HEADER SIGNALING PROTEIN, HYDROLASE 23-DEC-14 4XEE 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 4XEE 1 REMARK REVDAT 2 05-AUG-15 4XEE 1 JRNL REVDAT 1 29-JUL-15 4XEE 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. 2.90 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2 REMARK 3 NUMBER OF REFLECTIONS : 13831 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) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.231 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 769 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 957 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.50 REMARK 3 BIN R VALUE (WORKING SET) : 0.3210 REMARK 3 BIN FREE R VALUE SET COUNT : 59 REMARK 3 BIN FREE R VALUE : 0.3770 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3724 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 67 REMARK 3 SOLVENT ATOMS : 10 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 61.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.92 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.18000 REMARK 3 B22 (A**2) : -3.31000 REMARK 3 B33 (A**2) : 3.12000 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.450 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.406 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.622 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.884 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3866 ; 0.006 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3792 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5237 ; 1.008 ; 1.963 REMARK 3 BOND ANGLES OTHERS (DEGREES): 8654 ; 0.725 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 465 ; 5.194 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;28.885 ;22.342 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 629 ;15.038 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.813 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 609 ; 0.056 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4240 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 932 ; 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): 1874 ; 0.918 ; 3.568 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1873 ; 0.912 ; 3.566 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2334 ; 1.582 ; 5.347 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2335 ; 1.583 ; 5.350 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1991 ; 1.003 ; 3.852 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1989 ; 0.991 ; 3.847 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2902 ; 1.677 ; 5.679 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4578 ; 4.599 ;29.349 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4579 ; 4.600 ;29.362 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 : 9 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 105 REMARK 3 ORIGIN FOR THE GROUP (A): 30.5902 -42.0912 -12.6280 REMARK 3 T TENSOR REMARK 3 T11: 0.6787 T22: 0.3034 REMARK 3 T33: 0.3376 T12: 0.0407 REMARK 3 T13: -0.2561 T23: -0.0180 REMARK 3 L TENSOR REMARK 3 L11: 1.8296 L22: 5.8121 REMARK 3 L33: 1.9114 L12: 1.5199 REMARK 3 L13: -0.8849 L23: 0.3681 REMARK 3 S TENSOR REMARK 3 S11: 0.0842 S12: 0.0780 S13: 0.1253 REMARK 3 S21: 0.7318 S22: 0.2241 S23: -1.0895 REMARK 3 S31: 0.1594 S32: 0.1143 S33: -0.3083 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 106 A 165 REMARK 3 ORIGIN FOR THE GROUP (A): 22.4201 -46.8106 -9.6940 REMARK 3 T TENSOR REMARK 3 T11: 0.9706 T22: 0.1920 REMARK 3 T33: 0.1313 T12: 0.0688 REMARK 3 T13: 0.0647 T23: -0.0233 REMARK 3 L TENSOR REMARK 3 L11: 1.9538 L22: 6.6638 REMARK 3 L33: 0.0490 L12: -0.7888 REMARK 3 L13: 0.2123 L23: 0.2499 REMARK 3 S TENSOR REMARK 3 S11: -0.0721 S12: 0.3668 S13: -0.0978 REMARK 3 S21: 1.4739 S22: 0.0487 S23: -0.0754 REMARK 3 S31: 0.0572 S32: 0.0443 S33: 0.0233 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 166 A 180 REMARK 3 ORIGIN FOR THE GROUP (A): 5.2828 -19.4573 -18.0571 REMARK 3 T TENSOR REMARK 3 T11: 0.5102 T22: 0.5988 REMARK 3 T33: 0.7045 T12: 0.0314 REMARK 3 T13: -0.0905 T23: -0.0446 REMARK 3 L TENSOR REMARK 3 L11: 14.6445 L22: 9.6500 REMARK 3 L33: 14.1993 L12: -6.0703 REMARK 3 L13: -13.9304 L23: 3.2527 REMARK 3 S TENSOR REMARK 3 S11: 0.1236 S12: -0.0290 S13: 0.7517 REMARK 3 S21: -0.2043 S22: 0.4925 S23: -0.2820 REMARK 3 S31: -0.1334 S32: -0.2901 S33: -0.6161 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 181 A 244 REMARK 3 ORIGIN FOR THE GROUP (A): 12.6402 -51.0954 -10.6200 REMARK 3 T TENSOR REMARK 3 T11: 0.7856 T22: 0.2967 REMARK 3 T33: 0.3487 T12: 0.0241 REMARK 3 T13: 0.2132 T23: 0.0539 REMARK 3 L TENSOR REMARK 3 L11: 3.8387 L22: 4.1607 REMARK 3 L33: 1.6148 L12: -0.8235 REMARK 3 L13: 0.7241 L23: 0.2968 REMARK 3 S TENSOR REMARK 3 S11: -0.1331 S12: -0.1019 S13: -0.2893 REMARK 3 S21: 0.2370 S22: 0.2301 S23: 1.0660 REMARK 3 S31: 0.1720 S32: -0.3614 S33: -0.0969 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 245 A 311 REMARK 3 ORIGIN FOR THE GROUP (A): 15.9261 -24.4322 -26.6537 REMARK 3 T TENSOR REMARK 3 T11: 0.4067 T22: 0.2388 REMARK 3 T33: 0.3168 T12: 0.0368 REMARK 3 T13: 0.0251 T23: 0.0668 REMARK 3 L TENSOR REMARK 3 L11: 1.1651 L22: 5.3181 REMARK 3 L33: 4.3660 L12: 2.4453 REMARK 3 L13: -0.8038 L23: -2.2105 REMARK 3 S TENSOR REMARK 3 S11: -0.2246 S12: 0.1552 S13: -0.2551 REMARK 3 S21: -0.2853 S22: 0.3771 S23: -0.3954 REMARK 3 S31: 0.1428 S32: 0.0036 S33: -0.1524 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 312 A 371 REMARK 3 ORIGIN FOR THE GROUP (A): 23.6023 -48.5642 -23.2288 REMARK 3 T TENSOR REMARK 3 T11: 0.4969 T22: 0.2930 REMARK 3 T33: 0.1970 T12: -0.0261 REMARK 3 T13: 0.0275 T23: -0.0462 REMARK 3 L TENSOR REMARK 3 L11: 0.8257 L22: 10.4600 REMARK 3 L33: 0.3516 L12: -2.1476 REMARK 3 L13: -0.3609 L23: 0.1580 REMARK 3 S TENSOR REMARK 3 S11: 0.0620 S12: 0.1817 S13: -0.0458 REMARK 3 S21: 0.2431 S22: -0.0778 S23: -0.1394 REMARK 3 S31: 0.0132 S32: -0.0836 S33: 0.0158 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 372 A 384 REMARK 3 ORIGIN FOR THE GROUP (A): 32.2865 -22.0844 -13.6882 REMARK 3 T TENSOR REMARK 3 T11: 0.7862 T22: 0.8631 REMARK 3 T33: 0.8550 T12: -0.0910 REMARK 3 T13: -0.1269 T23: -0.1212 REMARK 3 L TENSOR REMARK 3 L11: 4.4182 L22: 4.5196 REMARK 3 L33: 3.3174 L12: 1.2498 REMARK 3 L13: -2.4470 L23: -3.5492 REMARK 3 S TENSOR REMARK 3 S11: 0.4697 S12: -0.2441 S13: -0.5928 REMARK 3 S21: -0.6761 S22: -0.4800 S23: 0.2998 REMARK 3 S31: 0.3114 S32: 0.3696 S33: 0.0102 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 1002 A 1033 REMARK 3 ORIGIN FOR THE GROUP (A): 11.7913 4.0058 -27.4235 REMARK 3 T TENSOR REMARK 3 T11: 0.3783 T22: 0.2895 REMARK 3 T33: 0.1504 T12: 0.0095 REMARK 3 T13: 0.0161 T23: -0.0635 REMARK 3 L TENSOR REMARK 3 L11: 7.8423 L22: 3.6513 REMARK 3 L33: 5.5885 L12: -4.2634 REMARK 3 L13: -3.9023 L23: 4.3000 REMARK 3 S TENSOR REMARK 3 S11: 0.0578 S12: -0.5429 S13: 1.0043 REMARK 3 S21: -0.2406 S22: 0.1857 S23: -0.3910 REMARK 3 S31: -0.2356 S32: 0.2146 S33: -0.2435 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 1034 A 1165 REMARK 3 ORIGIN FOR THE GROUP (A): 7.3449 -3.6643 -35.3251 REMARK 3 T TENSOR REMARK 3 T11: 0.1213 T22: 0.0902 REMARK 3 T33: 0.0188 T12: 0.0272 REMARK 3 T13: 0.0252 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 4.6948 L22: 3.7708 REMARK 3 L33: 2.5520 L12: 0.3632 REMARK 3 L13: 1.3371 L23: 1.0282 REMARK 3 S TENSOR REMARK 3 S11: -0.0815 S12: -0.5023 S13: 0.0577 REMARK 3 S21: 0.2593 S22: -0.0799 S23: 0.2301 REMARK 3 S31: 0.1702 S32: -0.1279 S33: 0.1614 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 4XEE 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_1000205517. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUL-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0-8.0 REMARK 200 NUMBER OF CRYSTALS USED : 5 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 REMARK 200 DATA SCALING SOFTWARE : XSCALE 10 JAN 2014 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14628 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 46.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.15300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.71100 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 VERSION 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 (%): 58.72 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16-24% PEG400, 75 MM HEPES, PH 7.0 REMARK 280 -8.0, 1.7 MM TCEP, 32 MM LITHIUM CITRATE, 0.9 MM NEUROTENSIN (8- REMARK 280 13), 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 24.53500 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.64500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 24.53500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.64500 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: 3110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 ALA A 49 REMARK 465 LYS A 93 REMARK 465 SER A 94 REMARK 465 LEU A 95 REMARK 465 GLN A 96 REMARK 465 SER A 97 REMARK 465 LEU A 98 REMARK 465 GLN A 99 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 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 OG REMARK 480 ASP A 60 CG OD1 OD2 REMARK 480 ILE A 61 CG2 CD1 REMARK 480 VAL A 65 CG1 CG2 REMARK 480 LEU A 72 CD1 CD2 REMARK 480 ARG A 91 CZ NH1 NH2 REMARK 480 LYS A 92 CD CE NZ REMARK 480 LEU A 119 CD1 CD2 REMARK 480 PHE A 175 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 MET A 181 CG SD CE REMARK 480 ARG A 183 CG CD NE CZ NH1 NH2 REMARK 480 LYS A 187 CG CD CE NZ REMARK 480 ILE A 202 CD1 REMARK 480 ILE A 238 CD1 REMARK 480 VAL A 240 CG1 CG2 REMARK 480 LEU A 247 CD1 CD2 REMARK 480 ILE A 334 CD1 REMARK 480 SER A 335 CB OG REMARK 480 GLU A 337 CB CG CD OE1 OE2 REMARK 480 LEU A 353 CD1 CD2 REMARK 480 GLN A 378 CG CD OE1 NE2 REMARK 480 LYS A 1016 CD CE NZ REMARK 480 GLU A 1022 CD OE1 OE2 REMARK 480 LEU A 1039 CD1 CD2 REMARK 480 LYS A 1060 CD CE NZ REMARK 480 LYS A 1065 CG CD CE NZ REMARK 480 LYS A 1085 CE NZ 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 ASP A 60 140.07 -39.14 REMARK 500 TYR A 62 -72.17 -54.20 REMARK 500 ARG A 91 49.87 -95.20 REMARK 500 TRP A 130 -71.71 -98.67 REMARK 500 LEU A 180 44.47 -95.95 REMARK 500 ILE A 228 43.37 -103.30 REMARK 500 PHE A 246 -56.87 -128.75 REMARK 500 ASN A 375 10.34 85.96 REMARK 500 ASN A1053 83.54 -69.45 REMARK 500 TYR A1161 49.60 -93.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1205 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XES RELATED DB: PDB DBREF 4XEE A 43 988 UNP P20789 NTR1_RAT 43 396 DBREF 4XEE A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 4XEE B 8 13 UNP P20068 NEUT_RAT 157 162 SEQADV 4XEE ASP A 33 UNP P20789 EXPRESSION TAG SEQADV 4XEE TYR A 34 UNP P20789 EXPRESSION TAG SEQADV 4XEE LYS A 35 UNP P20789 EXPRESSION TAG SEQADV 4XEE ASP A 36 UNP P20789 EXPRESSION TAG SEQADV 4XEE ASP A 37 UNP P20789 EXPRESSION TAG SEQADV 4XEE ASP A 38 UNP P20789 EXPRESSION TAG SEQADV 4XEE ASP A 39 UNP P20789 EXPRESSION TAG SEQADV 4XEE ALA A 40 UNP P20789 EXPRESSION TAG SEQADV 4XEE THR A 41 UNP P20789 EXPRESSION TAG SEQADV 4XEE SER A 42 UNP P20789 EXPRESSION TAG SEQADV 4XEE LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4XEE ALA A 215 UNP P20789 GLY 215 ENGINEERED MUTATION SEQADV 4XEE ALA A 360 UNP P20789 VAL 360 ENGINEERED MUTATION SEQADV 4XEE ALA A 989 UNP P20789 LINKER SEQADV 4XEE HIS A 990 UNP P20789 LINKER SEQADV 4XEE HIS A 991 UNP P20789 LINKER SEQADV 4XEE HIS A 992 UNP P20789 LINKER SEQADV 4XEE HIS A 993 UNP P20789 LINKER SEQADV 4XEE HIS A 994 UNP P20789 LINKER SEQADV 4XEE HIS A 995 UNP P20789 LINKER SEQADV 4XEE HIS A 996 UNP P20789 LINKER SEQADV 4XEE HIS A 997 UNP P20789 LINKER SEQADV 4XEE HIS A 998 UNP P20789 LINKER SEQADV 4XEE HIS A 999 UNP P20789 LINKER SEQADV 4XEE GLY A 1000 UNP P20789 LINKER SEQADV 4XEE GLY A 1001 UNP P20789 LINKER SEQADV 4XEE GLY A 1012 UNP P00720 ARG 12 CONFLICT SEQADV 4XEE THR A 1054 UNP P00720 CYS 54 CONFLICT SEQADV 4XEE ALA A 1097 UNP P00720 CYS 97 CONFLICT SEQADV 4XEE ASN A 1122 UNP P00720 GLN 122 CONFLICT SEQADV 4XEE ASN A 1123 UNP P00720 GLN 123 CONFLICT SEQADV 4XEE ARG A 1137 UNP P00720 ILE 137 CONFLICT SEQADV 4XEE GLY A 1162 UNP P00720 EXPRESSION TAG SEQADV 4XEE SER A 1163 UNP P00720 EXPRESSION TAG SEQADV 4XEE GLY A 1164 UNP P00720 EXPRESSION TAG SEQADV 4XEE 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 GLU 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 1PE A1201 16 HET 1PE A1202 16 HET EPE A1203 15 HET FLC A1204 13 HET PEG A1205 7 HETNAM 1PE PENTAETHYLENE GLYCOL HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM FLC CITRATE ANION HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN 1PE PEG400 HETSYN EPE HEPES FORMUL 3 1PE 2(C10 H22 O6) FORMUL 5 EPE C8 H18 N2 O4 S FORMUL 6 FLC C6 H5 O7 3- FORMUL 7 PEG C4 H10 O3 FORMUL 8 HOH *10(H2 O) HELIX 1 AA1 ASP A 60 ARG A 91 1 32 HELIX 2 AA2 THR A 101 PHE A 128 1 28 HELIX 3 AA3 PHE A 137 HIS A 173 1 37 HELIX 4 AA4 HIS A 173 LEU A 180 1 8 HELIX 5 AA5 SER A 182 ILE A 202 1 21 HELIX 6 AA6 ILE A 202 MET A 208 1 7 HELIX 7 AA7 HIS A 219 GLY A 221 5 3 HELIX 8 AA8 ASP A 230 PHE A 246 1 17 HELIX 9 AA9 PHE A 246 VAL A 268 1 23 HELIX 10 AB1 PRO A 297 ARG A 299 5 3 HELIX 11 AB2 VAL A 300 ILE A 334 1 35 HELIX 12 AB3 THR A 340 ASN A 370 1 31 HELIX 13 AB4 ASN A 375 PHE A 380 1 6 HELIX 14 AB5 ILE A 1003 GLU A 1011 1 9 HELIX 15 AB6 SER A 1038 GLY A 1051 1 14 HELIX 16 AB7 THR A 1059 ARG A 1080 1 22 HELIX 17 AB8 LEU A 1084 LEU A 1091 1 8 HELIX 18 AB9 ASP A 1092 GLY A 1107 1 16 HELIX 19 AC1 GLY A 1107 ALA A 1112 1 6 HELIX 20 AC2 PHE A 1114 ASN A 1123 1 10 HELIX 21 AC3 ARG A 1125 ALA A 1134 1 10 HELIX 22 AC4 SER A 1136 THR A 1142 1 7 HELIX 23 AC5 THR A 1142 GLY A 1156 1 15 SHEET 1 AA1 2 LEU A 210 ASN A 212 0 SHEET 2 AA1 2 LEU A 223 CYS A 225 -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 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 142 CYS A 225 1555 1555 2.04 CISPEP 1 HIS A 133 PRO A 134 0 2.06 SITE 1 AC1 4 THR A 258 LEU A 308 ARG A 311 ILE A 315 SITE 1 AC2 2 HIS A 305 ARG A 377 SITE 1 AC3 6 GLY A1030 LYS A1035 PHE A1104 GLN A1105 SITE 2 AC3 6 MET A1106 ASP A1159 SITE 1 AC4 4 ASP A 56 VAL A 57 TRP A 130 HIS A 132 SITE 1 AC5 2 ARG A1125 ARG B 8 CRYST1 49.070 88.110 161.290 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 0.020379 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011349 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006200 0.00000 ATOM 1 N GLY A 50 34.773 -76.963 -14.712 1.00115.67 N ANISOU 1 N GLY A 50 19703 7852 16393 1791 -1483 -1068 N ATOM 2 CA GLY A 50 34.308 -76.263 -13.476 1.00113.85 C ANISOU 2 CA GLY A 50 19731 7787 15737 1825 -2021 -820 C ATOM 3 C GLY A 50 32.795 -76.133 -13.422 1.00110.18 C ANISOU 3 C GLY A 50 19693 7685 14483 1487 -1828 -792 C ATOM 4 O GLY A 50 32.148 -76.056 -14.467 1.00107.80 O ANISOU 4 O GLY A 50 19344 7666 13946 1203 -1347 -967 O ATOM 5 N PRO A 51 32.217 -76.099 -12.205 1.00110.03 N ANISOU 5 N PRO A 51 20098 7651 14054 1501 -2203 -573 N ATOM 6 CA PRO A 51 30.758 -76.035 -12.078 1.00107.04 C ANISOU 6 CA PRO A 51 20117 7575 12975 1184 -2001 -549 C ATOM 7 C PRO A 51 30.158 -74.648 -12.373 1.00102.94 C ANISOU 7 C PRO A 51 19414 7571 12127 990 -1948 -580 C ATOM 8 O PRO A 51 28.960 -74.554 -12.651 1.00100.00 O ANISOU 8 O PRO A 51 19228 7493 11274 698 -1670 -618 O ATOM 9 CB PRO A 51 30.514 -76.449 -10.621 1.00108.56 C ANISOU 9 CB PRO A 51 20823 7512 12912 1290 -2419 -307 C ATOM 10 CG PRO A 51 31.755 -76.053 -9.899 1.00111.08 C ANISOU 10 CG PRO A 51 20945 7590 13668 1632 -2976 -173 C ATOM 11 CD PRO A 51 32.888 -76.079 -10.890 1.00112.59 C ANISOU 11 CD PRO A 51 20559 7674 14543 1795 -2832 -341 C ATOM 12 N ASN A 52 30.977 -73.594 -12.306 1.00102.72 N ANISOU 12 N ASN A 52 19014 7633 12381 1151 -2218 -561 N ATOM 13 CA ASN A 52 30.552 -72.234 -12.663 1.00 98.98 C ANISOU 13 CA ASN A 52 18320 7612 11674 996 -2159 -594 C ATOM 14 C ASN A 52 31.144 -71.775 -13.991 1.00 98.46 C ANISOU 14 C ASN A 52 17758 7698 11952 958 -1849 -790 C ATOM 15 O ASN A 52 30.844 -70.677 -14.447 1.00 96.59 O ANISOU 15 O ASN A 52 17323 7821 11555 825 -1763 -824 O ATOM 16 CB ASN A 52 30.995 -71.221 -11.600 1.00 98.96 C ANISOU 16 CB ASN A 52 18287 7623 11688 1169 -2676 -435 C ATOM 17 CG ASN A 52 30.826 -71.730 -10.184 1.00100.96 C ANISOU 17 CG ASN A 52 19033 7604 11720 1273 -3072 -233 C ATOM 18 OD1 ASN A 52 29.794 -72.301 -9.832 1.00100.41 O ANISOU 18 OD1 ASN A 52 19402 7541 11205 1104 -2925 -183 O ATOM 19 ND2 ASN A 52 31.844 -71.513 -9.357 1.00103.61 N ANISOU 19 ND2 ASN A 52 19310 7692 12365 1537 -3585 -115 N ATOM 20 N SER A 53 31.976 -72.613 -14.607 1.00101.54 N ANISOU 20 N SER A 53 17969 7794 12817 1068 -1661 -917 N ATOM 21 CA SER A 53 32.846 -72.202 -15.718 1.00101.79 C ANISOU 21 CA SER A 53 17519 7861 13295 1087 -1403 -1104 C ATOM 22 C SER A 53 32.136 -71.515 -16.886 1.00 98.32 C ANISOU 22 C SER A 53 16977 7852 12525 768 -985 -1239 C ATOM 23 O SER A 53 32.769 -70.772 -17.634 1.00 97.84 O ANISOU 23 O SER A 53 16546 7898 12729 765 -847 -1350 O ATOM 24 CB SER A 53 33.623 -73.407 -16.243 1.00105.84 C ANISOU 24 CB SER A 53 17936 7965 14311 1202 -1151 -1244 C ATOM 25 OG SER A 53 32.737 -74.417 -16.691 0.00106.35 O ANISOU 25 OG SER A 53 18345 8019 14042 975 -776 -1320 O ATOM 26 N ASP A 54 30.839 -71.776 -17.047 1.00 95.93 N ANISOU 26 N ASP A 54 17003 7780 11665 495 -792 -1226 N ATOM 27 CA ASP A 54 30.050 -71.147 -18.110 1.00 93.01 C ANISOU 27 CA ASP A 54 16571 7825 10942 180 -462 -1321 C ATOM 28 C ASP A 54 29.603 -69.730 -17.789 1.00 89.93 C ANISOU 28 C ASP A 54 16083 7795 10291 143 -687 -1197 C ATOM 29 O ASP A 54 29.396 -68.928 -18.699 1.00 88.98 O ANISOU 29 O ASP A 54 15777 7972 10058 -27 -489 -1263 O ATOM 30 CB ASP A 54 28.824 -71.994 -18.430 1.00 92.22 C ANISOU 30 CB ASP A 54 16824 7826 10389 -107 -190 -1360 C ATOM 31 CG ASP A 54 29.180 -73.283 -19.121 1.00 94.77 C ANISOU 31 CG ASP A 54 17223 7854 10928 -155 163 -1537 C ATOM 32 OD1 ASP A 54 30.382 -73.525 -19.371 1.00 96.90 O ANISOU 32 OD1 ASP A 54 17256 7832 11729 44 221 -1632 O ATOM 33 OD2 ASP A 54 28.249 -74.053 -19.415 1.00 94.74 O ANISOU 33 OD2 ASP A 54 17509 7902 10586 -402 398 -1591 O ATOM 34 N LEU A 55 29.442 -69.421 -16.505 1.00 89.57 N ANISOU 34 N LEU A 55 16190 7706 10136 292 -1089 -1015 N ATOM 35 CA LEU A 55 29.089 -68.065 -16.090 1.00 86.71 C ANISOU 35 CA LEU A 55 15744 7635 9566 279 -1304 -902 C ATOM 36 C LEU A 55 30.258 -67.105 -16.268 1.00 87.59 C ANISOU 36 C LEU A 55 15451 7730 10096 453 -1444 -933 C ATOM 37 O LEU A 55 30.068 -65.889 -16.195 1.00 87.16 O ANISOU 37 O LEU A 55 15267 7929 9918 421 -1546 -875 O ATOM 38 CB LEU A 55 28.607 -68.041 -14.641 1.00 86.03 C ANISOU 38 CB LEU A 55 15986 7472 9227 365 -1659 -720 C ATOM 39 CG LEU A 55 27.351 -68.863 -14.342 1.00 85.75 C ANISOU 39 CG LEU A 55 16364 7463 8754 172 -1512 -680 C ATOM 40 CD1 LEU A 55 27.090 -68.872 -12.841 1.00 86.47 C ANISOU 40 CD1 LEU A 55 16809 7400 8643 277 -1857 -508 C ATOM 41 CD2 LEU A 55 26.132 -68.350 -15.103 1.00 82.74 C ANISOU 41 CD2 LEU A 55 15949 7489 7999 -126 -1224 -717 C ATOM 42 N ASP A 56 31.457 -67.644 -16.498 1.00 90.09 N ANISOU 42 N ASP A 56 15556 7735 10936 635 -1434 -1031 N ATOM 43 CA ASP A 56 32.619 -66.823 -16.838 1.00 90.85 C ANISOU 43 CA ASP A 56 15219 7797 11502 773 -1488 -1101 C ATOM 44 C ASP A 56 32.291 -65.878 -17.991 1.00 87.06 C ANISOU 44 C ASP A 56 14551 7670 10856 545 -1156 -1191 C ATOM 45 O ASP A 56 31.758 -66.290 -19.019 1.00 86.08 O ANISOU 45 O ASP A 56 14505 7670 10530 316 -758 -1299 O ATOM 46 CB ASP A 56 33.825 -67.686 -17.234 1.00 96.01 C ANISOU 46 CB ASP A 56 15640 8069 12770 944 -1369 -1242 C ATOM 47 CG ASP A 56 34.362 -68.528 -16.085 1.00100.33 C ANISOU 47 CG ASP A 56 16313 8221 13587 1218 -1771 -1131 C ATOM 48 OD1 ASP A 56 33.664 -68.660 -15.055 1.00100.91 O ANISOU 48 OD1 ASP A 56 16753 8309 13279 1228 -2070 -958 O ATOM 49 OD2 ASP A 56 35.483 -69.070 -16.221 1.00104.39 O ANISOU 49 OD2 ASP A 56 16566 8391 14706 1421 -1777 -1215 O ATOM 50 N VAL A 57 32.596 -64.605 -17.793 1.00 84.38 N ANISOU 50 N VAL A 57 13995 7484 10581 599 -1340 -1138 N ATOM 51 CA VAL A 57 32.504 -63.618 -18.843 1.00 81.89 C ANISOU 51 CA VAL A 57 13475 7449 10188 424 -1066 -1208 C ATOM 52 C VAL A 57 33.906 -63.429 -19.391 1.00 83.83 C ANISOU 52 C VAL A 57 13326 7492 11034 545 -947 -1359 C ATOM 53 O VAL A 57 34.843 -63.220 -18.622 1.00 84.86 O ANISOU 53 O VAL A 57 13254 7407 11580 786 -1272 -1333 O ATOM 54 CB VAL A 57 31.952 -62.297 -18.290 1.00 79.02 C ANISOU 54 CB VAL A 57 13121 7359 9541 404 -1307 -1058 C ATOM 55 CG1 VAL A 57 32.128 -61.164 -19.291 1.00 77.85 C ANISOU 55 CG1 VAL A 57 12719 7437 9421 278 -1080 -1115 C ATOM 56 CG2 VAL A 57 30.490 -62.472 -17.904 1.00 76.95 C ANISOU 56 CG2 VAL A 57 13216 7305 8716 251 -1331 -934 C ATOM 57 N ASN A 58 34.047 -63.529 -20.713 1.00 84.67 N ANISOU 57 N ASN A 58 13333 7650 11186 363 -481 -1524 N ATOM 58 CA ASN A 58 35.344 -63.371 -21.377 1.00 87.47 C ANISOU 58 CA ASN A 58 13314 7801 12117 435 -257 -1702 C ATOM 59 C ASN A 58 35.514 -61.978 -21.994 1.00 86.59 C ANISOU 59 C ASN A 58 12996 7925 11976 321 -136 -1717 C ATOM 60 O ASN A 58 34.956 -61.681 -23.055 1.00 85.30 O ANISOU 60 O ASN A 58 12942 7992 11476 57 211 -1763 O ATOM 61 CB ASN A 58 35.534 -64.448 -22.449 1.00 89.66 C ANISOU 61 CB ASN A 58 13640 7910 12513 301 242 -1906 C ATOM 62 CG ASN A 58 36.935 -64.447 -23.036 1.00 93.03 C ANISOU 62 CG ASN A 58 13675 8050 13619 398 510 -2110 C ATOM 63 OD1 ASN A 58 37.731 -63.543 -22.771 1.00 93.55 O ANISOU 63 OD1 ASN A 58 13411 8084 14048 533 344 -2105 O ATOM 64 ND2 ASN A 58 37.245 -65.464 -23.833 1.00 95.44 N ANISOU 64 ND2 ASN A 58 14010 8130 14123 319 948 -2306 N ATOM 65 N THR A 59 36.291 -61.136 -21.314 1.00 87.49 N ANISOU 65 N THR A 59 12832 7969 12440 514 -444 -1673 N ATOM 66 CA THR A 59 36.581 -59.780 -21.770 1.00 86.78 C ANISOU 66 CA THR A 59 12526 8053 12392 435 -357 -1686 C ATOM 67 C THR A 59 38.061 -59.458 -21.587 1.00 90.39 C ANISOU 67 C THR A 59 12538 8233 13573 631 -428 -1804 C ATOM 68 O THR A 59 38.645 -59.790 -20.555 1.00 91.23 O ANISOU 68 O THR A 59 12521 8109 14033 879 -830 -1761 O ATOM 69 CB THR A 59 35.751 -58.731 -21.000 1.00 83.36 C ANISOU 69 CB THR A 59 12233 7899 11539 429 -708 -1477 C ATOM 70 OG1 THR A 59 35.801 -59.006 -19.594 1.00 82.48 O ANISOU 70 OG1 THR A 59 12194 7650 11494 649 -1200 -1359 O ATOM 71 CG2 THR A 59 34.304 -58.748 -21.462 1.00 80.96 C ANISOU 71 CG2 THR A 59 12274 7911 10573 191 -556 -1378 C ATOM 72 N ASP A 60 38.659 -58.815 -22.593 1.00 92.90 N ANISOU 72 N ASP A 60 12621 8563 14110 507 -44 -1949 N ATOM 73 CA ASP A 60 40.035 -58.307 -22.510 1.00 96.78 C ANISOU 73 CA ASP A 60 12646 8822 15303 654 -68 -2074 C ATOM 74 C ASP A 60 40.304 -57.727 -21.130 1.00 96.01 C ANISOU 74 C ASP A 60 12424 8694 15359 879 -690 -1928 C ATOM 75 O ASP A 60 39.443 -57.045 -20.569 1.00 94.17 O ANISOU 75 O ASP A 60 12428 8718 14634 837 -957 -1750 O ATOM 76 CB ASP A 60 40.259 -57.155 -23.504 1.00 97.78 C ANISOU 76 CB ASP A 60 12641 9099 15409 451 308 -2157 C ATOM 77 CG ASP A 60 40.452 -57.605 -24.940 0.00100.94 C ANISOU 77 CG ASP A 60 13076 9434 15842 227 968 -2360 C ATOM 78 OD1 ASP A 60 40.158 -58.777 -25.265 0.00103.86 O ANISOU 78 OD1 ASP A 60 13640 9708 16112 183 1164 -2426 O ATOM 79 OD2 ASP A 60 40.897 -56.754 -25.750 0.00101.79 O ANISOU 79 OD2 ASP A 60 13042 9575 16056 77 1307 -2459 O ATOM 80 N ILE A 61 41.494 -57.969 -20.590 1.00 98.47 N ANISOU 80 N ILE A 61 12364 8685 16363 1108 -920 -2007 N ATOM 81 CA ILE A 61 41.939 -57.229 -19.405 1.00 98.15 C ANISOU 81 CA ILE A 61 12160 8608 16523 1283 -1497 -1901 C ATOM 82 C ILE A 61 42.238 -55.763 -19.763 1.00 97.04 C ANISOU 82 C ILE A 61 11805 8629 16435 1164 -1380 -1943 C ATOM 83 O ILE A 61 42.033 -54.871 -18.937 1.00 95.81 O ANISOU 83 O ILE A 61 11706 8602 16096 1194 -1770 -1815 O ATOM 84 CB ILE A 61 43.154 -57.890 -18.708 1.00102.10 C ANISOU 84 CB ILE A 61 12300 8710 17781 1562 -1845 -1959 C ATOM 85 CG1 ILE A 61 43.341 -57.299 -17.305 1.00101.99 C ANISOU 85 CG1 ILE A 61 12278 8683 17788 1719 -2551 -1801 C ATOM 86 CG2 ILE A 61 44.427 -57.747 -19.538 0.00105.62 C ANISOU 86 CG2 ILE A 61 12207 8924 18999 1576 -1476 -2203 C ATOM 87 CD1 ILE A 61 44.346 -58.049 -16.462 0.00106.52 C ANISOU 87 CD1 ILE A 61 12592 8878 19002 1999 -3025 -1796 C ATOM 88 N TYR A 62 42.701 -55.496 -20.961 1.00 97.49 N ANISOU 88 N TYR A 62 11653 8663 16724 1014 -821 -2125 N ATOM 89 CA TYR A 62 42.824 -54.119 -21.308 1.00 96.22 C ANISOU 89 CA TYR A 62 11352 8658 16549 863 -624 -2162 C ATOM 90 C TYR A 62 41.431 -53.615 -21.038 1.00 92.15 C ANISOU 90 C TYR A 62 11254 8513 15246 723 -725 -1955 C ATOM 91 O TYR A 62 41.168 -52.939 -20.048 1.00 90.90 O ANISOU 91 O TYR A 62 11069 8467 15002 741 -1012 -1859 O ATOM 92 CB TYR A 62 43.165 -53.971 -22.770 1.00 97.62 C ANISOU 92 CB TYR A 62 11397 8776 16916 665 75 -2372 C ATOM 93 CG TYR A 62 44.503 -54.549 -23.138 1.00102.31 C ANISOU 93 CG TYR A 62 11522 8983 18368 780 289 -2612 C ATOM 94 CD1 TYR A 62 45.606 -54.367 -22.323 1.00104.75 C ANISOU 94 CD1 TYR A 62 11352 9127 19318 821 311 -2747 C ATOM 95 CD2 TYR A 62 44.671 -55.269 -24.300 1.00104.22 C ANISOU 95 CD2 TYR A 62 11783 9003 18812 840 499 -2716 C ATOM 96 CE1 TYR A 62 46.838 -54.889 -22.657 1.00109.23 C ANISOU 96 CE1 TYR A 62 11442 9323 20736 929 527 -2977 C ATOM 97 CE2 TYR A 62 45.897 -55.796 -24.643 1.00108.60 C ANISOU 97 CE2 TYR A 62 11881 9175 20207 957 724 -2942 C ATOM 98 CZ TYR A 62 46.974 -55.602 -23.816 1.00111.32 C ANISOU 98 CZ TYR A 62 11724 9364 21209 1004 736 -3071 C ATOM 99 OH TYR A 62 48.189 -56.129 -24.154 1.00116.38 O ANISOU 99 OH TYR A 62 11865 9608 22746 1124 973 -3303 O ATOM 100 N SER A 63 40.512 -54.005 -21.903 1.00 90.06 N ANISOU 100 N SER A 63 11362 8419 14436 582 -490 -1894 N ATOM 101 CA SER A 63 39.143 -53.483 -21.843 1.00 85.70 C ANISOU 101 CA SER A 63 11196 8207 13157 449 -560 -1697 C ATOM 102 C SER A 63 38.670 -53.188 -20.419 1.00 83.70 C ANISOU 102 C SER A 63 11080 8016 12704 599 -1125 -1515 C ATOM 103 O SER A 63 38.145 -52.109 -20.158 1.00 82.37 O ANISOU 103 O SER A 63 11003 8046 12245 543 -1238 -1396 O ATOM 104 CB SER A 63 38.171 -54.467 -22.504 1.00 84.28 C ANISOU 104 CB SER A 63 11360 8143 12520 304 -300 -1675 C ATOM 105 OG SER A 63 38.555 -54.741 -23.839 1.00 85.82 O ANISOU 105 OG SER A 63 11498 8278 12831 129 242 -1849 O ATOM 106 N LYS A 64 38.855 -54.137 -19.505 1.00 84.24 N ANISOU 106 N LYS A 64 11187 7897 12923 782 -1465 -1494 N ATOM 107 CA LYS A 64 38.436 -53.945 -18.112 1.00 82.95 C ANISOU 107 CA LYS A 64 11216 7757 12541 906 -1995 -1329 C ATOM 108 C LYS A 64 39.204 -52.821 -17.414 1.00 83.60 C ANISOU 108 C LYS A 64 11056 7780 12928 990 -2311 -1332 C ATOM 109 O LYS A 64 38.651 -52.136 -16.556 1.00 81.72 O ANISOU 109 O LYS A 64 11018 7660 12368 993 -2607 -1200 O ATOM 110 CB LYS A 64 38.562 -55.245 -17.310 1.00 84.66 C ANISOU 110 CB LYS A 64 11553 7744 12866 1077 -2295 -1301 C ATOM 111 CG LYS A 64 37.400 -56.204 -17.516 1.00 83.11 C ANISOU 111 CG LYS A 64 11748 7660 12167 983 -2130 -1229 C ATOM 112 CD LYS A 64 37.482 -57.414 -16.598 1.00 84.73 C ANISOU 112 CD LYS A 64 12125 7624 12444 1154 -2455 -1176 C ATOM 113 CE LYS A 64 38.581 -58.375 -17.026 1.00 88.49 C ANISOU 113 CE LYS A 64 12311 7779 13532 1281 -2338 -1330 C ATOM 114 NZ LYS A 64 38.444 -59.712 -16.381 1.00 90.21 N ANISOU 114 NZ LYS A 64 12762 7773 13740 1414 -2548 -1268 N ATOM 115 N VAL A 65 40.469 -52.634 -17.784 1.00 86.32 N ANISOU 115 N VAL A 65 10969 7927 13900 1045 -2228 -1495 N ATOM 116 CA VAL A 65 41.290 -51.571 -17.201 1.00 87.65 C ANISOU 116 CA VAL A 65 10861 8024 14416 1103 -2512 -1525 C ATOM 117 C VAL A 65 40.939 -50.212 -17.801 1.00 85.41 C ANISOU 117 C VAL A 65 10580 7971 13897 922 -2229 -1514 C ATOM 118 O VAL A 65 40.943 -49.205 -17.090 1.00 84.66 O ANISOU 118 O VAL A 65 10495 7931 13740 926 -2503 -1453 O ATOM 119 CB VAL A 65 42.795 -51.847 -17.385 1.00 92.00 C ANISOU 119 CB VAL A 65 10897 8263 15793 1222 -2517 -1716 C ATOM 120 CG1 VAL A 65 43.632 -50.662 -16.911 0.00 93.34 C ANISOU 120 CG1 VAL A 65 10755 8378 16332 1239 -2768 -1767 C ATOM 121 CG2 VAL A 65 43.193 -53.111 -16.636 0.00 94.65 C ANISOU 121 CG2 VAL A 65 11216 8336 16410 1437 -2893 -1696 C ATOM 122 N LEU A 66 40.650 -50.185 -19.102 1.00 84.29 N ANISOU 122 N LEU A 66 10454 7949 13623 755 -1688 -1570 N ATOM 123 CA LEU A 66 40.186 -48.964 -19.768 1.00 82.24 C ANISOU 123 CA LEU A 66 10260 7910 13076 575 -1406 -1524 C ATOM 124 C LEU A 66 38.890 -48.467 -19.126 1.00 78.98 C ANISOU 124 C LEU A 66 10225 7740 12042 546 -1625 -1310 C ATOM 125 O LEU A 66 38.835 -47.354 -18.598 1.00 79.18 O ANISOU 125 O LEU A 66 10247 7826 12012 542 -1796 -1249 O ATOM 126 CB LEU A 66 39.972 -49.205 -21.270 1.00 82.18 C ANISOU 126 CB LEU A 66 10302 7983 12939 384 -821 -1596 C ATOM 127 CG LEU A 66 39.335 -48.085 -22.114 1.00 80.57 C ANISOU 127 CG LEU A 66 10245 8014 12352 180 -514 -1511 C ATOM 128 CD1 LEU A 66 40.187 -46.824 -22.124 1.00 81.38 C ANISOU 128 CD1 LEU A 66 10067 8040 12812 159 -474 -1581 C ATOM 129 CD2 LEU A 66 39.079 -48.564 -23.539 1.00 81.03 C ANISOU 129 CD2 LEU A 66 10433 8134 12219 -20 4 -1572 C ATOM 130 N VAL A 67 37.855 -49.301 -19.160 1.00 76.72 N ANISOU 130 N VAL A 67 10256 7576 11317 520 -1601 -1210 N ATOM 131 CA VAL A 67 36.541 -48.914 -18.648 1.00 73.37 C ANISOU 131 CA VAL A 67 10174 7375 10328 478 -1739 -1018 C ATOM 132 C VAL A 67 36.610 -48.481 -17.180 1.00 73.38 C ANISOU 132 C VAL A 67 10243 7301 10336 609 -2215 -952 C ATOM 133 O VAL A 67 35.907 -47.565 -16.764 1.00 71.31 O ANISOU 133 O VAL A 67 10139 7178 9774 567 -2286 -838 O ATOM 134 CB VAL A 67 35.498 -50.042 -18.842 1.00 72.14 C ANISOU 134 CB VAL A 67 10316 7323 9768 430 -1655 -946 C ATOM 135 CG1 VAL A 67 35.751 -51.212 -17.896 1.00 73.68 C ANISOU 135 CG1 VAL A 67 10590 7320 10084 589 -1968 -964 C ATOM 136 CG2 VAL A 67 34.086 -49.509 -18.666 1.00 69.32 C ANISOU 136 CG2 VAL A 67 10246 7223 8868 342 -1667 -764 C ATOM 137 N THR A 68 37.469 -49.128 -16.403 1.00 75.64 N ANISOU 137 N THR A 68 10418 7349 10969 761 -2542 -1022 N ATOM 138 CA THR A 68 37.635 -48.763 -15.008 1.00 76.45 C ANISOU 138 CA THR A 68 10619 7355 11071 863 -3027 -968 C ATOM 139 C THR A 68 38.209 -47.351 -14.915 1.00 77.58 C ANISOU 139 C THR A 68 10550 7502 11425 824 -3066 -1014 C ATOM 140 O THR A 68 37.642 -46.492 -14.235 1.00 77.47 O ANISOU 140 O THR A 68 10739 7578 11117 788 -3206 -923 O ATOM 141 CB THR A 68 38.526 -49.780 -14.268 1.00 79.05 C ANISOU 141 CB THR A 68 10859 7407 11768 1034 -3409 -1022 C ATOM 142 OG1 THR A 68 37.861 -51.045 -14.238 1.00 78.41 O ANISOU 142 OG1 THR A 68 11046 7319 11427 1063 -3380 -960 O ATOM 143 CG2 THR A 68 38.804 -49.338 -12.840 1.00 80.08 C ANISOU 143 CG2 THR A 68 11110 7423 11893 1114 -3953 -968 C ATOM 144 N ALA A 69 39.317 -47.106 -15.611 1.00 79.50 N ANISOU 144 N ALA A 69 10390 7632 12185 820 -2903 -1164 N ATOM 145 CA ALA A 69 39.930 -45.780 -15.619 1.00 80.13 C ANISOU 145 CA ALA A 69 10241 7696 12506 764 -2894 -1228 C ATOM 146 C ALA A 69 38.902 -44.725 -16.029 1.00 77.80 C ANISOU 146 C ALA A 69 10160 7643 11757 625 -2620 -1112 C ATOM 147 O ALA A 69 38.740 -43.710 -15.353 1.00 77.20 O ANISOU 147 O ALA A 69 10170 7594 11569 604 -2788 -1065 O ATOM 148 CB ALA A 69 41.130 -45.752 -16.548 1.00 82.38 C ANISOU 148 CB ALA A 69 10073 7837 13389 745 -2621 -1414 C ATOM 149 N ILE A 70 38.196 -44.982 -17.126 1.00 76.86 N ANISOU 149 N ILE A 70 10138 7687 11378 526 -2211 -1063 N ATOM 150 CA ILE A 70 37.095 -44.119 -17.556 1.00 75.12 C ANISOU 150 CA ILE A 70 10131 7695 10714 409 -1983 -919 C ATOM 151 C ILE A 70 36.086 -43.944 -16.422 1.00 74.38 C ANISOU 151 C ILE A 70 10362 7682 10215 454 -2269 -774 C ATOM 152 O ILE A 70 35.821 -42.826 -15.986 1.00 74.39 O ANISOU 152 O ILE A 70 10426 7721 10115 428 -2321 -717 O ATOM 153 CB ILE A 70 36.370 -44.694 -18.795 1.00 73.42 C ANISOU 153 CB ILE A 70 10028 7642 10224 296 -1598 -868 C ATOM 154 CG1 ILE A 70 37.247 -44.542 -20.038 1.00 75.14 C ANISOU 154 CG1 ILE A 70 9991 7793 10763 196 -1215 -1004 C ATOM 155 CG2 ILE A 70 35.029 -44.004 -19.019 1.00 70.71 C ANISOU 155 CG2 ILE A 70 9939 7536 9389 207 -1484 -677 C ATOM 156 CD1 ILE A 70 36.861 -45.465 -21.173 1.00 75.38 C ANISOU 156 CD1 ILE A 70 10126 7904 10609 87 -879 -1017 C ATOM 157 N TYR A 71 35.534 -45.059 -15.953 1.00 74.67 N ANISOU 157 N TYR A 71 10614 7724 10031 511 -2419 -725 N ATOM 158 CA TYR A 71 34.498 -45.039 -14.928 1.00 73.84 C ANISOU 158 CA TYR A 71 10853 7683 9519 532 -2623 -598 C ATOM 159 C TYR A 71 34.865 -44.101 -13.796 1.00 74.80 C ANISOU 159 C TYR A 71 11013 7694 9710 568 -2922 -612 C ATOM 160 O TYR A 71 34.084 -43.214 -13.455 1.00 74.80 O ANISOU 160 O TYR A 71 11186 7786 9446 519 -2872 -523 O ATOM 161 CB TYR A 71 34.253 -46.448 -14.381 1.00 75.14 C ANISOU 161 CB TYR A 71 11216 7776 9556 603 -2811 -585 C ATOM 162 CG TYR A 71 33.201 -47.246 -15.123 1.00 74.13 C ANISOU 162 CG TYR A 71 11242 7815 9106 528 -2541 -511 C ATOM 163 CD1 TYR A 71 33.010 -47.105 -16.498 1.00 73.80 C ANISOU 163 CD1 TYR A 71 11064 7922 9052 417 -2168 -513 C ATOM 164 CD2 TYR A 71 32.402 -48.160 -14.446 1.00 74.41 C ANISOU 164 CD2 TYR A 71 11582 7849 8838 548 -2666 -441 C ATOM 165 CE1 TYR A 71 32.042 -47.836 -17.166 1.00 72.93 C ANISOU 165 CE1 TYR A 71 11106 7968 8636 326 -1960 -449 C ATOM 166 CE2 TYR A 71 31.439 -48.903 -15.109 1.00 74.02 C ANISOU 166 CE2 TYR A 71 11660 7950 8513 462 -2430 -386 C ATOM 167 CZ TYR A 71 31.265 -48.740 -16.469 1.00 73.27 C ANISOU 167 CZ TYR A 71 11412 8012 8413 350 -2094 -391 C ATOM 168 OH TYR A 71 30.305 -49.481 -17.127 1.00 73.46 O ANISOU 168 OH TYR A 71 11571 8186 8151 242 -1894 -340 O ATOM 169 N LEU A 72 36.057 -44.284 -13.233 1.00 77.06 N ANISOU 169 N LEU A 72 11132 7774 10373 648 -3230 -728 N ATOM 170 CA LEU A 72 36.524 -43.451 -12.113 1.00 78.66 C ANISOU 170 CA LEU A 72 11383 7852 10653 662 -3571 -760 C ATOM 171 C LEU A 72 36.749 -41.985 -12.506 1.00 78.66 C ANISOU 171 C LEU A 72 11206 7895 10782 575 -3376 -794 C ATOM 172 O LEU A 72 36.589 -41.088 -11.671 1.00 79.04 O ANISOU 172 O LEU A 72 11414 7911 10706 541 -3528 -779 O ATOM 173 CB LEU A 72 37.794 -44.037 -11.472 1.00 82.04 C ANISOU 173 CB LEU A 72 11635 8039 11494 764 -3997 -870 C ATOM 174 CG LEU A 72 37.599 -44.899 -10.214 1.00 83.52 C ANISOU 174 CG LEU A 72 12170 8104 11460 841 -4439 -807 C ATOM 175 CD1 LEU A 72 36.476 -45.914 -10.384 0.00 81.68 C ANISOU 175 CD1 LEU A 72 12236 7979 10820 846 -4260 -697 C ATOM 176 CD2 LEU A 72 38.896 -45.601 -9.826 0.00 87.25 C ANISOU 176 CD2 LEU A 72 12403 8333 12413 961 -4852 -896 C ATOM 177 N ALA A 73 37.119 -41.745 -13.765 1.00 78.52 N ANISOU 177 N ALA A 73 10895 7935 11002 527 -3022 -842 N ATOM 178 CA ALA A 73 37.244 -40.382 -14.287 1.00 77.65 C ANISOU 178 CA ALA A 73 10649 7867 10985 433 -2775 -854 C ATOM 179 C ALA A 73 35.884 -39.697 -14.298 1.00 75.31 C ANISOU 179 C ALA A 73 10641 7744 10227 379 -2587 -686 C ATOM 180 O ALA A 73 35.748 -38.557 -13.844 1.00 76.41 O ANISOU 180 O ALA A 73 10847 7861 10323 341 -2601 -668 O ATOM 181 CB ALA A 73 37.849 -40.385 -15.683 1.00 77.75 C ANISOU 181 CB ALA A 73 10353 7894 11294 373 -2400 -930 C ATOM 182 N LEU A 74 34.874 -40.396 -14.802 1.00 72.76 N ANISOU 182 N LEU A 74 10479 7580 9586 374 -2415 -569 N ATOM 183 CA LEU A 74 33.517 -39.864 -14.777 1.00 70.74 C ANISOU 183 CA LEU A 74 10463 7479 8933 337 -2263 -403 C ATOM 184 C LEU A 74 33.088 -39.632 -13.331 1.00 70.91 C ANISOU 184 C LEU A 74 10757 7422 8760 374 -2531 -384 C ATOM 185 O LEU A 74 32.499 -38.603 -13.010 1.00 70.48 O ANISOU 185 O LEU A 74 10818 7386 8572 343 -2446 -319 O ATOM 186 CB LEU A 74 32.535 -40.805 -15.483 1.00 68.60 C ANISOU 186 CB LEU A 74 10302 7381 8379 316 -2090 -296 C ATOM 187 CG LEU A 74 32.809 -41.138 -16.958 1.00 68.36 C ANISOU 187 CG LEU A 74 10088 7435 8448 244 -1800 -310 C ATOM 188 CD1 LEU A 74 31.619 -41.848 -17.585 1.00 66.17 C ANISOU 188 CD1 LEU A 74 9969 7350 7819 191 -1648 -182 C ATOM 189 CD2 LEU A 74 33.159 -39.889 -17.753 1.00 68.94 C ANISOU 189 CD2 LEU A 74 10003 7519 8670 170 -1563 -296 C ATOM 190 N PHE A 75 33.428 -40.579 -12.463 1.00 72.01 N ANISOU 190 N PHE A 75 11015 7449 8894 434 -2847 -446 N ATOM 191 CA PHE A 75 33.007 -40.554 -11.060 1.00 72.86 C ANISOU 191 CA PHE A 75 11463 7465 8754 446 -3108 -430 C ATOM 192 C PHE A 75 33.450 -39.318 -10.279 1.00 75.30 C ANISOU 192 C PHE A 75 11810 7649 9149 406 -3242 -494 C ATOM 193 O PHE A 75 32.639 -38.734 -9.553 1.00 75.52 O ANISOU 193 O PHE A 75 12121 7669 8902 366 -3203 -443 O ATOM 194 CB PHE A 75 33.505 -41.803 -10.338 1.00 73.15 C ANISOU 194 CB PHE A 75 11615 7370 8807 514 -3463 -481 C ATOM 195 CG PHE A 75 32.946 -41.969 -8.959 1.00 72.38 C ANISOU 195 CG PHE A 75 11951 7179 8369 503 -3701 -446 C ATOM 196 CD1 PHE A 75 31.733 -42.611 -8.760 1.00 70.26 C ANISOU 196 CD1 PHE A 75 11978 6993 7722 487 -3565 -345 C ATOM 197 CD2 PHE A 75 33.638 -41.490 -7.859 1.00 74.44 C ANISOU 197 CD2 PHE A 75 12341 7257 8683 488 -4057 -523 C ATOM 198 CE1 PHE A 75 31.223 -42.771 -7.487 1.00 70.83 C ANISOU 198 CE1 PHE A 75 12485 6955 7469 456 -3738 -324 C ATOM 199 CE2 PHE A 75 33.132 -41.645 -6.582 1.00 75.08 C ANISOU 199 CE2 PHE A 75 12887 7234 8406 450 -4262 -496 C ATOM 200 CZ PHE A 75 31.922 -42.286 -6.397 1.00 73.47 C ANISOU 200 CZ PHE A 75 12992 7102 7821 433 -4082 -398 C ATOM 201 N VAL A 76 34.718 -38.924 -10.405 1.00 77.34 N ANISOU 201 N VAL A 76 11788 7794 9800 404 -3382 -619 N ATOM 202 CA VAL A 76 35.181 -37.706 -9.725 1.00 78.74 C ANISOU 202 CA VAL A 76 11987 7850 10078 341 -3501 -697 C ATOM 203 C VAL A 76 34.488 -36.483 -10.336 1.00 77.40 C ANISOU 203 C VAL A 76 11794 7780 9832 282 -3099 -621 C ATOM 204 O VAL A 76 33.853 -35.710 -9.623 1.00 78.25 O ANISOU 204 O VAL A 76 12156 7851 9722 239 -3063 -591 O ATOM 205 CB VAL A 76 36.732 -37.555 -9.692 1.00 80.98 C ANISOU 205 CB VAL A 76 11941 7979 10849 340 -3763 -861 C ATOM 206 CG1 VAL A 76 37.371 -38.797 -9.087 1.00 82.88 C ANISOU 206 CG1 VAL A 76 12194 8102 11194 423 -4191 -908 C ATOM 207 CG2 VAL A 76 37.328 -37.274 -11.065 1.00 80.66 C ANISOU 207 CG2 VAL A 76 11475 7991 11178 327 -3441 -906 C ATOM 208 N VAL A 77 34.545 -36.359 -11.660 1.00 75.98 N ANISOU 208 N VAL A 77 11342 7713 9812 278 -2785 -582 N ATOM 209 CA VAL A 77 34.037 -35.177 -12.351 1.00 74.54 C ANISOU 209 CA VAL A 77 11110 7601 9608 227 -2432 -495 C ATOM 210 C VAL A 77 32.555 -34.977 -12.040 1.00 72.64 C ANISOU 210 C VAL A 77 11160 7455 8983 240 -2285 -338 C ATOM 211 O VAL A 77 32.093 -33.851 -11.827 1.00 72.77 O ANISOU 211 O VAL A 77 11263 7434 8950 211 -2134 -291 O ATOM 212 CB VAL A 77 34.251 -35.290 -13.880 1.00 73.70 C ANISOU 212 CB VAL A 77 10735 7607 9661 207 -2130 -455 C ATOM 213 CG1 VAL A 77 33.531 -34.169 -14.625 1.00 72.81 C ANISOU 213 CG1 VAL A 77 10634 7573 9455 163 -1788 -313 C ATOM 214 CG2 VAL A 77 35.738 -35.267 -14.214 1.00 75.46 C ANISOU 214 CG2 VAL A 77 10637 7702 10330 178 -2190 -632 C ATOM 215 N GLY A 78 31.823 -36.083 -12.011 1.00 71.37 N ANISOU 215 N GLY A 78 11134 7397 8583 281 -2314 -264 N ATOM 216 CA GLY A 78 30.396 -36.058 -11.753 1.00 70.19 C ANISOU 216 CA GLY A 78 11220 7337 8112 290 -2165 -125 C ATOM 217 C GLY A 78 30.053 -35.902 -10.285 1.00 70.79 C ANISOU 217 C GLY A 78 11629 7275 7992 278 -2324 -174 C ATOM 218 O GLY A 78 29.052 -35.270 -9.960 1.00 70.78 O ANISOU 218 O GLY A 78 11788 7274 7831 267 -2133 -97 O ATOM 219 N THR A 79 30.854 -36.483 -9.394 1.00 71.63 N ANISOU 219 N THR A 79 11856 7247 8112 275 -2670 -299 N ATOM 220 CA THR A 79 30.610 -36.316 -7.958 1.00 73.45 C ANISOU 220 CA THR A 79 12471 7322 8114 231 -2842 -355 C ATOM 221 C THR A 79 30.964 -34.903 -7.522 1.00 74.25 C ANISOU 221 C THR A 79 12596 7291 8323 164 -2808 -431 C ATOM 222 O THR A 79 30.227 -34.289 -6.760 1.00 75.09 O ANISOU 222 O THR A 79 12989 7317 8223 115 -2685 -425 O ATOM 223 CB THR A 79 31.398 -37.317 -7.088 1.00 75.92 C ANISOU 223 CB THR A 79 12947 7508 8389 238 -3281 -448 C ATOM 224 OG1 THR A 79 32.779 -37.310 -7.470 1.00 77.84 O ANISOU 224 OG1 THR A 79 12865 7696 9011 259 -3506 -549 O ATOM 225 CG2 THR A 79 30.826 -38.726 -7.225 1.00 74.94 C ANISOU 225 CG2 THR A 79 12927 7472 8075 290 -3295 -371 C ATOM 226 N VAL A 80 32.091 -34.395 -8.018 1.00 74.66 N ANISOU 226 N VAL A 80 12346 7305 8715 153 -2887 -514 N ATOM 227 CA VAL A 80 32.516 -33.017 -7.760 1.00 75.31 C ANISOU 227 CA VAL A 80 12404 7261 8947 77 -2830 -595 C ATOM 228 C VAL A 80 31.542 -32.016 -8.393 1.00 73.73 C ANISOU 228 C VAL A 80 12166 7128 8717 85 -2387 -469 C ATOM 229 O VAL A 80 30.987 -31.164 -7.699 1.00 74.54 O ANISOU 229 O VAL A 80 12503 7123 8694 39 -2258 -478 O ATOM 230 CB VAL A 80 33.941 -32.754 -8.302 1.00 76.22 C ANISOU 230 CB VAL A 80 12150 7327 9483 57 -2971 -713 C ATOM 231 CG1 VAL A 80 34.284 -31.269 -8.245 1.00 77.63 C ANISOU 231 CG1 VAL A 80 12273 7389 9832 -31 -2831 -784 C ATOM 232 CG2 VAL A 80 34.967 -33.563 -7.525 1.00 78.06 C ANISOU 232 CG2 VAL A 80 12401 7445 9811 52 -3462 -843 C ATOM 233 N GLY A 81 31.346 -32.130 -9.706 1.00 71.31 N ANISOU 233 N GLY A 81 11580 6985 8530 140 -2159 -351 N ATOM 234 CA GLY A 81 30.480 -31.226 -10.453 1.00 69.84 C ANISOU 234 CA GLY A 81 11325 6864 8347 160 -1785 -198 C ATOM 235 C GLY A 81 29.101 -31.074 -9.854 1.00 69.03 C ANISOU 235 C GLY A 81 11482 6758 7985 185 -1620 -99 C ATOM 236 O GLY A 81 28.599 -29.958 -9.713 1.00 69.25 O ANISOU 236 O GLY A 81 11567 6696 8046 179 -1393 -56 O ATOM 237 N ASN A 82 28.489 -32.194 -9.490 1.00 68.07 N ANISOU 237 N ASN A 82 11518 6715 7632 211 -1710 -71 N ATOM 238 CA ASN A 82 27.147 -32.178 -8.917 1.00 68.06 C ANISOU 238 CA ASN A 82 11749 6704 7406 225 -1524 8 C ATOM 239 C ASN A 82 27.140 -31.748 -7.463 1.00 69.25 C ANISOU 239 C ASN A 82 12263 6635 7411 150 -1582 -128 C ATOM 240 O ASN A 82 26.144 -31.210 -6.983 1.00 70.29 O ANISOU 240 O ASN A 82 12568 6689 7448 143 -1327 -92 O ATOM 241 CB ASN A 82 26.479 -33.544 -9.050 1.00 67.43 C ANISOU 241 CB ASN A 82 11718 6772 7128 255 -1571 77 C ATOM 242 CG ASN A 82 26.140 -33.885 -10.485 1.00 66.57 C ANISOU 242 CG ASN A 82 11307 6883 7103 304 -1447 232 C ATOM 243 OD1 ASN A 82 25.497 -33.100 -11.188 1.00 67.29 O ANISOU 243 OD1 ASN A 82 11250 7032 7284 334 -1212 372 O ATOM 244 ND2 ASN A 82 26.564 -35.064 -10.928 1.00 66.19 N ANISOU 244 ND2 ASN A 82 11184 6943 7019 307 -1610 212 N ATOM 245 N SER A 83 28.237 -31.999 -6.756 1.00 69.30 N ANISOU 245 N SER A 83 12394 6529 7407 86 -1918 -288 N ATOM 246 CA SER A 83 28.380 -31.488 -5.407 1.00 71.05 C ANISOU 246 CA SER A 83 12992 6527 7474 -19 -2011 -430 C ATOM 247 C SER A 83 28.536 -29.980 -5.477 1.00 71.26 C ANISOU 247 C SER A 83 12949 6432 7692 -59 -1800 -468 C ATOM 248 O SER A 83 27.693 -29.237 -4.974 1.00 71.64 O ANISOU 248 O SER A 83 13204 6364 7649 -88 -1514 -463 O ATOM 249 CB SER A 83 29.583 -32.118 -4.715 1.00 73.23 C ANISOU 249 CB SER A 83 13388 6714 7719 -80 -2490 -574 C ATOM 250 OG SER A 83 29.395 -33.514 -4.584 1.00 73.33 O ANISOU 250 OG SER A 83 13506 6807 7549 -38 -2673 -530 O ATOM 251 N VAL A 84 29.597 -29.540 -6.148 1.00 70.70 N ANISOU 251 N VAL A 84 12574 6375 7911 -61 -1905 -509 N ATOM 252 CA VAL A 84 29.872 -28.119 -6.338 1.00 70.84 C ANISOU 252 CA VAL A 84 12497 6274 8145 -105 -1706 -544 C ATOM 253 C VAL A 84 28.624 -27.422 -6.865 1.00 69.18 C ANISOU 253 C VAL A 84 12240 6092 7951 -26 -1261 -373 C ATOM 254 O VAL A 84 28.298 -26.328 -6.426 1.00 70.43 O ANISOU 254 O VAL A 84 12539 6078 8143 -67 -1034 -407 O ATOM 255 CB VAL A 84 31.066 -27.893 -7.294 1.00 71.04 C ANISOU 255 CB VAL A 84 12134 6348 8510 -105 -1806 -576 C ATOM 256 CG1 VAL A 84 31.191 -26.428 -7.697 1.00 71.88 C ANISOU 256 CG1 VAL A 84 12126 6342 8841 -141 -1525 -572 C ATOM 257 CG2 VAL A 84 32.360 -28.366 -6.646 1.00 73.00 C ANISOU 257 CG2 VAL A 84 12395 6513 8827 -188 -2256 -765 C ATOM 258 N THR A 85 27.915 -28.061 -7.789 1.00 66.92 N ANISOU 258 N THR A 85 11762 6009 7655 82 -1146 -191 N ATOM 259 CA THR A 85 26.646 -27.509 -8.262 1.00 66.59 C ANISOU 259 CA THR A 85 11660 5998 7643 168 -780 -7 C ATOM 260 C THR A 85 25.717 -27.263 -7.069 1.00 67.83 C ANISOU 260 C THR A 85 12160 5988 7622 135 -606 -63 C ATOM 261 O THR A 85 25.216 -26.158 -6.900 1.00 68.81 O ANISOU 261 O THR A 85 12327 5958 7858 145 -316 -41 O ATOM 262 CB THR A 85 25.987 -28.394 -9.350 1.00 64.16 C ANISOU 262 CB THR A 85 11124 5943 7309 264 -748 188 C ATOM 263 OG1 THR A 85 26.673 -28.189 -10.589 1.00 63.40 O ANISOU 263 OG1 THR A 85 10729 5951 7407 282 -763 263 O ATOM 264 CG2 THR A 85 24.514 -28.047 -9.558 1.00 63.87 C ANISOU 264 CG2 THR A 85 11061 5928 7276 348 -440 370 C ATOM 265 N LEU A 86 25.525 -28.271 -6.227 1.00 68.17 N ANISOU 265 N LEU A 86 12468 6036 7397 89 -764 -144 N ATOM 266 CA LEU A 86 24.682 -28.118 -5.040 1.00 69.98 C ANISOU 266 CA LEU A 86 13078 6086 7423 26 -573 -221 C ATOM 267 C LEU A 86 25.186 -27.004 -4.122 1.00 72.71 C ANISOU 267 C LEU A 86 13690 6163 7773 -94 -524 -399 C ATOM 268 O LEU A 86 24.391 -26.235 -3.581 1.00 73.50 O ANISOU 268 O LEU A 86 13973 6084 7870 -117 -178 -423 O ATOM 269 CB LEU A 86 24.586 -29.436 -4.272 1.00 69.78 C ANISOU 269 CB LEU A 86 13344 6091 7076 -31 -791 -289 C ATOM 270 CG LEU A 86 23.798 -30.517 -5.014 1.00 68.03 C ANISOU 270 CG LEU A 86 12926 6098 6821 66 -751 -128 C ATOM 271 CD1 LEU A 86 24.224 -31.908 -4.567 1.00 67.96 C ANISOU 271 CD1 LEU A 86 13114 6146 6561 20 -1087 -191 C ATOM 272 CD2 LEU A 86 22.297 -30.319 -4.840 1.00 68.35 C ANISOU 272 CD2 LEU A 86 13016 6101 6851 99 -344 -43 C ATOM 273 N PHE A 87 26.507 -26.924 -3.962 1.00 74.20 N ANISOU 273 N PHE A 87 13885 6314 7991 -179 -862 -531 N ATOM 274 CA PHE A 87 27.148 -25.889 -3.144 1.00 77.42 C ANISOU 274 CA PHE A 87 14528 6476 8409 -323 -880 -717 C ATOM 275 C PHE A 87 26.920 -24.497 -3.728 1.00 78.33 C ANISOU 275 C PHE A 87 14443 6497 8820 -278 -514 -658 C ATOM 276 O PHE A 87 26.771 -23.523 -2.988 1.00 80.55 O ANISOU 276 O PHE A 87 14981 6537 9086 -376 -303 -776 O ATOM 277 CB PHE A 87 28.657 -26.161 -3.029 1.00 78.52 C ANISOU 277 CB PHE A 87 14612 6624 8596 -411 -1362 -852 C ATOM 278 CG PHE A 87 29.374 -25.276 -2.033 1.00 81.79 C ANISOU 278 CG PHE A 87 15319 6789 8968 -599 -1476 -1068 C ATOM 279 CD1 PHE A 87 29.777 -23.989 -2.381 1.00 82.40 C ANISOU 279 CD1 PHE A 87 15235 6753 9319 -637 -1292 -1115 C ATOM 280 CD2 PHE A 87 29.664 -25.741 -0.751 1.00 84.19 C ANISOU 280 CD2 PHE A 87 16085 6961 8940 -756 -1783 -1224 C ATOM 281 CE1 PHE A 87 30.437 -23.182 -1.471 1.00 85.32 C ANISOU 281 CE1 PHE A 87 15880 6891 9647 -832 -1399 -1328 C ATOM 282 CE2 PHE A 87 30.325 -24.935 0.164 1.00 87.05 C ANISOU 282 CE2 PHE A 87 16743 7094 9235 -957 -1919 -1428 C ATOM 283 CZ PHE A 87 30.712 -23.656 -0.198 1.00 87.81 C ANISOU 283 CZ PHE A 87 16654 7088 9620 -998 -1724 -1488 C ATOM 284 N THR A 88 26.910 -24.417 -5.056 1.00 77.20 N ANISOU 284 N THR A 88 13870 6528 8931 -142 -437 -477 N ATOM 285 CA THR A 88 26.717 -23.160 -5.768 1.00 78.29 C ANISOU 285 CA THR A 88 13801 6585 9360 -82 -118 -378 C ATOM 286 C THR A 88 25.258 -22.726 -5.765 1.00 78.79 C ANISOU 286 C THR A 88 13897 6580 9460 23 300 -234 C ATOM 287 O THR A 88 24.958 -21.575 -5.482 1.00 81.51 O ANISOU 287 O THR A 88 14328 6698 9941 10 601 -261 O ATOM 288 CB THR A 88 27.214 -23.273 -7.222 1.00 77.43 C ANISOU 288 CB THR A 88 13267 6678 9474 8 -191 -221 C ATOM 289 OG1 THR A 88 28.632 -23.476 -7.221 1.00 78.62 O ANISOU 289 OG1 THR A 88 13345 6840 9686 -93 -517 -378 O ATOM 290 CG2 THR A 88 26.890 -22.019 -8.026 1.00 78.25 C ANISOU 290 CG2 THR A 88 13186 6694 9849 81 143 -72 C ATOM 291 N LEU A 89 24.351 -23.640 -6.083 1.00 78.13 N ANISOU 291 N LEU A 89 13725 6675 9286 125 326 -87 N ATOM 292 CA LEU A 89 22.926 -23.309 -6.125 1.00 79.89 C ANISOU 292 CA LEU A 89 13911 6839 9601 234 705 56 C ATOM 293 C LEU A 89 22.384 -22.899 -4.754 1.00 83.00 C ANISOU 293 C LEU A 89 14708 6955 9872 137 964 -120 C ATOM 294 O LEU A 89 21.529 -22.023 -4.668 1.00 85.05 O ANISOU 294 O LEU A 89 14949 7035 10327 202 1355 -64 O ATOM 295 CB LEU A 89 22.100 -24.484 -6.672 1.00 78.65 C ANISOU 295 CB LEU A 89 13584 6935 9363 331 645 222 C ATOM 296 CG LEU A 89 22.334 -24.945 -8.117 1.00 76.71 C ANISOU 296 CG LEU A 89 12960 6967 9219 424 461 423 C ATOM 297 CD1 LEU A 89 21.498 -26.188 -8.398 1.00 75.61 C ANISOU 297 CD1 LEU A 89 12738 7046 8943 474 397 533 C ATOM 298 CD2 LEU A 89 22.029 -23.845 -9.128 1.00 77.30 C ANISOU 298 CD2 LEU A 89 12758 7011 9598 536 665 631 C ATOM 299 N ALA A 90 22.882 -23.529 -3.693 1.00 84.66 N ANISOU 299 N ALA A 90 15292 7110 9762 -21 751 -330 N ATOM 300 CA ALA A 90 22.446 -23.221 -2.331 1.00 88.34 C ANISOU 300 CA ALA A 90 16230 7301 10034 -159 985 -522 C ATOM 301 C ALA A 90 22.779 -21.787 -1.893 1.00 92.66 C ANISOU 301 C ALA A 90 16930 7554 10719 -245 1213 -656 C ATOM 302 O ALA A 90 22.007 -21.174 -1.153 1.00 94.99 O ANISOU 302 O ALA A 90 17479 7595 11016 -291 1619 -740 O ATOM 303 CB ALA A 90 23.046 -24.216 -1.355 1.00 88.78 C ANISOU 303 CB ALA A 90 16686 7362 9681 -326 632 -699 C ATOM 304 N ARG A 91 23.911 -21.251 -2.353 1.00 94.49 N ANISOU 304 N ARG A 91 17009 7805 11087 -276 987 -686 N ATOM 305 CA ARG A 91 24.316 -19.873 -2.016 1.00 98.80 C ANISOU 305 CA ARG A 91 17682 8074 11782 -372 1189 -817 C ATOM 306 C ARG A 91 23.897 -18.852 -3.086 1.00 99.90 C ANISOU 306 C ARG A 91 17438 8178 12338 -195 1510 -612 C ATOM 307 O ARG A 91 24.696 -18.019 -3.525 1.00100.14 O ANISOU 307 O ARG A 91 17339 8143 12563 -223 1477 -629 O ATOM 308 CB ARG A 91 25.827 -19.792 -1.716 1.00100.30 C ANISOU 308 CB ARG A 91 17978 8248 11883 -551 768 -1008 C ATOM 309 CG ARG A 91 26.774 -20.091 -2.876 1.00 98.78 C ANISOU 309 CG ARG A 91 17343 8299 11889 -472 442 -897 C ATOM 310 CD ARG A 91 28.200 -20.364 -2.399 1.00100.29 C ANISOU 310 CD ARG A 91 17639 8490 11976 -652 -36 -1103 C ATOM 311 NE ARG A 91 28.998 -19.143 -2.250 1.00102.63 N ANISOU 311 NE ARG A 91 17963 8576 12455 -788 14 -1254 N ATOM 312 CZ ARG A 91 29.610 -18.496 -3.246 0.00102.98 C ANISOU 312 CZ ARG A 91 17640 8652 12835 -742 59 -1187 C ATOM 313 NH1 ARG A 91 30.310 -17.394 -2.985 0.00105.81 N ANISOU 313 NH1 ARG A 91 18068 8792 13343 -893 119 -1349 N ATOM 314 NH2 ARG A 91 29.527 -18.927 -4.504 0.00100.51 N ANISOU 314 NH2 ARG A 91 16917 8572 12697 -566 59 -967 N ATOM 315 N LYS A 92 22.623 -18.909 -3.470 1.00101.14 N ANISOU 315 N LYS A 92 17425 8361 12641 -21 1819 -418 N ATOM 316 CA LYS A 92 22.063 -18.022 -4.486 1.00102.39 C ANISOU 316 CA LYS A 92 17226 8482 13194 169 2096 -179 C ATOM 317 C LYS A 92 20.796 -17.368 -3.947 1.00104.51 C ANISOU 317 C LYS A 92 17594 8480 13633 239 2608 -167 C ATOM 318 O LYS A 92 19.890 -18.056 -3.480 1.00104.77 O ANISOU 318 O LYS A 92 17711 8536 13559 260 2732 -172 O ATOM 319 CB LYS A 92 21.766 -18.817 -5.769 1.00100.11 C ANISOU 319 CB LYS A 92 16520 8532 12985 343 1896 103 C ATOM 320 CG LYS A 92 21.065 -18.046 -6.884 1.00101.22 C ANISOU 320 CG LYS A 92 16300 8658 13498 549 2120 399 C ATOM 321 CD LYS A 92 21.699 -16.684 -7.166 0.00102.93 C ANISOU 321 CD LYS A 92 16502 8653 13953 534 2265 394 C ATOM 322 CE LYS A 92 21.021 -15.973 -8.328 0.00102.63 C ANISOU 322 CE LYS A 92 16129 8599 14266 744 2439 725 C ATOM 323 NZ LYS A 92 21.603 -14.624 -8.541 0.00104.09 N ANISOU 323 NZ LYS A 92 16339 8529 14680 724 2618 718 N ATOM 324 N SER A 100 14.233 -18.603 -11.384 1.00100.81 N ANISOU 324 N SER A 100 14252 9118 14931 1669 2449 2164 N ATOM 325 CA SER A 100 13.204 -18.567 -10.352 1.00103.80 C ANISOU 325 CA SER A 100 14658 9276 15503 1701 2820 2028 C ATOM 326 C SER A 100 12.963 -19.953 -9.764 1.00102.99 C ANISOU 326 C SER A 100 14668 9376 15087 1571 2735 1846 C ATOM 327 O SER A 100 13.270 -20.206 -8.599 1.00102.97 O ANISOU 327 O SER A 100 15024 9260 14838 1418 2880 1539 O ATOM 328 CB SER A 100 11.899 -18.000 -10.915 1.00106.42 C ANISOU 328 CB SER A 100 14593 9476 16365 1934 2987 2325 C ATOM 329 OG SER A 100 11.013 -17.629 -9.874 1.00108.77 O ANISOU 329 OG SER A 100 14902 9500 16923 1968 3427 2174 O ATOM 330 N THR A 101 12.412 -20.848 -10.578 1.00102.67 N ANISOU 330 N THR A 101 14348 9625 15037 1620 2488 2039 N ATOM 331 CA THR A 101 12.128 -22.209 -10.140 1.00100.66 C ANISOU 331 CA THR A 101 14174 9577 14495 1500 2389 1899 C ATOM 332 C THR A 101 13.110 -23.202 -10.755 1.00 96.67 C ANISOU 332 C THR A 101 13854 9351 13523 1354 1995 1814 C ATOM 333 O THR A 101 13.134 -24.375 -10.386 1.00 94.45 O ANISOU 333 O THR A 101 13885 9090 12909 1203 1966 1559 O ATOM 334 CB THR A 101 10.692 -22.631 -10.503 1.00101.91 C ANISOU 334 CB THR A 101 13919 9910 14892 1607 2305 2143 C ATOM 335 OG1 THR A 101 10.509 -22.544 -11.921 1.00106.08 O ANISOU 335 OG1 THR A 101 14231 10156 15917 1751 2687 2208 O ATOM 336 CG2 THR A 101 9.682 -21.730 -9.810 1.00100.39 C ANISOU 336 CG2 THR A 101 13808 9940 14392 1470 2192 2007 C ATOM 337 N VAL A 102 13.918 -22.722 -11.695 1.00 95.21 N ANISOU 337 N VAL A 102 13477 9362 13335 1402 1699 2041 N ATOM 338 CA VAL A 102 14.902 -23.565 -12.363 1.00 91.57 C ANISOU 338 CA VAL A 102 13137 9133 12519 1284 1360 1990 C ATOM 339 C VAL A 102 16.018 -23.974 -11.408 1.00 88.78 C ANISOU 339 C VAL A 102 13155 8732 11845 1123 1342 1656 C ATOM 340 O VAL A 102 16.565 -25.072 -11.510 1.00 87.92 O ANISOU 340 O VAL A 102 13136 8822 11446 1025 1132 1558 O ATOM 341 CB VAL A 102 15.517 -22.857 -13.584 1.00 92.35 C ANISOU 341 CB VAL A 102 13165 9200 12722 1331 1272 2155 C ATOM 342 CG1 VAL A 102 16.621 -23.708 -14.191 1.00 90.39 C ANISOU 342 CG1 VAL A 102 13078 9103 12161 1191 1024 2025 C ATOM 343 CG2 VAL A 102 14.442 -22.550 -14.616 1.00 93.32 C ANISOU 343 CG2 VAL A 102 12962 9449 13045 1458 1143 2521 C ATOM 344 N HIS A 103 16.353 -23.082 -10.481 1.00 89.37 N ANISOU 344 N HIS A 103 13450 8526 11980 1093 1552 1488 N ATOM 345 CA HIS A 103 17.411 -23.349 -9.502 1.00 87.75 C ANISOU 345 CA HIS A 103 13609 8246 11484 931 1482 1185 C ATOM 346 C HIS A 103 17.150 -24.583 -8.637 1.00 85.76 C ANISOU 346 C HIS A 103 13570 8068 10944 828 1431 1014 C ATOM 347 O HIS A 103 18.088 -25.284 -8.256 1.00 84.10 O ANISOU 347 O HIS A 103 13582 7933 10439 705 1189 843 O ATOM 348 CB HIS A 103 17.644 -22.111 -8.621 1.00 90.69 C ANISOU 348 CB HIS A 103 14201 8267 11987 903 1774 1030 C ATOM 349 CG HIS A 103 18.213 -20.940 -9.367 1.00 92.49 C ANISOU 349 CG HIS A 103 14299 8402 12441 963 1795 1149 C ATOM 350 ND1 HIS A 103 17.451 -19.853 -9.745 1.00 95.09 N ANISOU 350 ND1 HIS A 103 14439 8549 13141 1115 2065 1342 N ATOM 351 CD2 HIS A 103 19.465 -20.696 -9.823 1.00 91.58 C ANISOU 351 CD2 HIS A 103 14208 8334 12252 891 1589 1107 C ATOM 352 CE1 HIS A 103 18.211 -18.988 -10.393 1.00 95.66 C ANISOU 352 CE1 HIS A 103 14462 8559 13324 1127 2024 1419 C ATOM 353 NE2 HIS A 103 19.438 -19.476 -10.453 1.00 93.64 N ANISOU 353 NE2 HIS A 103 14329 8443 12806 984 1752 1270 N ATOM 354 N TYR A 104 15.884 -24.859 -8.340 1.00 85.40 N ANISOU 354 N TYR A 104 13451 7990 11006 878 1657 1064 N ATOM 355 CA TYR A 104 15.537 -26.058 -7.587 1.00 84.14 C ANISOU 355 CA TYR A 104 13495 7895 10580 775 1641 921 C ATOM 356 C TYR A 104 15.566 -27.308 -8.468 1.00 80.13 C ANISOU 356 C TYR A 104 12801 7728 9914 772 1310 1040 C ATOM 357 O TYR A 104 16.091 -28.342 -8.062 1.00 78.00 O ANISOU 357 O TYR A 104 12756 7553 9324 661 1113 900 O ATOM 358 CB TYR A 104 14.179 -25.890 -6.896 1.00 87.56 C ANISOU 358 CB TYR A 104 13922 8138 11208 806 2059 901 C ATOM 359 CG TYR A 104 14.176 -24.799 -5.834 1.00 90.93 C ANISOU 359 CG TYR A 104 14628 8191 11727 767 2434 724 C ATOM 360 CD1 TYR A 104 15.099 -24.809 -4.782 1.00 91.00 C ANISOU 360 CD1 TYR A 104 15122 8054 11400 594 2394 457 C ATOM 361 CD2 TYR A 104 13.250 -23.762 -5.877 1.00 94.29 C ANISOU 361 CD2 TYR A 104 14841 8396 12587 898 2820 821 C ATOM 362 CE1 TYR A 104 15.099 -23.814 -3.815 1.00 93.68 C ANISOU 362 CE1 TYR A 104 15755 8045 11791 527 2739 279 C ATOM 363 CE2 TYR A 104 13.241 -22.764 -4.911 1.00 97.00 C ANISOU 363 CE2 TYR A 104 15459 8375 13021 851 3203 641 C ATOM 364 CZ TYR A 104 14.165 -22.792 -3.884 1.00 96.69 C ANISOU 364 CZ TYR A 104 15931 8203 12602 653 3169 364 C ATOM 365 OH TYR A 104 14.143 -21.792 -2.933 1.00 99.37 O ANISOU 365 OH TYR A 104 16576 8173 13006 580 3557 174 O ATOM 366 N HIS A 105 15.072 -27.203 -9.680 1.00 78.64 N ANISOU 366 N HIS A 105 12225 7711 9943 887 1239 1299 N ATOM 367 CA HIS A 105 15.113 -28.320 -10.580 1.00 75.87 C ANISOU 367 CA HIS A 105 11711 7680 9436 864 932 1411 C ATOM 368 C HIS A 105 16.524 -28.723 -10.920 1.00 73.11 C ANISOU 368 C HIS A 105 11497 7451 8831 783 625 1321 C ATOM 369 O HIS A 105 16.820 -29.879 -11.039 1.00 70.70 O ANISOU 369 O HIS A 105 11262 7318 8280 705 418 1257 O ATOM 370 CB HIS A 105 14.374 -27.963 -11.839 1.00 76.42 C ANISOU 370 CB HIS A 105 11375 7892 9768 982 879 1718 C ATOM 371 CG HIS A 105 12.896 -28.095 -11.725 1.00 78.04 C ANISOU 371 CG HIS A 105 11364 8094 10191 1038 1053 1818 C ATOM 372 ND1 HIS A 105 12.057 -27.012 -11.709 1.00 80.69 N ANISOU 372 ND1 HIS A 105 11526 8211 10921 1162 1346 1912 N ATOM 373 CD2 HIS A 105 12.103 -29.183 -11.649 1.00 77.47 C ANISOU 373 CD2 HIS A 105 11202 8197 10035 982 989 1829 C ATOM 374 CE1 HIS A 105 10.811 -27.421 -11.618 1.00 81.81 C ANISOU 374 CE1 HIS A 105 11452 8394 11235 1185 1450 1977 C ATOM 375 NE2 HIS A 105 10.811 -28.736 -11.583 1.00 79.91 N ANISOU 375 NE2 HIS A 105 11264 8398 10699 1068 1236 1926 N ATOM 376 N LEU A 106 17.390 -27.758 -11.110 1.00 66.85 N ANISOU 376 N LEU A 106 12697 5993 6708 467 1254 1047 N ATOM 377 CA LEU A 106 18.813 -28.014 -11.363 1.00 66.70 C ANISOU 377 CA LEU A 106 12631 6090 6620 472 956 1076 C ATOM 378 C LEU A 106 19.474 -28.708 -10.186 1.00 67.25 C ANISOU 378 C LEU A 106 13147 5926 6477 512 849 939 C ATOM 379 O LEU A 106 20.364 -29.540 -10.371 1.00 66.70 O ANISOU 379 O LEU A 106 13058 5950 6334 519 676 910 O ATOM 380 CB LEU A 106 19.570 -26.711 -11.639 1.00 66.90 C ANISOU 380 CB LEU A 106 12478 6118 6823 459 747 1209 C ATOM 381 CG LEU A 106 19.274 -25.989 -12.949 1.00 66.55 C ANISOU 381 CG LEU A 106 11986 6326 6973 426 776 1387 C ATOM 382 CD1 LEU A 106 20.241 -24.826 -13.118 1.00 67.13 C ANISOU 382 CD1 LEU A 106 11911 6366 7229 416 566 1521 C ATOM 383 CD2 LEU A 106 19.365 -26.943 -14.129 1.00 65.58 C ANISOU 383 CD2 LEU A 106 11604 6525 6786 420 795 1422 C ATOM 384 N GLY A 107 19.057 -28.332 -8.980 1.00 68.05 N ANISOU 384 N GLY A 107 13668 5706 6479 543 943 855 N ATOM 385 CA GLY A 107 19.537 -28.971 -7.766 1.00 69.22 C ANISOU 385 CA GLY A 107 14340 5586 6372 596 851 724 C ATOM 386 C GLY A 107 19.008 -30.384 -7.612 1.00 68.83 C ANISOU 386 C GLY A 107 14443 5554 6153 606 1068 638 C ATOM 387 O GLY A 107 19.728 -31.276 -7.158 1.00 68.89 O ANISOU 387 O GLY A 107 14697 5491 5984 636 903 566 O ATOM 388 N SER A 108 17.744 -30.584 -7.979 1.00 68.32 N ANISOU 388 N SER A 108 14220 5557 6181 582 1424 644 N ATOM 389 CA SER A 108 17.129 -31.907 -7.918 1.00 68.56 C ANISOU 389 CA SER A 108 14328 5594 6125 586 1659 568 C ATOM 390 C SER A 108 17.835 -32.828 -8.904 1.00 67.80 C ANISOU 390 C SER A 108 13907 5807 6046 566 1454 581 C ATOM 391 O SER A 108 18.196 -33.956 -8.571 1.00 67.28 O ANISOU 391 O SER A 108 14033 5704 5825 587 1418 505 O ATOM 392 CB SER A 108 15.633 -31.822 -8.237 1.00 68.54 C ANISOU 392 CB SER A 108 14124 5585 6331 562 2049 574 C ATOM 393 OG SER A 108 15.006 -33.089 -8.113 1.00 68.63 O ANISOU 393 OG SER A 108 14206 5556 6312 567 2291 497 O ATOM 394 N LEU A 109 18.031 -32.317 -10.117 1.00 67.78 N ANISOU 394 N LEU A 109 13431 6096 6227 530 1332 683 N ATOM 395 CA LEU A 109 18.814 -32.988 -11.146 1.00 66.46 C ANISOU 395 CA LEU A 109 12951 6223 6074 518 1143 708 C ATOM 396 C LEU A 109 20.228 -33.309 -10.660 1.00 66.98 C ANISOU 396 C LEU A 109 13203 6211 6033 541 846 674 C ATOM 397 O LEU A 109 20.736 -34.398 -10.914 1.00 66.84 O ANISOU 397 O LEU A 109 13144 6293 5956 548 768 618 O ATOM 398 CB LEU A 109 18.890 -32.100 -12.384 1.00 66.24 C ANISOU 398 CB LEU A 109 12483 6458 6225 489 1068 848 C ATOM 399 CG LEU A 109 19.747 -32.606 -13.536 1.00 66.08 C ANISOU 399 CG LEU A 109 12152 6740 6215 484 911 893 C ATOM 400 CD1 LEU A 109 19.228 -33.953 -14.004 1.00 66.00 C ANISOU 400 CD1 LEU A 109 12070 6868 6136 491 1026 793 C ATOM 401 CD2 LEU A 109 19.745 -31.605 -14.680 1.00 66.46 C ANISOU 401 CD2 LEU A 109 11845 7001 6403 465 878 1055 C ATOM 402 N ALA A 110 20.857 -32.356 -9.973 1.00 68.04 N ANISOU 402 N ALA A 110 13527 6146 6178 556 660 701 N ATOM 403 CA ALA A 110 22.214 -32.536 -9.441 1.00 68.42 C ANISOU 403 CA ALA A 110 13749 6056 6191 583 317 663 C ATOM 404 C ALA A 110 22.287 -33.695 -8.457 1.00 69.08 C ANISOU 404 C ALA A 110 14275 5930 6040 625 298 531 C ATOM 405 O ALA A 110 23.263 -34.447 -8.437 1.00 69.67 O ANISOU 405 O ALA A 110 14358 6001 6109 640 57 487 O ATOM 406 CB ALA A 110 22.701 -31.260 -8.771 1.00 69.65 C ANISOU 406 CB ALA A 110 14069 5977 6418 600 110 694 C ATOM 407 N LEU A 111 21.251 -33.836 -7.639 1.00 69.26 N ANISOU 407 N LEU A 111 14667 5760 5889 647 568 474 N ATOM 408 CA LEU A 111 21.201 -34.903 -6.647 1.00 69.75 C ANISOU 408 CA LEU A 111 15210 5590 5698 693 607 369 C ATOM 409 C LEU A 111 21.014 -36.250 -7.342 1.00 68.16 C ANISOU 409 C LEU A 111 14768 5606 5520 671 725 338 C ATOM 410 O LEU A 111 21.831 -37.152 -7.187 1.00 66.65 O ANISOU 410 O LEU A 111 14669 5390 5264 690 511 286 O ATOM 411 CB LEU A 111 20.076 -34.637 -5.629 1.00 70.52 C ANISOU 411 CB LEU A 111 15766 5404 5622 724 950 332 C ATOM 412 CG LEU A 111 19.874 -35.658 -4.505 1.00 70.94 C ANISOU 412 CG LEU A 111 16405 5170 5376 782 1074 245 C ATOM 413 CD1 LEU A 111 21.123 -35.787 -3.650 1.00 71.67 C ANISOU 413 CD1 LEU A 111 16931 5031 5269 844 626 193 C ATOM 414 CD2 LEU A 111 18.669 -35.277 -3.665 1.00 72.13 C ANISOU 414 CD2 LEU A 111 16945 5054 5406 810 1513 227 C ATOM 415 N SER A 112 19.949 -36.357 -8.130 1.00 68.42 N ANISOU 415 N SER A 112 14479 5838 5678 632 1036 365 N ATOM 416 CA SER A 112 19.628 -37.585 -8.859 1.00 68.79 C ANISOU 416 CA SER A 112 14274 6086 5774 615 1154 321 C ATOM 417 C SER A 112 20.826 -38.143 -9.622 1.00 69.00 C ANISOU 417 C SER A 112 14028 6334 5855 609 853 316 C ATOM 418 O SER A 112 21.010 -39.356 -9.678 1.00 67.72 O ANISOU 418 O SER A 112 13880 6202 5648 618 841 242 O ATOM 419 CB SER A 112 18.474 -37.347 -9.838 1.00 67.96 C ANISOU 419 CB SER A 112 13768 6188 5865 577 1411 359 C ATOM 420 OG SER A 112 18.893 -36.563 -10.940 1.00 66.72 O ANISOU 420 OG SER A 112 13199 6302 5847 551 1245 450 O ATOM 421 N ASP A 113 21.627 -37.255 -10.209 1.00 70.93 N ANISOU 421 N ASP A 113 14014 6712 6223 594 637 396 N ATOM 422 CA ASP A 113 22.840 -37.656 -10.928 1.00 72.93 C ANISOU 422 CA ASP A 113 13994 7138 6577 590 388 401 C ATOM 423 C ASP A 113 23.999 -38.012 -10.000 1.00 72.73 C ANISOU 423 C ASP A 113 14265 6860 6507 625 74 342 C ATOM 424 O ASP A 113 24.770 -38.933 -10.297 1.00 73.48 O ANISOU 424 O ASP A 113 14243 7019 6657 631 -66 290 O ATOM 425 CB ASP A 113 23.283 -36.558 -11.896 1.00 76.09 C ANISOU 425 CB ASP A 113 14010 7739 7162 565 314 526 C ATOM 426 CG ASP A 113 22.467 -36.545 -13.178 1.00 79.23 C ANISOU 426 CG ASP A 113 14040 8454 7609 541 531 578 C ATOM 427 OD1 ASP A 113 21.804 -37.571 -13.483 1.00 80.44 O ANISOU 427 OD1 ASP A 113 14158 8706 7699 545 678 495 O ATOM 428 OD2 ASP A 113 22.506 -35.509 -13.887 1.00 82.57 O ANISOU 428 OD2 ASP A 113 14218 9010 8142 524 530 702 O ATOM 429 N LEU A 114 24.134 -37.276 -8.897 1.00 70.94 N ANISOU 429 N LEU A 114 14426 6331 6197 653 -55 343 N ATOM 430 CA LEU A 114 25.124 -37.607 -7.873 1.00 70.24 C ANISOU 430 CA LEU A 114 14709 5938 6038 701 -402 274 C ATOM 431 C LEU A 114 24.873 -39.007 -7.322 1.00 69.22 C ANISOU 431 C LEU A 114 14887 5702 5709 729 -332 180 C ATOM 432 O LEU A 114 25.814 -39.758 -7.081 1.00 68.59 O ANISOU 432 O LEU A 114 14879 5520 5658 753 -616 124 O ATOM 433 CB LEU A 114 25.084 -36.584 -6.734 1.00 71.06 C ANISOU 433 CB LEU A 114 15262 5715 6022 740 -527 274 C ATOM 434 CG LEU A 114 26.059 -36.755 -5.562 1.00 72.22 C ANISOU 434 CG LEU A 114 15885 5486 6068 807 -953 195 C ATOM 435 CD1 LEU A 114 27.507 -36.668 -6.015 1.00 72.46 C ANISOU 435 CD1 LEU A 114 15572 5530 6429 801 -1375 203 C ATOM 436 CD2 LEU A 114 25.769 -35.700 -4.509 1.00 73.48 C ANISOU 436 CD2 LEU A 114 16521 5340 6057 854 -1010 183 C ATOM 437 N LEU A 115 23.597 -39.342 -7.136 1.00 68.42 N ANISOU 437 N LEU A 115 14942 5603 5449 725 49 167 N ATOM 438 CA LEU A 115 23.188 -40.631 -6.574 1.00 69.19 C ANISOU 438 CA LEU A 115 15347 5572 5370 750 189 95 C ATOM 439 C LEU A 115 23.422 -41.794 -7.540 1.00 67.97 C ANISOU 439 C LEU A 115 14790 5679 5357 723 195 53 C ATOM 440 O LEU A 115 23.792 -42.885 -7.120 1.00 68.73 O ANISOU 440 O LEU A 115 15081 5654 5379 749 92 -9 O ATOM 441 CB LEU A 115 21.711 -40.598 -6.167 1.00 69.61 C ANISOU 441 CB LEU A 115 15618 5531 5298 750 649 100 C ATOM 442 CG LEU A 115 21.287 -39.644 -5.042 1.00 71.56 C ANISOU 442 CG LEU A 115 16373 5463 5352 790 744 118 C ATOM 443 CD1 LEU A 115 19.779 -39.432 -5.055 1.00 71.60 C ANISOU 443 CD1 LEU A 115 16362 5454 5388 769 1258 138 C ATOM 444 CD2 LEU A 115 21.747 -40.156 -3.684 1.00 73.35 C ANISOU 444 CD2 LEU A 115 17292 5308 5268 866 584 67 C ATOM 445 N ILE A 116 23.194 -41.571 -8.828 1.00 66.09 N ANISOU 445 N ILE A 116 14018 5783 5308 678 309 87 N ATOM 446 CA ILE A 116 23.529 -42.574 -9.828 1.00 65.08 C ANISOU 446 CA ILE A 116 13511 5909 5307 662 289 37 C ATOM 447 C ILE A 116 24.996 -42.988 -9.662 1.00 65.93 C ANISOU 447 C ILE A 116 13622 5931 5494 683 -83 1 C ATOM 448 O ILE A 116 25.301 -44.171 -9.595 1.00 66.37 O ANISOU 448 O ILE A 116 13709 5957 5550 697 -144 -78 O ATOM 449 CB ILE A 116 23.225 -42.071 -11.261 1.00 63.75 C ANISOU 449 CB ILE A 116 12824 6103 5292 625 413 89 C ATOM 450 CG1 ILE A 116 21.716 -42.121 -11.504 1.00 63.29 C ANISOU 450 CG1 ILE A 116 12719 6113 5215 610 751 84 C ATOM 451 CG2 ILE A 116 23.933 -42.915 -12.314 1.00 63.09 C ANISOU 451 CG2 ILE A 116 12378 6266 5326 623 326 37 C ATOM 452 CD1 ILE A 116 21.261 -41.420 -12.762 1.00 62.39 C ANISOU 452 CD1 ILE A 116 12190 6296 5219 585 839 150 C ATOM 453 N LEU A 117 25.895 -42.015 -9.562 1.00 67.16 N ANISOU 453 N LEU A 117 13739 6016 5761 686 -341 58 N ATOM 454 CA LEU A 117 27.324 -42.307 -9.441 1.00 68.38 C ANISOU 454 CA LEU A 117 13836 6053 6091 706 -717 24 C ATOM 455 C LEU A 117 27.653 -43.064 -8.155 1.00 69.44 C ANISOU 455 C LEU A 117 14482 5829 6074 756 -953 -51 C ATOM 456 O LEU A 117 28.387 -44.042 -8.196 1.00 69.91 O ANISOU 456 O LEU A 117 14478 5844 6240 770 -1137 -118 O ATOM 457 CB LEU A 117 28.150 -41.017 -9.515 1.00 69.78 C ANISOU 457 CB LEU A 117 13867 6170 6473 700 -945 103 C ATOM 458 CG LEU A 117 28.125 -40.277 -10.858 1.00 69.04 C ANISOU 458 CG LEU A 117 13254 6410 6566 657 -760 201 C ATOM 459 CD1 LEU A 117 28.640 -38.856 -10.708 1.00 70.28 C ANISOU 459 CD1 LEU A 117 13356 6454 6893 652 -928 297 C ATOM 460 CD2 LEU A 117 28.935 -41.021 -11.907 1.00 69.17 C ANISOU 460 CD2 LEU A 117 12847 6630 6801 648 -765 174 C ATOM 461 N LEU A 118 27.094 -42.621 -7.027 1.00 70.44 N ANISOU 461 N LEU A 118 15132 5687 5943 789 -936 -39 N ATOM 462 CA LEU A 118 27.420 -43.195 -5.707 1.00 73.17 C ANISOU 462 CA LEU A 118 16074 5646 6080 854 -1186 -96 C ATOM 463 C LEU A 118 26.741 -44.543 -5.389 1.00 74.23 C ANISOU 463 C LEU A 118 16449 5735 6017 867 -956 -143 C ATOM 464 O LEU A 118 27.308 -45.368 -4.678 1.00 74.30 O ANISOU 464 O LEU A 118 16783 5499 5948 914 -1211 -191 O ATOM 465 CB LEU A 118 27.084 -42.201 -4.586 1.00 74.45 C ANISOU 465 CB LEU A 118 16783 5509 5994 899 -1234 -70 C ATOM 466 CG LEU A 118 27.830 -40.861 -4.546 1.00 75.19 C ANISOU 466 CG LEU A 118 16784 5522 6263 904 -1548 -38 C ATOM 467 CD1 LEU A 118 27.377 -40.057 -3.337 1.00 76.68 C ANISOU 467 CD1 LEU A 118 17603 5385 6144 963 -1571 -41 C ATOM 468 CD2 LEU A 118 29.342 -41.039 -4.541 1.00 76.23 C ANISOU 468 CD2 LEU A 118 16765 5510 6686 925 -2084 -79 C ATOM 469 N LEU A 119 25.532 -44.756 -5.901 1.00 74.46 N ANISOU 469 N LEU A 119 16318 5975 5998 830 -494 -128 N ATOM 470 CA LEU A 119 24.769 -45.979 -5.622 1.00 75.02 C ANISOU 470 CA LEU A 119 16580 5986 5936 839 -226 -166 C ATOM 471 C LEU A 119 24.922 -47.064 -6.693 1.00 73.96 C ANISOU 471 C LEU A 119 15949 6129 6022 805 -183 -227 C ATOM 472 O LEU A 119 24.925 -48.261 -6.378 1.00 74.67 O ANISOU 472 O LEU A 119 16192 6109 6071 824 -178 -278 O ATOM 473 CB LEU A 119 23.288 -45.635 -5.465 1.00 75.00 C ANISOU 473 CB LEU A 119 16701 5981 5812 825 261 -127 C ATOM 474 CG LEU A 119 22.979 -44.736 -4.268 1.00 77.04 C ANISOU 474 CG LEU A 119 17549 5916 5806 872 306 -83 C ATOM 475 CD1 LEU A 119 21.612 -44.084 -4.413 0.00 76.77 C ANISOU 475 CD1 LEU A 119 17449 5938 5781 843 785 -41 C ATOM 476 CD2 LEU A 119 23.067 -45.541 -2.976 0.00 79.96 C ANISOU 476 CD2 LEU A 119 18606 5899 5875 943 261 -100 C ATOM 477 N ALA A 120 25.038 -46.650 -7.950 1.00 71.75 N ANISOU 477 N ALA A 120 15105 6194 5962 760 -145 -221 N ATOM 478 CA ALA A 120 25.077 -47.598 -9.048 1.00 71.62 C ANISOU 478 CA ALA A 120 14637 6453 6120 736 -67 -291 C ATOM 479 C ALA A 120 26.495 -47.980 -9.452 1.00 72.72 C ANISOU 479 C ALA A 120 14535 6633 6462 744 -409 -337 C ATOM 480 O ALA A 120 26.750 -49.146 -9.752 1.00 73.59 O ANISOU 480 O ALA A 120 14513 6787 6661 749 -433 -423 O ATOM 481 CB ALA A 120 24.315 -47.053 -10.242 1.00 70.60 C ANISOU 481 CB ALA A 120 14076 6664 6084 697 190 -267 C ATOM 482 N MET A 121 27.416 -47.017 -9.468 1.00 73.93 N ANISOU 482 N MET A 121 14607 6750 6733 745 -661 -286 N ATOM 483 CA MET A 121 28.749 -47.273 -10.031 1.00 75.52 C ANISOU 483 CA MET A 121 14471 6997 7223 746 -928 -324 C ATOM 484 C MET A 121 29.632 -48.201 -9.195 1.00 77.33 C ANISOU 484 C MET A 121 14943 6919 7516 785 -1272 -395 C ATOM 485 O MET A 121 30.337 -49.037 -9.762 1.00 77.98 O ANISOU 485 O MET A 121 14728 7073 7827 785 -1357 -469 O ATOM 486 CB MET A 121 29.506 -45.978 -10.349 1.00 76.46 C ANISOU 486 CB MET A 121 14374 7142 7535 734 -1081 -241 C ATOM 487 CG MET A 121 30.275 -46.074 -11.663 1.00 77.24 C ANISOU 487 CG MET A 121 13914 7500 7933 714 -1038 -251 C ATOM 488 SD MET A 121 31.430 -44.733 -12.007 1.00 79.29 S ANISOU 488 SD MET A 121 13879 7714 8531 704 -1228 -149 S ATOM 489 CE MET A 121 32.823 -45.279 -11.023 1.00 81.66 C ANISOU 489 CE MET A 121 14323 7587 9114 741 -1741 -229 C ATOM 490 N PRO A 122 29.605 -48.070 -7.858 1.00 78.92 N ANISOU 490 N PRO A 122 15705 6763 7516 826 -1474 -376 N ATOM 491 CA PRO A 122 30.508 -48.927 -7.076 1.00 81.01 C ANISOU 491 CA PRO A 122 16220 6710 7847 871 -1865 -437 C ATOM 492 C PRO A 122 30.283 -50.440 -7.234 1.00 80.49 C ANISOU 492 C PRO A 122 16119 6684 7777 874 -1749 -516 C ATOM 493 O PRO A 122 31.235 -51.171 -7.517 1.00 80.32 O ANISOU 493 O PRO A 122 15859 6625 8032 881 -1985 -587 O ATOM 494 CB PRO A 122 30.249 -48.490 -5.626 1.00 82.78 C ANISOU 494 CB PRO A 122 17150 6557 7745 926 -2034 -396 C ATOM 495 CG PRO A 122 28.959 -47.759 -5.651 1.00 81.44 C ANISOU 495 CG PRO A 122 17098 6529 7317 903 -1605 -330 C ATOM 496 CD PRO A 122 28.886 -47.114 -7.000 1.00 79.21 C ANISOU 496 CD PRO A 122 16184 6640 7271 842 -1400 -304 C ATOM 497 N VAL A 123 29.047 -50.898 -7.056 1.00 80.02 N ANISOU 497 N VAL A 123 16271 6676 7454 868 -1385 -507 N ATOM 498 CA VAL A 123 28.745 -52.333 -7.131 1.00 80.50 C ANISOU 498 CA VAL A 123 16322 6741 7521 872 -1263 -578 C ATOM 499 C VAL A 123 28.872 -52.858 -8.564 1.00 79.10 C ANISOU 499 C VAL A 123 15503 6932 7618 833 -1112 -662 C ATOM 500 O VAL A 123 29.363 -53.967 -8.784 1.00 78.00 O ANISOU 500 O VAL A 123 15213 6777 7646 841 -1215 -751 O ATOM 501 CB VAL A 123 27.340 -52.652 -6.583 1.00 80.11 C ANISOU 501 CB VAL A 123 16635 6621 7180 875 -873 -540 C ATOM 502 CG1 VAL A 123 26.995 -54.124 -6.796 1.00 80.09 C ANISOU 502 CG1 VAL A 123 16538 6640 7250 872 -724 -614 C ATOM 503 CG2 VAL A 123 27.265 -52.290 -5.109 1.00 82.16 C ANISOU 503 CG2 VAL A 123 17613 6477 7125 930 -998 -465 C ATOM 504 N GLU A 124 28.428 -52.064 -9.533 1.00 78.26 N ANISOU 504 N GLU A 124 15047 7144 7543 796 -873 -637 N ATOM 505 CA GLU A 124 28.595 -52.427 -10.928 1.00 77.62 C ANISOU 505 CA GLU A 124 14415 7405 7669 774 -740 -714 C ATOM 506 C GLU A 124 30.065 -52.681 -11.234 1.00 77.89 C ANISOU 506 C GLU A 124 14189 7392 8009 786 -1040 -767 C ATOM 507 O GLU A 124 30.402 -53.673 -11.881 1.00 79.20 O ANISOU 507 O GLU A 124 14079 7663 8347 790 -1017 -875 O ATOM 508 CB GLU A 124 28.037 -51.347 -11.858 1.00 77.72 C ANISOU 508 CB GLU A 124 14158 7724 7648 745 -503 -654 C ATOM 509 CG GLU A 124 28.442 -51.547 -13.316 1.00 79.57 C ANISOU 509 CG GLU A 124 13879 8287 8064 738 -410 -719 C ATOM 510 CD GLU A 124 27.594 -50.771 -14.305 1.00 80.38 C ANISOU 510 CD GLU A 124 13768 8701 8072 720 -142 -672 C ATOM 511 OE1 GLU A 124 28.111 -50.469 -15.407 1.00 80.02 O ANISOU 511 OE1 GLU A 124 13380 8888 8132 722 -95 -673 O ATOM 512 OE2 GLU A 124 26.415 -50.477 -13.999 1.00 81.69 O ANISOU 512 OE2 GLU A 124 14110 8860 8069 709 28 -632 O ATOM 513 N LEU A 125 30.934 -51.794 -10.759 1.00 77.99 N ANISOU 513 N LEU A 125 14281 7222 8127 794 -1323 -699 N ATOM 514 CA LEU A 125 32.362 -51.894 -11.049 1.00 78.84 C ANISOU 514 CA LEU A 125 14093 7242 8618 804 -1606 -741 C ATOM 515 C LEU A 125 33.005 -53.128 -10.419 1.00 79.61 C ANISOU 515 C LEU A 125 14327 7064 8856 835 -1893 -833 C ATOM 516 O LEU A 125 33.912 -53.715 -11.000 1.00 81.01 O ANISOU 516 O LEU A 125 14144 7258 9378 838 -1985 -917 O ATOM 517 CB LEU A 125 33.101 -50.633 -10.597 1.00 79.92 C ANISOU 517 CB LEU A 125 14287 7190 8887 808 -1878 -650 C ATOM 518 CG LEU A 125 34.580 -50.541 -10.984 1.00 81.53 C ANISOU 518 CG LEU A 125 14105 7284 9586 812 -2138 -679 C ATOM 519 CD1 LEU A 125 34.788 -50.692 -12.488 1.00 80.94 C ANISOU 519 CD1 LEU A 125 13472 7564 9717 789 -1804 -712 C ATOM 520 CD2 LEU A 125 35.147 -49.220 -10.492 1.00 82.73 C ANISOU 520 CD2 LEU A 125 14325 7231 9876 816 -2402 -586 C ATOM 521 N TYR A 126 32.545 -53.522 -9.238 1.00 78.76 N ANISOU 521 N TYR A 126 14748 6686 8488 862 -2019 -813 N ATOM 522 CA TYR A 126 33.027 -54.760 -8.625 1.00 79.37 C ANISOU 522 CA TYR A 126 15000 6496 8658 896 -2278 -886 C ATOM 523 C TYR A 126 32.383 -55.974 -9.303 1.00 76.01 C ANISOU 523 C TYR A 126 14367 6291 8220 881 -1962 -979 C ATOM 524 O TYR A 126 33.079 -56.875 -9.761 1.00 75.07 O ANISOU 524 O TYR A 126 13951 6176 8395 886 -2061 -1083 O ATOM 525 CB TYR A 126 32.763 -54.757 -7.104 1.00 81.60 C ANISOU 525 CB TYR A 126 15991 6386 8626 942 -2513 -819 C ATOM 526 CG TYR A 126 32.911 -56.105 -6.430 1.00 84.02 C ANISOU 526 CG TYR A 126 16576 6429 8915 979 -2692 -866 C ATOM 527 CD1 TYR A 126 31.843 -56.994 -6.392 1.00 84.67 C ANISOU 527 CD1 TYR A 126 16804 6589 8775 972 -2341 -874 C ATOM 528 CD2 TYR A 126 34.106 -56.489 -5.827 1.00 86.75 C ANISOU 528 CD2 TYR A 126 17031 6424 9504 1023 -3222 -900 C ATOM 529 CE1 TYR A 126 31.954 -58.234 -5.790 1.00 86.89 C ANISOU 529 CE1 TYR A 126 17339 6623 9052 1006 -2482 -903 C ATOM 530 CE2 TYR A 126 34.229 -57.728 -5.214 1.00 89.40 C ANISOU 530 CE2 TYR A 126 17635 6507 9823 1060 -3399 -932 C ATOM 531 CZ TYR A 126 33.146 -58.599 -5.202 1.00 89.30 C ANISOU 531 CZ TYR A 126 17772 6594 9561 1050 -3012 -928 C ATOM 532 OH TYR A 126 33.228 -59.839 -4.609 1.00 90.96 O ANISOU 532 OH TYR A 126 18247 6550 9761 1085 -3156 -945 O ATOM 533 N ASN A 127 31.057 -55.955 -9.399 1.00 73.50 N ANISOU 533 N ASN A 127 14177 6143 7604 863 -1585 -949 N ATOM 534 CA ASN A 127 30.270 -57.167 -9.611 1.00 72.73 C ANISOU 534 CA ASN A 127 14055 6122 7454 860 -1343 -1024 C ATOM 535 C ASN A 127 29.745 -57.376 -11.025 1.00 70.45 C ANISOU 535 C ASN A 127 13270 6241 7255 832 -1011 -1115 C ATOM 536 O ASN A 127 29.202 -58.446 -11.317 1.00 70.10 O ANISOU 536 O ASN A 127 13137 6258 7238 833 -852 -1207 O ATOM 537 CB ASN A 127 29.073 -57.171 -8.651 1.00 73.38 C ANISOU 537 CB ASN A 127 14649 6038 7192 867 -1142 -938 C ATOM 538 CG ASN A 127 28.976 -58.442 -7.813 1.00 75.31 C ANISOU 538 CG ASN A 127 15230 5991 7393 898 -1214 -955 C ATOM 539 OD1 ASN A 127 29.760 -59.386 -7.954 1.00 75.94 O ANISOU 539 OD1 ASN A 127 15148 5998 7705 911 -1434 -1041 O ATOM 540 ND2 ASN A 127 28.008 -58.450 -6.912 1.00 76.04 N ANISOU 540 ND2 ASN A 127 15806 5890 7194 911 -1008 -865 N ATOM 541 N PHE A 128 29.866 -56.361 -11.880 1.00 69.02 N ANISOU 541 N PHE A 128 12796 6318 7107 813 -913 -1087 N ATOM 542 CA PHE A 128 29.457 -56.478 -13.278 1.00 68.11 C ANISOU 542 CA PHE A 128 12255 6582 7041 801 -638 -1170 C ATOM 543 C PHE A 128 30.586 -56.296 -14.287 1.00 68.55 C ANISOU 543 C PHE A 128 11891 6802 7352 807 -695 -1224 C ATOM 544 O PHE A 128 30.484 -56.775 -15.413 1.00 68.19 O ANISOU 544 O PHE A 128 11528 7015 7364 817 -512 -1333 O ATOM 545 CB PHE A 128 28.339 -55.494 -13.603 1.00 67.36 C ANISOU 545 CB PHE A 128 12184 6684 6724 780 -379 -1087 C ATOM 546 CG PHE A 128 27.061 -55.742 -12.855 1.00 68.22 C ANISOU 546 CG PHE A 128 12616 6664 6639 774 -209 -1054 C ATOM 547 CD1 PHE A 128 26.631 -57.027 -12.562 1.00 69.87 C ANISOU 547 CD1 PHE A 128 12908 6755 6882 784 -154 -1140 C ATOM 548 CD2 PHE A 128 26.258 -54.677 -12.482 1.00 69.05 C ANISOU 548 CD2 PHE A 128 12918 6755 6561 757 -71 -936 C ATOM 549 CE1 PHE A 128 25.443 -57.241 -11.888 1.00 71.10 C ANISOU 549 CE1 PHE A 128 13342 6764 6908 778 57 -1098 C ATOM 550 CE2 PHE A 128 25.068 -54.881 -11.805 1.00 69.80 C ANISOU 550 CE2 PHE A 128 13293 6703 6523 753 141 -903 C ATOM 551 CZ PHE A 128 24.659 -56.165 -11.506 1.00 70.82 C ANISOU 551 CZ PHE A 128 13504 6702 6703 763 219 -980 C ATOM 552 N ILE A 129 31.643 -55.592 -13.905 1.00 70.18 N ANISOU 552 N ILE A 129 12101 6841 7723 808 -936 -1151 N ATOM 553 CA ILE A 129 32.786 -55.394 -14.790 1.00 72.16 C ANISOU 553 CA ILE A 129 11942 7187 8286 814 -957 -1187 C ATOM 554 C ILE A 129 33.866 -56.445 -14.544 1.00 73.49 C ANISOU 554 C ILE A 129 11998 7124 8799 835 -1202 -1298 C ATOM 555 O ILE A 129 34.361 -57.053 -15.496 1.00 73.99 O ANISOU 555 O ILE A 129 11705 7329 9079 848 -1075 -1414 O ATOM 556 CB ILE A 129 33.382 -53.977 -14.623 1.00 73.70 C ANISOU 556 CB ILE A 129 12118 7311 8571 800 -1069 -1046 C ATOM 557 CG1 ILE A 129 32.331 -52.910 -14.975 1.00 72.70 C ANISOU 557 CG1 ILE A 129 12061 7425 8134 779 -816 -936 C ATOM 558 CG2 ILE A 129 34.636 -53.804 -15.480 1.00 75.71 C ANISOU 558 CG2 ILE A 129 11936 7604 9224 807 -1062 -1072 C ATOM 559 CD1 ILE A 129 31.724 -53.059 -16.358 1.00 71.86 C ANISOU 559 CD1 ILE A 129 11679 7707 7914 783 -465 -989 C ATOM 560 N TRP A 130 34.218 -56.649 -13.272 1.00 74.20 N ANISOU 560 N TRP A 130 12414 6844 8935 845 -1555 -1264 N ATOM 561 CA TRP A 130 35.300 -57.559 -12.877 1.00 76.03 C ANISOU 561 CA TRP A 130 12574 6785 9528 868 -1875 -1352 C ATOM 562 C TRP A 130 34.794 -58.950 -12.421 1.00 76.24 C ANISOU 562 C TRP A 130 12804 6708 9453 883 -1902 -1440 C ATOM 563 O TRP A 130 34.968 -59.933 -13.136 1.00 76.49 O ANISOU 563 O TRP A 130 12542 6852 9668 891 -1785 -1578 O ATOM 564 CB TRP A 130 36.167 -56.905 -11.785 1.00 77.46 C ANISOU 564 CB TRP A 130 12983 6571 9875 882 -2332 -1265 C ATOM 565 CG TRP A 130 36.938 -55.700 -12.262 1.00 77.62 C ANISOU 565 CG TRP A 130 12706 6625 10159 868 -2353 -1199 C ATOM 566 CD1 TRP A 130 36.541 -54.399 -12.193 1.00 76.72 C ANISOU 566 CD1 TRP A 130 12705 6598 9846 851 -2274 -1072 C ATOM 567 CD2 TRP A 130 38.232 -55.687 -12.882 1.00 79.01 C ANISOU 567 CD2 TRP A 130 12406 6723 10889 872 -2433 -1253 C ATOM 568 NE1 TRP A 130 37.498 -53.576 -12.731 1.00 77.37 N ANISOU 568 NE1 TRP A 130 12417 6666 10313 842 -2306 -1035 N ATOM 569 CE2 TRP A 130 38.549 -54.339 -13.160 1.00 78.94 C ANISOU 569 CE2 TRP A 130 12246 6756 10989 855 -2388 -1142 C ATOM 570 CE3 TRP A 130 39.152 -56.681 -13.230 1.00 80.55 C ANISOU 570 CE3 TRP A 130 12272 6798 11533 888 -2517 -1384 C ATOM 571 CZ2 TRP A 130 39.745 -53.958 -13.768 1.00 80.70 C ANISOU 571 CZ2 TRP A 130 12003 6894 11765 853 -2401 -1148 C ATOM 572 CZ3 TRP A 130 40.344 -56.302 -13.838 1.00 82.29 C ANISOU 572 CZ3 TRP A 130 12025 6933 12308 888 -2525 -1400 C ATOM 573 CH2 TRP A 130 40.627 -54.951 -14.100 1.00 82.61 C ANISOU 573 CH2 TRP A 130 11924 7008 12454 870 -2456 -1278 C ATOM 574 N VAL A 131 34.171 -59.025 -11.246 1.00 76.57 N ANISOU 574 N VAL A 131 13360 6526 9207 892 -2033 -1359 N ATOM 575 CA VAL A 131 33.694 -60.294 -10.687 1.00 77.30 C ANISOU 575 CA VAL A 131 13697 6466 9207 908 -2053 -1410 C ATOM 576 C VAL A 131 32.213 -60.486 -11.003 1.00 75.52 C ANISOU 576 C VAL A 131 13547 6486 8660 889 -1633 -1408 C ATOM 577 O VAL A 131 31.347 -59.964 -10.306 1.00 74.81 O ANISOU 577 O VAL A 131 13845 6328 8250 885 -1532 -1295 O ATOM 578 CB VAL A 131 33.908 -60.353 -9.155 1.00 80.02 C ANISOU 578 CB VAL A 131 14618 6362 9421 942 -2435 -1313 C ATOM 579 CG1 VAL A 131 33.338 -61.646 -8.571 1.00 80.37 C ANISOU 579 CG1 VAL A 131 14951 6241 9345 961 -2404 -1337 C ATOM 580 CG2 VAL A 131 35.390 -60.214 -8.817 1.00 82.54 C ANISOU 580 CG2 VAL A 131 14850 6387 10124 968 -2929 -1330 C ATOM 581 N HIS A 132 31.927 -61.269 -12.035 1.00 75.08 N ANISOU 581 N HIS A 132 13123 6684 8717 883 -1396 -1545 N ATOM 582 CA HIS A 132 30.566 -61.387 -12.554 1.00 73.78 C ANISOU 582 CA HIS A 132 12928 6769 8334 868 -1023 -1569 C ATOM 583 C HIS A 132 29.766 -62.350 -11.703 1.00 75.38 C ANISOU 583 C HIS A 132 13462 6750 8429 874 -976 -1559 C ATOM 584 O HIS A 132 28.596 -62.098 -11.390 1.00 75.14 O ANISOU 584 O HIS A 132 13651 6728 8168 861 -737 -1486 O ATOM 585 CB HIS A 132 30.597 -61.841 -14.007 1.00 72.27 C ANISOU 585 CB HIS A 132 12247 6912 8300 872 -829 -1735 C ATOM 586 CG HIS A 132 31.412 -60.950 -14.881 1.00 70.91 C ANISOU 586 CG HIS A 132 11768 6939 8236 873 -818 -1734 C ATOM 587 ND1 HIS A 132 32.783 -61.046 -14.967 1.00 71.71 N ANISOU 587 ND1 HIS A 132 11668 6918 8659 886 -1027 -1772 N ATOM 588 CD2 HIS A 132 31.054 -59.921 -15.681 1.00 69.59 C ANISOU 588 CD2 HIS A 132 11464 7054 7922 863 -613 -1684 C ATOM 589 CE1 HIS A 132 33.235 -60.122 -15.793 1.00 71.77 C ANISOU 589 CE1 HIS A 132 11423 7124 8720 883 -913 -1743 C ATOM 590 NE2 HIS A 132 32.205 -59.427 -16.242 1.00 70.81 N ANISOU 590 NE2 HIS A 132 11353 7257 8294 871 -668 -1685 N ATOM 591 N HIS A 133 30.421 -63.447 -11.336 1.00 77.80 N ANISOU 591 N HIS A 133 13786 6835 8937 895 -1192 -1626 N ATOM 592 CA HIS A 133 29.896 -64.405 -10.378 1.00 79.86 C ANISOU 592 CA HIS A 133 14411 6809 9123 908 -1199 -1590 C ATOM 593 C HIS A 133 31.014 -64.724 -9.385 1.00 82.11 C ANISOU 593 C HIS A 133 14972 6713 9511 940 -1634 -1541 C ATOM 594 O HIS A 133 32.176 -64.832 -9.790 1.00 82.51 O ANISOU 594 O HIS A 133 14724 6760 9866 949 -1890 -1625 O ATOM 595 CB HIS A 133 29.458 -65.674 -11.092 1.00 80.73 C ANISOU 595 CB HIS A 133 14212 7036 9423 908 -1025 -1752 C ATOM 596 CG HIS A 133 30.588 -66.424 -11.727 1.00 82.65 C ANISOU 596 CG HIS A 133 14078 7308 10017 925 -1230 -1910 C ATOM 597 ND1 HIS A 133 31.094 -67.593 -11.200 1.00 84.62 N ANISOU 597 ND1 HIS A 133 14399 7279 10472 946 -1445 -1955 N ATOM 598 CD2 HIS A 133 31.326 -66.158 -12.831 1.00 82.91 C ANISOU 598 CD2 HIS A 133 13667 7592 10243 927 -1232 -2029 C ATOM 599 CE1 HIS A 133 32.087 -68.022 -11.959 1.00 85.38 C ANISOU 599 CE1 HIS A 133 14084 7454 10902 958 -1574 -2108 C ATOM 600 NE2 HIS A 133 32.249 -67.168 -12.954 1.00 84.61 N ANISOU 600 NE2 HIS A 133 13676 7674 10797 948 -1429 -2155 N ATOM 601 N PRO A 134 30.694 -64.880 -8.100 1.00 84.03 N ANISOU 601 N PRO A 134 15791 6612 9522 963 -1725 -1407 N ATOM 602 CA PRO A 134 29.329 -64.809 -7.573 1.00 83.47 C ANISOU 602 CA PRO A 134 16082 6498 9136 956 -1368 -1303 C ATOM 603 C PRO A 134 28.898 -63.406 -7.154 1.00 82.70 C ANISOU 603 C PRO A 134 16280 6418 8723 951 -1269 -1170 C ATOM 604 O PRO A 134 29.730 -62.512 -6.994 1.00 81.60 O ANISOU 604 O PRO A 134 16188 6244 8572 961 -1553 -1134 O ATOM 605 CB PRO A 134 29.398 -65.700 -6.335 1.00 86.15 C ANISOU 605 CB PRO A 134 16950 6402 9380 998 -1532 -1216 C ATOM 606 CG PRO A 134 30.805 -65.548 -5.864 1.00 87.93 C ANISOU 606 CG PRO A 134 17292 6398 9717 1033 -2074 -1209 C ATOM 607 CD PRO A 134 31.632 -65.453 -7.116 1.00 86.57 C ANISOU 607 CD PRO A 134 16436 6525 9929 1006 -2168 -1369 C ATOM 608 N TRP A 135 27.591 -63.241 -6.973 1.00 82.85 N ANISOU 608 N TRP A 135 16477 6466 8535 936 -863 -1103 N ATOM 609 CA TRP A 135 27.015 -62.004 -6.457 1.00 82.61 C ANISOU 609 CA TRP A 135 16779 6405 8202 934 -711 -974 C ATOM 610 C TRP A 135 27.250 -61.938 -4.945 1.00 84.15 C ANISOU 610 C TRP A 135 17713 6155 8101 989 -902 -833 C ATOM 611 O TRP A 135 26.629 -62.678 -4.174 1.00 84.88 O ANISOU 611 O TRP A 135 18206 5987 8057 1013 -719 -764 O ATOM 612 CB TRP A 135 25.515 -61.927 -6.777 1.00 82.12 C ANISOU 612 CB TRP A 135 16630 6483 8088 903 -196 -961 C ATOM 613 CG TRP A 135 24.847 -60.731 -6.189 1.00 83.32 C ANISOU 613 CG TRP A 135 17133 6566 7956 903 1 -831 C ATOM 614 CD1 TRP A 135 24.154 -60.673 -5.018 1.00 85.68 C ANISOU 614 CD1 TRP A 135 18028 6537 7989 931 218 -699 C ATOM 615 CD2 TRP A 135 24.828 -59.407 -6.733 1.00 82.67 C ANISOU 615 CD2 TRP A 135 16848 6730 7831 878 17 -818 C ATOM 616 NE1 TRP A 135 23.697 -59.396 -4.798 1.00 85.52 N ANISOU 616 NE1 TRP A 135 18176 6544 7771 926 369 -620 N ATOM 617 CE2 TRP A 135 24.095 -58.600 -5.839 1.00 83.81 C ANISOU 617 CE2 TRP A 135 17464 6681 7696 891 234 -688 C ATOM 618 CE3 TRP A 135 25.346 -58.828 -7.898 1.00 81.11 C ANISOU 618 CE3 TRP A 135 16128 6887 7803 851 -104 -897 C ATOM 619 CZ2 TRP A 135 23.877 -57.239 -6.066 1.00 83.52 C ANISOU 619 CZ2 TRP A 135 17367 6795 7570 873 299 -643 C ATOM 620 CZ3 TRP A 135 25.131 -57.476 -8.124 1.00 80.48 C ANISOU 620 CZ3 TRP A 135 16003 6954 7619 833 -35 -835 C ATOM 621 CH2 TRP A 135 24.401 -56.697 -7.212 1.00 81.82 C ANISOU 621 CH2 TRP A 135 16623 6930 7536 842 150 -713 C ATOM 622 N ALA A 136 28.148 -61.047 -4.532 1.00 84.06 N ANISOU 622 N ALA A 136 17898 6042 7999 1015 -1274 -792 N ATOM 623 CA ALA A 136 28.593 -60.971 -3.142 1.00 86.56 C ANISOU 623 CA ALA A 136 18934 5917 8037 1084 -1585 -685 C ATOM 624 C ALA A 136 27.707 -60.132 -2.221 1.00 86.66 C ANISOU 624 C ALA A 136 19554 5756 7617 1111 -1320 -550 C ATOM 625 O ALA A 136 28.069 -59.923 -1.064 1.00 89.46 O ANISOU 625 O ALA A 136 20571 5740 7677 1181 -1586 -465 O ATOM 626 CB ALA A 136 30.024 -60.450 -3.090 1.00 87.06 C ANISOU 626 CB ALA A 136 18925 5893 8259 1108 -2171 -722 C ATOM 627 N PHE A 137 26.562 -59.655 -2.706 1.00 84.08 N ANISOU 627 N PHE A 137 19028 5663 7253 1065 -815 -536 N ATOM 628 CA PHE A 137 25.694 -58.812 -1.878 1.00 85.13 C ANISOU 628 CA PHE A 137 19696 5627 7020 1089 -515 -418 C ATOM 629 C PHE A 137 24.341 -59.426 -1.536 1.00 85.09 C ANISOU 629 C PHE A 137 19908 5502 6921 1085 63 -353 C ATOM 630 O PHE A 137 23.400 -58.701 -1.218 1.00 84.14 O ANISOU 630 O PHE A 137 20008 5338 6621 1083 454 -281 O ATOM 631 CB PHE A 137 25.507 -57.444 -2.531 1.00 83.42 C ANISOU 631 CB PHE A 137 19152 5703 6840 1047 -428 -433 C ATOM 632 CG PHE A 137 26.797 -56.744 -2.813 1.00 83.17 C ANISOU 632 CG PHE A 137 18920 5748 6930 1052 -948 -478 C ATOM 633 CD1 PHE A 137 27.486 -56.101 -1.799 1.00 85.77 C ANISOU 633 CD1 PHE A 137 19797 5764 7026 1116 -1332 -424 C ATOM 634 CD2 PHE A 137 27.339 -56.759 -4.079 1.00 81.32 C ANISOU 634 CD2 PHE A 137 17967 5867 7061 1000 -1054 -579 C ATOM 635 CE1 PHE A 137 28.689 -55.466 -2.051 1.00 85.56 C ANISOU 635 CE1 PHE A 137 19546 5767 7193 1120 -1825 -470 C ATOM 636 CE2 PHE A 137 28.541 -56.128 -4.342 1.00 81.45 C ANISOU 636 CE2 PHE A 137 17773 5920 7252 1003 -1487 -612 C ATOM 637 CZ PHE A 137 29.217 -55.479 -3.326 1.00 83.43 C ANISOU 637 CZ PHE A 137 18518 5846 7334 1060 -1880 -557 C ATOM 638 N GLY A 138 24.248 -60.753 -1.587 1.00 84.82 N ANISOU 638 N GLY A 138 19795 5388 7044 1084 127 -376 N ATOM 639 CA GLY A 138 23.055 -61.466 -1.132 1.00 86.18 C ANISOU 639 CA GLY A 138 20213 5361 7170 1088 659 -300 C ATOM 640 C GLY A 138 21.792 -61.100 -1.883 1.00 84.48 C ANISOU 640 C GLY A 138 19555 5386 7156 1026 1185 -329 C ATOM 641 O GLY A 138 21.825 -60.311 -2.829 1.00 83.00 O ANISOU 641 O GLY A 138 18865 5550 7121 980 1127 -410 O ATOM 642 N ASP A 139 20.668 -61.662 -1.452 1.00 85.93 N ANISOU 642 N ASP A 139 19932 5352 7365 1028 1700 -257 N ATOM 643 CA ASP A 139 19.416 -61.517 -2.193 1.00 84.93 C ANISOU 643 CA ASP A 139 19324 5402 7542 969 2182 -300 C ATOM 644 C ASP A 139 18.780 -60.138 -2.037 1.00 84.37 C ANISOU 644 C ASP A 139 19374 5360 7321 962 2437 -243 C ATOM 645 O ASP A 139 18.255 -59.580 -3.000 1.00 81.97 O ANISOU 645 O ASP A 139 18521 5355 7269 909 2549 -320 O ATOM 646 CB ASP A 139 18.420 -62.605 -1.784 1.00 87.38 C ANISOU 646 CB ASP A 139 19752 5425 8024 973 2663 -242 C ATOM 647 CG ASP A 139 17.288 -62.747 -2.778 1.00 86.65 C ANISOU 647 CG ASP A 139 18997 5528 8399 910 3024 -337 C ATOM 648 OD1 ASP A 139 16.376 -61.897 -2.754 1.00 87.58 O ANISOU 648 OD1 ASP A 139 19095 5631 8549 893 3386 -298 O ATOM 649 OD2 ASP A 139 17.317 -63.694 -3.598 1.00 85.40 O ANISOU 649 OD2 ASP A 139 18331 5524 8592 882 2920 -463 O ATOM 650 N ALA A 140 18.816 -59.604 -0.820 1.00 86.77 N ANISOU 650 N ALA A 140 20420 5337 7211 1022 2521 -111 N ATOM 651 CA ALA A 140 18.267 -58.284 -0.542 1.00 86.58 C ANISOU 651 CA ALA A 140 20583 5294 7017 1025 2760 -58 C ATOM 652 C ALA A 140 19.143 -57.204 -1.152 1.00 83.94 C ANISOU 652 C ALA A 140 19973 5280 6638 1007 2287 -128 C ATOM 653 O ALA A 140 18.634 -56.198 -1.627 1.00 82.59 O ANISOU 653 O ALA A 140 19530 5294 6557 971 2442 -142 O ATOM 654 CB ALA A 140 18.124 -58.066 0.953 1.00 90.43 C ANISOU 654 CB ALA A 140 22003 5319 7037 1109 2970 87 C ATOM 655 N GLY A 141 20.458 -57.406 -1.135 1.00 83.66 N ANISOU 655 N GLY A 141 19996 5286 6503 1032 1717 -165 N ATOM 656 CA GLY A 141 21.365 -56.513 -1.847 1.00 81.99 C ANISOU 656 CA GLY A 141 19420 5379 6351 1008 1274 -236 C ATOM 657 C GLY A 141 21.026 -56.443 -3.328 1.00 79.49 C ANISOU 657 C GLY A 141 18270 5503 6428 931 1359 -340 C ATOM 658 O GLY A 141 20.969 -55.354 -3.906 1.00 78.06 O ANISOU 658 O GLY A 141 17809 5555 6292 901 1337 -353 O ATOM 659 N CYS A 142 20.787 -57.602 -3.938 1.00 78.76 N ANISOU 659 N CYS A 142 17807 5507 6610 906 1449 -416 N ATOM 660 CA CYS A 142 20.391 -57.665 -5.340 1.00 76.76 C ANISOU 660 CA CYS A 142 16820 5639 6704 848 1525 -530 C ATOM 661 C CYS A 142 19.082 -56.912 -5.589 1.00 76.05 C ANISOU 661 C CYS A 142 16581 5604 6707 817 1956 -501 C ATOM 662 O CYS A 142 18.954 -56.200 -6.585 1.00 74.71 O ANISOU 662 O CYS A 142 15957 5752 6677 782 1910 -553 O ATOM 663 CB CYS A 142 20.269 -59.122 -5.799 1.00 77.85 C ANISOU 663 CB CYS A 142 16669 5800 7110 838 1561 -625 C ATOM 664 SG CYS A 142 19.493 -59.348 -7.422 1.00 77.72 S ANISOU 664 SG CYS A 142 15850 6178 7502 787 1708 -780 S ATOM 665 N ARG A 143 18.118 -57.061 -4.686 1.00 77.75 N ANISOU 665 N ARG A 143 17188 5491 6861 834 2384 -412 N ATOM 666 CA ARG A 143 16.825 -56.380 -4.822 1.00 77.96 C ANISOU 666 CA ARG A 143 17079 5500 7040 807 2828 -383 C ATOM 667 C ARG A 143 16.907 -54.877 -4.495 1.00 77.42 C ANISOU 667 C ARG A 143 17236 5443 6733 814 2805 -311 C ATOM 668 O ARG A 143 16.241 -54.058 -5.126 1.00 75.68 O ANISOU 668 O ARG A 143 16671 5394 6689 779 2949 -326 O ATOM 669 CB ARG A 143 15.775 -57.065 -3.943 1.00 80.74 C ANISOU 669 CB ARG A 143 17765 5453 7457 824 3352 -308 C ATOM 670 CG ARG A 143 15.456 -58.487 -4.382 1.00 81.95 C ANISOU 670 CG ARG A 143 17595 5590 7950 808 3436 -384 C ATOM 671 CD ARG A 143 14.702 -59.266 -3.313 1.00 85.32 C ANISOU 671 CD ARG A 143 18468 5559 8389 836 3919 -278 C ATOM 672 NE ARG A 143 14.504 -60.667 -3.685 1.00 85.71 N ANISOU 672 NE ARG A 143 18218 5570 8775 823 3959 -349 N ATOM 673 CZ ARG A 143 13.523 -61.131 -4.462 1.00 86.14 C ANISOU 673 CZ ARG A 143 17714 5678 9337 783 4194 -440 C ATOM 674 NH1 ARG A 143 12.604 -60.319 -4.975 1.00 85.68 N ANISOU 674 NH1 ARG A 143 17316 5707 9531 751 4411 -470 N ATOM 675 NH2 ARG A 143 13.454 -62.433 -4.726 1.00 86.95 N ANISOU 675 NH2 ARG A 143 17589 5722 9727 778 4187 -509 N ATOM 676 N GLY A 144 17.724 -54.524 -3.508 1.00 78.18 N ANISOU 676 N GLY A 144 17918 5341 6446 864 2595 -239 N ATOM 677 CA GLY A 144 17.891 -53.139 -3.107 1.00 78.34 C ANISOU 677 CA GLY A 144 18200 5335 6231 880 2532 -182 C ATOM 678 C GLY A 144 18.671 -52.328 -4.122 1.00 76.74 C ANISOU 678 C GLY A 144 17517 5516 6122 846 2123 -238 C ATOM 679 O GLY A 144 18.392 -51.143 -4.323 1.00 75.41 O ANISOU 679 O GLY A 144 17253 5446 5953 829 2180 -211 O ATOM 680 N TYR A 145 19.646 -52.965 -4.771 1.00 75.96 N ANISOU 680 N TYR A 145 17116 5620 6124 837 1736 -311 N ATOM 681 CA TYR A 145 20.548 -52.258 -5.689 1.00 74.02 C ANISOU 681 CA TYR A 145 16457 5702 5965 813 1359 -352 C ATOM 682 C TYR A 145 19.916 -51.931 -7.031 1.00 71.72 C ANISOU 682 C TYR A 145 15528 5773 5948 760 1501 -403 C ATOM 683 O TYR A 145 20.163 -50.868 -7.582 1.00 71.36 O ANISOU 683 O TYR A 145 15262 5931 5920 741 1380 -381 O ATOM 684 CB TYR A 145 21.825 -53.051 -5.927 1.00 74.12 C ANISOU 684 CB TYR A 145 16358 5775 6027 826 933 -417 C ATOM 685 CG TYR A 145 22.579 -52.609 -7.153 1.00 72.67 C ANISOU 685 CG TYR A 145 15613 5961 6037 794 673 -474 C ATOM 686 CD1 TYR A 145 22.300 -53.162 -8.393 1.00 71.56 C ANISOU 686 CD1 TYR A 145 14922 6129 6138 761 763 -566 C ATOM 687 CD2 TYR A 145 23.568 -51.636 -7.076 1.00 73.00 C ANISOU 687 CD2 TYR A 145 15690 6019 6026 803 347 -438 C ATOM 688 CE1 TYR A 145 22.989 -52.768 -9.523 1.00 70.58 C ANISOU 688 CE1 TYR A 145 14338 6325 6151 743 572 -610 C ATOM 689 CE2 TYR A 145 24.263 -51.235 -8.203 1.00 71.70 C ANISOU 689 CE2 TYR A 145 15018 6166 6057 776 167 -473 C ATOM 690 CZ TYR A 145 23.969 -51.808 -9.423 1.00 70.54 C ANISOU 690 CZ TYR A 145 14371 6328 6103 748 300 -554 C ATOM 691 OH TYR A 145 24.649 -51.421 -10.555 1.00 71.28 O ANISOU 691 OH TYR A 145 14012 6717 6352 732 169 -581 O ATOM 692 N TYR A 146 19.140 -52.853 -7.578 1.00 71.44 N ANISOU 692 N TYR A 146 15202 5806 6135 740 1726 -471 N ATOM 693 CA TYR A 146 18.419 -52.564 -8.810 1.00 70.75 C ANISOU 693 CA TYR A 146 14565 6018 6298 703 1840 -526 C ATOM 694 C TYR A 146 17.243 -51.621 -8.551 1.00 71.16 C ANISOU 694 C TYR A 146 14679 5963 6393 689 2180 -455 C ATOM 695 O TYR A 146 16.895 -50.818 -9.418 1.00 70.73 O ANISOU 695 O TYR A 146 14269 6141 6461 664 2171 -458 O ATOM 696 CB TYR A 146 17.966 -53.846 -9.513 1.00 71.32 C ANISOU 696 CB TYR A 146 14293 6175 6627 695 1918 -645 C ATOM 697 CG TYR A 146 19.008 -54.387 -10.464 1.00 70.70 C ANISOU 697 CG TYR A 146 13885 6380 6596 699 1575 -748 C ATOM 698 CD1 TYR A 146 19.115 -53.892 -11.760 1.00 69.78 C ANISOU 698 CD1 TYR A 146 13324 6619 6568 687 1453 -803 C ATOM 699 CD2 TYR A 146 19.901 -55.376 -10.065 1.00 71.65 C ANISOU 699 CD2 TYR A 146 14158 6392 6671 721 1384 -788 C ATOM 700 CE1 TYR A 146 20.073 -54.376 -12.635 1.00 69.49 C ANISOU 700 CE1 TYR A 146 13013 6822 6566 698 1198 -898 C ATOM 701 CE2 TYR A 146 20.864 -55.864 -10.934 1.00 71.12 C ANISOU 701 CE2 TYR A 146 13774 6561 6685 726 1105 -890 C ATOM 702 CZ TYR A 146 20.942 -55.362 -12.215 1.00 70.12 C ANISOU 702 CZ TYR A 146 13219 6785 6638 716 1037 -947 C ATOM 703 OH TYR A 146 21.895 -55.848 -13.076 1.00 70.89 O ANISOU 703 OH TYR A 146 13030 7096 6808 729 818 -1049 O ATOM 704 N PHE A 147 16.645 -51.704 -7.364 1.00 72.61 N ANISOU 704 N PHE A 147 15328 5781 6477 708 2489 -387 N ATOM 705 CA PHE A 147 15.612 -50.744 -6.980 1.00 73.21 C ANISOU 705 CA PHE A 147 15514 5707 6595 700 2838 -317 C ATOM 706 C PHE A 147 16.184 -49.338 -6.949 1.00 73.28 C ANISOU 706 C PHE A 147 15609 5820 6414 701 2628 -256 C ATOM 707 O PHE A 147 15.621 -48.415 -7.543 1.00 72.34 O ANISOU 707 O PHE A 147 15195 5843 6445 674 2705 -240 O ATOM 708 CB PHE A 147 15.015 -51.056 -5.607 1.00 75.33 C ANISOU 708 CB PHE A 147 16360 5527 6733 734 3236 -247 C ATOM 709 CG PHE A 147 14.161 -49.941 -5.066 1.00 75.75 C ANISOU 709 CG PHE A 147 16613 5392 6775 736 3586 -174 C ATOM 710 CD1 PHE A 147 12.851 -49.781 -5.497 1.00 75.78 C ANISOU 710 CD1 PHE A 147 16261 5363 7169 703 3963 -189 C ATOM 711 CD2 PHE A 147 14.680 -49.025 -4.159 1.00 76.22 C ANISOU 711 CD2 PHE A 147 17196 5295 6469 775 3510 -104 C ATOM 712 CE1 PHE A 147 12.069 -48.739 -5.022 1.00 76.54 C ANISOU 712 CE1 PHE A 147 16508 5272 7302 705 4296 -129 C ATOM 713 CE2 PHE A 147 13.906 -47.978 -3.685 1.00 76.88 C ANISOU 713 CE2 PHE A 147 17457 5203 6549 780 3839 -51 C ATOM 714 CZ PHE A 147 12.597 -47.836 -4.117 1.00 76.99 C ANISOU 714 CZ PHE A 147 17099 5187 6966 743 4250 -60 C ATOM 715 N LEU A 148 17.295 -49.182 -6.233 1.00 74.94 N ANISOU 715 N LEU A 148 16225 5930 6318 736 2344 -223 N ATOM 716 CA LEU A 148 17.914 -47.871 -6.055 1.00 75.51 C ANISOU 716 CA LEU A 148 16425 6039 6224 744 2120 -168 C ATOM 717 C LEU A 148 18.525 -47.372 -7.344 1.00 75.18 C ANISOU 717 C LEU A 148 15830 6395 6339 708 1817 -191 C ATOM 718 O LEU A 148 18.536 -46.170 -7.584 1.00 75.24 O ANISOU 718 O LEU A 148 15736 6498 6354 694 1768 -139 O ATOM 719 CB LEU A 148 18.982 -47.896 -4.959 1.00 76.85 C ANISOU 719 CB LEU A 148 17170 5959 6067 799 1831 -142 C ATOM 720 CG LEU A 148 18.515 -48.043 -3.503 1.00 78.99 C ANISOU 720 CG LEU A 148 18167 5790 6055 857 2102 -93 C ATOM 721 CD1 LEU A 148 19.728 -47.978 -2.591 1.00 80.09 C ANISOU 721 CD1 LEU A 148 18841 5715 5872 920 1674 -82 C ATOM 722 CD2 LEU A 148 17.496 -46.987 -3.099 1.00 79.21 C ANISOU 722 CD2 LEU A 148 18359 5676 6058 858 2492 -42 C ATOM 723 N ARG A 149 19.036 -48.284 -8.168 1.00 76.55 N ANISOU 723 N ARG A 149 15663 6786 6636 697 1634 -265 N ATOM 724 CA ARG A 149 19.521 -47.913 -9.495 1.00 76.41 C ANISOU 724 CA ARG A 149 15125 7145 6761 670 1422 -288 C ATOM 725 C ARG A 149 18.380 -47.309 -10.294 1.00 75.58 C ANISOU 725 C ARG A 149 14681 7202 6833 641 1653 -275 C ATOM 726 O ARG A 149 18.501 -46.203 -10.817 1.00 73.55 O ANISOU 726 O ARG A 149 14243 7108 6592 626 1569 -215 O ATOM 727 CB ARG A 149 20.081 -49.122 -10.251 1.00 78.58 C ANISOU 727 CB ARG A 149 15115 7600 7143 672 1265 -390 C ATOM 728 CG ARG A 149 20.941 -48.725 -11.435 1.00 81.03 C ANISOU 728 CG ARG A 149 15014 8244 7528 662 1021 -403 C ATOM 729 CD ARG A 149 21.119 -49.830 -12.463 1.00 83.73 C ANISOU 729 CD ARG A 149 15000 8809 8003 666 972 -524 C ATOM 730 NE ARG A 149 21.931 -49.344 -13.583 1.00 85.85 N ANISOU 730 NE ARG A 149 14927 9376 8314 664 800 -521 N ATOM 731 CZ ARG A 149 23.265 -49.338 -13.618 1.00 87.18 C ANISOU 731 CZ ARG A 149 15067 9562 8495 674 560 -517 C ATOM 732 NH1 ARG A 149 23.983 -49.812 -12.598 1.00 87.32 N ANISOU 732 NH1 ARG A 149 15376 9317 8482 688 394 -526 N ATOM 733 NH2 ARG A 149 23.892 -48.856 -14.689 1.00 87.07 N ANISOU 733 NH2 ARG A 149 14734 9806 8542 674 487 -501 N ATOM 734 N ASP A 150 17.269 -48.038 -10.372 1.00 77.16 N ANISOU 734 N ASP A 150 14789 7329 7197 635 1932 -329 N ATOM 735 CA ASP A 150 16.109 -47.598 -11.155 1.00 77.37 C ANISOU 735 CA ASP A 150 14464 7469 7463 612 2116 -335 C ATOM 736 C ASP A 150 15.531 -46.275 -10.656 1.00 76.28 C ANISOU 736 C ASP A 150 14474 7194 7314 602 2286 -235 C ATOM 737 O ASP A 150 15.240 -45.394 -11.455 1.00 73.95 O ANISOU 737 O ASP A 150 13881 7086 7128 585 2233 -201 O ATOM 738 CB ASP A 150 15.016 -48.683 -11.197 1.00 79.46 C ANISOU 738 CB ASP A 150 14609 7602 7979 610 2378 -421 C ATOM 739 CG ASP A 150 15.109 -49.573 -12.440 1.00 80.28 C ANISOU 739 CG ASP A 150 14285 7980 8237 613 2194 -544 C ATOM 740 OD1 ASP A 150 16.237 -49.931 -12.857 1.00 80.88 O ANISOU 740 OD1 ASP A 150 14313 8251 8165 626 1918 -581 O ATOM 741 OD2 ASP A 150 14.041 -49.916 -13.000 1.00 80.99 O ANISOU 741 OD2 ASP A 150 14087 8066 8619 608 2323 -614 O ATOM 742 N ALA A 151 15.383 -46.138 -9.339 1.00 78.01 N ANISOU 742 N ALA A 151 15176 7076 7389 619 2487 -188 N ATOM 743 CA ALA A 151 14.803 -44.931 -8.742 1.00 78.28 C ANISOU 743 CA ALA A 151 15402 6931 7406 617 2692 -108 C ATOM 744 C ALA A 151 15.533 -43.669 -9.191 1.00 77.10 C ANISOU 744 C ALA A 151 15134 6990 7170 607 2402 -43 C ATOM 745 O ALA A 151 14.915 -42.754 -9.726 1.00 78.17 O ANISOU 745 O ALA A 151 15011 7216 7472 585 2471 -2 O ATOM 746 CB ALA A 151 14.814 -45.031 -7.227 1.00 80.16 C ANISOU 746 CB ALA A 151 16278 6776 7401 655 2899 -76 C ATOM 747 N CYS A 152 16.847 -43.633 -8.982 1.00 76.17 N ANISOU 747 N CYS A 152 15186 6924 6832 625 2073 -31 N ATOM 748 CA CYS A 152 17.679 -42.508 -9.425 1.00 75.24 C ANISOU 748 CA CYS A 152 14927 6984 6676 616 1786 34 C ATOM 749 C CYS A 152 17.587 -42.270 -10.925 1.00 73.24 C ANISOU 749 C CYS A 152 14115 7098 6613 586 1693 45 C ATOM 750 O CYS A 152 17.572 -41.126 -11.375 1.00 72.77 O ANISOU 750 O CYS A 152 13885 7151 6610 571 1637 125 O ATOM 751 CB CYS A 152 19.143 -42.740 -9.060 1.00 75.80 C ANISOU 751 CB CYS A 152 15193 7030 6576 640 1428 26 C ATOM 752 SG CYS A 152 19.469 -42.700 -7.286 1.00 79.89 S ANISOU 752 SG CYS A 152 16454 7097 6800 694 1405 28 S ATOM 753 N THR A 153 17.548 -43.357 -11.690 1.00 72.66 N ANISOU 753 N THR A 153 13786 7198 6622 585 1667 -35 N ATOM 754 CA THR A 153 17.392 -43.282 -13.140 1.00 70.66 C ANISOU 754 CA THR A 153 13065 7277 6504 574 1582 -43 C ATOM 755 C THR A 153 16.108 -42.528 -13.486 1.00 69.94 C ANISOU 755 C THR A 153 12797 7177 6597 558 1769 -3 C ATOM 756 O THR A 153 16.135 -41.624 -14.314 1.00 70.96 O ANISOU 756 O THR A 153 12691 7502 6768 550 1663 70 O ATOM 757 CB THR A 153 17.392 -44.690 -13.790 1.00 70.04 C ANISOU 757 CB THR A 153 12797 7329 6483 587 1550 -168 C ATOM 758 OG1 THR A 153 18.709 -45.254 -13.733 1.00 69.35 O ANISOU 758 OG1 THR A 153 12778 7300 6269 601 1333 -198 O ATOM 759 CG2 THR A 153 16.944 -44.631 -15.235 1.00 69.32 C ANISOU 759 CG2 THR A 153 12293 7531 6513 590 1492 -194 C ATOM 760 N TYR A 154 14.996 -42.886 -12.847 1.00 69.24 N ANISOU 760 N TYR A 154 12821 6838 6647 555 2054 -45 N ATOM 761 CA TYR A 154 13.723 -42.212 -13.103 1.00 69.28 C ANISOU 761 CA TYR A 154 12637 6777 6910 540 2243 -19 C ATOM 762 C TYR A 154 13.772 -40.751 -12.636 1.00 68.87 C ANISOU 762 C TYR A 154 12723 6636 6807 529 2271 97 C ATOM 763 O TYR A 154 13.260 -39.858 -13.316 1.00 68.82 O ANISOU 763 O TYR A 154 12456 6730 6960 516 2242 156 O ATOM 764 CB TYR A 154 12.551 -42.951 -12.434 1.00 71.19 C ANISOU 764 CB TYR A 154 12960 6713 7375 539 2594 -89 C ATOM 765 CG TYR A 154 12.264 -44.327 -13.009 1.00 71.54 C ANISOU 765 CG TYR A 154 12787 6824 7570 548 2574 -211 C ATOM 766 CD1 TYR A 154 11.797 -44.476 -14.309 1.00 71.42 C ANISOU 766 CD1 TYR A 154 12340 7032 7764 551 2409 -270 C ATOM 767 CD2 TYR A 154 12.450 -45.480 -12.245 1.00 72.54 C ANISOU 767 CD2 TYR A 154 13163 6771 7628 559 2703 -271 C ATOM 768 CE1 TYR A 154 11.536 -45.732 -14.837 1.00 71.96 C ANISOU 768 CE1 TYR A 154 12217 7146 7978 567 2363 -402 C ATOM 769 CE2 TYR A 154 12.193 -46.738 -12.764 1.00 72.37 C ANISOU 769 CE2 TYR A 154 12927 6796 7771 567 2679 -389 C ATOM 770 CZ TYR A 154 11.736 -46.859 -14.060 1.00 72.48 C ANISOU 770 CZ TYR A 154 12499 7035 8005 571 2506 -462 C ATOM 771 OH TYR A 154 11.479 -48.109 -14.581 1.00 73.11 O ANISOU 771 OH TYR A 154 12373 7148 8258 586 2456 -598 O ATOM 772 N ALA A 155 14.398 -40.507 -11.485 1.00 68.27 N ANISOU 772 N ALA A 155 13070 6359 6510 540 2300 127 N ATOM 773 CA ALA A 155 14.520 -39.150 -10.939 1.00 67.53 C ANISOU 773 CA ALA A 155 13153 6148 6355 537 2307 218 C ATOM 774 C ALA A 155 15.209 -38.212 -11.923 1.00 65.20 C ANISOU 774 C ALA A 155 12563 6145 6062 523 2012 307 C ATOM 775 O ALA A 155 14.697 -37.139 -12.220 1.00 65.05 O ANISOU 775 O ALA A 155 12389 6140 6183 508 2051 382 O ATOM 776 CB ALA A 155 15.272 -39.174 -9.617 1.00 68.37 C ANISOU 776 CB ALA A 155 13795 6002 6180 567 2287 212 C ATOM 777 N THR A 156 16.368 -38.633 -12.421 1.00 63.61 N ANISOU 777 N THR A 156 12285 6154 5729 530 1740 304 N ATOM 778 CA THR A 156 17.087 -37.906 -13.468 1.00 62.56 C ANISOU 778 CA THR A 156 11857 6302 5608 521 1504 396 C ATOM 779 C THR A 156 16.228 -37.758 -14.734 1.00 62.92 C ANISOU 779 C THR A 156 11514 6570 5822 513 1535 419 C ATOM 780 O THR A 156 16.161 -36.681 -15.336 1.00 62.76 O ANISOU 780 O THR A 156 11315 6661 5870 504 1468 531 O ATOM 781 CB THR A 156 18.419 -38.608 -13.817 1.00 61.25 C ANISOU 781 CB THR A 156 11654 6294 5322 534 1271 368 C ATOM 782 OG1 THR A 156 19.367 -38.391 -12.766 1.00 60.21 O ANISOU 782 OG1 THR A 156 11843 5955 5077 544 1138 375 O ATOM 783 CG2 THR A 156 19.001 -38.074 -15.127 1.00 61.45 C ANISOU 783 CG2 THR A 156 11332 6629 5386 530 1117 458 C ATOM 784 N ALA A 157 15.576 -38.845 -15.125 1.00 63.18 N ANISOU 784 N ALA A 157 11429 6645 5929 523 1612 312 N ATOM 785 CA ALA A 157 14.691 -38.836 -16.277 1.00 63.88 C ANISOU 785 CA ALA A 157 11184 6899 6187 528 1594 304 C ATOM 786 C ALA A 157 13.560 -37.840 -16.089 1.00 64.25 C ANISOU 786 C ALA A 157 11165 6782 6463 511 1735 366 C ATOM 787 O ALA A 157 13.302 -37.022 -16.968 1.00 64.51 O ANISOU 787 O ALA A 157 10973 6960 6576 512 1619 453 O ATOM 788 CB ALA A 157 14.128 -40.230 -16.523 1.00 64.81 C ANISOU 788 CB ALA A 157 11215 7013 6394 544 1648 152 C ATOM 789 N LEU A 158 12.897 -37.909 -14.940 1.00 65.10 N ANISOU 789 N LEU A 158 11485 6571 6678 500 1999 324 N ATOM 790 CA LEU A 158 11.773 -37.019 -14.641 1.00 67.52 C ANISOU 790 CA LEU A 158 11733 6666 7253 485 2193 365 C ATOM 791 C LEU A 158 12.210 -35.576 -14.330 1.00 67.96 C ANISOU 791 C LEU A 158 11889 6695 7235 472 2142 495 C ATOM 792 O LEU A 158 11.448 -34.631 -14.558 1.00 68.60 O ANISOU 792 O LEU A 158 11805 6714 7545 461 2191 559 O ATOM 793 CB LEU A 158 10.939 -37.585 -13.487 1.00 69.06 C ANISOU 793 CB LEU A 158 12150 6498 7591 483 2560 279 C ATOM 794 CG LEU A 158 10.293 -38.950 -13.769 1.00 70.11 C ANISOU 794 CG LEU A 158 12133 6596 7906 491 2650 153 C ATOM 795 CD1 LEU A 158 9.680 -39.548 -12.510 1.00 71.23 C ANISOU 795 CD1 LEU A 158 12562 6358 8144 492 3056 92 C ATOM 796 CD2 LEU A 158 9.254 -38.852 -14.882 1.00 71.28 C ANISOU 796 CD2 LEU A 158 11836 6818 8427 491 2561 128 C ATOM 797 N ASN A 159 13.427 -35.403 -13.820 1.00 67.53 N ANISOU 797 N ASN A 159 12086 6668 6904 477 2021 530 N ATOM 798 CA ASN A 159 13.950 -34.066 -13.558 1.00 67.87 C ANISOU 798 CA ASN A 159 12205 6680 6899 468 1930 645 C ATOM 799 C ASN A 159 14.220 -33.324 -14.858 1.00 67.01 C ANISOU 799 C ASN A 159 11749 6863 6848 460 1705 769 C ATOM 800 O ASN A 159 13.687 -32.241 -15.086 1.00 67.63 O ANISOU 800 O ASN A 159 11692 6908 7096 448 1720 860 O ATOM 801 CB ASN A 159 15.219 -34.124 -12.698 1.00 68.18 C ANISOU 801 CB ASN A 159 12586 6640 6676 481 1806 636 C ATOM 802 CG ASN A 159 14.910 -34.139 -11.213 1.00 69.70 C ANISOU 802 CG ASN A 159 13231 6464 6785 499 2025 568 C ATOM 803 OD1 ASN A 159 14.260 -33.228 -10.705 1.00 71.96 O ANISOU 803 OD1 ASN A 159 13609 6553 7177 496 2194 595 O ATOM 804 ND2 ASN A 159 15.374 -35.169 -10.509 1.00 69.65 N ANISOU 804 ND2 ASN A 159 13532 6349 6580 522 2032 481 N ATOM 805 N VAL A 160 15.046 -33.924 -15.706 1.00 65.80 N ANISOU 805 N VAL A 160 11469 6978 6552 472 1514 774 N ATOM 806 CA VAL A 160 15.361 -33.367 -17.020 1.00 65.08 C ANISOU 806 CA VAL A 160 11096 7170 6461 478 1332 897 C ATOM 807 C VAL A 160 14.086 -33.008 -17.783 1.00 65.72 C ANISOU 807 C VAL A 160 10935 7279 6754 481 1356 925 C ATOM 808 O VAL A 160 13.991 -31.932 -18.367 1.00 66.51 O ANISOU 808 O VAL A 160 10891 7451 6928 477 1268 1066 O ATOM 809 CB VAL A 160 16.235 -34.350 -17.833 1.00 64.19 C ANISOU 809 CB VAL A 160 10906 7314 6169 501 1200 857 C ATOM 810 CG1 VAL A 160 16.181 -34.058 -19.321 1.00 65.01 C ANISOU 810 CG1 VAL A 160 10752 7697 6251 525 1075 952 C ATOM 811 CG2 VAL A 160 17.671 -34.303 -17.334 1.00 63.59 C ANISOU 811 CG2 VAL A 160 10975 7224 5960 497 1107 884 C ATOM 812 N ALA A 161 13.107 -33.902 -17.759 1.00 66.12 N ANISOU 812 N ALA A 161 10938 7246 6937 489 1459 792 N ATOM 813 CA ALA A 161 11.829 -33.670 -18.425 1.00 67.41 C ANISOU 813 CA ALA A 161 10855 7380 7377 496 1448 792 C ATOM 814 C ALA A 161 11.054 -32.518 -17.797 1.00 68.11 C ANISOU 814 C ALA A 161 10934 7215 7726 470 1592 859 C ATOM 815 O ALA A 161 10.583 -31.632 -18.505 1.00 68.13 O ANISOU 815 O ALA A 161 10734 7263 7886 473 1473 963 O ATOM 816 CB ALA A 161 10.990 -34.936 -18.394 1.00 68.64 C ANISOU 816 CB ALA A 161 10950 7441 7688 509 1538 618 C ATOM 817 N SER A 162 10.915 -32.544 -16.471 1.00 68.95 N ANISOU 817 N SER A 162 11283 7040 7872 451 1850 797 N ATOM 818 CA SER A 162 10.218 -31.477 -15.736 1.00 70.33 C ANISOU 818 CA SER A 162 11499 6939 8282 432 2041 840 C ATOM 819 C SER A 162 10.869 -30.112 -15.996 1.00 70.11 C ANISOU 819 C SER A 162 11441 7013 8183 422 1870 1005 C ATOM 820 O SER A 162 10.189 -29.132 -16.312 1.00 71.75 O ANISOU 820 O SER A 162 11460 7154 8644 413 1856 1088 O ATOM 821 CB SER A 162 10.189 -31.780 -14.229 1.00 70.45 C ANISOU 821 CB SER A 162 11887 6643 8235 429 2354 746 C ATOM 822 OG SER A 162 11.439 -31.512 -13.611 1.00 68.90 O ANISOU 822 OG SER A 162 11995 6508 7674 436 2250 758 O ATOM 823 N LEU A 163 12.194 -30.082 -15.876 1.00 68.54 N ANISOU 823 N LEU A 163 11407 6955 7680 425 1734 1051 N ATOM 824 CA LEU A 163 13.018 -28.897 -16.136 1.00 67.44 C ANISOU 824 CA LEU A 163 11231 6912 7480 416 1563 1211 C ATOM 825 C LEU A 163 12.767 -28.261 -17.504 1.00 66.67 C ANISOU 825 C LEU A 163 10810 7032 7488 420 1382 1358 C ATOM 826 O LEU A 163 12.787 -27.049 -17.645 1.00 66.91 O ANISOU 826 O LEU A 163 10755 7033 7632 408 1325 1496 O ATOM 827 CB LEU A 163 14.485 -29.301 -16.017 1.00 67.02 C ANISOU 827 CB LEU A 163 11331 6990 7143 423 1423 1216 C ATOM 828 CG LEU A 163 15.572 -28.285 -16.324 1.00 67.85 C ANISOU 828 CG LEU A 163 11378 7195 7208 416 1242 1374 C ATOM 829 CD1 LEU A 163 15.396 -27.029 -15.493 1.00 69.19 C ANISOU 829 CD1 LEU A 163 11651 7116 7523 401 1290 1423 C ATOM 830 CD2 LEU A 163 16.917 -28.930 -16.044 1.00 67.98 C ANISOU 830 CD2 LEU A 163 11541 7266 7022 425 1129 1333 C ATOM 831 N SER A 164 12.547 -29.088 -18.514 1.00 66.02 N ANISOU 831 N SER A 164 10574 7157 7351 444 1279 1329 N ATOM 832 CA SER A 164 12.196 -28.599 -19.833 1.00 65.88 C ANISOU 832 CA SER A 164 10314 7323 7394 465 1090 1455 C ATOM 833 C SER A 164 10.766 -28.082 -19.865 1.00 66.57 C ANISOU 833 C SER A 164 10230 7212 7851 460 1125 1448 C ATOM 834 O SER A 164 10.507 -27.047 -20.460 1.00 67.59 O ANISOU 834 O SER A 164 10212 7363 8104 463 999 1599 O ATOM 835 CB SER A 164 12.361 -29.704 -20.868 1.00 66.26 C ANISOU 835 CB SER A 164 10301 7624 7250 507 953 1395 C ATOM 836 OG SER A 164 11.803 -29.315 -22.106 1.00 68.34 O ANISOU 836 OG SER A 164 10384 8017 7563 543 757 1492 O ATOM 837 N VAL A 165 9.838 -28.805 -19.241 1.00 66.87 N ANISOU 837 N VAL A 165 10272 7035 8099 455 1301 1280 N ATOM 838 CA VAL A 165 8.439 -28.360 -19.172 1.00 68.67 C ANISOU 838 CA VAL A 165 10305 7013 8773 448 1374 1255 C ATOM 839 C VAL A 165 8.356 -27.051 -18.400 1.00 69.14 C ANISOU 839 C VAL A 165 10413 6861 8994 417 1513 1345 C ATOM 840 O VAL A 165 7.550 -26.177 -18.724 1.00 70.65 O ANISOU 840 O VAL A 165 10397 6936 9511 413 1460 1419 O ATOM 841 CB VAL A 165 7.519 -29.406 -18.499 1.00 69.18 C ANISOU 841 CB VAL A 165 10371 6832 9081 445 1617 1057 C ATOM 842 CG1 VAL A 165 6.130 -28.835 -18.230 1.00 70.87 C ANISOU 842 CG1 VAL A 165 10377 6715 9834 432 1764 1032 C ATOM 843 CG2 VAL A 165 7.398 -30.642 -19.371 1.00 69.65 C ANISOU 843 CG2 VAL A 165 10321 7068 9074 479 1440 957 C ATOM 844 N GLU A 166 9.206 -26.927 -17.385 1.00 84.71 N ANISOU 844 N GLU A 166 10938 10213 11035 1402 329 10 N ATOM 845 CA GLU A 166 9.265 -25.732 -16.559 1.00 83.41 C ANISOU 845 CA GLU A 166 10342 10576 10773 1580 -225 -169 C ATOM 846 C GLU A 166 9.719 -24.517 -17.381 1.00 79.69 C ANISOU 846 C GLU A 166 9525 10190 10563 1152 -594 -512 C ATOM 847 O GLU A 166 9.062 -23.479 -17.368 1.00 77.56 O ANISOU 847 O GLU A 166 9108 9946 10415 876 -813 -668 O ATOM 848 CB GLU A 166 10.192 -25.980 -15.363 1.00 88.57 C ANISOU 848 CB GLU A 166 10807 11806 11038 2439 -280 -57 C ATOM 849 CG GLU A 166 10.027 -24.993 -14.220 1.00 90.45 C ANISOU 849 CG GLU A 166 10675 12647 11043 2660 -741 -337 C ATOM 850 CD GLU A 166 11.096 -23.920 -14.220 1.00 92.04 C ANISOU 850 CD GLU A 166 10236 13346 11387 2453 -1212 -947 C ATOM 851 OE1 GLU A 166 12.240 -24.227 -13.819 1.00 97.92 O ANISOU 851 OE1 GLU A 166 10555 14796 11854 2972 -1384 -1130 O ATOM 852 OE2 GLU A 166 10.791 -22.773 -14.612 1.00 89.24 O ANISOU 852 OE2 GLU A 166 9771 12699 11435 1811 -1319 -1259 O ATOM 853 N ARG A 167 10.782 -24.670 -18.143 1.00 79.39 N ANISOU 853 N ARG A 167 9410 10105 10649 1147 -508 -571 N ATOM 854 CA ARG A 167 11.261 -23.589 -18.969 1.00 77.68 C ANISOU 854 CA ARG A 167 8952 9805 10758 783 -610 -843 C ATOM 855 C ARG A 167 10.405 -23.333 -20.194 1.00 75.21 C ANISOU 855 C ARG A 167 8952 9115 10507 345 -503 -724 C ATOM 856 O ARG A 167 10.485 -22.298 -20.795 1.00 75.22 O ANISOU 856 O ARG A 167 8858 9001 10720 178 -466 -810 O ATOM 857 CB ARG A 167 12.700 -23.830 -19.363 1.00 80.03 C ANISOU 857 CB ARG A 167 9025 10173 11208 943 -472 -948 C ATOM 858 CG ARG A 167 13.629 -23.847 -18.177 1.00 84.63 C ANISOU 858 CG ARG A 167 9051 11468 11634 1462 -700 -1184 C ATOM 859 CD ARG A 167 14.883 -23.035 -18.416 1.00 88.43 C ANISOU 859 CD ARG A 167 8847 12241 12509 1293 -768 -1763 C ATOM 860 NE ARG A 167 16.054 -23.893 -18.526 1.00 92.39 N ANISOU 860 NE ARG A 167 9107 12953 13042 1633 -602 -1691 N ATOM 861 CZ ARG A 167 17.308 -23.490 -18.356 1.00 98.05 C ANISOU 861 CZ ARG A 167 9017 14195 14040 1644 -674 -2252 C ATOM 862 NH1 ARG A 167 17.571 -22.224 -18.059 1.00100.78 N ANISOU 862 NH1 ARG A 167 8725 14858 14708 1233 -848 -3052 N ATOM 863 NH2 ARG A 167 18.304 -24.358 -18.491 1.00101.69 N ANISOU 863 NH2 ARG A 167 9261 14863 14510 2039 -487 -2080 N ATOM 864 N TYR A 168 9.580 -24.279 -20.574 1.00 74.64 N ANISOU 864 N TYR A 168 9222 8905 10231 199 -375 -567 N ATOM 865 CA TYR A 168 8.606 -24.047 -21.643 1.00 74.18 C ANISOU 865 CA TYR A 168 9292 8840 10053 -145 -413 -571 C ATOM 866 C TYR A 168 7.585 -23.011 -21.205 1.00 74.48 C ANISOU 866 C TYR A 168 9105 9107 10084 -131 -665 -530 C ATOM 867 O TYR A 168 7.272 -22.087 -21.953 1.00 75.21 O ANISOU 867 O TYR A 168 9151 9289 10134 -120 -701 -437 O ATOM 868 CB TYR A 168 7.880 -25.332 -22.041 1.00 75.27 C ANISOU 868 CB TYR A 168 9691 8890 10016 -442 -190 -667 C ATOM 869 CG TYR A 168 6.783 -25.113 -23.066 1.00 76.44 C ANISOU 869 CG TYR A 168 9768 9376 9900 -774 -364 -837 C ATOM 870 CD1 TYR A 168 5.495 -24.777 -22.671 1.00 77.01 C ANISOU 870 CD1 TYR A 168 9557 9799 9902 -865 -592 -883 C ATOM 871 CD2 TYR A 168 7.032 -25.241 -24.428 1.00 78.37 C ANISOU 871 CD2 TYR A 168 10172 9719 9883 -915 -310 -957 C ATOM 872 CE1 TYR A 168 4.487 -24.577 -23.602 1.00 80.04 C ANISOU 872 CE1 TYR A 168 9710 10762 9938 -1051 -823 -1065 C ATOM 873 CE2 TYR A 168 6.028 -25.043 -25.365 1.00 81.42 C ANISOU 873 CE2 TYR A 168 10397 10706 9830 -1074 -551 -1151 C ATOM 874 CZ TYR A 168 4.761 -24.710 -24.944 1.00 82.51 C ANISOU 874 CZ TYR A 168 10143 11328 9879 -1123 -839 -1213 C ATOM 875 OH TYR A 168 3.758 -24.503 -25.855 1.00 87.47 O ANISOU 875 OH TYR A 168 10451 12804 9978 -1167 -1147 -1426 O ATOM 876 N LEU A 169 7.061 -23.176 -19.994 1.00 75.32 N ANISOU 876 N LEU A 169 9124 9292 10201 -24 -736 -525 N ATOM 877 CA LEU A 169 6.063 -22.250 -19.458 1.00 75.92 C ANISOU 877 CA LEU A 169 9012 9538 10296 18 -899 -466 C ATOM 878 C LEU A 169 6.647 -20.849 -19.277 1.00 76.26 C ANISOU 878 C LEU A 169 8894 9519 10561 154 -894 -525 C ATOM 879 O LEU A 169 6.040 -19.860 -19.695 1.00 77.07 O ANISOU 879 O LEU A 169 8956 9617 10709 193 -821 -374 O ATOM 880 CB LEU A 169 5.514 -22.755 -18.119 1.00 76.38 C ANISOU 880 CB LEU A 169 9077 9623 10318 162 -868 -442 C ATOM 881 CG LEU A 169 4.781 -24.101 -18.122 1.00 78.47 C ANISOU 881 CG LEU A 169 9521 9756 10537 -26 -587 -432 C ATOM 882 CD1 LEU A 169 4.301 -24.424 -16.713 1.00 79.65 C ANISOU 882 CD1 LEU A 169 9750 9834 10677 264 -390 -301 C ATOM 883 CD2 LEU A 169 3.619 -24.118 -19.108 1.00 80.04 C ANISOU 883 CD2 LEU A 169 9541 10169 10701 -455 -657 -569 C ATOM 884 N ALA A 170 7.830 -20.782 -18.666 1.00 77.00 N ANISOU 884 N ALA A 170 8861 9595 10798 251 -883 -780 N ATOM 885 CA ALA A 170 8.505 -19.516 -18.390 1.00 78.99 C ANISOU 885 CA ALA A 170 8866 9760 11385 213 -751 -1101 C ATOM 886 C ALA A 170 8.592 -18.622 -19.621 1.00 81.43 C ANISOU 886 C ALA A 170 9292 9692 11956 108 -368 -957 C ATOM 887 O ALA A 170 8.419 -17.404 -19.525 1.00 84.06 O ANISOU 887 O ALA A 170 9587 9765 12586 94 -21 -1021 O ATOM 888 CB ALA A 170 9.898 -19.778 -17.848 1.00 80.66 C ANISOU 888 CB ALA A 170 8762 10210 11674 281 -829 -1527 C ATOM 889 N ILE A 171 8.841 -19.238 -20.774 1.00 82.33 N ANISOU 889 N ILE A 171 9614 9734 11933 99 -310 -732 N ATOM 890 CA ILE A 171 9.152 -18.509 -21.998 1.00 85.43 C ANISOU 890 CA ILE A 171 10186 9791 12480 154 141 -537 C ATOM 891 C ILE A 171 8.010 -18.463 -23.024 1.00 87.66 C ANISOU 891 C ILE A 171 10724 10289 12293 395 123 -44 C ATOM 892 O ILE A 171 7.959 -17.537 -23.827 1.00 91.75 O ANISOU 892 O ILE A 171 11421 10602 12837 688 588 274 O ATOM 893 CB ILE A 171 10.452 -19.070 -22.615 1.00 85.91 C ANISOU 893 CB ILE A 171 10271 9674 12695 59 305 -685 C ATOM 894 CG1 ILE A 171 11.615 -18.815 -21.640 1.00 87.37 C ANISOU 894 CG1 ILE A 171 9992 9856 13348 -96 347 -1251 C ATOM 895 CG2 ILE A 171 10.740 -18.447 -23.975 1.00 88.83 C ANISOU 895 CG2 ILE A 171 10940 9661 13149 200 869 -395 C ATOM 896 CD1 ILE A 171 12.928 -19.464 -22.023 1.00 88.66 C ANISOU 896 CD1 ILE A 171 10012 9995 13678 -128 452 -1422 C ATOM 897 N CYS A 172 7.099 -19.435 -23.002 1.00 88.17 N ANISOU 897 N CYS A 172 10766 10814 11918 320 -327 -12 N ATOM 898 CA CYS A 172 5.974 -19.460 -23.954 1.00 92.74 C ANISOU 898 CA CYS A 172 11371 11910 11953 520 -470 264 C ATOM 899 C CYS A 172 4.610 -19.146 -23.344 1.00 94.42 C ANISOU 899 C CYS A 172 11312 12531 12030 636 -700 388 C ATOM 900 O CYS A 172 3.656 -18.906 -24.079 1.00 97.22 O ANISOU 900 O CYS A 172 11533 13485 11918 940 -817 635 O ATOM 901 CB CYS A 172 5.897 -20.817 -24.648 1.00 94.33 C ANISOU 901 CB CYS A 172 11645 12426 11769 226 -710 13 C ATOM 902 SG CYS A 172 7.409 -21.261 -25.530 1.00 96.88 S ANISOU 902 SG CYS A 172 12330 12299 12181 161 -376 -57 S ATOM 903 N HIS A 173 4.513 -19.173 -22.016 1.00 94.30 N ANISOU 903 N HIS A 173 11177 12302 12349 469 -768 218 N ATOM 904 CA HIS A 173 3.266 -18.878 -21.309 1.00 97.06 C ANISOU 904 CA HIS A 173 11290 12930 12656 572 -897 340 C ATOM 905 C HIS A 173 3.590 -18.116 -20.027 1.00 97.18 C ANISOU 905 C HIS A 173 11330 12500 13092 610 -690 257 C ATOM 906 O HIS A 173 3.377 -18.636 -18.931 1.00 96.98 O ANISOU 906 O HIS A 173 11243 12478 13126 473 -846 65 O ATOM 907 CB HIS A 173 2.526 -20.176 -20.958 1.00 97.37 C ANISOU 907 CB HIS A 173 11159 13275 12560 216 -1185 71 C ATOM 908 CG HIS A 173 1.873 -20.847 -22.128 1.00102.24 C ANISOU 908 CG HIS A 173 11586 14511 12747 60 -1389 -69 C ATOM 909 ND1 HIS A 173 2.568 -21.634 -23.022 1.00103.57 N ANISOU 909 ND1 HIS A 173 11955 14659 12737 -176 -1374 -313 N ATOM 910 CD2 HIS A 173 0.582 -20.867 -22.535 1.00106.73 C ANISOU 910 CD2 HIS A 173 11704 15854 12994 89 -1619 -112 C ATOM 911 CE1 HIS A 173 1.736 -22.099 -23.937 1.00108.30 C ANISOU 911 CE1 HIS A 173 12264 15999 12885 -333 -1594 -575 C ATOM 912 NE2 HIS A 173 0.524 -21.650 -23.663 1.00110.90 N ANISOU 912 NE2 HIS A 173 12129 16899 13108 -173 -1785 -486 N ATOM 913 N PRO A 174 4.117 -16.882 -20.152 1.00100.45 N ANISOU 913 N PRO A 174 11858 12510 13795 801 -230 351 N ATOM 914 CA PRO A 174 4.614 -16.164 -18.971 1.00101.32 C ANISOU 914 CA PRO A 174 11944 12224 14328 682 17 -1 C ATOM 915 C PRO A 174 3.519 -15.591 -18.051 1.00103.53 C ANISOU 915 C PRO A 174 12166 12538 14630 845 98 132 C ATOM 916 O PRO A 174 3.812 -15.220 -16.909 1.00101.92 O ANISOU 916 O PRO A 174 11931 12152 14640 707 193 -276 O ATOM 917 CB PRO A 174 5.472 -15.035 -19.575 1.00104.35 C ANISOU 917 CB PRO A 174 12470 12040 15135 724 718 -36 C ATOM 918 CG PRO A 174 5.487 -15.261 -21.057 1.00104.93 C ANISOU 918 CG PRO A 174 12723 12223 14920 986 798 423 C ATOM 919 CD PRO A 174 4.263 -16.063 -21.365 1.00103.89 C ANISOU 919 CD PRO A 174 12473 12811 14186 1159 223 743 C ATOM 920 N PHE A 175 2.282 -15.510 -18.549 1.00107.33 N ANISOU 920 N PHE A 175 12580 13351 14846 1166 58 651 N ATOM 921 CA PHE A 175 1.133 -15.103 -17.727 1.00109.57 C ANISOU 921 CA PHE A 175 12758 13726 15145 1361 132 849 C ATOM 922 C PHE A 175 0.858 -16.152 -16.648 1.00107.51 C ANISOU 922 C PHE A 175 12394 13656 14798 1085 -289 542 C ATOM 923 O PHE A 175 0.910 -15.853 -15.450 1.00107.15 O ANISOU 923 O PHE A 175 12431 13391 14890 1062 -167 310 O ATOM 924 CB PHE A 175 -0.126 -14.903 -18.589 1.00112.58 C ANISOU 924 CB PHE A 175 12917 14664 15193 1838 112 1457 C ATOM 925 CG PHE A 175 -0.247 -13.530 -19.197 1.00117.08 C ANISOU 925 CG PHE A 175 13675 14975 15833 2461 825 2016 C ATOM 926 CD1 PHE A 175 0.702 -13.065 -20.099 0.00118.10 C ANISOU 926 CD1 PHE A 175 14104 14728 16038 2603 1268 2120 C ATOM 927 CD2 PHE A 175 -1.327 -12.706 -18.882 0.00120.68 C ANISOU 927 CD2 PHE A 175 14048 15502 16303 2990 1206 2515 C ATOM 928 CE1 PHE A 175 0.584 -11.804 -20.664 0.00123.77 C ANISOU 928 CE1 PHE A 175 15106 15067 16855 3292 2181 2737 C ATOM 929 CE2 PHE A 175 -1.450 -11.446 -19.447 0.00126.01 C ANISOU 929 CE2 PHE A 175 14984 15853 17041 3721 2077 3161 C ATOM 930 CZ PHE A 175 -0.493 -10.996 -20.338 0.00127.97 C ANISOU 930 CZ PHE A 175 15599 15650 17371 3890 2617 3289 C ATOM 931 N LYS A 176 0.569 -17.372 -17.057 1.00106.85 N ANISOU 931 N LYS A 176 12168 13954 14474 902 -668 519 N ATOM 932 CA LYS A 176 0.391 -18.401 -16.074 1.00105.85 C ANISOU 932 CA LYS A 176 12045 13856 14318 701 -817 309 C ATOM 933 C LYS A 176 1.622 -18.327 -15.217 1.00105.88 C ANISOU 933 C LYS A 176 12286 13592 14349 700 -807 -11 C ATOM 934 O LYS A 176 1.585 -17.945 -14.049 1.00107.54 O ANISOU 934 O LYS A 176 12582 13763 14514 846 -743 -93 O ATOM 935 CB LYS A 176 0.320 -19.767 -16.739 1.00105.40 C ANISOU 935 CB LYS A 176 11870 14060 14115 395 -990 194 C ATOM 936 CG LYS A 176 -0.923 -19.990 -17.594 0.00 20.00 C ATOM 937 CD LYS A 176 -1.106 -21.463 -17.956 0.00 20.00 C ATOM 938 CE LYS A 176 -2.379 -21.723 -18.755 0.00 20.00 C ATOM 939 NZ LYS A 176 -2.584 -23.175 -19.023 0.00 20.00 N ATOM 940 N ALA A 177 2.737 -18.681 -15.824 1.00105.90 N ANISOU 940 N ALA A 177 12347 13518 14372 604 -864 -202 N ATOM 941 CA ALA A 177 3.976 -18.835 -15.056 1.00106.49 C ANISOU 941 CA ALA A 177 12458 13589 14413 653 -929 -583 C ATOM 942 C ALA A 177 4.066 -17.855 -13.886 1.00109.57 C ANISOU 942 C ALA A 177 12792 13985 14854 764 -831 -902 C ATOM 943 O ALA A 177 4.478 -18.235 -12.789 1.00110.99 O ANISOU 943 O ALA A 177 12958 14451 14758 974 -975 -1161 O ATOM 944 CB ALA A 177 5.185 -18.682 -15.966 1.00106.19 C ANISOU 944 CB ALA A 177 12369 13455 14521 503 -910 -770 C ATOM 945 N LYS A 178 3.673 -16.604 -14.120 1.00112.93 N ANISOU 945 N LYS A 178 13208 14124 15573 695 -508 -880 N ATOM 946 CA LYS A 178 3.706 -15.582 -13.075 1.00117.44 C ANISOU 946 CA LYS A 178 13766 14588 16266 694 -255 -1295 C ATOM 947 C LYS A 178 2.744 -15.939 -11.945 1.00118.93 C ANISOU 947 C LYS A 178 14065 14963 16157 956 -346 -1131 C ATOM 948 O LYS A 178 3.175 -16.261 -10.835 1.00121.09 O ANISOU 948 O LYS A 178 14333 15581 16093 1115 -535 -1508 O ATOM 949 CB LYS A 178 3.357 -14.194 -13.637 1.00119.83 C ANISOU 949 CB LYS A 178 14157 14350 17020 638 383 -1166 C ATOM 950 CG LYS A 178 3.584 -13.048 -12.649 0.00124.05 C ANISOU 950 CG LYS A 178 14708 14607 17817 476 860 -1801 C ATOM 951 CD LYS A 178 2.352 -12.165 -12.455 0.00125.26 C ANISOU 951 CD LYS A 178 15093 14357 18142 721 1428 -1347 C ATOM 952 CE LYS A 178 1.997 -11.358 -13.696 0.00126.59 C ANISOU 952 CE LYS A 178 15419 14018 18661 943 2097 -711 C ATOM 953 NZ LYS A 178 3.061 -10.391 -14.081 0.00130.64 N ANISOU 953 NZ LYS A 178 16012 13888 19738 627 2872 -1222 N ATOM 954 N THR A 179 1.446 -15.902 -12.244 1.00118.70 N ANISOU 954 N THR A 179 14095 14798 16204 1074 -194 -560 N ATOM 955 CA THR A 179 0.406 -16.028 -11.223 1.00120.06 C ANISOU 955 CA THR A 179 14365 15008 16243 1303 -92 -371 C ATOM 956 C THR A 179 0.227 -17.467 -10.743 1.00118.76 C ANISOU 956 C THR A 179 14276 15075 15773 1444 -302 -229 C ATOM 957 O THR A 179 0.135 -17.720 -9.537 1.00121.41 O ANISOU 957 O THR A 179 14796 15507 15827 1737 -228 -309 O ATOM 958 CB THR A 179 -0.949 -15.508 -11.744 1.00120.62 C ANISOU 958 CB THR A 179 14336 14949 16543 1419 185 186 C ATOM 959 OG1 THR A 179 -1.259 -16.142 -12.992 1.00118.77 O ANISOU 959 OG1 THR A 179 13870 14963 16295 1332 -44 498 O ATOM 960 CG2 THR A 179 -0.910 -13.993 -11.936 1.00123.42 C ANISOU 960 CG2 THR A 179 14776 14916 17202 1491 705 186 C ATOM 961 N LEU A 180 0.188 -18.403 -11.688 1.00115.14 N ANISOU 961 N LEU A 180 13724 14667 15354 1272 -440 -29 N ATOM 962 CA LEU A 180 -0.095 -19.803 -11.385 1.00113.74 C ANISOU 962 CA LEU A 180 13671 14493 15050 1336 -348 121 C ATOM 963 C LEU A 180 1.184 -20.641 -11.225 1.00112.98 C ANISOU 963 C LEU A 180 13753 14505 14667 1508 -460 -36 C ATOM 964 O LEU A 180 1.277 -21.750 -11.754 1.00111.83 O ANISOU 964 O LEU A 180 13689 14242 14556 1397 -330 76 O ATOM 965 CB LEU A 180 -1.015 -20.399 -12.466 1.00113.96 C ANISOU 965 CB LEU A 180 13444 14527 15326 969 -297 285 C ATOM 966 CG LEU A 180 -2.297 -19.614 -12.796 1.00114.74 C ANISOU 966 CG LEU A 180 13187 14781 15628 922 -254 485 C ATOM 967 CD1 LEU A 180 -3.040 -20.237 -13.969 1.00115.50 C ANISOU 967 CD1 LEU A 180 12847 15219 15817 558 -354 441 C ATOM 968 CD2 LEU A 180 -3.209 -19.512 -11.581 1.00116.74 C ANISOU 968 CD2 LEU A 180 13514 14873 15968 1152 94 646 C ATOM 969 N MET A 181 2.167 -20.104 -10.501 1.00141.38 N ANISOU 969 N MET A 181 18360 12474 22884 3492 -14 -263 N ATOM 970 CA MET A 181 3.302 -20.899 -10.019 1.00138.32 C ANISOU 970 CA MET A 181 18254 12328 21970 3326 198 -333 C ATOM 971 C MET A 181 4.076 -20.154 -8.936 1.00136.09 C ANISOU 971 C MET A 181 18125 11901 21680 3454 304 -661 C ATOM 972 O MET A 181 4.176 -18.926 -8.963 1.00136.96 O ANISOU 972 O MET A 181 18217 11665 22157 3572 102 -720 O ATOM 973 CB MET A 181 4.271 -21.266 -11.148 1.00138.54 C ANISOU 973 CB MET A 181 18513 12414 21711 3035 -13 18 C ATOM 974 CG MET A 181 3.665 -22.209 -12.186 0.00137.31 C ANISOU 974 CG MET A 181 18546 12610 21013 2845 215 13 C ATOM 975 SD MET A 181 3.109 -23.800 -11.537 0.00138.34 S ANISOU 975 SD MET A 181 19028 12731 20804 2618 132 123 S ATOM 976 CE MET A 181 4.663 -24.566 -11.059 0.00139.18 C ANISOU 976 CE MET A 181 19142 12570 21167 2509 -280 537 C ATOM 977 N SER A 182 4.626 -20.915 -7.994 1.00131.34 N ANISOU 977 N SER A 182 17680 11555 20667 3433 601 -873 N ATOM 978 CA SER A 182 5.453 -20.366 -6.923 1.00129.94 C ANISOU 978 CA SER A 182 17682 11288 20399 3545 692 -1206 C ATOM 979 C SER A 182 6.454 -21.416 -6.451 1.00124.51 C ANISOU 979 C SER A 182 17250 10901 19157 3388 883 -1247 C ATOM 980 O SER A 182 6.455 -22.548 -6.942 1.00123.59 O ANISOU 980 O SER A 182 17157 11045 18755 3202 959 -1025 O ATOM 981 CB SER A 182 4.577 -19.917 -5.751 1.00133.40 C ANISOU 981 CB SER A 182 17959 11692 21033 3869 919 -1599 C ATOM 982 OG SER A 182 4.045 -21.028 -5.048 1.00132.44 O ANISOU 982 OG SER A 182 17790 11928 20601 3908 1292 -1699 O ATOM 983 N ARG A 183 7.296 -21.035 -5.492 1.00121.66 N ANISOU 983 N ARG A 183 17073 10490 18660 3473 939 -1545 N ATOM 984 CA ARG A 183 8.295 -21.948 -4.921 1.00117.20 C ANISOU 984 CA ARG A 183 16756 10187 17587 3358 1096 -1620 C ATOM 985 C ARG A 183 7.688 -23.024 -3.992 1.00115.86 C ANISOU 985 C ARG A 183 16573 10364 17081 3457 1477 -1765 C ATOM 986 O ARG A 183 8.379 -23.967 -3.593 1.00112.71 O ANISOU 986 O ARG A 183 16367 10210 16246 3355 1617 -1771 O ATOM 987 CB ARG A 183 9.384 -21.147 -4.197 1.00117.15 C ANISOU 987 CB ARG A 183 16940 9997 17571 3428 988 -1905 C ATOM 988 CG ARG A 183 8.909 -20.449 -2.934 0.00120.31 C ANISOU 988 CG ARG A 183 17313 10315 18084 3753 1120 -2352 C ATOM 989 CD ARG A 183 9.499 -19.055 -2.785 0.00121.84 C ANISOU 989 CD ARG A 183 17547 10109 18637 3844 843 -2561 C ATOM 990 NE ARG A 183 9.002 -18.409 -1.575 0.00124.54 N ANISOU 990 NE ARG A 183 17866 10381 19071 4179 969 -3027 N ATOM 991 CZ ARG A 183 7.777 -17.906 -1.427 0.00127.71 C ANISOU 991 CZ ARG A 183 18041 10688 19795 4409 1059 -3142 C ATOM 992 NH1 ARG A 183 6.887 -17.951 -2.415 0.00127.38 N ANISOU 992 NH1 ARG A 183 17762 10595 20041 4343 1007 -2820 N ATOM 993 NH2 ARG A 183 7.436 -17.346 -0.274 0.00131.73 N ANISOU 993 NH2 ARG A 183 18556 11156 20339 4723 1194 -3601 N ATOM 994 N SER A 184 6.407 -22.870 -3.648 1.00117.37 N ANISOU 994 N SER A 184 16531 10566 17496 3658 1649 -1870 N ATOM 995 CA SER A 184 5.648 -23.914 -2.952 1.00115.96 C ANISOU 995 CA SER A 184 16282 10706 17070 3725 2031 -1924 C ATOM 996 C SER A 184 5.302 -25.050 -3.908 1.00111.76 C ANISOU 996 C SER A 184 15653 10354 16457 3483 2036 -1557 C ATOM 997 O SER A 184 5.714 -26.191 -3.696 1.00110.07 O ANISOU 997 O SER A 184 15581 10395 15845 3348 2200 -1479 O ATOM 998 CB SER A 184 4.358 -23.342 -2.350 1.00120.23 C ANISOU 998 CB SER A 184 16559 11189 17933 4013 2223 -2145 C ATOM 999 OG SER A 184 3.462 -24.379 -1.984 1.00120.71 O ANISOU 999 OG SER A 184 16473 11535 17856 4028 2579 -2092 O ATOM 1000 N ARG A 185 4.547 -24.725 -4.957 1.00110.70 N ANISOU 1000 N ARG A 185 15280 10070 16708 3438 1833 -1343 N ATOM 1001 CA ARG A 185 4.145 -25.706 -5.971 1.00107.94 C ANISOU 1001 CA ARG A 185 14822 9859 16328 3222 1775 -1015 C ATOM 1002 C ARG A 185 5.343 -26.410 -6.604 1.00103.90 C ANISOU 1002 C ARG A 185 14573 9454 15450 2952 1640 -812 C ATOM 1003 O ARG A 185 5.247 -27.576 -6.972 1.00100.62 O ANISOU 1003 O ARG A 185 14155 9247 14826 2787 1717 -641 O ATOM 1004 CB ARG A 185 3.281 -25.048 -7.053 1.00108.89 C ANISOU 1004 CB ARG A 185 14683 9766 16925 3235 1491 -830 C ATOM 1005 CG ARG A 185 1.811 -24.965 -6.673 1.00111.84 C ANISOU 1005 CG ARG A 185 14703 10140 17648 3434 1670 -937 C ATOM 1006 CD ARG A 185 1.180 -23.650 -7.097 1.00115.11 C ANISOU 1006 CD ARG A 185 14909 10229 18596 3606 1411 -959 C ATOM 1007 NE ARG A 185 -0.094 -23.421 -6.413 1.00118.50 N ANISOU 1007 NE ARG A 185 15011 10651 19361 3857 1645 -1165 N ATOM 1008 CZ ARG A 185 -0.742 -22.257 -6.368 1.00121.55 C ANISOU 1008 CZ ARG A 185 15190 10764 20228 4090 1524 -1300 C ATOM 1009 NH1 ARG A 185 -0.254 -21.174 -6.969 1.00121.93 N ANISOU 1009 NH1 ARG A 185 15331 10498 20498 4102 1154 -1233 N ATOM 1010 NH2 ARG A 185 -1.894 -22.173 -5.712 1.00124.82 N ANISOU 1010 NH2 ARG A 185 15290 11211 20925 4317 1786 -1497 N ATOM 1011 N THR A 186 6.460 -25.695 -6.720 1.00103.73 N ANISOU 1011 N THR A 186 14758 9274 15379 2911 1444 -842 N ATOM 1012 CA THR A 186 7.717 -26.270 -7.196 1.00100.95 C ANISOU 1012 CA THR A 186 14651 9015 14688 2679 1346 -692 C ATOM 1013 C THR A 186 8.138 -27.455 -6.345 1.00100.01 C ANISOU 1013 C THR A 186 14686 9182 14131 2642 1625 -795 C ATOM 1014 O THR A 186 8.426 -28.529 -6.870 1.00 99.13 O ANISOU 1014 O THR A 186 14638 9249 13775 2451 1640 -608 O ATOM 1015 CB THR A 186 8.853 -25.229 -7.172 1.00100.66 C ANISOU 1015 CB THR A 186 14784 8749 14713 2674 1143 -770 C ATOM 1016 OG1 THR A 186 8.545 -24.174 -8.091 1.00102.50 O ANISOU 1016 OG1 THR A 186 14895 8699 15349 2675 863 -607 O ATOM 1017 CG2 THR A 186 10.197 -25.861 -7.550 1.00 96.91 C ANISOU 1017 CG2 THR A 186 14539 8388 13892 2444 1085 -644 C ATOM 1018 N LYS A 187 8.178 -27.261 -5.034 1.00102.26 N ANISOU 1018 N LYS A 187 15040 9505 14306 2837 1837 -1095 N ATOM 1019 CA LYS A 187 8.580 -28.336 -4.133 1.00102.09 C ANISOU 1019 CA LYS A 187 15190 9748 13851 2827 2100 -1185 C ATOM 1020 C LYS A 187 7.504 -29.416 -4.035 1.00100.94 C ANISOU 1020 C LYS A 187 14880 9813 13658 2812 2365 -1075 C ATOM 1021 O LYS A 187 7.811 -30.570 -3.749 1.00 98.65 O ANISOU 1021 O LYS A 187 14709 9735 13037 2713 2528 -1009 O ATOM 1022 CB LYS A 187 8.954 -27.779 -2.762 1.00106.16 C ANISOU 1022 CB LYS A 187 15856 10252 14226 3054 2229 -1540 C ATOM 1023 CG LYS A 187 10.216 -26.927 -2.814 0.00107.59 C ANISOU 1023 CG LYS A 187 16219 10238 14422 3027 1956 -1651 C ATOM 1024 CD LYS A 187 10.635 -26.420 -1.444 0.00111.34 C ANISOU 1024 CD LYS A 187 16860 10705 14737 3256 2043 -2036 C ATOM 1025 CE LYS A 187 11.939 -25.639 -1.524 0.00111.71 C ANISOU 1025 CE LYS A 187 17063 10542 14837 3202 1746 -2146 C ATOM 1026 NZ LYS A 187 12.274 -24.986 -0.228 0.00115.10 N ANISOU 1026 NZ LYS A 187 17639 10922 15171 3448 1770 -2564 N ATOM 1027 N LYS A 188 6.253 -29.039 -4.289 1.00102.40 N ANISOU 1027 N LYS A 188 14778 9919 14209 2906 2396 -1048 N ATOM 1028 CA LYS A 188 5.179 -30.013 -4.485 1.00102.72 C ANISOU 1028 CA LYS A 188 14597 10111 14317 2847 2581 -895 C ATOM 1029 C LYS A 188 5.434 -30.830 -5.758 1.00 99.29 C ANISOU 1029 C LYS A 188 14169 9721 13836 2574 2365 -598 C ATOM 1030 O LYS A 188 5.198 -32.039 -5.785 1.00 98.20 O ANISOU 1030 O LYS A 188 14005 9759 13546 2453 2514 -481 O ATOM 1031 CB LYS A 188 3.817 -29.308 -4.567 1.00106.57 C ANISOU 1031 CB LYS A 188 14742 10474 15275 3014 2610 -942 C ATOM 1032 CG LYS A 188 2.611 -30.238 -4.485 1.00108.17 C ANISOU 1032 CG LYS A 188 14670 10829 15598 2994 2866 -844 C ATOM 1033 CD LYS A 188 1.295 -29.474 -4.546 1.00112.09 C ANISOU 1033 CD LYS A 188 14798 11190 16600 3175 2885 -912 C ATOM 1034 CE LYS A 188 0.942 -29.058 -5.968 1.00112.18 C ANISOU 1034 CE LYS A 188 14635 11013 16974 3074 2470 -705 C ATOM 1035 NZ LYS A 188 -0.190 -28.088 -6.006 1.00116.15 N ANISOU 1035 NZ LYS A 188 14801 11332 17996 3285 2425 -798 N ATOM 1036 N PHE A 189 5.919 -30.154 -6.798 1.00 97.98 N ANISOU 1036 N PHE A 189 14042 9386 13797 2484 2018 -479 N ATOM 1037 CA PHE A 189 6.243 -30.773 -8.091 1.00 95.48 C ANISOU 1037 CA PHE A 189 13761 9107 13408 2245 1786 -214 C ATOM 1038 C PHE A 189 7.437 -31.725 -7.976 1.00 91.37 C ANISOU 1038 C PHE A 189 13513 8752 12451 2087 1843 -186 C ATOM 1039 O PHE A 189 7.434 -32.810 -8.564 1.00 88.45 O ANISOU 1039 O PHE A 189 13148 8516 11943 1920 1832 -32 O ATOM 1040 CB PHE A 189 6.562 -29.675 -9.120 1.00 96.85 C ANISOU 1040 CB PHE A 189 13946 9059 13790 2213 1432 -93 C ATOM 1041 CG PHE A 189 6.207 -30.026 -10.541 1.00 97.66 C ANISOU 1041 CG PHE A 189 13962 9170 13972 2051 1180 180 C ATOM 1042 CD1 PHE A 189 6.928 -30.989 -11.244 1.00 94.88 C ANISOU 1042 CD1 PHE A 189 13772 8972 13305 1839 1115 330 C ATOM 1043 CD2 PHE A 189 5.175 -29.353 -11.197 1.00100.87 C ANISOU 1043 CD2 PHE A 189 14133 9424 14766 2127 983 276 C ATOM 1044 CE1 PHE A 189 6.611 -31.293 -12.558 1.00 94.91 C ANISOU 1044 CE1 PHE A 189 13719 8995 13344 1708 870 556 C ATOM 1045 CE2 PHE A 189 4.856 -29.654 -12.512 1.00101.10 C ANISOU 1045 CE2 PHE A 189 14106 9469 14838 1993 716 520 C ATOM 1046 CZ PHE A 189 5.575 -30.626 -13.193 1.00 98.08 C ANISOU 1046 CZ PHE A 189 13903 9257 14104 1785 662 654 C ATOM 1047 N ILE A 190 8.457 -31.313 -7.224 1.00 89.83 N ANISOU 1047 N ILE A 190 13533 8533 12063 2149 1885 -351 N ATOM 1048 CA ILE A 190 9.682 -32.104 -7.080 1.00 86.54 C ANISOU 1048 CA ILE A 190 13367 8248 11263 2021 1910 -343 C ATOM 1049 C ILE A 190 9.460 -33.316 -6.179 1.00 86.12 C ANISOU 1049 C ILE A 190 13358 8408 10955 2037 2209 -393 C ATOM 1050 O ILE A 190 9.915 -34.410 -6.500 1.00 83.95 O ANISOU 1050 O ILE A 190 13176 8261 10458 1880 2220 -277 O ATOM 1051 CB ILE A 190 10.856 -31.247 -6.568 1.00 86.18 C ANISOU 1051 CB ILE A 190 13517 8092 11133 2082 1823 -511 C ATOM 1052 CG1 ILE A 190 11.219 -30.197 -7.621 1.00 87.12 C ANISOU 1052 CG1 ILE A 190 13608 7995 11498 2009 1523 -389 C ATOM 1053 CG2 ILE A 190 12.076 -32.110 -6.277 1.00 83.30 C ANISOU 1053 CG2 ILE A 190 13385 7872 10391 1976 1862 -529 C ATOM 1054 CD1 ILE A 190 12.033 -29.037 -7.090 1.00 88.66 C ANISOU 1054 CD1 ILE A 190 13905 7996 11783 2104 1420 -575 C ATOM 1055 N SER A 191 8.759 -33.133 -5.063 1.00 88.49 N ANISOU 1055 N SER A 191 13592 8741 11288 2230 2461 -559 N ATOM 1056 CA SER A 191 8.346 -34.268 -4.234 1.00 88.64 C ANISOU 1056 CA SER A 191 13622 8956 11100 2248 2779 -556 C ATOM 1057 C SER A 191 7.706 -35.360 -5.084 1.00 88.21 C ANISOU 1057 C SER A 191 13406 8972 11136 2062 2778 -323 C ATOM 1058 O SER A 191 8.039 -36.537 -4.946 1.00 86.64 O ANISOU 1058 O SER A 191 13313 8905 10701 1949 2881 -238 O ATOM 1059 CB SER A 191 7.355 -33.826 -3.168 1.00 91.61 C ANISOU 1059 CB SER A 191 13867 9353 11587 2480 3063 -723 C ATOM 1060 OG SER A 191 7.966 -32.912 -2.289 1.00 93.46 O ANISOU 1060 OG SER A 191 14277 9535 11698 2666 3067 -978 O ATOM 1061 N ALA A 192 6.802 -34.953 -5.973 1.00 89.65 N ANISOU 1061 N ALA A 192 13334 9051 11678 2037 2631 -228 N ATOM 1062 CA ALA A 192 6.069 -35.885 -6.830 1.00 89.86 C ANISOU 1062 CA ALA A 192 13172 9121 11847 1875 2583 -36 C ATOM 1063 C ALA A 192 6.970 -36.741 -7.730 1.00 87.50 C ANISOU 1063 C ALA A 192 13044 8879 11322 1657 2389 100 C ATOM 1064 O ALA A 192 6.628 -37.882 -8.030 1.00 87.59 O ANISOU 1064 O ALA A 192 12988 8971 11320 1527 2433 208 O ATOM 1065 CB ALA A 192 5.048 -35.133 -7.673 1.00 91.61 C ANISOU 1065 CB ALA A 192 13111 9204 12493 1908 2387 23 C ATOM 1066 N ILE A 193 8.112 -36.201 -8.154 1.00 86.01 N ANISOU 1066 N ILE A 193 13061 8640 10976 1618 2182 88 N ATOM 1067 CA ILE A 193 9.012 -36.932 -9.064 1.00 83.17 C ANISOU 1067 CA ILE A 193 12855 8340 10404 1426 2009 203 C ATOM 1068 C ILE A 193 10.103 -37.751 -8.363 1.00 79.77 C ANISOU 1068 C ILE A 193 12667 8023 9617 1390 2146 141 C ATOM 1069 O ILE A 193 10.896 -38.405 -9.028 1.00 78.39 O ANISOU 1069 O ILE A 193 12616 7902 9267 1247 2029 212 O ATOM 1070 CB ILE A 193 9.637 -36.008 -10.144 1.00 83.19 C ANISOU 1070 CB ILE A 193 12920 8237 10451 1370 1706 277 C ATOM 1071 CG1 ILE A 193 10.638 -35.017 -9.528 1.00 83.63 C ANISOU 1071 CG1 ILE A 193 13141 8206 10426 1462 1700 147 C ATOM 1072 CG2 ILE A 193 8.533 -35.301 -10.922 1.00 85.43 C ANISOU 1072 CG2 ILE A 193 12972 8405 11079 1404 1533 371 C ATOM 1073 CD1 ILE A 193 11.025 -33.858 -10.429 1.00 84.46 C ANISOU 1073 CD1 ILE A 193 13257 8155 10679 1435 1440 232 C ATOM 1074 N TRP A 194 10.162 -37.713 -7.039 1.00 78.79 N ANISOU 1074 N TRP A 194 12619 7939 9376 1530 2383 6 N ATOM 1075 CA TRP A 194 10.902 -38.735 -6.306 1.00 76.72 C ANISOU 1075 CA TRP A 194 12555 7799 8796 1504 2533 -18 C ATOM 1076 C TRP A 194 9.896 -39.774 -5.844 1.00 77.95 C ANISOU 1076 C TRP A 194 12585 8036 8995 1492 2782 60 C ATOM 1077 O TRP A 194 10.109 -40.971 -6.006 1.00 76.73 O ANISOU 1077 O TRP A 194 12484 7947 8722 1367 2812 156 O ATOM 1078 CB TRP A 194 11.676 -38.138 -5.139 1.00 76.41 C ANISOU 1078 CB TRP A 194 12712 7765 8552 1665 2616 -205 C ATOM 1079 CG TRP A 194 12.775 -37.248 -5.599 1.00 74.78 C ANISOU 1079 CG TRP A 194 12619 7462 8332 1644 2368 -272 C ATOM 1080 CD1 TRP A 194 12.656 -35.953 -6.003 1.00 76.14 C ANISOU 1080 CD1 TRP A 194 12706 7483 8740 1695 2212 -315 C ATOM 1081 CD2 TRP A 194 14.160 -37.580 -5.724 1.00 72.06 C ANISOU 1081 CD2 TRP A 194 12470 7146 7763 1561 2249 -290 C ATOM 1082 NE1 TRP A 194 13.883 -35.450 -6.365 1.00 74.53 N ANISOU 1082 NE1 TRP A 194 12633 7208 8475 1636 2016 -345 N ATOM 1083 CE2 TRP A 194 14.825 -36.430 -6.201 1.00 72.28 C ANISOU 1083 CE2 TRP A 194 12511 7039 7911 1554 2040 -339 C ATOM 1084 CE3 TRP A 194 14.907 -38.730 -5.469 1.00 70.60 C ANISOU 1084 CE3 TRP A 194 12437 7072 7313 1495 2298 -267 C ATOM 1085 CZ2 TRP A 194 16.199 -36.399 -6.430 1.00 70.59 C ANISOU 1085 CZ2 TRP A 194 12437 6811 7570 1476 1898 -367 C ATOM 1086 CZ3 TRP A 194 16.277 -38.698 -5.698 1.00 69.14 C ANISOU 1086 CZ3 TRP A 194 12396 6877 6997 1433 2140 -311 C ATOM 1087 CH2 TRP A 194 16.907 -37.540 -6.174 1.00 69.03 C ANISOU 1087 CH2 TRP A 194 12372 6739 7116 1420 1952 -362 C ATOM 1088 N LEU A 195 8.785 -39.300 -5.289 1.00 80.59 N ANISOU 1088 N LEU A 195 12735 8354 9532 1622 2963 20 N ATOM 1089 CA LEU A 195 7.630 -40.145 -5.006 1.00 82.67 C ANISOU 1089 CA LEU A 195 12796 8669 9945 1596 3202 121 C ATOM 1090 C LEU A 195 7.319 -41.069 -6.185 1.00 81.64 C ANISOU 1090 C LEU A 195 12533 8517 9970 1383 3031 284 C ATOM 1091 O LEU A 195 7.205 -42.278 -6.018 1.00 81.85 O ANISOU 1091 O LEU A 195 12561 8596 9939 1281 3157 380 O ATOM 1092 CB LEU A 195 6.411 -39.272 -4.697 1.00 85.77 C ANISOU 1092 CB LEU A 195 12925 9011 10651 1746 3333 59 C ATOM 1093 CG LEU A 195 5.137 -39.970 -4.226 1.00 88.34 C ANISOU 1093 CG LEU A 195 12997 9389 11179 1749 3642 145 C ATOM 1094 CD1 LEU A 195 5.338 -40.554 -2.836 1.00 89.09 C ANISOU 1094 CD1 LEU A 195 13267 9620 10962 1840 4015 126 C ATOM 1095 CD2 LEU A 195 3.972 -38.991 -4.245 1.00 91.06 C ANISOU 1095 CD2 LEU A 195 13032 9655 11909 1886 3688 76 C ATOM 1096 N ALA A 196 7.197 -40.497 -7.378 1.00 81.42 N ANISOU 1096 N ALA A 196 12400 8404 10130 1321 2730 313 N ATOM 1097 CA ALA A 196 6.882 -41.279 -8.574 1.00 81.18 C ANISOU 1097 CA ALA A 196 12255 8358 10230 1139 2524 436 C ATOM 1098 C ALA A 196 8.049 -42.169 -8.986 1.00 79.42 C ANISOU 1098 C ALA A 196 12275 8192 9707 1003 2415 463 C ATOM 1099 O ALA A 196 7.846 -43.325 -9.360 1.00 79.86 O ANISOU 1099 O ALA A 196 12285 8266 9789 870 2400 535 O ATOM 1100 CB ALA A 196 6.488 -40.367 -9.724 1.00 81.45 C ANISOU 1100 CB ALA A 196 12152 8301 10494 1132 2217 465 C ATOM 1101 N SER A 197 9.263 -41.625 -8.922 1.00 78.23 N ANISOU 1101 N SER A 197 12362 8054 9306 1039 2333 394 N ATOM 1102 CA SER A 197 10.478 -42.378 -9.265 1.00 76.52 C ANISOU 1102 CA SER A 197 12368 7893 8813 932 2241 399 C ATOM 1103 C SER A 197 10.614 -43.643 -8.432 1.00 76.82 C ANISOU 1103 C SER A 197 12488 7990 8708 907 2455 415 C ATOM 1104 O SER A 197 10.852 -44.733 -8.962 1.00 75.44 O ANISOU 1104 O SER A 197 12345 7831 8485 777 2385 467 O ATOM 1105 CB SER A 197 11.722 -41.517 -9.043 1.00 75.25 C ANISOU 1105 CB SER A 197 12415 7726 8449 998 2173 307 C ATOM 1106 OG SER A 197 11.864 -40.560 -10.071 1.00 75.66 O ANISOU 1106 OG SER A 197 12431 7715 8599 970 1938 338 O ATOM 1107 N ALA A 198 10.477 -43.466 -7.118 1.00 78.19 N ANISOU 1107 N ALA A 198 12709 8191 8806 1043 2710 369 N ATOM 1108 CA ALA A 198 10.547 -44.557 -6.152 1.00 77.43 C ANISOU 1108 CA ALA A 198 12709 8151 8558 1047 2947 415 C ATOM 1109 C ALA A 198 9.427 -45.570 -6.386 1.00 78.41 C ANISOU 1109 C ALA A 198 12614 8248 8928 932 3048 549 C ATOM 1110 O ALA A 198 9.650 -46.777 -6.287 1.00 77.45 O ANISOU 1110 O ALA A 198 12560 8128 8739 838 3099 628 O ATOM 1111 CB ALA A 198 10.476 -44.000 -4.737 1.00 78.31 C ANISOU 1111 CB ALA A 198 12910 8315 8529 1239 3202 338 C ATOM 1112 N LEU A 199 8.230 -45.072 -6.698 1.00 79.81 N ANISOU 1112 N LEU A 199 12517 8382 9425 942 3062 572 N ATOM 1113 CA LEU A 199 7.099 -45.937 -7.026 1.00 81.66 C ANISOU 1113 CA LEU A 199 12489 8568 9969 823 3118 687 C ATOM 1114 C LEU A 199 7.427 -46.803 -8.226 1.00 81.19 C ANISOU 1114 C LEU A 199 12441 8465 9941 642 2837 718 C ATOM 1115 O LEU A 199 7.350 -48.027 -8.152 1.00 81.87 O ANISOU 1115 O LEU A 199 12520 8523 10063 532 2901 793 O ATOM 1116 CB LEU A 199 5.831 -45.121 -7.305 1.00 83.36 C ANISOU 1116 CB LEU A 199 12385 8734 10552 874 3113 681 C ATOM 1117 CG LEU A 199 4.912 -44.908 -6.099 1.00 85.83 C ANISOU 1117 CG LEU A 199 12542 9077 10990 1002 3498 699 C ATOM 1118 CD1 LEU A 199 3.890 -43.816 -6.375 1.00 87.50 C ANISOU 1118 CD1 LEU A 199 12466 9236 11541 1099 3456 645 C ATOM 1119 CD2 LEU A 199 4.218 -46.208 -5.724 1.00 87.59 C ANISOU 1119 CD2 LEU A 199 12619 9288 11372 884 3733 848 C ATOM 1120 N LEU A 200 7.817 -46.159 -9.321 1.00 80.86 N ANISOU 1120 N LEU A 200 12430 8416 9877 619 2530 659 N ATOM 1121 CA LEU A 200 8.113 -46.858 -10.574 1.00 80.71 C ANISOU 1121 CA LEU A 200 12432 8379 9855 469 2246 661 C ATOM 1122 C LEU A 200 9.223 -47.907 -10.455 1.00 79.08 C ANISOU 1122 C LEU A 200 12463 8200 9384 404 2257 646 C ATOM 1123 O LEU A 200 9.280 -48.825 -11.271 1.00 79.58 O ANISOU 1123 O LEU A 200 12514 8233 9488 279 2093 642 O ATOM 1124 CB LEU A 200 8.478 -45.856 -11.681 1.00 80.27 C ANISOU 1124 CB LEU A 200 12417 8337 9742 480 1951 619 C ATOM 1125 CG LEU A 200 7.333 -45.012 -12.257 1.00 82.32 C ANISOU 1125 CG LEU A 200 12424 8544 10310 512 1812 648 C ATOM 1126 CD1 LEU A 200 7.879 -43.826 -13.042 1.00 81.57 C ANISOU 1126 CD1 LEU A 200 12432 8457 10103 559 1582 639 C ATOM 1127 CD2 LEU A 200 6.407 -45.856 -13.125 1.00 83.52 C ANISOU 1127 CD2 LEU A 200 12363 8650 10717 387 1635 682 C ATOM 1128 N ALA A 201 10.099 -47.770 -9.461 1.00 77.97 N ANISOU 1128 N ALA A 201 12534 8106 8982 498 2427 621 N ATOM 1129 CA ALA A 201 11.214 -48.707 -9.271 1.00 77.75 C ANISOU 1129 CA ALA A 201 12731 8096 8714 460 2427 603 C ATOM 1130 C ALA A 201 10.853 -49.995 -8.500 1.00 79.73 C ANISOU 1130 C ALA A 201 12967 8296 9028 413 2631 703 C ATOM 1131 O ALA A 201 11.632 -50.950 -8.498 1.00 78.20 O ANISOU 1131 O ALA A 201 12924 8082 8705 364 2593 701 O ATOM 1132 CB ALA A 201 12.375 -47.998 -8.586 1.00 76.32 C ANISOU 1132 CB ALA A 201 12782 7979 8237 585 2471 527 C ATOM 1133 N ILE A 202 9.678 -50.017 -7.864 1.00 83.07 N ANISOU 1133 N ILE A 202 13199 8690 9672 428 2851 798 N ATOM 1134 CA ILE A 202 9.260 -51.131 -6.994 1.00 85.23 C ANISOU 1134 CA ILE A 202 13451 8912 10019 388 3102 937 C ATOM 1135 C ILE A 202 9.331 -52.503 -7.666 1.00 85.86 C ANISOU 1135 C ILE A 202 13504 8879 10237 220 2961 975 C ATOM 1136 O ILE A 202 9.809 -53.457 -7.045 1.00 88.13 O ANISOU 1136 O ILE A 202 13939 9126 10420 204 3072 1054 O ATOM 1137 CB ILE A 202 7.830 -50.915 -6.430 1.00 88.30 C ANISOU 1137 CB ILE A 202 13565 9283 10700 405 3362 1040 C ATOM 1138 CG1 ILE A 202 7.810 -49.761 -5.418 1.00 89.00 C ANISOU 1138 CG1 ILE A 202 13723 9481 10611 602 3582 999 C ATOM 1139 CG2 ILE A 202 7.285 -52.188 -5.786 1.00 90.27 C ANISOU 1139 CG2 ILE A 202 13742 9452 11105 312 3603 1221 C ATOM 1140 CD1 ILE A 202 8.518 -50.044 -4.107 0.00 89.48 C ANISOU 1140 CD1 ILE A 202 14061 9616 10320 714 3824 1046 C ATOM 1141 N PRO A 203 8.856 -52.620 -8.925 1.00 84.28 N ANISOU 1141 N PRO A 203 13126 8623 10272 105 2701 913 N ATOM 1142 CA PRO A 203 8.957 -53.909 -9.609 1.00 83.81 C ANISOU 1142 CA PRO A 203 13051 8448 10343 -41 2536 903 C ATOM 1143 C PRO A 203 10.329 -54.571 -9.489 1.00 81.97 C ANISOU 1143 C PRO A 203 13109 8220 9816 -23 2483 855 C ATOM 1144 O PRO A 203 10.408 -55.797 -9.377 1.00 83.16 O ANISOU 1144 O PRO A 203 13280 8248 10067 -107 2496 906 O ATOM 1145 CB PRO A 203 8.664 -53.547 -11.061 1.00 83.19 C ANISOU 1145 CB PRO A 203 12847 8376 10384 -104 2200 777 C ATOM 1146 CG PRO A 203 7.701 -52.422 -10.955 1.00 84.47 C ANISOU 1146 CG PRO A 203 12804 8579 10709 -41 2262 810 C ATOM 1147 CD PRO A 203 8.093 -51.646 -9.727 1.00 83.96 C ANISOU 1147 CD PRO A 203 12879 8605 10417 111 2544 856 C ATOM 1148 N MET A 204 11.393 -53.770 -9.490 1.00 79.02 N ANISOU 1148 N MET A 204 12941 7967 9115 85 2423 759 N ATOM 1149 CA MET A 204 12.754 -54.304 -9.420 1.00 76.92 C ANISOU 1149 CA MET A 204 12925 7713 8589 114 2355 693 C ATOM 1150 C MET A 204 13.030 -55.066 -8.125 1.00 77.44 C ANISOU 1150 C MET A 204 13125 7726 8571 162 2581 823 C ATOM 1151 O MET A 204 13.848 -55.986 -8.118 1.00 77.80 O ANISOU 1151 O MET A 204 13314 7709 8538 147 2513 804 O ATOM 1152 CB MET A 204 13.790 -53.190 -9.613 1.00 74.48 C ANISOU 1152 CB MET A 204 12769 7537 7992 217 2263 576 C ATOM 1153 CG MET A 204 13.703 -52.479 -10.962 1.00 73.91 C ANISOU 1153 CG MET A 204 12612 7520 7951 171 2031 476 C ATOM 1154 SD MET A 204 13.785 -53.563 -12.410 1.00 73.53 S ANISOU 1154 SD MET A 204 12526 7419 7991 35 1766 373 S ATOM 1155 CE MET A 204 15.498 -54.082 -12.336 1.00 71.90 C ANISOU 1155 CE MET A 204 12573 7249 7497 85 1735 268 C ATOM 1156 N LEU A 205 12.349 -54.698 -7.040 1.00 78.09 N ANISOU 1156 N LEU A 205 13168 7836 8667 229 2850 956 N ATOM 1157 CA LEU A 205 12.454 -55.447 -5.780 1.00 79.51 C ANISOU 1157 CA LEU A 205 13479 7974 8755 275 3091 1121 C ATOM 1158 C LEU A 205 11.904 -56.875 -5.879 1.00 80.72 C ANISOU 1158 C LEU A 205 13528 7944 9197 126 3124 1261 C ATOM 1159 O LEU A 205 12.345 -57.757 -5.148 1.00 80.45 O ANISOU 1159 O LEU A 205 13651 7835 9078 142 3220 1384 O ATOM 1160 CB LEU A 205 11.733 -54.710 -4.647 1.00 81.17 C ANISOU 1160 CB LEU A 205 13658 8275 8905 384 3400 1229 C ATOM 1161 CG LEU A 205 12.331 -53.368 -4.219 1.00 79.88 C ANISOU 1161 CG LEU A 205 13639 8268 8443 559 3400 1096 C ATOM 1162 CD1 LEU A 205 11.305 -52.576 -3.423 1.00 82.01 C ANISOU 1162 CD1 LEU A 205 13791 8613 8756 651 3681 1156 C ATOM 1163 CD2 LEU A 205 13.614 -53.548 -3.414 1.00 78.94 C ANISOU 1163 CD2 LEU A 205 13836 8198 7959 681 3387 1073 C ATOM 1164 N PHE A 206 10.947 -57.093 -6.778 1.00 81.71 N ANISOU 1164 N PHE A 206 13387 7980 9678 -14 3024 1241 N ATOM 1165 CA PHE A 206 10.301 -58.394 -6.942 1.00 83.86 C ANISOU 1165 CA PHE A 206 13511 8047 10302 -173 3033 1356 C ATOM 1166 C PHE A 206 10.747 -59.197 -8.178 1.00 83.67 C ANISOU 1166 C PHE A 206 13483 7905 10403 -280 2693 1187 C ATOM 1167 O PHE A 206 10.622 -60.419 -8.175 1.00 86.64 O ANISOU 1167 O PHE A 206 13827 8085 11006 -385 2674 1260 O ATOM 1168 CB PHE A 206 8.786 -58.205 -6.970 1.00 86.39 C ANISOU 1168 CB PHE A 206 13498 8323 11004 -263 3172 1455 C ATOM 1169 CG PHE A 206 8.230 -57.562 -5.724 1.00 88.17 C ANISOU 1169 CG PHE A 206 13702 8654 11145 -158 3552 1622 C ATOM 1170 CD1 PHE A 206 8.054 -58.306 -4.559 1.00 90.45 C ANISOU 1170 CD1 PHE A 206 14056 8883 11428 -159 3872 1869 C ATOM 1171 CD2 PHE A 206 7.873 -56.216 -5.714 1.00 87.37 C ANISOU 1171 CD2 PHE A 206 13519 8710 10965 -50 3598 1535 C ATOM 1172 CE1 PHE A 206 7.539 -57.721 -3.411 1.00 91.62 C ANISOU 1172 CE1 PHE A 206 14201 9155 11456 -47 4245 2013 C ATOM 1173 CE2 PHE A 206 7.356 -55.629 -4.569 1.00 88.74 C ANISOU 1173 CE2 PHE A 206 13674 8986 11056 64 3955 1655 C ATOM 1174 CZ PHE A 206 7.189 -56.383 -3.417 1.00 90.83 C ANISOU 1174 CZ PHE A 206 14014 9218 11278 69 4288 1888 C ATOM 1175 N THR A 207 11.262 -58.540 -9.221 1.00 81.32 N ANISOU 1175 N THR A 207 13220 7716 9960 -251 2434 968 N ATOM 1176 CA THR A 207 11.700 -59.253 -10.436 1.00 80.48 C ANISOU 1176 CA THR A 207 13125 7531 9921 -331 2123 781 C ATOM 1177 C THR A 207 13.161 -59.678 -10.381 1.00 78.36 C ANISOU 1177 C THR A 207 13125 7278 9369 -252 2046 687 C ATOM 1178 O THR A 207 13.528 -60.672 -10.992 1.00 79.38 O ANISOU 1178 O THR A 207 13280 7283 9597 -310 1872 579 O ATOM 1179 CB THR A 207 11.520 -58.422 -11.724 1.00 80.03 C ANISOU 1179 CB THR A 207 12977 7592 9836 -343 1872 596 C ATOM 1180 OG1 THR A 207 12.516 -57.391 -11.780 1.00 78.04 O ANISOU 1180 OG1 THR A 207 12911 7531 9210 -217 1854 515 O ATOM 1181 CG2 THR A 207 10.111 -57.810 -11.814 1.00 81.61 C ANISOU 1181 CG2 THR A 207 12900 7793 10314 -393 1914 672 C ATOM 1182 N MET A 208 14.000 -58.906 -9.696 1.00 76.78 N ANISOU 1182 N MET A 208 13109 7226 8837 -112 2155 703 N ATOM 1183 CA MET A 208 15.390 -59.302 -9.475 1.00 76.24 C ANISOU 1183 CA MET A 208 13273 7165 8527 -25 2098 631 C ATOM 1184 C MET A 208 15.462 -60.263 -8.298 1.00 78.15 C ANISOU 1184 C MET A 208 13615 7263 8813 -5 2267 826 C ATOM 1185 O MET A 208 14.464 -60.524 -7.618 1.00 79.22 O ANISOU 1185 O MET A 208 13649 7318 9132 -59 2464 1030 O ATOM 1186 CB MET A 208 16.282 -58.097 -9.173 1.00 74.99 C ANISOU 1186 CB MET A 208 13259 7202 8029 113 2122 565 C ATOM 1187 CG MET A 208 16.338 -57.024 -10.247 1.00 74.28 C ANISOU 1187 CG MET A 208 13101 7256 7863 105 1976 413 C ATOM 1188 SD MET A 208 17.062 -57.543 -11.815 1.00 74.17 S ANISOU 1188 SD MET A 208 13100 7250 7831 46 1697 183 S ATOM 1189 CE MET A 208 15.554 -57.891 -12.717 1.00 75.53 C ANISOU 1189 CE MET A 208 13037 7334 8326 -99 1586 185 C ATOM 1190 N GLY A 209 16.655 -60.796 -8.068 1.00 77.97 N ANISOU 1190 N GLY A 209 13786 7208 8628 73 2191 774 N ATOM 1191 CA GLY A 209 16.884 -61.710 -6.962 1.00 79.39 C ANISOU 1191 CA GLY A 209 14102 7251 8811 113 2315 969 C ATOM 1192 C GLY A 209 18.065 -62.623 -7.201 1.00 78.46 C ANISOU 1192 C GLY A 209 14123 7023 8664 159 2131 856 C ATOM 1193 O GLY A 209 18.533 -62.778 -8.326 1.00 76.42 O ANISOU 1193 O GLY A 209 13820 6764 8451 130 1921 622 O ATOM 1194 N LEU A 210 18.542 -63.219 -6.117 1.00 80.02 N ANISOU 1194 N LEU A 210 14494 7133 8775 244 2213 1027 N ATOM 1195 CA LEU A 210 19.685 -64.107 -6.161 1.00 80.22 C ANISOU 1195 CA LEU A 210 14655 7034 8787 315 2043 946 C ATOM 1196 C LEU A 210 19.249 -65.435 -6.758 1.00 82.19 C ANISOU 1196 C LEU A 210 14798 7009 9419 183 1944 946 C ATOM 1197 O LEU A 210 18.085 -65.825 -6.645 1.00 83.76 O ANISOU 1197 O LEU A 210 14865 7079 9881 51 2061 1117 O ATOM 1198 CB LEU A 210 20.247 -64.314 -4.754 1.00 81.78 C ANISOU 1198 CB LEU A 210 15081 7217 8773 457 2145 1156 C ATOM 1199 CG LEU A 210 21.720 -64.710 -4.665 1.00 82.07 C ANISOU 1199 CG LEU A 210 15279 7220 8680 599 1948 1028 C ATOM 1200 CD1 LEU A 210 22.609 -63.625 -5.261 1.00 79.50 C ANISOU 1200 CD1 LEU A 210 14942 7121 8143 675 1828 749 C ATOM 1201 CD2 LEU A 210 22.101 -64.993 -3.216 1.00 84.14 C ANISOU 1201 CD2 LEU A 210 15774 7450 8744 737 2031 1276 C ATOM 1202 N GLN A 211 20.183 -66.122 -7.405 1.00 81.91 N ANISOU 1202 N GLN A 211 14805 6875 9442 221 1726 740 N ATOM 1203 CA GLN A 211 19.889 -67.406 -8.031 1.00 83.80 C ANISOU 1203 CA GLN A 211 14953 6833 10054 115 1591 684 C ATOM 1204 C GLN A 211 21.181 -68.178 -8.259 1.00 83.35 C ANISOU 1204 C GLN A 211 15010 6663 9993 229 1396 507 C ATOM 1205 O GLN A 211 22.204 -67.588 -8.606 1.00 81.49 O ANISOU 1205 O GLN A 211 14833 6616 9513 345 1312 297 O ATOM 1206 CB GLN A 211 19.161 -67.188 -9.359 1.00 83.64 C ANISOU 1206 CB GLN A 211 14728 6852 10197 -15 1479 463 C ATOM 1207 CG GLN A 211 18.616 -68.460 -9.982 1.00 86.85 C ANISOU 1207 CG GLN A 211 15014 6954 11029 -144 1334 398 C ATOM 1208 CD GLN A 211 17.810 -68.206 -11.243 1.00 87.10 C ANISOU 1208 CD GLN A 211 14851 7037 11203 -266 1199 181 C ATOM 1209 OE1 GLN A 211 18.091 -67.284 -11.997 1.00 84.40 O ANISOU 1209 OE1 GLN A 211 14505 6951 10610 -223 1134 -16 O ATOM 1210 NE2 GLN A 211 16.808 -69.041 -11.480 1.00 90.84 N ANISOU 1210 NE2 GLN A 211 15163 7257 12094 -420 1142 224 N ATOM 1211 N ASN A 212 21.136 -69.493 -8.059 1.00 85.26 N ANISOU 1211 N ASN A 212 15271 6588 10537 198 1328 597 N ATOM 1212 CA ASN A 212 22.310 -70.324 -8.294 1.00 85.33 C ANISOU 1212 CA ASN A 212 15367 6450 10602 315 1130 418 C ATOM 1213 C ASN A 212 22.240 -70.991 -9.657 1.00 86.52 C ANISOU 1213 C ASN A 212 15381 6472 11019 242 925 90 C ATOM 1214 O ASN A 212 21.526 -71.977 -9.844 1.00 88.19 O ANISOU 1214 O ASN A 212 15507 6390 11608 123 865 134 O ATOM 1215 CB ASN A 212 22.485 -71.364 -7.197 1.00 87.12 C ANISOU 1215 CB ASN A 212 15730 6391 10980 362 1150 709 C ATOM 1216 CG ASN A 212 23.933 -71.774 -7.030 1.00 86.75 C ANISOU 1216 CG ASN A 212 15821 6296 10843 556 982 579 C ATOM 1217 OD1 ASN A 212 24.584 -72.179 -7.986 1.00 86.17 O ANISOU 1217 OD1 ASN A 212 15686 6170 10885 598 794 251 O ATOM 1218 ND2 ASN A 212 24.451 -71.647 -5.817 1.00 87.50 N ANISOU 1218 ND2 ASN A 212 16102 6421 10723 688 1044 823 N ATOM 1219 N ARG A 213 22.997 -70.434 -10.600 1.00 85.72 N ANISOU 1219 N ARG A 213 15262 6591 10716 317 822 -241 N ATOM 1220 CA ARG A 213 22.971 -70.876 -11.992 1.00 86.84 C ANISOU 1220 CA ARG A 213 15296 6691 11009 272 638 -596 C ATOM 1221 C ARG A 213 24.020 -71.925 -12.319 1.00 88.30 C ANISOU 1221 C ARG A 213 15528 6683 11336 394 462 -830 C ATOM 1222 O ARG A 213 23.929 -72.556 -13.370 1.00 91.56 O ANISOU 1222 O ARG A 213 15864 6990 11931 364 299 -1124 O ATOM 1223 CB ARG A 213 23.132 -69.686 -12.944 1.00 85.00 C ANISOU 1223 CB ARG A 213 15014 6817 10462 281 645 -819 C ATOM 1224 CG ARG A 213 21.833 -69.245 -13.590 1.00 85.39 C ANISOU 1224 CG ARG A 213 14929 6936 10579 120 647 -818 C ATOM 1225 CD ARG A 213 22.072 -68.114 -14.572 1.00 83.93 C ANISOU 1225 CD ARG A 213 14721 7091 10074 143 634 -1023 C ATOM 1226 NE ARG A 213 20.898 -67.855 -15.400 1.00 85.89 N ANISOU 1226 NE ARG A 213 14842 7382 10410 7 562 -1080 N ATOM 1227 CZ ARG A 213 19.763 -67.304 -14.968 1.00 86.99 C ANISOU 1227 CZ ARG A 213 14889 7536 10624 -100 663 -845 C ATOM 1228 NH1 ARG A 213 19.612 -66.948 -13.697 1.00 86.39 N ANISOU 1228 NH1 ARG A 213 14850 7452 10522 -89 866 -536 N ATOM 1229 NH2 ARG A 213 18.759 -67.107 -15.816 1.00 88.62 N ANISOU 1229 NH2 ARG A 213 14964 7775 10932 -210 553 -930 N ATOM 1230 N SER A 214 25.004 -72.110 -11.439 1.00 87.63 N ANISOU 1230 N SER A 214 15568 6552 11174 542 477 -721 N ATOM 1231 CA SER A 214 26.048 -73.124 -11.640 1.00 89.13 C ANISOU 1231 CA SER A 214 15794 6537 11533 681 306 -928 C ATOM 1232 C SER A 214 25.482 -74.442 -12.186 1.00 91.22 C ANISOU 1232 C SER A 214 15987 6433 12238 597 147 -1044 C ATOM 1233 O SER A 214 24.344 -74.807 -11.887 1.00 91.46 O ANISOU 1233 O SER A 214 15971 6269 12509 437 184 -821 O ATOM 1234 CB SER A 214 26.799 -73.386 -10.332 1.00 89.98 C ANISOU 1234 CB SER A 214 16046 6532 11608 819 324 -670 C ATOM 1235 OG SER A 214 25.964 -74.022 -9.380 1.00 92.34 O ANISOU 1235 OG SER A 214 16403 6561 12120 731 383 -294 O ATOM 1236 N ALA A 215 26.279 -75.139 -12.994 1.00 92.56 N ANISOU 1236 N ALA A 215 16133 6504 12530 706 -25 -1409 N ATOM 1237 CA ALA A 215 25.840 -76.378 -13.646 1.00 96.36 C ANISOU 1237 CA ALA A 215 16543 6633 13434 647 -213 -1605 C ATOM 1238 C ALA A 215 25.330 -77.370 -12.606 1.00 99.22 C ANISOU 1238 C ALA A 215 16945 6570 14183 580 -231 -1245 C ATOM 1239 O ALA A 215 24.222 -77.891 -12.726 1.00100.65 O ANISOU 1239 O ALA A 215 17040 6515 14685 404 -265 -1155 O ATOM 1240 CB ALA A 215 26.971 -76.987 -14.463 1.00 97.49 C ANISOU 1240 CB ALA A 215 16679 6730 13630 825 -377 -2041 C ATOM 1241 N ASP A 216 26.144 -77.615 -11.585 1.00100.36 N ANISOU 1241 N ASP A 216 17215 6617 14299 720 -212 -1029 N ATOM 1242 CA ASP A 216 25.681 -78.296 -10.381 1.00103.66 C ANISOU 1242 CA ASP A 216 17715 6709 14962 664 -166 -577 C ATOM 1243 C ASP A 216 24.582 -77.410 -9.794 1.00103.16 C ANISOU 1243 C ASP A 216 17657 6833 14705 510 81 -195 C ATOM 1244 O ASP A 216 24.707 -76.184 -9.804 1.00101.19 O ANISOU 1244 O ASP A 216 17453 6963 14028 561 222 -156 O ATOM 1245 CB ASP A 216 26.847 -78.543 -9.421 1.00104.42 C ANISOU 1245 CB ASP A 216 17970 6736 14966 876 -206 -423 C ATOM 1246 CG ASP A 216 26.385 -78.775 -7.990 1.00106.02 C ANISOU 1246 CG ASP A 216 18312 6767 15201 834 -81 130 C ATOM 1247 OD1 ASP A 216 25.510 -79.640 -7.785 1.00109.45 O ANISOU 1247 OD1 ASP A 216 18716 6849 16020 687 -80 350 O ATOM 1248 OD2 ASP A 216 26.888 -78.089 -7.073 1.00104.20 O ANISOU 1248 OD2 ASP A 216 18224 6756 14611 948 18 346 O ATOM 1249 N GLY A 217 23.529 -78.032 -9.263 1.00105.79 N ANISOU 1249 N GLY A 217 17933 6887 15376 326 139 80 N ATOM 1250 CA GLY A 217 22.403 -77.310 -8.658 1.00105.84 C ANISOU 1250 CA GLY A 217 17915 7036 15262 176 398 449 C ATOM 1251 C GLY A 217 22.809 -76.071 -7.865 1.00103.61 C ANISOU 1251 C GLY A 217 17766 7150 14448 286 594 622 C ATOM 1252 O GLY A 217 22.326 -74.970 -8.131 1.00 99.91 O ANISOU 1252 O GLY A 217 17227 7003 13729 226 722 576 O ATOM 1253 N THR A 218 23.705 -76.250 -6.894 1.00105.18 N ANISOU 1253 N THR A 218 18159 7313 14490 456 592 811 N ATOM 1254 CA THR A 218 24.097 -75.168 -5.991 1.00103.27 C ANISOU 1254 CA THR A 218 18064 7406 13767 571 751 990 C ATOM 1255 C THR A 218 25.569 -75.267 -5.592 1.00103.69 C ANISOU 1255 C THR A 218 18276 7485 13637 813 595 902 C ATOM 1256 O THR A 218 25.986 -76.236 -4.952 1.00107.14 O ANISOU 1256 O THR A 218 18831 7627 14247 899 495 1086 O ATOM 1257 CB THR A 218 23.232 -75.180 -4.714 1.00105.42 C ANISOU 1257 CB THR A 218 18438 7620 13997 498 999 1503 C ATOM 1258 OG1 THR A 218 21.848 -75.241 -5.076 1.00106.29 O ANISOU 1258 OG1 THR A 218 18360 7651 14371 267 1137 1593 O ATOM 1259 CG2 THR A 218 23.473 -73.932 -3.851 1.00103.35 C ANISOU 1259 CG2 THR A 218 18318 7737 13211 611 1172 1640 C ATOM 1260 N HIS A 219 26.344 -74.262 -5.993 1.00100.71 N ANISOU 1260 N HIS A 219 17882 7445 12937 920 567 626 N ATOM 1261 CA HIS A 219 27.728 -74.085 -5.554 1.00100.28 C ANISOU 1261 CA HIS A 219 17945 7481 12673 1147 440 541 C ATOM 1262 C HIS A 219 27.973 -72.580 -5.333 1.00 95.67 C ANISOU 1262 C HIS A 219 17385 7318 11647 1193 559 498 C ATOM 1263 O HIS A 219 27.605 -71.771 -6.187 1.00 92.40 O ANISOU 1263 O HIS A 219 16834 7129 11143 1095 635 296 O ATOM 1264 CB HIS A 219 28.680 -74.657 -6.610 1.00101.97 C ANISOU 1264 CB HIS A 219 18049 7599 13095 1238 219 122 C ATOM 1265 CG HIS A 219 30.128 -74.404 -6.329 1.00103.00 C ANISOU 1265 CG HIS A 219 18236 7842 13056 1465 87 -21 C ATOM 1266 ND1 HIS A 219 30.776 -73.260 -6.742 1.00101.05 N ANISOU 1266 ND1 HIS A 219 17920 7951 12523 1521 121 -261 N ATOM 1267 CD2 HIS A 219 31.056 -75.150 -5.686 1.00105.82 C ANISOU 1267 CD2 HIS A 219 18694 7988 13521 1649 -89 41 C ATOM 1268 CE1 HIS A 219 32.039 -73.308 -6.360 1.00101.49 C ANISOU 1268 CE1 HIS A 219 18014 8014 12532 1722 -24 -349 C ATOM 1269 NE2 HIS A 219 32.236 -74.445 -5.717 1.00104.64 N ANISOU 1269 NE2 HIS A 219 18519 8078 13161 1811 -164 -175 N ATOM 1270 N PRO A 220 28.599 -72.201 -4.197 1.00 95.01 N ANISOU 1270 N PRO A 220 17478 7330 11290 1349 554 682 N ATOM 1271 CA PRO A 220 28.607 -70.796 -3.734 1.00 91.85 C ANISOU 1271 CA PRO A 220 17126 7284 10488 1380 683 711 C ATOM 1272 C PRO A 220 29.155 -69.764 -4.726 1.00 88.04 C ANISOU 1272 C PRO A 220 16487 7081 9881 1381 658 341 C ATOM 1273 O PRO A 220 28.713 -68.610 -4.715 1.00 85.23 O ANISOU 1273 O PRO A 220 16106 6982 9296 1322 802 348 O ATOM 1274 CB PRO A 220 29.496 -70.836 -2.482 1.00 93.45 C ANISOU 1274 CB PRO A 220 17545 7481 10480 1589 578 882 C ATOM 1275 CG PRO A 220 29.536 -72.264 -2.068 1.00 97.19 C ANISOU 1275 CG PRO A 220 18116 7585 11224 1628 469 1090 C ATOM 1276 CD PRO A 220 29.449 -73.049 -3.341 1.00 97.53 C ANISOU 1276 CD PRO A 220 17960 7428 11667 1527 383 830 C ATOM 1277 N GLY A 221 30.110 -70.177 -5.561 1.00 87.17 N ANISOU 1277 N GLY A 221 16273 6917 9929 1452 489 32 N ATOM 1278 CA GLY A 221 30.688 -69.308 -6.592 1.00 83.39 C ANISOU 1278 CA GLY A 221 15639 6691 9354 1450 484 -307 C ATOM 1279 C GLY A 221 29.895 -69.158 -7.883 1.00 80.61 C ANISOU 1279 C GLY A 221 15130 6406 9089 1277 566 -483 C ATOM 1280 O GLY A 221 30.425 -68.648 -8.866 1.00 78.90 O ANISOU 1280 O GLY A 221 14793 6368 8815 1281 554 -767 O ATOM 1281 N GLY A 222 28.637 -69.600 -7.892 1.00 80.20 N ANISOU 1281 N GLY A 222 15077 6214 9180 1129 645 -310 N ATOM 1282 CA GLY A 222 27.762 -69.446 -9.056 1.00 78.78 C ANISOU 1282 CA GLY A 222 14755 6093 9085 965 692 -461 C ATOM 1283 C GLY A 222 26.443 -68.752 -8.769 1.00 77.29 C ANISOU 1283 C GLY A 222 14549 6000 8815 816 867 -232 C ATOM 1284 O GLY A 222 25.529 -68.794 -9.591 1.00 76.54 O ANISOU 1284 O GLY A 222 14337 5895 8847 672 882 -303 O ATOM 1285 N LEU A 223 26.333 -68.119 -7.603 1.00 76.91 N ANISOU 1285 N LEU A 223 14615 6047 8560 862 990 26 N ATOM 1286 CA LEU A 223 25.176 -67.285 -7.287 1.00 75.99 C ANISOU 1286 CA LEU A 223 14471 6063 8335 751 1180 216 C ATOM 1287 C LEU A 223 25.263 -65.985 -8.069 1.00 72.78 C ANISOU 1287 C LEU A 223 13970 5951 7730 728 1207 17 C ATOM 1288 O LEU A 223 26.325 -65.372 -8.137 1.00 69.86 O ANISOU 1288 O LEU A 223 13628 5737 7178 837 1150 -133 O ATOM 1289 CB LEU A 223 25.118 -66.974 -5.793 1.00 76.86 C ANISOU 1289 CB LEU A 223 14752 6206 8243 837 1308 520 C ATOM 1290 CG LEU A 223 24.677 -68.132 -4.900 1.00 80.13 C ANISOU 1290 CG LEU A 223 15271 6344 8829 827 1352 827 C ATOM 1291 CD1 LEU A 223 25.143 -67.914 -3.466 1.00 81.45 C ANISOU 1291 CD1 LEU A 223 15663 6566 8715 986 1406 1063 C ATOM 1292 CD2 LEU A 223 23.165 -68.307 -4.954 1.00 81.23 C ANISOU 1292 CD2 LEU A 223 15298 6398 9167 640 1531 1021 C ATOM 1293 N VAL A 224 24.144 -65.572 -8.657 1.00 73.02 N ANISOU 1293 N VAL A 224 13879 6042 7821 583 1285 27 N ATOM 1294 CA VAL A 224 24.093 -64.345 -9.455 1.00 72.06 C ANISOU 1294 CA VAL A 224 13670 6179 7530 550 1304 -126 C ATOM 1295 C VAL A 224 22.842 -63.533 -9.145 1.00 72.51 C ANISOU 1295 C VAL A 224 13666 6324 7558 458 1462 55 C ATOM 1296 O VAL A 224 21.806 -64.088 -8.776 1.00 74.43 O ANISOU 1296 O VAL A 224 13868 6418 7993 369 1544 239 O ATOM 1297 CB VAL A 224 24.128 -64.627 -10.978 1.00 71.93 C ANISOU 1297 CB VAL A 224 13536 6178 7616 481 1171 -402 C ATOM 1298 CG1 VAL A 224 25.428 -65.314 -11.371 1.00 72.42 C ANISOU 1298 CG1 VAL A 224 13635 6185 7693 590 1038 -625 C ATOM 1299 CG2 VAL A 224 22.920 -65.446 -11.423 1.00 73.47 C ANISOU 1299 CG2 VAL A 224 13631 6185 8098 338 1136 -367 C ATOM 1300 N CYS A 225 22.959 -62.216 -9.289 1.00 71.39 N ANISOU 1300 N CYS A 225 13506 6411 7205 481 1509 4 N ATOM 1301 CA CYS A 225 21.805 -61.325 -9.259 1.00 71.92 C ANISOU 1301 CA CYS A 225 13484 6577 7265 403 1632 115 C ATOM 1302 C CYS A 225 21.316 -61.202 -10.694 1.00 70.71 C ANISOU 1302 C CYS A 225 13183 6469 7213 291 1525 -48 C ATOM 1303 O CYS A 225 22.110 -60.925 -11.603 1.00 69.66 O ANISOU 1303 O CYS A 225 13049 6446 6970 315 1416 -252 O ATOM 1304 CB CYS A 225 22.189 -59.947 -8.697 1.00 71.73 C ANISOU 1304 CB CYS A 225 13518 6750 6983 494 1711 132 C ATOM 1305 SG CYS A 225 20.890 -58.684 -8.757 1.00 71.63 S ANISOU 1305 SG CYS A 225 13382 6863 6968 427 1842 224 S ATOM 1306 N THR A 226 20.018 -61.419 -10.894 1.00 70.61 N ANISOU 1306 N THR A 226 13044 6375 7409 172 1555 42 N ATOM 1307 CA THR A 226 19.447 -61.477 -12.234 1.00 70.96 C ANISOU 1307 CA THR A 226 12955 6434 7571 68 1411 -112 C ATOM 1308 C THR A 226 17.925 -61.471 -12.164 1.00 71.47 C ANISOU 1308 C THR A 226 12856 6420 7879 -49 1468 31 C ATOM 1309 O THR A 226 17.360 -61.758 -11.115 1.00 71.77 O ANISOU 1309 O THR A 226 12880 6349 8039 -63 1632 247 O ATOM 1310 CB THR A 226 19.914 -62.754 -12.972 1.00 72.96 C ANISOU 1310 CB THR A 226 13220 6536 7962 50 1239 -300 C ATOM 1311 OG1 THR A 226 19.545 -62.691 -14.359 1.00 73.67 O ANISOU 1311 OG1 THR A 226 13219 6691 8079 -19 1073 -499 O ATOM 1312 CG2 THR A 226 19.320 -64.011 -12.323 1.00 74.96 C ANISOU 1312 CG2 THR A 226 13447 6507 8528 -11 1263 -157 C ATOM 1313 N PRO A 227 17.253 -61.113 -13.272 1.00 71.78 N ANISOU 1313 N PRO A 227 12764 6523 7985 -128 1336 -80 N ATOM 1314 CA PRO A 227 15.812 -61.296 -13.268 1.00 73.97 C ANISOU 1314 CA PRO A 227 12848 6688 8566 -246 1352 30 C ATOM 1315 C PRO A 227 15.482 -62.757 -13.056 1.00 77.20 C ANISOU 1315 C PRO A 227 13210 6824 9296 -329 1321 66 C ATOM 1316 O PRO A 227 15.744 -63.597 -13.925 1.00 78.73 O ANISOU 1316 O PRO A 227 13406 6918 9589 -364 1114 -134 O ATOM 1317 CB PRO A 227 15.366 -60.816 -14.657 1.00 73.73 C ANISOU 1317 CB PRO A 227 12716 6766 8530 -298 1138 -143 C ATOM 1318 CG PRO A 227 16.615 -60.557 -15.420 1.00 72.55 C ANISOU 1318 CG PRO A 227 12724 6773 8068 -215 1031 -342 C ATOM 1319 CD PRO A 227 17.687 -60.297 -14.412 1.00 70.67 C ANISOU 1319 CD PRO A 227 12640 6583 7628 -104 1202 -262 C ATOM 1320 N ILE A 228 14.920 -63.035 -11.887 1.00 78.67 N ANISOU 1320 N ILE A 228 13360 6890 9638 -355 1537 322 N ATOM 1321 CA ILE A 228 14.607 -64.387 -11.463 1.00 81.31 C ANISOU 1321 CA ILE A 228 13658 6940 10297 -438 1557 432 C ATOM 1322 C ILE A 228 13.111 -64.651 -11.606 1.00 83.95 C ANISOU 1322 C ILE A 228 13723 7130 11043 -599 1576 534 C ATOM 1323 O ILE A 228 12.485 -65.225 -10.723 1.00 86.44 O ANISOU 1323 O ILE A 228 13963 7272 11605 -669 1766 781 O ATOM 1324 CB ILE A 228 15.056 -64.621 -10.006 1.00 81.85 C ANISOU 1324 CB ILE A 228 13888 6960 10252 -356 1801 688 C ATOM 1325 CG1 ILE A 228 14.501 -63.539 -9.074 1.00 81.56 C ANISOU 1325 CG1 ILE A 228 13831 7093 10063 -310 2071 895 C ATOM 1326 CG2 ILE A 228 16.572 -64.628 -9.921 1.00 80.25 C ANISOU 1326 CG2 ILE A 228 13922 6837 9732 -206 1722 563 C ATOM 1327 CD1 ILE A 228 14.366 -63.987 -7.640 1.00 83.99 C ANISOU 1327 CD1 ILE A 228 14232 7308 10372 -280 2341 1204 C ATOM 1328 N VAL A 229 12.540 -64.216 -12.724 1.00 84.67 N ANISOU 1328 N VAL A 229 13663 7296 11209 -657 1377 351 N ATOM 1329 CA VAL A 229 11.115 -64.393 -12.997 1.00 87.84 C ANISOU 1329 CA VAL A 229 13775 7570 12029 -807 1340 406 C ATOM 1330 C VAL A 229 10.959 -64.588 -14.508 1.00 89.01 C ANISOU 1330 C VAL A 229 13845 7712 12262 -859 968 96 C ATOM 1331 O VAL A 229 11.871 -64.260 -15.279 1.00 86.75 O ANISOU 1331 O VAL A 229 13729 7591 11639 -764 808 -122 O ATOM 1332 CB VAL A 229 10.270 -63.181 -12.518 1.00 87.97 C ANISOU 1332 CB VAL A 229 13653 7754 12018 -790 1542 572 C ATOM 1333 CG1 VAL A 229 8.789 -63.537 -12.459 1.00 91.28 C ANISOU 1333 CG1 VAL A 229 13741 7997 12942 -946 1582 694 C ATOM 1334 CG2 VAL A 229 10.726 -62.683 -11.154 1.00 86.59 C ANISOU 1334 CG2 VAL A 229 13639 7685 11575 -675 1880 798 C ATOM 1335 N ASP A 230 9.816 -65.134 -14.923 1.00 92.64 N ANISOU 1335 N ASP A 230 14047 7982 13169 -1006 832 76 N ATOM 1336 CA ASP A 230 9.585 -65.492 -16.330 1.00 94.89 C ANISOU 1336 CA ASP A 230 14259 8226 13566 -1058 442 -235 C ATOM 1337 C ASP A 230 9.717 -64.316 -17.292 1.00 92.74 C ANISOU 1337 C ASP A 230 14044 8257 12937 -970 276 -398 C ATOM 1338 O ASP A 230 9.533 -63.155 -16.918 1.00 91.52 O ANISOU 1338 O ASP A 230 13873 8294 12605 -912 439 -250 O ATOM 1339 CB ASP A 230 8.217 -66.172 -16.518 1.00 99.18 C ANISOU 1339 CB ASP A 230 14475 8507 14699 -1237 318 -214 C ATOM 1340 CG ASP A 230 7.047 -65.254 -16.194 1.00 99.80 C ANISOU 1340 CG ASP A 230 14298 8670 14951 -1282 452 -25 C ATOM 1341 OD1 ASP A 230 7.171 -64.429 -15.265 1.00 97.37 O ANISOU 1341 OD1 ASP A 230 14047 8518 14430 -1203 775 199 O ATOM 1342 OD2 ASP A 230 5.999 -65.371 -16.863 1.00102.82 O ANISOU 1342 OD2 ASP A 230 14413 8954 15698 -1389 223 -119 O ATOM 1343 N THR A 231 10.028 -64.647 -18.541 1.00 92.91 N ANISOU 1343 N THR A 231 14136 8308 12855 -955 -52 -705 N ATOM 1344 CA THR A 231 10.306 -63.652 -19.566 1.00 90.82 C ANISOU 1344 CA THR A 231 13974 8331 12200 -865 -223 -862 C ATOM 1345 C THR A 231 9.055 -62.847 -19.933 1.00 91.86 C ANISOU 1345 C THR A 231 13876 8522 12501 -916 -341 -799 C ATOM 1346 O THR A 231 9.164 -61.679 -20.299 1.00 90.51 O ANISOU 1346 O THR A 231 13770 8594 12023 -834 -355 -774 O ATOM 1347 CB THR A 231 10.912 -64.310 -20.825 1.00 91.38 C ANISOU 1347 CB THR A 231 14188 8424 12106 -829 -537 -1215 C ATOM 1348 OG1 THR A 231 11.786 -65.376 -20.437 1.00 90.37 O ANISOU 1348 OG1 THR A 231 14187 8134 12016 -809 -465 -1287 O ATOM 1349 CG2 THR A 231 11.702 -63.301 -21.632 1.00 89.40 C ANISOU 1349 CG2 THR A 231 14143 8509 11317 -701 -586 -1319 C ATOM 1350 N ALA A 232 7.876 -63.461 -19.815 1.00 94.61 N ANISOU 1350 N ALA A 232 13943 8636 13367 -1052 -427 -763 N ATOM 1351 CA ALA A 232 6.608 -62.760 -20.056 1.00 96.36 C ANISOU 1351 CA ALA A 232 13894 8881 13834 -1102 -534 -693 C ATOM 1352 C ALA A 232 6.426 -61.548 -19.129 1.00 94.89 C ANISOU 1352 C ALA A 232 13667 8844 13540 -1038 -203 -414 C ATOM 1353 O ALA A 232 5.779 -60.570 -19.500 1.00 95.37 O ANISOU 1353 O ALA A 232 13607 9030 13598 -1006 -298 -384 O ATOM 1354 CB ALA A 232 5.432 -63.714 -19.911 1.00 99.75 C ANISOU 1354 CB ALA A 232 13994 8999 14904 -1272 -630 -679 C ATOM 1355 N THR A 233 6.991 -61.623 -17.926 1.00 92.85 N ANISOU 1355 N THR A 233 13513 8566 13197 -1007 166 -220 N ATOM 1356 CA THR A 233 7.005 -60.489 -17.009 1.00 90.55 C ANISOU 1356 CA THR A 233 13238 8429 12736 -918 482 1 C ATOM 1357 C THR A 233 8.238 -59.621 -17.232 1.00 87.30 C ANISOU 1357 C THR A 233 13131 8266 11770 -772 501 -58 C ATOM 1358 O THR A 233 8.123 -58.397 -17.292 1.00 86.18 O ANISOU 1358 O THR A 233 12988 8295 11460 -694 531 -1 O ATOM 1359 CB THR A 233 6.968 -60.957 -15.544 1.00 90.92 C ANISOU 1359 CB THR A 233 13259 8346 12939 -945 873 245 C ATOM 1360 OG1 THR A 233 5.700 -61.560 -15.283 1.00 94.93 O ANISOU 1360 OG1 THR A 233 13437 8638 13994 -1089 909 350 O ATOM 1361 CG2 THR A 233 7.158 -59.794 -14.581 1.00 89.04 C ANISOU 1361 CG2 THR A 233 13095 8289 12446 -823 1191 427 C ATOM 1362 N VAL A 234 9.409 -60.250 -17.355 1.00 85.62 N ANISOU 1362 N VAL A 234 13161 8058 11311 -736 482 -173 N ATOM 1363 CA VAL A 234 10.679 -59.513 -17.478 1.00 82.06 C ANISOU 1363 CA VAL A 234 12980 7825 10372 -607 533 -221 C ATOM 1364 C VAL A 234 10.749 -58.679 -18.766 1.00 81.56 C ANISOU 1364 C VAL A 234 12966 7958 10062 -564 278 -361 C ATOM 1365 O VAL A 234 11.295 -57.577 -18.758 1.00 79.21 O ANISOU 1365 O VAL A 234 12786 7845 9463 -474 358 -306 O ATOM 1366 CB VAL A 234 11.906 -60.450 -17.382 1.00 80.96 C ANISOU 1366 CB VAL A 234 13055 7636 10071 -575 555 -331 C ATOM 1367 CG1 VAL A 234 13.200 -59.695 -17.668 1.00 77.89 C ANISOU 1367 CG1 VAL A 234 12900 7473 9219 -453 582 -405 C ATOM 1368 CG2 VAL A 234 11.977 -61.097 -16.004 1.00 81.34 C ANISOU 1368 CG2 VAL A 234 13105 7516 10284 -589 826 -141 C ATOM 1369 N LYS A 235 10.203 -59.194 -19.865 1.00 83.65 N ANISOU 1369 N LYS A 235 13150 8177 10455 -626 -35 -538 N ATOM 1370 CA LYS A 235 10.086 -58.389 -21.075 1.00 83.98 C ANISOU 1370 CA LYS A 235 13234 8406 10268 -583 -291 -636 C ATOM 1371 C LYS A 235 9.138 -57.212 -20.835 1.00 84.56 C ANISOU 1371 C LYS A 235 13131 8527 10468 -571 -257 -452 C ATOM 1372 O LYS A 235 9.445 -56.095 -21.232 1.00 84.22 O ANISOU 1372 O LYS A 235 13190 8667 10140 -491 -281 -404 O ATOM 1373 CB LYS A 235 9.647 -59.222 -22.290 1.00 86.68 C ANISOU 1373 CB LYS A 235 13536 8690 10707 -638 -668 -885 C ATOM 1374 CG LYS A 235 10.817 -59.800 -23.081 1.00 86.52 C ANISOU 1374 CG LYS A 235 13773 8766 10333 -581 -768 -1124 C ATOM 1375 CD LYS A 235 10.405 -60.372 -24.436 1.00 89.52 C ANISOU 1375 CD LYS A 235 14155 9152 10703 -599 -1171 -1400 C ATOM 1376 CE LYS A 235 10.185 -61.878 -24.405 1.00 91.79 C ANISOU 1376 CE LYS A 235 14358 9173 11342 -682 -1296 -1594 C ATOM 1377 NZ LYS A 235 9.837 -62.436 -25.743 1.00 95.03 N ANISOU 1377 NZ LYS A 235 14791 9593 11722 -683 -1716 -1911 N ATOM 1378 N VAL A 236 8.011 -57.458 -20.166 1.00 86.65 N ANISOU 1378 N VAL A 236 13125 8620 11177 -646 -187 -340 N ATOM 1379 CA VAL A 236 7.036 -56.393 -19.854 1.00 87.52 C ANISOU 1379 CA VAL A 236 13027 8755 11469 -624 -134 -177 C ATOM 1380 C VAL A 236 7.632 -55.308 -18.954 1.00 84.68 C ANISOU 1380 C VAL A 236 12787 8517 10870 -517 178 -12 C ATOM 1381 O VAL A 236 7.495 -54.116 -19.230 1.00 82.90 O ANISOU 1381 O VAL A 236 12561 8410 10525 -443 129 46 O ATOM 1382 CB VAL A 236 5.758 -56.961 -19.185 1.00 90.15 C ANISOU 1382 CB VAL A 236 13020 8874 12358 -729 -51 -85 C ATOM 1383 CG1 VAL A 236 4.919 -55.854 -18.551 1.00 90.34 C ANISOU 1383 CG1 VAL A 236 12837 8929 12556 -678 118 96 C ATOM 1384 CG2 VAL A 236 4.932 -57.736 -20.200 1.00 93.47 C ANISOU 1384 CG2 VAL A 236 13259 9170 13083 -831 -435 -256 C ATOM 1385 N VAL A 237 8.278 -55.734 -17.874 1.00 83.73 N ANISOU 1385 N VAL A 237 12768 8350 10694 -507 477 58 N ATOM 1386 CA VAL A 237 8.900 -54.808 -16.935 1.00 81.94 C ANISOU 1386 CA VAL A 237 12666 8224 10240 -401 759 184 C ATOM 1387 C VAL A 237 9.923 -53.930 -17.644 1.00 80.58 C ANISOU 1387 C VAL A 237 12722 8237 9658 -317 653 119 C ATOM 1388 O VAL A 237 9.885 -52.706 -17.515 1.00 79.99 O ANISOU 1388 O VAL A 237 12648 8249 9494 -241 703 202 O ATOM 1389 CB VAL A 237 9.572 -55.556 -15.760 1.00 81.23 C ANISOU 1389 CB VAL A 237 12696 8063 10105 -394 1042 247 C ATOM 1390 CG1 VAL A 237 10.511 -54.646 -14.974 1.00 78.83 C ANISOU 1390 CG1 VAL A 237 12584 7884 9481 -270 1255 312 C ATOM 1391 CG2 VAL A 237 8.513 -56.131 -14.831 1.00 84.08 C ANISOU 1391 CG2 VAL A 237 12830 8261 10856 -462 1240 390 C ATOM 1392 N ILE A 238 10.824 -54.549 -18.399 1.00 80.38 N ANISOU 1392 N ILE A 238 12876 8260 9404 -331 514 -27 N ATOM 1393 CA ILE A 238 11.894 -53.801 -19.051 1.00 79.25 C ANISOU 1393 CA ILE A 238 12945 8295 8869 -262 460 -74 C ATOM 1394 C ILE A 238 11.354 -52.832 -20.115 1.00 81.16 C ANISOU 1394 C ILE A 238 13144 8641 9050 -246 229 -55 C ATOM 1395 O ILE A 238 11.964 -51.788 -20.357 1.00 81.15 O ANISOU 1395 O ILE A 238 13263 8766 8801 -184 251 3 O ATOM 1396 CB ILE A 238 12.998 -54.739 -19.594 1.00 78.50 C ANISOU 1396 CB ILE A 238 13037 8237 8550 -269 398 -246 C ATOM 1397 CG1 ILE A 238 13.736 -55.361 -18.405 1.00 77.77 C ANISOU 1397 CG1 ILE A 238 13020 8058 8469 -248 645 -218 C ATOM 1398 CG2 ILE A 238 13.988 -53.987 -20.477 1.00 77.02 C ANISOU 1398 CG2 ILE A 238 13035 8250 7978 -212 335 -294 C ATOM 1399 CD1 ILE A 238 14.779 -56.398 -18.763 0.00 78.40 C ANISOU 1399 CD1 ILE A 238 13251 8131 8406 -244 602 -390 C ATOM 1400 N GLN A 239 10.207 -53.139 -20.721 1.00 83.86 N ANISOU 1400 N GLN A 239 13308 8917 9636 -302 -1 -93 N ATOM 1401 CA GLN A 239 9.637 -52.223 -21.714 1.00 85.87 C ANISOU 1401 CA GLN A 239 13524 9262 9839 -273 -254 -60 C ATOM 1402 C GLN A 239 8.775 -51.113 -21.094 1.00 86.11 C ANISOU 1402 C GLN A 239 13368 9247 10104 -228 -170 114 C ATOM 1403 O GLN A 239 8.456 -50.138 -21.768 1.00 88.13 O ANISOU 1403 O GLN A 239 13614 9571 10299 -181 -345 181 O ATOM 1404 CB GLN A 239 8.909 -52.971 -22.847 1.00 89.28 C ANISOU 1404 CB GLN A 239 13880 9671 10370 -332 -613 -211 C ATOM 1405 CG GLN A 239 7.545 -53.559 -22.529 1.00 92.26 C ANISOU 1405 CG GLN A 239 13947 9859 11249 -408 -702 -218 C ATOM 1406 CD GLN A 239 6.990 -54.372 -23.694 1.00 95.98 C ANISOU 1406 CD GLN A 239 14368 10300 11799 -465 -1096 -414 C ATOM 1407 OE1 GLN A 239 7.576 -55.380 -24.103 1.00 95.54 O ANISOU 1407 OE1 GLN A 239 14448 10237 11613 -497 -1171 -598 O ATOM 1408 NE2 GLN A 239 5.855 -53.935 -24.234 1.00 99.26 N ANISOU 1408 NE2 GLN A 239 14585 10690 12438 -466 -1370 -393 N ATOM 1409 N VAL A 240 8.412 -51.242 -19.822 1.00 85.58 N ANISOU 1409 N VAL A 240 13160 9065 10291 -231 100 190 N ATOM 1410 CA VAL A 240 7.851 -50.103 -19.082 1.00 85.89 C ANISOU 1410 CA VAL A 240 13064 9081 10487 -155 250 332 C ATOM 1411 C VAL A 240 8.987 -49.166 -18.668 1.00 83.50 C ANISOU 1411 C VAL A 240 12981 8874 9868 -67 425 387 C ATOM 1412 O VAL A 240 8.854 -47.943 -18.762 1.00 83.35 O ANISOU 1412 O VAL A 240 12948 8884 9835 6 395 471 O ATOM 1413 CB VAL A 240 7.048 -50.543 -17.836 1.00 86.84 C ANISOU 1413 CB VAL A 240 12962 9067 10964 -176 512 394 C ATOM 1414 CG1 VAL A 240 6.716 -49.351 -16.943 0.00 86.40 C ANISOU 1414 CG1 VAL A 240 12820 9014 10994 -67 726 507 C ATOM 1415 CG2 VAL A 240 5.770 -51.255 -18.254 0.00 89.81 C ANISOU 1415 CG2 VAL A 240 13053 9326 11745 -268 330 362 C ATOM 1416 N ASN A 241 10.092 -49.752 -18.203 1.00 81.76 N ANISOU 1416 N ASN A 241 12949 8682 9430 -75 591 334 N ATOM 1417 CA ASN A 241 11.291 -48.997 -17.840 1.00 79.12 C ANISOU 1417 CA ASN A 241 12818 8431 8813 -4 733 358 C ATOM 1418 C ASN A 241 11.741 -48.158 -19.023 1.00 79.07 C ANISOU 1418 C ASN A 241 12925 8536 8581 8 532 376 C ATOM 1419 O ASN A 241 11.849 -46.941 -18.920 1.00 78.85 O ANISOU 1419 O ASN A 241 12911 8521 8525 71 556 470 O ATOM 1420 CB ASN A 241 12.412 -49.946 -17.390 1.00 77.35 C ANISOU 1420 CB ASN A 241 12763 8218 8405 -22 871 276 C ATOM 1421 CG ASN A 241 13.705 -49.223 -17.046 1.00 75.35 C ANISOU 1421 CG ASN A 241 12696 8044 7889 44 991 281 C ATOM 1422 OD1 ASN A 241 14.742 -49.473 -17.659 1.00 75.19 O ANISOU 1422 OD1 ASN A 241 12826 8106 7633 28 938 209 O ATOM 1423 ND2 ASN A 241 13.656 -48.340 -16.054 1.00 74.39 N ANISOU 1423 ND2 ASN A 241 12552 7892 7819 122 1154 351 N ATOM 1424 N THR A 242 11.962 -48.812 -20.156 1.00 79.49 N ANISOU 1424 N THR A 242 13060 8662 8480 -46 331 290 N ATOM 1425 CA THR A 242 12.393 -48.117 -21.356 1.00 79.97 C ANISOU 1425 CA THR A 242 13252 8853 8279 -34 152 323 C ATOM 1426 C THR A 242 11.436 -46.981 -21.719 1.00 82.43 C ANISOU 1426 C THR A 242 13444 9138 8737 5 -5 462 C ATOM 1427 O THR A 242 11.878 -45.858 -21.926 1.00 83.41 O ANISOU 1427 O THR A 242 13653 9305 8734 49 2 580 O ATOM 1428 CB THR A 242 12.552 -49.093 -22.534 1.00 80.95 C ANISOU 1428 CB THR A 242 13469 9066 8220 -85 -55 182 C ATOM 1429 OG1 THR A 242 13.559 -50.055 -22.203 1.00 79.56 O ANISOU 1429 OG1 THR A 242 13409 8905 7914 -104 96 52 O ATOM 1430 CG2 THR A 242 12.962 -48.359 -23.814 1.00 81.98 C ANISOU 1430 CG2 THR A 242 13757 9359 8032 -64 -224 240 C ATOM 1431 N PHE A 243 10.136 -47.258 -21.767 1.00 85.01 N ANISOU 1431 N PHE A 243 13557 9376 9364 -9 -150 454 N ATOM 1432 CA PHE A 243 9.152 -46.243 -22.179 1.00 86.99 C ANISOU 1432 CA PHE A 243 13670 9591 9790 40 -342 574 C ATOM 1433 C PHE A 243 9.130 -45.032 -21.253 1.00 85.85 C ANISOU 1433 C PHE A 243 13464 9371 9782 123 -150 696 C ATOM 1434 O PHE A 243 9.136 -43.892 -21.717 1.00 87.15 O ANISOU 1434 O PHE A 243 13667 9543 9900 178 -262 821 O ATOM 1435 CB PHE A 243 7.744 -46.840 -22.262 1.00 89.70 C ANISOU 1435 CB PHE A 243 13745 9833 10502 8 -515 523 C ATOM 1436 CG PHE A 243 6.664 -45.820 -22.521 1.00 92.25 C ANISOU 1436 CG PHE A 243 13879 10094 11077 75 -702 639 C ATOM 1437 CD1 PHE A 243 6.053 -45.145 -21.465 1.00 92.51 C ANISOU 1437 CD1 PHE A 243 13708 10010 11429 141 -507 711 C ATOM 1438 CD2 PHE A 243 6.255 -45.534 -23.818 1.00 94.64 C ANISOU 1438 CD2 PHE A 243 14211 10457 11290 89 -1078 669 C ATOM 1439 CE1 PHE A 243 5.060 -44.206 -21.701 1.00 94.71 C ANISOU 1439 CE1 PHE A 243 13794 10217 11973 217 -684 804 C ATOM 1440 CE2 PHE A 243 5.261 -44.595 -24.058 1.00 97.06 C ANISOU 1440 CE2 PHE A 243 14338 10691 11849 163 -1278 783 C ATOM 1441 CZ PHE A 243 4.663 -43.930 -23.000 1.00 96.65 C ANISOU 1441 CZ PHE A 243 14061 10506 12156 227 -1080 847 C ATOM 1442 N MET A 244 9.095 -45.283 -19.948 1.00 84.53 N ANISOU 1442 N MET A 244 13212 9125 9779 139 130 661 N ATOM 1443 CA MET A 244 8.966 -44.209 -18.962 1.00 84.07 C ANISOU 1443 CA MET A 244 13083 8990 9869 236 316 731 C ATOM 1444 C MET A 244 10.302 -43.512 -18.665 1.00 80.98 C ANISOU 1444 C MET A 244 12915 8642 9210 271 455 753 C ATOM 1445 O MET A 244 10.332 -42.312 -18.388 1.00 80.20 O ANISOU 1445 O MET A 244 12806 8486 9179 349 482 825 O ATOM 1446 CB MET A 244 8.349 -44.756 -17.669 1.00 84.55 C ANISOU 1446 CB MET A 244 12972 8967 10182 252 573 685 C ATOM 1447 CG MET A 244 7.445 -43.762 -16.958 1.00 86.80 C ANISOU 1447 CG MET A 244 13054 9159 10764 361 667 737 C ATOM 1448 SD MET A 244 5.997 -43.303 -17.938 1.00 90.34 S ANISOU 1448 SD MET A 244 13232 9542 11550 376 342 800 S ATOM 1449 CE MET A 244 5.381 -41.893 -17.014 1.00 90.52 C ANISOU 1449 CE MET A 244 13085 9457 11851 541 496 843 C ATOM 1450 N SER A 245 11.396 -44.268 -18.735 1.00 78.58 N ANISOU 1450 N SER A 245 13227 7101 9527 63 -502 1110 N ATOM 1451 CA SER A 245 12.741 -43.752 -18.476 1.00 77.26 C ANISOU 1451 CA SER A 245 12805 6856 9691 405 -484 1087 C ATOM 1452 C SER A 245 13.398 -43.122 -19.721 1.00 76.78 C ANISOU 1452 C SER A 245 12640 6766 9767 510 -249 956 C ATOM 1453 O SER A 245 14.342 -42.343 -19.587 1.00 76.51 O ANISOU 1453 O SER A 245 12365 6680 10023 778 -212 945 O ATOM 1454 CB SER A 245 13.576 -44.843 -17.789 1.00 79.31 C ANISOU 1454 CB SER A 245 13206 6784 10143 613 -534 1134 C ATOM 1455 OG SER A 245 14.831 -44.357 -17.358 1.00 79.66 O ANISOU 1455 OG SER A 245 12951 6788 10526 917 -584 1179 O ATOM 1456 N PHE A 246 12.929 -43.451 -20.924 1.00 76.65 N ANISOU 1456 N PHE A 246 12807 6779 9536 276 -99 870 N ATOM 1457 CA PHE A 246 13.553 -42.910 -22.135 1.00 77.64 C ANISOU 1457 CA PHE A 246 12899 6850 9750 336 145 735 C ATOM 1458 C PHE A 246 12.645 -42.249 -23.166 1.00 76.53 C ANISOU 1458 C PHE A 246 12799 6936 9342 24 177 708 C ATOM 1459 O PHE A 246 12.859 -41.091 -23.511 1.00 75.96 O ANISOU 1459 O PHE A 246 12462 7059 9337 71 192 692 O ATOM 1460 CB PHE A 246 14.296 -44.082 -22.773 1.00 81.40 C ANISOU 1460 CB PHE A 246 13696 6918 10314 438 413 622 C ATOM 1461 CG PHE A 246 15.190 -43.675 -23.901 1.00 83.68 C ANISOU 1461 CG PHE A 246 13936 7113 10743 549 715 479 C ATOM 1462 CD1 PHE A 246 16.450 -43.151 -23.647 1.00 84.73 C ANISOU 1462 CD1 PHE A 246 13705 7226 11259 898 784 483 C ATOM 1463 CD2 PHE A 246 14.770 -43.795 -25.216 1.00 85.20 C ANISOU 1463 CD2 PHE A 246 14453 7246 10672 268 924 355 C ATOM 1464 CE1 PHE A 246 17.279 -42.760 -24.687 1.00 85.87 C ANISOU 1464 CE1 PHE A 246 13790 7296 11540 990 1090 355 C ATOM 1465 CE2 PHE A 246 15.594 -43.410 -26.258 1.00 86.48 C ANISOU 1465 CE2 PHE A 246 14606 7310 10941 347 1231 213 C ATOM 1466 CZ PHE A 246 16.848 -42.890 -25.993 1.00 86.66 C ANISOU 1466 CZ PHE A 246 14243 7319 11365 720 1331 207 C ATOM 1467 N LEU A 247 11.647 -42.978 -23.658 1.00 77.38 N ANISOU 1467 N LEU A 247 13243 7012 9143 -312 165 725 N ATOM 1468 CA LEU A 247 10.775 -42.472 -24.726 1.00 77.53 C ANISOU 1468 CA LEU A 247 13328 7229 8899 -658 161 742 C ATOM 1469 C LEU A 247 9.911 -41.278 -24.304 1.00 75.27 C ANISOU 1469 C LEU A 247 12665 7347 8584 -721 -52 903 C ATOM 1470 O LEU A 247 9.954 -40.217 -24.935 1.00 74.11 O ANISOU 1470 O LEU A 247 12328 7372 8457 -730 -26 898 O ATOM 1471 CB LEU A 247 9.891 -43.595 -25.270 1.00 79.95 C ANISOU 1471 CB LEU A 247 14097 7412 8868 -1056 154 762 C ATOM 1472 CG LEU A 247 10.646 -44.604 -26.143 1.00 83.33 C ANISOU 1472 CG LEU A 247 14999 7414 9246 -1072 452 576 C ATOM 1473 CD1 LEU A 247 9.894 -45.929 -26.249 0.00 85.97 C ANISOU 1473 CD1 LEU A 247 15847 7549 9266 -1414 426 601 C ATOM 1474 CD2 LEU A 247 10.924 -44.018 -27.523 0.00 83.36 C ANISOU 1474 CD2 LEU A 247 15100 7414 9157 -1215 644 461 C ATOM 1475 N PHE A 248 9.129 -41.448 -23.242 1.00 74.32 N ANISOU 1475 N PHE A 248 12456 7361 8422 -759 -235 1048 N ATOM 1476 CA PHE A 248 8.322 -40.347 -22.704 1.00 72.02 C ANISOU 1476 CA PHE A 248 11811 7413 8139 -766 -376 1208 C ATOM 1477 C PHE A 248 9.184 -39.087 -22.523 1.00 69.11 C ANISOU 1477 C PHE A 248 11137 7119 8003 -462 -324 1149 C ATOM 1478 O PHE A 248 8.857 -38.032 -23.072 1.00 67.08 O ANISOU 1478 O PHE A 248 10692 7064 7730 -507 -324 1197 O ATOM 1479 CB PHE A 248 7.607 -40.784 -21.410 1.00 71.94 C ANISOU 1479 CB PHE A 248 11776 7468 8090 -788 -512 1339 C ATOM 1480 CG PHE A 248 7.130 -39.649 -20.544 1.00 70.91 C ANISOU 1480 CG PHE A 248 11301 7597 8043 -668 -573 1463 C ATOM 1481 CD1 PHE A 248 6.273 -38.684 -21.043 1.00 71.00 C ANISOU 1481 CD1 PHE A 248 11079 7884 8012 -777 -584 1594 C ATOM 1482 CD2 PHE A 248 7.515 -39.569 -19.206 1.00 71.16 C ANISOU 1482 CD2 PHE A 248 11276 7574 8187 -458 -612 1465 C ATOM 1483 CE1 PHE A 248 5.832 -37.642 -20.236 1.00 70.33 C ANISOU 1483 CE1 PHE A 248 10713 7993 8016 -637 -580 1706 C ATOM 1484 CE2 PHE A 248 7.070 -38.537 -18.394 1.00 69.66 C ANISOU 1484 CE2 PHE A 248 10850 7577 8038 -368 -619 1563 C ATOM 1485 CZ PHE A 248 6.228 -37.570 -18.911 1.00 69.29 C ANISOU 1485 CZ PHE A 248 10577 7782 7967 -438 -577 1676 C ATOM 1486 N PRO A 249 10.302 -39.200 -21.789 1.00 68.35 N ANISOU 1486 N PRO A 249 10997 6851 8119 -172 -296 1065 N ATOM 1487 CA PRO A 249 11.170 -38.034 -21.669 1.00 67.57 C ANISOU 1487 CA PRO A 249 10634 6821 8218 61 -262 1019 C ATOM 1488 C PRO A 249 11.897 -37.640 -22.956 1.00 68.02 C ANISOU 1488 C PRO A 249 10691 6825 8328 74 -92 888 C ATOM 1489 O PRO A 249 12.347 -36.507 -23.061 1.00 66.63 O ANISOU 1489 O PRO A 249 10297 6765 8253 185 -72 870 O ATOM 1490 CB PRO A 249 12.172 -38.432 -20.574 1.00 68.01 C ANISOU 1490 CB PRO A 249 10659 6701 8478 309 -317 1004 C ATOM 1491 CG PRO A 249 12.078 -39.902 -20.451 1.00 69.68 C ANISOU 1491 CG PRO A 249 11153 6684 8637 250 -317 997 C ATOM 1492 CD PRO A 249 10.689 -40.273 -20.859 1.00 69.79 C ANISOU 1492 CD PRO A 249 11335 6814 8366 -68 -346 1062 C ATOM 1493 N MET A 250 12.024 -38.549 -23.918 1.00 70.39 N ANISOU 1493 N MET A 250 11269 6932 8540 -54 47 793 N ATOM 1494 CA MET A 250 12.589 -38.185 -25.215 1.00 72.04 C ANISOU 1494 CA MET A 250 11538 7085 8747 -100 242 665 C ATOM 1495 C MET A 250 11.642 -37.231 -25.922 1.00 70.02 C ANISOU 1495 C MET A 250 11212 7093 8298 -343 160 749 C ATOM 1496 O MET A 250 12.041 -36.140 -26.318 1.00 69.11 O ANISOU 1496 O MET A 250 10916 7087 8255 -273 202 719 O ATOM 1497 CB MET A 250 12.828 -39.419 -26.090 1.00 76.93 C ANISOU 1497 CB MET A 250 12563 7401 9263 -227 448 541 C ATOM 1498 CG MET A 250 13.639 -39.167 -27.354 1.00 79.54 C ANISOU 1498 CG MET A 250 13003 7600 9616 -241 726 377 C ATOM 1499 SD MET A 250 15.392 -38.915 -27.001 1.00 82.26 S ANISOU 1499 SD MET A 250 13063 7792 10398 209 926 276 S ATOM 1500 CE MET A 250 15.488 -37.134 -26.834 1.00 79.33 C ANISOU 1500 CE MET A 250 12266 7772 10103 265 774 336 C ATOM 1501 N LEU A 251 10.386 -37.648 -26.062 1.00 69.92 N ANISOU 1501 N LEU A 251 11331 7184 8049 -634 29 879 N ATOM 1502 CA LEU A 251 9.354 -36.815 -26.679 1.00 69.29 C ANISOU 1502 CA LEU A 251 11144 7371 7810 -874 -91 1030 C ATOM 1503 C LEU A 251 9.253 -35.450 -26.010 1.00 66.61 C ANISOU 1503 C LEU A 251 10420 7260 7628 -658 -168 1128 C ATOM 1504 O LEU A 251 9.205 -34.430 -26.682 1.00 66.17 O ANISOU 1504 O LEU A 251 10248 7329 7563 -691 -164 1157 O ATOM 1505 CB LEU A 251 7.989 -37.502 -26.609 1.00 70.53 C ANISOU 1505 CB LEU A 251 11407 7642 7748 -1192 -261 1219 C ATOM 1506 CG LEU A 251 7.777 -38.696 -27.537 1.00 73.35 C ANISOU 1506 CG LEU A 251 12216 7810 7843 -1549 -221 1167 C ATOM 1507 CD1 LEU A 251 6.426 -39.335 -27.262 1.00 74.84 C ANISOU 1507 CD1 LEU A 251 12457 8145 7831 -1869 -428 1387 C ATOM 1508 CD2 LEU A 251 7.883 -38.276 -28.994 1.00 74.77 C ANISOU 1508 CD2 LEU A 251 12566 7979 7863 -1796 -157 1120 C ATOM 1509 N VAL A 252 9.220 -35.440 -24.683 1.00 65.29 N ANISOU 1509 N VAL A 252 10102 7121 7583 -453 -228 1178 N ATOM 1510 CA VAL A 252 9.084 -34.198 -23.934 1.00 63.60 C ANISOU 1510 CA VAL A 252 9602 7079 7484 -264 -267 1264 C ATOM 1511 C VAL A 252 10.268 -33.272 -24.241 1.00 63.17 C ANISOU 1511 C VAL A 252 9457 6973 7569 -78 -169 1126 C ATOM 1512 O VAL A 252 10.089 -32.171 -24.776 1.00 63.14 O ANISOU 1512 O VAL A 252 9333 7101 7553 -93 -160 1170 O ATOM 1513 CB VAL A 252 8.959 -34.477 -22.415 1.00 62.48 C ANISOU 1513 CB VAL A 252 9410 6919 7408 -115 -325 1315 C ATOM 1514 CG1 VAL A 252 9.134 -33.208 -21.592 1.00 60.91 C ANISOU 1514 CG1 VAL A 252 9013 6813 7317 92 -312 1349 C ATOM 1515 CG2 VAL A 252 7.616 -35.120 -22.113 1.00 63.29 C ANISOU 1515 CG2 VAL A 252 9543 7134 7370 -317 -410 1487 C ATOM 1516 N ILE A 253 11.468 -33.749 -23.927 1.00 63.07 N ANISOU 1516 N ILE A 253 9496 6769 7697 85 -101 980 N ATOM 1517 CA ILE A 253 12.700 -32.986 -24.110 1.00 62.34 C ANISOU 1517 CA ILE A 253 9288 6631 7766 253 -13 866 C ATOM 1518 C ILE A 253 12.892 -32.530 -25.551 1.00 61.78 C ANISOU 1518 C ILE A 253 9272 6575 7626 121 108 786 C ATOM 1519 O ILE A 253 13.077 -31.342 -25.811 1.00 60.66 O ANISOU 1519 O ILE A 253 9001 6543 7503 153 117 791 O ATOM 1520 CB ILE A 253 13.927 -33.819 -23.661 1.00 64.82 C ANISOU 1520 CB ILE A 253 9624 6728 8275 431 39 768 C ATOM 1521 CG1 ILE A 253 13.914 -33.984 -22.144 1.00 65.24 C ANISOU 1521 CG1 ILE A 253 9611 6777 8399 556 -120 861 C ATOM 1522 CG2 ILE A 253 15.241 -33.180 -24.095 1.00 65.92 C ANISOU 1522 CG2 ILE A 253 9625 6824 8597 563 158 663 C ATOM 1523 CD1 ILE A 253 13.744 -32.679 -21.403 1.00 64.72 C ANISOU 1523 CD1 ILE A 253 9392 6875 8321 608 -208 936 C ATOM 1524 N SER A 254 12.849 -33.468 -26.487 1.00 62.07 N ANISOU 1524 N SER A 254 9546 6478 7557 -48 209 712 N ATOM 1525 CA SER A 254 13.140 -33.136 -27.870 1.00 62.31 C ANISOU 1525 CA SER A 254 9699 6479 7496 -206 351 616 C ATOM 1526 C SER A 254 12.149 -32.100 -28.405 1.00 61.67 C ANISOU 1526 C SER A 254 9551 6627 7254 -390 221 758 C ATOM 1527 O SER A 254 12.559 -31.115 -29.026 1.00 61.75 O ANISOU 1527 O SER A 254 9501 6689 7272 -394 277 717 O ATOM 1528 CB SER A 254 13.150 -34.390 -28.735 1.00 63.84 C ANISOU 1528 CB SER A 254 10250 6456 7549 -403 498 516 C ATOM 1529 OG SER A 254 11.949 -35.102 -28.573 1.00 64.27 O ANISOU 1529 OG SER A 254 10450 6559 7409 -619 341 648 O ATOM 1530 N ILE A 255 10.859 -32.301 -28.143 1.00 61.23 N ANISOU 1530 N ILE A 255 9484 6708 7070 -536 48 946 N ATOM 1531 CA ILE A 255 9.843 -31.366 -28.623 1.00 61.46 C ANISOU 1531 CA ILE A 255 9400 6957 6993 -690 -87 1141 C ATOM 1532 C ILE A 255 10.021 -30.005 -27.963 1.00 60.47 C ANISOU 1532 C ILE A 255 9003 6948 7023 -433 -99 1190 C ATOM 1533 O ILE A 255 10.387 -29.025 -28.622 1.00 60.18 O ANISOU 1533 O ILE A 255 8936 6943 6985 -436 -60 1161 O ATOM 1534 CB ILE A 255 8.403 -31.868 -28.369 1.00 62.00 C ANISOU 1534 CB ILE A 255 9437 7172 6947 -878 -267 1380 C ATOM 1535 CG1 ILE A 255 8.100 -33.088 -29.242 1.00 64.16 C ANISOU 1535 CG1 ILE A 255 10046 7340 6992 -1235 -285 1359 C ATOM 1536 CG2 ILE A 255 7.386 -30.772 -28.670 1.00 62.08 C ANISOU 1536 CG2 ILE A 255 9224 7423 6939 -950 -405 1637 C ATOM 1537 CD1 ILE A 255 6.882 -33.875 -28.803 1.00 64.94 C ANISOU 1537 CD1 ILE A 255 10141 7548 6986 -1427 -452 1567 C ATOM 1538 N LEU A 256 9.775 -29.953 -26.659 1.00 59.75 N ANISOU 1538 N LEU A 256 8762 6898 7040 -234 -140 1258 N ATOM 1539 CA LEU A 256 9.684 -28.676 -25.970 1.00 59.17 C ANISOU 1539 CA LEU A 256 8496 6920 7063 -33 -140 1336 C ATOM 1540 C LEU A 256 10.968 -27.865 -26.149 1.00 59.36 C ANISOU 1540 C LEU A 256 8519 6864 7170 92 -45 1167 C ATOM 1541 O LEU A 256 10.912 -26.670 -26.476 1.00 58.69 O ANISOU 1541 O LEU A 256 8369 6848 7080 120 -34 1215 O ATOM 1542 CB LEU A 256 9.369 -28.873 -24.486 1.00 58.24 C ANISOU 1542 CB LEU A 256 8306 6806 7016 132 -158 1396 C ATOM 1543 CG LEU A 256 8.054 -29.573 -24.128 1.00 58.85 C ANISOU 1543 CG LEU A 256 8345 6985 7028 20 -233 1585 C ATOM 1544 CD1 LEU A 256 7.848 -29.505 -22.624 1.00 58.86 C ANISOU 1544 CD1 LEU A 256 8296 6974 7091 196 -203 1625 C ATOM 1545 CD2 LEU A 256 6.858 -28.981 -24.853 1.00 59.16 C ANISOU 1545 CD2 LEU A 256 8241 7213 7022 -108 -291 1823 C ATOM 1546 N ASN A 257 12.121 -28.508 -25.963 1.00 59.21 N ANISOU 1546 N ASN A 257 8561 6697 7238 162 22 990 N ATOM 1547 CA ASN A 257 13.387 -27.803 -26.132 1.00 58.94 C ANISOU 1547 CA ASN A 257 8483 6605 7304 258 109 853 C ATOM 1548 C ASN A 257 13.451 -27.114 -27.482 1.00 59.62 C ANISOU 1548 C ASN A 257 8626 6730 7297 108 174 819 C ATOM 1549 O ASN A 257 13.739 -25.922 -27.550 1.00 60.77 O ANISOU 1549 O ASN A 257 8708 6927 7453 154 184 824 O ATOM 1550 CB ASN A 257 14.595 -28.721 -25.939 1.00 58.83 C ANISOU 1550 CB ASN A 257 8483 6430 7437 346 188 708 C ATOM 1551 CG ASN A 257 14.914 -28.954 -24.479 1.00 58.24 C ANISOU 1551 CG ASN A 257 8323 6320 7483 516 88 750 C ATOM 1552 OD1 ASN A 257 14.036 -28.899 -23.622 1.00 56.55 O ANISOU 1552 OD1 ASN A 257 8114 6168 7202 532 -12 865 O ATOM 1553 ND2 ASN A 257 16.181 -29.198 -24.186 1.00 59.48 N ANISOU 1553 ND2 ASN A 257 8398 6377 7824 631 119 675 N ATOM 1554 N THR A 258 13.149 -27.845 -28.549 1.00 60.58 N ANISOU 1554 N THR A 258 8908 6811 7296 -102 213 792 N ATOM 1555 CA THR A 258 13.177 -27.256 -29.885 1.00 61.94 C ANISOU 1555 CA THR A 258 9191 7004 7339 -301 263 767 C ATOM 1556 C THR A 258 12.160 -26.106 -30.033 1.00 61.11 C ANISOU 1556 C THR A 258 8996 7068 7154 -348 117 975 C ATOM 1557 O THR A 258 12.463 -25.097 -30.676 1.00 60.24 O ANISOU 1557 O THR A 258 8900 6982 7006 -391 143 960 O ATOM 1558 CB THR A 258 12.976 -28.323 -30.976 1.00 63.59 C ANISOU 1558 CB THR A 258 9670 7111 7379 -575 329 708 C ATOM 1559 OG1 THR A 258 13.868 -29.411 -30.725 1.00 65.16 O ANISOU 1559 OG1 THR A 258 9949 7120 7689 -473 498 536 O ATOM 1560 CG2 THR A 258 13.274 -27.754 -32.359 1.00 64.50 C ANISOU 1560 CG2 THR A 258 9956 7203 7346 -803 417 640 C ATOM 1561 N VAL A 259 10.981 -26.250 -29.423 1.00 60.54 N ANISOU 1561 N VAL A 259 8822 7104 7074 -326 -18 1179 N ATOM 1562 CA VAL A 259 9.973 -25.176 -29.402 1.00 61.00 C ANISOU 1562 CA VAL A 259 8738 7311 7126 -298 -124 1418 C ATOM 1563 C VAL A 259 10.489 -23.948 -28.647 1.00 60.74 C ANISOU 1563 C VAL A 259 8609 7262 7207 -42 -53 1384 C ATOM 1564 O VAL A 259 10.338 -22.808 -29.108 1.00 60.66 O ANISOU 1564 O VAL A 259 8581 7290 7175 -36 -63 1468 O ATOM 1565 CB VAL A 259 8.657 -25.629 -28.735 1.00 61.33 C ANISOU 1565 CB VAL A 259 8642 7469 7188 -286 -234 1653 C ATOM 1566 CG1 VAL A 259 7.718 -24.451 -28.514 1.00 61.61 C ANISOU 1566 CG1 VAL A 259 8480 7631 7296 -162 -277 1910 C ATOM 1567 CG2 VAL A 259 7.966 -26.686 -29.575 1.00 63.28 C ANISOU 1567 CG2 VAL A 259 9000 7759 7283 -610 -351 1745 C ATOM 1568 N ILE A 260 11.086 -24.195 -27.483 1.00 60.00 N ANISOU 1568 N ILE A 260 8484 7098 7213 143 5 1276 N ATOM 1569 CA ILE A 260 11.685 -23.138 -26.676 1.00 58.87 C ANISOU 1569 CA ILE A 260 8316 6914 7137 331 63 1229 C ATOM 1570 C ILE A 260 12.839 -22.494 -27.436 1.00 57.73 C ANISOU 1570 C ILE A 260 8239 6718 6978 270 125 1073 C ATOM 1571 O ILE A 260 12.929 -21.277 -27.522 1.00 57.72 O ANISOU 1571 O ILE A 260 8258 6721 6950 309 147 1104 O ATOM 1572 CB ILE A 260 12.209 -23.684 -25.336 1.00 58.91 C ANISOU 1572 CB ILE A 260 8314 6845 7223 467 71 1150 C ATOM 1573 CG1 ILE A 260 11.068 -24.245 -24.492 1.00 59.55 C ANISOU 1573 CG1 ILE A 260 8351 6970 7304 520 36 1299 C ATOM 1574 CG2 ILE A 260 12.897 -22.587 -24.540 1.00 58.96 C ANISOU 1574 CG2 ILE A 260 8355 6797 7250 587 109 1106 C ATOM 1575 CD1 ILE A 260 11.528 -25.266 -23.474 1.00 59.74 C ANISOU 1575 CD1 ILE A 260 8409 6914 7376 569 6 1220 C ATOM 1576 N ALA A 261 13.714 -23.325 -27.987 1.00 57.50 N ANISOU 1576 N ALA A 261 8253 6626 6968 175 179 909 N ATOM 1577 CA ALA A 261 14.850 -22.854 -28.768 1.00 58.59 C ANISOU 1577 CA ALA A 261 8434 6719 7107 100 278 756 C ATOM 1578 C ALA A 261 14.444 -21.900 -29.900 1.00 59.48 C ANISOU 1578 C ALA A 261 8637 6880 7080 -52 270 818 C ATOM 1579 O ALA A 261 15.061 -20.849 -30.090 1.00 58.80 O ANISOU 1579 O ALA A 261 8573 6786 6980 -53 311 770 O ATOM 1580 CB ALA A 261 15.607 -24.043 -29.333 1.00 59.63 C ANISOU 1580 CB ALA A 261 8611 6756 7286 23 394 600 C ATOM 1581 N ASN A 262 13.402 -22.276 -30.638 1.00 60.96 N ANISOU 1581 N ASN A 262 8887 7118 7156 -207 193 944 N ATOM 1582 CA ASN A 262 12.893 -21.471 -31.750 1.00 61.75 C ANISOU 1582 CA ASN A 262 9077 7267 7116 -385 133 1054 C ATOM 1583 C ASN A 262 12.322 -20.134 -31.293 1.00 61.69 C ANISOU 1583 C ASN A 262 8986 7311 7140 -229 67 1231 C ATOM 1584 O ASN A 262 12.642 -19.098 -31.865 1.00 62.42 O ANISOU 1584 O ASN A 262 9159 7385 7172 -280 82 1225 O ATOM 1585 CB ASN A 262 11.808 -22.237 -32.511 1.00 63.40 C ANISOU 1585 CB ASN A 262 9355 7533 7199 -617 8 1209 C ATOM 1586 CG ASN A 262 12.342 -23.459 -33.232 1.00 64.58 C ANISOU 1586 CG ASN A 262 9703 7582 7252 -831 110 1026 C ATOM 1587 OD1 ASN A 262 13.548 -23.613 -33.421 1.00 65.61 O ANISOU 1587 OD1 ASN A 262 9907 7599 7421 -812 301 791 O ATOM 1588 ND2 ASN A 262 11.439 -24.339 -33.639 1.00 66.02 N ANISOU 1588 ND2 ASN A 262 9978 7794 7312 -1044 -1 1146 N ATOM 1589 N LYS A 263 11.464 -20.175 -30.275 1.00 61.77 N ANISOU 1589 N LYS A 263 8860 7368 7242 -42 20 1390 N ATOM 1590 CA LYS A 263 10.863 -18.970 -29.685 1.00 61.44 C ANISOU 1590 CA LYS A 263 8757 7333 7254 156 26 1562 C ATOM 1591 C LYS A 263 11.938 -18.036 -29.148 1.00 59.77 C ANISOU 1591 C LYS A 263 8643 7017 7048 267 135 1399 C ATOM 1592 O LYS A 263 11.867 -16.830 -29.339 1.00 59.85 O ANISOU 1592 O LYS A 263 8727 6988 7024 313 158 1469 O ATOM 1593 CB LYS A 263 9.887 -19.369 -28.566 1.00 62.10 C ANISOU 1593 CB LYS A 263 8694 7458 7441 338 27 1718 C ATOM 1594 CG LYS A 263 9.380 -18.247 -27.663 1.00 63.65 C ANISOU 1594 CG LYS A 263 8865 7605 7712 596 129 1854 C ATOM 1595 CD LYS A 263 8.048 -17.652 -28.103 1.00 66.62 C ANISOU 1595 CD LYS A 263 9100 8058 8155 657 87 2183 C ATOM 1596 CE LYS A 263 7.445 -16.797 -26.990 1.00 67.74 C ANISOU 1596 CE LYS A 263 9213 8117 8405 963 268 2316 C ATOM 1597 NZ LYS A 263 6.214 -16.063 -27.399 1.00 70.34 N ANISOU 1597 NZ LYS A 263 9370 8497 8859 1085 268 2669 N ATOM 1598 N LEU A 264 12.935 -18.610 -28.482 1.00 59.32 N ANISOU 1598 N LEU A 264 8592 6913 7033 293 186 1202 N ATOM 1599 CA LEU A 264 14.016 -17.846 -27.865 1.00 58.90 C ANISOU 1599 CA LEU A 264 8616 6779 6982 349 250 1069 C ATOM 1600 C LEU A 264 14.884 -17.173 -28.916 1.00 57.86 C ANISOU 1600 C LEU A 264 8574 6634 6776 186 282 961 C ATOM 1601 O LEU A 264 15.312 -16.039 -28.730 1.00 57.88 O ANISOU 1601 O LEU A 264 8683 6582 6724 199 314 946 O ATOM 1602 CB LEU A 264 14.873 -18.761 -26.974 1.00 59.57 C ANISOU 1602 CB LEU A 264 8638 6838 7156 385 248 935 C ATOM 1603 CG LEU A 264 15.949 -18.143 -26.069 1.00 60.01 C ANISOU 1603 CG LEU A 264 8749 6830 7222 412 255 849 C ATOM 1604 CD1 LEU A 264 15.414 -16.949 -25.292 1.00 60.63 C ANISOU 1604 CD1 LEU A 264 8989 6838 7209 510 286 948 C ATOM 1605 CD2 LEU A 264 16.494 -19.192 -25.108 1.00 59.90 C ANISOU 1605 CD2 LEU A 264 8643 6800 7316 457 199 799 C ATOM 1606 N THR A 265 15.139 -17.869 -30.019 1.00 56.99 N ANISOU 1606 N THR A 265 8458 6555 6639 11 293 883 N ATOM 1607 CA THR A 265 15.890 -17.280 -31.132 1.00 57.64 C ANISOU 1607 CA THR A 265 8648 6620 6629 -176 353 781 C ATOM 1608 C THR A 265 15.225 -16.006 -31.667 1.00 57.21 C ANISOU 1608 C THR A 265 8717 6560 6457 -210 297 931 C ATOM 1609 O THR A 265 15.901 -15.013 -31.922 1.00 56.60 O ANISOU 1609 O THR A 265 8752 6441 6313 -274 341 868 O ATOM 1610 CB THR A 265 16.045 -18.267 -32.306 1.00 58.16 C ANISOU 1610 CB THR A 265 8762 6690 6645 -384 408 689 C ATOM 1611 OG1 THR A 265 16.444 -19.545 -31.804 1.00 59.12 O ANISOU 1611 OG1 THR A 265 8781 6789 6892 -314 467 588 O ATOM 1612 CG2 THR A 265 17.087 -17.768 -33.301 1.00 59.08 C ANISOU 1612 CG2 THR A 265 8992 6772 6684 -577 534 535 C ATOM 1613 N VAL A 266 13.906 -16.054 -31.836 1.00 56.91 N ANISOU 1613 N VAL A 266 8648 6566 6410 -171 194 1152 N ATOM 1614 CA VAL A 266 13.147 -14.928 -32.371 1.00 57.79 C ANISOU 1614 CA VAL A 266 8836 6666 6452 -173 123 1355 C ATOM 1615 C VAL A 266 13.156 -13.776 -31.371 1.00 57.83 C ANISOU 1615 C VAL A 266 8894 6580 6499 58 194 1402 C ATOM 1616 O VAL A 266 13.247 -12.615 -31.762 1.00 58.06 O ANISOU 1616 O VAL A 266 9074 6537 6450 39 204 1450 O ATOM 1617 CB VAL A 266 11.689 -15.331 -32.725 1.00 58.67 C ANISOU 1617 CB VAL A 266 8832 6867 6592 -180 -21 1638 C ATOM 1618 CG1 VAL A 266 10.856 -14.117 -33.122 1.00 60.14 C ANISOU 1618 CG1 VAL A 266 9042 7033 6774 -117 -101 1910 C ATOM 1619 CG2 VAL A 266 11.672 -16.355 -33.852 1.00 59.22 C ANISOU 1619 CG2 VAL A 266 8954 6996 6548 -491 -104 1599 C ATOM 1620 N MET A 267 13.068 -14.103 -30.085 1.00 57.85 N ANISOU 1620 N MET A 267 8819 6561 6597 255 252 1385 N ATOM 1621 CA MET A 267 13.128 -13.099 -29.029 1.00 58.93 C ANISOU 1621 CA MET A 267 9081 6575 6733 442 352 1403 C ATOM 1622 C MET A 267 14.445 -12.318 -29.031 1.00 57.98 C ANISOU 1622 C MET A 267 9149 6375 6503 317 396 1214 C ATOM 1623 O MET A 267 14.449 -11.099 -28.869 1.00 58.35 O ANISOU 1623 O MET A 267 9400 6300 6468 365 456 1259 O ATOM 1624 CB MET A 267 12.966 -13.754 -27.660 1.00 60.30 C ANISOU 1624 CB MET A 267 9186 6736 6989 600 401 1382 C ATOM 1625 CG MET A 267 11.563 -14.212 -27.306 1.00 62.52 C ANISOU 1625 CG MET A 267 9308 7066 7379 771 409 1601 C ATOM 1626 SD MET A 267 11.590 -15.124 -25.737 1.00 64.49 S ANISOU 1626 SD MET A 267 9522 7296 7684 886 466 1527 S ATOM 1627 CE MET A 267 11.911 -13.799 -24.567 1.00 63.98 C ANISOU 1627 CE MET A 267 9763 7019 7526 1017 638 1492 C ATOM 1628 N VAL A 268 15.560 -13.021 -29.199 1.00 56.81 N ANISOU 1628 N VAL A 268 8932 6290 6363 156 379 1018 N ATOM 1629 CA VAL A 268 16.879 -12.427 -28.961 1.00 57.14 C ANISOU 1629 CA VAL A 268 9082 6288 6340 32 411 862 C ATOM 1630 C VAL A 268 17.380 -11.618 -30.149 1.00 56.69 C ANISOU 1630 C VAL A 268 9151 6222 6163 -165 427 814 C ATOM 1631 O VAL A 268 17.419 -10.393 -30.112 1.00 56.36 O ANISOU 1631 O VAL A 268 9329 6080 6004 -181 450 854 O ATOM 1632 CB VAL A 268 17.933 -13.501 -28.610 1.00 57.31 C ANISOU 1632 CB VAL A 268 8918 6383 6473 -35 396 711 C ATOM 1633 CG1 VAL A 268 19.300 -12.863 -28.419 1.00 58.04 C ANISOU 1633 CG1 VAL A 268 9064 6463 6524 -193 403 600 C ATOM 1634 CG2 VAL A 268 17.536 -14.257 -27.346 1.00 57.42 C ANISOU 1634 CG2 VAL A 268 8848 6388 6579 132 359 758 C ATOM 1635 N PRO A 297 26.020 -7.384 -30.393 1.00 59.33 N ANISOU 1635 N PRO A 297 9734 6734 6073 -1766 485 240 N ATOM 1636 CA PRO A 297 25.510 -8.671 -29.968 1.00 58.75 C ANISOU 1636 CA PRO A 297 9403 6698 6220 -1500 474 259 C ATOM 1637 C PRO A 297 25.823 -9.032 -28.511 1.00 59.62 C ANISOU 1637 C PRO A 297 9407 6824 6418 -1449 316 338 C ATOM 1638 O PRO A 297 25.096 -9.826 -27.918 1.00 58.40 O ANISOU 1638 O PRO A 297 9185 6641 6363 -1215 280 377 O ATOM 1639 CB PRO A 297 26.217 -9.645 -30.914 1.00 59.17 C ANISOU 1639 CB PRO A 297 9104 6886 6492 -1542 622 165 C ATOM 1640 CG PRO A 297 27.498 -8.973 -31.273 1.00 61.05 C ANISOU 1640 CG PRO A 297 9281 7210 6704 -1841 665 130 C ATOM 1641 CD PRO A 297 27.327 -7.495 -31.056 1.00 61.30 C ANISOU 1641 CD PRO A 297 9729 7136 6424 -2012 568 170 C ATOM 1642 N GLY A 298 26.876 -8.442 -27.942 1.00 62.14 N ANISOU 1642 N GLY A 298 9735 7190 6684 -1700 205 378 N ATOM 1643 CA GLY A 298 27.423 -8.876 -26.656 1.00 63.22 C ANISOU 1643 CA GLY A 298 9724 7374 6919 -1734 15 478 C ATOM 1644 C GLY A 298 26.415 -9.022 -25.534 1.00 62.67 C ANISOU 1644 C GLY A 298 9894 7161 6756 -1543 -67 537 C ATOM 1645 O GLY A 298 26.495 -9.949 -24.729 1.00 62.36 O ANISOU 1645 O GLY A 298 9647 7164 6879 -1444 -177 599 O ATOM 1646 N ARG A 299 25.459 -8.106 -25.495 1.00 63.26 N ANISOU 1646 N ARG A 299 10407 7052 6577 -1483 6 526 N ATOM 1647 CA ARG A 299 24.456 -8.054 -24.433 1.00 63.77 C ANISOU 1647 CA ARG A 299 10757 6946 6526 -1308 -4 582 C ATOM 1648 C ARG A 299 23.506 -9.249 -24.377 1.00 62.17 C ANISOU 1648 C ARG A 299 10326 6769 6524 -983 46 591 C ATOM 1649 O ARG A 299 22.918 -9.513 -23.329 1.00 62.37 O ANISOU 1649 O ARG A 299 10481 6702 6514 -865 16 644 O ATOM 1650 CB ARG A 299 23.645 -6.774 -24.600 1.00 65.20 C ANISOU 1650 CB ARG A 299 11423 6909 6440 -1275 129 581 C ATOM 1651 CG ARG A 299 22.522 -6.555 -23.595 1.00 66.25 C ANISOU 1651 CG ARG A 299 11894 6825 6453 -1065 211 639 C ATOM 1652 CD ARG A 299 22.179 -5.073 -23.489 1.00 68.79 C ANISOU 1652 CD ARG A 299 12770 6888 6479 -1123 337 652 C ATOM 1653 NE ARG A 299 22.362 -4.389 -24.769 1.00 69.70 N ANISOU 1653 NE ARG A 299 12899 7027 6556 -1202 388 619 N ATOM 1654 CZ ARG A 299 22.244 -3.078 -24.945 1.00 72.75 C ANISOU 1654 CZ ARG A 299 13740 7202 6698 -1286 483 628 C ATOM 1655 NH1 ARG A 299 21.905 -2.279 -23.933 1.00 75.75 N ANISOU 1655 NH1 ARG A 299 14628 7307 6846 -1285 576 660 N ATOM 1656 NH2 ARG A 299 22.444 -2.568 -26.154 1.00 72.82 N ANISOU 1656 NH2 ARG A 299 13735 7250 6681 -1376 504 602 N ATOM 1657 N VAL A 300 23.348 -9.965 -25.488 1.00 61.64 N ANISOU 1657 N VAL A 300 9963 6815 6641 -871 132 538 N ATOM 1658 CA VAL A 300 22.447 -11.127 -25.526 1.00 61.07 C ANISOU 1658 CA VAL A 300 9697 6770 6736 -609 171 551 C ATOM 1659 C VAL A 300 23.154 -12.453 -25.871 1.00 62.22 C ANISOU 1659 C VAL A 300 9423 7066 7151 -594 152 508 C ATOM 1660 O VAL A 300 22.492 -13.460 -26.144 1.00 60.35 O ANISOU 1660 O VAL A 300 9040 6849 7039 -418 201 500 O ATOM 1661 CB VAL A 300 21.255 -10.889 -26.481 1.00 59.37 C ANISOU 1661 CB VAL A 300 9583 6504 6470 -461 298 563 C ATOM 1662 CG1 VAL A 300 20.440 -9.693 -26.019 1.00 59.46 C ANISOU 1662 CG1 VAL A 300 9979 6334 6277 -392 353 640 C ATOM 1663 CG2 VAL A 300 21.720 -10.698 -27.917 1.00 59.77 C ANISOU 1663 CG2 VAL A 300 9558 6629 6521 -607 368 486 C ATOM 1664 N GLN A 301 24.489 -12.453 -25.816 1.00 65.11 N ANISOU 1664 N GLN A 301 9601 7526 7612 -780 87 498 N ATOM 1665 CA GLN A 301 25.292 -13.638 -26.137 1.00 66.53 C ANISOU 1665 CA GLN A 301 9366 7823 8088 -744 112 477 C ATOM 1666 C GLN A 301 24.998 -14.783 -25.177 1.00 65.35 C ANISOU 1666 C GLN A 301 9077 7660 8093 -562 6 545 C ATOM 1667 O GLN A 301 25.114 -15.954 -25.537 1.00 64.35 O ANISOU 1667 O GLN A 301 8687 7567 8193 -428 79 518 O ATOM 1668 CB GLN A 301 26.790 -13.306 -26.104 1.00 69.87 C ANISOU 1668 CB GLN A 301 9576 8357 8612 -975 51 511 C ATOM 1669 CG GLN A 301 27.656 -14.266 -26.908 1.00 72.54 C ANISOU 1669 CG GLN A 301 9494 8800 9268 -933 203 469 C ATOM 1670 CD GLN A 301 27.359 -14.219 -28.402 1.00 73.21 C ANISOU 1670 CD GLN A 301 9646 8867 9303 -934 471 319 C ATOM 1671 OE1 GLN A 301 27.152 -13.140 -28.979 1.00 73.50 O ANISOU 1671 OE1 GLN A 301 9948 8878 9100 -1089 513 269 O ATOM 1672 NE2 GLN A 301 27.333 -15.395 -29.038 1.00 73.19 N ANISOU 1672 NE2 GLN A 301 9447 8854 9505 -781 654 250 N ATOM 1673 N ALA A 302 24.622 -14.424 -23.954 1.00 65.97 N ANISOU 1673 N ALA A 302 9377 7662 8024 -574 -148 630 N ATOM 1674 CA ALA A 302 24.216 -15.390 -22.944 1.00 66.02 C ANISOU 1674 CA ALA A 302 9332 7634 8117 -430 -259 701 C ATOM 1675 C ALA A 302 23.072 -16.244 -23.455 1.00 63.62 C ANISOU 1675 C ALA A 302 9001 7302 7869 -195 -122 649 C ATOM 1676 O ALA A 302 23.113 -17.468 -23.357 1.00 63.61 O ANISOU 1676 O ALA A 302 8782 7321 8064 -73 -137 659 O ATOM 1677 CB ALA A 302 23.795 -14.665 -21.677 1.00 66.86 C ANISOU 1677 CB ALA A 302 9803 7625 7975 -509 -380 775 C ATOM 1678 N LEU A 303 22.065 -15.581 -24.015 1.00 62.30 N ANISOU 1678 N LEU A 303 9057 7083 7531 -148 0 616 N ATOM 1679 CA LEU A 303 20.859 -16.249 -24.495 1.00 61.01 C ANISOU 1679 CA LEU A 303 8886 6907 7388 25 95 611 C ATOM 1680 C LEU A 303 21.099 -17.062 -25.768 1.00 60.77 C ANISOU 1680 C LEU A 303 8648 6942 7498 25 204 526 C ATOM 1681 O LEU A 303 20.364 -18.006 -26.041 1.00 60.39 O ANISOU 1681 O LEU A 303 8549 6892 7504 128 242 528 O ATOM 1682 CB LEU A 303 19.740 -15.228 -24.733 1.00 60.85 C ANISOU 1682 CB LEU A 303 9127 6817 7174 71 175 654 C ATOM 1683 CG LEU A 303 19.318 -14.402 -23.505 1.00 61.77 C ANISOU 1683 CG LEU A 303 9527 6812 7129 101 155 728 C ATOM 1684 CD1 LEU A 303 18.423 -13.238 -23.896 1.00 61.85 C ANISOU 1684 CD1 LEU A 303 9783 6728 6988 162 280 778 C ATOM 1685 CD2 LEU A 303 18.622 -15.268 -22.466 1.00 61.61 C ANISOU 1685 CD2 LEU A 303 9493 6761 7154 239 122 789 C ATOM 1686 N ARG A 304 22.120 -16.708 -26.541 1.00 61.16 N ANISOU 1686 N ARG A 304 8611 7038 7590 -114 272 453 N ATOM 1687 CA ARG A 304 22.421 -17.446 -27.756 1.00 62.08 C ANISOU 1687 CA ARG A 304 8588 7181 7818 -135 434 355 C ATOM 1688 C ARG A 304 23.197 -18.725 -27.472 1.00 63.65 C ANISOU 1688 C ARG A 304 8513 7386 8285 -45 459 340 C ATOM 1689 O ARG A 304 23.113 -19.676 -28.248 1.00 63.90 O ANISOU 1689 O ARG A 304 8489 7384 8405 -1 612 267 O ATOM 1690 CB ARG A 304 23.156 -16.566 -28.766 1.00 64.11 C ANISOU 1690 CB ARG A 304 8880 7471 8008 -324 549 276 C ATOM 1691 CG ARG A 304 22.291 -15.431 -29.295 1.00 64.33 C ANISOU 1691 CG ARG A 304 9197 7465 7780 -399 544 297 C ATOM 1692 CD ARG A 304 22.753 -14.921 -30.650 1.00 66.29 C ANISOU 1692 CD ARG A 304 9513 7729 7945 -593 689 203 C ATOM 1693 NE ARG A 304 22.030 -13.717 -31.082 1.00 66.67 N ANISOU 1693 NE ARG A 304 9843 7732 7756 -669 650 254 N ATOM 1694 CZ ARG A 304 20.795 -13.695 -31.595 1.00 66.19 C ANISOU 1694 CZ ARG A 304 9926 7634 7587 -621 623 329 C ATOM 1695 NH1 ARG A 304 20.083 -14.814 -31.743 1.00 65.45 N ANISOU 1695 NH1 ARG A 304 9750 7552 7563 -531 622 352 N ATOM 1696 NH2 ARG A 304 20.257 -12.531 -31.956 1.00 66.50 N ANISOU 1696 NH2 ARG A 304 10195 7621 7449 -674 583 407 N ATOM 1697 N HIS A 305 23.946 -18.761 -26.371 1.00 65.45 N ANISOU 1697 N HIS A 305 8595 7637 8636 -30 306 426 N ATOM 1698 CA HIS A 305 24.563 -20.014 -25.921 1.00 67.33 C ANISOU 1698 CA HIS A 305 8564 7862 9154 95 286 466 C ATOM 1699 C HIS A 305 23.499 -20.901 -25.290 1.00 64.64 C ANISOU 1699 C HIS A 305 8324 7452 8782 246 208 505 C ATOM 1700 O HIS A 305 23.509 -22.116 -25.471 1.00 64.94 O ANISOU 1700 O HIS A 305 8252 7435 8985 368 287 484 O ATOM 1701 CB HIS A 305 25.711 -19.758 -24.941 1.00 70.73 C ANISOU 1701 CB HIS A 305 8790 8354 9730 25 94 595 C ATOM 1702 CG HIS A 305 26.845 -18.983 -25.539 1.00 75.56 C ANISOU 1702 CG HIS A 305 9246 9056 10405 -144 168 582 C ATOM 1703 ND1 HIS A 305 27.341 -19.239 -26.802 1.00 78.01 N ANISOU 1703 ND1 HIS A 305 9415 9378 10848 -141 452 469 N ATOM 1704 CD2 HIS A 305 27.577 -17.951 -25.052 1.00 78.14 C ANISOU 1704 CD2 HIS A 305 9565 9462 10662 -352 7 669 C ATOM 1705 CE1 HIS A 305 28.325 -18.398 -27.067 1.00 79.86 C ANISOU 1705 CE1 HIS A 305 9523 9709 11109 -326 470 490 C ATOM 1706 NE2 HIS A 305 28.491 -17.608 -26.020 1.00 80.19 N ANISOU 1706 NE2 HIS A 305 9638 9800 11030 -464 186 617 N ATOM 1707 N GLY A 306 22.571 -20.278 -24.570 1.00 62.09 N ANISOU 1707 N GLY A 306 8231 7116 8242 235 81 561 N ATOM 1708 CA GLY A 306 21.429 -20.977 -23.999 1.00 60.79 C ANISOU 1708 CA GLY A 306 8176 6900 8019 355 30 604 C ATOM 1709 C GLY A 306 20.644 -21.768 -25.025 1.00 60.03 C ANISOU 1709 C GLY A 306 8105 6786 7917 405 180 537 C ATOM 1710 O GLY A 306 20.207 -22.880 -24.743 1.00 61.21 O ANISOU 1710 O GLY A 306 8234 6890 8131 496 163 557 O ATOM 1711 N VAL A 307 20.466 -21.194 -26.213 1.00 59.45 N ANISOU 1711 N VAL A 307 8107 6738 7742 311 310 468 N ATOM 1712 CA VAL A 307 19.795 -21.875 -27.326 1.00 59.16 C ANISOU 1712 CA VAL A 307 8141 6680 7656 278 436 413 C ATOM 1713 C VAL A 307 20.584 -23.096 -27.790 1.00 60.46 C ANISOU 1713 C VAL A 307 8189 6774 8009 310 580 320 C ATOM 1714 O VAL A 307 20.010 -24.170 -27.992 1.00 60.90 O ANISOU 1714 O VAL A 307 8311 6766 8062 339 621 308 O ATOM 1715 CB VAL A 307 19.594 -20.928 -28.533 1.00 59.48 C ANISOU 1715 CB VAL A 307 8312 6753 7533 124 524 371 C ATOM 1716 CG1 VAL A 307 19.163 -21.697 -29.782 1.00 59.92 C ANISOU 1716 CG1 VAL A 307 8471 6772 7522 16 652 307 C ATOM 1717 CG2 VAL A 307 18.573 -19.851 -28.200 1.00 58.96 C ANISOU 1717 CG2 VAL A 307 8380 6722 7298 134 414 490 C ATOM 1718 N LEU A 308 21.892 -22.922 -27.972 1.00 61.49 N ANISOU 1718 N LEU A 308 8151 6905 8304 302 677 265 N ATOM 1719 CA LEU A 308 22.757 -24.025 -28.381 1.00 63.72 C ANISOU 1719 CA LEU A 308 8291 7095 8821 378 872 193 C ATOM 1720 C LEU A 308 22.802 -25.107 -27.313 1.00 65.02 C ANISOU 1720 C LEU A 308 8340 7195 9168 558 755 279 C ATOM 1721 O LEU A 308 22.784 -26.291 -27.637 1.00 66.71 O ANISOU 1721 O LEU A 308 8581 7283 9481 639 900 231 O ATOM 1722 CB LEU A 308 24.165 -23.530 -28.698 1.00 65.16 C ANISOU 1722 CB LEU A 308 8252 7317 9189 345 1001 160 C ATOM 1723 CG LEU A 308 24.245 -22.621 -29.927 1.00 65.16 C ANISOU 1723 CG LEU A 308 8391 7352 9014 147 1171 50 C ATOM 1724 CD1 LEU A 308 25.663 -22.105 -30.103 1.00 67.33 C ANISOU 1724 CD1 LEU A 308 8411 7686 9482 102 1289 38 C ATOM 1725 CD2 LEU A 308 23.771 -23.326 -31.191 1.00 65.53 C ANISOU 1725 CD2 LEU A 308 8667 7283 8946 69 1424 -83 C ATOM 1726 N VAL A 309 22.846 -24.694 -26.047 1.00 65.09 N ANISOU 1726 N VAL A 309 8269 7268 9194 597 499 407 N ATOM 1727 CA VAL A 309 22.745 -25.621 -24.919 1.00 65.78 C ANISOU 1727 CA VAL A 309 8298 7294 9399 731 336 511 C ATOM 1728 C VAL A 309 21.421 -26.385 -24.942 1.00 64.51 C ANISOU 1728 C VAL A 309 8359 7073 9075 751 334 495 C ATOM 1729 O VAL A 309 21.404 -27.594 -24.731 1.00 65.42 O ANISOU 1729 O VAL A 309 8467 7078 9309 854 355 506 O ATOM 1730 CB VAL A 309 22.935 -24.888 -23.564 1.00 66.17 C ANISOU 1730 CB VAL A 309 8312 7415 9412 696 52 650 C ATOM 1731 CG1 VAL A 309 22.041 -25.460 -22.466 1.00 65.86 C ANISOU 1731 CG1 VAL A 309 8415 7328 9281 751 -122 734 C ATOM 1732 CG2 VAL A 309 24.396 -24.947 -23.134 1.00 68.71 C ANISOU 1732 CG2 VAL A 309 8329 7759 10018 718 -30 750 C ATOM 1733 N LEU A 310 20.322 -25.680 -25.194 1.00 63.08 N ANISOU 1733 N LEU A 310 8366 6962 8637 649 307 490 N ATOM 1734 CA LEU A 310 18.997 -26.306 -25.257 1.00 63.26 C ANISOU 1734 CA LEU A 310 8561 6966 8507 631 289 514 C ATOM 1735 C LEU A 310 18.928 -27.452 -26.259 1.00 65.01 C ANISOU 1735 C LEU A 310 8869 7080 8748 600 466 422 C ATOM 1736 O LEU A 310 18.286 -28.467 -26.006 1.00 65.36 O ANISOU 1736 O LEU A 310 9011 7059 8763 616 433 451 O ATOM 1737 CB LEU A 310 17.918 -25.277 -25.604 1.00 62.26 C ANISOU 1737 CB LEU A 310 8561 6942 8152 530 260 557 C ATOM 1738 CG LEU A 310 17.169 -24.693 -24.409 1.00 61.13 C ANISOU 1738 CG LEU A 310 8458 6847 7920 584 113 680 C ATOM 1739 CD1 LEU A 310 16.492 -23.392 -24.795 1.00 60.94 C ANISOU 1739 CD1 LEU A 310 8515 6898 7742 531 133 728 C ATOM 1740 CD2 LEU A 310 16.150 -25.696 -23.896 1.00 61.19 C ANISOU 1740 CD2 LEU A 310 8520 6837 7890 615 57 753 C ATOM 1741 N ARG A 311 19.582 -27.282 -27.399 1.00 66.98 N ANISOU 1741 N ARG A 311 9127 7297 9025 529 669 307 N ATOM 1742 CA ARG A 311 19.631 -28.335 -28.403 1.00 69.61 C ANISOU 1742 CA ARG A 311 9612 7482 9351 475 895 197 C ATOM 1743 C ARG A 311 20.659 -29.403 -28.041 1.00 69.41 C ANISOU 1743 C ARG A 311 9458 7295 9618 669 1021 169 C ATOM 1744 O ARG A 311 20.436 -30.581 -28.290 1.00 70.07 O ANISOU 1744 O ARG A 311 9705 7214 9702 686 1139 126 O ATOM 1745 CB ARG A 311 19.922 -27.735 -29.778 1.00 73.48 C ANISOU 1745 CB ARG A 311 10211 7974 9734 303 1101 80 C ATOM 1746 CG ARG A 311 18.780 -26.864 -30.295 1.00 74.65 C ANISOU 1746 CG ARG A 311 10521 8251 9592 99 969 139 C ATOM 1747 CD ARG A 311 18.924 -26.534 -31.773 1.00 77.45 C ANISOU 1747 CD ARG A 311 11072 8569 9786 -128 1161 29 C ATOM 1748 NE ARG A 311 17.743 -25.844 -32.296 1.00 77.41 N ANISOU 1748 NE ARG A 311 11221 8675 9516 -331 995 134 N ATOM 1749 CZ ARG A 311 17.708 -24.579 -32.721 1.00 77.75 C ANISOU 1749 CZ ARG A 311 11264 8816 9460 -424 943 167 C ATOM 1750 NH1 ARG A 311 18.795 -23.810 -32.714 1.00 78.85 N ANISOU 1750 NH1 ARG A 311 11282 8968 9710 -368 1046 84 N ATOM 1751 NH2 ARG A 311 16.564 -24.074 -33.170 1.00 77.50 N ANISOU 1751 NH2 ARG A 311 11351 8872 9223 -586 776 308 N ATOM 1752 N ALA A 312 21.774 -28.986 -27.445 1.00 63.51 N ANISOU 1752 N ALA A 312 9932 7671 6525 372 1311 290 N ATOM 1753 CA ALA A 312 22.822 -29.907 -26.992 1.00 61.98 C ANISOU 1753 CA ALA A 312 9628 7408 6511 287 1291 260 C ATOM 1754 C ALA A 312 22.288 -30.897 -25.978 1.00 60.40 C ANISOU 1754 C ALA A 312 9389 7285 6273 189 1074 178 C ATOM 1755 O ALA A 312 22.648 -32.071 -25.991 1.00 60.50 O ANISOU 1755 O ALA A 312 9378 7301 6308 162 1020 137 O ATOM 1756 CB ALA A 312 23.976 -29.135 -26.376 1.00 62.31 C ANISOU 1756 CB ALA A 312 9529 7280 6865 223 1348 288 C ATOM 1757 N VAL A 313 21.434 -30.400 -25.090 1.00 59.02 N ANISOU 1757 N VAL A 313 9232 7143 6047 148 994 163 N ATOM 1758 CA VAL A 313 20.832 -31.207 -24.032 1.00 56.96 C ANISOU 1758 CA VAL A 313 8996 6896 5750 77 880 106 C ATOM 1759 C VAL A 313 20.101 -32.442 -24.583 1.00 56.62 C ANISOU 1759 C VAL A 313 8931 6941 5641 97 836 61 C ATOM 1760 O VAL A 313 20.174 -33.526 -23.995 1.00 55.42 O ANISOU 1760 O VAL A 313 8780 6772 5504 41 775 15 O ATOM 1761 CB VAL A 313 19.925 -30.317 -23.144 1.00 56.11 C ANISOU 1761 CB VAL A 313 8958 6758 5601 64 909 122 C ATOM 1762 CG1 VAL A 313 19.166 -31.109 -22.090 1.00 56.24 C ANISOU 1762 CG1 VAL A 313 8984 6789 5592 55 933 95 C ATOM 1763 CG2 VAL A 313 20.763 -29.224 -22.502 1.00 56.51 C ANISOU 1763 CG2 VAL A 313 9120 6660 5691 13 836 113 C ATOM 1764 N VAL A 314 19.422 -32.280 -25.716 1.00 56.63 N ANISOU 1764 N VAL A 314 8938 7002 5574 190 836 66 N ATOM 1765 CA VAL A 314 18.686 -33.384 -26.335 1.00 56.76 C ANISOU 1765 CA VAL A 314 8939 7059 5565 226 720 3 C ATOM 1766 C VAL A 314 19.654 -34.399 -26.939 1.00 56.72 C ANISOU 1766 C VAL A 314 8983 7055 5511 241 717 -16 C ATOM 1767 O VAL A 314 19.527 -35.600 -26.709 1.00 55.92 O ANISOU 1767 O VAL A 314 8839 6966 5441 195 639 -74 O ATOM 1768 CB VAL A 314 17.725 -32.884 -27.429 1.00 57.79 C ANISOU 1768 CB VAL A 314 9122 7197 5639 354 622 -5 C ATOM 1769 CG1 VAL A 314 16.854 -34.022 -27.940 1.00 58.34 C ANISOU 1769 CG1 VAL A 314 9154 7253 5760 391 413 -98 C ATOM 1770 CG2 VAL A 314 16.866 -31.744 -26.897 1.00 58.21 C ANISOU 1770 CG2 VAL A 314 9104 7229 5781 347 658 28 C ATOM 1771 N ILE A 315 20.624 -33.911 -27.705 1.00 57.47 N ANISOU 1771 N ILE A 315 9169 7107 5559 311 847 40 N ATOM 1772 CA ILE A 315 21.653 -34.779 -28.271 1.00 58.38 C ANISOU 1772 CA ILE A 315 9332 7171 5676 334 928 41 C ATOM 1773 C ILE A 315 22.332 -35.558 -27.157 1.00 57.85 C ANISOU 1773 C ILE A 315 9115 7085 5778 198 882 11 C ATOM 1774 O ILE A 315 22.560 -36.752 -27.289 1.00 58.69 O ANISOU 1774 O ILE A 315 9218 7198 5882 183 839 -30 O ATOM 1775 CB ILE A 315 22.737 -33.996 -29.041 1.00 59.83 C ANISOU 1775 CB ILE A 315 9603 7231 5898 421 1191 133 C ATOM 1776 CG1 ILE A 315 22.154 -33.342 -30.294 1.00 61.82 C ANISOU 1776 CG1 ILE A 315 10127 7457 5903 603 1252 167 C ATOM 1777 CG2 ILE A 315 23.876 -34.922 -29.446 1.00 60.53 C ANISOU 1777 CG2 ILE A 315 9694 7214 6088 431 1339 146 C ATOM 1778 CD1 ILE A 315 23.116 -32.412 -31.000 1.00 63.95 C ANISOU 1778 CD1 ILE A 315 10523 7562 6213 706 1598 279 C ATOM 1779 N ALA A 316 22.655 -34.872 -26.064 1.00 58.11 N ANISOU 1779 N ALA A 316 9065 7071 5941 115 862 28 N ATOM 1780 CA ALA A 316 23.319 -35.490 -24.911 1.00 57.60 C ANISOU 1780 CA ALA A 316 8940 6933 6011 16 747 -8 C ATOM 1781 C ALA A 316 22.489 -36.629 -24.323 1.00 56.88 C ANISOU 1781 C ALA A 316 8890 6905 5814 -26 641 -71 C ATOM 1782 O ALA A 316 23.002 -37.712 -24.052 1.00 56.30 O ANISOU 1782 O ALA A 316 8803 6801 5787 -62 576 -107 O ATOM 1783 CB ALA A 316 23.600 -34.442 -23.845 1.00 57.58 C ANISOU 1783 CB ALA A 316 8944 6829 6104 -28 679 3 C ATOM 1784 N PHE A 317 21.202 -36.379 -24.133 1.00 57.06 N ANISOU 1784 N PHE A 317 8946 6986 5747 -17 648 -78 N ATOM 1785 CA PHE A 317 20.315 -37.394 -23.597 1.00 57.16 C ANISOU 1785 CA PHE A 317 8967 7004 5748 -51 620 -126 C ATOM 1786 C PHE A 317 20.319 -38.605 -24.522 1.00 57.26 C ANISOU 1786 C PHE A 317 8925 7074 5756 -29 568 -174 C ATOM 1787 O PHE A 317 20.669 -39.698 -24.105 1.00 57.62 O ANISOU 1787 O PHE A 317 8975 7094 5822 -74 534 -208 O ATOM 1788 CB PHE A 317 18.900 -36.839 -23.425 1.00 57.91 C ANISOU 1788 CB PHE A 317 9037 7095 5871 -34 683 -118 C ATOM 1789 CG PHE A 317 18.034 -37.663 -22.526 1.00 58.64 C ANISOU 1789 CG PHE A 317 9139 7099 6042 -74 757 -143 C ATOM 1790 CD1 PHE A 317 18.325 -37.770 -21.178 1.00 59.44 C ANISOU 1790 CD1 PHE A 317 9432 7073 6077 -107 836 -124 C ATOM 1791 CD2 PHE A 317 16.923 -38.323 -23.023 1.00 60.36 C ANISOU 1791 CD2 PHE A 317 9202 7308 6422 -61 747 -187 C ATOM 1792 CE1 PHE A 317 17.531 -38.531 -20.337 1.00 60.91 C ANISOU 1792 CE1 PHE A 317 9694 7126 6324 -119 993 -128 C ATOM 1793 CE2 PHE A 317 16.121 -39.084 -22.189 1.00 61.79 C ANISOU 1793 CE2 PHE A 317 9360 7354 6761 -97 891 -197 C ATOM 1794 CZ PHE A 317 16.426 -39.189 -20.843 1.00 61.81 C ANISOU 1794 CZ PHE A 317 9592 7230 6662 -122 1060 -157 C ATOM 1795 N VAL A 318 19.980 -38.399 -25.788 1.00 58.17 N ANISOU 1795 N VAL A 318 9041 7241 5819 56 543 -180 N ATOM 1796 CA VAL A 318 19.866 -39.512 -26.733 1.00 59.28 C ANISOU 1796 CA VAL A 318 9204 7401 5916 105 455 -239 C ATOM 1797 C VAL A 318 21.112 -40.383 -26.710 1.00 59.32 C ANISOU 1797 C VAL A 318 9227 7386 5923 73 504 -236 C ATOM 1798 O VAL A 318 21.043 -41.569 -26.403 1.00 60.00 O ANISOU 1798 O VAL A 318 9277 7472 6046 25 448 -287 O ATOM 1799 CB VAL A 318 19.666 -39.037 -28.185 1.00 60.30 C ANISOU 1799 CB VAL A 318 9477 7528 5904 251 408 -238 C ATOM 1800 CG1 VAL A 318 19.653 -40.231 -29.133 1.00 60.90 C ANISOU 1800 CG1 VAL A 318 9667 7581 5890 323 292 -309 C ATOM 1801 CG2 VAL A 318 18.394 -38.212 -28.317 1.00 61.23 C ANISOU 1801 CG2 VAL A 318 9562 7640 6062 299 295 -253 C ATOM 1802 N VAL A 319 22.247 -39.770 -27.021 1.00 59.49 N ANISOU 1802 N VAL A 319 9281 7361 5961 102 629 -172 N ATOM 1803 CA VAL A 319 23.507 -40.479 -27.187 1.00 60.40 C ANISOU 1803 CA VAL A 319 9374 7403 6169 91 709 -159 C ATOM 1804 C VAL A 319 23.917 -41.267 -25.933 1.00 61.64 C ANISOU 1804 C VAL A 319 9434 7529 6455 -21 601 -194 C ATOM 1805 O VAL A 319 24.390 -42.403 -26.035 1.00 62.34 O ANISOU 1805 O VAL A 319 9506 7596 6584 -36 586 -223 O ATOM 1806 CB VAL A 319 24.622 -39.492 -27.586 1.00 61.06 C ANISOU 1806 CB VAL A 319 9441 7369 6389 135 905 -74 C ATOM 1807 CG1 VAL A 319 26.002 -40.126 -27.477 1.00 62.02 C ANISOU 1807 CG1 VAL A 319 9445 7349 6769 101 991 -57 C ATOM 1808 CG2 VAL A 319 24.380 -38.990 -29.000 1.00 62.19 C ANISOU 1808 CG2 VAL A 319 9791 7492 6345 289 1068 -31 C ATOM 1809 N CYS A 320 23.732 -40.676 -24.756 1.00 62.55 N ANISOU 1809 N CYS A 320 9542 7615 6607 -81 523 -191 N ATOM 1810 CA CYS A 320 24.158 -41.320 -23.512 1.00 62.26 C ANISOU 1810 CA CYS A 320 9530 7491 6634 -149 394 -223 C ATOM 1811 C CYS A 320 23.197 -42.398 -23.022 1.00 62.88 C ANISOU 1811 C CYS A 320 9679 7610 6600 -175 371 -271 C ATOM 1812 O CYS A 320 23.619 -43.305 -22.309 1.00 63.51 O ANISOU 1812 O CYS A 320 9816 7615 6699 -206 292 -299 O ATOM 1813 CB CYS A 320 24.362 -40.279 -22.407 1.00 62.00 C ANISOU 1813 CB CYS A 320 9576 7347 6635 -168 303 -208 C ATOM 1814 SG CYS A 320 25.859 -39.283 -22.596 1.00 62.10 S ANISOU 1814 SG CYS A 320 9445 7200 6950 -161 259 -175 S ATOM 1815 N TRP A 321 21.918 -42.293 -23.386 1.00 64.11 N ANISOU 1815 N TRP A 321 9823 7846 6691 -157 436 -280 N ATOM 1816 CA TRP A 321 20.880 -43.164 -22.822 1.00 66.24 C ANISOU 1816 CA TRP A 321 10111 8089 6967 -184 469 -317 C ATOM 1817 C TRP A 321 20.276 -44.174 -23.805 1.00 67.01 C ANISOU 1817 C TRP A 321 10099 8247 7113 -169 434 -376 C ATOM 1818 O TRP A 321 19.743 -45.191 -23.366 1.00 68.35 O ANISOU 1818 O TRP A 321 10250 8364 7356 -202 461 -414 O ATOM 1819 CB TRP A 321 19.766 -42.322 -22.181 1.00 68.58 C ANISOU 1819 CB TRP A 321 10443 8330 7281 -180 578 -289 C ATOM 1820 CG TRP A 321 20.111 -41.800 -20.801 1.00 71.67 C ANISOU 1820 CG TRP A 321 11061 8585 7583 -188 619 -250 C ATOM 1821 CD1 TRP A 321 21.321 -41.328 -20.383 1.00 73.31 C ANISOU 1821 CD1 TRP A 321 11380 8737 7734 -185 482 -240 C ATOM 1822 CD2 TRP A 321 19.231 -41.690 -19.672 1.00 74.73 C ANISOU 1822 CD2 TRP A 321 11633 8814 7945 -177 801 -222 C ATOM 1823 NE1 TRP A 321 21.253 -40.941 -19.069 1.00 75.18 N ANISOU 1823 NE1 TRP A 321 11907 8800 7858 -164 493 -223 N ATOM 1824 CE2 TRP A 321 19.985 -41.153 -18.606 1.00 75.58 C ANISOU 1824 CE2 TRP A 321 12044 8784 7890 -151 731 -202 C ATOM 1825 CE3 TRP A 321 17.883 -42.000 -19.454 1.00 76.62 C ANISOU 1825 CE3 TRP A 321 11818 8965 8329 -175 1033 -212 C ATOM 1826 CZ2 TRP A 321 19.440 -40.915 -17.346 1.00 77.07 C ANISOU 1826 CZ2 TRP A 321 12578 8754 7950 -103 904 -166 C ATOM 1827 CZ3 TRP A 321 17.341 -41.763 -18.194 1.00 78.03 C ANISOU 1827 CZ3 TRP A 321 12276 8918 8452 -140 1283 -160 C ATOM 1828 CH2 TRP A 321 18.120 -41.224 -17.159 1.00 78.21 C ANISOU 1828 CH2 TRP A 321 12694 8813 8208 -95 1227 -134 C ATOM 1829 N LEU A 322 20.358 -43.924 -25.115 1.00 67.03 N ANISOU 1829 N LEU A 322 10074 8320 7072 -103 374 -389 N ATOM 1830 CA LEU A 322 19.753 -44.841 -26.104 1.00 66.29 C ANISOU 1830 CA LEU A 322 9949 8239 6995 -59 263 -466 C ATOM 1831 C LEU A 322 20.402 -46.222 -26.134 1.00 64.16 C ANISOU 1831 C LEU A 322 9694 7962 6719 -88 250 -503 C ATOM 1832 O LEU A 322 19.698 -47.229 -26.127 1.00 65.62 O ANISOU 1832 O LEU A 322 9813 8114 7003 -109 185 -572 O ATOM 1833 CB LEU A 322 19.762 -44.252 -27.519 1.00 67.58 C ANISOU 1833 CB LEU A 322 10222 8426 7027 63 185 -472 C ATOM 1834 CG LEU A 322 19.067 -45.107 -28.591 1.00 69.64 C ANISOU 1834 CG LEU A 322 10541 8647 7270 146 -22 -574 C ATOM 1835 CD1 LEU A 322 17.566 -45.203 -28.350 1.00 70.76 C ANISOU 1835 CD1 LEU A 322 10500 8721 7663 125 -187 -648 C ATOM 1836 CD2 LEU A 322 19.333 -44.542 -29.975 1.00 71.29 C ANISOU 1836 CD2 LEU A 322 11018 8827 7241 312 -78 -567 C ATOM 1837 N PRO A 323 21.739 -46.283 -26.184 1.00 61.27 N ANISOU 1837 N PRO A 323 9385 7597 6298 -88 316 -459 N ATOM 1838 CA PRO A 323 22.357 -47.607 -26.173 1.00 61.64 C ANISOU 1838 CA PRO A 323 9431 7622 6366 -115 308 -491 C ATOM 1839 C PRO A 323 22.038 -48.415 -24.909 1.00 62.14 C ANISOU 1839 C PRO A 323 9459 7642 6509 -201 300 -513 C ATOM 1840 O PRO A 323 21.892 -49.632 -24.984 1.00 62.45 O ANISOU 1840 O PRO A 323 9480 7667 6581 -220 275 -565 O ATOM 1841 CB PRO A 323 23.855 -47.301 -26.252 1.00 61.27 C ANISOU 1841 CB PRO A 323 9392 7525 6361 -105 398 -427 C ATOM 1842 CG PRO A 323 23.939 -45.914 -26.782 1.00 61.34 C ANISOU 1842 CG PRO A 323 9433 7535 6336 -43 476 -370 C ATOM 1843 CD PRO A 323 22.740 -45.212 -26.244 1.00 60.68 C ANISOU 1843 CD PRO A 323 9336 7503 6215 -65 405 -382 C ATOM 1844 N TYR A 324 21.924 -47.737 -23.768 1.00 62.71 N ANISOU 1844 N TYR A 324 9572 7662 6590 -235 339 -471 N ATOM 1845 CA TYR A 324 21.639 -48.390 -22.488 1.00 62.33 C ANISOU 1845 CA TYR A 324 9615 7511 6557 -278 386 -474 C ATOM 1846 C TYR A 324 20.311 -49.143 -22.518 1.00 62.52 C ANISOU 1846 C TYR A 324 9557 7498 6698 -294 470 -519 C ATOM 1847 O TYR A 324 20.221 -50.258 -22.007 1.00 62.63 O ANISOU 1847 O TYR A 324 9607 7433 6753 -319 525 -540 O ATOM 1848 CB TYR A 324 21.644 -47.342 -21.373 1.00 62.57 C ANISOU 1848 CB TYR A 324 9802 7447 6522 -272 423 -421 C ATOM 1849 CG TYR A 324 21.323 -47.832 -19.972 1.00 63.57 C ANISOU 1849 CG TYR A 324 10170 7399 6584 -270 518 -407 C ATOM 1850 CD1 TYR A 324 22.323 -48.315 -19.134 1.00 64.31 C ANISOU 1850 CD1 TYR A 324 10479 7372 6583 -254 391 -410 C ATOM 1851 CD2 TYR A 324 20.027 -47.762 -19.470 1.00 64.84 C ANISOU 1851 CD2 TYR A 324 10376 7460 6798 -263 749 -387 C ATOM 1852 CE1 TYR A 324 22.036 -48.743 -17.843 1.00 66.08 C ANISOU 1852 CE1 TYR A 324 11046 7386 6672 -212 483 -393 C ATOM 1853 CE2 TYR A 324 19.730 -48.186 -18.181 1.00 66.97 C ANISOU 1853 CE2 TYR A 324 10954 7509 6983 -231 928 -355 C ATOM 1854 CZ TYR A 324 20.736 -48.676 -17.367 1.00 67.34 C ANISOU 1854 CZ TYR A 324 11304 7442 6840 -195 792 -358 C ATOM 1855 OH TYR A 324 20.439 -49.082 -16.079 1.00 68.82 O ANISOU 1855 OH TYR A 324 11915 7364 6869 -124 976 -322 O ATOM 1856 N HIS A 325 19.292 -48.543 -23.121 1.00 62.82 N ANISOU 1856 N HIS A 325 9468 7559 6841 -273 469 -536 N ATOM 1857 CA HIS A 325 17.975 -49.177 -23.195 1.00 64.96 C ANISOU 1857 CA HIS A 325 9581 7733 7367 -287 515 -590 C ATOM 1858 C HIS A 325 17.842 -50.167 -24.343 1.00 65.15 C ANISOU 1858 C HIS A 325 9492 7792 7469 -271 324 -688 C ATOM 1859 O HIS A 325 16.932 -51.000 -24.351 1.00 66.02 O ANISOU 1859 O HIS A 325 9450 7785 7850 -293 323 -752 O ATOM 1860 CB HIS A 325 16.889 -48.120 -23.272 1.00 66.77 C ANISOU 1860 CB HIS A 325 9694 7909 7764 -265 553 -577 C ATOM 1861 CG HIS A 325 16.745 -47.348 -22.005 1.00 68.40 C ANISOU 1861 CG HIS A 325 10040 8014 7935 -276 800 -487 C ATOM 1862 ND1 HIS A 325 15.953 -47.778 -20.963 1.00 71.04 N ANISOU 1862 ND1 HIS A 325 10403 8131 8455 -293 1088 -456 N ATOM 1863 CD2 HIS A 325 17.322 -46.197 -21.590 1.00 68.49 C ANISOU 1863 CD2 HIS A 325 10218 8069 7735 -256 821 -421 C ATOM 1864 CE1 HIS A 325 16.031 -46.913 -19.968 1.00 71.63 C ANISOU 1864 CE1 HIS A 325 10713 8118 8383 -269 1278 -372 C ATOM 1865 NE2 HIS A 325 16.857 -45.945 -20.323 1.00 70.39 N ANISOU 1865 NE2 HIS A 325 10628 8126 7991 -253 1085 -359 N ATOM 1866 N VAL A 326 18.741 -50.072 -25.315 1.00 64.35 N ANISOU 1866 N VAL A 326 9482 7809 7157 -221 181 -699 N ATOM 1867 CA VAL A 326 18.865 -51.113 -26.321 1.00 64.39 C ANISOU 1867 CA VAL A 326 9498 7822 7145 -185 25 -784 C ATOM 1868 C VAL A 326 19.373 -52.368 -25.628 1.00 63.85 C ANISOU 1868 C VAL A 326 9433 7722 7101 -252 122 -786 C ATOM 1869 O VAL A 326 18.737 -53.414 -25.721 1.00 66.58 O ANISOU 1869 O VAL A 326 9682 7989 7623 -274 74 -862 O ATOM 1870 CB VAL A 326 19.807 -50.697 -27.467 1.00 64.06 C ANISOU 1870 CB VAL A 326 9637 7856 6845 -91 -41 -768 C ATOM 1871 CG1 VAL A 326 20.179 -51.890 -28.338 1.00 64.63 C ANISOU 1871 CG1 VAL A 326 9811 7904 6839 -44 -133 -839 C ATOM 1872 CG2 VAL A 326 19.157 -49.602 -28.300 1.00 64.71 C ANISOU 1872 CG2 VAL A 326 9774 7932 6878 5 -170 -783 C ATOM 1873 N ARG A 327 20.490 -52.254 -24.906 1.00 62.08 N ANISOU 1873 N ARG A 327 9315 7530 6743 -279 231 -709 N ATOM 1874 CA ARG A 327 21.090 -53.413 -24.237 1.00 61.60 C ANISOU 1874 CA ARG A 327 9298 7422 6684 -323 285 -709 C ATOM 1875 C ARG A 327 20.132 -54.073 -23.259 1.00 63.05 C ANISOU 1875 C ARG A 327 9453 7476 7028 -369 416 -721 C ATOM 1876 O ARG A 327 20.079 -55.292 -23.187 1.00 63.93 O ANISOU 1876 O ARG A 327 9542 7534 7215 -393 436 -762 O ATOM 1877 CB ARG A 327 22.385 -53.056 -23.511 1.00 60.35 C ANISOU 1877 CB ARG A 327 9256 7254 6419 -329 302 -638 C ATOM 1878 CG ARG A 327 23.156 -54.288 -23.053 1.00 60.82 C ANISOU 1878 CG ARG A 327 9369 7255 6484 -351 289 -649 C ATOM 1879 CD ARG A 327 24.353 -53.959 -22.171 1.00 61.55 C ANISOU 1879 CD ARG A 327 9573 7264 6547 -345 215 -598 C ATOM 1880 NE ARG A 327 24.017 -53.006 -21.113 1.00 62.33 N ANISOU 1880 NE ARG A 327 9825 7281 6575 -334 224 -559 N ATOM 1881 CZ ARG A 327 23.266 -53.268 -20.043 1.00 62.68 C ANISOU 1881 CZ ARG A 327 10062 7202 6549 -327 330 -548 C ATOM 1882 NH1 ARG A 327 22.759 -54.477 -19.834 1.00 62.54 N ANISOU 1882 NH1 ARG A 327 10072 7127 6563 -341 443 -572 N ATOM 1883 NH2 ARG A 327 23.027 -52.303 -19.162 1.00 64.02 N ANISOU 1883 NH2 ARG A 327 10432 7271 6620 -294 360 -506 N ATOM 1884 N ARG A 328 19.384 -53.275 -22.505 1.00 65.58 N ANISOU 1884 N ARG A 328 9788 7714 7414 -372 551 -676 N ATOM 1885 CA ARG A 328 18.393 -53.820 -21.572 1.00 68.35 C ANISOU 1885 CA ARG A 328 10133 7869 7967 -396 788 -665 C ATOM 1886 C ARG A 328 17.274 -54.565 -22.315 1.00 70.11 C ANISOU 1886 C ARG A 328 10072 8017 8548 -417 750 -757 C ATOM 1887 O ARG A 328 16.774 -55.581 -21.826 1.00 73.17 O ANISOU 1887 O ARG A 328 10410 8239 9150 -445 920 -772 O ATOM 1888 CB ARG A 328 17.810 -52.727 -20.655 1.00 69.69 C ANISOU 1888 CB ARG A 328 10410 7920 8146 -376 999 -586 C ATOM 1889 CG ARG A 328 18.420 -52.668 -19.258 1.00 70.59 C ANISOU 1889 CG ARG A 328 10910 7902 8008 -341 1155 -505 C ATOM 1890 CD ARG A 328 18.030 -51.375 -18.542 1.00 72.39 C ANISOU 1890 CD ARG A 328 11306 8033 8164 -300 1308 -432 C ATOM 1891 NE ARG A 328 17.861 -51.517 -17.088 1.00 75.09 N ANISOU 1891 NE ARG A 328 12067 8097 8367 -235 1604 -358 N ATOM 1892 CZ ARG A 328 18.847 -51.649 -16.192 1.00 76.30 C ANISOU 1892 CZ ARG A 328 12648 8157 8182 -173 1505 -334 C ATOM 1893 NH1 ARG A 328 20.130 -51.685 -16.567 1.00 74.78 N ANISOU 1893 NH1 ARG A 328 12437 8127 7845 -186 1123 -378 N ATOM 1894 NH2 ARG A 328 18.547 -51.755 -14.896 1.00 78.45 N ANISOU 1894 NH2 ARG A 328 13400 8120 8286 -76 1795 -266 N ATOM 1895 N LEU A 329 16.890 -54.080 -23.492 1.00 70.14 N ANISOU 1895 N LEU A 329 9912 8102 8634 -390 506 -826 N ATOM 1896 CA LEU A 329 15.875 -54.779 -24.296 1.00 72.22 C ANISOU 1896 CA LEU A 329 9922 8252 9264 -391 337 -945 C ATOM 1897 C LEU A 329 16.438 -56.011 -25.017 1.00 71.76 C ANISOU 1897 C LEU A 329 9903 8247 9116 -387 153 -1029 C ATOM 1898 O LEU A 329 15.759 -57.032 -25.134 1.00 71.84 O ANISOU 1898 O LEU A 329 9740 8105 9449 -414 114 -1114 O ATOM 1899 CB LEU A 329 15.202 -53.821 -25.280 1.00 72.13 C ANISOU 1899 CB LEU A 329 9793 8250 9361 -330 70 -1004 C ATOM 1900 CG LEU A 329 14.135 -52.958 -24.603 1.00 73.20 C ANISOU 1900 CG LEU A 329 9752 8228 9832 -346 261 -955 C ATOM 1901 CD1 LEU A 329 13.789 -51.752 -25.455 1.00 74.23 C ANISOU 1901 CD1 LEU A 329 9849 8415 9939 -274 3 -982 C ATOM 1902 CD2 LEU A 329 12.884 -53.766 -24.300 1.00 75.61 C ANISOU 1902 CD2 LEU A 329 9734 8234 10760 -388 367 -1016 C ATOM 1903 N MET A 330 17.679 -55.906 -25.482 1.00 70.44 N ANISOU 1903 N MET A 330 9949 8260 8555 -352 68 -1002 N ATOM 1904 CA MET A 330 18.378 -57.023 -26.100 1.00 71.49 C ANISOU 1904 CA MET A 330 10164 8433 8563 -339 -39 -1059 C ATOM 1905 C MET A 330 18.533 -58.191 -25.118 1.00 70.60 C ANISOU 1905 C MET A 330 10033 8240 8551 -411 159 -1039 C ATOM 1906 O MET A 330 18.379 -59.355 -25.495 1.00 71.94 O ANISOU 1906 O MET A 330 10144 8348 8840 -423 82 -1121 O ATOM 1907 CB MET A 330 19.751 -56.565 -26.592 1.00 72.58 C ANISOU 1907 CB MET A 330 10515 8721 8339 -287 -48 -998 C ATOM 1908 CG MET A 330 20.460 -57.567 -27.488 1.00 76.22 C ANISOU 1908 CG MET A 330 11094 9196 8667 -243 -135 -1052 C ATOM 1909 SD MET A 330 22.244 -57.312 -27.577 1.00 79.22 S ANISOU 1909 SD MET A 330 11638 9659 8800 -213 20 -944 S ATOM 1910 CE MET A 330 22.312 -55.531 -27.805 1.00 77.79 C ANISOU 1910 CE MET A 330 11507 9532 8517 -159 45 -869 C ATOM 1911 N PHE A 331 18.840 -57.870 -23.863 1.00 68.48 N ANISOU 1911 N PHE A 331 9862 7946 8211 -442 398 -933 N ATOM 1912 CA PHE A 331 18.935 -58.861 -22.792 1.00 67.73 C ANISOU 1912 CA PHE A 331 9844 7725 8163 -479 613 -899 C ATOM 1913 C PHE A 331 17.748 -59.823 -22.800 1.00 71.88 C ANISOU 1913 C PHE A 331 10158 8061 9092 -514 704 -971 C ATOM 1914 O PHE A 331 17.934 -61.039 -22.800 1.00 72.72 O ANISOU 1914 O PHE A 331 10259 8117 9252 -536 721 -1010 O ATOM 1915 CB PHE A 331 19.016 -58.152 -21.436 1.00 65.59 C ANISOU 1915 CB PHE A 331 9782 7362 7775 -466 844 -787 C ATOM 1916 CG PHE A 331 19.054 -59.080 -20.252 1.00 64.49 C ANISOU 1916 CG PHE A 331 9845 7033 7623 -463 1091 -740 C ATOM 1917 CD1 PHE A 331 17.880 -59.528 -19.671 1.00 65.52 C ANISOU 1917 CD1 PHE A 331 9916 6919 8058 -472 1408 -727 C ATOM 1918 CD2 PHE A 331 20.264 -59.473 -19.695 1.00 62.90 C ANISOU 1918 CD2 PHE A 331 9909 6849 7140 -434 1018 -705 C ATOM 1919 CE1 PHE A 331 17.909 -60.371 -18.578 1.00 66.29 C ANISOU 1919 CE1 PHE A 331 10276 6800 8111 -443 1696 -670 C ATOM 1920 CE2 PHE A 331 20.301 -60.315 -18.599 1.00 63.60 C ANISOU 1920 CE2 PHE A 331 10265 6732 7165 -402 1220 -662 C ATOM 1921 CZ PHE A 331 19.121 -60.766 -18.040 1.00 65.55 C ANISOU 1921 CZ PHE A 331 10515 6742 7648 -400 1584 -638 C ATOM 1922 N CYS A 332 16.535 -59.273 -22.820 1.00 74.83 N ANISOU 1922 N CYS A 332 10326 8299 9807 -520 761 -990 N ATOM 1923 CA CYS A 332 15.320 -60.076 -22.675 1.00 78.13 C ANISOU 1923 CA CYS A 332 10473 8448 10763 -557 899 -1049 C ATOM 1924 C CYS A 332 14.670 -60.513 -23.988 1.00 78.97 C ANISOU 1924 C CYS A 332 10295 8514 11196 -554 508 -1215 C ATOM 1925 O CYS A 332 13.994 -61.541 -24.009 1.00 82.64 O ANISOU 1925 O CYS A 332 10539 8765 12092 -590 536 -1292 O ATOM 1926 CB CYS A 332 14.291 -59.329 -21.818 1.00 81.64 C ANISOU 1926 CB CYS A 332 10821 8663 11534 -558 1242 -971 C ATOM 1927 SG CYS A 332 14.028 -57.594 -22.269 1.00 84.89 S ANISOU 1927 SG CYS A 332 11184 9197 11872 -519 1065 -954 S ATOM 1928 N TYR A 333 14.902 -59.807 -25.080 1.00 78.20 N ANISOU 1928 N TYR A 333 10234 8576 10901 -497 135 -1276 N ATOM 1929 CA TYR A 333 14.234 -60.154 -26.335 1.00 80.38 C ANISOU 1929 CA TYR A 333 10327 8744 11467 -453 -310 -1449 C ATOM 1930 C TYR A 333 14.928 -61.170 -27.248 1.00 80.52 C ANISOU 1930 C TYR A 333 10497 8824 11271 -417 -593 -1557 C ATOM 1931 O TYR A 333 14.321 -61.664 -28.181 1.00 81.85 O ANISOU 1931 O TYR A 333 10507 8803 11787 -395 -920 -1716 O ATOM 1932 CB TYR A 333 13.877 -58.896 -27.116 1.00 80.26 C ANISOU 1932 CB TYR A 333 10331 8779 11384 -372 -603 -1480 C ATOM 1933 CG TYR A 333 12.535 -58.362 -26.735 1.00 82.60 C ANISOU 1933 CG TYR A 333 10257 8812 12314 -394 -583 -1509 C ATOM 1934 CD1 TYR A 333 12.391 -57.535 -25.653 1.00 81.05 C ANISOU 1934 CD1 TYR A 333 10014 8599 12179 -429 -188 -1367 C ATOM 1935 CD2 TYR A 333 11.408 -58.717 -27.435 1.00 85.93 C ANISOU 1935 CD2 TYR A 333 10368 8949 13332 -373 -957 -1683 C ATOM 1936 CE1 TYR A 333 11.162 -57.062 -25.282 1.00 83.71 C ANISOU 1936 CE1 TYR A 333 9991 8650 13162 -445 -100 -1380 C ATOM 1937 CE2 TYR A 333 10.171 -58.244 -27.071 1.00 88.52 C ANISOU 1937 CE2 TYR A 333 10282 8973 14376 -396 -927 -1710 C ATOM 1938 CZ TYR A 333 10.055 -57.423 -25.995 1.00 87.64 C ANISOU 1938 CZ TYR A 333 10117 8857 14323 -434 -460 -1549 C ATOM 1939 OH TYR A 333 8.820 -56.952 -25.630 1.00 91.10 O ANISOU 1939 OH TYR A 333 10130 8956 15527 -450 -369 -1564 O ATOM 1940 N ILE A 334 16.182 -61.488 -26.968 1.00 26.08 N ATOM 1941 CA ILE A 334 16.897 -62.533 -27.667 1.00 25.36 C ATOM 1942 C ILE A 334 16.580 -63.795 -26.900 1.00 25.18 C ATOM 1943 O ILE A 334 16.740 -63.815 -25.708 1.00 23.02 O ATOM 1944 CB ILE A 334 18.396 -62.205 -27.652 1.00 25.59 C ATOM 1945 CG1 ILE A 334 18.750 -61.365 -28.853 1.00 25.36 C ATOM 1946 CG2 ILE A 334 19.305 -63.425 -27.607 1.00 25.64 C ATOM 1947 CD1 ILE A 334 20.221 -61.072 -28.930 0.00 20.00 C ATOM 1948 N SER A 335 16.113 -64.826 -27.596 1.00 27.20 N ATOM 1949 CA SER A 335 15.712 -66.070 -26.949 1.00 28.41 C ATOM 1950 C SER A 335 16.907 -66.971 -26.658 1.00 29.24 C ATOM 1951 O SER A 335 17.907 -66.945 -27.376 1.00 28.80 O ATOM 1952 CB SER A 335 14.690 -66.815 -27.809 0.00 20.00 C ATOM 1953 OG SER A 335 14.719 -68.207 -27.545 0.00 20.00 O ATOM 1954 N ASP A 336 16.793 -67.770 -25.602 1.00 31.09 N ATOM 1955 CA ASP A 336 17.852 -68.698 -25.228 1.00 31.63 C ATOM 1956 C ASP A 336 18.275 -69.538 -26.427 1.00 31.17 C ATOM 1957 O ASP A 336 19.408 -70.014 -26.495 1.00 31.21 O ATOM 1958 CB ASP A 336 17.391 -69.604 -24.085 1.00 32.52 C ATOM 1959 CG ASP A 336 16.038 -70.234 -24.350 1.00 33.08 C ATOM 1960 OD1 ASP A 336 15.892 -70.920 -25.383 1.00 33.45 O ATOM 1961 OD2 ASP A 336 15.120 -70.043 -23.523 1.00 34.23 O ATOM 1962 N GLU A 337 17.356 -69.714 -27.371 1.00 30.07 N ATOM 1963 CA GLU A 337 17.635 -70.470 -28.560 1.00 29.40 C ATOM 1964 C GLU A 337 18.636 -69.724 -29.425 1.00 28.58 C ATOM 1965 O GLU A 337 19.478 -70.331 -30.049 1.00 28.29 O ATOM 1966 CB GLU A 337 16.342 -70.748 -29.334 0.00 20.00 C ATOM 1967 CG GLU A 337 15.358 -71.681 -28.632 0.00 20.00 C ATOM 1968 CD GLU A 337 14.075 -71.865 -29.399 0.00 20.00 C ATOM 1969 OE1 GLU A 337 13.858 -71.126 -30.386 0.00 20.00 O ATOM 1970 OE2 GLU A 337 13.288 -72.748 -29.008 0.00 20.00 O ATOM 1971 N GLN A 338 18.550 -68.403 -29.459 1.00 28.06 N ATOM 1972 CA GLN A 338 19.359 -67.641 -30.388 1.00 27.52 C ATOM 1973 C GLN A 338 20.640 -67.126 -29.805 1.00 26.20 C ATOM 1974 O GLN A 338 21.421 -66.515 -30.496 1.00 25.05 O ATOM 1975 CB GLN A 338 18.572 -66.473 -30.955 1.00 28.20 C ATOM 1976 CG GLN A 338 17.239 -66.844 -31.554 1.00 28.72 C ATOM 1977 CD GLN A 338 16.145 -65.921 -31.091 1.00 29.50 C ATOM 1978 OE1 GLN A 338 15.642 -66.050 -29.978 1.00 29.88 O ATOM 1979 NE2 GLN A 338 15.768 -64.985 -31.940 1.00 29.73 N ATOM 1980 N TRP A 339 20.853 -67.369 -28.534 1.00 71.68 N ANISOU 1980 N TRP A 339 10462 8143 8628 -383 -344 -1551 N ATOM 1981 CA TRP A 339 22.051 -66.900 -27.901 1.00 69.10 C ANISOU 1981 CA TRP A 339 10224 7945 8082 -397 -101 -1399 C ATOM 1982 C TRP A 339 23.190 -67.786 -28.290 1.00 67.45 C ANISOU 1982 C TRP A 339 10162 7750 7715 -366 -35 -1386 C ATOM 1983 O TRP A 339 23.038 -68.974 -28.392 1.00 69.39 O ANISOU 1983 O TRP A 339 10389 7917 8057 -385 -70 -1462 O ATOM 1984 CB TRP A 339 21.878 -66.869 -26.400 1.00 68.55 C ANISOU 1984 CB TRP A 339 10033 7851 8160 -485 111 -1310 C ATOM 1985 CG TRP A 339 21.329 -65.592 -25.917 1.00 68.30 C ANISOU 1985 CG TRP A 339 9944 7835 8171 -493 149 -1257 C ATOM 1986 CD1 TRP A 339 20.063 -65.349 -25.553 1.00 69.60 C ANISOU 1986 CD1 TRP A 339 9938 7880 8625 -527 179 -1290 C ATOM 1987 CD2 TRP A 339 22.034 -64.373 -25.757 1.00 67.20 C ANISOU 1987 CD2 TRP A 339 9900 7807 7826 -462 178 -1161 C ATOM 1988 NE1 TRP A 339 19.924 -64.060 -25.168 1.00 69.09 N ANISOU 1988 NE1 TRP A 339 9886 7863 8502 -517 233 -1216 N ATOM 1989 CE2 TRP A 339 21.131 -63.437 -25.287 1.00 67.69 C ANISOU 1989 CE2 TRP A 339 9876 7834 8005 -478 215 -1140 C ATOM 1990 CE3 TRP A 339 23.351 -63.986 -25.961 1.00 66.58 C ANISOU 1990 CE3 TRP A 339 9941 7816 7539 -421 193 -1089 C ATOM 1991 CZ2 TRP A 339 21.495 -62.144 -25.014 1.00 66.97 C ANISOU 1991 CZ2 TRP A 339 9850 7823 7771 -456 241 -1057 C ATOM 1992 CZ3 TRP A 339 23.701 -62.705 -25.699 1.00 65.44 C ANISOU 1992 CZ3 TRP A 339 9824 7728 7311 -404 214 -1009 C ATOM 1993 CH2 TRP A 339 22.786 -61.801 -25.227 1.00 65.75 C ANISOU 1993 CH2 TRP A 339 9809 7760 7410 -421 225 -997 C ATOM 1994 N THR A 340 24.341 -67.186 -28.502 1.00 65.26 N ANISOU 1994 N THR A 340 10006 7541 7248 -315 77 -1288 N ATOM 1995 CA THR A 340 25.549 -67.911 -28.880 1.00 64.44 C ANISOU 1995 CA THR A 340 10011 7412 7062 -277 202 -1251 C ATOM 1996 C THR A 340 26.754 -67.334 -28.145 1.00 63.06 C ANISOU 1996 C THR A 340 9770 7262 6925 -295 358 -1115 C ATOM 1997 O THR A 340 26.720 -66.186 -27.692 1.00 62.49 O ANISOU 1997 O THR A 340 9647 7237 6859 -306 352 -1056 O ATOM 1998 CB THR A 340 25.815 -67.803 -30.390 1.00 66.15 C ANISOU 1998 CB THR A 340 10497 7569 7064 -140 189 -1291 C ATOM 1999 OG1 THR A 340 26.106 -66.443 -30.737 1.00 66.81 O ANISOU 1999 OG1 THR A 340 10664 7682 7036 -73 257 -1216 O ATOM 2000 CG2 THR A 340 24.608 -68.264 -31.177 1.00 68.10 C ANISOU 2000 CG2 THR A 340 10856 7741 7275 -93 -85 -1453 C ATOM 2001 N THR A 341 27.824 -68.120 -28.043 1.00 62.81 N ANISOU 2001 N THR A 341 9732 7170 6962 -292 467 -1072 N ATOM 2002 CA THR A 341 29.059 -67.673 -27.385 1.00 61.68 C ANISOU 2002 CA THR A 341 9490 6981 6964 -299 544 -962 C ATOM 2003 C THR A 341 29.496 -66.293 -27.882 1.00 62.65 C ANISOU 2003 C THR A 341 9618 7100 7085 -243 624 -894 C ATOM 2004 O THR A 341 29.897 -65.447 -27.081 1.00 61.91 O ANISOU 2004 O THR A 341 9413 6996 7113 -271 574 -832 O ATOM 2005 CB THR A 341 30.202 -68.689 -27.580 1.00 61.45 C ANISOU 2005 CB THR A 341 9437 6837 7073 -277 661 -934 C ATOM 2006 OG1 THR A 341 29.958 -69.841 -26.770 1.00 60.12 O ANISOU 2006 OG1 THR A 341 9243 6659 6940 -337 576 -973 O ATOM 2007 CG2 THR A 341 31.542 -68.097 -27.186 1.00 61.89 C ANISOU 2007 CG2 THR A 341 9344 6776 7395 -262 716 -831 C ATOM 2008 N PHE A 342 29.406 -66.063 -29.194 1.00 64.64 N ANISOU 2008 N PHE A 342 10044 7329 7186 -147 740 -910 N ATOM 2009 CA PHE A 342 29.736 -64.753 -29.752 1.00 65.04 C ANISOU 2009 CA PHE A 342 10150 7350 7211 -74 867 -839 C ATOM 2010 C PHE A 342 28.818 -63.642 -29.243 1.00 63.16 C ANISOU 2010 C PHE A 342 9862 7236 6899 -116 696 -852 C ATOM 2011 O PHE A 342 29.297 -62.603 -28.789 1.00 62.88 O ANISOU 2011 O PHE A 342 9713 7191 6985 -130 731 -775 O ATOM 2012 CB PHE A 342 29.701 -64.758 -31.272 1.00 67.31 C ANISOU 2012 CB PHE A 342 10764 7544 7264 75 1032 -855 C ATOM 2013 CG PHE A 342 29.949 -63.403 -31.866 1.00 69.88 C ANISOU 2013 CG PHE A 342 11205 7815 7532 169 1200 -777 C ATOM 2014 CD1 PHE A 342 31.155 -62.749 -31.638 1.00 71.26 C ANISOU 2014 CD1 PHE A 342 11198 7866 8009 170 1457 -649 C ATOM 2015 CD2 PHE A 342 28.971 -62.760 -32.614 1.00 71.61 C ANISOU 2015 CD2 PHE A 342 11691 8070 7445 260 1079 -834 C ATOM 2016 CE1 PHE A 342 31.392 -61.490 -32.163 1.00 72.67 C ANISOU 2016 CE1 PHE A 342 11466 7968 8177 255 1654 -569 C ATOM 2017 CE2 PHE A 342 29.204 -61.502 -33.147 1.00 73.11 C ANISOU 2017 CE2 PHE A 342 12018 8197 7563 358 1253 -754 C ATOM 2018 CZ PHE A 342 30.416 -60.867 -32.922 1.00 73.57 C ANISOU 2018 CZ PHE A 342 11896 8140 7914 353 1572 -615 C ATOM 2019 N LEU A 343 27.508 -63.850 -29.339 1.00 61.80 N ANISOU 2019 N LEU A 343 9754 7145 6580 -132 511 -951 N ATOM 2020 CA LEU A 343 26.547 -62.881 -28.809 1.00 60.30 C ANISOU 2020 CA LEU A 343 9490 7044 6376 -174 376 -963 C ATOM 2021 C LEU A 343 26.754 -62.660 -27.319 1.00 59.45 C ANISOU 2021 C LEU A 343 9211 6957 6417 -272 357 -906 C ATOM 2022 O LEU A 343 26.733 -61.525 -26.862 1.00 59.08 O ANISOU 2022 O LEU A 343 9125 6938 6382 -281 345 -854 O ATOM 2023 CB LEU A 343 25.111 -63.340 -29.034 1.00 60.35 C ANISOU 2023 CB LEU A 343 9512 7066 6352 -185 180 -1086 C ATOM 2024 CG LEU A 343 24.457 -63.043 -30.375 1.00 61.43 C ANISOU 2024 CG LEU A 343 9865 7159 6315 -65 37 -1170 C ATOM 2025 CD1 LEU A 343 23.116 -63.754 -30.425 1.00 62.38 C ANISOU 2025 CD1 LEU A 343 9909 7228 6562 -96 -221 -1314 C ATOM 2026 CD2 LEU A 343 24.286 -61.550 -30.578 1.00 60.95 C ANISOU 2026 CD2 LEU A 343 9850 7137 6168 -14 36 -1118 C ATOM 2027 N PHE A 344 26.932 -63.743 -26.564 1.00 60.07 N ANISOU 2027 N PHE A 344 9244 6997 6582 -327 343 -919 N ATOM 2028 CA PHE A 344 27.220 -63.646 -25.131 1.00 60.03 C ANISOU 2028 CA PHE A 344 9203 6949 6657 -379 301 -869 C ATOM 2029 C PHE A 344 28.410 -62.714 -24.887 1.00 62.08 C ANISOU 2029 C PHE A 344 9414 7151 7021 -354 284 -788 C ATOM 2030 O PHE A 344 28.343 -61.820 -24.039 1.00 62.73 O ANISOU 2030 O PHE A 344 9514 7215 7102 -366 201 -754 O ATOM 2031 CB PHE A 344 27.497 -65.031 -24.537 1.00 59.07 C ANISOU 2031 CB PHE A 344 9100 6751 6591 -406 297 -888 C ATOM 2032 CG PHE A 344 27.808 -65.021 -23.060 1.00 58.10 C ANISOU 2032 CG PHE A 344 9062 6527 6486 -418 219 -843 C ATOM 2033 CD1 PHE A 344 29.091 -64.744 -22.606 1.00 58.21 C ANISOU 2033 CD1 PHE A 344 9064 6437 6617 -389 98 -794 C ATOM 2034 CD2 PHE A 344 26.827 -65.321 -22.129 1.00 57.83 C ANISOU 2034 CD2 PHE A 344 9150 6443 6379 -437 266 -854 C ATOM 2035 CE1 PHE A 344 29.385 -64.744 -21.256 1.00 58.68 C ANISOU 2035 CE1 PHE A 344 9290 6351 6653 -365 -61 -772 C ATOM 2036 CE2 PHE A 344 27.115 -65.329 -20.777 1.00 58.44 C ANISOU 2036 CE2 PHE A 344 9439 6373 6391 -405 205 -810 C ATOM 2037 CZ PHE A 344 28.397 -65.040 -20.338 1.00 58.84 C ANISOU 2037 CZ PHE A 344 9536 6327 6491 -362 -1 -777 C ATOM 2038 N ASP A 345 29.490 -62.916 -25.637 1.00 64.19 N ANISOU 2038 N ASP A 345 9619 7349 7420 -314 379 -757 N ATOM 2039 CA ASP A 345 30.696 -62.108 -25.458 1.00 66.38 C ANISOU 2039 CA ASP A 345 9773 7502 7944 -293 380 -684 C ATOM 2040 C ASP A 345 30.485 -60.661 -25.910 1.00 66.15 C ANISOU 2040 C ASP A 345 9740 7517 7875 -264 446 -646 C ATOM 2041 O ASP A 345 30.957 -59.737 -25.251 1.00 67.69 O ANISOU 2041 O ASP A 345 9850 7639 8227 -275 345 -607 O ATOM 2042 CB ASP A 345 31.896 -62.748 -26.171 1.00 68.54 C ANISOU 2042 CB ASP A 345 9945 7626 8468 -252 549 -648 C ATOM 2043 CG ASP A 345 32.447 -63.966 -25.422 1.00 69.70 C ANISOU 2043 CG ASP A 345 10040 7677 8765 -281 420 -669 C ATOM 2044 OD1 ASP A 345 31.731 -64.528 -24.566 1.00 69.93 O ANISOU 2044 OD1 ASP A 345 10182 7773 8613 -320 257 -717 O ATOM 2045 OD2 ASP A 345 33.603 -64.363 -25.684 1.00 71.49 O ANISOU 2045 OD2 ASP A 345 10118 7726 9319 -254 509 -630 O ATOM 2046 N PHE A 346 29.769 -60.475 -27.019 1.00 65.82 N ANISOU 2046 N PHE A 346 9819 7568 7619 -216 579 -667 N ATOM 2047 CA PHE A 346 29.422 -59.141 -27.543 1.00 64.64 C ANISOU 2047 CA PHE A 346 9720 7462 7376 -171 642 -635 C ATOM 2048 C PHE A 346 28.728 -58.296 -26.478 1.00 62.56 C ANISOU 2048 C PHE A 346 9419 7279 7071 -232 461 -640 C ATOM 2049 O PHE A 346 29.171 -57.193 -26.154 1.00 61.70 O ANISOU 2049 O PHE A 346 9240 7124 7077 -231 452 -586 O ATOM 2050 CB PHE A 346 28.512 -59.291 -28.776 1.00 65.13 C ANISOU 2050 CB PHE A 346 10001 7590 7156 -91 694 -691 C ATOM 2051 CG PHE A 346 27.941 -57.994 -29.291 1.00 65.14 C ANISOU 2051 CG PHE A 346 10101 7635 7012 -32 704 -674 C ATOM 2052 CD1 PHE A 346 26.767 -57.468 -28.752 1.00 63.43 C ANISOU 2052 CD1 PHE A 346 9849 7536 6714 -81 511 -719 C ATOM 2053 CD2 PHE A 346 28.563 -57.310 -30.337 1.00 66.08 C ANISOU 2053 CD2 PHE A 346 10369 7644 7091 87 946 -604 C ATOM 2054 CE1 PHE A 346 26.242 -56.279 -29.233 1.00 63.29 C ANISOU 2054 CE1 PHE A 346 9916 7551 6580 -22 504 -704 C ATOM 2055 CE2 PHE A 346 28.040 -56.121 -30.819 1.00 65.47 C ANISOU 2055 CE2 PHE A 346 10421 7594 6859 157 954 -585 C ATOM 2056 CZ PHE A 346 26.878 -55.607 -30.267 1.00 64.45 C ANISOU 2056 CZ PHE A 346 10230 7609 6648 98 703 -641 C ATOM 2057 N TYR A 347 27.645 -58.846 -25.937 1.00 61.43 N ANISOU 2057 N TYR A 347 9327 7217 6794 -279 348 -703 N ATOM 2058 CA TYR A 347 26.833 -58.194 -24.904 1.00 60.39 C ANISOU 2058 CA TYR A 347 9214 7119 6610 -322 254 -703 C ATOM 2059 C TYR A 347 27.651 -57.585 -23.761 1.00 60.55 C ANISOU 2059 C TYR A 347 9232 7036 6736 -335 152 -651 C ATOM 2060 O TYR A 347 27.434 -56.437 -23.382 1.00 60.61 O ANISOU 2060 O TYR A 347 9264 7049 6717 -332 116 -623 O ATOM 2061 CB TYR A 347 25.833 -59.206 -24.340 1.00 59.27 C ANISOU 2061 CB TYR A 347 9114 6981 6423 -364 235 -761 C ATOM 2062 CG TYR A 347 24.954 -58.674 -23.247 1.00 58.06 C ANISOU 2062 CG TYR A 347 9025 6797 6236 -390 241 -746 C ATOM 2063 CD1 TYR A 347 25.378 -58.697 -21.927 1.00 58.54 C ANISOU 2063 CD1 TYR A 347 9232 6738 6270 -390 202 -707 C ATOM 2064 CD2 TYR A 347 23.694 -58.162 -23.528 1.00 57.96 C ANISOU 2064 CD2 TYR A 347 8966 6827 6227 -395 283 -773 C ATOM 2065 CE1 TYR A 347 24.576 -58.210 -20.909 1.00 59.43 C ANISOU 2065 CE1 TYR A 347 9499 6771 6309 -385 271 -681 C ATOM 2066 CE2 TYR A 347 22.876 -57.675 -22.520 1.00 58.55 C ANISOU 2066 CE2 TYR A 347 9104 6829 6314 -410 367 -744 C ATOM 2067 CZ TYR A 347 23.322 -57.700 -21.209 1.00 59.19 C ANISOU 2067 CZ TYR A 347 9386 6787 6315 -400 395 -692 C ATOM 2068 OH TYR A 347 22.532 -57.220 -20.188 1.00 59.29 O ANISOU 2068 OH TYR A 347 9557 6677 6292 -386 538 -652 O ATOM 2069 N HIS A 348 28.589 -58.353 -23.218 1.00 61.35 N ANISOU 2069 N HIS A 348 9323 7017 6969 -340 64 -648 N ATOM 2070 CA HIS A 348 29.385 -57.901 -22.076 1.00 61.94 C ANISOU 2070 CA HIS A 348 9440 6927 7164 -330 -146 -627 C ATOM 2071 C HIS A 348 30.385 -56.801 -22.440 1.00 63.08 C ANISOU 2071 C HIS A 348 9409 6982 7574 -311 -179 -585 C ATOM 2072 O HIS A 348 30.789 -56.035 -21.567 1.00 64.61 O ANISOU 2072 O HIS A 348 9643 7043 7862 -299 -394 -580 O ATOM 2073 CB HIS A 348 30.096 -59.085 -21.415 1.00 62.65 C ANISOU 2073 CB HIS A 348 9580 6872 7349 -322 -291 -648 C ATOM 2074 CG HIS A 348 29.156 -60.082 -20.810 1.00 62.62 C ANISOU 2074 CG HIS A 348 9787 6897 7108 -331 -243 -679 C ATOM 2075 ND1 HIS A 348 28.599 -61.114 -21.533 1.00 62.38 N ANISOU 2075 ND1 HIS A 348 9696 6975 7029 -360 -67 -709 N ATOM 2076 CD2 HIS A 348 28.666 -60.197 -19.553 1.00 63.71 C ANISOU 2076 CD2 HIS A 348 10222 6923 7060 -301 -316 -680 C ATOM 2077 CE1 HIS A 348 27.808 -61.823 -20.748 1.00 62.71 C ANISOU 2077 CE1 HIS A 348 9922 6974 6928 -364 -22 -726 C ATOM 2078 NE2 HIS A 348 27.834 -61.290 -19.540 1.00 63.69 N ANISOU 2078 NE2 HIS A 348 10290 6958 6950 -321 -135 -700 N ATOM 2079 N TYR A 349 30.786 -56.719 -23.711 1.00 63.35 N ANISOU 2079 N TYR A 349 9285 7045 7740 -293 45 -554 N ATOM 2080 CA TYR A 349 31.551 -55.560 -24.196 1.00 64.60 C ANISOU 2080 CA TYR A 349 9280 7099 8163 -266 132 -497 C ATOM 2081 C TYR A 349 30.612 -54.388 -24.367 1.00 63.22 C ANISOU 2081 C TYR A 349 9201 7068 7752 -261 186 -484 C ATOM 2082 O TYR A 349 30.879 -53.286 -23.884 1.00 63.65 O ANISOU 2082 O TYR A 349 9207 7044 7930 -263 83 -462 O ATOM 2083 CB TYR A 349 32.236 -55.842 -25.531 1.00 66.49 C ANISOU 2083 CB TYR A 349 9409 7266 8585 -217 457 -448 C ATOM 2084 CG TYR A 349 33.484 -56.673 -25.400 1.00 68.81 C ANISOU 2084 CG TYR A 349 9513 7336 9296 -216 445 -437 C ATOM 2085 CD1 TYR A 349 34.608 -56.171 -24.755 1.00 71.09 C ANISOU 2085 CD1 TYR A 349 9555 7361 10093 -225 265 -420 C ATOM 2086 CD2 TYR A 349 33.544 -57.959 -25.925 1.00 69.28 C ANISOU 2086 CD2 TYR A 349 9621 7413 9289 -202 583 -451 C ATOM 2087 CE1 TYR A 349 35.754 -56.929 -24.627 1.00 73.93 C ANISOU 2087 CE1 TYR A 349 9693 7469 10925 -220 218 -417 C ATOM 2088 CE2 TYR A 349 34.684 -58.727 -25.806 1.00 71.42 C ANISOU 2088 CE2 TYR A 349 9699 7461 9975 -199 583 -437 C ATOM 2089 CZ TYR A 349 35.785 -58.210 -25.156 1.00 73.96 C ANISOU 2089 CZ TYR A 349 9748 7512 10841 -208 399 -419 C ATOM 2090 OH TYR A 349 36.920 -58.976 -25.037 1.00 77.07 O ANISOU 2090 OH TYR A 349 9905 7642 11734 -200 365 -411 O ATOM 2091 N PHE A 350 29.505 -54.645 -25.058 1.00 61.36 N ANISOU 2091 N PHE A 350 9094 7013 7205 -248 314 -507 N ATOM 2092 CA PHE A 350 28.433 -53.668 -25.215 1.00 59.86 C ANISOU 2092 CA PHE A 350 8992 6953 6797 -239 332 -507 C ATOM 2093 C PHE A 350 28.016 -53.108 -23.861 1.00 60.61 C ANISOU 2093 C PHE A 350 9146 7035 6845 -282 149 -515 C ATOM 2094 O PHE A 350 27.728 -51.921 -23.749 1.00 61.57 O ANISOU 2094 O PHE A 350 9280 7178 6935 -274 147 -488 O ATOM 2095 CB PHE A 350 27.235 -54.313 -25.920 1.00 58.21 C ANISOU 2095 CB PHE A 350 8892 6880 6343 -223 376 -564 C ATOM 2096 CG PHE A 350 26.259 -53.333 -26.516 1.00 56.75 C ANISOU 2096 CG PHE A 350 8774 6786 6000 -181 398 -567 C ATOM 2097 CD1 PHE A 350 26.694 -52.225 -27.232 1.00 56.70 C ANISOU 2097 CD1 PHE A 350 8790 6751 6002 -114 519 -507 C ATOM 2098 CD2 PHE A 350 24.891 -53.556 -26.406 1.00 55.91 C ANISOU 2098 CD2 PHE A 350 8699 6757 5787 -200 308 -631 C ATOM 2099 CE1 PHE A 350 25.786 -51.346 -27.790 1.00 56.26 C ANISOU 2099 CE1 PHE A 350 8826 6764 5785 -61 510 -513 C ATOM 2100 CE2 PHE A 350 23.980 -52.683 -26.968 1.00 55.48 C ANISOU 2100 CE2 PHE A 350 8683 6753 5644 -153 278 -643 C ATOM 2101 CZ PHE A 350 24.428 -51.576 -27.659 1.00 55.84 C ANISOU 2101 CZ PHE A 350 8791 6792 5632 -80 361 -586 C ATOM 2102 N TYR A 351 28.006 -53.960 -22.836 1.00 61.59 N ANISOU 2102 N TYR A 351 9359 7096 6945 -309 13 -546 N ATOM 2103 CA TYR A 351 27.782 -53.515 -21.464 1.00 62.64 C ANISOU 2103 CA TYR A 351 9671 7135 6995 -311 -146 -548 C ATOM 2104 C TYR A 351 28.776 -52.428 -21.082 1.00 64.82 C ANISOU 2104 C TYR A 351 9895 7264 7468 -292 -321 -525 C ATOM 2105 O TYR A 351 28.375 -51.375 -20.590 1.00 66.49 O ANISOU 2105 O TYR A 351 10212 7463 7586 -281 -365 -511 O ATOM 2106 CB TYR A 351 27.903 -54.677 -20.474 1.00 63.27 C ANISOU 2106 CB TYR A 351 9928 7095 7016 -305 -263 -578 C ATOM 2107 CG TYR A 351 27.287 -54.391 -19.121 1.00 63.73 C ANISOU 2107 CG TYR A 351 10321 7033 6860 -271 -327 -575 C ATOM 2108 CD1 TYR A 351 25.945 -54.654 -18.885 1.00 63.52 C ANISOU 2108 CD1 TYR A 351 10424 7055 6655 -278 -96 -568 C ATOM 2109 CD2 TYR A 351 28.044 -53.859 -18.077 1.00 64.95 C ANISOU 2109 CD2 TYR A 351 10689 6970 7019 -214 -613 -580 C ATOM 2110 CE1 TYR A 351 25.368 -54.398 -17.652 1.00 64.69 C ANISOU 2110 CE1 TYR A 351 10935 7036 6606 -223 -51 -546 C ATOM 2111 CE2 TYR A 351 27.472 -53.594 -16.838 1.00 65.80 C ANISOU 2111 CE2 TYR A 351 11226 6918 6857 -146 -644 -573 C ATOM 2112 CZ TYR A 351 26.134 -53.872 -16.631 1.00 65.83 C ANISOU 2112 CZ TYR A 351 11383 6970 6656 -148 -314 -545 C ATOM 2113 OH TYR A 351 25.543 -53.621 -15.414 1.00 68.22 O ANISOU 2113 OH TYR A 351 12161 7064 6695 -60 -240 -518 O ATOM 2114 N MET A 352 30.065 -52.673 -21.313 1.00 66.47 N ANISOU 2114 N MET A 352 9920 7329 8003 -286 -416 -523 N ATOM 2115 CA MET A 352 31.101 -51.700 -20.943 1.00 68.75 C ANISOU 2115 CA MET A 352 10090 7407 8623 -270 -624 -515 C ATOM 2116 C MET A 352 30.899 -50.367 -21.641 1.00 67.83 C ANISOU 2116 C MET A 352 9858 7366 8546 -270 -441 -466 C ATOM 2117 O MET A 352 31.027 -49.319 -21.024 1.00 68.26 O ANISOU 2117 O MET A 352 9952 7317 8663 -261 -612 -469 O ATOM 2118 CB MET A 352 32.495 -52.218 -21.270 1.00 71.61 C ANISOU 2118 CB MET A 352 10176 7561 9471 -265 -689 -514 C ATOM 2119 CG MET A 352 32.932 -53.388 -20.420 1.00 73.40 C ANISOU 2119 CG MET A 352 10509 7641 9735 -251 -971 -569 C ATOM 2120 SD MET A 352 34.627 -53.834 -20.803 1.00 76.95 S ANISOU 2120 SD MET A 352 10553 7784 10898 -244 -1060 -566 S ATOM 2121 CE MET A 352 34.575 -55.594 -20.465 1.00 78.17 C ANISOU 2121 CE MET A 352 10861 7961 10878 -237 -1136 -605 C ATOM 2122 N LEU A 353 30.584 -50.413 -22.928 1.00 67.08 N ANISOU 2122 N LEU A 353 9670 7425 8392 -263 -109 -425 N ATOM 2123 CA LEU A 353 30.300 -49.200 -23.681 1.00 66.75 C ANISOU 2123 CA LEU A 353 9585 7451 8326 -239 89 -373 C ATOM 2124 C LEU A 353 29.077 -48.491 -23.114 1.00 64.88 C ANISOU 2124 C LEU A 353 9538 7356 7754 -250 20 -388 C ATOM 2125 O LEU A 353 29.182 -47.362 -22.640 1.00 65.01 O ANISOU 2125 O LEU A 353 9557 7304 7837 -249 -71 -373 O ATOM 2126 CB LEU A 353 30.071 -49.529 -25.156 1.00 67.49 C ANISOU 2126 CB LEU A 353 9683 7647 8310 -190 422 -338 C ATOM 2127 CG LEU A 353 30.046 -48.358 -26.145 1.00 68.97 C ANISOU 2127 CG LEU A 353 9871 7831 8500 -126 677 -270 C ATOM 2128 CD1 LEU A 353 29.990 -48.894 -27.568 0.00 70.11 C ANISOU 2128 CD1 LEU A 353 10144 7993 8502 -34 979 -242 C ATOM 2129 CD2 LEU A 353 28.888 -47.399 -25.905 0.00 68.07 C ANISOU 2129 CD2 LEU A 353 9884 7878 8098 -129 600 -279 C ATOM 2130 N THR A 354 27.929 -49.169 -23.153 1.00 63.20 N ANISOU 2130 N THR A 354 9465 7307 7240 -258 73 -417 N ATOM 2131 CA THR A 354 26.633 -48.544 -22.849 1.00 62.30 C ANISOU 2131 CA THR A 354 9480 7305 6885 -261 100 -420 C ATOM 2132 C THR A 354 26.589 -47.896 -21.483 1.00 62.45 C ANISOU 2132 C THR A 354 9656 7207 6862 -268 -61 -421 C ATOM 2133 O THR A 354 26.088 -46.788 -21.328 1.00 63.29 O ANISOU 2133 O THR A 354 9811 7338 6899 -258 -29 -396 O ATOM 2134 CB THR A 354 25.480 -49.555 -22.873 1.00 61.75 C ANISOU 2134 CB THR A 354 9483 7333 6642 -276 159 -462 C ATOM 2135 OG1 THR A 354 25.751 -50.611 -21.942 1.00 61.90 O ANISOU 2135 OG1 THR A 354 9601 7255 6661 -297 67 -490 O ATOM 2136 CG2 THR A 354 25.286 -50.122 -24.278 1.00 62.64 C ANISOU 2136 CG2 THR A 354 9519 7546 6735 -247 263 -483 C ATOM 2137 N ASN A 355 27.101 -48.605 -20.491 1.00 62.60 N ANISOU 2137 N ASN A 355 9809 7077 6897 -266 -245 -452 N ATOM 2138 CA ASN A 355 27.059 -48.117 -19.135 1.00 62.92 C ANISOU 2138 CA ASN A 355 10137 6947 6823 -233 -430 -462 C ATOM 2139 C ASN A 355 28.066 -47.002 -18.915 1.00 64.48 C ANISOU 2139 C ASN A 355 10266 6987 7244 -217 -658 -464 C ATOM 2140 O ASN A 355 27.813 -46.111 -18.117 1.00 66.74 O ANISOU 2140 O ASN A 355 10776 7173 7408 -184 -764 -466 O ATOM 2141 CB ASN A 355 27.238 -49.268 -18.143 1.00 63.50 C ANISOU 2141 CB ASN A 355 10473 6863 6788 -202 -575 -499 C ATOM 2142 CG ASN A 355 26.018 -50.179 -18.097 1.00 63.18 C ANISOU 2142 CG ASN A 355 10546 6919 6539 -212 -305 -491 C ATOM 2143 OD1 ASN A 355 25.382 -50.435 -19.124 1.00 61.82 O ANISOU 2143 OD1 ASN A 355 10134 6941 6413 -258 -96 -485 O ATOM 2144 ND2 ASN A 355 25.667 -50.652 -16.906 1.00 64.53 N ANISOU 2144 ND2 ASN A 355 11111 6908 6499 -154 -310 -493 N ATOM 2145 N ALA A 356 29.186 -47.016 -19.634 1.00 65.09 N ANISOU 2145 N ALA A 356 10033 7008 7687 -234 -706 -462 N ATOM 2146 CA ALA A 356 30.138 -45.902 -19.557 1.00 66.64 C ANISOU 2146 CA ALA A 356 10073 7016 8228 -226 -883 -462 C ATOM 2147 C ALA A 356 29.489 -44.612 -20.053 1.00 66.20 C ANISOU 2147 C ALA A 356 9981 7096 8076 -231 -669 -410 C ATOM 2148 O ALA A 356 29.674 -43.553 -19.454 1.00 68.81 O ANISOU 2148 O ALA A 356 10380 7291 8472 -215 -846 -422 O ATOM 2149 CB ALA A 356 31.397 -46.195 -20.352 1.00 67.97 C ANISOU 2149 CB ALA A 356 9865 7056 8903 -241 -851 -449 C ATOM 2150 N LEU A 357 28.727 -44.704 -21.141 1.00 64.08 N ANISOU 2150 N LEU A 357 9631 7068 7647 -240 -330 -363 N ATOM 2151 CA LEU A 357 27.973 -43.557 -21.646 1.00 63.22 C ANISOU 2151 CA LEU A 357 9524 7089 7405 -229 -143 -317 C ATOM 2152 C LEU A 357 26.916 -43.104 -20.648 1.00 62.22 C ANISOU 2152 C LEU A 357 9668 6992 6980 -224 -207 -330 C ATOM 2153 O LEU A 357 26.756 -41.918 -20.402 1.00 63.69 O ANISOU 2153 O LEU A 357 9897 7145 7155 -212 -222 -310 O ATOM 2154 CB LEU A 357 27.296 -43.892 -22.977 1.00 62.65 C ANISOU 2154 CB LEU A 357 9391 7222 7188 -209 144 -285 C ATOM 2155 CG LEU A 357 28.193 -43.990 -24.216 1.00 63.76 C ANISOU 2155 CG LEU A 357 9358 7310 7555 -173 347 -241 C ATOM 2156 CD1 LEU A 357 27.370 -44.497 -25.391 1.00 63.09 C ANISOU 2156 CD1 LEU A 357 9368 7393 7209 -120 542 -236 C ATOM 2157 CD2 LEU A 357 28.859 -42.658 -24.555 1.00 64.22 C ANISOU 2157 CD2 LEU A 357 9291 7241 7866 -147 458 -181 C ATOM 2158 N PHE A 358 26.195 -44.062 -20.083 1.00 61.29 N ANISOU 2158 N PHE A 358 9738 6905 6642 -225 -200 -356 N ATOM 2159 CA PHE A 358 25.156 -43.792 -19.094 1.00 60.71 C ANISOU 2159 CA PHE A 358 9960 6795 6312 -203 -158 -352 C ATOM 2160 C PHE A 358 25.683 -42.938 -17.946 1.00 63.09 C ANISOU 2160 C PHE A 358 10519 6867 6585 -160 -401 -368 C ATOM 2161 O PHE A 358 25.041 -41.966 -17.537 1.00 63.93 O ANISOU 2161 O PHE A 358 10784 6950 6554 -136 -326 -342 O ATOM 2162 CB PHE A 358 24.628 -45.123 -18.564 1.00 60.24 C ANISOU 2162 CB PHE A 358 10073 6705 6108 -199 -97 -374 C ATOM 2163 CG PHE A 358 23.611 -44.995 -17.475 1.00 60.23 C ANISOU 2163 CG PHE A 358 10423 6583 5879 -155 41 -354 C ATOM 2164 CD1 PHE A 358 22.266 -44.876 -17.780 1.00 59.41 C ANISOU 2164 CD1 PHE A 358 10242 6571 5759 -169 341 -321 C ATOM 2165 CD2 PHE A 358 23.997 -45.031 -16.144 1.00 61.68 C ANISOU 2165 CD2 PHE A 358 11043 6504 5888 -81 -124 -369 C ATOM 2166 CE1 PHE A 358 21.322 -44.774 -16.780 1.00 60.50 C ANISOU 2166 CE1 PHE A 358 10688 6538 5759 -121 565 -285 C ATOM 2167 CE2 PHE A 358 23.060 -44.928 -15.140 1.00 62.99 C ANISOU 2167 CE2 PHE A 358 11620 6500 5813 -11 90 -333 C ATOM 2168 CZ PHE A 358 21.719 -44.799 -15.458 1.00 62.45 C ANISOU 2168 CZ PHE A 358 11427 6521 5779 -36 482 -282 C ATOM 2169 N TYR A 359 26.853 -43.305 -17.430 1.00 65.00 N ANISOU 2169 N TYR A 359 10811 6908 6977 -141 -723 -419 N ATOM 2170 CA TYR A 359 27.466 -42.567 -16.326 1.00 68.11 C ANISOU 2170 CA TYR A 359 11486 7017 7373 -79 -1078 -464 C ATOM 2171 C TYR A 359 27.986 -41.206 -16.775 1.00 68.46 C ANISOU 2171 C TYR A 359 11279 7038 7693 -101 -1146 -454 C ATOM 2172 O TYR A 359 28.113 -40.284 -15.961 1.00 70.15 O ANISOU 2172 O TYR A 359 11738 7057 7859 -52 -1371 -484 O ATOM 2173 CB TYR A 359 28.574 -43.395 -15.660 1.00 70.68 C ANISOU 2173 CB TYR A 359 11927 7083 7844 -36 -1492 -540 C ATOM 2174 CG TYR A 359 28.033 -44.554 -14.848 1.00 71.57 C ANISOU 2174 CG TYR A 359 12463 7128 7599 24 -1461 -551 C ATOM 2175 CD1 TYR A 359 27.233 -44.329 -13.734 1.00 73.13 C ANISOU 2175 CD1 TYR A 359 13239 7170 7376 122 -1410 -542 C ATOM 2176 CD2 TYR A 359 28.309 -45.872 -15.199 1.00 71.60 C ANISOU 2176 CD2 TYR A 359 12322 7195 7688 -4 -1430 -561 C ATOM 2177 CE1 TYR A 359 26.722 -45.383 -12.993 1.00 74.29 C ANISOU 2177 CE1 TYR A 359 13812 7206 7208 196 -1295 -534 C ATOM 2178 CE2 TYR A 359 27.802 -46.933 -14.463 1.00 72.50 C ANISOU 2178 CE2 TYR A 359 12827 7229 7491 55 -1364 -564 C ATOM 2179 CZ TYR A 359 27.011 -46.681 -13.361 1.00 73.53 C ANISOU 2179 CZ TYR A 359 13534 7185 7217 159 -1281 -546 C ATOM 2180 OH TYR A 359 26.509 -47.722 -12.625 1.00 74.45 O ANISOU 2180 OH TYR A 359 14077 7170 7038 236 -1138 -533 O ATOM 2181 N ALA A 360 28.273 -41.084 -18.069 1.00 67.49 N ANISOU 2181 N ALA A 360 10715 7082 7843 -161 -930 -410 N ATOM 2182 CA ALA A 360 28.635 -39.797 -18.664 1.00 67.29 C ANISOU 2182 CA ALA A 360 10445 7046 8074 -177 -867 -376 C ATOM 2183 C ALA A 360 27.537 -38.764 -18.464 1.00 66.10 C ANISOU 2183 C ALA A 360 10487 7006 7621 -160 -707 -338 C ATOM 2184 O ALA A 360 27.826 -37.624 -18.106 1.00 67.09 O ANISOU 2184 O ALA A 360 10642 6994 7853 -145 -843 -346 O ATOM 2185 CB ALA A 360 28.949 -39.952 -20.146 1.00 66.32 C ANISOU 2185 CB ALA A 360 9943 7066 8189 -206 -552 -315 C ATOM 2186 N SER A 361 26.286 -39.166 -18.676 1.00 64.51 N ANISOU 2186 N SER A 361 10392 7017 7098 -161 -434 -302 N ATOM 2187 CA SER A 361 25.155 -38.251 -18.527 1.00 65.32 C ANISOU 2187 CA SER A 361 10635 7204 6977 -144 -247 -260 C ATOM 2188 C SER A 361 25.232 -37.510 -17.208 1.00 67.17 C ANISOU 2188 C SER A 361 11235 7201 7085 -93 -456 -289 C ATOM 2189 O SER A 361 25.128 -36.289 -17.167 1.00 67.66 O ANISOU 2189 O SER A 361 11305 7235 7164 -83 -445 -268 O ATOM 2190 CB SER A 361 23.831 -38.997 -18.561 1.00 65.26 C ANISOU 2190 CB SER A 361 10720 7336 6739 -143 4 -239 C ATOM 2191 OG SER A 361 23.459 -39.403 -17.247 1.00 69.12 O ANISOU 2191 OG SER A 361 11610 7642 7010 -99 -30 -256 O ATOM 2192 N SER A 362 25.411 -38.266 -16.131 1.00 69.21 N ANISOU 2192 N SER A 362 11849 7263 7184 -44 -653 -338 N ATOM 2193 CA SER A 362 25.480 -37.688 -14.799 1.00 72.66 C ANISOU 2193 CA SER A 362 12786 7408 7414 45 -886 -377 C ATOM 2194 C SER A 362 26.676 -36.755 -14.625 1.00 74.89 C ANISOU 2194 C SER A 362 12985 7481 7988 54 -1306 -441 C ATOM 2195 O SER A 362 26.578 -35.742 -13.928 1.00 75.86 O ANISOU 2195 O SER A 362 13403 7428 7991 112 -1437 -459 O ATOM 2196 CB SER A 362 25.508 -38.792 -13.745 1.00 74.66 C ANISOU 2196 CB SER A 362 13511 7447 7409 129 -1026 -418 C ATOM 2197 OG SER A 362 24.264 -39.465 -13.719 1.00 74.74 O ANISOU 2197 OG SER A 362 13644 7573 7181 133 -584 -352 O ATOM 2198 N ALA A 363 27.793 -37.091 -15.265 1.00 75.64 N ANISOU 2198 N ALA A 363 12669 7558 8513 0 -1497 -475 N ATOM 2199 CA ALA A 363 28.994 -36.262 -15.204 1.00 78.53 C ANISOU 2199 CA ALA A 363 12832 7673 9330 -2 -1876 -537 C ATOM 2200 C ALA A 363 28.858 -34.933 -15.974 1.00 78.38 C ANISOU 2200 C ALA A 363 12509 7770 9499 -50 -1638 -475 C ATOM 2201 O ALA A 363 29.272 -33.882 -15.481 1.00 80.91 O ANISOU 2201 O ALA A 363 12901 7865 9976 -23 -1902 -522 O ATOM 2202 CB ALA A 363 30.191 -37.049 -15.715 1.00 79.30 C ANISOU 2202 CB ALA A 363 12525 7673 9930 -44 -2056 -574 C ATOM 2203 N ILE A 364 28.282 -34.977 -17.172 1.00 75.78 N ANISOU 2203 N ILE A 364 11881 7762 9148 -105 -1169 -378 N ATOM 2204 CA ILE A 364 28.219 -33.784 -18.018 1.00 75.93 C ANISOU 2204 CA ILE A 364 11632 7874 9344 -130 -926 -312 C ATOM 2205 C ILE A 364 27.041 -32.876 -17.665 1.00 74.88 C ANISOU 2205 C ILE A 364 11773 7849 8827 -102 -764 -273 C ATOM 2206 O ILE A 364 27.183 -31.655 -17.675 1.00 75.79 O ANISOU 2206 O ILE A 364 11838 7887 9072 -98 -780 -261 O ATOM 2207 CB ILE A 364 28.218 -34.127 -19.530 1.00 75.38 C ANISOU 2207 CB ILE A 364 11198 8030 9413 -162 -526 -228 C ATOM 2208 CG1 ILE A 364 26.906 -34.793 -19.964 1.00 73.49 C ANISOU 2208 CG1 ILE A 364 11088 8096 8737 -155 -241 -183 C ATOM 2209 CG2 ILE A 364 29.418 -35.005 -19.875 1.00 76.90 C ANISOU 2209 CG2 ILE A 364 11120 8073 10025 -183 -623 -254 C ATOM 2210 CD1 ILE A 364 26.941 -35.341 -21.377 1.00 72.48 C ANISOU 2210 CD1 ILE A 364 10724 8136 8679 -154 50 -128 C ATOM 2211 N ASN A 365 25.894 -33.468 -17.341 1.00 72.78 N ANISOU 2211 N ASN A 365 11777 7728 8148 -80 -588 -250 N ATOM 2212 CA ASN A 365 24.701 -32.698 -16.971 1.00 72.25 C ANISOU 2212 CA ASN A 365 11954 7722 7775 -48 -379 -205 C ATOM 2213 C ASN A 365 24.955 -31.448 -16.130 1.00 73.35 C ANISOU 2213 C ASN A 365 12335 7632 7901 -5 -584 -234 C ATOM 2214 O ASN A 365 24.510 -30.368 -16.509 1.00 73.68 O ANISOU 2214 O ASN A 365 12284 7759 7952 -11 -403 -182 O ATOM 2215 CB ASN A 365 23.683 -33.583 -16.248 1.00 72.67 C ANISOU 2215 CB ASN A 365 12351 7776 7481 -10 -232 -197 C ATOM 2216 CG ASN A 365 22.749 -34.298 -17.201 1.00 71.11 C ANISOU 2216 CG ASN A 365 11901 7848 7270 -48 98 -144 C ATOM 2217 OD1 ASN A 365 23.021 -34.412 -18.397 1.00 70.79 O ANISOU 2217 OD1 ASN A 365 11497 7985 7413 -89 154 -128 O ATOM 2218 ND2 ASN A 365 21.637 -34.786 -16.673 1.00 71.38 N ANISOU 2218 ND2 ASN A 365 12152 7861 7105 -20 324 -119 N ATOM 2219 N PRO A 366 25.656 -31.581 -14.988 1.00 74.76 N ANISOU 2219 N PRO A 366 12861 7494 8048 51 -997 -326 N ATOM 2220 CA PRO A 366 25.918 -30.364 -14.216 1.00 76.54 C ANISOU 2220 CA PRO A 366 13352 7465 8265 105 -1249 -372 C ATOM 2221 C PRO A 366 26.599 -29.278 -15.050 1.00 76.11 C ANISOU 2221 C PRO A 366 12826 7431 8660 41 -1272 -360 C ATOM 2222 O PRO A 366 26.249 -28.111 -14.925 1.00 75.73 O ANISOU 2222 O PRO A 366 12860 7356 8555 57 -1200 -337 O ATOM 2223 CB PRO A 366 26.836 -30.842 -13.079 1.00 79.28 C ANISOU 2223 CB PRO A 366 14086 7427 8609 187 -1816 -500 C ATOM 2224 CG PRO A 366 27.352 -32.167 -13.518 1.00 79.18 C ANISOU 2224 CG PRO A 366 13814 7495 8776 143 -1865 -515 C ATOM 2225 CD PRO A 366 26.259 -32.763 -14.355 1.00 76.06 C ANISOU 2225 CD PRO A 366 13227 7484 8185 86 -1300 -402 C ATOM 2226 N ILE A 367 27.535 -29.670 -15.912 1.00 76.08 N ANISOU 2226 N ILE A 367 12344 7452 9108 -22 -1310 -364 N ATOM 2227 CA ILE A 367 28.253 -28.720 -16.772 1.00 77.17 C ANISOU 2227 CA ILE A 367 12026 7553 9740 -71 -1237 -335 C ATOM 2228 C ILE A 367 27.366 -28.154 -17.891 1.00 74.66 C ANISOU 2228 C ILE A 367 11525 7561 9279 -91 -708 -206 C ATOM 2229 O ILE A 367 27.415 -26.964 -18.194 1.00 75.28 O ANISOU 2229 O ILE A 367 11485 7608 9510 -92 -605 -170 O ATOM 2230 CB ILE A 367 29.505 -29.374 -17.402 1.00 78.89 C ANISOU 2230 CB ILE A 367 11801 7646 10527 -115 -1330 -357 C ATOM 2231 CG1 ILE A 367 30.475 -29.840 -16.306 1.00 82.06 C ANISOU 2231 CG1 ILE A 367 12343 7662 11171 -85 -1951 -501 C ATOM 2232 CG2 ILE A 367 30.200 -28.409 -18.364 1.00 79.43 C ANISOU 2232 CG2 ILE A 367 11407 7630 11141 -150 -1114 -299 C ATOM 2233 CD1 ILE A 367 31.506 -30.845 -16.778 1.00 82.63 C ANISOU 2233 CD1 ILE A 367 12037 7625 11734 -120 -2034 -524 C ATOM 2234 N LEU A 368 26.557 -29.012 -18.498 1.00 72.78 N ANISOU 2234 N LEU A 368 11281 7608 8764 -95 -410 -147 N ATOM 2235 CA LEU A 368 25.735 -28.623 -19.634 1.00 70.93 C ANISOU 2235 CA LEU A 368 10899 7643 8405 -89 1 -45 C ATOM 2236 C LEU A 368 24.569 -27.749 -19.192 1.00 71.53 C ANISOU 2236 C LEU A 368 11215 7795 8165 -59 115 -12 C ATOM 2237 O LEU A 368 24.318 -26.696 -19.781 1.00 74.89 O ANISOU 2237 O LEU A 368 11535 8283 8635 -45 297 47 O ATOM 2238 CB LEU A 368 25.211 -29.866 -20.351 1.00 68.98 C ANISOU 2238 CB LEU A 368 10599 7620 7990 -89 186 -19 C ATOM 2239 CG LEU A 368 24.968 -29.751 -21.851 1.00 67.69 C ANISOU 2239 CG LEU A 368 10236 7637 7844 -59 506 61 C ATOM 2240 CD1 LEU A 368 26.252 -29.365 -22.578 1.00 68.94 C ANISOU 2240 CD1 LEU A 368 10142 7634 8418 -55 594 93 C ATOM 2241 CD2 LEU A 368 24.416 -31.069 -22.374 1.00 65.90 C ANISOU 2241 CD2 LEU A 368 10023 7582 7432 -51 583 55 C ATOM 2242 N TYR A 369 23.866 -28.180 -18.151 1.00 71.49 N ANISOU 2242 N TYR A 369 11555 7751 7857 -37 43 -45 N ATOM 2243 CA TYR A 369 22.701 -27.445 -17.657 1.00 71.38 C ANISOU 2243 CA TYR A 369 11785 7759 7574 0 218 -4 C ATOM 2244 C TYR A 369 23.052 -26.148 -16.937 1.00 73.73 C ANISOU 2244 C TYR A 369 12267 7844 7901 26 59 -28 C ATOM 2245 O TYR A 369 22.187 -25.291 -16.774 1.00 74.74 O ANISOU 2245 O TYR A 369 12523 8000 7875 55 253 21 O ATOM 2246 CB TYR A 369 21.851 -28.325 -16.739 1.00 71.00 C ANISOU 2246 CB TYR A 369 12085 7659 7230 35 290 -15 C ATOM 2247 CG TYR A 369 20.971 -29.282 -17.495 1.00 68.96 C ANISOU 2247 CG TYR A 369 11629 7624 6948 14 544 25 C ATOM 2248 CD1 TYR A 369 19.742 -28.871 -17.991 1.00 68.23 C ANISOU 2248 CD1 TYR A 369 11425 7664 6835 27 828 90 C ATOM 2249 CD2 TYR A 369 21.370 -30.591 -17.731 1.00 68.64 C ANISOU 2249 CD2 TYR A 369 11497 7632 6951 -12 460 -10 C ATOM 2250 CE1 TYR A 369 18.926 -29.738 -18.694 1.00 67.57 C ANISOU 2250 CE1 TYR A 369 11141 7730 6799 16 978 105 C ATOM 2251 CE2 TYR A 369 20.561 -31.469 -18.434 1.00 67.67 C ANISOU 2251 CE2 TYR A 369 11196 7684 6831 -26 649 10 C ATOM 2252 CZ TYR A 369 19.339 -31.037 -18.912 1.00 67.20 C ANISOU 2252 CZ TYR A 369 11025 7728 6777 -10 884 62 C ATOM 2253 OH TYR A 369 18.526 -31.898 -19.607 1.00 66.27 O ANISOU 2253 OH TYR A 369 10717 7730 6730 -17 991 61 O ATOM 2254 N ASN A 370 24.301 -26.006 -16.495 1.00 76.23 N ANISOU 2254 N ASN A 370 12590 7918 8455 20 -313 -111 N ATOM 2255 CA ASN A 370 24.746 -24.777 -15.834 1.00 78.67 C ANISOU 2255 CA ASN A 370 13056 7976 8857 47 -547 -157 C ATOM 2256 C ASN A 370 25.617 -23.879 -16.715 1.00 79.04 C ANISOU 2256 C ASN A 370 12653 7994 9381 -1 -546 -140 C ATOM 2257 O ASN A 370 26.072 -22.837 -16.253 1.00 80.82 O ANISOU 2257 O ASN A 370 12938 7992 9778 10 -757 -186 O ATOM 2258 CB ASN A 370 25.513 -25.103 -14.548 1.00 82.32 C ANISOU 2258 CB ASN A 370 13910 8073 9293 102 -1062 -288 C ATOM 2259 CG ASN A 370 24.716 -25.972 -13.583 1.00 83.42 C ANISOU 2259 CG ASN A 370 14601 8162 8932 182 -1019 -296 C ATOM 2260 OD1 ASN A 370 23.773 -26.664 -13.973 1.00 81.39 O ANISOU 2260 OD1 ASN A 370 14295 8151 8478 167 -628 -214 O ATOM 2261 ND2 ASN A 370 25.112 -25.952 -12.312 1.00 87.17 N ANISOU 2261 ND2 ASN A 370 15633 8267 9221 285 -1434 -400 N ATOM 2262 N LEU A 371 25.850 -24.275 -17.970 1.00 78.20 N ANISOU 2262 N LEU A 371 12138 8078 9495 -42 -290 -73 N ATOM 2263 CA LEU A 371 26.677 -23.481 -18.894 1.00 78.07 C ANISOU 2263 CA LEU A 371 11725 7989 9948 -66 -166 -31 C ATOM 2264 C LEU A 371 26.092 -22.087 -19.112 1.00 77.47 C ANISOU 2264 C LEU A 371 11679 7966 9788 -44 45 34 C ATOM 2265 O LEU A 371 26.776 -21.082 -18.924 1.00 77.26 O ANISOU 2265 O LEU A 371 11547 7706 10100 -53 -80 8 O ATOM 2266 CB LEU A 371 26.839 -24.183 -20.257 1.00 76.64 C ANISOU 2266 CB LEU A 371 11244 7990 9886 -72 172 51 C ATOM 2267 CG LEU A 371 28.203 -24.775 -20.637 1.00 78.81 C ANISOU 2267 CG LEU A 371 11193 8051 10697 -102 99 24 C ATOM 2268 CD1 LEU A 371 28.089 -25.494 -21.970 1.00 78.43 C ANISOU 2268 CD1 LEU A 371 11003 8199 10595 -74 504 119 C ATOM 2269 CD2 LEU A 371 29.299 -23.725 -20.727 1.00 81.70 C ANISOU 2269 CD2 LEU A 371 11266 8087 11687 -118 57 18 C ATOM 2270 N VAL A 372 24.821 -22.060 -19.513 1.00118.41 N ANISOU 2270 N VAL A 372 15151 14292 15548 -947 -3049 -1682 N ATOM 2271 CA VAL A 372 24.104 -20.827 -19.873 1.00119.54 C ANISOU 2271 CA VAL A 372 15126 14560 15734 -941 -3059 -1507 C ATOM 2272 C VAL A 372 24.175 -19.713 -18.826 1.00118.03 C ANISOU 2272 C VAL A 372 14657 14470 15719 -917 -2674 -1361 C ATOM 2273 O VAL A 372 24.337 -18.543 -19.179 1.00118.26 O ANISOU 2273 O VAL A 372 14662 14599 15670 -817 -2486 -1290 O ATOM 2274 CB VAL A 372 22.611 -21.117 -20.185 1.00122.68 C ANISOU 2274 CB VAL A 372 15362 14897 16353 -1119 -3453 -1347 C ATOM 2275 CG1 VAL A 372 21.880 -21.692 -18.970 1.00122.22 C ANISOU 2275 CG1 VAL A 372 15014 14734 16689 -1268 -3460 -1226 C ATOM 2276 CG2 VAL A 372 21.908 -19.861 -20.698 1.00123.53 C ANISOU 2276 CG2 VAL A 372 15278 15142 16515 -1079 -3456 -1096 C ATOM 2277 N SER A 373 24.044 -20.085 -17.564 1.00117.45 N ANISOU 2277 N SER A 373 14393 14359 15870 -1022 -2539 -1319 N ATOM 2278 CA SER A 373 24.007 -19.126 -16.477 1.00115.70 C ANISOU 2278 CA SER A 373 13952 14209 15799 -1058 -2166 -1207 C ATOM 2279 C SER A 373 25.351 -18.472 -16.231 1.00114.12 C ANISOU 2279 C SER A 373 13872 14142 15346 -994 -1830 -1323 C ATOM 2280 O SER A 373 26.390 -19.026 -16.538 1.00112.89 O ANISOU 2280 O SER A 373 13892 14025 14975 -933 -1857 -1447 O ATOM 2281 CB SER A 373 23.555 -19.818 -15.207 1.00114.97 C ANISOU 2281 CB SER A 373 13649 14058 15976 -1208 -2131 -1125 C ATOM 2282 OG SER A 373 24.625 -20.539 -14.645 1.00114.06 O ANISOU 2282 OG SER A 373 13631 13934 15770 -1234 -2200 -1239 O ATOM 2283 N ALA A 374 25.318 -17.279 -15.662 1.00114.65 N ANISOU 2283 N ALA A 374 13840 14260 15460 -1016 -1495 -1261 N ATOM 2284 CA ALA A 374 26.531 -16.560 -15.345 1.00114.49 C ANISOU 2284 CA ALA A 374 13911 14369 15221 -1023 -1173 -1355 C ATOM 2285 C ALA A 374 27.153 -17.242 -14.169 1.00115.23 C ANISOU 2285 C ALA A 374 13948 14555 15276 -1192 -1063 -1393 C ATOM 2286 O ALA A 374 26.438 -17.843 -13.384 1.00117.01 O ANISOU 2286 O ALA A 374 14022 14738 15696 -1326 -1041 -1325 O ATOM 2287 CB ALA A 374 26.197 -15.141 -14.985 1.00114.50 C ANISOU 2287 CB ALA A 374 13846 14347 15310 -1038 -824 -1294 C ATOM 2288 N ASN A 375 28.476 -17.155 -14.057 1.00115.43 N ANISOU 2288 N ASN A 375 14075 14728 15055 -1183 -990 -1459 N ATOM 2289 CA ASN A 375 29.248 -17.828 -13.008 1.00114.85 C ANISOU 2289 CA ASN A 375 13931 14807 14898 -1333 -935 -1433 C ATOM 2290 C ASN A 375 29.660 -19.257 -13.289 1.00115.84 C ANISOU 2290 C ASN A 375 14088 14897 15029 -1223 -1180 -1404 C ATOM 2291 O ASN A 375 30.157 -19.918 -12.400 1.00114.64 O ANISOU 2291 O ASN A 375 13824 14856 14877 -1329 -1158 -1316 O ATOM 2292 CB ASN A 375 28.530 -17.768 -11.672 1.00114.31 C ANISOU 2292 CB ASN A 375 13702 14768 14962 -1571 -797 -1381 C ATOM 2293 CG ASN A 375 27.789 -16.478 -11.491 1.00114.31 C ANISOU 2293 CG ASN A 375 13713 14749 14970 -1694 -469 -1425 C ATOM 2294 OD1 ASN A 375 28.245 -15.430 -11.919 1.00114.01 O ANISOU 2294 OD1 ASN A 375 13769 14808 14741 -1748 -264 -1494 O ATOM 2295 ND2 ASN A 375 26.605 -16.558 -10.907 1.00114.99 N ANISOU 2295 ND2 ASN A 375 13701 14685 15302 -1735 -388 -1370 N ATOM 2296 N PHE A 376 29.480 -19.712 -14.525 1.00118.80 N ANISOU 2296 N PHE A 376 14624 15114 15399 -1023 -1390 -1468 N ATOM 2297 CA PHE A 376 29.926 -21.044 -14.916 1.00121.72 C ANISOU 2297 CA PHE A 376 15099 15396 15751 -904 -1540 -1477 C ATOM 2298 C PHE A 376 31.449 -21.127 -14.864 1.00122.86 C ANISOU 2298 C PHE A 376 15303 15692 15686 -801 -1355 -1428 C ATOM 2299 O PHE A 376 32.015 -21.844 -14.038 1.00124.46 O ANISOU 2299 O PHE A 376 15410 15961 15917 -814 -1304 -1304 O ATOM 2300 CB PHE A 376 29.426 -21.388 -16.320 1.00123.98 C ANISOU 2300 CB PHE A 376 15614 15464 16028 -760 -1796 -1597 C ATOM 2301 CG PHE A 376 30.032 -22.639 -16.889 1.00125.84 C ANISOU 2301 CG PHE A 376 16054 15566 16192 -614 -1845 -1652 C ATOM 2302 CD1 PHE A 376 29.696 -23.882 -16.378 1.00126.24 C ANISOU 2302 CD1 PHE A 376 16043 15481 16441 -670 -1928 -1611 C ATOM 2303 CD2 PHE A 376 30.936 -22.572 -17.936 1.00127.01 C ANISOU 2303 CD2 PHE A 376 16457 15706 16094 -406 -1754 -1725 C ATOM 2304 CE1 PHE A 376 30.252 -25.035 -16.900 1.00128.20 C ANISOU 2304 CE1 PHE A 376 16492 15553 16662 -521 -1899 -1651 C ATOM 2305 CE2 PHE A 376 31.495 -23.721 -18.462 1.00128.87 C ANISOU 2305 CE2 PHE A 376 16907 15774 16280 -250 -1718 -1768 C ATOM 2306 CZ PHE A 376 31.153 -24.954 -17.944 1.00129.73 C ANISOU 2306 CZ PHE A 376 16965 15717 16608 -307 -1778 -1735 C ATOM 2307 N ARG A 377 32.091 -20.374 -15.751 1.00123.04 N ANISOU 2307 N ARG A 377 15452 15769 15525 -689 -1249 -1480 N ATOM 2308 CA ARG A 377 33.535 -20.240 -15.760 1.00122.57 C ANISOU 2308 CA ARG A 377 15410 15874 15285 -602 -1049 -1394 C ATOM 2309 C ARG A 377 34.017 -20.096 -14.347 1.00122.70 C ANISOU 2309 C ARG A 377 15172 16143 15304 -847 -904 -1236 C ATOM 2310 O ARG A 377 35.027 -20.651 -13.935 1.00123.15 O ANISOU 2310 O ARG A 377 15146 16351 15292 -821 -811 -1065 O ATOM 2311 CB ARG A 377 33.924 -18.932 -16.432 1.00120.91 C ANISOU 2311 CB ARG A 377 15321 15703 14916 -499 -935 -1453 C ATOM 2312 CG ARG A 377 34.260 -19.043 -17.895 1.00120.57 C ANISOU 2312 CG ARG A 377 15323 15787 14700 -353 -748 -1350 C ATOM 2313 CD ARG A 377 35.724 -19.351 -18.097 1.00122.05 C ANISOU 2313 CD ARG A 377 15785 15809 14776 -36 -789 -1403 C ATOM 2314 NE ARG A 377 35.964 -19.801 -19.460 1.00123.86 N ANISOU 2314 NE ARG A 377 16101 15858 15101 28 -918 -1430 N ATOM 2315 CZ ARG A 377 35.668 -21.016 -19.901 1.00126.10 C ANISOU 2315 CZ ARG A 377 16688 15926 15295 255 -960 -1535 C ATOM 2316 NH1 ARG A 377 35.133 -21.906 -19.082 1.00127.11 N ANISOU 2316 NH1 ARG A 377 17061 16028 15204 453 -898 -1607 N ATOM 2317 NH2 ARG A 377 35.916 -21.342 -21.157 1.00126.85 N ANISOU 2317 NH2 ARG A 377 16865 15819 15512 274 -1043 -1571 N ATOM 2318 N GLN A 378 33.256 -19.311 -13.614 1.00122.21 N ANISOU 2318 N GLN A 378 14988 16131 15315 -1093 -878 -1271 N ATOM 2319 CA GLN A 378 33.543 -18.976 -12.219 1.00121.90 C ANISOU 2319 CA GLN A 378 14745 16332 15239 -1387 -772 -1151 C ATOM 2320 C GLN A 378 33.535 -20.219 -11.311 1.00121.52 C ANISOU 2320 C GLN A 378 14546 16300 15322 -1420 -893 -1001 C ATOM 2321 O GLN A 378 34.571 -20.592 -10.763 1.00121.30 O ANISOU 2321 O GLN A 378 14421 16413 15254 -1378 -877 -805 O ATOM 2322 CB GLN A 378 32.662 -17.922 -11.523 1.00122.06 C ANISOU 2322 CB GLN A 378 14743 16350 15283 -1626 -641 -1261 C ATOM 2323 CG GLN A 378 32.850 -17.799 -10.015 0.00122.81 C ANISOU 2323 CG GLN A 378 14691 16681 15287 -1979 -523 -1184 C ATOM 2324 CD GLN A 378 34.295 -17.580 -9.616 0.00123.77 C ANISOU 2324 CD GLN A 378 14740 17120 15166 -2145 -446 -1050 C ATOM 2325 OE1 GLN A 378 34.832 -18.297 -8.771 0.00125.31 O ANISOU 2325 OE1 GLN A 378 14762 17547 15300 -2294 -505 -851 O ATOM 2326 NE2 GLN A 378 34.935 -16.592 -10.229 0.00123.92 N ANISOU 2326 NE2 GLN A 378 14859 17165 15058 -2126 -320 -1115 N ATOM 2327 N VAL A 379 32.369 -20.862 -11.180 1.00120.64 N ANISOU 2327 N VAL A 379 14394 16038 15403 -1478 -1000 -1052 N ATOM 2328 CA VAL A 379 32.064 -21.712 -10.021 1.00120.44 C ANISOU 2328 CA VAL A 379 14174 16085 15501 -1605 -1054 -887 C ATOM 2329 C VAL A 379 32.652 -23.112 -10.193 1.00121.98 C ANISOU 2329 C VAL A 379 14322 16232 15793 -1425 -1137 -718 C ATOM 2330 O VAL A 379 33.270 -23.626 -9.259 1.00124.31 O ANISOU 2330 O VAL A 379 14420 16770 16041 -1524 -1071 -471 O ATOM 2331 CB VAL A 379 30.574 -21.904 -9.628 1.00119.59 C ANISOU 2331 CB VAL A 379 14018 15794 15625 -1677 -1141 -948 C ATOM 2332 CG1 VAL A 379 29.961 -20.571 -9.204 1.00118.93 C ANISOU 2332 CG1 VAL A 379 13955 15751 15481 -1855 -962 -1057 C ATOM 2333 CG2 VAL A 379 29.766 -22.570 -10.740 1.00119.83 C ANISOU 2333 CG2 VAL A 379 14175 15492 15861 -1458 -1365 -1051 C ATOM 2334 N PHE A 380 32.467 -23.710 -11.349 1.00121.84 N ANISOU 2334 N PHE A 380 14486 15904 15903 -1178 -1261 -830 N ATOM 2335 CA PHE A 380 32.952 -25.054 -11.484 1.00123.94 C ANISOU 2335 CA PHE A 380 14747 16033 16310 -1003 -1280 -693 C ATOM 2336 C PHE A 380 34.445 -24.864 -11.618 1.00125.37 C ANISOU 2336 C PHE A 380 14935 16360 16339 -851 -1103 -531 C ATOM 2337 O PHE A 380 35.232 -25.420 -10.855 1.00127.42 O ANISOU 2337 O PHE A 380 15037 16675 16700 -781 -1013 -258 O ATOM 2338 CB PHE A 380 32.366 -25.758 -12.707 1.00124.13 C ANISOU 2338 CB PHE A 380 15025 15652 16487 -838 -1453 -902 C ATOM 2339 CG PHE A 380 32.567 -27.245 -12.704 1.00124.97 C ANISOU 2339 CG PHE A 380 15179 15530 16774 -672 -1421 -801 C ATOM 2340 CD1 PHE A 380 32.129 -28.011 -11.653 1.00125.02 C ANISOU 2340 CD1 PHE A 380 14912 15593 16995 -745 -1378 -538 C ATOM 2341 CD2 PHE A 380 33.209 -27.872 -13.749 1.00125.88 C ANISOU 2341 CD2 PHE A 380 15631 15352 16844 -440 -1403 -963 C ATOM 2342 CE1 PHE A 380 32.325 -29.378 -11.649 1.00126.29 C ANISOU 2342 CE1 PHE A 380 15110 15501 17372 -573 -1294 -419 C ATOM 2343 CE2 PHE A 380 33.401 -29.236 -13.749 1.00127.33 C ANISOU 2343 CE2 PHE A 380 15901 15261 17214 -283 -1302 -887 C ATOM 2344 CZ PHE A 380 32.965 -29.990 -12.697 1.00127.36 C ANISOU 2344 CZ PHE A 380 15607 15300 17483 -340 -1239 -606 C ATOM 2345 N LEU A 381 34.816 -24.048 -12.590 1.00124.18 N ANISOU 2345 N LEU A 381 14930 16277 15974 -796 -1033 -652 N ATOM 2346 CA LEU A 381 36.216 -23.904 -13.016 1.00124.48 C ANISOU 2346 CA LEU A 381 14966 16448 15879 -639 -854 -481 C ATOM 2347 C LEU A 381 37.071 -23.045 -12.055 1.00123.15 C ANISOU 2347 C LEU A 381 14532 16709 15549 -895 -752 -260 C ATOM 2348 O LEU A 381 38.210 -22.693 -12.377 1.00122.77 O ANISOU 2348 O LEU A 381 14445 16815 15387 -814 -617 -97 O ATOM 2349 CB LEU A 381 36.290 -23.367 -14.460 1.00123.96 C ANISOU 2349 CB LEU A 381 15224 16199 15673 -405 -825 -708 C ATOM 2350 CG LEU A 381 35.869 -24.297 -15.617 1.00124.44 C ANISOU 2350 CG LEU A 381 15613 15867 15798 -143 -890 -896 C ATOM 2351 CD1 LEU A 381 36.661 -25.599 -15.611 1.00126.13 C ANISOU 2351 CD1 LEU A 381 15815 15944 16162 55 -735 -688 C ATOM 2352 CD2 LEU A 381 34.371 -24.580 -15.616 1.00123.96 C ANISOU 2352 CD2 LEU A 381 15636 15599 15861 -270 -1147 -1121 C ATOM 2353 N SER A 382 36.518 -22.711 -10.886 1.00121.65 N ANISOU 2353 N SER A 382 14173 16708 15338 -1222 -811 -251 N ATOM 2354 CA SER A 382 37.307 -22.176 -9.768 1.00121.00 C ANISOU 2354 CA SER A 382 13838 17054 15082 -1545 -745 -17 C ATOM 2355 C SER A 382 37.837 -23.309 -8.886 1.00121.60 C ANISOU 2355 C SER A 382 13614 17321 15265 -1588 -765 376 C ATOM 2356 O SER A 382 38.828 -23.138 -8.172 1.00122.94 O ANISOU 2356 O SER A 382 13535 17880 15296 -1793 -728 692 O ATOM 2357 CB SER A 382 36.463 -21.235 -8.908 1.00119.74 C ANISOU 2357 CB SER A 382 13693 16999 14801 -1898 -749 -212 C ATOM 2358 OG SER A 382 35.384 -21.931 -8.307 1.00119.74 O ANISOU 2358 OG SER A 382 13644 16876 14975 -1944 -840 -244 O ATOM 2359 N THR A 383 37.178 -24.467 -8.953 1.00120.13 N ANISOU 2359 N THR A 383 13438 16866 15338 -1409 -828 383 N ATOM 2360 CA THR A 383 37.485 -25.609 -8.092 1.00120.16 C ANISOU 2360 CA THR A 383 13148 17000 15507 -1429 -829 766 C ATOM 2361 C THR A 383 38.710 -26.426 -8.537 1.00121.81 C ANISOU 2361 C THR A 383 13229 17204 15849 -1144 -687 1136 C ATOM 2362 O THR A 383 39.047 -27.434 -7.907 1.00123.84 O ANISOU 2362 O THR A 383 13215 17544 16294 -1109 -648 1521 O ATOM 2363 CB THR A 383 36.268 -26.547 -8.014 1.00118.84 C ANISOU 2363 CB THR A 383 13043 16495 15616 -1344 -926 636 C ATOM 2364 OG1 THR A 383 35.931 -27.000 -9.331 1.00117.34 O ANISOU 2364 OG1 THR A 383 13159 15847 15579 -1020 -931 385 O ATOM 2365 CG2 THR A 383 35.076 -25.818 -7.410 1.00116.93 C ANISOU 2365 CG2 THR A 383 12850 16283 15292 -1617 -1024 379 C ATOM 2366 N LEU A 384 39.377 -25.984 -9.604 1.00120.51 N ANISOU 2366 N LEU A 384 13243 16939 15604 -928 -577 1057 N ATOM 2367 CA LEU A 384 40.526 -26.693 -10.169 1.00121.73 C ANISOU 2367 CA LEU A 384 13318 17030 15902 -604 -373 1398 C ATOM 2368 C LEU A 384 41.840 -26.121 -9.628 1.00122.31 C ANISOU 2368 C LEU A 384 13048 17599 15823 -773 -310 1839 C ATOM 2369 O LEU A 384 42.789 -26.858 -9.351 1.00123.88 O ANISOU 2369 O LEU A 384 12939 17942 16185 -653 -179 2356 O ATOM 2370 CB LEU A 384 40.498 -26.601 -11.701 1.00120.41 C ANISOU 2370 CB LEU A 384 13568 16454 15728 -251 -263 1076 C ATOM 2371 CG LEU A 384 39.419 -27.398 -12.449 1.00119.59 C ANISOU 2371 CG LEU A 384 13821 15832 15782 -54 -314 707 C ATOM 2372 CD1 LEU A 384 38.020 -27.184 -11.886 1.00117.20 C ANISOU 2372 CD1 LEU A 384 13548 15502 15479 -328 -573 418 C ATOM 2373 CD2 LEU A 384 39.455 -27.045 -13.928 1.00119.13 C ANISOU 2373 CD2 LEU A 384 14188 15485 15591 208 -237 385 C ATOM 2374 N ASN A1002 15.907 -12.431 -31.775 1.00 57.38 N ANISOU 2374 N ASN A1002 9795 6755 5251 756 1361 483 N ATOM 2375 CA ASN A1002 16.350 -11.529 -32.823 1.00 54.64 C ANISOU 2375 CA ASN A1002 9211 6695 4853 633 1029 327 C ATOM 2376 C ASN A1002 15.702 -10.157 -32.665 1.00 52.81 C ANISOU 2376 C ASN A1002 8838 6627 4600 496 860 284 C ATOM 2377 O ASN A1002 16.305 -9.149 -32.999 1.00 51.99 O ANISOU 2377 O ASN A1002 8612 6740 4399 490 645 264 O ATOM 2378 CB ASN A1002 16.024 -12.119 -34.195 1.00 54.97 C ANISOU 2378 CB ASN A1002 9124 6670 5089 457 1049 103 C ATOM 2379 CG ASN A1002 16.777 -13.413 -34.480 1.00 56.26 C ANISOU 2379 CG ASN A1002 9402 6667 5307 587 1199 106 C ATOM 2380 OD1 ASN A1002 17.805 -13.706 -33.869 1.00 57.20 O ANISOU 2380 OD1 ASN A1002 9679 6809 5244 855 1204 291 O ATOM 2381 ND2 ASN A1002 16.260 -14.191 -35.417 1.00 57.08 N ANISOU 2381 ND2 ASN A1002 9397 6633 5656 431 1316 -149 N ATOM 2382 N ILE A1003 14.485 -10.124 -32.128 1.00 53.45 N ANISOU 2382 N ILE A1003 8937 6573 4797 387 1004 261 N ATOM 2383 CA ILE A1003 13.726 -8.878 -32.009 1.00 51.82 C ANISOU 2383 CA ILE A1003 8597 6502 4588 274 855 196 C ATOM 2384 C ILE A1003 14.278 -7.866 -30.987 1.00 51.17 C ANISOU 2384 C ILE A1003 8521 6586 4333 406 721 303 C ATOM 2385 O ILE A1003 14.171 -6.661 -31.212 1.00 50.73 O ANISOU 2385 O ILE A1003 8335 6653 4284 331 553 241 O ATOM 2386 CB ILE A1003 12.221 -9.150 -31.739 1.00 53.08 C ANISOU 2386 CB ILE A1003 8724 6507 4935 112 1048 68 C ATOM 2387 CG1 ILE A1003 11.395 -7.870 -31.887 1.00 52.58 C ANISOU 2387 CG1 ILE A1003 8497 6621 4861 28 854 -44 C ATOM 2388 CG2 ILE A1003 11.984 -9.709 -30.349 1.00 54.72 C ANISOU 2388 CG2 ILE A1003 9130 6530 5131 207 1333 243 C ATOM 2389 CD1 ILE A1003 11.551 -7.175 -33.223 1.00 51.66 C ANISOU 2389 CD1 ILE A1003 8238 6699 4692 32 622 -140 C ATOM 2390 N PHE A1004 14.851 -8.326 -29.874 1.00 52.04 N ANISOU 2390 N PHE A1004 8770 6715 4287 639 812 435 N ATOM 2391 CA PHE A1004 15.402 -7.394 -28.883 1.00 51.86 C ANISOU 2391 CA PHE A1004 8674 6942 4086 802 660 420 C ATOM 2392 C PHE A1004 16.484 -6.527 -29.509 1.00 50.84 C ANISOU 2392 C PHE A1004 8354 6998 3964 758 441 278 C ATOM 2393 O PHE A1004 16.415 -5.313 -29.420 1.00 49.66 O ANISOU 2393 O PHE A1004 8048 6931 3889 652 330 159 O ATOM 2394 CB PHE A1004 15.966 -8.124 -27.663 1.00 54.64 C ANISOU 2394 CB PHE A1004 9193 7394 4172 1187 773 561 C ATOM 2395 CG PHE A1004 16.606 -7.209 -26.631 1.00 56.34 C ANISOU 2395 CG PHE A1004 9254 7984 4168 1417 579 429 C ATOM 2396 CD1 PHE A1004 17.955 -6.867 -26.713 1.00 56.76 C ANISOU 2396 CD1 PHE A1004 9124 8328 4113 1561 378 236 C ATOM 2397 CD2 PHE A1004 15.865 -6.713 -25.554 1.00 57.97 C ANISOU 2397 CD2 PHE A1004 9452 8289 4285 1497 609 429 C ATOM 2398 CE1 PHE A1004 18.541 -6.046 -25.760 1.00 58.12 C ANISOU 2398 CE1 PHE A1004 9070 8888 4123 1767 206 -15 C ATOM 2399 CE2 PHE A1004 16.449 -5.888 -24.599 1.00 58.55 C ANISOU 2399 CE2 PHE A1004 9327 8759 4161 1729 419 219 C ATOM 2400 CZ PHE A1004 17.786 -5.554 -24.705 1.00 59.18 C ANISOU 2400 CZ PHE A1004 9186 9134 4164 1861 216 -34 C ATOM 2401 N GLU A1005 17.472 -7.154 -30.144 1.00 51.84 N ANISOU 2401 N GLU A1005 8493 7155 4046 830 425 280 N ATOM 2402 CA GLU A1005 18.577 -6.421 -30.772 1.00 52.31 C ANISOU 2402 CA GLU A1005 8361 7373 4139 769 290 130 C ATOM 2403 C GLU A1005 18.092 -5.417 -31.799 1.00 50.36 C ANISOU 2403 C GLU A1005 8026 7021 4087 499 277 112 C ATOM 2404 O GLU A1005 18.572 -4.283 -31.851 1.00 51.14 O ANISOU 2404 O GLU A1005 7970 7171 4287 409 249 -1 O ATOM 2405 CB GLU A1005 19.519 -7.366 -31.498 1.00 54.29 C ANISOU 2405 CB GLU A1005 8647 7651 4327 860 299 142 C ATOM 2406 CG GLU A1005 20.384 -8.235 -30.613 1.00 58.16 C ANISOU 2406 CG GLU A1005 9210 8307 4579 1228 296 146 C ATOM 2407 CD GLU A1005 21.567 -8.794 -31.385 1.00 61.04 C ANISOU 2407 CD GLU A1005 9518 8776 4897 1307 249 67 C ATOM 2408 OE1 GLU A1005 21.767 -10.040 -31.391 1.00 62.96 O ANISOU 2408 OE1 GLU A1005 9950 8935 5037 1531 338 189 O ATOM 2409 OE2 GLU A1005 22.282 -7.971 -32.013 1.00 61.55 O ANISOU 2409 OE2 GLU A1005 9353 8976 5057 1138 165 -117 O ATOM 2410 N MET A1006 17.154 -5.856 -32.628 1.00 48.17 N ANISOU 2410 N MET A1006 7837 6599 3864 403 329 198 N ATOM 2411 CA MET A1006 16.655 -5.043 -33.717 1.00 47.15 C ANISOU 2411 CA MET A1006 7658 6435 3819 278 316 212 C ATOM 2412 C MET A1006 15.920 -3.798 -33.214 1.00 46.18 C ANISOU 2412 C MET A1006 7494 6270 3780 221 299 201 C ATOM 2413 O MET A1006 16.147 -2.696 -33.704 1.00 46.73 O ANISOU 2413 O MET A1006 7518 6303 3932 177 329 223 O ATOM 2414 CB MET A1006 15.758 -5.884 -34.611 1.00 47.59 C ANISOU 2414 CB MET A1006 7753 6456 3872 262 340 197 C ATOM 2415 CG MET A1006 16.545 -6.911 -35.396 1.00 48.80 C ANISOU 2415 CG MET A1006 7914 6646 3980 308 358 175 C ATOM 2416 SD MET A1006 15.543 -7.888 -36.524 1.00 51.57 S ANISOU 2416 SD MET A1006 8213 7007 4373 284 385 10 S ATOM 2417 CE MET A1006 14.609 -6.601 -37.361 1.00 52.07 C ANISOU 2417 CE MET A1006 8186 7240 4358 325 287 -1 C ATOM 2418 N LEU A1007 15.059 -3.971 -32.222 1.00 44.91 N ANISOU 2418 N LEU A1007 7364 6087 3613 234 298 176 N ATOM 2419 CA LEU A1007 14.340 -2.845 -31.649 1.00 44.60 C ANISOU 2419 CA LEU A1007 7272 6025 3648 196 268 135 C ATOM 2420 C LEU A1007 15.238 -1.989 -30.748 1.00 45.75 C ANISOU 2420 C LEU A1007 7300 6235 3845 211 242 20 C ATOM 2421 O LEU A1007 15.111 -0.763 -30.721 1.00 47.10 O ANISOU 2421 O LEU A1007 7393 6334 4169 143 254 -43 O ATOM 2422 CB LEU A1007 13.095 -3.330 -30.904 1.00 44.28 C ANISOU 2422 CB LEU A1007 7274 5963 3586 195 300 113 C ATOM 2423 CG LEU A1007 11.955 -3.774 -31.833 1.00 44.30 C ANISOU 2423 CG LEU A1007 7274 5932 3624 138 324 67 C ATOM 2424 CD1 LEU A1007 10.826 -4.405 -31.041 1.00 44.76 C ANISOU 2424 CD1 LEU A1007 7339 5939 3726 84 438 -12 C ATOM 2425 CD2 LEU A1007 11.422 -2.613 -32.666 1.00 44.31 C ANISOU 2425 CD2 LEU A1007 7218 5975 3641 169 235 54 C ATOM 2426 N ARG A1008 16.160 -2.619 -30.031 1.00 46.20 N ANISOU 2426 N ARG A1008 7325 6442 3785 331 218 -47 N ATOM 2427 CA ARG A1008 17.152 -1.876 -29.265 1.00 47.31 C ANISOU 2427 CA ARG A1008 7262 6747 3965 376 169 -288 C ATOM 2428 C ARG A1008 17.833 -0.836 -30.155 1.00 47.52 C ANISOU 2428 C ARG A1008 7160 6647 4247 188 253 -381 C ATOM 2429 O ARG A1008 18.108 0.273 -29.709 1.00 47.98 O ANISOU 2429 O ARG A1008 7030 6686 4512 102 292 -612 O ATOM 2430 CB ARG A1008 18.177 -2.836 -28.662 1.00 49.33 C ANISOU 2430 CB ARG A1008 7493 7257 3990 620 115 -362 C ATOM 2431 CG ARG A1008 19.277 -2.198 -27.831 1.00 52.68 C ANISOU 2431 CG ARG A1008 7620 7985 4409 733 26 -738 C ATOM 2432 CD ARG A1008 18.733 -1.459 -26.614 1.00 54.81 C ANISOU 2432 CD ARG A1008 7761 8401 4663 812 -37 -926 C ATOM 2433 NE ARG A1008 19.793 -0.759 -25.887 1.00 58.36 N ANISOU 2433 NE ARG A1008 7830 9188 5154 906 -129 -1422 N ATOM 2434 CZ ARG A1008 20.389 0.354 -26.314 1.00 60.04 C ANISOU 2434 CZ ARG A1008 7766 9293 5752 626 -52 -1749 C ATOM 2435 NH1 ARG A1008 20.033 0.931 -27.461 1.00 58.68 N ANISOU 2435 NH1 ARG A1008 7717 8679 5899 296 130 -1541 N ATOM 2436 NH2 ARG A1008 21.353 0.903 -25.584 1.00 63.86 N ANISOU 2436 NH2 ARG A1008 7833 10124 6306 706 -122 -2316 N ATOM 2437 N ILE A1009 18.090 -1.196 -31.412 1.00 47.30 N ANISOU 2437 N ILE A1009 7231 6516 4223 130 326 -214 N ATOM 2438 CA ILE A1009 18.644 -0.258 -32.388 1.00 48.73 C ANISOU 2438 CA ILE A1009 7361 6529 4625 -17 499 -205 C ATOM 2439 C ILE A1009 17.597 0.729 -32.910 1.00 49.20 C ANISOU 2439 C ILE A1009 7541 6345 4805 -59 605 -28 C ATOM 2440 O ILE A1009 17.832 1.942 -32.917 1.00 50.84 O ANISOU 2440 O ILE A1009 7680 6353 5282 -164 789 -98 O ATOM 2441 CB ILE A1009 19.272 -0.991 -33.592 1.00 48.44 C ANISOU 2441 CB ILE A1009 7398 6517 4488 -3 553 -65 C ATOM 2442 CG1 ILE A1009 20.517 -1.746 -33.159 1.00 49.18 C ANISOU 2442 CG1 ILE A1009 7345 6842 4500 57 480 -276 C ATOM 2443 CG2 ILE A1009 19.650 -0.011 -34.701 1.00 50.50 C ANISOU 2443 CG2 ILE A1009 7676 6575 4935 -111 810 43 C ATOM 2444 CD1 ILE A1009 21.582 -0.868 -32.540 1.00 51.63 C ANISOU 2444 CD1 ILE A1009 7358 7229 5030 -39 555 -643 C ATOM 2445 N ASP A1010 16.459 0.208 -33.360 1.00 47.79 N ANISOU 2445 N ASP A1010 7527 6184 4447 41 516 162 N ATOM 2446 CA ASP A1010 15.478 1.024 -34.066 1.00 48.95 C ANISOU 2446 CA ASP A1010 7793 6189 4614 110 588 333 C ATOM 2447 C ASP A1010 14.704 1.939 -33.137 1.00 50.68 C ANISOU 2447 C ASP A1010 7973 6312 4970 93 568 239 C ATOM 2448 O ASP A1010 14.483 3.100 -33.459 1.00 53.83 O ANISOU 2448 O ASP A1010 8428 6496 5527 120 725 321 O ATOM 2449 CB ASP A1010 14.510 0.147 -34.852 1.00 47.53 C ANISOU 2449 CB ASP A1010 7710 6158 4191 251 470 434 C ATOM 2450 CG ASP A1010 15.180 -0.565 -36.007 1.00 47.58 C ANISOU 2450 CG ASP A1010 7751 6261 4064 308 507 523 C ATOM 2451 OD1 ASP A1010 16.120 0.006 -36.606 1.00 48.75 O ANISOU 2451 OD1 ASP A1010 7923 6316 4282 294 687 628 O ATOM 2452 OD2 ASP A1010 14.759 -1.698 -36.325 1.00 46.62 O ANISOU 2452 OD2 ASP A1010 7619 6297 3797 355 392 459 O ATOM 2453 N GLU A1011 14.285 1.422 -31.993 1.00 50.79 N ANISOU 2453 N GLU A1011 7910 6468 4918 78 409 85 N ATOM 2454 CA GLU A1011 13.579 2.237 -31.016 1.00 51.97 C ANISOU 2454 CA GLU A1011 7990 6579 5176 69 372 -43 C ATOM 2455 C GLU A1011 14.561 2.960 -30.095 1.00 54.15 C ANISOU 2455 C GLU A1011 8064 6839 5669 -27 425 -311 C ATOM 2456 O GLU A1011 14.254 4.038 -29.592 1.00 57.36 O ANISOU 2456 O GLU A1011 8387 7122 6286 -65 475 -451 O ATOM 2457 CB GLU A1011 12.593 1.385 -30.213 1.00 50.62 C ANISOU 2457 CB GLU A1011 7826 6582 4823 118 230 -86 C ATOM 2458 CG GLU A1011 11.414 0.861 -31.034 1.00 50.53 C ANISOU 2458 CG GLU A1011 7913 6598 4688 179 196 19 C ATOM 2459 CD GLU A1011 10.288 1.874 -31.228 1.00 52.46 C ANISOU 2459 CD GLU A1011 8163 6791 4977 263 172 11 C ATOM 2460 OE1 GLU A1011 10.457 3.067 -30.875 1.00 54.62 O ANISOU 2460 OE1 GLU A1011 8413 6919 5420 263 224 -16 O ATOM 2461 OE2 GLU A1011 9.213 1.474 -31.733 1.00 52.30 O ANISOU 2461 OE2 GLU A1011 8145 6884 4839 345 109 -15 O ATOM 2462 N GLY A1012 15.739 2.380 -29.880 1.00 54.83 N ANISOU 2462 N GLY A1012 8037 7078 5716 -48 411 -442 N ATOM 2463 CA GLY A1012 16.730 2.967 -28.971 1.00 56.81 C ANISOU 2463 CA GLY A1012 8002 7433 6149 -104 428 -832 C ATOM 2464 C GLY A1012 16.352 2.760 -27.515 1.00 56.79 C ANISOU 2464 C GLY A1012 7875 7727 5974 42 240 -1044 C ATOM 2465 O GLY A1012 15.418 2.018 -27.211 1.00 55.52 O ANISOU 2465 O GLY A1012 7883 7652 5558 163 143 -841 O ATOM 2466 N LEU A1013 17.079 3.413 -26.611 1.00 58.89 N ANISOU 2466 N LEU A1013 7821 8168 6385 41 217 -1490 N ATOM 2467 CA LEU A1013 16.775 3.343 -25.180 1.00 59.36 C ANISOU 2467 CA LEU A1013 7728 8588 6238 250 38 -1734 C ATOM 2468 C LEU A1013 17.005 4.678 -24.504 1.00 61.24 C ANISOU 2468 C LEU A1013 7611 8833 6821 147 72 -2242 C ATOM 2469 O LEU A1013 18.113 5.203 -24.513 1.00 63.11 O ANISOU 2469 O LEU A1013 7535 9110 7332 35 156 -2667 O ATOM 2470 CB LEU A1013 17.628 2.279 -24.485 1.00 60.72 C ANISOU 2470 CB LEU A1013 7817 9226 6026 553 -106 -1851 C ATOM 2471 CG LEU A1013 17.362 2.070 -22.985 1.00 62.17 C ANISOU 2471 CG LEU A1013 7886 9867 5867 903 -270 -2040 C ATOM 2472 CD1 LEU A1013 16.062 1.320 -22.753 1.00 60.29 C ANISOU 2472 CD1 LEU A1013 8002 9543 5360 1013 -243 -1580 C ATOM 2473 CD2 LEU A1013 18.509 1.324 -22.321 1.00 64.86 C ANISOU 2473 CD2 LEU A1013 8065 10730 5846 1289 -400 -2273 C ATOM 2474 N ARG A1014 15.950 5.212 -23.902 1.00 61.26 N ANISOU 2474 N ARG A1014 7629 8803 6843 174 23 -2255 N ATOM 2475 CA ARG A1014 16.045 6.447 -23.149 1.00 64.26 C ANISOU 2475 CA ARG A1014 7657 9201 7555 98 45 -2779 C ATOM 2476 C ARG A1014 15.291 6.301 -21.833 1.00 63.81 C ANISOU 2476 C ARG A1014 7520 9553 7173 362 -169 -2910 C ATOM 2477 O ARG A1014 14.321 5.551 -21.741 1.00 61.01 O ANISOU 2477 O ARG A1014 7460 9240 6478 496 -233 -2493 O ATOM 2478 CB ARG A1014 15.535 7.618 -23.987 1.00 65.28 C ANISOU 2478 CB ARG A1014 7896 8730 8176 -173 301 -2667 C ATOM 2479 CG ARG A1014 16.560 8.108 -24.997 1.00 68.09 C ANISOU 2479 CG ARG A1014 8204 8711 8952 -423 609 -2724 C ATOM 2480 CD ARG A1014 16.036 9.273 -25.818 1.00 71.23 C ANISOU 2480 CD ARG A1014 8788 8474 9800 -599 943 -2525 C ATOM 2481 NE ARG A1014 17.056 9.798 -26.731 1.00 76.01 N ANISOU 2481 NE ARG A1014 9360 8678 10841 -835 1344 -2567 N ATOM 2482 CZ ARG A1014 17.932 10.768 -26.448 1.00 81.61 C ANISOU 2482 CZ ARG A1014 9702 9175 12131 -1083 1642 -3129 C ATOM 2483 NH1 ARG A1014 17.950 11.368 -25.257 1.00 84.93 N ANISOU 2483 NH1 ARG A1014 9712 9790 12767 -1111 1540 -3763 N ATOM 2484 NH2 ARG A1014 18.810 11.146 -27.374 1.00 84.45 N ANISOU 2484 NH2 ARG A1014 10075 9127 12882 -1312 2081 -3099 N ATOM 2485 N LEU A1015 15.774 6.992 -20.808 1.00 66.51 N ANISOU 2485 N LEU A1015 7425 10220 7624 443 -254 -3538 N ATOM 2486 CA LEU A1015 15.237 6.847 -19.466 1.00 68.05 C ANISOU 2486 CA LEU A1015 7491 10921 7442 770 -462 -3724 C ATOM 2487 C LEU A1015 14.335 8.019 -19.070 1.00 69.89 C ANISOU 2487 C LEU A1015 7597 10965 7993 638 -438 -3952 C ATOM 2488 O LEU A1015 13.432 7.860 -18.250 1.00 70.38 O ANISOU 2488 O LEU A1015 7709 11287 7744 850 -560 -3881 O ATOM 2489 CB LEU A1015 16.383 6.675 -18.471 1.00 71.33 C ANISOU 2489 CB LEU A1015 7467 12016 7619 1092 -639 -4327 C ATOM 2490 CG LEU A1015 17.333 5.501 -18.740 1.00 70.37 C ANISOU 2490 CG LEU A1015 7448 12158 7129 1319 -689 -4149 C ATOM 2491 CD1 LEU A1015 18.563 5.600 -17.853 1.00 75.13 C ANISOU 2491 CD1 LEU A1015 7510 13462 7575 1643 -871 -4905 C ATOM 2492 CD2 LEU A1015 16.646 4.160 -18.542 1.00 67.83 C ANISOU 2492 CD2 LEU A1015 7600 11961 6210 1648 -720 -3479 C ATOM 2493 N LYS A1016 14.590 9.196 -19.635 1.00 72.20 N ANISOU 2493 N LYS A1016 7732 10784 8915 305 -237 -4225 N ATOM 2494 CA LYS A1016 13.644 10.305 -19.545 1.00 72.99 C ANISOU 2494 CA LYS A1016 7825 10534 9374 167 -150 -4310 C ATOM 2495 C LYS A1016 12.624 10.184 -20.679 1.00 69.04 C ANISOU 2495 C LYS A1016 7835 9513 8882 61 -22 -3603 C ATOM 2496 O LYS A1016 12.862 9.502 -21.683 1.00 65.66 O ANISOU 2496 O LYS A1016 7694 8903 8351 6 60 -3160 O ATOM 2497 CB LYS A1016 14.359 11.659 -19.626 1.00 77.61 C ANISOU 2497 CB LYS A1016 8032 10770 10684 -115 94 -4924 C ATOM 2498 CG LYS A1016 15.259 11.956 -18.443 1.00 82.80 C ANISOU 2498 CG LYS A1016 8059 12002 11397 -7 -49 -5816 C ATOM 2499 CD LYS A1016 16.206 13.111 -18.730 0.00 88.13 C ANISOU 2499 CD LYS A1016 8327 12270 12887 -374 288 -6474 C ATOM 2500 CE LYS A1016 17.192 13.322 -17.590 0.00 93.13 C ANISOU 2500 CE LYS A1016 8232 13587 13566 -250 116 -7503 C ATOM 2501 NZ LYS A1016 18.443 13.982 -18.056 0.00 97.75 N ANISOU 2501 NZ LYS A1016 8406 13866 14868 -627 470 -8129 N ATOM 2502 N ILE A1017 11.492 10.856 -20.508 1.00 68.27 N ANISOU 2502 N ILE A1017 7813 9235 8890 70 -25 -3554 N ATOM 2503 CA ILE A1017 10.451 10.882 -21.523 1.00 65.26 C ANISOU 2503 CA ILE A1017 7844 8449 8503 47 65 -3000 C ATOM 2504 C ILE A1017 10.954 11.676 -22.718 1.00 66.44 C ANISOU 2504 C ILE A1017 8130 7980 9134 -136 397 -2867 C ATOM 2505 O ILE A1017 11.569 12.727 -22.546 1.00 69.55 O ANISOU 2505 O ILE A1017 8284 8095 10047 -291 615 -3279 O ATOM 2506 CB ILE A1017 9.159 11.535 -20.982 1.00 65.43 C ANISOU 2506 CB ILE A1017 7857 8463 8540 142 -20 -3073 C ATOM 2507 CG1 ILE A1017 8.530 10.641 -19.910 1.00 63.61 C ANISOU 2507 CG1 ILE A1017 7564 8817 7787 336 -275 -3090 C ATOM 2508 CG2 ILE A1017 8.172 11.801 -22.115 1.00 64.85 C ANISOU 2508 CG2 ILE A1017 8149 7976 8513 173 85 -2607 C ATOM 2509 CD1 ILE A1017 7.249 11.180 -19.315 1.00 63.97 C ANISOU 2509 CD1 ILE A1017 7569 8931 7805 428 -367 -3189 C ATOM 2510 N TYR A1018 10.703 11.161 -23.920 1.00 64.23 N ANISOU 2510 N TYR A1018 8221 7493 8690 -106 475 -2317 N ATOM 2511 CA TYR A1018 10.944 11.913 -25.151 1.00 66.11 C ANISOU 2511 CA TYR A1018 8688 7146 9282 -173 829 -2052 C ATOM 2512 C TYR A1018 9.688 11.960 -26.009 1.00 65.12 C ANISOU 2512 C TYR A1018 8933 6868 8942 53 814 -1567 C ATOM 2513 O TYR A1018 8.662 11.391 -25.645 1.00 62.38 O ANISOU 2513 O TYR A1018 8612 6859 8228 192 533 -1506 O ATOM 2514 CB TYR A1018 12.141 11.352 -25.939 1.00 66.01 C ANISOU 2514 CB TYR A1018 8722 7072 9286 -299 988 -1916 C ATOM 2515 CG TYR A1018 12.063 9.895 -26.375 1.00 62.99 C ANISOU 2515 CG TYR A1018 8516 7044 8372 -195 760 -1567 C ATOM 2516 CD1 TYR A1018 12.411 8.873 -25.502 1.00 61.73 C ANISOU 2516 CD1 TYR A1018 8174 7382 7896 -168 497 -1758 C ATOM 2517 CD2 TYR A1018 11.701 9.544 -27.679 1.00 62.08 C ANISOU 2517 CD2 TYR A1018 8744 6766 8077 -88 841 -1068 C ATOM 2518 CE1 TYR A1018 12.370 7.546 -25.892 1.00 59.34 C ANISOU 2518 CE1 TYR A1018 8046 7315 7183 -84 362 -1451 C ATOM 2519 CE2 TYR A1018 11.659 8.213 -28.083 1.00 59.39 C ANISOU 2519 CE2 TYR A1018 8517 6726 7323 -22 659 -836 C ATOM 2520 CZ TYR A1018 11.993 7.212 -27.184 1.00 58.23 C ANISOU 2520 CZ TYR A1018 8204 6980 6939 -46 441 -1022 C ATOM 2521 OH TYR A1018 11.971 5.870 -27.548 1.00 54.94 O ANISOU 2521 OH TYR A1018 7913 6785 6174 11 323 -801 O ATOM 2522 N LYS A1019 9.771 12.681 -27.122 1.00 68.27 N ANISOU 2522 N LYS A1019 9598 6771 9570 120 1149 -1257 N ATOM 2523 CA LYS A1019 8.737 12.669 -28.147 1.00 69.14 C ANISOU 2523 CA LYS A1019 10063 6813 9393 440 1139 -786 C ATOM 2524 C LYS A1019 9.235 11.843 -29.337 1.00 69.69 C ANISOU 2524 C LYS A1019 10345 6933 9199 494 1203 -403 C ATOM 2525 O LYS A1019 10.284 12.151 -29.901 1.00 72.07 O ANISOU 2525 O LYS A1019 10709 6908 9766 374 1543 -309 O ATOM 2526 CB LYS A1019 8.426 14.097 -28.587 1.00 73.10 C ANISOU 2526 CB LYS A1019 10769 6743 10261 615 1503 -649 C ATOM 2527 CG LYS A1019 7.862 14.966 -27.473 1.00 74.75 C ANISOU 2527 CG LYS A1019 10768 6879 10752 586 1444 -1049 C ATOM 2528 CD LYS A1019 7.833 16.444 -27.840 1.00 79.99 C ANISOU 2528 CD LYS A1019 11623 6841 11926 706 1919 -961 C ATOM 2529 CE LYS A1019 6.933 16.711 -29.032 1.00 81.84 C ANISOU 2529 CE LYS A1019 12320 6920 11854 1212 2023 -381 C ATOM 2530 NZ LYS A1019 6.602 18.157 -29.150 1.00 87.61 N ANISOU 2530 NZ LYS A1019 13260 7008 13018 1436 2440 -296 N ATOM 2531 N ASP A1020 8.505 10.792 -29.712 1.00 68.12 N ANISOU 2531 N ASP A1020 10222 7143 8515 655 908 -233 N ATOM 2532 CA ASP A1020 8.921 9.955 -30.847 1.00 69.01 C ANISOU 2532 CA ASP A1020 10498 7357 8363 727 938 70 C ATOM 2533 C ASP A1020 8.742 10.708 -32.163 1.00 73.64 C ANISOU 2533 C ASP A1020 11416 7674 8887 1088 1200 483 C ATOM 2534 O ASP A1020 8.319 11.863 -32.167 1.00 75.65 O ANISOU 2534 O ASP A1020 11801 7669 9271 1317 1341 559 O ATOM 2535 CB ASP A1020 8.259 8.565 -30.817 1.00 65.85 C ANISOU 2535 CB ASP A1020 10027 7457 7534 758 587 34 C ATOM 2536 CG ASP A1020 6.752 8.607 -31.043 1.00 66.69 C ANISOU 2536 CG ASP A1020 10176 7778 7383 1050 399 45 C ATOM 2537 OD1 ASP A1020 6.198 9.676 -31.386 1.00 68.95 O ANISOU 2537 OD1 ASP A1020 10601 7868 7729 1325 506 157 O ATOM 2538 OD2 ASP A1020 6.118 7.544 -30.866 1.00 65.14 O ANISOU 2538 OD2 ASP A1020 9862 7947 6940 1014 170 -87 O ATOM 2539 N THR A1021 9.065 10.037 -33.268 1.00 75.83 N ANISOU 2539 N THR A1021 11840 8034 8936 1189 1275 756 N ATOM 2540 CA THR A1021 9.009 10.620 -34.619 1.00 80.37 C ANISOU 2540 CA THR A1021 12757 8425 9354 1614 1557 1202 C ATOM 2541 C THR A1021 7.763 11.487 -34.817 1.00 83.38 C ANISOU 2541 C THR A1021 13315 8768 9597 2085 1547 1334 C ATOM 2542 O THR A1021 7.864 12.648 -35.209 1.00 87.70 O ANISOU 2542 O THR A1021 14133 8840 10348 2324 1958 1616 O ATOM 2543 CB THR A1021 8.978 9.493 -35.683 1.00 79.86 C ANISOU 2543 CB THR A1021 12743 8793 8806 1812 1380 1364 C ATOM 2544 OG1 THR A1021 9.958 8.487 -35.368 1.00 76.37 O ANISOU 2544 OG1 THR A1021 12104 8472 8437 1398 1292 1185 O ATOM 2545 CG2 THR A1021 9.225 10.058 -37.095 1.00 83.91 C ANISOU 2545 CG2 THR A1021 13612 9128 9141 2257 1747 1853 C ATOM 2546 N GLU A1022 6.598 10.910 -34.524 1.00 82.29 N ANISOU 2546 N GLU A1022 13016 9113 9135 2222 1113 1110 N ATOM 2547 CA GLU A1022 5.307 11.564 -34.758 1.00 84.67 C ANISOU 2547 CA GLU A1022 13426 9533 9210 2729 1014 1158 C ATOM 2548 C GLU A1022 5.072 12.729 -33.802 1.00 83.85 C ANISOU 2548 C GLU A1022 13319 9019 9519 2650 1155 1038 C ATOM 2549 O GLU A1022 4.313 13.641 -34.119 1.00 88.60 O ANISOU 2549 O GLU A1022 14122 9495 10044 3123 1250 1200 O ATOM 2550 CB GLU A1022 4.152 10.556 -34.630 1.00 84.31 C ANISOU 2550 CB GLU A1022 13115 10144 8775 2811 531 823 C ATOM 2551 CG GLU A1022 4.216 9.368 -35.591 1.00 85.52 C ANISOU 2551 CG GLU A1022 13209 10742 8540 2912 372 830 C ATOM 2552 CD GLU A1022 4.154 9.772 -37.061 0.00 91.89 C ANISOU 2552 CD GLU A1022 14305 11641 8965 3558 522 1211 C ATOM 2553 OE1 GLU A1022 3.363 10.686 -37.395 0.00 96.03 O ANISOU 2553 OE1 GLU A1022 15000 12176 9309 4110 561 1350 O ATOM 2554 OE2 GLU A1022 4.891 9.169 -37.883 0.00 92.42 O ANISOU 2554 OE2 GLU A1022 14436 11800 8877 3566 604 1378 O ATOM 2555 N GLY A1023 5.722 12.688 -32.639 1.00 78.86 N ANISOU 2555 N GLY A1023 12445 8219 9298 2106 1160 726 N ATOM 2556 CA GLY A1023 5.628 13.750 -31.631 1.00 77.88 C ANISOU 2556 CA GLY A1023 12236 7733 9620 1968 1287 500 C ATOM 2557 C GLY A1023 4.892 13.337 -30.369 1.00 72.40 C ANISOU 2557 C GLY A1023 11203 7427 8876 1764 885 48 C ATOM 2558 O GLY A1023 4.432 14.197 -29.628 1.00 73.38 O ANISOU 2558 O GLY A1023 11252 7385 9242 1785 901 -154 O ATOM 2559 N TYR A1024 4.793 12.028 -30.123 1.00 66.55 N ANISOU 2559 N TYR A1024 10270 7173 7842 1577 573 -99 N ATOM 2560 CA TYR A1024 4.058 11.481 -28.978 1.00 62.41 C ANISOU 2560 CA TYR A1024 9461 7033 7217 1409 259 -465 C ATOM 2561 C TYR A1024 4.995 11.060 -27.849 1.00 59.96 C ANISOU 2561 C TYR A1024 8921 6759 7101 992 245 -720 C ATOM 2562 O TYR A1024 6.056 10.483 -28.106 1.00 58.45 O ANISOU 2562 O TYR A1024 8742 6534 6929 815 333 -633 O ATOM 2563 CB TYR A1024 3.266 10.249 -29.397 1.00 59.46 C ANISOU 2563 CB TYR A1024 9025 7146 6419 1491 4 -485 C ATOM 2564 CG TYR A1024 2.180 10.480 -30.414 1.00 60.84 C ANISOU 2564 CG TYR A1024 9312 7503 6299 1962 -83 -385 C ATOM 2565 CD1 TYR A1024 1.241 11.475 -30.242 1.00 63.13 C ANISOU 2565 CD1 TYR A1024 9621 7760 6604 2270 -123 -462 C ATOM 2566 CD2 TYR A1024 2.063 9.659 -31.522 1.00 60.66 C ANISOU 2566 CD2 TYR A1024 9337 7757 5952 2143 -154 -273 C ATOM 2567 CE1 TYR A1024 0.229 11.669 -31.162 1.00 65.82 C ANISOU 2567 CE1 TYR A1024 10038 8363 6606 2796 -238 -414 C ATOM 2568 CE2 TYR A1024 1.055 9.839 -32.447 1.00 63.07 C ANISOU 2568 CE2 TYR A1024 9683 8356 5922 2654 -275 -268 C ATOM 2569 CZ TYR A1024 0.139 10.844 -32.260 1.00 65.83 C ANISOU 2569 CZ TYR A1024 10059 8700 6253 3001 -324 -334 C ATOM 2570 OH TYR A1024 -0.867 11.028 -33.178 1.00 69.41 O ANISOU 2570 OH TYR A1024 10531 9528 6310 3601 -472 -366 O ATOM 2571 N TYR A1025 4.576 11.299 -26.605 1.00 58.97 N ANISOU 2571 N TYR A1025 8573 6773 7060 892 116 -1050 N ATOM 2572 CA TYR A1025 5.435 11.051 -25.445 1.00 57.75 C ANISOU 2572 CA TYR A1025 8176 6732 7034 619 91 -1339 C ATOM 2573 C TYR A1025 5.706 9.560 -25.230 1.00 55.29 C ANISOU 2573 C TYR A1025 7821 6789 6397 504 -38 -1290 C ATOM 2574 O TYR A1025 4.790 8.769 -25.035 1.00 53.23 O ANISOU 2574 O TYR A1025 7547 6817 5860 545 -174 -1280 O ATOM 2575 CB TYR A1025 4.855 11.688 -24.177 1.00 58.25 C ANISOU 2575 CB TYR A1025 8006 6921 7206 617 -18 -1711 C ATOM 2576 CG TYR A1025 4.743 13.203 -24.240 1.00 61.52 C ANISOU 2576 CG TYR A1025 8436 6903 8034 704 156 -1824 C ATOM 2577 CD1 TYR A1025 5.829 13.997 -24.628 1.00 63.97 C ANISOU 2577 CD1 TYR A1025 8785 6735 8786 593 473 -1832 C ATOM 2578 CD2 TYR A1025 3.559 13.846 -23.898 1.00 62.48 C ANISOU 2578 CD2 TYR A1025 8529 7062 8148 891 53 -1944 C ATOM 2579 CE1 TYR A1025 5.728 15.377 -24.693 1.00 67.29 C ANISOU 2579 CE1 TYR A1025 9248 6657 9658 663 732 -1925 C ATOM 2580 CE2 TYR A1025 3.453 15.224 -23.958 1.00 65.96 C ANISOU 2580 CE2 TYR A1025 9016 7054 8992 1002 251 -2032 C ATOM 2581 CZ TYR A1025 4.539 15.983 -24.355 1.00 68.76 C ANISOU 2581 CZ TYR A1025 9440 6871 9814 885 613 -2009 C ATOM 2582 OH TYR A1025 4.425 17.354 -24.410 1.00 74.18 O ANISOU 2582 OH TYR A1025 10197 7016 10972 987 902 -2090 O ATOM 2583 N THR A1026 6.986 9.206 -25.252 1.00 56.09 N ANISOU 2583 N THR A1026 7890 6849 6570 361 47 -1287 N ATOM 2584 CA THR A1026 7.450 7.818 -25.230 1.00 54.90 C ANISOU 2584 CA THR A1026 7759 6960 6139 299 -17 -1181 C ATOM 2585 C THR A1026 8.568 7.670 -24.198 1.00 55.60 C ANISOU 2585 C THR A1026 7634 7228 6263 221 -35 -1448 C ATOM 2586 O THR A1026 9.158 8.663 -23.767 1.00 58.47 O ANISOU 2586 O THR A1026 7808 7476 6930 164 28 -1746 O ATOM 2587 CB THR A1026 7.984 7.444 -26.628 1.00 54.88 C ANISOU 2587 CB THR A1026 7959 6774 6116 299 94 -874 C ATOM 2588 OG1 THR A1026 6.924 7.569 -27.584 1.00 56.01 O ANISOU 2588 OG1 THR A1026 8265 6866 6149 470 77 -680 O ATOM 2589 CG2 THR A1026 8.537 6.027 -26.683 1.00 52.76 C ANISOU 2589 CG2 THR A1026 7717 6721 5606 239 49 -777 C ATOM 2590 N ILE A1027 8.854 6.441 -23.785 1.00 54.08 N ANISOU 2590 N ILE A1027 7450 7330 5765 254 -102 -1383 N ATOM 2591 CA ILE A1027 9.969 6.203 -22.882 1.00 55.63 C ANISOU 2591 CA ILE A1027 7452 7791 5893 297 -142 -1629 C ATOM 2592 C ILE A1027 10.542 4.810 -23.066 1.00 54.68 C ANISOU 2592 C ILE A1027 7467 7831 5475 364 -137 -1402 C ATOM 2593 O ILE A1027 9.828 3.890 -23.458 1.00 53.40 O ANISOU 2593 O ILE A1027 7515 7642 5131 372 -102 -1112 O ATOM 2594 CB ILE A1027 9.528 6.372 -21.415 1.00 57.59 C ANISOU 2594 CB ILE A1027 7503 8396 5981 446 -256 -1908 C ATOM 2595 CG1 ILE A1027 10.703 6.854 -20.544 1.00 60.66 C ANISOU 2595 CG1 ILE A1027 7552 9052 6442 523 -320 -2378 C ATOM 2596 CG2 ILE A1027 8.917 5.077 -20.880 1.00 56.32 C ANISOU 2596 CG2 ILE A1027 7501 8503 5394 597 -258 -1662 C ATOM 2597 CD1 ILE A1027 10.294 7.344 -19.168 1.00 62.52 C ANISOU 2597 CD1 ILE A1027 7528 9657 6569 696 -443 -2753 C ATOM 2598 N GLY A1028 11.827 4.657 -22.767 1.00 56.27 N ANISOU 2598 N GLY A1028 7519 8206 5652 420 -157 -1589 N ATOM 2599 CA GLY A1028 12.471 3.348 -22.818 1.00 56.47 C ANISOU 2599 CA GLY A1028 7669 8412 5374 554 -155 -1399 C ATOM 2600 C GLY A1028 12.688 2.869 -24.237 1.00 55.36 C ANISOU 2600 C GLY A1028 7736 7974 5325 401 -61 -1101 C ATOM 2601 O GLY A1028 13.180 3.621 -25.088 1.00 57.89 O ANISOU 2601 O GLY A1028 8009 8048 5936 237 9 -1150 O ATOM 2602 N ILE A1029 12.310 1.621 -24.500 1.00 53.58 N ANISOU 2602 N ILE A1029 7737 7754 4866 463 -17 -801 N ATOM 2603 CA ILE A1029 12.497 1.023 -25.821 1.00 50.85 C ANISOU 2603 CA ILE A1029 7557 7196 4566 354 51 -567 C ATOM 2604 C ILE A1029 11.214 1.137 -26.642 1.00 48.66 C ANISOU 2604 C ILE A1029 7396 6718 4372 244 85 -421 C ATOM 2605 O ILE A1029 10.489 0.166 -26.834 1.00 48.25 O ANISOU 2605 O ILE A1029 7462 6658 4211 241 142 -294 O ATOM 2606 CB ILE A1029 12.952 -0.443 -25.694 1.00 50.95 C ANISOU 2606 CB ILE A1029 7713 7321 4325 497 102 -401 C ATOM 2607 CG1 ILE A1029 14.207 -0.510 -24.817 1.00 52.84 C ANISOU 2607 CG1 ILE A1029 7808 7865 4404 719 29 -591 C ATOM 2608 CG2 ILE A1029 13.223 -1.045 -27.068 1.00 50.18 C ANISOU 2608 CG2 ILE A1029 7738 7037 4290 385 157 -230 C ATOM 2609 CD1 ILE A1029 14.735 -1.906 -24.584 1.00 53.99 C ANISOU 2609 CD1 ILE A1029 8124 8134 4254 968 92 -406 C ATOM 2610 N GLY A1030 10.926 2.345 -27.105 1.00 48.03 N ANISOU 2610 N GLY A1030 7265 6482 4498 179 76 -478 N ATOM 2611 CA GLY A1030 9.753 2.576 -27.924 1.00 47.79 C ANISOU 2611 CA GLY A1030 7322 6344 4491 179 75 -378 C ATOM 2612 C GLY A1030 8.405 2.361 -27.260 1.00 48.55 C ANISOU 2612 C GLY A1030 7388 6555 4502 200 35 -456 C ATOM 2613 O GLY A1030 7.417 2.145 -27.956 1.00 49.78 O ANISOU 2613 O GLY A1030 7573 6716 4623 216 24 -438 O ATOM 2614 N HIS A1031 8.338 2.427 -25.930 1.00 49.89 N ANISOU 2614 N HIS A1031 7467 6863 4623 226 19 -585 N ATOM 2615 CA HIS A1031 7.050 2.325 -25.229 1.00 49.95 C ANISOU 2615 CA HIS A1031 7432 6979 4565 236 25 -670 C ATOM 2616 C HIS A1031 6.340 3.668 -25.244 1.00 49.95 C ANISOU 2616 C HIS A1031 7338 6928 4714 263 -67 -815 C ATOM 2617 O HIS A1031 6.688 4.578 -24.493 1.00 50.77 O ANISOU 2617 O HIS A1031 7327 7046 4915 294 -113 -972 O ATOM 2618 CB HIS A1031 7.211 1.848 -23.789 1.00 50.91 C ANISOU 2618 CB HIS A1031 7521 7307 4513 323 78 -712 C ATOM 2619 CG HIS A1031 5.915 1.732 -23.046 1.00 52.03 C ANISOU 2619 CG HIS A1031 7623 7551 4592 322 147 -785 C ATOM 2620 ND1 HIS A1031 5.223 0.546 -22.936 1.00 53.01 N ANISOU 2620 ND1 HIS A1031 7844 7656 4638 267 366 -682 N ATOM 2621 CD2 HIS A1031 5.187 2.655 -22.374 1.00 53.17 C ANISOU 2621 CD2 HIS A1031 7626 7800 4774 353 65 -978 C ATOM 2622 CE1 HIS A1031 4.123 0.743 -22.229 1.00 53.96 C ANISOU 2622 CE1 HIS A1031 7877 7877 4745 252 430 -806 C ATOM 2623 NE2 HIS A1031 4.081 2.013 -21.871 1.00 53.82 N ANISOU 2623 NE2 HIS A1031 7715 7962 4770 320 221 -982 N ATOM 2624 N LEU A1032 5.357 3.772 -26.130 1.00 49.78 N ANISOU 2624 N LEU A1032 7343 6865 4705 287 -93 -801 N ATOM 2625 CA LEU A1032 4.499 4.945 -26.252 1.00 50.42 C ANISOU 2625 CA LEU A1032 7368 6910 4877 395 -174 -913 C ATOM 2626 C LEU A1032 3.621 5.089 -25.011 1.00 51.59 C ANISOU 2626 C LEU A1032 7372 7233 4996 381 -206 -1123 C ATOM 2627 O LEU A1032 2.818 4.209 -24.710 1.00 52.20 O ANISOU 2627 O LEU A1032 7403 7468 4963 318 -150 -1187 O ATOM 2628 CB LEU A1032 3.621 4.778 -27.490 1.00 50.10 C ANISOU 2628 CB LEU A1032 7364 6920 4752 515 -218 -889 C ATOM 2629 CG LEU A1032 2.496 5.761 -27.761 1.00 51.49 C ANISOU 2629 CG LEU A1032 7490 7147 4926 731 -318 -1009 C ATOM 2630 CD1 LEU A1032 3.066 7.120 -28.109 1.00 53.02 C ANISOU 2630 CD1 LEU A1032 7817 7055 5271 894 -274 -856 C ATOM 2631 CD2 LEU A1032 1.632 5.231 -28.893 1.00 52.47 C ANISOU 2631 CD2 LEU A1032 7572 7487 4875 890 -389 -1086 C ATOM 2632 N LEU A1033 3.765 6.196 -24.294 1.00 52.84 N ANISOU 2632 N LEU A1033 7443 7352 5282 428 -257 -1261 N ATOM 2633 CA LEU A1033 2.993 6.397 -23.083 1.00 54.15 C ANISOU 2633 CA LEU A1033 7455 7723 5397 443 -296 -1478 C ATOM 2634 C LEU A1033 1.583 6.911 -23.361 1.00 55.95 C ANISOU 2634 C LEU A1033 7617 8001 5638 532 -372 -1612 C ATOM 2635 O LEU A1033 0.642 6.483 -22.703 1.00 56.81 O ANISOU 2635 O LEU A1033 7615 8330 5641 497 -354 -1757 O ATOM 2636 CB LEU A1033 3.730 7.340 -22.135 1.00 56.12 C ANISOU 2636 CB LEU A1033 7569 7972 5780 472 -338 -1672 C ATOM 2637 CG LEU A1033 5.048 6.795 -21.571 1.00 56.59 C ANISOU 2637 CG LEU A1033 7599 8145 5756 452 -302 -1668 C ATOM 2638 CD1 LEU A1033 5.859 7.904 -20.915 1.00 58.49 C ANISOU 2638 CD1 LEU A1033 7626 8380 6218 474 -349 -1991 C ATOM 2639 CD2 LEU A1033 4.804 5.668 -20.578 1.00 56.71 C ANISOU 2639 CD2 LEU A1033 7618 8485 5443 517 -247 -1620 C ATOM 2640 N THR A1034 1.426 7.813 -24.328 1.00 63.82 N ANISOU 2640 N THR A1034 7196 9674 7378 1059 613 -3671 N ATOM 2641 CA THR A1034 0.122 8.440 -24.578 1.00 66.48 C ANISOU 2641 CA THR A1034 7265 9946 8047 1168 662 -3981 C ATOM 2642 C THR A1034 0.148 9.298 -25.839 1.00 66.22 C ANISOU 2642 C THR A1034 7179 9441 8539 1262 353 -3952 C ATOM 2643 O THR A1034 1.197 9.826 -26.205 1.00 66.32 O ANISOU 2643 O THR A1034 7326 9206 8664 1270 104 -3853 O ATOM 2644 CB THR A1034 -0.305 9.315 -23.375 1.00 70.66 C ANISOU 2644 CB THR A1034 7634 10713 8497 1296 752 -4529 C ATOM 2645 OG1 THR A1034 -1.396 10.164 -23.741 1.00 72.91 O ANISOU 2645 OG1 THR A1034 7640 10837 9224 1450 709 -4873 O ATOM 2646 CG2 THR A1034 0.841 10.189 -22.904 1.00 71.56 C ANISOU 2646 CG2 THR A1034 7869 10733 8588 1368 512 -4705 C ATOM 2647 N LYS A1035 -1.006 9.438 -26.494 1.00 67.80 N ANISOU 2647 N LYS A1035 7179 9522 9060 1323 362 -4031 N ATOM 2648 CA LYS A1035 -1.132 10.300 -27.686 1.00 68.01 C ANISOU 2648 CA LYS A1035 7152 9101 9586 1421 47 -4004 C ATOM 2649 C LYS A1035 -1.483 11.756 -27.339 1.00 71.59 C ANISOU 2649 C LYS A1035 7421 9381 10397 1624 -130 -4483 C ATOM 2650 O LYS A1035 -1.445 12.635 -28.202 1.00 71.44 O ANISOU 2650 O LYS A1035 7385 8955 10801 1710 -437 -4467 O ATOM 2651 CB LYS A1035 -2.165 9.733 -28.671 1.00 67.14 C ANISOU 2651 CB LYS A1035 6928 8908 9672 1396 77 -3830 C ATOM 2652 CG LYS A1035 -1.671 8.547 -29.495 1.00 63.76 C ANISOU 2652 CG LYS A1035 6707 8461 9056 1221 107 -3330 C ATOM 2653 CD LYS A1035 -2.611 8.253 -30.660 1.00 63.51 C ANISOU 2653 CD LYS A1035 6570 8263 9297 1222 30 -3193 C ATOM 2654 CE LYS A1035 -2.461 6.842 -31.222 1.00 60.64 C ANISOU 2654 CE LYS A1035 6350 7984 8706 1047 153 -2798 C ATOM 2655 NZ LYS A1035 -1.080 6.560 -31.699 1.00 57.54 N ANISOU 2655 NZ LYS A1035 6238 7476 8145 960 42 -2466 N ATOM 2656 N SER A1036 -1.826 12.005 -26.080 1.00 75.45 N ANISOU 2656 N SER A1036 7779 10177 10712 1698 58 -4909 N ATOM 2657 CA SER A1036 -2.080 13.357 -25.589 1.00 79.75 C ANISOU 2657 CA SER A1036 8148 10586 11568 1904 -96 -5432 C ATOM 2658 C SER A1036 -0.877 14.278 -25.849 1.00 79.20 C ANISOU 2658 C SER A1036 8249 10151 11691 1926 -445 -5386 C ATOM 2659 O SER A1036 0.260 13.801 -25.952 1.00 78.12 O ANISOU 2659 O SER A1036 8355 10026 11298 1777 -477 -5041 O ATOM 2660 CB SER A1036 -2.378 13.299 -24.086 1.00 83.74 C ANISOU 2660 CB SER A1036 8544 11567 11705 1941 202 -5867 C ATOM 2661 OG SER A1036 -2.528 14.588 -23.519 1.00 88.41 O ANISOU 2661 OG SER A1036 8974 12050 12567 2148 55 -6426 O ATOM 2662 N PRO A1037 -1.124 15.595 -25.983 1.00 80.69 N ANISOU 2662 N PRO A1037 8297 9992 12369 2108 -719 -5730 N ATOM 2663 CA PRO A1037 -0.027 16.560 -26.036 1.00 80.67 C ANISOU 2663 CA PRO A1037 8425 9654 12570 2120 -1036 -5758 C ATOM 2664 C PRO A1037 0.417 17.026 -24.651 1.00 83.68 C ANISOU 2664 C PRO A1037 8786 10271 12734 2186 -981 -6229 C ATOM 2665 O PRO A1037 1.427 17.721 -24.542 1.00 84.13 O ANISOU 2665 O PRO A1037 8954 10102 12906 2170 -1224 -6268 O ATOM 2666 CB PRO A1037 -0.635 17.728 -26.814 1.00 82.48 C ANISOU 2666 CB PRO A1037 8504 9378 13456 2290 -1368 -5912 C ATOM 2667 CG PRO A1037 -2.083 17.682 -26.470 1.00 84.93 C ANISOU 2667 CG PRO A1037 8517 9880 13870 2456 -1188 -6293 C ATOM 2668 CD PRO A1037 -2.426 16.233 -26.256 1.00 83.07 C ANISOU 2668 CD PRO A1037 8306 10132 13124 2305 -788 -6058 C ATOM 2669 N SER A1038 -0.333 16.642 -23.616 1.00 86.07 N ANISOU 2669 N SER A1038 8945 11037 12720 2247 -662 -6582 N ATOM 2670 CA SER A1038 -0.088 17.077 -22.242 1.00 89.50 C ANISOU 2670 CA SER A1038 9343 11765 12898 2327 -582 -7094 C ATOM 2671 C SER A1038 1.069 16.320 -21.592 1.00 88.19 C ANISOU 2671 C SER A1038 9438 11914 12153 2149 -485 -6850 C ATOM 2672 O SER A1038 0.969 15.118 -21.351 1.00 86.38 O ANISOU 2672 O SER A1038 9299 12068 11451 2010 -192 -6564 O ATOM 2673 CB SER A1038 -1.356 16.881 -21.410 1.00 93.26 C ANISOU 2673 CB SER A1038 9563 12671 13198 2436 -238 -7537 C ATOM 2674 OG SER A1038 -1.187 17.369 -20.090 1.00 98.85 O ANISOU 2674 OG SER A1038 10227 13686 13643 2528 -157 -8083 O ATOM 2675 N LEU A1039 2.157 17.035 -21.297 1.00 89.80 N ANISOU 2675 N LEU A1039 9754 11939 12425 2155 -751 -6971 N ATOM 2676 CA LEU A1039 3.367 16.440 -20.703 1.00 88.41 C ANISOU 2676 CA LEU A1039 9813 12012 11765 2006 -736 -6762 C ATOM 2677 C LEU A1039 3.088 15.814 -19.337 1.00 90.65 C ANISOU 2677 C LEU A1039 10110 12919 11412 2001 -417 -7012 C ATOM 2678 O LEU A1039 3.745 14.846 -18.948 1.00 88.97 O ANISOU 2678 O LEU A1039 10096 13006 10701 1853 -303 -6693 O ATOM 2679 CB LEU A1039 4.487 17.484 -20.575 1.00 89.84 C ANISOU 2679 CB LEU A1039 10053 11874 12206 2030 -1104 -6944 C ATOM 2680 CG LEU A1039 5.889 16.941 -20.259 1.00 88.22 C ANISOU 2680 CG LEU A1039 10072 11807 11639 1870 -1177 -6653 C ATOM 2681 CD1 LEU A1039 6.503 16.287 -21.488 0.00 84.12 C ANISOU 2681 CD1 LEU A1039 9683 11043 11233 1702 -1234 -5997 C ATOM 2682 CD2 LEU A1039 6.806 18.037 -19.741 0.00 91.15 C ANISOU 2682 CD2 LEU A1039 10443 11979 12208 1917 -1501 -7018 C ATOM 2683 N ASN A1040 2.128 16.373 -18.606 1.00 94.24 N ANISOU 2683 N ASN A1040 10354 13571 11881 2163 -279 -7584 N ATOM 2684 CA ASN A1040 1.685 15.760 -17.363 1.00 96.68 C ANISOU 2684 CA ASN A1040 10658 14515 11560 2142 79 -7814 C ATOM 2685 C ASN A1040 0.969 14.439 -17.626 1.00 94.84 C ANISOU 2685 C ASN A1040 10437 14564 11032 1993 438 -7380 C ATOM 2686 O ASN A1040 1.320 13.420 -17.038 1.00 94.46 O ANISOU 2686 O ASN A1040 10576 14909 10404 1836 635 -7100 O ATOM 2687 CB ASN A1040 0.800 16.718 -16.563 1.00101.24 C ANISOU 2687 CB ASN A1040 10972 15246 12246 2358 161 -8575 C ATOM 2688 CG ASN A1040 1.601 17.802 -15.866 1.00103.82 C ANISOU 2688 CG ASN A1040 11332 15471 12641 2476 -133 -9064 C ATOM 2689 OD1 ASN A1040 2.830 17.757 -15.829 1.00101.19 O ANISOU 2689 OD1 ASN A1040 11221 15033 12191 2377 -367 -8834 O ATOM 2690 ND2 ASN A1040 0.906 18.782 -15.305 1.00108.67 N ANISOU 2690 ND2 ASN A1040 11707 16114 13468 2693 -130 -9770 N ATOM 2691 N ALA A1041 -0.005 14.449 -18.532 1.00 94.24 N ANISOU 2691 N ALA A1041 10168 14260 11377 2037 492 -7306 N ATOM 2692 CA ALA A1041 -0.761 13.237 -18.866 1.00 92.77 C ANISOU 2692 CA ALA A1041 9960 14293 10993 1893 811 -6920 C ATOM 2693 C ALA A1041 0.152 12.022 -19.071 1.00 89.19 C ANISOU 2693 C ALA A1041 9814 13918 10156 1669 835 -6280 C ATOM 2694 O ALA A1041 -0.196 10.902 -18.685 1.00 89.20 O ANISOU 2694 O ALA A1041 9874 14289 9726 1519 1145 -6034 O ATOM 2695 CB ALA A1041 -1.623 13.467 -20.101 1.00 91.17 C ANISOU 2695 CB ALA A1041 9556 13697 11386 1964 723 -6833 C ATOM 2696 N ALA A1042 1.315 12.248 -19.676 1.00 86.41 N ANISOU 2696 N ALA A1042 9643 13207 9981 1645 506 -6018 N ATOM 2697 CA ALA A1042 2.304 11.191 -19.854 1.00 83.24 C ANISOU 2697 CA ALA A1042 9512 12852 9261 1467 488 -5469 C ATOM 2698 C ALA A1042 2.834 10.720 -18.503 1.00 86.06 C ANISOU 2698 C ALA A1042 10031 13683 8982 1402 615 -5534 C ATOM 2699 O ALA A1042 2.722 9.541 -18.170 1.00 87.08 O ANISOU 2699 O ALA A1042 10282 14121 8683 1257 850 -5210 O ATOM 2700 CB ALA A1042 3.445 11.675 -20.735 1.00 80.28 C ANISOU 2700 CB ALA A1042 9249 12015 9236 1465 119 -5252 C ATOM 2701 N LYS A1043 3.387 11.648 -17.722 1.00 88.48 N ANISOU 2701 N LYS A1043 10344 14040 9235 1508 442 -5955 N ATOM 2702 CA LYS A1043 3.932 11.329 -16.397 1.00 90.51 C ANISOU 2702 CA LYS A1043 10763 14757 8868 1465 511 -6065 C ATOM 2703 C LYS A1043 2.946 10.513 -15.563 1.00 92.54 C ANISOU 2703 C LYS A1043 10999 15554 8608 1384 938 -6086 C ATOM 2704 O LYS A1043 3.330 9.557 -14.897 1.00 92.65 O ANISOU 2704 O LYS A1043 11224 15911 8066 1247 1056 -5795 O ATOM 2705 CB LYS A1043 4.333 12.608 -15.652 1.00 93.78 C ANISOU 2705 CB LYS A1043 11117 15165 9347 1622 291 -6665 C ATOM 2706 CG LYS A1043 5.614 13.243 -16.169 1.00 91.97 C ANISOU 2706 CG LYS A1043 10970 14499 9474 1639 -133 -6587 C ATOM 2707 CD LYS A1043 5.882 14.598 -15.527 1.00 96.19 C ANISOU 2707 CD LYS A1043 11408 14955 10184 1797 -369 -7222 C ATOM 2708 CE LYS A1043 7.333 15.021 -15.716 1.00 95.06 C ANISOU 2708 CE LYS A1043 11381 14509 10225 1761 -766 -7119 C ATOM 2709 NZ LYS A1043 7.523 16.495 -15.642 1.00 97.46 N ANISOU 2709 NZ LYS A1043 11543 14480 11006 1903 -1065 -7656 N ATOM 2710 N SER A1044 1.673 10.889 -15.623 1.00 94.68 N ANISOU 2710 N SER A1044 11005 15885 9081 1463 1162 -6416 N ATOM 2711 CA SER A1044 0.606 10.158 -14.943 1.00 97.83 C ANISOU 2711 CA SER A1044 11324 16785 9063 1367 1609 -6445 C ATOM 2712 C SER A1044 0.537 8.709 -15.420 1.00 94.49 C ANISOU 2712 C SER A1044 11046 16395 8460 1146 1777 -5773 C ATOM 2713 O SER A1044 0.443 7.786 -14.614 1.00 96.73 O ANISOU 2713 O SER A1044 11468 17111 8170 986 2033 -5565 O ATOM 2714 CB SER A1044 -0.741 10.859 -15.175 1.00100.34 C ANISOU 2714 CB SER A1044 11272 17066 9784 1506 1780 -6906 C ATOM 2715 OG SER A1044 -1.825 10.103 -14.663 1.00103.53 O ANISOU 2715 OG SER A1044 11554 17931 9851 1386 2237 -6898 O ATOM 2716 N GLU A1045 0.592 8.521 -16.733 1.00 89.72 N ANISOU 2716 N GLU A1045 10418 15325 8345 1135 1618 -5438 N ATOM 2717 CA GLU A1045 0.479 7.198 -17.336 1.00 86.94 C ANISOU 2717 CA GLU A1045 10176 14934 7922 946 1745 -4846 C ATOM 2718 C GLU A1045 1.731 6.336 -17.127 1.00 85.25 C ANISOU 2718 C GLU A1045 10297 14747 7346 824 1604 -4381 C ATOM 2719 O GLU A1045 1.648 5.105 -17.127 1.00 83.34 O ANISOU 2719 O GLU A1045 10187 14626 6851 650 1766 -3936 O ATOM 2720 CB GLU A1045 0.187 7.354 -18.828 1.00 83.40 C ANISOU 2720 CB GLU A1045 9600 13984 8101 992 1587 -4687 C ATOM 2721 CG GLU A1045 -0.154 6.064 -19.554 1.00 81.34 C ANISOU 2721 CG GLU A1045 9395 13661 7847 817 1726 -4167 C ATOM 2722 CD GLU A1045 -1.345 5.347 -18.960 1.00 84.54 C ANISOU 2722 CD GLU A1045 9667 14460 7993 687 2141 -4184 C ATOM 2723 OE1 GLU A1045 -2.314 6.031 -18.553 1.00 87.47 O ANISOU 2723 OE1 GLU A1045 9769 15013 8453 777 2316 -4645 O ATOM 2724 OE2 GLU A1045 -1.307 4.097 -18.914 1.00 83.97 O ANISOU 2724 OE2 GLU A1045 9746 14501 7654 490 2290 -3738 O ATOM 2725 N LEU A1046 2.880 6.992 -16.961 1.00 85.66 N ANISOU 2725 N LEU A1046 10468 14663 7414 919 1287 -4494 N ATOM 2726 CA LEU A1046 4.159 6.318 -16.711 1.00 84.54 C ANISOU 2726 CA LEU A1046 10609 14540 6971 840 1102 -4122 C ATOM 2727 C LEU A1046 4.251 5.801 -15.274 1.00 89.76 C ANISOU 2727 C LEU A1046 11439 15734 6931 758 1262 -4136 C ATOM 2728 O LEU A1046 4.719 4.682 -15.043 1.00 89.33 O ANISOU 2728 O LEU A1046 11607 15794 6538 623 1278 -3679 O ATOM 2729 CB LEU A1046 5.325 7.274 -16.990 1.00 82.99 C ANISOU 2729 CB LEU A1046 10440 14031 7059 961 707 -4282 C ATOM 2730 CG LEU A1046 6.744 6.756 -16.719 1.00 82.08 C ANISOU 2730 CG LEU A1046 10566 13919 6699 912 466 -3979 C ATOM 2731 CD1 LEU A1046 7.072 5.575 -17.617 1.00 78.05 C ANISOU 2731 CD1 LEU A1046 10167 13204 6283 798 465 -3397 C ATOM 2732 CD2 LEU A1046 7.764 7.870 -16.900 1.00 81.81 C ANISOU 2732 CD2 LEU A1046 10497 13607 6979 1023 104 -4232 C ATOM 2733 N ASP A1047 3.824 6.626 -14.316 1.00 94.95 N ANISOU 2733 N ASP A1047 11996 16708 7369 845 1363 -4663 N ATOM 2734 CA ASP A1047 3.722 6.209 -12.912 1.00100.00 C ANISOU 2734 CA ASP A1047 12782 17927 7287 760 1566 -4726 C ATOM 2735 C ASP A1047 2.766 5.023 -12.816 1.00101.42 C ANISOU 2735 C ASP A1047 12975 18362 7198 558 1963 -4361 C ATOM 2736 O ASP A1047 3.043 4.032 -12.143 1.00103.61 O ANISOU 2736 O ASP A1047 13495 18926 6946 399 2049 -3986 O ATOM 2737 CB ASP A1047 3.196 7.349 -12.028 1.00104.64 C ANISOU 2737 CB ASP A1047 13201 18819 7739 897 1665 -5432 C ATOM 2738 CG ASP A1047 4.112 8.567 -12.014 1.00104.47 C ANISOU 2738 CG ASP A1047 13161 18546 7987 1086 1264 -5839 C ATOM 2739 OD1 ASP A1047 5.090 8.603 -12.793 1.00100.13 O ANISOU 2739 OD1 ASP A1047 12692 17566 7786 1105 928 -5577 O ATOM 2740 OD2 ASP A1047 3.846 9.497 -11.223 1.00108.37 O ANISOU 2740 OD2 ASP A1047 13546 19275 8354 1211 1290 -6441 O ATOM 2741 N LYS A1048 1.640 5.123 -13.510 1.00100.95 N ANISOU 2741 N LYS A1048 12646 18171 7538 563 2180 -4470 N ATOM 2742 CA LYS A1048 0.677 4.036 -13.568 1.00101.87 C ANISOU 2742 CA LYS A1048 12704 18454 7547 367 2553 -4159 C ATOM 2743 C LYS A1048 1.316 2.808 -14.148 1.00 98.07 C ANISOU 2743 C LYS A1048 12440 17715 7108 212 2453 -3475 C ATOM 2744 O LYS A1048 1.058 1.700 -13.724 1.00 98.74 O ANISOU 2744 O LYS A1048 12607 18007 6901 2 2712 -3108 O ATOM 2745 CB LYS A1048 -0.476 4.350 -14.513 1.00101.60 C ANISOU 2745 CB LYS A1048 12300 18232 8069 451 2700 -4462 C ATOM 2746 CG LYS A1048 -1.244 5.635 -14.316 1.00103.20 C ANISOU 2746 CG LYS A1048 12347 18636 8227 261 3112 -4279 C ATOM 2747 CD LYS A1048 -2.656 5.434 -14.846 1.00102.38 C ANISOU 2747 CD LYS A1048 11876 18251 8772 373 3151 -4551 C ATOM 2748 CE LYS A1048 -3.230 6.677 -15.497 1.00105.46 C ANISOU 2748 CE LYS A1048 11996 18720 9352 611 3141 -5267 C ATOM 2749 NZ LYS A1048 -4.417 6.369 -16.341 1.00104.82 N ANISOU 2749 NZ LYS A1048 11549 18367 9909 726 3163 -5510 N ATOM 2750 N ALA A1049 2.104 3.004 -15.187 1.00 94.58 N ANISOU 2750 N ALA A1049 12076 16814 7046 310 2085 -3315 N ATOM 2751 CA ALA A1049 2.688 1.866 -15.891 1.00 91.73 C ANISOU 2751 CA ALA A1049 11900 16179 6771 199 1962 -2728 C ATOM 2752 C ALA A1049 3.458 0.956 -14.944 1.00 93.97 C ANISOU 2752 C ALA A1049 12500 16722 6480 80 1921 -2370 C ATOM 2753 O ALA A1049 3.142 -0.226 -14.827 1.00 95.15 O ANISOU 2753 O ALA A1049 12768 16959 6426 -105 2094 -1944 O ATOM 2754 CB ALA A1049 3.591 2.340 -17.020 1.00 87.00 C ANISOU 2754 CB ALA A1049 11294 15081 6678 336 1596 -2694 C ATOM 2755 N ILE A1050 4.453 1.512 -14.259 1.00 95.36 N ANISOU 2755 N ILE A1050 12810 17008 6412 186 1674 -2543 N ATOM 2756 CA ILE A1050 5.331 0.711 -13.401 1.00 97.60 C ANISOU 2756 CA ILE A1050 13405 17500 6176 104 1546 -2200 C ATOM 2757 C ILE A1050 4.842 0.618 -11.945 1.00102.64 C ANISOU 2757 C ILE A1050 14148 18735 6112 2 1797 -2318 C ATOM 2758 O ILE A1050 5.051 -0.402 -11.289 1.00105.26 O ANISOU 2758 O ILE A1050 14733 19282 5977 -150 1836 -1896 O ATOM 2759 CB ILE A1050 6.798 1.195 -13.472 1.00 96.75 C ANISOU 2759 CB ILE A1050 13403 17184 6173 257 1098 -2254 C ATOM 2760 CG1 ILE A1050 7.007 2.518 -12.730 1.00100.42 C ANISOU 2760 CG1 ILE A1050 13791 17857 6505 402 993 -2840 C ATOM 2761 CG2 ILE A1050 7.234 1.340 -14.923 1.00 91.04 C ANISOU 2761 CG2 ILE A1050 12557 15915 6116 338 899 -2155 C ATOM 2762 CD1 ILE A1050 8.465 2.914 -12.636 1.00100.28 C ANISOU 2762 CD1 ILE A1050 13880 17685 6536 518 554 -2880 C ATOM 2763 N GLY A1051 4.202 1.678 -11.451 1.00104.10 N ANISOU 2763 N GLY A1051 14143 19185 6223 88 1960 -2889 N ATOM 2764 CA GLY A1051 3.545 1.662 -10.139 1.00108.78 C ANISOU 2764 CA GLY A1051 14782 20391 6156 -12 2278 -3074 C ATOM 2765 C GLY A1051 4.227 2.471 -9.052 1.00111.64 C ANISOU 2765 C GLY A1051 15258 21083 6074 108 2094 -3479 C ATOM 2766 O GLY A1051 4.261 2.044 -7.902 1.00116.97 O ANISOU 2766 O GLY A1051 16148 22247 6046 -6 2208 -3382 O ATOM 2767 N ARG A1052 4.748 3.645 -9.405 1.00109.13 N ANISOU 2767 N ARG A1052 14802 20503 6158 330 1806 -3935 N ATOM 2768 CA ARG A1052 5.447 4.516 -8.450 1.00112.25 C ANISOU 2768 CA ARG A1052 15279 21152 6218 462 1578 -4384 C ATOM 2769 C ARG A1052 5.702 5.901 -9.046 1.00109.21 C ANISOU 2769 C ARG A1052 14653 20393 6447 690 1328 -4929 C ATOM 2770 O ARG A1052 5.769 6.050 -10.262 1.00105.75 O ANISOU 2770 O ARG A1052 14074 19437 6668 740 1208 -4808 O ATOM 2771 CB ARG A1052 6.778 3.891 -8.024 1.00112.79 C ANISOU 2771 CB ARG A1052 15678 21232 5945 431 1214 -3988 C ATOM 2772 CG ARG A1052 7.649 3.445 -9.186 1.00107.42 C ANISOU 2772 CG ARG A1052 15025 19970 5817 455 902 -3555 C ATOM 2773 CD ARG A1052 9.060 3.083 -8.749 1.00108.28 C ANISOU 2773 CD ARG A1052 15393 20070 5677 482 481 -3305 C ATOM 2774 NE ARG A1052 10.046 3.455 -9.764 1.00104.18 N ANISOU 2774 NE ARG A1052 14775 19014 5792 603 116 -3280 N ATOM 2775 CZ ARG A1052 10.463 4.701 -9.996 1.00103.77 C ANISOU 2775 CZ ARG A1052 14548 18765 6113 756 -102 -3766 C ATOM 2776 NH1 ARG A1052 9.984 5.721 -9.286 1.00107.71 N ANISOU 2776 NH1 ARG A1052 14947 19534 6443 835 -19 -4355 N ATOM 2777 NH2 ARG A1052 11.361 4.936 -10.947 1.00 99.49 N ANISOU 2777 NH2 ARG A1052 13921 17749 6130 824 -400 -3672 N ATOM 2778 N ASN A1053 5.865 6.904 -8.189 1.00111.89 N ANISOU 2778 N ASN A1053 14959 20989 6563 820 1235 -5520 N ATOM 2779 CA ASN A1053 6.029 8.291 -8.639 1.00110.11 C ANISOU 2779 CA ASN A1053 14501 20414 6922 1030 1001 -6085 C ATOM 2780 C ASN A1053 7.366 8.538 -9.342 1.00105.86 C ANISOU 2780 C ASN A1053 14028 19370 6823 1096 516 -5905 C ATOM 2781 O ASN A1053 8.326 9.022 -8.745 1.00107.44 O ANISOU 2781 O ASN A1053 14330 19629 6860 1168 194 -6126 O ATOM 2782 CB ASN A1053 5.858 9.258 -7.464 1.00115.70 C ANISOU 2782 CB ASN A1053 15159 21543 7256 1151 1024 -6797 C ATOM 2783 CG ASN A1053 4.481 9.178 -6.834 1.00119.56 C ANISOU 2783 CG ASN A1053 15513 22533 7380 1104 1536 -7073 C ATOM 2784 OD1 ASN A1053 3.555 8.599 -7.402 1.00117.27 O ANISOU 2784 OD1 ASN A1053 15097 22197 7263 1002 1861 -6806 O ATOM 2785 ND2 ASN A1053 4.342 9.761 -5.648 1.00125.33 N ANISOU 2785 ND2 ASN A1053 16255 23762 7601 1173 1614 -7633 N ATOM 2786 N THR A1054 7.398 8.220 -10.630 1.00100.83 N ANISOU 2786 N THR A1054 13314 18248 6748 1065 474 -5523 N ATOM 2787 CA THR A1054 8.620 8.269 -11.433 1.00 97.30 C ANISOU 2787 CA THR A1054 12916 17334 6719 1089 81 -5261 C ATOM 2788 C THR A1054 9.140 9.680 -11.700 1.00 98.13 C ANISOU 2788 C THR A1054 12857 17104 7321 1242 -234 -5748 C ATOM 2789 O THR A1054 10.345 9.916 -11.643 1.00 97.74 O ANISOU 2789 O THR A1054 12885 16907 7345 1265 -592 -5727 O ATOM 2790 CB THR A1054 8.398 7.594 -12.801 1.00 91.45 C ANISOU 2790 CB THR A1054 12118 16187 6440 1014 160 -4767 C ATOM 2791 OG1 THR A1054 7.395 8.309 -13.537 1.00 89.76 O ANISOU 2791 OG1 THR A1054 11647 15740 6714 1082 311 -5035 O ATOM 2792 CG2 THR A1054 7.964 6.158 -12.621 1.00 91.23 C ANISOU 2792 CG2 THR A1054 12252 16409 6000 850 431 -4255 C ATOM 2793 N ASN A1055 8.223 10.596 -12.011 1.00 99.47 N ANISOU 2793 N ASN A1055 12791 17136 7867 1342 -112 -6173 N ATOM 2794 CA ASN A1055 8.560 11.955 -12.445 1.00 99.37 C ANISOU 2794 CA ASN A1055 12603 16707 8444 1478 -404 -6597 C ATOM 2795 C ASN A1055 9.209 11.987 -13.841 1.00 93.94 C ANISOU 2795 C ASN A1055 11875 15436 8380 1440 -626 -6208 C ATOM 2796 O ASN A1055 10.012 12.867 -14.143 1.00 93.21 O ANISOU 2796 O ASN A1055 11723 15000 8689 1490 -954 -6380 O ATOM 2797 CB ASN A1055 9.454 12.650 -11.404 1.00103.48 C ANISOU 2797 CB ASN A1055 13197 17401 8719 1552 -697 -7023 C ATOM 2798 CG ASN A1055 9.445 14.163 -11.530 1.00105.48 C ANISOU 2798 CG ASN A1055 13242 17323 9509 1705 -924 -7628 C ATOM 2799 OD1 ASN A1055 8.653 14.740 -12.282 1.00104.39 O ANISOU 2799 OD1 ASN A1055 12906 16870 9888 1775 -842 -7771 O ATOM 2800 ND2 ASN A1055 10.334 14.817 -10.792 1.00108.53 N ANISOU 2800 ND2 ASN A1055 13677 17763 9797 1761 -1240 -7989 N ATOM 2801 N GLY A1056 8.843 11.030 -14.693 1.00 90.80 N ANISOU 2801 N GLY A1056 11505 14936 8057 1339 -439 -5693 N ATOM 2802 CA GLY A1056 9.339 10.978 -16.077 1.00 86.80 C ANISOU 2802 CA GLY A1056 10963 13925 8090 1294 -596 -5317 C ATOM 2803 C GLY A1056 10.677 10.281 -16.293 1.00 84.55 C ANISOU 2803 C GLY A1056 10837 13560 7727 1205 -806 -4886 C ATOM 2804 O GLY A1056 11.231 10.334 -17.390 1.00 79.99 O ANISOU 2804 O GLY A1056 10218 12592 7581 1166 -947 -4625 O ATOM 2805 N VAL A1057 11.191 9.625 -15.254 1.00 87.40 N ANISOU 2805 N VAL A1057 11374 14301 7533 1173 -829 -4814 N ATOM 2806 CA VAL A1057 12.491 8.950 -15.310 1.00 85.89 C ANISOU 2806 CA VAL A1057 11318 14064 7250 1114 -1060 -4447 C ATOM 2807 C VAL A1057 12.361 7.518 -14.790 1.00 86.57 C ANISOU 2807 C VAL A1057 11610 14492 6788 1031 -886 -4038 C ATOM 2808 O VAL A1057 11.593 7.253 -13.862 1.00 90.16 O ANISOU 2808 O VAL A1057 12144 15348 6763 1017 -669 -4154 O ATOM 2809 CB VAL A1057 13.566 9.715 -14.500 1.00 88.14 C ANISOU 2809 CB VAL A1057 11616 14409 7463 1174 -1408 -4786 C ATOM 2810 CG1 VAL A1057 13.142 9.889 -13.047 1.00 93.24 C ANISOU 2810 CG1 VAL A1057 12353 15548 7526 1227 -1341 -5170 C ATOM 2811 CG2 VAL A1057 14.921 9.022 -14.587 1.00 86.58 C ANISOU 2811 CG2 VAL A1057 11518 14156 7221 1126 -1663 -4420 C ATOM 2812 N ILE A1058 13.120 6.603 -15.387 1.00 83.60 N ANISOU 2812 N ILE A1058 11316 13952 6495 971 -983 -3562 N ATOM 2813 CA ILE A1058 13.064 5.184 -15.027 1.00 83.24 C ANISOU 2813 CA ILE A1058 11471 14137 6019 890 -861 -3117 C ATOM 2814 C ILE A1058 14.454 4.558 -15.018 1.00 81.93 C ANISOU 2814 C ILE A1058 11408 13889 5830 893 -1168 -2816 C ATOM 2815 O ILE A1058 15.422 5.188 -15.427 1.00 80.76 O ANISOU 2815 O ILE A1058 11149 13498 6036 941 -1435 -2932 O ATOM 2816 CB ILE A1058 12.156 4.407 -15.999 1.00 79.83 C ANISOU 2816 CB ILE A1058 11006 13544 5780 811 -570 -2783 C ATOM 2817 CG1 ILE A1058 12.509 4.745 -17.447 1.00 75.08 C ANISOU 2817 CG1 ILE A1058 10250 12472 5803 828 -666 -2696 C ATOM 2818 CG2 ILE A1058 10.694 4.742 -15.742 1.00 81.74 C ANISOU 2818 CG2 ILE A1058 11162 13976 5918 797 -239 -3037 C ATOM 2819 CD1 ILE A1058 11.888 3.806 -18.451 1.00 72.10 C ANISOU 2819 CD1 ILE A1058 9872 11927 5594 752 -454 -2319 C ATOM 2820 N THR A1059 14.550 3.323 -14.539 1.00 83.10 N ANISOU 2820 N THR A1059 11759 14235 5580 838 -1135 -2429 N ATOM 2821 CA THR A1059 15.812 2.583 -14.562 1.00 83.55 C ANISOU 2821 CA THR A1059 11907 14198 5641 859 -1431 -2111 C ATOM 2822 C THR A1059 15.846 1.652 -15.773 1.00 80.38 C ANISOU 2822 C THR A1059 11473 13473 5593 818 -1340 -1691 C ATOM 2823 O THR A1059 14.819 1.412 -16.407 1.00 77.54 O ANISOU 2823 O THR A1059 11075 13028 5357 755 -1045 -1600 O ATOM 2824 CB THR A1059 16.017 1.758 -13.276 1.00 87.48 C ANISOU 2824 CB THR A1059 12666 15076 5496 839 -1521 -1916 C ATOM 2825 OG1 THR A1059 15.212 0.573 -13.320 1.00 87.70 O ANISOU 2825 OG1 THR A1059 12841 15175 5305 733 -1253 -1503 O ATOM 2826 CG2 THR A1059 15.653 2.576 -12.044 1.00 91.70 C ANISOU 2826 CG2 THR A1059 13256 16014 5569 859 -1510 -2342 C ATOM 2827 N LYS A1060 17.030 1.129 -16.084 1.00 81.09 N ANISOU 2827 N LYS A1060 11566 13392 5852 860 -1603 -1465 N ATOM 2828 CA LYS A1060 17.208 0.233 -17.234 1.00 78.82 C ANISOU 2828 CA LYS A1060 11239 12801 5907 841 -1545 -1109 C ATOM 2829 C LYS A1060 16.394 -1.052 -17.059 1.00 78.95 C ANISOU 2829 C LYS A1060 11443 12908 5644 763 -1334 -733 C ATOM 2830 O LYS A1060 15.776 -1.535 -18.006 1.00 76.46 O ANISOU 2830 O LYS A1060 11082 12393 5573 710 -1122 -563 O ATOM 2831 CB LYS A1060 18.691 -0.109 -17.447 1.00 80.33 C ANISOU 2831 CB LYS A1060 11378 12836 6305 920 -1878 -979 C ATOM 2832 CG LYS A1060 19.030 -0.510 -18.876 1.00 78.35 C ANISOU 2832 CG LYS A1060 10982 12237 6548 921 -1825 -799 C ATOM 2833 CD LYS A1060 20.388 -1.192 -18.989 0.00 80.75 C ANISOU 2833 CD LYS A1060 11247 12430 7002 1004 -2113 -617 C ATOM 2834 CE LYS A1060 20.590 -1.766 -20.390 0.00 79.31 C ANISOU 2834 CE LYS A1060 10938 11946 7247 1004 -2004 -434 C ATOM 2835 NZ LYS A1060 21.748 -2.701 -20.512 0.00 80.51 N ANISOU 2835 NZ LYS A1060 11058 11993 7539 1100 -2240 -230 N ATOM 2836 N ASP A1061 16.398 -1.594 -15.844 1.00 82.43 N ANISOU 2836 N ASP A1061 12099 13648 5569 743 -1402 -600 N ATOM 2837 CA ASP A1061 15.577 -2.757 -15.508 1.00 83.21 C ANISOU 2837 CA ASP A1061 12396 13862 5357 633 -1196 -233 C ATOM 2838 C ASP A1061 14.103 -2.491 -15.811 1.00 80.63 C ANISOU 2838 C ASP A1061 11998 13596 5042 527 -789 -349 C ATOM 2839 O ASP A1061 13.419 -3.331 -16.401 1.00 77.82 O ANISOU 2839 O ASP A1061 11660 13100 4806 438 -584 -76 O ATOM 2840 CB ASP A1061 15.739 -3.122 -14.026 1.00 89.03 C ANISOU 2840 CB ASP A1061 13385 14977 5464 608 -1322 -120 C ATOM 2841 CG ASP A1061 17.130 -3.632 -13.697 1.00 91.61 C ANISOU 2841 CG ASP A1061 13803 15234 5767 714 -1752 74 C ATOM 2842 OD1 ASP A1061 18.032 -3.524 -14.559 1.00 89.56 O ANISOU 2842 OD1 ASP A1061 13370 14664 5992 816 -1944 38 O ATOM 2843 OD2 ASP A1061 17.319 -4.142 -12.572 1.00 96.21 O ANISOU 2843 OD2 ASP A1061 14627 16084 5843 694 -1899 266 O ATOM 2844 N GLU A1062 13.628 -1.317 -15.398 1.00 80.77 N ANISOU 2844 N GLU A1062 11917 13810 4959 545 -693 -777 N ATOM 2845 CA GLU A1062 12.236 -0.925 -15.607 1.00 79.97 C ANISOU 2845 CA GLU A1062 11708 13789 4889 471 -330 -961 C ATOM 2846 C GLU A1062 11.926 -0.759 -17.101 1.00 75.52 C ANISOU 2846 C GLU A1062 10944 12832 4916 484 -239 -963 C ATOM 2847 O GLU A1062 10.825 -1.086 -17.549 1.00 74.59 O ANISOU 2847 O GLU A1062 10772 12682 4884 398 40 -888 O ATOM 2848 CB GLU A1062 11.909 0.354 -14.815 1.00 82.07 C ANISOU 2848 CB GLU A1062 11895 14333 4954 523 -293 -1474 C ATOM 2849 CG GLU A1062 11.899 0.136 -13.302 1.00 87.30 C ANISOU 2849 CG GLU A1062 12767 15468 4932 481 -294 -1485 C ATOM 2850 CD GLU A1062 11.813 1.418 -12.479 1.00 90.16 C ANISOU 2850 CD GLU A1062 13058 16107 5090 563 -326 -2047 C ATOM 2851 OE1 GLU A1062 12.237 2.488 -12.967 1.00 88.65 O ANISOU 2851 OE1 GLU A1062 12685 15687 5308 676 -495 -2399 O ATOM 2852 OE2 GLU A1062 11.329 1.351 -11.324 1.00 93.30 O ANISOU 2852 OE2 GLU A1062 13586 16956 4907 505 -181 -2139 O ATOM 2853 N ALA A1063 12.903 -0.276 -17.868 1.00 72.79 N ANISOU 2853 N ALA A1063 10488 12201 4965 578 -478 -1039 N ATOM 2854 CA ALA A1063 12.761 -0.150 -19.321 1.00 67.99 C ANISOU 2854 CA ALA A1063 9721 11234 4877 584 -423 -1006 C ATOM 2855 C ALA A1063 12.672 -1.511 -19.990 1.00 66.02 C ANISOU 2855 C ALA A1063 9550 10818 4717 523 -348 -584 C ATOM 2856 O ALA A1063 11.862 -1.717 -20.891 1.00 64.38 O ANISOU 2856 O ALA A1063 9262 10451 4745 473 -160 -525 O ATOM 2857 CB ALA A1063 13.922 0.638 -19.902 1.00 66.45 C ANISOU 2857 CB ALA A1063 9402 10813 5033 672 -686 -1154 C ATOM 2858 N GLU A1064 13.514 -2.436 -19.547 1.00 68.11 N ANISOU 2858 N GLU A1064 9967 11105 4807 536 -524 -306 N ATOM 2859 CA GLU A1064 13.542 -3.789 -20.103 1.00 67.57 C ANISOU 2859 CA GLU A1064 9982 10849 4841 494 -499 84 C ATOM 2860 C GLU A1064 12.330 -4.621 -19.682 1.00 67.41 C ANISOU 2860 C GLU A1064 10082 10966 4562 352 -235 297 C ATOM 2861 O GLU A1064 11.933 -5.533 -20.399 1.00 65.32 O ANISOU 2861 O GLU A1064 9829 10500 4486 291 -135 538 O ATOM 2862 CB GLU A1064 14.867 -4.486 -19.754 1.00 70.39 C ANISOU 2862 CB GLU A1064 10446 11154 5144 575 -809 300 C ATOM 2863 CG GLU A1064 16.032 -3.950 -20.588 1.00 70.27 C ANISOU 2863 CG GLU A1064 10254 10917 5527 690 -1020 155 C ATOM 2864 CD GLU A1064 17.396 -4.462 -20.155 1.00 73.99 C ANISOU 2864 CD GLU A1064 10776 11366 5970 792 -1352 291 C ATOM 2865 OE1 GLU A1064 17.644 -4.525 -18.931 1.00 79.26 O ANISOU 2865 OE1 GLU A1064 11591 12271 6253 805 -1504 322 O ATOM 2866 OE2 GLU A1064 18.228 -4.784 -21.040 1.00 73.22 O ANISOU 2866 OE2 GLU A1064 10560 11028 6230 864 -1465 350 O ATOM 2867 N LYS A1065 11.734 -4.296 -18.537 1.00 70.33 N ANISOU 2867 N LYS A1065 10530 11683 4508 290 -113 190 N ATOM 2868 CA LYS A1065 10.504 -4.957 -18.100 1.00 72.12 C ANISOU 2868 CA LYS A1065 10835 12085 4481 124 186 361 C ATOM 2869 C LYS A1065 9.336 -4.541 -18.985 1.00 70.13 C ANISOU 2869 C LYS A1065 10375 11731 4539 77 457 175 C ATOM 2870 O LYS A1065 8.540 -5.386 -19.393 1.00 71.31 O ANISOU 2870 O LYS A1065 10527 11787 4779 -43 643 399 O ATOM 2871 CB LYS A1065 10.199 -4.642 -16.636 1.00 76.23 C ANISOU 2871 CB LYS A1065 11476 13055 4432 67 269 258 C ATOM 2872 CG LYS A1065 8.929 -5.300 -16.112 0.00 78.84 C ANISOU 2872 CG LYS A1065 11873 13617 4466 -133 618 439 C ATOM 2873 CD LYS A1065 8.659 -4.944 -14.656 0.00 83.30 C ANISOU 2873 CD LYS A1065 12555 14680 4413 -194 723 313 C ATOM 2874 CE LYS A1065 9.598 -5.680 -13.719 0.00 86.31 C ANISOU 2874 CE LYS A1065 13233 15187 4371 -206 465 654 C ATOM 2875 NZ LYS A1065 9.227 -5.424 -12.304 0.00 92.06 N ANISOU 2875 NZ LYS A1065 14102 16444 4429 -294 600 562 N ATOM 2876 N LEU A1066 9.233 -3.243 -19.268 1.00 68.61 N ANISOU 2876 N LEU A1066 10001 11541 4525 172 454 -232 N ATOM 2877 CA LEU A1066 8.243 -2.720 -20.229 1.00 66.03 C ANISOU 2877 CA LEU A1066 9462 11067 4558 165 637 -427 C ATOM 2878 C LEU A1066 8.372 -3.360 -21.604 1.00 61.47 C ANISOU 2878 C LEU A1066 8844 10118 4394 163 587 -209 C ATOM 2879 O LEU A1066 7.381 -3.778 -22.202 1.00 59.58 O ANISOU 2879 O LEU A1066 8528 9793 4315 78 775 -140 O ATOM 2880 CB LEU A1066 8.402 -1.208 -20.403 1.00 65.10 C ANISOU 2880 CB LEU A1066 9180 10923 4633 294 542 -862 C ATOM 2881 CG LEU A1066 7.717 -0.317 -19.382 1.00 68.68 C ANISOU 2881 CG LEU A1066 9566 11705 4821 307 683 -1232 C ATOM 2882 CD1 LEU A1066 8.196 1.114 -19.556 1.00 68.46 C ANISOU 2882 CD1 LEU A1066 9407 11571 5031 450 493 -1632 C ATOM 2883 CD2 LEU A1066 6.207 -0.409 -19.533 1.00 69.83 C ANISOU 2883 CD2 LEU A1066 9571 11943 5017 221 1008 -1308 C ATOM 2884 N PHE A1067 9.607 -3.407 -22.097 1.00 59.43 N ANISOU 2884 N PHE A1067 8620 9655 4305 257 331 -131 N ATOM 2885 CA PHE A1067 9.895 -3.939 -23.416 1.00 56.62 C ANISOU 2885 CA PHE A1067 8222 8972 4319 274 271 26 C ATOM 2886 C PHE A1067 9.284 -5.313 -23.599 1.00 57.58 C ANISOU 2886 C PHE A1067 8431 9020 4425 161 401 342 C ATOM 2887 O PHE A1067 8.563 -5.546 -24.561 1.00 56.42 O ANISOU 2887 O PHE A1067 8194 8707 4534 117 514 356 O ATOM 2888 CB PHE A1067 11.404 -4.032 -23.651 1.00 55.50 C ANISOU 2888 CB PHE A1067 8116 8690 4280 379 -1 99 C ATOM 2889 CG PHE A1067 11.766 -4.556 -25.014 1.00 51.99 C ANISOU 2889 CG PHE A1067 7615 7945 4190 404 -45 223 C ATOM 2890 CD1 PHE A1067 11.696 -3.737 -26.112 1.00 49.04 C ANISOU 2890 CD1 PHE A1067 7093 7421 4118 433 -33 48 C ATOM 2891 CD2 PHE A1067 12.147 -5.873 -25.192 1.00 52.79 C ANISOU 2891 CD2 PHE A1067 7821 7919 4318 397 -101 510 C ATOM 2892 CE1 PHE A1067 12.009 -4.209 -27.362 1.00 47.28 C ANISOU 2892 CE1 PHE A1067 6828 6968 4166 448 -56 146 C ATOM 2893 CE2 PHE A1067 12.466 -6.358 -26.444 1.00 50.07 C ANISOU 2893 CE2 PHE A1067 7417 7320 4285 431 -130 574 C ATOM 2894 CZ PHE A1067 12.398 -5.522 -27.531 1.00 47.78 C ANISOU 2894 CZ PHE A1067 6981 6927 4244 452 -96 387 C ATOM 2895 N ASN A1068 9.576 -6.214 -22.668 1.00 60.93 N ANISOU 2895 N ASN A1068 9038 9557 4555 108 363 602 N ATOM 2896 CA ASN A1068 9.099 -7.590 -22.761 1.00 62.40 C ANISOU 2896 CA ASN A1068 9331 9635 4744 -13 451 941 C ATOM 2897 C ASN A1068 7.573 -7.684 -22.802 1.00 62.70 C ANISOU 2897 C ASN A1068 9283 9763 4777 -170 758 913 C ATOM 2898 O ASN A1068 7.019 -8.490 -23.555 1.00 60.45 O ANISOU 2898 O ASN A1068 8971 9272 4725 -251 835 1062 O ATOM 2899 CB ASN A1068 9.666 -8.428 -21.614 1.00 66.49 C ANISOU 2899 CB ASN A1068 10078 10270 4913 -50 334 1242 C ATOM 2900 CG ASN A1068 11.183 -8.546 -21.672 1.00 66.83 C ANISOU 2900 CG ASN A1068 10182 10177 5032 112 2 1298 C ATOM 2901 OD1 ASN A1068 11.781 -8.613 -22.748 1.00 62.86 O ANISOU 2901 OD1 ASN A1068 9581 9409 4895 213 -111 1252 O ATOM 2902 ND2 ASN A1068 11.814 -8.577 -20.504 1.00 71.60 N ANISOU 2902 ND2 ASN A1068 10940 10985 5279 137 -154 1390 N ATOM 2903 N GLN A1069 6.899 -6.844 -22.021 1.00 64.76 N ANISOU 2903 N GLN A1069 9477 10331 4798 -206 926 687 N ATOM 2904 CA GLN A1069 5.440 -6.772 -22.066 1.00 66.94 C ANISOU 2904 CA GLN A1069 9609 10719 5103 -338 1226 590 C ATOM 2905 C GLN A1069 4.948 -6.308 -23.436 1.00 64.15 C ANISOU 2905 C GLN A1069 9048 10119 5206 -278 1234 394 C ATOM 2906 O GLN A1069 3.983 -6.851 -23.964 1.00 66.04 O ANISOU 2906 O GLN A1069 9198 10269 5624 -389 1386 465 O ATOM 2907 CB GLN A1069 4.904 -5.847 -20.973 1.00 70.67 C ANISOU 2907 CB GLN A1069 10020 11585 5244 -352 1396 314 C ATOM 2908 CG GLN A1069 5.130 -6.385 -19.565 1.00 76.02 C ANISOU 2908 CG GLN A1069 10914 12574 5395 -457 1446 529 C ATOM 2909 CD GLN A1069 4.666 -5.440 -18.468 1.00 79.99 C ANISOU 2909 CD GLN A1069 11361 13505 5524 -457 1612 206 C ATOM 2910 OE1 GLN A1069 4.593 -4.221 -18.668 1.00 84.40 O ANISOU 2910 OE1 GLN A1069 12102 14371 5593 -525 1636 325 O ATOM 2911 NE2 GLN A1069 4.355 -5.994 -17.303 1.00 79.51 N ANISOU 2911 NE2 GLN A1069 11052 13468 5688 -373 1716 -211 N ATOM 2912 N ASP A1070 5.620 -5.317 -24.014 1.00 61.00 N ANISOU 2912 N ASP A1070 8575 9607 4992 -114 1056 164 N ATOM 2913 CA ASP A1070 5.256 -4.812 -25.335 1.00 58.45 C ANISOU 2913 CA ASP A1070 8087 9052 5069 -54 1025 7 C ATOM 2914 C ASP A1070 5.504 -5.856 -26.453 1.00 58.05 C ANISOU 2914 C ASP A1070 8086 8702 5266 -78 944 249 C ATOM 2915 O ASP A1070 4.666 -6.039 -27.336 1.00 58.77 O ANISOU 2915 O ASP A1070 8068 8661 5600 -123 1016 224 O ATOM 2916 CB ASP A1070 6.014 -3.509 -25.635 1.00 56.45 C ANISOU 2916 CB ASP A1070 7768 8741 4937 101 844 -251 C ATOM 2917 CG ASP A1070 5.682 -2.377 -24.650 1.00 58.22 C ANISOU 2917 CG ASP A1070 7915 9221 4984 144 907 -565 C ATOM 2918 OD1 ASP A1070 4.582 -2.393 -24.056 1.00 58.94 O ANISOU 2918 OD1 ASP A1070 7928 9520 4943 68 1131 -660 O ATOM 2919 OD2 ASP A1070 6.528 -1.459 -24.477 1.00 57.04 O ANISOU 2919 OD2 ASP A1070 7765 9063 4841 253 734 -740 O ATOM 2920 N VAL A1071 6.645 -6.539 -26.411 1.00 57.91 N ANISOU 2920 N VAL A1071 8221 8581 5199 -38 779 457 N ATOM 2921 CA VAL A1071 6.955 -7.596 -27.381 1.00 56.68 C ANISOU 2921 CA VAL A1071 8116 8151 5269 -44 698 655 C ATOM 2922 C VAL A1071 6.013 -8.794 -27.250 1.00 58.06 C ANISOU 2922 C VAL A1071 8332 8282 5443 -207 846 873 C ATOM 2923 O VAL A1071 5.596 -9.378 -28.251 1.00 56.30 O ANISOU 2923 O VAL A1071 8061 7848 5480 -242 853 909 O ATOM 2924 CB VAL A1071 8.404 -8.088 -27.224 1.00 58.09 C ANISOU 2924 CB VAL A1071 8426 8240 5403 51 484 808 C ATOM 2925 CG1 VAL A1071 8.639 -9.370 -28.011 1.00 58.43 C ANISOU 2925 CG1 VAL A1071 8528 8014 5656 42 418 1010 C ATOM 2926 CG2 VAL A1071 9.366 -7.006 -27.679 1.00 57.50 C ANISOU 2926 CG2 VAL A1071 8271 8144 5429 191 337 601 C ATOM 2927 N ASP A1072 5.706 -9.178 -26.017 1.00 59.92 N ANISOU 2927 N ASP A1072 8664 8720 5382 -320 957 1024 N ATOM 2928 CA ASP A1072 4.686 -10.186 -25.780 1.00 62.09 C ANISOU 2928 CA ASP A1072 8958 8986 5647 -518 1136 1232 C ATOM 2929 C ASP A1072 3.429 -9.730 -26.509 1.00 60.06 C ANISOU 2929 C ASP A1072 8474 8724 5619 -574 1302 1011 C ATOM 2930 O ASP A1072 2.841 -10.483 -27.286 1.00 59.26 O ANISOU 2930 O ASP A1072 8322 8419 5771 -658 1330 1090 O ATOM 2931 CB ASP A1072 4.440 -10.345 -24.270 1.00 67.09 C ANISOU 2931 CB ASP A1072 9704 9926 5859 -648 1277 1383 C ATOM 2932 CG ASP A1072 3.268 -11.276 -23.939 1.00 70.55 C ANISOU 2932 CG ASP A1072 10135 10400 6270 -899 1515 1601 C ATOM 2933 OD1 ASP A1072 2.120 -10.984 -24.342 1.00 71.21 O ANISOU 2933 OD1 ASP A1072 10010 10529 6518 -981 1712 1425 O ATOM 2934 OD2 ASP A1072 3.489 -12.284 -23.235 1.00 73.33 O ANISOU 2934 OD2 ASP A1072 10685 10737 6440 -1022 1499 1957 O ATOM 2935 N ALA A1073 3.050 -8.477 -26.269 1.00 59.07 N ANISOU 2935 N ALA A1073 8207 8809 5427 -511 1383 714 N ATOM 2936 CA ALA A1073 1.833 -7.901 -26.832 1.00 57.97 C ANISOU 2936 CA ALA A1073 7831 8691 5503 -538 1520 474 C ATOM 2937 C ALA A1073 1.804 -7.982 -28.360 1.00 55.08 C ANISOU 2937 C ALA A1073 7392 8020 5514 -470 1374 421 C ATOM 2938 O ALA A1073 0.778 -8.347 -28.947 1.00 55.09 O ANISOU 2938 O ALA A1073 7261 7940 5730 -563 1459 398 O ATOM 2939 CB ALA A1073 1.674 -6.459 -26.375 1.00 57.70 C ANISOU 2939 CB ALA A1073 7670 8877 5376 -429 1560 139 C ATOM 2940 N ALA A1074 2.932 -7.647 -28.988 1.00 51.75 N ANISOU 2940 N ALA A1074 7051 7450 5159 -317 1159 398 N ATOM 2941 CA ALA A1074 3.053 -7.668 -30.446 1.00 48.94 C ANISOU 2941 CA ALA A1074 6654 6845 5096 -248 1019 347 C ATOM 2942 C ALA A1074 2.958 -9.079 -31.028 1.00 49.52 C ANISOU 2942 C ALA A1074 6798 6707 5307 -337 998 553 C ATOM 2943 O ALA A1074 2.322 -9.283 -32.060 1.00 48.24 O ANISOU 2943 O ALA A1074 6546 6403 5378 -359 976 486 O ATOM 2944 CB ALA A1074 4.360 -7.023 -30.867 1.00 47.04 C ANISOU 2944 CB ALA A1074 6481 6535 4857 -93 830 294 C ATOM 2945 N VAL A1075 3.596 -10.043 -30.367 1.00 51.78 N ANISOU 2945 N VAL A1075 7249 6963 5462 -380 979 794 N ATOM 2946 CA VAL A1075 3.616 -11.426 -30.842 1.00 52.28 C ANISOU 2946 CA VAL A1075 7394 6784 5686 -452 929 989 C ATOM 2947 C VAL A1075 2.254 -12.071 -30.672 1.00 54.90 C ANISOU 2947 C VAL A1075 7640 7113 6105 -656 1101 1060 C ATOM 2948 O VAL A1075 1.811 -12.795 -31.551 1.00 56.19 O ANISOU 2948 O VAL A1075 7765 7063 6521 -709 1061 1067 O ATOM 2949 CB VAL A1075 4.690 -12.268 -30.131 1.00 53.66 C ANISOU 2949 CB VAL A1075 7768 6893 5725 -430 824 1242 C ATOM 2950 CG1 VAL A1075 4.566 -13.742 -30.500 1.00 55.10 C ANISOU 2950 CG1 VAL A1075 8031 6796 6108 -518 773 1446 C ATOM 2951 CG2 VAL A1075 6.073 -11.755 -30.497 1.00 51.83 C ANISOU 2951 CG2 VAL A1075 7578 6628 5485 -229 639 1153 C ATOM 2952 N ARG A1076 1.586 -11.823 -29.552 1.00 58.21 N ANISOU 2952 N ARG A1076 8018 7780 6317 -777 1296 1097 N ATOM 2953 CA ARG A1076 0.196 -12.256 -29.417 1.00 61.24 C ANISOU 2953 CA ARG A1076 8258 8205 6803 -985 1498 1119 C ATOM 2954 C ARG A1076 -0.635 -11.595 -30.512 1.00 58.63 C ANISOU 2954 C ARG A1076 7701 7829 6747 -934 1483 830 C ATOM 2955 O ARG A1076 -1.465 -12.241 -31.143 1.00 59.14 O ANISOU 2955 O ARG A1076 7661 7746 7062 -1048 1503 833 O ATOM 2956 CB ARG A1076 -0.375 -11.906 -28.042 1.00 65.39 C ANISOU 2956 CB ARG A1076 8744 9073 7026 -1113 1745 1150 C ATOM 2957 CG ARG A1076 0.220 -12.710 -26.906 1.00 69.31 C ANISOU 2957 CG ARG A1076 9476 9630 7225 -1216 1769 1492 C ATOM 2958 CD ARG A1076 -0.455 -12.392 -25.583 1.00 74.08 C ANISOU 2958 CD ARG A1076 10039 10619 7487 -1370 2048 1515 C ATOM 2959 NE ARG A1076 0.372 -12.823 -24.457 1.00 78.00 N ANISOU 2959 NE ARG A1076 10799 11230 7606 -1406 2011 1805 N ATOM 2960 CZ ARG A1076 0.509 -14.086 -24.046 1.00 82.52 C ANISOU 2960 CZ ARG A1076 11562 11663 8126 -1575 1993 2209 C ATOM 2961 NH1 ARG A1076 -0.139 -15.083 -24.644 1.00 83.59 N ANISOU 2961 NH1 ARG A1076 11649 11531 8581 -1740 2024 2364 N ATOM 2962 NH2 ARG A1076 1.299 -14.355 -23.010 1.00 86.34 N ANISOU 2962 NH2 ARG A1076 12293 12266 8244 -1582 1920 2465 N ATOM 2963 N GLY A1077 -0.397 -10.308 -30.740 1.00 56.32 N ANISOU 2963 N GLY A1077 7335 7645 6419 -763 1423 586 N ATOM 2964 CA GLY A1077 -1.070 -9.583 -31.813 1.00 56.13 C ANISOU 2964 CA GLY A1077 7123 7558 6645 -687 1354 332 C ATOM 2965 C GLY A1077 -0.990 -10.308 -33.147 1.00 55.37 C ANISOU 2965 C GLY A1077 7060 7180 6797 -675 1184 362 C ATOM 2966 O GLY A1077 -2.009 -10.564 -33.786 1.00 57.42 O ANISOU 2966 O GLY A1077 7167 7363 7285 -752 1191 278 O ATOM 2967 N ILE A1078 0.228 -10.655 -33.550 1.00 52.89 N ANISOU 2967 N ILE A1078 6932 6723 6438 -575 1030 460 N ATOM 2968 CA ILE A1078 0.466 -11.391 -34.789 1.00 50.79 C ANISOU 2968 CA ILE A1078 6718 6210 6368 -546 873 463 C ATOM 2969 C ILE A1078 -0.149 -12.795 -34.781 1.00 52.07 C ANISOU 2969 C ILE A1078 6887 6206 6691 -719 916 606 C ATOM 2970 O ILE A1078 -0.765 -13.198 -35.754 1.00 52.40 O ANISOU 2970 O ILE A1078 6849 6101 6957 -755 842 511 O ATOM 2971 CB ILE A1078 1.975 -11.497 -35.068 1.00 49.09 C ANISOU 2971 CB ILE A1078 6678 5910 6063 -402 733 524 C ATOM 2972 CG1 ILE A1078 2.532 -10.116 -35.381 1.00 47.17 C ANISOU 2972 CG1 ILE A1078 6408 5781 5732 -254 666 370 C ATOM 2973 CG2 ILE A1078 2.261 -12.442 -36.228 1.00 48.83 C ANISOU 2973 CG2 ILE A1078 6703 5638 6211 -376 600 515 C ATOM 2974 CD1 ILE A1078 4.001 -9.975 -35.059 1.00 47.47 C ANISOU 2974 CD1 ILE A1078 6575 5836 5623 -142 594 441 C ATOM 2975 N LEU A1079 0.018 -13.539 -33.696 1.00 53.87 N ANISOU 2975 N LEU A1079 7214 6446 6806 -834 1016 842 N ATOM 2976 CA LEU A1079 -0.509 -14.909 -33.634 1.00 57.14 C ANISOU 2976 CA LEU A1079 7651 6661 7396 -1020 1045 1019 C ATOM 2977 C LEU A1079 -2.043 -14.980 -33.597 1.00 59.52 C ANISOU 2977 C LEU A1079 7731 7022 7860 -1218 1202 955 C ATOM 2978 O LEU A1079 -2.621 -15.999 -33.960 1.00 61.70 O ANISOU 2978 O LEU A1079 7973 7090 8378 -1368 1184 1021 O ATOM 2979 CB LEU A1079 0.076 -15.670 -32.435 1.00 58.49 C ANISOU 2979 CB LEU A1079 8008 6822 7391 -1106 1095 1338 C ATOM 2980 CG LEU A1079 1.575 -15.965 -32.524 1.00 57.04 C ANISOU 2980 CG LEU A1079 8028 6502 7141 -924 900 1424 C ATOM 2981 CD1 LEU A1079 2.113 -16.465 -31.191 1.00 59.08 C ANISOU 2981 CD1 LEU A1079 8464 6809 7175 -991 930 1738 C ATOM 2982 CD2 LEU A1079 1.870 -16.958 -33.642 1.00 56.98 C ANISOU 2982 CD2 LEU A1079 8064 6153 7433 -876 720 1388 C ATOM 2983 N ARG A1080 -2.692 -13.902 -33.169 1.00 59.71 N ANISOU 2983 N ARG A1080 7586 7318 7780 -1215 1346 805 N ATOM 2984 CA ARG A1080 -4.140 -13.875 -33.017 1.00 62.90 C ANISOU 2984 CA ARG A1080 7735 7825 8339 -1393 1518 718 C ATOM 2985 C ARG A1080 -4.821 -13.274 -34.251 1.00 60.10 C ANISOU 2985 C ARG A1080 7182 7413 8239 -1297 1382 423 C ATOM 2986 O ARG A1080 -6.046 -13.188 -34.303 1.00 61.22 O ANISOU 2986 O ARG A1080 7071 7622 8568 -1413 1479 300 O ATOM 2987 CB ARG A1080 -4.480 -13.057 -31.774 1.00 67.98 C ANISOU 2987 CB ARG A1080 8286 8817 8724 -1433 1762 692 C ATOM 2988 CG ARG A1080 -5.895 -13.220 -31.229 1.00 74.79 C ANISOU 2988 CG ARG A1080 8886 9843 9685 -1665 2025 663 C ATOM 2989 CD ARG A1080 -6.363 -11.929 -30.566 1.00 78.28 C ANISOU 2989 CD ARG A1080 9138 10631 9973 -1588 2196 420 C ATOM 2990 NE ARG A1080 -6.296 -10.789 -31.491 1.00 78.12 N ANISOU 2990 NE ARG A1080 9020 10569 10091 -1338 1993 115 N ATOM 2991 CZ ARG A1080 -6.459 -9.511 -31.144 1.00 80.55 C ANISOU 2991 CZ ARG A1080 9196 11092 10316 -1194 2042 -135 C ATOM 2992 NH1 ARG A1080 -6.711 -9.172 -29.880 1.00 84.20 N ANISOU 2992 NH1 ARG A1080 9593 11863 10533 -1263 2305 -165 N ATOM 2993 NH2 ARG A1080 -6.375 -8.559 -32.070 1.00 78.21 N ANISOU 2993 NH2 ARG A1080 8839 10697 10180 -982 1819 -360 N ATOM 2994 N ASN A1081 -4.029 -12.878 -35.248 1.00 55.95 N ANISOU 2994 N ASN A1081 6767 6772 7719 -1092 1152 317 N ATOM 2995 CA ASN A1081 -4.535 -12.182 -36.436 1.00 53.77 C ANISOU 2995 CA ASN A1081 6351 6459 7619 -979 986 65 C ATOM 2996 C ASN A1081 -4.517 -13.064 -37.677 1.00 52.48 C ANISOU 2996 C ASN A1081 6243 6038 7657 -986 786 34 C ATOM 2997 O ASN A1081 -3.497 -13.653 -38.008 1.00 50.06 O ANISOU 2997 O ASN A1081 6145 5587 7286 -923 687 126 O ATOM 2998 CB ASN A1081 -3.692 -10.925 -36.699 1.00 51.24 C ANISOU 2998 CB ASN A1081 6111 6227 7127 -755 877 -37 C ATOM 2999 CG ASN A1081 -4.334 -9.984 -37.699 1.00 49.94 C ANISOU 2999 CG ASN A1081 5795 6063 7114 -649 720 -266 C ATOM 3000 OD1 ASN A1081 -4.788 -10.401 -38.761 1.00 50.46 O ANISOU 3000 OD1 ASN A1081 5820 5990 7360 -663 566 -340 O ATOM 3001 ND2 ASN A1081 -4.374 -8.706 -37.361 1.00 49.22 N ANISOU 3001 ND2 ASN A1081 5626 6118 6954 -536 733 -382 N ATOM 3002 N ALA A1082 -5.643 -13.119 -38.378 1.00 54.03 N ANISOU 3002 N ALA A1082 6237 6187 8103 -1049 715 -126 N ATOM 3003 CA ALA A1082 -5.758 -13.926 -39.585 1.00 54.54 C ANISOU 3003 CA ALA A1082 6336 6026 8360 -1060 508 -204 C ATOM 3004 C ALA A1082 -4.793 -13.444 -40.653 1.00 52.38 C ANISOU 3004 C ALA A1082 6238 5718 7946 -848 299 -293 C ATOM 3005 O ALA A1082 -4.100 -14.234 -41.277 1.00 52.92 O ANISOU 3005 O ALA A1082 6467 5624 8013 -816 190 -278 O ATOM 3006 CB ALA A1082 -7.181 -13.890 -40.114 1.00 56.20 C ANISOU 3006 CB ALA A1082 6271 6228 8854 -1152 445 -388 C ATOM 3007 N LYS A1083 -4.732 -12.141 -40.853 1.00 51.52 N ANISOU 3007 N LYS A1083 6091 5759 7723 -707 249 -387 N ATOM 3008 CA LYS A1083 -3.880 -11.595 -41.892 1.00 51.44 C ANISOU 3008 CA LYS A1083 6237 5737 7569 -537 66 -448 C ATOM 3009 C LYS A1083 -2.382 -11.643 -41.547 1.00 49.99 C ANISOU 3009 C LYS A1083 6273 5563 7155 -451 124 -312 C ATOM 3010 O LYS A1083 -1.551 -11.427 -42.421 1.00 50.15 O ANISOU 3010 O LYS A1083 6427 5570 7057 -338 5 -348 O ATOM 3011 CB LYS A1083 -4.313 -10.164 -42.234 1.00 52.20 C ANISOU 3011 CB LYS A1083 6228 5953 7650 -428 -32 -563 C ATOM 3012 CG LYS A1083 -3.661 -9.618 -43.494 1.00 52.22 C ANISOU 3012 CG LYS A1083 6380 5941 7521 -294 -243 -609 C ATOM 3013 CD LYS A1083 -4.426 -8.460 -44.106 1.00 52.79 C ANISOU 3013 CD LYS A1083 6335 6058 7664 -216 -421 -720 C ATOM 3014 CE LYS A1083 -5.567 -8.940 -44.974 1.00 54.99 C ANISOU 3014 CE LYS A1083 6484 6264 8146 -267 -601 -860 C ATOM 3015 NZ LYS A1083 -6.125 -7.791 -45.731 1.00 56.09 N ANISOU 3015 NZ LYS A1083 6557 6430 8325 -161 -838 -943 N ATOM 3016 N LEU A1084 -2.026 -11.928 -40.296 1.00 50.40 N ANISOU 3016 N LEU A1084 6359 5654 7136 -508 301 -157 N ATOM 3017 CA LEU A1084 -0.611 -11.937 -39.898 1.00 48.14 C ANISOU 3017 CA LEU A1084 6256 5382 6651 -417 330 -36 C ATOM 3018 C LEU A1084 -0.040 -13.300 -39.503 1.00 49.68 C ANISOU 3018 C LEU A1084 6575 5420 6881 -475 362 111 C ATOM 3019 O LEU A1084 1.168 -13.505 -39.638 1.00 50.61 O ANISOU 3019 O LEU A1084 6834 5494 6901 -369 312 154 O ATOM 3020 CB LEU A1084 -0.378 -10.956 -38.756 1.00 46.46 C ANISOU 3020 CB LEU A1084 6021 5356 6276 -387 456 20 C ATOM 3021 CG LEU A1084 -0.835 -9.533 -39.047 1.00 45.75 C ANISOU 3021 CG LEU A1084 5815 5386 6182 -307 406 -127 C ATOM 3022 CD1 LEU A1084 -0.920 -8.741 -37.757 1.00 46.59 C ANISOU 3022 CD1 LEU A1084 5855 5667 6180 -307 553 -117 C ATOM 3023 CD2 LEU A1084 0.096 -8.852 -40.031 1.00 43.52 C ANISOU 3023 CD2 LEU A1084 5642 5085 5807 -171 254 -167 C ATOM 3024 N LYS A1085 -0.873 -14.220 -39.009 1.00 50.99 N ANISOU 3024 N LYS A1085 6678 5489 7205 -645 436 193 N ATOM 3025 CA LYS A1085 -0.361 -15.494 -38.489 1.00 52.19 C ANISOU 3025 CA LYS A1085 6958 5458 7410 -713 452 379 C ATOM 3026 C LYS A1085 0.302 -16.344 -39.579 1.00 51.19 C ANISOU 3026 C LYS A1085 6936 5107 7405 -622 278 286 C ATOM 3027 O LYS A1085 1.427 -16.812 -39.390 1.00 49.84 O ANISOU 3027 O LYS A1085 6906 4848 7181 -528 236 372 O ATOM 3028 CB LYS A1085 -1.447 -16.303 -37.757 1.00 56.18 C ANISOU 3028 CB LYS A1085 7373 5892 8078 -950 574 515 C ATOM 3029 CG LYS A1085 -0.877 -17.276 -36.726 1.00 59.40 C ANISOU 3029 CG LYS A1085 7936 6182 8450 -1035 629 803 C ATOM 3030 CD LYS A1085 -1.616 -18.613 -36.646 1.00 64.18 C ANISOU 3030 CD LYS A1085 8520 6529 9333 -1254 633 929 C ATOM 3031 CE LYS A1085 -2.653 -18.636 -35.531 0.00 67.98 C ANISOU 3031 CE LYS A1085 8886 7152 9790 -1504 866 1106 C ATOM 3032 NZ LYS A1085 -3.398 -19.926 -35.459 0.00 72.09 N ANISOU 3032 NZ LYS A1085 9373 7409 10608 -1755 878 1253 N ATOM 3033 N PRO A1086 -0.378 -16.530 -40.728 1.00 51.29 N ANISOU 3033 N PRO A1086 6871 5038 7578 -637 164 85 N ATOM 3034 CA PRO A1086 0.193 -17.368 -41.796 1.00 51.43 C ANISOU 3034 CA PRO A1086 6981 4861 7697 -550 5 -54 C ATOM 3035 C PRO A1086 1.449 -16.783 -42.433 1.00 48.61 C ANISOU 3035 C PRO A1086 6726 4614 7129 -344 -47 -149 C ATOM 3036 O PRO A1086 2.345 -17.521 -42.833 1.00 49.23 O ANISOU 3036 O PRO A1086 6899 4559 7245 -248 -116 -204 O ATOM 3037 CB PRO A1086 -0.937 -17.467 -42.822 1.00 52.30 C ANISOU 3037 CB PRO A1086 6970 4927 7972 -619 -105 -265 C ATOM 3038 CG PRO A1086 -1.805 -16.297 -42.566 1.00 51.83 C ANISOU 3038 CG PRO A1086 6763 5088 7841 -660 -36 -272 C ATOM 3039 CD PRO A1086 -1.670 -15.940 -41.118 1.00 51.61 C ANISOU 3039 CD PRO A1086 6728 5174 7707 -716 159 -49 C ATOM 3040 N VAL A1087 1.509 -15.464 -42.515 1.00 46.89 N ANISOU 3040 N VAL A1087 6472 4629 6713 -282 -11 -173 N ATOM 3041 CA VAL A1087 2.706 -14.789 -42.981 1.00 45.77 C ANISOU 3041 CA VAL A1087 6410 4611 6367 -124 -29 -220 C ATOM 3042 C VAL A1087 3.852 -15.093 -42.016 1.00 46.55 C ANISOU 3042 C VAL A1087 6590 4683 6411 -64 35 -62 C ATOM 3043 O VAL A1087 4.879 -15.648 -42.430 1.00 47.83 O ANISOU 3043 O VAL A1087 6822 4771 6580 44 -12 -120 O ATOM 3044 CB VAL A1087 2.505 -13.265 -43.082 1.00 43.59 C ANISOU 3044 CB VAL A1087 6080 4553 5926 -95 -11 -233 C ATOM 3045 CG1 VAL A1087 3.740 -12.617 -43.687 1.00 42.76 C ANISOU 3045 CG1 VAL A1087 6054 4561 5630 33 -29 -271 C ATOM 3046 CG2 VAL A1087 1.261 -12.939 -43.899 1.00 43.89 C ANISOU 3046 CG2 VAL A1087 6025 4608 6043 -151 -108 -364 C ATOM 3047 N TYR A1088 3.656 -14.746 -40.739 1.00 45.75 N ANISOU 3047 N TYR A1088 6471 4655 6257 -130 136 116 N ATOM 3048 CA TYR A1088 4.638 -15.008 -39.677 1.00 45.50 C ANISOU 3048 CA TYR A1088 6521 4612 6153 -84 172 291 C ATOM 3049 C TYR A1088 5.058 -16.479 -39.630 1.00 46.25 C ANISOU 3049 C TYR A1088 6698 4445 6427 -76 97 353 C ATOM 3050 O TYR A1088 6.249 -16.793 -39.609 1.00 45.01 O ANISOU 3050 O TYR A1088 6605 4236 6260 56 37 361 O ATOM 3051 CB TYR A1088 4.071 -14.587 -38.317 1.00 46.62 C ANISOU 3051 CB TYR A1088 6636 4875 6200 -194 293 463 C ATOM 3052 CG TYR A1088 4.981 -14.876 -37.131 1.00 48.16 C ANISOU 3052 CG TYR A1088 6934 5078 6286 -163 306 665 C ATOM 3053 CD1 TYR A1088 5.934 -13.950 -36.712 1.00 47.15 C ANISOU 3053 CD1 TYR A1088 6824 5120 5968 -51 304 665 C ATOM 3054 CD2 TYR A1088 4.873 -16.073 -36.421 1.00 50.59 C ANISOU 3054 CD2 TYR A1088 7324 5211 6688 -255 299 867 C ATOM 3055 CE1 TYR A1088 6.763 -14.216 -35.634 1.00 48.58 C ANISOU 3055 CE1 TYR A1088 7097 5316 6043 -15 280 839 C ATOM 3056 CE2 TYR A1088 5.694 -16.344 -35.345 1.00 51.69 C ANISOU 3056 CE2 TYR A1088 7573 5355 6710 -222 274 1073 C ATOM 3057 CZ TYR A1088 6.634 -15.415 -34.956 1.00 51.08 C ANISOU 3057 CZ TYR A1088 7507 5468 6431 -95 259 1048 C ATOM 3058 OH TYR A1088 7.448 -15.694 -33.887 1.00 54.83 O ANISOU 3058 OH TYR A1088 8090 5954 6785 -56 201 1244 O ATOM 3059 N ASP A1089 4.079 -17.376 -39.631 1.00 47.96 N ANISOU 3059 N ASP A1089 6898 4483 6841 -216 86 386 N ATOM 3060 CA ASP A1089 4.363 -18.815 -39.580 1.00 51.13 C ANISOU 3060 CA ASP A1089 7378 4576 7469 -225 -9 452 C ATOM 3061 C ASP A1089 5.326 -19.275 -40.678 1.00 51.07 C ANISOU 3061 C ASP A1089 7403 4455 7545 -40 -135 228 C ATOM 3062 O ASP A1089 6.154 -20.152 -40.438 1.00 51.86 O ANISOU 3062 O ASP A1089 7575 4355 7772 47 -222 281 O ATOM 3063 CB ASP A1089 3.071 -19.637 -39.657 1.00 53.66 C ANISOU 3063 CB ASP A1089 7649 4707 8030 -424 -12 473 C ATOM 3064 CG ASP A1089 2.261 -19.600 -38.363 1.00 56.04 C ANISOU 3064 CG ASP A1089 7928 5071 8291 -630 131 745 C ATOM 3065 OD1 ASP A1089 2.797 -19.211 -37.297 1.00 57.11 O ANISOU 3065 OD1 ASP A1089 8131 5345 8219 -612 205 944 O ATOM 3066 OD2 ASP A1089 1.070 -19.975 -38.413 1.00 58.64 O ANISOU 3066 OD2 ASP A1089 8162 5324 8791 -820 174 749 O ATOM 3067 N SER A1090 5.223 -18.675 -41.868 1.00 50.13 N ANISOU 3067 N SER A1090 7227 4471 7346 20 -146 -22 N ATOM 3068 CA SER A1090 6.056 -19.063 -43.017 1.00 49.77 C ANISOU 3068 CA SER A1090 7199 4377 7334 181 -231 -275 C ATOM 3069 C SER A1090 7.475 -18.479 -42.989 1.00 49.18 C ANISOU 3069 C SER A1090 7133 4466 7086 351 -196 -293 C ATOM 3070 O SER A1090 8.344 -18.932 -43.741 1.00 49.98 O ANISOU 3070 O SER A1090 7232 4525 7232 495 -242 -488 O ATOM 3071 CB SER A1090 5.373 -18.673 -44.332 1.00 48.52 C ANISOU 3071 CB SER A1090 6995 4326 7114 161 -263 -523 C ATOM 3072 OG SER A1090 5.662 -17.338 -44.698 1.00 45.71 O ANISOU 3072 OG SER A1090 6618 4266 6484 208 -197 -549 O ATOM 3073 N LEU A1091 7.712 -17.482 -42.137 1.00 47.80 N ANISOU 3073 N LEU A1091 6950 4483 6729 335 -112 -116 N ATOM 3074 CA LEU A1091 8.991 -16.786 -42.127 1.00 47.09 C ANISOU 3074 CA LEU A1091 6841 4565 6486 470 -80 -138 C ATOM 3075 C LEU A1091 10.014 -17.443 -41.219 1.00 49.38 C ANISOU 3075 C LEU A1091 7162 4728 6872 570 -139 -12 C ATOM 3076 O LEU A1091 9.661 -18.049 -40.206 1.00 51.35 O ANISOU 3076 O LEU A1091 7474 4824 7213 501 -178 196 O ATOM 3077 CB LEU A1091 8.797 -15.345 -41.694 1.00 44.83 C ANISOU 3077 CB LEU A1091 6523 4526 5981 413 5 -42 C ATOM 3078 CG LEU A1091 7.933 -14.497 -42.615 1.00 43.78 C ANISOU 3078 CG LEU A1091 6356 4527 5750 344 30 -155 C ATOM 3079 CD1 LEU A1091 7.916 -13.075 -42.080 1.00 42.51 C ANISOU 3079 CD1 LEU A1091 6162 4566 5421 314 91 -60 C ATOM 3080 CD2 LEU A1091 8.449 -14.527 -44.043 1.00 44.02 C ANISOU 3080 CD2 LEU A1091 6383 4617 5725 424 9 -372 C ATOM 3081 N ASP A1092 11.284 -17.309 -41.598 1.00 50.27 N ANISOU 3081 N ASP A1092 7222 4915 6960 727 -147 -135 N ATOM 3082 CA ASP A1092 12.400 -17.776 -40.782 1.00 52.07 C ANISOU 3082 CA ASP A1092 7449 5053 7280 853 -229 -39 C ATOM 3083 C ASP A1092 12.602 -16.858 -39.586 1.00 50.73 C ANISOU 3083 C ASP A1092 7292 5050 6932 809 -204 181 C ATOM 3084 O ASP A1092 11.963 -15.807 -39.484 1.00 47.94 O ANISOU 3084 O ASP A1092 6934 4884 6397 698 -108 220 O ATOM 3085 CB ASP A1092 13.691 -17.863 -41.610 1.00 54.83 C ANISOU 3085 CB ASP A1092 7692 5462 7679 1036 -231 -279 C ATOM 3086 CG ASP A1092 14.244 -16.496 -42.013 1.00 54.91 C ANISOU 3086 CG ASP A1092 7611 5793 7458 1031 -107 -347 C ATOM 3087 OD1 ASP A1092 13.452 -15.565 -42.261 1.00 54.81 O ANISOU 3087 OD1 ASP A1092 7624 5932 7267 900 -24 -311 O ATOM 3088 OD2 ASP A1092 15.485 -16.361 -42.102 1.00 57.71 O ANISOU 3088 OD2 ASP A1092 7857 6234 7835 1158 -101 -437 O ATOM 3089 N ALA A1093 13.501 -17.261 -38.693 1.00 52.55 N ANISOU 3089 N ALA A1093 7537 5204 7224 909 -311 305 N ATOM 3090 CA ALA A1093 13.722 -16.559 -37.428 1.00 52.57 C ANISOU 3090 CA ALA A1093 7573 5348 7053 875 -324 513 C ATOM 3091 C ALA A1093 13.971 -15.068 -37.619 1.00 51.74 C ANISOU 3091 C ALA A1093 7378 5533 6745 853 -219 423 C ATOM 3092 O ALA A1093 13.411 -14.241 -36.887 1.00 51.76 O ANISOU 3092 O ALA A1093 7414 5677 6572 748 -166 533 O ATOM 3093 CB ALA A1093 14.892 -17.180 -36.690 1.00 54.42 C ANISOU 3093 CB ALA A1093 7810 5472 7393 1027 -495 605 C ATOM 3094 N VAL A1094 14.808 -14.734 -38.601 1.00 50.92 N ANISOU 3094 N VAL A1094 7156 5514 6674 946 -184 219 N ATOM 3095 CA VAL A1094 15.206 -13.348 -38.844 1.00 48.58 C ANISOU 3095 CA VAL A1094 6771 5462 6224 918 -99 152 C ATOM 3096 C VAL A1094 14.056 -12.523 -39.395 1.00 45.56 C ANISOU 3096 C VAL A1094 6420 5174 5716 777 8 129 C ATOM 3097 O VAL A1094 13.766 -11.457 -38.876 1.00 45.25 O ANISOU 3097 O VAL A1094 6380 5262 5550 703 37 193 O ATOM 3098 CB VAL A1094 16.378 -13.264 -39.833 1.00 49.86 C ANISOU 3098 CB VAL A1094 6789 5701 6451 1024 -61 -47 C ATOM 3099 CG1 VAL A1094 16.698 -11.813 -40.161 1.00 48.45 C ANISOU 3099 CG1 VAL A1094 6529 5752 6127 951 34 -82 C ATOM 3100 CG2 VAL A1094 17.597 -13.968 -39.261 1.00 52.31 C ANISOU 3100 CG2 VAL A1094 7024 5928 6922 1187 -187 -51 C ATOM 3101 N ARG A1095 13.411 -13.012 -40.449 1.00 44.59 N ANISOU 3101 N ARG A1095 6317 4980 5642 751 44 19 N ATOM 3102 CA ARG A1095 12.283 -12.293 -41.045 1.00 43.18 C ANISOU 3102 CA ARG A1095 6163 4877 5366 631 107 -6 C ATOM 3103 C ARG A1095 11.072 -12.224 -40.114 1.00 41.33 C ANISOU 3103 C ARG A1095 5986 4599 5115 523 106 134 C ATOM 3104 O ARG A1095 10.278 -11.298 -40.192 1.00 39.74 O ANISOU 3104 O ARG A1095 5772 4494 4834 441 145 134 O ATOM 3105 CB ARG A1095 11.877 -12.914 -42.385 1.00 44.59 C ANISOU 3105 CB ARG A1095 6354 4997 5591 634 115 -173 C ATOM 3106 CG ARG A1095 12.928 -12.765 -43.477 1.00 45.42 C ANISOU 3106 CG ARG A1095 6391 5221 5644 712 166 -342 C ATOM 3107 CD ARG A1095 12.385 -13.156 -44.844 1.00 46.02 C ANISOU 3107 CD ARG A1095 6499 5301 5686 696 178 -521 C ATOM 3108 NE ARG A1095 13.331 -12.830 -45.905 1.00 45.67 N ANISOU 3108 NE ARG A1095 6394 5438 5520 741 265 -672 N ATOM 3109 CZ ARG A1095 14.262 -13.651 -46.379 1.00 47.98 C ANISOU 3109 CZ ARG A1095 6620 5725 5886 862 296 -858 C ATOM 3110 NH1 ARG A1095 15.068 -13.228 -47.336 1.00 50.35 N ANISOU 3110 NH1 ARG A1095 6849 6241 6038 875 414 -990 N ATOM 3111 NH2 ARG A1095 14.398 -14.888 -45.919 1.00 49.76 N ANISOU 3111 NH2 ARG A1095 6840 5726 6339 968 212 -915 N ATOM 3112 N ARG A1096 10.921 -13.209 -39.243 1.00 41.92 N ANISOU 3112 N ARG A1096 6118 4532 5276 520 62 255 N ATOM 3113 CA ARG A1096 9.891 -13.129 -38.217 1.00 42.33 C ANISOU 3113 CA ARG A1096 6212 4590 5280 401 96 406 C ATOM 3114 C ARG A1096 10.098 -11.891 -37.369 1.00 40.75 C ANISOU 3114 C ARG A1096 5986 4587 4907 391 130 453 C ATOM 3115 O ARG A1096 9.148 -11.169 -37.072 1.00 39.31 O ANISOU 3115 O ARG A1096 5780 4500 4654 302 197 453 O ATOM 3116 CB ARG A1096 9.893 -14.375 -37.325 1.00 44.62 C ANISOU 3116 CB ARG A1096 6588 4704 5659 386 40 581 C ATOM 3117 CG ARG A1096 9.108 -15.520 -37.922 1.00 45.96 C ANISOU 3117 CG ARG A1096 6785 4652 6025 324 19 557 C ATOM 3118 CD ARG A1096 9.239 -16.797 -37.117 1.00 49.09 C ANISOU 3118 CD ARG A1096 7278 4823 6551 309 -63 754 C ATOM 3119 NE ARG A1096 8.331 -17.814 -37.638 1.00 50.71 N ANISOU 3119 NE ARG A1096 7498 4797 6970 213 -82 733 N ATOM 3120 CZ ARG A1096 8.245 -19.060 -37.195 1.00 52.83 C ANISOU 3120 CZ ARG A1096 7851 4795 7426 169 -168 892 C ATOM 3121 NH1 ARG A1096 9.019 -19.492 -36.209 1.00 54.93 N ANISOU 3121 NH1 ARG A1096 8209 4985 7674 225 -258 1106 N ATOM 3122 NH2 ARG A1096 7.374 -19.883 -37.751 1.00 54.81 N ANISOU 3122 NH2 ARG A1096 8095 4833 7894 66 -187 840 N ATOM 3123 N ALA A1097 11.345 -11.654 -36.978 1.00 40.58 N ANISOU 3123 N ALA A1097 5953 4622 4843 490 73 467 N ATOM 3124 CA ALA A1097 11.665 -10.520 -36.135 1.00 40.00 C ANISOU 3124 CA ALA A1097 5854 4719 4623 487 76 486 C ATOM 3125 C ALA A1097 11.291 -9.230 -36.839 1.00 39.28 C ANISOU 3125 C ALA A1097 5691 4734 4500 447 131 362 C ATOM 3126 O ALA A1097 10.722 -8.328 -36.224 1.00 39.67 O ANISOU 3126 O ALA A1097 5725 4883 4464 396 162 355 O ATOM 3127 CB ALA A1097 13.135 -10.524 -35.769 1.00 40.45 C ANISOU 3127 CB ALA A1097 5881 4803 4683 603 -19 494 C ATOM 3128 N ALA A1098 11.584 -9.149 -38.135 1.00 39.31 N ANISOU 3128 N ALA A1098 5655 4713 4567 471 138 261 N ATOM 3129 CA ALA A1098 11.244 -7.948 -38.908 1.00 39.62 C ANISOU 3129 CA ALA A1098 5649 4828 4575 425 163 183 C ATOM 3130 C ALA A1098 9.743 -7.706 -38.915 1.00 38.55 C ANISOU 3130 C ALA A1098 5523 4676 4446 344 188 175 C ATOM 3131 O ALA A1098 9.303 -6.570 -38.820 1.00 39.55 O ANISOU 3131 O ALA A1098 5612 4864 4550 314 184 142 O ATOM 3132 CB ALA A1098 11.772 -8.038 -40.336 1.00 40.35 C ANISOU 3132 CB ALA A1098 5721 4920 4688 446 176 100 C ATOM 3133 N LEU A1099 8.962 -8.772 -39.028 1.00 38.15 N ANISOU 3133 N LEU A1099 5505 4528 4459 311 204 192 N ATOM 3134 CA LEU A1099 7.516 -8.643 -38.972 1.00 37.44 C ANISOU 3134 CA LEU A1099 5387 4428 4407 228 232 174 C ATOM 3135 C LEU A1099 7.099 -8.101 -37.615 1.00 37.42 C ANISOU 3135 C LEU A1099 5358 4522 4337 193 287 219 C ATOM 3136 O LEU A1099 6.141 -7.353 -37.526 1.00 37.78 O ANISOU 3136 O LEU A1099 5333 4619 4401 154 311 153 O ATOM 3137 CB LEU A1099 6.822 -9.982 -39.240 1.00 37.66 C ANISOU 3137 CB LEU A1099 5442 4320 4546 178 238 190 C ATOM 3138 CG LEU A1099 5.306 -9.897 -39.419 1.00 38.10 C ANISOU 3138 CG LEU A1099 5430 4362 4684 83 258 143 C ATOM 3139 CD1 LEU A1099 4.959 -8.967 -40.570 1.00 39.15 C ANISOU 3139 CD1 LEU A1099 5521 4533 4820 104 186 25 C ATOM 3140 CD2 LEU A1099 4.699 -11.260 -39.675 1.00 39.62 C ANISOU 3140 CD2 LEU A1099 5637 4397 5016 15 251 156 C ATOM 3141 N ILE A1100 7.813 -8.479 -36.561 1.00 38.06 N ANISOU 3141 N ILE A1100 5489 4635 4334 215 297 316 N ATOM 3142 CA ILE A1100 7.499 -7.979 -35.228 1.00 39.14 C ANISOU 3142 CA ILE A1100 5618 4905 4349 183 353 345 C ATOM 3143 C ILE A1100 7.923 -6.521 -35.073 1.00 39.13 C ANISOU 3143 C ILE A1100 5561 5010 4295 235 316 233 C ATOM 3144 O ILE A1100 7.260 -5.747 -34.382 1.00 39.43 O ANISOU 3144 O ILE A1100 5545 5152 4282 212 363 156 O ATOM 3145 CB ILE A1100 8.140 -8.828 -34.119 1.00 39.76 C ANISOU 3145 CB ILE A1100 5792 4997 4318 188 344 503 C ATOM 3146 CG1 ILE A1100 7.455 -10.195 -34.057 1.00 40.51 C ANISOU 3146 CG1 ILE A1100 5942 4966 4483 99 388 638 C ATOM 3147 CG2 ILE A1100 8.020 -8.116 -32.775 1.00 40.59 C ANISOU 3147 CG2 ILE A1100 5899 5293 4230 168 390 501 C ATOM 3148 CD1 ILE A1100 8.186 -11.213 -33.205 1.00 42.22 C ANISOU 3148 CD1 ILE A1100 6279 5123 4636 113 329 836 C ATOM 3149 N ASN A1101 9.023 -6.145 -35.709 1.00 39.00 N ANISOU 3149 N ASN A1101 5545 4965 4308 299 236 210 N ATOM 3150 CA ASN A1101 9.452 -4.756 -35.683 1.00 39.22 C ANISOU 3150 CA ASN A1101 5516 5051 4333 326 185 116 C ATOM 3151 C ASN A1101 8.336 -3.839 -36.198 1.00 39.28 C ANISOU 3151 C ASN A1101 5461 5039 4425 295 189 17 C ATOM 3152 O ASN A1101 8.079 -2.775 -35.638 1.00 41.56 O ANISOU 3152 O ASN A1101 5695 5377 4717 306 169 -81 O ATOM 3153 CB ASN A1101 10.719 -4.582 -36.511 1.00 39.74 C ANISOU 3153 CB ASN A1101 5572 5082 4445 365 124 124 C ATOM 3154 CG ASN A1101 11.507 -3.356 -36.114 1.00 41.70 C ANISOU 3154 CG ASN A1101 5767 5384 4692 379 60 65 C ATOM 3155 OD1 ASN A1101 10.940 -2.300 -35.833 1.00 42.77 O ANISOU 3155 OD1 ASN A1101 5867 5531 4850 361 39 -17 O ATOM 3156 ND2 ASN A1101 12.833 -3.487 -36.094 1.00 43.54 N ANISOU 3156 ND2 ASN A1101 5976 5635 4931 416 16 88 N ATOM 3157 N MET A1102 7.649 -4.277 -37.246 1.00 37.59 N ANISOU 3157 N MET A1102 5246 4743 4291 266 193 25 N ATOM 3158 CA MET A1102 6.567 -3.497 -37.824 1.00 36.52 C ANISOU 3158 CA MET A1102 5046 4572 4256 249 156 -58 C ATOM 3159 C MET A1102 5.373 -3.420 -36.899 1.00 36.22 C ANISOU 3159 C MET A1102 4928 4596 4238 227 230 -135 C ATOM 3160 O MET A1102 4.767 -2.363 -36.747 1.00 36.85 O ANISOU 3160 O MET A1102 4920 4684 4394 251 195 -254 O ATOM 3161 CB MET A1102 6.130 -4.097 -39.155 1.00 36.59 C ANISOU 3161 CB MET A1102 5080 4498 4324 225 121 -37 C ATOM 3162 CG MET A1102 7.203 -4.023 -40.216 1.00 36.72 C ANISOU 3162 CG MET A1102 5160 4492 4298 240 71 8 C ATOM 3163 SD MET A1102 6.568 -4.533 -41.809 1.00 40.44 S ANISOU 3163 SD MET A1102 5671 4905 4789 214 11 -7 S ATOM 3164 CE MET A1102 5.410 -3.212 -42.147 1.00 40.37 C ANISOU 3164 CE MET A1102 5602 4858 4878 206 -111 -50 C ATOM 3165 N VAL A1103 5.031 -4.544 -36.290 1.00 36.15 N ANISOU 3165 N VAL A1103 4938 4622 4173 176 334 -70 N ATOM 3166 CA VAL A1103 3.878 -4.598 -35.408 1.00 37.47 C ANISOU 3166 CA VAL A1103 5015 4882 4339 123 448 -130 C ATOM 3167 C VAL A1103 4.173 -3.845 -34.120 1.00 38.26 C ANISOU 3167 C VAL A1103 5099 5134 4302 154 497 -202 C ATOM 3168 O VAL A1103 3.291 -3.212 -33.553 1.00 39.46 O ANISOU 3168 O VAL A1103 5135 5382 4474 153 564 -348 O ATOM 3169 CB VAL A1103 3.470 -6.049 -35.112 1.00 37.99 C ANISOU 3169 CB VAL A1103 5119 4934 4381 26 552 -1 C ATOM 3170 CG1 VAL A1103 2.307 -6.096 -34.131 1.00 39.88 C ANISOU 3170 CG1 VAL A1103 5249 5307 4596 -59 711 -47 C ATOM 3171 CG2 VAL A1103 3.084 -6.736 -36.410 1.00 38.02 C ANISOU 3171 CG2 VAL A1103 5121 4781 4541 1 484 12 C ATOM 3172 N PHE A1104 5.418 -3.907 -33.669 1.00 38.19 N ANISOU 3172 N PHE A1104 5193 5155 4162 191 453 -125 N ATOM 3173 CA PHE A1104 5.832 -3.154 -32.503 1.00 39.53 C ANISOU 3173 CA PHE A1104 5360 5469 4189 228 459 -214 C ATOM 3174 C PHE A1104 5.676 -1.668 -32.782 1.00 40.07 C ANISOU 3174 C PHE A1104 5330 5504 4391 293 373 -412 C ATOM 3175 O PHE A1104 5.211 -0.911 -31.926 1.00 43.13 O ANISOU 3175 O PHE A1104 5641 6005 4740 318 412 -587 O ATOM 3176 CB PHE A1104 7.287 -3.464 -32.140 1.00 39.42 C ANISOU 3176 CB PHE A1104 5457 5465 4052 266 376 -103 C ATOM 3177 CG PHE A1104 7.684 -3.004 -30.763 1.00 39.92 C ANISOU 3177 CG PHE A1104 5544 5707 3915 290 376 -172 C ATOM 3178 CD1 PHE A1104 8.081 -1.694 -30.540 1.00 40.14 C ANISOU 3178 CD1 PHE A1104 5513 5761 3976 351 286 -358 C ATOM 3179 CD2 PHE A1104 7.662 -3.881 -29.697 1.00 41.15 C ANISOU 3179 CD2 PHE A1104 5791 5998 3844 243 450 -47 C ATOM 3180 CE1 PHE A1104 8.447 -1.271 -29.279 1.00 41.46 C ANISOU 3180 CE1 PHE A1104 5702 6101 3947 378 268 -458 C ATOM 3181 CE2 PHE A1104 8.025 -3.465 -28.431 1.00 43.01 C ANISOU 3181 CE2 PHE A1104 6066 6429 3846 264 437 -115 C ATOM 3182 CZ PHE A1104 8.419 -2.159 -28.222 1.00 43.02 C ANISOU 3182 CZ PHE A1104 5998 6470 3875 338 345 -341 C ATOM 3183 N GLN A1105 6.057 -1.254 -33.983 1.00 39.06 N ANISOU 3183 N GLN A1105 5206 5217 4418 317 252 -386 N ATOM 3184 CA GLN A1105 6.014 0.163 -34.348 1.00 39.46 C ANISOU 3184 CA GLN A1105 5186 5181 4623 367 132 -524 C ATOM 3185 C GLN A1105 4.595 0.671 -34.603 1.00 39.01 C ANISOU 3185 C GLN A1105 5005 5087 4730 385 134 -664 C ATOM 3186 O GLN A1105 4.179 1.651 -33.998 1.00 39.70 O ANISOU 3186 O GLN A1105 4997 5198 4889 440 111 -859 O ATOM 3187 CB GLN A1105 6.881 0.400 -35.579 1.00 39.38 C ANISOU 3187 CB GLN A1105 5233 5029 4699 359 15 -408 C ATOM 3188 CG GLN A1105 7.096 1.852 -35.945 1.00 40.82 C ANISOU 3188 CG GLN A1105 5374 5093 5041 383 -129 -486 C ATOM 3189 CD GLN A1105 8.079 2.016 -37.087 1.00 42.55 C ANISOU 3189 CD GLN A1105 5658 5213 5294 338 -207 -334 C ATOM 3190 OE1 GLN A1105 8.715 1.045 -37.527 1.00 45.31 O ANISOU 3190 OE1 GLN A1105 6069 5606 5539 309 -144 -209 O ATOM 3191 NE2 GLN A1105 8.212 3.245 -37.580 1.00 43.65 N ANISOU 3191 NE2 GLN A1105 5778 5216 5588 329 -340 -345 N ATOM 3192 N MET A1106 3.864 -0.014 -35.480 1.00 38.72 N ANISOU 3192 N MET A1106 4957 4989 4766 347 147 -587 N ATOM 3193 CA MET A1106 2.583 0.470 -36.011 1.00 40.12 C ANISOU 3193 CA MET A1106 5004 5094 5145 373 93 -704 C ATOM 3194 C MET A1106 1.342 -0.250 -35.493 1.00 40.20 C ANISOU 3194 C MET A1106 4890 5214 5166 329 248 -779 C ATOM 3195 O MET A1106 0.220 0.124 -35.818 1.00 39.31 O ANISOU 3195 O MET A1106 4628 5063 5244 357 209 -907 O ATOM 3196 CB MET A1106 2.610 0.336 -37.524 1.00 41.17 C ANISOU 3196 CB MET A1106 5200 5076 5366 358 -45 -579 C ATOM 3197 CG MET A1106 3.650 1.228 -38.165 1.00 42.79 C ANISOU 3197 CG MET A1106 5497 5172 5589 378 -191 -503 C ATOM 3198 SD MET A1106 3.638 1.030 -39.946 1.00 45.78 S ANISOU 3198 SD MET A1106 5969 5432 5993 341 -329 -347 S ATOM 3199 CE MET A1106 4.309 -0.622 -40.051 1.00 44.63 C ANISOU 3199 CE MET A1106 5922 5383 5651 281 -176 -233 C ATOM 3200 N GLY A1107 1.543 -1.287 -34.698 1.00 40.71 N ANISOU 3200 N GLY A1107 5011 5412 5043 253 416 -687 N ATOM 3201 CA GLY A1107 0.445 -2.092 -34.221 1.00 42.64 C ANISOU 3201 CA GLY A1107 5150 5762 5288 168 587 -707 C ATOM 3202 C GLY A1107 0.067 -3.210 -35.165 1.00 42.54 C ANISOU 3202 C GLY A1107 5162 5638 5361 87 571 -571 C ATOM 3203 O GLY A1107 0.441 -3.226 -36.325 1.00 42.14 O ANISOU 3203 O GLY A1107 5187 5440 5384 118 416 -508 O ATOM 3204 N GLU A1108 -0.688 -4.150 -34.627 1.00 45.64 N ANISOU 3204 N GLU A1108 5491 6114 5735 -27 739 -532 N ATOM 3205 CA GLU A1108 -1.223 -5.288 -35.354 1.00 48.10 C ANISOU 3205 CA GLU A1108 5795 6316 6161 -126 737 -433 C ATOM 3206 C GLU A1108 -2.097 -4.871 -36.545 1.00 46.79 C ANISOU 3206 C GLU A1108 5497 6034 6245 -84 580 -562 C ATOM 3207 O GLU A1108 -1.861 -5.300 -37.669 1.00 46.07 O ANISOU 3207 O GLU A1108 5494 5800 6209 -78 436 -497 O ATOM 3208 CB GLU A1108 -2.022 -6.123 -34.353 1.00 53.13 C ANISOU 3208 CB GLU A1108 6343 7084 6757 -279 968 -387 C ATOM 3209 CG GLU A1108 -2.854 -7.263 -34.893 1.00 57.45 C ANISOU 3209 CG GLU A1108 6822 7525 7478 -417 995 -319 C ATOM 3210 CD GLU A1108 -3.741 -7.851 -33.804 1.00 65.16 C ANISOU 3210 CD GLU A1108 7672 8660 8423 -592 1253 -280 C ATOM 3211 OE1 GLU A1108 -3.624 -7.415 -32.629 1.00 68.33 O ANISOU 3211 OE1 GLU A1108 8068 9277 8617 -598 1416 -299 O ATOM 3212 OE2 GLU A1108 -4.567 -8.744 -34.113 1.00 71.54 O ANISOU 3212 OE2 GLU A1108 8382 9390 9409 -737 1298 -236 O ATOM 3213 N THR A1109 -3.094 -4.026 -36.296 1.00 46.37 N ANISOU 3213 N THR A1109 5230 6050 6338 -44 596 -759 N ATOM 3214 CA THR A1109 -4.033 -3.614 -37.343 1.00 45.60 C ANISOU 3214 CA THR A1109 4983 5843 6500 5 418 -886 C ATOM 3215 C THR A1109 -3.425 -2.627 -38.340 1.00 44.32 C ANISOU 3215 C THR A1109 4931 5542 6367 139 158 -884 C ATOM 3216 O THR A1109 -3.986 -2.399 -39.407 1.00 45.72 O ANISOU 3216 O THR A1109 5057 5605 6706 178 -40 -924 O ATOM 3217 CB THR A1109 -5.297 -2.972 -36.747 1.00 46.84 C ANISOU 3217 CB THR A1109 4842 6109 6846 29 501 -1122 C ATOM 3218 OG1 THR A1109 -4.946 -1.769 -36.058 1.00 46.23 O ANISOU 3218 OG1 THR A1109 4745 6099 6719 151 506 -1256 O ATOM 3219 CG2 THR A1109 -5.983 -3.934 -35.786 1.00 48.92 C ANISOU 3219 CG2 THR A1109 4976 6537 7073 -138 789 -1111 C ATOM 3220 N GLY A1110 -2.300 -2.020 -37.985 1.00 42.33 N ANISOU 3220 N GLY A1110 4824 5302 5958 199 152 -830 N ATOM 3221 CA GLY A1110 -1.573 -1.182 -38.916 1.00 40.52 C ANISOU 3221 CA GLY A1110 4720 4941 5733 282 -65 -775 C ATOM 3222 C GLY A1110 -0.896 -2.055 -39.951 1.00 39.00 C ANISOU 3222 C GLY A1110 4709 4681 5427 229 -126 -601 C ATOM 3223 O GLY A1110 -0.997 -1.806 -41.154 1.00 38.32 O ANISOU 3223 O GLY A1110 4672 4496 5390 254 -316 -569 O ATOM 3224 N VAL A1111 -0.219 -3.099 -39.475 1.00 38.36 N ANISOU 3224 N VAL A1111 4728 4658 5188 161 26 -496 N ATOM 3225 CA VAL A1111 0.533 -3.989 -40.351 1.00 36.87 C ANISOU 3225 CA VAL A1111 4699 4410 4900 129 -12 -371 C ATOM 3226 C VAL A1111 -0.398 -4.825 -41.214 1.00 38.43 C ANISOU 3226 C VAL A1111 4850 4541 5209 76 -78 -405 C ATOM 3227 O VAL A1111 -0.039 -5.191 -42.323 1.00 39.60 O ANISOU 3227 O VAL A1111 5106 4631 5307 79 -185 -368 O ATOM 3228 CB VAL A1111 1.481 -4.893 -39.562 1.00 35.98 C ANISOU 3228 CB VAL A1111 4689 4344 4636 91 136 -263 C ATOM 3229 CG1 VAL A1111 2.165 -5.888 -40.484 1.00 35.84 C ANISOU 3229 CG1 VAL A1111 4801 4252 4564 78 95 -184 C ATOM 3230 CG2 VAL A1111 2.528 -4.049 -38.857 1.00 35.73 C ANISOU 3230 CG2 VAL A1111 4709 4376 4489 149 156 -241 C ATOM 3231 N ALA A1112 -1.602 -5.105 -40.725 1.00 40.46 N ANISOU 3231 N ALA A1112 4932 4820 5618 22 -12 -493 N ATOM 3232 CA ALA A1112 -2.604 -5.826 -41.517 1.00 41.49 C ANISOU 3232 CA ALA A1112 4977 4881 5903 -36 -98 -554 C ATOM 3233 C ALA A1112 -2.993 -5.034 -42.766 1.00 42.02 C ANISOU 3233 C ALA A1112 5037 4885 6043 42 -356 -619 C ATOM 3234 O ALA A1112 -3.607 -5.573 -43.686 1.00 42.59 O ANISOU 3234 O ALA A1112 5086 4897 6199 13 -490 -668 O ATOM 3235 CB ALA A1112 -3.838 -6.113 -40.673 1.00 42.94 C ANISOU 3235 CB ALA A1112 4930 5121 6262 -120 36 -645 C ATOM 3236 N GLY A1113 -2.655 -3.746 -42.775 1.00 41.62 N ANISOU 3236 N GLY A1113 5007 4837 5967 138 -443 -616 N ATOM 3237 CA GLY A1113 -2.943 -2.878 -43.902 1.00 42.69 C ANISOU 3237 CA GLY A1113 5165 4898 6156 211 -708 -627 C ATOM 3238 C GLY A1113 -2.030 -3.113 -45.084 1.00 42.00 C ANISOU 3238 C GLY A1113 5307 4790 5858 202 -812 -504 C ATOM 3239 O GLY A1113 -2.391 -2.797 -46.216 1.00 42.87 O ANISOU 3239 O GLY A1113 5463 4857 5966 226 -1039 -496 O ATOM 3240 N PHE A1114 -0.848 -3.669 -44.836 1.00 40.59 N ANISOU 3240 N PHE A1114 5268 4659 5494 169 -653 -415 N ATOM 3241 CA PHE A1114 0.078 -4.000 -45.922 1.00 41.75 C ANISOU 3241 CA PHE A1114 5606 4822 5432 157 -703 -332 C ATOM 3242 C PHE A1114 -0.388 -5.270 -46.667 1.00 42.75 C ANISOU 3242 C PHE A1114 5749 4933 5557 112 -744 -412 C ATOM 3243 O PHE A1114 0.356 -6.239 -46.792 1.00 43.65 O ANISOU 3243 O PHE A1114 5956 5063 5565 89 -641 -408 O ATOM 3244 CB PHE A1114 1.506 -4.191 -45.376 1.00 40.29 C ANISOU 3244 CB PHE A1114 5522 4691 5094 153 -524 -245 C ATOM 3245 CG PHE A1114 2.125 -2.940 -44.820 1.00 39.69 C ANISOU 3245 CG PHE A1114 5449 4624 5006 186 -514 -176 C ATOM 3246 CD1 PHE A1114 1.912 -2.571 -43.500 1.00 39.68 C ANISOU 3246 CD1 PHE A1114 5335 4630 5110 207 -419 -223 C ATOM 3247 CD2 PHE A1114 2.932 -2.138 -45.611 1.00 39.83 C ANISOU 3247 CD2 PHE A1114 5581 4649 4904 185 -595 -71 C ATOM 3248 CE1 PHE A1114 2.483 -1.424 -42.975 1.00 39.28 C ANISOU 3248 CE1 PHE A1114 5282 4573 5068 241 -430 -198 C ATOM 3249 CE2 PHE A1114 3.512 -0.991 -45.092 1.00 40.20 C ANISOU 3249 CE2 PHE A1114 5622 4672 4981 199 -599 -12 C ATOM 3250 CZ PHE A1114 3.288 -0.633 -43.770 1.00 39.57 C ANISOU 3250 CZ PHE A1114 5426 4578 5029 236 -529 -90 C ATOM 3251 N THR A1115 -1.611 -5.254 -47.182 1.00 44.13 N ANISOU 3251 N THR A1115 5824 5066 5875 109 -915 -505 N ATOM 3252 CA THR A1115 -2.252 -6.472 -47.664 1.00 46.10 C ANISOU 3252 CA THR A1115 6038 5279 6196 54 -959 -618 C ATOM 3253 C THR A1115 -1.374 -7.237 -48.638 1.00 46.18 C ANISOU 3253 C THR A1115 6239 5320 5985 48 -971 -624 C ATOM 3254 O THR A1115 -1.142 -8.429 -48.454 1.00 47.44 O ANISOU 3254 O THR A1115 6411 5436 6175 8 -865 -681 O ATOM 3255 CB THR A1115 -3.598 -6.155 -48.330 1.00 49.31 C ANISOU 3255 CB THR A1115 6318 5648 6767 65 -1207 -723 C ATOM 3256 OG1 THR A1115 -4.489 -5.589 -47.359 1.00 51.40 O ANISOU 3256 OG1 THR A1115 6355 5891 7281 76 -1167 -769 O ATOM 3257 CG2 THR A1115 -4.226 -7.397 -48.904 1.00 51.39 C ANISOU 3257 CG2 THR A1115 6544 5866 7114 0 -1281 -859 C ATOM 3258 N ASN A1116 -0.865 -6.544 -49.652 1.00 46.31 N ANISOU 3258 N ASN A1116 6403 5411 5782 84 -1094 -565 N ATOM 3259 CA ASN A1116 -0.079 -7.188 -50.709 1.00 47.29 C ANISOU 3259 CA ASN A1116 6697 5612 5659 81 -1100 -605 C ATOM 3260 C ASN A1116 1.392 -7.428 -50.385 1.00 44.67 C ANISOU 3260 C ASN A1116 6457 5340 5174 92 -878 -541 C ATOM 3261 O ASN A1116 1.922 -8.504 -50.664 1.00 44.53 O ANISOU 3261 O ASN A1116 6490 5329 5099 96 -799 -646 O ATOM 3262 CB ASN A1116 -0.216 -6.417 -52.020 1.00 49.77 C ANISOU 3262 CB ASN A1116 7137 6014 5758 93 -1324 -562 C ATOM 3263 CG ASN A1116 -1.442 -6.832 -52.790 1.00 53.52 C ANISOU 3263 CG ASN A1116 7566 6456 6310 86 -1572 -707 C ATOM 3264 OD1 ASN A1116 -1.659 -8.028 -53.031 1.00 58.07 O ANISOU 3264 OD1 ASN A1116 8126 7007 6932 63 -1566 -882 O ATOM 3265 ND2 ASN A1116 -2.261 -5.865 -53.168 1.00 55.21 N ANISOU 3265 ND2 ASN A1116 7751 6651 6572 112 -1815 -648 N ATOM 3266 N SER A1117 2.052 -6.437 -49.801 1.00 42.52 N ANISOU 3266 N SER A1117 6191 5100 4865 105 -793 -392 N ATOM 3267 CA SER A1117 3.414 -6.637 -49.308 1.00 41.32 C ANISOU 3267 CA SER A1117 6079 4996 4623 118 -590 -340 C ATOM 3268 C SER A1117 3.495 -7.881 -48.408 1.00 40.69 C ANISOU 3268 C SER A1117 5934 4829 4697 126 -459 -415 C ATOM 3269 O SER A1117 4.500 -8.587 -48.417 1.00 41.56 O ANISOU 3269 O SER A1117 6089 4960 4741 154 -347 -446 O ATOM 3270 CB SER A1117 3.918 -5.395 -48.564 1.00 39.86 C ANISOU 3270 CB SER A1117 5869 4821 4452 122 -540 -191 C ATOM 3271 OG SER A1117 3.617 -4.204 -49.289 1.00 40.48 O ANISOU 3271 OG SER A1117 6000 4918 4460 107 -701 -96 O ATOM 3272 N LEU A1118 2.429 -8.158 -47.658 1.00 40.26 N ANISOU 3272 N LEU A1118 5766 4675 4856 97 -478 -441 N ATOM 3273 CA LEU A1118 2.375 -9.335 -46.788 1.00 40.62 C ANISOU 3273 CA LEU A1118 5761 4619 5051 72 -367 -467 C ATOM 3274 C LEU A1118 2.292 -10.630 -47.586 1.00 42.79 C ANISOU 3274 C LEU A1118 6081 4817 5358 64 -420 -609 C ATOM 3275 O LEU A1118 3.071 -11.561 -47.365 1.00 41.19 O ANISOU 3275 O LEU A1118 5921 4553 5174 90 -337 -630 O ATOM 3276 CB LEU A1118 1.185 -9.238 -45.829 1.00 40.22 C ANISOU 3276 CB LEU A1118 5565 4512 5205 13 -351 -451 C ATOM 3277 CG LEU A1118 1.320 -8.188 -44.728 1.00 38.85 C ANISOU 3277 CG LEU A1118 5333 4402 5024 29 -262 -352 C ATOM 3278 CD1 LEU A1118 -0.011 -7.994 -44.025 1.00 39.33 C ANISOU 3278 CD1 LEU A1118 5223 4448 5272 -23 -250 -391 C ATOM 3279 CD2 LEU A1118 2.415 -8.570 -43.745 1.00 38.55 C ANISOU 3279 CD2 LEU A1118 5349 4375 4919 45 -108 -256 C ATOM 3280 N ARG A1119 1.324 -10.676 -48.500 1.00 46.21 N ANISOU 3280 N ARG A1119 6496 5242 5819 36 -584 -722 N ATOM 3281 CA ARG A1119 1.171 -11.784 -49.447 1.00 48.57 C ANISOU 3281 CA ARG A1119 6842 5481 6131 32 -677 -906 C ATOM 3282 C ARG A1119 2.490 -12.126 -50.141 1.00 47.17 C ANISOU 3282 C ARG A1119 6795 5386 5739 107 -614 -974 C ATOM 3283 O ARG A1119 2.801 -13.293 -50.371 1.00 46.97 O ANISOU 3283 O ARG A1119 6794 5266 5783 130 -603 -1119 O ATOM 3284 CB ARG A1119 0.144 -11.418 -50.523 1.00 53.05 C ANISOU 3284 CB ARG A1119 7399 6094 6661 13 -900 -1011 C ATOM 3285 CG ARG A1119 -1.218 -12.089 -50.412 1.00 57.43 C ANISOU 3285 CG ARG A1119 7813 6508 7499 -65 -1015 -1122 C ATOM 3286 CD ARG A1119 -1.693 -12.546 -51.791 1.00 62.46 C ANISOU 3286 CD ARG A1119 8503 7161 8066 -62 -1240 -1333 C ATOM 3287 NE ARG A1119 -1.643 -11.455 -52.772 1.00 66.01 N ANISOU 3287 NE ARG A1119 9054 7790 8235 -10 -1389 -1299 N ATOM 3288 CZ ARG A1119 -1.579 -11.610 -54.098 1.00 72.10 C ANISOU 3288 CZ ARG A1119 9955 8669 8770 14 -1555 -1440 C ATOM 3289 NH1 ARG A1119 -1.553 -12.824 -54.658 1.00 74.04 N ANISOU 3289 NH1 ARG A1119 10233 8859 9037 10 -1599 -1676 N ATOM 3290 NH2 ARG A1119 -1.539 -10.533 -54.879 1.00 73.89 N ANISOU 3290 NH2 ARG A1119 10288 9057 8729 42 -1687 -1343 N ATOM 3291 N MET A1120 3.248 -11.092 -50.495 1.00 45.31 N ANISOU 3291 N MET A1120 6629 5322 5263 142 -575 -881 N ATOM 3292 CA MET A1120 4.504 -11.275 -51.203 1.00 45.07 C ANISOU 3292 CA MET A1120 6691 5421 5010 199 -486 -949 C ATOM 3293 C MET A1120 5.527 -11.936 -50.296 1.00 43.59 C ANISOU 3293 C MET A1120 6467 5156 4938 253 -323 -932 C ATOM 3294 O MET A1120 6.212 -12.862 -50.722 1.00 44.08 O ANISOU 3294 O MET A1120 6553 5206 4989 316 -280 -1095 O ATOM 3295 CB MET A1120 5.022 -9.937 -51.727 1.00 45.19 C ANISOU 3295 CB MET A1120 6774 5631 4762 185 -473 -811 C ATOM 3296 CG MET A1120 4.178 -9.353 -52.849 1.00 46.54 C ANISOU 3296 CG MET A1120 7021 5891 4768 145 -669 -822 C ATOM 3297 SD MET A1120 4.598 -7.640 -53.225 1.00 47.31 S ANISOU 3297 SD MET A1120 7200 6141 4631 100 -689 -570 S ATOM 3298 CE MET A1120 3.290 -7.250 -54.385 1.00 49.39 C ANISOU 3298 CE MET A1120 7546 6436 4783 71 -996 -590 C ATOM 3299 N LEU A1121 5.613 -11.473 -49.048 1.00 41.38 N ANISOU 3299 N LEU A1121 6127 4823 4773 239 -249 -752 N ATOM 3300 CA LEU A1121 6.459 -12.129 -48.044 1.00 40.94 C ANISOU 3300 CA LEU A1121 6040 4674 4840 289 -138 -707 C ATOM 3301 C LEU A1121 6.004 -13.577 -47.827 1.00 41.73 C ANISOU 3301 C LEU A1121 6129 4559 5168 287 -182 -808 C ATOM 3302 O LEU A1121 6.819 -14.502 -47.750 1.00 41.36 O ANISOU 3302 O LEU A1121 6092 4422 5200 364 -150 -884 O ATOM 3303 CB LEU A1121 6.417 -11.378 -46.710 1.00 39.37 C ANISOU 3303 CB LEU A1121 5789 4469 4699 260 -80 -507 C ATOM 3304 CG LEU A1121 6.918 -9.934 -46.670 1.00 39.06 C ANISOU 3304 CG LEU A1121 5748 4587 4506 257 -46 -397 C ATOM 3305 CD1 LEU A1121 6.876 -9.406 -45.246 1.00 38.34 C ANISOU 3305 CD1 LEU A1121 5601 4471 4493 243 2 -257 C ATOM 3306 CD2 LEU A1121 8.327 -9.806 -47.223 1.00 39.79 C ANISOU 3306 CD2 LEU A1121 5864 4802 4451 311 32 -427 C ATOM 3307 N ASN A1122 4.692 -13.761 -47.731 1.00 42.39 N ANISOU 3307 N ASN A1122 6175 4543 5387 198 -268 -811 N ATOM 3308 CA ASN A1122 4.106 -15.092 -47.618 1.00 44.47 C ANISOU 3308 CA ASN A1122 6421 4581 5895 158 -328 -899 C ATOM 3309 C ASN A1122 4.600 -16.002 -48.737 1.00 46.69 C ANISOU 3309 C ASN A1122 6759 4819 6162 237 -392 -1151 C ATOM 3310 O ASN A1122 4.935 -17.151 -48.488 1.00 47.97 O ANISOU 3310 O ASN A1122 6927 4780 6518 273 -402 -1217 O ATOM 3311 CB ASN A1122 2.569 -15.016 -47.637 1.00 44.89 C ANISOU 3311 CB ASN A1122 6394 4577 6082 36 -420 -907 C ATOM 3312 CG ASN A1122 1.914 -16.203 -46.958 1.00 45.70 C ANISOU 3312 CG ASN A1122 6444 4432 6484 -60 -428 -885 C ATOM 3313 OD1 ASN A1122 2.579 -17.161 -46.586 1.00 46.66 O ANISOU 3313 OD1 ASN A1122 6614 4392 6721 -27 -400 -869 O ATOM 3314 ND2 ASN A1122 0.603 -16.138 -46.789 1.00 46.13 N ANISOU 3314 ND2 ASN A1122 6390 4447 6690 -185 -474 -875 N ATOM 3315 N ASN A1123 4.664 -15.461 -49.956 1.00 47.92 N ANISOU 3315 N ASN A1123 6960 5166 6080 267 -441 -1291 N ATOM 3316 CA ASN A1123 5.131 -16.195 -51.139 1.00 50.62 C ANISOU 3316 CA ASN A1123 7358 5538 6334 345 -486 -1574 C ATOM 3317 C ASN A1123 6.613 -15.996 -51.492 1.00 50.96 C ANISOU 3317 C ASN A1123 7430 5759 6171 459 -347 -1631 C ATOM 3318 O ASN A1123 7.007 -16.192 -52.643 1.00 53.55 O ANISOU 3318 O ASN A1123 7805 6233 6308 514 -350 -1862 O ATOM 3319 CB ASN A1123 4.277 -15.795 -52.336 1.00 51.99 C ANISOU 3319 CB ASN A1123 7576 5850 6327 299 -631 -1707 C ATOM 3320 CG ASN A1123 2.818 -16.101 -52.125 1.00 53.04 C ANISOU 3320 CG ASN A1123 7641 5810 6699 193 -786 -1711 C ATOM 3321 OD1 ASN A1123 2.448 -17.221 -51.812 1.00 54.94 O ANISOU 3321 OD1 ASN A1123 7839 5808 7227 165 -834 -1805 O ATOM 3322 ND2 ASN A1123 1.980 -15.100 -52.289 1.00 54.18 N ANISOU 3322 ND2 ASN A1123 7764 6066 6753 131 -872 -1608 N ATOM 3323 N LYS A1124 7.419 -15.597 -50.509 1.00 49.34 N ANISOU 3323 N LYS A1124 7185 5561 5997 489 -224 -1435 N ATOM 3324 CA LYS A1124 8.867 -15.430 -50.666 1.00 49.71 C ANISOU 3324 CA LYS A1124 7212 5759 5915 590 -85 -1478 C ATOM 3325 C LYS A1124 9.325 -14.511 -51.811 1.00 49.52 C ANISOU 3325 C LYS A1124 7228 6054 5533 575 -13 -1534 C ATOM 3326 O LYS A1124 10.479 -14.578 -52.228 1.00 49.27 O ANISOU 3326 O LYS A1124 7161 6171 5386 651 114 -1649 O ATOM 3327 CB LYS A1124 9.524 -16.803 -50.789 1.00 53.59 C ANISOU 3327 CB LYS A1124 7673 6089 6598 718 -91 -1716 C ATOM 3328 CG LYS A1124 9.425 -17.628 -49.520 1.00 55.31 C ANISOU 3328 CG LYS A1124 7862 5993 7158 735 -146 -1586 C ATOM 3329 CD LYS A1124 9.233 -19.111 -49.807 1.00 59.81 C ANISOU 3329 CD LYS A1124 8439 6286 8000 798 -261 -1821 C ATOM 3330 CE LYS A1124 9.665 -19.969 -48.623 1.00 62.59 C ANISOU 3330 CE LYS A1124 8768 6340 8671 857 -302 -1686 C ATOM 3331 NZ LYS A1124 9.259 -19.425 -47.285 1.00 61.79 N ANISOU 3331 NZ LYS A1124 8679 6200 8597 745 -281 -1314 N ATOM 3332 N ARG A1125 8.441 -13.629 -52.280 1.00 49.34 N ANISOU 3332 N ARG A1125 7269 6136 5340 473 -94 -1436 N ATOM 3333 CA ARG A1125 8.783 -12.656 -53.320 1.00 50.50 C ANISOU 3333 CA ARG A1125 7484 6572 5131 428 -47 -1413 C ATOM 3334 C ARG A1125 9.526 -11.479 -52.687 1.00 47.29 C ANISOU 3334 C ARG A1125 7038 6262 4666 389 70 -1156 C ATOM 3335 O ARG A1125 9.024 -10.367 -52.687 1.00 46.37 O ANISOU 3335 O ARG A1125 6963 6195 4459 303 8 -959 O ATOM 3336 CB ARG A1125 7.517 -12.111 -53.994 1.00 52.52 C ANISOU 3336 CB ARG A1125 7828 6865 5261 340 -231 -1370 C ATOM 3337 CG ARG A1125 6.548 -13.134 -54.541 1.00 55.77 C ANISOU 3337 CG ARG A1125 8264 7159 5763 352 -398 -1608 C ATOM 3338 CD ARG A1125 7.081 -13.736 -55.813 1.00 61.97 C ANISOU 3338 CD ARG A1125 9120 8127 6298 405 -370 -1897 C ATOM 3339 NE ARG A1125 6.032 -14.424 -56.560 1.00 67.32 N ANISOU 3339 NE ARG A1125 9846 8741 6989 395 -579 -2124 N ATOM 3340 CZ ARG A1125 5.119 -13.820 -57.316 1.00 69.13 C ANISOU 3340 CZ ARG A1125 10162 9081 7023 324 -764 -2086 C ATOM 3341 NH1 ARG A1125 4.215 -14.555 -57.954 1.00 71.90 N ANISOU 3341 NH1 ARG A1125 10537 9362 7418 323 -970 -2328 N ATOM 3342 NH2 ARG A1125 5.087 -12.494 -57.422 1.00 68.94 N ANISOU 3342 NH2 ARG A1125 10196 9211 6787 256 -770 -1809 N ATOM 3343 N TRP A1126 10.722 -11.716 -52.163 1.00 46.54 N ANISOU 3343 N TRP A1126 6853 6181 4648 459 218 -1172 N ATOM 3344 CA TRP A1126 11.389 -10.731 -51.298 1.00 44.84 C ANISOU 3344 CA TRP A1126 6575 6000 4462 426 301 -944 C ATOM 3345 C TRP A1126 11.586 -9.386 -51.974 1.00 46.04 C ANISOU 3345 C TRP A1126 6777 6363 4351 313 341 -789 C ATOM 3346 O TRP A1126 11.297 -8.353 -51.377 1.00 44.91 O ANISOU 3346 O TRP A1126 6637 6174 4251 246 291 -573 O ATOM 3347 CB TRP A1126 12.750 -11.228 -50.804 1.00 44.84 C ANISOU 3347 CB TRP A1126 6452 6010 4573 526 436 -1019 C ATOM 3348 CG TRP A1126 12.744 -12.623 -50.295 1.00 44.76 C ANISOU 3348 CG TRP A1126 6404 5783 4819 648 384 -1173 C ATOM 3349 CD1 TRP A1126 13.508 -13.654 -50.740 1.00 46.06 C ANISOU 3349 CD1 TRP A1126 6506 5946 5045 772 440 -1428 C ATOM 3350 CD2 TRP A1126 11.912 -13.153 -49.261 1.00 43.10 C ANISOU 3350 CD2 TRP A1126 6215 5311 4850 652 263 -1080 C ATOM 3351 NE1 TRP A1126 13.211 -14.790 -50.044 1.00 46.40 N ANISOU 3351 NE1 TRP A1126 6544 5707 5380 857 331 -1482 N ATOM 3352 CE2 TRP A1126 12.235 -14.510 -49.127 1.00 44.10 C ANISOU 3352 CE2 TRP A1126 6308 5260 5186 770 232 -1252 C ATOM 3353 CE3 TRP A1126 10.930 -12.607 -48.430 1.00 41.79 C ANISOU 3353 CE3 TRP A1126 6082 5048 4746 564 185 -873 C ATOM 3354 CZ2 TRP A1126 11.616 -15.334 -48.201 1.00 43.97 C ANISOU 3354 CZ2 TRP A1126 6312 4965 5427 778 123 -1178 C ATOM 3355 CZ3 TRP A1126 10.313 -13.427 -47.501 1.00 41.32 C ANISOU 3355 CZ3 TRP A1126 6026 4755 4917 570 110 -823 C ATOM 3356 CH2 TRP A1126 10.661 -14.776 -47.395 1.00 42.87 C ANISOU 3356 CH2 TRP A1126 6210 4769 5307 664 78 -953 C ATOM 3357 N ASP A1127 12.078 -9.409 -53.211 1.00 49.50 N ANISOU 3357 N ASP A1127 7258 7029 4517 289 429 -902 N ATOM 3358 CA ASP A1127 12.341 -8.186 -53.973 1.00 51.07 C ANISOU 3358 CA ASP A1127 7526 7444 4432 156 478 -726 C ATOM 3359 C ASP A1127 11.080 -7.356 -54.194 1.00 50.08 C ANISOU 3359 C ASP A1127 7531 7249 4246 70 269 -544 C ATOM 3360 O ASP A1127 11.111 -6.134 -54.090 1.00 50.34 O ANISOU 3360 O ASP A1127 7593 7296 4237 -26 241 -300 O ATOM 3361 CB ASP A1127 12.962 -8.513 -55.339 1.00 55.79 C ANISOU 3361 CB ASP A1127 8165 8332 4698 136 617 -900 C ATOM 3362 CG ASP A1127 14.403 -9.007 -55.241 1.00 57.96 C ANISOU 3362 CG ASP A1127 8274 8736 5013 203 857 -1062 C ATOM 3363 OD1 ASP A1127 15.207 -8.404 -54.500 1.00 56.31 O ANISOU 3363 OD1 ASP A1127 7946 8515 4934 174 951 -913 O ATOM 3364 OD2 ASP A1127 14.733 -9.999 -55.929 1.00 62.66 O ANISOU 3364 OD2 ASP A1127 8843 9444 5519 292 941 -1364 O ATOM 3365 N GLU A1128 9.972 -8.015 -54.502 1.00 50.45 N ANISOU 3365 N GLU A1128 7641 7203 4321 110 105 -673 N ATOM 3366 CA GLU A1128 8.735 -7.303 -54.804 1.00 51.46 C ANISOU 3366 CA GLU A1128 7868 7272 4411 49 -119 -538 C ATOM 3367 C GLU A1128 8.127 -6.677 -53.557 1.00 48.43 C ANISOU 3367 C GLU A1128 7406 6666 4327 51 -207 -373 C ATOM 3368 O GLU A1128 7.626 -5.557 -53.600 1.00 48.07 O ANISOU 3368 O GLU A1128 7405 6591 4267 -8 -333 -182 O ATOM 3369 CB GLU A1128 7.719 -8.243 -55.442 1.00 54.44 C ANISOU 3369 CB GLU A1128 8300 7610 4773 91 -280 -754 C ATOM 3370 CG GLU A1128 8.145 -8.811 -56.782 1.00 58.48 C ANISOU 3370 CG GLU A1128 8909 8364 4945 92 -228 -957 C ATOM 3371 CD GLU A1128 7.054 -9.656 -57.396 1.00 61.66 C ANISOU 3371 CD GLU A1128 9366 8710 5351 129 -435 -1183 C ATOM 3372 OE1 GLU A1128 7.229 -10.892 -57.469 1.00 64.34 O ANISOU 3372 OE1 GLU A1128 9660 9003 5783 211 -388 -1472 O ATOM 3373 OE2 GLU A1128 6.008 -9.083 -57.774 1.00 63.23 O ANISOU 3373 OE2 GLU A1128 9641 8886 5494 80 -666 -1079 O ATOM 3374 N ALA A1129 8.161 -7.416 -52.453 1.00 46.42 N ANISOU 3374 N ALA A1129 7040 6256 4341 124 -148 -454 N ATOM 3375 CA ALA A1129 7.746 -6.889 -51.161 1.00 43.65 C ANISOU 3375 CA ALA A1129 6606 5741 4238 127 -182 -325 C ATOM 3376 C ALA A1129 8.525 -5.614 -50.836 1.00 43.11 C ANISOU 3376 C ALA A1129 6525 5727 4126 76 -120 -131 C ATOM 3377 O ALA A1129 7.931 -4.584 -50.516 1.00 42.84 O ANISOU 3377 O ALA A1129 6491 5617 4169 41 -232 3 O ATOM 3378 CB ALA A1129 7.956 -7.928 -50.072 1.00 41.81 C ANISOU 3378 CB ALA A1129 6280 5379 4226 197 -96 -414 C ATOM 3379 N ALA A1130 9.850 -5.692 -50.950 1.00 42.96 N ANISOU 3379 N ALA A1130 6479 5833 4010 72 49 -137 N ATOM 3380 CA ALA A1130 10.746 -4.581 -50.619 1.00 42.60 C ANISOU 3380 CA ALA A1130 6394 5834 3954 7 122 28 C ATOM 3381 C ALA A1130 10.393 -3.302 -51.378 1.00 44.00 C ANISOU 3381 C ALA A1130 6675 6047 3995 -105 12 220 C ATOM 3382 O ALA A1130 10.300 -2.209 -50.792 1.00 42.66 O ANISOU 3382 O ALA A1130 6484 5772 3953 -145 -59 372 O ATOM 3383 CB ALA A1130 12.187 -4.978 -50.904 1.00 43.55 C ANISOU 3383 CB ALA A1130 6450 6119 3977 9 325 -41 C ATOM 3384 N VAL A1131 10.203 -3.452 -52.685 1.00 45.75 N ANISOU 3384 N VAL A1131 7015 6410 3957 -152 -15 209 N ATOM 3385 CA VAL A1131 9.858 -2.326 -53.556 1.00 47.38 C ANISOU 3385 CA VAL A1131 7354 6656 3990 -265 -147 422 C ATOM 3386 C VAL A1131 8.498 -1.734 -53.185 1.00 47.50 C ANISOU 3386 C VAL A1131 7390 6459 4197 -231 -408 492 C ATOM 3387 O VAL A1131 8.338 -0.513 -53.169 1.00 49.14 O ANISOU 3387 O VAL A1131 7637 6575 4458 -294 -532 697 O ATOM 3388 CB VAL A1131 9.881 -2.739 -55.048 1.00 48.42 C ANISOU 3388 CB VAL A1131 7628 7018 3751 -317 -135 377 C ATOM 3389 CG1 VAL A1131 9.167 -1.721 -55.912 1.00 50.25 C ANISOU 3389 CG1 VAL A1131 8028 7250 3811 -413 -357 606 C ATOM 3390 CG2 VAL A1131 11.313 -2.909 -55.519 1.00 49.21 C ANISOU 3390 CG2 VAL A1131 7695 7363 3638 -387 140 354 C ATOM 3391 N ASN A1132 7.531 -2.565 -52.849 1.00 47.01 N ANISOU 3391 N ASN A1132 7285 6309 4267 -133 -494 314 N ATOM 3392 CA ASN A1132 6.204 -2.090 -52.512 1.00 47.08 C ANISOU 3392 CA ASN A1132 7265 6137 4484 -91 -723 333 C ATOM 3393 C ASN A1132 6.121 -1.541 -51.116 1.00 45.57 C ANISOU 3393 C ASN A1132 6945 5787 4582 -57 -701 373 C ATOM 3394 O ASN A1132 5.327 -0.683 -50.836 1.00 44.48 O ANISOU 3394 O ASN A1132 6790 5516 4594 -49 -873 459 O ATOM 3395 CB ASN A1132 5.205 -3.216 -52.677 1.00 47.50 C ANISOU 3395 CB ASN A1132 7276 6153 4619 -20 -790 120 C ATOM 3396 CG ASN A1132 3.787 -2.736 -52.773 1.00 48.74 C ANISOU 3396 CG ASN A1132 7402 6178 4939 8 -1050 124 C ATOM 3397 OD1 ASN A1132 2.934 -3.208 -52.066 1.00 49.81 O ANISOU 3397 OD1 ASN A1132 7632 6312 4980 -21 -1251 263 O ATOM 3398 ND2 ASN A1132 3.529 -1.812 -53.656 1.00 48.92 N ANISOU 3398 ND2 ASN A1132 7282 6088 5215 62 -1054 -20 N ATOM 3399 N LEU A1133 6.932 -2.073 -50.224 1.00 45.70 N ANISOU 3399 N LEU A1133 6870 5817 4676 -27 -504 294 N ATOM 3400 CA LEU A1133 7.051 -1.552 -48.864 1.00 43.72 C ANISOU 3400 CA LEU A1133 6507 5457 4646 4 -465 307 C ATOM 3401 C LEU A1133 7.729 -0.204 -48.846 1.00 44.46 C ANISOU 3401 C LEU A1133 6620 5523 4747 -63 -491 475 C ATOM 3402 O LEU A1133 7.405 0.640 -48.012 1.00 45.97 O ANISOU 3402 O LEU A1133 6745 5585 5135 -39 -568 492 O ATOM 3403 CB LEU A1133 7.852 -2.505 -47.984 1.00 41.97 C ANISOU 3403 CB LEU A1133 6210 5275 4460 47 -274 209 C ATOM 3404 CG LEU A1133 7.134 -3.781 -47.564 1.00 42.01 C ANISOU 3404 CG LEU A1133 6172 5236 4551 107 -252 65 C ATOM 3405 CD1 LEU A1133 8.112 -4.684 -46.837 1.00 42.47 C ANISOU 3405 CD1 LEU A1133 6187 5321 4629 147 -93 13 C ATOM 3406 CD2 LEU A1133 5.930 -3.480 -46.689 1.00 41.33 C ANISOU 3406 CD2 LEU A1133 6003 5037 4662 131 -335 37 C ATOM 3407 N ALA A1134 8.666 0.001 -49.763 1.00 44.85 N ANISOU 3407 N ALA A1134 6752 5696 4591 -155 -421 587 N ATOM 3408 CA ALA A1134 9.404 1.251 -49.806 1.00 45.49 C ANISOU 3408 CA ALA A1134 6849 5743 4690 -255 -433 772 C ATOM 3409 C ALA A1134 8.598 2.389 -50.421 1.00 46.39 C ANISOU 3409 C ALA A1134 7063 5727 4836 -302 -676 944 C ATOM 3410 O ALA A1134 9.118 3.486 -50.566 1.00 48.89 O ANISOU 3410 O ALA A1134 7414 5974 5186 -404 -722 1129 O ATOM 3411 CB ALA A1134 10.712 1.064 -50.559 1.00 47.26 C ANISOU 3411 CB ALA A1134 7102 6165 4686 -361 -244 841 C ATOM 3412 N LYS A1135 7.342 2.142 -50.782 1.00 46.47 N ANISOU 3412 N LYS A1135 7111 5683 4861 -233 -851 888 N ATOM 3413 CA LYS A1135 6.483 3.192 -51.330 1.00 49.73 C ANISOU 3413 CA LYS A1135 7605 5945 5343 -246 -1131 1040 C ATOM 3414 C LYS A1135 5.367 3.565 -50.372 1.00 47.83 C ANISOU 3414 C LYS A1135 7232 5501 5440 -119 -1288 910 C ATOM 3415 O LYS A1135 4.316 4.028 -50.806 1.00 49.77 O ANISOU 3415 O LYS A1135 7502 5629 5778 -73 -1542 943 O ATOM 3416 CB LYS A1135 5.872 2.737 -52.658 1.00 53.46 C ANISOU 3416 CB LYS A1135 8221 6528 5560 -265 -1260 1079 C ATOM 3417 CG LYS A1135 6.824 2.832 -53.838 1.00 58.13 C ANISOU 3417 CG LYS A1135 8981 7317 5787 -416 -1169 1269 C ATOM 3418 CD LYS A1135 6.457 1.866 -54.960 1.00 62.19 C ANISOU 3418 CD LYS A1135 9609 8033 5984 -412 -1190 1183 C ATOM 3419 CE LYS A1135 5.105 2.183 -55.592 1.00 65.34 C ANISOU 3419 CE LYS A1135 10095 8330 6399 -363 -1541 1231 C ATOM 3420 NZ LYS A1135 3.939 1.777 -54.750 1.00 64.36 N ANISOU 3420 NZ LYS A1135 9801 8040 6612 -210 -1659 1006 N ATOM 3421 N SER A1136 5.593 3.375 -49.074 1.00 45.31 N ANISOU 3421 N SER A1136 6766 5154 5295 -59 -1143 756 N ATOM 3422 CA SER A1136 4.538 3.553 -48.077 1.00 43.95 C ANISOU 3422 CA SER A1136 6443 4852 5404 60 -1227 584 C ATOM 3423 C SER A1136 4.703 4.838 -47.281 1.00 45.17 C ANISOU 3423 C SER A1136 6531 4830 5800 80 -1308 597 C ATOM 3424 O SER A1136 5.784 5.421 -47.233 1.00 44.76 O ANISOU 3424 O SER A1136 6526 4762 5719 -4 -1254 718 O ATOM 3425 CB SER A1136 4.486 2.355 -47.123 1.00 39.96 C ANISOU 3425 CB SER A1136 5826 4454 4903 113 -1014 386 C ATOM 3426 OG SER A1136 5.746 2.114 -46.547 1.00 37.63 O ANISOU 3426 OG SER A1136 5529 4244 4523 74 -813 398 O ATOM 3427 N ARG A1137 3.606 5.266 -46.664 1.00 47.24 N ANISOU 3427 N ARG A1137 6665 4961 6321 194 -1440 447 N ATOM 3428 CA ARG A1137 3.618 6.355 -45.696 1.00 48.80 C ANISOU 3428 CA ARG A1137 6760 4997 6782 250 -1504 360 C ATOM 3429 C ARG A1137 4.569 6.006 -44.575 1.00 45.97 C ANISOU 3429 C ARG A1137 6346 4754 6366 232 -1262 260 C ATOM 3430 O ARG A1137 5.304 6.854 -44.100 1.00 47.45 O ANISOU 3430 O ARG A1137 6525 4852 6651 205 -1279 277 O ATOM 3431 CB ARG A1137 2.223 6.576 -45.122 1.00 52.38 C ANISOU 3431 CB ARG A1137 7042 5359 7501 395 -1622 137 C ATOM 3432 CG ARG A1137 2.093 7.814 -44.245 1.00 56.60 C ANISOU 3432 CG ARG A1137 7464 5705 8336 479 -1731 4 C ATOM 3433 CD ARG A1137 0.661 8.011 -43.760 1.00 59.61 C ANISOU 3433 CD ARG A1137 7642 6020 8988 634 -1835 -248 C ATOM 3434 NE ARG A1137 -0.295 8.089 -44.866 1.00 61.56 N ANISOU 3434 NE ARG A1137 7907 6167 9317 673 -2088 -162 N ATOM 3435 CZ ARG A1137 -0.531 9.179 -45.592 1.00 66.02 C ANISOU 3435 CZ ARG A1137 8534 6480 10069 707 -2411 -27 C ATOM 3436 NH1 ARG A1137 0.105 10.324 -45.351 1.00 67.92 N ANISOU 3436 NH1 ARG A1137 8822 6515 10469 698 -2518 37 N ATOM 3437 NH2 ARG A1137 -1.421 9.128 -46.569 1.00 68.85 N ANISOU 3437 NH2 ARG A1137 8911 6775 10471 748 -2653 49 N ATOM 3438 N TRP A1138 4.551 4.750 -44.161 1.00 43.21 N ANISOU 3438 N TRP A1138 5960 4588 5870 244 -1060 162 N ATOM 3439 CA TRP A1138 5.509 4.259 -43.189 1.00 42.65 C ANISOU 3439 CA TRP A1138 5860 4640 5705 227 -852 102 C ATOM 3440 C TRP A1138 6.935 4.642 -43.572 1.00 43.22 C ANISOU 3440 C TRP A1138 6017 4719 5682 125 -818 264 C ATOM 3441 O TRP A1138 7.611 5.382 -42.856 1.00 42.05 O ANISOU 3441 O TRP A1138 5827 4517 5633 114 -823 233 O ATOM 3442 CB TRP A1138 5.379 2.743 -43.077 1.00 41.47 C ANISOU 3442 CB TRP A1138 5708 4654 5392 230 -678 55 C ATOM 3443 CG TRP A1138 6.455 2.091 -42.296 1.00 40.80 C ANISOU 3443 CG TRP A1138 5625 4689 5188 213 -498 43 C ATOM 3444 CD1 TRP A1138 6.880 2.420 -41.042 1.00 41.45 C ANISOU 3444 CD1 TRP A1138 5641 4795 5312 244 -442 -49 C ATOM 3445 CD2 TRP A1138 7.230 0.969 -42.700 1.00 41.15 C ANISOU 3445 CD2 TRP A1138 5733 4843 5056 176 -371 108 C ATOM 3446 NE1 TRP A1138 7.881 1.573 -40.646 1.00 40.42 N ANISOU 3446 NE1 TRP A1138 5535 4778 5042 227 -308 -18 N ATOM 3447 CE2 TRP A1138 8.112 0.669 -41.649 1.00 40.63 C ANISOU 3447 CE2 TRP A1138 5633 4849 4955 192 -260 72 C ATOM 3448 CE3 TRP A1138 7.263 0.178 -43.853 1.00 42.11 C ANISOU 3448 CE3 TRP A1138 5935 5012 5051 143 -354 171 C ATOM 3449 CZ2 TRP A1138 9.022 -0.385 -41.719 1.00 40.56 C ANISOU 3449 CZ2 TRP A1138 5654 4931 4823 185 -146 107 C ATOM 3450 CZ3 TRP A1138 8.176 -0.865 -43.918 1.00 40.87 C ANISOU 3450 CZ3 TRP A1138 5804 4954 4768 136 -218 177 C ATOM 3451 CH2 TRP A1138 9.039 -1.134 -42.860 1.00 39.58 C ANISOU 3451 CH2 TRP A1138 5593 4835 4609 162 -121 150 C ATOM 3452 N TYR A1139 7.373 4.143 -44.720 1.00 45.30 N ANISOU 3452 N TYR A1139 6390 5063 5759 45 -783 419 N ATOM 3453 CA TYR A1139 8.712 4.408 -45.228 1.00 47.08 C ANISOU 3453 CA TYR A1139 6675 5337 5874 -72 -713 575 C ATOM 3454 C TYR A1139 9.026 5.908 -45.227 1.00 49.58 C ANISOU 3454 C TYR A1139 6997 5468 6370 -139 -863 683 C ATOM 3455 O TYR A1139 10.146 6.311 -44.939 1.00 50.14 O ANISOU 3455 O TYR A1139 7037 5546 6467 -219 -798 729 O ATOM 3456 CB TYR A1139 8.860 3.835 -46.644 1.00 47.15 C ANISOU 3456 CB TYR A1139 6805 5462 5645 -148 -679 712 C ATOM 3457 CG TYR A1139 10.232 4.035 -47.234 1.00 48.50 C ANISOU 3457 CG TYR A1139 7016 5733 5680 -285 -561 862 C ATOM 3458 CD1 TYR A1139 10.559 5.209 -47.903 1.00 50.70 C ANISOU 3458 CD1 TYR A1139 7365 5915 5980 -416 -665 1077 C ATOM 3459 CD2 TYR A1139 11.208 3.059 -47.110 1.00 48.52 C ANISOU 3459 CD2 TYR A1139 6968 5915 5552 -287 -348 791 C ATOM 3460 CE1 TYR A1139 11.821 5.403 -48.435 1.00 53.09 C ANISOU 3460 CE1 TYR A1139 7679 6329 6161 -570 -526 1221 C ATOM 3461 CE2 TYR A1139 12.475 3.240 -47.643 1.00 50.87 C ANISOU 3461 CE2 TYR A1139 7257 6326 5744 -412 -218 901 C ATOM 3462 CZ TYR A1139 12.779 4.415 -48.304 1.00 53.44 C ANISOU 3462 CZ TYR A1139 7643 6583 6075 -566 -291 1117 C ATOM 3463 OH TYR A1139 14.041 4.599 -48.836 1.00 55.91 O ANISOU 3463 OH TYR A1139 7926 7031 6286 -719 -132 1233 O ATOM 3464 N ASN A1140 8.039 6.725 -45.566 1.00 52.05 N ANISOU 3464 N ASN A1140 7340 5598 6835 -106 -1084 721 N ATOM 3465 CA ASN A1140 8.214 8.172 -45.552 1.00 55.82 C ANISOU 3465 CA ASN A1140 7828 5840 7541 -157 -1269 820 C ATOM 3466 C ASN A1140 8.505 8.734 -44.173 1.00 56.57 C ANISOU 3466 C ASN A1140 7789 5846 7859 -97 -1265 620 C ATOM 3467 O ASN A1140 9.402 9.554 -44.025 1.00 57.93 O ANISOU 3467 O ASN A1140 7955 5913 8143 -194 -1298 695 O ATOM 3468 CB ASN A1140 6.990 8.875 -46.134 1.00 58.49 C ANISOU 3468 CB ASN A1140 8211 5972 8037 -96 -1545 876 C ATOM 3469 CG ASN A1140 7.201 9.294 -47.563 1.00 61.45 C ANISOU 3469 CG ASN A1140 8765 6302 8277 -238 -1667 1201 C ATOM 3470 OD1 ASN A1140 7.841 10.315 -47.822 1.00 65.79 O ANISOU 3470 OD1 ASN A1140 9375 6692 8928 -362 -1760 1398 O ATOM 3471 ND2 ASN A1140 6.675 8.509 -48.503 1.00 60.70 N ANISOU 3471 ND2 ASN A1140 8764 6353 7945 -234 -1670 1264 N ATOM 3472 N GLN A1141 7.752 8.293 -43.170 1.00 56.54 N ANISOU 3472 N GLN A1141 7676 5894 7910 50 -1222 363 N ATOM 3473 CA GLN A1141 7.909 8.822 -41.822 1.00 57.45 C ANISOU 3473 CA GLN A1141 7672 5959 8196 121 -1224 136 C ATOM 3474 C GLN A1141 9.287 8.468 -41.267 1.00 52.89 C ANISOU 3474 C GLN A1141 7077 5524 7494 46 -1061 138 C ATOM 3475 O GLN A1141 9.987 9.322 -40.750 1.00 55.99 O ANISOU 3475 O GLN A1141 7425 5809 8037 7 -1128 95 O ATOM 3476 CB GLN A1141 6.838 8.287 -40.857 1.00 62.03 C ANISOU 3476 CB GLN A1141 8141 6635 8792 274 -1159 -132 C ATOM 3477 CG GLN A1141 5.389 8.260 -41.348 1.00 67.11 C ANISOU 3477 CG GLN A1141 8753 7208 9536 363 -1273 -175 C ATOM 3478 CD GLN A1141 4.785 9.625 -41.634 1.00 74.11 C ANISOU 3478 CD GLN A1141 9612 7804 10742 419 -1552 -193 C ATOM 3479 OE1 GLN A1141 5.457 10.660 -41.542 1.00 80.39 O ANISOU 3479 OE1 GLN A1141 10430 8415 11697 374 -1672 -149 O ATOM 3480 NE2 GLN A1141 3.493 9.632 -41.982 1.00 75.20 N ANISOU 3480 NE2 GLN A1141 9687 7877 11007 521 -1677 -263 N ATOM 3481 N THR A1142 9.669 7.205 -41.374 1.00 48.03 N ANISOU 3481 N THR A1142 6485 5133 6631 32 -869 174 N ATOM 3482 CA THR A1142 10.885 6.715 -40.746 1.00 44.67 C ANISOU 3482 CA THR A1142 6018 4853 6101 0 -731 145 C ATOM 3483 C THR A1142 11.686 5.910 -41.754 1.00 43.03 C ANISOU 3483 C THR A1142 5868 4779 5700 -94 -599 325 C ATOM 3484 O THR A1142 11.746 4.686 -41.646 1.00 41.60 O ANISOU 3484 O THR A1142 5690 4760 5355 -45 -462 288 O ATOM 3485 CB THR A1142 10.528 5.816 -39.567 1.00 43.12 C ANISOU 3485 CB THR A1142 5768 4808 5804 115 -625 -44 C ATOM 3486 OG1 THR A1142 9.539 4.875 -39.992 1.00 42.47 O ANISOU 3486 OG1 THR A1142 5725 4794 5616 161 -561 -31 O ATOM 3487 CG2 THR A1142 9.964 6.633 -38.433 1.00 44.08 C ANISOU 3487 CG2 THR A1142 5813 4856 6078 202 -716 -265 C ATOM 3488 N PRO A1143 12.295 6.594 -42.747 1.00 43.18 N ANISOU 3488 N PRO A1143 5932 4731 5744 -235 -636 520 N ATOM 3489 CA PRO A1143 13.040 5.950 -43.836 1.00 42.85 C ANISOU 3489 CA PRO A1143 5937 4841 5500 -338 -493 678 C ATOM 3490 C PRO A1143 14.171 5.055 -43.360 1.00 43.19 C ANISOU 3490 C PRO A1143 5887 5069 5454 -324 -319 599 C ATOM 3491 O PRO A1143 14.237 3.898 -43.760 1.00 43.85 O ANISOU 3491 O PRO A1143 5990 5305 5364 -283 -191 581 O ATOM 3492 CB PRO A1143 13.606 7.130 -44.634 1.00 44.79 C ANISOU 3492 CB PRO A1143 6219 4969 5829 -517 -567 894 C ATOM 3493 CG PRO A1143 13.470 8.319 -43.758 1.00 45.11 C ANISOU 3493 CG PRO A1143 6202 4778 6158 -504 -745 819 C ATOM 3494 CD PRO A1143 12.271 8.057 -42.908 1.00 44.26 C ANISOU 3494 CD PRO A1143 6078 4631 6107 -314 -820 603 C ATOM 3495 N ASN A1144 15.041 5.588 -42.504 1.00 44.56 N ANISOU 3495 N ASN A1144 5950 5211 5767 -349 -341 536 N ATOM 3496 CA ASN A1144 16.146 4.823 -41.933 1.00 43.47 C ANISOU 3496 CA ASN A1144 5701 5229 5584 -319 -224 450 C ATOM 3497 C ASN A1144 15.707 3.485 -41.332 1.00 42.44 C ANISOU 3497 C ASN A1144 5589 5209 5326 -159 -162 327 C ATOM 3498 O ASN A1144 16.233 2.428 -41.693 1.00 42.37 O ANISOU 3498 O ASN A1144 5560 5333 5204 -131 -38 327 O ATOM 3499 CB ASN A1144 16.868 5.666 -40.885 1.00 43.93 C ANISOU 3499 CB ASN A1144 5644 5213 5833 -340 -323 358 C ATOM 3500 CG ASN A1144 17.698 6.776 -41.505 1.00 46.62 C ANISOU 3500 CG ASN A1144 5928 5462 6322 -535 -349 497 C ATOM 3501 OD1 ASN A1144 18.196 6.651 -42.622 1.00 47.76 O ANISOU 3501 OD1 ASN A1144 6078 5689 6379 -661 -225 660 O ATOM 3502 ND2 ASN A1144 17.866 7.864 -40.773 1.00 48.70 N ANISOU 3502 ND2 ASN A1144 6133 5560 6810 -571 -504 427 N ATOM 3503 N ARG A1145 14.727 3.529 -40.435 1.00 42.29 N ANISOU 3503 N ARG A1145 5603 5129 5336 -59 -243 219 N ATOM 3504 CA ARG A1145 14.251 2.322 -39.774 1.00 41.30 C ANISOU 3504 CA ARG A1145 5502 5093 5097 61 -185 134 C ATOM 3505 C ARG A1145 13.617 1.404 -40.788 1.00 41.93 C ANISOU 3505 C ARG A1145 5662 5205 5063 69 -108 197 C ATOM 3506 O ARG A1145 13.937 0.228 -40.829 1.00 44.16 O ANISOU 3506 O ARG A1145 5946 5572 5258 118 -20 184 O ATOM 3507 CB ARG A1145 13.237 2.658 -38.689 1.00 41.57 C ANISOU 3507 CB ARG A1145 5544 5081 5168 135 -259 11 C ATOM 3508 CG ARG A1145 12.750 1.460 -37.891 1.00 41.27 C ANISOU 3508 CG ARG A1145 5534 5141 5003 226 -188 -43 C ATOM 3509 CD ARG A1145 11.755 1.899 -36.827 1.00 42.17 C ANISOU 3509 CD ARG A1145 5638 5253 5130 278 -225 -177 C ATOM 3510 NE ARG A1145 11.247 0.772 -36.046 1.00 42.49 N ANISOU 3510 NE ARG A1145 5712 5400 5031 329 -138 -193 N ATOM 3511 CZ ARG A1145 10.451 0.885 -34.981 1.00 43.98 C ANISOU 3511 CZ ARG A1145 5888 5654 5167 365 -117 -307 C ATOM 3512 NH1 ARG A1145 10.046 2.074 -34.546 1.00 44.10 N ANISOU 3512 NH1 ARG A1145 5845 5634 5275 383 -186 -460 N ATOM 3513 NH2 ARG A1145 10.056 -0.205 -34.341 1.00 45.05 N ANISOU 3513 NH2 ARG A1145 6066 5890 5161 377 -23 -271 N ATOM 3514 N ALA A1146 12.720 1.934 -41.612 1.00 42.24 N ANISOU 3514 N ALA A1146 5766 5162 5119 27 -165 255 N ATOM 3515 CA ALA A1146 12.033 1.101 -42.596 1.00 42.64 C ANISOU 3515 CA ALA A1146 5896 5246 5058 35 -123 291 C ATOM 3516 C ALA A1146 13.000 0.430 -43.578 1.00 43.32 C ANISOU 3516 C ALA A1146 5991 5450 5016 -10 -5 346 C ATOM 3517 O ALA A1146 12.825 -0.740 -43.920 1.00 42.77 O ANISOU 3517 O ALA A1146 5951 5442 4856 40 63 297 O ATOM 3518 CB ALA A1146 10.993 1.912 -43.350 1.00 44.13 C ANISOU 3518 CB ALA A1146 6148 5326 5291 -1 -247 352 C ATOM 3519 N LYS A1147 14.021 1.165 -44.018 1.00 43.70 N ANISOU 3519 N LYS A1147 6000 5529 5072 -111 22 431 N ATOM 3520 CA LYS A1147 14.991 0.632 -44.967 1.00 44.37 C ANISOU 3520 CA LYS A1147 6063 5763 5031 -166 165 462 C ATOM 3521 C LYS A1147 15.783 -0.521 -44.345 1.00 44.01 C ANISOU 3521 C LYS A1147 5921 5804 4996 -60 260 335 C ATOM 3522 O LYS A1147 16.054 -1.512 -45.019 1.00 45.98 O ANISOU 3522 O LYS A1147 6171 6152 5145 -23 363 277 O ATOM 3523 CB LYS A1147 15.916 1.744 -45.480 1.00 46.30 C ANISOU 3523 CB LYS A1147 6261 6027 5301 -326 192 595 C ATOM 3524 CG LYS A1147 16.888 1.371 -46.597 1.00 48.79 C ANISOU 3524 CG LYS A1147 6541 6537 5461 -418 374 635 C ATOM 3525 CD LYS A1147 16.274 0.451 -47.642 1.00 50.74 C ANISOU 3525 CD LYS A1147 6902 6887 5488 -379 432 600 C ATOM 3526 CE LYS A1147 17.028 0.491 -48.960 1.00 55.35 C ANISOU 3526 CE LYS A1147 7490 7676 5862 -514 599 673 C ATOM 3527 NZ LYS A1147 16.423 1.474 -49.916 1.00 58.78 N ANISOU 3527 NZ LYS A1147 8087 8083 6163 -666 514 894 N ATOM 3528 N ARG A1148 16.129 -0.422 -43.061 1.00 42.44 N ANISOU 3528 N ARG A1148 5644 5561 4919 0 205 279 N ATOM 3529 CA ARG A1148 16.756 -1.564 -42.362 1.00 41.42 C ANISOU 3529 CA ARG A1148 5445 5483 4809 119 242 182 C ATOM 3530 C ARG A1148 15.816 -2.772 -42.299 1.00 39.28 C ANISOU 3530 C ARG A1148 5270 5174 4482 218 243 136 C ATOM 3531 O ARG A1148 16.230 -3.908 -42.522 1.00 38.19 O ANISOU 3531 O ARG A1148 5110 5069 4331 294 300 74 O ATOM 3532 CB ARG A1148 17.175 -1.187 -40.940 1.00 41.29 C ANISOU 3532 CB ARG A1148 5357 5434 4895 163 146 145 C ATOM 3533 CG ARG A1148 18.312 -0.174 -40.853 1.00 42.27 C ANISOU 3533 CG ARG A1148 5348 5586 5125 73 131 157 C ATOM 3534 CD ARG A1148 18.837 -0.067 -39.422 1.00 41.80 C ANISOU 3534 CD ARG A1148 5213 5521 5147 144 16 81 C ATOM 3535 NE ARG A1148 17.947 0.677 -38.528 1.00 38.55 N ANISOU 3535 NE ARG A1148 4877 5025 4743 150 -98 52 N ATOM 3536 CZ ARG A1148 18.024 1.980 -38.294 1.00 38.11 C ANISOU 3536 CZ ARG A1148 4784 4897 4797 67 -184 35 C ATOM 3537 NH1 ARG A1148 18.940 2.736 -38.877 1.00 38.80 N ANISOU 3537 NH1 ARG A1148 4767 4973 5001 -54 -173 81 N ATOM 3538 NH2 ARG A1148 17.168 2.537 -37.464 1.00 38.70 N ANISOU 3538 NH2 ARG A1148 4917 4907 4879 102 -280 -38 N ATOM 3539 N VAL A1149 14.550 -2.508 -41.996 1.00 38.20 N ANISOU 3539 N VAL A1149 5221 4953 4340 213 173 155 N ATOM 3540 CA VAL A1149 13.540 -3.556 -41.923 1.00 38.30 C ANISOU 3540 CA VAL A1149 5307 4917 4325 271 173 123 C ATOM 3541 C VAL A1149 13.286 -4.171 -43.309 1.00 38.02 C ANISOU 3541 C VAL A1149 5325 4906 4212 255 223 100 C ATOM 3542 O VAL A1149 13.144 -5.393 -43.437 1.00 38.97 O ANISOU 3542 O VAL A1149 5468 5002 4334 317 249 36 O ATOM 3543 CB VAL A1149 12.223 -3.040 -41.292 1.00 38.48 C ANISOU 3543 CB VAL A1149 5370 4869 4380 259 103 127 C ATOM 3544 CG1 VAL A1149 11.138 -4.108 -41.366 1.00 38.97 C ANISOU 3544 CG1 VAL A1149 5486 4884 4436 284 116 102 C ATOM 3545 CG2 VAL A1149 12.443 -2.621 -39.833 1.00 38.41 C ANISOU 3545 CG2 VAL A1149 5319 4869 4406 289 67 108 C ATOM 3546 N ILE A1150 13.257 -3.337 -44.343 1.00 36.66 N ANISOU 3546 N ILE A1150 5181 4777 3969 167 223 150 N ATOM 3547 CA ILE A1150 13.113 -3.835 -45.706 1.00 35.95 C ANISOU 3547 CA ILE A1150 5153 4756 3749 144 267 120 C ATOM 3548 C ILE A1150 14.317 -4.692 -46.107 1.00 35.37 C ANISOU 3548 C ILE A1150 5010 4792 3635 189 396 27 C ATOM 3549 O ILE A1150 14.150 -5.760 -46.684 1.00 35.26 O ANISOU 3549 O ILE A1150 5027 4793 3576 246 428 -86 O ATOM 3550 CB ILE A1150 12.849 -2.690 -46.705 1.00 37.35 C ANISOU 3550 CB ILE A1150 5398 4968 3824 27 224 235 C ATOM 3551 CG1 ILE A1150 11.444 -2.128 -46.453 1.00 37.37 C ANISOU 3551 CG1 ILE A1150 5459 4839 3900 25 69 275 C ATOM 3552 CG2 ILE A1150 12.946 -3.178 -48.150 1.00 38.34 C ANISOU 3552 CG2 ILE A1150 5594 5226 3746 -8 288 203 C ATOM 3553 CD1 ILE A1150 11.176 -0.789 -47.108 1.00 38.99 C ANISOU 3553 CD1 ILE A1150 5724 5010 4078 -72 -34 419 C ATOM 3554 N THR A1151 15.521 -4.239 -45.775 1.00 35.13 N ANISOU 3554 N THR A1151 4867 4829 3649 171 458 49 N ATOM 3555 CA THR A1151 16.733 -5.014 -46.040 1.00 35.91 C ANISOU 3555 CA THR A1151 4850 5036 3758 232 578 -66 C ATOM 3556 C THR A1151 16.662 -6.371 -45.357 1.00 36.43 C ANISOU 3556 C THR A1151 4904 4999 3938 387 537 -177 C ATOM 3557 O THR A1151 17.070 -7.393 -45.918 1.00 36.96 O ANISOU 3557 O THR A1151 4935 5100 4007 470 601 -321 O ATOM 3558 CB THR A1151 17.985 -4.274 -45.550 1.00 35.90 C ANISOU 3558 CB THR A1151 4693 5101 3845 190 620 -27 C ATOM 3559 OG1 THR A1151 18.132 -3.059 -46.284 1.00 36.78 O ANISOU 3559 OG1 THR A1151 4815 5290 3867 21 667 96 O ATOM 3560 CG2 THR A1151 19.229 -5.107 -45.745 1.00 37.38 C ANISOU 3560 CG2 THR A1151 4717 5397 4087 275 733 -174 C ATOM 3561 N THR A1152 16.134 -6.372 -44.140 1.00 36.22 N ANISOU 3561 N THR A1152 4910 4842 4007 423 427 -111 N ATOM 3562 CA THR A1152 15.995 -7.599 -43.385 1.00 37.02 C ANISOU 3562 CA THR A1152 5028 4825 4213 541 370 -154 C ATOM 3563 C THR A1152 15.030 -8.554 -44.088 1.00 38.06 C ANISOU 3563 C THR A1152 5258 4877 4324 558 365 -226 C ATOM 3564 O THR A1152 15.310 -9.751 -44.188 1.00 38.67 O ANISOU 3564 O THR A1152 5322 4882 4488 658 361 -329 O ATOM 3565 CB THR A1152 15.562 -7.313 -41.935 1.00 35.83 C ANISOU 3565 CB THR A1152 4909 4592 4110 545 271 -47 C ATOM 3566 OG1 THR A1152 16.585 -6.541 -41.284 1.00 35.55 O ANISOU 3566 OG1 THR A1152 4771 4628 4108 544 251 -22 O ATOM 3567 CG2 THR A1152 15.356 -8.613 -41.175 1.00 36.18 C ANISOU 3567 CG2 THR A1152 4999 4509 4239 638 210 -40 C ATOM 3568 N PHE A1153 13.917 -8.031 -44.596 1.00 38.50 N ANISOU 3568 N PHE A1153 5403 4933 4292 468 344 -187 N ATOM 3569 CA PHE A1153 12.983 -8.866 -45.341 1.00 40.36 C ANISOU 3569 CA PHE A1153 5717 5102 4513 472 319 -273 C ATOM 3570 C PHE A1153 13.564 -9.367 -46.659 1.00 44.85 C ANISOU 3570 C PHE A1153 6276 5777 4988 501 394 -433 C ATOM 3571 O PHE A1153 13.273 -10.493 -47.063 1.00 48.23 O ANISOU 3571 O PHE A1153 6732 6124 5468 562 373 -573 O ATOM 3572 CB PHE A1153 11.675 -8.133 -45.636 1.00 39.73 C ANISOU 3572 CB PHE A1153 5711 5009 4372 378 253 -209 C ATOM 3573 CG PHE A1153 10.687 -8.141 -44.503 1.00 38.40 C ANISOU 3573 CG PHE A1153 5551 4722 4314 362 191 -133 C ATOM 3574 CD1 PHE A1153 10.443 -9.287 -43.770 1.00 39.41 C ANISOU 3574 CD1 PHE A1153 5684 4726 4561 403 180 -142 C ATOM 3575 CD2 PHE A1153 9.969 -7.007 -44.207 1.00 37.35 C ANISOU 3575 CD2 PHE A1153 5416 4602 4170 301 146 -56 C ATOM 3576 CE1 PHE A1153 9.525 -9.284 -42.741 1.00 39.04 C ANISOU 3576 CE1 PHE A1153 5641 4610 4583 362 158 -61 C ATOM 3577 CE2 PHE A1153 9.056 -6.996 -43.184 1.00 37.38 C ANISOU 3577 CE2 PHE A1153 5403 4536 4261 286 120 -20 C ATOM 3578 CZ PHE A1153 8.828 -8.136 -42.449 1.00 38.03 C ANISOU 3578 CZ PHE A1153 5491 4535 4423 305 142 -16 C ATOM 3579 N ARG A1154 14.368 -8.557 -47.345 1.00 47.09 N ANISOU 3579 N ARG A1154 6515 6241 5132 449 488 -424 N ATOM 3580 CA ARG A1154 14.851 -8.976 -48.657 1.00 50.40 C ANISOU 3580 CA ARG A1154 6927 6813 5405 460 590 -588 C ATOM 3581 C ARG A1154 16.112 -9.862 -48.607 1.00 50.63 C ANISOU 3581 C ARG A1154 6816 6880 5539 587 686 -763 C ATOM 3582 O ARG A1154 16.442 -10.517 -49.593 1.00 54.66 O ANISOU 3582 O ARG A1154 7307 7494 5967 635 770 -969 O ATOM 3583 CB ARG A1154 14.957 -7.789 -49.646 1.00 53.86 C ANISOU 3583 CB ARG A1154 7409 7453 5601 317 657 -490 C ATOM 3584 CG ARG A1154 16.247 -6.974 -49.666 1.00 57.15 C ANISOU 3584 CG ARG A1154 7704 8030 5981 252 795 -420 C ATOM 3585 CD ARG A1154 16.457 -6.318 -51.031 1.00 61.06 C ANISOU 3585 CD ARG A1154 8253 8758 6187 115 907 -380 C ATOM 3586 NE ARG A1154 16.574 -7.344 -52.073 1.00 66.94 N ANISOU 3586 NE ARG A1154 9014 9644 6777 179 999 -619 N ATOM 3587 CZ ARG A1154 17.699 -7.980 -52.421 1.00 71.21 C ANISOU 3587 CZ ARG A1154 9404 10341 7309 247 1178 -823 C ATOM 3588 NH1 ARG A1154 18.864 -7.689 -51.845 1.00 72.26 N ANISOU 3588 NH1 ARG A1154 9346 10522 7585 252 1286 -803 N ATOM 3589 NH2 ARG A1154 17.665 -8.917 -53.372 1.00 73.65 N ANISOU 3589 NH2 ARG A1154 9739 10766 7477 319 1244 -1080 N ATOM 3590 N THR A1155 16.794 -9.906 -47.469 1.00 47.45 N ANISOU 3590 N THR A1155 6311 6394 5321 654 659 -705 N ATOM 3591 CA THR A1155 18.012 -10.705 -47.342 1.00 48.09 C ANISOU 3591 CA THR A1155 6234 6490 5548 794 714 -868 C ATOM 3592 C THR A1155 17.870 -11.894 -46.415 1.00 46.91 C ANISOU 3592 C THR A1155 6095 6089 5639 940 573 -899 C ATOM 3593 O THR A1155 18.487 -12.918 -46.641 1.00 48.45 O ANISOU 3593 O THR A1155 6205 6231 5971 1084 578 -1093 O ATOM 3594 CB THR A1155 19.170 -9.867 -46.780 1.00 49.16 C ANISOU 3594 CB THR A1155 6208 6736 5735 771 767 -787 C ATOM 3595 OG1 THR A1155 18.765 -9.259 -45.542 1.00 47.74 O ANISOU 3595 OG1 THR A1155 6082 6436 5622 731 638 -582 O ATOM 3596 CG2 THR A1155 19.586 -8.791 -47.766 1.00 50.40 C ANISOU 3596 CG2 THR A1155 6322 7142 5685 616 932 -757 C ATOM 3597 N GLY A1156 17.087 -11.743 -45.352 1.00 45.04 N ANISOU 3597 N GLY A1156 5957 5698 5457 902 450 -706 N ATOM 3598 CA GLY A1156 17.021 -12.738 -44.293 1.00 44.49 C ANISOU 3598 CA GLY A1156 5911 5400 5591 1006 315 -659 C ATOM 3599 C GLY A1156 18.255 -12.732 -43.411 1.00 45.21 C ANISOU 3599 C GLY A1156 5869 5496 5810 1109 267 -627 C ATOM 3600 O GLY A1156 18.454 -13.664 -42.632 1.00 45.68 O ANISOU 3600 O GLY A1156 5938 5369 6047 1224 137 -597 O ATOM 3601 N THR A1157 19.070 -11.679 -43.518 1.00 45.73 N ANISOU 3601 N THR A1157 5814 5762 5798 1061 352 -621 N ATOM 3602 CA THR A1157 20.345 -11.574 -42.796 1.00 48.43 C ANISOU 3602 CA THR A1157 5988 6139 6271 1153 303 -626 C ATOM 3603 C THR A1157 20.339 -10.372 -41.864 1.00 47.49 C ANISOU 3603 C THR A1157 5879 6086 6078 1048 254 -445 C ATOM 3604 O THR A1157 19.357 -9.633 -41.807 1.00 47.59 O ANISOU 3604 O THR A1157 6020 6109 5950 917 268 -330 O ATOM 3605 CB THR A1157 21.526 -11.368 -43.761 1.00 51.27 C ANISOU 3605 CB THR A1157 6132 6699 6647 1178 460 -820 C ATOM 3606 OG1 THR A1157 21.455 -10.054 -44.324 1.00 51.47 O ANISOU 3606 OG1 THR A1157 6151 6921 6482 993 596 -750 O ATOM 3607 CG2 THR A1157 21.514 -12.392 -44.879 1.00 53.40 C ANISOU 3607 CG2 THR A1157 6384 6963 6942 1270 546 -1058 C ATOM 3608 N TRP A1158 21.446 -10.156 -41.159 1.00 48.71 N ANISOU 3608 N TRP A1158 5881 6282 6343 1114 183 -448 N ATOM 3609 CA TRP A1158 21.591 -8.968 -40.319 1.00 49.29 C ANISOU 3609 CA TRP A1158 5938 6427 6360 1019 127 -327 C ATOM 3610 C TRP A1158 22.370 -7.844 -41.020 1.00 50.15 C ANISOU 3610 C TRP A1158 5878 6722 6452 904 261 -383 C ATOM 3611 O TRP A1158 23.012 -7.012 -40.363 1.00 51.00 O ANISOU 3611 O TRP A1158 5881 6886 6609 861 198 -348 O ATOM 3612 CB TRP A1158 22.293 -9.331 -39.015 1.00 51.25 C ANISOU 3612 CB TRP A1158 6132 6611 6728 1143 -71 -283 C ATOM 3613 CG TRP A1158 21.524 -10.254 -38.136 1.00 52.33 C ANISOU 3613 CG TRP A1158 6458 6573 6849 1212 -214 -157 C ATOM 3614 CD1 TRP A1158 21.483 -11.610 -38.209 1.00 53.54 C ANISOU 3614 CD1 TRP A1158 6655 6559 7128 1342 -281 -177 C ATOM 3615 CD2 TRP A1158 20.703 -9.885 -37.026 1.00 52.40 C ANISOU 3615 CD2 TRP A1158 6634 6559 6714 1143 -302 9 C ATOM 3616 NE1 TRP A1158 20.685 -12.110 -37.219 1.00 54.00 N ANISOU 3616 NE1 TRP A1158 6906 6483 7127 1336 -405 6 N ATOM 3617 CE2 TRP A1158 20.193 -11.072 -36.477 1.00 53.06 C ANISOU 3617 CE2 TRP A1158 6861 6474 6822 1214 -403 117 C ATOM 3618 CE3 TRP A1158 20.348 -8.662 -36.443 1.00 51.87 C ANISOU 3618 CE3 TRP A1158 6603 6598 6507 1026 -301 64 C ATOM 3619 CZ2 TRP A1158 19.346 -11.078 -35.371 1.00 54.51 C ANISOU 3619 CZ2 TRP A1158 7221 6630 6859 1153 -474 294 C ATOM 3620 CZ3 TRP A1158 19.505 -8.665 -35.347 1.00 51.67 C ANISOU 3620 CZ3 TRP A1158 6742 6548 6342 993 -376 196 C ATOM 3621 CH2 TRP A1158 19.013 -9.866 -34.821 1.00 53.68 C ANISOU 3621 CH2 TRP A1158 7135 6671 6587 1047 -446 318 C ATOM 3622 N ASP A1159 22.312 -7.804 -42.348 1.00 49.52 N ANISOU 3622 N ASP A1159 5778 6743 6295 837 443 -463 N ATOM 3623 CA ASP A1159 23.116 -6.848 -43.095 1.00 48.94 C ANISOU 3623 CA ASP A1159 5542 6857 6196 707 597 -493 C ATOM 3624 C ASP A1159 22.801 -5.428 -42.659 1.00 45.81 C ANISOU 3624 C ASP A1159 5200 6461 5745 539 551 -332 C ATOM 3625 O ASP A1159 23.693 -4.593 -42.576 1.00 46.55 O ANISOU 3625 O ASP A1159 5126 6642 5917 450 578 -325 O ATOM 3626 CB ASP A1159 22.893 -6.992 -44.605 1.00 49.93 C ANISOU 3626 CB ASP A1159 5696 7111 6165 637 801 -570 C ATOM 3627 CG ASP A1159 23.605 -8.195 -45.202 1.00 52.15 C ANISOU 3627 CG ASP A1159 5834 7449 6530 794 891 -806 C ATOM 3628 OD1 ASP A1159 24.705 -8.572 -44.734 1.00 53.53 O ANISOU 3628 OD1 ASP A1159 5788 7638 6910 915 859 -917 O ATOM 3629 OD2 ASP A1159 23.052 -8.756 -46.168 1.00 53.58 O ANISOU 3629 OD2 ASP A1159 6115 7662 6580 804 982 -901 O ATOM 3630 N ALA A1160 21.535 -5.158 -42.371 1.00 42.63 N ANISOU 3630 N ALA A1160 5011 5949 5235 497 474 -220 N ATOM 3631 CA ALA A1160 21.135 -3.818 -41.972 1.00 40.98 C ANISOU 3631 CA ALA A1160 4855 5712 5000 360 414 -100 C ATOM 3632 C ALA A1160 21.710 -3.447 -40.617 1.00 40.45 C ANISOU 3632 C ALA A1160 4702 5609 5055 403 261 -103 C ATOM 3633 O ALA A1160 22.167 -2.325 -40.422 1.00 42.54 O ANISOU 3633 O ALA A1160 4882 5897 5384 292 234 -76 O ATOM 3634 CB ALA A1160 19.619 -3.696 -41.939 1.00 39.14 C ANISOU 3634 CB ALA A1160 4840 5375 4655 334 363 -21 C ATOM 3635 N TYR A1161 21.719 -4.393 -39.689 1.00 38.85 N ANISOU 3635 N TYR A1161 4527 5348 4885 557 146 -133 N ATOM 3636 CA TYR A1161 21.974 -4.057 -38.296 1.00 38.45 C ANISOU 3636 CA TYR A1161 4461 5271 4876 599 -30 -119 C ATOM 3637 C TYR A1161 23.426 -4.159 -37.831 1.00 39.55 C ANISOU 3637 C TYR A1161 4379 5471 5175 671 -116 -200 C ATOM 3638 O TYR A1161 23.713 -4.711 -36.787 1.00 39.59 O ANISOU 3638 O TYR A1161 4389 5447 5206 796 -284 -203 O ATOM 3639 CB TYR A1161 21.040 -4.877 -37.420 1.00 37.78 C ANISOU 3639 CB TYR A1161 4560 5097 4694 695 -125 -60 C ATOM 3640 CG TYR A1161 19.615 -4.459 -37.626 1.00 36.16 C ANISOU 3640 CG TYR A1161 4526 4847 4366 606 -68 -1 C ATOM 3641 CD1 TYR A1161 19.117 -3.335 -36.994 1.00 35.64 C ANISOU 3641 CD1 TYR A1161 4500 4784 4256 531 -124 9 C ATOM 3642 CD2 TYR A1161 18.782 -5.159 -38.477 1.00 35.80 C ANISOU 3642 CD2 TYR A1161 4579 4752 4272 605 27 15 C ATOM 3643 CE1 TYR A1161 17.821 -2.928 -37.190 1.00 35.24 C ANISOU 3643 CE1 TYR A1161 4571 4688 4130 468 -83 39 C ATOM 3644 CE2 TYR A1161 17.474 -4.763 -38.677 1.00 35.26 C ANISOU 3644 CE2 TYR A1161 4635 4643 4118 529 59 57 C ATOM 3645 CZ TYR A1161 17.001 -3.644 -38.031 1.00 35.42 C ANISOU 3645 CZ TYR A1161 4679 4667 4111 466 6 70 C ATOM 3646 OH TYR A1161 15.699 -3.232 -38.224 1.00 36.83 O ANISOU 3646 OH TYR A1161 4951 4801 4242 410 26 88 O ATOM 3647 N GLY A1162 24.336 -3.562 -38.584 1.00 41.56 N ANISOU 3647 N GLY A1162 4434 5818 5536 577 -10 -256 N ATOM 3648 CA GLY A1162 25.737 -3.532 -38.190 1.00 44.53 C ANISOU 3648 CA GLY A1162 4551 6264 6102 625 -88 -352 C ATOM 3649 C GLY A1162 25.976 -2.828 -36.867 1.00 45.54 C ANISOU 3649 C GLY A1162 4664 6367 6271 624 -314 -352 C ATOM 3650 O GLY A1162 26.962 -3.113 -36.183 1.00 47.47 O ANISOU 3650 O GLY A1162 4743 6642 6650 726 -468 -428 O ATOM 3651 N SER A1163 25.078 -1.908 -36.512 1.00 45.36 N ANISOU 3651 N SER A1163 4806 6291 6138 519 -348 -288 N ATOM 3652 CA SER A1163 25.165 -1.151 -35.258 1.00 47.16 C ANISOU 3652 CA SER A1163 5043 6503 6371 513 -557 -325 C ATOM 3653 C SER A1163 24.812 -1.942 -33.991 1.00 48.40 C ANISOU 3653 C SER A1163 5349 6652 6388 675 -740 -310 C ATOM 3654 O SER A1163 25.134 -1.497 -32.891 1.00 49.78 O ANISOU 3654 O SER A1163 5506 6857 6550 699 -936 -368 O ATOM 3655 CB SER A1163 24.264 0.080 -35.327 1.00 46.28 C ANISOU 3655 CB SER A1163 5052 6325 6205 365 -530 -296 C ATOM 3656 OG SER A1163 22.897 -0.297 -35.460 1.00 45.05 O ANISOU 3656 OG SER A1163 5129 6119 5868 393 -458 -220 O ATOM 3657 N GLY A1164 24.158 -3.095 -34.138 1.00 49.32 N ANISOU 3657 N GLY A1164 5616 6730 6394 773 -685 -229 N ATOM 3658 CA GLY A1164 23.783 -3.946 -32.997 1.00 51.31 C ANISOU 3658 CA GLY A1164 6030 6966 6499 901 -841 -161 C ATOM 3659 C GLY A1164 24.926 -4.280 -32.050 1.00 55.58 C ANISOU 3659 C GLY A1164 6455 7549 7113 1025 -1085 -200 C ATOM 3660 O GLY A1164 26.060 -4.448 -32.493 1.00 56.64 O ANISOU 3660 O GLY A1164 6356 7699 7463 1072 -1107 -280 O ATOM 3661 N SER A1165 24.620 -4.383 -30.750 1.00 59.07 N ANISOU 3661 N SER A1165 7052 8026 7366 1077 -1267 -148 N ATOM 3662 CA SER A1165 25.625 -4.637 -29.697 1.00 63.86 C ANISOU 3662 CA SER A1165 7585 8685 7990 1197 -1555 -170 C ATOM 3663 C SER A1165 25.122 -5.590 -28.603 1.00 65.21 C ANISOU 3663 C SER A1165 8003 8855 7918 1296 -1710 -4 C ATOM 3664 O SER A1165 24.176 -6.359 -28.800 1.00 63.92 O ANISOU 3664 O SER A1165 8024 8616 7644 1291 -1585 138 O ATOM 3665 CB SER A1165 26.056 -3.323 -29.049 1.00 65.94 C ANISOU 3665 CB SER A1165 7752 9047 8252 1120 -1684 -318 C ATOM 3666 OG SER A1165 24.931 -2.615 -28.566 1.00 68.25 O ANISOU 3666 OG SER A1165 8239 9379 8311 1026 -1620 -324 O TER 3667 SER A1165 ATOM 3668 N ARG B 8 23.071 -70.567 -23.352 1.00 68.21 N ATOM 3669 CA ARG B 8 23.942 -69.752 -22.464 1.00 66.26 C ATOM 3670 C ARG B 8 23.802 -68.298 -22.869 1.00 66.72 C ATOM 3671 O ARG B 8 24.014 -67.934 -24.029 1.00 64.04 O ATOM 3672 CB ARG B 8 25.398 -70.197 -22.572 1.00 66.19 C ATOM 3673 CG ARG B 8 26.353 -69.529 -21.597 1.00 65.28 C ATOM 3674 CD ARG B 8 27.661 -69.222 -22.298 1.00 67.81 C ATOM 3675 NE ARG B 8 28.692 -68.725 -21.395 1.00 69.63 N ATOM 3676 CZ ARG B 8 29.902 -68.324 -21.785 1.00 72.67 C ATOM 3677 NH1 ARG B 8 30.777 -67.892 -20.883 1.00 73.66 N ATOM 3678 NH2 ARG B 8 30.246 -68.352 -23.073 1.00 73.42 N ATOM 3679 N ARG B 9 23.467 -67.474 -21.885 1.00 68.04 N ATOM 3680 CA ARG B 9 23.052 -66.103 -22.119 1.00 66.33 C ATOM 3681 C ARG B 9 23.468 -65.236 -20.936 1.00 64.24 C ATOM 3682 O ARG B 9 23.801 -65.763 -19.871 1.00 65.09 O ATOM 3683 CB ARG B 9 21.535 -66.065 -22.309 1.00 66.21 C ATOM 3684 CG ARG B 9 20.773 -67.030 -21.407 1.00 66.48 C ATOM 3685 CD ARG B 9 19.287 -66.733 -21.400 1.00 66.61 C ATOM 3686 NE ARG B 9 19.095 -65.297 -21.281 1.00 70.88 N ATOM 3687 CZ ARG B 9 18.401 -64.532 -22.117 1.00 72.66 C ATOM 3688 NH1 ARG B 9 18.345 -63.223 -21.886 1.00 74.09 N ATOM 3689 NH2 ARG B 9 17.744 -65.051 -23.152 1.00 69.60 N ATOM 3690 N PRO B 10 23.449 -63.904 -21.112 1.00 60.87 N ATOM 3691 CA PRO B 10 23.866 -63.063 -20.002 1.00 59.62 C ATOM 3692 C PRO B 10 22.867 -63.135 -18.866 1.00 57.68 C ATOM 3693 O PRO B 10 21.664 -63.249 -19.100 1.00 54.52 O ATOM 3694 CB PRO B 10 23.901 -61.648 -20.604 1.00 59.60 C ATOM 3695 CG PRO B 10 23.728 -61.824 -22.078 1.00 60.00 C ATOM 3696 CD PRO B 10 22.972 -63.103 -22.247 1.00 59.91 C ATOM 3697 N TYR B 11 23.384 -63.111 -17.648 1.00 60.19 N ATOM 3698 CA TYR B 11 22.554 -63.008 -16.451 1.00 63.42 C ATOM 3699 C TYR B 11 22.564 -61.565 -15.940 1.00 65.01 C ATOM 3700 O TYR B 11 21.654 -61.158 -15.215 1.00 66.28 O ATOM 3701 CB TYR B 11 23.020 -63.984 -15.358 1.00 61.65 C ATOM 3702 CG TYR B 11 24.518 -64.015 -15.144 1.00 60.82 C ATOM 3703 CD1 TYR B 11 25.136 -63.134 -14.265 1.00 60.23 C ATOM 3704 CD2 TYR B 11 25.318 -64.925 -15.825 1.00 60.82 C ATOM 3705 CE1 TYR B 11 26.508 -63.158 -14.071 1.00 58.62 C ATOM 3706 CE2 TYR B 11 26.689 -64.954 -15.639 1.00 60.01 C ATOM 3707 CZ TYR B 11 27.276 -64.068 -14.761 1.00 58.63 C ATOM 3708 OH TYR B 11 28.635 -64.104 -14.574 1.00 58.26 O ATOM 3709 N ILE B 12 23.581 -60.797 -16.340 1.00 64.44 N ATOM 3710 CA ILE B 12 23.732 -59.408 -15.912 1.00 63.74 C ATOM 3711 C ILE B 12 22.850 -58.465 -16.725 1.00 62.73 C ATOM 3712 O ILE B 12 22.734 -58.588 -17.941 1.00 57.60 O ATOM 3713 CB ILE B 12 25.208 -58.949 -16.000 1.00 64.69 C ATOM 3714 CG1 ILE B 12 26.034 -59.669 -14.940 1.00 64.23 C ATOM 3715 CG2 ILE B 12 25.347 -57.440 -15.804 1.00 65.49 C ATOM 3716 CD1 ILE B 12 27.527 -59.577 -15.160 1.00 65.86 C ATOM 3717 N LEU B 13 22.258 -57.507 -16.016 1.00 68.31 N ATOM 3718 CA LEU B 13 21.388 -56.488 -16.589 1.00 70.44 C ATOM 3719 C LEU B 13 21.932 -55.062 -16.315 1.00 73.34 C ATOM 3720 O LEU B 13 21.538 -54.098 -16.983 1.00 76.66 O ATOM 3721 CB LEU B 13 19.980 -56.660 -16.002 1.00 69.36 C ATOM 3722 CG LEU B 13 18.795 -56.017 -16.719 1.00 69.69 C ATOM 3723 CD1 LEU B 13 18.866 -56.260 -18.215 1.00 70.78 C ATOM 3724 CD2 LEU B 13 17.484 -56.549 -16.157 1.00 69.39 C ATOM 3725 OXT LEU B 13 22.785 -54.812 -15.443 1.00 69.77 O TER 3726 LEU B 13 HETATM 3727 OH2 1PE A1201 16.850 -31.434 -30.733 1.00 82.84 O HETATM 3728 C12 1PE A1201 17.273 -30.250 -31.418 1.00 86.33 C HETATM 3729 C22 1PE A1201 18.729 -30.399 -31.849 1.00 88.21 C HETATM 3730 OH3 1PE A1201 18.845 -31.189 -33.036 1.00 91.28 O HETATM 3731 C13 1PE A1201 19.780 -29.727 -34.743 1.00 93.85 C HETATM 3732 C23 1PE A1201 20.028 -30.896 -33.790 1.00 93.44 C HETATM 3733 OH4 1PE A1201 20.380 -28.534 -34.235 1.00 94.84 O HETATM 3734 C14 1PE A1201 21.263 -26.461 -35.213 1.00100.77 C HETATM 3735 C24 1PE A1201 20.049 -27.372 -35.005 1.00 99.22 C HETATM 3736 OH5 1PE A1201 22.343 -26.823 -34.346 1.00103.99 O HETATM 3737 C15 1PE A1201 23.220 -26.645 -32.072 1.00100.05 C HETATM 3738 C25 1PE A1201 22.554 -25.926 -33.247 1.00101.48 C HETATM 3739 OH6 1PE A1201 22.819 -28.023 -32.002 1.00100.06 O HETATM 3740 C16 1PE A1201 24.336 -29.373 -30.651 1.00 92.30 C HETATM 3741 C26 1PE A1201 23.889 -28.976 -32.057 1.00 96.02 C HETATM 3742 OH7 1PE A1201 24.983 -28.279 -29.993 1.00 90.84 O HETATM 3743 OH2 1PE A1202 27.724 -27.388 -25.729 1.00 86.57 O HETATM 3744 C12 1PE A1202 27.177 -26.153 -26.177 1.00 87.49 C HETATM 3745 C22 1PE A1202 28.040 -25.017 -25.671 1.00 88.85 C HETATM 3746 OH3 1PE A1202 27.577 -23.809 -26.247 1.00 92.85 O HETATM 3747 C13 1PE A1202 29.262 -22.264 -25.417 1.00 95.71 C HETATM 3748 C23 1PE A1202 27.799 -22.677 -25.415 1.00 95.28 C HETATM 3749 OH4 1PE A1202 29.409 -21.088 -24.634 1.00 96.32 O HETATM 3750 C14 1PE A1202 29.774 -20.414 -22.326 1.00101.66 C HETATM 3751 C24 1PE A1202 30.220 -21.295 -23.483 1.00101.04 C HETATM 3752 OH5 1PE A1202 30.714 -19.362 -22.174 1.00103.95 O HETATM 3753 C15 1PE A1202 32.732 -20.227 -21.167 1.00108.28 C HETATM 3754 C25 1PE A1202 31.450 -19.434 -20.959 1.00106.44 C HETATM 3755 OH6 1PE A1202 33.856 -19.400 -20.913 1.00108.68 O HETATM 3756 C16 1PE A1202 34.189 -17.467 -22.302 1.00108.41 C HETATM 3757 C26 1PE A1202 34.447 -18.954 -22.123 1.00109.64 C HETATM 3758 OH7 1PE A1202 35.426 -16.749 -22.291 1.00106.16 O HETATM 3759 N1 EPE A1203 0.715 1.348 -30.965 1.00 82.43 N HETATM 3760 C2 EPE A1203 0.801 -0.034 -30.479 1.00 82.42 C HETATM 3761 C3 EPE A1203 1.831 -0.091 -29.360 1.00 81.96 C HETATM 3762 N4 EPE A1203 3.159 0.375 -29.801 1.00 77.96 N HETATM 3763 C5 EPE A1203 3.084 1.691 -30.472 1.00 76.38 C HETATM 3764 C6 EPE A1203 2.014 1.711 -31.555 1.00 78.01 C HETATM 3765 C7 EPE A1203 4.016 0.456 -28.599 1.00 79.54 C HETATM 3766 C8 EPE A1203 5.389 -0.121 -28.893 1.00 81.18 C HETATM 3767 O8 EPE A1203 6.031 0.673 -29.900 1.00 87.79 O HETATM 3768 C9 EPE A1203 -0.386 1.465 -31.938 1.00 83.57 C HETATM 3769 C10 EPE A1203 -0.776 2.936 -32.080 1.00 84.16 C HETATM 3770 S EPE A1203 -0.505 3.517 -33.619 1.00 83.77 S HETATM 3771 O1S EPE A1203 0.695 2.910 -34.238 1.00 79.39 O HETATM 3772 O2S EPE A1203 -1.682 3.209 -34.455 1.00 87.44 O HETATM 3773 O3S EPE A1203 -0.351 4.985 -33.547 1.00 83.68 O HETATM 3774 CAC FLC A1204 38.512 -61.982 -12.267 1.00 91.07 C HETATM 3775 CA FLC A1204 37.347 -62.065 -13.233 1.00 92.89 C HETATM 3776 CB FLC A1204 37.037 -63.483 -13.739 1.00 92.49 C HETATM 3777 CBC FLC A1204 36.277 -64.271 -12.677 1.00 90.91 C HETATM 3778 CG FLC A1204 36.237 -63.399 -15.050 1.00 92.48 C HETATM 3779 CGC FLC A1204 35.060 -64.348 -15.067 1.00 94.43 C HETATM 3780 OA1 FLC A1204 39.548 -61.375 -12.638 1.00 84.98 O HETATM 3781 OA2 FLC A1204 38.380 -62.500 -11.133 1.00 87.49 O HETATM 3782 OB1 FLC A1204 36.682 -65.413 -12.375 1.00 92.64 O HETATM 3783 OB2 FLC A1204 35.259 -63.784 -12.129 1.00 86.44 O HETATM 3784 OG1 FLC A1204 35.272 -65.551 -15.324 1.00 96.84 O HETATM 3785 OG2 FLC A1204 33.916 -63.902 -14.821 1.00 95.50 O HETATM 3786 OHB FLC A1204 38.280 -64.141 -14.039 1.00 89.72 O HETATM 3787 C1 PEG A1205 35.602 -69.924 -24.929 1.00 20.00 C HETATM 3788 O1 PEG A1205 36.660 -69.783 -25.865 1.00 20.00 O HETATM 3789 C2 PEG A1205 34.409 -70.435 -25.697 1.00 20.00 C HETATM 3790 O2 PEG A1205 33.670 -71.272 -24.842 1.00 20.00 O HETATM 3791 C3 PEG A1205 33.052 -70.543 -23.801 1.00 20.00 C HETATM 3792 C4 PEG A1205 32.102 -71.468 -23.067 1.00 20.00 C HETATM 3793 O4 PEG A1205 32.458 -71.481 -21.692 1.00 20.00 O HETATM 3794 O HOH A1301 19.302 -64.312 -15.903 1.00 57.96 O HETATM 3795 O HOH A1302 18.799 -24.235 -21.037 1.00 59.51 O HETATM 3796 O HOH A1303 30.594 -56.849 -18.123 1.00 36.09 O HETATM 3797 O HOH A1304 34.337 -70.365 -9.657 1.00 54.84 O HETATM 3798 O HOH A1305 27.183 -24.287 -11.257 1.00 42.03 O HETATM 3799 O HOH A1306 37.224 -70.275 -14.182 1.00 56.10 O HETATM 3800 O HOH A1307 21.190 -73.852 -13.648 1.00 60.09 O HETATM 3801 O HOH A1308 18.229 -19.572 -16.567 1.00 74.09 O HETATM 3802 O HOH A1309 17.921 -20.901 -21.414 1.00 46.34 O HETATM 3803 O HOH A1310 17.143 -63.326 -17.768 1.00 53.67 O CONECT 664 1305 CONECT 1305 664 CONECT 3727 3728 CONECT 3728 3727 3729 CONECT 3729 3728 3730 CONECT 3730 3729 3732 CONECT 3731 3732 3733 CONECT 3732 3730 3731 CONECT 3733 3731 3735 CONECT 3734 3735 3736 CONECT 3735 3733 3734 CONECT 3736 3734 3738 CONECT 3737 3738 3739 CONECT 3738 3736 3737 CONECT 3739 3737 3741 CONECT 3740 3741 3742 CONECT 3741 3739 3740 CONECT 3742 3740 CONECT 3743 3744 CONECT 3744 3743 3745 CONECT 3745 3744 3746 CONECT 3746 3745 3748 CONECT 3747 3748 3749 CONECT 3748 3746 3747 CONECT 3749 3747 3751 CONECT 3750 3751 3752 CONECT 3751 3749 3750 CONECT 3752 3750 3754 CONECT 3753 3754 3755 CONECT 3754 3752 3753 CONECT 3755 3753 3757 CONECT 3756 3757 3758 CONECT 3757 3755 3756 CONECT 3758 3756 CONECT 3759 3760 3764 3768 CONECT 3760 3759 3761 CONECT 3761 3760 3762 CONECT 3762 3761 3763 3765 CONECT 3763 3762 3764 CONECT 3764 3759 3763 CONECT 3765 3762 3766 CONECT 3766 3765 3767 CONECT 3767 3766 CONECT 3768 3759 3769 CONECT 3769 3768 3770 CONECT 3770 3769 3771 3772 3773 CONECT 3771 3770 CONECT 3772 3770 CONECT 3773 3770 CONECT 3774 3775 3780 3781 CONECT 3775 3774 3776 CONECT 3776 3775 3777 3778 3786 CONECT 3777 3776 3782 3783 CONECT 3778 3776 3779 CONECT 3779 3778 3784 3785 CONECT 3780 3774 CONECT 3781 3774 CONECT 3782 3777 CONECT 3783 3777 CONECT 3784 3779 CONECT 3785 3779 CONECT 3786 3776 CONECT 3787 3788 3789 CONECT 3788 3787 CONECT 3789 3787 3790 CONECT 3790 3789 3791 CONECT 3791 3790 3792 CONECT 3792 3791 3793 CONECT 3793 3792 MASTER 573 0 5 23 5 0 6 6 3801 2 69 43 END