363 C SER A 97 11376 9998 11912 412 -664 713 C ATOM 364 O SER A 97 14.065 -25.063 -9.748 1.00 87.49 O ANISOU 364 O SER A 97 11379 10027 11833 410 -614 700 O ATOM 365 CB SER A 97 15.597 -27.375 -8.277 0.00 88.02 C ANISOU 365 CB SER A 97 11358 9998 12086 390 -783 765 C ATOM 366 OG SER A 97 16.295 -26.159 -8.222 0.00 20.00 O ATOM 367 N LEU A 98 13.839 -26.874 -11.077 1.00 86.68 N ANISOU 367 N LEU A 98 11279 9830 11823 444 -654 671 N ATOM 368 CA LEU A 98 13.622 -26.094 -12.289 1.00 85.63 C ANISOU 368 CA LEU A 98 11218 9689 11628 485 -585 610 C ATOM 369 C LEU A 98 12.201 -25.537 -12.320 1.00 84.85 C ANISOU 369 C LEU A 98 11151 9635 11450 476 -600 621 C ATOM 370 O LEU A 98 11.990 -24.362 -12.622 1.00 85.18 O ANISOU 370 O LEU A 98 11234 9716 11415 484 -543 598 O ATOM 371 CB LEU A 98 13.881 -26.949 -13.531 0.00 20.00 C ATOM 372 CG LEU A 98 13.724 -26.247 -14.881 0.00 20.00 C ATOM 373 CD1 LEU A 98 14.447 -24.909 -14.878 0.00 20.00 C ATOM 374 CD2 LEU A 98 14.232 -27.132 -16.010 0.00 20.00 C ATOM 375 N GLN A 99 11.220 -26.324 -11.930 1.00 83.90 N ANISOU 375 N GLN A 99 11003 9503 11372 457 -675 658 N ATOM 376 CA GLN A 99 9.862 -25.831 -11.986 1.00 82.91 C ANISOU 376 CA GLN A 99 10881 9394 11225 446 -694 670 C ATOM 377 C GLN A 99 9.536 -24.899 -10.852 1.00 82.34 C ANISOU 377 C GLN A 99 10792 9400 11092 407 -640 718 C ATOM 378 O GLN A 99 8.637 -24.098 -10.953 1.00 82.16 O ANISOU 378 O GLN A 99 10788 9401 11028 408 -620 707 O ATOM 379 CB GLN A 99 8.865 -26.972 -11.996 0.00 20.00 C ATOM 380 CG GLN A 99 7.618 -26.663 -12.795 0.00 20.00 C ATOM 381 CD GLN A 99 6.376 -27.170 -12.120 0.00 20.00 C ATOM 382 OE1 GLN A 99 6.435 -27.705 -11.012 0.00 20.00 O ATOM 383 NE2 GLN A 99 5.239 -27.010 -12.781 0.00 20.00 N ATOM 384 N SER A 100 10.256 -25.022 -9.758 1.00 81.51 N ANISOU 384 N SER A 100 10663 9324 10982 380 -628 768 N ATOM 385 CA SER A 100 10.046 -24.117 -8.616 1.00 80.22 C ANISOU 385 CA SER A 100 10511 9221 10747 354 -587 816 C ATOM 386 C SER A 100 10.689 -22.741 -8.818 1.00 78.52 C ANISOU 386 C SER A 100 10327 9054 10453 366 -536 771 C ATOM 387 O SER A 100 10.154 -21.743 -8.335 1.00 77.67 O ANISOU 387 O SER A 100 10241 8996 10272 354 -495 788 O ATOM 388 CB SER A 100 10.532 -24.754 -7.301 1.00 80.57 C ANISOU 388 CB SER A 100 10551 9256 10803 334 -616 886 C ATOM 389 OG SER A 100 9.504 -25.532 -6.707 1.00 81.08 O ANISOU 389 OG SER A 100 10605 9292 10907 316 -614 956 O ATOM 390 N THR A 101 11.827 -22.684 -9.513 1.00 77.37 N ANISOU 390 N THR A 101 10180 8882 10333 391 -525 716 N ATOM 391 CA THR A 101 12.401 -21.401 -9.930 1.00 76.47 C ANISOU 391 CA THR A 101 10090 8791 10171 408 -457 666 C ATOM 392 C THR A 101 11.356 -20.590 -10.688 1.00 75.41 C ANISOU 392 C THR A 101 10008 8683 9959 423 -415 637 C ATOM 393 O THR A 101 11.112 -19.427 -10.381 1.00 75.18 O ANISOU 393 O THR A 101 9997 8708 9860 414 -373 637 O ATOM 394 CB THR A 101 13.619 -21.588 -10.851 1.00 76.74 C ANISOU 394 CB THR A 101 10119 8763 10276 442 -417 610 C ATOM 395 OG1 THR A 101 14.727 -22.056 -10.083 1.00 77.02 O ANISOU 395 OG1 THR A 101 10091 8769 10403 428 -460 627 O ATOM 396 CG2 THR A 101 14.004 -20.275 -11.531 1.00 76.62 C ANISOU 396 CG2 THR A 101 10140 8752 10218 468 -316 559 C ATOM 397 N VAL A 102 10.740 -21.223 -11.678 1.00 74.74 N ANISOU 397 N VAL A 102 9953 8551 9893 450 -442 609 N ATOM 398 CA VAL A 102 9.692 -20.583 -12.458 1.00 74.16 C ANISOU 398 CA VAL A 102 9938 8478 9761 474 -438 573 C ATOM 399 C VAL A 102 8.554 -20.094 -11.553 1.00 73.61 C ANISOU 399 C VAL A 102 9831 8462 9674 433 -447 623 C ATOM 400 O VAL A 102 8.044 -18.999 -11.753 1.00 73.72 O ANISOU 400 O VAL A 102 9878 8509 9621 440 -412 601 O ATOM 401 CB VAL A 102 9.175 -21.519 -13.575 1.00 74.19 C ANISOU 401 CB VAL A 102 9986 8397 9803 518 -508 532 C ATOM 402 CG1 VAL A 102 7.908 -20.969 -14.224 1.00 74.11 C ANISOU 402 CG1 VAL A 102 10029 8371 9758 543 -551 496 C ATOM 403 CG2 VAL A 102 10.266 -21.722 -14.618 1.00 74.21 C ANISOU 403 CG2 VAL A 102 10067 8339 9791 574 -462 477 C ATOM 404 N HIS A 103 8.173 -20.890 -10.559 1.00 73.60 N ANISOU 404 N HIS A 103 9769 8460 9734 396 -478 691 N ATOM 405 CA HIS A 103 7.143 -20.475 -9.600 1.00 73.61 C ANISOU 405 CA HIS A 103 9744 8495 9730 362 -451 750 C ATOM 406 C HIS A 103 7.551 -19.232 -8.801 1.00 72.81 C ANISOU 406 C HIS A 103 9672 8467 9524 348 -386 767 C ATOM 407 O HIS A 103 6.708 -18.396 -8.492 1.00 72.05 O ANISOU 407 O HIS A 103 9582 8402 9390 337 -344 782 O ATOM 408 CB HIS A 103 6.770 -21.620 -8.646 1.00 74.29 C ANISOU 408 CB HIS A 103 9781 8546 9899 333 -469 829 C ATOM 409 CG HIS A 103 5.923 -22.684 -9.280 1.00 75.48 C ANISOU 409 CG HIS A 103 9882 8616 10178 339 -531 821 C ATOM 410 ND1 HIS A 103 5.828 -23.963 -8.772 1.00 76.44 N ANISOU 410 ND1 HIS A 103 9958 8686 10398 322 -557 876 N ATOM 411 CD2 HIS A 103 5.136 -22.661 -10.383 1.00 75.89 C ANISOU 411 CD2 HIS A 103 9930 8619 10285 365 -588 761 C ATOM 412 CE1 HIS A 103 5.010 -24.675 -9.527 1.00 76.93 C ANISOU 412 CE1 HIS A 103 9973 8671 10583 333 -623 850 C ATOM 413 NE2 HIS A 103 4.578 -23.909 -10.513 1.00 76.34 N ANISOU 413 NE2 HIS A 103 9926 8592 10484 362 -654 778 N ATOM 414 N TYR A 104 8.824 -19.082 -8.522 1.00 72.73 N ANISOU 414 N TYR A 104 9674 8473 9486 352 -384 759 N ATOM 415 CA TYR A 104 9.274 -17.907 -7.837 1.00 73.08 C ANISOU 415 CA TYR A 104 9745 8572 9447 345 -346 764 C ATOM 416 C TYR A 104 9.197 -16.708 -8.742 1.00 73.05 C ANISOU 416 C TYR A 104 9768 8598 9387 364 -294 700 C ATOM 417 O TYR A 104 8.573 -15.722 -8.432 1.00 71.93 O ANISOU 417 O TYR A 104 9648 8506 9173 355 -254 710 O ATOM 418 CB TYR A 104 10.687 -18.108 -7.343 1.00 73.51 C ANISOU 418 CB TYR A 104 9791 8609 9527 348 -386 766 C ATOM 419 CG TYR A 104 10.766 -19.126 -6.249 1.00 74.75 C ANISOU 419 CG TYR A 104 9955 8738 9708 335 -442 835 C ATOM 420 CD1 TYR A 104 9.697 -19.354 -5.412 1.00 75.10 C ANISOU 420 CD1 TYR A 104 10037 8791 9708 321 -417 908 C ATOM 421 CD2 TYR A 104 11.901 -19.870 -6.056 1.00 75.73 C ANISOU 421 CD2 TYR A 104 10055 8814 9905 342 -511 830 C ATOM 422 CE1 TYR A 104 9.762 -20.292 -4.413 1.00 75.86 C ANISOU 422 CE1 TYR A 104 10164 8845 9811 319 -450 977 C ATOM 423 CE2 TYR A 104 11.972 -20.814 -5.061 1.00 76.27 C ANISOU 423 CE2 TYR A 104 10148 8848 9983 338 -569 892 C ATOM 424 CZ TYR A 104 10.901 -21.014 -4.246 1.00 76.40 C ANISOU 424 CZ TYR A 104 10221 8871 9934 329 -534 967 C ATOM 425 OH TYR A 104 10.991 -21.956 -3.259 0.00 20.00 O ATOM 426 N HIS A 105 9.829 -16.793 -9.886 1.00 61.61 N ANISOU 426 N HIS A 105 11543 5106 6760 450 -432 -912 N ATOM 427 CA HIS A 105 9.754 -15.676 -10.816 1.00 61.40 C ANISOU 427 CA HIS A 105 11299 5265 6763 371 -441 -858 C ATOM 428 C HIS A 105 8.292 -15.270 -11.061 1.00 60.53 C ANISOU 428 C HIS A 105 11186 5227 6583 323 -274 -828 C ATOM 429 O HIS A 105 7.971 -14.080 -11.097 1.00 61.00 O ANISOU 429 O HIS A 105 11232 5321 6625 303 -307 -751 O ATOM 430 CB HIS A 105 10.480 -15.997 -12.124 1.00 62.09 C ANISOU 430 CB HIS A 105 11094 5547 6949 301 -435 -904 C ATOM 431 CG HIS A 105 11.956 -15.746 -12.068 1.00 63.82 C ANISOU 431 CG HIS A 105 11241 5722 7285 325 -618 -906 C ATOM 432 ND1 HIS A 105 12.872 -16.731 -11.764 1.00 65.90 N ANISOU 432 ND1 HIS A 105 11520 5885 7633 378 -696 -983 N ATOM 433 CD2 HIS A 105 12.675 -14.617 -12.280 1.00 64.55 C ANISOU 433 CD2 HIS A 105 11232 5843 7450 305 -738 -848 C ATOM 434 CE1 HIS A 105 14.092 -16.219 -11.791 1.00 66.88 C ANISOU 434 CE1 HIS A 105 11543 5977 7890 390 -862 -980 C ATOM 435 NE2 HIS A 105 14.000 -14.938 -12.104 1.00 65.87 N ANISOU 435 NE2 HIS A 105 11342 5925 7759 343 -882 -899 N ATOM 436 N LEU A 106 7.408 -16.254 -11.199 1.00 59.95 N ANISOU 436 N LEU A 106 11123 5162 6492 307 -99 -896 N ATOM 437 CA LEU A 106 5.984 -15.978 -11.409 1.00 58.98 C ANISOU 437 CA LEU A 106 10980 5086 6343 266 58 -891 C ATOM 438 C LEU A 106 5.352 -15.290 -10.228 1.00 58.67 C ANISOU 438 C LEU A 106 11186 4860 6244 317 79 -831 C ATOM 439 O LEU A 106 4.455 -14.473 -10.410 1.00 58.36 O ANISOU 439 O LEU A 106 11101 4866 6206 285 138 -793 O ATOM 440 CB LEU A 106 5.203 -17.260 -11.679 1.00 59.05 C ANISOU 440 CB LEU A 106 10954 5104 6376 243 242 -993 C ATOM 441 CG LEU A 106 5.360 -17.841 -13.077 1.00 59.09 C ANISOU 441 CG LEU A 106 10686 5330 6433 172 270 -1067 C ATOM 442 CD1 LEU A 106 4.799 -19.258 -13.117 1.00 59.58 C ANISOU 442 CD1 LEU A 106 10750 5353 6534 166 431 -1181 C ATOM 443 CD2 LEU A 106 4.674 -16.959 -14.103 1.00 58.84 C ANISOU 443 CD2 LEU A 106 10465 5489 6400 105 278 -1038 C ATOM 444 N GLY A 107 5.786 -15.649 -9.022 1.00 58.78 N ANISOU 444 N GLY A 107 11473 4657 6204 401 34 -827 N ATOM 445 CA GLY A 107 5.267 -15.024 -7.817 1.00 59.30 C ANISOU 445 CA GLY A 107 11818 4523 6188 458 58 -775 C ATOM 446 C GLY A 107 5.665 -13.555 -7.750 1.00 59.32 C ANISOU 446 C GLY A 107 11800 4554 6185 460 -106 -688 C ATOM 447 O GLY A 107 4.842 -12.680 -7.482 1.00 59.05 O ANISOU 447 O GLY A 107 11817 4487 6130 450 -42 -643 O ATOM 448 N SER A 108 6.942 -13.300 -8.004 1.00 59.04 N ANISOU 448 N SER A 108 11673 4569 6189 471 -312 -672 N ATOM 449 CA SER A 108 7.476 -11.963 -8.038 1.00 59.02 C ANISOU 449 CA SER A 108 11617 4596 6212 466 -474 -599 C ATOM 450 C SER A 108 6.640 -11.124 -9.001 1.00 58.63 C ANISOU 450 C SER A 108 11353 4726 6195 381 -382 -554 C ATOM 451 O SER A 108 6.138 -10.055 -8.639 1.00 57.99 O ANISOU 451 O SER A 108 11338 4598 6094 385 -389 -491 O ATOM 452 CB SER A 108 8.940 -12.021 -8.479 1.00 59.76 C ANISOU 452 CB SER A 108 11561 4748 6397 467 -664 -613 C ATOM 453 OG SER A 108 9.626 -10.812 -8.218 1.00 60.96 O ANISOU 453 OG SER A 108 11711 4859 6588 481 -843 -553 O ATOM 454 N LEU A 109 6.453 -11.640 -10.214 1.00 58.32 N ANISOU 454 N LEU A 109 11071 4883 6203 311 -299 -590 N ATOM 455 CA LEU A 109 5.678 -10.947 -11.236 1.00 57.53 C ANISOU 455 CA LEU A 109 10770 4961 6126 238 -233 -554 C ATOM 456 C LEU A 109 4.282 -10.585 -10.752 1.00 57.49 C ANISOU 456 C LEU A 109 10866 4877 6100 245 -103 -543 C ATOM 457 O LEU A 109 3.836 -9.451 -10.940 1.00 58.45 O ANISOU 457 O LEU A 109 10936 5036 6235 225 -126 -474 O ATOM 458 CB LEU A 109 5.588 -11.795 -12.491 1.00 57.25 C ANISOU 458 CB LEU A 109 10514 5120 6118 176 -155 -619 C ATOM 459 CG LEU A 109 4.764 -11.257 -13.650 1.00 57.45 C ANISOU 459 CG LEU A 109 10344 5334 6150 110 -103 -596 C ATOM 460 CD1 LEU A 109 5.200 -9.851 -14.019 1.00 58.01 C ANISOU 460 CD1 LEU A 109 10346 5470 6226 90 -220 -485 C ATOM 461 CD2 LEU A 109 4.903 -12.186 -14.850 1.00 57.82 C ANISOU 461 CD2 LEU A 109 10203 5560 6204 58 -51 -674 C ATOM 462 N ALA A 110 3.601 -11.527 -10.109 1.00 57.27 N ANISOU 462 N ALA A 110 10981 4723 6052 273 43 -612 N ATOM 463 CA ALA A 110 2.237 -11.282 -9.618 1.00 57.19 C ANISOU 463 CA ALA A 110 11060 4614 6054 276 204 -619 C ATOM 464 C ALA A 110 2.165 -10.233 -8.506 1.00 57.13 C ANISOU 464 C ALA A 110 11276 4431 6000 327 164 -548 C ATOM 465 O ALA A 110 1.118 -9.619 -8.305 1.00 56.98 O ANISOU 465 O ALA A 110 11272 4362 6014 318 269 -534 O ATOM 466 CB ALA A 110 1.598 -12.573 -9.135 1.00 57.45 C ANISOU 466 CB ALA A 110 11210 4527 6092 291 396 -711 C ATOM 467 N LEU A 111 3.252 -10.051 -7.767 1.00 56.89 N ANISOU 467 N LEU A 111 11418 4292 5903 384 10 -515 N ATOM 468 CA LEU A 111 3.261 -9.071 -6.684 1.00 57.84 C ANISOU 468 CA LEU A 111 11770 4238 5967 439 -47 -459 C ATOM 469 C LEU A 111 3.457 -7.662 -7.274 1.00 57.52 C ANISOU 469 C LEU A 111 11554 4316 5982 401 -176 -377 C ATOM 470 O LEU A 111 2.699 -6.745 -6.976 1.00 56.37 O ANISOU 470 O LEU A 111 11453 4116 5849 400 -125 -338 O ATOM 471 CB LEU A 111 4.349 -9.404 -5.642 1.00 57.90 C ANISOU 471 CB LEU A 111 12043 4071 5884 525 -194 -465 C ATOM 472 CG LEU A 111 4.543 -8.396 -4.497 1.00 57.97 C ANISOU 472 CG LEU A 111 12315 3892 5817 591 -299 -418 C ATOM 473 CD1 LEU A 111 3.298 -8.302 -3.634 1.00 58.12 C ANISOU 473 CD1 LEU A 111 12569 3741 5771 613 -80 -425 C ATOM 474 CD2 LEU A 111 5.762 -8.754 -3.660 1.00 58.61 C ANISOU 474 CD2 LEU A 111 12618 3826 5824 680 -504 -435 C ATOM 475 N SER A 112 4.476 -7.527 -8.118 1.00 57.94 N ANISOU 475 N SER A 112 11412 4522 6080 370 -328 -355 N ATOM 476 CA SER A 112 4.753 -6.281 -8.799 1.00 58.84 C ANISOU 476 CA SER A 112 11350 4753 6252 328 -436 -274 C ATOM 477 C SER A 112 3.543 -5.832 -9.612 1.00 59.78 C ANISOU 477 C SER A 112 11303 4996 6411 272 -315 -249 C ATOM 478 O SER A 112 3.266 -4.639 -9.685 1.00 60.76 O ANISOU 478 O SER A 112 11391 5126 6567 262 -357 -176 O ATOM 479 CB SER A 112 5.987 -6.399 -9.691 1.00 58.68 C ANISOU 479 CB SER A 112 11134 4876 6283 293 -564 -266 C ATOM 480 OG SER A 112 5.730 -7.214 -10.816 1.00 58.92 O ANISOU 480 OG SER A 112 10970 5087 6328 237 -467 -307 O ATOM 481 N ASP A 113 2.800 -6.769 -10.196 1.00 60.38 N ANISOU 481 N ASP A 113 11280 5160 6500 242 -177 -315 N ATOM 482 CA ASP A 113 1.547 -6.398 -10.858 1.00 60.84 C ANISOU 482 CA ASP A 113 11195 5306 6615 203 -79 -311 C ATOM 483 C ASP A 113 0.461 -5.954 -9.880 1.00 60.21 C ANISOU 483 C ASP A 113 11271 5045 6559 235 38 -315 C ATOM 484 O ASP A 113 -0.194 -4.941 -10.111 1.00 60.70 O ANISOU 484 O ASP A 113 11257 5127 6679 222 33 -264 O ATOM 485 CB ASP A 113 1.047 -7.528 -11.742 1.00 62.44 C ANISOU 485 CB ASP A 113 11241 5639 6841 164 20 -398 C ATOM 486 CG ASP A 113 1.774 -7.577 -13.065 1.00 64.93 C ANISOU 486 CG ASP A 113 11348 6177 7144 115 -78 -378 C ATOM 487 OD1 ASP A 113 2.518 -6.598 -13.362 1.00 66.56 O ANISOU 487 OD1 ASP A 113 11511 6437 7341 104 -204 -285 O ATOM 488 OD2 ASP A 113 1.596 -8.581 -13.810 1.00 67.15 O ANISOU 488 OD2 ASP A 113 11513 6571 7429 85 -17 -458 O ATOM 489 N LEU A 114 0.276 -6.696 -8.791 1.00 58.91 N ANISOU 489 N LEU A 114 11335 4694 6353 280 153 -375 N ATOM 490 CA LEU A 114 -0.687 -6.307 -7.762 1.00 58.50 C ANISOU 490 CA LEU A 114 11470 4441 6315 312 296 -384 C ATOM 491 C LEU A 114 -0.387 -4.884 -7.241 1.00 58.35 C ANISOU 491 C LEU A 114 11544 4348 6278 339 176 -295 C ATOM 492 O LEU A 114 -1.289 -4.069 -7.045 1.00 57.18 O ANISOU 492 O LEU A 114 11391 4137 6195 336 252 -276 O ATOM 493 CB LEU A 114 -0.638 -7.307 -6.609 1.00 58.68 C ANISOU 493 CB LEU A 114 11781 4257 6254 365 420 -445 C ATOM 494 CG LEU A 114 -1.559 -7.140 -5.400 1.00 59.43 C ANISOU 494 CG LEU A 114 12137 4107 6337 403 617 -467 C ATOM 495 CD1 LEU A 114 -3.024 -7.195 -5.811 1.00 59.65 C ANISOU 495 CD1 LEU A 114 11998 4145 6522 357 830 -522 C ATOM 496 CD2 LEU A 114 -1.237 -8.229 -4.381 1.00 60.21 C ANISOU 496 CD2 LEU A 114 12545 4017 6314 460 708 -513 C ATOM 497 N LEU A 115 0.896 -4.614 -7.032 1.00 58.03 N ANISOU 497 N LEU A 115 11575 4307 6167 364 -13 -250 N ATOM 498 CA LEU A 115 1.352 -3.368 -6.463 1.00 58.45 C ANISOU 498 CA LEU A 115 11731 4272 6204 393 -145 -180 C ATOM 499 C LEU A 115 1.181 -2.193 -7.435 1.00 58.21 C ANISOU 499 C LEU A 115 11454 4393 6269 342 -222 -99 C ATOM 500 O LEU A 115 0.924 -1.077 -7.008 1.00 57.61 O ANISOU 500 O LEU A 115 11437 4232 6219 356 -249 -50 O ATOM 501 CB LEU A 115 2.816 -3.495 -6.025 1.00 58.95 C ANISOU 501 CB LEU A 115 11910 4287 6199 434 -343 -174 C ATOM 502 CG LEU A 115 3.120 -4.333 -4.778 1.00 59.76 C ANISOU 502 CG LEU A 115 12339 4181 6183 512 -327 -233 C ATOM 503 CD1 LEU A 115 4.610 -4.625 -4.693 1.00 59.82 C ANISOU 503 CD1 LEU A 115 12370 4190 6170 546 -553 -240 C ATOM 504 CD2 LEU A 115 2.650 -3.620 -3.519 1.00 60.53 C ANISOU 504 CD2 LEU A 115 12734 4053 6209 570 -284 -225 C ATOM 505 N ILE A 116 1.316 -2.430 -8.735 1.00 57.98 N ANISOU 505 N ILE A 116 11166 4580 6283 286 -255 -85 N ATOM 506 CA ILE A 116 1.024 -1.374 -9.682 1.00 57.86 C ANISOU 506 CA ILE A 116 10947 4697 6340 244 -312 -4 C ATOM 507 C ILE A 116 -0.428 -0.956 -9.457 1.00 58.80 C ANISOU 507 C ILE A 116 11067 4743 6530 250 -177 -17 C ATOM 508 O ILE A 116 -0.721 0.226 -9.233 1.00 59.15 O ANISOU 508 O ILE A 116 11123 4727 6624 259 -212 45 O ATOM 509 CB ILE A 116 1.257 -1.782 -11.154 1.00 57.13 C ANISOU 509 CB ILE A 116 10607 4842 6257 187 -346 5 C ATOM 510 CG1 ILE A 116 2.751 -1.815 -11.463 1.00 56.64 C ANISOU 510 CG1 ILE A 116 10509 4845 6165 174 -481 37 C ATOM 511 CG2 ILE A 116 0.617 -0.761 -12.086 1.00 57.57 C ANISOU 511 CG2 ILE A 116 10490 5010 6371 156 -378 84 C ATOM 512 CD1 ILE A 116 3.098 -2.458 -12.785 1.00 56.36 C ANISOU 512 CD1 ILE A 116 10277 5020 6116 122 -482 26 C ATOM 513 N LEU A 117 -1.331 -1.928 -9.492 1.00 58.67 N ANISOU 513 N LEU A 117 11032 4718 6541 245 -19 -107 N ATOM 514 CA LEU A 117 -2.754 -1.617 -9.433 1.00 59.30 C ANISOU 514 CA LEU A 117 11059 4735 6735 243 116 -138 C ATOM 515 C LEU A 117 -3.160 -0.935 -8.124 1.00 59.81 C ANISOU 515 C LEU A 117 11347 4564 6811 287 202 -134 C ATOM 516 O LEU A 117 -4.033 -0.076 -8.137 1.00 60.62 O ANISOU 516 O LEU A 117 11385 4622 7025 286 243 -114 O ATOM 517 CB LEU A 117 -3.595 -2.872 -9.667 1.00 59.45 C ANISOU 517 CB LEU A 117 11011 4768 6808 227 280 -253 C ATOM 518 CG LEU A 117 -3.470 -3.496 -11.060 1.00 59.41 C ANISOU 518 CG LEU A 117 10767 4997 6808 183 207 -274 C ATOM 519 CD1 LEU A 117 -3.981 -4.926 -11.059 1.00 59.83 C ANISOU 519 CD1 LEU A 117 10804 5033 6893 172 363 -402 C ATOM 520 CD2 LEU A 117 -4.199 -2.676 -12.109 1.00 59.60 C ANISOU 520 CD2 LEU A 117 10567 5149 6929 161 130 -234 C ATOM 521 N LEU A 118 -2.523 -1.305 -7.012 1.00 59.96 N ANISOU 521 N LEU A 118 11637 4428 6716 329 222 -155 N ATOM 522 CA LEU A 118 -2.900 -0.797 -5.680 1.00 61.08 C ANISOU 522 CA LEU A 118 12046 4327 6834 376 324 -166 C ATOM 523 C LEU A 118 -2.285 0.562 -5.361 1.00 61.67 C ANISOU 523 C LEU A 118 12182 4359 6888 397 157 -79 C ATOM 524 O LEU A 118 -2.865 1.338 -4.612 1.00 61.94 O ANISOU 524 O LEU A 118 12344 4236 6955 421 235 -76 O ATOM 525 CB LEU A 118 -2.460 -1.761 -4.569 1.00 61.56 C ANISOU 525 CB LEU A 118 12420 4218 6750 425 400 -223 C ATOM 526 CG LEU A 118 -3.104 -3.132 -4.391 1.00 61.70 C ANISOU 526 CG LEU A 118 12496 4177 6770 422 621 -318 C ATOM 527 CD1 LEU A 118 -2.470 -3.787 -3.176 1.00 62.09 C ANISOU 527 CD1 LEU A 118 12913 4034 6644 487 646 -343 C ATOM 528 CD2 LEU A 118 -4.617 -3.052 -4.233 1.00 62.50 C ANISOU 528 CD2 LEU A 118 12553 4175 7019 403 877 -376 C ATOM 529 N LEU A 119 -1.098 0.816 -5.906 1.00 62.11 N ANISOU 529 N LEU A 119 12149 4545 6904 385 -57 -17 N ATOM 530 CA LEU A 119 -0.332 2.021 -5.622 1.00 62.66 C ANISOU 530 CA LEU A 119 12266 4571 6968 401 -231 56 C ATOM 531 C LEU A 119 -0.456 3.117 -6.682 1.00 63.40 C ANISOU 531 C LEU A 119 12100 4812 7176 355 -322 149 C ATOM 532 O LEU A 119 -0.445 4.317 -6.351 1.00 63.92 O ANISOU 532 O LEU A 119 12200 4797 7287 367 -384 204 O ATOM 533 CB LEU A 119 1.139 1.654 -5.461 1.00 62.32 C ANISOU 533 CB LEU A 119 12297 4543 6839 419 -411 58 C ATOM 534 CG LEU A 119 1.414 0.650 -4.350 1.00 62.85 C ANISOU 534 CG LEU A 119 12658 4445 6775 480 -367 -22 C ATOM 535 CD1 LEU A 119 2.911 0.375 -4.275 1.00 63.10 C ANISOU 535 CD1 LEU A 119 12723 4491 6759 503 -584 -23 C ATOM 536 CD2 LEU A 119 0.874 1.165 -3.026 1.00 63.58 C ANISOU 536 CD2 LEU A 119 13053 4294 6807 537 -282 -45 C ATOM 537 N ALA A 120 -0.551 2.722 -7.946 1.00 63.00 N ANISOU 537 N ALA A 120 11804 4967 7163 307 -334 168 N ATOM 538 CA ALA A 120 -0.595 3.697 -9.017 1.00 63.73 C ANISOU 538 CA ALA A 120 11678 5200 7335 270 -428 266 C ATOM 539 C ALA A 120 -2.012 4.139 -9.363 1.00 65.49 C ANISOU 539 C ALA A 120 11788 5425 7670 265 -332 268 C ATOM 540 O ALA A 120 -2.227 5.302 -9.706 1.00 68.84 O ANISOU 540 O ALA A 120 12126 5859 8170 261 -400 352 O ATOM 541 CB ALA A 120 0.106 3.164 -10.248 1.00 63.55 C ANISOU 541 CB ALA A 120 11474 5393 7279 225 -506 292 C ATOM 542 N MET A 121 -2.984 3.239 -9.272 1.00 66.22 N ANISOU 542 N MET A 121 11872 5494 7793 269 -176 173 N ATOM 543 CA MET A 121 -4.318 3.539 -9.803 1.00 67.46 C ANISOU 543 CA MET A 121 11866 5673 8093 262 -106 158 C ATOM 544 C MET A 121 -5.212 4.479 -8.982 1.00 67.88 C ANISOU 544 C MET A 121 11992 5534 8264 292 -17 155 C ATOM 545 O MET A 121 -5.818 5.376 -9.552 1.00 67.85 O ANISOU 545 O MET A 121 11837 5563 8378 290 -71 209 O ATOM 546 CB MET A 121 -5.088 2.260 -10.096 1.00 68.19 C ANISOU 546 CB MET A 121 11881 5805 8221 249 27 43 C ATOM 547 CG MET A 121 -6.400 2.534 -10.801 1.00 69.57 C ANISOU 547 CG MET A 121 11847 6017 8569 244 57 17 C ATOM 548 SD MET A 121 -6.992 1.140 -11.773 1.00 71.39 S ANISOU 548 SD MET A 121 11892 6394 8840 216 104 -96 S ATOM 549 CE MET A 121 -8.716 1.294 -11.312 1.00 72.34 C ANISOU 549 CE MET A 121 11933 6333 9217 234 283 -201 C ATOM 550 N PRO A 122 -5.332 4.254 -7.663 1.00 68.66 N ANISOU 550 N PRO A 122 12331 5425 8330 323 125 89 N ATOM 551 CA PRO A 122 -6.247 5.069 -6.853 1.00 69.15 C ANISOU 551 CA PRO A 122 12474 5290 8508 349 248 69 C ATOM 552 C PRO A 122 -6.051 6.572 -7.044 1.00 69.39 C ANISOU 552 C PRO A 122 12445 5322 8598 355 101 178 C ATOM 553 O PRO A 122 -7.012 7.307 -7.303 1.00 69.25 O ANISOU 553 O PRO A 122 12293 5270 8747 359 132 189 O ATOM 554 CB PRO A 122 -5.892 4.667 -5.421 1.00 69.38 C ANISOU 554 CB PRO A 122 12837 5114 8408 385 367 11 C ATOM 555 CG PRO A 122 -5.412 3.267 -5.546 1.00 69.63 C ANISOU 555 CG PRO A 122 12911 5219 8325 376 392 -41 C ATOM 556 CD PRO A 122 -4.682 3.203 -6.857 1.00 68.71 C ANISOU 556 CD PRO A 122 12561 5356 8188 339 189 26 C ATOM 557 N VAL A 123 -4.801 7.004 -6.927 1.00 68.75 N ANISOU 557 N VAL A 123 12453 5271 8398 357 -60 252 N ATOM 558 CA VAL A 123 -4.433 8.405 -7.070 1.00 69.07 C ANISOU 558 CA VAL A 123 12451 5302 8488 359 -203 358 C ATOM 559 C VAL A 123 -4.561 8.894 -8.520 1.00 68.65 C ANISOU 559 C VAL A 123 12123 5445 8515 327 -328 455 C ATOM 560 O VAL A 123 -5.020 10.006 -8.764 1.00 69.01 O ANISOU 560 O VAL A 123 12080 5461 8678 334 -372 522 O ATOM 561 CB VAL A 123 -3.007 8.633 -6.541 1.00 68.68 C ANISOU 561 CB VAL A 123 12563 5219 8313 367 -342 393 C ATOM 562 CG1 VAL A 123 -2.462 9.988 -6.966 1.00 69.12 C ANISOU 562 CG1 VAL A 123 12523 5304 8435 354 -505 509 C ATOM 563 CG2 VAL A 123 -3.016 8.497 -5.030 1.00 69.59 C ANISOU 563 CG2 VAL A 123 12985 5103 8351 415 -244 309 C ATOM 564 N GLU A 124 -4.156 8.071 -9.478 1.00 67.46 N ANISOU 564 N GLU A 124 11852 5484 8292 297 -384 462 N ATOM 565 CA GLU A 124 -4.347 8.421 -10.867 1.00 66.90 C ANISOU 565 CA GLU A 124 11558 5594 8265 273 -490 546 C ATOM 566 C GLU A 124 -5.816 8.714 -11.134 1.00 67.44 C ANISOU 566 C GLU A 124 11498 5626 8498 293 -429 516 C ATOM 567 O GLU A 124 -6.146 9.697 -11.798 1.00 69.38 O ANISOU 567 O GLU A 124 11624 5907 8829 299 -528 607 O ATOM 568 CB GLU A 124 -3.865 7.307 -11.790 1.00 66.30 C ANISOU 568 CB GLU A 124 11394 5713 8082 241 -522 526 C ATOM 569 CG GLU A 124 -4.307 7.529 -13.229 1.00 66.86 C ANISOU 569 CG GLU A 124 11261 5960 8182 226 -613 591 C ATOM 570 CD GLU A 124 -3.452 6.817 -14.247 1.00 66.89 C ANISOU 570 CD GLU A 124 11200 6162 8051 189 -679 615 C ATOM 571 OE1 GLU A 124 -4.012 6.405 -15.291 1.00 68.04 O ANISOU 571 OE1 GLU A 124 11213 6447 8190 182 -709 601 O ATOM 572 OE2 GLU A 124 -2.226 6.683 -14.019 1.00 66.20 O ANISOU 572 OE2 GLU A 124 11191 6085 7874 168 -706 640 O ATOM 573 N LEU A 125 -6.700 7.871 -10.617 1.00 66.91 N ANISOU 573 N LEU A 125 11455 5475 8493 304 -266 387 N ATOM 574 CA LEU A 125 -8.127 8.002 -10.912 1.00 67.25 C ANISOU 574 CA LEU A 125 11342 5477 8732 321 -203 331 C ATOM 575 C LEU A 125 -8.714 9.305 -10.347 1.00 67.79 C ANISOU 575 C LEU A 125 11426 5375 8953 352 -185 368 C ATOM 576 O LEU A 125 -9.575 9.926 -10.970 1.00 67.36 O ANISOU 576 O LEU A 125 11198 5331 9062 369 -244 392 O ATOM 577 CB LEU A 125 -8.897 6.784 -10.388 1.00 66.61 C ANISOU 577 CB LEU A 125 11285 5314 8709 320 0 173 C ATOM 578 CG LEU A 125 -10.314 6.506 -10.906 1.00 67.27 C ANISOU 578 CG LEU A 125 11155 5389 9013 328 61 79 C ATOM 579 CD1 LEU A 125 -10.462 6.768 -12.400 1.00 67.25 C ANISOU 579 CD1 LEU A 125 10928 5590 9034 328 -155 144 C ATOM 580 CD2 LEU A 125 -10.696 5.062 -10.578 1.00 67.54 C ANISOU 580 CD2 LEU A 125 11214 5388 9060 311 247 -68 C ATOM 581 N TYR A 126 -8.190 9.753 -9.235 1.00 68.09 N ANISOU 581 N TYR A 126 11677 5252 8941 363 -115 369 N ATOM 582 CA TYR A 126 -8.711 10.944 -8.629 1.00 69.75 C ANISOU 582 CA TYR A 126 11923 5288 9290 391 -85 395 C ATOM 583 C TYR A 126 -8.101 12.193 -9.221 1.00 69.18 C ANISOU 583 C TYR A 126 11779 5293 9213 389 -293 551 C ATOM 584 O TYR A 126 -8.788 13.103 -9.591 1.00 68.67 O ANISOU 584 O TYR A 126 11575 5207 9309 408 -348 601 O ATOM 585 CB TYR A 126 -8.420 10.901 -7.149 1.00 70.64 C ANISOU 585 CB TYR A 126 12317 5186 9335 408 66 329 C ATOM 586 CG TYR A 126 -8.888 12.115 -6.453 1.00 72.93 C ANISOU 586 CG TYR A 126 12663 5288 9759 436 107 346 C ATOM 587 CD1 TYR A 126 -10.226 12.403 -6.390 1.00 74.56 C ANISOU 587 CD1 TYR A 126 12754 5375 10198 453 245 281 C ATOM 588 CD2 TYR A 126 -8.000 12.988 -5.884 1.00 73.13 C ANISOU 588 CD2 TYR A 126 12839 5247 9699 445 5 417 C ATOM 589 CE1 TYR A 126 -10.677 13.523 -5.765 1.00 76.00 C ANISOU 589 CE1 TYR A 126 12979 5379 10518 479 291 291 C ATOM 590 CE2 TYR A 126 -8.444 14.111 -5.256 1.00 75.20 C ANISOU 590 CE2 TYR A 126 13150 5334 10088 470 43 426 C ATOM 591 CZ TYR A 126 -9.786 14.362 -5.202 1.00 76.21 C ANISOU 591 CZ TYR A 126 13169 5348 10438 487 191 366 C ATOM 592 OH TYR A 126 -10.243 15.480 -4.580 0.00 20.00 O ATOM 593 N ASN A 127 -6.790 12.197 -9.311 1.00 68.47 N ANISOU 593 N ASN A 127 11774 5288 8952 367 -406 623 N ATOM 594 CA ASN A 127 -6.006 13.375 -9.636 1.00 68.96 C ANISOU 594 CA ASN A 127 11820 5373 9007 360 -564 760 C ATOM 595 C ASN A 127 -5.525 13.537 -11.077 1.00 68.66 C ANISOU 595 C ASN A 127 11618 5547 8923 333 -723 884 C ATOM 596 O ASN A 127 -5.163 14.654 -11.466 1.00 69.51 O ANISOU 596 O ASN A 127 11686 5655 9070 330 -831 1007 O ATOM 597 CB ASN A 127 -4.781 13.432 -8.718 1.00 69.44 C ANISOU 597 CB ASN A 127 12085 5354 8944 354 -588 755 C ATOM 598 CG ASN A 127 -4.915 14.459 -7.618 1.00 71.10 C ANISOU 598 CG ASN A 127 12438 5346 9231 384 -553 744 C ATOM 599 OD1 ASN A 127 -6.011 14.899 -7.264 1.00 73.55 O ANISOU 599 OD1 ASN A 127 12733 5533 9679 410 -450 706 O ATOM 600 ND2 ASN A 127 -3.791 14.845 -7.067 1.00 70.88 N ANISOU 600 ND2 ASN A 127 12543 5259 9125 381 -641 767 N ATOM 601 N PHE A 128 -5.461 12.452 -11.847 1.00 67.64 N ANISOU 601 N PHE A 128 11413 5584 8701 313 -729 853 N ATOM 602 CA PHE A 128 -5.083 12.552 -13.264 1.00 68.40 C ANISOU 602 CA PHE A 128 11376 5878 8733 290 -861 963 C ATOM 603 C PHE A 128 -6.237 12.305 -14.237 1.00 69.28 C ANISOU 603 C PHE A 128 11325 6084 8914 310 -894 947 C ATOM 604 O PHE A 128 -6.092 12.549 -15.435 1.00 70.07 O ANISOU 604 O PHE A 128 11336 6328 8958 305 -1016 1047 O ATOM 605 CB PHE A 128 -3.928 11.614 -13.618 1.00 68.06 C ANISOU 605 CB PHE A 128 11366 5975 8517 248 -877 956 C ATOM 606 CG PHE A 128 -2.654 11.870 -12.852 1.00 68.35 C ANISOU 606 CG PHE A 128 11535 5935 8499 230 -892 975 C ATOM 607 CD1 PHE A 128 -2.209 13.157 -12.595 1.00 69.28 C ANISOU 607 CD1 PHE A 128 11682 5954 8684 231 -959 1072 C ATOM 608 CD2 PHE A 128 -1.876 10.803 -12.415 1.00 68.28 C ANISOU 608 CD2 PHE A 128 11613 5945 8383 215 -854 891 C ATOM 609 CE1 PHE A 128 -1.027 13.374 -11.899 1.00 69.51 C ANISOU 609 CE1 PHE A 128 11819 5904 8685 217 -993 1073 C ATOM 610 CE2 PHE A 128 -0.697 11.014 -11.718 1.00 68.31 C ANISOU 610 CE2 PHE A 128 11729 5869 8355 207 -898 896 C ATOM 611 CZ PHE A 128 -0.268 12.301 -11.462 1.00 68.49 C ANISOU 611 CZ PHE A 128 11772 5793 8455 207 -972 982 C ATOM 612 N ILE A 129 -7.379 11.833 -13.743 1.00 69.35 N ANISOU 612 N ILE A 129 11298 6001 9048 337 -788 819 N ATOM 613 CA ILE A 129 -8.543 11.637 -14.607 1.00 69.95 C ANISOU 613 CA ILE A 129 11200 6141 9235 363 -838 783 C ATOM 614 C ILE A 129 -9.669 12.628 -14.317 1.00 70.89 C ANISOU 614 C ILE A 129 11242 6102 9590 410 -838 782 C ATOM 615 O ILE A 129 -10.130 13.302 -15.234 1.00 72.08 O ANISOU 615 O ILE A 129 11273 6304 9808 440 -988 864 O ATOM 616 CB ILE A 129 -9.071 10.194 -14.518 1.00 69.78 C ANISOU 616 CB ILE A 129 11139 6153 9220 354 -725 619 C ATOM 617 CG1 ILE A 129 -7.956 9.192 -14.867 1.00 69.02 C ANISOU 617 CG1 ILE A 129 11107 6215 8900 310 -731 618 C ATOM 618 CG2 ILE A 129 -10.272 10.002 -15.437 1.00 70.95 C ANISOU 618 CG2 ILE A 129 11089 6359 9508 384 -803 566 C ATOM 619 CD1 ILE A 129 -7.366 9.345 -16.260 1.00 68.99 C ANISOU 619 CD1 ILE A 129 11036 6417 8759 296 -900 734 C ATOM 620 N TRP A 130 -10.093 12.721 -13.055 1.00 70.86 N ANISOU 620 N TRP A 130 11320 5898 9705 419 -671 691 N ATOM 621 CA TRP A 130 -11.261 13.537 -12.655 1.00 72.24 C ANISOU 621 CA TRP A 130 11414 5895 10137 462 -626 656 C ATOM 622 C TRP A 130 -10.926 14.981 -12.214 1.00 71.89 C ANISOU 622 C TRP A 130 11445 5731 10139 477 -672 771 C ATOM 623 O TRP A 130 -11.630 15.917 -12.570 1.00 72.62 O ANISOU 623 O TRP A 130 11420 5766 10407 515 -755 822 O ATOM 624 CB TRP A 130 -12.053 12.829 -11.528 1.00 72.62 C ANISOU 624 CB TRP A 130 11510 5767 10314 464 -377 478 C ATOM 625 CG TRP A 130 -12.886 11.653 -11.987 1.00 73.21 C ANISOU 625 CG TRP A 130 11440 5900 10475 461 -322 344 C ATOM 626 CD1 TRP A 130 -12.555 10.325 -11.899 1.00 72.47 C ANISOU 626 CD1 TRP A 130 11403 5881 10250 428 -227 257 C ATOM 627 CD2 TRP A 130 -14.181 11.699 -12.604 1.00 74.49 C ANISOU 627 CD2 TRP A 130 11366 6039 10895 495 -367 273 C ATOM 628 NE1 TRP A 130 -13.560 9.548 -12.433 1.00 73.35 N ANISOU 628 NE1 TRP A 130 11329 6021 10520 434 -203 136 N ATOM 629 CE2 TRP A 130 -14.569 10.366 -12.868 1.00 74.74 C ANISOU 629 CE2 TRP A 130 11318 6136 10941 476 -294 138 C ATOM 630 CE3 TRP A 130 -15.049 12.733 -12.958 1.00 76.11 C ANISOU 630 CE3 TRP A 130 11414 6166 11335 543 -473 304 C ATOM 631 CZ2 TRP A 130 -15.787 10.046 -13.467 1.00 75.91 C ANISOU 631 CZ2 TRP A 130 11229 6273 11340 502 -330 26 C ATOM 632 CZ3 TRP A 130 -16.262 12.409 -13.559 1.00 77.54 C ANISOU 632 CZ3 TRP A 130 11360 6336 11764 575 -519 195 C ATOM 633 CH2 TRP A 130 -16.615 11.079 -13.806 1.00 77.24 C ANISOU 633 CH2 TRP A 130 11241 6363 11742 553 -451 53 C ATOM 634 N VAL A 131 -9.869 15.136 -11.420 1.00 71.03 N ANISOU 634 N VAL A 131 11526 5574 9887 451 -625 801 N ATOM 635 CA VAL A 131 -9.525 16.405 -10.769 1.00 70.76 C ANISOU 635 CA VAL A 131 11586 5395 9903 462 -640 876 C ATOM 636 C VAL A 131 -8.050 16.695 -11.013 1.00 69.87 C ANISOU 636 C VAL A 131 11565 5380 9602 428 -760 996 C ATOM 637 O VAL A 131 -7.181 16.277 -10.242 1.00 68.52 O ANISOU 637 O VAL A 131 11557 5176 9300 406 -706 953 O ATOM 638 CB VAL A 131 -9.773 16.349 -9.241 1.00 71.03 C ANISOU 638 CB VAL A 131 11797 5206 9983 472 -437 752 C ATOM 639 CG1 VAL A 131 -9.483 17.701 -8.590 1.00 71.31 C ANISOU 639 CG1 VAL A 131 11925 5085 10083 487 -462 817 C ATOM 640 CG2 VAL A 131 -11.197 15.895 -8.940 1.00 71.85 C ANISOU 640 CG2 VAL A 131 11814 5198 10287 496 -268 612 C ATOM 641 N HIS A 132 -7.776 17.452 -12.068 1.00 70.28 N ANISOU 641 N HIS A 132 11514 5533 9653 427 -920 1145 N ATOM 642 CA HIS A 132 -6.416 17.602 -12.568 1.00 69.49 C ANISOU 642 CA HIS A 132 11459 5549 9393 386 -1020 1260 C ATOM 643 C HIS A 132 -5.664 18.635 -11.748 1.00 69.57 C ANISOU 643 C HIS A 132 11584 5412 9438 378 -1029 1309 C ATOM 644 O HIS A 132 -4.446 18.548 -11.601 1.00 69.53 O ANISOU 644 O HIS A 132 11659 5437 9321 342 -1061 1336 O ATOM 645 CB HIS A 132 -6.432 17.969 -14.048 1.00 70.06 C ANISOU 645 CB HIS A 132 11403 5778 9438 386 -1164 1402 C ATOM 646 CG HIS A 132 -7.268 17.050 -14.878 1.00 70.45 C ANISOU 646 CG HIS A 132 11339 5959 9469 404 -1185 1344 C ATOM 647 ND1 HIS A 132 -8.645 17.109 -14.889 1.00 71.66 N ANISOU 647 ND1 HIS A 132 11383 6043 9800 453 -1180 1275 N ATOM 648 CD2 HIS A 132 -6.928 16.033 -15.705 1.00 70.26 C ANISOU 648 CD2 HIS A 132 11287 6123 9286 379 -1214 1331 C ATOM 649 CE1 HIS A 132 -9.117 16.177 -15.696 1.00 71.83 C ANISOU 649 CE1 HIS A 132 11311 6204 9776 460 -1218 1219 C ATOM 650 NE2 HIS A 132 -8.096 15.511 -16.206 1.00 71.12 N ANISOU 650 NE2 HIS A 132 11275 6274 9471 415 -1238 1254 N ATOM 651 N HIS A 133 -6.397 19.604 -11.208 1.00 70.48 N ANISOU 651 N HIS A 133 11696 5357 9723 414 -1004 1308 N ATOM 652 CA HIS A 133 -5.817 20.595 -10.319 1.00 70.84 C ANISOU 652 CA HIS A 133 11857 5238 9820 412 -1006 1329 C ATOM 653 C HIS A 133 -6.813 20.946 -9.215 1.00 71.47 C ANISOU 653 C HIS A 133 11999 5106 10048 453 -880 1219 C ATOM 654 O HIS A 133 -8.022 21.019 -9.471 1.00 71.89 O ANISOU 654 O HIS A 133 11937 5130 10247 486 -838 1192 O ATOM 655 CB HIS A 133 -5.435 21.849 -11.097 1.00 71.86 C ANISOU 655 CB HIS A 133 11904 5378 10018 405 -1135 1503 C ATOM 656 CG HIS A 133 -6.611 22.632 -11.596 1.00 73.19 C ANISOU 656 CG HIS A 133 11947 5498 10363 451 -1169 1561 C ATOM 657 ND1 HIS A 133 -7.097 23.741 -10.939 1.00 74.11 N ANISOU 657 ND1 HIS A 133 12077 5419 10661 482 -1148 1563 N ATOM 658 CD2 HIS A 133 -7.404 22.459 -12.679 1.00 74.10 C ANISOU 658 CD2 HIS A 133 11921 5724 10508 478 -1237 1611 C ATOM 659 CE1 HIS A 133 -8.130 24.226 -11.603 1.00 75.27 C ANISOU 659 CE1 HIS A 133 12085 5557 10956 526 -1200 1617 C ATOM 660 NE2 HIS A 133 -8.338 23.467 -12.663 1.00 75.00 N ANISOU 660 NE2 HIS A 133 11958 5706 10830 527 -1265 1646 N ATOM 661 N PRO A 134 -6.320 21.153 -7.992 1.00 71.42 N ANISOU 661 N PRO A 134 12179 4944 10011 453 -819 1147 N ATOM 662 CA PRO A 134 -4.898 21.040 -7.672 1.00 70.62 C ANISOU 662 CA PRO A 134 12202 4866 9764 422 -894 1161 C ATOM 663 C PRO A 134 -4.501 19.629 -7.220 1.00 69.77 C ANISOU 663 C PRO A 134 12216 4813 9477 412 -829 1047 C ATOM 664 O PRO A 134 -5.357 18.830 -6.833 1.00 69.21 O ANISOU 664 O PRO A 134 12186 4712 9399 432 -690 939 O ATOM 665 CB PRO A 134 -4.745 21.997 -6.502 1.00 71.21 C ANISOU 665 CB PRO A 134 12428 4717 9911 442 -874 1119 C ATOM 666 CG PRO A 134 -6.050 21.875 -5.779 1.00 71.97 C ANISOU 666 CG PRO A 134 12576 4672 10098 482 -701 1005 C ATOM 667 CD PRO A 134 -7.106 21.553 -6.810 1.00 72.02 C ANISOU 667 CD PRO A 134 12366 4795 10202 489 -678 1038 C ATOM 668 N TRP A 135 -3.201 19.354 -7.288 1.00 69.01 N ANISOU 668 N TRP A 135 12170 4787 9260 382 -927 1071 N ATOM 669 CA TRP A 135 -2.611 18.157 -6.734 1.00 68.28 C ANISOU 669 CA TRP A 135 12218 4718 9005 380 -898 968 C ATOM 670 C TRP A 135 -2.863 18.156 -5.224 1.00 68.71 C ANISOU 670 C TRP A 135 12520 4553 9031 422 -803 840 C ATOM 671 O TRP A 135 -2.507 19.113 -4.537 1.00 70.26 O ANISOU 671 O TRP A 135 12818 4600 9277 437 -856 840 O ATOM 672 CB TRP A 135 -1.108 18.124 -7.047 1.00 68.17 C ANISOU 672 CB TRP A 135 12194 4783 8922 344 -1042 1019 C ATOM 673 CG TRP A 135 -0.378 16.977 -6.391 1.00 68.22 C ANISOU 673 CG TRP A 135 12354 4788 8777 351 -1044 911 C ATOM 674 CD1 TRP A 135 0.342 17.021 -5.234 1.00 68.70 C ANISOU 674 CD1 TRP A 135 12622 4695 8784 378 -1099 828 C ATOM 675 CD2 TRP A 135 -0.314 15.624 -6.848 1.00 67.36 C ANISOU 675 CD2 TRP A 135 12212 4828 8552 337 -1002 871 C ATOM 676 NE1 TRP A 135 0.851 15.784 -4.939 1.00 67.87 N ANISOU 676 NE1 TRP A 135 12620 4629 8537 387 -1100 745 N ATOM 677 CE2 TRP A 135 0.466 14.906 -5.916 1.00 67.33 C ANISOU 677 CE2 TRP A 135 12401 4747 8434 359 -1031 770 C ATOM 678 CE3 TRP A 135 -0.828 14.950 -7.962 1.00 67.19 C ANISOU 678 CE3 TRP A 135 12023 4993 8512 312 -954 906 C ATOM 679 CZ2 TRP A 135 0.734 13.546 -6.056 1.00 66.38 C ANISOU 679 CZ2 TRP A 135 12303 4725 8192 355 -1001 710 C ATOM 680 CZ3 TRP A 135 -0.567 13.590 -8.097 1.00 66.57 C ANISOU 680 CZ3 TRP A 135 11964 5016 8312 304 -918 837 C ATOM 681 CH2 TRP A 135 0.208 12.905 -7.150 1.00 65.95 C ANISOU 681 CH2 TRP A 135 12071 4854 8131 324 -936 744 C ATOM 682 N ALA A 136 -3.462 17.083 -4.714 1.00 67.45 N ANISOU 682 N ALA A 136 12470 4366 8788 442 -657 729 N ATOM 683 CA ALA A 136 -4.002 17.055 -3.365 1.00 68.00 C ANISOU 683 CA ALA A 136 12785 4219 8832 485 -511 611 C ATOM 684 C ALA A 136 -3.168 16.203 -2.413 1.00 67.87 C ANISOU 684 C ALA A 136 13036 4135 8616 508 -524 519 C ATOM 685 O ALA A 136 -3.624 15.884 -1.314 1.00 69.45 O ANISOU 685 O ALA A 136 13480 4163 8742 546 -378 414 O ATOM 686 CB ALA A 136 -5.432 16.534 -3.407 1.00 68.25 C ANISOU 686 CB ALA A 136 12759 4225 8945 495 -300 547 C ATOM 687 N PHE A 137 -1.952 15.841 -2.809 1.00 66.40 N ANISOU 687 N PHE A 137 12817 4068 8345 487 -693 555 N ATOM 688 CA PHE A 137 -1.149 14.938 -1.995 1.00 66.03 C ANISOU 688 CA PHE A 137 13005 3963 8117 516 -732 467 C ATOM 689 C PHE A 137 0.193 15.499 -1.555 1.00 65.93 C ANISOU 689 C PHE A 137 13087 3884 8078 528 -951 470 C ATOM 690 O PHE A 137 1.050 14.740 -1.096 1.00 66.77 O ANISOU 690 O PHE A 137 13341 3973 8055 551 -1041 409 O ATOM 691 CB PHE A 137 -0.953 13.593 -2.718 1.00 65.36 C ANISOU 691 CB PHE A 137 12822 4062 7950 491 -714 463 C ATOM 692 CG PHE A 137 -2.228 12.858 -2.949 1.00 65.04 C ANISOU 692 CG PHE A 137 12728 4055 7928 487 -500 424 C ATOM 693 CD1 PHE A 137 -2.820 12.143 -1.920 1.00 65.82 C ANISOU 693 CD1 PHE A 137 13073 4001 7934 526 -319 315 C ATOM 694 CD2 PHE A 137 -2.855 12.904 -4.178 1.00 65.12 C ANISOU 694 CD2 PHE A 137 12453 4233 8056 447 -477 492 C ATOM 695 CE1 PHE A 137 -4.015 11.470 -2.115 1.00 66.08 C ANISOU 695 CE1 PHE A 137 13040 4044 8021 517 -104 267 C ATOM 696 CE2 PHE A 137 -4.049 12.231 -4.388 1.00 65.82 C ANISOU 696 CE2 PHE A 137 12473 4340 8195 445 -296 438 C ATOM 697 CZ PHE A 137 -4.629 11.508 -3.351 1.00 66.04 C ANISOU 697 CZ PHE A 137 12721 4209 8159 477 -101 322 C ATOM 698 N GLY A 138 0.377 16.813 -1.653 1.00 65.94 N ANISOU 698 N GLY A 138 13006 3833 8215 516 -1042 531 N ATOM 699 CA GLY A 138 1.578 17.451 -1.118 1.00 66.31 C ANISOU 699 CA GLY A 138 13143 3778 8271 530 -1246 513 C ATOM 700 C GLY A 138 2.850 17.134 -1.889 1.00 66.26 C ANISOU 700 C GLY A 138 12970 3916 8290 490 -1418 559 C ATOM 701 O GLY A 138 2.847 16.341 -2.835 1.00 65.11 O ANISOU 701 O GLY A 138 12657 3956 8124 453 -1375 604 O ATOM 702 N ASP A 139 3.948 17.754 -1.475 1.00 67.72 N ANISOU 702 N ASP A 139 13194 4002 8532 498 -1610 536 N ATOM 703 CA ASP A 139 5.209 17.656 -2.214 1.00 68.31 C ANISOU 703 CA ASP A 139 13078 4184 8690 454 -1765 577 C ATOM 704 C ASP A 139 5.802 16.256 -2.103 1.00 68.43 C ANISOU 704 C ASP A 139 13166 4262 8571 473 -1806 503 C ATOM 705 O ASP A 139 6.307 15.713 -3.088 1.00 67.61 O ANISOU 705 O ASP A 139 12859 4327 8501 424 -1815 553 O ATOM 706 CB ASP A 139 6.219 18.706 -1.729 1.00 69.05 C ANISOU 706 CB ASP A 139 13186 4128 8921 459 -1962 552 C ATOM 707 CG ASP A 139 7.566 18.586 -2.423 1.00 69.14 C ANISOU 707 CG ASP A 139 12994 4220 9053 411 -2107 575 C ATOM 708 OD1 ASP A 139 7.650 18.911 -3.618 1.00 69.07 O ANISOU 708 OD1 ASP A 139 12728 4353 9161 340 -2050 697 O ATOM 709 OD2 ASP A 139 8.547 18.154 -1.782 1.00 70.12 O ANISOU 709 OD2 ASP A 139 13220 4259 9162 447 -2277 469 O ATOM 710 N ALA A 140 5.743 15.687 -0.900 1.00 69.50 N ANISOU 710 N ALA A 140 13603 4251 8549 547 -1828 384 N ATOM 711 CA ALA A 140 6.237 14.335 -0.658 1.00 69.13 C ANISOU 711 CA ALA A 140 13667 4235 8363 580 -1869 309 C ATOM 712 C ALA A 140 5.283 13.274 -1.198 1.00 68.60 C ANISOU 712 C ALA A 140 13559 4312 8192 561 -1651 332 C ATOM 713 O ALA A 140 5.707 12.162 -1.494 1.00 68.07 O ANISOU 713 O ALA A 140 13464 4340 8058 559 -1664 307 O ATOM 714 CB ALA A 140 6.471 14.120 0.823 1.00 70.35 C ANISOU 714 CB ALA A 140 14194 4167 8366 674 -1969 182 C ATOM 715 N GLY A 141 3.997 13.599 -1.304 1.00 68.60 N ANISOU 715 N GLY A 141 13551 4316 8196 551 -1456 369 N ATOM 716 CA GLY A 141 3.059 12.715 -1.983 1.00 67.85 C ANISOU 716 CA GLY A 141 13356 4366 8058 524 -1260 392 C ATOM 717 C GLY A 141 3.436 12.605 -3.446 1.00 67.22 C ANISOU 717 C GLY A 141 12949 4515 8073 452 -1294 487 C ATOM 718 O GLY A 141 3.487 11.505 -4.003 1.00 68.36 O ANISOU 718 O GLY A 141 13021 4796 8156 434 -1246 475 O ATOM 719 N CYS A 142 3.713 13.754 -4.055 1.00 66.86 N ANISOU 719 N CYS A 142 12725 4502 8175 412 -1369 580 N ATOM 720 CA CYS A 142 4.159 13.841 -5.439 1.00 65.76 C ANISOU 720 CA CYS A 142 12304 4557 8122 344 -1399 683 C ATOM 721 C CYS A 142 5.439 13.053 -5.691 1.00 65.03 C ANISOU 721 C CYS A 142 12162 4535 8009 328 -1509 650 C ATOM 722 O CYS A 142 5.532 12.330 -6.677 1.00 64.69 O ANISOU 722 O CYS A 142 11965 4669 7944 287 -1459 683 O ATOM 723 CB CYS A 142 4.375 15.312 -5.829 1.00 66.68 C ANISOU 723 CB CYS A 142 12292 4642 8400 313 -1467 785 C ATOM 724 SG CYS A 142 5.160 15.560 -7.448 1.00 67.83 S ANISOU 724 SG CYS A 142 12140 4985 8647 230 -1503 919 S ATOM 725 N ARG A 143 6.426 13.196 -4.815 1.00 65.29 N ANISOU 725 N ARG A 143 12322 4423 8061 363 -1666 577 N ATOM 726 CA ARG A 143 7.698 12.491 -4.989 1.00 65.75 C ANISOU 726 CA ARG A 143 12320 4521 8140 354 -1790 531 C ATOM 727 C ARG A 143 7.570 10.984 -4.733 1.00 65.10 C ANISOU 727 C ARG A 143 12356 4480 7898 389 -1739 447 C ATOM 728 O ARG A 143 8.130 10.185 -5.469 1.00 64.49 O ANISOU 728 O ARG A 143 12137 4535 7828 356 -1739 448 O ATOM 729 CB ARG A 143 8.772 13.086 -4.077 1.00 67.36 C ANISOU 729 CB ARG A 143 12623 4536 8433 391 -2003 461 C ATOM 730 CG ARG A 143 9.322 14.409 -4.587 1.00 68.80 C ANISOU 730 CG ARG A 143 12615 4700 8826 337 -2072 540 C ATOM 731 CD ARG A 143 9.861 15.297 -3.474 1.00 70.10 C ANISOU 731 CD ARG A 143 12923 4637 9072 385 -2253 466 C ATOM 732 NE ARG A 143 10.079 16.660 -3.960 1.00 71.57 N ANISOU 732 NE ARG A 143 12935 4798 9460 330 -2271 555 N ATOM 733 CZ ARG A 143 11.181 17.089 -4.579 1.00 72.80 C ANISOU 733 CZ ARG A 143 12872 4965 9821 273 -2353 584 C ATOM 734 NH1 ARG A 143 12.207 16.275 -4.805 1.00 73.40 N ANISOU 734 NH1 ARG A 143 12859 5081 9948 263 -2435 525 N ATOM 735 NH2 ARG A 143 11.260 18.350 -4.980 1.00 73.62 N ANISOU 735 NH2 ARG A 143 12842 5029 10101 225 -2343 672 N ATOM 736 N GLY A 144 6.842 10.617 -3.682 1.00 64.84 N ANISOU 736 N GLY A 144 12589 4321 7724 455 -1682 375 N ATOM 737 CA GLY A 144 6.655 9.233 -3.305 1.00 64.26 C ANISOU 737 CA GLY A 144 12666 4252 7496 494 -1618 297 C ATOM 738 C GLY A 144 5.860 8.451 -4.335 1.00 63.97 C ANISOU 738 C GLY A 144 12463 4411 7429 444 -1431 338 C ATOM 739 O GLY A 144 6.115 7.263 -4.545 1.00 62.30 O ANISOU 739 O GLY A 144 12245 4273 7149 447 -1409 293 O ATOM 740 N TYR A 145 4.906 9.120 -4.986 1.00 64.10 N ANISOU 740 N TYR A 145 12343 4506 7504 404 -1312 418 N ATOM 741 CA TYR A 145 4.046 8.472 -5.975 1.00 63.48 C ANISOU 741 CA TYR A 145 12106 4604 7407 362 -1155 448 C ATOM 742 C TYR A 145 4.827 8.028 -7.200 1.00 62.48 C ANISOU 742 C TYR A 145 11747 4673 7316 305 -1201 491 C ATOM 743 O TYR A 145 4.733 6.882 -7.622 1.00 62.05 O ANISOU 743 O TYR A 145 11653 4727 7195 294 -1132 451 O ATOM 744 CB TYR A 145 2.919 9.401 -6.414 1.00 64.43 C ANISOU 744 CB TYR A 145 12124 4749 7605 341 -1059 523 C ATOM 745 CG TYR A 145 2.066 8.809 -7.510 1.00 64.67 C ANISOU 745 CG TYR A 145 11975 4960 7635 304 -938 549 C ATOM 746 CD1 TYR A 145 1.115 7.846 -7.220 1.00 65.20 C ANISOU 746 CD1 TYR A 145 12118 5013 7642 324 -786 468 C ATOM 747 CD2 TYR A 145 2.216 9.204 -8.835 1.00 64.88 C ANISOU 747 CD2 TYR A 145 11768 5161 7720 250 -975 649 C ATOM 748 CE1 TYR A 145 0.332 7.286 -8.215 1.00 65.36 C ANISOU 748 CE1 TYR A 145 11964 5190 7678 293 -695 475 C ATOM 749 CE2 TYR A 145 1.435 8.655 -9.839 1.00 65.13 C ANISOU 749 CE2 TYR A 145 11653 5353 7738 225 -891 662 C ATOM 750 CZ TYR A 145 0.495 7.692 -9.521 1.00 65.50 C ANISOU 750 CZ TYR A 145 11758 5384 7741 247 -762 569 C ATOM 751 OH TYR A 145 -0.293 7.129 -10.501 1.00 66.43 O ANISOU 751 OH TYR A 145 11723 5651 7863 224 -695 564 O ATOM 752 N TYR A 146 5.592 8.938 -7.777 1.00 62.60 N ANISOU 752 N TYR A 146 11615 4727 7442 265 -1302 570 N ATOM 753 CA TYR A 146 6.401 8.587 -8.935 1.00 62.81 C ANISOU 753 CA TYR A 146 11435 4921 7507 206 -1323 611 C ATOM 754 C TYR A 146 7.545 7.623 -8.574 1.00 62.10 C ANISOU 754 C TYR A 146 11387 4804 7402 223 -1412 518 C ATOM 755 O TYR A 146 7.990 6.848 -9.422 1.00 61.70 O ANISOU 755 O TYR A 146 11200 4895 7345 185 -1380 514 O ATOM 756 CB TYR A 146 6.896 9.845 -9.669 1.00 63.68 C ANISOU 756 CB TYR A 146 11383 5061 7749 155 -1375 726 C ATOM 757 CG TYR A 146 5.797 10.459 -10.515 1.00 64.73 C ANISOU 757 CG TYR A 146 11420 5293 7879 130 -1279 831 C ATOM 758 CD1 TYR A 146 5.540 9.982 -11.798 1.00 65.33 C ANISOU 758 CD1 TYR A 146 11348 5566 7906 86 -1202 883 C ATOM 759 CD2 TYR A 146 4.982 11.486 -10.025 1.00 65.02 C ANISOU 759 CD2 TYR A 146 11521 5219 7961 156 -1273 870 C ATOM 760 CE1 TYR A 146 4.524 10.520 -12.576 1.00 65.55 C ANISOU 760 CE1 TYR A 146 11300 5676 7927 76 -1146 973 C ATOM 761 CE2 TYR A 146 3.956 12.018 -10.797 1.00 64.79 C ANISOU 761 CE2 TYR A 146 11399 5271 7947 143 -1204 959 C ATOM 762 CZ TYR A 146 3.733 11.532 -12.070 1.00 65.07 C ANISOU 762 CZ TYR A 146 11292 5500 7929 106 -1153 1011 C ATOM 763 OH TYR A 146 2.723 12.040 -12.855 1.00 65.93 O ANISOU 763 OH TYR A 146 11317 5682 8048 104 -1117 1095 O ATOM 764 N PHE A 147 8.011 7.651 -7.330 1.00 61.48 N ANISOU 764 N PHE A 147 11502 4538 7318 285 -1528 440 N ATOM 765 CA PHE A 147 9.033 6.707 -6.919 1.00 62.11 C ANISOU 765 CA PHE A 147 11637 4572 7387 317 -1635 345 C ATOM 766 C PHE A 147 8.471 5.286 -6.990 1.00 61.98 C ANISOU 766 C PHE A 147 11683 4633 7231 333 -1514 289 C ATOM 767 O PHE A 147 9.033 4.401 -7.646 1.00 61.01 O ANISOU 767 O PHE A 147 11437 4624 7120 306 -1505 263 O ATOM 768 CB PHE A 147 9.510 6.983 -5.494 1.00 62.60 C ANISOU 768 CB PHE A 147 11942 4403 7439 398 -1803 265 C ATOM 769 CG PHE A 147 10.462 5.945 -4.972 1.00 62.89 C ANISOU 769 CG PHE A 147 12069 4371 7453 449 -1934 161 C ATOM 770 CD1 PHE A 147 11.808 5.987 -5.314 1.00 63.42 C ANISOU 770 CD1 PHE A 147 11967 4441 7688 429 -2088 136 C ATOM 771 CD2 PHE A 147 10.009 4.907 -4.164 1.00 63.06 C ANISOU 771 CD2 PHE A 147 12340 4318 7302 519 -1896 88 C ATOM 772 CE1 PHE A 147 12.691 5.025 -4.844 1.00 64.06 C ANISOU 772 CE1 PHE A 147 12116 4449 7771 483 -2227 34 C ATOM 773 CE2 PHE A 147 10.886 3.939 -3.697 1.00 63.34 C ANISOU 773 CE2 PHE A 147 12468 4283 7316 574 -2030 -2 C ATOM 774 CZ PHE A 147 12.229 3.998 -4.036 1.00 63.87 C ANISOU 774 CZ PHE A 147 12354 4353 7558 560 -2208 -31 C ATOM 775 N LEU A 148 7.350 5.095 -6.306 1.00 62.19 N ANISOU 775 N LEU A 148 11900 4585 7141 374 -1407 264 N ATOM 776 CA LEU A 148 6.736 3.794 -6.181 1.00 62.36 C ANISOU 776 CA LEU A 148 12014 4636 7043 395 -1278 201 C ATOM 777 C LEU A 148 6.297 3.282 -7.541 1.00 62.56 C ANISOU 777 C LEU A 148 11799 4888 7083 326 -1150 238 C ATOM 778 O LEU A 148 6.564 2.130 -7.886 1.00 60.68 O ANISOU 778 O LEU A 148 11519 4729 6806 319 -1117 187 O ATOM 779 CB LEU A 148 5.544 3.856 -5.228 1.00 62.34 C ANISOU 779 CB LEU A 148 12247 4493 6944 443 -1152 174 C ATOM 780 CG LEU A 148 5.892 4.108 -3.759 1.00 63.41 C ANISOU 780 CG LEU A 148 12697 4388 7007 527 -1259 117 C ATOM 781 CD1 LEU A 148 4.623 4.386 -2.969 1.00 63.87 C ANISOU 781 CD1 LEU A 148 12962 4313 6990 559 -1091 104 C ATOM 782 CD2 LEU A 148 6.662 2.949 -3.149 1.00 63.53 C ANISOU 782 CD2 LEU A 148 12882 4326 6930 586 -1346 33 C ATOM 783 N ARG A 149 5.636 4.150 -8.306 1.00 63.67 N ANISOU 783 N ARG A 149 11791 5123 7278 279 -1091 325 N ATOM 784 CA ARG A 149 5.130 3.792 -9.627 1.00 64.39 C ANISOU 784 CA ARG A 149 11673 5422 7369 221 -991 363 C ATOM 785 C ARG A 149 6.252 3.214 -10.468 1.00 63.69 C ANISOU 785 C ARG A 149 11434 5462 7302 180 -1042 359 C ATOM 786 O ARG A 149 6.143 2.104 -10.981 1.00 61.72 O ANISOU 786 O ARG A 149 11128 5321 6998 165 -969 308 O ATOM 787 CB ARG A 149 4.532 5.012 -10.333 1.00 67.13 C ANISOU 787 CB ARG A 149 11892 5832 7781 187 -978 472 C ATOM 788 CG ARG A 149 3.596 4.651 -11.471 1.00 69.54 C ANISOU 788 CG ARG A 149 12045 6313 8061 151 -875 496 C ATOM 789 CD ARG A 149 3.398 5.791 -12.449 1.00 71.97 C ANISOU 789 CD ARG A 149 12207 6711 8425 115 -905 620 C ATOM 790 NE ARG A 149 2.553 5.359 -13.562 1.00 74.55 N ANISOU 790 NE ARG A 149 12406 7206 8712 91 -839 630 N ATOM 791 CZ ARG A 149 1.225 5.478 -13.613 1.00 76.26 C ANISOU 791 CZ ARG A 149 12607 7417 8951 111 -782 620 C ATOM 792 NH1 ARG A 149 0.542 6.042 -12.615 1.00 75.89 N ANISOU 792 NH1 ARG A 149 12664 7203 8966 151 -754 604 N ATOM 793 NH2 ARG A 149 0.572 5.031 -14.682 1.00 77.48 N ANISOU 793 NH2 ARG A 149 12638 7726 9075 94 -755 617 N ATOM 794 N ASP A 150 7.341 3.965 -10.585 1.00 64.52 N ANISOU 794 N ASP A 150 11471 5542 7502 161 -1160 404 N ATOM 795 CA ASP A 150 8.492 3.523 -11.377 1.00 65.47 C ANISOU 795 CA ASP A 150 11434 5762 7678 116 -1193 397 C ATOM 796 C ASP A 150 9.170 2.266 -10.842 1.00 64.94 C ANISOU 796 C ASP A 150 11440 5646 7588 153 -1234 282 C ATOM 797 O ASP A 150 9.701 1.481 -11.622 1.00 65.19 O ANISOU 797 O ASP A 150 11341 5795 7631 117 -1197 254 O ATOM 798 CB ASP A 150 9.534 4.637 -11.501 1.00 66.96 C ANISOU 798 CB ASP A 150 11532 5896 8013 88 -1299 458 C ATOM 799 CG ASP A 150 9.318 5.503 -12.727 1.00 68.20 C ANISOU 799 CG ASP A 150 11525 6184 8201 20 -1226 584 C ATOM 800 OD1 ASP A 150 8.139 5.812 -13.049 1.00 68.02 O ANISOU 800 OD1 ASP A 150 11516 6224 8102 20 -1151 641 O ATOM 801 OD2 ASP A 150 10.341 5.870 -13.359 1.00 69.79 O ANISOU 801 OD2 ASP A 150 11589 6414 8512 -29 -1243 622 O ATOM 802 N ALA A 151 9.168 2.091 -9.521 1.00 64.54 N ANISOU 802 N ALA A 151 11607 5412 7501 228 -1312 216 N ATOM 803 CA ALA A 151 9.802 0.936 -8.897 1.00 63.95 C ANISOU 803 CA ALA A 151 11638 5260 7397 278 -1375 111 C ATOM 804 C ALA A 151 9.071 -0.351 -9.279 1.00 62.83 C ANISOU 804 C ALA A 151 11498 5224 7148 272 -1220 65 C ATOM 805 O ALA A 151 9.678 -1.270 -9.815 1.00 62.38 O ANISOU 805 O ALA A 151 11337 5251 7113 253 -1212 17 O ATOM 806 CB ALA A 151 9.842 1.101 -7.384 1.00 64.25 C ANISOU 806 CB ALA A 151 11957 5068 7387 369 -1491 60 C ATOM 807 N CYS A 152 7.770 -0.395 -9.003 1.00 62.10 N ANISOU 807 N CYS A 152 11514 5118 6962 286 -1092 71 N ATOM 808 CA CYS A 152 6.917 -1.522 -9.370 1.00 61.87 C ANISOU 808 CA CYS A 152 11473 5178 6856 274 -932 22 C ATOM 809 C CYS A 152 7.015 -1.840 -10.862 1.00 61.39 C ANISOU 809 C CYS A 152 11154 5346 6826 199 -872 43 C ATOM 810 O CYS A 152 7.166 -2.999 -11.249 1.00 60.21 O ANISOU 810 O CYS A 152 10954 5270 6649 188 -817 -23 O ATOM 811 CB CYS A 152 5.464 -1.223 -9.006 1.00 62.08 C ANISOU 811 CB CYS A 152 11597 5155 6834 286 -798 35 C ATOM 812 SG CYS A 152 5.124 -1.271 -7.228 1.00 64.64 S ANISOU 812 SG CYS A 152 12283 5202 7074 378 -789 -16 S ATOM 813 N THR A 153 6.914 -0.787 -11.671 1.00 61.48 N ANISOU 813 N THR A 153 11020 5456 6883 150 -881 137 N ATOM 814 CA THR A 153 7.161 -0.820 -13.113 1.00 61.31 C ANISOU 814 CA THR A 153 10781 5637 6877 80 -842 177 C ATOM 815 C THR A 153 8.495 -1.471 -13.460 1.00 61.17 C ANISOU 815 C THR A 153 10674 5656 6909 60 -887 132 C ATOM 816 O THR A 153 8.523 -2.439 -14.221 1.00 61.62 O ANISOU 816 O THR A 153 10640 5840 6930 30 -809 82 O ATOM 817 CB THR A 153 7.085 0.617 -13.717 1.00 62.29 C ANISOU 817 CB THR A 153 10812 5806 7046 43 -873 302 C ATOM 818 OG1 THR A 153 5.728 0.907 -14.059 1.00 62.01 O ANISOU 818 OG1 THR A 153 10768 5830 6964 41 -799 337 O ATOM 819 CG2 THR A 153 7.948 0.792 -14.979 1.00 63.03 C ANISOU 819 CG2 THR A 153 10726 6046 7174 -23 -867 356 C ATOM 820 N TYR A 154 9.593 -0.947 -12.922 1.00 61.01 N ANISOU 820 N TYR A 154 10671 5519 6990 75 -1013 139 N ATOM 821 CA TYR A 154 10.899 -1.546 -13.175 1.00 61.74 C ANISOU 821 CA TYR A 154 10664 5619 7175 61 -1063 82 C ATOM 822 C TYR A 154 10.901 -3.010 -12.730 1.00 60.60 C ANISOU 822 C TYR A 154 10603 5445 6976 104 -1044 -31 C ATOM 823 O TYR A 154 11.429 -3.884 -13.418 1.00 60.59 O ANISOU 823 O TYR A 154 10482 5538 6999 74 -996 -84 O ATOM 824 CB TYR A 154 12.013 -0.795 -12.445 1.00 63.51 C ANISOU 824 CB TYR A 154 10905 5679 7544 87 -1229 83 C ATOM 825 CG TYR A 154 12.436 0.514 -13.079 1.00 65.31 C ANISOU 825 CG TYR A 154 10995 5936 7882 28 -1239 183 C ATOM 826 CD1 TYR A 154 12.815 0.579 -14.418 1.00 66.55 C ANISOU 826 CD1 TYR A 154 10958 6250 8077 -52 -1130 230 C ATOM 827 CD2 TYR A 154 12.503 1.682 -12.326 1.00 65.99 C ANISOU 827 CD2 TYR A 154 11157 5879 8034 54 -1350 228 C ATOM 828 CE1 TYR A 154 13.219 1.778 -14.997 1.00 67.59 C ANISOU 828 CE1 TYR A 154 10981 6391 8307 -106 -1118 330 C ATOM 829 CE2 TYR A 154 12.906 2.881 -12.895 1.00 67.61 C ANISOU 829 CE2 TYR A 154 11235 6096 8356 0 -1350 321 C ATOM 830 CZ TYR A 154 13.264 2.925 -14.230 1.00 68.04 C ANISOU 830 CZ TYR A 154 11103 6302 8446 -81 -1229 377 C ATOM 831 OH TYR A 154 13.658 4.122 -14.795 1.00 69.67 O ANISOU 831 OH TYR A 154 11202 6504 8763 -136 -1208 478 O ATOM 832 N ALA A 155 10.291 -3.270 -11.581 1.00 59.42 N ANISOU 832 N ALA A 155 10670 5154 6749 175 -1069 -67 N ATOM 833 CA ALA A 155 10.285 -4.606 -11.013 1.00 59.20 C ANISOU 833 CA ALA A 155 10762 5062 6666 225 -1052 -166 C ATOM 834 C ALA A 155 9.531 -5.601 -11.890 1.00 58.35 C ANISOU 834 C ALA A 155 10562 5117 6489 183 -881 -202 C ATOM 835 O ALA A 155 9.869 -6.782 -11.906 1.00 57.93 O ANISOU 835 O ALA A 155 10508 5068 6434 197 -857 -284 O ATOM 836 CB ALA A 155 9.700 -4.585 -9.608 1.00 59.21 C ANISOU 836 CB ALA A 155 11048 4866 6580 308 -1084 -185 C ATOM 837 N THR A 156 8.510 -5.127 -12.601 1.00 57.45 N ANISOU 837 N THR A 156 10371 5127 6328 137 -775 -147 N ATOM 838 CA THR A 156 7.753 -5.979 -13.502 1.00 56.89 C ANISOU 838 CA THR A 156 10200 5212 6201 97 -634 -188 C ATOM 839 C THR A 156 8.576 -6.235 -14.770 1.00 57.66 C ANISOU 839 C THR A 156 10093 5480 6335 34 -621 -192 C ATOM 840 O THR A 156 8.787 -7.382 -15.161 1.00 57.88 O ANISOU 840 O THR A 156 10066 5570 6353 23 -562 -276 O ATOM 841 CB THR A 156 6.372 -5.378 -13.835 1.00 55.98 C ANISOU 841 CB THR A 156 10069 5159 6041 78 -553 -140 C ATOM 842 OG1 THR A 156 5.543 -5.418 -12.676 1.00 54.88 O ANISOU 842 OG1 THR A 156 10119 4854 5877 133 -514 -164 O ATOM 843 CG2 THR A 156 5.680 -6.171 -14.913 1.00 56.03 C ANISOU 843 CG2 THR A 156 9944 5336 6006 35 -443 -190 C ATOM 844 N ALA A 157 9.055 -5.170 -15.397 1.00 58.44 N ANISOU 844 N ALA A 157 10086 5641 6476 -7 -662 -103 N ATOM 845 CA ALA A 157 9.849 -5.305 -16.616 1.00 59.37 C ANISOU 845 CA ALA A 157 10028 5905 6623 -72 -621 -98 C ATOM 846 C ALA A 157 11.046 -6.239 -16.414 1.00 60.20 C ANISOU 846 C ALA A 157 10094 5958 6819 -62 -649 -191 C ATOM 847 O ALA A 157 11.309 -7.098 -17.250 1.00 60.29 O ANISOU 847 O ALA A 157 10000 6086 6819 -98 -564 -251 O ATOM 848 CB ALA A 157 10.316 -3.942 -17.101 1.00 59.67 C ANISOU 848 CB ALA A 157 9992 5964 6715 -112 -656 18 C ATOM 849 N LEU A 158 11.760 -6.075 -15.304 1.00 61.27 N ANISOU 849 N LEU A 158 10318 5912 7049 -7 -780 -210 N ATOM 850 CA LEU A 158 12.922 -6.919 -15.018 1.00 62.61 C ANISOU 850 CA LEU A 158 10451 6004 7332 16 -842 -304 C ATOM 851 C LEU A 158 12.494 -8.367 -14.776 1.00 62.13 C ANISOU 851 C LEU A 158 10465 5943 7199 51 -782 -404 C ATOM 852 O LEU A 158 13.132 -9.291 -15.266 1.00 61.83 O ANISOU 852 O LEU A 158 10321 5954 7216 33 -743 -482 O ATOM 853 CB LEU A 158 13.703 -6.382 -13.813 1.00 63.65 C ANISOU 853 CB LEU A 158 10682 5923 7576 82 -1032 -308 C ATOM 854 CG LEU A 158 14.315 -4.981 -13.988 1.00 64.83 C ANISOU 854 CG LEU A 158 10740 6045 7846 47 -1102 -225 C ATOM 855 CD1 LEU A 158 14.798 -4.418 -12.655 1.00 65.16 C ANISOU 855 CD1 LEU A 158 10922 5865 7968 124 -1307 -237 C ATOM 856 CD2 LEU A 158 15.448 -4.988 -15.010 1.00 66.17 C ANISOU 856 CD2 LEU A 158 10675 6291 8173 -22 -1052 -240 C ATOM 857 N ASN A 159 11.403 -8.539 -14.030 1.00 61.99 N ANISOU 857 N ASN A 159 10624 5860 7068 97 -760 -404 N ATOM 858 CA ASN A 159 10.817 -9.853 -13.749 1.00 62.09 C ANISOU 858 CA ASN A 159 10725 5854 7010 127 -677 -491 C ATOM 859 C ASN A 159 10.538 -10.667 -15.018 1.00 60.78 C ANISOU 859 C ASN A 159 10390 5885 6816 61 -533 -543 C ATOM 860 O ASN A 159 11.103 -11.737 -15.231 1.00 59.54 O ANISOU 860 O ASN A 159 10179 5741 6702 62 -508 -630 O ATOM 861 CB ASN A 159 9.514 -9.686 -12.945 1.00 62.49 C ANISOU 861 CB ASN A 159 10967 5819 6955 166 -625 -468 C ATOM 862 CG ASN A 159 9.717 -9.890 -11.457 1.00 64.30 C ANISOU 862 CG ASN A 159 11449 5813 7167 259 -719 -491 C ATOM 863 OD1 ASN A 159 10.385 -10.842 -11.051 1.00 68.16 O ANISOU 863 OD1 ASN A 159 11998 6217 7682 304 -768 -561 O ATOM 864 ND2 ASN A 159 9.125 -9.023 -10.634 1.00 64.09 N ANISOU 864 ND2 ASN A 159 11588 5672 7088 294 -744 -433 N ATOM 865 N VAL A 160 9.657 -10.123 -15.844 1.00 59.74 N ANISOU 865 N VAL A 160 10185 5898 6613 9 -451 -491 N ATOM 866 CA VAL A 160 9.315 -10.682 -17.137 1.00 59.69 C ANISOU 866 CA VAL A 160 10032 6088 6559 -52 -335 -532 C ATOM 867 C VAL A 160 10.566 -11.063 -17.934 1.00 59.87 C ANISOU 867 C VAL A 160 9907 6187 6651 -93 -324 -569 C ATOM 868 O VAL A 160 10.586 -12.078 -18.609 1.00 59.24 O ANISOU 868 O VAL A 160 9749 6204 6554 -119 -236 -657 O ATOM 869 CB VAL A 160 8.472 -9.666 -17.939 1.00 60.09 C ANISOU 869 CB VAL A 160 10027 6267 6535 -94 -309 -442 C ATOM 870 CG1 VAL A 160 8.392 -10.052 -19.399 1.00 61.08 C ANISOU 870 CG1 VAL A 160 10010 6598 6598 -157 -224 -473 C ATOM 871 CG2 VAL A 160 7.070 -9.558 -17.365 1.00 59.77 C ANISOU 871 CG2 VAL A 160 10090 6172 6448 -62 -281 -440 C ATOM 872 N ALA A 161 11.603 -10.237 -17.851 1.00 60.77 N ANISOU 872 N ALA A 161 9976 6250 6862 -100 -406 -511 N ATOM 873 CA ALA A 161 12.839 -10.449 -18.613 1.00 61.20 C ANISOU 873 CA ALA A 161 9875 6359 7020 -146 -376 -544 C ATOM 874 C ALA A 161 13.706 -11.551 -18.018 1.00 60.92 C ANISOU 874 C ALA A 161 9835 6208 7104 -102 -422 -657 C ATOM 875 O ALA A 161 14.273 -12.352 -18.733 1.00 61.12 O ANISOU 875 O ALA A 161 9740 6305 7178 -136 -340 -736 O ATOM 876 CB ALA A 161 13.629 -9.145 -18.699 1.00 61.23 C ANISOU 876 CB ALA A 161 9818 6322 7121 -171 -437 -448 C ATOM 877 N SER A 162 13.822 -11.560 -16.701 1.00 61.59 N ANISOU 877 N SER A 162 10064 6103 7233 -23 -557 -664 N ATOM 878 CA SER A 162 14.629 -12.542 -15.999 1.00 62.78 C ANISOU 878 CA SER A 162 10246 6115 7493 37 -639 -762 C ATOM 879 C SER A 162 14.022 -13.925 -16.173 1.00 63.13 C ANISOU 879 C SER A 162 10320 6209 7458 44 -527 -853 C ATOM 880 O SER A 162 14.737 -14.919 -16.321 1.00 63.85 O ANISOU 880 O SER A 162 10337 6280 7643 53 -517 -948 O ATOM 881 CB SER A 162 14.672 -12.197 -14.514 1.00 63.11 C ANISOU 881 CB SER A 162 10494 5938 7544 132 -815 -739 C ATOM 882 OG SER A 162 13.351 -12.075 -14.012 1.00 62.75 O ANISOU 882 OG SER A 162 10628 5880 7332 155 -765 -696 O ATOM 883 N LEU A 163 12.693 -13.963 -16.141 1.00 62.57 N ANISOU 883 N LEU A 163 10347 6190 7236 41 -442 -828 N ATOM 884 CA LEU A 163 11.923 -15.179 -16.362 1.00 62.18 C ANISOU 884 CA LEU A 163 10316 6191 7117 38 -318 -914 C ATOM 885 C LEU A 163 12.221 -15.784 -17.722 1.00 62.12 C ANISOU 885 C LEU A 163 10109 6366 7124 -35 -201 -982 C ATOM 886 O LEU A 163 12.400 -16.989 -17.847 1.00 63.62 O ANISOU 886 O LEU A 163 10269 6554 7349 -28 -144 -1087 O ATOM 887 CB LEU A 163 10.435 -14.861 -16.264 1.00 61.84 C ANISOU 887 CB LEU A 163 10365 6184 6946 31 -243 -873 C ATOM 888 CG LEU A 163 9.469 -16.006 -16.529 1.00 62.32 C ANISOU 888 CG LEU A 163 10428 6293 6954 21 -104 -966 C ATOM 889 CD1 LEU A 163 9.762 -17.182 -15.618 1.00 62.44 C ANISOU 889 CD1 LEU A 163 10567 6142 7013 85 -106 -1044 C ATOM 890 CD2 LEU A 163 8.051 -15.504 -16.326 1.00 62.54 C ANISOU 890 CD2 LEU A 163 10533 6325 6904 19 -47 -925 C ATOM 891 N SER A 164 12.270 -14.935 -18.737 1.00 61.58 N ANISOU 891 N SER A 164 9923 6450 7024 -102 -162 -922 N ATOM 892 CA SER A 164 12.584 -15.362 -20.085 1.00 61.65 C ANISOU 892 CA SER A 164 9769 6631 7020 -174 -44 -977 C ATOM 893 C SER A 164 13.985 -15.953 -20.134 1.00 61.90 C ANISOU 893 C SER A 164 9697 6604 7218 -173 -52 -1052 C ATOM 894 O SER A 164 14.214 -16.955 -20.815 1.00 61.23 O ANISOU 894 O SER A 164 9521 6593 7148 -201 48 -1155 O ATOM 895 CB SER A 164 12.465 -14.184 -21.058 1.00 61.99 C ANISOU 895 CB SER A 164 9749 6816 6988 -237 -10 -875 C ATOM 896 OG SER A 164 12.488 -14.623 -22.409 1.00 62.93 O ANISOU 896 OG SER A 164 9761 7113 7035 -302 118 -928 O ATOM 897 N VAL A 165 14.916 -15.346 -19.404 1.00 62.23 N ANISOU 897 N VAL A 165 9744 6500 7398 -138 -179 -1010 N ATOM 898 CA VAL A 165 16.282 -15.873 -19.344 1.00 63.98 C ANISOU 898 CA VAL A 165 9852 6633 7823 -127 -214 -1091 C ATOM 899 C VAL A 165 16.292 -17.239 -18.658 1.00 64.26 C ANISOU 899 C VAL A 165 9956 6561 7898 -60 -246 -1200 C ATOM 900 O VAL A 165 16.824 -18.209 -19.207 1.00 65.05 O ANISOU 900 O VAL A 165 9939 6695 8081 -79 -165 -1305 O ATOM 901 CB VAL A 165 17.251 -14.899 -18.647 1.00 64.78 C ANISOU 901 CB VAL A 165 9939 6582 8091 -96 -373 -1036 C ATOM 902 CG1 VAL A 165 18.613 -15.544 -18.417 1.00 65.94 C ANISOU 902 CG1 VAL A 165 9966 6601 8485 -67 -442 -1140 C ATOM 903 CG2 VAL A 165 17.411 -13.642 -19.489 1.00 65.35 C ANISOU 903 CG2 VAL A 165 9913 6758 8157 -175 -305 -938 C ATOM 904 N ALA A 166 15.681 -17.312 -17.478 1.00 63.74 N ANISOU 904 N ALA A 166 10090 6359 7768 18 -350 -1173 N ATOM 905 CA ALA A 166 15.522 -18.570 -16.764 1.00 64.27 C ANISOU 905 CA ALA A 166 10270 6310 7840 86 -366 -1257 C ATOM 906 C ALA A 166 15.034 -19.703 -17.692 1.00 65.58 C ANISOU 906 C ALA A 166 10345 6617 7955 35 -184 -1354 C ATOM 907 O ALA A 166 15.608 -20.792 -17.698 1.00 65.52 O ANISOU 907 O ALA A 166 10287 6557 8050 57 -170 -1456 O ATOM 908 CB ALA A 166 14.567 -18.390 -15.599 1.00 63.50 C ANISOU 908 CB ALA A 166 10425 6085 7616 155 -426 -1198 C ATOM 909 N ARG A 167 13.995 -19.440 -18.483 1.00 65.87 N ANISOU 909 N ARG A 167 10357 6825 7844 -28 -58 -1328 N ATOM 910 CA ARG A 167 13.446 -20.456 -19.378 1.00 66.51 C ANISOU 910 CA ARG A 167 10358 7042 7869 -76 97 -1429 C ATOM 911 C ARG A 167 14.390 -20.786 -20.537 1.00 66.38 C ANISOU 911 C ARG A 167 10142 7144 7932 -139 181 -1502 C ATOM 912 O ARG A 167 14.442 -21.924 -20.998 1.00 66.19 O ANISOU 912 O ARG A 167 10053 7160 7937 -153 277 -1620 O ATOM 913 CB ARG A 167 12.089 -20.024 -19.936 1.00 67.79 C ANISOU 913 CB ARG A 167 10542 7348 7865 -121 177 -1391 C ATOM 914 CG ARG A 167 10.949 -20.021 -18.930 1.00 68.67 C ANISOU 914 CG ARG A 167 10830 7348 7912 -70 160 -1359 C ATOM 915 CD ARG A 167 9.610 -20.162 -19.646 1.00 70.95 C ANISOU 915 CD ARG A 167 11086 7776 8095 -116 267 -1393 C ATOM 916 NE ARG A 167 8.589 -19.254 -19.101 1.00 73.54 N ANISOU 916 NE ARG A 167 11521 8063 8357 -98 237 -1302 N ATOM 917 CZ ARG A 167 7.359 -19.604 -18.705 1.00 74.72 C ANISOU 917 CZ ARG A 167 11744 8161 8483 -85 306 -1335 C ATOM 918 NH1 ARG A 167 6.933 -20.873 -18.782 1.00 75.32 N ANISOU 918 NH1 ARG A 167 11803 8221 8594 -87 410 -1458 N ATOM 919 NH2 ARG A 167 6.537 -18.664 -18.237 1.00 73.19 N ANISOU 919 NH2 ARG A 167 11632 7925 8250 -71 281 -1250 N ATOM 920 N TYR A 168 15.125 -19.788 -21.012 1.00 65.96 N ANISOU 920 N TYR A 168 9997 7139 7923 -178 163 -1436 N ATOM 921 CA TYR A 168 16.129 -20.014 -22.048 1.00 66.57 C ANISOU 921 CA TYR A 168 9895 7300 8096 -239 265 -1501 C ATOM 922 C TYR A 168 17.234 -20.944 -21.557 1.00 66.46 C ANISOU 922 C TYR A 168 9811 7136 8302 -193 220 -1605 C ATOM 923 O TYR A 168 17.701 -21.797 -22.296 1.00 66.18 O ANISOU 923 O TYR A 168 9654 7157 8334 -228 338 -1716 O ATOM 924 CB TYR A 168 16.736 -18.686 -22.502 1.00 67.07 C ANISOU 924 CB TYR A 168 9889 7403 8190 -287 263 -1399 C ATOM 925 CG TYR A 168 17.865 -18.831 -23.495 1.00 68.50 C ANISOU 925 CG TYR A 168 9890 7637 8497 -351 392 -1462 C ATOM 926 CD1 TYR A 168 17.608 -19.096 -24.831 1.00 68.86 C ANISOU 926 CD1 TYR A 168 9883 7870 8410 -428 578 -1503 C ATOM 927 CD2 TYR A 168 19.194 -18.690 -23.096 1.00 69.69 C ANISOU 927 CD2 TYR A 168 9930 7640 8909 -335 331 -1487 C ATOM 928 CE1 TYR A 168 18.642 -19.226 -25.746 1.00 70.75 C ANISOU 928 CE1 TYR A 168 9976 8147 8758 -490 728 -1563 C ATOM 929 CE2 TYR A 168 20.236 -18.820 -24.003 1.00 71.24 C ANISOU 929 CE2 TYR A 168 9948 7868 9251 -399 478 -1553 C ATOM 930 CZ TYR A 168 19.956 -19.086 -25.329 1.00 71.78 C ANISOU 930 CZ TYR A 168 9980 8122 9168 -479 691 -1588 C ATOM 931 OH TYR A 168 20.983 -19.217 -26.241 1.00 73.70 O ANISOU 931 OH TYR A 168 10065 8388 9548 -546 869 -1656 O ATOM 932 N LEU A 169 17.651 -20.763 -20.310 1.00 66.26 N ANISOU 932 N LEU A 169 9873 6912 8389 -110 40 -1572 N ATOM 933 CA LEU A 169 18.687 -21.607 -19.728 1.00 67.13 C ANISOU 933 CA LEU A 169 9935 6854 8716 -47 -48 -1667 C ATOM 934 C LEU A 169 18.178 -23.015 -19.473 1.00 66.71 C ANISOU 934 C LEU A 169 9955 6765 8624 -6 -4 -1762 C ATOM 935 O LEU A 169 18.830 -23.984 -19.827 1.00 68.49 O ANISOU 935 O LEU A 169 10063 6973 8986 -9 51 -1878 O ATOM 936 CB LEU A 169 19.208 -21.005 -18.424 1.00 67.26 C ANISOU 936 CB LEU A 169 10058 6658 8839 43 -285 -1606 C ATOM 937 CG LEU A 169 19.874 -19.631 -18.534 1.00 67.66 C ANISOU 937 CG LEU A 169 10020 6701 8985 12 -353 -1526 C ATOM 938 CD1 LEU A 169 20.466 -19.255 -17.186 1.00 68.10 C ANISOU 938 CD1 LEU A 169 10181 6522 9169 116 -616 -1502 C ATOM 939 CD2 LEU A 169 20.940 -19.604 -19.623 1.00 68.78 C ANISOU 939 CD2 LEU A 169 9905 6912 9315 -66 -228 -1590 C ATOM 940 N ALA A 170 17.010 -23.126 -18.863 1.00 65.54 N ANISOU 940 N ALA A 170 9998 6596 8306 27 -14 -1717 N ATOM 941 CA ALA A 170 16.425 -24.420 -18.585 1.00 65.60 C ANISOU 941 CA ALA A 170 10089 6555 8279 62 46 -1800 C ATOM 942 C ALA A 170 16.417 -25.310 -19.834 1.00 67.15 C ANISOU 942 C ALA A 170 10113 6913 8488 -13 232 -1922 C ATOM 943 O ALA A 170 16.801 -26.486 -19.776 1.00 67.99 O ANISOU 943 O ALA A 170 10182 6947 8703 13 261 -2031 O ATOM 944 CB ALA A 170 15.015 -24.245 -18.050 1.00 64.27 C ANISOU 944 CB ALA A 170 10114 6383 7924 77 73 -1735 C ATOM 945 N ILE A 171 16.003 -24.738 -20.964 1.00 67.74 N ANISOU 945 N ILE A 171 10094 7196 8446 -104 350 -1905 N ATOM 946 CA ILE A 171 15.743 -25.523 -22.170 1.00 68.29 C ANISOU 946 CA ILE A 171 10045 7432 8469 -175 526 -2019 C ATOM 947 C ILE A 171 16.978 -25.668 -23.050 1.00 69.75 C ANISOU 947 C ILE A 171 10039 7667 8792 -223 603 -2092 C ATOM 948 O ILE A 171 17.252 -26.768 -23.524 1.00 71.53 O ANISOU 948 O ILE A 171 10176 7910 9089 -238 704 -2225 O ATOM 949 CB ILE A 171 14.550 -24.955 -22.977 1.00 68.06 C ANISOU 949 CB ILE A 171 10039 7597 8223 -239 606 -1978 C ATOM 950 CG1 ILE A 171 13.218 -25.422 -22.371 1.00 68.02 C ANISOU 950 CG1 ILE A 171 10167 7549 8126 -206 606 -1988 C ATOM 951 CG2 ILE A 171 14.571 -25.435 -24.424 1.00 68.83 C ANISOU 951 CG2 ILE A 171 10006 7884 8260 -319 765 -2085 C ATOM 952 CD1 ILE A 171 12.981 -25.061 -20.915 1.00 67.46 C ANISOU 952 CD1 ILE A 171 10273 7284 8075 -124 480 -1892 C ATOM 953 N CYS A 172 17.717 -24.581 -23.272 1.00 80.29 N ANISOU 953 N CYS A 172 10074 10865 9566 -1130 289 382 N ATOM 954 CA CYS A 172 18.859 -24.605 -24.204 1.00 82.43 C ANISOU 954 CA CYS A 172 10251 11476 9590 -1411 377 353 C ATOM 955 C CYS A 172 20.196 -24.986 -23.560 1.00 82.47 C ANISOU 955 C CYS A 172 9978 11787 9568 -1470 497 213 C ATOM 956 O CYS A 172 21.101 -25.434 -24.248 1.00 83.90 O ANISOU 956 O CYS A 172 9932 12338 9606 -1606 597 62 O ATOM 957 CB CYS A 172 19.004 -23.260 -24.932 1.00 85.24 C ANISOU 957 CB CYS A 172 10966 11753 9667 -1771 292 509 C ATOM 958 SG CYS A 172 17.639 -22.852 -26.056 1.00 87.02 S ANISOU 958 SG CYS A 172 11566 11673 9822 -1667 70 602 S ATOM 959 N HIS A 173 20.323 -24.795 -22.254 1.00 81.57 N ANISOU 959 N HIS A 173 9870 11540 9581 -1351 469 220 N ATOM 960 CA HIS A 173 21.552 -25.126 -21.539 1.00 82.67 C ANISOU 960 CA HIS A 173 9763 11944 9701 -1330 517 42 C ATOM 961 C HIS A 173 21.204 -25.828 -20.229 1.00 81.14 C ANISOU 961 C HIS A 173 9590 11527 9710 -953 470 8 C ATOM 962 O HIS A 173 21.442 -25.276 -19.157 1.00 81.52 O ANISOU 962 O HIS A 173 9717 11461 9793 -936 425 40 O ATOM 963 CB HIS A 173 22.353 -23.852 -21.230 1.00 84.71 C ANISOU 963 CB HIS A 173 10090 12282 9814 -1679 521 78 C ATOM 964 CG HIS A 173 23.028 -23.244 -22.422 1.00 87.55 C ANISOU 964 CG HIS A 173 10450 12921 9893 -2151 622 51 C ATOM 965 ND1 HIS A 173 24.370 -23.421 -22.686 1.00 90.11 N ANISOU 965 ND1 HIS A 173 10430 13739 10066 -2383 754 -231 N ATOM 966 CD2 HIS A 173 22.553 -22.443 -23.406 1.00 88.68 C ANISOU 966 CD2 HIS A 173 10931 12917 9843 -2453 610 241 C ATOM 967 CE1 HIS A 173 24.690 -22.769 -23.789 1.00 92.76 C ANISOU 967 CE1 HIS A 173 10887 14238 10118 -2876 875 -205 C ATOM 968 NE2 HIS A 173 23.606 -22.168 -24.246 1.00 92.16 N ANISOU 968 NE2 HIS A 173 11276 13744 9996 -2919 776 107 N ATOM 969 N PRO A 174 20.690 -27.030 -20.298 1.00 80.09 N ANISOU 969 N PRO A 174 9436 11309 9684 -679 487 -56 N ATOM 970 CA PRO A 174 20.244 -27.750 -19.112 1.00 79.28 C ANISOU 970 CA PRO A 174 9474 10937 9712 -385 470 -77 C ATOM 971 C PRO A 174 21.372 -28.207 -18.207 1.00 81.40 C ANISOU 971 C PRO A 174 9675 11328 9923 -190 390 -255 C ATOM 972 O PRO A 174 21.181 -28.396 -17.021 1.00 80.52 O ANISOU 972 O PRO A 174 9779 10956 9857 -14 351 -231 O ATOM 973 CB PRO A 174 19.548 -28.964 -19.695 1.00 78.49 C ANISOU 973 CB PRO A 174 9387 10753 9679 -228 523 -133 C ATOM 974 CG PRO A 174 20.000 -29.043 -21.095 1.00 79.57 C ANISOU 974 CG PRO A 174 9283 11241 9708 -327 529 -229 C ATOM 975 CD PRO A 174 20.223 -27.652 -21.529 1.00 80.27 C ANISOU 975 CD PRO A 174 9340 11482 9677 -661 530 -126 C ATOM 976 N PHE A 175 22.546 -28.410 -18.777 1.00 84.67 N ANISOU 976 N PHE A 175 9797 12150 10222 -212 353 -475 N ATOM 977 CA PHE A 175 23.708 -28.777 -18.001 1.00 86.91 C ANISOU 977 CA PHE A 175 9953 12622 10446 14 217 -743 C ATOM 978 C PHE A 175 24.053 -27.649 -17.058 1.00 87.62 C ANISOU 978 C PHE A 175 10087 12670 10533 -115 187 -685 C ATOM 979 O PHE A 175 24.056 -27.813 -15.854 1.00 87.94 O ANISOU 979 O PHE A 175 10313 12498 10599 145 73 -713 O ATOM 980 CB PHE A 175 24.871 -29.091 -18.928 1.00 89.34 C ANISOU 980 CB PHE A 175 9838 13472 10634 -19 196 -1085 C ATOM 981 CG PHE A 175 24.910 -30.518 -19.366 0.00 89.24 C ANISOU 981 CG PHE A 175 9773 13515 10618 214 164 -1216 C ATOM 982 CD1 PHE A 175 24.472 -31.519 -18.518 0.00 20.00 C ATOM 983 CD2 PHE A 175 25.364 -30.864 -20.623 0.00 20.00 C ATOM 984 CE1 PHE A 175 24.493 -32.837 -18.912 0.00 20.00 C ATOM 985 CE2 PHE A 175 25.387 -32.181 -21.023 0.00 20.00 C ATOM 986 CZ PHE A 175 24.954 -33.169 -20.166 0.00 20.00 C ATOM 987 N LYS A 176 24.307 -26.469 -17.614 1.00 88.51 N ANISOU 987 N LYS A 176 10089 12953 10587 -530 281 -599 N ATOM 988 CA LYS A 176 24.587 -25.292 -16.797 1.00 88.62 C ANISOU 988 CA LYS A 176 10186 12887 10596 -712 260 -513 C ATOM 989 C LYS A 176 23.403 -24.942 -15.892 1.00 86.89 C ANISOU 989 C LYS A 176 10338 12166 10508 -571 232 -240 C ATOM 990 O LYS A 176 23.582 -24.606 -14.721 1.00 86.94 O ANISOU 990 O LYS A 176 10457 12025 10550 -401 149 -259 O ATOM 991 CB LYS A 176 24.942 -24.097 -17.683 1.00 89.38 C ANISOU 991 CB LYS A 176 10245 13148 10564 -1236 370 -420 C ATOM 992 CG LYS A 176 26.006 -24.393 -18.727 0.00 91.91 C ANISOU 992 CG LYS A 176 10211 13997 10711 -1511 477 -696 C ATOM 993 CD LYS A 176 26.724 -23.124 -19.159 0.00 20.00 C ATOM 994 CE LYS A 176 25.737 -22.009 -19.467 0.00 20.00 C ATOM 995 NZ LYS A 176 26.422 -20.705 -19.682 0.00 20.00 N ATOM 996 N ALA A 177 22.198 -25.025 -16.447 1.00 85.87 N ANISOU 996 N ALA A 177 10376 11806 10443 -632 299 -37 N ATOM 997 CA ALA A 177 20.963 -24.711 -15.716 1.00 84.93 C ANISOU 997 CA ALA A 177 10539 11280 10449 -551 300 147 C ATOM 998 C ALA A 177 20.910 -25.250 -14.287 1.00 85.28 C ANISOU 998 C ALA A 177 10749 11109 10542 -273 270 104 C ATOM 999 O ALA A 177 20.755 -24.474 -13.339 1.00 85.60 O ANISOU 999 O ALA A 177 10930 10979 10614 -289 233 181 O ATOM 1000 CB ALA A 177 19.749 -25.202 -16.495 1.00 84.05 C ANISOU 1000 CB ALA A 177 10489 11030 10415 -524 369 212 C ATOM 1001 N LYS A 178 21.044 -26.564 -14.136 1.00 86.19 N ANISOU 1001 N LYS A 178 10906 11205 10635 -22 271 -19 N ATOM 1002 CA LYS A 178 21.005 -27.190 -12.819 1.00 86.66 C ANISOU 1002 CA LYS A 178 11257 11001 10669 235 230 -57 C ATOM 1003 C LYS A 178 22.178 -26.746 -11.948 1.00 88.57 C ANISOU 1003 C LYS A 178 11457 11364 10830 364 62 -182 C ATOM 1004 O LYS A 178 22.065 -26.685 -10.724 1.00 88.96 O ANISOU 1004 O LYS A 178 11785 11165 10850 510 13 -157 O ATOM 1005 CB LYS A 178 20.998 -28.715 -12.952 1.00 87.10 C ANISOU 1005 CB LYS A 178 11472 10956 10666 464 231 -165 C ATOM 1006 CG LYS A 178 19.687 -29.286 -13.468 0.00 20.00 C ATOM 1007 CD LYS A 178 18.733 -29.598 -12.327 0.00 20.00 C ATOM 1008 CE LYS A 178 17.299 -29.255 -12.697 0.00 20.00 C ATOM 1009 NZ LYS A 178 16.678 -30.307 -13.548 0.00 20.00 N ATOM 1010 N THR A 179 23.301 -26.438 -12.588 1.00 89.36 N ANISOU 1010 N THR A 179 11202 11867 10883 289 -12 -353 N ATOM 1011 CA THR A 179 24.505 -26.010 -11.876 1.00 90.55 C ANISOU 1011 CA THR A 179 11203 12227 10975 357 -163 -550 C ATOM 1012 C THR A 179 24.631 -24.487 -11.706 1.00 89.92 C ANISOU 1012 C THR A 179 11118 12107 10938 60 -124 -396 C ATOM 1013 O THR A 179 25.564 -24.010 -11.060 1.00 89.74 O ANISOU 1013 O THR A 179 11108 12093 10893 161 -243 -499 O ATOM 1014 CB THR A 179 25.779 -26.539 -12.562 1.00 92.27 C ANISOU 1014 CB THR A 179 10971 12969 11118 320 -219 -883 C ATOM 1015 OG1 THR A 179 25.670 -27.956 -12.752 0.00 20.00 O ATOM 1016 CG2 THR A 179 27.005 -26.239 -11.713 0.00 20.00 C ATOM 1017 N LEU A 180 23.619 -23.768 -12.175 1.00 89.19 N ANISOU 1017 N LEU A 180 11046 11949 10893 -270 4 -170 N ATOM 1018 CA LEU A 180 23.635 -22.312 -12.242 1.00 88.98 C ANISOU 1018 CA LEU A 180 11045 11895 10867 -591 5 -41 C ATOM 1019 C LEU A 180 22.516 -21.642 -11.490 1.00 86.90 C ANISOU 1019 C LEU A 180 11093 11222 10701 -567 0 192 C ATOM 1020 O LEU A 180 22.438 -20.428 -11.449 1.00 87.76 O ANISOU 1020 O LEU A 180 11285 11250 10807 -795 -39 305 O ATOM 1021 CB LEU A 180 23.509 -21.893 -13.697 0.00 89.67 C ANISOU 1021 CB LEU A 180 11012 12190 10869 -998 92 8 C ATOM 1022 CG LEU A 180 23.429 -20.420 -14.067 0.00 92.44 C ANISOU 1022 CG LEU A 180 11025 13017 11079 -1260 131 -253 C ATOM 1023 CD1 LEU A 180 24.699 -19.690 -13.673 0.00 20.00 C ATOM 1024 CD2 LEU A 180 23.098 -20.214 -15.537 0.00 20.00 C ATOM 1025 N MET A 181 21.617 -22.440 -10.926 1.00 85.08 N ANISOU 1025 N MET A 181 11050 10739 10538 -315 42 231 N ATOM 1026 CA MET A 181 20.453 -21.886 -10.248 1.00 83.56 C ANISOU 1026 CA MET A 181 11084 10226 10436 -306 67 366 C ATOM 1027 C MET A 181 19.630 -22.938 -9.515 1.00 82.97 C ANISOU 1027 C MET A 181 11214 9927 10382 -91 171 335 C ATOM 1028 O MET A 181 19.150 -23.904 -10.109 1.00 82.33 O ANISOU 1028 O MET A 181 11129 9848 10304 -47 268 301 O ATOM 1029 CB MET A 181 19.567 -21.132 -11.244 0.00 20.00 C ATOM 1030 CG MET A 181 20.047 -19.725 -11.560 0.00 20.00 C ATOM 1031 SD MET A 181 18.885 -18.808 -12.590 0.00 20.00 S ATOM 1032 CE MET A 181 18.148 -17.715 -11.378 0.00 20.00 C ATOM 1033 N SER A 182 19.472 -22.728 -8.214 1.00 83.14 N ANISOU 1033 N SER A 182 11445 9751 10392 10 162 340 N ATOM 1034 CA SER A 182 18.633 -23.577 -7.364 1.00 83.02 C ANISOU 1034 CA SER A 182 11716 9482 10344 117 306 312 C ATOM 1035 C SER A 182 17.823 -22.704 -6.407 1.00 82.30 C ANISOU 1035 C SER A 182 11748 9214 10306 61 348 334 C ATOM 1036 O SER A 182 17.975 -21.485 -6.407 1.00 82.90 O ANISOU 1036 O SER A 182 11708 9340 10450 -7 220 381 O ATOM 1037 CB SER A 182 19.492 -24.558 -6.567 0.00 84.85 C ANISOU 1037 CB SER A 182 12192 9639 10405 357 236 236 C ATOM 1038 OG SER A 182 20.070 -23.864 -5.406 0.00 20.00 O ATOM 1039 N ARG A 183 16.962 -23.289 -5.609 1.00 81.99 N ANISOU 1039 N ARG A 183 11969 8968 10213 67 532 278 N ATOM 1040 CA ARG A 183 16.064 -22.491 -4.808 1.00 80.96 C ANISOU 1040 CA ARG A 183 11928 8710 10123 0 619 229 C ATOM 1041 C ARG A 183 16.685 -21.294 -4.098 1.00 80.42 C ANISOU 1041 C ARG A 183 11814 8658 10084 53 414 282 C ATOM 1042 O ARG A 183 16.114 -20.235 -4.124 1.00 80.34 O ANISOU 1042 O ARG A 183 11667 8659 10198 -10 355 256 O ATOM 1043 CB ARG A 183 15.289 -23.376 -3.844 0.00 20.00 C ATOM 1044 CG ARG A 183 14.709 -24.618 -4.504 0.00 20.00 C ATOM 1045 CD ARG A 183 13.256 -24.841 -4.126 0.00 20.00 C ATOM 1046 NE ARG A 183 13.110 -25.714 -2.966 0.00 20.00 N ATOM 1047 CZ ARG A 183 13.149 -27.047 -3.006 0.00 20.00 C ATOM 1048 NH1 ARG A 183 13.338 -27.689 -4.159 0.00 20.00 N ATOM 1049 NH2 ARG A 183 13.000 -27.745 -1.881 0.00 20.00 N ATOM 1050 N SER A 184 17.858 -21.428 -3.519 1.00 80.33 N ANISOU 1050 N SER A 184 11922 8644 9953 196 275 322 N ATOM 1051 CA SER A 184 18.422 -20.291 -2.819 1.00 79.86 C ANISOU 1051 CA SER A 184 11839 8597 9907 242 88 346 C ATOM 1052 C SER A 184 19.076 -19.264 -3.723 1.00 79.12 C ANISOU 1052 C SER A 184 11456 8691 9915 122 -88 402 C ATOM 1053 O SER A 184 19.130 -18.109 -3.380 1.00 79.30 O ANISOU 1053 O SER A 184 11460 8676 9992 66 -209 428 O ATOM 1054 CB SER A 184 19.360 -20.748 -1.700 1.00 80.76 C ANISOU 1054 CB SER A 184 12173 8661 9851 461 -25 307 C ATOM 1055 OG SER A 184 20.504 -21.448 -2.164 0.00 20.00 O ATOM 1056 N ARG A 185 19.605 -19.690 -4.853 1.00 78.44 N ANISOU 1056 N ARG A 185 11185 8791 9826 55 -99 410 N ATOM 1057 CA ARG A 185 20.252 -18.754 -5.786 1.00 78.25 C ANISOU 1057 CA ARG A 185 10952 8947 9830 -144 -222 454 C ATOM 1058 C ARG A 185 19.257 -17.849 -6.547 1.00 77.96 C ANISOU 1058 C ARG A 185 10921 8817 9882 -310 -252 540 C ATOM 1059 O ARG A 185 19.592 -16.704 -6.878 1.00 78.16 O ANISOU 1059 O ARG A 185 10956 8845 9894 -484 -395 601 O ATOM 1060 CB ARG A 185 21.156 -19.505 -6.768 1.00 78.52 C ANISOU 1060 CB ARG A 185 10784 9248 9801 -184 -205 389 C ATOM 1061 CG ARG A 185 22.484 -19.904 -6.409 0.00 20.00 C ATOM 1062 CD ARG A 185 23.311 -20.605 -7.473 0.00 20.00 C ATOM 1063 NE ARG A 185 24.570 -21.146 -6.954 0.00 20.00 N ATOM 1064 CZ ARG A 185 25.743 -20.508 -6.950 0.00 20.00 C ATOM 1065 NH1 ARG A 185 25.863 -19.271 -7.435 0.00 20.00 N ATOM 1066 NH2 ARG A 185 26.815 -21.116 -6.456 0.00 20.00 N ATOM 1067 N THR A 186 18.044 -18.347 -6.810 1.00 77.26 N ANISOU 1067 N THR A 186 10857 8634 9864 -254 -140 511 N ATOM 1068 CA THR A 186 17.015 -17.531 -7.478 1.00 77.37 C ANISOU 1068 CA THR A 186 10878 8555 9961 -314 -232 514 C ATOM 1069 C THR A 186 16.355 -16.591 -6.480 1.00 77.47 C ANISOU 1069 C THR A 186 11003 8394 10037 -228 -334 451 C ATOM 1070 O THR A 186 16.205 -15.403 -6.764 1.00 78.99 O ANISOU 1070 O THR A 186 11280 8490 10242 -272 -558 483 O ATOM 1071 CB THR A 186 15.923 -18.350 -8.218 1.00 76.98 C ANISOU 1071 CB THR A 186 10743 8521 9984 -275 -101 421 C ATOM 1072 OG1 THR A 186 14.929 -18.819 -7.295 1.00 76.79 O ANISOU 1072 OG1 THR A 186 10745 8409 10023 -176 61 263 O ATOM 1073 CG2 THR A 186 16.538 -19.512 -9.003 1.00 76.60 C ANISOU 1073 CG2 THR A 186 10593 8636 9873 -314 24 455 C ATOM 1074 N LYS A 187 15.980 -17.113 -5.314 1.00 76.62 N ANISOU 1074 N LYS A 187 10942 8229 9938 -114 -181 353 N ATOM 1075 CA LYS A 187 15.474 -16.277 -4.223 1.00 76.92 C ANISOU 1075 CA LYS A 187 11068 8142 10016 -33 -253 263 C ATOM 1076 C LYS A 187 16.342 -15.029 -4.031 1.00 77.39 C ANISOU 1076 C LYS A 187 11209 8148 10048 -72 -512 377 C ATOM 1077 O LYS A 187 15.816 -13.945 -3.802 1.00 77.58 O ANISOU 1077 O LYS A 187 11300 8050 10126 -26 -700 321 O ATOM 1078 CB LYS A 187 15.402 -17.070 -2.919 1.00 76.69 C ANISOU 1078 CB LYS A 187 11160 8067 9911 34 -35 190 C ATOM 1079 CG LYS A 187 14.502 -18.199 -3.071 0.00 20.00 C ATOM 1080 CD LYS A 187 13.156 -18.045 -2.385 0.00 20.00 C ATOM 1081 CE LYS A 187 12.888 -19.221 -1.461 0.00 20.00 C ATOM 1082 NZ LYS A 187 11.588 -19.099 -0.752 0.00 20.00 N ATOM 1083 N LYS A 188 17.634 -15.164 -4.240 1.00 77.60 N ANISOU 1083 N LYS A 188 11222 8277 9985 -159 -529 491 N ATOM 1084 CA LYS A 188 18.548 -14.047 -4.114 1.00 78.93 C ANISOU 1084 CA LYS A 188 11443 8436 10109 -286 -730 567 C ATOM 1085 C LYS A 188 18.530 -13.164 -5.335 1.00 80.67 C ANISOU 1085 C LYS A 188 11733 8616 10299 -505 -895 660 C ATOM 1086 O LYS A 188 18.711 -11.971 -5.231 1.00 82.09 O ANISOU 1086 O LYS A 188 12082 8662 10445 -615 -1098 707 O ATOM 1087 CB LYS A 188 19.976 -14.546 -3.941 0.00 20.00 C ATOM 1088 CG LYS A 188 20.441 -14.755 -2.511 0.00 20.00 C ATOM 1089 CD LYS A 188 21.961 -14.864 -2.461 0.00 20.00 C ATOM 1090 CE LYS A 188 22.453 -16.306 -2.387 0.00 20.00 C ATOM 1091 NZ LYS A 188 23.933 -16.421 -2.533 0.00 20.00 N ATOM 1092 N PHE A 189 18.369 -13.763 -6.501 1.00 80.31 N ANISOU 1092 N PHE A 189 12400 6867 11246 1767 -732 118 N ATOM 1093 CA PHE A 189 18.249 -12.998 -7.755 1.00 78.82 C ANISOU 1093 CA PHE A 189 12233 6715 10998 1628 -634 -8 C ATOM 1094 C PHE A 189 16.975 -12.167 -7.774 1.00 75.58 C ANISOU 1094 C PHE A 189 11947 6361 10406 1453 -719 -45 C ATOM 1095 O PHE A 189 16.973 -11.055 -8.295 1.00 74.79 O ANISOU 1095 O PHE A 189 11807 6361 10246 1339 -733 -99 O ATOM 1096 CB PHE A 189 18.263 -13.932 -8.976 1.00 80.49 C ANISOU 1096 CB PHE A 189 12560 6772 11247 1649 -415 -104 C ATOM 1097 CG PHE A 189 18.566 -13.234 -10.286 1.00 80.99 C ANISOU 1097 CG PHE A 189 12609 6888 11273 1561 -287 -214 C ATOM 1098 CD1 PHE A 189 17.598 -12.465 -10.932 1.00 79.46 C ANISOU 1098 CD1 PHE A 189 12534 6741 10914 1378 -306 -291 C ATOM 1099 CD2 PHE A 189 19.817 -13.365 -10.883 1.00 82.94 C ANISOU 1099 CD2 PHE A 189 12720 7139 11654 1672 -137 -224 C ATOM 1100 CE1 PHE A 189 17.876 -11.834 -12.135 1.00 80.04 C ANISOU 1100 CE1 PHE A 189 12603 6867 10941 1304 -186 -376 C ATOM 1101 CE2 PHE A 189 20.101 -12.733 -12.085 1.00 83.30 C ANISOU 1101 CE2 PHE A 189 12756 7237 11655 1601 0 -308 C ATOM 1102 CZ PHE A 189 19.129 -11.969 -12.714 1.00 81.73 C ANISOU 1102 CZ PHE A 189 12690 7086 11275 1415 -28 -385 C ATOM 1103 N ILE A 190 15.890 -12.705 -7.220 1.00 73.82 N ANISOU 1103 N ILE A 190 11867 6069 10110 1435 -766 0 N ATOM 1104 CA ILE A 190 14.633 -11.961 -7.146 1.00 71.31 C ANISOU 1104 CA ILE A 190 11650 5805 9637 1287 -841 -8 C ATOM 1105 C ILE A 190 14.870 -10.732 -6.264 1.00 70.68 C ANISOU 1105 C ILE A 190 11467 5885 9502 1280 -999 36 C ATOM 1106 O ILE A 190 14.385 -9.653 -6.561 1.00 70.13 O ANISOU 1106 O ILE A 190 11412 5896 9338 1158 -1035 -6 O ATOM 1107 CB ILE A 190 13.454 -12.800 -6.588 1.00 70.74 C ANISOU 1107 CB ILE A 190 11721 5633 9524 1282 -859 64 C ATOM 1108 CG1 ILE A 190 13.265 -14.128 -7.348 1.00 72.15 C ANISOU 1108 CG1 ILE A 190 12014 5619 9778 1291 -724 19 C ATOM 1109 CG2 ILE A 190 12.151 -12.018 -6.644 1.00 68.87 C ANISOU 1109 CG2 ILE A 190 11566 5453 9146 1132 -912 66 C ATOM 1110 CD1 ILE A 190 12.981 -14.023 -8.833 1.00 71.84 C ANISOU 1110 CD1 ILE A 190 12065 5535 9693 1159 -620 -124 C ATOM 1111 N SER A 191 15.638 -10.893 -5.194 1.00 71.54 N ANISOU 1111 N SER A 191 11478 6033 9670 1412 -1099 120 N ATOM 1112 CA SER A 191 15.998 -9.768 -4.344 1.00 71.68 C ANISOU 1112 CA SER A 191 11408 6191 9636 1408 -1268 145 C ATOM 1113 C SER A 191 16.826 -8.727 -5.091 1.00 72.10 C ANISOU 1113 C SER A 191 11326 6322 9746 1328 -1266 67 C ATOM 1114 O SER A 191 16.591 -7.527 -4.938 1.00 71.06 O ANISOU 1114 O SER A 191 11190 6275 9532 1233 -1361 37 O ATOM 1115 CB SER A 191 16.754 -10.245 -3.108 1.00 73.07 C ANISOU 1115 CB SER A 191 11505 6392 9864 1567 -1391 252 C ATOM 1116 OG SER A 191 15.884 -10.977 -2.271 1.00 73.16 O ANISOU 1116 OG SER A 191 11649 6352 9794 1631 -1408 344 O ATOM 1117 N ALA A 192 17.783 -9.181 -5.898 1.00 73.59 N ANISOU 1117 N ALA A 192 11405 6473 10079 1372 -1145 42 N ATOM 1118 CA ALA A 192 18.625 -8.270 -6.672 1.00 74.44 C ANISOU 1118 CA ALA A 192 11367 6652 10263 1303 -1112 -8 C ATOM 1119 C ALA A 192 17.792 -7.337 -7.540 1.00 74.11 C ANISOU 1119 C ALA A 192 11420 6635 10101 1135 -1064 -89 C ATOM 1120 O ALA A 192 18.134 -6.160 -7.699 1.00 74.95 O ANISOU 1120 O ALA A 192 11436 6825 10217 1047 -1122 -108 O ATOM 1121 CB ALA A 192 19.608 -9.038 -7.535 1.00 75.65 C ANISOU 1121 CB ALA A 192 11418 6748 10576 1391 -934 -17 C ATOM 1122 N ILE A 193 16.689 -7.846 -8.083 1.00 73.27 N ANISOU 1122 N ILE A 193 11492 6454 9892 1084 -970 -126 N ATOM 1123 CA ILE A 193 15.892 -7.051 -9.012 1.00 72.51 C ANISOU 1123 CA ILE A 193 11482 6383 9686 930 -920 -190 C ATOM 1124 C ILE A 193 14.862 -6.138 -8.357 1.00 70.42 C ANISOU 1124 C ILE A 193 11290 6173 9292 847 -1053 -167 C ATOM 1125 O ILE A 193 14.392 -5.215 -9.012 1.00 69.76 O ANISOU 1125 O ILE A 193 11234 6130 9139 726 -1037 -202 O ATOM 1126 CB ILE A 193 15.242 -7.904 -10.125 1.00 73.43 C ANISOU 1126 CB ILE A 193 11748 6401 9752 890 -762 -252 C ATOM 1127 CG1 ILE A 193 14.226 -8.902 -9.552 1.00 74.05 C ANISOU 1127 CG1 ILE A 193 11969 6384 9783 917 -792 -215 C ATOM 1128 CG2 ILE A 193 16.335 -8.606 -10.926 1.00 75.34 C ANISOU 1128 CG2 ILE A 193 11927 6591 10107 977 -600 -293 C ATOM 1129 CD1 ILE A 193 13.660 -9.882 -10.566 1.00 75.05 C ANISOU 1129 CD1 ILE A 193 12248 6386 9882 875 -664 -283 C ATOM 1130 N TRP A 194 14.509 -6.367 -7.093 1.00 69.60 N ANISOU 1130 N TRP A 194 11222 6070 9150 920 -1170 -101 N ATOM 1131 CA TRP A 194 13.694 -5.379 -6.368 1.00 68.41 C ANISOU 1131 CA TRP A 194 11132 5980 8879 869 -1288 -79 C ATOM 1132 C TRP A 194 14.572 -4.227 -5.884 1.00 69.49 C ANISOU 1132 C TRP A 194 11153 6199 9049 861 -1416 -95 C ATOM 1133 O TRP A 194 14.164 -3.072 -5.944 1.00 69.34 O ANISOU 1133 O TRP A 194 11160 6221 8965 771 -1464 -122 O ATOM 1134 CB TRP A 194 12.907 -6.003 -5.210 1.00 67.58 C ANISOU 1134 CB TRP A 194 11128 5850 8696 955 -1347 3 C ATOM 1135 CG TRP A 194 11.732 -6.796 -5.680 1.00 66.46 C ANISOU 1135 CG TRP A 194 11107 5629 8514 913 -1246 28 C ATOM 1136 CD1 TRP A 194 11.751 -8.074 -6.156 1.00 67.26 C ANISOU 1136 CD1 TRP A 194 11241 5626 8686 941 -1148 29 C ATOM 1137 CD2 TRP A 194 10.369 -6.372 -5.739 1.00 64.54 C ANISOU 1137 CD2 TRP A 194 10962 5395 8165 828 -1239 58 C ATOM 1138 NE1 TRP A 194 10.486 -8.474 -6.503 1.00 66.31 N ANISOU 1138 NE1 TRP A 194 11234 5446 8513 863 -1099 54 N ATOM 1139 CE2 TRP A 194 9.618 -7.445 -6.258 1.00 64.78 C ANISOU 1139 CE2 TRP A 194 11068 5328 8215 794 -1153 82 C ATOM 1140 CE3 TRP A 194 9.707 -5.195 -5.398 1.00 63.92 C ANISOU 1140 CE3 TRP A 194 10911 5387 7987 782 -1297 72 C ATOM 1141 CZ2 TRP A 194 8.240 -7.373 -6.449 1.00 63.90 C ANISOU 1141 CZ2 TRP A 194 11035 5203 8038 705 -1135 132 C ATOM 1142 CZ3 TRP A 194 8.328 -5.125 -5.590 1.00 63.04 C ANISOU 1142 CZ3 TRP A 194 10880 5262 7807 713 -1257 126 C ATOM 1143 CH2 TRP A 194 7.615 -6.207 -6.112 1.00 63.06 C ANISOU 1143 CH2 TRP A 194 10934 5183 7843 671 -1183 162 C ATOM 1144 N LEU A 195 15.780 -4.533 -5.421 1.00 71.65 N ANISOU 1144 N LEU A 195 11295 6489 9436 950 -1478 -75 N ATOM 1145 CA LEU A 195 16.753 -3.482 -5.115 1.00 73.24 C ANISOU 1145 CA LEU A 195 11360 6759 9707 918 -1609 -93 C ATOM 1146 C LEU A 195 17.117 -2.672 -6.355 1.00 72.83 C ANISOU 1146 C LEU A 195 11220 6722 9729 794 -1514 -144 C ATOM 1147 O LEU A 195 17.162 -1.443 -6.304 1.00 73.49 O ANISOU 1147 O LEU A 195 11279 6841 9801 701 -1600 -171 O ATOM 1148 CB LEU A 195 18.031 -4.053 -4.498 1.00 75.81 C ANISOU 1148 CB LEU A 195 11529 7103 10170 1032 -1694 -43 C ATOM 1149 CG LEU A 195 18.089 -3.943 -2.980 1.00 77.27 C ANISOU 1149 CG LEU A 195 11749 7331 10278 1112 -1909 0 C ATOM 1150 CD1 LEU A 195 17.030 -4.834 -2.338 1.00 77.17 C ANISOU 1150 CD1 LEU A 195 11916 7278 10125 1202 -1876 51 C ATOM 1151 CD2 LEU A 195 19.484 -4.306 -2.499 1.00 79.31 C ANISOU 1151 CD2 LEU A 195 11814 7625 10695 1200 -2019 54 C ATOM 1152 N ALA A 196 17.384 -3.358 -7.462 1.00 71.91 N ANISOU 1152 N ALA A 196 11070 6571 9682 799 -1333 -156 N ATOM 1153 CA ALA A 196 17.726 -2.682 -8.707 1.00 71.45 C ANISOU 1153 CA ALA A 196 10940 6531 9675 696 -1214 -190 C ATOM 1154 C ALA A 196 16.588 -1.786 -9.182 1.00 69.48 C ANISOU 1154 C ALA A 196 10822 6289 9286 567 -1202 -222 C ATOM 1155 O ALA A 196 16.822 -0.689 -9.680 1.00 70.28 O ANISOU 1155 O ALA A 196 10861 6425 9416 468 -1203 -232 O ATOM 1156 CB ALA A 196 18.083 -3.695 -9.778 1.00 72.38 C ANISOU 1156 CB ALA A 196 11048 6603 9848 746 -1005 -205 C ATOM 1157 N SER A 197 15.357 -2.252 -9.020 1.00 68.24 N ANISOU 1157 N SER A 197 10835 6097 8994 570 -1192 -222 N ATOM 1158 CA SER A 197 14.180 -1.450 -9.336 1.00 67.42 C ANISOU 1158 CA SER A 197 10847 6004 8764 464 -1194 -229 C ATOM 1159 C SER A 197 14.144 -0.203 -8.466 1.00 67.80 C ANISOU 1159 C SER A 197 10878 6087 8793 436 -1347 -223 C ATOM 1160 O SER A 197 13.919 0.914 -8.955 1.00 67.43 O ANISOU 1160 O SER A 197 10831 6058 8730 335 -1345 -234 O ATOM 1161 CB SER A 197 12.900 -2.255 -9.098 1.00 66.99 C ANISOU 1161 CB SER A 197 10947 5906 8597 486 -1177 -205 C ATOM 1162 OG SER A 197 12.950 -3.522 -9.745 1.00 68.27 O ANISOU 1162 OG SER A 197 11146 6008 8783 518 -1060 -222 O ATOM 1163 N ALA A 198 14.360 -0.416 -7.169 1.00 68.30 N ANISOU 1163 N ALA A 198 10944 6154 8850 530 -1480 -205 N ATOM 1164 CA ALA A 198 14.378 0.659 -6.192 1.00 68.29 C ANISOU 1164 CA ALA A 198 10959 6174 8811 522 -1642 -217 C ATOM 1165 C ALA A 198 15.442 1.712 -6.516 1.00 68.90 C ANISOU 1165 C ALA A 198 10892 6269 9016 437 -1702 -249 C ATOM 1166 O ALA A 198 15.158 2.905 -6.456 1.00 69.07 O ANISOU 1166 O ALA A 198 10950 6283 9009 358 -1761 -273 O ATOM 1167 CB ALA A 198 14.581 0.095 -4.794 1.00 68.95 C ANISOU 1167 CB ALA A 198 11074 6266 8855 649 -1774 -192 C ATOM 1168 N LEU A 199 16.645 1.280 -6.882 1.00 69.73 N ANISOU 1168 N LEU A 199 10829 6389 9276 453 -1675 -238 N ATOM 1169 CA LEU A 199 17.724 2.219 -7.194 1.00 71.22 C ANISOU 1169 CA LEU A 199 10847 6594 9619 367 -1726 -244 C ATOM 1170 C LEU A 199 17.420 3.041 -8.440 1.00 71.02 C ANISOU 1170 C LEU A 199 10820 6562 9602 242 -1593 -248 C ATOM 1171 O LEU A 199 17.638 4.252 -8.462 1.00 71.00 O ANISOU 1171 O LEU A 199 10774 6548 9652 143 -1666 -257 O ATOM 1172 CB LEU A 199 19.053 1.485 -7.389 1.00 72.88 C ANISOU 1172 CB LEU A 199 10853 6827 10010 427 -1693 -205 C ATOM 1173 CG LEU A 199 19.624 0.682 -6.215 1.00 74.09 C ANISOU 1173 CG LEU A 199 10959 6995 10196 554 -1836 -177 C ATOM 1174 CD1 LEU A 199 21.113 0.450 -6.425 1.00 76.08 C ANISOU 1174 CD1 LEU A 199 10951 7276 10678 580 -1839 -124 C ATOM 1175 CD2 LEU A 199 19.379 1.374 -4.880 1.00 74.46 C ANISOU 1175 CD2 LEU A 199 11095 7049 10146 552 -2079 -205 C ATOM 1176 N LEU A 200 16.912 2.380 -9.476 1.00 71.00 N ANISOU 1176 N LEU A 200 10874 6559 9542 244 -1403 -240 N ATOM 1177 CA LEU A 200 16.598 3.056 -10.743 1.00 70.72 C ANISOU 1177 CA LEU A 200 10850 6529 9489 135 -1269 -232 C ATOM 1178 C LEU A 200 15.416 4.026 -10.650 1.00 68.88 C ANISOU 1178 C LEU A 200 10757 6279 9133 61 -1318 -236 C ATOM 1179 O LEU A 200 15.193 4.804 -11.577 1.00 68.46 O ANISOU 1179 O LEU A 200 10705 6231 9075 -33 -1239 -215 O ATOM 1180 CB LEU A 200 16.319 2.025 -11.846 1.00 70.69 C ANISOU 1180 CB LEU A 200 10903 6529 9426 161 -1072 -234 C ATOM 1181 CG LEU A 200 17.515 1.199 -12.313 1.00 72.46 C ANISOU 1181 CG LEU A 200 10989 6762 9779 232 -956 -226 C ATOM 1182 CD1 LEU A 200 17.042 -0.067 -13.026 1.00 72.81 C ANISOU 1182 CD1 LEU A 200 11158 6778 9728 291 -800 -257 C ATOM 1183 CD2 LEU A 200 18.427 2.031 -13.205 1.00 73.22 C ANISOU 1183 CD2 LEU A 200 10929 6893 9997 158 -862 -188 C ATOM 1184 N ALA A 201 14.651 3.961 -9.558 1.00 67.94 N ANISOU 1184 N ALA A 201 10757 6141 8913 117 -1434 -250 N ATOM 1185 CA ALA A 201 13.530 4.883 -9.338 1.00 67.24 C ANISOU 1185 CA ALA A 201 10798 6031 8718 75 -1473 -245 C ATOM 1186 C ALA A 201 13.913 6.119 -8.503 1.00 67.87 C ANISOU 1186 C ALA A 201 10864 6077 8846 45 -1631 -276 C ATOM 1187 O ALA A 201 13.098 7.032 -8.342 1.00 66.98 O ANISOU 1187 O ALA A 201 10854 5930 8665 15 -1655 -276 O ATOM 1188 CB ALA A 201 12.364 4.150 -8.687 1.00 65.86 C ANISOU 1188 CB ALA A 201 10770 5852 8401 159 -1479 -230 C ATOM 1189 N ILE A 202 15.145 6.148 -7.989 1.00 69.35 N ANISOU 1189 N ILE A 202 10925 6266 9158 52 -1741 -301 N ATOM 1190 CA ILE A 202 15.592 7.215 -7.086 1.00 70.72 C ANISOU 1190 CA ILE A 202 11096 6396 9378 18 -1929 -347 C ATOM 1191 C ILE A 202 15.587 8.581 -7.772 1.00 70.93 C ANISOU 1191 C ILE A 202 11098 6371 9480 -113 -1908 -342 C ATOM 1192 O ILE A 202 15.129 9.551 -7.175 1.00 70.96 O ANISOU 1192 O ILE A 202 11215 6310 9435 -133 -2007 -382 O ATOM 1193 CB ILE A 202 17.001 6.946 -6.495 1.00 72.79 C ANISOU 1193 CB ILE A 202 11195 6677 9785 32 -2071 -360 C ATOM 1194 CG1 ILE A 202 17.011 5.664 -5.641 1.00 73.27 C ANISOU 1194 CG1 ILE A 202 11292 6779 9767 177 -2116 -355 C ATOM 1195 CG2 ILE A 202 17.480 8.137 -5.669 1.00 73.83 C ANISOU 1195 CG2 ILE A 202 11328 6750 9971 -34 -2287 -418 C ATOM 1196 CD1 ILE A 202 16.321 5.780 -4.296 1.00 73.42 C ANISOU 1196 CD1 ILE A 202 11499 6782 9612 261 -2260 -396 C ATOM 1197 N PRO A 203 16.088 8.667 -9.022 1.00 70.86 N ANISOU 1197 N PRO A 203 10952 6383 9586 -195 -1771 -288 N ATOM 1198 CA PRO A 203 15.983 9.929 -9.749 1.00 70.93 C ANISOU 1198 CA PRO A 203 10946 6342 9659 -317 -1730 -259 C ATOM 1199 C PRO A 203 14.600 10.589 -9.693 1.00 70.03 C ANISOU 1199 C PRO A 203 11023 6184 9400 -313 -1710 -259 C ATOM 1200 O PRO A 203 14.516 11.812 -9.659 1.00 71.49 O ANISOU 1200 O PRO A 203 11235 6290 9636 -387 -1761 -263 O ATOM 1201 CB PRO A 203 16.327 9.524 -11.179 1.00 70.86 C ANISOU 1201 CB PRO A 203 10824 6393 9706 -358 -1527 -186 C ATOM 1202 CG PRO A 203 17.317 8.428 -11.004 1.00 71.54 C ANISOU 1202 CG PRO A 203 10777 6531 9872 -289 -1523 -191 C ATOM 1203 CD PRO A 203 16.887 7.680 -9.775 1.00 71.07 C ANISOU 1203 CD PRO A 203 10830 6473 9700 -174 -1647 -248 C ATOM 1204 N MET A 204 13.529 9.805 -9.655 1.00 68.97 N ANISOU 1204 N MET A 204 11012 6090 9101 -229 -1638 -248 N ATOM 1205 CA MET A 204 12.184 10.381 -9.613 1.00 68.48 C ANISOU 1205 CA MET A 204 11104 5995 8918 -215 -1608 -224 C ATOM 1206 C MET A 204 11.870 11.103 -8.292 1.00 68.44 C ANISOU 1206 C MET A 204 11225 5913 8864 -159 -1752 -288 C ATOM 1207 O MET A 204 10.981 11.949 -8.260 1.00 68.44 O ANISOU 1207 O MET A 204 11333 5859 8812 -157 -1731 -269 O ATOM 1208 CB MET A 204 11.124 9.317 -9.917 1.00 68.04 C ANISOU 1208 CB MET A 204 11126 6002 8722 -149 -1503 -180 C ATOM 1209 CG MET A 204 11.249 8.678 -11.301 1.00 68.79 C ANISOU 1209 CG MET A 204 11149 6160 8827 -206 -1358 -131 C ATOM 1210 SD MET A 204 11.059 9.828 -12.690 1.00 70.12 S ANISOU 1210 SD MET A 204 11286 6324 9031 -332 -1258 -53 S ATOM 1211 CE MET A 204 9.289 10.114 -12.668 1.00 68.85 C ANISOU 1211 CE MET A 204 11272 6158 8727 -306 -1240 12 C ATOM 1212 N LEU A 205 12.587 10.778 -7.214 1.00 68.72 N ANISOU 1212 N LEU A 205 11256 5944 8908 -105 -1896 -360 N ATOM 1213 CA LEU A 205 12.484 11.534 -5.947 1.00 69.10 C ANISOU 1213 CA LEU A 205 11439 5914 8899 -59 -2054 -442 C ATOM 1214 C LEU A 205 13.041 12.951 -6.074 1.00 70.04 C ANISOU 1214 C LEU A 205 11534 5924 9151 -177 -2140 -482 C ATOM 1215 O LEU A 205 12.583 13.860 -5.389 1.00 70.04 O ANISOU 1215 O LEU A 205 11688 5829 9094 -154 -2213 -540 O ATOM 1216 CB LEU A 205 13.233 10.826 -4.814 1.00 69.60 C ANISOU 1216 CB LEU A 205 11498 6009 8934 16 -2210 -504 C ATOM 1217 CG LEU A 205 12.750 9.426 -4.433 1.00 68.23 C ANISOU 1217 CG LEU A 205 11366 5923 8635 146 -2151 -466 C ATOM 1218 CD1 LEU A 205 13.778 8.735 -3.554 1.00 69.05 C ANISOU 1218 CD1 LEU A 205 11410 6064 8761 200 -2305 -503 C ATOM 1219 CD2 LEU A 205 11.396 9.491 -3.740 1.00 67.48 C ANISOU 1219 CD2 LEU A 205 11476 5814 8350 259 -2107 -455 C ATOM 1220 N PHE A 206 14.031 13.117 -6.950 1.00 70.71 N ANISOU 1220 N PHE A 206 11428 6017 9420 -299 -2120 -446 N ATOM 1221 CA PHE A 206 14.731 14.386 -7.134 1.00 71.83 C ANISOU 1221 CA PHE A 206 11507 6052 9733 -433 -2205 -465 C ATOM 1222 C PHE A 206 14.244 15.208 -8.344 1.00 71.77 C ANISOU 1222 C PHE A 206 11480 6003 9785 -519 -2047 -374 C ATOM 1223 O PHE A 206 14.477 16.418 -8.394 1.00 73.75 O ANISOU 1223 O PHE A 206 11737 6132 10153 -614 -2105 -384 O ATOM 1224 CB PHE A 206 16.244 14.131 -7.223 1.00 72.94 C ANISOU 1224 CB PHE A 206 11423 6221 10068 -515 -2297 -462 C ATOM 1225 CG PHE A 206 16.844 13.568 -5.952 1.00 73.78 C ANISOU 1225 CG PHE A 206 11540 6350 10140 -447 -2501 -547 C ATOM 1226 CD1 PHE A 206 17.094 14.394 -4.854 1.00 75.02 C ANISOU 1226 CD1 PHE A 206 11804 6405 10295 -472 -2731 -655 C ATOM 1227 CD2 PHE A 206 17.158 12.209 -5.846 1.00 72.97 C ANISOU 1227 CD2 PHE A 206 11355 6367 10001 -354 -2469 -518 C ATOM 1228 CE1 PHE A 206 17.641 13.879 -3.686 1.00 75.97 C ANISOU 1228 CE1 PHE A 206 11947 6557 10361 -409 -2935 -727 C ATOM 1229 CE2 PHE A 206 17.706 11.692 -4.679 1.00 73.56 C ANISOU 1229 CE2 PHE A 206 11438 6468 10041 -285 -2661 -577 C ATOM 1230 CZ PHE A 206 17.947 12.527 -3.598 1.00 75.21 C ANISOU 1230 CZ PHE A 206 11752 6592 10232 -313 -2900 -678 C ATOM 1231 N THR A 207 13.554 14.578 -9.298 1.00 70.16 N ANISOU 1231 N THR A 207 11265 5892 9500 -490 -1860 -283 N ATOM 1232 CA THR A 207 13.089 15.284 -10.501 1.00 69.83 C ANISOU 1232 CA THR A 207 11205 5832 9495 -566 -1716 -180 C ATOM 1233 C THR A 207 11.626 15.722 -10.442 1.00 68.74 C ANISOU 1233 C THR A 207 11240 5658 9218 -500 -1658 -148 C ATOM 1234 O THR A 207 11.279 16.751 -10.997 1.00 70.00 O ANISOU 1234 O THR A 207 11419 5744 9431 -558 -1608 -85 O ATOM 1235 CB THR A 207 13.259 14.437 -11.777 1.00 69.48 C ANISOU 1235 CB THR A 207 11042 5912 9444 -591 -1546 -90 C ATOM 1236 OG1 THR A 207 12.338 13.347 -11.748 1.00 68.33 O ANISOU 1236 OG1 THR A 207 10986 5853 9120 -490 -1482 -87 O ATOM 1237 CG2 THR A 207 14.691 13.902 -11.920 1.00 70.41 C ANISOU 1237 CG2 THR A 207 10971 6076 9706 -632 -1563 -100 C ATOM 1238 N MET A 208 10.757 14.937 -9.817 1.00 68.15 N ANISOU 1238 N MET A 208 11277 5637 8979 -376 -1652 -170 N ATOM 1239 CA MET A 208 9.365 15.361 -9.624 1.00 68.30 C ANISOU 1239 CA MET A 208 11445 5621 8884 -298 -1598 -128 C ATOM 1240 C MET A 208 9.302 16.316 -8.442 1.00 69.85 C ANISOU 1240 C MET A 208 11780 5680 9078 -248 -1716 -223 C ATOM 1241 O MET A 208 10.224 16.379 -7.625 1.00 71.10 O ANISOU 1241 O MET A 208 11939 5792 9280 -260 -1862 -333 O ATOM 1242 CB MET A 208 8.427 14.176 -9.356 1.00 67.75 C ANISOU 1242 CB MET A 208 11433 5653 8655 -186 -1542 -100 C ATOM 1243 CG MET A 208 8.229 13.191 -10.507 1.00 67.02 C ANISOU 1243 CG MET A 208 11251 5681 8533 -227 -1428 -16 C ATOM 1244 SD MET A 208 7.678 13.904 -12.081 1.00 67.29 S ANISOU 1244 SD MET A 208 11240 5732 8594 -329 -1305 119 S ATOM 1245 CE MET A 208 9.270 14.001 -12.890 1.00 68.00 C ANISOU 1245 CE MET A 208 11176 5832 8827 -452 -1293 98 C ATOM 1246 N GLY A 209 8.209 17.061 -8.352 1.00 70.64 N ANISOU 1246 N GLY A 209 12003 5711 9124 -187 -1656 -178 N ATOM 1247 CA GLY A 209 8.063 18.075 -7.310 1.00 72.22 C ANISOU 1247 CA GLY A 209 12368 5758 9313 -128 -1742 -273 C ATOM 1248 C GLY A 209 6.749 18.820 -7.402 1.00 72.10 C ANISOU 1248 C GLY A 209 12468 5676 9249 -42 -1628 -191 C ATOM 1249 O GLY A 209 6.146 18.895 -8.471 1.00 71.53 O ANISOU 1249 O GLY A 209 12317 5652 9206 -78 -1507 -49 O ATOM 1250 N LEU A 210 6.299 19.344 -6.264 1.00 73.43 N ANISOU 1250 N LEU A 210 12826 5738 9333 81 -1666 -276 N ATOM 1251 CA LEU A 210 5.095 20.168 -6.199 1.00 73.72 C ANISOU 1251 CA LEU A 210 12985 5686 9337 188 -1553 -206 C ATOM 1252 C LEU A 210 5.456 21.548 -6.681 1.00 74.16 C ANISOU 1252 C LEU A 210 13051 5567 9556 89 -1572 -210 C ATOM 1253 O LEU A 210 6.568 22.004 -6.450 1.00 75.65 O ANISOU 1253 O LEU A 210 13240 5659 9844 -17 -1712 -328 O ATOM 1254 CB LEU A 210 4.568 20.265 -4.771 1.00 75.36 C ANISOU 1254 CB LEU A 210 13412 5830 9388 372 -1570 -306 C ATOM 1255 CG LEU A 210 3.202 20.941 -4.637 1.00 76.75 C ANISOU 1255 CG LEU A 210 13707 5935 9518 525 -1415 -213 C ATOM 1256 CD1 LEU A 210 2.123 20.101 -5.310 1.00 75.51 C ANISOU 1256 CD1 LEU A 210 13420 5945 9324 571 -1265 -15 C ATOM 1257 CD2 LEU A 210 2.864 21.185 -3.173 0.00 78.57 C ANISOU 1257 CD2 LEU A 210 14185 6077 9589 711 -1429 -338 C ATOM 1258 N GLN A 211 4.514 22.216 -7.335 1.00 73.19 N ANISOU 1258 N GLN A 211 12932 5402 9475 123 -1439 -70 N ATOM 1259 CA GLN A 211 4.804 23.480 -7.987 1.00 74.12 C ANISOU 1259 CA GLN A 211 13037 5359 9765 22 -1436 -33 C ATOM 1260 C GLN A 211 3.521 24.223 -8.334 1.00 74.24 C ANISOU 1260 C GLN A 211 13109 5310 9789 129 -1285 115 C ATOM 1261 O GLN A 211 2.553 23.615 -8.798 1.00 73.06 O ANISOU 1261 O GLN A 211 12888 5307 9565 196 -1173 265 O ATOM 1262 CB GLN A 211 5.646 23.216 -9.235 1.00 73.68 C ANISOU 1262 CB GLN A 211 12767 5397 9832 -166 -1441 51 C ATOM 1263 CG GLN A 211 5.685 24.334 -10.257 1.00 75.16 C ANISOU 1263 CG GLN A 211 12897 5475 10185 -266 -1380 175 C ATOM 1264 CD GLN A 211 6.803 24.145 -11.265 1.00 75.85 C ANISOU 1264 CD GLN A 211 12792 5631 10395 -452 -1399 223 C ATOM 1265 OE1 GLN A 211 6.555 23.817 -12.432 1.00 75.97 O ANISOU 1265 OE1 GLN A 211 12686 5778 10401 -500 -1295 381 O ATOM 1266 NE2 GLN A 211 8.046 24.334 -10.816 1.00 76.87 N ANISOU 1266 NE2 GLN A 211 12894 5676 10635 -556 -1535 92 N ATOM 1267 N ASN A 212 3.518 25.536 -8.099 1.00 75.25 N ANISOU 1267 N ASN A 212 13363 5210 10018 144 -1291 76 N ATOM 1268 CA ASN A 212 2.364 26.363 -8.423 1.00 75.51 C ANISOU 1268 CA ASN A 212 13448 5155 10087 255 -1145 225 C ATOM 1269 C ASN A 212 2.468 26.936 -9.830 1.00 75.97 C ANISOU 1269 C ASN A 212 13352 5205 10306 119 -1093 405 C ATOM 1270 O ASN A 212 3.373 27.714 -10.122 1.00 76.97 O ANISOU 1270 O ASN A 212 13466 5188 10588 -18 -1161 364 O ATOM 1271 CB ASN A 212 2.179 27.499 -7.412 1.00 76.75 C ANISOU 1271 CB ASN A 212 13850 5049 10261 375 -1154 95 C ATOM 1272 CG ASN A 212 0.780 28.069 -7.462 1.00 76.39 C ANISOU 1272 CG ASN A 212 13872 4944 10206 563 -974 247 C ATOM 1273 OD1 ASN A 212 0.348 28.538 -8.505 1.00 76.32 O ANISOU 1273 OD1 ASN A 212 13748 4935 10315 526 -887 443 O ATOM 1274 ND2 ASN A 212 0.048 27.983 -6.360 1.00 76.41 N ANISOU 1274 ND2 ASN A 212 14051 4915 10066 775 -911 177 N ATOM 1275 N ARG A 213 1.529 26.551 -10.692 1.00 75.62 N ANISOU 1275 N ARG A 213 13190 5317 10224 154 -977 615 N ATOM 1276 CA ARG A 213 1.524 27.008 -12.080 1.00 76.48 C ANISOU 1276 CA ARG A 213 13160 5451 10447 38 -922 810 C ATOM 1277 C ARG A 213 0.409 28.015 -12.385 1.00 77.26 C ANISOU 1277 C ARG A 213 13299 5438 10615 154 -803 989 C ATOM 1278 O ARG A 213 0.239 28.410 -13.536 1.00 77.33 O ANISOU 1278 O ARG A 213 13200 5479 10702 80 -752 1181 O ATOM 1279 CB ARG A 213 1.471 25.812 -13.048 1.00 75.14 C ANISOU 1279 CB ARG A 213 12813 5550 10184 -45 -908 921 C ATOM 1280 CG ARG A 213 2.836 25.424 -13.605 1.00 75.55 C ANISOU 1280 CG ARG A 213 12759 5663 10283 -231 -981 853 C ATOM 1281 CD ARG A 213 2.723 24.331 -14.656 1.00 75.25 C ANISOU 1281 CD ARG A 213 12577 5869 10143 -301 -947 964 C ATOM 1282 NE ARG A 213 3.901 23.458 -14.644 1.00 76.21 N ANISOU 1282 NE ARG A 213 12630 6079 10246 -404 -1014 834 N ATOM 1283 CZ ARG A 213 5.005 23.639 -15.373 1.00 77.51 C ANISOU 1283 CZ ARG A 213 12697 6243 10507 -550 -1020 844 C ATOM 1284 NH1 ARG A 213 5.116 24.675 -16.206 1.00 79.20 N ANISOU 1284 NH1 ARG A 213 12877 6373 10842 -623 -965 979 N ATOM 1285 NH2 ARG A 213 6.010 22.770 -15.269 1.00 76.39 N ANISOU 1285 NH2 ARG A 213 12486 6187 10351 -615 -1070 732 N ATOM 1286 N SER A 214 -0.328 28.448 -11.363 1.00 78.15 N ANISOU 1286 N SER A 214 13574 5421 10698 342 -753 933 N ATOM 1287 CA SER A 214 -1.344 29.494 -11.542 1.00 79.50 C ANISOU 1287 CA SER A 214 13795 5453 10958 476 -629 1096 C ATOM 1288 C SER A 214 -0.762 30.735 -12.216 1.00 80.84 C ANISOU 1288 C SER A 214 13968 5420 11325 363 -637 1149 C ATOM 1289 O SER A 214 0.441 30.995 -12.129 1.00 80.06 O ANISOU 1289 O SER A 214 13895 5217 11306 212 -744 1002 O ATOM 1290 CB SER A 214 -1.964 29.905 -10.201 1.00 80.76 C ANISOU 1290 CB SER A 214 14169 5451 11065 700 -569 978 C ATOM 1291 OG SER A 214 -1.088 30.733 -9.452 1.00 82.04 O ANISOU 1291 OG SER A 214 14521 5357 11293 671 -653 755 O ATOM 1292 N ALA A 215 -1.627 31.483 -12.897 1.00 82.54 N ANISOU 1292 N ALA A 215 14145 5583 11631 434 -526 1378 N ATOM 1293 CA ALA A 215 -1.233 32.744 -13.520 1.00 85.15 C ANISOU 1293 CA ALA A 215 14489 5700 12163 353 -510 1463 C ATOM 1294 C ALA A 215 -0.768 33.644 -12.401 1.00 88.10 C ANISOU 1294 C ALA A 215 15093 5759 12622 405 -548 1236 C ATOM 1295 O ALA A 215 0.382 34.093 -12.380 1.00 88.92 O ANISOU 1295 O ALA A 215 15228 5715 12840 240 -652 1108 O ATOM 1296 CB ALA A 215 -2.399 33.375 -14.272 1.00 85.66 C ANISOU 1296 CB ALA A 215 14491 5757 12299 468 -378 1755 C ATOM 1297 N ASP A 216 -1.671 33.862 -11.449 1.00 90.29 N ANISOU 1297 N ASP A 216 15531 5939 12836 635 -465 1185 N ATOM 1298 CA ASP A 216 -1.352 34.516 -10.188 1.00 93.41 C ANISOU 1298 CA ASP A 216 16191 6059 13239 720 -503 928 C ATOM 1299 C ASP A 216 -0.089 33.883 -9.598 1.00 92.85 C ANISOU 1299 C ASP A 216 16154 6028 13096 561 -690 665 C ATOM 1300 O ASP A 216 0.198 32.715 -9.864 1.00 90.82 O ANISOU 1300 O ASP A 216 15740 6040 12725 474 -745 674 O ATOM 1301 CB ASP A 216 -2.535 34.331 -9.226 1.00 94.27 C ANISOU 1301 CB ASP A 216 16437 6176 13205 1005 -373 911 C ATOM 1302 CG ASP A 216 -2.261 34.883 -7.841 1.00 96.41 C ANISOU 1302 CG ASP A 216 17019 6187 13425 1120 -407 625 C ATOM 1303 OD1 ASP A 216 -2.084 36.119 -7.733 1.00 98.48 O ANISOU 1303 OD1 ASP A 216 17441 6135 13840 1132 -396 571 O ATOM 1304 OD2 ASP A 216 -2.228 34.082 -6.871 1.00 95.07 O ANISOU 1304 OD2 ASP A 216 16943 6122 13056 1197 -446 456 O ATOM 1305 N GLY A 217 0.666 34.647 -8.810 1.00 94.77 N ANISOU 1305 N GLY A 217 16600 5998 13410 520 -797 435 N ATOM 1306 CA GLY A 217 1.816 34.092 -8.096 1.00 94.77 C ANISOU 1306 CA GLY A 217 16645 6024 13339 389 -993 180 C ATOM 1307 C GLY A 217 1.552 32.674 -7.579 1.00 93.27 C ANISOU 1307 C GLY A 217 16409 6124 12903 473 -1001 130 C ATOM 1308 O GLY A 217 2.178 31.703 -8.026 1.00 89.28 O ANISOU 1308 O GLY A 217 15715 5843 12361 329 -1080 148 O ATOM 1309 N THR A 218 0.601 32.550 -6.655 1.00 93.97 N ANISOU 1309 N THR A 218 16670 6202 12829 717 -903 82 N ATOM 1310 CA THR A 218 0.366 31.285 -5.968 1.00 91.73 C ANISOU 1310 CA THR A 218 16382 6153 12316 810 -911 18 C ATOM 1311 C THR A 218 -1.034 31.239 -5.329 1.00 91.92 C ANISOU 1311 C THR A 218 16528 6193 12205 1102 -718 90 C ATOM 1312 O THR A 218 -1.242 31.704 -4.206 1.00 95.02 O ANISOU 1312 O THR A 218 17189 6414 12500 1270 -694 -74 O ATOM 1313 CB THR A 218 1.502 31.030 -4.940 1.00 93.01 C ANISOU 1313 CB THR A 218 16690 6260 12390 730 -1121 -273 C ATOM 1314 OG1 THR A 218 2.722 30.775 -5.650 1.00 92.15 O ANISOU 1314 OG1 THR A 218 16388 6215 12409 464 -1277 -283 O ATOM 1315 CG2 THR A 218 1.222 29.834 -3.989 0.00 92.33 C ANISOU 1315 CG2 THR A 218 16659 6374 12046 866 -1125 -356 C ATOM 1316 N HIS A 219 -1.986 30.701 -6.089 1.00 89.33 N ANISOU 1316 N HIS A 219 15997 6068 11875 1158 -579 348 N ATOM 1317 CA HIS A 219 -3.322 30.357 -5.604 1.00 88.47 C ANISOU 1317 CA HIS A 219 15917 6048 11648 1412 -395 468 C ATOM 1318 C HIS A 219 -3.332 28.838 -5.283 1.00 85.66 C ANISOU 1318 C HIS A 219 15458 5973 11113 1403 -435 455 C ATOM 1319 O HIS A 219 -2.721 28.047 -6.014 1.00 81.86 O ANISOU 1319 O HIS A 219 14785 5667 10648 1205 -543 487 O ATOM 1320 CB HIS A 219 -4.344 30.715 -6.694 1.00 88.73 C ANISOU 1320 CB HIS A 219 15764 6128 11819 1455 -246 778 C ATOM 1321 CG HIS A 219 -5.776 30.638 -6.255 1.00 90.22 C ANISOU 1321 CG HIS A 219 15966 6362 11949 1726 -40 937 C ATOM 1322 ND1 HIS A 219 -6.423 29.441 -6.035 1.00 89.25 N ANISOU 1322 ND1 HIS A 219 15725 6490 11695 1796 10 1031 N ATOM 1323 CD2 HIS A 219 -6.693 31.607 -6.019 1.00 92.60 C ANISOU 1323 CD2 HIS A 219 16372 6487 12324 1946 136 1037 C ATOM 1324 CE1 HIS A 219 -7.672 29.672 -5.673 1.00 90.51 C ANISOU 1324 CE1 HIS A 219 15900 6635 11853 2043 209 1189 C ATOM 1325 NE2 HIS A 219 -7.862 30.980 -5.657 1.00 92.61 N ANISOU 1325 NE2 HIS A 219 16300 6646 12239 2147 295 1195 N ATOM 1326 N PRO A 220 -4.002 28.427 -4.185 1.00 85.85 N ANISOU 1326 N PRO A 220 15618 6033 10966 1622 -338 411 N ATOM 1327 CA PRO A 220 -3.947 27.022 -3.733 1.00 84.00 C ANISOU 1327 CA PRO A 220 15317 6033 10564 1622 -378 385 C ATOM 1328 C PRO A 220 -4.561 26.004 -4.697 1.00 81.83 C ANISOU 1328 C PRO A 220 14750 6019 10322 1551 -333 630 C ATOM 1329 O PRO A 220 -4.185 24.828 -4.669 1.00 81.00 O ANISOU 1329 O PRO A 220 14550 6096 10129 1461 -416 600 O ATOM 1330 CB PRO A 220 -4.722 27.037 -2.406 1.00 85.54 C ANISOU 1330 CB PRO A 220 15733 6180 10588 1906 -235 332 C ATOM 1331 CG PRO A 220 -5.544 28.276 -2.439 1.00 87.76 C ANISOU 1331 CG PRO A 220 16115 6259 10968 2077 -65 419 C ATOM 1332 CD PRO A 220 -4.754 29.269 -3.238 1.00 88.32 C ANISOU 1332 CD PRO A 220 16179 6151 11228 1889 -182 367 C ATOM 1333 N GLY A 221 -5.516 26.444 -5.509 1.00 81.35 N ANISOU 1333 N GLY A 221 14557 5968 10385 1596 -207 870 N ATOM 1334 CA GLY A 221 -6.028 25.651 -6.630 1.00 78.97 C ANISOU 1334 CA GLY A 221 13977 5889 10135 1486 -203 1103 C ATOM 1335 C GLY A 221 -5.101 25.474 -7.827 1.00 76.72 C ANISOU 1335 C GLY A 221 13545 5672 9930 1217 -351 1102 C ATOM 1336 O GLY A 221 -5.449 24.771 -8.772 1.00 74.71 O ANISOU 1336 O GLY A 221 13089 5604 9693 1116 -364 1269 O ATOM 1337 N GLY A 222 -3.930 26.105 -7.804 1.00 76.94 N ANISOU 1337 N GLY A 222 13674 5550 10007 1100 -461 920 N ATOM 1338 CA GLY A 222 -2.982 26.006 -8.912 1.00 76.04 C ANISOU 1338 CA GLY A 222 13422 5490 9976 856 -577 925 C ATOM 1339 C GLY A 222 -1.741 25.178 -8.635 1.00 74.70 C ANISOU 1339 C GLY A 222 13251 5393 9738 715 -726 727 C ATOM 1340 O GLY A 222 -0.761 25.266 -9.370 1.00 75.44 O ANISOU 1340 O GLY A 222 13263 5487 9913 528 -816 695 O ATOM 1341 N LEU A 223 -1.773 24.380 -7.576 1.00 73.94 N ANISOU 1341 N LEU A 223 13239 5357 9497 813 -744 609 N ATOM 1342 CA LEU A 223 -0.668 23.477 -7.258 1.00 72.80 C ANISOU 1342 CA LEU A 223 13079 5297 9282 701 -884 443 C ATOM 1343 C LEU A 223 -0.779 22.184 -8.061 1.00 69.97 C ANISOU 1343 C LEU A 223 12522 5173 8886 606 -887 556 C ATOM 1344 O LEU A 223 -1.855 21.591 -8.138 1.00 68.20 O ANISOU 1344 O LEU A 223 12237 5068 8607 694 -795 702 O ATOM 1345 CB LEU A 223 -0.664 23.165 -5.763 1.00 73.87 C ANISOU 1345 CB LEU A 223 13403 5398 9266 856 -905 280 C ATOM 1346 CG LEU A 223 -0.357 24.402 -4.905 1.00 75.84 C ANISOU 1346 CG LEU A 223 13888 5398 9527 933 -936 115 C ATOM 1347 CD1 LEU A 223 -0.941 24.266 -3.505 1.00 77.13 C ANISOU 1347 CD1 LEU A 223 14266 5530 9509 1164 -875 27 C ATOM 1348 CD2 LEU A 223 1.147 24.653 -4.858 1.00 75.91 C ANISOU 1348 CD2 LEU A 223 13918 5320 9605 750 -1134 -75 C ATOM 1349 N VAL A 224 0.334 21.773 -8.668 1.00 68.98 N ANISOU 1349 N VAL A 224 12300 5107 8802 425 -990 491 N ATOM 1350 CA VAL A 224 0.389 20.567 -9.500 1.00 67.44 C ANISOU 1350 CA VAL A 224 11941 5113 8571 323 -998 569 C ATOM 1351 C VAL A 224 1.691 19.808 -9.274 1.00 66.67 C ANISOU 1351 C VAL A 224 11815 5060 8453 224 -1114 408 C ATOM 1352 O VAL A 224 2.756 20.417 -9.152 1.00 67.02 O ANISOU 1352 O VAL A 224 11885 4998 8580 143 -1199 291 O ATOM 1353 CB VAL A 224 0.270 20.876 -11.024 1.00 67.66 C ANISOU 1353 CB VAL A 224 11829 5192 8685 193 -961 733 C ATOM 1354 CG1 VAL A 224 -1.101 21.453 -11.364 1.00 68.43 C ANISOU 1354 CG1 VAL A 224 11914 5280 8803 289 -854 931 C ATOM 1355 CG2 VAL A 224 1.375 21.812 -11.508 1.00 68.37 C ANISOU 1355 CG2 VAL A 224 11909 5162 8903 63 -1010 676 C ATOM 1356 N CYS A 225 1.593 18.476 -9.231 1.00 65.04 N ANISOU 1356 N CYS A 225 11547 5007 8155 228 -1119 415 N ATOM 1357 CA CYS A 225 2.762 17.598 -9.240 1.00 63.63 C ANISOU 1357 CA CYS A 225 11309 4897 7971 135 -1208 301 C ATOM 1358 C CYS A 225 3.169 17.398 -10.691 1.00 61.44 C ANISOU 1358 C CYS A 225 10885 4700 7758 -20 -1186 381 C ATOM 1359 O CYS A 225 2.328 17.079 -11.524 1.00 60.20 O ANISOU 1359 O CYS A 225 10669 4634 7569 -36 -1116 521 O ATOM 1360 CB CYS A 225 2.434 16.239 -8.602 1.00 63.75 C ANISOU 1360 CB CYS A 225 11330 5025 7866 217 -1209 287 C ATOM 1361 SG CYS A 225 3.733 14.994 -8.801 1.00 63.21 S ANISOU 1361 SG CYS A 225 11163 5052 7800 116 -1292 187 S ATOM 1362 N THR A 226 4.455 17.570 -10.975 1.00 60.57 N ANISOU 1362 N THR A 226 10719 4561 7734 -131 -1248 298 N ATOM 1363 CA THR A 226 4.961 17.602 -12.340 1.00 60.53 C ANISOU 1363 CA THR A 226 10591 4613 7794 -270 -1206 374 C ATOM 1364 C THR A 226 6.479 17.627 -12.223 1.00 60.59 C ANISOU 1364 C THR A 226 10534 4585 7903 -359 -1282 259 C ATOM 1365 O THR A 226 6.988 17.927 -11.156 1.00 60.95 O ANISOU 1365 O THR A 226 10640 4537 7981 -324 -1380 138 O ATOM 1366 CB THR A 226 4.415 18.850 -13.106 1.00 62.16 C ANISOU 1366 CB THR A 226 10799 4745 8071 -303 -1143 507 C ATOM 1367 OG1 THR A 226 5.090 19.036 -14.363 1.00 63.21 O ANISOU 1367 OG1 THR A 226 10825 4920 8271 -439 -1103 578 O ATOM 1368 CG2 THR A 226 4.573 20.128 -12.281 1.00 63.60 C ANISOU 1368 CG2 THR A 226 11082 4734 8349 -264 -1187 442 C ATOM 1369 N PRO A 227 7.211 17.269 -13.294 1.00 60.66 N ANISOU 1369 N PRO A 227 10419 4673 7954 -467 -1237 300 N ATOM 1370 CA PRO A 227 8.657 17.462 -13.230 1.00 62.14 C ANISOU 1370 CA PRO A 227 10516 4818 8277 -553 -1296 223 C ATOM 1371 C PRO A 227 8.971 18.930 -13.003 1.00 64.59 C ANISOU 1371 C PRO A 227 10850 4957 8733 -607 -1346 218 C ATOM 1372 O PRO A 227 8.226 19.791 -13.478 1.00 64.49 O ANISOU 1372 O PRO A 227 10883 4886 8732 -609 -1283 320 O ATOM 1373 CB PRO A 227 9.165 17.028 -14.607 1.00 61.75 C ANISOU 1373 CB PRO A 227 10340 4876 8242 -646 -1190 310 C ATOM 1374 CG PRO A 227 8.043 16.340 -15.276 1.00 60.67 C ANISOU 1374 CG PRO A 227 10249 4854 7948 -607 -1107 394 C ATOM 1375 CD PRO A 227 6.788 16.509 -14.479 1.00 60.02 C ANISOU 1375 CD PRO A 227 10283 4732 7787 -504 -1141 402 C ATOM 1376 N ILE A 228 10.054 19.201 -12.279 1.00 66.69 N ANISOU 1376 N ILE A 228 11086 5138 9114 -651 -1468 105 N ATOM 1377 CA ILE A 228 10.399 20.564 -11.876 1.00 69.09 C ANISOU 1377 CA ILE A 228 11435 5250 9565 -709 -1550 69 C ATOM 1378 C ILE A 228 11.896 20.837 -12.000 1.00 71.11 C ANISOU 1378 C ILE A 228 11537 5460 10021 -849 -1631 38 C ATOM 1379 O ILE A 228 12.463 21.600 -11.223 1.00 72.82 O ANISOU 1379 O ILE A 228 11789 5523 10353 -897 -1776 -57 O ATOM 1380 CB ILE A 228 9.910 20.866 -10.440 1.00 69.55 C ANISOU 1380 CB ILE A 228 11684 5196 9544 -595 -1666 -65 C ATOM 1381 CG1 ILE A 228 10.282 19.747 -9.461 1.00 69.43 C ANISOU 1381 CG1 ILE A 228 11684 5271 9424 -523 -1768 -188 C ATOM 1382 CG2 ILE A 228 8.397 21.008 -10.422 1.00 68.82 C ANISOU 1382 CG2 ILE A 228 11726 5106 9314 -466 -1560 6 C ATOM 1383 CD1 ILE A 228 11.760 19.496 -9.272 1.00 70.51 C ANISOU 1383 CD1 ILE A 228 11682 5415 9693 -625 -1896 -260 C ATOM 1384 N VAL A 229 12.533 20.210 -12.985 1.00 71.32 N ANISOU 1384 N VAL A 229 11393 5615 10089 -915 -1535 122 N ATOM 1385 CA VAL A 229 13.944 20.465 -13.272 1.00 72.84 C ANISOU 1385 CA VAL A 229 11401 5780 10495 -1047 -1573 137 C ATOM 1386 C VAL A 229 14.098 20.784 -14.758 1.00 73.28 C ANISOU 1386 C VAL A 229 11338 5883 10620 -1133 -1392 313 C ATOM 1387 O VAL A 229 13.141 20.699 -15.535 1.00 71.43 O ANISOU 1387 O VAL A 229 11171 5718 10249 -1089 -1260 410 O ATOM 1388 CB VAL A 229 14.874 19.295 -12.841 1.00 72.68 C ANISOU 1388 CB VAL A 229 11263 5872 10480 -1026 -1638 60 C ATOM 1389 CG1 VAL A 229 15.046 19.270 -11.329 1.00 72.98 C ANISOU 1389 CG1 VAL A 229 11396 5833 10499 -977 -1855 -103 C ATOM 1390 CG2 VAL A 229 14.360 17.952 -13.338 1.00 70.91 C ANISOU 1390 CG2 VAL A 229 11046 5828 10067 -926 -1506 89 C ATOM 1391 N ASP A 230 15.311 21.170 -15.140 1.00 75.54 N ANISOU 1391 N ASP A 230 11445 6132 11123 -1258 -1394 365 N ATOM 1392 CA ASP A 230 15.600 21.579 -16.509 1.00 76.82 C ANISOU 1392 CA ASP A 230 11492 6329 11368 -1344 -1216 546 C ATOM 1393 C ASP A 230 15.207 20.516 -17.527 1.00 75.54 C ANISOU 1393 C ASP A 230 11325 6370 11004 -1271 -1035 617 C ATOM 1394 O ASP A 230 15.603 19.355 -17.415 1.00 75.00 O ANISOU 1394 O ASP A 230 11212 6419 10863 -1211 -1029 547 O ATOM 1395 CB ASP A 230 17.083 21.926 -16.661 1.00 79.11 C ANISOU 1395 CB ASP A 230 11554 6568 11934 -1481 -1236 598 C ATOM 1396 CG ASP A 230 17.992 20.868 -16.068 0.00 78.93 C ANISOU 1396 CG ASP A 230 11397 6641 11951 -1457 -1307 509 C ATOM 1397 OD1 ASP A 230 17.751 20.451 -14.916 0.00 20.00 O ATOM 1398 OD2 ASP A 230 18.949 20.453 -16.755 0.00 20.00 O ATOM 1399 N THR A 231 14.428 20.924 -18.523 1.00 75.59 N ANISOU 1399 N THR A 231 11389 6409 10921 -1276 -896 755 N ATOM 1400 CA THR A 231 14.021 20.025 -19.604 1.00 75.08 C ANISOU 1400 CA THR A 231 11343 6528 10655 -1226 -733 828 C ATOM 1401 C THR A 231 15.147 19.109 -20.089 1.00 75.68 C ANISOU 1401 C THR A 231 11268 6724 10761 -1234 -632 828 C ATOM 1402 O THR A 231 14.884 17.969 -20.483 1.00 75.50 O ANISOU 1402 O THR A 231 11291 6840 10554 -1159 -555 796 O ATOM 1403 CB THR A 231 13.488 20.817 -20.813 1.00 75.70 C ANISOU 1403 CB THR A 231 11451 6617 10693 -1271 -598 1016 C ATOM 1404 OG1 THR A 231 12.691 21.908 -20.347 1.00 76.02 O ANISOU 1404 OG1 THR A 231 11592 6506 10784 -1274 -684 1039 O ATOM 1405 CG2 THR A 231 12.638 19.930 -21.720 1.00 74.78 C ANISOU 1405 CG2 THR A 231 11428 6676 10307 -1205 -491 1062 C ATOM 1406 N ALA A 232 16.382 19.611 -20.071 1.00 76.83 N ANISOU 1406 N ALA A 232 11234 6808 11150 -1324 -630 871 N ATOM 1407 CA ALA A 232 17.558 18.810 -20.407 1.00 77.76 C ANISOU 1407 CA ALA A 232 11177 7025 11342 -1321 -533 881 C ATOM 1408 C ALA A 232 17.670 17.553 -19.539 1.00 76.96 C ANISOU 1408 C ALA A 232 11093 6985 11163 -1219 -625 718 C ATOM 1409 O ALA A 232 17.914 16.462 -20.056 1.00 76.50 O ANISOU 1409 O ALA A 232 11011 7054 10999 -1148 -498 710 O ATOM 1410 CB ALA A 232 18.814 19.646 -20.272 1.00 79.85 C ANISOU 1410 CB ALA A 232 11225 7188 11924 -1442 -562 953 C ATOM 1411 N THR A 233 17.489 17.715 -18.228 1.00 76.62 N ANISOU 1411 N THR A 233 11103 6843 11165 -1207 -841 591 N ATOM 1412 CA THR A 233 17.533 16.592 -17.282 1.00 75.77 C ANISOU 1412 CA THR A 233 11024 6783 10979 -1106 -947 447 C ATOM 1413 C THR A 233 16.282 15.709 -17.355 1.00 73.49 C ANISOU 1413 C THR A 233 10931 6577 10415 -995 -907 394 C ATOM 1414 O THR A 233 16.370 14.481 -17.249 1.00 72.67 O ANISOU 1414 O THR A 233 10832 6562 10216 -908 -879 332 O ATOM 1415 CB THR A 233 17.693 17.086 -15.834 1.00 76.26 C ANISOU 1415 CB THR A 233 11109 6718 11148 -1123 -1196 331 C ATOM 1416 OG1 THR A 233 18.619 18.179 -15.806 1.00 78.58 O ANISOU 1416 OG1 THR A 233 11253 6898 11704 -1259 -1261 387 O ATOM 1417 CG2 THR A 233 18.199 15.960 -14.932 1.00 75.94 C ANISOU 1417 CG2 THR A 233 11025 6736 11092 -1037 -1300 220 C ATOM 1418 N VAL A 234 15.126 16.341 -17.527 1.00 72.26 N ANISOU 1418 N VAL A 234 10924 6381 10147 -999 -909 428 N ATOM 1419 CA VAL A 234 13.859 15.629 -17.697 1.00 70.47 C ANISOU 1419 CA VAL A 234 10862 6230 9681 -915 -874 410 C ATOM 1420 C VAL A 234 13.887 14.748 -18.961 1.00 70.90 C ANISOU 1420 C VAL A 234 10908 6422 9605 -901 -695 467 C ATOM 1421 O VAL A 234 13.431 13.604 -18.944 1.00 69.64 O ANISOU 1421 O VAL A 234 10827 6338 9293 -827 -680 405 O ATOM 1422 CB VAL A 234 12.673 16.625 -17.738 1.00 70.00 C ANISOU 1422 CB VAL A 234 10931 6101 9564 -927 -900 471 C ATOM 1423 CG1 VAL A 234 11.373 15.939 -18.131 1.00 68.95 C ANISOU 1423 CG1 VAL A 234 10930 6059 9206 -861 -854 493 C ATOM 1424 CG2 VAL A 234 12.509 17.311 -16.388 1.00 69.85 C ANISOU 1424 CG2 VAL A 234 10971 5941 9625 -906 -1070 382 C ATOM 1425 N LYS A 235 14.466 15.286 -20.029 1.00 72.83 N ANISOU 1425 N LYS A 235 11069 6694 9909 -972 -557 586 N ATOM 1426 CA LYS A 235 14.608 14.552 -21.279 1.00 73.75 C ANISOU 1426 CA LYS A 235 11198 6938 9882 -954 -374 635 C ATOM 1427 C LYS A 235 15.539 13.349 -21.136 1.00 75.14 C ANISOU 1427 C LYS A 235 11272 7171 10107 -896 -305 565 C ATOM 1428 O LYS A 235 15.343 12.328 -21.796 1.00 76.06 O ANISOU 1428 O LYS A 235 11443 7383 10074 -850 -166 560 O ATOM 1429 CB LYS A 235 15.115 15.478 -22.388 1.00 75.29 C ANISOU 1429 CB LYS A 235 11349 7154 10101 -1033 -226 801 C ATOM 1430 CG LYS A 235 14.034 16.341 -23.018 1.00 74.74 C ANISOU 1430 CG LYS A 235 11417 7082 9896 -1061 -241 893 C ATOM 1431 CD LYS A 235 14.413 16.757 -24.430 1.00 75.89 C ANISOU 1431 CD LYS A 235 11556 7295 9982 -1114 -68 1064 C ATOM 1432 CE LYS A 235 14.069 18.215 -24.688 1.00 77.05 C ANISOU 1432 CE LYS A 235 11602 7330 10342 -1204 -62 1200 C ATOM 1433 NZ LYS A 235 14.344 18.609 -26.097 0.00 20.00 N ATOM 1434 N VAL A 236 16.551 13.466 -20.279 1.00 76.25 N ANISOU 1434 N VAL A 236 11268 7248 10453 -897 -402 515 N ATOM 1435 CA VAL A 236 17.512 12.369 -20.101 1.00 77.47 C ANISOU 1435 CA VAL A 236 11316 7453 10665 -823 -352 456 C ATOM 1436 C VAL A 236 16.946 11.334 -19.134 1.00 76.33 C ANISOU 1436 C VAL A 236 11281 7307 10413 -727 -478 320 C ATOM 1437 O VAL A 236 17.043 10.128 -19.378 1.00 76.80 O ANISOU 1437 O VAL A 236 11373 7426 10380 -642 -392 269 O ATOM 1438 CB VAL A 236 18.933 12.836 -19.670 1.00 79.40 C ANISOU 1438 CB VAL A 236 11315 7652 11200 -870 -386 496 C ATOM 1439 CG1 VAL A 236 18.975 13.318 -18.228 1.00 79.01 C ANISOU 1439 CG1 VAL A 236 11242 7498 11278 -897 -643 415 C ATOM 1440 CG2 VAL A 236 19.943 11.706 -19.864 1.00 80.33 C ANISOU 1440 CG2 VAL A 236 11304 7844 11373 -781 -265 483 C ATOM 1441 N VAL A 237 16.335 11.800 -18.051 1.00 75.14 N ANISOU 1441 N VAL A 237 11198 7080 10271 -735 -668 266 N ATOM 1442 CA VAL A 237 15.683 10.892 -17.127 1.00 74.21 C ANISOU 1442 CA VAL A 237 11194 6961 10039 -642 -776 160 C ATOM 1443 C VAL A 237 14.688 10.038 -17.913 1.00 73.78 C ANISOU 1443 C VAL A 237 11293 6976 9762 -602 -670 157 C ATOM 1444 O VAL A 237 14.834 8.814 -17.987 1.00 74.19 O ANISOU 1444 O VAL A 237 11368 7070 9751 -528 -616 102 O ATOM 1445 CB VAL A 237 14.967 11.657 -15.998 1.00 73.63 C ANISOU 1445 CB VAL A 237 11208 6801 9965 -649 -960 120 C ATOM 1446 CG1 VAL A 237 14.011 10.749 -15.228 1.00 72.34 C ANISOU 1446 CG1 VAL A 237 11189 6651 9644 -550 -1031 45 C ATOM 1447 CG2 VAL A 237 15.989 12.267 -15.053 1.00 74.96 C ANISOU 1447 CG2 VAL A 237 11251 6895 10336 -683 -1106 86 C ATOM 1448 N ILE A 238 13.701 10.701 -18.506 1.00 72.92 N ANISOU 1448 N ILE A 238 11286 6873 9546 -656 -644 222 N ATOM 1449 CA ILE A 238 12.663 10.034 -19.278 1.00 72.07 C ANISOU 1449 CA ILE A 238 11328 6828 9227 -640 -587 226 C ATOM 1450 C ILE A 238 13.212 8.968 -20.221 1.00 73.16 C ANISOU 1450 C ILE A 238 11474 7041 9280 -617 -425 210 C ATOM 1451 O ILE A 238 12.695 7.852 -20.265 1.00 72.49 O ANISOU 1451 O ILE A 238 11507 6984 9050 -577 -415 153 O ATOM 1452 CB ILE A 238 11.835 11.044 -20.096 1.00 71.88 C ANISOU 1452 CB ILE A 238 11382 6809 9120 -709 -584 329 C ATOM 1453 CG1 ILE A 238 11.174 12.067 -19.169 1.00 70.88 C ANISOU 1453 CG1 ILE A 238 11294 6600 9035 -697 -731 329 C ATOM 1454 CG2 ILE A 238 10.790 10.323 -20.933 1.00 71.47 C ANISOU 1454 CG2 ILE A 238 11466 6834 8853 -711 -537 344 C ATOM 1455 CD1 ILE A 238 10.056 12.849 -19.821 0.00 20.00 C ATOM 1456 N GLN A 239 14.251 9.306 -20.981 1.00 74.60 N ANISOU 1456 N GLN A 239 11539 7249 9556 -639 -293 261 N ATOM 1457 CA GLN A 239 14.771 8.358 -21.973 1.00 75.85 C ANISOU 1457 CA GLN A 239 11721 7474 9624 -594 -114 241 C ATOM 1458 C GLN A 239 15.452 7.157 -21.299 1.00 75.37 C ANISOU 1458 C GLN A 239 11611 7393 9632 -490 -114 139 C ATOM 1459 O GLN A 239 15.333 6.032 -21.784 1.00 74.68 O ANISOU 1459 O GLN A 239 11629 7328 9417 -430 -26 73 O ATOM 1460 CB GLN A 239 15.658 9.040 -23.032 1.00 78.18 C ANISOU 1460 CB GLN A 239 11914 7814 9974 -635 65 351 C ATOM 1461 CG GLN A 239 17.126 9.246 -22.687 1.00 80.30 C ANISOU 1461 CG GLN A 239 11952 8062 10495 -617 120 383 C ATOM 1462 CD GLN A 239 17.830 10.176 -23.678 1.00 83.48 C ANISOU 1462 CD GLN A 239 12243 8499 10974 -680 287 530 C ATOM 1463 OE1 GLN A 239 17.183 10.976 -24.370 1.00 83.35 O ANISOU 1463 OE1 GLN A 239 12310 8501 10856 -753 311 618 O ATOM 1464 NE2 GLN A 239 19.162 10.082 -23.744 1.00 85.77 N ANISOU 1464 NE2 GLN A 239 12331 8800 11456 -650 405 576 N ATOM 1465 N VAL A 240 16.119 7.377 -20.168 1.00 75.19 N ANISOU 1465 N VAL A 240 11443 7319 9806 -469 -226 124 N ATOM 1466 CA VAL A 240 16.687 6.254 -19.414 1.00 75.55 C ANISOU 1466 CA VAL A 240 11440 7345 9919 -364 -253 43 C ATOM 1467 C VAL A 240 15.556 5.320 -18.973 1.00 74.03 C ANISOU 1467 C VAL A 240 11430 7131 9565 -318 -338 -38 C ATOM 1468 O VAL A 240 15.592 4.115 -19.238 1.00 74.13 O ANISOU 1468 O VAL A 240 11514 7146 9507 -243 -258 -99 O ATOM 1469 CB VAL A 240 17.520 6.721 -18.195 1.00 75.63 C ANISOU 1469 CB VAL A 240 11272 7311 10153 -359 -402 48 C ATOM 1470 CG1 VAL A 240 17.912 5.542 -17.311 1.00 75.71 C ANISOU 1470 CG1 VAL A 240 11253 7303 10207 -243 -460 -23 C ATOM 1471 CG2 VAL A 240 18.772 7.443 -18.660 1.00 77.31 C ANISOU 1471 CG2 VAL A 240 11271 7539 10562 -406 -310 138 C ATOM 1472 N ASN A 241 14.552 5.895 -18.315 1.00 73.06 N ANISOU 1472 N ASN A 241 11382 6981 9395 -360 -489 -33 N ATOM 1473 CA ASN A 241 13.344 5.170 -17.904 1.00 72.02 C ANISOU 1473 CA ASN A 241 11406 6831 9123 -332 -569 -78 C ATOM 1474 C ASN A 241 12.708 4.378 -19.056 1.00 72.30 C ANISOU 1474 C ASN A 241 11588 6900 8982 -348 -460 -97 C ATOM 1475 O ASN A 241 12.219 3.266 -18.857 1.00 71.81 O ANISOU 1475 O ASN A 241 11624 6813 8847 -303 -479 -156 O ATOM 1476 CB ASN A 241 12.335 6.163 -17.316 1.00 71.28 C ANISOU 1476 CB ASN A 241 11363 6716 9004 -382 -700 -35 C ATOM 1477 CG ASN A 241 10.989 5.534 -17.006 1.00 70.93 C ANISOU 1477 CG ASN A 241 11460 6664 8826 -363 -764 -47 C ATOM 1478 OD1 ASN A 241 9.946 6.030 -17.439 1.00 70.31 O ANISOU 1478 OD1 ASN A 241 11457 6602 8654 -422 -779 10 O ATOM 1479 ND2 ASN A 241 11.003 4.448 -16.244 1.00 71.40 N ANISOU 1479 ND2 ASN A 241 11542 6695 8889 -282 -803 -104 N ATOM 1480 N THR A 242 12.725 4.962 -20.254 1.00 72.89 N ANISOU 1480 N THR A 242 11682 7026 8984 -416 -354 -43 N ATOM 1481 CA THR A 242 12.195 4.319 -21.449 1.00 72.73 C ANISOU 1481 CA THR A 242 11816 7045 8772 -441 -260 -65 C ATOM 1482 C THR A 242 13.093 3.186 -21.919 1.00 74.97 C ANISOU 1482 C THR A 242 12115 7322 9047 -358 -112 -145 C ATOM 1483 O THR A 242 12.592 2.135 -22.302 1.00 76.45 O ANISOU 1483 O THR A 242 12455 7489 9102 -341 -93 -222 O ATOM 1484 CB THR A 242 11.990 5.334 -22.594 1.00 72.88 C ANISOU 1484 CB THR A 242 11859 7130 8699 -530 -190 29 C ATOM 1485 OG1 THR A 242 10.907 6.206 -22.260 1.00 71.52 O ANISOU 1485 OG1 THR A 242 11711 6956 8508 -596 -325 102 O ATOM 1486 CG2 THR A 242 11.665 4.637 -23.913 1.00 73.90 C ANISOU 1486 CG2 THR A 242 12157 7310 8609 -548 -84 -3 C ATOM 1487 N PHE A 243 14.408 3.396 -21.904 1.00 76.17 N ANISOU 1487 N PHE A 243 12108 7482 9349 -306 -4 -125 N ATOM 1488 CA PHE A 243 15.350 2.355 -22.318 1.00 77.55 C ANISOU 1488 CA PHE A 243 12277 7647 9541 -203 161 -187 C ATOM 1489 C PHE A 243 15.362 1.200 -21.313 1.00 77.30 C ANISOU 1489 C PHE A 243 12256 7539 9576 -109 83 -271 C ATOM 1490 O PHE A 243 15.289 0.023 -21.687 1.00 77.32 O ANISOU 1490 O PHE A 243 12387 7500 9491 -45 162 -356 O ATOM 1491 CB PHE A 243 16.764 2.930 -22.464 1.00 79.29 C ANISOU 1491 CB PHE A 243 12282 7899 9945 -169 291 -112 C ATOM 1492 CG PHE A 243 17.799 1.904 -22.840 1.00 81.89 C ANISOU 1492 CG PHE A 243 12575 8218 10319 -39 484 -156 C ATOM 1493 CD1 PHE A 243 18.490 1.189 -21.858 1.00 82.26 C ANISOU 1493 CD1 PHE A 243 12499 8213 10543 65 442 -188 C ATOM 1494 CD2 PHE A 243 18.076 1.637 -24.176 1.00 84.06 C ANISOU 1494 CD2 PHE A 243 12948 8536 10452 -8 713 -162 C ATOM 1495 CE1 PHE A 243 19.437 0.237 -22.207 1.00 84.12 C ANISOU 1495 CE1 PHE A 243 12694 8431 10834 202 631 -217 C ATOM 1496 CE2 PHE A 243 19.021 0.681 -24.527 1.00 86.27 C ANISOU 1496 CE2 PHE A 243 13208 8798 10773 131 914 -204 C ATOM 1497 CZ PHE A 243 19.702 -0.020 -23.542 1.00 85.96 C ANISOU 1497 CZ PHE A 243 13030 8698 10933 239 877 -229 C ATOM 1498 N MET A 244 15.443 1.547 -20.035 1.00 76.25 N ANISOU 1498 N MET A 244 12001 7379 9590 -99 -75 -246 N ATOM 1499 CA MET A 244 15.673 0.552 -19.001 1.00 76.39 C ANISOU 1499 CA MET A 244 11993 7334 9695 3 -143 -297 C ATOM 1500 C MET A 244 14.416 -0.224 -18.598 1.00 74.72 C ANISOU 1500 C MET A 244 11958 7070 9360 -3 -249 -348 C ATOM 1501 O MET A 244 14.521 -1.246 -17.915 1.00 76.07 O ANISOU 1501 O MET A 244 12144 7179 9580 86 -277 -388 O ATOM 1502 CB MET A 244 16.303 1.210 -17.771 1.00 76.75 C ANISOU 1502 CB MET A 244 11852 7379 9930 20 -281 -249 C ATOM 1503 CG MET A 244 17.255 0.294 -17.021 1.00 78.41 C ANISOU 1503 CG MET A 244 11951 7554 10285 150 -281 -268 C ATOM 1504 SD MET A 244 18.603 -0.314 -18.057 1.00 80.92 S ANISOU 1504 SD MET A 244 12165 7887 10692 244 -24 -262 S ATOM 1505 CE MET A 244 19.042 -1.817 -17.178 1.00 81.53 C ANISOU 1505 CE MET A 244 12226 7889 10862 412 -41 -304 C ATOM 1506 N SER A 245 13.237 0.242 -19.008 1.00 72.36 N ANISOU 1506 N SER A 245 11780 6794 8918 -107 -308 -329 N ATOM 1507 CA SER A 245 12.000 -0.486 -18.722 1.00 70.07 C ANISOU 1507 CA SER A 245 11638 6456 8526 -129 -403 -357 C ATOM 1508 C SER A 245 11.123 -0.762 -19.952 1.00 69.75 C ANISOU 1508 C SER A 245 11774 6429 8297 -218 -362 -384 C ATOM 1509 O SER A 245 9.981 -1.196 -19.801 1.00 68.93 O ANISOU 1509 O SER A 245 11776 6294 8117 -267 -460 -386 O ATOM 1510 CB SER A 245 11.186 0.243 -17.648 1.00 68.24 C ANISOU 1510 CB SER A 245 11373 6231 8323 -160 -569 -292 C ATOM 1511 OG SER A 245 10.316 1.200 -18.212 1.00 67.56 O ANISOU 1511 OG SER A 245 11330 6194 8143 -266 -602 -232 O ATOM 1512 N PHE A 246 11.634 -0.530 -21.159 1.00 69.87 N ANISOU 1512 N PHE A 246 11820 6492 8233 -239 -222 -398 N ATOM 1513 CA PHE A 246 10.891 -0.934 -22.352 1.00 70.32 C ANISOU 1513 CA PHE A 246 12072 6560 8085 -314 -191 -441 C ATOM 1514 C PHE A 246 11.827 -1.561 -23.378 1.00 72.31 C ANISOU 1514 C PHE A 246 12410 6812 8253 -259 7 -521 C ATOM 1515 O PHE A 246 11.635 -2.710 -23.733 1.00 73.51 O ANISOU 1515 O PHE A 246 12744 6906 8280 -260 32 -621 O ATOM 1516 CB PHE A 246 10.023 0.201 -22.896 1.00 70.01 C ANISOU 1516 CB PHE A 246 12053 6605 7939 -437 -263 -348 C ATOM 1517 CG PHE A 246 9.176 -0.204 -24.071 1.00 71.30 C ANISOU 1517 CG PHE A 246 12417 6790 7881 -526 -272 -383 C ATOM 1518 CD1 PHE A 246 7.967 -0.868 -23.879 1.00 71.11 C ANISOU 1518 CD1 PHE A 246 12502 6721 7796 -592 -420 -403 C ATOM 1519 CD2 PHE A 246 9.593 0.056 -25.373 1.00 72.83 C ANISOU 1519 CD2 PHE A 246 12695 7051 7924 -545 -138 -391 C ATOM 1520 CE1 PHE A 246 7.188 -1.257 -24.963 1.00 71.81 C ANISOU 1520 CE1 PHE A 246 12775 6826 7683 -690 -460 -439 C ATOM 1521 CE2 PHE A 246 8.815 -0.326 -26.457 1.00 73.93 C ANISOU 1521 CE2 PHE A 246 13040 7214 7832 -629 -168 -432 C ATOM 1522 CZ PHE A 246 7.613 -0.982 -26.251 1.00 73.47 C ANISOU 1522 CZ PHE A 246 13086 7106 7721 -709 -343 -461 C ATOM 1523 N LEU A 247 12.808 -0.802 -23.854 1.00 73.19 N ANISOU 1523 N LEU A 247 12396 6981 8429 -213 153 -476 N ATOM 1524 CA LEU A 247 13.721 -1.291 -24.882 1.00 75.09 C ANISOU 1524 CA LEU A 247 12717 7233 8579 -144 377 -535 C ATOM 1525 C LEU A 247 14.532 -2.520 -24.485 1.00 76.07 C ANISOU 1525 C LEU A 247 12815 7264 8821 5 485 -620 C ATOM 1526 O LEU A 247 14.483 -3.551 -25.155 1.00 78.10 O ANISOU 1526 O LEU A 247 13253 7465 8956 60 602 -729 O ATOM 1527 CB LEU A 247 14.648 -0.156 -25.323 1.00 75.68 C ANISOU 1527 CB LEU A 247 12662 7410 8682 -150 519 -429 C ATOM 1528 CG LEU A 247 14.432 0.384 -26.738 1.00 76.19 C ANISOU 1528 CG LEU A 247 12882 7561 8505 -247 562 -394 C ATOM 1529 CD1 LEU A 247 13.066 1.043 -26.859 0.00 20.00 C ATOM 1530 CD2 LEU A 247 15.537 1.358 -27.117 0.00 20.00 C ATOM 1531 N PHE A 248 15.279 -2.399 -23.394 1.00 75.34 N ANISOU 1531 N PHE A 248 12510 7152 8963 76 442 -571 N ATOM 1532 CA PHE A 248 16.136 -3.488 -22.916 1.00 76.81 C ANISOU 1532 CA PHE A 248 12646 7252 9285 229 531 -626 C ATOM 1533 C PHE A 248 15.352 -4.802 -22.788 1.00 77.12 C ANISOU 1533 C PHE A 248 12896 7169 9236 246 472 -741 C ATOM 1534 O PHE A 248 15.684 -5.787 -23.456 1.00 77.61 O ANISOU 1534 O PHE A 248 13099 7157 9230 331 626 -841 O ATOM 1535 CB PHE A 248 16.826 -3.096 -21.598 1.00 76.54 C ANISOU 1535 CB PHE A 248 12352 7225 9503 280 431 -542 C ATOM 1536 CG PHE A 248 17.499 -4.240 -20.878 1.00 77.67 C ANISOU 1536 CG PHE A 248 12440 7277 9792 433 463 -578 C ATOM 1537 CD1 PHE A 248 18.561 -4.923 -21.458 1.00 80.11 C ANISOU 1537 CD1 PHE A 248 12721 7557 10158 572 689 -605 C ATOM 1538 CD2 PHE A 248 17.091 -4.610 -19.597 1.00 76.87 C ANISOU 1538 CD2 PHE A 248 12309 7121 9776 449 276 -569 C ATOM 1539 CE1 PHE A 248 19.185 -5.968 -20.789 1.00 81.10 C ANISOU 1539 CE1 PHE A 248 12785 7593 10433 724 720 -623 C ATOM 1540 CE2 PHE A 248 17.711 -5.655 -18.923 1.00 77.73 C ANISOU 1540 CE2 PHE A 248 12364 7146 10021 595 300 -584 C ATOM 1541 CZ PHE A 248 18.758 -6.335 -19.521 1.00 79.83 C ANISOU 1541 CZ PHE A 248 12596 7378 10355 732 518 -609 C ATOM 1542 N PRO A 249 14.287 -4.812 -21.963 1.00 75.92 N ANISOU 1542 N PRO A 249 12774 6988 9084 165 257 -725 N ATOM 1543 CA PRO A 249 13.523 -6.045 -21.796 1.00 76.57 C ANISOU 1543 CA PRO A 249 13036 6944 9111 167 193 -814 C ATOM 1544 C PRO A 249 12.829 -6.491 -23.080 1.00 78.90 C ANISOU 1544 C PRO A 249 13592 7212 9175 84 236 -915 C ATOM 1545 O PRO A 249 12.633 -7.692 -23.285 1.00 80.33 O ANISOU 1545 O PRO A 249 13944 7263 9313 117 263 -1025 O ATOM 1546 CB PRO A 249 12.490 -5.673 -20.735 1.00 74.01 C ANISOU 1546 CB PRO A 249 12662 6629 8829 82 -30 -738 C ATOM 1547 CG PRO A 249 12.312 -4.214 -20.895 1.00 72.90 C ANISOU 1547 CG PRO A 249 12423 6618 8657 -9 -79 -647 C ATOM 1548 CD PRO A 249 13.679 -3.700 -21.214 1.00 73.87 C ANISOU 1548 CD PRO A 249 12400 6800 8867 69 77 -623 C ATOM 1549 N MET A 250 12.471 -5.535 -23.935 1.00 79.85 N ANISOU 1549 N MET A 250 13748 7445 9144 -21 236 -879 N ATOM 1550 CA MET A 250 11.871 -5.849 -25.226 1.00 82.41 C ANISOU 1550 CA MET A 250 14325 7767 9221 -103 265 -969 C ATOM 1551 C MET A 250 12.728 -6.831 -25.995 1.00 83.89 C ANISOU 1551 C MET A 250 14659 7872 9343 21 483 -1102 C ATOM 1552 O MET A 250 12.230 -7.843 -26.461 1.00 85.10 O ANISOU 1552 O MET A 250 15048 7913 9372 0 467 -1232 O ATOM 1553 CB MET A 250 11.702 -4.595 -26.075 1.00 84.77 C ANISOU 1553 CB MET A 250 14610 8216 9379 -196 280 -887 C ATOM 1554 CG MET A 250 10.968 -4.816 -27.385 1.00 88.12 C ANISOU 1554 CG MET A 250 15300 8660 9519 -296 270 -964 C ATOM 1555 SD MET A 250 9.215 -5.033 -27.043 1.00 90.49 S ANISOU 1555 SD MET A 250 15693 8923 9764 -474 -31 -950 S ATOM 1556 CE MET A 250 9.049 -6.815 -26.932 1.00 91.25 C ANISOU 1556 CE MET A 250 15994 8815 9861 -439 -44 -1129 C ATOM 1557 N LEU A 251 14.012 -6.521 -26.132 1.00 67.37 N ANISOU 1557 N LEU A 251 9530 6951 9114 -170 -265 235 N ATOM 1558 CA LEU A 251 14.935 -7.411 -26.823 1.00 68.01 C ANISOU 1558 CA LEU A 251 9450 7058 9330 -179 -228 150 C ATOM 1559 C LEU A 251 15.028 -8.757 -26.133 1.00 66.56 C ANISOU 1559 C LEU A 251 9352 6851 9087 -108 -411 51 C ATOM 1560 O LEU A 251 14.826 -9.789 -26.764 1.00 67.55 O ANISOU 1560 O LEU A 251 9466 7081 9118 -104 -340 51 O ATOM 1561 CB LEU A 251 16.336 -6.809 -26.897 1.00 70.78 C ANISOU 1561 CB LEU A 251 9582 7281 10028 -213 -237 47 C ATOM 1562 CG LEU A 251 16.540 -5.528 -27.709 1.00 72.33 C ANISOU 1562 CG LEU A 251 9672 7467 10344 -296 -12 127 C ATOM 1563 CD1 LEU A 251 17.999 -5.465 -28.155 0.00 74.62 C ANISOU 1563 CD1 LEU A 251 9700 7647 11003 -345 65 -4 C ATOM 1564 CD2 LEU A 251 15.593 -5.426 -28.907 0.00 71.62 C ANISOU 1564 CD2 LEU A 251 9672 7534 10005 -329 232 287 C ATOM 1565 N VAL A 252 15.336 -8.741 -24.842 1.00 65.43 N ANISOU 1565 N VAL A 252 9315 6555 8987 -43 -653 -34 N ATOM 1566 CA VAL A 252 15.484 -9.972 -24.071 1.00 65.31 C ANISOU 1566 CA VAL A 252 9436 6475 8902 40 -851 -131 C ATOM 1567 C VAL A 252 14.295 -10.911 -24.327 1.00 63.53 C ANISOU 1567 C VAL A 252 9366 6378 8393 41 -733 -46 C ATOM 1568 O VAL A 252 14.444 -12.017 -24.835 1.00 62.05 O ANISOU 1568 O VAL A 252 9128 6258 8187 50 -709 -84 O ATOM 1569 CB VAL A 252 15.594 -9.678 -22.559 1.00 65.61 C ANISOU 1569 CB VAL A 252 9690 6321 8917 127 -1115 -196 C ATOM 1570 CG1 VAL A 252 15.561 -10.971 -21.748 1.00 65.71 C ANISOU 1570 CG1 VAL A 252 9932 6250 8783 224 -1299 -272 C ATOM 1571 CG2 VAL A 252 16.862 -8.899 -22.267 1.00 67.47 C ANISOU 1571 CG2 VAL A 252 9747 6406 9479 144 -1281 -324 C ATOM 1572 N ILE A 253 13.117 -10.425 -23.976 1.00 62.91 N ANISOU 1572 N ILE A 253 9458 6321 8123 30 -657 55 N ATOM 1573 CA ILE A 253 11.864 -11.109 -24.218 1.00 61.96 C ANISOU 1573 CA ILE A 253 9456 6302 7784 22 -523 123 C ATOM 1574 C ILE A 253 11.751 -11.540 -25.690 1.00 60.20 C ANISOU 1574 C ILE A 253 9046 6256 7568 -22 -352 158 C ATOM 1575 O ILE A 253 11.748 -12.729 -26.001 1.00 61.11 O ANISOU 1575 O ILE A 253 9155 6424 7639 -3 -347 116 O ATOM 1576 CB ILE A 253 10.708 -10.158 -23.824 1.00 63.35 C ANISOU 1576 CB ILE A 253 9759 6468 7840 0 -436 215 C ATOM 1577 CG1 ILE A 253 10.608 -10.040 -22.300 1.00 64.92 C ANISOU 1577 CG1 ILE A 253 10221 6483 7962 56 -579 178 C ATOM 1578 CG2 ILE A 253 9.365 -10.598 -24.373 1.00 63.43 C ANISOU 1578 CG2 ILE A 253 9803 6593 7703 -24 -264 274 C ATOM 1579 CD1 ILE A 253 10.026 -8.710 -21.853 1.00 66.10 C ANISOU 1579 CD1 ILE A 253 10436 6587 8092 34 -541 243 C ATOM 1580 N SER A 254 11.690 -10.575 -26.595 1.00 58.33 N ANISOU 1580 N SER A 254 8683 6097 7380 -72 -218 232 N ATOM 1581 CA SER A 254 11.350 -10.860 -27.982 1.00 57.09 C ANISOU 1581 CA SER A 254 8428 6094 7169 -97 -52 281 C ATOM 1582 C SER A 254 12.319 -11.825 -28.659 1.00 57.02 C ANISOU 1582 C SER A 254 8283 6125 7255 -95 -40 205 C ATOM 1583 O SER A 254 11.909 -12.594 -29.516 1.00 56.72 O ANISOU 1583 O SER A 254 8227 6201 7122 -88 46 214 O ATOM 1584 CB SER A 254 11.222 -9.564 -28.801 1.00 57.29 C ANISOU 1584 CB SER A 254 8394 6158 7215 -138 82 376 C ATOM 1585 OG SER A 254 12.475 -8.938 -28.984 1.00 58.35 O ANISOU 1585 OG SER A 254 8393 6223 7552 -174 103 349 O ATOM 1586 N ILE A 255 13.592 -11.790 -28.285 1.00 57.37 N ANISOU 1586 N ILE A 255 8224 6067 7505 -95 -136 114 N ATOM 1587 CA ILE A 255 14.563 -12.703 -28.868 1.00 57.79 C ANISOU 1587 CA ILE A 255 8129 6139 7689 -94 -127 18 C ATOM 1588 C ILE A 255 14.463 -14.068 -28.196 1.00 57.56 C ANISOU 1588 C ILE A 255 8196 6088 7586 -32 -286 -61 C ATOM 1589 O ILE A 255 14.271 -15.079 -28.868 1.00 57.16 O ANISOU 1589 O ILE A 255 8119 6136 7462 -24 -222 -74 O ATOM 1590 CB ILE A 255 16.004 -12.160 -28.768 1.00 59.49 C ANISOU 1590 CB ILE A 255 8156 6229 8215 -118 -167 -81 C ATOM 1591 CG1 ILE A 255 16.174 -10.937 -29.684 1.00 60.10 C ANISOU 1591 CG1 ILE A 255 8134 6326 8373 -193 59 0 C ATOM 1592 CG2 ILE A 255 17.017 -13.238 -29.153 1.00 60.31 C ANISOU 1592 CG2 ILE A 255 8102 6324 8488 -106 -194 -217 C ATOM 1593 CD1 ILE A 255 17.355 -10.051 -29.336 1.00 61.59 C ANISOU 1593 CD1 ILE A 255 8156 6355 8888 -227 28 -88 C ATOM 1594 N LEU A 256 14.587 -14.095 -26.873 1.00 57.74 N ANISOU 1594 N LEU A 256 8356 5968 7615 19 -492 -115 N ATOM 1595 CA LEU A 256 14.657 -15.361 -26.146 1.00 58.11 C ANISOU 1595 CA LEU A 256 8535 5947 7597 89 -657 -199 C ATOM 1596 C LEU A 256 13.373 -16.181 -26.250 1.00 56.91 C ANISOU 1596 C LEU A 256 8538 5885 7200 92 -555 -131 C ATOM 1597 O LEU A 256 13.436 -17.402 -26.400 1.00 56.64 O ANISOU 1597 O LEU A 256 8516 5874 7130 120 -582 -186 O ATOM 1598 CB LEU A 256 15.013 -15.138 -24.676 1.00 59.04 C ANISOU 1598 CB LEU A 256 8836 5863 7734 162 -906 -266 C ATOM 1599 CG LEU A 256 16.386 -14.527 -24.386 1.00 60.74 C ANISOU 1599 CG LEU A 256 8892 5944 8242 185 -1081 -389 C ATOM 1600 CD1 LEU A 256 16.674 -14.581 -22.892 1.00 61.88 C ANISOU 1600 CD1 LEU A 256 9279 5870 8360 294 -1383 -476 C ATOM 1601 CD2 LEU A 256 17.483 -15.231 -25.160 1.00 61.66 C ANISOU 1601 CD2 LEU A 256 8752 6082 8592 179 -1090 -510 C ATOM 1602 N ASN A 257 12.217 -15.518 -26.189 1.00 55.73 N ANISOU 1602 N ASN A 257 8488 5775 6911 63 -438 -27 N ATOM 1603 CA ASN A 257 10.942 -16.224 -26.326 1.00 53.99 C ANISOU 1603 CA ASN A 257 8375 5621 6515 60 -326 12 C ATOM 1604 C ASN A 257 10.725 -16.783 -27.711 1.00 53.08 C ANISOU 1604 C ASN A 257 8096 5677 6395 38 -196 21 C ATOM 1605 O ASN A 257 10.001 -17.746 -27.858 1.00 52.79 O ANISOU 1605 O ASN A 257 8108 5681 6268 51 -150 5 O ATOM 1606 CB ASN A 257 9.763 -15.330 -25.979 1.00 53.65 C ANISOU 1606 CB ASN A 257 8441 5566 6376 34 -232 94 C ATOM 1607 CG ASN A 257 9.532 -15.219 -24.490 1.00 54.36 C ANISOU 1607 CG ASN A 257 8788 5475 6391 66 -318 81 C ATOM 1608 OD1 ASN A 257 10.446 -15.388 -23.675 1.00 54.86 O ANISOU 1608 OD1 ASN A 257 8948 5407 6489 116 -494 19 O ATOM 1609 ND2 ASN A 257 8.294 -14.929 -24.123 1.00 54.48 N ANISOU 1609 ND2 ASN A 257 8926 5465 6306 45 -198 126 N ATOM 1610 N THR A 258 11.318 -16.165 -28.728 1.00 52.94 N ANISOU 1610 N THR A 258 7902 5742 6469 9 -125 44 N ATOM 1611 CA THR A 258 11.256 -16.705 -30.077 1.00 52.39 C ANISOU 1611 CA THR A 258 7713 5817 6376 3 -9 46 C ATOM 1612 C THR A 258 12.183 -17.907 -30.212 1.00 52.81 C ANISOU 1612 C THR A 258 7686 5868 6512 25 -73 -55 C ATOM 1613 O THR A 258 11.885 -18.839 -30.951 1.00 52.72 O ANISOU 1613 O THR A 258 7639 5951 6438 39 -18 -77 O ATOM 1614 CB THR A 258 11.611 -15.644 -31.130 1.00 52.57 C ANISOU 1614 CB THR A 258 7628 5900 6446 -31 120 109 C ATOM 1615 OG1 THR A 258 10.678 -14.575 -31.037 1.00 52.20 O ANISOU 1615 OG1 THR A 258 7664 5853 6315 -41 162 200 O ATOM 1616 CG2 THR A 258 11.523 -16.216 -32.538 1.00 52.72 C ANISOU 1616 CG2 THR A 258 7582 6049 6400 -21 242 111 C ATOM 1617 N VAL A 259 13.309 -17.876 -29.506 1.00 53.36 N ANISOU 1617 N VAL A 259 7719 5818 6735 35 -205 -130 N ATOM 1618 CA VAL A 259 14.255 -18.979 -29.525 1.00 53.88 C ANISOU 1618 CA VAL A 259 7703 5854 6912 66 -301 -249 C ATOM 1619 C VAL A 259 13.712 -20.165 -28.736 1.00 53.07 C ANISOU 1619 C VAL A 259 7777 5703 6683 119 -414 -285 C ATOM 1620 O VAL A 259 13.881 -21.305 -29.138 1.00 52.65 O ANISOU 1620 O VAL A 259 7679 5695 6629 140 -422 -345 O ATOM 1621 CB VAL A 259 15.617 -18.547 -28.954 1.00 55.53 C ANISOU 1621 CB VAL A 259 7811 5920 7366 76 -446 -349 C ATOM 1622 CG1 VAL A 259 16.542 -19.745 -28.750 1.00 56.28 C ANISOU 1622 CG1 VAL A 259 7843 5950 7590 129 -604 -497 C ATOM 1623 CG2 VAL A 259 16.265 -17.523 -29.871 1.00 56.32 C ANISOU 1623 CG2 VAL A 259 7711 6054 7633 11 -282 -331 C ATOM 1624 N ILE A 260 13.069 -19.895 -27.608 1.00 52.84 N ANISOU 1624 N ILE A 260 7963 5566 6545 139 -485 -249 N ATOM 1625 CA ILE A 260 12.415 -20.951 -26.842 1.00 52.61 C ANISOU 1625 CA ILE A 260 8152 5464 6374 180 -533 -269 C ATOM 1626 C ILE A 260 11.306 -21.596 -27.661 1.00 51.83 C ANISOU 1626 C ILE A 260 8021 5500 6169 153 -360 -231 C ATOM 1627 O ILE A 260 11.314 -22.807 -27.866 1.00 52.26 O ANISOU 1627 O ILE A 260 8076 5573 6204 176 -371 -287 O ATOM 1628 CB ILE A 260 11.822 -20.427 -25.526 1.00 52.50 C ANISOU 1628 CB ILE A 260 8406 5293 6246 199 -581 -228 C ATOM 1629 CG1 ILE A 260 12.933 -20.087 -24.546 1.00 53.88 C ANISOU 1629 CG1 ILE A 260 8667 5293 6509 261 -819 -299 C ATOM 1630 CG2 ILE A 260 10.933 -21.468 -24.878 1.00 52.40 C ANISOU 1630 CG2 ILE A 260 8636 5199 6072 222 -539 -232 C ATOM 1631 CD1 ILE A 260 12.492 -19.123 -23.461 1.00 54.32 C ANISOU 1631 CD1 ILE A 260 8946 5215 6475 274 -854 -249 C ATOM 1632 N ALA A 261 10.367 -20.784 -28.132 1.00 51.25 N ANISOU 1632 N ALA A 261 7917 5512 6044 112 -218 -150 N ATOM 1633 CA ALA A 261 9.224 -21.270 -28.905 1.00 51.07 C ANISOU 1633 CA ALA A 261 7855 5599 5950 100 -83 -135 C ATOM 1634 C ALA A 261 9.607 -22.243 -30.016 1.00 51.36 C ANISOU 1634 C ALA A 261 7740 5757 6015 115 -67 -189 C ATOM 1635 O ALA A 261 9.035 -23.329 -30.117 1.00 51.13 O ANISOU 1635 O ALA A 261 7736 5742 5946 130 -42 -234 O ATOM 1636 CB ALA A 261 8.460 -20.104 -29.500 1.00 50.91 C ANISOU 1636 CB ALA A 261 7777 5656 5908 72 17 -59 C ATOM 1637 N ASN A 262 10.567 -21.828 -30.841 1.00 52.03 N ANISOU 1637 N ASN A 262 7672 5917 6178 108 -61 -189 N ATOM 1638 CA ASN A 262 11.099 -22.640 -31.937 1.00 52.19 C ANISOU 1638 CA ASN A 262 7553 6043 6231 121 -28 -243 C ATOM 1639 C ASN A 262 11.714 -23.941 -31.450 1.00 52.72 C ANISOU 1639 C ASN A 262 7632 6049 6348 152 -139 -340 C ATOM 1640 O ASN A 262 11.505 -24.993 -32.043 1.00 52.29 O ANISOU 1640 O ASN A 262 7535 6066 6266 172 -114 -388 O ATOM 1641 CB ASN A 262 12.179 -21.872 -32.703 1.00 52.95 C ANISOU 1641 CB ASN A 262 7508 6177 6432 97 29 -234 C ATOM 1642 CG ASN A 262 11.651 -20.625 -33.370 1.00 53.14 C ANISOU 1642 CG ASN A 262 7541 6259 6390 75 150 -133 C ATOM 1643 OD1 ASN A 262 10.448 -20.465 -33.538 1.00 53.10 O ANISOU 1643 OD1 ASN A 262 7612 6298 6265 90 180 -87 O ATOM 1644 ND2 ASN A 262 12.552 -19.723 -33.743 1.00 54.01 N ANISOU 1644 ND2 ASN A 262 7571 6350 6600 41 220 -111 N ATOM 1645 N LYS A 263 12.500 -23.861 -30.386 1.00 53.48 N ANISOU 1645 N LYS A 263 7794 6003 6521 167 -280 -378 N ATOM 1646 CA LYS A 263 13.180 -25.030 -29.881 1.00 54.69 C ANISOU 1646 CA LYS A 263 7981 6071 6725 213 -424 -480 C ATOM 1647 C LYS A 263 12.171 -25.983 -29.261 1.00 53.64 C ANISOU 1647 C LYS A 263 8047 5883 6451 235 -422 -476 C ATOM 1648 O LYS A 263 12.242 -27.195 -29.467 1.00 53.60 O ANISOU 1648 O LYS A 263 8033 5889 6442 261 -447 -540 O ATOM 1649 CB LYS A 263 14.255 -24.647 -28.869 1.00 56.70 C ANISOU 1649 CB LYS A 263 8281 6159 7101 247 -618 -539 C ATOM 1650 CG LYS A 263 14.937 -25.850 -28.231 1.00 58.87 C ANISOU 1650 CG LYS A 263 8636 6312 7420 318 -815 -655 C ATOM 1651 CD LYS A 263 16.376 -25.537 -27.842 1.00 61.50 C ANISOU 1651 CD LYS A 263 8865 6522 7978 359 -1018 -771 C ATOM 1652 CE LYS A 263 17.099 -26.743 -27.247 1.00 63.43 C ANISOU 1652 CE LYS A 263 9189 6630 8280 450 -1255 -906 C ATOM 1653 NZ LYS A 263 17.433 -27.811 -28.240 1.00 63.43 N ANISOU 1653 NZ LYS A 263 8999 6744 8358 443 -1194 -977 N ATOM 1654 N LEU A 264 11.228 -25.420 -28.515 1.00 52.57 N ANISOU 1654 N LEU A 264 8086 5675 6213 219 -372 -406 N ATOM 1655 CA LEU A 264 10.174 -26.195 -27.860 1.00 51.78 C ANISOU 1655 CA LEU A 264 8187 5487 5999 224 -311 -403 C ATOM 1656 C LEU A 264 9.245 -26.849 -28.891 1.00 50.26 C ANISOU 1656 C LEU A 264 7867 5433 5796 202 -166 -415 C ATOM 1657 O LEU A 264 8.770 -27.961 -28.690 1.00 50.11 O ANISOU 1657 O LEU A 264 7929 5362 5747 212 -133 -460 O ATOM 1658 CB LEU A 264 9.405 -25.287 -26.900 1.00 51.98 C ANISOU 1658 CB LEU A 264 8406 5397 5944 203 -254 -334 C ATOM 1659 CG LEU A 264 8.364 -25.855 -25.943 1.00 52.60 C ANISOU 1659 CG LEU A 264 8749 5319 5916 198 -152 -330 C ATOM 1660 CD1 LEU A 264 8.978 -26.863 -24.983 1.00 53.80 C ANISOU 1660 CD1 LEU A 264 9151 5288 6001 260 -281 -382 C ATOM 1661 CD2 LEU A 264 7.718 -24.707 -25.176 1.00 52.51 C ANISOU 1661 CD2 LEU A 264 8881 5216 5852 171 -77 -264 C ATOM 1662 N THR A 265 9.012 -26.159 -30.001 1.00 49.09 N ANISOU 1662 N THR A 265 7532 5443 5674 180 -89 -382 N ATOM 1663 CA THR A 265 8.263 -26.714 -31.121 1.00 48.53 C ANISOU 1663 CA THR A 265 7333 5506 5600 183 -1 -411 C ATOM 1664 C THR A 265 8.877 -28.006 -31.677 1.00 48.68 C ANISOU 1664 C THR A 265 7268 5577 5651 214 -49 -493 C ATOM 1665 O THR A 265 8.151 -28.933 -32.003 1.00 47.75 O ANISOU 1665 O THR A 265 7132 5483 5527 225 -3 -544 O ATOM 1666 CB THR A 265 8.153 -25.686 -32.259 1.00 48.06 C ANISOU 1666 CB THR A 265 7137 5587 5537 179 51 -362 C ATOM 1667 OG1 THR A 265 7.294 -24.630 -31.839 1.00 48.21 O ANISOU 1667 OG1 THR A 265 7224 5563 5531 156 101 -301 O ATOM 1668 CG2 THR A 265 7.586 -26.295 -33.522 1.00 48.01 C ANISOU 1668 CG2 THR A 265 7017 5710 5512 212 95 -410 C ATOM 1669 N VAL A 266 10.206 -28.029 -31.800 1.00 49.42 N ANISOU 1669 N VAL A 266 7293 5680 5804 228 -138 -518 N ATOM 1670 CA VAL A 266 10.942 -29.169 -32.336 1.00 49.92 C ANISOU 1670 CA VAL A 266 7258 5789 5920 258 -189 -604 C ATOM 1671 C VAL A 266 11.019 -30.308 -31.310 1.00 50.53 C ANISOU 1671 C VAL A 266 7488 5720 5990 286 -287 -662 C ATOM 1672 O VAL A 266 10.914 -31.468 -31.663 1.00 50.03 O ANISOU 1672 O VAL A 266 7393 5683 5931 307 -287 -726 O ATOM 1673 CB VAL A 266 12.364 -28.766 -32.796 1.00 50.57 C ANISOU 1673 CB VAL A 266 7193 5904 6117 258 -233 -635 C ATOM 1674 CG1 VAL A 266 13.148 -29.991 -33.258 1.00 51.31 C ANISOU 1674 CG1 VAL A 266 7181 6023 6288 289 -288 -742 C ATOM 1675 CG2 VAL A 266 12.299 -27.755 -33.933 1.00 50.53 C ANISOU 1675 CG2 VAL A 266 7074 6027 6097 232 -97 -575 C ATOM 1676 N MET A 267 11.193 -29.962 -30.045 1.00 51.85 N ANISOU 1676 N MET A 267 7848 5720 6132 294 -370 -638 N ATOM 1677 CA MET A 267 11.219 -30.941 -28.971 1.00 53.29 C ANISOU 1677 CA MET A 267 8258 5724 6265 333 -460 -679 C ATOM 1678 C MET A 267 9.946 -31.776 -28.895 1.00 53.01 C ANISOU 1678 C MET A 267 8324 5659 6156 313 -315 -678 C ATOM 1679 O MET A 267 10.007 -32.972 -28.650 1.00 54.10 O ANISOU 1679 O MET A 267 8553 5720 6281 342 -349 -735 O ATOM 1680 CB MET A 267 11.413 -30.237 -27.632 1.00 54.98 C ANISOU 1680 CB MET A 267 8718 5749 6421 353 -555 -642 C ATOM 1681 CG MET A 267 12.820 -29.717 -27.404 1.00 56.74 C ANISOU 1681 CG MET A 267 8876 5925 6755 396 -761 -690 C ATOM 1682 SD MET A 267 13.006 -28.932 -25.790 1.00 59.12 S ANISOU 1682 SD MET A 267 9501 5983 6976 445 -913 -662 S ATOM 1683 CE MET A 267 12.990 -30.359 -24.704 1.00 59.55 C ANISOU 1683 CE MET A 267 9923 5806 6896 532 -1037 -718 C ATOM 1684 N VAL A 268 8.823 -31.149 -29.153 1.00 52.04 N ANISOU 1684 N VAL A 268 8182 5581 6009 265 -154 -624 N ATOM 1685 CA VAL A 268 7.553 -31.801 -29.098 1.00 51.57 C ANISOU 1685 CA VAL A 268 8194 5463 5937 237 5 -643 C ATOM 1686 C VAL A 268 7.318 -32.596 -30.355 1.00 51.06 C ANISOU 1686 C VAL A 268 7910 5546 5941 246 35 -716 C ATOM 1687 O VAL A 268 6.801 -33.674 -30.301 1.00 51.24 O ANISOU 1687 O VAL A 268 7980 5505 5984 250 79 -777 O ATOM 1688 CB VAL A 268 6.456 -30.762 -28.889 1.00 51.46 C ANISOU 1688 CB VAL A 268 8187 5441 5923 188 149 -591 C ATOM 1689 CG1 VAL A 268 5.103 -31.393 -28.791 1.00 51.79 C ANISOU 1689 CG1 VAL A 268 8224 5427 6025 154 329 -646 C ATOM 1690 CG2 VAL A 268 6.715 -29.978 -27.632 1.00 51.90 C ANISOU 1690 CG2 VAL A 268 8498 5324 5897 181 138 -525 C ATOM 1691 N PRO A 297 -1.751 -37.027 -29.988 1.00 60.18 N ANISOU 1691 N PRO A 297 8777 5973 8112 -21 1292 -1369 N ATOM 1692 CA PRO A 297 -1.297 -35.658 -29.692 1.00 58.12 C ANISOU 1692 CA PRO A 297 8608 5778 7696 -15 1216 -1240 C ATOM 1693 C PRO A 297 -1.786 -35.068 -28.360 1.00 58.53 C ANISOU 1693 C PRO A 297 8897 5594 7745 -92 1453 -1196 C ATOM 1694 O PRO A 297 -1.262 -34.044 -27.921 1.00 58.40 O ANISOU 1694 O PRO A 297 9008 5603 7576 -87 1394 -1082 O ATOM 1695 CB PRO A 297 -1.865 -34.847 -30.859 1.00 57.61 C ANISOU 1695 CB PRO A 297 8237 5900 7751 29 1090 -1305 C ATOM 1696 CG PRO A 297 -3.072 -35.609 -31.288 1.00 59.07 C ANISOU 1696 CG PRO A 297 8215 6005 8224 18 1195 -1492 C ATOM 1697 CD PRO A 297 -2.735 -37.059 -31.084 1.00 59.42 C ANISOU 1697 CD PRO A 297 8333 5992 8249 14 1228 -1521 C ATOM 1698 N GLY A 298 -2.773 -35.702 -27.737 1.00 59.71 N ANISOU 1698 N GLY A 298 9109 5506 8072 -163 1736 -1292 N ATOM 1699 CA GLY A 298 -3.373 -35.217 -26.494 1.00 60.27 C ANISOU 1699 CA GLY A 298 9433 5323 8145 -242 2014 -1261 C ATOM 1700 C GLY A 298 -2.324 -35.079 -25.419 1.00 59.80 C ANISOU 1700 C GLY A 298 9789 5170 7761 -224 1974 -1098 C ATOM 1701 O GLY A 298 -2.273 -34.099 -24.702 1.00 59.96 O ANISOU 1701 O GLY A 298 9988 5125 7667 -238 2013 -1013 O ATOM 1702 N ARG A 299 -1.458 -36.072 -25.348 1.00 60.05 N ANISOU 1702 N ARG A 299 9969 5195 7651 -180 1865 -1067 N ATOM 1703 CA ARG A 299 -0.379 -36.120 -24.373 1.00 60.12 C ANISOU 1703 CA ARG A 299 10380 5097 7364 -135 1767 -941 C ATOM 1704 C ARG A 299 0.441 -34.833 -24.304 1.00 58.75 C ANISOU 1704 C ARG A 299 10225 5066 7029 -87 1534 -831 C ATOM 1705 O ARG A 299 0.887 -34.439 -23.239 1.00 58.37 O ANISOU 1705 O ARG A 299 10528 4862 6785 -68 1528 -745 O ATOM 1706 CB ARG A 299 0.540 -37.281 -24.735 1.00 59.92 C ANISOU 1706 CB ARG A 299 10369 5132 7264 -72 1578 -952 C ATOM 1707 CG ARG A 299 1.185 -37.976 -23.552 1.00 61.61 C ANISOU 1707 CG ARG A 299 11065 5093 7249 -36 1591 -889 C ATOM 1708 CD ARG A 299 1.204 -39.486 -23.790 1.00 62.05 C ANISOU 1708 CD ARG A 299 11133 5079 7364 -29 1630 -963 C ATOM 1709 NE ARG A 299 1.643 -39.766 -25.148 1.00 60.03 N ANISOU 1709 NE ARG A 299 10457 5124 7225 10 1396 -1023 N ATOM 1710 CZ ARG A 299 1.336 -40.853 -25.842 1.00 60.40 C ANISOU 1710 CZ ARG A 299 10312 5207 7428 1 1436 -1124 C ATOM 1711 NH1 ARG A 299 0.575 -41.822 -25.332 1.00 61.94 N ANISOU 1711 NH1 ARG A 299 10670 5153 7710 -54 1711 -1184 N ATOM 1712 NH2 ARG A 299 1.808 -40.966 -27.072 1.00 59.52 N ANISOU 1712 NH2 ARG A 299 9850 5374 7388 48 1209 -1171 N ATOM 1713 N VAL A 300 0.634 -34.191 -25.447 1.00 57.81 N ANISOU 1713 N VAL A 300 9745 5227 6992 -61 1345 -841 N ATOM 1714 CA VAL A 300 1.512 -33.038 -25.537 1.00 57.45 C ANISOU 1714 CA VAL A 300 9678 5328 6819 -17 1123 -745 C ATOM 1715 C VAL A 300 0.774 -31.736 -25.866 1.00 57.95 C ANISOU 1715 C VAL A 300 9558 5479 6982 -51 1177 -738 C ATOM 1716 O VAL A 300 1.399 -30.735 -26.217 1.00 56.96 O ANISOU 1716 O VAL A 300 9342 5508 6792 -19 1002 -670 O ATOM 1717 CB VAL A 300 2.628 -33.288 -26.572 1.00 55.98 C ANISOU 1717 CB VAL A 300 9279 5382 6608 50 848 -744 C ATOM 1718 CG1 VAL A 300 3.353 -34.579 -26.241 1.00 56.83 C ANISOU 1718 CG1 VAL A 300 9557 5395 6637 90 777 -766 C ATOM 1719 CG2 VAL A 300 2.083 -33.324 -27.988 1.00 55.04 C ANISOU 1719 CG2 VAL A 300 8782 5474 6654 51 830 -823 C ATOM 1720 N GLN A 301 -0.546 -31.736 -25.718 1.00 59.91 N ANISOU 1720 N GLN A 301 9753 5607 7403 -116 1426 -817 N ATOM 1721 CA GLN A 301 -1.348 -30.610 -26.167 1.00 60.94 C ANISOU 1721 CA GLN A 301 9664 5818 7670 -137 1456 -842 C ATOM 1722 C GLN A 301 -1.053 -29.347 -25.343 1.00 60.45 C ANISOU 1722 C GLN A 301 9796 5704 7465 -145 1444 -730 C ATOM 1723 O GLN A 301 -1.170 -28.233 -25.843 1.00 59.57 O ANISOU 1723 O GLN A 301 9515 5728 7390 -134 1352 -705 O ATOM 1724 CB GLN A 301 -2.843 -30.976 -26.146 1.00 63.44 C ANISOU 1724 CB GLN A 301 9858 5984 8262 -204 1727 -989 C ATOM 1725 CG GLN A 301 -3.709 -30.203 -27.143 1.00 64.75 C ANISOU 1725 CG GLN A 301 9671 6284 8646 -191 1669 -1082 C ATOM 1726 CD GLN A 301 -3.250 -30.339 -28.603 1.00 64.89 C ANISOU 1726 CD GLN A 301 9420 6571 8662 -104 1387 -1106 C ATOM 1727 OE1 GLN A 301 -2.852 -29.345 -29.231 1.00 64.71 O ANISOU 1727 OE1 GLN A 301 9307 6726 8554 -54 1196 -1039 O ATOM 1728 NE2 GLN A 301 -3.297 -31.566 -29.146 1.00 64.95 N ANISOU 1728 NE2 GLN A 301 9323 6598 8756 -86 1374 -1201 N ATOM 1729 N ALA A 302 -0.633 -29.527 -24.096 1.00 61.55 N ANISOU 1729 N ALA A 302 10312 5642 7432 -152 1519 -662 N ATOM 1730 CA ALA A 302 -0.318 -28.398 -23.225 1.00 61.60 C ANISOU 1730 CA ALA A 302 10539 5574 7291 -147 1495 -565 C ATOM 1731 C ALA A 302 0.961 -27.695 -23.654 1.00 60.45 C ANISOU 1731 C ALA A 302 10315 5627 7023 -79 1176 -478 C ATOM 1732 O ALA A 302 1.033 -26.464 -23.616 1.00 60.98 O ANISOU 1732 O ALA A 302 10340 5754 7074 -79 1115 -423 O ATOM 1733 CB ALA A 302 -0.205 -28.855 -21.781 1.00 63.13 C ANISOU 1733 CB ALA A 302 11206 5471 7309 -152 1643 -528 C ATOM 1734 N LEU A 303 1.966 -28.463 -24.072 1.00 59.62 N ANISOU 1734 N LEU A 303 10179 5614 6857 -25 987 -477 N ATOM 1735 CA LEU A 303 3.238 -27.870 -24.499 1.00 58.38 C ANISOU 1735 CA LEU A 303 9926 5622 6631 32 712 -419 C ATOM 1736 C LEU A 303 3.078 -27.065 -25.789 1.00 56.82 C ANISOU 1736 C LEU A 303 9371 5670 6547 25 652 -418 C ATOM 1737 O LEU A 303 3.805 -26.110 -26.020 1.00 56.19 O ANISOU 1737 O LEU A 303 9224 5691 6435 45 511 -358 O ATOM 1738 CB LEU A 303 4.334 -28.929 -24.653 1.00 58.42 C ANISOU 1738 CB LEU A 303 9965 5649 6581 91 538 -442 C ATOM 1739 CG LEU A 303 4.656 -29.741 -23.387 1.00 60.20 C ANISOU 1739 CG LEU A 303 10595 5616 6661 126 540 -441 C ATOM 1740 CD1 LEU A 303 5.546 -30.921 -23.726 1.00 61.12 C ANISOU 1740 CD1 LEU A 303 10690 5765 6768 184 377 -490 C ATOM 1741 CD2 LEU A 303 5.292 -28.926 -22.275 1.00 60.49 C ANISOU 1741 CD2 LEU A 303 10926 5505 6551 172 419 -381 C ATOM 1742 N ARG A 304 2.117 -27.433 -26.620 1.00 56.46 N ANISOU 1742 N ARG A 304 9113 5699 6639 2 756 -492 N ATOM 1743 CA ARG A 304 1.867 -26.672 -27.826 1.00 56.12 C ANISOU 1743 CA ARG A 304 8791 5856 6676 16 688 -497 C ATOM 1744 C ARG A 304 1.134 -25.365 -27.532 1.00 57.16 C ANISOU 1744 C ARG A 304 8921 5950 6845 -13 760 -464 C ATOM 1745 O ARG A 304 1.314 -24.387 -28.261 1.00 55.20 O ANISOU 1745 O ARG A 304 8535 5843 6595 8 659 -421 O ATOM 1746 CB ARG A 304 1.106 -27.508 -28.846 1.00 56.30 C ANISOU 1746 CB ARG A 304 8598 5958 6834 28 724 -608 C ATOM 1747 CG ARG A 304 1.880 -28.733 -29.312 1.00 56.14 C ANISOU 1747 CG ARG A 304 8545 6005 6779 63 635 -641 C ATOM 1748 CD ARG A 304 1.665 -29.019 -30.783 1.00 55.83 C ANISOU 1748 CD ARG A 304 8249 6149 6814 110 554 -711 C ATOM 1749 NE ARG A 304 2.320 -30.255 -31.221 1.00 56.67 N ANISOU 1749 NE ARG A 304 8319 6311 6901 141 488 -756 N ATOM 1750 CZ ARG A 304 3.606 -30.375 -31.582 1.00 56.04 C ANISOU 1750 CZ ARG A 304 8231 6335 6724 174 356 -711 C ATOM 1751 NH1 ARG A 304 4.443 -29.340 -31.539 1.00 54.81 N ANISOU 1751 NH1 ARG A 304 8100 6233 6491 178 280 -619 N ATOM 1752 NH2 ARG A 304 4.063 -31.560 -31.984 1.00 56.12 N ANISOU 1752 NH2 ARG A 304 8195 6384 6743 202 308 -771 N ATOM 1753 N HIS A 305 0.318 -25.343 -26.475 1.00 59.60 N ANISOU 1753 N HIS A 305 9400 6057 7187 -63 948 -486 N ATOM 1754 CA HIS A 305 -0.304 -24.091 -26.033 1.00 61.41 C ANISOU 1754 CA HIS A 305 9656 6228 7449 -93 1023 -456 C ATOM 1755 C HIS A 305 0.752 -23.173 -25.427 1.00 60.20 C ANISOU 1755 C HIS A 305 9666 6074 7132 -75 894 -336 C ATOM 1756 O HIS A 305 0.795 -21.979 -25.740 1.00 59.50 O ANISOU 1756 O HIS A 305 9482 6072 7050 -70 823 -285 O ATOM 1757 CB HIS A 305 -1.451 -24.322 -25.039 1.00 64.43 C ANISOU 1757 CB HIS A 305 10184 6370 7923 -158 1297 -523 C ATOM 1758 CG HIS A 305 -2.637 -25.033 -25.626 1.00 67.97 C ANISOU 1758 CG HIS A 305 10421 6794 8610 -183 1439 -671 C ATOM 1759 ND1 HIS A 305 -2.978 -24.955 -26.962 1.00 69.38 N ANISOU 1759 ND1 HIS A 305 10283 7154 8924 -140 1306 -742 N ATOM 1760 CD2 HIS A 305 -3.576 -25.822 -25.047 1.00 70.72 C ANISOU 1760 CD2 HIS A 305 10835 6933 9102 -243 1706 -775 C ATOM 1761 CE1 HIS A 305 -4.062 -25.679 -27.183 1.00 71.02 C ANISOU 1761 CE1 HIS A 305 10347 7272 9364 -164 1450 -896 C ATOM 1762 NE2 HIS A 305 -4.447 -26.214 -26.037 1.00 72.12 N ANISOU 1762 NE2 HIS A 305 10698 7173 9530 -236 1712 -920 N ATOM 1763 N GLY A 306 1.614 -23.741 -24.585 1.00 59.48 N ANISOU 1763 N GLY A 306 9821 5874 6903 -56 846 -302 N ATOM 1764 CA GLY A 306 2.771 -23.022 -24.051 1.00 58.17 C ANISOU 1764 CA GLY A 306 9792 5697 6611 -19 671 -219 C ATOM 1765 C GLY A 306 3.512 -22.224 -25.107 1.00 56.14 C ANISOU 1765 C GLY A 306 9281 5657 6392 2 499 -178 C ATOM 1766 O GLY A 306 3.813 -21.057 -24.900 1.00 56.74 O ANISOU 1766 O GLY A 306 9365 5741 6450 1 438 -118 O ATOM 1767 N VAL A 307 3.793 -22.856 -26.239 1.00 54.61 N ANISOU 1767 N VAL A 307 8877 5621 6248 21 440 -212 N ATOM 1768 CA VAL A 307 4.443 -22.204 -27.380 1.00 53.75 C ANISOU 1768 CA VAL A 307 8549 5705 6169 40 327 -178 C ATOM 1769 C VAL A 307 3.670 -20.972 -27.860 1.00 53.96 C ANISOU 1769 C VAL A 307 8468 5796 6238 23 376 -142 C ATOM 1770 O VAL A 307 4.277 -19.960 -28.223 1.00 53.52 O ANISOU 1770 O VAL A 307 8350 5813 6171 28 303 -77 O ATOM 1771 CB VAL A 307 4.609 -23.190 -28.574 1.00 53.18 C ANISOU 1771 CB VAL A 307 8296 5777 6132 66 300 -234 C ATOM 1772 CG1 VAL A 307 4.950 -22.466 -29.873 1.00 52.92 C ANISOU 1772 CG1 VAL A 307 8072 5922 6113 85 247 -201 C ATOM 1773 CG2 VAL A 307 5.680 -24.223 -28.271 1.00 53.32 C ANISOU 1773 CG2 VAL A 307 8382 5758 6118 91 206 -263 C ATOM 1774 N LEU A 308 2.341 -21.077 -27.892 1.00 54.62 N ANISOU 1774 N LEU A 308 8520 5839 6393 5 500 -197 N ATOM 1775 CA LEU A 308 1.483 -19.974 -28.321 1.00 54.97 C ANISOU 1775 CA LEU A 308 8463 5920 6500 1 527 -189 C ATOM 1776 C LEU A 308 1.464 -18.874 -27.269 1.00 55.26 C ANISOU 1776 C LEU A 308 8645 5843 6506 -29 559 -124 C ATOM 1777 O LEU A 308 1.578 -17.697 -27.600 1.00 55.46 O ANISOU 1777 O LEU A 308 8614 5928 6527 -23 503 -63 O ATOM 1778 CB LEU A 308 0.059 -20.459 -28.643 1.00 55.32 C ANISOU 1778 CB LEU A 308 8401 5930 6685 0 632 -305 C ATOM 1779 CG LEU A 308 -0.032 -21.394 -29.861 1.00 55.46 C ANISOU 1779 CG LEU A 308 8254 6073 6745 48 568 -382 C ATOM 1780 CD1 LEU A 308 -1.446 -21.919 -30.071 1.00 56.07 C ANISOU 1780 CD1 LEU A 308 8212 6082 7009 49 657 -529 C ATOM 1781 CD2 LEU A 308 0.479 -20.722 -31.129 1.00 55.31 C ANISOU 1781 CD2 LEU A 308 8128 6227 6657 108 425 -330 C ATOM 1782 N VAL A 309 1.350 -19.268 -26.008 1.00 55.91 N ANISOU 1782 N VAL A 309 8939 5750 6553 -58 651 -136 N ATOM 1783 CA VAL A 309 1.466 -18.340 -24.894 1.00 56.30 C ANISOU 1783 CA VAL A 309 9177 5669 6542 -76 670 -78 C ATOM 1784 C VAL A 309 2.746 -17.524 -24.978 1.00 56.03 C ANISOU 1784 C VAL A 309 9137 5706 6442 -50 490 6 C ATOM 1785 O VAL A 309 2.722 -16.333 -24.720 1.00 55.89 O ANISOU 1785 O VAL A 309 9135 5672 6427 -59 471 57 O ATOM 1786 CB VAL A 309 1.434 -19.087 -23.546 1.00 57.68 C ANISOU 1786 CB VAL A 309 9655 5628 6633 -88 772 -99 C ATOM 1787 CG1 VAL A 309 1.957 -18.213 -22.411 1.00 58.39 C ANISOU 1787 CG1 VAL A 309 9986 5586 6611 -77 718 -34 C ATOM 1788 CG2 VAL A 309 0.023 -19.569 -23.239 1.00 58.45 C ANISOU 1788 CG2 VAL A 309 9779 5596 6831 -137 1022 -184 C ATOM 1789 N LEU A 310 3.860 -18.164 -25.333 1.00 56.36 N ANISOU 1789 N LEU A 310 9144 5815 6453 -19 365 7 N ATOM 1790 CA LEU A 310 5.160 -17.475 -25.412 1.00 56.34 C ANISOU 1790 CA LEU A 310 9106 5855 6444 0 208 57 C ATOM 1791 C LEU A 310 5.200 -16.384 -26.478 1.00 56.59 C ANISOU 1791 C LEU A 310 8937 6031 6531 -10 199 110 C ATOM 1792 O LEU A 310 5.792 -15.323 -26.268 1.00 57.56 O ANISOU 1792 O LEU A 310 9060 6136 6671 -15 137 162 O ATOM 1793 CB LEU A 310 6.299 -18.460 -25.672 1.00 55.78 C ANISOU 1793 CB LEU A 310 9000 5817 6376 34 92 18 C ATOM 1794 CG LEU A 310 6.798 -19.250 -24.468 1.00 56.12 C ANISOU 1794 CG LEU A 310 9290 5684 6348 70 11 -21 C ATOM 1795 CD1 LEU A 310 7.669 -20.389 -24.951 1.00 56.51 C ANISOU 1795 CD1 LEU A 310 9260 5785 6425 104 -86 -79 C ATOM 1796 CD2 LEU A 310 7.577 -18.381 -23.501 1.00 56.51 C ANISOU 1796 CD2 LEU A 310 9484 5606 6380 99 -130 -1 C ATOM 1797 N ARG A 311 4.573 -16.633 -27.614 1.00 56.74 N ANISOU 1797 N ARG A 311 8805 6176 6576 -5 255 93 N ATOM 1798 CA ARG A 311 4.529 -15.625 -28.663 1.00 58.12 C ANISOU 1798 CA ARG A 311 8848 6464 6769 0 248 146 C ATOM 1799 C ARG A 311 3.523 -14.544 -28.277 1.00 57.38 C ANISOU 1799 C ARG A 311 8794 6312 6695 -14 296 172 C ATOM 1800 O ARG A 311 3.720 -13.377 -28.564 1.00 57.61 O ANISOU 1800 O ARG A 311 8794 6366 6727 -17 272 238 O ATOM 1801 CB ARG A 311 4.192 -16.263 -30.014 1.00 60.05 C ANISOU 1801 CB ARG A 311 8964 6842 7010 35 261 109 C ATOM 1802 CG ARG A 311 5.067 -17.480 -30.325 1.00 61.96 C ANISOU 1802 CG ARG A 311 9168 7131 7240 48 229 67 C ATOM 1803 CD ARG A 311 5.093 -17.882 -31.795 1.00 63.54 C ANISOU 1803 CD ARG A 311 9254 7472 7416 89 231 48 C ATOM 1804 NE ARG A 311 6.476 -18.147 -32.200 1.00 65.39 N ANISOU 1804 NE ARG A 311 9440 7753 7653 86 210 60 N ATOM 1805 CZ ARG A 311 6.989 -19.333 -32.525 1.00 66.60 C ANISOU 1805 CZ ARG A 311 9544 7947 7812 101 195 -1 C ATOM 1806 NH1 ARG A 311 6.246 -20.438 -32.538 1.00 67.38 N ANISOU 1806 NH1 ARG A 311 9641 8053 7903 123 195 -74 N ATOM 1807 NH2 ARG A 311 8.276 -19.409 -32.858 1.00 67.31 N ANISOU 1807 NH2 ARG A 311 9572 8060 7941 93 188 -1 N ATOM 1808 N ALA A 312 2.458 -14.945 -27.595 1.00 56.85 N ANISOU 1808 N ALA A 312 8794 6149 6656 -28 381 111 N ATOM 1809 CA ALA A 312 1.453 -14.016 -27.106 1.00 56.68 C ANISOU 1809 CA ALA A 312 8805 6047 6682 -47 446 111 C ATOM 1810 C ALA A 312 2.022 -13.022 -26.093 1.00 56.29 C ANISOU 1810 C ALA A 312 8891 5903 6592 -69 418 182 C ATOM 1811 O ALA A 312 1.629 -11.867 -26.059 1.00 56.42 O ANISOU 1811 O ALA A 312 8891 5906 6637 -77 421 218 O ATOM 1812 CB ALA A 312 0.302 -14.789 -26.475 1.00 57.12 C ANISOU 1812 CB ALA A 312 8912 5984 6805 -70 587 13 C ATOM 1813 N VAL A 313 2.941 -13.491 -25.263 1.00 56.19 N ANISOU 1813 N VAL A 313 9018 5814 6518 -69 371 189 N ATOM 1814 CA VAL A 313 3.487 -12.700 -24.168 1.00 55.98 C ANISOU 1814 CA VAL A 313 9152 5666 6452 -72 316 230 C ATOM 1815 C VAL A 313 4.220 -11.457 -24.680 1.00 56.12 C ANISOU 1815 C VAL A 313 9054 5758 6510 -72 221 302 C ATOM 1816 O VAL A 313 4.131 -10.378 -24.081 1.00 54.87 O ANISOU 1816 O VAL A 313 8961 5527 6358 -82 209 338 O ATOM 1817 CB VAL A 313 4.381 -13.594 -23.283 1.00 56.41 C ANISOU 1817 CB VAL A 313 9389 5611 6432 -44 235 201 C ATOM 1818 CG1 VAL A 313 5.575 -12.852 -22.700 1.00 57.01 C ANISOU 1818 CG1 VAL A 313 9532 5623 6507 -17 67 228 C ATOM 1819 CG2 VAL A 313 3.536 -14.220 -22.178 1.00 57.28 C ANISOU 1819 CG2 VAL A 313 9750 5545 6469 -51 366 158 C ATOM 1820 N VAL A 314 4.929 -11.614 -25.792 1.00 56.11 N ANISOU 1820 N VAL A 314 8890 5889 6539 -63 174 318 N ATOM 1821 CA VAL A 314 5.616 -10.497 -26.415 1.00 56.56 C ANISOU 1821 CA VAL A 314 8840 6003 6646 -72 134 384 C ATOM 1822 C VAL A 314 4.568 -9.533 -26.939 1.00 56.85 C ANISOU 1822 C VAL A 314 8835 6079 6684 -77 197 427 C ATOM 1823 O VAL A 314 4.556 -8.368 -26.565 1.00 58.13 O ANISOU 1823 O VAL A 314 9026 6188 6871 -91 184 474 O ATOM 1824 CB VAL A 314 6.519 -10.943 -27.577 1.00 56.72 C ANISOU 1824 CB VAL A 314 8717 6137 6693 -65 124 386 C ATOM 1825 CG1 VAL A 314 7.261 -9.750 -28.153 1.00 56.90 C ANISOU 1825 CG1 VAL A 314 8656 6181 6780 -85 130 453 C ATOM 1826 CG2 VAL A 314 7.492 -12.025 -27.119 1.00 56.79 C ANISOU 1826 CG2 VAL A 314 8745 6106 6725 -52 46 320 C ATOM 1827 N ILE A 315 3.670 -10.031 -27.781 1.00 56.92 N ANISOU 1827 N ILE A 315 8778 6168 6678 -56 247 396 N ATOM 1828 CA ILE A 315 2.585 -9.219 -28.328 1.00 57.04 C ANISOU 1828 CA ILE A 315 8754 6205 6711 -38 269 407 C ATOM 1829 C ILE A 315 1.891 -8.431 -27.228 1.00 56.90 C ANISOU 1829 C ILE A 315 8818 6067 6732 -63 299 403 C ATOM 1830 O ILE A 315 1.675 -7.232 -27.366 1.00 57.97 O ANISOU 1830 O ILE A 315 8944 6193 6888 -62 281 453 O ATOM 1831 CB ILE A 315 1.549 -10.082 -29.088 1.00 57.18 C ANISOU 1831 CB ILE A 315 8701 6280 6743 1 289 323 C ATOM 1832 CG1 ILE A 315 2.140 -10.523 -30.428 1.00 57.48 C ANISOU 1832 CG1 ILE A 315 8673 6444 6720 43 252 341 C ATOM 1833 CG2 ILE A 315 0.250 -9.312 -29.324 1.00 57.38 C ANISOU 1833 CG2 ILE A 315 8691 6276 6832 29 286 289 C ATOM 1834 CD1 ILE A 315 1.281 -11.514 -31.178 1.00 58.14 C ANISOU 1834 CD1 ILE A 315 8692 6582 6817 95 240 244 C ATOM 1835 N ALA A 316 1.548 -9.107 -26.137 1.00 56.77 N ANISOU 1835 N ALA A 316 8902 5946 6719 -85 358 343 N ATOM 1836 CA ALA A 316 0.909 -8.452 -24.996 1.00 56.75 C ANISOU 1836 CA ALA A 316 9015 5805 6740 -110 419 331 C ATOM 1837 C ALA A 316 1.757 -7.310 -24.454 1.00 56.72 C ANISOU 1837 C ALA A 316 9079 5757 6713 -119 342 411 C ATOM 1838 O ALA A 316 1.222 -6.274 -24.089 1.00 57.13 O ANISOU 1838 O ALA A 316 9155 5752 6799 -130 362 428 O ATOM 1839 CB ALA A 316 0.628 -9.456 -23.891 1.00 56.96 C ANISOU 1839 CB ALA A 316 9203 5700 6736 -129 518 264 C ATOM 1840 N PHE A 317 3.073 -7.505 -24.411 1.00 56.95 N ANISOU 1840 N PHE A 317 9123 5803 6711 -113 249 443 N ATOM 1841 CA PHE A 317 3.983 -6.523 -23.842 1.00 58.19 C ANISOU 1841 CA PHE A 317 9327 5896 6885 -118 158 491 C ATOM 1842 C PHE A 317 4.079 -5.259 -24.705 1.00 58.42 C ANISOU 1842 C PHE A 317 9228 5995 6971 -128 147 565 C ATOM 1843 O PHE A 317 3.940 -4.159 -24.189 1.00 58.83 O ANISOU 1843 O PHE A 317 9323 5978 7052 -138 132 597 O ATOM 1844 CB PHE A 317 5.374 -7.132 -23.625 1.00 59.17 C ANISOU 1844 CB PHE A 317 9465 6001 7015 -101 47 471 C ATOM 1845 CG PHE A 317 6.237 -6.337 -22.686 1.00 60.72 C ANISOU 1845 CG PHE A 317 9745 6074 7249 -90 -74 473 C ATOM 1846 CD1 PHE A 317 5.929 -6.271 -21.327 1.00 61.35 C ANISOU 1846 CD1 PHE A 317 10057 5996 7256 -67 -103 442 C ATOM 1847 CD2 PHE A 317 7.345 -5.630 -23.158 1.00 61.79 C ANISOU 1847 CD2 PHE A 317 9737 6233 7505 -100 -149 496 C ATOM 1848 CE1 PHE A 317 6.709 -5.517 -20.453 1.00 62.40 C ANISOU 1848 CE1 PHE A 317 10283 6003 7421 -39 -247 430 C ATOM 1849 CE2 PHE A 317 8.132 -4.880 -22.286 1.00 62.66 C ANISOU 1849 CE2 PHE A 317 9902 6215 7689 -84 -281 474 C ATOM 1850 CZ PHE A 317 7.816 -4.828 -20.931 1.00 62.82 C ANISOU 1850 CZ PHE A 317 10158 6085 7623 -46 -351 439 C ATOM 1851 N VAL A 318 4.288 -5.424 -26.010 1.00 58.21 N ANISOU 1851 N VAL A 318 9072 6093 6950 -121 163 593 N ATOM 1852 CA VAL A 318 4.402 -4.293 -26.932 1.00 58.22 C ANISOU 1852 CA VAL A 318 9001 6142 6976 -123 173 671 C ATOM 1853 C VAL A 318 3.112 -3.481 -26.923 1.00 58.50 C ANISOU 1853 C VAL A 318 9059 6155 7010 -109 193 680 C ATOM 1854 O VAL A 318 3.116 -2.295 -26.624 1.00 58.52 O ANISOU 1854 O VAL A 318 9084 6101 7048 -122 177 728 O ATOM 1855 CB VAL A 318 4.681 -4.751 -28.383 1.00 58.19 C ANISOU 1855 CB VAL A 318 8916 6257 6935 -102 209 693 C ATOM 1856 CG1 VAL A 318 4.672 -3.565 -29.343 1.00 58.63 C ANISOU 1856 CG1 VAL A 318 8964 6333 6979 -93 239 781 C ATOM 1857 CG2 VAL A 318 6.013 -5.473 -28.472 1.00 58.39 C ANISOU 1857 CG2 VAL A 318 8889 6298 6997 -121 204 675 C ATOM 1858 N VAL A 319 2.003 -4.135 -27.233 1.00 58.72 N ANISOU 1858 N VAL A 319 9070 6217 7024 -81 221 616 N ATOM 1859 CA VAL A 319 0.731 -3.440 -27.382 1.00 59.45 C ANISOU 1859 CA VAL A 319 9147 6281 7157 -56 224 592 C ATOM 1860 C VAL A 319 0.392 -2.634 -26.120 1.00 60.77 C ANISOU 1860 C VAL A 319 9387 6326 7375 -90 247 586 C ATOM 1861 O VAL A 319 -0.019 -1.473 -26.202 1.00 61.35 O ANISOU 1861 O VAL A 319 9454 6368 7485 -82 223 619 O ATOM 1862 CB VAL A 319 -0.408 -4.432 -27.697 1.00 59.23 C ANISOU 1862 CB VAL A 319 9065 6274 7166 -23 250 479 C ATOM 1863 CG1 VAL A 319 -1.754 -3.727 -27.683 1.00 59.86 C ANISOU 1863 CG1 VAL A 319 9105 6292 7347 2 243 415 C ATOM 1864 CG2 VAL A 319 -0.184 -5.106 -29.047 1.00 59.14 C ANISOU 1864 CG2 VAL A 319 8994 6380 7094 28 205 479 C ATOM 1865 N CYS A 320 0.592 -3.251 -24.957 1.00 61.40 N ANISOU 1865 N CYS A 320 9562 6324 7442 -121 290 545 N ATOM 1866 CA CYS A 320 0.195 -2.661 -23.681 1.00 61.59 C ANISOU 1866 CA CYS A 320 9702 6210 7486 -145 333 525 C ATOM 1867 C CYS A 320 1.139 -1.592 -23.125 1.00 61.35 C ANISOU 1867 C CYS A 320 9734 6128 7447 -156 253 599 C ATOM 1868 O CYS A 320 0.684 -0.746 -22.352 1.00 62.19 O ANISOU 1868 O CYS A 320 9913 6137 7579 -166 273 595 O ATOM 1869 CB CYS A 320 0.009 -3.758 -22.617 1.00 62.40 C ANISOU 1869 CB CYS A 320 9949 6211 7547 -160 422 451 C ATOM 1870 SG CYS A 320 -1.577 -4.632 -22.696 1.00 64.15 S ANISOU 1870 SG CYS A 320 10121 6394 7857 -170 589 324 S ATOM 1871 N TRP A 321 2.429 -1.635 -23.477 1.00 60.61 N ANISOU 1871 N TRP A 321 9604 6082 7341 -156 172 650 N ATOM 1872 CA TRP A 321 3.428 -0.713 -22.896 1.00 61.47 C ANISOU 1872 CA TRP A 321 9749 6118 7487 -166 85 691 C ATOM 1873 C TRP A 321 4.018 0.360 -23.840 1.00 61.70 C ANISOU 1873 C TRP A 321 9654 6200 7586 -178 61 774 C ATOM 1874 O TRP A 321 4.461 1.411 -23.374 1.00 61.50 O ANISOU 1874 O TRP A 321 9643 6099 7623 -191 13 804 O ATOM 1875 CB TRP A 321 4.573 -1.504 -22.272 1.00 62.38 C ANISOU 1875 CB TRP A 321 9929 6182 7588 -154 1 651 C ATOM 1876 CG TRP A 321 4.287 -1.981 -20.884 1.00 64.68 C ANISOU 1876 CG TRP A 321 10440 6335 7799 -132 -9 588 C ATOM 1877 CD1 TRP A 321 3.080 -2.380 -20.378 1.00 66.03 C ANISOU 1877 CD1 TRP A 321 10731 6453 7903 -136 115 549 C ATOM 1878 CD2 TRP A 321 5.232 -2.135 -19.823 1.00 66.22 C ANISOU 1878 CD2 TRP A 321 10789 6400 7972 -95 -146 545 C ATOM 1879 NE1 TRP A 321 3.212 -2.758 -19.065 1.00 67.14 N ANISOU 1879 NE1 TRP A 321 11124 6434 7951 -109 96 502 N ATOM 1880 CE2 TRP A 321 4.523 -2.619 -18.698 1.00 67.40 C ANISOU 1880 CE2 TRP A 321 11195 6417 7994 -72 -88 498 C ATOM 1881 CE3 TRP A 321 6.606 -1.907 -19.710 1.00 66.42 C ANISOU 1881 CE3 TRP A 321 10763 6386 8088 -71 -314 526 C ATOM 1882 CZ2 TRP A 321 5.145 -2.884 -17.478 1.00 68.01 C ANISOU 1882 CZ2 TRP A 321 11526 6325 7986 -12 -215 446 C ATOM 1883 CZ3 TRP A 321 7.222 -2.176 -18.500 1.00 67.63 C ANISOU 1883 CZ3 TRP A 321 11124 6376 8196 -9 -470 454 C ATOM 1884 CH2 TRP A 321 6.491 -2.661 -17.399 1.00 68.18 C ANISOU 1884 CH2 TRP A 321 11495 6317 8091 27 -430 422 C ATOM 1885 N LEU A 322 4.049 0.094 -25.145 1.00 60.80 N ANISOU 1885 N LEU A 322 9443 6199 7456 -172 103 810 N ATOM 1886 CA LEU A 322 4.623 1.024 -26.118 1.00 59.93 C ANISOU 1886 CA LEU A 322 9264 6117 7387 -184 122 895 C ATOM 1887 C LEU A 322 3.911 2.373 -26.126 1.00 59.51 C ANISOU 1887 C LEU A 322 9239 6019 7351 -180 120 946 C ATOM 1888 O LEU A 322 4.574 3.413 -26.065 1.00 60.16 O ANISOU 1888 O LEU A 322 9308 6041 7508 -206 114 1001 O ATOM 1889 CB LEU A 322 4.593 0.415 -27.521 1.00 60.37 C ANISOU 1889 CB LEU A 322 9275 6286 7375 -161 180 919 C ATOM 1890 CG LEU A 322 5.166 1.252 -28.660 1.00 62.00 C ANISOU 1890 CG LEU A 322 9466 6503 7585 -168 244 1012 C ATOM 1891 CD1 LEU A 322 6.683 1.305 -28.560 1.00 63.13 C ANISOU 1891 CD1 LEU A 322 9537 6602 7848 -222 285 1017 C ATOM 1892 CD2 LEU A 322 4.736 0.674 -29.999 1.00 62.45 C ANISOU 1892 CD2 LEU A 322 9549 6656 7522 -116 285 1028 C ATOM 1893 N PRO A 323 2.567 2.371 -26.208 1.00 58.01 N ANISOU 1893 N PRO A 323 9075 5844 7122 -145 122 916 N ATOM 1894 CA PRO A 323 1.867 3.654 -26.238 1.00 58.19 C ANISOU 1894 CA PRO A 323 9116 5815 7176 -133 102 952 C ATOM 1895 C PRO A 323 1.985 4.479 -24.943 1.00 57.71 C ANISOU 1895 C PRO A 323 9100 5642 7183 -165 77 944 C ATOM 1896 O PRO A 323 1.771 5.682 -24.971 1.00 58.64 O ANISOU 1896 O PRO A 323 9225 5710 7342 -164 57 990 O ATOM 1897 CB PRO A 323 0.409 3.261 -26.519 1.00 58.21 C ANISOU 1897 CB PRO A 323 9106 5842 7167 -83 96 875 C ATOM 1898 CG PRO A 323 0.300 1.834 -26.132 1.00 57.67 C ANISOU 1898 CG PRO A 323 9028 5802 7079 -92 136 790 C ATOM 1899 CD PRO A 323 1.642 1.242 -26.401 1.00 57.71 C ANISOU 1899 CD PRO A 323 9025 5860 7040 -114 141 835 C ATOM 1900 N TYR A 324 2.327 3.833 -23.832 1.00 56.92 N ANISOU 1900 N TYR A 324 9054 5490 7081 -183 68 884 N ATOM 1901 CA TYR A 324 2.575 4.513 -22.563 1.00 55.90 C ANISOU 1901 CA TYR A 324 9008 5238 6992 -197 25 867 C ATOM 1902 C TYR A 324 3.909 5.247 -22.603 1.00 56.76 C ANISOU 1902 C TYR A 324 9070 5310 7184 -218 -39 918 C ATOM 1903 O TYR A 324 4.051 6.331 -22.030 1.00 57.47 O ANISOU 1903 O TYR A 324 9184 5311 7339 -227 -83 934 O ATOM 1904 CB TYR A 324 2.564 3.482 -21.424 1.00 54.78 C ANISOU 1904 CB TYR A 324 8994 5030 6788 -190 27 783 C ATOM 1905 CG TYR A 324 2.828 4.012 -20.033 1.00 54.04 C ANISOU 1905 CG TYR A 324 9050 4789 6693 -183 -31 752 C ATOM 1906 CD1 TYR A 324 1.793 4.454 -19.233 1.00 53.93 C ANISOU 1906 CD1 TYR A 324 9147 4685 6658 -181 33 716 C ATOM 1907 CD2 TYR A 324 4.113 4.031 -19.504 1.00 54.35 C ANISOU 1907 CD2 TYR A 324 9126 4762 6761 -169 -159 739 C ATOM 1908 CE1 TYR A 324 2.030 4.920 -17.952 1.00 54.47 C ANISOU 1908 CE1 TYR A 324 9392 4606 6698 -164 -19 685 C ATOM 1909 CE2 TYR A 324 4.362 4.495 -18.226 1.00 54.73 C ANISOU 1909 CE2 TYR A 324 9340 4659 6795 -140 -249 696 C ATOM 1910 CZ TYR A 324 3.319 4.937 -17.449 1.00 54.70 C ANISOU 1910 CZ TYR A 324 9479 4571 6731 -137 -174 676 C ATOM 1911 OH TYR A 324 3.564 5.401 -16.172 1.00 55.23 O ANISOU 1911 OH TYR A 324 9749 4477 6759 -98 -262 633 O ATOM 1912 N HIS A 325 4.891 4.657 -23.269 1.00 56.87 N ANISOU 1912 N HIS A 325 9006 5380 7221 -229 -35 930 N ATOM 1913 CA HIS A 325 6.194 5.285 -23.385 1.00 58.38 C ANISOU 1913 CA HIS A 325 9116 5518 7547 -258 -68 954 C ATOM 1914 C HIS A 325 6.238 6.317 -24.502 1.00 59.13 C ANISOU 1914 C HIS A 325 9146 5633 7685 -283 18 1053 C ATOM 1915 O HIS A 325 6.958 7.312 -24.424 1.00 59.60 O ANISOU 1915 O HIS A 325 9157 5608 7877 -314 15 1080 O ATOM 1916 CB HIS A 325 7.241 4.218 -23.576 1.00 59.10 C ANISOU 1916 CB HIS A 325 9142 5633 7678 -262 -84 903 C ATOM 1917 CG HIS A 325 7.504 3.461 -22.326 1.00 60.27 C ANISOU 1917 CG HIS A 325 9385 5706 7808 -227 -209 804 C ATOM 1918 ND1 HIS A 325 8.747 3.401 -21.743 1.00 62.07 N ANISOU 1918 ND1 HIS A 325 9575 5833 8172 -217 -335 729 N ATOM 1919 CD2 HIS A 325 6.667 2.795 -21.502 1.00 60.55 C ANISOU 1919 CD2 HIS A 325 9578 5722 7707 -193 -227 759 C ATOM 1920 CE1 HIS A 325 8.674 2.696 -20.630 1.00 62.45 C ANISOU 1920 CE1 HIS A 325 9784 5808 8137 -164 -453 649 C ATOM 1921 NE2 HIS A 325 7.419 2.320 -20.458 1.00 61.76 N ANISOU 1921 NE2 HIS A 325 9827 5764 7873 -155 -367 674 N ATOM 1922 N VAL A 326 5.462 6.080 -25.546 1.00 59.24 N ANISOU 1922 N VAL A 326 9176 5742 7587 -261 91 1101 N ATOM 1923 CA VAL A 326 5.265 7.099 -26.540 1.00 60.23 C ANISOU 1923 CA VAL A 326 9316 5864 7702 -260 156 1198 C ATOM 1924 C VAL A 326 4.749 8.350 -25.842 1.00 60.68 C ANISOU 1924 C VAL A 326 9410 5833 7813 -261 101 1215 C ATOM 1925 O VAL A 326 5.307 9.415 -26.061 1.00 61.98 O ANISOU 1925 O VAL A 326 9560 5923 8064 -291 134 1278 O ATOM 1926 CB VAL A 326 4.311 6.633 -27.649 1.00 60.15 C ANISOU 1926 CB VAL A 326 9359 5950 7543 -204 184 1222 C ATOM 1927 CG1 VAL A 326 3.763 7.816 -28.439 1.00 60.92 C ANISOU 1927 CG1 VAL A 326 9535 6011 7600 -172 196 1309 C ATOM 1928 CG2 VAL A 326 5.039 5.661 -28.559 1.00 60.27 C ANISOU 1928 CG2 VAL A 326 9348 6038 7512 -208 264 1229 C ATOM 1929 N ARG A 327 3.733 8.219 -24.978 1.00 60.15 N ANISOU 1929 N ARG A 327 9388 5756 7708 -234 37 1152 N ATOM 1930 CA ARG A 327 3.112 9.397 -24.351 1.00 60.43 C ANISOU 1930 CA ARG A 327 9460 5707 7790 -230 -6 1160 C ATOM 1931 C ARG A 327 4.033 10.146 -23.409 1.00 60.97 C ANISOU 1931 C ARG A 327 9519 5666 7980 -266 -54 1153 C ATOM 1932 O ARG A 327 3.979 11.359 -23.361 1.00 62.58 O ANISOU 1932 O ARG A 327 9725 5801 8251 -276 -66 1199 O ATOM 1933 CB ARG A 327 1.811 9.077 -23.612 1.00 59.91 C ANISOU 1933 CB ARG A 327 9443 5634 7685 -200 -25 1076 C ATOM 1934 CG ARG A 327 1.071 10.347 -23.176 1.00 60.74 C ANISOU 1934 CG ARG A 327 9574 5655 7847 -192 -56 1081 C ATOM 1935 CD ARG A 327 -0.141 10.102 -22.297 1.00 60.75 C ANISOU 1935 CD ARG A 327 9616 5614 7850 -177 -38 979 C ATOM 1936 NE ARG A 327 0.139 9.103 -21.275 1.00 61.28 N ANISOU 1936 NE ARG A 327 9756 5654 7875 -193 -8 908 N ATOM 1937 CZ ARG A 327 0.906 9.282 -20.196 1.00 61.49 C ANISOU 1937 CZ ARG A 327 9869 5591 7903 -207 -50 895 C ATOM 1938 NH1 ARG A 327 1.485 10.449 -19.943 1.00 61.07 N ANISOU 1938 NH1 ARG A 327 9809 5471 7922 -216 -119 939 N ATOM 1939 NH2 ARG A 327 1.089 8.264 -19.350 1.00 62.04 N ANISOU 1939 NH2 ARG A 327 10050 5622 7900 -202 -34 827 N ATOM 1940 N ARG A 328 4.859 9.450 -22.647 1.00 61.76 N ANISOU 1940 N ARG A 328 9613 5737 8116 -276 -102 1086 N ATOM 1941 CA ARG A 328 5.832 10.140 -21.793 1.00 63.14 C ANISOU 1941 CA ARG A 328 9770 5789 8431 -293 -189 1055 C ATOM 1942 C ARG A 328 6.847 10.901 -22.638 1.00 63.36 C ANISOU 1942 C ARG A 328 9676 5784 8611 -340 -130 1118 C ATOM 1943 O ARG A 328 7.261 12.006 -22.268 1.00 64.21 O ANISOU 1943 O ARG A 328 9753 5785 8857 -360 -166 1125 O ATOM 1944 CB ARG A 328 6.557 9.177 -20.838 1.00 64.09 C ANISOU 1944 CB ARG A 328 9928 5862 8560 -271 -293 950 C ATOM 1945 CG ARG A 328 5.740 8.806 -19.606 1.00 64.85 C ANISOU 1945 CG ARG A 328 10204 5906 8530 -227 -349 883 C ATOM 1946 CD ARG A 328 6.061 7.411 -19.079 1.00 65.78 C ANISOU 1946 CD ARG A 328 10412 6019 8562 -193 -399 803 C ATOM 1947 NE ARG A 328 7.042 7.375 -17.985 1.00 67.69 N ANISOU 1947 NE ARG A 328 10738 6119 8859 -148 -577 713 N ATOM 1948 CZ ARG A 328 6.764 7.568 -16.688 1.00 69.54 C ANISOU 1948 CZ ARG A 328 11186 6221 9013 -96 -668 654 C ATOM 1949 NH1 ARG A 328 5.527 7.860 -16.282 1.00 69.67 N ANISOU 1949 NH1 ARG A 328 11335 6225 8910 -99 -562 675 N ATOM 1950 NH2 ARG A 328 7.738 7.484 -15.778 1.00 70.64 N ANISOU 1950 NH2 ARG A 328 11418 6220 9200 -33 -871 559 N ATOM 1951 N LEU A 329 7.242 10.329 -23.770 1.00 62.79 N ANISOU 1951 N LEU A 329 9544 5788 8521 -359 -21 1159 N ATOM 1952 CA LEU A 329 8.264 10.963 -24.609 1.00 64.40 C ANISOU 1952 CA LEU A 329 9652 5938 8878 -414 91 1212 C ATOM 1953 C LEU A 329 7.759 12.223 -25.324 1.00 65.14 C ANISOU 1953 C LEU A 329 9803 5998 8949 -424 181 1328 C ATOM 1954 O LEU A 329 8.491 13.193 -25.462 1.00 65.71 O ANISOU 1954 O LEU A 329 9818 5959 9187 -472 246 1359 O ATOM 1955 CB LEU A 329 8.844 9.950 -25.594 1.00 64.38 C ANISOU 1955 CB LEU A 329 9597 6011 8852 -430 206 1216 C ATOM 1956 CG LEU A 329 9.870 9.052 -24.901 1.00 64.56 C ANISOU 1956 CG LEU A 329 9515 6002 9011 -436 117 1090 C ATOM 1957 CD1 LEU A 329 10.038 7.736 -25.648 1.00 64.73 C ANISOU 1957 CD1 LEU A 329 9516 6133 8943 -429 189 1075 C ATOM 1958 CD2 LEU A 329 11.206 9.769 -24.740 1.00 65.71 C ANISOU 1958 CD2 LEU A 329 9508 5998 9460 -490 134 1037 C ATOM 1959 N MET A 330 6.506 12.179 -25.763 1.00 65.53 N ANISOU 1959 N MET A 330 9962 6128 8807 -374 177 1378 N ATOM 1960 CA MET A 330 5.785 13.330 -26.306 1.00 67.35 C ANISOU 1960 CA MET A 330 10281 6320 8987 -354 203 1471 C ATOM 1961 C MET A 330 5.630 14.482 -25.293 1.00 66.75 C ANISOU 1961 C MET A 330 10194 6139 9027 -365 114 1455 C ATOM 1962 O MET A 330 5.663 15.652 -25.677 1.00 67.54 O ANISOU 1962 O MET A 330 10327 6156 9178 -379 160 1533 O ATOM 1963 CB MET A 330 4.410 12.849 -26.798 1.00 68.95 C ANISOU 1963 CB MET A 330 10577 6622 8996 -277 157 1474 C ATOM 1964 CG MET A 330 3.372 13.926 -27.111 1.00 71.66 C ANISOU 1964 CG MET A 330 11015 6922 9290 -227 109 1526 C ATOM 1965 SD MET A 330 1.758 13.194 -27.516 1.00 74.69 S ANISOU 1965 SD MET A 330 11453 7401 9525 -127 11 1463 S ATOM 1966 CE MET A 330 0.722 14.654 -27.679 1.00 74.67 C ANISOU 1966 CE MET A 330 11532 7305 9534 -67 -80 1497 C ATOM 1967 N PHE A 331 5.447 14.141 -24.016 1.00 65.20 N ANISOU 1967 N PHE A 331 9979 5935 8857 -354 -4 1355 N ATOM 1968 CA PHE A 331 5.350 15.108 -22.910 1.00 65.11 C ANISOU 1968 CA PHE A 331 9975 5818 8946 -356 -100 1319 C ATOM 1969 C PHE A 331 6.575 16.022 -22.820 1.00 67.99 C ANISOU 1969 C PHE A 331 10249 6057 9526 -409 -85 1331 C ATOM 1970 O PHE A 331 6.443 17.217 -22.534 1.00 68.95 O ANISOU 1970 O PHE A 331 10379 6086 9732 -418 -111 1358 O ATOM 1971 CB PHE A 331 5.149 14.360 -21.572 1.00 63.43 C ANISOU 1971 CB PHE A 331 9804 5598 8696 -327 -211 1202 C ATOM 1972 CG PHE A 331 5.271 15.230 -20.341 1.00 62.53 C ANISOU 1972 CG PHE A 331 9723 5357 8677 -320 -321 1148 C ATOM 1973 CD1 PHE A 331 6.515 15.523 -19.798 1.00 62.68 C ANISOU 1973 CD1 PHE A 331 9676 5269 8869 -337 -404 1094 C ATOM 1974 CD2 PHE A 331 4.135 15.727 -19.701 1.00 61.84 C ANISOU 1974 CD2 PHE A 331 9730 5243 8522 -291 -348 1130 C ATOM 1975 CE1 PHE A 331 6.626 16.315 -18.664 1.00 62.75 C ANISOU 1975 CE1 PHE A 331 9730 5151 8958 -315 -531 1033 C ATOM 1976 CE2 PHE A 331 4.238 16.514 -18.562 1.00 61.75 C ANISOU 1976 CE2 PHE A 331 9771 5109 8580 -279 -445 1077 C ATOM 1977 CZ PHE A 331 5.488 16.813 -18.046 1.00 62.40 C ANISOU 1977 CZ PHE A 331 9806 5090 8811 -286 -547 1032 C ATOM 1978 N CYS A 332 7.763 15.467 -23.055 1.00 70.02 N ANISOU 1978 N CYS A 332 10404 6297 9901 -447 -40 1297 N ATOM 1979 CA CYS A 332 9.003 16.230 -22.900 1.00 71.89 C ANISOU 1979 CA CYS A 332 10514 6391 10411 -501 -23 1267 C ATOM 1980 C CYS A 332 9.627 16.713 -24.210 1.00 72.44 C ANISOU 1980 C CYS A 332 10535 6417 10572 -567 200 1364 C ATOM 1981 O CYS A 332 10.265 17.764 -24.208 1.00 75.00 O ANISOU 1981 O CYS A 332 10786 6601 11110 -618 257 1374 O ATOM 1982 CB CYS A 332 10.024 15.425 -22.097 1.00 73.51 C ANISOU 1982 CB CYS A 332 10616 6551 10763 -495 -146 1122 C ATOM 1983 SG CYS A 332 10.351 13.762 -22.732 1.00 76.65 S ANISOU 1983 SG CYS A 332 10985 7074 11063 -490 -82 1093 S ATOM 1984 N TYR A 333 9.444 15.986 -25.315 1.00 71.10 N ANISOU 1984 N TYR A 333 10422 6347 10243 -565 339 1432 N ATOM 1985 CA TYR A 333 10.111 16.338 -26.589 1.00 72.28 C ANISOU 1985 CA TYR A 333 10573 6433 10454 -625 589 1522 C ATOM 1986 C TYR A 333 9.350 17.310 -27.512 1.00 72.30 C ANISOU 1986 C TYR A 333 10763 6407 10299 -608 699 1675 C ATOM 1987 O TYR A 333 9.935 17.830 -28.464 1.00 73.01 O ANISOU 1987 O TYR A 333 10900 6396 10443 -659 926 1758 O ATOM 1988 CB TYR A 333 10.523 15.083 -27.365 1.00 72.80 C ANISOU 1988 CB TYR A 333 10623 6589 10447 -631 702 1509 C ATOM 1989 CG TYR A 333 11.901 14.585 -26.992 1.00 74.32 C ANISOU 1989 CG TYR A 333 10600 6706 10928 -689 725 1379 C ATOM 1990 CD1 TYR A 333 13.042 15.127 -27.586 1.00 76.59 C ANISOU 1990 CD1 TYR A 333 10777 6842 11478 -779 953 1377 C ATOM 1991 CD2 TYR A 333 12.068 13.584 -26.036 1.00 73.71 C ANISOU 1991 CD2 TYR A 333 10437 6688 10881 -651 521 1244 C ATOM 1992 CE1 TYR A 333 14.309 14.680 -27.246 1.00 77.68 C ANISOU 1992 CE1 TYR A 333 10684 6892 11937 -829 961 1225 C ATOM 1993 CE2 TYR A 333 13.333 13.135 -25.688 1.00 75.03 C ANISOU 1993 CE2 TYR A 333 10407 6769 11332 -686 499 1103 C ATOM 1994 CZ TYR A 333 14.448 13.686 -26.294 1.00 76.90 C ANISOU 1994 CZ TYR A 333 10495 6858 11863 -775 710 1084 C ATOM 1995 OH TYR A 333 15.700 13.237 -25.944 1.00 78.80 O ANISOU 1995 OH TYR A 333 10505 6996 12437 -805 675 913 O ATOM 1996 N ILE A 334 8.063 17.538 -27.234 1.00 71.06 N ANISOU 1996 N ILE A 334 10723 6320 9956 -533 547 1703 N ATOM 1997 CA ILE A 334 7.275 18.596 -27.888 1.00 70.97 C ANISOU 1997 CA ILE A 334 10884 6257 9824 -496 579 1821 C ATOM 1998 C ILE A 334 7.438 19.907 -27.117 1.00 71.53 C ANISOU 1998 C ILE A 334 10900 6192 10084 -531 529 1818 C ATOM 1999 O ILE A 334 6.955 20.044 -25.995 1.00 68.43 O ANISOU 1999 O ILE A 334 10450 5819 9729 -505 346 1740 O ATOM 2000 CB ILE A 334 5.775 18.242 -27.946 1.00 69.78 C ANISOU 2000 CB ILE A 334 10852 6225 9435 -392 419 1820 C ATOM 2001 CG1 ILE A 334 5.548 16.987 -28.792 1.00 69.14 C ANISOU 2001 CG1 ILE A 334 10833 6269 9168 -348 457 1820 C ATOM 2002 CG2 ILE A 334 4.963 19.399 -28.511 1.00 70.67 C ANISOU 2002 CG2 ILE A 334 11135 6263 9454 -338 400 1917 C ATOM 2003 CD1 ILE A 334 4.075 16.763 -29.039 0.00 20.00 C ATOM 2004 N SER A 335 8.106 20.876 -27.742 1.00 75.07 N ANISOU 2004 N SER A 335 11383 6489 10647 -588 711 1903 N ATOM 2005 CA SER A 335 8.480 22.129 -27.076 1.00 76.86 C ANISOU 2005 CA SER A 335 11532 6565 11105 -636 693 1892 C ATOM 2006 C SER A 335 7.340 23.154 -27.049 1.00 77.67 C ANISOU 2006 C SER A 335 11786 6642 11081 -573 586 1966 C ATOM 2007 O SER A 335 6.319 22.988 -27.726 1.00 77.89 O ANISOU 2007 O SER A 335 11992 6745 10857 -490 545 2031 O ATOM 2008 CB SER A 335 9.721 22.729 -27.732 1.00 78.87 C ANISOU 2008 CB SER A 335 11743 6642 11581 -737 964 1937 C ATOM 2009 OG SER A 335 9.447 23.096 -29.068 1.00 80.80 O ANISOU 2009 OG SER A 335 12234 6835 11632 -723 1165 2092 O ATOM 2010 N ASP A 336 7.539 24.215 -26.266 1.00 78.53 N ANISOU 2010 N ASP A 336 11815 6634 11388 -605 526 1939 N ATOM 2011 CA ASP A 336 6.479 25.176 -25.939 1.00 78.61 C ANISOU 2011 CA ASP A 336 11921 6620 11326 -546 385 1972 C ATOM 2012 C ASP A 336 5.875 25.890 -27.136 1.00 79.67 C ANISOU 2012 C ASP A 336 12293 6692 11284 -500 473 2120 C ATOM 2013 O ASP A 336 4.662 26.060 -27.206 1.00 79.85 O ANISOU 2013 O ASP A 336 12432 6767 11137 -407 323 2133 O ATOM 2014 CB ASP A 336 6.998 26.211 -24.949 1.00 79.75 C ANISOU 2014 CB ASP A 336 11933 6628 11737 -596 327 1915 C ATOM 2015 CG ASP A 336 7.220 25.627 -23.587 1.00 79.59 C ANISOU 2015 CG ASP A 336 11753 6661 11826 -592 148 1756 C ATOM 2016 OD1 ASP A 336 8.139 24.792 -23.446 1.00 80.87 O ANISOU 2016 OD1 ASP A 336 11794 6838 12093 -629 182 1681 O ATOM 2017 OD2 ASP A 336 6.461 25.981 -22.661 1.00 80.02 O ANISOU 2017 OD2 ASP A 336 11822 6729 11851 -544 -26 1702 O ATOM 2018 N GLU A 337 6.716 26.306 -28.075 1.00 81.29 N ANISOU 2018 N GLU A 337 12583 6764 11536 -559 719 2221 N ATOM 2019 CA GLU A 337 6.239 26.963 -29.287 1.00 82.38 C ANISOU 2019 CA GLU A 337 13016 6810 11472 -505 819 2373 C ATOM 2020 C GLU A 337 5.327 26.075 -30.141 1.00 81.31 C ANISOU 2020 C GLU A 337 13074 6806 11012 -389 743 2403 C ATOM 2021 O GLU A 337 4.685 26.576 -31.059 1.00 82.39 O ANISOU 2021 O GLU A 337 13488 6873 10942 -300 736 2506 O ATOM 2022 CB GLU A 337 7.276 27.482 -30.185 0.00 20.00 C ATOM 2023 CG GLU A 337 8.147 28.579 -29.557 0.00 20.00 C ATOM 2024 CD GLU A 337 9.287 29.069 -30.448 0.00 20.00 C ATOM 2025 OE1 GLU A 337 9.541 28.440 -31.492 0.00 20.00 O ATOM 2026 OE2 GLU A 337 9.918 30.090 -30.113 0.00 20.00 O ATOM 2027 N GLN A 338 5.272 24.774 -29.832 1.00 79.09 N ANISOU 2027 N GLN A 338 12659 6697 10693 -380 671 2306 N ATOM 2028 CA GLN A 338 4.501 23.786 -30.607 1.00 78.26 C ANISOU 2028 CA GLN A 338 12696 6719 10317 -277 600 2310 C ATOM 2029 C GLN A 338 3.200 23.311 -29.941 1.00 75.34 C ANISOU 2029 C GLN A 338 12254 6491 9880 -185 320 2198 C ATOM 2030 O GLN A 338 2.348 22.716 -30.598 1.00 74.36 O ANISOU 2030 O GLN A 338 12252 6441 9558 -79 220 2188 O ATOM 2031 CB GLN A 338 5.378 22.564 -30.876 1.00 78.60 C ANISOU 2031 CB GLN A 338 12650 6845 10368 -335 751 2277 C ATOM 2032 CG GLN A 338 6.764 22.892 -31.418 1.00 81.05 C ANISOU 2032 CG GLN A 338 12971 7007 10817 -448 1065 2347 C ATOM 2033 CD GLN A 338 7.698 21.694 -31.407 1.00 81.44 C ANISOU 2033 CD GLN A 338 12851 7135 10955 -517 1187 2273 C ATOM 2034 OE1 GLN A 338 7.583 20.808 -30.553 1.00 80.06 O ANISOU 2034 OE1 GLN A 338 12480 7102 10835 -513 1023 2152 O ATOM 2035 NE2 GLN A 338 8.638 21.663 -32.349 1.00 83.59 N ANISOU 2035 NE2 GLN A 338 13213 7298 11248 -581 1491 2341 N ATOM 2036 N TRP A 339 3.055 23.551 -28.643 1.00 73.79 N ANISOU 2036 N TRP A 339 11863 6315 9858 -222 204 2103 N ATOM 2037 CA TRP A 339 1.849 23.143 -27.919 1.00 72.50 C ANISOU 2037 CA TRP A 339 11627 6255 9664 -152 -7 1986 C ATOM 2038 C TRP A 339 0.659 24.038 -28.259 1.00 72.71 C ANISOU 2038 C TRP A 339 11789 6217 9621 -49 -154 2004 C ATOM 2039 O TRP A 339 0.754 25.259 -28.196 1.00 73.47 O ANISOU 2039 O TRP A 339 11940 6183 9789 -60 -150 2066 O ATOM 2040 CB TRP A 339 2.086 23.155 -26.403 1.00 71.69 C ANISOU 2040 CB TRP A 339 11325 6165 9748 -218 -64 1879 C ATOM 2041 CG TRP A 339 2.802 21.949 -25.918 1.00 71.09 C ANISOU 2041 CG TRP A 339 11123 6181 9705 -271 -19 1806 C ATOM 2042 CD1 TRP A 339 4.098 21.870 -25.503 1.00 71.59 C ANISOU 2042 CD1 TRP A 339 11075 6199 9925 -358 67 1792 C ATOM 2043 CD2 TRP A 339 2.263 20.627 -25.812 1.00 70.45 C ANISOU 2043 CD2 TRP A 339 11013 6237 9515 -234 -69 1723 C ATOM 2044 NE1 TRP A 339 4.399 20.580 -25.141 1.00 70.84 N ANISOU 2044 NE1 TRP A 339 10899 6208 9809 -368 56 1709 N ATOM 2045 CE2 TRP A 339 3.291 19.796 -25.323 1.00 69.61 C ANISOU 2045 CE2 TRP A 339 10800 6167 9482 -298 -13 1675 C ATOM 2046 CE3 TRP A 339 1.008 20.063 -26.084 1.00 69.89 C ANISOU 2046 CE3 TRP A 339 10987 6248 9318 -149 -160 1671 C ATOM 2047 CZ2 TRP A 339 3.107 18.438 -25.101 1.00 68.41 C ANISOU 2047 CZ2 TRP A 339 10610 6132 9250 -282 -35 1595 C ATOM 2048 CZ3 TRP A 339 0.829 18.711 -25.864 1.00 68.33 C ANISOU 2048 CZ3 TRP A 339 10731 6164 9064 -143 -165 1586 C ATOM 2049 CH2 TRP A 339 1.873 17.914 -25.378 1.00 67.70 C ANISOU 2049 CH2 TRP A 339 10571 6122 9030 -210 -98 1558 C ATOM 2050 N THR A 340 -0.455 23.410 -28.617 1.00 55.18 N ANISOU 2050 N THR A 340 7277 6619 7069 138 -341 532 N ATOM 2051 CA THR A 340 -1.698 24.105 -28.939 1.00 54.89 C ANISOU 2051 CA THR A 340 7183 6627 7043 122 -324 582 C ATOM 2052 C THR A 340 -2.821 23.536 -28.088 1.00 55.09 C ANISOU 2052 C THR A 340 7241 6619 7072 102 -294 571 C ATOM 2053 O THR A 340 -2.677 22.474 -27.463 1.00 54.70 O ANISOU 2053 O THR A 340 7272 6534 6975 95 -294 513 O ATOM 2054 CB THR A 340 -2.081 23.919 -30.424 1.00 54.76 C ANISOU 2054 CB THR A 340 7146 6688 6973 94 -351 625 C ATOM 2055 OG1 THR A 340 -2.163 22.522 -30.737 1.00 55.08 O ANISOU 2055 OG1 THR A 340 7279 6729 6916 62 -383 577 O ATOM 2056 CG2 THR A 340 -1.056 24.549 -31.315 1.00 55.00 C ANISOU 2056 CG2 THR A 340 7166 6731 6999 138 -316 661 C ATOM 2057 N THR A 341 -3.958 24.224 -28.079 1.00 55.55 N ANISOU 2057 N THR A 341 7219 6670 7215 101 -249 648 N ATOM 2058 CA THR A 341 -5.154 23.665 -27.450 1.00 55.51 C ANISOU 2058 CA THR A 341 7196 6610 7284 92 -179 689 C ATOM 2059 C THR A 341 -5.513 22.297 -28.044 1.00 54.93 C ANISOU 2059 C THR A 341 7106 6570 7192 24 -273 682 C ATOM 2060 O THR A 341 -5.884 21.400 -27.303 1.00 55.23 O ANISOU 2060 O THR A 341 7180 6554 7248 22 -224 668 O ATOM 2061 CB THR A 341 -6.327 24.653 -27.498 1.00 56.50 C ANISOU 2061 CB THR A 341 7188 6699 7579 106 -98 818 C ATOM 2062 OG1 THR A 341 -6.080 25.693 -26.548 1.00 56.49 O ANISOU 2062 OG1 THR A 341 7281 6615 7568 185 30 806 O ATOM 2063 CG2 THR A 341 -7.639 23.977 -27.133 1.00 58.26 C ANISOU 2063 CG2 THR A 341 7320 6847 7968 92 -23 917 C ATOM 2064 N PHE A 342 -5.352 22.120 -29.354 1.00 54.59 N ANISOU 2064 N PHE A 342 7052 6595 7094 -25 -404 688 N ATOM 2065 CA PHE A 342 -5.595 20.823 -29.977 1.00 55.23 C ANISOU 2065 CA PHE A 342 7190 6676 7116 -91 -523 667 C ATOM 2066 C PHE A 342 -4.745 19.674 -29.430 1.00 54.10 C ANISOU 2066 C PHE A 342 7171 6523 6861 -74 -486 555 C ATOM 2067 O PHE A 342 -5.294 18.649 -29.065 1.00 54.17 O ANISOU 2067 O PHE A 342 7187 6492 6901 -110 -510 550 O ATOM 2068 CB PHE A 342 -5.408 20.872 -31.488 1.00 56.51 C ANISOU 2068 CB PHE A 342 7433 6872 7164 -129 -660 679 C ATOM 2069 CG PHE A 342 -5.607 19.535 -32.154 1.00 58.61 C ANISOU 2069 CG PHE A 342 7842 7100 7326 -195 -802 646 C ATOM 2070 CD1 PHE A 342 -6.803 18.841 -31.997 1.00 60.37 C ANISOU 2070 CD1 PHE A 342 7991 7257 7690 -278 -933 712 C ATOM 2071 CD2 PHE A 342 -4.599 18.954 -32.913 1.00 59.68 C ANISOU 2071 CD2 PHE A 342 8192 7236 7246 -168 -790 563 C ATOM 2072 CE1 PHE A 342 -6.995 17.602 -32.594 1.00 61.89 C ANISOU 2072 CE1 PHE A 342 8336 7389 7790 -349 -1102 680 C ATOM 2073 CE2 PHE A 342 -4.787 17.717 -33.521 1.00 61.27 C ANISOU 2073 CE2 PHE A 342 8583 7373 7321 -222 -917 523 C ATOM 2074 CZ PHE A 342 -5.988 17.042 -33.360 1.00 62.20 C ANISOU 2074 CZ PHE A 342 8641 7430 7561 -322 -1099 573 C ATOM 2075 N LEU A 343 -3.418 19.832 -29.419 1.00 53.37 N ANISOU 2075 N LEU A 343 7151 6449 6675 -22 -437 487 N ATOM 2076 CA LEU A 343 -2.494 18.786 -28.941 1.00 52.35 C ANISOU 2076 CA LEU A 343 7116 6294 6480 -4 -410 404 C ATOM 2077 C LEU A 343 -2.667 18.542 -27.453 1.00 52.09 C ANISOU 2077 C LEU A 343 7096 6201 6492 10 -362 379 C ATOM 2078 O LEU A 343 -2.625 17.407 -26.997 1.00 51.98 O ANISOU 2078 O LEU A 343 7143 6158 6448 -3 -364 333 O ATOM 2079 CB LEU A 343 -1.027 19.168 -29.196 1.00 52.08 C ANISOU 2079 CB LEU A 343 7100 6253 6433 52 -365 389 C ATOM 2080 CG LEU A 343 -0.432 19.065 -30.605 1.00 52.65 C ANISOU 2080 CG LEU A 343 7237 6340 6427 76 -331 407 C ATOM 2081 CD1 LEU A 343 1.033 19.455 -30.548 1.00 52.60 C ANISOU 2081 CD1 LEU A 343 7185 6287 6513 147 -241 436 C ATOM 2082 CD2 LEU A 343 -0.581 17.669 -31.192 1.00 53.25 C ANISOU 2082 CD2 LEU A 343 7464 6393 6375 50 -349 358 C ATOM 2083 N PHE A 344 -2.841 19.626 -26.704 1.00 52.18 N ANISOU 2083 N PHE A 344 7090 6177 6558 47 -309 410 N ATOM 2084 CA PHE A 344 -3.090 19.566 -25.273 1.00 52.46 C ANISOU 2084 CA PHE A 344 7224 6114 6592 80 -236 395 C ATOM 2085 C PHE A 344 -4.339 18.747 -24.969 1.00 54.13 C ANISOU 2085 C PHE A 344 7407 6297 6860 62 -164 438 C ATOM 2086 O PHE A 344 -4.315 17.891 -24.090 1.00 54.96 O ANISOU 2086 O PHE A 344 7618 6338 6926 75 -121 403 O ATOM 2087 CB PHE A 344 -3.236 20.985 -24.736 1.00 51.98 C ANISOU 2087 CB PHE A 344 7193 5994 6560 130 -176 433 C ATOM 2088 CG PHE A 344 -3.523 21.076 -23.262 1.00 51.84 C ANISOU 2088 CG PHE A 344 7375 5830 6492 187 -71 422 C ATOM 2089 CD1 PHE A 344 -4.811 20.898 -22.776 1.00 52.62 C ANISOU 2089 CD1 PHE A 344 7474 5865 6653 220 109 494 C ATOM 2090 CD2 PHE A 344 -2.520 21.420 -22.370 1.00 51.80 C ANISOU 2090 CD2 PHE A 344 7578 5711 6390 212 -152 363 C ATOM 2091 CE1 PHE A 344 -5.088 21.024 -21.420 1.00 53.78 C ANISOU 2091 CE1 PHE A 344 7869 5841 6723 300 267 495 C ATOM 2092 CE2 PHE A 344 -2.789 21.562 -21.021 1.00 53.01 C ANISOU 2092 CE2 PHE A 344 8012 5689 6437 272 -63 350 C ATOM 2093 CZ PHE A 344 -4.075 21.359 -20.543 1.00 54.03 C ANISOU 2093 CZ PHE A 344 8184 5759 6585 328 177 411 C ATOM 2094 N ASP A 345 -5.430 19.007 -25.685 1.00 55.61 N ANISOU 2094 N ASP A 345 7444 6512 7173 30 -163 534 N ATOM 2095 CA ASP A 345 -6.648 18.211 -25.512 1.00 57.10 C ANISOU 2095 CA ASP A 345 7545 6646 7503 1 -122 618 C ATOM 2096 C ASP A 345 -6.406 16.761 -25.916 1.00 57.37 C ANISOU 2096 C ASP A 345 7614 6706 7475 -62 -245 555 C ATOM 2097 O ASP A 345 -6.813 15.840 -25.201 1.00 58.29 O ANISOU 2097 O ASP A 345 7751 6757 7639 -61 -183 566 O ATOM 2098 CB ASP A 345 -7.812 18.779 -26.327 1.00 58.28 C ANISOU 2098 CB ASP A 345 7493 6792 7859 -42 -168 765 C ATOM 2099 CG ASP A 345 -8.362 20.084 -25.753 1.00 59.30 C ANISOU 2099 CG ASP A 345 7562 6855 8112 33 15 863 C ATOM 2100 OD1 ASP A 345 -8.179 20.366 -24.546 1.00 59.10 O ANISOU 2100 OD1 ASP A 345 7683 6743 8026 125 212 836 O ATOM 2101 OD2 ASP A 345 -8.998 20.829 -26.531 1.00 60.91 O ANISOU 2101 OD2 ASP A 345 7601 7072 8467 2 -44 973 O ATOM 2102 N PHE A 346 -5.738 16.572 -27.054 1.00 56.68 N ANISOU 2102 N PHE A 346 7561 6696 7276 -106 -393 496 N ATOM 2103 CA PHE A 346 -5.415 15.238 -27.574 1.00 57.19 C ANISOU 2103 CA PHE A 346 7712 6766 7250 -156 -499 428 C ATOM 2104 C PHE A 346 -4.533 14.411 -26.621 1.00 55.36 C ANISOU 2104 C PHE A 346 7589 6512 6933 -116 -423 334 C ATOM 2105 O PHE A 346 -4.643 13.185 -26.572 1.00 54.54 O ANISOU 2105 O PHE A 346 7527 6380 6814 -150 -461 303 O ATOM 2106 CB PHE A 346 -4.733 15.366 -28.939 1.00 58.48 C ANISOU 2106 CB PHE A 346 7965 6980 7273 -172 -600 389 C ATOM 2107 CG PHE A 346 -4.216 14.068 -29.490 1.00 60.52 C ANISOU 2107 CG PHE A 346 8379 7216 7398 -196 -660 309 C ATOM 2108 CD1 PHE A 346 -5.059 13.211 -30.195 1.00 62.32 C ANISOU 2108 CD1 PHE A 346 8668 7388 7622 -282 -829 331 C ATOM 2109 CD2 PHE A 346 -2.879 13.702 -29.307 1.00 60.67 C ANISOU 2109 CD2 PHE A 346 8489 7240 7320 -133 -559 229 C ATOM 2110 CE1 PHE A 346 -4.585 12.016 -30.709 1.00 63.04 C ANISOU 2110 CE1 PHE A 346 8954 7434 7565 -297 -877 250 C ATOM 2111 CE2 PHE A 346 -2.397 12.508 -29.818 1.00 61.78 C ANISOU 2111 CE2 PHE A 346 8782 7339 7349 -138 -572 166 C ATOM 2112 CZ PHE A 346 -3.254 11.665 -30.520 1.00 63.10 C ANISOU 2112 CZ PHE A 346 9056 7456 7463 -216 -721 165 C ATOM 2113 N TYR A 347 -3.665 15.092 -25.876 1.00 53.17 N ANISOU 2113 N TYR A 347 7361 6228 6611 -52 -347 299 N ATOM 2114 CA TYR A 347 -2.771 14.440 -24.924 1.00 51.53 C ANISOU 2114 CA TYR A 347 7265 5970 6343 -23 -324 230 C ATOM 2115 C TYR A 347 -3.557 13.740 -23.805 1.00 51.72 C ANISOU 2115 C TYR A 347 7338 5916 6396 -15 -245 247 C ATOM 2116 O TYR A 347 -3.378 12.554 -23.554 1.00 50.33 O ANISOU 2116 O TYR A 347 7212 5718 6193 -34 -263 207 O ATOM 2117 CB TYR A 347 -1.802 15.473 -24.347 1.00 50.29 C ANISOU 2117 CB TYR A 347 7162 5777 6168 26 -326 218 C ATOM 2118 CG TYR A 347 -0.820 14.911 -23.365 1.00 49.67 C ANISOU 2118 CG TYR A 347 7206 5612 6054 41 -371 170 C ATOM 2119 CD1 TYR A 347 0.399 14.395 -23.783 1.00 49.07 C ANISOU 2119 CD1 TYR A 347 7103 5534 6006 36 -439 149 C ATOM 2120 CD2 TYR A 347 -1.108 14.903 -22.009 1.00 49.86 C ANISOU 2120 CD2 TYR A 347 7393 5526 6025 69 -339 164 C ATOM 2121 CE1 TYR A 347 1.303 13.872 -22.873 1.00 49.21 C ANISOU 2121 CE1 TYR A 347 7208 5449 6041 39 -518 131 C ATOM 2122 CE2 TYR A 347 -0.217 14.376 -21.092 1.00 50.02 C ANISOU 2122 CE2 TYR A 347 7562 5441 6001 72 -429 128 C ATOM 2123 CZ TYR A 347 0.985 13.859 -21.524 1.00 49.54 C ANISOU 2123 CZ TYR A 347 7427 5386 6008 48 -542 116 C ATOM 2124 OH TYR A 347 1.855 13.344 -20.591 1.00 49.59 O ANISOU 2124 OH TYR A 347 7559 5266 6016 40 -667 105 O ATOM 2125 N HIS A 348 -4.446 14.489 -23.164 1.00 52.53 N ANISOU 2125 N HIS A 348 7432 5962 6564 22 -127 321 N ATOM 2126 CA HIS A 348 -5.199 14.008 -22.006 1.00 53.52 C ANISOU 2126 CA HIS A 348 7636 5975 6725 63 25 367 C ATOM 2127 C HIS A 348 -6.245 12.931 -22.356 1.00 54.57 C ANISOU 2127 C HIS A 348 7623 6099 7012 11 32 439 C ATOM 2128 O HIS A 348 -6.621 12.117 -21.502 1.00 55.30 O ANISOU 2128 O HIS A 348 7775 6103 7131 36 141 464 O ATOM 2129 CB HIS A 348 -5.849 15.197 -21.288 1.00 54.47 C ANISOU 2129 CB HIS A 348 7812 5999 6883 144 207 447 C ATOM 2130 CG HIS A 348 -4.856 16.184 -20.740 1.00 54.10 C ANISOU 2130 CG HIS A 348 7966 5910 6678 191 171 377 C ATOM 2131 ND1 HIS A 348 -4.490 17.328 -21.415 1.00 53.41 N ANISOU 2131 ND1 HIS A 348 7801 5886 6605 182 93 376 N ATOM 2132 CD2 HIS A 348 -4.146 16.186 -19.587 1.00 54.43 C ANISOU 2132 CD2 HIS A 348 8298 5825 6555 237 163 316 C ATOM 2133 CE1 HIS A 348 -3.597 17.990 -20.702 1.00 53.83 C ANISOU 2133 CE1 HIS A 348 8063 5853 6534 217 35 321 C ATOM 2134 NE2 HIS A 348 -3.366 17.315 -19.591 1.00 54.47 N ANISOU 2134 NE2 HIS A 348 8385 5811 6499 246 55 282 N ATOM 2135 N TYR A 349 -6.711 12.931 -23.602 1.00 54.85 N ANISOU 2135 N TYR A 349 7488 6202 7150 -64 -103 481 N ATOM 2136 CA TYR A 349 -7.519 11.833 -24.121 1.00 55.99 C ANISOU 2136 CA TYR A 349 7518 6318 7435 -145 -203 539 C ATOM 2137 C TYR A 349 -6.630 10.610 -24.365 1.00 54.84 C ANISOU 2137 C TYR A 349 7496 6209 7132 -182 -318 410 C ATOM 2138 O TYR A 349 -6.967 9.503 -23.950 1.00 55.21 O ANISOU 2138 O TYR A 349 7543 6195 7236 -203 -307 421 O ATOM 2139 CB TYR A 349 -8.248 12.241 -25.408 1.00 57.71 C ANISOU 2139 CB TYR A 349 7582 6557 7786 -227 -381 627 C ATOM 2140 CG TYR A 349 -9.616 12.866 -25.176 1.00 60.18 C ANISOU 2140 CG TYR A 349 7679 6773 8411 -221 -289 828 C ATOM 2141 CD1 TYR A 349 -10.679 12.099 -24.690 1.00 61.97 C ANISOU 2141 CD1 TYR A 349 7761 6870 8914 -238 -226 973 C ATOM 2142 CD2 TYR A 349 -9.855 14.220 -25.455 1.00 60.88 C ANISOU 2142 CD2 TYR A 349 7686 6881 8563 -193 -249 897 C ATOM 2143 CE1 TYR A 349 -11.932 12.660 -24.479 1.00 64.32 C ANISOU 2143 CE1 TYR A 349 7821 7044 9573 -219 -105 1201 C ATOM 2144 CE2 TYR A 349 -11.109 14.789 -25.249 1.00 62.39 C ANISOU 2144 CE2 TYR A 349 7656 6961 9088 -177 -138 1108 C ATOM 2145 CZ TYR A 349 -12.140 14.009 -24.758 1.00 64.46 C ANISOU 2145 CZ TYR A 349 7759 7079 9651 -186 -56 1268 C ATOM 2146 OH TYR A 349 -13.382 14.558 -24.552 1.00 66.50 O ANISOU 2146 OH TYR A 349 7760 7192 10312 -159 88 1518 O ATOM 2147 N PHE A 350 -5.489 10.834 -25.021 1.00 53.26 N ANISOU 2147 N PHE A 350 7391 6088 6756 -180 -398 304 N ATOM 2148 CA PHE A 350 -4.454 9.812 -25.235 1.00 51.86 C ANISOU 2148 CA PHE A 350 7336 5925 6443 -187 -450 194 C ATOM 2149 C PHE A 350 -4.017 9.194 -23.905 1.00 52.24 C ANISOU 2149 C PHE A 350 7461 5919 6467 -143 -354 159 C ATOM 2150 O PHE A 350 -3.927 7.977 -23.782 1.00 52.68 O ANISOU 2150 O PHE A 350 7558 5944 6511 -167 -379 123 O ATOM 2151 CB PHE A 350 -3.260 10.445 -25.961 1.00 50.60 C ANISOU 2151 CB PHE A 350 7237 5824 6165 -155 -467 136 C ATOM 2152 CG PHE A 350 -2.294 9.468 -26.565 1.00 50.09 C ANISOU 2152 CG PHE A 350 7281 5748 6000 -153 -489 60 C ATOM 2153 CD1 PHE A 350 -2.735 8.332 -27.251 1.00 50.70 C ANISOU 2153 CD1 PHE A 350 7436 5788 6036 -209 -573 35 C ATOM 2154 CD2 PHE A 350 -0.931 9.716 -26.501 1.00 49.22 C ANISOU 2154 CD2 PHE A 350 7200 5637 5864 -91 -426 32 C ATOM 2155 CE1 PHE A 350 -1.830 7.454 -27.815 1.00 50.53 C ANISOU 2155 CE1 PHE A 350 7556 5732 5910 -187 -549 -31 C ATOM 2156 CE2 PHE A 350 -0.020 8.839 -27.074 1.00 49.51 C ANISOU 2156 CE2 PHE A 350 7324 5635 5851 -68 -389 -8 C ATOM 2157 CZ PHE A 350 -0.470 7.707 -27.728 1.00 50.06 C ANISOU 2157 CZ PHE A 350 7508 5671 5841 -108 -429 -47 C ATOM 2158 N TYR A 351 -3.782 10.043 -22.910 1.00 52.94 N ANISOU 2158 N TYR A 351 7602 5977 6536 -79 -258 172 N ATOM 2159 CA TYR A 351 -3.478 9.614 -21.553 1.00 53.44 C ANISOU 2159 CA TYR A 351 7806 5951 6545 -34 -186 152 C ATOM 2160 C TYR A 351 -4.465 8.555 -21.084 1.00 55.81 C ANISOU 2160 C TYR A 351 8086 6190 6930 -46 -105 203 C ATOM 2161 O TYR A 351 -4.056 7.543 -20.517 1.00 55.40 O ANISOU 2161 O TYR A 351 8126 6095 6829 -45 -110 161 O ATOM 2162 CB TYR A 351 -3.514 10.812 -20.592 1.00 53.15 C ANISOU 2162 CB TYR A 351 7891 5841 6463 36 -92 183 C ATOM 2163 CG TYR A 351 -3.057 10.488 -19.183 1.00 53.08 C ANISOU 2163 CG TYR A 351 8130 5700 6336 85 -57 156 C ATOM 2164 CD1 TYR A 351 -3.940 9.963 -18.245 1.00 54.04 C ANISOU 2164 CD1 TYR A 351 8359 5714 6458 132 117 211 C ATOM 2165 CD2 TYR A 351 -1.737 10.705 -18.791 1.00 52.54 C ANISOU 2165 CD2 TYR A 351 8199 5586 6175 85 -211 96 C ATOM 2166 CE1 TYR A 351 -3.520 9.661 -16.953 1.00 54.69 C ANISOU 2166 CE1 TYR A 351 8739 5651 6389 182 144 187 C ATOM 2167 CE2 TYR A 351 -1.309 10.417 -17.507 1.00 53.08 C ANISOU 2167 CE2 TYR A 351 8540 5503 6124 116 -243 79 C ATOM 2168 CZ TYR A 351 -2.204 9.891 -16.596 1.00 54.27 C ANISOU 2168 CZ TYR A 351 8853 5553 6214 167 -62 114 C ATOM 2169 OH TYR A 351 -1.789 9.593 -15.328 1.00 55.23 O ANISOU 2169 OH TYR A 351 9307 5502 6174 203 -95 97 O ATOM 2170 N MET A 352 -5.759 8.798 -21.311 1.00 58.66 N ANISOU 2170 N MET A 352 8305 6528 7455 -57 -32 315 N ATOM 2171 CA MET A 352 -6.799 7.838 -20.931 1.00 61.14 C ANISOU 2171 CA MET A 352 8540 6755 7934 -71 49 409 C ATOM 2172 C MET A 352 -6.551 6.500 -21.616 1.00 61.44 C ANISOU 2172 C MET A 352 8549 6826 7969 -156 -123 345 C ATOM 2173 O MET A 352 -6.560 5.458 -20.959 1.00 61.53 O ANISOU 2173 O MET A 352 8613 6776 7987 -151 -75 339 O ATOM 2174 CB MET A 352 -8.206 8.340 -21.288 1.00 63.56 C ANISOU 2174 CB MET A 352 8627 7009 8512 -86 111 581 C ATOM 2175 CG MET A 352 -8.814 9.339 -20.310 1.00 65.77 C ANISOU 2175 CG MET A 352 8941 7184 8865 27 393 696 C ATOM 2176 SD MET A 352 -10.329 10.094 -20.959 1.00 69.29 S ANISOU 2176 SD MET A 352 9063 7565 9696 5 443 925 S ATOM 2177 CE MET A 352 -10.884 11.020 -19.532 1.00 71.35 C ANISOU 2177 CE MET A 352 9453 7652 10002 185 888 1052 C ATOM 2178 N LEU A 353 -6.292 6.542 -22.918 1.00 61.09 N ANISOU 2178 N LEU A 353 8460 6857 7893 -227 -311 298 N ATOM 2179 CA LEU A 353 -6.062 5.335 -23.702 1.00 61.56 C ANISOU 2179 CA LEU A 353 8561 6916 7912 -301 -471 231 C ATOM 2180 C LEU A 353 -4.790 4.577 -23.314 1.00 60.52 C ANISOU 2180 C LEU A 353 8579 6798 7616 -263 -437 110 C ATOM 2181 O LEU A 353 -4.811 3.352 -23.196 1.00 61.51 O ANISOU 2181 O LEU A 353 8733 6873 7762 -287 -454 91 O ATOM 2182 CB LEU A 353 -6.031 5.669 -25.196 1.00 62.19 C ANISOU 2182 CB LEU A 353 8660 7037 7930 -363 -655 205 C ATOM 2183 CG LEU A 353 -5.704 4.512 -26.143 1.00 62.50 C ANISOU 2183 CG LEU A 353 8827 7031 7886 -434 -828 136 C ATOM 2184 CD1 LEU A 353 -6.773 3.433 -26.062 0.00 20.00 C ATOM 2185 CD2 LEU A 353 -5.549 5.014 -27.571 0.00 20.00 C ATOM 2186 N THR A 354 -3.686 5.295 -23.125 1.00 58.49 N ANISOU 2186 N THR A 354 8395 6590 7237 -206 -401 51 N ATOM 2187 CA THR A 354 -2.399 4.634 -22.870 1.00 57.62 C ANISOU 2187 CA THR A 354 8385 6469 7039 -179 -402 -29 C ATOM 2188 C THR A 354 -2.326 3.995 -21.490 1.00 57.60 C ANISOU 2188 C THR A 354 8448 6394 7043 -152 -340 -23 C ATOM 2189 O THR A 354 -1.680 2.967 -21.318 1.00 58.01 O ANISOU 2189 O THR A 354 8552 6413 7075 -156 -364 -68 O ATOM 2190 CB THR A 354 -1.185 5.583 -23.000 1.00 56.60 C ANISOU 2190 CB THR A 354 8276 6368 6858 -130 -400 -52 C ATOM 2191 OG1 THR A 354 -1.199 6.550 -21.943 1.00 56.13 O ANISOU 2191 OG1 THR A 354 8244 6281 6799 -91 -366 -17 O ATOM 2192 CG2 THR A 354 -1.173 6.279 -24.349 1.00 56.93 C ANISOU 2192 CG2 THR A 354 8283 6471 6875 -139 -427 -50 C ATOM 2193 N ASN A 355 -2.965 4.627 -20.513 1.00 57.38 N ANISOU 2193 N ASN A 355 8447 6321 7032 -113 -245 38 N ATOM 2194 CA ASN A 355 -2.926 4.157 -19.134 1.00 57.50 C ANISOU 2194 CA ASN A 355 8604 6236 7007 -70 -165 53 C ATOM 2195 C ASN A 355 -3.928 3.032 -18.858 1.00 58.43 C ANISOU 2195 C ASN A 355 8673 6300 7227 -88 -85 108 C ATOM 2196 O ASN A 355 -3.721 2.221 -17.952 1.00 58.54 O ANISOU 2196 O ASN A 355 8803 6236 7200 -65 -42 103 O ATOM 2197 CB ASN A 355 -3.139 5.324 -18.157 1.00 57.45 C ANISOU 2197 CB ASN A 355 8739 6156 6932 2 -59 99 C ATOM 2198 CG ASN A 355 -1.924 6.215 -18.052 1.00 56.79 C ANISOU 2198 CG ASN A 355 8756 6071 6749 16 -185 47 C ATOM 2199 OD1 ASN A 355 -1.318 6.577 -19.064 1.00 56.18 O ANISOU 2199 OD1 ASN A 355 8549 6085 6711 -15 -284 17 O ATOM 2200 ND2 ASN A 355 -1.546 6.563 -16.832 1.00 57.25 N ANISOU 2200 ND2 ASN A 355 9069 5997 6684 64 -190 49 N ATOM 2201 N ALA A 356 -5.016 2.992 -19.619 1.00 58.96 N ANISOU 2201 N ALA A 356 8566 6385 7451 -135 -86 177 N ATOM 2202 CA ALA A 356 -5.913 1.846 -19.576 1.00 60.25 C ANISOU 2202 CA ALA A 356 8633 6481 7775 -176 -69 245 C ATOM 2203 C ALA A 356 -5.145 0.598 -20.021 1.00 60.35 C ANISOU 2203 C ALA A 356 8694 6515 7719 -230 -208 139 C ATOM 2204 O ALA A 356 -5.135 -0.405 -19.315 1.00 61.30 O ANISOU 2204 O ALA A 356 8862 6570 7856 -221 -159 144 O ATOM 2205 CB ALA A 356 -7.127 2.069 -20.468 1.00 61.24 C ANISOU 2205 CB ALA A 356 8547 6594 8125 -242 -134 355 C ATOM 2206 N LEU A 357 -4.493 0.676 -21.183 1.00 60.00 N ANISOU 2206 N LEU A 357 8659 6544 7592 -272 -352 52 N ATOM 2207 CA LEU A 357 -3.679 -0.434 -21.701 1.00 59.29 C ANISOU 2207 CA LEU A 357 8649 6449 7428 -300 -438 -44 C ATOM 2208 C LEU A 357 -2.531 -0.788 -20.756 1.00 58.52 C ANISOU 2208 C LEU A 357 8650 6333 7250 -242 -376 -91 C ATOM 2209 O LEU A 357 -2.203 -1.959 -20.568 1.00 59.27 O ANISOU 2209 O LEU A 357 8787 6382 7351 -254 -388 -123 O ATOM 2210 CB LEU A 357 -3.099 -0.091 -23.077 1.00 58.61 C ANISOU 2210 CB LEU A 357 8614 6413 7242 -318 -530 -111 C ATOM 2211 CG LEU A 357 -4.090 0.134 -24.218 1.00 59.50 C ANISOU 2211 CG LEU A 357 8696 6513 7395 -393 -669 -77 C ATOM 2212 CD1 LEU A 357 -3.360 0.480 -25.512 1.00 59.05 C ANISOU 2212 CD1 LEU A 357 8778 6481 7177 -384 -720 -149 C ATOM 2213 CD2 LEU A 357 -4.975 -1.087 -24.405 1.00 60.90 C ANISOU 2213 CD2 LEU A 357 8864 6592 7682 -478 -794 -48 C ATOM 2214 N PHE A 358 -1.911 0.224 -20.172 1.00 57.35 N ANISOU 2214 N PHE A 358 8547 6202 7042 -187 -340 -85 N ATOM 2215 CA PHE A 358 -0.822 -0.012 -19.246 1.00 57.09 C ANISOU 2215 CA PHE A 358 8617 6114 6961 -149 -351 -105 C ATOM 2216 C PHE A 358 -1.281 -0.954 -18.144 1.00 57.52 C ANISOU 2216 C PHE A 358 8748 6083 7022 -142 -295 -75 C ATOM 2217 O PHE A 358 -0.621 -1.932 -17.865 1.00 57.49 O ANISOU 2217 O PHE A 358 8786 6035 7023 -149 -335 -101 O ATOM 2218 CB PHE A 358 -0.323 1.299 -18.633 1.00 56.43 C ANISOU 2218 CB PHE A 358 8606 6015 6821 -106 -368 -83 C ATOM 2219 CG PHE A 358 0.714 1.101 -17.574 1.00 56.45 C ANISOU 2219 CG PHE A 358 8746 5913 6789 -85 -453 -80 C ATOM 2220 CD1 PHE A 358 2.004 0.725 -17.917 1.00 56.57 C ANISOU 2220 CD1 PHE A 358 8703 5904 6885 -95 -554 -91 C ATOM 2221 CD2 PHE A 358 0.396 1.259 -16.232 1.00 56.98 C ANISOU 2221 CD2 PHE A 358 9021 5871 6756 -51 -428 -48 C ATOM 2222 CE1 PHE A 358 2.965 0.522 -16.938 1.00 57.09 C ANISOU 2222 CE1 PHE A 358 8875 5844 6973 -93 -688 -60 C ATOM 2223 CE2 PHE A 358 1.351 1.058 -15.252 1.00 57.40 C ANISOU 2223 CE2 PHE A 358 9251 5795 6761 -46 -568 -39 C ATOM 2224 CZ PHE A 358 2.636 0.690 -15.605 1.00 57.23 C ANISOU 2224 CZ PHE A 358 9128 5755 6861 -78 -727 -40 C ATOM 2225 N TYR A 359 -2.417 -0.641 -17.530 1.00 58.79 N ANISOU 2225 N TYR A 359 8925 6206 7204 -119 -177 -2 N ATOM 2226 CA TYR A 359 -2.944 -1.420 -16.411 1.00 60.41 C ANISOU 2226 CA TYR A 359 9228 6306 7419 -88 -63 54 C ATOM 2227 C TYR A 359 -3.412 -2.810 -16.854 1.00 60.46 C ANISOU 2227 C TYR A 359 9113 6306 7553 -145 -81 58 C ATOM 2228 O TYR A 359 -3.253 -3.788 -16.118 1.00 60.47 O ANISOU 2228 O TYR A 359 9193 6234 7546 -134 -52 64 O ATOM 2229 CB TYR A 359 -4.088 -0.665 -15.703 1.00 61.90 C ANISOU 2229 CB TYR A 359 9463 6421 7634 -22 140 165 C ATOM 2230 CG TYR A 359 -3.644 0.545 -14.894 1.00 62.78 C ANISOU 2230 CG TYR A 359 9809 6474 7569 52 179 161 C ATOM 2231 CD1 TYR A 359 -2.575 0.461 -14.015 1.00 63.62 C ANISOU 2231 CD1 TYR A 359 10173 6498 7502 73 74 111 C ATOM 2232 CD2 TYR A 359 -4.311 1.763 -14.989 1.00 63.82 C ANISOU 2232 CD2 TYR A 359 9923 6605 7721 94 296 218 C ATOM 2233 CE1 TYR A 359 -2.167 1.551 -13.269 1.00 64.64 C ANISOU 2233 CE1 TYR A 359 10567 6533 7460 127 51 109 C ATOM 2234 CE2 TYR A 359 -3.906 2.868 -14.248 1.00 64.53 C ANISOU 2234 CE2 TYR A 359 10270 6615 7631 162 320 208 C ATOM 2235 CZ TYR A 359 -2.831 2.753 -13.387 1.00 64.76 C ANISOU 2235 CZ TYR A 359 10587 6549 7467 174 181 149 C ATOM 2236 OH TYR A 359 -2.403 3.818 -12.632 1.00 64.57 O ANISOU 2236 OH TYR A 359 10872 6406 7254 227 143 139 O ATOM 2237 N ALA A 360 -3.981 -2.888 -18.055 1.00 60.52 N ANISOU 2237 N ALA A 360 8954 6369 7670 -211 -156 56 N ATOM 2238 CA ALA A 360 -4.400 -4.158 -18.637 1.00 60.88 C ANISOU 2238 CA ALA A 360 8918 6383 7829 -283 -235 51 C ATOM 2239 C ALA A 360 -3.282 -5.186 -18.522 1.00 60.33 C ANISOU 2239 C ALA A 360 8948 6302 7672 -283 -286 -41 C ATOM 2240 O ALA A 360 -3.529 -6.322 -18.117 1.00 61.39 O ANISOU 2240 O ALA A 360 9082 6367 7874 -300 -270 -22 O ATOM 2241 CB ALA A 360 -4.807 -3.975 -20.086 1.00 61.24 C ANISOU 2241 CB ALA A 360 8874 6468 7925 -361 -387 31 C ATOM 2242 N SER A 361 -2.055 -4.774 -18.835 1.00 58.81 N ANISOU 2242 N SER A 361 8819 6157 7366 -259 -334 -118 N ATOM 2243 CA SER A 361 -0.890 -5.623 -18.636 1.00 58.52 C ANISOU 2243 CA SER A 361 8848 6083 7301 -244 -361 -170 C ATOM 2244 C SER A 361 -0.960 -6.322 -17.288 1.00 59.63 C ANISOU 2244 C SER A 361 9062 6143 7452 -222 -314 -125 C ATOM 2245 O SER A 361 -0.931 -7.544 -17.225 1.00 60.33 O ANISOU 2245 O SER A 361 9148 6181 7590 -245 -321 -137 O ATOM 2246 CB SER A 361 0.396 -4.819 -18.713 1.00 57.64 C ANISOU 2246 CB SER A 361 8762 5993 7145 -203 -393 -190 C ATOM 2247 OG SER A 361 1.481 -5.556 -18.188 1.00 57.87 O ANISOU 2247 OG SER A 361 8827 5948 7212 -185 -424 -190 O ATOM 2248 N SER A 362 -1.072 -5.545 -16.217 1.00 60.41 N ANISOU 2248 N SER A 362 9261 6208 7483 -174 -263 -71 N ATOM 2249 CA SER A 362 -1.116 -6.117 -14.874 1.00 61.41 C ANISOU 2249 CA SER A 362 9539 6225 7566 -138 -208 -22 C ATOM 2250 C SER A 362 -2.302 -7.052 -14.625 1.00 62.47 C ANISOU 2250 C SER A 362 9619 6310 7805 -146 -81 41 C ATOM 2251 O SER A 362 -2.191 -7.987 -13.825 1.00 62.87 O ANISOU 2251 O SER A 362 9760 6276 7851 -131 -49 65 O ATOM 2252 CB SER A 362 -1.081 -5.017 -13.812 1.00 62.08 C ANISOU 2252 CB SER A 362 9835 6241 7508 -73 -168 21 C ATOM 2253 OG SER A 362 0.264 -4.692 -13.490 1.00 62.17 O ANISOU 2253 OG SER A 362 9960 6211 7449 -75 -348 -9 O ATOM 2254 N ALA A 363 -3.420 -6.811 -15.303 1.00 63.15 N ANISOU 2254 N ALA A 363 9545 6430 8018 -173 -26 87 N ATOM 2255 CA ALA A 363 -4.605 -7.671 -15.168 1.00 64.94 C ANISOU 2255 CA ALA A 363 9659 6582 8434 -193 68 186 C ATOM 2256 C ALA A 363 -4.530 -8.967 -16.006 1.00 65.83 C ANISOU 2256 C ALA A 363 9666 6694 8649 -281 -76 129 C ATOM 2257 O ALA A 363 -4.990 -10.014 -15.569 1.00 67.25 O ANISOU 2257 O ALA A 363 9815 6789 8946 -292 -29 187 O ATOM 2258 CB ALA A 363 -5.870 -6.888 -15.507 1.00 65.19 C ANISOU 2258 CB ALA A 363 9533 6602 8634 -195 156 301 C ATOM 2259 N ILE A 364 -3.968 -8.900 -17.205 1.00 65.76 N ANISOU 2259 N ILE A 364 9635 6760 8591 -335 -235 23 N ATOM 2260 CA ILE A 364 -3.896 -10.081 -18.053 1.00 67.39 C ANISOU 2260 CA ILE A 364 9822 6931 8851 -408 -363 -39 C ATOM 2261 C ILE A 364 -2.745 -11.011 -17.673 1.00 68.19 C ANISOU 2261 C ILE A 364 10026 7007 8873 -381 -356 -110 C ATOM 2262 O ILE A 364 -2.890 -12.232 -17.732 1.00 68.44 O ANISOU 2262 O ILE A 364 10054 6967 8981 -418 -389 -119 O ATOM 2263 CB ILE A 364 -3.799 -9.722 -19.550 1.00 67.68 C ANISOU 2263 CB ILE A 364 9872 7008 8834 -462 -510 -118 C ATOM 2264 CG1 ILE A 364 -2.460 -9.037 -19.872 1.00 66.88 C ANISOU 2264 CG1 ILE A 364 9868 6985 8559 -403 -483 -208 C ATOM 2265 CG2 ILE A 364 -5.011 -8.889 -19.956 1.00 68.28 C ANISOU 2265 CG2 ILE A 364 9825 7087 9031 -506 -562 -26 C ATOM 2266 CD1 ILE A 364 -2.408 -8.363 -21.231 1.00 67.60 C ANISOU 2266 CD1 ILE A 364 10001 7113 8568 -426 -565 -262 C ATOM 2267 N ASN A 365 -1.610 -10.439 -17.280 1.00 68.57 N ANISOU 2267 N ASN A 365 10153 7095 8804 -322 -331 -145 N ATOM 2268 CA ASN A 365 -0.414 -11.236 -16.986 1.00 69.00 C ANISOU 2268 CA ASN A 365 10270 7105 8841 -299 -347 -184 C ATOM 2269 C ASN A 365 -0.672 -12.458 -16.133 1.00 69.48 C ANISOU 2269 C ASN A 365 10351 7079 8966 -306 -316 -145 C ATOM 2270 O ASN A 365 -0.192 -13.524 -16.468 1.00 70.54 O ANISOU 2270 O ASN A 365 10488 7166 9145 -323 -343 -188 O ATOM 2271 CB ASN A 365 0.667 -10.394 -16.317 1.00 69.56 C ANISOU 2271 CB ASN A 365 10401 7181 8845 -246 -366 -167 C ATOM 2272 CG ASN A 365 1.500 -9.610 -17.314 1.00 70.33 C ANISOU 2272 CG ASN A 365 10458 7331 8932 -231 -395 -210 C ATOM 2273 OD1 ASN A 365 1.217 -9.604 -18.520 1.00 70.64 O ANISOU 2273 OD1 ASN A 365 10469 7407 8962 -252 -382 -261 O ATOM 2274 ND2 ASN A 365 2.534 -8.929 -16.811 1.00 70.49 N ANISOU 2274 ND2 ASN A 365 10496 7328 8960 -197 -450 -174 N ATOM 2275 N PRO A 366 -1.419 -12.312 -15.024 1.00 69.75 N ANISOU 2275 N PRO A 366 10420 7075 9004 -279 -231 -54 N ATOM 2276 CA PRO A 366 -1.706 -13.513 -14.259 1.00 70.27 C ANISOU 2276 CA PRO A 366 10509 7049 9139 -280 -180 -4 C ATOM 2277 C PRO A 366 -2.427 -14.568 -15.086 1.00 70.99 C ANISOU 2277 C PRO A 366 10477 7109 9385 -351 -220 -17 C ATOM 2278 O PRO A 366 -2.015 -15.724 -15.074 1.00 72.00 O ANISOU 2278 O PRO A 366 10620 7181 9554 -370 -252 -48 O ATOM 2279 CB PRO A 366 -2.588 -13.010 -13.105 1.00 70.98 C ANISOU 2279 CB PRO A 366 10678 7082 9210 -220 -21 114 C ATOM 2280 CG PRO A 366 -3.039 -11.654 -13.506 1.00 70.55 C ANISOU 2280 CG PRO A 366 10586 7093 9124 -206 8 126 C ATOM 2281 CD PRO A 366 -1.920 -11.111 -14.339 1.00 69.95 C ANISOU 2281 CD PRO A 366 10506 7110 8958 -229 -143 13 C ATOM 2282 N ILE A 367 -3.465 -14.182 -15.821 1.00 71.26 N ANISOU 2282 N ILE A 367 10401 7158 9516 -399 -248 12 N ATOM 2283 CA ILE A 367 -4.236 -15.174 -16.581 1.00 72.68 C ANISOU 2283 CA ILE A 367 10488 7261 9863 -488 -355 19 C ATOM 2284 C ILE A 367 -3.561 -15.648 -17.875 1.00 72.07 C ANISOU 2284 C ILE A 367 10499 7184 9700 -538 -508 -122 C ATOM 2285 O ILE A 367 -4.006 -16.612 -18.474 1.00 73.46 O ANISOU 2285 O ILE A 367 10679 7263 9968 -611 -627 -139 O ATOM 2286 CB ILE A 367 -5.671 -14.699 -16.885 1.00 74.59 C ANISOU 2286 CB ILE A 367 10568 7464 10307 -538 -382 142 C ATOM 2287 CG1 ILE A 367 -5.677 -13.468 -17.791 1.00 75.33 C ANISOU 2287 CG1 ILE A 367 10660 7645 10315 -554 -465 97 C ATOM 2288 CG2 ILE A 367 -6.402 -14.401 -15.582 1.00 75.29 C ANISOU 2288 CG2 ILE A 367 10591 7502 10514 -462 -149 311 C ATOM 2289 CD1 ILE A 367 -7.048 -13.114 -18.336 0.00 77.47 C ANISOU 2289 CD1 ILE A 367 10755 7851 10827 -629 -566 223 C ATOM 2290 N LEU A 368 -2.495 -14.976 -18.298 1.00 70.48 N ANISOU 2290 N LEU A 368 10389 7060 9331 -491 -494 -211 N ATOM 2291 CA LEU A 368 -1.788 -15.336 -19.521 1.00 69.95 C ANISOU 2291 CA LEU A 368 10449 6963 9165 -502 -558 -328 C ATOM 2292 C LEU A 368 -0.559 -16.175 -19.206 1.00 69.95 C ANISOU 2292 C LEU A 368 10513 6918 9146 -445 -473 -370 C ATOM 2293 O LEU A 368 -0.368 -17.246 -19.779 1.00 73.06 O ANISOU 2293 O LEU A 368 11004 7211 9544 -464 -494 -428 O ATOM 2294 CB LEU A 368 -1.393 -14.078 -20.297 1.00 68.94 C ANISOU 2294 CB LEU A 368 10364 6917 8911 -473 -556 -369 C ATOM 2295 CG LEU A 368 -0.919 -14.268 -21.738 1.00 69.75 C ANISOU 2295 CG LEU A 368 10655 6960 8886 -473 -592 -473 C ATOM 2296 CD1 LEU A 368 -1.889 -15.122 -22.543 1.00 71.71 C ANISOU 2296 CD1 LEU A 368 11015 7081 9148 -572 -774 -503 C ATOM 2297 CD2 LEU A 368 -0.730 -12.919 -22.412 1.00 69.26 C ANISOU 2297 CD2 LEU A 368 10617 6980 8716 -444 -580 -485 C ATOM 2298 N TYR A 369 0.269 -15.707 -18.283 1.00 68.08 N ANISOU 2298 N TYR A 369 10235 6729 8902 -380 -394 -327 N ATOM 2299 CA TYR A 369 1.428 -16.483 -17.848 1.00 67.99 C ANISOU 2299 CA TYR A 369 10241 6652 8938 -335 -343 -326 C ATOM 2300 C TYR A 369 1.075 -17.784 -17.115 1.00 69.62 C ANISOU 2300 C TYR A 369 10439 6778 9233 -362 -347 -295 C ATOM 2301 O TYR A 369 1.977 -18.550 -16.779 1.00 69.80 O ANISOU 2301 O TYR A 369 10471 6731 9316 -331 -316 -286 O ATOM 2302 CB TYR A 369 2.325 -15.649 -16.932 1.00 66.49 C ANISOU 2302 CB TYR A 369 10016 6494 8750 -282 -338 -260 C ATOM 2303 CG TYR A 369 3.283 -14.742 -17.654 1.00 65.04 C ANISOU 2303 CG TYR A 369 9815 6335 8559 -236 -313 -272 C ATOM 2304 CD1 TYR A 369 2.892 -13.464 -18.070 1.00 64.58 C ANISOU 2304 CD1 TYR A 369 9751 6372 8415 -238 -327 -284 C ATOM 2305 CD2 TYR A 369 4.589 -15.146 -17.900 1.00 64.69 C ANISOU 2305 CD2 TYR A 369 9741 6203 8634 -184 -256 -248 C ATOM 2306 CE1 TYR A 369 3.775 -12.621 -18.732 1.00 63.67 C ANISOU 2306 CE1 TYR A 369 9610 6269 8310 -190 -290 -280 C ATOM 2307 CE2 TYR A 369 5.478 -14.318 -18.554 1.00 64.85 C ANISOU 2307 CE2 TYR A 369 9717 6218 8702 -130 -198 -223 C ATOM 2308 CZ TYR A 369 5.067 -13.058 -18.969 1.00 64.22 C ANISOU 2308 CZ TYR A 369 9642 6241 8516 -134 -217 -244 C ATOM 2309 OH TYR A 369 5.955 -12.244 -19.614 1.00 63.88 O ANISOU 2309 OH TYR A 369 9548 6184 8540 -75 -145 -206 O ATOM 2310 N ASN A 370 -0.208 -18.036 -16.849 1.00 71.12 N ANISOU 2310 N ASN A 370 10591 6960 9469 -415 -379 -257 N ATOM 2311 CA ASN A 370 -0.595 -19.216 -16.075 1.00 72.70 C ANISOU 2311 CA ASN A 370 10768 7077 9777 -435 -364 -204 C ATOM 2312 C ASN A 370 -1.801 -19.993 -16.591 1.00 74.04 C ANISOU 2312 C ASN A 370 10894 7170 10067 -517 -439 -194 C ATOM 2313 O ASN A 370 -2.315 -20.845 -15.870 1.00 74.56 O ANISOU 2313 O ASN A 370 10907 7164 10257 -533 -412 -120 O ATOM 2314 CB ASN A 370 -0.869 -18.801 -14.624 1.00 73.54 C ANISOU 2314 CB ASN A 370 10868 7196 9878 -392 -287 -93 C ATOM 2315 CG ASN A 370 0.361 -18.234 -13.935 1.00 74.19 C ANISOU 2315 CG ASN A 370 11030 7296 9860 -331 -290 -85 C ATOM 2316 OD1 ASN A 370 1.301 -18.972 -13.628 1.00 75.61 O ANISOU 2316 OD1 ASN A 370 11235 7413 10077 -316 -316 -86 O ATOM 2317 ND2 ASN A 370 0.363 -16.920 -13.686 1.00 73.55 N ANISOU 2317 ND2 ASN A 370 10987 7279 9679 -301 -287 -64 N ATOM 2318 N LEU A 371 -2.266 -19.730 -17.813 1.00 75.25 N ANISOU 2318 N LEU A 371 11079 7312 10198 -575 -554 -253 N ATOM 2319 CA LEU A 371 -3.474 -20.422 -18.295 1.00 77.07 C ANISOU 2319 CA LEU A 371 11267 7430 10585 -677 -704 -218 C ATOM 2320 C LEU A 371 -3.188 -21.843 -18.777 1.00 78.02 C ANISOU 2320 C LEU A 371 11510 7412 10721 -715 -780 -295 C ATOM 2321 O LEU A 371 -4.037 -22.716 -18.650 1.00 79.21 O ANISOU 2321 O LEU A 371 11593 7446 11055 -789 -880 -232 O ATOM 2322 CB LEU A 371 -4.253 -19.609 -19.352 1.00 77.48 C ANISOU 2322 CB LEU A 371 11326 7481 10631 -747 -868 -224 C ATOM 2323 CG LEU A 371 -3.666 -19.248 -20.721 1.00 77.62 C ANISOU 2323 CG LEU A 371 11568 7492 10431 -751 -958 -364 C ATOM 2324 CD1 LEU A 371 -3.821 -20.390 -21.703 1.00 80.00 C ANISOU 2324 CD1 LEU A 371 12081 7608 10705 -827 -1140 -447 C ATOM 2325 CD2 LEU A 371 -4.362 -18.035 -21.306 1.00 78.12 C ANISOU 2325 CD2 LEU A 371 11590 7608 10484 -791 -1067 -329 C ATOM 2326 N VAL A 372 -1.990 -22.069 -19.308 1.00 80.43 N ANISOU 2326 N VAL A 372 9849 10571 10136 -567 -176 -230 N ATOM 2327 CA VAL A 372 -1.608 -23.391 -19.818 1.00 82.10 C ANISOU 2327 CA VAL A 372 10047 10798 10347 -562 -193 -226 C ATOM 2328 C VAL A 372 -1.194 -24.378 -18.729 1.00 83.91 C ANISOU 2328 C VAL A 372 10129 11090 10662 -639 -300 -261 C ATOM 2329 O VAL A 372 -0.989 -25.564 -19.018 1.00 85.74 O ANISOU 2329 O VAL A 372 10377 11330 10870 -625 -320 -257 O ATOM 2330 CB VAL A 372 -0.466 -23.320 -20.853 1.00 82.91 C ANISOU 2330 CB VAL A 372 10226 10765 10512 -528 23 -188 C ATOM 2331 CG1 VAL A 372 -0.957 -22.644 -22.122 1.00 83.73 C ANISOU 2331 CG1 VAL A 372 10607 10769 10435 -375 145 -137 C ATOM 2332 CG2 VAL A 372 0.769 -22.627 -20.278 1.00 83.75 C ANISOU 2332 CG2 VAL A 372 10160 10790 10871 -640 151 -220 C ATOM 2333 N SER A 373 -1.047 -23.895 -17.495 1.00 84.92 N ANISOU 2333 N SER A 373 10170 11238 10857 -684 -369 -299 N ATOM 2334 CA SER A 373 -0.788 -24.769 -16.342 1.00 84.88 C ANISOU 2334 CA SER A 373 10116 11273 10859 -684 -489 -333 C ATOM 2335 C SER A 373 -1.917 -25.792 -16.138 1.00 84.51 C ANISOU 2335 C SER A 373 10148 11270 10691 -677 -518 -303 C ATOM 2336 O SER A 373 -3.031 -25.636 -16.661 1.00 83.21 O ANISOU 2336 O SER A 373 10002 11135 10476 -689 -501 -288 O ATOM 2337 CB SER A 373 -0.587 -23.942 -15.061 1.00 85.18 C ANISOU 2337 CB SER A 373 10131 11300 10931 -684 -584 -392 C ATOM 2338 OG SER A 373 0.651 -23.242 -15.074 1.00 86.27 O ANISOU 2338 OG SER A 373 10139 11380 11258 -725 -589 -473 O ATOM 2339 N ALA A 374 -1.608 -26.802 -15.349 1.00 85.21 N ANISOU 2339 N ALA A 374 10279 11346 10750 -648 -558 -310 N ATOM 2340 CA ALA A 374 -2.479 -27.925 -15.116 1.00 85.19 C ANISOU 2340 CA ALA A 374 10368 11325 10674 -671 -516 -286 C ATOM 2341 C ALA A 374 -3.696 -27.664 -14.275 1.00 85.88 C ANISOU 2341 C ALA A 374 10482 11412 10733 -691 -468 -272 C ATOM 2342 O ALA A 374 -4.819 -27.770 -14.725 1.00 85.26 O ANISOU 2342 O ALA A 374 10326 11369 10697 -756 -428 -277 O ATOM 2343 CB ALA A 374 -1.694 -29.014 -14.412 0.00 20.00 C ATOM 2344 N ASN A 375 -3.458 -27.359 -13.019 1.00 87.46 N ANISOU 2344 N ASN A 375 10799 11569 10863 -605 -477 -265 N ATOM 2345 CA ASN A 375 -4.546 -27.173 -12.098 1.00 89.81 C ANISOU 2345 CA ASN A 375 11180 11830 11112 -585 -371 -231 C ATOM 2346 C ASN A 375 -5.097 -25.769 -12.205 1.00 90.86 C ANISOU 2346 C ASN A 375 11204 12031 11285 -599 -386 -234 C ATOM 2347 O ASN A 375 -6.303 -25.508 -12.136 1.00 89.40 O ANISOU 2347 O ASN A 375 10949 11872 11147 -634 -277 -213 O ATOM 2348 CB ASN A 375 -4.038 -27.326 -10.670 0.00 20.00 C ATOM 2349 CG ASN A 375 -3.242 -28.609 -10.477 0.00 20.00 C ATOM 2350 OD1 ASN A 375 -3.538 -29.638 -11.089 0.00 20.00 O ATOM 2351 ND2 ASN A 375 -2.222 -28.551 -9.630 0.00 20.00 N ATOM 2352 N PHE A 376 -4.166 -24.865 -12.394 1.00 91.43 N ANISOU 2352 N PHE A 376 11254 12121 11363 -568 -509 -273 N ATOM 2353 CA PHE A 376 -4.485 -23.435 -12.501 1.00 91.78 C ANISOU 2353 CA PHE A 376 11263 12188 11419 -564 -514 -277 C ATOM 2354 C PHE A 376 -5.722 -23.173 -13.374 1.00 92.34 C ANISOU 2354 C PHE A 376 11234 12332 11520 -586 -437 -248 C ATOM 2355 O PHE A 376 -6.567 -22.337 -13.025 1.00 93.34 O ANISOU 2355 O PHE A 376 11374 12474 11614 -527 -387 -227 O ATOM 2356 CB PHE A 376 -3.270 -22.707 -13.098 1.00 91.26 C ANISOU 2356 CB PHE A 376 11137 12099 11435 -598 -591 -332 C ATOM 2357 CG PHE A 376 -2.788 -21.550 -12.270 1.00 90.41 C ANISOU 2357 CG PHE A 376 11099 11924 11327 -571 -665 -393 C ATOM 2358 CD1 PHE A 376 -3.626 -20.472 -11.996 1.00 90.38 C ANISOU 2358 CD1 PHE A 376 11190 11900 11247 -530 -608 -364 C ATOM 2359 CD2 PHE A 376 -1.496 -21.535 -11.767 1.00 90.48 C ANISOU 2359 CD2 PHE A 376 11070 11885 11422 -573 -812 -502 C ATOM 2360 CE1 PHE A 376 -3.184 -19.408 -11.232 1.00 90.02 C ANISOU 2360 CE1 PHE A 376 11251 11762 11189 -509 -682 -435 C ATOM 2361 CE2 PHE A 376 -1.049 -20.470 -11.007 1.00 91.92 C ANISOU 2361 CE2 PHE A 376 11309 11987 11629 -564 -924 -604 C ATOM 2362 CZ PHE A 376 -1.896 -19.405 -10.739 1.00 91.50 C ANISOU 2362 CZ PHE A 376 11400 11888 11476 -540 -852 -566 C ATOM 2363 N ARG A 377 -5.836 -23.910 -14.475 1.00 91.56 N ANISOU 2363 N ARG A 377 11046 12272 11470 -637 -454 -262 N ATOM 2364 CA ARG A 377 -7.027 -23.850 -15.309 1.00 93.24 C ANISOU 2364 CA ARG A 377 11148 12561 11716 -629 -459 -285 C ATOM 2365 C ARG A 377 -8.258 -23.954 -14.418 1.00 95.26 C ANISOU 2365 C ARG A 377 11318 12842 12034 -632 -362 -280 C ATOM 2366 O ARG A 377 -9.129 -23.085 -14.442 1.00 95.95 O ANISOU 2366 O ARG A 377 11325 12994 12134 -552 -355 -289 O ATOM 2367 CB ARG A 377 -7.021 -24.980 -16.340 1.00 93.35 C ANISOU 2367 CB ARG A 377 11122 12579 11766 -687 -516 -331 C ATOM 2368 CG ARG A 377 -8.383 -25.271 -16.949 1.00 93.38 C ANISOU 2368 CG ARG A 377 10974 12651 11854 -706 -579 -415 C ATOM 2369 CD ARG A 377 -8.882 -24.095 -17.773 1.00 93.54 C ANISOU 2369 CD ARG A 377 10953 12758 11830 -558 -674 -450 C ATOM 2370 NE ARG A 377 -9.983 -24.473 -18.654 1.00 94.94 N ANISOU 2370 NE ARG A 377 10977 13009 12086 -535 -834 -585 N ATOM 2371 CZ ARG A 377 -11.246 -24.599 -18.261 0.00 20.00 C ATOM 2372 NH1 ARG A 377 -11.573 -24.378 -16.995 1.00 84.77 N ANISOU 2372 NH1 ARG A 377 9283 11839 11085 -546 -657 -610 N ATOM 2373 NH2 ARG A 377 -12.183 -24.948 -19.132 1.00 86.77 N ANISOU 2373 NH2 ARG A 377 9451 12151 11366 -516 -1114 -889 N ATOM 2374 N GLN A 378 -8.280 -24.981 -13.590 1.00 95.84 N ANISOU 2374 N GLN A 378 11429 12842 12142 -700 -251 -261 N ATOM 2375 CA GLN A 378 -9.333 -25.119 -12.621 1.00 96.55 C ANISOU 2375 CA GLN A 378 11486 12895 12303 -702 -56 -233 C ATOM 2376 C GLN A 378 -9.322 -24.052 -11.558 1.00 96.66 C ANISOU 2376 C GLN A 378 11666 12871 12186 -564 7 -166 C ATOM 2377 O GLN A 378 -10.342 -23.498 -11.166 1.00 98.09 O ANISOU 2377 O GLN A 378 11772 13083 12415 -502 123 -147 O ATOM 2378 CB GLN A 378 -9.101 -26.389 -11.819 0.00 20.00 C ATOM 2379 CG GLN A 378 -9.443 -27.664 -12.571 0.00 20.00 C ATOM 2380 CD GLN A 378 -10.464 -28.511 -11.844 0.00 20.00 C ATOM 2381 OE1 GLN A 378 -10.116 -29.497 -11.196 0.00 20.00 O ATOM 2382 NE2 GLN A 378 -11.733 -28.134 -11.952 0.00 20.00 N ATOM 2383 N VAL A 379 -8.124 -23.772 -11.095 1.00 94.57 N ANISOU 2383 N VAL A 379 11620 12540 11771 -503 -86 -152 N ATOM 2384 CA VAL A 379 -7.927 -22.877 -9.960 1.00 93.71 C ANISOU 2384 CA VAL A 379 11729 12361 11515 -366 -81 -123 C ATOM 2385 C VAL A 379 -8.719 -21.577 -10.064 1.00 93.75 C ANISOU 2385 C VAL A 379 11681 12420 11517 -294 -44 -107 C ATOM 2386 O VAL A 379 -9.508 -21.249 -9.178 1.00 95.40 O ANISOU 2386 O VAL A 379 11968 12586 11690 -196 133 -51 O ATOM 2387 CB VAL A 379 -6.451 -22.444 -9.866 1.00 91.79 C ANISOU 2387 CB VAL A 379 11611 12075 11187 -337 -297 -184 C ATOM 2388 CG1 VAL A 379 -6.263 -21.446 -8.734 0.00 20.00 C ATOM 2389 CG2 VAL A 379 -5.554 -23.657 -9.672 0.00 20.00 C ATOM 2390 N PHE A 380 -8.500 -20.801 -11.111 1.00 92.20 N ANISOU 2390 N PHE A 380 11392 12296 11344 -314 -172 -144 N ATOM 2391 CA PHE A 380 -9.199 -19.519 -11.249 1.00 92.65 C ANISOU 2391 CA PHE A 380 11450 12390 11360 -204 -143 -127 C ATOM 2392 C PHE A 380 -10.661 -19.780 -11.573 1.00 93.89 C ANISOU 2392 C PHE A 380 11384 12660 11629 -152 -36 -118 C ATOM 2393 O PHE A 380 -11.513 -18.913 -11.434 1.00 93.18 O ANISOU 2393 O PHE A 380 11306 12592 11503 -8 48 -88 O ATOM 2394 CB PHE A 380 -8.553 -18.699 -12.369 0.00 20.00 C ATOM 2395 CG PHE A 380 -8.566 -17.198 -12.162 0.00 20.00 C ATOM 2396 CD1 PHE A 380 -7.942 -16.616 -11.085 0.00 20.00 C ATOM 2397 CD2 PHE A 380 -9.155 -16.365 -13.109 0.00 20.00 C ATOM 2398 CE1 PHE A 380 -7.942 -15.238 -10.934 0.00 20.00 C ATOM 2399 CE2 PHE A 380 -9.157 -14.987 -12.961 0.00 20.00 C ATOM 2400 CZ PHE A 380 -8.551 -14.421 -11.869 0.00 20.00 C ATOM 2401 N LEU A 381 -10.931 -20.993 -12.026 1.00 94.97 N ANISOU 2401 N LEU A 381 11300 12860 11923 -265 -50 -165 N ATOM 2402 CA LEU A 381 -12.289 -21.427 -12.314 1.00 96.87 C ANISOU 2402 CA LEU A 381 11246 13197 12363 -265 31 -210 C ATOM 2403 C LEU A 381 -12.977 -21.808 -11.016 1.00 99.25 C ANISOU 2403 C LEU A 381 11537 13415 12757 -267 331 -148 C ATOM 2404 O LEU A 381 -14.180 -22.030 -10.997 1.00101.68 O ANISOU 2404 O LEU A 381 11563 13790 13278 -250 460 -185 O ATOM 2405 CB LEU A 381 -12.283 -22.617 -13.287 0.00 20.00 C ATOM 2406 CG LEU A 381 -13.577 -23.341 -13.726 0.00 20.00 C ATOM 2407 CD1 LEU A 381 -14.563 -22.476 -14.501 0.00 20.00 C ATOM 2408 CD2 LEU A 381 -13.304 -24.645 -14.467 0.00 20.00 C ATOM 2409 N SER A 382 -12.203 -21.871 -9.934 1.00 98.46 N ANISOU 2409 N SER A 382 11748 13156 12503 -264 446 -66 N ATOM 2410 CA SER A 382 -12.730 -22.130 -8.605 1.00 99.09 C ANISOU 2410 CA SER A 382 11973 13094 12581 -201 778 21 C ATOM 2411 C SER A 382 -12.709 -20.880 -7.760 1.00 98.78 C ANISOU 2411 C SER A 382 12212 12992 12328 19 851 100 C ATOM 2412 O SER A 382 -12.611 -20.962 -6.549 1.00100.85 O ANISOU 2412 O SER A 382 12729 13092 12495 129 1121 189 O ATOM 2413 CB SER A 382 -11.901 -23.195 -7.897 1.00 98.28 C ANISOU 2413 CB SER A 382 12145 12820 12375 -255 859 59 C ATOM 2414 OG SER A 382 -11.837 -24.396 -8.635 0.00 20.00 O ATOM 2415 N THR A 383 -12.775 -19.716 -8.388 1.00102.06 N ANISOU 2415 N THR A 383 13881 13397 11499 1263 3670 -1808 N ATOM 2416 CA THR A 383 -12.817 -18.467 -7.622 1.00103.62 C ANISOU 2416 CA THR A 383 14249 13677 11445 1426 3641 -2136 C ATOM 2417 C THR A 383 -14.111 -17.710 -7.913 1.00103.56 C ANISOU 2417 C THR A 383 14077 13420 11851 1389 3825 -2194 C ATOM 2418 O THR A 383 -14.892 -17.417 -7.007 1.00106.14 O ANISOU 2418 O THR A 383 14487 13781 12057 1631 4155 -2210 O ATOM 2419 CB THR A 383 -11.622 -17.552 -7.961 1.00102.12 C ANISOU 2419 CB THR A 383 14128 13535 11136 1291 3152 -2483 C ATOM 2420 OG1 THR A 383 -11.819 -16.957 -9.248 1.00 99.90 O ANISOU 2420 OG1 THR A 383 13628 12986 11343 997 2944 -2554 O ATOM 2421 CG2 THR A 383 -10.308 -18.338 -7.963 1.00100.75 C ANISOU 2421 CG2 THR A 383 14046 13550 10684 1260 2917 -2417 C ATOM 2422 N ASN A1002 7.702 -32.058 -31.490 1.00 38.99 N ANISOU 2422 N ASN A1002 5306 4997 4510 -621 377 -104 N ATOM 2423 CA ASN A1002 7.613 -32.776 -32.731 1.00 40.05 C ANISOU 2423 CA ASN A1002 5532 5106 4577 -457 345 -67 C ATOM 2424 C ASN A1002 8.288 -34.116 -32.607 1.00 40.40 C ANISOU 2424 C ASN A1002 5493 5236 4621 -469 313 -31 C ATOM 2425 O ASN A1002 7.708 -35.118 -32.869 1.00 39.30 O ANISOU 2425 O ASN A1002 5344 5095 4492 -391 207 -70 O ATOM 2426 CB ASN A1002 8.282 -31.988 -33.847 1.00 40.98 C ANISOU 2426 CB ASN A1002 5780 5150 4639 -346 471 21 C ATOM 2427 CG ASN A1002 7.440 -30.855 -34.362 1.00 41.23 C ANISOU 2427 CG ASN A1002 5919 5080 4667 -288 490 1 C ATOM 2428 OD1 ASN A1002 6.386 -30.597 -33.885 1.00 41.17 O ANISOU 2428 OD1 ASN A1002 5889 5052 4701 -325 395 -95 O ATOM 2429 ND2 ASN A1002 7.924 -30.187 -35.338 1.00 42.78 N ANISOU 2429 ND2 ASN A1002 6229 5200 4823 -184 635 111 N ATOM 2430 N ILE A1003 9.536 -34.108 -32.194 1.00 41.63 N ANISOU 2430 N ILE A1003 5566 5448 4804 -566 393 31 N ATOM 2431 CA ILE A1003 10.324 -35.328 -32.040 1.00 42.09 C ANISOU 2431 CA ILE A1003 5542 5579 4871 -573 372 77 C ATOM 2432 C ILE A1003 9.835 -36.271 -30.925 1.00 41.74 C ANISOU 2432 C ILE A1003 5391 5610 4858 -638 273 48 C ATOM 2433 O ILE A1003 9.839 -37.477 -31.117 1.00 41.43 O ANISOU 2433 O ILE A1003 5315 5586 4839 -583 220 69 O ATOM 2434 CB ILE A1003 11.866 -35.053 -31.954 1.00 43.51 C ANISOU 2434 CB ILE A1003 5646 5777 5109 -643 481 152 C ATOM 2435 CG1 ILE A1003 12.656 -36.364 -32.035 1.00 43.39 C ANISOU 2435 CG1 ILE A1003 5561 5822 5103 -617 461 204 C ATOM 2436 CG2 ILE A1003 12.279 -34.345 -30.668 1.00 43.80 C ANISOU 2436 CG2 ILE A1003 5564 5852 5223 -805 465 107 C ATOM 2437 CD1 ILE A1003 12.394 -37.176 -33.281 1.00 43.26 C ANISOU 2437 CD1 ILE A1003 5653 5772 5011 -437 454 218 C ATOM 2438 N PHE A1004 9.375 -35.767 -29.788 1.00 42.29 N ANISOU 2438 N PHE A1004 5414 5717 4934 -734 260 8 N ATOM 2439 CA PHE A1004 8.751 -36.683 -28.828 1.00 42.97 C ANISOU 2439 CA PHE A1004 5425 5860 5041 -750 210 17 C ATOM 2440 C PHE A1004 7.606 -37.492 -29.451 1.00 43.54 C ANISOU 2440 C PHE A1004 5502 5843 5195 -651 153 -2 C ATOM 2441 O PHE A1004 7.493 -38.688 -29.196 1.00 44.80 O ANISOU 2441 O PHE A1004 5578 6010 5432 -630 123 42 O ATOM 2442 CB PHE A1004 8.217 -35.991 -27.573 1.00 43.30 C ANISOU 2442 CB PHE A1004 5452 5953 5047 -819 227 -23 C ATOM 2443 CG PHE A1004 7.490 -36.938 -26.639 1.00 44.02 C ANISOU 2443 CG PHE A1004 5480 6087 5158 -801 232 27 C ATOM 2444 CD1 PHE A1004 8.187 -37.663 -25.672 1.00 44.78 C ANISOU 2444 CD1 PHE A1004 5518 6301 5195 -816 233 105 C ATOM 2445 CD2 PHE A1004 6.122 -37.143 -26.758 1.00 44.47 C ANISOU 2445 CD2 PHE A1004 5525 6050 5319 -754 243 10 C ATOM 2446 CE1 PHE A1004 7.532 -38.547 -24.822 1.00 45.39 C ANISOU 2446 CE1 PHE A1004 5545 6406 5293 -776 280 194 C ATOM 2447 CE2 PHE A1004 5.463 -38.039 -25.923 1.00 45.41 C ANISOU 2447 CE2 PHE A1004 5563 6177 5512 -731 294 90 C ATOM 2448 CZ PHE A1004 6.172 -38.741 -24.953 1.00 45.77 C ANISOU 2448 CZ PHE A1004 5568 6344 5475 -737 329 197 C ATOM 2449 N GLU A1005 6.741 -36.850 -30.227 1.00 43.87 N ANISOU 2449 N GLU A1005 5627 5786 5254 -585 125 -75 N ATOM 2450 CA GLU A1005 5.608 -37.555 -30.819 1.00 45.05 C ANISOU 2450 CA GLU A1005 5761 5828 5525 -478 26 -136 C ATOM 2451 C GLU A1005 6.062 -38.582 -31.832 1.00 43.57 C ANISOU 2451 C GLU A1005 5588 5614 5351 -363 -50 -141 C ATOM 2452 O GLU A1005 5.583 -39.713 -31.832 1.00 43.51 O ANISOU 2452 O GLU A1005 5483 5551 5498 -319 -130 -163 O ATOM 2453 CB GLU A1005 4.648 -36.610 -31.520 1.00 48.19 C ANISOU 2453 CB GLU A1005 6256 6126 5929 -404 -21 -229 C ATOM 2454 CG GLU A1005 3.820 -35.738 -30.595 1.00 51.32 C ANISOU 2454 CG GLU A1005 6620 6509 6369 -489 32 -256 C ATOM 2455 CD GLU A1005 2.732 -34.993 -31.356 1.00 55.78 C ANISOU 2455 CD GLU A1005 7258 6950 6985 -396 -43 -355 C ATOM 2456 OE1 GLU A1005 2.848 -33.754 -31.522 1.00 59.34 O ANISOU 2456 OE1 GLU A1005 7806 7395 7345 -411 7 -365 O ATOM 2457 OE2 GLU A1005 1.770 -35.654 -31.816 1.00 58.93 O ANISOU 2457 OE2 GLU A1005 7607 7241 7543 -299 -166 -431 O ATOM 2458 N MET A1006 6.987 -38.183 -32.691 1.00 41.57 N ANISOU 2458 N MET A1006 5449 5387 4956 -304 -11 -120 N ATOM 2459 CA MET A1006 7.431 -39.043 -33.767 1.00 41.02 C ANISOU 2459 CA MET A1006 5430 5296 4856 -157 -70 -137 C ATOM 2460 C MET A1006 8.143 -40.269 -33.212 1.00 39.96 C ANISOU 2460 C MET A1006 5161 5218 4804 -217 -65 -74 C ATOM 2461 O MET A1006 7.860 -41.385 -33.645 1.00 39.68 O ANISOU 2461 O MET A1006 5078 5125 4871 -121 -173 -130 O ATOM 2462 CB MET A1006 8.323 -38.280 -34.741 1.00 41.79 C ANISOU 2462 CB MET A1006 5687 5411 4778 -67 32 -89 C ATOM 2463 CG MET A1006 7.597 -37.130 -35.435 1.00 43.15 C ANISOU 2463 CG MET A1006 6016 5516 4863 34 27 -133 C ATOM 2464 SD MET A1006 8.670 -36.093 -36.442 1.00 44.65 S ANISOU 2464 SD MET A1006 6384 5705 4874 138 226 -11 S ATOM 2465 CE MET A1006 9.542 -37.384 -37.348 1.00 45.70 C ANISOU 2465 CE MET A1006 6563 5876 4925 309 224 7 C ATOM 2466 N LEU A1007 9.044 -40.063 -32.252 1.00 38.49 N ANISOU 2466 N LEU A1007 4903 5130 4590 -363 38 25 N ATOM 2467 CA LEU A1007 9.791 -41.174 -31.652 1.00 38.52 C ANISOU 2467 CA LEU A1007 4781 5193 4659 -414 42 101 C ATOM 2468 C LEU A1007 8.946 -42.075 -30.762 1.00 38.37 C ANISOU 2468 C LEU A1007 4633 5150 4795 -447 -6 120 C ATOM 2469 O LEU A1007 9.206 -43.256 -30.646 1.00 39.00 O ANISOU 2469 O LEU A1007 4616 5220 4982 -427 -35 164 O ATOM 2470 CB LEU A1007 11.009 -40.672 -30.868 1.00 38.42 C ANISOU 2470 CB LEU A1007 4726 5288 4582 -536 132 185 C ATOM 2471 CG LEU A1007 12.202 -40.198 -31.706 1.00 38.28 C ANISOU 2471 CG LEU A1007 4764 5273 4507 -506 219 214 C ATOM 2472 CD1 LEU A1007 13.211 -39.523 -30.812 1.00 38.53 C ANISOU 2472 CD1 LEU A1007 4716 5372 4551 -641 275 258 C ATOM 2473 CD2 LEU A1007 12.867 -41.328 -32.461 1.00 38.88 C ANISOU 2473 CD2 LEU A1007 4822 5339 4610 -407 212 241 C ATOM 2474 N ARG A1008 7.920 -41.522 -30.153 1.00 38.96 N ANISOU 2474 N ARG A1008 4699 5198 4904 -489 5 98 N ATOM 2475 CA ARG A1008 7.021 -42.298 -29.318 1.00 39.70 C ANISOU 2475 CA ARG A1008 4666 5242 5174 -505 11 142 C ATOM 2476 C ARG A1008 6.199 -43.277 -30.158 1.00 39.91 C ANISOU 2476 C ARG A1008 4620 5105 5438 -396 -104 60 C ATOM 2477 O ARG A1008 5.777 -44.327 -29.662 1.00 40.47 O ANISOU 2477 O ARG A1008 4541 5103 5733 -396 -96 120 O ATOM 2478 CB ARG A1008 6.151 -41.337 -28.519 1.00 40.44 C ANISOU 2478 CB ARG A1008 4778 5343 5241 -560 78 134 C ATOM 2479 CG ARG A1008 5.105 -41.961 -27.636 1.00 42.17 C ANISOU 2479 CG ARG A1008 4873 5497 5653 -561 141 202 C ATOM 2480 CD ARG A1008 5.678 -42.893 -26.583 1.00 43.89 C ANISOU 2480 CD ARG A1008 5006 5799 5869 -583 228 370 C ATOM 2481 NE ARG A1008 4.568 -43.491 -25.846 1.00 45.94 N ANISOU 2481 NE ARG A1008 5143 5959 6349 -559 333 464 N ATOM 2482 CZ ARG A1008 3.795 -44.478 -26.304 1.00 46.74 C ANISOU 2482 CZ ARG A1008 5096 5870 6793 -509 301 459 C ATOM 2483 NH1 ARG A1008 4.003 -45.039 -27.495 1.00 45.87 N ANISOU 2483 NH1 ARG A1008 4958 5664 6806 -462 137 343 N ATOM 2484 NH2 ARG A1008 2.796 -44.912 -25.552 1.00 49.50 N ANISOU 2484 NH2 ARG A1008 5314 6111 7380 -493 440 568 N ATOM 2485 N ILE A1009 5.996 -42.935 -31.431 1.00 39.66 N ANISOU 2485 N ILE A1009 4695 5006 5367 -286 -215 -78 N ATOM 2486 CA ILE A1009 5.422 -43.848 -32.414 1.00 39.77 C ANISOU 2486 CA ILE A1009 4665 4872 5572 -143 -382 -210 C ATOM 2487 C ILE A1009 6.469 -44.841 -32.923 1.00 39.70 C ANISOU 2487 C ILE A1009 4647 4893 5542 -82 -414 -196 C ATOM 2488 O ILE A1009 6.208 -46.027 -32.979 1.00 39.80 O ANISOU 2488 O ILE A1009 4520 4800 5799 -38 -497 -227 O ATOM 2489 CB ILE A1009 4.830 -43.078 -33.614 1.00 40.22 C ANISOU 2489 CB ILE A1009 4878 4863 5538 1 -512 -377 C ATOM 2490 CG1 ILE A1009 3.675 -42.207 -33.165 1.00 40.67 C ANISOU 2490 CG1 ILE A1009 4918 4859 5676 -46 -502 -410 C ATOM 2491 CG2 ILE A1009 4.308 -44.019 -34.697 1.00 41.57 C ANISOU 2491 CG2 ILE A1009 5025 4889 5880 192 -737 -560 C ATOM 2492 CD1 ILE A1009 2.522 -42.996 -32.589 1.00 42.09 C ANISOU 2492 CD1 ILE A1009 4878 4881 6233 -70 -547 -436 C ATOM 2493 N ASP A1010 7.654 -44.350 -33.278 1.00 39.81 N ANISOU 2493 N ASP A1010 4791 5033 5301 -80 -336 -145 N ATOM 2494 CA ASP A1010 8.667 -45.153 -33.968 1.00 40.00 C ANISOU 2494 CA ASP A1010 4833 5080 5282 7 -355 -147 C ATOM 2495 C ASP A1010 9.460 -46.068 -33.040 1.00 40.74 C ANISOU 2495 C ASP A1010 4771 5229 5477 -102 -284 -7 C ATOM 2496 O ASP A1010 9.823 -47.179 -33.417 1.00 40.93 O ANISOU 2496 O ASP A1010 4726 5207 5615 -30 -344 -30 O ATOM 2497 CB ASP A1010 9.611 -44.254 -34.776 1.00 39.42 C ANISOU 2497 CB ASP A1010 4948 5094 4935 72 -262 -129 C ATOM 2498 CG ASP A1010 8.937 -43.642 -36.019 1.00 39.85 C ANISOU 2498 CG ASP A1010 5192 5085 4862 268 -352 -267 C ATOM 2499 OD1 ASP A1010 7.927 -44.170 -36.515 1.00 40.12 O ANISOU 2499 OD1 ASP A1010 5216 5007 5020 396 -542 -425 O ATOM 2500 OD2 ASP A1010 9.414 -42.611 -36.508 1.00 39.91 O ANISOU 2500 OD2 ASP A1010 5357 5144 4661 309 -237 -218 O ATOM 2501 N GLU A1011 9.718 -45.615 -31.825 1.00 41.86 N ANISOU 2501 N GLU A1011 4863 5467 5574 -256 -171 126 N ATOM 2502 CA GLU A1011 10.427 -46.434 -30.857 1.00 43.28 C ANISOU 2502 CA GLU A1011 4913 5709 5822 -336 -117 269 C ATOM 2503 C GLU A1011 9.491 -47.178 -29.904 1.00 44.48 C ANISOU 2503 C GLU A1011 4918 5788 6193 -369 -108 344 C ATOM 2504 O GLU A1011 9.876 -48.198 -29.321 1.00 47.07 O ANISOU 2504 O GLU A1011 5126 6116 6641 -382 -83 461 O ATOM 2505 CB GLU A1011 11.407 -45.574 -30.057 1.00 44.01 C ANISOU 2505 CB GLU A1011 5040 5956 5724 -448 -20 364 C ATOM 2506 CG GLU A1011 12.487 -44.897 -30.895 1.00 44.52 C ANISOU 2506 CG GLU A1011 5201 6066 5647 -428 19 332 C ATOM 2507 CD GLU A1011 13.546 -45.855 -31.388 1.00 46.29 C ANISOU 2507 CD GLU A1011 5371 6293 5922 -373 18 365 C ATOM 2508 OE1 GLU A1011 13.365 -47.079 -31.234 1.00 50.19 O ANISOU 2508 OE1 GLU A1011 5763 6740 6566 -340 -39 387 O ATOM 2509 OE2 GLU A1011 14.573 -45.395 -31.929 1.00 46.57 O ANISOU 2509 OE2 GLU A1011 5452 6362 5878 -361 92 376 O ATOM 2510 N GLY A1012 8.270 -46.688 -29.733 1.00 44.42 N ANISOU 2510 N GLY A1012 4912 5706 6260 -373 -108 296 N ATOM 2511 CA GLY A1012 7.334 -47.293 -28.786 1.00 44.41 C ANISOU 2511 CA GLY A1012 4764 5618 6492 -398 -44 396 C ATOM 2512 C GLY A1012 7.719 -46.953 -27.363 1.00 43.72 C ANISOU 2512 C GLY A1012 4690 5685 6235 -478 102 575 C ATOM 2513 O GLY A1012 8.644 -46.194 -27.145 1.00 43.97 O ANISOU 2513 O GLY A1012 4827 5874 6002 -525 114 580 O ATOM 2514 N LEU A1013 6.994 -47.501 -26.396 1.00 45.13 N ANISOU 2514 N LEU A1013 4758 5808 6579 -476 215 717 N ATOM 2515 CA LEU A1013 7.331 -47.355 -24.970 1.00 45.50 C ANISOU 2515 CA LEU A1013 4837 6011 6439 -497 357 902 C ATOM 2516 C LEU A1013 7.189 -48.702 -24.306 1.00 46.52 C ANISOU 2516 C LEU A1013 4818 6062 6795 -447 459 1108 C ATOM 2517 O LEU A1013 6.096 -49.220 -24.211 1.00 47.21 O ANISOU 2517 O LEU A1013 4775 5970 7193 -418 544 1163 O ATOM 2518 CB LEU A1013 6.406 -46.356 -24.275 1.00 45.91 C ANISOU 2518 CB LEU A1013 4954 6090 6398 -509 464 902 C ATOM 2519 CG LEU A1013 6.610 -46.116 -22.771 1.00 47.18 C ANISOU 2519 CG LEU A1013 5184 6420 6320 -483 608 1068 C ATOM 2520 CD1 LEU A1013 7.926 -45.413 -22.462 1.00 46.69 C ANISOU 2520 CD1 LEU A1013 5254 6572 5912 -512 515 1016 C ATOM 2521 CD2 LEU A1013 5.458 -45.289 -22.225 1.00 47.94 C ANISOU 2521 CD2 LEU A1013 5320 6494 6398 -471 734 1057 C ATOM 2522 N ARG A1014 8.297 -49.275 -23.864 1.00 47.23 N ANISOU 2522 N ARG A1014 4910 6266 6766 -434 454 1227 N ATOM 2523 CA ARG A1014 8.264 -50.524 -23.127 1.00 48.84 C ANISOU 2523 CA ARG A1014 4990 6411 7157 -372 570 1461 C ATOM 2524 C ARG A1014 8.980 -50.337 -21.792 1.00 49.84 C ANISOU 2524 C ARG A1014 5226 6760 6950 -325 653 1640 C ATOM 2525 O ARG A1014 10.048 -49.729 -21.729 1.00 49.02 O ANISOU 2525 O ARG A1014 5233 6834 6555 -352 537 1559 O ATOM 2526 CB ARG A1014 8.883 -51.641 -23.961 1.00 49.41 C ANISOU 2526 CB ARG A1014 4939 6373 7459 -364 458 1433 C ATOM 2527 CG ARG A1014 7.847 -52.456 -24.718 1.00 51.32 C ANISOU 2527 CG ARG A1014 4998 6332 8167 -340 439 1368 C ATOM 2528 CD ARG A1014 8.438 -53.254 -25.879 1.00 52.16 C ANISOU 2528 CD ARG A1014 5028 6338 8450 -321 264 1223 C ATOM 2529 NE ARG A1014 8.639 -52.423 -27.074 1.00 52.44 N ANISOU 2529 NE ARG A1014 5193 6415 8316 -329 98 956 N ATOM 2530 CZ ARG A1014 8.805 -52.882 -28.322 1.00 52.90 C ANISOU 2530 CZ ARG A1014 5224 6365 8508 -272 -64 762 C ATOM 2531 NH1 ARG A1014 8.799 -54.192 -28.578 1.00 54.58 N ANISOU 2531 NH1 ARG A1014 5263 6408 9066 -219 -112 772 N ATOM 2532 NH2 ARG A1014 8.987 -52.024 -29.323 1.00 51.22 N ANISOU 2532 NH2 ARG A1014 5167 6212 8079 -248 -174 560 N ATOM 2533 N LEU A1015 8.407 -50.877 -20.735 1.00 51.73 N ANISOU 2533 N LEU A1015 5430 6974 7248 -237 854 1882 N ATOM 2534 CA LEU A1015 8.953 -50.733 -19.410 1.00 53.48 C ANISOU 2534 CA LEU A1015 5784 7409 7124 -134 941 2065 C ATOM 2535 C LEU A1015 9.768 -51.914 -18.933 1.00 55.40 C ANISOU 2535 C LEU A1015 5969 7678 7402 -52 947 2276 C ATOM 2536 O LEU A1015 10.365 -51.853 -17.896 1.00 56.61 O ANISOU 2536 O LEU A1015 6250 8035 7223 47 938 2386 O ATOM 2537 CB LEU A1015 7.836 -50.495 -18.425 1.00 55.56 C ANISOU 2537 CB LEU A1015 6084 7653 7372 -36 1200 2240 C ATOM 2538 CG LEU A1015 6.929 -49.307 -18.628 1.00 54.70 C ANISOU 2538 CG LEU A1015 6039 7527 7217 -92 1227 2066 C ATOM 2539 CD1 LEU A1015 5.869 -49.314 -17.567 1.00 57.06 C ANISOU 2539 CD1 LEU A1015 6357 7799 7522 31 1528 2284 C ATOM 2540 CD2 LEU A1015 7.716 -48.035 -18.539 1.00 53.84 C ANISOU 2540 CD2 LEU A1015 6117 7640 6700 -137 1045 1845 C ATOM 2541 N LYS A1016 9.783 -52.985 -19.698 1.00 55.57 N ANISOU 2541 N LYS A1016 5799 7488 7827 -78 948 2322 N ATOM 2542 CA LYS A1016 10.583 -54.136 -19.382 1.00 56.90 C ANISOU 2542 CA LYS A1016 5890 7655 8073 -15 931 2499 C ATOM 2543 C LYS A1016 11.588 -54.302 -20.487 1.00 55.10 C ANISOU 2543 C LYS A1016 5620 7432 7882 -109 689 2281 C ATOM 2544 O LYS A1016 11.323 -53.910 -21.595 1.00 54.47 O ANISOU 2544 O LYS A1016 5518 7266 7910 -204 582 2035 O ATOM 2545 CB LYS A1016 9.709 -55.374 -19.346 1.00 58.88 C ANISOU 2545 CB LYS A1016 5931 7638 8801 38 1123 2724 C ATOM 2546 CG LYS A1016 9.102 -55.704 -18.001 1.00 61.91 C ANISOU 2546 CG LYS A1016 6350 8040 9131 195 1419 3081 C ATOM 2547 CD LYS A1016 8.312 -57.005 -18.065 0.00 20.00 C ATOM 2548 CE LYS A1016 6.948 -56.898 -17.393 0.00 20.00 C ATOM 2549 NZ LYS A1016 6.467 -58.189 -16.818 0.00 20.00 N ATOM 2550 N ILE A1017 12.723 -54.923 -20.202 1.00 54.45 N ANISOU 2550 N ILE A1017 5530 7443 7714 -62 614 2378 N ATOM 2551 CA ILE A1017 13.808 -55.040 -21.192 1.00 52.64 C ANISOU 2551 CA ILE A1017 5255 7220 7524 -136 417 2193 C ATOM 2552 C ILE A1017 13.419 -55.919 -22.375 1.00 52.29 C ANISOU 2552 C ILE A1017 5037 6925 7903 -172 393 2103 C ATOM 2553 O ILE A1017 12.922 -57.015 -22.194 1.00 53.52 O ANISOU 2553 O ILE A1017 5047 6906 8381 -120 495 2269 O ATOM 2554 CB ILE A1017 15.110 -55.575 -20.572 1.00 53.25 C ANISOU 2554 CB ILE A1017 5334 7430 7467 -69 339 2321 C ATOM 2555 CG1 ILE A1017 15.641 -54.557 -19.564 1.00 53.89 C ANISOU 2555 CG1 ILE A1017 5594 7766 7114 -23 277 2315 C ATOM 2556 CG2 ILE A1017 16.149 -55.846 -21.655 1.00 52.09 C ANISOU 2556 CG2 ILE A1017 5103 7246 7442 -138 181 2152 C ATOM 2557 CD1 ILE A1017 17.075 -54.759 -19.126 1.00 54.63 C ANISOU 2557 CD1 ILE A1017 5694 8006 7055 28 116 2339 C ATOM 2558 N TYR A1018 13.656 -55.424 -23.585 1.00 51.31 N ANISOU 2558 N TYR A1018 4934 6779 7782 -244 259 1838 N ATOM 2559 CA TYR A1018 13.346 -56.162 -24.811 1.00 51.02 C ANISOU 2559 CA TYR A1018 4770 6526 8090 -244 191 1692 C ATOM 2560 C TYR A1018 14.553 -56.119 -25.733 1.00 50.63 C ANISOU 2560 C TYR A1018 4749 6540 7949 -258 56 1532 C ATOM 2561 O TYR A1018 15.502 -55.407 -25.467 1.00 49.63 O ANISOU 2561 O TYR A1018 4720 6598 7538 -289 26 1524 O ATOM 2562 CB TYR A1018 12.106 -55.586 -25.516 1.00 49.91 C ANISOU 2562 CB TYR A1018 4644 6259 8057 -266 178 1511 C ATOM 2563 CG TYR A1018 12.235 -54.140 -25.984 1.00 48.05 C ANISOU 2563 CG TYR A1018 4593 6169 7496 -318 115 1322 C ATOM 2564 CD1 TYR A1018 12.214 -53.090 -25.068 1.00 47.90 C ANISOU 2564 CD1 TYR A1018 4702 6323 7174 -355 185 1388 C ATOM 2565 CD2 TYR A1018 12.354 -53.822 -27.337 1.00 46.61 C ANISOU 2565 CD2 TYR A1018 4460 5939 7308 -309 -5 1080 C ATOM 2566 CE1 TYR A1018 12.331 -51.775 -25.479 1.00 46.48 C ANISOU 2566 CE1 TYR A1018 4667 6247 6747 -407 136 1223 C ATOM 2567 CE2 TYR A1018 12.467 -52.504 -27.761 1.00 45.47 C ANISOU 2567 CE2 TYR A1018 4480 5907 6888 -345 -31 943 C ATOM 2568 CZ TYR A1018 12.455 -51.480 -26.826 1.00 45.55 C ANISOU 2568 CZ TYR A1018 4587 6068 6650 -406 40 1016 C ATOM 2569 OH TYR A1018 12.562 -50.149 -27.205 1.00 44.70 O ANISOU 2569 OH TYR A1018 4622 6048 6313 -447 22 888 O ATOM 2570 N LYS A1019 14.506 -56.907 -26.800 1.00 52.13 N ANISOU 2570 N LYS A1019 4840 6561 8406 -219 -19 1400 N ATOM 2571 CA LYS A1019 15.536 -56.919 -27.820 1.00 53.12 C ANISOU 2571 CA LYS A1019 4998 6721 8463 -201 -114 1240 C ATOM 2572 C LYS A1019 15.076 -56.116 -29.024 1.00 53.02 C ANISOU 2572 C LYS A1019 5104 6680 8360 -182 -178 986 C ATOM 2573 O LYS A1019 13.928 -56.249 -29.450 1.00 56.16 O ANISOU 2573 O LYS A1019 5473 6926 8939 -146 -219 880 O ATOM 2574 CB LYS A1019 15.821 -58.350 -28.249 1.00 55.62 C ANISOU 2574 CB LYS A1019 5148 6873 9109 -132 -160 1244 C ATOM 2575 CG LYS A1019 16.195 -59.263 -27.096 1.00 58.58 C ANISOU 2575 CG LYS A1019 5398 7246 9613 -127 -89 1519 C ATOM 2576 CD LYS A1019 17.297 -60.244 -27.485 1.00 61.28 C ANISOU 2576 CD LYS A1019 5635 7549 10097 -81 -146 1521 C ATOM 2577 CE LYS A1019 16.901 -61.159 -28.642 1.00 63.00 C ANISOU 2577 CE LYS A1019 5741 7536 10660 -7 -231 1328 C ATOM 2578 NZ LYS A1019 18.095 -61.863 -29.202 1.00 64.53 N ANISOU 2578 NZ LYS A1019 5876 7726 10916 44 -286 1277 N ATOM 2579 N ASP A1020 15.952 -55.293 -29.591 1.00 52.04 N ANISOU 2579 N ASP A1020 5105 6684 7981 -190 -185 893 N ATOM 2580 CA ASP A1020 15.521 -54.384 -30.642 1.00 51.57 C ANISOU 2580 CA ASP A1020 5193 6618 7780 -152 -216 695 C ATOM 2581 C ASP A1020 15.518 -55.109 -31.975 1.00 53.36 C ANISOU 2581 C ASP A1020 5418 6716 8138 -12 -307 509 C ATOM 2582 O ASP A1020 15.692 -56.331 -32.026 1.00 53.60 O ANISOU 2582 O ASP A1020 5309 6640 8417 36 -354 521 O ATOM 2583 CB ASP A1020 16.352 -53.085 -30.659 1.00 50.46 C ANISOU 2583 CB ASP A1020 5189 6645 7339 -211 -149 696 C ATOM 2584 CG ASP A1020 17.761 -53.261 -31.227 1.00 51.24 C ANISOU 2584 CG ASP A1020 5279 6791 7398 -177 -118 690 C ATOM 2585 OD1 ASP A1020 18.090 -54.351 -31.749 1.00 51.66 O ANISOU 2585 OD1 ASP A1020 5253 6760 7612 -92 -154 659 O ATOM 2586 OD2 ASP A1020 18.546 -52.278 -31.150 1.00 50.10 O ANISOU 2586 OD2 ASP A1020 5193 6752 7088 -233 -49 712 O ATOM 2587 N THR A1021 15.279 -54.350 -33.041 1.00 54.39 N ANISOU 2587 N THR A1021 5713 6854 8098 72 -337 334 N ATOM 2588 CA THR A1021 15.321 -54.848 -34.413 1.00 55.46 C ANISOU 2588 CA THR A1021 5911 6901 8259 257 -431 128 C ATOM 2589 C THR A1021 16.477 -55.804 -34.607 1.00 56.65 C ANISOU 2589 C THR A1021 5975 7051 8498 304 -406 164 C ATOM 2590 O THR A1021 16.298 -56.910 -35.110 1.00 58.15 O ANISOU 2590 O THR A1021 6079 7104 8911 417 -516 47 O ATOM 2591 CB THR A1021 15.539 -53.676 -35.405 1.00 55.61 C ANISOU 2591 CB THR A1021 6168 7010 7951 351 -380 28 C ATOM 2592 OG1 THR A1021 14.634 -52.591 -35.104 1.00 54.65 O ANISOU 2592 OG1 THR A1021 6131 6914 7719 283 -377 27 O ATOM 2593 CG2 THR A1021 15.373 -54.147 -36.858 1.00 56.70 C ANISOU 2593 CG2 THR A1021 6419 7063 8058 602 -495 -205 C ATOM 2594 N GLU A1022 17.657 -55.348 -34.179 1.00 56.06 N ANISOU 2594 N GLU A1022 5907 7116 8276 215 -270 315 N ATOM 2595 CA GLU A1022 18.938 -55.985 -34.471 1.00 56.21 C ANISOU 2595 CA GLU A1022 5864 7154 8336 262 -214 350 C ATOM 2596 C GLU A1022 19.348 -57.006 -33.416 1.00 55.30 C ANISOU 2596 C GLU A1022 5537 7014 8459 171 -234 512 C ATOM 2597 O GLU A1022 20.433 -57.558 -33.502 1.00 56.63 O ANISOU 2597 O GLU A1022 5628 7196 8693 194 -195 559 O ATOM 2598 CB GLU A1022 20.022 -54.898 -34.574 1.00 56.99 C ANISOU 2598 CB GLU A1022 6051 7389 8211 217 -56 426 C ATOM 2599 CG GLU A1022 20.957 -55.018 -35.771 1.00 59.59 C ANISOU 2599 CG GLU A1022 6458 7716 8468 377 44 353 C ATOM 2600 CD GLU A1022 20.293 -54.747 -37.133 1.00 62.22 C ANISOU 2600 CD GLU A1022 7008 8007 8624 593 24 161 C ATOM 2601 OE1 GLU A1022 19.357 -53.899 -37.234 1.00 62.75 O ANISOU 2601 OE1 GLU A1022 7204 8085 8552 591 -11 108 O ATOM 2602 OE2 GLU A1022 20.729 -55.390 -38.124 1.00 64.05 O ANISOU 2602 OE2 GLU A1022 7292 8199 8845 788 40 55 O ATOM 2603 N GLY A1023 18.498 -57.247 -32.418 1.00 53.41 N ANISOU 2603 N GLY A1023 5207 6733 8351 84 -276 613 N ATOM 2604 CA GLY A1023 18.780 -58.234 -31.376 1.00 52.71 C ANISOU 2604 CA GLY A1023 4936 6613 8477 29 -278 801 C ATOM 2605 C GLY A1023 19.434 -57.714 -30.106 1.00 51.37 C ANISOU 2605 C GLY A1023 4752 6604 8161 -87 -214 1010 C ATOM 2606 O GLY A1023 19.841 -58.515 -29.268 1.00 51.99 O ANISOU 2606 O GLY A1023 4703 6678 8371 -100 -217 1179 O ATOM 2607 N TYR A1024 19.521 -56.389 -29.941 1.00 49.51 N ANISOU 2607 N TYR A1024 4645 6502 7661 -155 -173 994 N ATOM 2608 CA TYR A1024 20.183 -55.780 -28.770 1.00 47.77 C ANISOU 2608 CA TYR A1024 4420 6437 7291 -245 -155 1138 C ATOM 2609 C TYR A1024 19.194 -55.375 -27.694 1.00 47.23 C ANISOU 2609 C TYR A1024 4394 6413 7135 -291 -145 1236 C ATOM 2610 O TYR A1024 18.153 -54.830 -27.993 1.00 45.61 O ANISOU 2610 O TYR A1024 4273 6168 6887 -299 -128 1152 O ATOM 2611 CB TYR A1024 20.948 -54.518 -29.146 1.00 46.19 C ANISOU 2611 CB TYR A1024 4309 6338 6900 -292 -115 1056 C ATOM 2612 CG TYR A1024 21.994 -54.646 -30.224 1.00 45.76 C ANISOU 2612 CG TYR A1024 4235 6252 6900 -237 -65 978 C ATOM 2613 CD1 TYR A1024 22.990 -55.612 -30.157 1.00 45.87 C ANISOU 2613 CD1 TYR A1024 4108 6243 7077 -206 -81 1041 C ATOM 2614 CD2 TYR A1024 22.014 -53.750 -31.288 1.00 44.82 C ANISOU 2614 CD2 TYR A1024 4241 6125 6660 -203 20 857 C ATOM 2615 CE1 TYR A1024 23.960 -55.703 -31.131 1.00 46.24 C ANISOU 2615 CE1 TYR A1024 4132 6257 7178 -145 -4 977 C ATOM 2616 CE2 TYR A1024 22.980 -53.827 -32.266 1.00 45.53 C ANISOU 2616 CE2 TYR A1024 4326 6186 6784 -127 114 813 C ATOM 2617 CZ TYR A1024 23.956 -54.799 -32.189 1.00 46.29 C ANISOU 2617 CZ TYR A1024 4274 6258 7053 -101 108 869 C ATOM 2618 OH TYR A1024 24.913 -54.847 -33.183 1.00 46.49 O ANISOU 2618 OH TYR A1024 4294 6249 7117 -12 234 830 O ATOM 2619 N TYR A1025 19.566 -55.583 -26.437 1.00 48.77 N ANISOU 2619 N TYR A1025 4545 6701 7283 -304 -156 1411 N ATOM 2620 CA TYR A1025 18.705 -55.249 -25.312 1.00 49.46 C ANISOU 2620 CA TYR A1025 4690 6848 7253 -311 -120 1530 C ATOM 2621 C TYR A1025 18.502 -53.752 -25.221 1.00 48.20 C ANISOU 2621 C TYR A1025 4671 6799 6843 -375 -119 1418 C ATOM 2622 O TYR A1025 19.458 -53.002 -25.228 1.00 48.26 O ANISOU 2622 O TYR A1025 4703 6905 6726 -416 -168 1349 O ATOM 2623 CB TYR A1025 19.290 -55.769 -23.991 1.00 51.82 C ANISOU 2623 CB TYR A1025 4948 7248 7493 -262 -140 1742 C ATOM 2624 CG TYR A1025 19.555 -57.263 -23.983 1.00 53.68 C ANISOU 2624 CG TYR A1025 5035 7367 7993 -194 -132 1884 C ATOM 2625 CD1 TYR A1025 18.535 -58.186 -24.231 1.00 54.56 C ANISOU 2625 CD1 TYR A1025 5060 7288 8381 -159 -53 1947 C ATOM 2626 CD2 TYR A1025 20.823 -57.749 -23.739 1.00 55.01 C ANISOU 2626 CD2 TYR A1025 5127 7593 8181 -165 -211 1944 C ATOM 2627 CE1 TYR A1025 18.787 -59.550 -24.239 1.00 56.05 C ANISOU 2627 CE1 TYR A1025 5093 7344 8857 -99 -46 2071 C ATOM 2628 CE2 TYR A1025 21.080 -59.102 -23.741 1.00 56.57 C ANISOU 2628 CE2 TYR A1025 5185 7675 8634 -101 -204 2075 C ATOM 2629 CZ TYR A1025 20.067 -59.997 -23.990 1.00 57.12 C ANISOU 2629 CZ TYR A1025 5174 7553 8974 -69 -117 2140 C ATOM 2630 OH TYR A1025 20.371 -61.343 -23.973 1.00 59.88 O ANISOU 2630 OH TYR A1025 5367 7769 9615 -5 -111 2270 O ATOM 2631 N THR A1026 17.244 -53.349 -25.098 1.00 48.25 N ANISOU 2631 N THR A1026 4744 6766 6819 -382 -60 1405 N ATOM 2632 CA THR A1026 16.814 -51.964 -25.148 1.00 47.62 C ANISOU 2632 CA THR A1026 4794 6754 6544 -438 -50 1285 C ATOM 2633 C THR A1026 15.716 -51.775 -24.087 1.00 48.53 C ANISOU 2633 C THR A1026 4958 6896 6582 -417 23 1394 C ATOM 2634 O THR A1026 15.174 -52.758 -23.580 1.00 50.98 O ANISOU 2634 O THR A1026 5195 7134 7038 -358 92 1558 O ATOM 2635 CB THR A1026 16.312 -51.663 -26.584 1.00 47.38 C ANISOU 2635 CB THR A1026 4801 6603 6598 -444 -47 1105 C ATOM 2636 OG1 THR A1026 17.410 -51.782 -27.504 1.00 47.84 O ANISOU 2636 OG1 THR A1026 4836 6654 6685 -434 -76 1027 O ATOM 2637 CG2 THR A1026 15.706 -50.259 -26.741 1.00 46.64 C ANISOU 2637 CG2 THR A1026 4838 6547 6334 -492 -26 990 C ATOM 2638 N ILE A1027 15.410 -50.535 -23.713 1.00 47.98 N ANISOU 2638 N ILE A1027 5006 6921 6300 -455 30 1320 N ATOM 2639 CA ILE A1027 14.323 -50.273 -22.781 1.00 48.60 C ANISOU 2639 CA ILE A1027 5145 7024 6295 -421 125 1409 C ATOM 2640 C ILE A1027 13.711 -48.887 -22.965 1.00 48.43 C ANISOU 2640 C ILE A1027 5236 7028 6134 -478 132 1253 C ATOM 2641 O ILE A1027 14.379 -47.964 -23.426 1.00 48.95 O ANISOU 2641 O ILE A1027 5352 7147 6099 -539 56 1105 O ATOM 2642 CB ILE A1027 14.819 -50.395 -21.334 1.00 50.50 C ANISOU 2642 CB ILE A1027 5432 7430 6325 -340 124 1568 C ATOM 2643 CG1 ILE A1027 13.639 -50.617 -20.383 1.00 52.53 C ANISOU 2643 CG1 ILE A1027 5729 7676 6553 -253 289 1742 C ATOM 2644 CG2 ILE A1027 15.608 -49.155 -20.937 1.00 50.34 C ANISOU 2644 CG2 ILE A1027 5511 7574 6041 -370 3 1424 C ATOM 2645 CD1 ILE A1027 14.022 -51.119 -19.005 1.00 55.22 C ANISOU 2645 CD1 ILE A1027 6122 8156 6702 -108 325 1962 C ATOM 2646 N GLY A1028 12.444 -48.729 -22.587 1.00 48.70 N ANISOU 2646 N GLY A1028 5298 7012 6194 -455 241 1297 N ATOM 2647 CA GLY A1028 11.810 -47.411 -22.580 1.00 47.73 C ANISOU 2647 CA GLY A1028 5282 6919 5933 -497 256 1165 C ATOM 2648 C GLY A1028 11.402 -46.969 -23.967 1.00 46.06 C ANISOU 2648 C GLY A1028 5070 6577 5852 -554 213 990 C ATOM 2649 O GLY A1028 10.712 -47.699 -24.672 1.00 46.90 O ANISOU 2649 O GLY A1028 5095 6524 6198 -530 224 984 O ATOM 2650 N ILE A1029 11.825 -45.767 -24.351 1.00 45.23 N ANISOU 2650 N ILE A1029 5054 6530 5600 -611 158 844 N ATOM 2651 CA ILE A1029 11.614 -45.238 -25.703 1.00 43.94 C ANISOU 2651 CA ILE A1029 4927 6265 5503 -634 123 694 C ATOM 2652 C ILE A1029 12.928 -45.268 -26.499 1.00 43.69 C ANISOU 2652 C ILE A1029 4887 6253 5459 -647 70 651 C ATOM 2653 O ILE A1029 13.609 -44.251 -26.662 1.00 43.56 O ANISOU 2653 O ILE A1029 4922 6286 5342 -694 63 581 O ATOM 2654 CB ILE A1029 11.073 -43.793 -25.643 1.00 43.77 C ANISOU 2654 CB ILE A1029 5010 6262 5356 -675 142 586 C ATOM 2655 CG1 ILE A1029 9.881 -43.720 -24.685 1.00 43.96 C ANISOU 2655 CG1 ILE A1029 5039 6284 5377 -655 221 642 C ATOM 2656 CG2 ILE A1029 10.688 -43.295 -27.041 1.00 43.09 C ANISOU 2656 CG2 ILE A1029 4980 6062 5329 -662 116 459 C ATOM 2657 CD1 ILE A1029 9.400 -42.312 -24.412 1.00 43.78 C ANISOU 2657 CD1 ILE A1029 5116 6296 5222 -691 242 538 C ATOM 2658 N GLY A1030 13.297 -46.456 -26.961 1.00 43.63 N ANISOU 2658 N GLY A1030 4797 6190 5589 -600 48 699 N ATOM 2659 CA GLY A1030 14.461 -46.623 -27.812 1.00 43.29 C ANISOU 2659 CA GLY A1030 4739 6146 5562 -589 26 666 C ATOM 2660 C GLY A1030 15.816 -46.505 -27.143 1.00 43.83 C ANISOU 2660 C GLY A1030 4754 6326 5571 -636 8 721 C ATOM 2661 O GLY A1030 16.819 -46.344 -27.831 1.00 43.73 O ANISOU 2661 O GLY A1030 4724 6305 5587 -640 19 689 O ATOM 2662 N HIS A1031 15.879 -46.619 -25.821 1.00 44.76 N ANISOU 2662 N HIS A1031 4845 6544 5618 -650 -20 806 N ATOM 2663 CA HIS A1031 17.174 -46.550 -25.139 1.00 45.86 C ANISOU 2663 CA HIS A1031 4925 6786 5712 -671 -89 832 C ATOM 2664 C HIS A1031 17.961 -47.859 -25.237 1.00 46.30 C ANISOU 2664 C HIS A1031 4868 6826 5897 -627 -116 931 C ATOM 2665 O HIS A1031 17.590 -48.860 -24.641 1.00 46.37 O ANISOU 2665 O HIS A1031 4840 6839 5939 -571 -114 1057 O ATOM 2666 CB HIS A1031 17.014 -46.168 -23.676 1.00 47.19 C ANISOU 2666 CB HIS A1031 5134 7084 5709 -656 -140 866 C ATOM 2667 CG HIS A1031 18.317 -45.939 -22.979 1.00 49.96 C ANISOU 2667 CG HIS A1031 5429 7536 6014 -659 -266 841 C ATOM 2668 ND1 HIS A1031 19.077 -44.808 -23.179 1.00 50.95 N ANISOU 2668 ND1 HIS A1031 5532 7660 6164 -730 -323 696 N ATOM 2669 CD2 HIS A1031 19.003 -46.701 -22.094 1.00 52.37 C ANISOU 2669 CD2 HIS A1031 5683 7931 6283 -589 -358 936 C ATOM 2670 CE1 HIS A1031 20.172 -44.877 -22.443 1.00 52.55 C ANISOU 2670 CE1 HIS A1031 5655 7939 6371 -709 -466 679 C ATOM 2671 NE2 HIS A1031 20.153 -46.017 -21.776 1.00 53.78 N ANISOU 2671 NE2 HIS A1031 5806 8164 6465 -617 -499 822 N ATOM 2672 N LEU A1032 19.061 -47.836 -25.983 1.00 46.41 N ANISOU 2672 N LEU A1032 4818 6811 6004 -646 -122 885 N ATOM 2673 CA LEU A1032 19.941 -48.989 -26.102 1.00 46.19 C ANISOU 2673 CA LEU A1032 4672 6765 6111 -606 -150 963 C ATOM 2674 C LEU A1032 20.771 -49.081 -24.860 1.00 47.24 C ANISOU 2674 C LEU A1032 4740 7013 6196 -603 -262 1025 C ATOM 2675 O LEU A1032 21.448 -48.122 -24.512 1.00 48.75 O ANISOU 2675 O LEU A1032 4917 7258 6345 -650 -327 941 O ATOM 2676 CB LEU A1032 20.869 -48.824 -27.295 1.00 46.20 C ANISOU 2676 CB LEU A1032 4631 6696 6226 -612 -91 896 C ATOM 2677 CG LEU A1032 21.916 -49.919 -27.506 1.00 47.03 C ANISOU 2677 CG LEU A1032 4602 6774 6490 -571 -108 958 C ATOM 2678 CD1 LEU A1032 21.275 -51.233 -27.916 1.00 46.71 C ANISOU 2678 CD1 LEU A1032 4550 6657 6540 -491 -97 1006 C ATOM 2679 CD2 LEU A1032 22.905 -49.466 -28.563 1.00 47.65 C ANISOU 2679 CD2 LEU A1032 4644 6792 6666 -574 -10 898 C ATOM 2680 N LEU A1033 20.732 -50.234 -24.202 1.00 47.63 N ANISOU 2680 N LEU A1033 4741 7085 6269 -534 -296 1166 N ATOM 2681 CA LEU A1033 21.437 -50.437 -22.946 1.00 48.81 C ANISOU 2681 CA LEU A1033 4856 7358 6332 -484 -421 1243 C ATOM 2682 C LEU A1033 22.849 -50.947 -23.196 1.00 49.90 C ANISOU 2682 C LEU A1033 4845 7478 6637 -482 -500 1243 C ATOM 2683 O LEU A1033 23.801 -50.457 -22.606 1.00 50.93 O ANISOU 2683 O LEU A1033 4922 7681 6746 -485 -637 1184 O ATOM 2684 CB LEU A1033 20.677 -51.430 -22.061 1.00 49.73 C ANISOU 2684 CB LEU A1033 5005 7503 6387 -382 -388 1437 C ATOM 2685 CG LEU A1033 19.394 -50.952 -21.372 1.00 49.34 C ANISOU 2685 CG LEU A1033 5092 7499 6156 -350 -310 1477 C ATOM 2686 CD1 LEU A1033 18.595 -52.127 -20.854 1.00 49.84 C ANISOU 2686 CD1 LEU A1033 5143 7514 6277 -253 -199 1703 C ATOM 2687 CD2 LEU A1033 19.715 -50.004 -20.233 1.00 50.58 C ANISOU 2687 CD2 LEU A1033 5346 7826 6045 -307 -426 1420 C ATOM 2688 N THR A1034 22.981 -51.946 -24.063 1.00 49.79 N ANISOU 2688 N THR A1034 4752 7355 6810 -467 -426 1293 N ATOM 2689 CA THR A1034 24.286 -52.531 -24.360 1.00 50.38 C ANISOU 2689 CA THR A1034 4675 7398 7069 -457 -475 1302 C ATOM 2690 C THR A1034 24.195 -53.417 -25.579 1.00 49.29 C ANISOU 2690 C THR A1034 4490 7124 7114 -436 -361 1307 C ATOM 2691 O THR A1034 23.119 -53.920 -25.900 1.00 48.45 O ANISOU 2691 O THR A1034 4442 6951 7014 -405 -295 1334 O ATOM 2692 CB THR A1034 24.804 -53.394 -23.195 1.00 52.40 C ANISOU 2692 CB THR A1034 4865 7732 7312 -371 -607 1445 C ATOM 2693 OG1 THR A1034 26.070 -53.971 -23.540 1.00 54.31 O ANISOU 2693 OG1 THR A1034 4942 7926 7767 -363 -658 1445 O ATOM 2694 CG2 THR A1034 23.845 -54.521 -22.893 1.00 52.89 C ANISOU 2694 CG2 THR A1034 4961 7757 7377 -293 -536 1620 C ATOM 2695 N LYS A1035 25.331 -53.624 -26.238 1.00 49.84 N ANISOU 2695 N LYS A1035 4442 7142 7352 -438 -345 1268 N ATOM 2696 CA LYS A1035 25.402 -54.527 -27.384 1.00 49.89 C ANISOU 2696 CA LYS A1035 4406 7028 7521 -384 -249 1256 C ATOM 2697 C LYS A1035 25.855 -55.939 -27.004 1.00 51.52 C ANISOU 2697 C LYS A1035 4480 7201 7892 -319 -312 1376 C ATOM 2698 O LYS A1035 25.946 -56.798 -27.876 1.00 50.99 O ANISOU 2698 O LYS A1035 4363 7027 7981 -262 -253 1355 O ATOM 2699 CB LYS A1035 26.325 -53.960 -28.456 1.00 49.85 C ANISOU 2699 CB LYS A1035 4363 6970 7605 -396 -139 1158 C ATOM 2700 CG LYS A1035 25.965 -52.549 -28.877 1.00 49.01 C ANISOU 2700 CG LYS A1035 4377 6875 7366 -450 -53 1065 C ATOM 2701 CD LYS A1035 26.435 -52.253 -30.281 1.00 49.32 C ANISOU 2701 CD LYS A1035 4440 6828 7470 -401 132 1003 C ATOM 2702 CE LYS A1035 26.087 -50.839 -30.703 1.00 49.18 C ANISOU 2702 CE LYS A1035 4544 6808 7334 -441 236 940 C ATOM 2703 NZ LYS A1035 26.222 -50.672 -32.178 1.00 49.43 N ANISOU 2703 NZ LYS A1035 4667 6757 7356 -334 445 907 N ATOM 2704 N SER A1036 26.115 -56.179 -25.715 1.00 53.74 N ANISOU 2704 N SER A1036 4716 7571 8129 -306 -437 1496 N ATOM 2705 CA SER A1036 26.539 -57.493 -25.232 1.00 56.11 C ANISOU 2705 CA SER A1036 4897 7842 8578 -231 -499 1642 C ATOM 2706 C SER A1036 25.388 -58.482 -25.210 1.00 56.90 C ANISOU 2706 C SER A1036 5024 7853 8741 -176 -438 1749 C ATOM 2707 O SER A1036 24.297 -58.143 -24.749 1.00 57.54 O ANISOU 2707 O SER A1036 5216 7962 8683 -182 -405 1789 O ATOM 2708 CB SER A1036 27.095 -57.395 -23.811 1.00 58.42 C ANISOU 2708 CB SER A1036 5169 8268 8758 -193 -660 1748 C ATOM 2709 OG SER A1036 27.086 -58.680 -23.183 1.00 60.33 O ANISOU 2709 OG SER A1036 5349 8486 9085 -93 -695 1943 O ATOM 2710 N PRO A1037 25.635 -59.730 -25.643 1.00 58.30 N ANISOU 2710 N PRO A1037 5079 7905 9165 -118 -421 1799 N ATOM 2711 CA PRO A1037 24.579 -60.751 -25.594 1.00 58.71 C ANISOU 2711 CA PRO A1037 5109 7829 9369 -65 -370 1901 C ATOM 2712 C PRO A1037 24.180 -61.211 -24.174 1.00 60.14 C ANISOU 2712 C PRO A1037 5294 8058 9498 -8 -382 2156 C ATOM 2713 O PRO A1037 23.228 -61.969 -24.044 1.00 61.39 O ANISOU 2713 O PRO A1037 5420 8090 9816 31 -304 2270 O ATOM 2714 CB PRO A1037 25.188 -61.921 -26.371 1.00 59.33 C ANISOU 2714 CB PRO A1037 5035 7761 9743 -11 -370 1873 C ATOM 2715 CG PRO A1037 26.653 -61.793 -26.112 1.00 60.32 C ANISOU 2715 CG PRO A1037 5082 7979 9857 -14 -440 1891 C ATOM 2716 CD PRO A1037 26.938 -60.309 -26.023 1.00 59.29 C ANISOU 2716 CD PRO A1037 5055 7992 9477 -92 -456 1784 C ATOM 2717 N SER A1038 24.873 -60.762 -23.129 1.00 61.30 N ANISOU 2717 N SER A1038 5479 8373 9437 16 -474 2246 N ATOM 2718 CA SER A1038 24.496 -61.118 -21.754 1.00 63.58 C ANISOU 2718 CA SER A1038 5820 8736 9599 120 -474 2498 C ATOM 2719 C SER A1038 23.337 -60.276 -21.220 1.00 63.98 C ANISOU 2719 C SER A1038 6038 8862 9408 112 -394 2519 C ATOM 2720 O SER A1038 23.424 -59.050 -21.180 1.00 64.35 O ANISOU 2720 O SER A1038 6192 9035 9221 52 -451 2363 O ATOM 2721 CB SER A1038 25.679 -60.947 -20.811 1.00 65.09 C ANISOU 2721 CB SER A1038 6012 9092 9627 193 -645 2559 C ATOM 2722 OG SER A1038 25.215 -60.675 -19.504 1.00 66.43 O ANISOU 2722 OG SER A1038 6330 9404 9506 304 -657 2724 O ATOM 2723 N LEU A1039 22.271 -60.939 -20.771 1.00 65.28 N ANISOU 2723 N LEU A1039 6210 8935 9659 178 -251 2720 N ATOM 2724 CA LEU A1039 21.096 -60.246 -20.222 1.00 64.81 C ANISOU 2724 CA LEU A1039 6292 8925 9406 187 -138 2768 C ATOM 2725 C LEU A1039 21.399 -59.609 -18.858 1.00 66.66 C ANISOU 2725 C LEU A1039 6690 9395 9241 299 -201 2878 C ATOM 2726 O LEU A1039 20.787 -58.613 -18.490 1.00 66.56 O ANISOU 2726 O LEU A1039 6824 9486 8979 289 -171 2815 O ATOM 2727 CB LEU A1039 19.895 -61.201 -20.142 1.00 64.93 C ANISOU 2727 CB LEU A1039 6228 8736 9703 234 59 2968 C ATOM 2728 CG LEU A1039 18.566 -60.701 -19.554 1.00 64.73 C ANISOU 2728 CG LEU A1039 6310 8714 9570 260 230 3067 C ATOM 2729 CD1 LEU A1039 18.048 -59.464 -20.263 1.00 62.60 C ANISOU 2729 CD1 LEU A1039 6128 8478 9177 132 196 2785 C ATOM 2730 CD2 LEU A1039 17.526 -61.807 -19.614 1.00 65.51 C ANISOU 2730 CD2 LEU A1039 6255 8547 10087 297 427 3261 C ATOM 2731 N ASN A1040 22.341 -60.185 -18.116 1.00 69.34 N ANISOU 2731 N ASN A1040 7010 9819 9516 424 -306 3026 N ATOM 2732 CA ASN A1040 22.841 -59.570 -16.880 1.00 71.28 C ANISOU 2732 CA ASN A1040 7418 10304 9362 564 -442 3072 C ATOM 2733 C ASN A1040 23.661 -58.304 -17.155 1.00 69.93 C ANISOU 2733 C ASN A1040 7275 10260 9034 462 -660 2755 C ATOM 2734 O ASN A1040 23.680 -57.382 -16.339 1.00 71.33 O ANISOU 2734 O ASN A1040 7607 10615 8880 534 -763 2687 O ATOM 2735 CB ASN A1040 23.715 -60.559 -16.087 1.00 73.99 C ANISOU 2735 CB ASN A1040 7724 10693 9696 745 -537 3297 C ATOM 2736 CG ASN A1040 22.933 -61.746 -15.541 1.00 75.48 C ANISOU 2736 CG ASN A1040 7905 10768 10006 891 -303 3669 C ATOM 2737 OD1 ASN A1040 21.706 -61.726 -15.463 1.00 74.60 O ANISOU 2737 OD1 ASN A1040 7843 10577 9923 890 -70 3781 O ATOM 2738 ND2 ASN A1040 23.656 -62.789 -15.150 1.00 77.55 N ANISOU 2738 ND2 ASN A1040 8089 11004 10371 1022 -354 3873 N ATOM 2739 N ALA A1041 24.362 -58.278 -18.286 1.00 67.83 N ANISOU 2739 N ALA A1041 6854 9893 9022 313 -722 2564 N ATOM 2740 CA ALA A1041 25.134 -57.103 -18.679 1.00 66.65 C ANISOU 2740 CA ALA A1041 6693 9813 8818 204 -877 2284 C ATOM 2741 C ALA A1041 24.197 -55.922 -18.896 1.00 64.91 C ANISOU 2741 C ALA A1041 6603 9620 8440 113 -794 2140 C ATOM 2742 O ALA A1041 24.438 -54.819 -18.407 1.00 65.04 O ANISOU 2742 O ALA A1041 6703 9763 8245 112 -921 1994 O ATOM 2743 CB ALA A1041 25.927 -57.389 -19.943 1.00 65.49 C ANISOU 2743 CB ALA A1041 6361 9525 8994 82 -877 2154 C ATOM 2744 N ALA A1042 23.120 -56.171 -19.631 1.00 63.21 N ANISOU 2744 N ALA A1042 6391 9271 8353 45 -597 2168 N ATOM 2745 CA ALA A1042 22.074 -55.177 -19.825 1.00 61.77 C ANISOU 2745 CA ALA A1042 6330 9096 8042 -24 -503 2061 C ATOM 2746 C ALA A1042 21.564 -54.681 -18.485 1.00 63.49 C ANISOU 2746 C ALA A1042 6717 9475 7931 95 -512 2152 C ATOM 2747 O ALA A1042 21.546 -53.478 -18.219 1.00 63.72 O ANISOU 2747 O ALA A1042 6847 9609 7753 66 -589 1988 O ATOM 2748 CB ALA A1042 20.931 -55.774 -20.626 1.00 60.29 C ANISOU 2748 CB ALA A1042 6106 8728 8073 -68 -316 2111 C ATOM 2749 N LYS A1043 21.126 -55.617 -17.662 1.00 65.94 N ANISOU 2749 N LYS A1043 7058 9796 8198 248 -424 2422 N ATOM 2750 CA LYS A1043 20.482 -55.340 -16.391 1.00 67.82 C ANISOU 2750 CA LYS A1043 7481 10178 8107 414 -365 2567 C ATOM 2751 C LYS A1043 21.370 -54.549 -15.518 1.00 68.77 C ANISOU 2751 C LYS A1043 7713 10518 7898 516 -617 2437 C ATOM 2752 O LYS A1043 20.944 -53.683 -14.813 1.00 69.22 O ANISOU 2752 O LYS A1043 7933 10702 7665 574 -637 2354 O ATOM 2753 CB LYS A1043 20.192 -56.640 -15.688 1.00 70.83 C ANISOU 2753 CB LYS A1043 7856 10511 8543 587 -202 2923 C ATOM 2754 CG LYS A1043 18.736 -57.014 -15.619 1.00 73.02 C ANISOU 2754 CG LYS A1043 8251 10771 8722 681 62 3120 C ATOM 2755 CD LYS A1043 18.588 -58.419 -15.094 1.00 75.36 C ANISOU 2755 CD LYS A1043 8477 10936 9220 818 285 3493 C ATOM 2756 CE LYS A1043 17.162 -58.891 -15.200 1.00 73.92 C ANISOU 2756 CE LYS A1043 8053 10467 9563 654 380 3481 C ATOM 2757 NZ LYS A1043 17.077 -60.187 -15.910 1.00 76.25 N ANISOU 2757 NZ LYS A1043 8261 10571 10137 756 666 3823 N ATOM 2758 N SER A1044 22.632 -54.882 -15.566 1.00 69.52 N ANISOU 2758 N SER A1044 7706 10642 8064 543 -826 2400 N ATOM 2759 CA SER A1044 23.615 -54.197 -14.797 1.00 71.36 C ANISOU 2759 CA SER A1044 7990 11045 8077 625 -1125 2217 C ATOM 2760 C SER A1044 23.737 -52.784 -15.278 1.00 70.59 C ANISOU 2760 C SER A1044 7886 10946 7988 455 -1207 1896 C ATOM 2761 O SER A1044 23.963 -51.873 -14.520 1.00 72.57 O ANISOU 2761 O SER A1044 8262 11337 7972 537 -1363 1745 O ATOM 2762 CB SER A1044 24.929 -54.927 -14.975 1.00 71.76 C ANISOU 2762 CB SER A1044 7867 11070 8327 639 -1327 2203 C ATOM 2763 OG SER A1044 26.029 -54.092 -14.704 0.00 20.00 O ATOM 2764 N GLU A1045 23.604 -52.607 -16.571 1.00 69.23 N ANISOU 2764 N GLU A1045 7574 10607 8120 238 -1099 1793 N ATOM 2765 CA GLU A1045 23.852 -51.324 -17.173 1.00 68.71 C ANISOU 2765 CA GLU A1045 7480 10508 8118 75 -1148 1519 C ATOM 2766 C GLU A1045 22.684 -50.396 -16.963 1.00 67.58 C ANISOU 2766 C GLU A1045 7507 10406 7763 62 -1030 1469 C ATOM 2767 O GLU A1045 22.844 -49.202 -16.814 1.00 66.09 O ANISOU 2767 O GLU A1045 7354 10259 7495 13 -1138 1250 O ATOM 2768 CB GLU A1045 24.125 -51.525 -18.645 1.00 67.60 C ANISOU 2768 CB GLU A1045 7174 10184 8325 -104 -1032 1463 C ATOM 2769 CG GLU A1045 24.572 -50.278 -19.354 1.00 67.64 C ANISOU 2769 CG GLU A1045 7112 10133 8452 -252 -1078 1215 C ATOM 2770 CD GLU A1045 25.965 -49.876 -18.980 1.00 70.10 C ANISOU 2770 CD GLU A1045 7307 10492 8834 -230 -1336 1068 C ATOM 2771 OE1 GLU A1045 26.872 -50.693 -19.166 1.00 70.65 O ANISOU 2771 OE1 GLU A1045 7234 10532 9078 -197 -1417 1126 O ATOM 2772 OE2 GLU A1045 26.138 -48.742 -18.504 1.00 71.92 O ANISOU 2772 OE2 GLU A1045 7575 10775 8976 -243 -1467 881 O ATOM 2773 N LEU A1046 21.504 -50.983 -16.952 1.00 67.13 N ANISOU 2773 N LEU A1046 7531 10313 7661 106 -805 1670 N ATOM 2774 CA LEU A1046 20.252 -50.286 -16.632 1.00 67.25 C ANISOU 2774 CA LEU A1046 7701 10360 7487 121 -666 1663 C ATOM 2775 C LEU A1046 20.266 -49.754 -15.194 1.00 71.48 C ANISOU 2775 C LEU A1046 8419 11103 7636 317 -786 1651 C ATOM 2776 O LEU A1046 20.041 -48.564 -14.957 1.00 72.15 O ANISOU 2776 O LEU A1046 8596 11253 7565 298 -853 1454 O ATOM 2777 CB LEU A1046 19.060 -51.234 -16.822 1.00 65.98 C ANISOU 2777 CB LEU A1046 7542 10086 7439 144 -398 1903 C ATOM 2778 CG LEU A1046 17.660 -50.771 -16.389 1.00 65.34 C ANISOU 2778 CG LEU A1046 7598 10015 7210 187 -207 1961 C ATOM 2779 CD1 LEU A1046 17.188 -49.597 -17.231 1.00 63.31 C ANISOU 2779 CD1 LEU A1046 7347 9693 7013 18 -200 1720 C ATOM 2780 CD2 LEU A1046 16.669 -51.917 -16.480 1.00 64.77 C ANISOU 2780 CD2 LEU A1046 7469 9798 7342 229 43 2226 C ATOM 2781 N ASP A1047 20.532 -50.641 -14.239 1.00 74.84 N ANISOU 2781 N ASP A1047 8905 11630 7898 527 -817 1861 N ATOM 2782 CA ASP A1047 20.645 -50.242 -12.838 1.00 79.59 C ANISOU 2782 CA ASP A1047 9709 12449 8080 776 -956 1854 C ATOM 2783 C ASP A1047 21.589 -49.047 -12.703 1.00 80.69 C ANISOU 2783 C ASP A1047 9833 12669 8154 740 -1287 1498 C ATOM 2784 O ASP A1047 21.291 -48.081 -12.006 1.00 82.91 O ANISOU 2784 O ASP A1047 10271 13071 8158 837 -1373 1341 O ATOM 2785 CB ASP A1047 21.129 -51.416 -11.981 1.00 83.09 C ANISOU 2785 CB ASP A1047 10198 12982 8390 1018 -996 2117 C ATOM 2786 CG ASP A1047 20.112 -52.554 -11.921 1.00 84.85 C ANISOU 2786 CG ASP A1047 10440 13111 8687 1088 -643 2494 C ATOM 2787 OD1 ASP A1047 19.252 -52.641 -12.831 1.00 84.00 O ANISOU 2787 OD1 ASP A1047 10231 12823 8860 898 -415 2521 O ATOM 2788 OD2 ASP A1047 20.162 -53.360 -10.966 1.00 88.47 O ANISOU 2788 OD2 ASP A1047 11008 13663 8943 1345 -595 2765 O ATOM 2789 N LYS A1048 22.682 -49.105 -13.428 1.00 80.22 N ANISOU 2789 N LYS A1048 9566 12520 8392 602 -1459 1368 N ATOM 2790 CA LYS A1048 23.646 -48.040 -13.493 1.00 80.54 C ANISOU 2790 CA LYS A1048 9513 12566 8523 525 -1749 1031 C ATOM 2791 C LYS A1048 23.037 -46.768 -14.067 1.00 78.44 C ANISOU 2791 C LYS A1048 9254 12221 8327 344 -1661 825 C ATOM 2792 O LYS A1048 23.302 -45.684 -13.603 1.00 79.83 O ANISOU 2792 O LYS A1048 9462 12453 8414 369 -1866 565 O ATOM 2793 CB LYS A1048 24.775 -48.529 -14.388 1.00 80.15 C ANISOU 2793 CB LYS A1048 9204 12383 8867 387 -1847 993 C ATOM 2794 CG LYS A1048 26.110 -47.837 -14.262 1.00 81.88 C ANISOU 2794 CG LYS A1048 9273 12591 9246 356 -2178 690 C ATOM 2795 CD LYS A1048 27.182 -48.618 -15.011 0.00 81.94 C ANISOU 2795 CD LYS A1048 9027 12476 9627 272 -2243 716 C ATOM 2796 CE LYS A1048 27.124 -50.117 -14.721 0.00 20.00 C ATOM 2797 NZ LYS A1048 27.919 -50.988 -15.638 0.00 20.00 N ATOM 2798 N ALA A1049 22.227 -46.909 -15.099 1.00 75.70 N ANISOU 2798 N ALA A1049 8874 11736 8152 178 -1374 929 N ATOM 2799 CA ALA A1049 21.658 -45.758 -15.807 1.00 74.42 C ANISOU 2799 CA ALA A1049 8711 11481 8084 7 -1280 756 C ATOM 2800 C ALA A1049 20.769 -44.888 -14.935 1.00 75.86 C ANISOU 2800 C ALA A1049 9094 11779 7950 111 -1276 672 C ATOM 2801 O ALA A1049 20.753 -43.664 -15.100 1.00 76.84 O ANISOU 2801 O ALA A1049 9211 11869 8114 21 -1347 437 O ATOM 2802 CB ALA A1049 20.875 -46.213 -17.032 1.00 71.62 C ANISOU 2802 CB ALA A1049 8305 10966 7940 -142 -999 889 C ATOM 2803 N ILE A1050 20.014 -45.512 -14.034 1.00 75.86 N ANISOU 2803 N ILE A1050 9266 11900 7656 306 -1166 876 N ATOM 2804 CA ILE A1050 19.088 -44.760 -13.187 1.00 76.60 C ANISOU 2804 CA ILE A1050 9567 12107 7429 434 -1114 824 C ATOM 2805 C ILE A1050 19.458 -44.735 -11.694 1.00 79.32 C ANISOU 2805 C ILE A1050 10095 12679 7363 738 -1320 795 C ATOM 2806 O ILE A1050 19.042 -43.827 -10.981 1.00 80.86 O ANISOU 2806 O ILE A1050 10451 12980 7291 852 -1378 637 O ATOM 2807 CB ILE A1050 17.629 -45.230 -13.374 1.00 75.76 C ANISOU 2807 CB ILE A1050 9537 11939 7308 431 -756 1066 C ATOM 2808 CG1 ILE A1050 17.428 -46.665 -12.919 1.00 76.62 C ANISOU 2808 CG1 ILE A1050 9675 12077 7361 589 -602 1410 C ATOM 2809 CG2 ILE A1050 17.202 -45.122 -14.832 1.00 73.26 C ANISOU 2809 CG2 ILE A1050 9068 11410 7357 169 -605 1040 C ATOM 2810 CD1 ILE A1050 15.964 -46.979 -12.746 1.00 76.72 C ANISOU 2810 CD1 ILE A1050 9774 12040 7334 645 -261 1634 C ATOM 2811 N GLY A1051 20.232 -45.715 -11.228 1.00 79.71 N ANISOU 2811 N GLY A1051 10132 12804 7350 887 -1438 937 N ATOM 2812 CA GLY A1051 20.688 -45.752 -9.840 1.00 82.47 C ANISOU 2812 CA GLY A1051 10669 13377 7287 1216 -1673 907 C ATOM 2813 C GLY A1051 19.680 -46.402 -8.920 1.00 83.59 C ANISOU 2813 C GLY A1051 11057 13645 7056 1482 -1402 1228 C ATOM 2814 O GLY A1051 19.168 -45.765 -8.001 1.00 85.67 O ANISOU 2814 O GLY A1051 11553 14065 6932 1699 -1410 1158 O ATOM 2815 N ARG A1052 19.331 -47.645 -9.206 1.00 82.28 N ANISOU 2815 N ARG A1052 10830 13397 7032 1475 -1149 1583 N ATOM 2816 CA ARG A1052 18.283 -48.315 -8.459 1.00 83.57 C ANISOU 2816 CA ARG A1052 11171 13613 6966 1695 -804 1955 C ATOM 2817 C ARG A1052 18.233 -49.742 -8.943 1.00 83.08 C ANISOU 2817 C ARG A1052 10973 13429 7164 1675 -629 2303 C ATOM 2818 O ARG A1052 18.394 -50.008 -10.134 1.00 81.25 O ANISOU 2818 O ARG A1052 10497 13014 7361 1404 -640 2260 O ATOM 2819 CB ARG A1052 16.936 -47.630 -8.687 1.00 81.49 C ANISOU 2819 CB ARG A1052 10928 13242 6789 1561 -480 1977 C ATOM 2820 CG ARG A1052 15.734 -48.496 -8.345 1.00 82.43 C ANISOU 2820 CG ARG A1052 11161 13344 6811 1740 -58 2381 C ATOM 2821 CD ARG A1052 14.463 -47.666 -8.261 1.00 81.85 C ANISOU 2821 CD ARG A1052 11180 13242 6675 1714 189 2338 C ATOM 2822 NE ARG A1052 13.723 -47.669 -9.519 1.00 77.45 N ANISOU 2822 NE ARG A1052 10400 12432 6594 1383 354 2300 N ATOM 2823 CZ ARG A1052 13.452 -48.763 -10.224 1.00 76.31 C ANISOU 2823 CZ ARG A1052 10108 12086 6799 1301 653 2580 C ATOM 2824 NH1 ARG A1052 13.860 -49.949 -9.794 1.00 78.05 N ANISOU 2824 NH1 ARG A1052 10357 12305 6992 1503 861 2952 N ATOM 2825 NH2 ARG A1052 12.772 -48.672 -11.359 1.00 73.20 N ANISOU 2825 NH2 ARG A1052 9528 11476 6807 1027 734 2483 N ATOM 2826 N ASN A1053 18.026 -50.670 -8.022 1.00 85.37 N ANISOU 2826 N ASN A1053 11422 13812 7200 1976 -453 2652 N ATOM 2827 CA ASN A1053 18.138 -52.062 -8.385 1.00 85.15 C ANISOU 2827 CA ASN A1053 11262 13645 7446 1975 -249 3015 C ATOM 2828 C ASN A1053 16.919 -52.605 -9.094 1.00 82.89 C ANISOU 2828 C ASN A1053 10834 13114 7544 1782 155 3208 C ATOM 2829 O ASN A1053 16.218 -53.466 -8.608 1.00 85.04 O ANISOU 2829 O ASN A1053 11172 13342 7794 1950 499 3569 O ATOM 2830 CB ASN A1053 18.482 -52.868 -7.140 0.00 20.00 C ATOM 2831 CG ASN A1053 19.897 -52.596 -6.632 0.00 20.00 C ATOM 2832 OD1 ASN A1053 20.770 -52.157 -7.382 0.00 20.00 O ATOM 2833 ND2 ASN A1053 20.124 -52.851 -5.344 0.00 20.00 N ATOM 2834 N THR A1054 16.706 -52.081 -10.282 1.00 88.77 N ANISOU 2834 N THR A1054 11463 14399 7867 -620 -1171 4011 N ATOM 2835 CA THR A1054 15.521 -52.326 -11.062 1.00 85.66 C ANISOU 2835 CA THR A1054 11074 13722 7747 -570 -816 3821 C ATOM 2836 C THR A1054 15.094 -53.770 -11.201 1.00 85.98 C ANISOU 2836 C THR A1054 11044 13496 8128 -490 -699 4208 C ATOM 2837 O THR A1054 13.933 -54.064 -11.068 1.00 85.92 O ANISOU 2837 O THR A1054 11083 13394 8166 -524 -408 4167 O ATOM 2838 CB THR A1054 15.683 -51.708 -12.458 1.00 81.11 C ANISOU 2838 CB THR A1054 10382 12856 7579 -473 -766 3414 C ATOM 2839 OG1 THR A1054 16.789 -52.311 -13.120 1.00 79.84 O ANISOU 2839 OG1 THR A1054 10032 12471 7830 -340 -974 3575 O ATOM 2840 CG2 THR A1054 15.954 -50.254 -12.338 1.00 80.35 C ANISOU 2840 CG2 THR A1054 10375 12953 7198 -562 -814 2989 C ATOM 2841 N ASN A1055 16.028 -54.660 -11.485 1.00 86.72 N ANISOU 2841 N ASN A1055 11012 13452 8484 -385 -922 4575 N ATOM 2842 CA ASN A1055 15.724 -55.993 -11.950 1.00 86.16 C ANISOU 2842 CA ASN A1055 10856 13009 8868 -279 -827 4893 C ATOM 2843 C ASN A1055 15.236 -56.049 -13.382 1.00 81.25 C ANISOU 2843 C ASN A1055 10152 11986 8731 -200 -614 4573 C ATOM 2844 O ASN A1055 14.664 -57.025 -13.800 1.00 81.43 O ANISOU 2844 O ASN A1055 10161 11722 9057 -181 -445 4724 O ATOM 2845 CB ASN A1055 14.685 -56.626 -11.061 1.00 89.31 C ANISOU 2845 CB ASN A1055 11381 13511 9041 -384 -673 5257 C ATOM 2846 CG ASN A1055 14.987 -58.070 -10.766 1.00 90.94 C ANISOU 2846 CG ASN A1055 11517 13409 9627 -286 -711 5753 C ATOM 2847 OD1 ASN A1055 15.187 -58.876 -11.671 0.00 20.00 O ATOM 2848 ND2 ASN A1055 15.030 -58.405 -9.490 0.00 20.00 N ATOM 2849 N GLY A1056 15.478 -55.007 -14.142 1.00 77.16 N ANISOU 2849 N GLY A1056 9583 11450 8282 -171 -632 4143 N ATOM 2850 CA GLY A1056 15.040 -54.961 -15.540 1.00 73.41 C ANISOU 2850 CA GLY A1056 9027 10631 8231 -100 -466 3850 C ATOM 2851 C GLY A1056 13.657 -54.383 -15.814 1.00 71.23 C ANISOU 2851 C GLY A1056 8818 10363 7881 -190 -187 3547 C ATOM 2852 O GLY A1056 13.115 -54.579 -16.903 1.00 68.63 O ANISOU 2852 O GLY A1056 8423 9756 7896 -155 -45 3384 O ATOM 2853 N VAL A1057 13.087 -53.668 -14.842 1.00 72.77 N ANISOU 2853 N VAL A1057 9138 10884 7626 -305 -106 3468 N ATOM 2854 CA VAL A1057 11.781 -53.008 -15.012 1.00 70.73 C ANISOU 2854 CA VAL A1057 8921 10667 7284 -369 171 3182 C ATOM 2855 C VAL A1057 11.793 -51.572 -14.472 1.00 70.30 C ANISOU 2855 C VAL A1057 8973 10905 6832 -419 179 2854 C ATOM 2856 O VAL A1057 12.337 -51.295 -13.404 1.00 73.02 O ANISOU 2856 O VAL A1057 9428 11537 6779 -486 47 2939 O ATOM 2857 CB VAL A1057 10.642 -53.813 -14.350 1.00 72.80 C ANISOU 2857 CB VAL A1057 9231 10982 7448 -465 390 3443 C ATOM 2858 CG1 VAL A1057 10.921 -54.034 -12.872 1.00 76.94 C ANISOU 2858 CG1 VAL A1057 9887 11835 7511 -550 313 3747 C ATOM 2859 CG2 VAL A1057 9.306 -53.114 -14.558 1.00 71.68 C ANISOU 2859 CG2 VAL A1057 9085 10895 7254 -512 682 3155 C ATOM 2860 N ILE A1058 11.179 -50.662 -15.215 1.00 67.60 N ANISOU 2860 N ILE A1058 8604 10481 6598 -391 333 2481 N ATOM 2861 CA ILE A1058 11.237 -49.242 -14.882 1.00 67.24 C ANISOU 2861 CA ILE A1058 8660 10626 6259 -418 351 2129 C ATOM 2862 C ILE A1058 9.861 -48.599 -14.935 1.00 66.37 C ANISOU 2862 C ILE A1058 8572 10548 6097 -421 670 1890 C ATOM 2863 O ILE A1058 8.916 -49.183 -15.453 1.00 65.16 O ANISOU 2863 O ILE A1058 8315 10254 6189 -402 848 1970 O ATOM 2864 CB ILE A1058 12.193 -48.491 -15.825 1.00 64.27 C ANISOU 2864 CB ILE A1058 8217 10100 6102 -350 171 1880 C ATOM 2865 CG1 ILE A1058 11.718 -48.599 -17.277 1.00 60.89 C ANISOU 2865 CG1 ILE A1058 7644 9359 6131 -257 277 1755 C ATOM 2866 CG2 ILE A1058 13.603 -49.042 -15.694 1.00 64.97 C ANISOU 2866 CG2 ILE A1058 8254 10197 6232 -339 -139 2114 C ATOM 2867 CD1 ILE A1058 12.500 -47.727 -18.233 1.00 58.23 C ANISOU 2867 CD1 ILE A1058 7251 8893 5981 -199 152 1492 C ATOM 2868 N THR A1059 9.769 -47.390 -14.394 1.00 67.28 N ANISOU 2868 N THR A1059 8816 10843 5902 -447 740 1595 N ATOM 2869 CA THR A1059 8.534 -46.626 -14.408 1.00 67.75 C ANISOU 2869 CA THR A1059 8890 10933 5917 -417 1053 1343 C ATOM 2870 C THR A1059 8.458 -45.763 -15.660 1.00 65.77 C ANISOU 2870 C THR A1059 8541 10439 6007 -311 1068 1039 C ATOM 2871 O THR A1059 9.465 -45.526 -16.336 1.00 63.83 O ANISOU 2871 O THR A1059 8264 10053 5933 -285 841 968 O ATOM 2872 CB THR A1059 8.445 -45.653 -13.228 1.00 70.57 C ANISOU 2872 CB THR A1059 9459 11571 5780 -482 1156 1127 C ATOM 2873 OG1 THR A1059 9.308 -44.538 -13.472 1.00 69.28 O ANISOU 2873 OG1 THR A1059 9375 11356 5589 -475 994 817 O ATOM 2874 CG2 THR A1059 8.817 -46.330 -11.903 1.00 74.52 C ANISOU 2874 CG2 THR A1059 10099 12369 5846 -611 1070 1411 C ATOM 2875 N LYS A1060 7.256 -45.262 -15.926 1.00 67.17 N ANISOU 2875 N LYS A1060 8663 10589 6270 -250 1345 875 N ATOM 2876 CA LYS A1060 7.001 -44.350 -17.038 1.00 65.48 C ANISOU 2876 CA LYS A1060 8358 10171 6350 -140 1391 606 C ATOM 2877 C LYS A1060 7.795 -43.039 -16.917 1.00 65.62 C ANISOU 2877 C LYS A1060 8523 10182 6227 -130 1294 294 C ATOM 2878 O LYS A1060 8.260 -42.496 -17.924 1.00 63.56 O ANISOU 2878 O LYS A1060 8202 9722 6227 -73 1180 155 O ATOM 2879 CB LYS A1060 5.502 -44.049 -17.140 1.00 67.11 C ANISOU 2879 CB LYS A1060 8465 10396 6636 -70 1717 525 C ATOM 2880 CG LYS A1060 5.078 -43.616 -18.529 1.00 65.85 C ANISOU 2880 CG LYS A1060 8129 10007 6881 39 1733 401 C ATOM 2881 CD LYS A1060 3.647 -43.106 -18.549 1.00 68.59 C ANISOU 2881 CD LYS A1060 8363 10400 7296 129 2045 306 C ATOM 2882 CE LYS A1060 3.350 -42.379 -19.855 1.00 67.19 C ANISOU 2882 CE LYS A1060 8039 10018 7469 251 2032 156 C ATOM 2883 NZ LYS A1060 1.980 -41.793 -19.843 1.00 69.96 N ANISOU 2883 NZ LYS A1060 8256 10422 7903 366 2330 75 N ATOM 2884 N ASP A1061 7.955 -42.538 -15.695 1.00 68.01 N ANISOU 2884 N ASP A1061 9026 10702 6110 -203 1341 184 N ATOM 2885 CA ASP A1061 8.743 -41.330 -15.467 1.00 69.10 C ANISOU 2885 CA ASP A1061 9330 10836 6088 -236 1238 -121 C ATOM 2886 C ASP A1061 10.236 -41.569 -15.691 1.00 67.72 C ANISOU 2886 C ASP A1061 9152 10632 5947 -319 869 -27 C ATOM 2887 O ASP A1061 10.944 -40.691 -16.197 1.00 66.69 O ANISOU 2887 O ASP A1061 9045 10368 5925 -323 741 -240 O ATOM 2888 CB ASP A1061 8.497 -40.779 -14.057 1.00 74.13 C ANISOU 2888 CB ASP A1061 10205 11731 6229 -317 1391 -284 C ATOM 2889 CG ASP A1061 7.087 -40.229 -13.886 1.00 76.59 C ANISOU 2889 CG ASP A1061 10520 12049 6532 -205 1792 -460 C ATOM 2890 OD1 ASP A1061 6.552 -39.652 -14.865 1.00 75.59 O ANISOU 2890 OD1 ASP A1061 10265 11688 6764 -63 1905 -598 O ATOM 2891 OD2 ASP A1061 6.513 -40.372 -12.779 1.00 80.18 O ANISOU 2891 OD2 ASP A1061 11091 12750 6621 -253 1998 -446 O ATOM 2892 N GLU A1062 10.720 -42.749 -15.320 1.00 67.59 N ANISOU 2892 N GLU A1062 9091 10731 5857 -381 704 306 N ATOM 2893 CA GLU A1062 12.115 -43.089 -15.577 1.00 66.67 C ANISOU 2893 CA GLU A1062 8919 10586 5824 -430 365 440 C ATOM 2894 C GLU A1062 12.391 -43.170 -17.086 1.00 63.11 C ANISOU 2894 C GLU A1062 8278 9838 5861 -325 298 430 C ATOM 2895 O GLU A1062 13.429 -42.696 -17.569 1.00 61.34 O ANISOU 2895 O GLU A1062 8022 9535 5750 -343 97 339 O ATOM 2896 CB GLU A1062 12.486 -44.384 -14.865 1.00 68.34 C ANISOU 2896 CB GLU A1062 9111 10964 5890 -487 227 835 C ATOM 2897 CG GLU A1062 12.687 -44.179 -13.370 1.00 72.84 C ANISOU 2897 CG GLU A1062 9884 11874 5915 -629 181 847 C ATOM 2898 CD GLU A1062 12.559 -45.453 -12.555 1.00 75.81 C ANISOU 2898 CD GLU A1062 10262 12433 6108 -672 155 1265 C ATOM 2899 OE1 GLU A1062 12.104 -46.479 -13.111 1.00 74.63 O ANISOU 2899 OE1 GLU A1062 9968 12118 6267 -590 231 1519 O ATOM 2900 OE2 GLU A1062 12.906 -45.430 -11.349 1.00 79.56 O ANISOU 2900 OE2 GLU A1062 10892 13216 6119 -801 57 1344 O ATOM 2901 N ALA A1063 11.443 -43.744 -17.822 1.00 60.87 N ANISOU 2901 N ALA A1063 7869 9407 5849 -231 471 519 N ATOM 2902 CA ALA A1063 11.546 -43.865 -19.268 1.00 57.24 C ANISOU 2902 CA ALA A1063 7247 8689 5813 -142 436 502 C ATOM 2903 C ALA A1063 11.717 -42.503 -19.929 1.00 55.99 C ANISOU 2903 C ALA A1063 7109 8410 5752 -108 445 188 C ATOM 2904 O ALA A1063 12.576 -42.313 -20.789 1.00 53.31 O ANISOU 2904 O ALA A1063 6695 7936 5624 -94 289 154 O ATOM 2905 CB ALA A1063 10.306 -44.549 -19.808 1.00 56.44 C ANISOU 2905 CB ALA A1063 7032 8492 5917 -84 638 603 C ATOM 2906 N GLU A1064 10.886 -41.561 -19.511 1.00 57.91 N ANISOU 2906 N GLU A1064 7456 8697 5851 -91 646 -31 N ATOM 2907 CA GLU A1064 10.904 -40.215 -20.061 1.00 57.20 C ANISOU 2907 CA GLU A1064 7405 8462 5863 -48 691 -322 C ATOM 2908 C GLU A1064 12.134 -39.430 -19.605 1.00 57.24 C ANISOU 2908 C GLU A1064 7543 8508 5695 -160 492 -477 C ATOM 2909 O GLU A1064 12.573 -38.511 -20.290 1.00 56.26 O ANISOU 2909 O GLU A1064 7420 8221 5734 -153 441 -653 O ATOM 2910 CB GLU A1064 9.605 -39.481 -19.705 1.00 59.80 C ANISOU 2910 CB GLU A1064 7797 8805 6117 29 992 -502 C ATOM 2911 CG GLU A1064 8.368 -40.087 -20.373 1.00 60.33 C ANISOU 2911 CG GLU A1064 7682 8817 6422 135 1173 -365 C ATOM 2912 CD GLU A1064 7.044 -39.484 -19.896 1.00 64.75 C ANISOU 2912 CD GLU A1064 8262 9433 6906 224 1489 -496 C ATOM 2913 OE1 GLU A1064 6.898 -39.224 -18.673 1.00 69.41 O ANISOU 2913 OE1 GLU A1064 9016 10195 7159 179 1611 -589 O ATOM 2914 OE2 GLU A1064 6.136 -39.284 -20.743 1.00 64.53 O ANISOU 2914 OE2 GLU A1064 8075 9293 7150 341 1620 -501 O ATOM 2915 N LYS A1065 12.708 -39.795 -18.466 1.00 59.30 N ANISOU 2915 N LYS A1065 7909 8992 5627 -280 368 -395 N ATOM 2916 CA LYS A1065 13.938 -39.149 -18.010 1.00 60.50 C ANISOU 2916 CA LYS A1065 8163 9218 5606 -422 136 -517 C ATOM 2917 C LYS A1065 15.076 -39.521 -18.956 1.00 57.68 C ANISOU 2917 C LYS A1065 7625 8751 5539 -423 -109 -372 C ATOM 2918 O LYS A1065 15.741 -38.643 -19.496 1.00 57.82 O ANISOU 2918 O LYS A1065 7637 8646 5686 -464 -201 -541 O ATOM 2919 CB LYS A1065 14.268 -39.553 -16.573 1.00 64.24 C ANISOU 2919 CB LYS A1065 8773 9999 5634 -560 33 -422 C ATOM 2920 CG LYS A1065 15.270 -38.639 -15.883 1.00 67.13 C ANISOU 2920 CG LYS A1065 9294 10481 5729 -743 -165 -631 C ATOM 2921 CD LYS A1065 15.914 -39.492 -14.921 0.00 20.00 C ATOM 2922 CE LYS A1065 15.331 -39.435 -13.513 0.00 20.00 C ATOM 2923 NZ LYS A1065 16.373 -39.371 -12.454 0.00 20.00 N ATOM 2924 N LEU A1066 15.270 -40.821 -19.177 1.00 56.03 N ANISOU 2924 N LEU A1066 7268 8569 5452 -373 -191 -60 N ATOM 2925 CA LEU A1066 16.252 -41.319 -20.152 1.00 53.49 C ANISOU 2925 CA LEU A1066 6755 8127 5440 -336 -370 87 C ATOM 2926 C LEU A1066 16.039 -40.741 -21.539 1.00 50.31 C ANISOU 2926 C LEU A1066 6268 7473 5372 -250 -273 -61 C ATOM 2927 O LEU A1066 17.000 -40.432 -22.224 1.00 49.67 O ANISOU 2927 O LEU A1066 6095 7311 5464 -270 -410 -86 O ATOM 2928 CB LEU A1066 16.183 -42.836 -20.288 1.00 52.84 C ANISOU 2928 CB LEU A1066 6546 8041 5487 -257 -388 417 C ATOM 2929 CG LEU A1066 16.566 -43.699 -19.094 1.00 56.62 C ANISOU 2929 CG LEU A1066 7059 8746 5707 -318 -524 680 C ATOM 2930 CD1 LEU A1066 16.213 -45.149 -19.392 1.00 56.38 C ANISOU 2930 CD1 LEU A1066 6921 8622 5878 -219 -470 984 C ATOM 2931 CD2 LEU A1066 18.043 -43.561 -18.777 1.00 58.39 C ANISOU 2931 CD2 LEU A1066 7221 9093 5868 -401 -824 751 C ATOM 2932 N PHE A1067 14.783 -40.632 -21.961 1.00 48.94 N ANISOU 2932 N PHE A1067 6107 7196 5289 -157 -40 -133 N ATOM 2933 CA PHE A1067 14.461 -40.183 -23.310 1.00 47.20 C ANISOU 2933 CA PHE A1067 5798 6761 5373 -70 45 -229 C ATOM 2934 C PHE A1067 14.951 -38.762 -23.545 1.00 47.76 C ANISOU 2934 C PHE A1067 5942 6743 5460 -120 11 -470 C ATOM 2935 O PHE A1067 15.606 -38.485 -24.538 1.00 44.98 O ANISOU 2935 O PHE A1067 5497 6266 5327 -115 -68 -480 O ATOM 2936 CB PHE A1067 12.948 -40.259 -23.577 1.00 47.02 C ANISOU 2936 CB PHE A1067 5764 6685 5416 27 287 -249 C ATOM 2937 CG PHE A1067 12.546 -39.713 -24.919 1.00 45.43 C ANISOU 2937 CG PHE A1067 5473 6294 5491 110 360 -335 C ATOM 2938 CD1 PHE A1067 12.626 -40.496 -26.049 1.00 43.74 C ANISOU 2938 CD1 PHE A1067 5115 5987 5515 151 320 -205 C ATOM 2939 CD2 PHE A1067 12.108 -38.407 -25.053 1.00 46.73 C ANISOU 2939 CD2 PHE A1067 5711 6371 5673 147 468 -543 C ATOM 2940 CE1 PHE A1067 12.280 -39.989 -27.288 1.00 42.31 C ANISOU 2940 CE1 PHE A1067 4862 5668 5547 211 369 -269 C ATOM 2941 CE2 PHE A1067 11.758 -37.894 -26.292 1.00 44.70 C ANISOU 2941 CE2 PHE A1067 5368 5952 5663 226 516 -580 C ATOM 2942 CZ PHE A1067 11.846 -38.689 -27.409 1.00 42.66 C ANISOU 2942 CZ PHE A1067 4963 5641 5603 250 458 -437 C ATOM 2943 N ASN A1068 14.624 -37.868 -22.616 1.00 50.97 N ANISOU 2943 N ASN A1068 6525 7207 5633 -174 86 -667 N ATOM 2944 CA ASN A1068 15.069 -36.490 -22.698 1.00 51.71 C ANISOU 2944 CA ASN A1068 6723 7187 5734 -243 62 -914 C ATOM 2945 C ASN A1068 16.584 -36.394 -22.738 1.00 51.86 C ANISOU 2945 C ASN A1068 6695 7247 5762 -385 -203 -885 C ATOM 2946 O ASN A1068 17.124 -35.560 -23.464 1.00 52.15 O ANISOU 2946 O ASN A1068 6709 7128 5976 -423 -248 -989 O ATOM 2947 CB ASN A1068 14.506 -35.678 -21.538 1.00 55.49 C ANISOU 2947 CB ASN A1068 7428 7730 5925 -289 195 -1148 C ATOM 2948 CG ASN A1068 12.985 -35.620 -21.553 1.00 55.94 C ANISOU 2948 CG ASN A1068 7500 7738 6014 -130 489 -1189 C ATOM 2949 OD1 ASN A1068 12.353 -35.614 -22.621 1.00 54.98 O ANISOU 2949 OD1 ASN A1068 7248 7463 6179 4 591 -1132 O ATOM 2950 ND2 ASN A1068 12.387 -35.581 -20.367 1.00 58.48 N ANISOU 2950 ND2 ASN A1068 7971 8214 6032 -149 628 -1280 N ATOM 2951 N GLN A1069 17.263 -37.278 -22.053 1.00 52.75 N ANISOU 2951 N GLN A1069 6771 7570 5700 -462 -378 -715 N ATOM 2952 CA GLN A1069 18.698 -37.316 -22.132 1.00 53.20 C ANISOU 2952 CA GLN A1069 6717 7697 5796 -580 -646 -629 C ATOM 2953 C GLN A1069 19.221 -37.768 -23.464 1.00 50.77 C ANISOU 2953 C GLN A1069 6189 7246 5853 -488 -676 -485 C ATOM 2954 O GLN A1069 20.136 -37.197 -23.974 1.00 51.48 O ANISOU 2954 O GLN A1069 6206 7273 6080 -567 -784 -540 O ATOM 2955 CB GLN A1069 19.225 -38.226 -21.070 1.00 55.63 C ANISOU 2955 CB GLN A1069 7008 8273 5856 -650 -828 -424 C ATOM 2956 CG GLN A1069 19.166 -37.605 -19.703 1.00 59.89 C ANISOU 2956 CG GLN A1069 7770 9008 5975 -812 -875 -586 C ATOM 2957 CD GLN A1069 19.446 -38.600 -18.610 0.00 62.04 C ANISOU 2957 CD GLN A1069 8035 9572 5962 -868 -1039 -338 C ATOM 2958 OE1 GLN A1069 19.019 -38.431 -17.477 0.00 20.00 O ATOM 2959 NE2 GLN A1069 20.177 -39.646 -18.945 0.00 20.00 N ATOM 2960 N ASP A1070 18.648 -38.815 -24.018 1.00 48.51 N ANISOU 2960 N ASP A1070 5804 6911 5717 -338 -570 -314 N ATOM 2961 CA ASP A1070 19.075 -39.324 -25.322 1.00 46.88 C ANISOU 2961 CA ASP A1070 5411 6576 5822 -250 -574 -198 C ATOM 2962 C ASP A1070 18.786 -38.335 -26.473 1.00 46.18 C ANISOU 2962 C ASP A1070 5325 6293 5925 -224 -459 -359 C ATOM 2963 O ASP A1070 19.478 -38.320 -27.477 1.00 46.78 O ANISOU 2963 O ASP A1070 5273 6291 6209 -213 -496 -317 O ATOM 2964 CB ASP A1070 18.396 -40.667 -25.642 1.00 45.65 C ANISOU 2964 CB ASP A1070 5186 6394 5765 -118 -477 -12 C ATOM 2965 CG ASP A1070 18.771 -41.804 -24.654 1.00 47.92 C ANISOU 2965 CG ASP A1070 5445 6840 5922 -123 -593 215 C ATOM 2966 OD1 ASP A1070 19.954 -41.920 -24.245 1.00 49.45 O ANISOU 2966 OD1 ASP A1070 5559 7145 6084 -182 -792 314 O ATOM 2967 OD2 ASP A1070 17.870 -42.618 -24.312 1.00 46.95 O ANISOU 2967 OD2 ASP A1070 5364 6729 5745 -68 -487 322 O ATOM 2968 N VAL A1071 17.746 -37.531 -26.350 1.00 46.82 N ANISOU 2968 N VAL A1071 5546 6297 5943 -202 -307 -523 N ATOM 2969 CA VAL A1071 17.428 -36.540 -27.375 1.00 45.60 C ANISOU 2969 CA VAL A1071 5400 5954 5969 -167 -206 -643 C ATOM 2970 C VAL A1071 18.374 -35.350 -27.251 1.00 46.55 C ANISOU 2970 C VAL A1071 5579 6020 6086 -311 -310 -786 C ATOM 2971 O VAL A1071 18.833 -34.814 -28.252 1.00 45.55 O ANISOU 2971 O VAL A1071 5384 5769 6154 -327 -318 -791 O ATOM 2972 CB VAL A1071 15.963 -36.075 -27.272 1.00 45.33 C ANISOU 2972 CB VAL A1071 5472 5846 5904 -69 -1 -747 C ATOM 2973 CG1 VAL A1071 15.701 -34.899 -28.196 1.00 45.26 C ANISOU 2973 CG1 VAL A1071 5484 5637 6075 -34 82 -855 C ATOM 2974 CG2 VAL A1071 15.040 -37.219 -27.627 1.00 43.98 C ANISOU 2974 CG2 VAL A1071 5207 5714 5788 45 93 -595 C ATOM 2975 N ASP A1072 18.641 -34.937 -26.018 1.00 48.65 N ANISOU 2975 N ASP A1072 5979 6385 6119 -434 -387 -905 N ATOM 2976 CA ASP A1072 19.698 -33.974 -25.739 1.00 51.84 C ANISOU 2976 CA ASP A1072 6431 6772 6495 -622 -534 -1035 C ATOM 2977 C ASP A1072 20.979 -34.425 -26.430 1.00 50.37 C ANISOU 2977 C ASP A1072 6022 6637 6479 -677 -701 -865 C ATOM 2978 O ASP A1072 21.619 -33.647 -27.129 1.00 50.69 O ANISOU 2978 O ASP A1072 6014 6559 6686 -759 -732 -911 O ATOM 2979 CB ASP A1072 19.921 -33.875 -24.222 1.00 56.36 C ANISOU 2979 CB ASP A1072 7151 7527 6733 -767 -642 -1140 C ATOM 2980 CG ASP A1072 20.986 -32.847 -23.828 1.00 61.12 C ANISOU 2980 CG ASP A1072 7820 8123 7278 -1007 -815 -1305 C ATOM 2981 OD1 ASP A1072 22.202 -33.083 -24.057 1.00 63.41 O ANISOU 2981 OD1 ASP A1072 7932 8506 7653 -1117 -1022 -1179 O ATOM 2982 OD2 ASP A1072 20.604 -31.811 -23.238 1.00 64.78 O ANISOU 2982 OD2 ASP A1072 8512 8490 7609 -1093 -740 -1570 O ATOM 2983 N ALA A1073 21.337 -35.692 -26.224 1.00 49.33 N ANISOU 2983 N ALA A1073 5751 6673 6318 -623 -792 -657 N ATOM 2984 CA ALA A1073 22.531 -36.289 -26.816 1.00 47.77 C ANISOU 2984 CA ALA A1073 5317 6537 6294 -633 -926 -476 C ATOM 2985 C ALA A1073 22.523 -36.213 -28.334 1.00 45.32 C ANISOU 2985 C ALA A1073 4896 6060 6263 -541 -801 -441 C ATOM 2986 O ALA A1073 23.540 -35.948 -28.947 1.00 46.97 O ANISOU 2986 O ALA A1073 4960 6261 6625 -609 -870 -400 O ATOM 2987 CB ALA A1073 22.654 -37.734 -26.381 1.00 47.17 C ANISOU 2987 CB ALA A1073 5133 6615 6171 -536 -991 -251 C ATOM 2988 N ALA A1074 21.376 -36.449 -28.940 1.00 43.69 N ANISOU 2988 N ALA A1074 4748 5742 6109 -396 -618 -450 N ATOM 2989 CA ALA A1074 21.279 -36.498 -30.393 1.00 42.68 C ANISOU 2989 CA ALA A1074 4526 5490 6199 -310 -505 -404 C ATOM 2990 C ALA A1074 21.391 -35.105 -31.031 1.00 43.61 C ANISOU 2990 C ALA A1074 4699 5460 6411 -393 -463 -522 C ATOM 2991 O ALA A1074 21.956 -34.963 -32.119 1.00 43.33 O ANISOU 2991 O ALA A1074 4549 5374 6540 -400 -440 -461 O ATOM 2992 CB ALA A1074 19.982 -37.170 -30.804 1.00 40.61 C ANISOU 2992 CB ALA A1074 4305 5178 5946 -158 -351 -373 C ATOM 2993 N VAL A1075 20.872 -34.080 -30.362 1.00 44.53 N ANISOU 2993 N VAL A1075 4995 5498 6427 -454 -440 -686 N ATOM 2994 CA VAL A1075 20.938 -32.732 -30.919 1.00 45.44 C ANISOU 2994 CA VAL A1075 5182 5427 6656 -528 -393 -788 C ATOM 2995 C VAL A1075 22.334 -32.149 -30.751 1.00 46.59 C ANISOU 2995 C VAL A1075 5263 5595 6842 -736 -548 -810 C ATOM 2996 O VAL A1075 22.815 -31.450 -31.622 1.00 46.98 O ANISOU 2996 O VAL A1075 5263 5530 7057 -802 -528 -790 O ATOM 2997 CB VAL A1075 19.852 -31.814 -30.337 1.00 47.33 C ANISOU 2997 CB VAL A1075 5639 5526 6817 -497 -280 -966 C ATOM 2998 CG1 VAL A1075 19.913 -30.437 -30.969 1.00 48.65 C ANISOU 2998 CG1 VAL A1075 5883 5454 7145 -556 -223 -1045 C ATOM 2999 CG2 VAL A1075 18.488 -32.417 -30.608 1.00 46.78 C ANISOU 2999 CG2 VAL A1075 5575 5457 6740 -296 -129 -911 C ATOM 3000 N ARG A1076 23.005 -32.458 -29.655 1.00 48.27 N ANISOU 3000 N ARG A1076 5460 5975 6903 -850 -712 -830 N ATOM 3001 CA ARG A1076 24.389 -32.030 -29.503 1.00 50.23 C ANISOU 3001 CA ARG A1076 5595 6289 7198 -1062 -890 -823 C ATOM 3002 C ARG A1076 25.257 -32.626 -30.607 1.00 48.51 C ANISOU 3002 C ARG A1076 5112 6129 7189 -1020 -894 -623 C ATOM 3003 O ARG A1076 26.009 -31.911 -31.265 1.00 49.31 O ANISOU 3003 O ARG A1076 5128 6161 7446 -1144 -905 -611 O ATOM 3004 CB ARG A1076 24.916 -32.400 -28.125 1.00 53.01 C ANISOU 3004 CB ARG A1076 5954 6861 7326 -1183 -1091 -844 C ATOM 3005 CG ARG A1076 24.260 -31.592 -27.033 1.00 56.18 C ANISOU 3005 CG ARG A1076 6637 7209 7500 -1279 -1083 -1088 C ATOM 3006 CD ARG A1076 24.908 -31.835 -25.692 1.00 60.54 C ANISOU 3006 CD ARG A1076 7204 8006 7790 -1449 -1311 -1114 C ATOM 3007 NE ARG A1076 24.093 -31.285 -24.606 1.00 64.65 N ANISOU 3007 NE ARG A1076 8020 8506 8036 -1502 -1257 -1354 N ATOM 3008 CZ ARG A1076 24.000 -29.985 -24.290 1.00 68.11 C ANISOU 3008 CZ ARG A1076 8677 8768 8431 -1664 -1226 -1630 C ATOM 3009 NH1 ARG A1076 24.667 -29.060 -24.983 1.00 69.10 N ANISOU 3009 NH1 ARG A1076 8759 8710 8782 -1808 -1256 -1685 N ATOM 3010 NH2 ARG A1076 23.228 -29.599 -23.267 1.00 69.63 N ANISOU 3010 NH2 ARG A1076 9142 8957 8357 -1687 -1146 -1859 N ATOM 3011 N GLY A1077 25.127 -33.930 -30.823 1.00 46.87 N ANISOU 3011 N GLY A1077 4782 6034 6990 -846 -863 -471 N ATOM 3012 CA GLY A1077 25.792 -34.602 -31.942 1.00 45.76 C ANISOU 3012 CA GLY A1077 4414 5928 7044 -764 -811 -307 C ATOM 3013 C GLY A1077 25.646 -33.862 -33.263 1.00 44.34 C ANISOU 3013 C GLY A1077 4243 5587 7015 -764 -659 -321 C ATOM 3014 O GLY A1077 26.634 -33.567 -33.924 1.00 44.83 O ANISOU 3014 O GLY A1077 4145 5668 7220 -853 -667 -252 O ATOM 3015 N ILE A1078 24.410 -33.541 -33.635 1.00 42.08 N ANISOU 3015 N ILE A1078 4133 5158 6697 -669 -523 -391 N ATOM 3016 CA ILE A1078 24.150 -32.775 -34.851 1.00 41.11 C ANISOU 3016 CA ILE A1078 4039 4887 6693 -666 -393 -378 C ATOM 3017 C ILE A1078 24.845 -31.407 -34.858 1.00 43.57 C ANISOU 3017 C ILE A1078 4378 5085 7088 -872 -442 -432 C ATOM 3018 O ILE A1078 25.456 -31.029 -35.851 1.00 43.48 O ANISOU 3018 O ILE A1078 4264 5042 7211 -933 -390 -343 O ATOM 3019 CB ILE A1078 22.645 -32.531 -35.046 1.00 39.19 C ANISOU 3019 CB ILE A1078 3974 4516 6398 -536 -271 -436 C ATOM 3020 CG1 ILE A1078 21.919 -33.840 -35.341 1.00 36.85 C ANISOU 3020 CG1 ILE A1078 3637 4310 6054 -360 -205 -368 C ATOM 3021 CG2 ILE A1078 22.400 -31.544 -36.181 1.00 39.10 C ANISOU 3021 CG2 ILE A1078 4005 4347 6504 -549 -170 -400 C ATOM 3022 CD1 ILE A1078 20.424 -33.744 -35.108 1.00 36.40 C ANISOU 3022 CD1 ILE A1078 3726 4182 5922 -248 -123 -427 C ATOM 3023 N LEU A1079 24.741 -30.668 -33.761 1.00 45.79 N ANISOU 3023 N LEU A1079 4809 5301 7284 -989 -531 -584 N ATOM 3024 CA LEU A1079 25.188 -29.277 -33.744 1.00 49.08 C ANISOU 3024 CA LEU A1079 5309 5546 7790 -1192 -559 -671 C ATOM 3025 C LEU A1079 26.708 -29.161 -33.717 1.00 52.08 C ANISOU 3025 C LEU A1079 5488 6043 8257 -1409 -700 -608 C ATOM 3026 O LEU A1079 27.250 -28.135 -34.126 1.00 54.60 O ANISOU 3026 O LEU A1079 5808 6225 8710 -1587 -698 -613 O ATOM 3027 CB LEU A1079 24.570 -28.507 -32.568 1.00 50.89 C ANISOU 3027 CB LEU A1079 5790 5649 7895 -1257 -590 -894 C ATOM 3028 CG LEU A1079 23.031 -28.471 -32.516 1.00 49.93 C ANISOU 3028 CG LEU A1079 5853 5405 7713 -1043 -431 -963 C ATOM 3029 CD1 LEU A1079 22.552 -27.886 -31.202 1.00 51.56 C ANISOU 3029 CD1 LEU A1079 6289 5536 7764 -1101 -447 -1200 C ATOM 3030 CD2 LEU A1079 22.430 -27.711 -33.692 1.00 49.88 C ANISOU 3030 CD2 LEU A1079 5893 5171 7885 -956 -277 -892 C ATOM 3031 N ARG A1080 27.407 -30.198 -33.256 1.00 52.73 N ANISOU 3031 N ARG A1080 5381 6370 8282 -1397 -821 -528 N ATOM 3032 CA ARG A1080 28.872 -30.170 -33.258 1.00 54.48 C ANISOU 3032 CA ARG A1080 5352 6736 8608 -1584 -957 -436 C ATOM 3033 C ARG A1080 29.445 -30.855 -34.488 1.00 51.73 C ANISOU 3033 C ARG A1080 4751 6479 8422 -1473 -841 -238 C ATOM 3034 O ARG A1080 30.646 -31.014 -34.577 1.00 52.76 O ANISOU 3034 O ARG A1080 4625 6757 8662 -1580 -921 -131 O ATOM 3035 CB ARG A1080 29.422 -30.856 -32.019 1.00 58.55 C ANISOU 3035 CB ARG A1080 5774 7485 8986 -1637 -1174 -433 C ATOM 3036 CG ARG A1080 29.211 -32.367 -32.017 1.00 60.46 C ANISOU 3036 CG ARG A1080 5896 7889 9185 -1385 -1145 -292 C ATOM 3037 CD ARG A1080 30.328 -33.097 -31.288 1.00 66.35 C ANISOU 3037 CD ARG A1080 6390 8895 9923 -1441 -1357 -161 C ATOM 3038 NE ARG A1080 30.053 -34.529 -31.199 1.00 68.64 N ANISOU 3038 NE ARG A1080 6601 9291 10186 -1191 -1323 -24 N ATOM 3039 CZ ARG A1080 29.277 -35.109 -30.276 1.00 71.05 C ANISOU 3039 CZ ARG A1080 7063 9640 10291 -1101 -1370 -50 C ATOM 3040 NH1 ARG A1080 28.672 -34.395 -29.316 1.00 72.47 N ANISOU 3040 NH1 ARG A1080 7494 9789 10252 -1227 -1443 -227 N ATOM 3041 NH2 ARG A1080 29.106 -36.428 -30.314 1.00 70.96 N ANISOU 3041 NH2 ARG A1080 6963 9694 10304 -883 -1326 99 N ATOM 3042 N ASN A1081 28.594 -31.275 -35.422 1.00 47.69 N ANISOU 3042 N ASN A1081 4305 5894 7918 -1265 -650 -194 N ATOM 3043 CA ASN A1081 29.033 -32.061 -36.566 1.00 46.22 C ANISOU 3043 CA ASN A1081 3917 5804 7840 -1142 -516 -41 C ATOM 3044 C ASN A1081 29.099 -31.215 -37.823 1.00 46.24 C ANISOU 3044 C ASN A1081 3929 5689 7948 -1208 -365 14 C ATOM 3045 O ASN A1081 28.110 -30.699 -38.278 1.00 44.93 O ANISOU 3045 O ASN A1081 3962 5364 7744 -1155 -270 -21 O ATOM 3046 CB ASN A1081 28.098 -33.266 -36.766 1.00 43.47 C ANISOU 3046 CB ASN A1081 3628 5484 7403 -885 -419 -31 C ATOM 3047 CG ASN A1081 28.715 -34.364 -37.602 1.00 42.52 C ANISOU 3047 CG ASN A1081 3290 5488 7376 -753 -311 90 C ATOM 3048 OD1 ASN A1081 28.906 -34.233 -38.801 1.00 42.38 O ANISOU 3048 OD1 ASN A1081 3217 5458 7428 -741 -155 145 O ATOM 3049 ND2 ASN A1081 29.012 -35.461 -36.968 1.00 42.93 N ANISOU 3049 ND2 ASN A1081 3229 5655 7424 -648 -381 134 N ATOM 3050 N ALA A1082 30.282 -31.077 -38.388 1.00 49.53 N ANISOU 3050 N ALA A1082 4115 6200 8505 -1323 -340 127 N ATOM 3051 CA ALA A1082 30.466 -30.301 -39.610 1.00 50.95 C ANISOU 3051 CA ALA A1082 4284 6296 8777 -1405 -187 217 C ATOM 3052 C ALA A1082 29.503 -30.700 -40.726 1.00 49.60 C ANISOU 3052 C ALA A1082 4231 6087 8526 -1209 2 254 C ATOM 3053 O ALA A1082 29.113 -29.848 -41.510 1.00 51.61 O ANISOU 3053 O ALA A1082 4602 6213 8793 -1260 95 304 O ATOM 3054 CB ALA A1082 31.899 -30.419 -40.093 1.00 52.84 C ANISOU 3054 CB ALA A1082 4206 6702 9167 -1516 -152 352 C ATOM 3055 N LYS A1083 29.101 -31.970 -40.785 1.00 47.59 N ANISOU 3055 N LYS A1083 3953 5937 8190 -998 48 236 N ATOM 3056 CA LYS A1083 28.319 -32.484 -41.911 1.00 46.29 C ANISOU 3056 CA LYS A1083 3870 5776 7939 -841 218 263 C ATOM 3057 C LYS A1083 26.800 -32.467 -41.673 1.00 44.23 C ANISOU 3057 C LYS A1083 3856 5396 7553 -728 195 180 C ATOM 3058 O LYS A1083 26.021 -32.609 -42.619 1.00 45.38 O ANISOU 3058 O LYS A1083 4090 5532 7620 -641 303 210 O ATOM 3059 CB LYS A1083 28.795 -33.904 -42.241 1.00 48.03 C ANISOU 3059 CB LYS A1083 3922 6158 8167 -689 308 280 C ATOM 3060 CG LYS A1083 28.495 -34.394 -43.660 1.00 49.25 C ANISOU 3060 CG LYS A1083 4101 6363 8247 -592 516 310 C ATOM 3061 CD LYS A1083 29.378 -35.567 -44.076 1.00 50.89 C ANISOU 3061 CD LYS A1083 4103 6712 8520 -482 647 324 C ATOM 3062 CE LYS A1083 30.802 -35.099 -44.397 1.00 55.05 C ANISOU 3062 CE LYS A1083 4377 7344 9193 -605 713 434 C ATOM 3063 NZ LYS A1083 31.909 -36.077 -44.100 1.00 56.34 N ANISOU 3063 NZ LYS A1083 4263 7634 9508 -508 748 464 N ATOM 3064 N LEU A1084 26.373 -32.305 -40.422 1.00 42.81 N ANISOU 3064 N LEU A1084 3774 5146 7343 -736 57 80 N ATOM 3065 CA LEU A1084 24.952 -32.291 -40.066 1.00 39.73 C ANISOU 3065 CA LEU A1084 3587 4657 6849 -624 47 2 C ATOM 3066 C LEU A1084 24.433 -30.895 -39.668 1.00 40.45 C ANISOU 3066 C LEU A1084 3851 4550 6967 -713 10 -49 C ATOM 3067 O LEU A1084 23.269 -30.564 -39.931 1.00 40.06 O ANISOU 3067 O LEU A1084 3944 4395 6880 -618 62 -55 O ATOM 3068 CB LEU A1084 24.674 -33.272 -38.924 1.00 38.14 C ANISOU 3068 CB LEU A1084 3391 4527 6572 -534 -40 -76 C ATOM 3069 CG LEU A1084 25.136 -34.716 -39.092 1.00 37.57 C ANISOU 3069 CG LEU A1084 3167 4602 6505 -426 -10 -30 C ATOM 3070 CD1 LEU A1084 24.820 -35.503 -37.840 1.00 37.05 C ANISOU 3070 CD1 LEU A1084 3130 4577 6368 -358 -114 -76 C ATOM 3071 CD2 LEU A1084 24.532 -35.410 -40.299 1.00 36.73 C ANISOU 3071 CD2 LEU A1084 3079 4512 6363 -306 137 -3 C ATOM 3072 N LYS A1085 25.256 -30.078 -39.024 1.00 41.64 N ANISOU 3072 N LYS A1085 3988 4639 7192 -893 -80 -91 N ATOM 3073 CA LYS A1085 24.778 -28.770 -38.581 1.00 43.41 C ANISOU 3073 CA LYS A1085 4403 4634 7457 -977 -101 -174 C ATOM 3074 C LYS A1085 24.222 -27.873 -39.712 1.00 43.20 C ANISOU 3074 C LYS A1085 4464 4437 7511 -955 17 -62 C ATOM 3075 O LYS A1085 23.108 -27.333 -39.591 1.00 42.20 O ANISOU 3075 O LYS A1085 4506 4145 7382 -856 55 -101 O ATOM 3076 CB LYS A1085 25.844 -28.026 -37.784 1.00 46.51 C ANISOU 3076 CB LYS A1085 4769 4981 7919 -1218 -224 -249 C ATOM 3077 CG LYS A1085 25.377 -26.642 -37.352 1.00 49.44 C ANISOU 3077 CG LYS A1085 5366 5067 8349 -1316 -225 -365 C ATOM 3078 CD LYS A1085 26.035 -26.187 -36.061 1.00 52.47 C ANISOU 3078 CD LYS A1085 5800 5429 8708 -1527 -381 -542 C ATOM 3079 CE LYS A1085 25.595 -24.789 -35.664 1.00 54.58 C ANISOU 3079 CE LYS A1085 6318 5371 9050 -1630 -356 -691 C ATOM 3080 NZ LYS A1085 26.166 -23.781 -36.585 1.00 57.01 N ANISOU 3080 NZ LYS A1085 6603 5492 9566 -1790 -303 -569 N ATOM 3081 N PRO A1086 24.981 -27.708 -40.808 1.00 43.14 N ANISOU 3081 N PRO A1086 4335 4478 7576 -1039 82 94 N ATOM 3082 CA PRO A1086 24.423 -26.932 -41.921 1.00 43.14 C ANISOU 3082 CA PRO A1086 4420 4347 7623 -1012 186 242 C ATOM 3083 C PRO A1086 23.076 -27.435 -42.443 1.00 41.31 C ANISOU 3083 C PRO A1086 4262 4151 7281 -791 243 282 C ATOM 3084 O PRO A1086 22.276 -26.623 -42.907 1.00 42.72 O ANISOU 3084 O PRO A1086 4555 4170 7505 -738 284 370 O ATOM 3085 CB PRO A1086 25.484 -27.029 -43.019 1.00 43.91 C ANISOU 3085 CB PRO A1086 4348 4581 7755 -1122 264 407 C ATOM 3086 CG PRO A1086 26.529 -27.951 -42.520 1.00 44.75 C ANISOU 3086 CG PRO A1086 4260 4891 7851 -1169 214 343 C ATOM 3087 CD PRO A1086 26.374 -28.107 -41.042 1.00 44.32 C ANISOU 3087 CD PRO A1086 4264 4800 7776 -1168 70 159 C ATOM 3088 N VAL A1087 22.823 -28.745 -42.355 1.00 38.62 N ANISOU 3088 N VAL A1087 3850 4009 6813 -670 239 228 N ATOM 3089 CA VAL A1087 21.635 -29.350 -42.954 1.00 36.64 C ANISOU 3089 CA VAL A1087 3638 3829 6452 -499 283 269 C ATOM 3090 C VAL A1087 20.456 -29.132 -42.039 1.00 35.86 C ANISOU 3090 C VAL A1087 3664 3610 6351 -385 245 168 C ATOM 3091 O VAL A1087 19.405 -28.673 -42.481 1.00 35.50 O ANISOU 3091 O VAL A1087 3688 3485 6315 -286 275 245 O ATOM 3092 CB VAL A1087 21.816 -30.861 -43.217 1.00 35.27 C ANISOU 3092 CB VAL A1087 3354 3881 6164 -430 305 235 C ATOM 3093 CG1 VAL A1087 20.640 -31.411 -43.993 1.00 34.36 C ANISOU 3093 CG1 VAL A1087 3281 3841 5932 -305 342 280 C ATOM 3094 CG2 VAL A1087 23.089 -31.117 -43.983 1.00 36.09 C ANISOU 3094 CG2 VAL A1087 3318 4107 6284 -527 372 307 C ATOM 3095 N TYR A1088 20.655 -29.461 -40.763 1.00 35.92 N ANISOU 3095 N TYR A1088 3684 3620 6342 -399 181 10 N ATOM 3096 CA TYR A1088 19.745 -29.058 -39.669 1.00 36.71 C ANISOU 3096 CA TYR A1088 3916 3591 6439 -326 164 -117 C ATOM 3097 C TYR A1088 19.332 -27.591 -39.686 1.00 38.34 C ANISOU 3097 C TYR A1088 4257 3533 6776 -336 204 -107 C ATOM 3098 O TYR A1088 18.166 -27.275 -39.483 1.00 39.07 O ANISOU 3098 O TYR A1088 4432 3526 6886 -193 252 -125 O ATOM 3099 CB TYR A1088 20.387 -29.321 -38.306 1.00 37.37 C ANISOU 3099 CB TYR A1088 4010 3712 6474 -412 79 -278 C ATOM 3100 CG TYR A1088 19.401 -29.279 -37.161 1.00 37.84 C ANISOU 3100 CG TYR A1088 4196 3716 6462 -320 86 -421 C ATOM 3101 CD1 TYR A1088 18.569 -30.362 -36.912 1.00 36.65 C ANISOU 3101 CD1 TYR A1088 4016 3706 6204 -183 106 -424 C ATOM 3102 CD2 TYR A1088 19.311 -28.165 -36.321 1.00 39.96 C ANISOU 3102 CD2 TYR A1088 4621 3789 6771 -380 89 -563 C ATOM 3103 CE1 TYR A1088 17.657 -30.341 -35.873 1.00 37.75 C ANISOU 3103 CE1 TYR A1088 4255 3817 6268 -102 138 -541 C ATOM 3104 CE2 TYR A1088 18.411 -28.131 -35.270 1.00 41.00 C ANISOU 3104 CE2 TYR A1088 4873 3885 6818 -290 129 -709 C ATOM 3105 CZ TYR A1088 17.582 -29.227 -35.049 1.00 40.12 C ANISOU 3105 CZ TYR A1088 4709 3943 6592 -147 158 -686 C ATOM 3106 OH TYR A1088 16.671 -29.230 -34.015 1.00 40.61 O ANISOU 3106 OH TYR A1088 4873 3995 6561 -58 221 -815 O ATOM 3107 N ASP A1089 20.281 -26.688 -39.885 1.00 40.61 N ANISOU 3107 N ASP A1089 4560 3691 7175 -501 191 -77 N ATOM 3108 CA ASP A1089 19.939 -25.260 -39.866 1.00 43.60 C ANISOU 3108 CA ASP A1089 5087 3765 7711 -519 236 -70 C ATOM 3109 C ASP A1089 18.982 -24.930 -40.985 1.00 43.78 C ANISOU 3109 C ASP A1089 5115 3730 7787 -367 310 135 C ATOM 3110 O ASP A1089 18.081 -24.131 -40.779 1.00 45.19 O ANISOU 3110 O ASP A1089 5407 3692 8072 -250 362 131 O ATOM 3111 CB ASP A1089 21.170 -24.351 -39.972 1.00 45.62 C ANISOU 3111 CB ASP A1089 5354 3880 8098 -758 209 -52 C ATOM 3112 CG ASP A1089 22.050 -24.400 -38.733 1.00 46.82 C ANISOU 3112 CG ASP A1089 5520 4053 8215 -934 108 -266 C ATOM 3113 OD1 ASP A1089 21.554 -24.772 -37.637 1.00 45.74 O ANISOU 3113 OD1 ASP A1089 5458 3952 7968 -863 77 -451 O ATOM 3114 OD2 ASP A1089 23.253 -24.052 -38.865 1.00 49.45 O ANISOU 3114 OD2 ASP A1089 5779 4385 8624 -1156 55 -235 O ATOM 3115 N SER A1090 19.146 -25.563 -42.148 1.00 42.64 N ANISOU 3115 N SER A1090 4847 3789 7562 -361 316 313 N ATOM 3116 CA SER A1090 18.363 -25.186 -43.320 1.00 44.01 C ANISOU 3116 CA SER A1090 5020 3942 7759 -256 358 543 C ATOM 3117 C SER A1090 16.904 -25.671 -43.298 1.00 43.58 C ANISOU 3117 C SER A1090 4953 3963 7640 -40 360 554 C ATOM 3118 O SER A1090 16.108 -25.295 -44.158 1.00 45.32 O ANISOU 3118 O SER A1090 5164 4168 7888 61 371 753 O ATOM 3119 CB SER A1090 19.053 -25.680 -44.583 1.00 44.43 C ANISOU 3119 CB SER A1090 4963 4211 7708 -346 370 712 C ATOM 3120 OG SER A1090 18.997 -27.091 -44.678 1.00 44.33 O ANISOU 3120 OG SER A1090 4851 4474 7516 -300 354 637 O ATOM 3121 N LEU A1091 16.550 -26.483 -42.309 1.00 42.40 N ANISOU 3121 N LEU A1091 4793 3904 7410 21 343 363 N ATOM 3122 CA LEU A1091 15.300 -27.214 -42.314 1.00 40.93 C ANISOU 3122 CA LEU A1091 4554 3853 7144 187 343 374 C ATOM 3123 C LEU A1091 14.225 -26.532 -41.460 1.00 42.63 C ANISOU 3123 C LEU A1091 4843 3881 7474 343 398 304 C ATOM 3124 O LEU A1091 14.535 -25.887 -40.466 1.00 44.57 O ANISOU 3124 O LEU A1091 5202 3934 7797 310 433 142 O ATOM 3125 CB LEU A1091 15.558 -28.634 -41.798 1.00 38.30 C ANISOU 3125 CB LEU A1091 4154 3742 6655 156 310 233 C ATOM 3126 CG LEU A1091 16.311 -29.633 -42.685 1.00 36.87 C ANISOU 3126 CG LEU A1091 3878 3777 6353 66 286 287 C ATOM 3127 CD1 LEU A1091 16.435 -30.974 -41.994 1.00 34.79 C ANISOU 3127 CD1 LEU A1091 3566 3665 5986 70 264 148 C ATOM 3128 CD2 LEU A1091 15.637 -29.868 -44.021 1.00 37.33 C ANISOU 3128 CD2 LEU A1091 3883 3966 6334 111 284 459 C ATOM 3129 N ASP A1092 12.964 -26.679 -41.867 1.00 43.16 N ANISOU 3129 N ASP A1092 4836 4014 7547 507 409 422 N ATOM 3130 CA ASP A1092 11.796 -26.296 -41.058 1.00 44.78 C ANISOU 3130 CA ASP A1092 5059 4103 7850 690 484 358 C ATOM 3131 C ASP A1092 11.668 -27.220 -39.847 1.00 43.36 C ANISOU 3131 C ASP A1092 4883 4045 7547 686 505 134 C ATOM 3132 O ASP A1092 12.325 -28.258 -39.785 1.00 42.89 O ANISOU 3132 O ASP A1092 4788 4170 7337 568 443 73 O ATOM 3133 CB ASP A1092 10.509 -26.407 -41.885 1.00 46.58 C ANISOU 3133 CB ASP A1092 5148 4443 8107 851 468 574 C ATOM 3134 CG ASP A1092 10.261 -27.848 -42.411 1.00 46.68 C ANISOU 3134 CG ASP A1092 5027 4789 7919 796 383 606 C ATOM 3135 OD1 ASP A1092 11.044 -28.323 -43.282 1.00 47.49 O ANISOU 3135 OD1 ASP A1092 5118 5025 7901 656 315 667 O ATOM 3136 OD2 ASP A1092 9.292 -28.499 -41.957 1.00 45.87 O ANISOU 3136 OD2 ASP A1092 4834 4807 7785 885 398 564 O ATOM 3137 N ALA A1093 10.780 -26.873 -38.921 1.00 43.30 N ANISOU 3137 N ALA A1093 4909 3937 7604 829 606 31 N ATOM 3138 CA ALA A1093 10.677 -27.582 -37.645 1.00 42.75 C ANISOU 3138 CA ALA A1093 4872 3963 7404 817 646 -177 C ATOM 3139 C ALA A1093 10.288 -29.068 -37.742 1.00 40.78 C ANISOU 3139 C ALA A1093 4485 4007 7001 803 593 -138 C ATOM 3140 O ALA A1093 10.599 -29.857 -36.852 1.00 39.84 O ANISOU 3140 O ALA A1093 4394 3994 6746 735 588 -271 O ATOM 3141 CB ALA A1093 9.689 -26.874 -36.750 1.00 44.77 C ANISOU 3141 CB ALA A1093 5185 4065 7757 990 800 -282 C ATOM 3142 N VAL A1094 9.594 -29.449 -38.799 1.00 39.82 N ANISOU 3142 N VAL A1094 4220 4011 6897 858 549 48 N ATOM 3143 CA VAL A1094 9.083 -30.796 -38.881 1.00 38.19 C ANISOU 3143 CA VAL A1094 3893 4046 6569 836 509 71 C ATOM 3144 C VAL A1094 10.171 -31.698 -39.424 1.00 36.28 C ANISOU 3144 C VAL A1094 3657 3921 6206 672 411 65 C ATOM 3145 O VAL A1094 10.462 -32.728 -38.843 1.00 35.71 O ANISOU 3145 O VAL A1094 3585 3951 6032 607 398 -25 O ATOM 3146 CB VAL A1094 7.793 -30.851 -39.704 1.00 38.31 C ANISOU 3146 CB VAL A1094 3743 4164 6648 946 493 254 C ATOM 3147 CG1 VAL A1094 7.460 -32.269 -40.118 1.00 37.37 C ANISOU 3147 CG1 VAL A1094 3510 4287 6401 859 417 287 C ATOM 3148 CG2 VAL A1094 6.677 -30.288 -38.867 1.00 39.68 C ANISOU 3148 CG2 VAL A1094 3875 4261 6938 1126 623 229 C ATOM 3149 N ARG A1095 10.794 -31.270 -40.505 1.00 36.22 N ANISOU 3149 N ARG A1095 3656 3885 6220 613 358 170 N ATOM 3150 CA ARG A1095 11.921 -31.980 -41.079 1.00 34.41 C ANISOU 3150 CA ARG A1095 3429 3750 5893 471 300 159 C ATOM 3151 C ARG A1095 13.145 -32.025 -40.156 1.00 33.52 C ANISOU 3151 C ARG A1095 3396 3572 5765 381 302 14 C ATOM 3152 O ARG A1095 13.865 -33.003 -40.151 1.00 33.15 O ANISOU 3152 O ARG A1095 3321 3632 5640 304 271 -28 O ATOM 3153 CB ARG A1095 12.302 -31.349 -42.411 1.00 35.33 C ANISOU 3153 CB ARG A1095 3539 3855 6029 429 270 316 C ATOM 3154 CG ARG A1095 11.224 -31.409 -43.473 1.00 36.20 C ANISOU 3154 CG ARG A1095 3559 4084 6111 487 227 487 C ATOM 3155 CD ARG A1095 11.853 -31.211 -44.839 1.00 37.98 C ANISOU 3155 CD ARG A1095 3788 4377 6263 394 190 625 C ATOM 3156 NE ARG A1095 10.891 -31.370 -45.920 1.00 39.59 N ANISOU 3156 NE ARG A1095 3909 4745 6387 418 120 793 N ATOM 3157 CZ ARG A1095 10.038 -30.436 -46.320 1.00 42.77 C ANISOU 3157 CZ ARG A1095 4267 5102 6880 522 88 989 C ATOM 3158 NH1 ARG A1095 9.204 -30.702 -47.317 1.00 45.23 N ANISOU 3158 NH1 ARG A1095 4484 5610 7089 520 -6 1149 N ATOM 3159 NH2 ARG A1095 10.001 -29.240 -45.735 1.00 44.25 N ANISOU 3159 NH2 ARG A1095 4504 5045 7263 628 146 1027 N ATOM 3160 N ARG A1096 13.400 -30.984 -39.377 1.00 34.92 N ANISOU 3160 N ARG A1096 3670 3575 6020 386 334 -62 N ATOM 3161 CA ARG A1096 14.451 -31.069 -38.348 1.00 35.00 C ANISOU 3161 CA ARG A1096 3747 3560 5990 283 309 -208 C ATOM 3162 C ARG A1096 14.237 -32.249 -37.418 1.00 33.66 C ANISOU 3162 C ARG A1096 3555 3532 5701 296 299 -292 C ATOM 3163 O ARG A1096 15.186 -32.861 -36.986 1.00 34.29 O ANISOU 3163 O ARG A1096 3625 3683 5720 208 241 -338 O ATOM 3164 CB ARG A1096 14.498 -29.826 -37.470 1.00 37.04 C ANISOU 3164 CB ARG A1096 4139 3611 6323 281 350 -324 C ATOM 3165 CG ARG A1096 15.253 -28.693 -38.104 1.00 39.67 C ANISOU 3165 CG ARG A1096 4521 3771 6781 195 339 -269 C ATOM 3166 CD ARG A1096 15.336 -27.487 -37.193 1.00 42.17 C ANISOU 3166 CD ARG A1096 4996 3845 7181 169 383 -418 C ATOM 3167 NE ARG A1096 15.857 -26.343 -37.914 1.00 44.25 N ANISOU 3167 NE ARG A1096 5307 3900 7604 96 388 -332 N ATOM 3168 CZ ARG A1096 16.181 -25.184 -37.352 1.00 47.70 C ANISOU 3168 CZ ARG A1096 5894 4078 8151 24 418 -451 C ATOM 3169 NH1 ARG A1096 16.054 -24.991 -36.048 1.00 48.81 N ANISOU 3169 NH1 ARG A1096 6161 4150 8232 11 445 -687 N ATOM 3170 NH2 ARG A1096 16.655 -24.209 -38.104 1.00 50.46 N ANISOU 3170 NH2 ARG A1096 6278 4231 8662 -53 424 -337 N ATOM 3171 N ALA A1097 12.989 -32.526 -37.075 1.00 33.16 N ANISOU 3171 N ALA A1097 3472 3507 5618 407 357 -292 N ATOM 3172 CA ALA A1097 12.675 -33.573 -36.141 1.00 32.41 C ANISOU 3172 CA ALA A1097 3364 3533 5414 414 366 -348 C ATOM 3173 C ALA A1097 12.952 -34.909 -36.793 1.00 31.07 C ANISOU 3173 C ALA A1097 3101 3500 5203 368 310 -274 C ATOM 3174 O ALA A1097 13.306 -35.876 -36.141 1.00 30.26 O ANISOU 3174 O ALA A1097 2993 3474 5028 332 285 -301 O ATOM 3175 CB ALA A1097 11.223 -33.467 -35.739 1.00 33.69 C ANISOU 3175 CB ALA A1097 3504 3705 5589 540 464 -346 C ATOM 3176 N ALA A1098 12.805 -34.931 -38.104 1.00 30.90 N ANISOU 3176 N ALA A1098 3016 3499 5225 369 296 -180 N ATOM 3177 CA ALA A1098 12.932 -36.125 -38.873 1.00 30.71 C ANISOU 3177 CA ALA A1098 2923 3583 5160 326 266 -137 C ATOM 3178 C ALA A1098 14.395 -36.437 -39.022 1.00 31.56 C ANISOU 3178 C ALA A1098 3034 3691 5263 248 233 -162 C ATOM 3179 O ALA A1098 14.782 -37.604 -39.155 1.00 31.02 O ANISOU 3179 O ALA A1098 2929 3684 5170 223 226 -169 O ATOM 3180 CB ALA A1098 12.278 -35.928 -40.230 1.00 31.29 C ANISOU 3180 CB ALA A1098 2943 3701 5245 337 258 -38 C ATOM 3181 N LEU A1099 15.220 -35.391 -39.001 1.00 32.41 N ANISOU 3181 N LEU A1099 3177 3718 5416 208 220 -170 N ATOM 3182 CA LEU A1099 16.661 -35.596 -38.974 1.00 31.51 C ANISOU 3182 CA LEU A1099 3034 3619 5318 128 187 -186 C ATOM 3183 C LEU A1099 17.055 -36.128 -37.609 1.00 31.35 C ANISOU 3183 C LEU A1099 3025 3625 5258 118 140 -249 C ATOM 3184 O LEU A1099 17.895 -37.018 -37.528 1.00 31.75 O ANISOU 3184 O LEU A1099 3010 3739 5314 98 111 -233 O ATOM 3185 CB LEU A1099 17.424 -34.313 -39.294 1.00 32.06 C ANISOU 3185 CB LEU A1099 3126 3596 5456 57 179 -167 C ATOM 3186 CG LEU A1099 18.952 -34.474 -39.339 1.00 31.92 C ANISOU 3186 CG LEU A1099 3035 3618 5475 -39 146 -163 C ATOM 3187 CD1 LEU A1099 19.339 -35.523 -40.366 1.00 32.03 C ANISOU 3187 CD1 LEU A1099 2956 3738 5475 -23 194 -113 C ATOM 3188 CD2 LEU A1099 19.624 -33.160 -39.666 1.00 32.65 C ANISOU 3188 CD2 LEU A1099 3146 3610 5649 -138 143 -134 C ATOM 3189 N ILE A1100 16.445 -35.598 -36.544 1.00 30.85 N ANISOU 3189 N ILE A1100 3046 3521 5153 139 141 -313 N ATOM 3190 CA ILE A1100 16.745 -36.063 -35.184 1.00 31.18 C ANISOU 3190 CA ILE A1100 3118 3619 5108 116 90 -363 C ATOM 3191 C ILE A1100 16.283 -37.513 -35.003 1.00 31.26 C ANISOU 3191 C ILE A1100 3080 3718 5076 168 104 -307 C ATOM 3192 O ILE A1100 16.839 -38.270 -34.228 1.00 30.02 O ANISOU 3192 O ILE A1100 2906 3625 4873 150 48 -283 O ATOM 3193 CB ILE A1100 16.132 -35.172 -34.091 1.00 30.91 C ANISOU 3193 CB ILE A1100 3207 3532 5004 122 117 -468 C ATOM 3194 CG1 ILE A1100 16.699 -33.763 -34.172 1.00 32.26 C ANISOU 3194 CG1 ILE A1100 3448 3572 5238 49 101 -540 C ATOM 3195 CG2 ILE A1100 16.461 -35.730 -32.721 1.00 31.45 C ANISOU 3195 CG2 ILE A1100 3315 3701 4933 81 57 -505 C ATOM 3196 CD1 ILE A1100 16.012 -32.733 -33.298 1.00 33.35 C ANISOU 3196 CD1 ILE A1100 3732 3602 5337 71 166 -675 C ATOM 3197 N ASN A1101 15.251 -37.895 -35.728 1.00 33.56 N ANISOU 3197 N ASN A1101 3348 4011 5391 224 169 -273 N ATOM 3198 CA ASN A1101 14.817 -39.271 -35.690 1.00 34.59 C ANISOU 3198 CA ASN A1101 3439 4196 5508 246 185 -225 C ATOM 3199 C ASN A1101 15.945 -40.195 -36.154 1.00 34.03 C ANISOU 3199 C ASN A1101 3306 4131 5491 226 152 -189 C ATOM 3200 O ASN A1101 16.292 -41.142 -35.461 1.00 35.77 O ANISOU 3200 O ASN A1101 3513 4372 5706 235 126 -147 O ATOM 3201 CB ASN A1101 13.567 -39.467 -36.524 1.00 34.53 C ANISOU 3201 CB ASN A1101 3401 4197 5520 275 241 -201 C ATOM 3202 CG ASN A1101 12.872 -40.767 -36.191 1.00 35.86 C ANISOU 3202 CG ASN A1101 3546 4404 5674 273 265 -165 C ATOM 3203 OD1 ASN A1101 13.518 -41.738 -35.817 1.00 35.89 O ANISOU 3203 OD1 ASN A1101 3550 4401 5685 258 243 -140 O ATOM 3204 ND2 ASN A1101 11.551 -40.785 -36.298 1.00 36.77 N ANISOU 3204 ND2 ASN A1101 3630 4554 5787 288 309 -145 N ATOM 3205 N MET A1102 16.543 -39.874 -37.296 1.00 33.68 N ANISOU 3205 N MET A1102 3223 4068 5504 207 164 -193 N ATOM 3206 CA MET A1102 17.650 -40.659 -37.846 1.00 33.31 C ANISOU 3206 CA MET A1102 3104 4026 5524 206 171 -172 C ATOM 3207 C MET A1102 18.830 -40.746 -36.895 1.00 33.42 C ANISOU 3207 C MET A1102 3067 4064 5565 198 96 -139 C ATOM 3208 O MET A1102 19.392 -41.812 -36.741 1.00 35.69 O ANISOU 3208 O MET A1102 3295 4353 5911 239 95 -91 O ATOM 3209 CB MET A1102 18.121 -40.105 -39.186 1.00 33.14 C ANISOU 3209 CB MET A1102 3052 4007 5532 176 216 -181 C ATOM 3210 CG MET A1102 17.063 -40.141 -40.270 1.00 33.55 C ANISOU 3210 CG MET A1102 3140 4071 5535 172 266 -192 C ATOM 3211 SD MET A1102 17.811 -40.132 -41.903 1.00 36.09 S ANISOU 3211 SD MET A1102 3429 4433 5850 135 341 -196 S ATOM 3212 CE MET A1102 18.329 -38.435 -42.011 1.00 39.64 C ANISOU 3212 CE MET A1102 3873 4868 6317 88 315 -136 C ATOM 3213 N VAL A1103 19.190 -39.642 -36.250 1.00 33.51 N ANISOU 3213 N VAL A1103 3101 4088 5541 142 30 -161 N ATOM 3214 CA VAL A1103 20.362 -39.603 -35.371 1.00 34.20 C ANISOU 3214 CA VAL A1103 3125 4230 5637 99 -74 -128 C ATOM 3215 C VAL A1103 20.088 -40.363 -34.087 1.00 35.49 C ANISOU 3215 C VAL A1103 3323 4446 5716 126 -136 -83 C ATOM 3216 O VAL A1103 20.966 -41.064 -33.577 1.00 37.67 O ANISOU 3216 O VAL A1103 3509 4777 6024 140 -213 6 O ATOM 3217 CB VAL A1103 20.828 -38.154 -35.092 1.00 35.09 C ANISOU 3217 CB VAL A1103 3270 4332 5731 -8 -136 -187 C ATOM 3218 CG1 VAL A1103 21.912 -38.097 -34.023 1.00 36.43 C ANISOU 3218 CG1 VAL A1103 3379 4588 5873 -86 -280 -162 C ATOM 3219 CG2 VAL A1103 21.374 -37.532 -36.373 1.00 35.21 C ANISOU 3219 CG2 VAL A1103 3223 4307 5849 -46 -78 -178 C ATOM 3220 N PHE A1104 18.869 -40.253 -33.582 1.00 35.51 N ANISOU 3220 N PHE A1104 3439 4438 5615 140 -97 -124 N ATOM 3221 CA PHE A1104 18.425 -41.076 -32.465 1.00 36.15 C ANISOU 3221 CA PHE A1104 3560 4574 5599 164 -121 -62 C ATOM 3222 C PHE A1104 18.593 -42.573 -32.736 1.00 37.35 C ANISOU 3222 C PHE A1104 3639 4699 5851 233 -100 52 C ATOM 3223 O PHE A1104 18.999 -43.333 -31.843 1.00 37.33 O ANISOU 3223 O PHE A1104 3614 4745 5822 249 -170 166 O ATOM 3224 CB PHE A1104 16.950 -40.822 -32.172 1.00 35.96 C ANISOU 3224 CB PHE A1104 3640 4539 5484 181 -29 -117 C ATOM 3225 CG PHE A1104 16.543 -41.207 -30.783 1.00 36.81 C ANISOU 3225 CG PHE A1104 3816 4733 5435 171 -48 -75 C ATOM 3226 CD1 PHE A1104 16.699 -40.319 -29.744 1.00 37.23 C ANISOU 3226 CD1 PHE A1104 3960 4856 5329 111 -96 -153 C ATOM 3227 CD2 PHE A1104 16.007 -42.462 -30.523 1.00 36.73 C ANISOU 3227 CD2 PHE A1104 3791 4734 5429 207 -10 39 C ATOM 3228 CE1 PHE A1104 16.331 -40.665 -28.466 1.00 39.00 C ANISOU 3228 CE1 PHE A1104 4260 5188 5366 92 -102 -115 C ATOM 3229 CE2 PHE A1104 15.649 -42.823 -29.247 1.00 37.51 C ANISOU 3229 CE2 PHE A1104 3955 4928 5368 189 -18 107 C ATOM 3230 CZ PHE A1104 15.802 -41.918 -28.218 1.00 39.26 C ANISOU 3230 CZ PHE A1104 4268 5250 5398 134 -61 30 C ATOM 3231 N GLN A1105 18.251 -43.008 -33.951 1.00 37.04 N ANISOU 3231 N GLN A1105 3575 4578 5919 270 -4 26 N ATOM 3232 CA GLN A1105 18.243 -44.442 -34.246 1.00 37.46 C ANISOU 3232 CA GLN A1105 3595 4561 6076 328 43 97 C ATOM 3233 C GLN A1105 19.636 -44.956 -34.583 1.00 38.09 C ANISOU 3233 C GLN A1105 3558 4617 6295 382 22 155 C ATOM 3234 O GLN A1105 19.968 -46.089 -34.229 1.00 40.03 O ANISOU 3234 O GLN A1105 3767 4812 6630 449 19 261 O ATOM 3235 CB GLN A1105 17.281 -44.760 -35.391 1.00 37.16 C ANISOU 3235 CB GLN A1105 3591 4450 6075 321 150 21 C ATOM 3236 CG GLN A1105 17.086 -46.255 -35.648 1.00 37.23 C ANISOU 3236 CG GLN A1105 3604 4352 6189 353 210 61 C ATOM 3237 CD GLN A1105 16.437 -46.552 -36.989 1.00 37.70 C ANISOU 3237 CD GLN A1105 3691 4352 6279 318 297 -45 C ATOM 3238 OE1 GLN A1105 16.198 -45.659 -37.786 1.00 39.39 O ANISOU 3238 OE1 GLN A1105 3907 4623 6434 282 306 -122 O ATOM 3239 NE2 GLN A1105 16.129 -47.817 -37.233 1.00 40.03 N ANISOU 3239 NE2 GLN A1105 4016 4529 6661 315 355 -46 N ATOM 3240 N MET A1106 20.442 -44.127 -35.251 1.00 36.76 N ANISOU 3240 N MET A1106 3321 4480 6162 359 19 101 N ATOM 3241 CA MET A1106 21.715 -44.567 -35.842 1.00 37.38 C ANISOU 3241 CA MET A1106 3260 4544 6395 418 46 140 C ATOM 3242 C MET A1106 22.975 -43.887 -35.344 1.00 37.73 C ANISOU 3242 C MET A1106 3174 4695 6467 384 -67 203 C ATOM 3243 O MET A1106 24.060 -44.384 -35.567 1.00 37.88 O ANISOU 3243 O MET A1106 3038 4723 6632 451 -57 277 O ATOM 3244 CB MET A1106 21.667 -44.338 -37.341 1.00 38.41 C ANISOU 3244 CB MET A1106 3393 4635 6563 410 177 32 C ATOM 3245 CG MET A1106 21.014 -45.463 -38.108 1.00 39.44 C ANISOU 3245 CG MET A1106 3590 4657 6739 458 300 -22 C ATOM 3246 SD MET A1106 21.031 -45.013 -39.843 1.00 41.17 S ANISOU 3246 SD MET A1106 3825 4889 6929 417 433 -151 S ATOM 3247 CE MET A1106 19.626 -43.900 -39.853 1.00 42.20 C ANISOU 3247 CE MET A1106 4072 5072 6888 316 370 -188 C ATOM 3248 N GLY A1107 22.830 -42.724 -34.721 1.00 37.80 N ANISOU 3248 N GLY A1107 3238 4778 6346 275 -166 163 N ATOM 3249 CA GLY A1107 23.956 -41.950 -34.259 1.00 37.70 C ANISOU 3249 CA GLY A1107 3115 4866 6343 192 -291 196 C ATOM 3250 C GLY A1107 24.447 -40.887 -35.217 1.00 36.90 C ANISOU 3250 C GLY A1107 2966 4758 6294 111 -242 124 C ATOM 3251 O GLY A1107 24.254 -40.963 -36.421 1.00 35.24 O ANISOU 3251 O GLY A1107 2758 4486 6142 148 -99 82 O ATOM 3252 N GLU A1108 25.116 -39.906 -34.633 1.00 38.22 N ANISOU 3252 N GLU A1108 3092 4997 6430 -18 -370 118 N ATOM 3253 CA GLU A1108 25.756 -38.804 -35.332 1.00 39.35 C ANISOU 3253 CA GLU A1108 3177 5136 6639 -133 -351 79 C ATOM 3254 C GLU A1108 26.527 -39.304 -36.558 1.00 37.56 C ANISOU 3254 C GLU A1108 2777 4917 6575 -62 -217 139 C ATOM 3255 O GLU A1108 26.231 -38.931 -37.676 1.00 36.56 O ANISOU 3255 O GLU A1108 2697 4733 6459 -68 -80 93 O ATOM 3256 CB GLU A1108 26.671 -38.054 -34.316 1.00 43.04 C ANISOU 3256 CB GLU A1108 3570 5703 7079 -294 -546 93 C ATOM 3257 CG GLU A1108 27.567 -36.951 -34.863 1.00 45.80 C ANISOU 3257 CG GLU A1108 3819 6055 7526 -453 -557 80 C ATOM 3258 CD GLU A1108 28.598 -36.392 -33.854 1.00 50.21 C ANISOU 3258 CD GLU A1108 4267 6735 8075 -636 -775 102 C ATOM 3259 OE1 GLU A1108 28.857 -37.028 -32.802 1.00 52.68 O ANISOU 3259 OE1 GLU A1108 4526 7174 8316 -619 -929 167 O ATOM 3260 OE2 GLU A1108 29.178 -35.302 -34.123 1.00 51.78 O ANISOU 3260 OE2 GLU A1108 4427 6909 8335 -817 -803 64 O ATOM 3261 N THR A1109 27.501 -40.169 -36.346 1.00 37.74 N ANISOU 3261 N THR A1109 2601 5019 6719 13 -247 250 N ATOM 3262 CA THR A1109 28.419 -40.574 -37.425 1.00 38.14 C ANISOU 3262 CA THR A1109 2456 5092 6940 83 -101 300 C ATOM 3263 C THR A1109 27.780 -41.560 -38.416 1.00 37.31 C ANISOU 3263 C THR A1109 2434 4888 6854 236 103 246 C ATOM 3264 O THR A1109 28.188 -41.655 -39.572 1.00 38.07 O ANISOU 3264 O THR A1109 2460 4984 7020 269 276 222 O ATOM 3265 CB THR A1109 29.733 -41.116 -36.834 1.00 39.43 C ANISOU 3265 CB THR A1109 2343 5376 7261 128 -200 451 C ATOM 3266 OG1 THR A1109 29.439 -42.160 -35.907 1.00 39.82 O ANISOU 3266 OG1 THR A1109 2418 5415 7297 250 -289 528 O ATOM 3267 CG2 THR A1109 30.435 -40.035 -36.070 1.00 40.26 C ANISOU 3267 CG2 THR A1109 2356 5600 7341 -72 -403 485 C ATOM 3268 N GLY A1110 26.754 -42.270 -37.960 1.00 36.28 N ANISOU 3268 N GLY A1110 2463 4678 6644 309 87 217 N ATOM 3269 CA GLY A1110 25.892 -43.054 -38.833 1.00 34.58 C ANISOU 3269 CA GLY A1110 2375 4355 6407 397 250 132 C ATOM 3270 C GLY A1110 25.165 -42.227 -39.861 1.00 32.74 C ANISOU 3270 C GLY A1110 2274 4108 6057 310 337 28 C ATOM 3271 O GLY A1110 25.215 -42.528 -41.053 1.00 32.83 O ANISOU 3271 O GLY A1110 2289 4107 6079 340 499 -28 O ATOM 3272 N VAL A1111 24.494 -41.172 -39.410 1.00 31.70 N ANISOU 3272 N VAL A1111 2253 3981 5809 205 235 6 N ATOM 3273 CA VAL A1111 23.696 -40.346 -40.316 1.00 30.66 C ANISOU 3273 CA VAL A1111 2245 3827 5579 139 298 -54 C ATOM 3274 C VAL A1111 24.632 -39.563 -41.215 1.00 31.53 C ANISOU 3274 C VAL A1111 2255 3988 5735 66 369 -24 C ATOM 3275 O VAL A1111 24.324 -39.318 -42.368 1.00 32.43 O ANISOU 3275 O VAL A1111 2423 4109 5789 45 479 -45 O ATOM 3276 CB VAL A1111 22.710 -39.426 -39.572 1.00 29.63 C ANISOU 3276 CB VAL A1111 2251 3658 5346 78 195 -79 C ATOM 3277 CG1 VAL A1111 21.898 -38.588 -40.542 1.00 29.09 C ANISOU 3277 CG1 VAL A1111 2283 3559 5207 37 255 -102 C ATOM 3278 CG2 VAL A1111 21.765 -40.254 -38.749 1.00 28.98 C ANISOU 3278 CG2 VAL A1111 2252 3548 5210 145 156 -96 C ATOM 3279 N ALA A1112 25.798 -39.228 -40.695 1.00 32.86 N ANISOU 3279 N ALA A1112 2267 4210 6006 17 304 38 N ATOM 3280 CA ALA A1112 26.799 -38.469 -41.437 1.00 34.41 C ANISOU 3280 CA ALA A1112 2336 4466 6272 -74 371 89 C ATOM 3281 C ALA A1112 27.273 -39.131 -42.715 1.00 35.35 C ANISOU 3281 C ALA A1112 2371 4634 6423 -3 578 87 C ATOM 3282 O ALA A1112 27.788 -38.453 -43.589 1.00 36.50 O ANISOU 3282 O ALA A1112 2461 4832 6573 -85 676 125 O ATOM 3283 CB ALA A1112 27.986 -38.191 -40.540 1.00 36.06 C ANISOU 3283 CB ALA A1112 2355 4745 6601 -145 244 162 C ATOM 3284 N GLY A1113 27.135 -40.453 -42.806 1.00 36.35 N ANISOU 3284 N GLY A1113 2496 4738 6577 144 657 41 N ATOM 3285 CA GLY A1113 27.522 -41.208 -43.992 1.00 37.40 C ANISOU 3285 CA GLY A1113 2583 4899 6729 226 880 -5 C ATOM 3286 C GLY A1113 26.590 -41.061 -45.178 1.00 37.40 C ANISOU 3286 C GLY A1113 2770 4896 6540 183 989 -91 C ATOM 3287 O GLY A1113 26.970 -41.389 -46.296 1.00 39.88 O ANISOU 3287 O GLY A1113 3065 5267 6819 204 1184 -138 O ATOM 3288 N PHE A1114 25.374 -40.575 -44.940 1.00 36.24 N ANISOU 3288 N PHE A1114 2798 4702 6267 126 868 -107 N ATOM 3289 CA PHE A1114 24.394 -40.316 -45.990 1.00 36.36 C ANISOU 3289 CA PHE A1114 2976 4741 6099 72 921 -151 C ATOM 3290 C PHE A1114 24.737 -39.044 -46.747 1.00 37.71 C ANISOU 3290 C PHE A1114 3130 4985 6211 -44 956 -57 C ATOM 3291 O PHE A1114 23.895 -38.154 -46.858 1.00 36.73 O ANISOU 3291 O PHE A1114 3117 4841 5997 -111 870 -6 O ATOM 3292 CB PHE A1114 23.012 -40.090 -45.386 1.00 35.56 C ANISOU 3292 CB PHE A1114 3017 4572 5919 59 770 -162 C ATOM 3293 CG PHE A1114 22.356 -41.320 -44.877 1.00 35.79 C ANISOU 3293 CG PHE A1114 3101 4533 5961 142 749 -244 C ATOM 3294 CD1 PHE A1114 22.626 -41.785 -43.614 1.00 36.55 C ANISOU 3294 CD1 PHE A1114 3139 4568 6178 205 666 -221 C ATOM 3295 CD2 PHE A1114 21.453 -41.997 -45.661 1.00 37.50 C ANISOU 3295 CD2 PHE A1114 3434 4754 6061 136 802 -333 C ATOM 3296 CE1 PHE A1114 22.011 -42.924 -43.137 1.00 38.32 C ANISOU 3296 CE1 PHE A1114 3420 4716 6424 272 653 -268 C ATOM 3297 CE2 PHE A1114 20.823 -43.135 -45.200 1.00 38.65 C ANISOU 3297 CE2 PHE A1114 3633 4815 6235 186 785 -405 C ATOM 3298 CZ PHE A1114 21.101 -43.602 -43.928 1.00 38.97 C ANISOU 3298 CZ PHE A1114 3616 4774 6415 260 719 -363 C ATOM 3299 N THR A1115 25.951 -38.969 -47.281 1.00 39.15 N ANISOU 3299 N THR A1115 3168 5248 6458 -63 1093 -18 N ATOM 3300 CA THR A1115 26.490 -37.728 -47.772 1.00 41.18 C ANISOU 3300 CA THR A1115 3374 5562 6710 -192 1119 105 C ATOM 3301 C THR A1115 25.629 -37.077 -48.848 1.00 42.51 C ANISOU 3301 C THR A1115 3705 5770 6675 -268 1148 151 C ATOM 3302 O THR A1115 25.385 -35.873 -48.782 1.00 43.90 O ANISOU 3302 O THR A1115 3925 5900 6855 -363 1061 268 O ATOM 3303 CB THR A1115 27.918 -37.905 -48.316 1.00 42.96 C ANISOU 3303 CB THR A1115 3395 5897 7029 -197 1304 143 C ATOM 3304 OG1 THR A1115 28.697 -38.623 -47.364 1.00 43.75 O ANISOU 3304 OG1 THR A1115 3320 5975 7328 -102 1269 123 O ATOM 3305 CG2 THR A1115 28.565 -36.571 -48.549 1.00 43.43 C ANISOU 3305 CG2 THR A1115 3373 5994 7132 -359 1303 295 C ATOM 3306 N ASN A1116 25.177 -37.855 -49.824 1.00 43.93 N ANISOU 3306 N ASN A1116 3977 6031 6680 -232 1264 65 N ATOM 3307 CA ASN A1116 24.422 -37.293 -50.949 1.00 46.06 C ANISOU 3307 CA ASN A1116 4387 6389 6723 -315 1281 131 C ATOM 3308 C ASN A1116 22.968 -36.974 -50.620 1.00 44.51 C ANISOU 3308 C ASN A1116 4329 6122 6459 -311 1092 153 C ATOM 3309 O ASN A1116 22.422 -35.993 -51.119 1.00 46.79 O ANISOU 3309 O ASN A1116 4686 6432 6657 -378 1035 295 O ATOM 3310 CB ASN A1116 24.488 -38.200 -52.181 1.00 48.00 C ANISOU 3310 CB ASN A1116 4693 6780 6765 -309 1470 17 C ATOM 3311 CG ASN A1116 25.823 -38.124 -52.880 1.00 51.40 C ANISOU 3311 CG ASN A1116 4997 7327 7206 -339 1698 50 C ATOM 3312 OD1 ASN A1116 26.456 -37.075 -52.915 1.00 54.60 O ANISOU 3312 OD1 ASN A1116 5309 7753 7681 -425 1708 221 O ATOM 3313 ND2 ASN A1116 26.256 -39.233 -53.459 1.00 54.39 N ANISOU 3313 ND2 ASN A1116 5370 7772 7522 -271 1901 -115 N ATOM 3314 N SER A1117 22.329 -37.794 -49.804 1.00 42.56 N ANISOU 3314 N SER A1117 4111 5793 6264 -227 1004 33 N ATOM 3315 CA SER A1117 20.955 -37.508 -49.426 1.00 41.44 C ANISOU 3315 CA SER A1117 4065 5596 6080 -215 843 59 C ATOM 3316 C SER A1117 20.886 -36.249 -48.567 1.00 40.82 C ANISOU 3316 C SER A1117 3969 5398 6140 -227 729 179 C ATOM 3317 O SER A1117 19.855 -35.574 -48.557 1.00 40.79 O ANISOU 3317 O SER A1117 4035 5359 6104 -223 632 258 O ATOM 3318 CB SER A1117 20.347 -38.683 -48.670 1.00 39.98 C ANISOU 3318 CB SER A1117 3904 5349 5937 -137 793 -83 C ATOM 3319 OG SER A1117 20.514 -39.879 -49.402 1.00 42.07 O ANISOU 3319 OG SER A1117 4199 5676 6109 -130 914 -220 O ATOM 3320 N LEU A1118 21.972 -35.949 -47.846 1.00 40.01 N ANISOU 3320 N LEU A1118 3769 5232 6199 -241 742 185 N ATOM 3321 CA LEU A1118 22.007 -34.798 -46.953 1.00 40.23 C ANISOU 3321 CA LEU A1118 3799 5128 6358 -276 639 254 C ATOM 3322 C LEU A1118 22.189 -33.471 -47.727 1.00 43.16 C ANISOU 3322 C LEU A1118 4195 5478 6724 -376 665 420 C ATOM 3323 O LEU A1118 21.736 -32.427 -47.275 1.00 42.45 O ANISOU 3323 O LEU A1118 4168 5247 6713 -392 584 485 O ATOM 3324 CB LEU A1118 23.102 -34.954 -45.896 1.00 38.90 C ANISOU 3324 CB LEU A1118 3514 4919 6345 -289 613 202 C ATOM 3325 CG LEU A1118 22.886 -35.952 -44.761 1.00 37.13 C ANISOU 3325 CG LEU A1118 3277 4671 6160 -197 541 89 C ATOM 3326 CD1 LEU A1118 24.174 -36.233 -44.009 1.00 37.13 C ANISOU 3326 CD1 LEU A1118 3123 4690 6291 -213 523 80 C ATOM 3327 CD2 LEU A1118 21.836 -35.460 -43.797 1.00 36.28 C ANISOU 3327 CD2 LEU A1118 3277 4456 6050 -172 420 64 C ATOM 3328 N ARG A1119 22.865 -33.517 -48.872 1.00 45.69 N ANISOU 3328 N ARG A1119 4472 5926 6960 -439 795 489 N ATOM 3329 CA ARG A1119 23.007 -32.342 -49.720 1.00 49.10 C ANISOU 3329 CA ARG A1119 4935 6355 7365 -541 832 681 C ATOM 3330 C ARG A1119 21.716 -32.060 -50.455 1.00 47.82 C ANISOU 3330 C ARG A1119 4897 6224 7047 -508 777 781 C ATOM 3331 O ARG A1119 21.391 -30.904 -50.751 1.00 48.38 O ANISOU 3331 O ARG A1119 5024 6209 7149 -547 739 963 O ATOM 3332 CB ARG A1119 24.110 -32.527 -50.756 1.00 53.84 C ANISOU 3332 CB ARG A1119 5447 7119 7890 -624 1010 737 C ATOM 3333 CG ARG A1119 25.512 -32.275 -50.243 1.00 58.12 C ANISOU 3333 CG ARG A1119 5825 7632 8624 -703 1065 743 C ATOM 3334 CD ARG A1119 26.476 -31.921 -51.379 1.00 64.52 C ANISOU 3334 CD ARG A1119 6552 8583 9379 -819 1249 883 C ATOM 3335 NE ARG A1119 26.363 -32.835 -52.526 1.00 67.43 N ANISOU 3335 NE ARG A1119 6953 9157 9507 -772 1408 832 N ATOM 3336 CZ ARG A1119 25.666 -32.604 -53.644 1.00 70.52 C ANISOU 3336 CZ ARG A1119 7482 9656 9657 -805 1442 932 C ATOM 3337 NH1 ARG A1119 24.986 -31.471 -53.836 1.00 70.79 N ANISOU 3337 NH1 ARG A1119 7619 9603 9676 -863 1332 1128 N ATOM 3338 NH2 ARG A1119 25.650 -33.530 -54.596 1.00 73.64 N ANISOU 3338 NH2 ARG A1119 7914 10247 9819 -778 1588 837 N ATOM 3339 N MET A1120 21.006 -33.129 -50.790 1.00 45.37 N ANISOU 3339 N MET A1120 4623 6036 6576 -442 772 674 N ATOM 3340 CA MET A1120 19.719 -33.008 -51.452 1.00 43.89 C ANISOU 3340 CA MET A1120 4525 5919 6232 -417 690 761 C ATOM 3341 C MET A1120 18.763 -32.309 -50.494 1.00 42.05 C ANISOU 3341 C MET A1120 4318 5502 6154 -336 551 804 C ATOM 3342 O MET A1120 18.151 -31.312 -50.845 1.00 44.11 O ANISOU 3342 O MET A1120 4620 5711 6428 -328 493 992 O ATOM 3343 CB MET A1120 19.211 -34.385 -51.886 1.00 42.84 C ANISOU 3343 CB MET A1120 4420 5943 5914 -394 704 599 C ATOM 3344 CG MET A1120 19.975 -34.984 -53.064 1.00 44.42 C ANISOU 3344 CG MET A1120 4629 6334 5913 -471 865 555 C ATOM 3345 SD MET A1120 19.702 -36.763 -53.282 1.00 44.62 S ANISOU 3345 SD MET A1120 4697 6457 5798 -445 922 276 S ATOM 3346 CE MET A1120 20.645 -37.066 -54.771 1.00 47.53 C ANISOU 3346 CE MET A1120 5099 7041 5916 -540 1147 248 C ATOM 3347 N LEU A1121 18.689 -32.805 -49.268 1.00 39.46 N ANISOU 3347 N LEU A1121 3967 5073 5952 -268 511 640 N ATOM 3348 CA LEU A1121 17.907 -32.166 -48.213 1.00 38.15 C ANISOU 3348 CA LEU A1121 3829 4732 5933 -188 418 642 C ATOM 3349 C LEU A1121 18.284 -30.690 -47.959 1.00 38.46 C ANISOU 3349 C LEU A1121 3900 4577 6135 -225 416 766 C ATOM 3350 O LEU A1121 17.431 -29.833 -47.769 1.00 38.92 O ANISOU 3350 O LEU A1121 4007 4502 6276 -157 365 858 O ATOM 3351 CB LEU A1121 18.063 -32.974 -46.920 1.00 36.25 C ANISOU 3351 CB LEU A1121 3561 4440 5770 -141 400 446 C ATOM 3352 CG LEU A1121 17.290 -34.301 -46.859 1.00 35.04 C ANISOU 3352 CG LEU A1121 3400 4396 5516 -84 379 334 C ATOM 3353 CD1 LEU A1121 17.442 -34.895 -45.474 1.00 33.59 C ANISOU 3353 CD1 LEU A1121 3198 4136 5425 -37 357 194 C ATOM 3354 CD2 LEU A1121 15.813 -34.142 -47.189 1.00 34.79 C ANISOU 3354 CD2 LEU A1121 3390 4402 5424 -29 307 413 C ATOM 3355 N ASN A1122 19.573 -30.424 -47.962 1.00 38.95 N ANISOU 3355 N ASN A1122 3924 4614 6259 -333 478 765 N ATOM 3356 CA ASN A1122 20.116 -29.103 -47.748 1.00 40.60 C ANISOU 3356 CA ASN A1122 4162 4630 6632 -414 483 865 C ATOM 3357 C ASN A1122 19.764 -28.157 -48.922 1.00 43.03 C ANISOU 3357 C ASN A1122 4520 4920 6907 -441 505 1123 C ATOM 3358 O ASN A1122 19.677 -26.951 -48.728 1.00 43.55 O ANISOU 3358 O ASN A1122 4650 4764 7133 -459 490 1234 O ATOM 3359 CB ASN A1122 21.646 -29.227 -47.550 1.00 40.72 C ANISOU 3359 CB ASN A1122 4082 4677 6712 -548 541 809 C ATOM 3360 CG ASN A1122 22.277 -27.981 -46.954 1.00 42.32 C ANISOU 3360 CG ASN A1122 4309 4657 7114 -667 519 844 C ATOM 3361 OD1 ASN A1122 21.596 -27.102 -46.439 1.00 43.16 O ANISOU 3361 OD1 ASN A1122 4525 4548 7326 -630 466 853 O ATOM 3362 ND2 ASN A1122 23.591 -27.916 -47.005 1.00 43.39 N ANISOU 3362 ND2 ASN A1122 4335 4838 7312 -813 566 854 N ATOM 3363 N ASN A1123 19.562 -28.727 -50.120 1.00 43.61 N ANISOU 3363 N ASN A1123 4577 5224 6766 -447 539 1215 N ATOM 3364 CA ASN A1123 19.151 -27.992 -51.328 1.00 45.03 C ANISOU 3364 CA ASN A1123 4802 5454 6851 -472 542 1488 C ATOM 3365 C ASN A1123 17.677 -28.139 -51.694 1.00 45.41 C ANISOU 3365 C ASN A1123 4880 5580 6793 -350 436 1573 C ATOM 3366 O ASN A1123 17.270 -27.740 -52.792 1.00 46.76 O ANISOU 3366 O ASN A1123 5074 5862 6830 -369 413 1810 O ATOM 3367 CB ASN A1123 19.936 -28.489 -52.516 1.00 46.16 C ANISOU 3367 CB ASN A1123 4913 5848 6776 -587 653 1546 C ATOM 3368 CG ASN A1123 21.408 -28.261 -52.366 1.00 47.52 C ANISOU 3368 CG ASN A1123 5017 5981 7057 -717 771 1522 C ATOM 3369 OD1 ASN A1123 21.843 -27.284 -51.760 1.00 48.66 O ANISOU 3369 OD1 ASN A1123 5163 5897 7426 -774 758 1577 O ATOM 3370 ND2 ASN A1123 22.194 -29.152 -52.944 1.00 48.40 N ANISOU 3370 ND2 ASN A1123 5060 6313 7016 -771 895 1439 N ATOM 3371 N LYS A1124 16.887 -28.714 -50.790 1.00 43.58 N ANISOU 3371 N LYS A1124 4633 5313 6613 -235 368 1399 N ATOM 3372 CA LYS A1124 15.438 -28.811 -50.944 1.00 44.67 C ANISOU 3372 CA LYS A1124 4759 5509 6702 -115 262 1476 C ATOM 3373 C LYS A1124 14.931 -29.749 -52.047 1.00 45.30 C ANISOU 3373 C LYS A1124 4816 5901 6494 -157 216 1504 C ATOM 3374 O LYS A1124 13.779 -29.654 -52.464 1.00 45.86 O ANISOU 3374 O LYS A1124 4859 6062 6502 -93 107 1643 O ATOM 3375 CB LYS A1124 14.836 -27.419 -51.085 1.00 47.47 C ANISOU 3375 CB LYS A1124 5143 5676 7218 -36 220 1735 C ATOM 3376 CG LYS A1124 14.999 -26.617 -49.818 1.00 48.51 C ANISOU 3376 CG LYS A1124 5317 5478 7635 26 255 1637 C ATOM 3377 CD LYS A1124 14.616 -25.167 -50.026 1.00 53.14 C ANISOU 3377 CD LYS A1124 5954 5819 8416 95 250 1891 C ATOM 3378 CE LYS A1124 14.467 -24.457 -48.691 1.00 55.12 C ANISOU 3378 CE LYS A1124 6266 5735 8940 187 288 1743 C ATOM 3379 NZ LYS A1124 15.680 -24.644 -47.830 1.00 55.02 N ANISOU 3379 NZ LYS A1124 6296 5641 8968 46 344 1493 N ATOM 3380 N ARG A1125 15.775 -30.684 -52.474 1.00 45.77 N ANISOU 3380 N ARG A1125 4882 6122 6386 -263 300 1359 N ATOM 3381 CA ARG A1125 15.400 -31.680 -53.471 1.00 47.20 C ANISOU 3381 CA ARG A1125 5073 6584 6277 -327 279 1317 C ATOM 3382 C ARG A1125 14.774 -32.859 -52.739 1.00 44.77 C ANISOU 3382 C ARG A1125 4736 6293 5981 -275 233 1077 C ATOM 3383 O ARG A1125 15.419 -33.887 -52.514 1.00 43.08 O ANISOU 3383 O ARG A1125 4528 6106 5734 -310 320 854 O ATOM 3384 CB ARG A1125 16.629 -32.126 -54.263 1.00 49.72 C ANISOU 3384 CB ARG A1125 5422 7041 6426 -452 431 1252 C ATOM 3385 CG ARG A1125 17.318 -31.010 -55.026 1.00 53.66 C ANISOU 3385 CG ARG A1125 5945 7543 6900 -530 499 1504 C ATOM 3386 CD ARG A1125 18.530 -31.512 -55.793 1.00 56.49 C ANISOU 3386 CD ARG A1125 6312 8065 7086 -648 683 1430 C ATOM 3387 NE ARG A1125 18.613 -30.879 -57.108 1.00 60.51 N ANISOU 3387 NE ARG A1125 6874 8753 7363 -752 716 1689 N ATOM 3388 CZ ARG A1125 19.571 -30.044 -57.505 1.00 65.11 C ANISOU 3388 CZ ARG A1125 7448 9308 7981 -839 838 1870 C ATOM 3389 NH1 ARG A1125 19.513 -29.519 -58.729 1.00 68.24 N ANISOU 3389 NH1 ARG A1125 7904 9891 8133 -935 857 2131 N ATOM 3390 NH2 ARG A1125 20.590 -29.720 -56.702 1.00 66.25 N ANISOU 3390 NH2 ARG A1125 7520 9255 8395 -848 933 1808 N ATOM 3391 N TRP A1126 13.511 -32.687 -52.365 1.00 44.20 N ANISOU 3391 N TRP A1126 4618 6196 5977 -186 105 1142 N ATOM 3392 CA TRP A1126 12.869 -33.556 -51.399 1.00 42.36 C ANISOU 3392 CA TRP A1126 4343 5924 5827 -126 70 954 C ATOM 3393 C TRP A1126 12.610 -34.918 -51.998 1.00 43.02 C ANISOU 3393 C TRP A1126 4440 6209 5694 -224 53 798 C ATOM 3394 O TRP A1126 12.732 -35.933 -51.321 1.00 42.59 O ANISOU 3394 O TRP A1126 4387 6108 5687 -223 94 586 O ATOM 3395 CB TRP A1126 11.539 -32.978 -50.937 1.00 42.74 C ANISOU 3395 CB TRP A1126 4315 5919 6004 -6 -40 1085 C ATOM 3396 CG TRP A1126 11.570 -31.559 -50.469 1.00 43.66 C ANISOU 3396 CG TRP A1126 4434 5815 6338 103 -23 1247 C ATOM 3397 CD1 TRP A1126 10.844 -30.525 -50.972 1.00 45.00 C ANISOU 3397 CD1 TRP A1126 4567 5969 6561 178 -97 1515 C ATOM 3398 CD2 TRP A1126 12.359 -31.014 -49.408 1.00 42.68 C ANISOU 3398 CD2 TRP A1126 4358 5442 6415 144 69 1150 C ATOM 3399 NE1 TRP A1126 11.129 -29.378 -50.298 1.00 45.20 N ANISOU 3399 NE1 TRP A1126 4630 5717 6825 271 -35 1577 N ATOM 3400 CE2 TRP A1126 12.059 -29.644 -49.333 1.00 43.77 C ANISOU 3400 CE2 TRP A1126 4507 5396 6725 236 61 1342 C ATOM 3401 CE3 TRP A1126 13.294 -31.549 -48.517 1.00 40.83 C ANISOU 3401 CE3 TRP A1126 4156 5124 6232 107 147 927 C ATOM 3402 CZ2 TRP A1126 12.647 -28.802 -48.398 1.00 43.34 C ANISOU 3402 CZ2 TRP A1126 4516 5068 6880 270 136 1281 C ATOM 3403 CZ3 TRP A1126 13.893 -30.705 -47.598 1.00 40.41 C ANISOU 3403 CZ3 TRP A1126 4147 4840 6366 134 198 889 C ATOM 3404 CH2 TRP A1126 13.561 -29.349 -47.542 1.00 41.73 C ANISOU 3404 CH2 TRP A1126 4345 4818 6690 204 195 1047 C ATOM 3405 N ASP A1127 12.233 -34.920 -53.269 1.00 45.49 N ANISOU 3405 N ASP A1127 4775 6742 5768 -318 -12 911 N ATOM 3406 CA ASP A1127 11.903 -36.134 -53.992 1.00 46.06 C ANISOU 3406 CA ASP A1127 4883 7016 5598 -444 -42 756 C ATOM 3407 C ASP A1127 13.143 -36.941 -54.316 1.00 45.76 C ANISOU 3407 C ASP A1127 4940 6989 5458 -519 133 542 C ATOM 3408 O ASP A1127 13.135 -38.157 -54.170 1.00 46.52 O ANISOU 3408 O ASP A1127 5070 7086 5518 -563 172 307 O ATOM 3409 CB ASP A1127 11.166 -35.791 -55.282 1.00 49.68 C ANISOU 3409 CB ASP A1127 5344 7735 5795 -538 -180 954 C ATOM 3410 CG ASP A1127 9.696 -35.469 -55.060 1.00 51.25 C ANISOU 3410 CG ASP A1127 5413 7986 6071 -478 -377 1121 C ATOM 3411 OD1 ASP A1127 9.217 -35.421 -53.906 1.00 50.86 O ANISOU 3411 OD1 ASP A1127 5277 7765 6281 -355 -384 1088 O ATOM 3412 OD2 ASP A1127 8.994 -35.280 -56.065 1.00 55.36 O ANISOU 3412 OD2 ASP A1127 5907 8745 6379 -559 -526 1294 O ATOM 3413 N GLU A1128 14.207 -36.279 -54.754 1.00 45.82 N ANISOU 3413 N GLU A1128 4981 6991 5436 -532 250 629 N ATOM 3414 CA GLU A1128 15.476 -36.963 -54.988 1.00 45.56 C ANISOU 3414 CA GLU A1128 4999 6959 5351 -574 448 442 C ATOM 3415 C GLU A1128 15.993 -37.639 -53.730 1.00 42.29 C ANISOU 3415 C GLU A1128 4541 6336 5191 -482 520 250 C ATOM 3416 O GLU A1128 16.328 -38.817 -53.748 1.00 42.66 O ANISOU 3416 O GLU A1128 4623 6381 5204 -498 613 28 O ATOM 3417 CB GLU A1128 16.522 -35.992 -55.496 1.00 47.92 C ANISOU 3417 CB GLU A1128 5299 7274 5632 -599 563 606 C ATOM 3418 CG GLU A1128 16.431 -35.713 -56.987 1.00 52.24 C ANISOU 3418 CG GLU A1128 5923 8082 5842 -724 571 742 C ATOM 3419 CD GLU A1128 17.034 -34.369 -57.352 1.00 55.37 C ANISOU 3419 CD GLU A1128 6303 8464 6271 -741 616 1027 C ATOM 3420 OE1 GLU A1128 16.315 -33.347 -57.215 1.00 57.39 O ANISOU 3420 OE1 GLU A1128 6530 8655 6619 -696 468 1279 O ATOM 3421 OE2 GLU A1128 18.222 -34.330 -57.762 1.00 56.90 O ANISOU 3421 OE2 GLU A1128 6503 8697 6418 -794 810 1008 O ATOM 3422 N ALA A1129 16.044 -36.882 -52.640 1.00 39.80 N ANISOU 3422 N ALA A1129 4157 5840 5124 -385 475 341 N ATOM 3423 CA ALA A1129 16.489 -37.379 -51.344 1.00 36.42 C ANISOU 3423 CA ALA A1129 3683 5232 4920 -302 511 202 C ATOM 3424 C ALA A1129 15.745 -38.637 -50.947 1.00 35.72 C ANISOU 3424 C ALA A1129 3610 5136 4825 -292 470 31 C ATOM 3425 O ALA A1129 16.352 -39.612 -50.514 1.00 34.85 O ANISOU 3425 O ALA A1129 3501 4953 4788 -266 558 -130 O ATOM 3426 CB ALA A1129 16.288 -36.309 -50.284 1.00 35.02 C ANISOU 3426 CB ALA A1129 3459 4892 4951 -223 433 320 C ATOM 3427 N ALA A1130 14.418 -38.585 -51.092 1.00 35.85 N ANISOU 3427 N ALA A1130 3624 5222 4773 -312 333 91 N ATOM 3428 CA ALA A1130 13.520 -39.662 -50.729 1.00 34.71 C ANISOU 3428 CA ALA A1130 3480 5076 4631 -331 274 -36 C ATOM 3429 C ALA A1130 13.777 -40.927 -51.545 1.00 36.63 C ANISOU 3429 C ALA A1130 3810 5393 4713 -435 352 -235 C ATOM 3430 O ALA A1130 13.867 -42.025 -51.003 1.00 36.11 O ANISOU 3430 O ALA A1130 3764 5218 4736 -425 403 -401 O ATOM 3431 CB ALA A1130 12.102 -39.198 -50.936 1.00 35.63 C ANISOU 3431 CB ALA A1130 3543 5297 4695 -349 112 105 C ATOM 3432 N VAL A1131 13.869 -40.772 -52.859 1.00 38.79 N ANISOU 3432 N VAL A1131 4147 5847 4744 -537 367 -218 N ATOM 3433 CA VAL A1131 14.257 -41.871 -53.731 1.00 40.73 C ANISOU 3433 CA VAL A1131 4503 6161 4808 -639 480 -438 C ATOM 3434 C VAL A1131 15.595 -42.471 -53.322 1.00 40.92 C ANISOU 3434 C VAL A1131 4538 6029 4980 -552 686 -586 C ATOM 3435 O VAL A1131 15.757 -43.684 -53.341 1.00 43.05 O ANISOU 3435 O VAL A1131 4874 6218 5263 -569 779 -803 O ATOM 3436 CB VAL A1131 14.365 -41.399 -55.191 1.00 42.80 C ANISOU 3436 CB VAL A1131 4840 6666 4756 -757 492 -374 C ATOM 3437 CG1 VAL A1131 15.181 -42.366 -56.034 1.00 44.29 C ANISOU 3437 CG1 VAL A1131 5154 6901 4770 -830 691 -621 C ATOM 3438 CG2 VAL A1131 12.981 -41.210 -55.768 1.00 44.02 C ANISOU 3438 CG2 VAL A1131 4991 7011 4722 -872 274 -269 C ATOM 3439 N ASN A1132 16.552 -41.623 -52.971 1.00 40.28 N ANISOU 3439 N ASN A1132 4383 5898 5023 -463 756 -462 N ATOM 3440 CA ASN A1132 17.891 -42.080 -52.592 1.00 41.02 C ANISOU 3440 CA ASN A1132 4438 5875 5273 -375 939 -560 C ATOM 3441 C ASN A1132 17.958 -42.714 -51.196 1.00 39.78 C ANISOU 3441 C ASN A1132 4219 5511 5382 -265 912 -614 C ATOM 3442 O ASN A1132 18.728 -43.653 -50.975 1.00 41.78 O ANISOU 3442 O ASN A1132 4464 5660 5747 -199 1045 -747 O ATOM 3443 CB ASN A1132 18.864 -40.906 -52.635 1.00 41.50 C ANISOU 3443 CB ASN A1132 4415 5965 5387 -347 997 -389 C ATOM 3444 CG ASN A1132 20.277 -41.339 -52.892 1.00 43.16 C ANISOU 3444 CG ASN A1132 4579 6167 5653 -305 1219 -480 C ATOM 3445 OD1 ASN A1132 20.573 -41.955 -53.917 1.00 45.70 O ANISOU 3445 OD1 ASN A1132 4976 6590 5798 -350 1376 -615 O ATOM 3446 ND2 ASN A1132 21.171 -41.006 -51.973 1.00 43.20 N ANISOU 3446 ND2 ASN A1132 4452 6064 5898 -220 1240 -411 N ATOM 3447 N LEU A1133 17.187 -42.181 -50.250 1.00 36.82 N ANISOU 3447 N LEU A1133 3798 5079 5112 -235 752 -498 N ATOM 3448 CA LEU A1133 17.137 -42.747 -48.919 1.00 35.06 C ANISOU 3448 CA LEU A1133 3531 4694 5094 -149 716 -528 C ATOM 3449 C LEU A1133 16.536 -44.143 -48.957 1.00 35.98 C ANISOU 3449 C LEU A1133 3720 4748 5202 -183 732 -688 C ATOM 3450 O LEU A1133 16.879 -44.994 -48.149 1.00 35.38 O ANISOU 3450 O LEU A1133 3629 4524 5290 -111 774 -746 O ATOM 3451 CB LEU A1133 16.333 -41.863 -47.971 1.00 33.07 C ANISOU 3451 CB LEU A1133 3233 4415 4917 -120 567 -388 C ATOM 3452 CG LEU A1133 17.029 -40.612 -47.468 1.00 32.89 C ANISOU 3452 CG LEU A1133 3148 4364 4985 -74 553 -260 C ATOM 3453 CD1 LEU A1133 16.075 -39.735 -46.702 1.00 32.16 C ANISOU 3453 CD1 LEU A1133 3043 4236 4941 -46 431 -156 C ATOM 3454 CD2 LEU A1133 18.217 -40.957 -46.590 1.00 33.05 C ANISOU 3454 CD2 LEU A1133 3104 4287 5166 -6 611 -294 C ATOM 3455 N ALA A1134 15.637 -44.368 -49.902 1.00 37.73 N ANISOU 3455 N ALA A1134 4019 5081 5233 -305 686 -747 N ATOM 3456 CA ALA A1134 14.948 -45.644 -50.022 1.00 39.15 C ANISOU 3456 CA ALA A1134 4280 5199 5395 -384 684 -910 C ATOM 3457 C ALA A1134 15.862 -46.751 -50.518 1.00 40.03 C ANISOU 3457 C ALA A1134 4478 5209 5522 -370 875 -1117 C ATOM 3458 O ALA A1134 15.471 -47.907 -50.498 1.00 41.81 O ANISOU 3458 O ALA A1134 4785 5314 5786 -421 902 -1271 O ATOM 3459 CB ALA A1134 13.722 -45.519 -50.936 1.00 39.98 C ANISOU 3459 CB ALA A1134 4431 5483 5275 -548 555 -914 C ATOM 3460 N LYS A1135 17.087 -46.424 -50.853 1.00 40.54 N ANISOU 3460 N LYS A1135 4520 5307 5575 -299 1021 -1119 N ATOM 3461 CA LYS A1135 18.012 -47.389 -51.390 1.00 42.30 C ANISOU 3461 CA LYS A1135 4804 5436 5830 -253 1244 -1315 C ATOM 3462 C LYS A1135 18.958 -47.935 -50.383 1.00 40.93 C ANISOU 3462 C LYS A1135 4534 5052 5963 -74 1332 -1294 C ATOM 3463 O LYS A1135 19.786 -48.733 -50.694 1.00 43.63 O ANISOU 3463 O LYS A1135 4902 5280 6394 5 1528 -1438 O ATOM 3464 CB LYS A1135 18.826 -46.738 -52.465 1.00 44.31 C ANISOU 3464 CB LYS A1135 5066 5865 5902 -272 1390 -1327 C ATOM 3465 CG LYS A1135 18.135 -46.688 -53.785 1.00 46.80 C ANISOU 3465 CG LYS A1135 5528 6381 5871 -456 1370 -1425 C ATOM 3466 CD LYS A1135 19.154 -46.636 -54.877 1.00 49.84 C ANISOU 3466 CD LYS A1135 5954 6920 6060 -473 1585 -1490 C ATOM 3467 CE LYS A1135 19.208 -45.258 -55.469 1.00 49.90 C ANISOU 3467 CE LYS A1135 5940 7183 5834 -568 1487 -1278 C ATOM 3468 NZ LYS A1135 18.114 -45.088 -56.445 1.00 20.00 N ATOM 3469 N SER A1136 18.808 -47.504 -49.162 1.00 37.79 N ANISOU 3469 N SER A1136 4030 4604 5723 -8 1191 -1116 N ATOM 3470 CA SER A1136 19.802 -47.735 -48.130 1.00 37.05 C ANISOU 3470 CA SER A1136 3814 4381 5882 152 1232 -1033 C ATOM 3471 C SER A1136 19.616 -49.012 -47.330 1.00 37.44 C ANISOU 3471 C SER A1136 3893 4207 6122 220 1242 -1078 C ATOM 3472 O SER A1136 18.542 -49.578 -47.284 1.00 36.95 O ANISOU 3472 O SER A1136 3935 4083 6019 126 1176 -1141 O ATOM 3473 CB SER A1136 19.782 -46.559 -47.150 1.00 34.77 C ANISOU 3473 CB SER A1136 3412 4163 5637 171 1069 -826 C ATOM 3474 OG SER A1136 18.537 -46.480 -46.489 1.00 33.38 O ANISOU 3474 OG SER A1136 3279 3971 5431 113 910 -776 O ATOM 3475 N ARG A1137 20.686 -49.427 -46.666 1.00 38.86 N ANISOU 3475 N ARG A1137 3965 4275 6525 379 1315 -1016 N ATOM 3476 CA ARG A1137 20.621 -50.479 -45.667 1.00 40.76 C ANISOU 3476 CA ARG A1137 4205 4305 6978 468 1296 -973 C ATOM 3477 C ARG A1137 19.630 -50.165 -44.569 1.00 39.26 C ANISOU 3477 C ARG A1137 4017 4133 6766 406 1093 -833 C ATOM 3478 O ARG A1137 18.982 -51.054 -44.068 1.00 40.89 O ANISOU 3478 O ARG A1137 4293 4190 7051 389 1069 -835 O ATOM 3479 CB ARG A1137 21.987 -50.687 -45.029 1.00 42.87 C ANISOU 3479 CB ARG A1137 4303 4508 7476 658 1359 -855 C ATOM 3480 CG ARG A1137 22.118 -51.980 -44.223 1.00 45.45 C ANISOU 3480 CG ARG A1137 4633 4587 8048 782 1386 -807 C ATOM 3481 CD ARG A1137 23.558 -52.240 -43.780 1.00 47.55 C ANISOU 3481 CD ARG A1137 4703 4806 8555 990 1460 -681 C ATOM 3482 NE ARG A1137 24.514 -51.873 -44.823 1.00 49.45 N ANISOU 3482 NE ARG A1137 4860 5149 8780 1038 1639 -780 N ATOM 3483 CZ ARG A1137 25.044 -52.701 -45.719 1.00 54.05 C ANISOU 3483 CZ ARG A1137 5475 5601 9458 1136 1891 -951 C ATOM 3484 NH1 ARG A1137 24.769 -54.013 -45.726 1.00 55.90 N ANISOU 3484 NH1 ARG A1137 5835 5555 9847 1208 1999 -1055 N ATOM 3485 NH2 ARG A1137 25.882 -52.203 -46.618 1.00 56.25 N ANISOU 3485 NH2 ARG A1137 5664 6024 9685 1162 2054 -1019 N ATOM 3486 N TRP A1138 19.550 -48.900 -44.181 1.00 38.02 N ANISOU 3486 N TRP A1138 3786 4146 6512 373 967 -712 N ATOM 3487 CA TRP A1138 18.635 -48.447 -43.151 1.00 36.65 C ANISOU 3487 CA TRP A1138 3613 4011 6299 326 803 -594 C ATOM 3488 C TRP A1138 17.189 -48.735 -43.497 1.00 36.74 C ANISOU 3488 C TRP A1138 3733 4022 6201 194 760 -666 C ATOM 3489 O TRP A1138 16.386 -49.099 -42.652 1.00 36.96 O ANISOU 3489 O TRP A1138 3778 3999 6264 168 689 -602 O ATOM 3490 CB TRP A1138 18.821 -46.942 -42.987 1.00 36.11 C ANISOU 3490 CB TRP A1138 3474 4107 6136 304 714 -505 C ATOM 3491 CG TRP A1138 17.783 -46.260 -42.223 1.00 34.47 C ANISOU 3491 CG TRP A1138 3286 3957 5852 250 583 -429 C ATOM 3492 CD1 TRP A1138 17.354 -46.558 -40.965 1.00 34.49 C ANISOU 3492 CD1 TRP A1138 3287 3915 5901 273 510 -345 C ATOM 3493 CD2 TRP A1138 17.031 -45.133 -42.652 1.00 34.50 C ANISOU 3493 CD2 TRP A1138 3309 4077 5721 177 525 -420 C ATOM 3494 NE1 TRP A1138 16.358 -45.684 -40.584 1.00 34.18 N ANISOU 3494 NE1 TRP A1138 3264 3959 5760 221 430 -308 N ATOM 3495 CE2 TRP A1138 16.155 -44.786 -41.600 1.00 34.01 C ANISOU 3495 CE2 TRP A1138 3249 4024 5645 173 434 -347 C ATOM 3496 CE3 TRP A1138 17.024 -44.360 -43.817 1.00 34.99 C ANISOU 3496 CE3 TRP A1138 3384 4237 5672 122 548 -447 C ATOM 3497 CZ2 TRP A1138 15.296 -43.691 -41.678 1.00 33.01 C ANISOU 3497 CZ2 TRP A1138 3126 3981 5433 138 376 -312 C ATOM 3498 CZ3 TRP A1138 16.149 -43.266 -43.892 1.00 33.50 C ANISOU 3498 CZ3 TRP A1138 3201 4131 5394 79 465 -384 C ATOM 3499 CH2 TRP A1138 15.298 -42.958 -42.837 1.00 32.52 C ANISOU 3499 CH2 TRP A1138 3070 3993 5293 97 386 -323 C ATOM 3500 N TYR A1139 16.863 -48.531 -44.756 1.00 37.80 N ANISOU 3500 N TYR A1139 3929 4240 6190 100 800 -787 N ATOM 3501 CA TYR A1139 15.549 -48.803 -45.261 1.00 38.03 C ANISOU 3501 CA TYR A1139 4041 4305 6104 -45 745 -861 C ATOM 3502 C TYR A1139 15.206 -50.318 -45.274 1.00 39.25 C ANISOU 3502 C TYR A1139 4291 4262 6360 -93 809 -980 C ATOM 3503 O TYR A1139 14.046 -50.683 -45.070 1.00 39.65 O ANISOU 3503 O TYR A1139 4371 4301 6392 -210 731 -978 O ATOM 3504 CB TYR A1139 15.421 -48.199 -46.667 1.00 38.85 C ANISOU 3504 CB TYR A1139 4186 4574 5998 -141 759 -947 C ATOM 3505 CG TYR A1139 14.044 -48.372 -47.238 1.00 40.08 C ANISOU 3505 CG TYR A1139 4399 4815 6013 -309 663 -1001 C ATOM 3506 CD1 TYR A1139 13.043 -47.469 -46.940 1.00 38.29 C ANISOU 3506 CD1 TYR A1139 4099 4726 5724 -349 517 -861 C ATOM 3507 CD2 TYR A1139 13.733 -49.473 -48.039 1.00 42.08 C ANISOU 3507 CD2 TYR A1139 4772 5003 6211 -432 719 -1195 C ATOM 3508 CE1 TYR A1139 11.773 -47.637 -47.438 1.00 39.76 C ANISOU 3508 CE1 TYR A1139 4293 5012 5799 -501 414 -884 C ATOM 3509 CE2 TYR A1139 12.465 -49.648 -48.545 1.00 43.25 C ANISOU 3509 CE2 TYR A1139 4954 5250 6228 -617 604 -1241 C ATOM 3510 CZ TYR A1139 11.488 -48.724 -48.239 1.00 42.64 C ANISOU 3510 CZ TYR A1139 4766 5338 6096 -648 444 -1069 C ATOM 3511 OH TYR A1139 10.214 -48.878 -48.737 1.00 45.05 O ANISOU 3511 OH TYR A1139 5061 5769 6286 -830 314 -1086 O ATOM 3512 N ASN A1140 16.169 -51.192 -45.545 1.00 40.20 N ANISOU 3512 N ASN A1140 4454 4218 6600 -9 960 -1083 N ATOM 3513 CA ASN A1140 15.876 -52.632 -45.502 1.00 43.60 C ANISOU 3513 CA ASN A1140 4993 4406 7166 -46 1034 -1194 C ATOM 3514 C ASN A1140 15.709 -53.131 -44.070 1.00 43.83 C ANISOU 3514 C ASN A1140 4974 4290 7389 22 976 -1013 C ATOM 3515 O ASN A1140 14.853 -53.952 -43.796 1.00 44.17 O ANISOU 3515 O ASN A1140 5085 4202 7492 -80 954 -1027 O ATOM 3516 CB ASN A1140 16.951 -53.464 -46.197 1.00 45.98 C ANISOU 3516 CB ASN A1140 5360 4536 7571 50 1242 -1363 C ATOM 3517 CG ASN A1140 17.122 -53.090 -47.649 1.00 47.56 C ANISOU 3517 CG ASN A1140 5634 4887 7549 -32 1329 -1557 C ATOM 3518 OD1 ASN A1140 16.156 -53.043 -48.396 1.00 48.44 O ANISOU 3518 OD1 ASN A1140 5842 5102 7459 -226 1262 -1672 O ATOM 3519 ND2 ASN A1140 18.360 -52.811 -48.060 1.00 49.17 N ANISOU 3519 ND2 ASN A1140 5778 5127 7776 106 1476 -1579 N ATOM 3520 N GLN A1141 16.522 -52.616 -43.161 1.00 44.22 N ANISOU 3520 N GLN A1141 4904 4379 7518 177 945 -836 N ATOM 3521 CA GLN A1141 16.523 -53.088 -41.800 1.00 45.76 C ANISOU 3521 CA GLN A1141 5057 4463 7864 251 891 -648 C ATOM 3522 C GLN A1141 15.220 -52.778 -41.130 1.00 44.32 C ANISOU 3522 C GLN A1141 4876 4376 7585 126 767 -556 C ATOM 3523 O GLN A1141 14.672 -53.621 -40.444 1.00 47.09 O ANISOU 3523 O GLN A1141 5264 4591 8035 88 761 -478 O ATOM 3524 CB GLN A1141 17.686 -52.478 -41.006 1.00 48.07 C ANISOU 3524 CB GLN A1141 5213 4833 8217 417 854 -482 C ATOM 3525 CG GLN A1141 19.045 -53.092 -41.327 1.00 51.66 C ANISOU 3525 CG GLN A1141 5618 5152 8857 582 988 -507 C ATOM 3526 CD GLN A1141 19.049 -54.598 -41.115 1.00 57.90 C ANISOU 3526 CD GLN A1141 6485 5641 9872 643 1083 -506 C ATOM 3527 OE1 GLN A1141 18.728 -55.089 -40.021 1.00 60.29 O ANISOU 3527 OE1 GLN A1141 6787 5855 10264 658 1007 -327 O ATOM 3528 NE2 GLN A1141 19.377 -55.346 -42.171 1.00 62.11 N ANISOU 3528 NE2 GLN A1141 7101 6005 10491 669 1262 -710 N ATOM 3529 N THR A1142 14.708 -51.573 -41.334 1.00 42.25 N ANISOU 3529 N THR A1142 4569 4340 7142 65 682 -552 N ATOM 3530 CA THR A1142 13.463 -51.157 -40.686 1.00 40.73 C ANISOU 3530 CA THR A1142 4349 4258 6868 -26 585 -460 C ATOM 3531 C THR A1142 12.609 -50.333 -41.631 1.00 38.22 C ANISOU 3531 C THR A1142 4019 4117 6383 -139 533 -542 C ATOM 3532 O THR A1142 12.656 -49.118 -41.561 1.00 38.42 O ANISOU 3532 O THR A1142 3984 4298 6315 -96 480 -487 O ATOM 3533 CB THR A1142 13.776 -50.308 -39.447 1.00 40.11 C ANISOU 3533 CB THR A1142 4193 4282 6764 72 519 -293 C ATOM 3534 OG1 THR A1142 14.648 -49.235 -39.815 1.00 39.38 O ANISOU 3534 OG1 THR A1142 4054 4299 6609 143 505 -315 O ATOM 3535 CG2 THR A1142 14.452 -51.158 -38.384 1.00 41.15 C ANISOU 3535 CG2 THR A1142 4325 4276 7035 167 534 -162 C ATOM 3536 N PRO A1143 11.829 -50.984 -42.507 1.00 36.89 N ANISOU 3536 N PRO A1143 3911 3922 6183 -291 538 -665 N ATOM 3537 CA PRO A1143 11.166 -50.270 -43.594 1.00 36.47 C ANISOU 3537 CA PRO A1143 3843 4056 5957 -399 474 -736 C ATOM 3538 C PRO A1143 9.936 -49.394 -43.279 1.00 35.55 C ANISOU 3538 C PRO A1143 3616 4126 5764 -450 362 -616 C ATOM 3539 O PRO A1143 9.670 -48.447 -44.014 1.00 34.28 O ANISOU 3539 O PRO A1143 3414 4134 5474 -467 301 -609 O ATOM 3540 CB PRO A1143 10.776 -51.393 -44.561 1.00 38.05 C ANISOU 3540 CB PRO A1143 4149 4162 6143 -566 505 -920 C ATOM 3541 CG PRO A1143 10.755 -52.615 -43.743 1.00 38.62 C ANISOU 3541 CG PRO A1143 4269 3994 6408 -571 564 -903 C ATOM 3542 CD PRO A1143 11.844 -52.433 -42.752 1.00 38.35 C ANISOU 3542 CD PRO A1143 4198 3881 6489 -361 617 -774 C ATOM 3543 N ASN A1144 9.156 -49.722 -42.261 1.00 35.91 N ANISOU 3543 N ASN A1144 3609 4145 5890 -473 345 -513 N ATOM 3544 CA ASN A1144 8.007 -48.886 -41.962 1.00 35.92 C ANISOU 3544 CA ASN A1144 3485 4323 5839 -495 271 -402 C ATOM 3545 C ASN A1144 8.487 -47.550 -41.415 1.00 35.43 C ANISOU 3545 C ASN A1144 3379 4340 5741 -328 270 -313 C ATOM 3546 O ASN A1144 8.075 -46.483 -41.881 1.00 35.40 O ANISOU 3546 O ASN A1144 3309 4476 5663 -306 217 -275 O ATOM 3547 CB ASN A1144 7.025 -49.544 -40.986 1.00 36.24 C ANISOU 3547 CB ASN A1144 3465 4335 5969 -566 282 -308 C ATOM 3548 CG ASN A1144 6.529 -50.893 -41.459 1.00 37.29 C ANISOU 3548 CG ASN A1144 3649 4355 6165 -761 281 -396 C ATOM 3549 OD1 ASN A1144 6.108 -51.055 -42.604 1.00 37.69 O ANISOU 3549 OD1 ASN A1144 3708 4469 6143 -905 218 -508 O ATOM 3550 ND2 ASN A1144 6.547 -51.865 -40.560 1.00 37.72 N ANISOU 3550 ND2 ASN A1144 3743 4241 6347 -781 346 -338 N ATOM 3551 N ARG A1145 9.392 -47.622 -40.447 1.00 36.01 N ANISOU 3551 N ARG A1145 3493 4314 5873 -217 322 -275 N ATOM 3552 CA ARG A1145 9.902 -46.446 -39.758 1.00 34.65 C ANISOU 3552 CA ARG A1145 3299 4195 5671 -86 319 -211 C ATOM 3553 C ARG A1145 10.608 -45.579 -40.742 1.00 34.04 C ANISOU 3553 C ARG A1145 3234 4161 5535 -54 300 -261 C ATOM 3554 O ARG A1145 10.412 -44.378 -40.760 1.00 37.37 O ANISOU 3554 O ARG A1145 3617 4663 5915 -5 273 -217 O ATOM 3555 CB ARG A1145 10.887 -46.842 -38.679 1.00 33.80 C ANISOU 3555 CB ARG A1145 3235 3988 5617 -6 351 -168 C ATOM 3556 CG ARG A1145 11.659 -45.689 -38.109 1.00 32.81 C ANISOU 3556 CG ARG A1145 3106 3909 5450 92 331 -141 C ATOM 3557 CD ARG A1145 12.493 -46.128 -36.931 1.00 33.01 C ANISOU 3557 CD ARG A1145 3156 3880 5505 148 330 -74 C ATOM 3558 NE ARG A1145 12.788 -44.990 -36.078 1.00 33.02 N ANISOU 3558 NE ARG A1145 3159 3955 5430 199 299 -51 N ATOM 3559 CZ ARG A1145 13.474 -45.060 -34.943 1.00 33.70 C ANISOU 3559 CZ ARG A1145 3264 4049 5488 233 267 9 C ATOM 3560 NH1 ARG A1145 13.939 -46.222 -34.496 1.00 34.61 N ANISOU 3560 NH1 ARG A1145 3384 4100 5663 244 261 90 N ATOM 3561 NH2 ARG A1145 13.679 -43.953 -34.244 1.00 33.72 N ANISOU 3561 NH2 ARG A1145 3288 4120 5401 251 236 -8 N ATOM 3562 N ALA A1146 11.441 -46.197 -41.555 1.00 33.58 N ANISOU 3562 N ALA A1146 3234 4039 5485 -78 333 -350 N ATOM 3563 CA ALA A1146 12.186 -45.476 -42.559 1.00 32.59 C ANISOU 3563 CA ALA A1146 3122 3967 5293 -62 340 -391 C ATOM 3564 C ALA A1146 11.240 -44.732 -43.471 1.00 32.25 C ANISOU 3564 C ALA A1146 3045 4065 5140 -128 275 -369 C ATOM 3565 O ALA A1146 11.404 -43.552 -43.709 1.00 32.07 O ANISOU 3565 O ALA A1146 2998 4109 5078 -81 250 -305 O ATOM 3566 CB ALA A1146 13.032 -46.439 -43.363 1.00 33.54 C ANISOU 3566 CB ALA A1146 3308 4006 5429 -87 418 -511 C ATOM 3567 N LYS A1147 10.225 -45.413 -43.968 1.00 33.55 N ANISOU 3567 N LYS A1147 3203 4277 5267 -244 236 -404 N ATOM 3568 CA LYS A1147 9.319 -44.764 -44.889 1.00 34.09 C ANISOU 3568 CA LYS A1147 3217 4510 5224 -313 147 -358 C ATOM 3569 C LYS A1147 8.553 -43.599 -44.266 1.00 32.39 C ANISOU 3569 C LYS A1147 2893 4366 5048 -222 99 -207 C ATOM 3570 O LYS A1147 8.228 -42.642 -44.958 1.00 31.70 O ANISOU 3570 O LYS A1147 2759 4387 4897 -208 39 -123 O ATOM 3571 CB LYS A1147 8.340 -45.735 -45.491 1.00 36.16 C ANISOU 3571 CB LYS A1147 3473 4827 5437 -483 91 -425 C ATOM 3572 CG LYS A1147 7.869 -45.222 -46.826 1.00 39.14 C ANISOU 3572 CG LYS A1147 3831 5396 5645 -577 -7 -408 C ATOM 3573 CD LYS A1147 6.640 -45.957 -47.296 1.00 43.45 C ANISOU 3573 CD LYS A1147 4324 6046 6138 -765 -112 -439 C ATOM 3574 CE LYS A1147 6.044 -45.258 -48.501 1.00 46.69 C ANISOU 3574 CE LYS A1147 4677 6694 6367 -848 -250 -362 C ATOM 3575 NZ LYS A1147 7.078 -45.107 -49.560 1.00 49.01 N ANISOU 3575 NZ LYS A1147 5115 7019 6488 -867 -204 -453 N ATOM 3576 N ARG A1148 8.249 -43.688 -42.978 1.00 31.13 N ANISOU 3576 N ARG A1148 2695 4142 4989 -157 136 -168 N ATOM 3577 CA ARG A1148 7.553 -42.612 -42.306 1.00 30.60 C ANISOU 3577 CA ARG A1148 2539 4120 4966 -54 131 -57 C ATOM 3578 C ARG A1148 8.429 -41.363 -42.277 1.00 29.65 C ANISOU 3578 C ARG A1148 2466 3953 4846 56 150 -32 C ATOM 3579 O ARG A1148 7.997 -40.282 -42.654 1.00 29.21 O ANISOU 3579 O ARG A1148 2359 3945 4794 113 119 56 O ATOM 3580 CB ARG A1148 7.148 -43.025 -40.892 1.00 30.91 C ANISOU 3580 CB ARG A1148 2553 4111 5079 -17 194 -40 C ATOM 3581 CG ARG A1148 5.928 -43.945 -40.825 1.00 32.29 C ANISOU 3581 CG ARG A1148 2634 4352 5282 -126 179 -12 C ATOM 3582 CD ARG A1148 5.270 -43.961 -39.437 1.00 32.14 C ANISOU 3582 CD ARG A1148 2553 4335 5321 -69 260 52 C ATOM 3583 NE ARG A1148 6.042 -44.711 -38.460 1.00 30.79 N ANISOU 3583 NE ARG A1148 2490 4049 5159 -66 322 22 N ATOM 3584 CZ ARG A1148 6.059 -46.032 -38.359 1.00 30.72 C ANISOU 3584 CZ ARG A1148 2517 3969 5185 -177 331 8 C ATOM 3585 NH1 ARG A1148 5.336 -46.791 -39.158 1.00 31.99 N ANISOU 3585 NH1 ARG A1148 2628 4156 5371 -325 285 -10 N ATOM 3586 NH2 ARG A1148 6.815 -46.593 -37.445 1.00 30.75 N ANISOU 3586 NH2 ARG A1148 2611 3869 5203 -146 379 20 N ATOM 3587 N VAL A1149 9.676 -41.535 -41.855 1.00 29.04 N ANISOU 3587 N VAL A1149 2476 3774 4781 79 197 -97 N ATOM 3588 CA VAL A1149 10.680 -40.472 -41.930 1.00 28.66 C ANISOU 3588 CA VAL A1149 2472 3678 4738 139 208 -86 C ATOM 3589 C VAL A1149 10.914 -39.963 -43.350 1.00 28.85 C ANISOU 3589 C VAL A1149 2501 3766 4693 97 178 -51 C ATOM 3590 O VAL A1149 10.944 -38.763 -43.594 1.00 29.87 O ANISOU 3590 O VAL A1149 2625 3888 4836 144 164 30 O ATOM 3591 CB VAL A1149 12.019 -40.948 -41.388 1.00 28.57 C ANISOU 3591 CB VAL A1149 2517 3583 4753 144 246 -152 C ATOM 3592 CG1 VAL A1149 13.072 -39.884 -41.616 1.00 29.14 C ANISOU 3592 CG1 VAL A1149 2612 3623 4836 166 250 -137 C ATOM 3593 CG2 VAL A1149 11.908 -41.270 -39.902 1.00 28.92 C ANISOU 3593 CG2 VAL A1149 2570 3583 4836 185 262 -155 C ATOM 3594 N ILE A1150 11.090 -40.867 -44.291 1.00 28.61 N ANISOU 3594 N ILE A1150 2495 3791 4583 5 176 -113 N ATOM 3595 CA ILE A1150 11.200 -40.453 -45.661 1.00 30.04 C ANISOU 3595 CA ILE A1150 2691 4073 4650 -51 150 -76 C ATOM 3596 C ILE A1150 10.028 -39.579 -46.081 1.00 30.89 C ANISOU 3596 C ILE A1150 2723 4281 4732 -36 60 67 C ATOM 3597 O ILE A1150 10.249 -38.529 -46.660 1.00 31.84 O ANISOU 3597 O ILE A1150 2847 4424 4827 -9 43 177 O ATOM 3598 CB ILE A1150 11.402 -41.661 -46.600 1.00 32.21 C ANISOU 3598 CB ILE A1150 3021 4402 4813 -168 172 -200 C ATOM 3599 CG1 ILE A1150 12.855 -42.129 -46.494 1.00 32.05 C ANISOU 3599 CG1 ILE A1150 3059 4283 4834 -141 286 -300 C ATOM 3600 CG2 ILE A1150 11.116 -41.304 -48.059 1.00 33.93 C ANISOU 3600 CG2 ILE A1150 3255 4785 4851 -258 119 -155 C ATOM 3601 CD1 ILE A1150 13.051 -43.547 -46.966 1.00 33.68 C ANISOU 3601 CD1 ILE A1150 3330 4460 5003 -214 349 -460 C ATOM 3602 N THR A1151 8.796 -40.015 -45.788 1.00 31.90 N ANISOU 3602 N THR A1151 2769 4468 4882 -53 5 87 N ATOM 3603 CA THR A1151 7.578 -39.270 -46.096 1.00 32.56 C ANISOU 3603 CA THR A1151 2734 4660 4975 -19 -83 245 C ATOM 3604 C THR A1151 7.553 -37.905 -45.442 1.00 32.90 C ANISOU 3604 C THR A1151 2751 4602 5148 142 -47 355 C ATOM 3605 O THR A1151 7.201 -36.913 -46.066 1.00 34.72 O ANISOU 3605 O THR A1151 2935 4872 5383 194 -99 511 O ATOM 3606 CB THR A1151 6.340 -40.038 -45.644 1.00 33.49 C ANISOU 3606 CB THR A1151 2740 4848 5136 -62 -123 241 C ATOM 3607 OG1 THR A1151 6.158 -41.154 -46.504 1.00 35.79 O ANISOU 3607 OG1 THR A1151 3053 5243 5300 -242 -186 153 O ATOM 3608 CG2 THR A1151 5.063 -39.183 -45.720 1.00 35.03 C ANISOU 3608 CG2 THR A1151 2762 5149 5396 17 -196 427 C ATOM 3609 N THR A1152 7.922 -37.855 -44.175 1.00 31.70 N ANISOU 3609 N THR A1152 2637 4309 5097 218 41 277 N ATOM 3610 CA THR A1152 8.078 -36.597 -43.514 1.00 32.21 C ANISOU 3610 CA THR A1152 2721 4244 5271 349 93 325 C ATOM 3611 C THR A1152 9.083 -35.672 -44.221 1.00 33.63 C ANISOU 3611 C THR A1152 2981 4357 5438 343 91 377 C ATOM 3612 O THR A1152 8.838 -34.479 -44.289 1.00 34.40 O ANISOU 3612 O THR A1152 3069 4377 5623 434 94 490 O ATOM 3613 CB THR A1152 8.532 -36.790 -42.068 1.00 30.90 C ANISOU 3613 CB THR A1152 2618 3962 5160 389 180 201 C ATOM 3614 OG1 THR A1152 7.723 -37.789 -41.462 1.00 31.16 O ANISOU 3614 OG1 THR A1152 2587 4064 5188 368 194 166 O ATOM 3615 CG2 THR A1152 8.374 -35.491 -41.295 1.00 31.50 C ANISOU 3615 CG2 THR A1152 2717 3907 5343 519 242 221 C ATOM 3616 N PHE A1153 10.214 -36.209 -44.702 1.00 33.96 N ANISOU 3616 N PHE A1153 3096 4413 5391 243 102 302 N ATOM 3617 CA PHE A1153 11.211 -35.393 -45.408 1.00 34.74 C ANISOU 3617 CA PHE A1153 3254 4470 5474 215 117 363 C ATOM 3618 C PHE A1153 10.608 -34.826 -46.675 1.00 37.06 C ANISOU 3618 C PHE A1153 3511 4874 5694 202 48 541 C ATOM 3619 O PHE A1153 10.750 -33.652 -46.941 1.00 38.51 O ANISOU 3619 O PHE A1153 3711 4978 5942 248 49 678 O ATOM 3620 CB PHE A1153 12.520 -36.160 -45.752 1.00 33.56 C ANISOU 3620 CB PHE A1153 3158 4345 5247 118 166 254 C ATOM 3621 CG PHE A1153 13.549 -36.166 -44.641 1.00 32.48 C ANISOU 3621 CG PHE A1153 3052 4081 5207 135 219 153 C ATOM 3622 CD1 PHE A1153 13.892 -34.996 -43.971 1.00 32.63 C ANISOU 3622 CD1 PHE A1153 3099 3963 5334 174 228 183 C ATOM 3623 CD2 PHE A1153 14.178 -37.341 -44.262 1.00 32.02 C ANISOU 3623 CD2 PHE A1153 2995 4035 5135 106 251 32 C ATOM 3624 CE1 PHE A1153 14.817 -35.009 -42.944 1.00 32.48 C ANISOU 3624 CE1 PHE A1153 3105 3860 5377 161 247 88 C ATOM 3625 CE2 PHE A1153 15.115 -37.354 -43.232 1.00 31.87 C ANISOU 3625 CE2 PHE A1153 2981 3930 5195 120 270 -28 C ATOM 3626 CZ PHE A1153 15.434 -36.195 -42.574 1.00 31.65 C ANISOU 3626 CZ PHE A1153 2977 3804 5243 135 258 -4 C ATOM 3627 N ARG A1154 9.911 -35.632 -47.452 1.00 38.99 N ANISOU 3627 N ARG A1154 3709 5301 5805 130 -21 552 N ATOM 3628 CA ARG A1154 9.458 -35.109 -48.729 1.00 42.80 C ANISOU 3628 CA ARG A1154 4161 5927 6172 95 -109 738 C ATOM 3629 C ARG A1154 8.246 -34.180 -48.676 1.00 43.37 C ANISOU 3629 C ARG A1154 4120 6001 6356 217 -188 945 C ATOM 3630 O ARG A1154 8.043 -33.402 -49.600 1.00 45.58 O ANISOU 3630 O ARG A1154 4380 6349 6588 225 -256 1155 O ATOM 3631 CB ARG A1154 9.271 -36.204 -49.780 1.00 45.42 C ANISOU 3631 CB ARG A1154 4504 6478 6275 -59 -170 674 C ATOM 3632 CG ARG A1154 8.235 -37.253 -49.494 1.00 47.38 C ANISOU 3632 CG ARG A1154 4675 6815 6510 -106 -236 584 C ATOM 3633 CD ARG A1154 8.320 -38.317 -50.585 1.00 50.44 C ANISOU 3633 CD ARG A1154 5125 7379 6659 -291 -276 471 C ATOM 3634 NE ARG A1154 8.175 -37.715 -51.902 1.00 53.88 N ANISOU 3634 NE ARG A1154 5566 8004 6899 -358 -369 637 N ATOM 3635 CZ ARG A1154 7.014 -37.315 -52.428 1.00 59.89 C ANISOU 3635 CZ ARG A1154 6209 8939 7606 -371 -535 832 C ATOM 3636 NH1 ARG A1154 5.856 -37.457 -51.767 1.00 60.35 N ANISOU 3636 NH1 ARG A1154 6113 9008 7808 -319 -613 876 N ATOM 3637 NH2 ARG A1154 7.002 -36.763 -53.635 1.00 63.52 N ANISOU 3637 NH2 ARG A1154 6688 9582 7864 -435 -623 1006 N ATOM 3638 N THR A1155 7.469 -34.243 -47.604 1.00 42.20 N ANISOU 3638 N THR A1155 3894 5780 6360 321 -166 902 N ATOM 3639 CA THR A1155 6.259 -33.440 -47.480 1.00 43.53 C ANISOU 3639 CA THR A1155 3923 5948 6665 466 -213 1088 C ATOM 3640 C THR A1155 6.353 -32.294 -46.457 1.00 42.81 C ANISOU 3640 C THR A1155 3864 5597 6803 644 -99 1099 C ATOM 3641 O THR A1155 5.714 -31.279 -46.628 1.00 43.59 O ANISOU 3641 O THR A1155 3892 5634 7035 783 -114 1290 O ATOM 3642 CB THR A1155 5.077 -34.329 -47.069 1.00 44.58 C ANISOU 3642 CB THR A1155 3906 6218 6811 458 -256 1048 C ATOM 3643 OG1 THR A1155 5.382 -34.981 -45.827 1.00 44.68 O ANISOU 3643 OG1 THR A1155 3975 6120 6881 460 -141 836 O ATOM 3644 CG2 THR A1155 4.783 -35.377 -48.121 1.00 45.18 C ANISOU 3644 CG2 THR A1155 3946 6543 6675 267 -388 1039 C ATOM 3645 N GLY A1156 7.117 -32.472 -45.383 1.00 41.31 N ANISOU 3645 N GLY A1156 3782 5253 6657 640 10 895 N ATOM 3646 CA GLY A1156 7.086 -31.550 -44.249 1.00 41.42 C ANISOU 3646 CA GLY A1156 3841 5038 6856 785 123 844 C ATOM 3647 C GLY A1156 5.766 -31.583 -43.484 1.00 43.28 C ANISOU 3647 C GLY A1156 3944 5296 7204 927 169 854 C ATOM 3648 O GLY A1156 5.538 -30.758 -42.594 1.00 45.63 O ANISOU 3648 O GLY A1156 4271 5410 7655 1071 284 814 O ATOM 3649 N THR A1157 4.901 -32.547 -43.808 1.00 43.12 N ANISOU 3649 N THR A1157 3776 5498 7107 876 95 894 N ATOM 3650 CA THR A1157 3.591 -32.700 -43.169 1.00 43.66 C ANISOU 3650 CA THR A1157 3673 5635 7281 988 139 927 C ATOM 3651 C THR A1157 3.661 -33.770 -42.096 1.00 41.59 C ANISOU 3651 C THR A1157 3442 5403 6956 915 217 729 C ATOM 3652 O THR A1157 4.671 -34.428 -41.953 1.00 37.92 O ANISOU 3652 O THR A1157 3117 4914 6375 786 212 589 O ATOM 3653 CB THR A1157 2.533 -33.168 -44.185 1.00 44.94 C ANISOU 3653 CB THR A1157 3624 6051 7399 940 -11 1112 C ATOM 3654 OG1 THR A1157 2.948 -34.423 -44.771 1.00 43.59 O ANISOU 3654 OG1 THR A1157 3499 6038 7023 712 -110 1018 O ATOM 3655 CG2 THR A1157 2.341 -32.117 -45.275 1.00 46.61 C ANISOU 3655 CG2 THR A1157 3780 6267 7660 1021 -110 1364 C ATOM 3656 N TRP A1158 2.559 -33.956 -41.375 1.00 42.88 N ANISOU 3656 N TRP A1158 3458 5629 7204 1001 292 743 N ATOM 3657 CA TRP A1158 2.434 -35.064 -40.436 1.00 42.12 C ANISOU 3657 CA TRP A1158 3364 5596 7042 917 359 607 C ATOM 3658 C TRP A1158 1.774 -36.312 -41.051 1.00 40.42 C ANISOU 3658 C TRP A1158 3004 5598 6754 753 243 661 C ATOM 3659 O TRP A1158 1.370 -37.216 -40.315 1.00 38.52 O ANISOU 3659 O TRP A1158 2718 5418 6499 689 301 600 O ATOM 3660 CB TRP A1158 1.638 -34.611 -39.214 1.00 45.23 C ANISOU 3660 CB TRP A1158 3689 5942 7551 1084 539 579 C ATOM 3661 CG TRP A1158 2.434 -33.796 -38.268 1.00 47.37 C ANISOU 3661 CG TRP A1158 4164 6000 7832 1172 670 429 C ATOM 3662 CD1 TRP A1158 2.632 -32.445 -38.305 1.00 49.37 C ANISOU 3662 CD1 TRP A1158 4490 6061 8205 1320 728 440 C ATOM 3663 CD2 TRP A1158 3.151 -34.276 -37.134 1.00 47.59 C ANISOU 3663 CD2 TRP A1158 4357 5982 7743 1101 750 246 C ATOM 3664 NE1 TRP A1158 3.424 -32.053 -37.253 1.00 49.31 N ANISOU 3664 NE1 TRP A1158 4690 5890 8153 1326 838 245 N ATOM 3665 CE2 TRP A1158 3.760 -33.159 -36.521 1.00 48.31 C ANISOU 3665 CE2 TRP A1158 4617 5871 7867 1194 843 132 C ATOM 3666 CE3 TRP A1158 3.333 -35.541 -36.570 1.00 46.76 C ANISOU 3666 CE3 TRP A1158 4275 5983 7509 964 745 181 C ATOM 3667 CZ2 TRP A1158 4.540 -33.272 -35.375 1.00 48.66 C ANISOU 3667 CZ2 TRP A1158 4843 5853 7791 1138 911 -49 C ATOM 3668 CZ3 TRP A1158 4.099 -35.653 -35.434 1.00 47.33 C ANISOU 3668 CZ3 TRP A1158 4519 5987 7474 934 818 33 C ATOM 3669 CH2 TRP A1158 4.695 -34.523 -34.842 1.00 48.27 C ANISOU 3669 CH2 TRP A1158 4797 5941 7600 1014 891 -83 C ATOM 3670 N ASP A1159 1.703 -36.360 -42.383 1.00 40.14 N ANISOU 3670 N ASP A1159 2915 5675 6661 668 81 770 N ATOM 3671 CA ASP A1159 0.992 -37.407 -43.139 1.00 41.07 C ANISOU 3671 CA ASP A1159 2894 6007 6702 491 -56 820 C ATOM 3672 C ASP A1159 1.269 -38.838 -42.655 1.00 38.98 C ANISOU 3672 C ASP A1159 2707 5746 6356 314 -28 656 C ATOM 3673 O ASP A1159 0.385 -39.671 -42.637 1.00 40.92 O ANISOU 3673 O ASP A1159 2810 6122 6615 202 -67 681 O ATOM 3674 CB ASP A1159 1.348 -37.342 -44.643 1.00 42.16 C ANISOU 3674 CB ASP A1159 3068 6245 6703 379 -229 891 C ATOM 3675 CG ASP A1159 0.683 -36.163 -45.394 1.00 45.22 C ANISOU 3675 CG ASP A1159 3307 6709 7165 513 -319 1138 C ATOM 3676 OD1 ASP A1159 -0.259 -35.496 -44.897 1.00 47.67 O ANISOU 3676 OD1 ASP A1159 3434 7019 7657 692 -266 1269 O ATOM 3677 OD2 ASP A1159 1.106 -35.917 -46.539 1.00 46.85 O ANISOU 3677 OD2 ASP A1159 3574 6983 7242 442 -440 1215 O ATOM 3678 N ALA A1160 2.502 -39.117 -42.270 1.00 36.17 N ANISOU 3678 N ALA A1160 2566 5240 5935 287 34 506 N ATOM 3679 CA ALA A1160 2.922 -40.465 -41.943 1.00 34.18 C ANISOU 3679 CA ALA A1160 2404 4959 5620 135 51 375 C ATOM 3680 C ALA A1160 2.554 -40.872 -40.502 1.00 33.65 C ANISOU 3680 C ALA A1160 2313 4848 5621 176 184 347 C ATOM 3681 O ALA A1160 2.616 -42.042 -40.156 1.00 33.01 O ANISOU 3681 O ALA A1160 2269 4752 5519 51 200 287 O ATOM 3682 CB ALA A1160 4.423 -40.589 -42.186 1.00 31.91 C ANISOU 3682 CB ALA A1160 2326 4546 5250 107 60 257 C ATOM 3683 N TYR A1161 2.127 -39.915 -39.685 1.00 33.90 N ANISOU 3683 N TYR A1161 2286 4859 5733 348 289 395 N ATOM 3684 CA TYR A1161 1.960 -40.130 -38.250 1.00 33.34 C ANISOU 3684 CA TYR A1161 2236 4751 5680 400 441 353 C ATOM 3685 C TYR A1161 0.530 -39.939 -37.775 1.00 35.49 C ANISOU 3685 C TYR A1161 2286 5145 6052 471 530 457 C ATOM 3686 O TYR A1161 0.278 -39.284 -36.780 1.00 36.19 O ANISOU 3686 O TYR A1161 2372 5201 6175 618 685 442 O ATOM 3687 CB TYR A1161 2.901 -39.186 -37.512 1.00 32.42 C ANISOU 3687 CB TYR A1161 2290 4488 5539 532 526 266 C ATOM 3688 CG TYR A1161 4.323 -39.614 -37.659 1.00 30.54 C ANISOU 3688 CG TYR A1161 2239 4152 5213 447 465 171 C ATOM 3689 CD1 TYR A1161 4.784 -40.756 -36.991 1.00 29.64 C ANISOU 3689 CD1 TYR A1161 2201 4019 5039 350 483 121 C ATOM 3690 CD2 TYR A1161 5.201 -38.930 -38.468 1.00 29.51 C ANISOU 3690 CD2 TYR A1161 2191 3949 5071 463 395 152 C ATOM 3691 CE1 TYR A1161 6.073 -41.190 -37.120 1.00 28.17 C ANISOU 3691 CE1 TYR A1161 2152 3747 4802 295 432 54 C ATOM 3692 CE2 TYR A1161 6.507 -39.374 -38.599 1.00 28.77 C ANISOU 3692 CE2 TYR A1161 2233 3784 4914 389 354 73 C ATOM 3693 CZ TYR A1161 6.928 -40.511 -37.917 1.00 28.06 C ANISOU 3693 CZ TYR A1161 2199 3678 4782 315 373 23 C ATOM 3694 OH TYR A1161 8.231 -40.975 -38.022 1.00 28.21 O ANISOU 3694 OH TYR A1161 2323 3627 4768 267 340 -35 O ATOM 3695 N GLY A1162 -0.414 -40.532 -38.490 1.00 37.50 N ANISOU 3695 N GLY A1162 2346 5551 6350 357 436 556 N ATOM 3696 CA GLY A1162 -1.776 -40.683 -37.982 1.00 39.94 C ANISOU 3696 CA GLY A1162 2407 6004 6762 375 521 664 C ATOM 3697 C GLY A1162 -1.877 -41.473 -36.682 1.00 40.49 C ANISOU 3697 C GLY A1162 2517 6062 6803 323 680 622 C ATOM 3698 O GLY A1162 -2.794 -41.239 -35.904 1.00 41.73 O ANISOU 3698 O GLY A1162 2515 6307 7032 412 835 689 O ATOM 3699 N SER A1163 -0.947 -42.406 -36.451 1.00 39.50 N ANISOU 3699 N SER A1163 2596 5833 6577 188 653 530 N ATOM 3700 CA SER A1163 -0.915 -43.175 -35.192 1.00 40.57 C ANISOU 3700 CA SER A1163 2798 5948 6667 138 792 521 C ATOM 3701 C SER A1163 -0.696 -42.339 -33.939 1.00 42.03 C ANISOU 3701 C SER A1163 3074 6102 6791 319 974 475 C ATOM 3702 O SER A1163 -1.180 -42.719 -32.885 1.00 44.06 O ANISOU 3702 O SER A1163 3298 6424 7016 307 1125 514 O ATOM 3703 CB SER A1163 0.126 -44.306 -35.213 1.00 38.55 C ANISOU 3703 CB SER A1163 2745 5564 6338 -13 719 455 C ATOM 3704 OG SER A1163 1.268 -44.005 -35.989 1.00 36.24 O ANISOU 3704 OG SER A1163 2610 5161 5999 10 604 359 O ATOM 3705 N GLY A1164 -0.043 -41.204 -34.033 1.00 42.50 N ANISOU 3705 N GLY A1164 3254 6066 6826 469 966 389 N ATOM 3706 CA GLY A1164 0.230 -40.411 -32.865 1.00 43.26 C ANISOU 3706 CA GLY A1164 3469 6112 6853 626 1130 303 C ATOM 3707 C GLY A1164 -0.944 -40.030 -32.023 1.00 47.13 C ANISOU 3707 C GLY A1164 3802 6723 7382 726 1345 351 C ATOM 3708 O GLY A1164 -1.984 -39.767 -32.532 1.00 48.63 O ANISOU 3708 O GLY A1164 3746 7007 7721 784 1365 454 O ATOM 3709 N SER A1165 -0.750 -39.982 -30.721 1.00 49.45 N ANISOU 3709 N SER A1165 4220 7033 7533 742 1506 290 N ATOM 3710 CA SER A1165 -1.718 -39.452 -29.790 1.00 53.76 C ANISOU 3710 CA SER A1165 4643 7696 8087 855 1759 308 C ATOM 3711 C SER A1165 -1.281 -38.081 -29.327 1.00 54.84 C ANISOU 3711 C SER A1165 4850 7740 8247 1083 1899 175 C ATOM 3712 O SER A1165 -0.549 -37.975 -28.377 1.00 52.08 O ANISOU 3712 O SER A1165 4753 7268 7763 1111 1899 18 O ATOM 3713 CB SER A1165 -1.812 -40.353 -28.579 1.00 56.39 C ANISOU 3713 CB SER A1165 5083 8117 8225 759 1892 313 C ATOM 3714 OG SER A1165 -2.445 -41.568 -28.876 1.00 59.23 O ANISOU 3714 OG SER A1165 5267 8594 8642 594 1878 481 O TER 3715 SER A1165 ATOM 3716 N ARG B 8 0.957 26.985 -22.948 1.00 59.09 N ATOM 3717 CA ARG B 8 0.037 26.012 -22.282 1.00 57.52 C ATOM 3718 C ARG B 8 0.292 24.593 -22.772 1.00 57.35 C ATOM 3719 O ARG B 8 -0.261 24.173 -23.786 1.00 58.87 O ATOM 3720 CB ARG B 8 -1.423 26.382 -22.534 1.00 56.37 C ATOM 3721 CG ARG B 8 -2.399 25.666 -21.627 1.00 58.16 C ATOM 3722 CD ARG B 8 -3.641 25.257 -22.393 1.00 61.15 C ATOM 3723 NE ARG B 8 -4.720 24.882 -21.489 1.00 62.97 N ATOM 3724 CZ ARG B 8 -5.899 24.413 -21.879 1.00 65.83 C ATOM 3725 NH1 ARG B 8 -6.818 24.097 -20.972 1.00 68.10 N ATOM 3726 NH2 ARG B 8 -6.164 24.253 -23.171 1.00 68.88 N ATOM 3727 N ARG B 9 1.133 23.873 -22.033 1.00 55.99 N ATOM 3728 CA ARG B 9 1.442 22.468 -22.296 1.00 53.67 C ATOM 3729 C ARG B 9 0.978 21.610 -21.116 1.00 50.63 C ATOM 3730 O ARG B 9 0.749 22.135 -20.035 1.00 48.47 O ATOM 3731 CB ARG B 9 2.954 22.303 -22.490 1.00 54.87 C ATOM 3732 CG ARG B 9 3.770 22.395 -21.204 1.00 54.79 C ATOM 3733 CD ARG B 9 5.249 22.429 -21.509 1.00 56.38 C ATOM 3734 NE ARG B 9 5.656 21.241 -22.254 1.00 61.20 N ATOM 3735 CZ ARG B 9 6.889 21.019 -22.699 1.00 62.35 C ATOM 3736 NH1 ARG B 9 7.158 19.907 -23.369 1.00 64.98 N ATOM 3737 NH2 ARG B 9 7.857 21.896 -22.474 1.00 63.88 N ATOM 3738 N PRO B 10 0.869 20.282 -21.300 1.00 50.84 N ATOM 3739 CA PRO B 10 0.410 19.472 -20.173 1.00 48.73 C ATOM 3740 C PRO B 10 1.400 19.409 -19.024 1.00 48.22 C ATOM 3741 O PRO B 10 2.626 19.441 -19.229 1.00 47.65 O ATOM 3742 CB PRO B 10 0.208 18.082 -20.789 1.00 51.31 C ATOM 3743 CG PRO B 10 0.072 18.325 -22.251 1.00 52.34 C ATOM 3744 CD PRO B 10 1.010 19.471 -22.518 1.00 51.91 C ATOM 3745 N TYR B 11 0.854 19.339 -17.815 1.00 49.80 N ATOM 3746 CA TYR B 11 1.675 19.209 -16.604 1.00 52.35 C ATOM 3747 C TYR B 11 1.704 17.743 -16.073 1.00 52.90 C ATOM 3748 O TYR B 11 2.683 17.326 -15.444 1.00 51.91 O ATOM 3749 CB TYR B 11 1.230 20.213 -15.532 1.00 47.72 C ATOM 3750 CG TYR B 11 -0.256 20.244 -15.255 1.00 47.28 C ATOM 3751 CD1 TYR B 11 -1.110 21.022 -16.023 1.00 48.46 C ATOM 3752 CD2 TYR B 11 -0.807 19.512 -14.207 1.00 47.80 C ATOM 3753 CE1 TYR B 11 -2.475 21.062 -15.771 1.00 47.20 C ATOM 3754 CE2 TYR B 11 -2.170 19.544 -13.945 1.00 46.37 C ATOM 3755 CZ TYR B 11 -2.999 20.321 -14.731 1.00 48.03 C ATOM 3756 OH TYR B 11 -4.354 20.368 -14.478 1.00 49.47 O ATOM 3757 N ILE B 12 0.652 16.977 -16.371 1.00 52.82 N ATOM 3758 CA ILE B 12 0.538 15.564 -15.983 1.00 52.67 C ATOM 3759 C ILE B 12 1.400 14.637 -16.843 1.00 54.25 C ATOM 3760 O ILE B 12 1.104 14.427 -18.015 1.00 50.94 O ATOM 3761 CB ILE B 12 -0.926 15.099 -16.077 1.00 50.71 C ATOM 3762 CG1 ILE B 12 -1.750 15.802 -15.002 1.00 50.48 C ATOM 3763 CG2 ILE B 12 -1.042 13.590 -15.909 1.00 53.37 C ATOM 3764 CD1 ILE B 12 -3.248 15.694 -15.211 1.00 52.45 C ATOM 3765 N LEU B 13 2.455 14.087 -16.237 1.00 60.34 N ATOM 3766 CA LEU B 13 3.324 13.084 -16.869 1.00 66.85 C ATOM 3767 C LEU B 13 2.842 11.668 -16.507 1.00 73.97 C ATOM 3768 O LEU B 13 2.610 10.811 -17.376 1.00 73.56 O ATOM 3769 CB LEU B 13 4.778 13.271 -16.416 1.00 67.49 C ATOM 3770 CG LEU B 13 5.815 12.187 -16.764 1.00 67.90 C ATOM 3771 CD1 LEU B 13 6.215 12.265 -18.229 1.00 67.20 C ATOM 3772 CD2 LEU B 13 7.053 12.301 -15.880 1.00 67.61 C ATOM 3773 OXT LEU B 13 2.668 11.347 -15.323 1.00 77.22 O TER 3774 LEU B 13 HETATM 3775 C1 CIT A1201 23.668 -41.502 -49.121 1.00 56.73 C HETATM 3776 O1 CIT A1201 24.333 -40.480 -49.430 1.00 56.85 O HETATM 3777 O2 CIT A1201 22.445 -41.480 -48.833 1.00 51.10 O HETATM 3778 C2 CIT A1201 24.371 -42.841 -49.061 1.00 57.73 C HETATM 3779 C3 CIT A1201 25.038 -43.293 -50.366 1.00 57.53 C HETATM 3780 O7 CIT A1201 26.445 -43.299 -50.141 1.00 62.87 O HETATM 3781 C4 CIT A1201 24.672 -44.716 -50.753 1.00 58.03 C HETATM 3782 C5 CIT A1201 25.615 -45.241 -51.812 1.00 55.51 C HETATM 3783 O3 CIT A1201 25.546 -44.785 -52.977 1.00 53.94 O HETATM 3784 O4 CIT A1201 26.429 -46.133 -51.488 1.00 52.29 O HETATM 3785 C6 CIT A1201 24.710 -42.396 -51.538 1.00 56.74 C HETATM 3786 O5 CIT A1201 23.617 -42.562 -52.106 1.00 62.54 O HETATM 3787 O6 CIT A1201 25.530 -41.534 -51.912 1.00 51.40 O HETATM 3788 C1 PEG A1202 19.679 -28.940 -25.566 1.00 60.58 C HETATM 3789 O1 PEG A1202 18.581 -29.748 -26.035 1.00 62.27 O HETATM 3790 C2 PEG A1202 20.604 -28.513 -26.701 1.00 58.79 C HETATM 3791 O2 PEG A1202 20.424 -27.122 -26.996 1.00 59.65 O HETATM 3792 C3 PEG A1202 20.910 -26.725 -28.287 1.00 61.07 C HETATM 3793 C4 PEG A1202 20.126 -25.526 -28.835 1.00 62.87 C HETATM 3794 O4 PEG A1202 19.272 -25.901 -29.935 1.00 63.25 O HETATM 3795 C1 PEG A1203 16.470 -27.244 -31.506 1.00 55.64 C HETATM 3796 O1 PEG A1203 16.192 -26.827 -32.865 1.00 48.27 O HETATM 3797 C2 PEG A1203 16.211 -28.749 -31.275 1.00 56.63 C HETATM 3798 O2 PEG A1203 16.162 -29.125 -29.887 1.00 58.20 O HETATM 3799 C3 PEG A1203 15.461 -30.365 -29.678 1.00 58.57 C HETATM 3800 C4 PEG A1203 15.882 -31.105 -28.402 1.00 60.36 C HETATM 3801 O4 PEG A1203 16.422 -30.217 -27.413 1.00 64.37 O HETATM 3802 C1 PEG A1204 8.608 -33.571 -24.648 1.00 88.82 C HETATM 3803 O1 PEG A1204 8.843 -32.233 -24.233 1.00 88.52 O HETATM 3804 C2 PEG A1204 7.401 -34.114 -23.917 1.00 92.32 C HETATM 3805 O2 PEG A1204 7.766 -35.287 -23.220 1.00 94.24 O HETATM 3806 C3 PEG A1204 7.652 -35.119 -21.815 1.00 95.76 C HETATM 3807 C4 PEG A1204 8.705 -35.939 -21.090 1.00 93.39 C HETATM 3808 O4 PEG A1204 9.169 -35.206 -19.963 1.00 86.97 O HETATM 3809 C1 PEG A1205 0.822 8.091 -1.964 1.00 78.88 C HETATM 3810 O1 PEG A1205 -0.075 9.208 -1.897 1.00 76.29 O HETATM 3811 C2 PEG A1205 2.258 8.500 -1.620 1.00 78.25 C HETATM 3812 O2 PEG A1205 2.724 7.751 -0.487 1.00 78.27 O HETATM 3813 C3 PEG A1205 4.104 7.972 -0.171 1.00 77.64 C HETATM 3814 C4 PEG A1205 4.727 6.710 0.431 1.00 76.81 C HETATM 3815 O4 PEG A1205 5.502 7.026 1.595 1.00 73.38 O HETATM 3816 C1 PEG A1206 32.351 -36.645 -33.798 1.00 72.62 C HETATM 3817 O1 PEG A1206 32.644 -38.044 -33.970 1.00 74.18 O HETATM 3818 C2 PEG A1206 32.260 -35.921 -35.146 1.00 69.50 C HETATM 3819 O2 PEG A1206 32.727 -34.556 -35.043 1.00 66.14 O HETATM 3820 C3 PEG A1206 32.193 -33.665 -36.037 1.00 63.80 C HETATM 3821 C4 PEG A1206 33.221 -33.086 -37.018 1.00 64.18 C HETATM 3822 O4 PEG A1206 32.917 -33.396 -38.395 1.00 64.40 O HETATM 3823 C1 GOL A1207 15.531 -26.193 -56.024 1.00 72.25 C HETATM 3824 O1 GOL A1207 14.339 -26.142 -55.229 1.00 69.16 O HETATM 3825 C2 GOL A1207 15.673 -27.584 -56.630 1.00 74.38 C HETATM 3826 O2 GOL A1207 14.494 -27.907 -57.387 1.00 77.32 O HETATM 3827 C3 GOL A1207 16.921 -27.662 -57.514 1.00 74.79 C HETATM 3828 O3 GOL A1207 16.675 -27.236 -58.865 1.00 73.84 O HETATM 3829 C1 GOL A1208 -9.144 16.239 -29.185 1.00 71.06 C HETATM 3830 O1 GOL A1208 -9.879 17.336 -29.742 1.00 74.67 O HETATM 3831 C2 GOL A1208 -9.655 14.906 -29.736 1.00 68.76 C HETATM 3832 O2 GOL A1208 -8.975 14.602 -30.957 1.00 64.05 O HETATM 3833 C3 GOL A1208 -9.411 13.776 -28.731 1.00 70.73 C HETATM 3834 O3 GOL A1208 -9.001 12.562 -29.383 1.00 73.19 O HETATM 3835 C1 GOL A1209 10.013 -50.730 -39.434 1.00 56.08 C HETATM 3836 O1 GOL A1209 9.836 -51.786 -40.376 1.00 56.32 O HETATM 3837 C2 GOL A1209 9.990 -51.224 -38.004 1.00 60.51 C HETATM 3838 O2 GOL A1209 10.558 -52.533 -37.912 1.00 57.74 O HETATM 3839 C3 GOL A1209 10.752 -50.213 -37.159 1.00 64.19 C HETATM 3840 O3 GOL A1209 10.320 -50.275 -35.796 1.00 68.94 O HETATM 3841 N1 EPE A1210 22.692 -45.525 -30.846 1.00 51.37 N HETATM 3842 C2 EPE A1210 22.431 -44.067 -30.901 1.00 49.80 C HETATM 3843 C3 EPE A1210 21.636 -43.590 -29.692 1.00 48.61 C HETATM 3844 N4 EPE A1210 20.375 -44.357 -29.638 1.00 48.59 N HETATM 3845 C5 EPE A1210 20.703 -45.766 -29.394 1.00 49.25 C HETATM 3846 C6 EPE A1210 21.439 -46.284 -30.620 1.00 48.49 C HETATM 3847 C7 EPE A1210 19.394 -43.839 -28.677 1.00 47.18 C HETATM 3848 C8 EPE A1210 19.871 -43.884 -27.231 1.00 47.93 C HETATM 3849 O8 EPE A1210 19.483 -45.124 -26.645 1.00 48.93 O HETATM 3850 C9 EPE A1210 23.409 -45.922 -32.094 1.00 54.60 C HETATM 3851 C10 EPE A1210 23.102 -47.358 -32.541 1.00 58.11 C HETATM 3852 S EPE A1210 24.120 -47.959 -33.709 1.00 61.49 S HETATM 3853 O1S EPE A1210 24.054 -49.442 -33.617 1.00 62.84 O HETATM 3854 O2S EPE A1210 23.666 -47.561 -35.066 1.00 57.95 O HETATM 3855 O3S EPE A1210 25.516 -47.497 -33.456 1.00 62.65 O HETATM 3856 N1 EPE A1211 -13.838 19.421 -13.677 1.00 96.24 N HETATM 3857 C2 EPE A1211 -13.968 18.762 -12.359 1.00 95.25 C HETATM 3858 C3 EPE A1211 -14.731 17.441 -12.487 1.00 91.50 C HETATM 3859 N4 EPE A1211 -16.066 17.665 -13.076 1.00 89.63 N HETATM 3860 C5 EPE A1211 -15.950 18.343 -14.387 1.00 90.42 C HETATM 3861 C6 EPE A1211 -15.185 19.662 -14.245 1.00 92.76 C HETATM 3862 C7 EPE A1211 -16.788 16.382 -13.196 1.00 85.40 C HETATM 3863 C8 EPE A1211 -18.160 16.465 -12.530 1.00 85.00 C HETATM 3864 O8 EPE A1211 -18.074 17.096 -11.244 1.00 82.72 O HETATM 3865 C9 EPE A1211 -13.051 20.673 -13.568 1.00 97.90 C HETATM 3866 C10 EPE A1211 -11.923 20.702 -14.609 1.00102.64 C HETATM 3867 S EPE A1211 -10.472 20.150 -13.987 1.00113.70 S HETATM 3868 O1S EPE A1211 -9.366 20.329 -14.961 1.00 99.72 O HETATM 3869 O2S EPE A1211 -10.612 18.703 -13.710 1.00121.63 O HETATM 3870 O3S EPE A1211 -10.147 20.840 -12.714 1.00111.49 O HETATM 3871 O HOH A1301 0.558 8.811 -15.413 1.00 52.16 O HETATM 3872 O HOH A1302 1.560 -43.660 -38.434 0.69 17.43 O HETATM 3873 O HOH A1303 -4.664 13.109 -17.399 1.00 45.98 O HETATM 3874 O HOH A1304 3.048 8.112 -16.522 1.00 52.59 O HETATM 3875 O HOH A1305 28.430 -41.756 -33.612 1.00 45.32 O HETATM 3876 O HOH A1306 5.855 20.876 -17.079 1.00 72.82 O HETATM 3877 O HOH A1307 13.959 6.394 -13.478 1.00 71.13 O HETATM 3878 O HOH A1308 8.339 -16.916 -20.329 1.00 61.75 O HETATM 3879 O HOH A1309 -5.477 24.227 -30.971 1.00 46.88 O HETATM 3880 O HOH A1310 -0.603 -42.179 -40.641 1.00 50.09 O HETATM 3881 O HOH A1311 -1.011 -32.930 -44.337 1.00 45.34 O HETATM 3882 O HOH A1312 23.869 -27.584 -21.531 1.00 52.90 O HETATM 3883 O HOH A1313 21.963 -40.420 -31.085 1.00 34.83 O HETATM 3884 O HOH A1314 4.667 -37.390 -42.084 1.00 37.80 O HETATM 3885 O HOH A1315 16.560 -27.466 -46.596 1.00 43.14 O HETATM 3886 O HOH A1316 10.309 20.502 -15.658 1.00 55.65 O HETATM 3887 O HOH A1317 21.041 -18.484 -28.989 1.00 54.95 O HETATM 3888 O HOH A1318 -18.261 12.173 -26.972 1.00 63.11 O HETATM 3889 O HOH A1319 -4.670 -16.884 -11.504 1.00 66.06 O HETATM 3890 O HOH A1320 13.738 -33.217 -55.954 1.00 44.14 O HETATM 3891 O HOH A1321 24.968 -39.658 -31.678 1.00 36.13 O HETATM 3892 O HOH A1322 22.092 -32.018 -54.252 1.00 37.86 O HETATM 3893 O HOH A1323 -3.349 -43.671 -30.995 1.00 43.45 O HETATM 3894 O HOH A1324 -7.265 13.035 -18.683 1.00 57.00 O HETATM 3895 O HOH A1325 4.242 -38.616 -49.439 1.00 41.43 O HETATM 3896 O HOH A1326 5.155 -20.747 -21.280 1.00 54.92 O HETATM 3897 O HOH A1327 11.375 -34.487 -26.345 1.00 48.88 O HETATM 3898 O HOH A1328 6.521 -53.377 -20.995 1.00 56.00 O HETATM 3899 O HOH A1329 0.157 -31.873 -41.411 1.00 50.30 O HETATM 3900 O HOH A1330 7.616 -14.820 -31.902 1.00 73.77 O HETATM 3901 O HOH A1331 9.671 -23.875 -39.083 1.00 54.76 O HETATM 3902 O HOH A1332 -0.829 17.027 -10.989 1.00 54.00 O HETATM 3903 O HOH A1333 0.434 28.445 -29.020 1.00 53.99 O HETATM 3904 O HOH A1334 27.138 -45.137 -31.780 1.00 59.09 O HETATM 3905 O HOH A1335 -5.610 -20.548 -16.361 1.00 71.97 O HETATM 3906 O HOH A1336 7.839 -17.117 -35.337 1.00 60.56 O HETATM 3907 O HOH A1337 3.308 -28.653 -41.082 1.00 51.38 O HETATM 3908 O HOH A1338 13.509 -22.832 -41.676 1.00 50.62 O HETATM 3909 O HOH A1339 20.519 6.006 -7.760 1.00 68.33 O HETATM 3910 O HOH A1340 28.334 -32.293 -26.607 1.00 73.04 O HETATM 3911 O HOH A1341 4.315 -28.830 -36.410 1.00 57.91 O HETATM 3912 O HOH A1342 30.200 -27.531 -35.826 1.00 58.64 O HETATM 3913 O HOH A1343 7.348 -50.289 -31.830 1.00 59.31 O HETATM 3914 O HOH A1344 20.669 -54.908 -46.552 1.00 48.36 O HETATM 3915 O HOH A1345 11.093 -32.351 -55.310 1.00 46.02 O HETATM 3916 O HOH A1346 24.894 -57.489 -45.496 1.00 48.89 O HETATM 3917 O HOH A1347 6.544 -23.072 -21.581 1.00 58.63 O HETATM 3918 O HOH A1348 8.641 -21.512 -37.248 1.00 60.74 O HETATM 3919 O HOH A1349 -17.604 8.848 -26.184 1.00 56.95 O HETATM 3920 O HOH A1350 9.321 19.501 -18.797 1.00 50.21 O HETATM 3921 O HOH A1351 2.883 -26.072 -35.454 1.00 50.14 O HETATM 3922 O HOH A1352 9.850 -15.046 -36.850 1.00 66.06 O HETATM 3923 O HOH A1353 10.192 -20.590 -39.682 1.00 69.97 O HETATM 3924 O HOH B 101 4.267 19.000 -21.258 1.00 51.85 O HETATM 3925 O HOH B 102 -8.502 23.034 -23.545 1.00 42.58 O CONECT 724 1361 CONECT 1361 724 CONECT 3775 3776 3777 3778 CONECT 3776 3775 CONECT 3777 3775 CONECT 3778 3775 3779 CONECT 3779 3778 3780 3781 3785 CONECT 3780 3779 CONECT 3781 3779 3782 CONECT 3782 3781 3783 3784 CONECT 3783 3782 CONECT 3784 3782 CONECT 3785 3779 3786 3787 CONECT 3786 3785 CONECT 3787 3785 CONECT 3788 3789 3790 CONECT 3789 3788 CONECT 3790 3788 3791 CONECT 3791 3790 3792 CONECT 3792 3791 3793 CONECT 3793 3792 3794 CONECT 3794 3793 CONECT 3795 3796 3797 CONECT 3796 3795 CONECT 3797 3795 3798 CONECT 3798 3797 3799 CONECT 3799 3798 3800 CONECT 3800 3799 3801 CONECT 3801 3800 CONECT 3802 3803 3804 CONECT 3803 3802 CONECT 3804 3802 3805 CONECT 3805 3804 3806 CONECT 3806 3805 3807 CONECT 3807 3806 3808 CONECT 3808 3807 CONECT 3809 3810 3811 CONECT 3810 3809 CONECT 3811 3809 3812 CONECT 3812 3811 3813 CONECT 3813 3812 3814 CONECT 3814 3813 3815 CONECT 3815 3814 CONECT 3816 3817 3818 CONECT 3817 3816 CONECT 3818 3816 3819 CONECT 3819 3818 3820 CONECT 3820 3819 3821 CONECT 3821 3820 3822 CONECT 3822 3821 CONECT 3823 3824 3825 CONECT 3824 3823 CONECT 3825 3823 3826 3827 CONECT 3826 3825 CONECT 3827 3825 3828 CONECT 3828 3827 CONECT 3829 3830 3831 CONECT 3830 3829 CONECT 3831 3829 3832 3833 CONECT 3832 3831 CONECT 3833 3831 3834 CONECT 3834 3833 CONECT 3835 3836 3837 CONECT 3836 3835 CONECT 3837 3835 3838 3839 CONECT 3838 3837 CONECT 3839 3837 3840 CONECT 3840 3839 CONECT 3841 3842 3846 3850 CONECT 3842 3841 3843 CONECT 3843 3842 3844 CONECT 3844 3843 3845 3847 CONECT 3845 3844 3846 CONECT 3846 3841 3845 CONECT 3847 3844 3848 CONECT 3848 3847 3849 CONECT 3849 3848 CONECT 3850 3841 3851 CONECT 3851 3850 3852 CONECT 3852 3851 3853 3854 3855 CONECT 3853 3852 CONECT 3854 3852 CONECT 3855 3852 CONECT 3856 3857 3861 3865 CONECT 3857 3856 3858 CONECT 3858 3857 3859 CONECT 3859 3858 3860 3862 CONECT 3860 3859 3861 CONECT 3861 3856 3860 CONECT 3862 3859 3863 CONECT 3863 3862 3864 CONECT 3864 3863 CONECT 3865 3856 3866 CONECT 3866 3865 3867 CONECT 3867 3866 3868 3869 3870 CONECT 3868 3867 CONECT 3869 3867 CONECT 3870 3867 MASTER 653 0 11 25 5 0 17 6 3923 2 98 43 END