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*** 3S0E ***elNémo ID: 22060800463427577Job options:ID = 22060800463427577 JOBID = 3S0E USERID = unknown PRIVAT = 0 NMODES = 10 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = on DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 3S0E HEADER TRANSPORT PROTEIN 13-MAY-11 3S0E TITLE APIS MELLIFERA OBP14 IN COMPLEX WITH THE ODORANT EUGENOL (2-METHOXY- TITLE 2 4(2-PROPENYL)-PHENOL) COMPND MOL_ID: 1; COMPND 2 MOLECULE: OBP14; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 18-135; COMPND 5 SYNONYM: ODORANT BINDING PROTEIN 14; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA; SOURCE 3 ORGANISM_COMMON: HONEYBEE; SOURCE 4 ORGANISM_TAXID: 7460; SOURCE 5 GENE: NP_001035313; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-5 B(+) KEYWDS ALL HELICAL PROTEIN, UNKNOWN ODORANT MOLECULES, ANTENNAE, TRANSPORT KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.SPINELLI,A.LAGARDE,I.IOVINELLA,M.TEGONI,P.PELOSI,C.CAMBILLAU REVDAT 2 11-JAN-12 3S0E 1 JRNL REVDAT 1 30-NOV-11 3S0E 0 JRNL AUTH S.SPINELLI,A.LAGARDE,I.IOVINELLA,P.LEGRAND,M.TEGONI, JRNL AUTH 2 P.PELOSI,C.CAMBILLAU JRNL TITL CRYSTAL STRUCTURE OF APIS MELLIFERA OBP14, A C-MINUS JRNL TITL 2 ODORANT-BINDING PROTEIN, AND ITS COMPLEXES WITH ODORANT JRNL TITL 3 MOLECULES. JRNL REF INSECT BIOCHEM.MOL.BIOL. V. 42 41 2012 JRNL REFN ISSN 0965-1748 JRNL PMID 22075131 JRNL DOI 10.1016/J.IBMB.2011.10.005 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.39 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 17183 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) : 0.190 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180 REMARK 3 FREE R VALUE TEST SET COUNT : 890 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.70 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2635 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2093 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2497 REMARK 3 BIN R VALUE (WORKING SET) : 0.2074 REMARK 3 BIN FREE R VALUE : 0.2470 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.24 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 943 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 139 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.37 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 5.00290 REMARK 3 B22 (A**2) : -6.13650 REMARK 3 B33 (A**2) : 1.13350 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 975 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 1312 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 368 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 36 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 129 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 963 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 133 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 1293 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.07 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.61 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.79 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: A 1 A 10 REMARK 3 ORIGIN FOR THE GROUP (A): -2.5236 -1.2336 -12.3114 REMARK 3 T TENSOR REMARK 3 T11: 0.0158 T22: -0.0130 REMARK 3 T33: -0.0034 T12: 0.0175 REMARK 3 T13: -0.0062 T23: -0.0094 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.0438 REMARK 3 L33: 0.0415 L12: -0.0850 REMARK 3 L13: 0.0293 L23: -0.0460 REMARK 3 S TENSOR REMARK 3 S11: 0.0003 S12: -0.0005 S13: 0.0030 REMARK 3 S21: -0.0012 S22: -0.0012 S23: 0.0016 REMARK 3 S31: -0.0016 S32: 0.0012 S33: 0.0009 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: A 11 A 20 REMARK 3 ORIGIN FOR THE GROUP (A): -6.7950 -13.1349 -19.7384 REMARK 3 T TENSOR REMARK 3 T11: 0.0038 T22: -0.0085 REMARK 3 T33: -0.0036 T12: 0.0089 REMARK 3 T13: -0.0292 T23: 0.0058 REMARK 3 L TENSOR REMARK 3 L11: 0.0172 L22: 0.0851 REMARK 3 L33: 0.0647 L12: -0.0942 REMARK 3 L13: 0.1106 L23: -0.0954 REMARK 3 S TENSOR REMARK 3 S11: 0.0008 S12: -0.0005 S13: 0.0007 REMARK 3 S21: -0.0010 S22: 0.0006 S23: 0.0032 REMARK 3 S31: -0.0025 S32: -0.0018 S33: -0.0014 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: A 21 A 30 REMARK 3 ORIGIN FOR THE GROUP (A): -8.7118 -21.2512 -13.0302 REMARK 3 T TENSOR REMARK 3 T11: -0.0010 T22: -0.0024 REMARK 3 T33: 0.0020 T12: -0.0027 REMARK 3 T13: -0.0047 T23: -0.0137 REMARK 3 L TENSOR REMARK 3 L11: 0.0384 L22: 0.0368 REMARK 3 L33: 0.0000 L12: 0.0482 REMARK 3 L13: 0.0330 L23: 0.0360 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: -0.0015 S13: 0.0000 REMARK 3 S21: -0.0014 S22: -0.0018 S23: 0.0063 REMARK 3 S31: 0.0030 S32: -0.0011 S33: 0.0019 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: A 31 A 40 REMARK 3 ORIGIN FOR THE GROUP (A): -0.8091 -22.7215 -9.2514 REMARK 3 T TENSOR REMARK 3 T11: 0.0048 T22: -0.0042 REMARK 3 T33: -0.0056 T12: 0.0178 REMARK 3 T13: -0.0165 T23: -0.0153 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.0030 REMARK 3 L33: 0.0405 L12: -0.0950 REMARK 3 L13: 0.2262 L23: 0.0592 REMARK 3 S TENSOR REMARK 3 S11: 0.0001 S12: -0.0095 S13: -0.0046 REMARK 3 S21: -0.0009 S22: -0.0010 S23: 0.0006 REMARK 3 S31: 0.0041 S32: -0.0035 S33: 0.0009 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: A 41 A 50 REMARK 3 ORIGIN FOR THE GROUP (A): -0.3215 -21.0566 -18.3989 REMARK 3 T TENSOR REMARK 3 T11: 0.0148 T22: -0.0144 REMARK 3 T33: 0.0073 T12: 0.0262 REMARK 3 T13: -0.0206 T23: -0.0393 REMARK 3 L TENSOR REMARK 3 L11: 0.0978 L22: 0.0478 REMARK 3 L33: 0.0533 L12: 0.0321 REMARK 3 L13: 0.0398 L23: 0.0805 REMARK 3 S TENSOR REMARK 3 S11: 0.0006 S12: 0.0073 S13: 0.0003 REMARK 3 S21: 0.0012 S22: 0.0012 S23: 0.0030 REMARK 3 S31: 0.0017 S32: 0.0027 S33: -0.0018 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: A 51 A 60 REMARK 3 ORIGIN FOR THE GROUP (A): 7.3821 -12.4562 -21.7971 REMARK 3 T TENSOR REMARK 3 T11: 0.0040 T22: 0.0012 REMARK 3 T33: -0.0031 T12: -0.0028 REMARK 3 T13: -0.0116 T23: 0.0222 REMARK 3 L TENSOR REMARK 3 L11: 0.0330 L22: 0.0346 REMARK 3 L33: 0.0046 L12: 0.0043 REMARK 3 L13: 0.0511 L23: -0.0326 REMARK 3 S TENSOR REMARK 3 S11: -0.0006 S12: 0.0031 S13: 0.0018 REMARK 3 S21: -0.0019 S22: 0.0003 S23: 0.0001 REMARK 3 S31: 0.0007 S32: 0.0022 S33: 0.0003 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: A 61 A 70 REMARK 3 ORIGIN FOR THE GROUP (A): 12.5709 -9.6730 -16.5647 REMARK 3 T TENSOR REMARK 3 T11: -0.0046 T22: 0.0019 REMARK 3 T33: -0.0015 T12: -0.0034 REMARK 3 T13: -0.0014 T23: 0.0037 REMARK 3 L TENSOR REMARK 3 L11: 0.0278 L22: 0.0025 REMARK 3 L33: 0.0015 L12: -0.0038 REMARK 3 L13: 0.0165 L23: -0.0022 REMARK 3 S TENSOR REMARK 3 S11: 0.0006 S12: 0.0015 S13: -0.0002 REMARK 3 S21: 0.0012 S22: 0.0004 S23: -0.0006 REMARK 3 S31: -0.0030 S32: 0.0021 S33: -0.0011 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: A 71 A 80 REMARK 3 ORIGIN FOR THE GROUP (A): 9.7593 -3.7074 -5.4056 REMARK 3 T TENSOR REMARK 3 T11: -0.0091 T22: -0.0064 REMARK 3 T33: 0.0081 T12: -0.0078 REMARK 3 T13: -0.0119 T23: -0.0295 REMARK 3 L TENSOR REMARK 3 L11: 0.0000 L22: 0.0631 REMARK 3 L33: 0.0000 L12: -0.0133 REMARK 3 L13: 0.0430 L23: 0.1033 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: -0.0004 S13: 0.0014 REMARK 3 S21: -0.0011 S22: -0.0003 S23: 0.0011 REMARK 3 S31: -0.0040 S32: 0.0016 S33: 0.0003 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: A 81 A 90 REMARK 3 ORIGIN FOR THE GROUP (A): 15.8085 -12.6113 -7.5771 REMARK 3 T TENSOR REMARK 3 T11: -0.0160 T22: 0.0203 REMARK 3 T33: 0.0007 T12: 0.0009 REMARK 3 T13: -0.0081 T23: -0.0294 REMARK 3 L TENSOR REMARK 3 L11: 0.0870 L22: 0.0050 REMARK 3 L33: 0.0025 L12: -0.0414 REMARK 3 L13: 0.0198 L23: 0.0717 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: 0.0002 S13: 0.0007 REMARK 3 S21: 0.0012 S22: -0.0020 S23: -0.0002 REMARK 3 S31: -0.0012 S32: 0.0009 S33: 0.0020 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: A 91 A 100 REMARK 3 ORIGIN FOR THE GROUP (A): 10.6463 -24.4883 -18.0195 REMARK 3 T TENSOR REMARK 3 T11: -0.0079 T22: 0.0041 REMARK 3 T33: 0.0004 T12: 0.0184 REMARK 3 T13: -0.0168 T23: -0.0402 REMARK 3 L TENSOR REMARK 3 L11: 0.0743 L22: 0.0002 REMARK 3 L33: 0.0143 L12: -0.0181 REMARK 3 L13: 0.0080 L23: 0.0922 REMARK 3 S TENSOR REMARK 3 S11: -0.0006 S12: -0.0001 S13: 0.0005 REMARK 3 S21: -0.0042 S22: 0.0006 S23: -0.0013 REMARK 3 S31: -0.0014 S32: 0.0030 S33: 0.0000 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: A 101 A 110 REMARK 3 ORIGIN FOR THE GROUP (A): 7.3803 -17.7479 -8.0322 REMARK 3 T TENSOR REMARK 3 T11: -0.0181 T22: 0.0113 REMARK 3 T33: -0.0018 T12: 0.0035 REMARK 3 T13: -0.0285 T23: -0.0333 REMARK 3 L TENSOR REMARK 3 L11: 0.0919 L22: 0.0142 REMARK 3 L33: 0.0289 L12: -0.0601 REMARK 3 L13: 0.1250 L23: 0.0431 REMARK 3 S TENSOR REMARK 3 S11: 0.0005 S12: -0.0075 S13: 0.0019 REMARK 3 S21: 0.0000 S22: -0.0003 S23: -0.0007 REMARK 3 S31: 0.0025 S32: 0.0016 S33: -0.0003 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: A 111 A 119 REMARK 3 ORIGIN FOR THE GROUP (A): -2.8395 -8.1337 -4.2900 REMARK 3 T TENSOR REMARK 3 T11: -0.0087 T22: 0.0175 REMARK 3 T33: -0.0175 T12: 0.0057 REMARK 3 T13: 0.0025 T23: -0.0576 REMARK 3 L TENSOR REMARK 3 L11: 0.0612 L22: 0.0059 REMARK 3 L33: 0.0378 L12: 0.0533 REMARK 3 L13: 0.0312 L23: 0.1281 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: 0.0041 S13: -0.0007 REMARK 3 S21: 0.0026 S22: 0.0021 S23: -0.0008 REMARK 3 S31: -0.0045 S32: 0.0004 S33: -0.0021 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3S0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11. REMARK 100 THE RCSB ID CODE IS RCSB065602. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-FEB-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8265 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17204 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 45.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 9.600 REMARK 200 R MERGE (I) : 0.01000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2 REMARK 200 DATA REDUNDANCY IN SHELL : 5.50 REMARK 200 R MERGE FOR SHELL (I) : 0.36000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 4.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3S0A REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-1.9 M TRI-SODIUM CITRATE, 25 MM REMARK 280 CHES, PH 9.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 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 17.30500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.99500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.13000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.99500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.30500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.13000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 203 DISTANCE = 6.25 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EOL A 120 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3RZS RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH TA6BR14 REMARK 900 RELATED ID: 3S0A RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14, NATIVE APO-PROTEIN REMARK 900 RELATED ID: 3S0B RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE FLUORESCENT PROBE REMARK 900 1-N-PHENYLNAPHTHYLAMINE REMARK 900 RELATED ID: 3S0D RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP 14 IN COMPLEX WITH THE CITRUS ODORANT REMARK 900 CITRALVA REMARK 900 RELATED ID: 3S0F RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14, NATIVE APO, CRYSTAL FORM 2 REMARK 900 RELATED ID: 3S0G RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP 14 DOUBLE MUTANT GLN44CYS, HIS97CYS DBREF 3S0E A 2 119 UNP Q1W640 Q1W640_APIME 18 135 SEQADV 3S0E MET A 1 UNP Q1W640 INITIATING METHIONINE SEQRES 1 A 119 MET THR ILE GLU GLU LEU LYS THR ARG LEU HIS THR GLU SEQRES 2 A 119 GLN SER VAL CYS LYS THR GLU THR GLY ILE ASP GLN GLN SEQRES 3 A 119 LYS ALA ASN ASP VAL ILE GLU GLY ASN ILE ASP VAL GLU SEQRES 4 A 119 ASP LYS LYS VAL GLN LEU TYR CYS GLU CYS ILE LEU LYS SEQRES 5 A 119 ASN PHE ASN ILE LEU ASP LYS ASN ASN VAL PHE LYS PRO SEQRES 6 A 119 GLN GLY ILE LYS ALA VAL MET GLU LEU LEU ILE ASP GLU SEQRES 7 A 119 ASN SER VAL LYS GLN LEU VAL SER ASP CYS SER THR ILE SEQRES 8 A 119 SER GLU GLU ASN PRO HIS LEU LYS ALA SER LYS LEU VAL SEQRES 9 A 119 GLN CYS VAL SER LYS TYR LYS THR MET LYS SER VAL ASP SEQRES 10 A 119 PHE LEU HET EOL A 120 12 HETNAM EOL 2-METHOXY-4-(PROP-2-EN-1-YL)PHENOL HETSYN EOL EUGENOL FORMUL 2 EOL C10 H12 O2 FORMUL 3 HOH *139(H2 O) HELIX 1 1 THR A 2 GLY A 22 1 21 HELIX 2 2 ASP A 24 GLU A 33 1 10 HELIX 3 3 ASP A 40 PHE A 54 1 15 HELIX 4 4 LYS A 64 GLU A 73 1 10 HELIX 5 5 ASP A 77 SER A 89 1 13 HELIX 6 6 ASN A 95 LYS A 109 1 15 HELIX 7 7 MET A 113 LEU A 119 5 7 SSBOND 1 CYS A 17 CYS A 49 1555 1555 2.05 SSBOND 2 CYS A 88 CYS A 106 1555 1555 2.05 SITE 1 AC1 9 ILE A 56 ILE A 68 VAL A 71 LEU A 75 SITE 2 AC1 9 VAL A 107 SER A 108 LYS A 111 THR A 112 SITE 3 AC1 9 MET A 113 CRYST1 34.610 40.260 91.990 90.00 90.00 90.00 P 21 21 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 0.028893 0.000000 0.000000 0.00000 SCALE2 0.000000 0.024839 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010871 0.00000 ATOM 1 N MET A 1 3.756 3.534 -14.028 1.00 42.17 N ANISOU 1 N MET A 1 5493 5210 5318 171 -64 -80 N ATOM 2 CA MET A 1 2.506 2.818 -13.794 1.00 41.29 C ANISOU 2 CA MET A 1 5385 5100 5204 172 -63 -85 C ATOM 3 C MET A 1 2.074 2.981 -12.341 1.00 44.04 C ANISOU 3 C MET A 1 5735 5447 5552 171 -65 -88 C ATOM 4 O MET A 1 2.878 2.771 -11.435 1.00 44.16 O ANISOU 4 O MET A 1 5749 5461 5567 170 -67 -88 O ATOM 5 CB MET A 1 2.662 1.328 -14.175 1.00 43.43 C ANISOU 5 CB MET A 1 5656 5373 5472 174 -61 -84 C ATOM 6 CG MET A 1 1.447 0.456 -13.842 1.00 46.57 C ANISOU 6 CG MET A 1 6057 5772 5868 174 -61 -88 C ATOM 7 SD MET A 1 1.394 -1.185 -14.614 1.00 50.27 S ANISOU 7 SD MET A 1 6526 6241 6332 177 -60 -87 S ATOM 8 CE MET A 1 3.042 -1.801 -14.257 1.00 47.08 C ANISOU 8 CE MET A 1 6122 5841 5927 177 -59 -84 C ATOM 9 N THR A 2 0.814 3.366 -12.117 1.00 39.85 N ANISOU 9 N THR A 2 5206 4915 5020 171 -66 -91 N ATOM 10 CA THR A 2 0.301 3.506 -10.757 1.00 39.25 C ANISOU 10 CA THR A 2 5132 4838 4943 172 -67 -93 C ATOM 11 C THR A 2 -0.180 2.136 -10.282 1.00 41.14 C ANISOU 11 C THR A 2 5371 5079 5180 173 -65 -94 C ATOM 12 O THR A 2 -0.237 1.190 -11.077 1.00 39.63 O ANISOU 12 O THR A 2 5179 4889 4988 173 -63 -94 O ATOM 13 CB THR A 2 -0.816 4.563 -10.666 1.00 48.12 C ANISOU 13 CB THR A 2 6258 5961 6066 173 -69 -94 C ATOM 14 OG1 THR A 2 -1.968 4.114 -11.375 1.00 47.76 O ANISOU 14 OG1 THR A 2 6212 5916 6018 174 -66 -95 O ATOM 15 CG2 THR A 2 -0.379 5.946 -11.142 1.00 47.89 C ANISOU 15 CG2 THR A 2 6229 5930 6038 172 -71 -93 C ATOM 16 N ILE A 3 -0.533 2.036 -8.991 1.00 36.62 N ANISOU 16 N ILE A 3 4800 4507 4608 175 -66 -96 N ATOM 17 CA ILE A 3 -1.079 0.822 -8.386 1.00 35.33 C ANISOU 17 CA ILE A 3 4637 4345 4443 177 -64 -97 C ATOM 18 C ILE A 3 -2.429 0.529 -9.018 1.00 36.97 C ANISOU 18 C ILE A 3 4843 4553 4649 177 -63 -96 C ATOM 19 O ILE A 3 -2.683 -0.609 -9.417 1.00 35.80 O ANISOU 19 O ILE A 3 4694 4406 4501 177 -61 -96 O ATOM 20 CB ILE A 3 -1.182 0.980 -6.839 1.00 38.37 C ANISOU 20 CB ILE A 3 5023 4729 4827 180 -65 -98 C ATOM 21 CG1 ILE A 3 0.216 1.019 -6.180 1.00 38.72 C ANISOU 21 CG1 ILE A 3 5068 4772 4872 180 -67 -99 C ATOM 22 CG2 ILE A 3 -2.094 -0.086 -6.197 1.00 38.55 C ANISOU 22 CG2 ILE A 3 5046 4754 4849 183 -62 -98 C ATOM 23 CD1 ILE A 3 1.169 -0.136 -6.536 1.00 45.23 C ANISOU 23 CD1 ILE A 3 5890 5598 5696 178 -64 -99 C ATOM 24 N GLU A 4 -3.278 1.577 -9.136 1.00 32.66 N ANISOU 24 N GLU A 4 4298 4006 4103 178 -63 -96 N ATOM 25 CA GLU A 4 -4.607 1.467 -9.727 1.00 31.76 C ANISOU 25 CA GLU A 4 4184 3893 3989 178 -62 -95 C ATOM 26 C GLU A 4 -4.518 1.018 -11.186 1.00 31.94 C ANISOU 26 C GLU A 4 4207 3917 4014 176 -62 -95 C ATOM 27 O GLU A 4 -5.334 0.209 -11.620 1.00 31.80 O ANISOU 27 O GLU A 4 4188 3900 3996 176 -62 -94 O ATOM 28 CB GLU A 4 -5.389 2.781 -9.581 1.00 33.40 C ANISOU 28 CB GLU A 4 4394 4101 4195 180 -63 -95 C ATOM 29 CG GLU A 4 -5.867 3.052 -8.157 1.00 44.56 C ANISOU 29 CG GLU A 4 5809 5514 5607 184 -64 -94 C ATOM 30 CD GLU A 4 -6.822 2.049 -7.531 1.00 65.10 C ANISOU 30 CD GLU A 4 8409 8117 8208 186 -62 -92 C ATOM 31 OE1 GLU A 4 -7.703 1.523 -8.250 1.00 54.43 O ANISOU 31 OE1 GLU A 4 7055 6767 6858 185 -60 -90 O ATOM 32 OE2 GLU A 4 -6.706 1.812 -6.307 1.00 62.72 O ANISOU 32 OE2 GLU A 4 8108 7816 7907 190 -61 -91 O ATOM 33 N GLU A 5 -3.488 1.489 -11.915 1.00 26.86 N ANISOU 33 N GLU A 5 3563 3272 3370 175 -62 -95 N ATOM 34 CA GLU A 5 -3.244 1.103 -13.308 1.00 25.78 C ANISOU 34 CA GLU A 5 3426 3136 3234 175 -62 -94 C ATOM 35 C GLU A 5 -2.764 -0.335 -13.379 1.00 26.54 C ANISOU 35 C GLU A 5 3521 3232 3329 175 -62 -94 C ATOM 36 O GLU A 5 -3.189 -1.065 -14.274 1.00 24.75 O ANISOU 36 O GLU A 5 3295 3006 3102 177 -62 -94 O ATOM 37 CB GLU A 5 -2.262 2.055 -13.988 1.00 27.64 C ANISOU 37 CB GLU A 5 3661 3370 3469 175 -62 -93 C ATOM 38 CG GLU A 5 -2.972 3.296 -14.504 1.00 37.93 C ANISOU 38 CG GLU A 5 4965 4673 4773 175 -62 -94 C ATOM 39 CD GLU A 5 -2.134 4.529 -14.770 1.00 57.32 C ANISOU 39 CD GLU A 5 7421 7128 7230 175 -62 -93 C ATOM 40 OE1 GLU A 5 -0.886 4.420 -14.796 1.00 44.20 O ANISOU 40 OE1 GLU A 5 5757 5466 5570 174 -62 -90 O ATOM 41 OE2 GLU A 5 -2.735 5.609 -14.970 1.00 52.79 O ANISOU 41 OE2 GLU A 5 6849 6554 6656 175 -62 -94 O ATOM 42 N LEU A 6 -1.918 -0.755 -12.419 1.00 21.73 N ANISOU 42 N LEU A 6 2912 2624 2719 175 -62 -94 N ATOM 43 CA LEU A 6 -1.437 -2.142 -12.362 1.00 20.21 C ANISOU 43 CA LEU A 6 2720 2433 2526 175 -61 -93 C ATOM 44 C LEU A 6 -2.600 -3.089 -12.047 1.00 21.69 C ANISOU 44 C LEU A 6 2908 2621 2714 175 -61 -94 C ATOM 45 O LEU A 6 -2.688 -4.155 -12.662 1.00 18.98 O ANISOU 45 O LEU A 6 2566 2278 2370 176 -62 -94 O ATOM 46 CB LEU A 6 -0.290 -2.312 -11.346 1.00 20.00 C ANISOU 46 CB LEU A 6 2693 2407 2498 175 -60 -94 C ATOM 47 CG LEU A 6 0.246 -3.750 -11.135 1.00 23.07 C ANISOU 47 CG LEU A 6 3082 2798 2885 175 -60 -94 C ATOM 48 CD1 LEU A 6 0.780 -4.368 -12.428 1.00 22.49 C ANISOU 48 CD1 LEU A 6 3010 2725 2809 176 -60 -92 C ATOM 49 CD2 LEU A 6 1.290 -3.790 -10.042 1.00 24.04 C ANISOU 49 CD2 LEU A 6 3205 2922 3007 175 -59 -95 C ATOM 50 N LYS A 7 -3.488 -2.696 -11.099 1.00 18.99 N ANISOU 50 N LYS A 7 2564 2278 2373 176 -61 -94 N ATOM 51 CA LYS A 7 -4.688 -3.460 -10.736 1.00 19.47 C ANISOU 51 CA LYS A 7 2624 2338 2435 176 -61 -93 C ATOM 52 C LYS A 7 -5.519 -3.762 -11.993 1.00 22.18 C ANISOU 52 C LYS A 7 2968 2681 2780 176 -63 -93 C ATOM 53 O LYS A 7 -5.863 -4.918 -12.239 1.00 20.68 O ANISOU 53 O LYS A 7 2777 2490 2591 175 -65 -92 O ATOM 54 CB LYS A 7 -5.571 -2.678 -9.739 1.00 21.96 C ANISOU 54 CB LYS A 7 2938 2654 2751 178 -60 -93 C ATOM 55 CG LYS A 7 -5.186 -2.808 -8.285 1.00 38.58 C ANISOU 55 CG LYS A 7 5043 4759 4855 180 -58 -93 C ATOM 56 CD LYS A 7 -6.292 -2.260 -7.393 1.00 49.92 C ANISOU 56 CD LYS A 7 6479 6196 6292 183 -58 -91 C ATOM 57 CE LYS A 7 -5.752 -1.494 -6.213 1.00 61.16 C ANISOU 57 CE LYS A 7 7905 7619 7714 187 -57 -92 C ATOM 58 NZ LYS A 7 -6.808 -1.239 -5.198 1.00 70.78 N ANISOU 58 NZ LYS A 7 9123 8838 8931 192 -56 -89 N ATOM 59 N THR A 8 -5.822 -2.718 -12.788 1.00 19.29 N ANISOU 59 N THR A 8 2602 2313 2413 176 -63 -93 N ATOM 60 CA THR A 8 -6.587 -2.815 -14.030 1.00 18.64 C ANISOU 60 CA THR A 8 2520 2230 2332 176 -65 -93 C ATOM 61 C THR A 8 -5.864 -3.699 -15.055 1.00 21.27 C ANISOU 61 C THR A 8 2855 2562 2664 178 -67 -94 C ATOM 62 O THR A 8 -6.493 -4.548 -15.697 1.00 20.25 O ANISOU 62 O THR A 8 2726 2430 2536 178 -70 -94 O ATOM 63 CB THR A 8 -6.844 -1.399 -14.579 1.00 26.32 C ANISOU 63 CB THR A 8 3494 3203 3305 177 -65 -94 C ATOM 64 OG1 THR A 8 -7.547 -0.647 -13.588 1.00 28.51 O ANISOU 64 OG1 THR A 8 3770 3481 3582 177 -63 -94 O ATOM 65 CG2 THR A 8 -7.624 -1.397 -15.898 1.00 25.20 C ANISOU 65 CG2 THR A 8 3353 3059 3164 178 -66 -95 C ATOM 66 N ARG A 9 -4.543 -3.486 -15.211 1.00 17.37 N ANISOU 66 N ARG A 9 2363 2070 2168 178 -66 -94 N ATOM 67 CA ARG A 9 -3.725 -4.238 -16.154 1.00 15.81 C ANISOU 67 CA ARG A 9 2167 1871 1968 181 -67 -93 C ATOM 68 C ARG A 9 -3.722 -5.716 -15.786 1.00 18.13 C ANISOU 68 C ARG A 9 2462 2165 2261 181 -69 -93 C ATOM 69 O ARG A 9 -3.883 -6.558 -16.672 1.00 16.91 O ANISOU 69 O ARG A 9 2310 2009 2105 183 -73 -92 O ATOM 70 CB ARG A 9 -2.298 -3.662 -16.205 1.00 17.12 C ANISOU 70 CB ARG A 9 2333 2040 2132 182 -65 -92 C ATOM 71 CG ARG A 9 -1.357 -4.410 -17.124 1.00 18.49 C ANISOU 71 CG ARG A 9 2510 2214 2303 185 -66 -90 C ATOM 72 CD ARG A 9 -1.693 -4.296 -18.605 1.00 18.80 C ANISOU 72 CD ARG A 9 2551 2251 2341 190 -68 -89 C ATOM 73 NE ARG A 9 -0.785 -5.146 -19.363 1.00 19.68 N ANISOU 73 NE ARG A 9 2665 2363 2448 195 -69 -86 N ATOM 74 CZ ARG A 9 0.476 -4.833 -19.639 1.00 23.81 C ANISOU 74 CZ ARG A 9 3188 2888 2969 198 -66 -83 C ATOM 75 NH1 ARG A 9 0.956 -3.639 -19.305 1.00 19.55 N ANISOU 75 NH1 ARG A 9 2645 2350 2432 195 -63 -82 N ATOM 76 NH2 ARG A 9 1.254 -5.688 -20.278 1.00 20.61 N ANISOU 76 NH2 ARG A 9 2787 2485 2559 203 -67 -80 N ATOM 77 N LEU A 10 -3.552 -6.034 -14.496 1.00 14.78 N ANISOU 77 N LEU A 10 2036 1743 1837 178 -68 -93 N ATOM 78 CA LEU A 10 -3.577 -7.439 -14.059 1.00 13.15 C ANISOU 78 CA LEU A 10 1830 1536 1630 178 -69 -93 C ATOM 79 C LEU A 10 -4.934 -8.062 -14.354 1.00 17.19 C ANISOU 79 C LEU A 10 2342 2045 2145 177 -73 -92 C ATOM 80 O LEU A 10 -4.974 -9.161 -14.887 1.00 16.65 O ANISOU 80 O LEU A 10 2276 1975 2076 178 -76 -92 O ATOM 81 CB LEU A 10 -3.254 -7.564 -12.566 1.00 13.55 C ANISOU 81 CB LEU A 10 1879 1589 1680 176 -66 -93 C ATOM 82 CG LEU A 10 -1.780 -7.438 -12.200 1.00 16.77 C ANISOU 82 CG LEU A 10 2287 1999 2084 177 -63 -94 C ATOM 83 CD1 LEU A 10 -1.633 -7.129 -10.722 1.00 18.75 C ANISOU 83 CD1 LEU A 10 2537 2251 2337 176 -60 -95 C ATOM 84 CD2 LEU A 10 -1.006 -8.715 -12.540 1.00 16.02 C ANISOU 84 CD2 LEU A 10 2196 1906 1986 178 -64 -93 C ATOM 85 N HIS A 11 -6.046 -7.358 -14.059 1.00 15.01 N ANISOU 85 N HIS A 11 1990 1830 1884 108 -309 55 N ATOM 86 CA HIS A 11 -7.370 -7.903 -14.373 1.00 15.51 C ANISOU 86 CA HIS A 11 2048 1899 1944 110 -302 55 C ATOM 87 C HIS A 11 -7.524 -8.169 -15.875 1.00 17.81 C ANISOU 87 C HIS A 11 2335 2193 2239 103 -300 56 C ATOM 88 O HIS A 11 -8.053 -9.209 -16.254 1.00 18.67 O ANISOU 88 O HIS A 11 2439 2306 2350 101 -295 57 O ATOM 89 CB HIS A 11 -8.497 -6.981 -13.874 1.00 17.70 C ANISOU 89 CB HIS A 11 2330 2178 2216 118 -304 55 C ATOM 90 CG HIS A 11 -8.577 -6.841 -12.384 1.00 22.74 C ANISOU 90 CG HIS A 11 2975 2816 2850 129 -305 55 C ATOM 91 ND1 HIS A 11 -8.224 -7.875 -11.534 1.00 25.43 N ANISOU 91 ND1 HIS A 11 3314 3157 3192 130 -302 56 N ATOM 92 CD2 HIS A 11 -9.003 -5.793 -11.641 1.00 25.63 C ANISOU 92 CD2 HIS A 11 3350 3181 3209 139 -310 55 C ATOM 93 CE1 HIS A 11 -8.437 -7.423 -10.308 1.00 25.52 C ANISOU 93 CE1 HIS A 11 3333 3166 3197 141 -304 56 C ATOM 94 NE2 HIS A 11 -8.895 -6.172 -10.323 1.00 26.07 N ANISOU 94 NE2 HIS A 11 3409 3235 3262 148 -310 55 N ATOM 95 N THR A 12 -7.044 -7.234 -16.726 1.00 15.26 N ANISOU 95 N THR A 12 2012 1868 1918 100 -304 56 N ATOM 96 CA THR A 12 -7.131 -7.373 -18.182 1.00 14.70 C ANISOU 96 CA THR A 12 1937 1799 1849 95 -302 56 C ATOM 97 C THR A 12 -6.357 -8.611 -18.629 1.00 16.05 C ANISOU 97 C THR A 12 2105 1971 2023 92 -298 57 C ATOM 98 O THR A 12 -6.924 -9.462 -19.329 1.00 15.14 O ANISOU 98 O THR A 12 1987 1859 1908 91 -295 57 O ATOM 99 CB THR A 12 -6.666 -6.084 -18.874 1.00 21.57 C ANISOU 99 CB THR A 12 2808 2666 2720 93 -307 57 C ATOM 100 OG1 THR A 12 -7.532 -5.026 -18.486 1.00 19.83 O ANISOU 100 OG1 THR A 12 2593 2446 2496 97 -311 55 O ATOM 101 CG2 THR A 12 -6.661 -6.201 -20.394 1.00 21.08 C ANISOU 101 CG2 THR A 12 2742 2606 2660 90 -304 58 C ATOM 102 N GLU A 13 -5.087 -8.743 -18.192 1.00 13.55 N ANISOU 102 N GLU A 13 1788 1652 1708 90 -300 59 N ATOM 103 CA GLU A 13 -4.281 -9.898 -18.601 1.00 11.56 C ANISOU 103 CA GLU A 13 1533 1402 1457 88 -297 60 C ATOM 104 C GLU A 13 -4.837 -11.199 -18.089 1.00 14.17 C ANISOU 104 C GLU A 13 1863 1734 1787 89 -294 58 C ATOM 105 O GLU A 13 -4.787 -12.211 -18.794 1.00 15.10 O ANISOU 105 O GLU A 13 1979 1854 1904 88 -292 58 O ATOM 106 CB GLU A 13 -2.794 -9.749 -18.231 1.00 12.99 C ANISOU 106 CB GLU A 13 1714 1580 1641 86 -300 63 C ATOM 107 CG GLU A 13 -2.132 -8.500 -18.801 1.00 17.26 C ANISOU 107 CG GLU A 13 2254 2120 2185 85 -304 68 C ATOM 108 CD GLU A 13 -2.008 -8.378 -20.314 1.00 28.04 C ANISOU 108 CD GLU A 13 3615 3489 3550 84 -302 71 C ATOM 109 OE1 GLU A 13 -2.367 -9.330 -21.044 1.00 19.65 O ANISOU 109 OE1 GLU A 13 2552 2430 2485 86 -297 69 O ATOM 110 OE2 GLU A 13 -1.510 -7.325 -20.769 1.00 20.97 O ANISOU 110 OE2 GLU A 13 2717 2592 2657 82 -306 76 O ATOM 111 N GLN A 14 -5.357 -11.192 -16.864 1.00 11.87 N ANISOU 111 N GLN A 14 1573 1442 1494 91 -294 57 N ATOM 112 CA GLN A 14 -5.943 -12.397 -16.279 1.00 11.25 C ANISOU 112 CA GLN A 14 1493 1365 1415 92 -291 56 C ATOM 113 C GLN A 14 -7.141 -12.855 -17.116 1.00 14.66 C ANISOU 113 C GLN A 14 1922 1800 1847 92 -290 58 C ATOM 114 O GLN A 14 -7.282 -14.046 -17.380 1.00 14.70 O ANISOU 114 O GLN A 14 1926 1807 1854 90 -290 58 O ATOM 115 CB GLN A 14 -6.364 -12.125 -14.837 1.00 12.53 C ANISOU 115 CB GLN A 14 1658 1527 1576 97 -291 56 C ATOM 116 CG GLN A 14 -5.174 -12.039 -13.900 1.00 12.84 C ANISOU 116 CG GLN A 14 1701 1563 1616 97 -293 55 C ATOM 117 CD GLN A 14 -5.501 -11.308 -12.621 1.00 16.18 C ANISOU 117 CD GLN A 14 2129 1983 2035 105 -295 54 C ATOM 118 OE1 GLN A 14 -6.642 -10.877 -12.386 1.00 16.27 O ANISOU 118 OE1 GLN A 14 2141 1998 2044 110 -293 55 O ATOM 119 NE2 GLN A 14 -4.496 -11.134 -11.776 1.00 15.49 N ANISOU 119 NE2 GLN A 14 2046 1890 1948 106 -298 53 N ATOM 120 N SER A 15 -7.976 -11.911 -17.569 1.00 12.58 N ANISOU 120 N SER A 15 1659 1537 1583 93 -290 58 N ATOM 121 CA SER A 15 -9.131 -12.237 -18.397 1.00 12.09 C ANISOU 121 CA SER A 15 1595 1476 1523 93 -290 60 C ATOM 122 C SER A 15 -8.716 -12.729 -19.796 1.00 16.78 C ANISOU 122 C SER A 15 2189 2068 2118 90 -292 59 C ATOM 123 O SER A 15 -9.189 -13.781 -20.229 1.00 16.96 O ANISOU 123 O SER A 15 2211 2090 2142 89 -294 60 O ATOM 124 CB SER A 15 -10.058 -11.030 -18.488 1.00 16.22 C ANISOU 124 CB SER A 15 2119 1999 2044 95 -290 60 C ATOM 125 OG SER A 15 -11.197 -11.359 -19.263 1.00 23.07 O ANISOU 125 OG SER A 15 2984 2867 2914 94 -290 63 O ATOM 126 N VAL A 16 -7.818 -11.988 -20.488 1.00 14.37 N ANISOU 126 N VAL A 16 1885 1762 1811 90 -292 58 N ATOM 127 CA VAL A 16 -7.321 -12.354 -21.828 1.00 13.98 C ANISOU 127 CA VAL A 16 1837 1713 1762 90 -292 58 C ATOM 128 C VAL A 16 -6.657 -13.734 -21.772 1.00 15.80 C ANISOU 128 C VAL A 16 2069 1944 1992 91 -293 58 C ATOM 129 O VAL A 16 -6.969 -14.598 -22.593 1.00 16.42 O ANISOU 129 O VAL A 16 2149 2021 2070 92 -296 58 O ATOM 130 CB VAL A 16 -6.361 -11.270 -22.378 1.00 18.74 C ANISOU 130 CB VAL A 16 2439 2315 2364 90 -292 59 C ATOM 131 CG1 VAL A 16 -5.667 -11.730 -23.663 1.00 19.32 C ANISOU 131 CG1 VAL A 16 2514 2390 2437 93 -291 60 C ATOM 132 CG2 VAL A 16 -7.110 -9.958 -22.607 1.00 18.66 C ANISOU 132 CG2 VAL A 16 2430 2305 2355 90 -293 58 C ATOM 133 N CYS A 17 -5.780 -13.950 -20.777 1.00 12.75 N ANISOU 133 N CYS A 17 1681 1558 1605 89 -292 58 N ATOM 134 CA CYS A 17 -5.067 -15.217 -20.655 1.00 13.28 C ANISOU 134 CA CYS A 17 1749 1627 1671 90 -293 57 C ATOM 135 C CYS A 17 -5.925 -16.394 -20.258 1.00 15.71 C ANISOU 135 C CYS A 17 2056 1933 1979 89 -296 57 C ATOM 136 O CYS A 17 -5.620 -17.528 -20.649 1.00 15.09 O ANISOU 136 O CYS A 17 1979 1854 1899 90 -300 56 O ATOM 137 CB CYS A 17 -3.836 -15.066 -19.774 1.00 14.70 C ANISOU 137 CB CYS A 17 1929 1807 1851 88 -291 57 C ATOM 138 SG CYS A 17 -2.561 -14.009 -20.512 1.00 18.98 S ANISOU 138 SG CYS A 17 2469 2350 2393 89 -290 61 S ATOM 139 N LYS A 18 -7.015 -16.147 -19.513 1.00 13.97 N ANISOU 139 N LYS A 18 1833 1712 1761 88 -296 58 N ATOM 140 CA LYS A 18 -7.945 -17.223 -19.159 1.00 13.86 C ANISOU 140 CA LYS A 18 1818 1699 1750 87 -299 61 C ATOM 141 C LYS A 18 -8.668 -17.674 -20.437 1.00 17.96 C ANISOU 141 C LYS A 18 2338 2215 2270 88 -305 62 C ATOM 142 O LYS A 18 -8.760 -18.876 -20.698 1.00 17.98 O ANISOU 142 O LYS A 18 2342 2215 2273 88 -311 63 O ATOM 143 CB LYS A 18 -8.960 -16.792 -18.084 1.00 15.56 C ANISOU 143 CB LYS A 18 2029 1916 1967 87 -297 64 C ATOM 144 CG LYS A 18 -9.868 -17.938 -17.661 1.00 22.03 C ANISOU 144 CG LYS A 18 2845 2736 2791 86 -300 69 C ATOM 145 CD LYS A 18 -11.186 -17.474 -17.113 1.00 31.85 C ANISOU 145 CD LYS A 18 4084 3983 4037 87 -298 75 C ATOM 146 CE LYS A 18 -12.167 -18.604 -16.862 1.00 32.79 C ANISOU 146 CE LYS A 18 4197 4102 4161 85 -303 83 C ATOM 147 NZ LYS A 18 -12.663 -19.224 -18.118 1.00 36.67 N ANISOU 147 NZ LYS A 18 4690 4588 4656 83 -312 85 N ATOM 148 N THR A 19 -9.136 -16.718 -21.250 1.00 15.82 N ANISOU 148 N THR A 19 2068 1942 1999 89 -304 62 N ATOM 149 CA THR A 19 -9.815 -17.040 -22.511 1.00 16.53 C ANISOU 149 CA THR A 19 2161 2028 2091 90 -309 63 C ATOM 150 C THR A 19 -8.891 -17.793 -23.492 1.00 21.18 C ANISOU 150 C THR A 19 2756 2615 2676 94 -313 61 C ATOM 151 O THR A 19 -9.319 -18.778 -24.110 1.00 21.64 O ANISOU 151 O THR A 19 2818 2669 2735 96 -321 62 O ATOM 152 CB THR A 19 -10.430 -15.771 -23.120 1.00 24.76 C ANISOU 152 CB THR A 19 3204 3069 3134 91 -306 63 C ATOM 153 OG1 THR A 19 -11.270 -15.167 -22.143 1.00 24.01 O ANISOU 153 OG1 THR A 19 3105 2978 3042 89 -303 65 O ATOM 154 CG2 THR A 19 -11.229 -16.052 -24.387 1.00 24.75 C ANISOU 154 CG2 THR A 19 3207 3063 3136 93 -312 63 C ATOM 155 N AGLU A 20 -7.632 -17.331 -23.620 0.50 17.45 N ANISOU 155 N AGLU A 20 2285 2146 2199 96 -308 58 N ATOM 156 N BGLU A 20 -7.635 -17.350 -23.614 0.50 17.72 N ANISOU 156 N BGLU A 20 2319 2181 2234 96 -308 58 N ATOM 157 CA AGLU A 20 -6.629 -17.899 -24.528 0.50 16.99 C ANISOU 157 CA AGLU A 20 2231 2088 2135 102 -310 57 C ATOM 158 CA BGLU A 20 -6.685 -17.963 -24.543 0.50 17.39 C ANISOU 158 CA BGLU A 20 2282 2139 2186 102 -310 57 C ATOM 159 C AGLU A 20 -6.226 -19.336 -24.187 0.50 19.50 C ANISOU 159 C AGLU A 20 2552 2406 2451 103 -316 57 C ATOM 160 C BGLU A 20 -6.237 -19.366 -24.187 0.50 19.73 C ANISOU 160 C BGLU A 20 2582 2436 2481 104 -316 57 C ATOM 161 O AGLU A 20 -5.951 -20.115 -25.096 0.50 19.55 O ANISOU 161 O AGLU A 20 2565 2411 2453 110 -321 56 O ATOM 162 O BGLU A 20 -5.933 -20.146 -25.083 0.50 19.83 O ANISOU 162 O BGLU A 20 2600 2447 2488 110 -322 56 O ATOM 163 CB AGLU A 20 -5.388 -16.987 -24.580 0.50 18.66 C ANISOU 163 CB AGLU A 20 2441 2305 2344 104 -303 58 C ATOM 164 CB BGLU A 20 -5.470 -17.068 -24.750 0.50 19.13 C ANISOU 164 CB BGLU A 20 2500 2363 2403 104 -303 58 C ATOM 165 CG AGLU A 20 -4.342 -17.379 -25.617 0.50 26.20 C ANISOU 165 CG AGLU A 20 3400 3262 3293 112 -303 59 C ATOM 166 CG BGLU A 20 -5.792 -15.813 -25.530 0.50 27.38 C ANISOU 166 CG BGLU A 20 3545 3408 3450 105 -300 58 C ATOM 167 CD AGLU A 20 -3.001 -16.683 -25.479 0.50 45.95 C ANISOU 167 CD AGLU A 20 5897 5769 5793 112 -296 62 C ATOM 168 CD BGLU A 20 -4.624 -14.915 -25.870 0.50 43.78 C ANISOU 168 CD BGLU A 20 5620 5490 5525 107 -295 61 C ATOM 169 OE1AGLU A 20 -2.985 -15.435 -25.381 0.50 44.00 O ANISOU 169 OE1AGLU A 20 5646 5522 5549 108 -292 64 O ATOM 170 OE1BGLU A 20 -3.476 -15.253 -25.500 0.50 43.95 O ANISOU 170 OE1BGLU A 20 5639 5514 5544 108 -293 63 O ATOM 171 OE2AGLU A 20 -1.962 -17.382 -25.493 0.50 32.69 O ANISOU 171 OE2AGLU A 20 4218 4092 4109 116 -296 64 O ATOM 172 OE2BGLU A 20 -4.858 -13.882 -26.539 0.50 26.18 O ANISOU 172 OE2BGLU A 20 3390 3260 3297 107 -293 62 O ATOM 173 N THR A 21 -6.170 -19.680 -22.889 1.00 15.84 N ANISOU 173 N THR A 21 2011 1990 2018 -41 -57 -138 N ATOM 174 CA THR A 21 -5.700 -20.990 -22.421 1.00 15.06 C ANISOU 174 CA THR A 21 1910 1892 1920 -39 -54 -140 C ATOM 175 C THR A 21 -6.763 -22.009 -22.089 1.00 18.84 C ANISOU 175 C THR A 21 2388 2369 2402 -37 -53 -139 C ATOM 176 O THR A 21 -6.445 -23.201 -21.983 1.00 19.43 O ANISOU 176 O THR A 21 2462 2444 2478 -36 -51 -141 O ATOM 177 CB THR A 21 -4.768 -20.787 -21.214 1.00 18.59 C ANISOU 177 CB THR A 21 2356 2339 2367 -36 -52 -140 C ATOM 178 OG1 THR A 21 -5.544 -20.217 -20.157 1.00 16.92 O ANISOU 178 OG1 THR A 21 2144 2126 2158 -34 -53 -138 O ATOM 179 CG2 THR A 21 -3.575 -19.889 -21.537 1.00 18.85 C ANISOU 179 CG2 THR A 21 2391 2374 2397 -38 -52 -141 C ATOM 180 N GLY A 22 -7.981 -21.550 -21.833 1.00 16.25 N ANISOU 180 N GLY A 22 2060 2039 2076 -36 -55 -137 N ATOM 181 CA GLY A 22 -9.078 -22.437 -21.461 1.00 16.42 C ANISOU 181 CA GLY A 22 2081 2059 2101 -34 -55 -137 C ATOM 182 C GLY A 22 -9.042 -22.887 -20.012 1.00 19.01 C ANISOU 182 C GLY A 22 2407 2387 2430 -31 -53 -137 C ATOM 183 O GLY A 22 -9.804 -23.779 -19.621 1.00 20.02 O ANISOU 183 O GLY A 22 2534 2513 2559 -30 -52 -137 O ATOM 184 N ILE A 23 -8.169 -22.278 -19.196 1.00 14.76 N ANISOU 184 N ILE A 23 1868 1849 1891 -31 -52 -137 N ATOM 185 CA ILE A 23 -8.060 -22.600 -17.771 1.00 13.12 C ANISOU 185 CA ILE A 23 1659 1641 1683 -29 -50 -137 C ATOM 186 C ILE A 23 -9.393 -22.320 -17.060 1.00 17.73 C ANISOU 186 C ILE A 23 2242 2224 2270 -28 -51 -137 C ATOM 187 O ILE A 23 -10.067 -21.333 -17.356 1.00 17.03 O ANISOU 187 O ILE A 23 2154 2135 2183 -29 -53 -137 O ATOM 188 CB ILE A 23 -6.863 -21.870 -17.087 1.00 15.00 C ANISOU 188 CB ILE A 23 1898 1881 1921 -28 -50 -137 C ATOM 189 CG1 ILE A 23 -6.580 -22.447 -15.672 1.00 14.97 C ANISOU 189 CG1 ILE A 23 1894 1877 1918 -27 -48 -137 C ATOM 190 CG2 ILE A 23 -7.059 -20.336 -17.057 1.00 15.29 C ANISOU 190 CG2 ILE A 23 1934 1917 1957 -29 -51 -136 C ATOM 191 CD1 ILE A 23 -5.246 -21.972 -15.039 1.00 16.33 C ANISOU 191 CD1 ILE A 23 2066 2050 2089 -26 -47 -137 C ATOM 192 N ASP A 24 -9.766 -23.199 -16.142 1.00 15.66 N ANISOU 192 N ASP A 24 1980 1962 2009 -28 -50 -137 N ATOM 193 CA ASP A 24 -10.962 -23.067 -15.315 1.00 16.15 C ANISOU 193 CA ASP A 24 2040 2023 2072 -28 -49 -137 C ATOM 194 C ASP A 24 -10.778 -21.837 -14.396 1.00 17.74 C ANISOU 194 C ASP A 24 2241 2225 2274 -28 -49 -138 C ATOM 195 O ASP A 24 -9.659 -21.565 -13.932 1.00 16.13 O ANISOU 195 O ASP A 24 2038 2023 2069 -28 -48 -137 O ATOM 196 CB ASP A 24 -11.122 -24.366 -14.501 1.00 19.07 C ANISOU 196 CB ASP A 24 2411 2394 2443 -28 -48 -137 C ATOM 197 CG ASP A 24 -12.181 -24.362 -13.431 1.00 38.51 C ANISOU 197 CG ASP A 24 4871 4855 4905 -29 -47 -138 C ATOM 198 OD1 ASP A 24 -13.378 -24.452 -13.780 1.00 41.39 O ANISOU 198 OD1 ASP A 24 5235 5219 5272 -30 -47 -139 O ATOM 199 OD2 ASP A 24 -11.815 -24.343 -12.241 1.00 45.86 O ANISOU 199 OD2 ASP A 24 5802 5788 5835 -30 -46 -138 O ATOM 200 N GLN A 25 -11.845 -21.057 -14.190 1.00 14.87 N ANISOU 200 N GLN A 25 1875 1861 1913 -28 -49 -139 N ATOM 201 CA GLN A 25 -11.742 -19.865 -13.341 1.00 14.05 C ANISOU 201 CA GLN A 25 1770 1758 1810 -29 -49 -140 C ATOM 202 C GLN A 25 -11.180 -20.168 -11.951 1.00 17.80 C ANISOU 202 C GLN A 25 2245 2236 2284 -29 -47 -140 C ATOM 203 O GLN A 25 -10.392 -19.378 -11.444 1.00 17.49 O ANISOU 203 O GLN A 25 2205 2197 2244 -29 -46 -140 O ATOM 204 CB GLN A 25 -13.092 -19.136 -13.220 1.00 14.83 C ANISOU 204 CB GLN A 25 1866 1856 1913 -29 -50 -143 C ATOM 205 CG GLN A 25 -13.016 -17.791 -12.468 1.00 20.27 C ANISOU 205 CG GLN A 25 2552 2545 2603 -29 -51 -144 C ATOM 206 CD GLN A 25 -12.171 -16.765 -13.183 1.00 30.28 C ANISOU 206 CD GLN A 25 3821 3813 3871 -28 -53 -143 C ATOM 207 OE1 GLN A 25 -11.073 -16.396 -12.739 1.00 23.06 O ANISOU 207 OE1 GLN A 25 2907 2900 2954 -28 -52 -141 O ATOM 208 NE2 GLN A 25 -12.640 -16.302 -14.324 1.00 23.78 N ANISOU 208 NE2 GLN A 25 2998 2988 3050 -28 -57 -143 N ATOM 209 N GLN A 26 -11.586 -21.286 -11.325 1.00 16.92 N ANISOU 209 N GLN A 26 2134 2124 2172 -30 -45 -140 N ATOM 210 CA GLN A 26 -11.091 -21.611 -9.985 1.00 17.51 C ANISOU 210 CA GLN A 26 2209 2200 2244 -32 -43 -139 C ATOM 211 C GLN A 26 -9.591 -21.875 -9.993 1.00 18.79 C ANISOU 211 C GLN A 26 2373 2363 2405 -31 -44 -137 C ATOM 212 O GLN A 26 -8.898 -21.446 -9.068 1.00 17.45 O ANISOU 212 O GLN A 26 2203 2194 2234 -31 -43 -137 O ATOM 213 CB GLN A 26 -11.849 -22.787 -9.373 1.00 19.57 C ANISOU 213 CB GLN A 26 2470 2461 2504 -34 -42 -140 C ATOM 214 CG GLN A 26 -13.297 -22.466 -9.047 1.00 42.82 C ANISOU 214 CG GLN A 26 5412 5406 5451 -36 -41 -143 C ATOM 215 CD GLN A 26 -14.057 -23.662 -8.526 1.00 73.17 C ANISOU 215 CD GLN A 26 9257 9250 9294 -39 -41 -143 C ATOM 216 OE1 GLN A 26 -13.738 -24.827 -8.803 1.00 71.21 O ANISOU 216 OE1 GLN A 26 9012 9002 9045 -39 -41 -141 O ATOM 217 NE2 GLN A 26 -15.109 -23.396 -7.773 1.00 68.91 N ANISOU 217 NE2 GLN A 26 8715 8712 8755 -42 -39 -147 N ATOM 218 N LYS A 27 -9.095 -22.561 -11.041 1.00 14.61 N ANISOU 218 N LYS A 27 1845 1832 1874 -29 -45 -136 N ATOM 219 CA LYS A 27 -7.665 -22.828 -11.197 1.00 14.38 C ANISOU 219 CA LYS A 27 1817 1802 1844 -28 -45 -135 C ATOM 220 C LYS A 27 -6.919 -21.518 -11.421 1.00 16.05 C ANISOU 220 C LYS A 27 2028 2015 2055 -27 -45 -135 C ATOM 221 O LYS A 27 -5.848 -21.332 -10.844 1.00 15.70 O ANISOU 221 O LYS A 27 1984 1970 2009 -27 -45 -135 O ATOM 222 CB LYS A 27 -7.405 -23.812 -12.345 1.00 16.43 C ANISOU 222 CB LYS A 27 2077 2060 2103 -28 -46 -135 C ATOM 223 CG LYS A 27 -7.215 -25.261 -11.911 1.00 35.14 C ANISOU 223 CG LYS A 27 4447 4429 4473 -28 -47 -135 C ATOM 224 CD LYS A 27 -5.852 -25.490 -11.268 1.00 40.36 C ANISOU 224 CD LYS A 27 5110 5090 5135 -28 -48 -134 C ATOM 225 CE LYS A 27 -5.326 -26.879 -11.499 1.00 44.32 C ANISOU 225 CE LYS A 27 5612 5590 5638 -28 -50 -134 C ATOM 226 NZ LYS A 27 -4.716 -27.430 -10.265 1.00 41.19 N ANISOU 226 NZ LYS A 27 5217 5192 5242 -29 -51 -133 N ATOM 227 N ALA A 28 -7.489 -20.591 -12.227 1.00 13.14 N ANISOU 227 N ALA A 28 1659 1646 1687 -27 -46 -136 N ATOM 228 CA ALA A 28 -6.881 -19.275 -12.445 1.00 12.51 C ANISOU 228 CA ALA A 28 1578 1567 1607 -26 -46 -136 C ATOM 229 C ALA A 28 -6.841 -18.513 -11.119 1.00 14.06 C ANISOU 229 C ALA A 28 1773 1764 1804 -26 -45 -136 C ATOM 230 O ALA A 28 -5.825 -17.890 -10.802 1.00 13.82 O ANISOU 230 O ALA A 28 1744 1735 1773 -25 -45 -135 O ATOM 231 CB ALA A 28 -7.676 -18.487 -13.477 1.00 13.15 C ANISOU 231 CB ALA A 28 1660 1648 1690 -26 -49 -136 C ATOM 232 N ASN A 29 -7.935 -18.590 -10.326 1.00 11.57 N ANISOU 232 N ASN A 29 1457 1450 1490 -27 -44 -137 N ATOM 233 CA ASN A 29 -7.994 -17.945 -9.011 1.00 11.05 C ANISOU 233 CA ASN A 29 1389 1385 1425 -28 -43 -138 C ATOM 234 C ASN A 29 -6.904 -18.480 -8.070 1.00 14.38 C ANISOU 234 C ASN A 29 1813 1808 1844 -29 -41 -136 C ATOM 235 O ASN A 29 -6.320 -17.691 -7.336 1.00 14.33 O ANISOU 235 O ASN A 29 1806 1803 1837 -29 -40 -136 O ATOM 236 CB ASN A 29 -9.388 -18.089 -8.378 1.00 14.05 C ANISOU 236 CB ASN A 29 1767 1766 1807 -31 -42 -140 C ATOM 237 CG ASN A 29 -10.497 -17.302 -9.050 1.00 23.60 C ANISOU 237 CG ASN A 29 2974 2974 3020 -30 -43 -143 C ATOM 238 OD1 ASN A 29 -11.690 -17.488 -8.740 1.00 23.88 O ANISOU 238 OD1 ASN A 29 3007 3009 3057 -32 -43 -145 O ATOM 239 ND2 ASN A 29 -10.156 -16.385 -9.945 1.00 13.67 N ANISOU 239 ND2 ASN A 29 1716 1715 1763 -29 -46 -142 N ATOM 240 N ASP A 30 -6.610 -19.801 -8.118 1.00 13.25 N ANISOU 240 N ASP A 30 1672 1664 1700 -29 -41 -135 N ATOM 241 CA ASP A 30 -5.527 -20.387 -7.328 1.00 13.82 C ANISOU 241 CA ASP A 30 1746 1735 1771 -30 -41 -133 C ATOM 242 C ASP A 30 -4.185 -19.723 -7.708 1.00 16.44 C ANISOU 242 C ASP A 30 2078 2067 2101 -27 -41 -133 C ATOM 243 O ASP A 30 -3.438 -19.294 -6.821 1.00 16.26 O ANISOU 243 O ASP A 30 2056 2045 2078 -27 -41 -132 O ATOM 244 CB ASP A 30 -5.436 -21.909 -7.558 1.00 15.60 C ANISOU 244 CB ASP A 30 1973 1959 1995 -30 -43 -133 C ATOM 245 CG ASP A 30 -6.601 -22.739 -7.052 1.00 24.96 C ANISOU 245 CG ASP A 30 3158 3144 3181 -33 -43 -133 C ATOM 246 OD1 ASP A 30 -7.369 -22.235 -6.193 1.00 25.91 O ANISOU 246 OD1 ASP A 30 3277 3266 3301 -36 -41 -134 O ATOM 247 OD2 ASP A 30 -6.701 -23.924 -7.453 1.00 29.64 O ANISOU 247 OD2 ASP A 30 3752 3736 3774 -33 -44 -132 O ATOM 248 N VAL A 31 -3.913 -19.569 -9.024 1.00 12.36 N ANISOU 248 N VAL A 31 1629 1550 1519 179 -175 -167 N ATOM 249 CA VAL A 31 -2.685 -18.929 -9.508 1.00 11.97 C ANISOU 249 CA VAL A 31 1581 1496 1471 179 -177 -166 C ATOM 250 C VAL A 31 -2.606 -17.481 -9.015 1.00 14.90 C ANISOU 250 C VAL A 31 1951 1870 1839 182 -187 -169 C ATOM 251 O VAL A 31 -1.572 -17.051 -8.504 1.00 14.03 O ANISOU 251 O VAL A 31 1839 1760 1730 184 -190 -165 O ATOM 252 CB VAL A 31 -2.602 -19.012 -11.056 1.00 14.66 C ANISOU 252 CB VAL A 31 1926 1829 1814 177 -175 -167 C ATOM 253 CG1 VAL A 31 -1.465 -18.150 -11.612 1.00 14.30 C ANISOU 253 CG1 VAL A 31 1882 1782 1768 176 -178 -165 C ATOM 254 CG2 VAL A 31 -2.462 -20.467 -11.519 1.00 14.60 C ANISOU 254 CG2 VAL A 31 1919 1819 1810 178 -169 -163 C ATOM 255 N ILE A 32 -3.715 -16.759 -9.110 1.00 11.47 N ANISOU 255 N ILE A 32 1518 1438 1400 182 -194 -177 N ATOM 256 CA ILE A 32 -3.773 -15.359 -8.701 1.00 11.05 C ANISOU 256 CA ILE A 32 1466 1390 1344 186 -209 -182 C ATOM 257 C ILE A 32 -3.498 -15.236 -7.192 1.00 16.07 C ANISOU 257 C ILE A 32 2095 2033 1978 194 -213 -178 C ATOM 258 O ILE A 32 -2.888 -14.259 -6.770 1.00 15.09 O ANISOU 258 O ILE A 32 1969 1909 1854 199 -225 -177 O ATOM 259 CB ILE A 32 -5.133 -14.742 -9.134 1.00 13.72 C ANISOU 259 CB ILE A 32 1807 1729 1675 185 -217 -195 C ATOM 260 CG1 ILE A 32 -5.243 -14.694 -10.666 1.00 14.10 C ANISOU 260 CG1 ILE A 32 1863 1767 1726 178 -215 -199 C ATOM 261 CG2 ILE A 32 -5.368 -13.349 -8.511 1.00 15.03 C ANISOU 261 CG2 ILE A 32 1972 1903 1835 190 -237 -202 C ATOM 262 CD1 ILE A 32 -6.688 -14.425 -11.205 1.00 14.32 C ANISOU 262 CD1 ILE A 32 1897 1793 1750 177 -219 -213 C ATOM 263 N GLU A 33 -3.889 -16.249 -6.405 1.00 14.89 N ANISOU 263 N GLU A 33 1941 1889 1827 195 -204 -176 N ATOM 264 CA GLU A 33 -3.701 -16.233 -4.946 1.00 15.32 C ANISOU 264 CA GLU A 33 1990 1951 1881 204 -206 -172 C ATOM 265 C GLU A 33 -2.316 -16.772 -4.545 1.00 19.91 C ANISOU 265 C GLU A 33 2571 2524 2469 205 -200 -164 C ATOM 266 O GLU A 33 -1.983 -16.831 -3.361 1.00 19.65 O ANISOU 266 O GLU A 33 2536 2495 2437 213 -201 -162 O ATOM 267 CB GLU A 33 -4.828 -17.020 -4.244 1.00 17.03 C ANISOU 267 CB GLU A 33 2200 2178 2091 204 -201 -173 C ATOM 268 CG GLU A 33 -6.157 -16.289 -4.242 1.00 28.20 C ANISOU 268 CG GLU A 33 3614 3604 3498 206 -210 -183 C ATOM 269 CD GLU A 33 -7.422 -17.076 -3.953 1.00 51.28 C ANISOU 269 CD GLU A 33 6531 6537 6415 203 -203 -184 C ATOM 270 OE1 GLU A 33 -7.319 -18.226 -3.471 1.00 35.27 O ANISOU 270 OE1 GLU A 33 4501 4509 4389 199 -192 -175 O ATOM 271 OE2 GLU A 33 -8.525 -16.527 -4.190 1.00 42.92 O ANISOU 271 OE2 GLU A 33 5472 5486 5349 203 -210 -194 O ATOM 272 N GLY A 34 -1.521 -17.164 -5.532 1.00 16.84 N ANISOU 272 N GLY A 34 2187 2126 2085 198 -194 -162 N ATOM 273 CA GLY A 34 -0.177 -17.655 -5.269 1.00 17.58 C ANISOU 273 CA GLY A 34 2282 2213 2184 199 -188 -157 C ATOM 274 C GLY A 34 -0.084 -19.128 -4.948 1.00 21.80 C ANISOU 274 C GLY A 34 2818 2747 2720 196 -178 -154 C ATOM 275 O GLY A 34 0.963 -19.567 -4.461 1.00 23.47 O ANISOU 275 O GLY A 34 3030 2952 2934 198 -175 -153 O ATOM 276 N ASN A 35 -1.148 -19.911 -5.244 1.00 17.36 N ANISOU 276 N ASN A 35 2254 2188 2154 191 -174 -155 N ATOM 277 CA ASN A 35 -1.125 -21.362 -5.063 1.00 17.67 C ANISOU 277 CA ASN A 35 2294 2225 2193 187 -168 -152 C ATOM 278 C ASN A 35 -0.978 -21.945 -6.464 1.00 21.29 C ANISOU 278 C ASN A 35 2757 2679 2654 182 -166 -152 C ATOM 279 O ASN A 35 -1.964 -22.073 -7.192 1.00 20.70 O ANISOU 279 O ASN A 35 2681 2605 2579 179 -166 -153 O ATOM 280 CB ASN A 35 -2.383 -21.878 -4.356 1.00 19.52 C ANISOU 280 CB ASN A 35 2525 2467 2423 185 -167 -150 C ATOM 281 CG ASN A 35 -2.338 -23.375 -4.091 1.00 49.44 C ANISOU 281 CG ASN A 35 6316 6255 6214 179 -164 -146 C ATOM 282 OD1 ASN A 35 -1.276 -23.973 -3.861 1.00 47.86 O ANISOU 282 OD1 ASN A 35 6120 6049 6016 179 -163 -146 O ATOM 283 ND2 ASN A 35 -3.494 -24.012 -4.101 1.00 41.91 N ANISOU 283 ND2 ASN A 35 5360 5307 5258 174 -163 -142 N ATOM 284 N ILE A 36 0.273 -22.218 -6.860 1.00 18.74 N ANISOU 284 N ILE A 36 2436 2351 2333 182 -165 -152 N ATOM 285 CA ILE A 36 0.572 -22.657 -8.213 1.00 18.63 C ANISOU 285 CA ILE A 36 2424 2334 2320 179 -165 -153 C ATOM 286 C ILE A 36 0.826 -24.147 -8.337 1.00 21.96 C ANISOU 286 C ILE A 36 2847 2754 2742 178 -166 -152 C ATOM 287 O ILE A 36 1.796 -24.669 -7.779 1.00 22.31 O ANISOU 287 O ILE A 36 2894 2797 2786 178 -167 -154 O ATOM 288 CB ILE A 36 1.651 -21.743 -8.872 1.00 22.26 C ANISOU 288 CB ILE A 36 2883 2793 2781 180 -165 -153 C ATOM 289 CG1 ILE A 36 1.117 -20.278 -8.980 1.00 24.18 C ANISOU 289 CG1 ILE A 36 3126 3037 3024 181 -168 -154 C ATOM 290 CG2 ILE A 36 2.051 -22.231 -10.276 1.00 20.92 C ANISOU 290 CG2 ILE A 36 2714 2623 2610 180 -165 -153 C ATOM 291 CD1 ILE A 36 1.700 -19.368 -8.065 1.00 36.70 C ANISOU 291 CD1 ILE A 36 4710 4623 4611 184 -172 -153 C ATOM 292 N ASP A 37 -0.053 -24.820 -9.095 1.00 18.57 N ANISOU 292 N ASP A 37 2418 2324 2314 177 -168 -150 N ATOM 293 CA ASP A 37 0.056 -26.243 -9.407 1.00 18.06 C ANISOU 293 CA ASP A 37 2356 2258 2249 177 -174 -149 C ATOM 294 C ASP A 37 0.971 -26.277 -10.640 1.00 19.96 C ANISOU 294 C ASP A 37 2596 2498 2489 182 -176 -152 C ATOM 295 O ASP A 37 0.503 -26.274 -11.782 1.00 19.52 O ANISOU 295 O ASP A 37 2541 2442 2436 185 -177 -151 O ATOM 296 CB ASP A 37 -1.336 -26.823 -9.705 1.00 19.66 C ANISOU 296 CB ASP A 37 2558 2459 2455 176 -176 -145 C ATOM 297 CG ASP A 37 -1.407 -28.328 -9.890 1.00 28.00 C ANISOU 297 CG ASP A 37 3615 3513 3512 177 -187 -142 C ATOM 298 OD1 ASP A 37 -2.523 -28.843 -10.098 1.00 28.66 O ANISOU 298 OD1 ASP A 37 3698 3594 3599 176 -190 -138 O ATOM 299 OD2 ASP A 37 -0.343 -28.988 -9.850 1.00 31.41 O ANISOU 299 OD2 ASP A 37 4049 3944 3941 178 -193 -145 O ATOM 300 N VAL A 38 2.295 -26.225 -10.389 1.00 16.30 N ANISOU 300 N VAL A 38 2134 2037 2024 182 -176 -155 N ATOM 301 CA VAL A 38 3.338 -26.117 -11.416 1.00 15.94 C ANISOU 301 CA VAL A 38 2087 1995 1976 186 -177 -158 C ATOM 302 C VAL A 38 3.280 -27.133 -12.552 1.00 19.02 C ANISOU 302 C VAL A 38 2476 2387 2364 192 -185 -159 C ATOM 303 O VAL A 38 3.635 -26.801 -13.681 1.00 17.60 O ANISOU 303 O VAL A 38 2294 2211 2183 196 -184 -159 O ATOM 304 CB VAL A 38 4.764 -25.969 -10.835 1.00 19.80 C ANISOU 304 CB VAL A 38 2576 2486 2462 185 -176 -163 C ATOM 305 CG1 VAL A 38 4.888 -24.713 -9.974 1.00 19.06 C ANISOU 305 CG1 VAL A 38 2482 2390 2371 183 -169 -161 C ATOM 306 CG2 VAL A 38 5.169 -27.209 -10.048 1.00 20.02 C ANISOU 306 CG2 VAL A 38 2608 2511 2487 185 -183 -168 C ATOM 307 N GLU A 39 2.860 -28.369 -12.247 1.00 17.42 N ANISOU 307 N GLU A 39 2276 2181 2162 193 -195 -158 N ATOM 308 CA GLU A 39 2.799 -29.459 -13.214 1.00 17.08 C ANISOU 308 CA GLU A 39 2232 2139 2117 201 -207 -159 C ATOM 309 C GLU A 39 1.543 -29.460 -14.096 1.00 20.36 C ANISOU 309 C GLU A 39 2647 2549 2539 206 -208 -154 C ATOM 310 O GLU A 39 1.529 -30.153 -15.118 1.00 20.49 O ANISOU 310 O GLU A 39 2662 2566 2557 216 -218 -154 O ATOM 311 CB GLU A 39 2.953 -30.817 -12.502 1.00 18.60 C ANISOU 311 CB GLU A 39 2428 2330 2308 199 -222 -161 C ATOM 312 CG GLU A 39 4.279 -31.002 -11.769 1.00 30.63 C ANISOU 312 CG GLU A 39 3954 3857 3826 196 -224 -170 C ATOM 313 CD GLU A 39 5.547 -30.989 -12.605 1.00 56.49 C ANISOU 313 CD GLU A 39 7228 7142 7095 203 -228 -177 C ATOM 314 OE1 GLU A 39 5.556 -31.602 -13.697 1.00 52.02 O ANISOU 314 OE1 GLU A 39 6658 6580 6525 213 -239 -178 O ATOM 315 OE2 GLU A 39 6.547 -30.388 -12.148 1.00 53.46 O ANISOU 315 OE2 GLU A 39 6843 6760 6707 200 -220 -183 O ATOM 316 N ASP A 40 0.505 -28.679 -13.730 1.00 16.19 N ANISOU 316 N ASP A 40 2119 2016 2015 200 -198 -150 N ATOM 317 CA ASP A 40 -0.726 -28.608 -14.502 1.00 15.35 C ANISOU 317 CA ASP A 40 2014 1904 1916 205 -198 -148 C ATOM 318 C ASP A 40 -0.528 -27.831 -15.803 1.00 17.69 C ANISOU 318 C ASP A 40 2309 2199 2212 212 -193 -150 C ATOM 319 O ASP A 40 -0.066 -26.686 -15.775 1.00 15.87 O ANISOU 319 O ASP A 40 2078 1972 1979 207 -184 -152 O ATOM 320 CB ASP A 40 -1.847 -27.992 -13.663 1.00 16.71 C ANISOU 320 CB ASP A 40 2186 2073 2091 197 -190 -146 C ATOM 321 CG ASP A 40 -3.182 -28.019 -14.371 1.00 25.77 C ANISOU 321 CG ASP A 40 3335 3212 3245 201 -190 -145 C ATOM 322 OD1 ASP A 40 -3.825 -29.093 -14.384 1.00 28.47 O ANISOU 322 OD1 ASP A 40 3677 3550 3592 204 -199 -140 O ATOM 323 OD2 ASP A 40 -3.546 -26.999 -14.980 1.00 24.91 O ANISOU 323 OD2 ASP A 40 3227 3099 3136 202 -183 -149 O ATOM 324 N LYS A 41 -0.895 -28.455 -16.943 1.00 15.68 N ANISOU 324 N LYS A 41 2116 1802 2038 263 -215 -399 N ATOM 325 CA LYS A 41 -0.745 -27.856 -18.272 1.00 13.98 C ANISOU 325 CA LYS A 41 1896 1592 1823 265 -214 -401 C ATOM 326 C LYS A 41 -1.424 -26.514 -18.411 1.00 15.44 C ANISOU 326 C LYS A 41 2081 1780 2007 263 -210 -399 C ATOM 327 O LYS A 41 -0.800 -25.574 -18.900 1.00 14.67 O ANISOU 327 O LYS A 41 1982 1686 1908 264 -210 -399 O ATOM 328 CB LYS A 41 -1.247 -28.797 -19.366 1.00 17.27 C ANISOU 328 CB LYS A 41 2310 2010 2242 265 -215 -404 C ATOM 329 CG LYS A 41 -0.791 -28.376 -20.755 1.00 21.05 C ANISOU 329 CG LYS A 41 2783 2494 2719 266 -214 -407 C ATOM 330 CD LYS A 41 0.691 -28.642 -20.909 1.00 22.02 C ANISOU 330 CD LYS A 41 2905 2619 2843 268 -217 -410 C ATOM 331 CE LYS A 41 1.293 -27.821 -21.991 1.00 24.71 C ANISOU 331 CE LYS A 41 3242 2966 3181 267 -216 -412 C ATOM 332 NZ LYS A 41 2.653 -28.340 -22.291 1.00 23.11 N ANISOU 332 NZ LYS A 41 3036 2766 2979 269 -219 -418 N ATOM 333 N LYS A 42 -2.703 -26.413 -17.998 1.00 12.84 N ANISOU 333 N LYS A 42 1752 1450 1678 261 -208 -398 N ATOM 334 CA LYS A 42 -3.378 -25.126 -18.138 1.00 12.65 C ANISOU 334 CA LYS A 42 1726 1427 1653 261 -206 -397 C ATOM 335 C LYS A 42 -2.800 -24.049 -17.272 1.00 14.62 C ANISOU 335 C LYS A 42 1977 1677 1902 260 -205 -396 C ATOM 336 O LYS A 42 -2.735 -22.893 -17.699 1.00 14.43 O ANISOU 336 O LYS A 42 1951 1654 1877 261 -205 -395 O ATOM 337 CB LYS A 42 -4.892 -25.248 -18.034 1.00 15.42 C ANISOU 337 CB LYS A 42 2077 1777 2005 259 -204 -399 C ATOM 338 CG LYS A 42 -5.442 -25.896 -19.303 1.00 22.06 C ANISOU 338 CG LYS A 42 2915 2619 2847 260 -205 -401 C ATOM 339 CD LYS A 42 -6.936 -25.976 -19.303 1.00 28.30 C ANISOU 339 CD LYS A 42 3704 3410 3639 259 -203 -404 C ATOM 340 CE LYS A 42 -7.408 -26.682 -20.541 1.00 25.31 C ANISOU 340 CE LYS A 42 3323 3033 3262 261 -203 -406 C ATOM 341 NZ LYS A 42 -7.160 -28.160 -20.480 1.00 33.96 N ANISOU 341 NZ LYS A 42 4418 4126 4358 260 -204 -407 N ATOM 342 N VAL A 43 -2.332 -24.417 -16.066 1.00 12.65 N ANISOU 342 N VAL A 43 1731 1425 1651 260 -206 -395 N ATOM 343 CA VAL A 43 -1.656 -23.474 -15.183 1.00 11.99 C ANISOU 343 CA VAL A 43 1647 1341 1566 260 -205 -394 C ATOM 344 C VAL A 43 -0.355 -23.005 -15.889 1.00 13.93 C ANISOU 344 C VAL A 43 1891 1589 1812 262 -207 -394 C ATOM 345 O VAL A 43 -0.055 -21.808 -15.911 1.00 12.45 O ANISOU 345 O VAL A 43 1702 1403 1624 262 -206 -394 O ATOM 346 CB VAL A 43 -1.368 -24.118 -13.801 1.00 14.96 C ANISOU 346 CB VAL A 43 2028 1716 1941 258 -206 -393 C ATOM 347 CG1 VAL A 43 -0.375 -23.279 -12.991 1.00 14.91 C ANISOU 347 CG1 VAL A 43 2022 1711 1934 259 -206 -393 C ATOM 348 CG2 VAL A 43 -2.659 -24.313 -13.014 1.00 14.75 C ANISOU 348 CG2 VAL A 43 2003 1689 1914 254 -203 -393 C ATOM 349 N GLN A 44 0.387 -23.940 -16.498 1.00 11.78 N ANISOU 349 N GLN A 44 1620 1317 1540 264 -209 -396 N ATOM 350 CA GLN A 44 1.615 -23.583 -17.228 1.00 11.06 C ANISOU 350 CA GLN A 44 1526 1229 1448 265 -210 -398 C ATOM 351 C GLN A 44 1.332 -22.593 -18.361 1.00 15.07 C ANISOU 351 C GLN A 44 2032 1740 1955 264 -208 -397 C ATOM 352 O GLN A 44 1.996 -21.543 -18.444 1.00 14.22 O ANISOU 352 O GLN A 44 1923 1634 1847 263 -207 -397 O ATOM 353 CB GLN A 44 2.277 -24.838 -17.789 1.00 11.83 C ANISOU 353 CB GLN A 44 1623 1327 1546 266 -213 -402 C ATOM 354 CG GLN A 44 2.939 -25.674 -16.701 1.00 16.13 C ANISOU 354 CG GLN A 44 2171 1868 2092 268 -216 -403 C ATOM 355 CD GLN A 44 3.355 -27.018 -17.233 1.00 21.28 C ANISOU 355 CD GLN A 44 2821 2518 2746 270 -220 -406 C ATOM 356 OE1 GLN A 44 3.190 -27.326 -18.420 1.00 18.65 O ANISOU 356 OE1 GLN A 44 2484 2188 2413 270 -220 -409 O ATOM 357 NE2 GLN A 44 3.935 -27.837 -16.365 1.00 19.39 N ANISOU 357 NE2 GLN A 44 2585 2274 2507 272 -224 -407 N ATOM 358 N LEU A 45 0.300 -22.895 -19.194 1.00 11.97 N ANISOU 358 N LEU A 45 1638 1348 1563 263 -208 -397 N ATOM 359 CA LEU A 45 -0.080 -22.016 -20.306 1.00 11.29 C ANISOU 359 CA LEU A 45 1549 1264 1475 262 -208 -395 C ATOM 360 C LEU A 45 -0.542 -20.659 -19.807 1.00 13.82 C ANISOU 360 C LEU A 45 1870 1583 1796 262 -207 -392 C ATOM 361 O LEU A 45 -0.177 -19.651 -20.393 1.00 13.95 O ANISOU 361 O LEU A 45 1887 1602 1813 260 -207 -391 O ATOM 362 CB LEU A 45 -1.160 -22.667 -21.169 1.00 11.91 C ANISOU 362 CB LEU A 45 1627 1344 1555 262 -208 -396 C ATOM 363 CG LEU A 45 -0.745 -23.935 -21.897 1.00 16.81 C ANISOU 363 CG LEU A 45 2246 1968 2175 263 -209 -399 C ATOM 364 CD1 LEU A 45 -1.957 -24.581 -22.529 1.00 16.76 C ANISOU 364 CD1 LEU A 45 2238 1961 2170 264 -209 -400 C ATOM 365 CD2 LEU A 45 0.340 -23.653 -22.936 1.00 18.95 C ANISOU 365 CD2 LEU A 45 2513 2243 2442 262 -209 -401 C ATOM 366 N TYR A 46 -1.349 -20.618 -18.731 1.00 11.00 N ANISOU 366 N TYR A 46 1515 1223 1442 262 -206 -392 N ATOM 367 CA TYR A 46 -1.837 -19.353 -18.167 1.00 10.76 C ANISOU 367 CA TYR A 46 1483 1191 1413 261 -206 -391 C ATOM 368 C TYR A 46 -0.659 -18.506 -17.643 1.00 13.94 C ANISOU 368 C TYR A 46 1886 1594 1816 261 -205 -391 C ATOM 369 O TYR A 46 -0.572 -17.302 -17.935 1.00 13.47 O ANISOU 369 O TYR A 46 1827 1535 1758 261 -206 -389 O ATOM 370 CB TYR A 46 -2.816 -19.691 -17.029 1.00 12.26 C ANISOU 370 CB TYR A 46 1674 1379 1605 261 -205 -393 C ATOM 371 CG TYR A 46 -3.473 -18.504 -16.362 1.00 12.98 C ANISOU 371 CG TYR A 46 1763 1469 1699 260 -205 -394 C ATOM 372 CD1 TYR A 46 -4.439 -17.751 -17.024 1.00 13.60 C ANISOU 372 CD1 TYR A 46 1840 1547 1780 261 -207 -395 C ATOM 373 CD2 TYR A 46 -3.245 -18.235 -15.015 1.00 15.10 C ANISOU 373 CD2 TYR A 46 2032 1738 1968 259 -203 -395 C ATOM 374 CE1 TYR A 46 -5.096 -16.694 -16.389 1.00 12.59 C ANISOU 374 CE1 TYR A 46 1709 1417 1656 260 -207 -397 C ATOM 375 CE2 TYR A 46 -3.911 -17.198 -14.364 1.00 16.11 C ANISOU 375 CE2 TYR A 46 2157 1865 2099 259 -203 -398 C ATOM 376 CZ TYR A 46 -4.840 -16.437 -15.050 1.00 20.12 C ANISOU 376 CZ TYR A 46 2663 2372 2611 259 -205 -399 C ATOM 377 OH TYR A 46 -5.464 -15.410 -14.384 1.00 22.30 O ANISOU 377 OH TYR A 46 2935 2648 2891 259 -206 -402 O ATOM 378 N CYS A 47 0.264 -19.138 -16.884 1.00 11.93 N ANISOU 378 N CYS A 47 1632 1339 1560 262 -205 -392 N ATOM 379 CA CYS A 47 1.453 -18.466 -16.354 1.00 11.51 C ANISOU 379 CA CYS A 47 1579 1287 1506 262 -204 -392 C ATOM 380 C CYS A 47 2.321 -17.905 -17.492 1.00 13.71 C ANISOU 380 C CYS A 47 1857 1567 1784 261 -204 -392 C ATOM 381 O CYS A 47 2.792 -16.763 -17.405 1.00 14.32 O ANISOU 381 O CYS A 47 1934 1645 1863 260 -203 -391 O ATOM 382 CB CYS A 47 2.252 -19.431 -15.490 1.00 11.39 C ANISOU 382 CB CYS A 47 1566 1272 1490 263 -204 -394 C ATOM 383 SG CYS A 47 1.484 -19.777 -13.889 1.00 14.92 S ANISOU 383 SG CYS A 47 2015 1716 1937 263 -204 -394 S ATOM 384 N GLU A 48 2.529 -18.703 -18.546 1.00 12.25 N ANISOU 384 N GLU A 48 1673 1386 1597 261 -205 -393 N ATOM 385 CA GLU A 48 3.311 -18.256 -19.700 1.00 12.15 C ANISOU 385 CA GLU A 48 1658 1376 1581 258 -205 -393 C ATOM 386 C GLU A 48 2.683 -17.040 -20.348 1.00 15.46 C ANISOU 386 C GLU A 48 2078 1794 2001 256 -205 -389 C ATOM 387 O GLU A 48 3.383 -16.067 -20.641 1.00 15.70 O ANISOU 387 O GLU A 48 2109 1826 2030 254 -204 -387 O ATOM 388 CB GLU A 48 3.424 -19.366 -20.725 1.00 13.63 C ANISOU 388 CB GLU A 48 1845 1567 1767 258 -205 -395 C ATOM 389 CG GLU A 48 4.346 -18.964 -21.858 1.00 19.26 C ANISOU 389 CG GLU A 48 2556 2286 2477 255 -205 -396 C ATOM 390 CD GLU A 48 4.321 -19.946 -22.996 1.00 32.06 C ANISOU 390 CD GLU A 48 4175 3912 4096 254 -205 -399 C ATOM 391 OE1 GLU A 48 3.228 -20.186 -23.558 1.00 29.88 O ANISOU 391 OE1 GLU A 48 3899 3634 3818 254 -206 -397 O ATOM 392 OE2 GLU A 48 5.395 -20.511 -23.292 1.00 30.68 O ANISOU 392 OE2 GLU A 48 3997 3740 3919 253 -205 -405 O ATOM 393 N CYS A 49 1.361 -17.098 -20.562 1.00 12.55 N ANISOU 393 N CYS A 49 1710 1424 1634 257 -207 -387 N ATOM 394 CA CYS A 49 0.616 -16.015 -21.187 1.00 13.70 C ANISOU 394 CA CYS A 49 1856 1568 1780 256 -209 -383 C ATOM 395 C CYS A 49 0.762 -14.732 -20.373 1.00 15.19 C ANISOU 395 C CYS A 49 2046 1753 1973 256 -209 -382 C ATOM 396 O CYS A 49 1.031 -13.661 -20.931 1.00 14.98 O ANISOU 396 O CYS A 49 2020 1726 1946 253 -210 -378 O ATOM 397 CB CYS A 49 -0.846 -16.433 -21.351 1.00 15.45 C ANISOU 397 CB CYS A 49 2078 1788 2004 258 -210 -383 C ATOM 398 SG CYS A 49 -1.923 -15.172 -22.080 1.00 21.27 S ANISOU 398 SG CYS A 49 2816 2522 2743 257 -215 -379 S ATOM 399 N ILE A 50 0.576 -14.810 -19.046 1.00 11.54 N ANISOU 399 N ILE A 50 1582 1288 1513 258 -208 -384 N ATOM 400 CA ILE A 50 0.675 -13.615 -18.199 1.00 11.79 C ANISOU 400 CA ILE A 50 1613 1318 1549 258 -208 -384 C ATOM 401 C ILE A 50 2.105 -13.064 -18.231 1.00 14.02 C ANISOU 401 C ILE A 50 1896 1602 1831 256 -206 -384 C ATOM 402 O ILE A 50 2.295 -11.854 -18.410 1.00 14.50 O ANISOU 402 O ILE A 50 1956 1660 1893 255 -207 -382 O ATOM 403 CB ILE A 50 0.207 -13.932 -16.757 1.00 15.31 C ANISOU 403 CB ILE A 50 2057 1762 1997 260 -207 -388 C ATOM 404 CG1 ILE A 50 -1.332 -14.162 -16.749 1.00 16.58 C ANISOU 404 CG1 ILE A 50 2217 1923 2161 261 -208 -389 C ATOM 405 CG2 ILE A 50 0.605 -12.799 -15.775 1.00 17.23 C ANISOU 405 CG2 ILE A 50 2297 2004 2244 260 -206 -389 C ATOM 406 CD1 ILE A 50 -1.873 -14.639 -15.467 1.00 23.90 C ANISOU 406 CD1 ILE A 50 3142 2849 3088 261 -207 -392 C ATOM 407 N LEU A 51 3.107 -13.931 -18.053 1.00 11.68 N ANISOU 407 N LEU A 51 1511 1484 1443 -26 -117 223 N ATOM 408 CA LEU A 51 4.490 -13.430 -18.056 1.00 11.55 C ANISOU 408 CA LEU A 51 1495 1467 1426 -27 -116 222 C ATOM 409 C LEU A 51 4.918 -12.823 -19.381 1.00 15.34 C ANISOU 409 C LEU A 51 1976 1946 1906 -27 -116 222 C ATOM 410 O LEU A 51 5.576 -11.780 -19.392 1.00 15.69 O ANISOU 410 O LEU A 51 2021 1991 1951 -27 -116 222 O ATOM 411 CB LEU A 51 5.499 -14.486 -17.599 1.00 11.00 C ANISOU 411 CB LEU A 51 1425 1397 1356 -27 -117 221 C ATOM 412 CG LEU A 51 5.323 -15.036 -16.184 1.00 14.79 C ANISOU 412 CG LEU A 51 1905 1878 1836 -28 -117 222 C ATOM 413 CD1 LEU A 51 6.317 -16.167 -15.940 1.00 15.36 C ANISOU 413 CD1 LEU A 51 1978 1951 1909 -29 -118 221 C ATOM 414 CD2 LEU A 51 5.504 -13.943 -15.125 1.00 19.27 C ANISOU 414 CD2 LEU A 51 2473 2446 2403 -27 -116 221 C ATOM 415 N LYS A 52 4.518 -13.442 -20.501 1.00 12.92 N ANISOU 415 N LYS A 52 1670 1640 1600 -27 -117 223 N ATOM 416 CA LYS A 52 4.849 -12.888 -21.814 1.00 12.67 C ANISOU 416 CA LYS A 52 1639 1609 1568 -28 -117 223 C ATOM 417 C LYS A 52 4.184 -11.552 -22.042 1.00 17.54 C ANISOU 417 C LYS A 52 2254 2224 2185 -28 -117 223 C ATOM 418 O LYS A 52 4.832 -10.620 -22.534 1.00 16.99 O ANISOU 418 O LYS A 52 2185 2155 2116 -29 -118 223 O ATOM 419 CB LYS A 52 4.519 -13.878 -22.924 1.00 14.93 C ANISOU 419 CB LYS A 52 1926 1894 1853 -28 -118 223 C ATOM 420 CG LYS A 52 5.515 -15.031 -22.976 1.00 22.62 C ANISOU 420 CG LYS A 52 2900 2869 2826 -27 -118 222 C ATOM 421 CD LYS A 52 5.280 -15.958 -24.148 1.00 28.06 C ANISOU 421 CD LYS A 52 3591 3558 3515 -26 -119 222 C ATOM 422 CE LYS A 52 6.459 -16.886 -24.315 1.00 38.75 C ANISOU 422 CE LYS A 52 4944 4912 4866 -25 -119 220 C ATOM 423 NZ LYS A 52 6.249 -17.855 -25.419 1.00 51.63 N ANISOU 423 NZ LYS A 52 6578 6543 6497 -24 -121 220 N ATOM 424 N ASN A 53 2.909 -11.430 -21.639 1.00 14.77 N ANISOU 424 N ASN A 53 1904 1873 1836 -28 -117 224 N ATOM 425 CA ASN A 53 2.172 -10.183 -21.820 1.00 14.35 C ANISOU 425 CA ASN A 53 1850 1818 1785 -29 -118 224 C ATOM 426 C ASN A 53 2.722 -9.025 -21.014 1.00 17.08 C ANISOU 426 C ASN A 53 2195 2165 2131 -28 -118 223 C ATOM 427 O ASN A 53 2.575 -7.875 -21.435 1.00 16.56 O ANISOU 427 O ASN A 53 2128 2097 2066 -29 -119 223 O ATOM 428 CB ASN A 53 0.687 -10.406 -21.587 1.00 16.84 C ANISOU 428 CB ASN A 53 2165 2133 2102 -29 -118 225 C ATOM 429 CG ASN A 53 0.016 -11.215 -22.680 1.00 22.46 C ANISOU 429 CG ASN A 53 2878 2843 2814 -30 -119 227 C ATOM 430 OD1 ASN A 53 0.637 -11.633 -23.672 1.00 19.92 O ANISOU 430 OD1 ASN A 53 2557 2521 2491 -31 -119 227 O ATOM 431 ND2 ASN A 53 -1.270 -11.457 -22.520 1.00 19.81 N ANISOU 431 ND2 ASN A 53 2541 2505 2479 -30 -119 229 N ATOM 432 N PHE A 54 3.430 -9.331 -19.903 1.00 14.23 N ANISOU 432 N PHE A 54 1834 1804 1769 -27 -117 222 N ATOM 433 CA PHE A 54 4.081 -8.325 -19.062 1.00 13.83 C ANISOU 433 CA PHE A 54 1784 1753 1718 -26 -118 221 C ATOM 434 C PHE A 54 5.554 -8.141 -19.429 1.00 17.72 C ANISOU 434 C PHE A 54 2277 2246 2211 -27 -119 222 C ATOM 435 O PHE A 54 6.267 -7.415 -18.736 1.00 18.89 O ANISOU 435 O PHE A 54 2425 2393 2359 -26 -120 222 O ATOM 436 CB PHE A 54 3.935 -8.682 -17.582 1.00 15.24 C ANISOU 436 CB PHE A 54 1963 1932 1896 -25 -117 220 C ATOM 437 CG PHE A 54 2.659 -8.186 -16.959 1.00 15.97 C ANISOU 437 CG PHE A 54 2055 2025 1989 -24 -116 220 C ATOM 438 CD1 PHE A 54 2.548 -6.875 -16.513 1.00 18.10 C ANISOU 438 CD1 PHE A 54 2325 2294 2259 -22 -117 218 C ATOM 439 CD2 PHE A 54 1.574 -9.040 -16.787 1.00 17.88 C ANISOU 439 CD2 PHE A 54 2296 2268 2231 -23 -115 221 C ATOM 440 CE1 PHE A 54 1.375 -6.425 -15.904 1.00 19.63 C ANISOU 440 CE1 PHE A 54 2518 2488 2454 -21 -117 217 C ATOM 441 CE2 PHE A 54 0.407 -8.593 -16.166 1.00 21.11 C ANISOU 441 CE2 PHE A 54 2704 2678 2640 -22 -114 220 C ATOM 442 CZ PHE A 54 0.318 -7.287 -15.731 1.00 19.50 C ANISOU 442 CZ PHE A 54 2501 2473 2437 -20 -115 219 C ATOM 443 N ASN A 55 6.008 -8.781 -20.527 1.00 13.96 N ANISOU 443 N ASN A 55 1799 1770 1733 -28 -118 223 N ATOM 444 CA ASN A 55 7.396 -8.681 -20.998 1.00 14.13 C ANISOU 444 CA ASN A 55 1822 1793 1755 -28 -119 224 C ATOM 445 C ASN A 55 8.397 -9.227 -19.967 1.00 18.68 C ANISOU 445 C ASN A 55 2398 2369 2330 -28 -118 223 C ATOM 446 O ASN A 55 9.521 -8.723 -19.852 1.00 19.06 O ANISOU 446 O ASN A 55 2446 2416 2379 -28 -119 225 O ATOM 447 CB ASN A 55 7.724 -7.227 -21.400 1.00 15.60 C ANISOU 447 CB ASN A 55 2007 1979 1942 -29 -121 225 C ATOM 448 CG ASN A 55 8.841 -7.116 -22.398 1.00 26.63 C ANISOU 448 CG ASN A 55 3403 3378 3339 -30 -122 227 C ATOM 449 OD1 ASN A 55 9.079 -8.026 -23.194 1.00 18.91 O ANISOU 449 OD1 ASN A 55 2425 2401 2360 -30 -120 227 O ATOM 450 ND2 ASN A 55 9.508 -5.971 -22.420 1.00 21.80 N ANISOU 450 ND2 ASN A 55 2790 2766 2728 -31 -124 229 N ATOM 451 N ILE A 56 7.993 -10.284 -19.235 1.00 14.63 N ANISOU 451 N ILE A 56 1886 1856 1817 -27 -117 222 N ATOM 452 CA ILE A 56 8.832 -10.936 -18.222 1.00 14.57 C ANISOU 452 CA ILE A 56 1878 1847 1809 -27 -117 222 C ATOM 453 C ILE A 56 9.519 -12.153 -18.819 1.00 19.09 C ANISOU 453 C ILE A 56 2451 2421 2382 -28 -116 222 C ATOM 454 O ILE A 56 10.571 -12.578 -18.333 1.00 18.78 O ANISOU 454 O ILE A 56 2412 2381 2343 -28 -116 222 O ATOM 455 CB ILE A 56 8.027 -11.212 -16.931 1.00 17.44 C ANISOU 455 CB ILE A 56 2243 2211 2173 -27 -117 221 C ATOM 456 CG1 ILE A 56 7.614 -9.865 -16.306 1.00 18.50 C ANISOU 456 CG1 ILE A 56 2377 2344 2307 -26 -117 220 C ATOM 457 CG2 ILE A 56 8.819 -12.070 -15.911 1.00 17.85 C ANISOU 457 CG2 ILE A 56 2295 2262 2224 -28 -116 221 C ATOM 458 CD1 ILE A 56 6.517 -9.942 -15.443 1.00 27.38 C ANISOU 458 CD1 ILE A 56 3503 3470 3431 -25 -117 220 C ATOM 459 N LEU A 57 8.944 -12.688 -19.900 1.00 18.23 N ANISOU 459 N LEU A 57 2342 2313 2271 -27 -116 222 N ATOM 460 CA LEU A 57 9.532 -13.790 -20.648 1.00 18.45 C ANISOU 460 CA LEU A 57 2370 2342 2299 -27 -115 221 C ATOM 461 C LEU A 57 9.628 -13.331 -22.070 1.00 25.38 C ANISOU 461 C LEU A 57 3247 3221 3176 -27 -115 222 C ATOM 462 O LEU A 57 8.657 -12.790 -22.611 1.00 24.65 O ANISOU 462 O LEU A 57 3155 3128 3083 -27 -115 222 O ATOM 463 CB LEU A 57 8.690 -15.074 -20.597 1.00 18.43 C ANISOU 463 CB LEU A 57 2367 2339 2296 -27 -116 220 C ATOM 464 CG LEU A 57 8.724 -15.899 -19.330 1.00 22.90 C ANISOU 464 CG LEU A 57 2933 2904 2863 -27 -117 220 C ATOM 465 CD1 LEU A 57 7.825 -17.122 -19.468 1.00 23.66 C ANISOU 465 CD1 LEU A 57 3030 3001 2960 -27 -119 220 C ATOM 466 CD2 LEU A 57 10.137 -16.365 -19.013 1.00 24.67 C ANISOU 466 CD2 LEU A 57 3158 3129 3089 -28 -117 219 C ATOM 467 N ASP A 58 10.790 -13.542 -22.687 1.00 25.01 N ANISOU 467 N ASP A 58 3200 3175 3128 -26 -114 222 N ATOM 468 CA ASP A 58 10.919 -13.162 -24.079 1.00 26.84 C ANISOU 468 CA ASP A 58 3430 3408 3358 -26 -114 223 C ATOM 469 C ASP A 58 10.440 -14.311 -24.961 1.00 33.85 C ANISOU 469 C ASP A 58 4320 4297 4245 -25 -114 221 C ATOM 470 O ASP A 58 10.083 -15.376 -24.445 1.00 32.35 O ANISOU 470 O ASP A 58 4132 4106 4056 -25 -115 220 O ATOM 471 CB ASP A 58 12.349 -12.685 -24.412 1.00 29.20 C ANISOU 471 CB ASP A 58 3728 3709 3657 -26 -113 225 C ATOM 472 CG ASP A 58 13.466 -13.713 -24.410 1.00 38.74 C ANISOU 472 CG ASP A 58 4936 4918 4865 -25 -112 224 C ATOM 473 OD1 ASP A 58 13.170 -14.924 -24.285 1.00 37.78 O ANISOU 473 OD1 ASP A 58 4816 4796 4743 -24 -112 222 O ATOM 474 OD2 ASP A 58 14.641 -13.309 -24.554 1.00 46.54 O ANISOU 474 OD2 ASP A 58 5922 5907 5853 -24 -111 226 O ATOM 475 N LYS A 59 10.457 -14.102 -26.289 1.00 33.49 N ANISOU 475 N LYS A 59 4274 4253 4197 -25 -113 222 N ATOM 476 CA LYS A 59 10.033 -15.077 -27.302 1.00 34.66 C ANISOU 476 CA LYS A 59 4424 4401 4343 -24 -114 220 C ATOM 477 C LYS A 59 10.753 -16.419 -27.131 1.00 39.86 C ANISOU 477 C LYS A 59 5083 5060 5001 -22 -113 218 C ATOM 478 O LYS A 59 10.214 -17.467 -27.496 1.00 40.04 O ANISOU 478 O LYS A 59 5108 5082 5023 -20 -115 217 O ATOM 479 CB LYS A 59 10.254 -14.501 -28.718 1.00 38.04 C ANISOU 479 CB LYS A 59 4853 4833 4769 -24 -113 221 C ATOM 480 CG LYS A 59 9.974 -13.002 -28.780 1.00 56.57 C ANISOU 480 CG LYS A 59 7198 7179 7117 -26 -113 224 C ATOM 481 CD LYS A 59 9.454 -12.492 -30.098 1.00 68.70 C ANISOU 481 CD LYS A 59 8735 8717 8652 -28 -114 225 C ATOM 482 CE LYS A 59 8.703 -11.201 -29.876 1.00 81.67 C ANISOU 482 CE LYS A 59 10377 10358 10297 -31 -115 227 C ATOM 483 NZ LYS A 59 7.367 -11.223 -30.527 1.00 91.12 N ANISOU 483 NZ LYS A 59 11575 11552 11493 -32 -117 227 N ATOM 484 N ASN A 60 11.945 -16.383 -26.509 1.00 37.08 N ANISOU 484 N ASN A 60 4729 4708 4649 -21 -112 219 N ATOM 485 CA ASN A 60 12.764 -17.556 -26.235 1.00 37.27 C ANISOU 485 CA ASN A 60 4753 4733 4674 -20 -112 217 C ATOM 486 C ASN A 60 12.688 -18.060 -24.798 1.00 40.64 C ANISOU 486 C ASN A 60 5181 5158 5105 -21 -114 216 C ATOM 487 O ASN A 60 13.531 -18.861 -24.377 1.00 41.13 O ANISOU 487 O ASN A 60 5242 5219 5168 -20 -114 215 O ATOM 488 CB ASN A 60 14.194 -17.302 -26.667 1.00 40.81 C ANISOU 488 CB ASN A 60 5200 5183 5122 -18 -110 218 C ATOM 489 CG ASN A 60 14.397 -17.747 -28.084 1.00 68.68 C ANISOU 489 CG ASN A 60 8731 8717 8649 -16 -109 216 C ATOM 490 OD1 ASN A 60 14.129 -18.904 -28.442 1.00 65.12 O ANISOU 490 OD1 ASN A 60 8282 8265 8197 -14 -110 214 O ATOM 491 ND2 ASN A 60 14.799 -16.823 -28.936 1.00 61.84 N ANISOU 491 ND2 ASN A 60 7864 7853 7780 -16 -107 219 N ATOM 492 N ASN A 61 11.653 -17.609 -24.057 1.00 35.15 N ANISOU 492 N ASN A 61 4409 4491 4455 -26 -20 30 N ATOM 493 CA ASN A 61 11.380 -17.974 -22.666 1.00 34.14 C ANISOU 493 CA ASN A 61 4282 4362 4329 -27 -20 31 C ATOM 494 C ASN A 61 12.502 -17.716 -21.678 1.00 34.77 C ANISOU 494 C ASN A 61 4362 4441 4408 -28 -20 31 C ATOM 495 O ASN A 61 12.642 -18.428 -20.684 1.00 34.46 O ANISOU 495 O ASN A 61 4323 4401 4370 -28 -21 31 O ATOM 496 CB ASN A 61 10.766 -19.365 -22.542 1.00 38.36 C ANISOU 496 CB ASN A 61 4815 4895 4866 -26 -22 31 C ATOM 497 CG ASN A 61 9.324 -19.361 -22.959 1.00 66.61 C ANISOU 497 CG ASN A 61 8393 8472 8444 -25 -22 31 C ATOM 498 OD1 ASN A 61 8.990 -19.136 -24.129 1.00 62.20 O ANISOU 498 OD1 ASN A 61 7835 7914 7885 -24 -21 31 O ATOM 499 ND2 ASN A 61 8.434 -19.545 -21.998 1.00 58.91 N ANISOU 499 ND2 ASN A 61 7419 7495 7470 -25 -22 33 N ATOM 500 N VAL A 62 13.272 -16.662 -21.944 1.00 28.80 N ANISOU 500 N VAL A 62 3606 3686 3650 -29 -19 31 N ATOM 501 CA VAL A 62 14.328 -16.222 -21.056 1.00 27.58 C ANISOU 501 CA VAL A 62 3453 3531 3496 -30 -18 32 C ATOM 502 C VAL A 62 13.670 -15.209 -20.143 1.00 26.68 C ANISOU 502 C VAL A 62 3341 3416 3381 -31 -17 33 C ATOM 503 O VAL A 62 12.939 -14.334 -20.613 1.00 25.01 O ANISOU 503 O VAL A 62 3130 3204 3169 -31 -17 34 O ATOM 504 CB VAL A 62 15.546 -15.623 -21.809 1.00 32.33 C ANISOU 504 CB VAL A 62 4053 4135 4096 -31 -18 31 C ATOM 505 CG1 VAL A 62 16.619 -15.130 -20.833 1.00 31.93 C ANISOU 505 CG1 VAL A 62 4003 4083 4044 -32 -18 31 C ATOM 506 CG2 VAL A 62 16.134 -16.636 -22.790 1.00 32.31 C ANISOU 506 CG2 VAL A 62 4050 4135 4094 -30 -19 29 C ATOM 507 N PHE A 63 13.938 -15.329 -18.844 1.00 21.84 N ANISOU 507 N PHE A 63 2728 2802 2769 -31 -18 34 N ATOM 508 CA PHE A 63 13.444 -14.420 -17.829 1.00 21.14 C ANISOU 508 CA PHE A 63 2641 2712 2679 -32 -17 35 C ATOM 509 C PHE A 63 14.082 -13.044 -18.041 1.00 25.42 C ANISOU 509 C PHE A 63 3184 3255 3221 -33 -16 35 C ATOM 510 O PHE A 63 15.303 -12.946 -18.204 1.00 26.11 O ANISOU 510 O PHE A 63 3270 3343 3307 -33 -16 34 O ATOM 511 CB PHE A 63 13.786 -14.995 -16.449 1.00 22.67 C ANISOU 511 CB PHE A 63 2834 2905 2873 -32 -18 35 C ATOM 512 CG PHE A 63 13.498 -14.111 -15.269 1.00 24.82 C ANISOU 512 CG PHE A 63 3109 3178 3146 -33 -17 36 C ATOM 513 CD1 PHE A 63 12.194 -13.743 -14.957 1.00 28.18 C ANISOU 513 CD1 PHE A 63 3535 3603 3571 -32 -16 37 C ATOM 514 CD2 PHE A 63 14.524 -13.690 -14.433 1.00 27.30 C ANISOU 514 CD2 PHE A 63 3422 3491 3458 -34 -17 36 C ATOM 515 CE1 PHE A 63 11.926 -12.941 -13.846 1.00 29.58 C ANISOU 515 CE1 PHE A 63 3713 3779 3747 -33 -16 37 C ATOM 516 CE2 PHE A 63 14.258 -12.875 -13.334 1.00 30.69 C ANISOU 516 CE2 PHE A 63 3853 3920 3888 -34 -16 36 C ATOM 517 CZ PHE A 63 12.961 -12.520 -13.036 1.00 29.00 C ANISOU 517 CZ PHE A 63 3639 3705 3673 -33 -16 37 C ATOM 518 N LYS A 64 13.245 -11.998 -18.092 1.00 21.30 N ANISOU 518 N LYS A 64 2663 2732 2697 -33 -15 36 N ATOM 519 CA LYS A 64 13.664 -10.614 -18.300 1.00 21.09 C ANISOU 519 CA LYS A 64 2637 2705 2670 -34 -15 36 C ATOM 520 C LYS A 64 13.600 -9.851 -16.977 1.00 24.96 C ANISOU 520 C LYS A 64 3129 3195 3161 -34 -15 37 C ATOM 521 O LYS A 64 12.509 -9.451 -16.543 1.00 23.69 O ANISOU 521 O LYS A 64 2969 3034 3000 -34 -14 37 O ATOM 522 CB LYS A 64 12.828 -9.920 -19.397 1.00 23.75 C ANISOU 522 CB LYS A 64 2974 3043 3006 -33 -14 37 C ATOM 523 CG LYS A 64 12.738 -10.707 -20.701 1.00 36.41 C ANISOU 523 CG LYS A 64 4576 4647 4610 -33 -14 36 C ATOM 524 CD LYS A 64 13.472 -10.016 -21.838 1.00 53.22 C ANISOU 524 CD LYS A 64 6705 6779 6739 -33 -14 36 C ATOM 525 CE LYS A 64 12.524 -9.365 -22.820 1.00 68.94 C ANISOU 525 CE LYS A 64 8696 8769 8729 -33 -14 37 C ATOM 526 NZ LYS A 64 13.148 -9.217 -24.162 1.00 80.16 N ANISOU 526 NZ LYS A 64 10116 10193 10149 -33 -13 37 N ATOM 527 N PRO A 65 14.762 -9.658 -16.308 1.00 23.30 N ANISOU 527 N PRO A 65 2918 2984 2949 -35 -15 36 N ATOM 528 CA PRO A 65 14.770 -8.940 -15.022 1.00 24.13 C ANISOU 528 CA PRO A 65 3025 3089 3055 -35 -15 37 C ATOM 529 C PRO A 65 14.147 -7.550 -15.086 1.00 28.77 C ANISOU 529 C PRO A 65 3614 3676 3643 -35 -14 37 C ATOM 530 O PRO A 65 13.568 -7.116 -14.099 1.00 29.34 O ANISOU 530 O PRO A 65 3686 3747 3714 -35 -14 37 O ATOM 531 CB PRO A 65 16.264 -8.836 -14.691 1.00 25.99 C ANISOU 531 CB PRO A 65 3260 3325 3291 -36 -15 36 C ATOM 532 CG PRO A 65 16.881 -9.980 -15.389 1.00 29.97 C ANISOU 532 CG PRO A 65 3763 3830 3795 -36 -15 36 C ATOM 533 CD PRO A 65 16.125 -10.097 -16.677 1.00 25.00 C ANISOU 533 CD PRO A 65 3133 3201 3166 -35 -15 36 C ATOM 534 N GLN A 66 14.254 -6.850 -16.231 1.00 25.97 N ANISOU 534 N GLN A 66 3258 3321 3287 -35 -14 37 N ATOM 535 CA GLN A 66 13.686 -5.506 -16.322 1.00 26.50 C ANISOU 535 CA GLN A 66 3326 3388 3355 -36 -14 38 C ATOM 536 C GLN A 66 12.155 -5.490 -16.316 1.00 29.23 C ANISOU 536 C GLN A 66 3672 3732 3700 -35 -14 38 C ATOM 537 O GLN A 66 11.564 -4.567 -15.750 1.00 28.96 O ANISOU 537 O GLN A 66 3639 3697 3666 -35 -14 38 O ATOM 538 CB GLN A 66 14.298 -4.694 -17.475 1.00 28.52 C ANISOU 538 CB GLN A 66 3582 3644 3611 -37 -14 39 C ATOM 539 CG GLN A 66 15.805 -4.408 -17.294 1.00 47.83 C ANISOU 539 CG GLN A 66 6027 6089 6056 -37 -15 39 C ATOM 540 CD GLN A 66 16.147 -3.663 -16.017 1.00 74.29 C ANISOU 540 CD GLN A 66 9379 9440 9408 -38 -15 38 C ATOM 541 OE1 GLN A 66 15.467 -2.711 -15.611 1.00 72.45 O ANISOU 541 OE1 GLN A 66 9147 9206 9175 -37 -16 38 O ATOM 542 NE2 GLN A 66 17.223 -4.074 -15.363 1.00 67.00 N ANISOU 542 NE2 GLN A 66 8455 8516 8484 -38 -16 38 N ATOM 543 N GLY A 67 11.539 -6.522 -16.893 1.00 24.55 N ANISOU 543 N GLY A 67 3079 3140 3107 -34 -14 38 N ATOM 544 CA GLY A 67 10.092 -6.683 -16.927 1.00 24.03 C ANISOU 544 CA GLY A 67 3014 3074 3042 -33 -13 38 C ATOM 545 C GLY A 67 9.524 -6.891 -15.539 1.00 26.36 C ANISOU 545 C GLY A 67 3310 3369 3337 -33 -13 38 C ATOM 546 O GLY A 67 8.523 -6.264 -15.183 1.00 26.86 O ANISOU 546 O GLY A 67 3373 3431 3400 -32 -13 38 O ATOM 547 N ILE A 68 10.161 -7.778 -14.738 1.00 21.93 N ANISOU 547 N ILE A 68 2749 2809 2776 -33 -14 38 N ATOM 548 CA ILE A 68 9.715 -8.060 -13.369 1.00 21.33 C ANISOU 548 CA ILE A 68 2672 2732 2700 -32 -14 38 C ATOM 549 C ILE A 68 9.970 -6.865 -12.437 1.00 24.75 C ANISOU 549 C ILE A 68 3106 3165 3132 -33 -14 37 C ATOM 550 O ILE A 68 9.151 -6.595 -11.566 1.00 23.90 O ANISOU 550 O ILE A 68 2999 3057 3024 -32 -14 37 O ATOM 551 CB ILE A 68 10.250 -9.416 -12.815 1.00 24.27 C ANISOU 551 CB ILE A 68 3044 3105 3072 -32 -14 38 C ATOM 552 CG1 ILE A 68 9.452 -9.902 -11.588 1.00 24.40 C ANISOU 552 CG1 ILE A 68 3060 3122 3088 -32 -14 38 C ATOM 553 CG2 ILE A 68 11.753 -9.360 -12.504 1.00 26.33 C ANISOU 553 CG2 ILE A 68 3304 3366 3333 -33 -15 37 C ATOM 554 CD1 ILE A 68 8.026 -10.292 -11.816 1.00 29.20 C ANISOU 554 CD1 ILE A 68 3668 3730 3697 -31 -14 39 C ATOM 555 N LYS A 69 11.092 -6.148 -12.637 1.00 21.92 N ANISOU 555 N LYS A 69 2748 2807 2774 -33 -14 37 N ATOM 556 CA LYS A 69 11.433 -4.953 -11.862 1.00 22.46 C ANISOU 556 CA LYS A 69 2818 2875 2843 -33 -15 37 C ATOM 557 C LYS A 69 10.345 -3.894 -12.057 1.00 26.50 C ANISOU 557 C LYS A 69 3329 3385 3354 -33 -14 36 C ATOM 558 O LYS A 69 9.849 -3.364 -11.064 1.00 26.46 O ANISOU 558 O LYS A 69 3325 3379 3348 -32 -15 36 O ATOM 559 CB LYS A 69 12.818 -4.413 -12.271 1.00 25.40 C ANISOU 559 CB LYS A 69 3190 3247 3216 -34 -15 36 C ATOM 560 CG LYS A 69 13.265 -3.183 -11.488 1.00 45.37 C ANISOU 560 CG LYS A 69 5719 5774 5744 -35 -16 36 C ATOM 561 CD LYS A 69 14.650 -2.728 -11.905 1.00 57.73 C ANISOU 561 CD LYS A 69 7285 7340 7311 -36 -16 36 C ATOM 562 CE LYS A 69 15.069 -1.489 -11.157 1.00 72.54 C ANISOU 562 CE LYS A 69 9161 9215 9187 -36 -17 36 C ATOM 563 NZ LYS A 69 16.425 -1.040 -11.562 1.00 83.31 N ANISOU 563 NZ LYS A 69 10525 10578 10552 -37 -18 36 N ATOM 564 N ALA A 70 9.927 -3.640 -13.319 1.00 22.83 N ANISOU 564 N ALA A 70 2865 2920 2890 -33 -14 37 N ATOM 565 CA ALA A 70 8.888 -2.658 -13.656 1.00 22.78 C ANISOU 565 CA ALA A 70 2859 2913 2884 -33 -14 37 C ATOM 566 C ALA A 70 7.571 -2.882 -12.900 1.00 26.19 C ANISOU 566 C ALA A 70 3292 3345 3315 -32 -14 37 C ATOM 567 O ALA A 70 6.936 -1.915 -12.488 1.00 26.57 O ANISOU 567 O ALA A 70 3339 3392 3363 -32 -14 36 O ATOM 568 CB ALA A 70 8.646 -2.634 -15.156 1.00 23.17 C ANISOU 568 CB ALA A 70 2909 2963 2934 -34 -14 38 C ATOM 569 N VAL A 71 7.192 -4.155 -12.675 1.00 22.10 N ANISOU 569 N VAL A 71 2742 2751 2906 -67 -124 -296 N ATOM 570 CA VAL A 71 5.991 -4.515 -11.931 1.00 21.79 C ANISOU 570 CA VAL A 71 2700 2711 2870 -64 -125 -299 C ATOM 571 C VAL A 71 6.256 -4.495 -10.416 1.00 24.54 C ANISOU 571 C VAL A 71 3045 3062 3218 -67 -124 -298 C ATOM 572 O VAL A 71 5.539 -3.816 -9.680 1.00 23.14 O ANISOU 572 O VAL A 71 2868 2882 3040 -68 -124 -301 O ATOM 573 CB VAL A 71 5.423 -5.891 -12.394 1.00 26.17 C ANISOU 573 CB VAL A 71 3250 3266 3428 -60 -125 -299 C ATOM 574 CG1 VAL A 71 4.267 -6.353 -11.508 1.00 26.07 C ANISOU 574 CG1 VAL A 71 3234 3252 3418 -58 -125 -303 C ATOM 575 CG2 VAL A 71 4.989 -5.845 -13.857 1.00 26.25 C ANISOU 575 CG2 VAL A 71 3263 3273 3439 -55 -127 -301 C ATOM 576 N MET A 72 7.266 -5.258 -9.957 1.00 20.51 N ANISOU 576 N MET A 72 2531 2554 2706 -70 -122 -296 N ATOM 577 CA MET A 72 7.545 -5.432 -8.532 1.00 19.29 C ANISOU 577 CA MET A 72 2376 2402 2552 -72 -121 -296 C ATOM 578 C MET A 72 7.995 -4.211 -7.762 1.00 23.59 C ANISOU 578 C MET A 72 2922 2946 3095 -74 -121 -296 C ATOM 579 O MET A 72 7.715 -4.132 -6.564 1.00 23.25 O ANISOU 579 O MET A 72 2878 2903 3052 -75 -120 -296 O ATOM 580 CB MET A 72 8.422 -6.656 -8.249 1.00 20.72 C ANISOU 580 CB MET A 72 2554 2586 2733 -73 -121 -294 C ATOM 581 CG MET A 72 7.877 -7.950 -8.828 1.00 23.64 C ANISOU 581 CG MET A 72 2921 2956 3105 -70 -122 -294 C ATOM 582 SD MET A 72 6.197 -8.410 -8.316 1.00 27.45 S ANISOU 582 SD MET A 72 3403 3437 3590 -68 -120 -296 S ATOM 583 CE MET A 72 6.493 -8.889 -6.667 1.00 23.99 C ANISOU 583 CE MET A 72 2965 2999 3150 -71 -119 -296 C ATOM 584 N GLU A 73 8.631 -3.236 -8.437 1.00 22.69 N ANISOU 584 N GLU A 73 2810 2831 2979 -75 -121 -295 N ATOM 585 CA GLU A 73 9.078 -2.011 -7.761 1.00 23.95 C ANISOU 585 CA GLU A 73 2972 2990 3138 -77 -121 -295 C ATOM 586 C GLU A 73 7.926 -1.132 -7.267 1.00 29.12 C ANISOU 586 C GLU A 73 3627 3644 3793 -76 -123 -297 C ATOM 587 O GLU A 73 8.141 -0.227 -6.463 1.00 28.71 O ANISOU 587 O GLU A 73 3575 3592 3742 -77 -124 -297 O ATOM 588 CB GLU A 73 10.115 -1.232 -8.581 1.00 25.61 C ANISOU 588 CB GLU A 73 3184 3200 3346 -79 -120 -294 C ATOM 589 CG GLU A 73 9.592 -0.434 -9.766 1.00 37.00 C ANISOU 589 CG GLU A 73 4632 4639 4787 -79 -121 -294 C ATOM 590 CD GLU A 73 10.689 0.136 -10.649 1.00 63.80 C ANISOU 590 CD GLU A 73 8030 8032 8179 -82 -119 -293 C ATOM 591 OE1 GLU A 73 11.881 -0.165 -10.402 1.00 59.68 O ANISOU 591 OE1 GLU A 73 7506 7513 7658 -84 -117 -294 O ATOM 592 OE2 GLU A 73 10.354 0.878 -11.599 1.00 61.37 O ANISOU 592 OE2 GLU A 73 7728 7722 7869 -82 -121 -293 O ATOM 593 N LEU A 74 6.709 -1.411 -7.739 1.00 26.69 N ANISOU 593 N LEU A 74 3320 3334 3487 -74 -124 -299 N ATOM 594 CA LEU A 74 5.513 -0.687 -7.320 1.00 26.41 C ANISOU 594 CA LEU A 74 3285 3298 3453 -73 -127 -303 C ATOM 595 C LEU A 74 4.925 -1.320 -6.056 1.00 28.28 C ANISOU 595 C LEU A 74 3517 3536 3691 -74 -125 -304 C ATOM 596 O LEU A 74 4.167 -0.668 -5.337 1.00 27.90 O ANISOU 596 O LEU A 74 3468 3488 3645 -75 -127 -308 O ATOM 597 CB LEU A 74 4.461 -0.726 -8.448 1.00 26.81 C ANISOU 597 CB LEU A 74 3338 3344 3505 -70 -130 -307 C ATOM 598 CG LEU A 74 4.872 -0.178 -9.821 1.00 32.07 C ANISOU 598 CG LEU A 74 4010 4007 4168 -69 -132 -305 C ATOM 599 CD1 LEU A 74 3.787 -0.432 -10.844 1.00 32.30 C ANISOU 599 CD1 LEU A 74 4042 4032 4200 -65 -135 -310 C ATOM 600 CD2 LEU A 74 5.199 1.321 -9.752 1.00 35.80 C ANISOU 600 CD2 LEU A 74 4486 4479 4639 -71 -135 -305 C ATOM 601 N LEU A 75 5.309 -2.581 -5.774 1.00 22.43 N ANISOU 601 N LEU A 75 2775 2797 2951 -74 -122 -302 N ATOM 602 CA LEU A 75 4.745 -3.417 -4.717 1.00 21.12 C ANISOU 602 CA LEU A 75 2607 2632 2786 -75 -120 -304 C ATOM 603 C LEU A 75 5.621 -3.746 -3.521 1.00 24.11 C ANISOU 603 C LEU A 75 2986 3013 3163 -77 -118 -301 C ATOM 604 O LEU A 75 5.075 -3.975 -2.440 1.00 24.32 O ANISOU 604 O LEU A 75 3012 3040 3190 -78 -116 -302 O ATOM 605 CB LEU A 75 4.260 -4.736 -5.343 1.00 20.57 C ANISOU 605 CB LEU A 75 2537 2562 2718 -74 -118 -304 C ATOM 606 CG LEU A 75 3.397 -4.633 -6.598 1.00 24.28 C ANISOU 606 CG LEU A 75 3007 3029 3191 -70 -120 -308 C ATOM 607 CD1 LEU A 75 3.123 -5.999 -7.160 1.00 23.40 C ANISOU 607 CD1 LEU A 75 2893 2917 3081 -68 -119 -307 C ATOM 608 CD2 LEU A 75 2.091 -3.896 -6.316 1.00 26.51 C ANISOU 608 CD2 LEU A 75 3289 3309 3475 -70 -122 -314 C ATOM 609 N ILE A 76 6.944 -3.881 -3.723 1.00 21.51 N ANISOU 609 N ILE A 76 2657 2684 2832 -77 -118 -298 N ATOM 610 CA ILE A 76 7.880 -4.265 -2.665 1.00 22.26 C ANISOU 610 CA ILE A 76 2753 2779 2925 -78 -118 -296 C ATOM 611 C ILE A 76 9.099 -3.382 -2.686 1.00 25.67 C ANISOU 611 C ILE A 76 3184 3211 3357 -77 -119 -296 C ATOM 612 O ILE A 76 9.421 -2.796 -3.724 1.00 24.48 O ANISOU 612 O ILE A 76 3034 3061 3206 -77 -119 -295 O ATOM 613 CB ILE A 76 8.292 -5.770 -2.722 1.00 26.30 C ANISOU 613 CB ILE A 76 3265 3291 3437 -78 -118 -296 C ATOM 614 CG1 ILE A 76 8.916 -6.157 -4.084 1.00 26.71 C ANISOU 614 CG1 ILE A 76 3316 3344 3489 -77 -119 -295 C ATOM 615 CG2 ILE A 76 7.149 -6.688 -2.319 1.00 29.76 C ANISOU 615 CG2 ILE A 76 3704 3729 3875 -78 -116 -297 C ATOM 616 CD1 ILE A 76 9.615 -7.532 -4.178 1.00 37.86 C ANISOU 616 CD1 ILE A 76 4728 4757 4901 -77 -120 -295 C ATOM 617 N ASP A 77 9.807 -3.342 -1.541 1.00 23.22 N ANISOU 617 N ASP A 77 2875 2901 3046 -77 -119 -296 N ATOM 618 CA ASP A 77 11.035 -2.571 -1.376 1.00 23.07 C ANISOU 618 CA ASP A 77 2856 2882 3028 -76 -119 -296 C ATOM 619 C ASP A 77 12.114 -2.996 -2.368 1.00 28.04 C ANISOU 619 C ASP A 77 3485 3511 3657 -77 -119 -297 C ATOM 620 O ASP A 77 12.118 -4.144 -2.840 1.00 27.07 O ANISOU 620 O ASP A 77 3362 3388 3534 -77 -120 -297 O ATOM 621 CB ASP A 77 11.565 -2.680 0.060 1.00 24.25 C ANISOU 621 CB ASP A 77 3006 3031 3178 -74 -120 -297 C ATOM 622 CG ASP A 77 12.050 -4.066 0.406 1.00 30.93 C ANISOU 622 CG ASP A 77 3855 3875 4022 -74 -120 -298 C ATOM 623 OD1 ASP A 77 11.206 -4.917 0.738 1.00 30.42 O ANISOU 623 OD1 ASP A 77 3793 3811 3956 -75 -120 -297 O ATOM 624 OD2 ASP A 77 13.271 -4.310 0.307 1.00 36.23 O ANISOU 624 OD2 ASP A 77 4526 4545 4693 -73 -122 -301 O ATOM 625 N GLU A 78 13.029 -2.075 -2.646 1.00 26.94 N ANISOU 625 N GLU A 78 3345 3372 3519 -77 -119 -298 N ATOM 626 CA GLU A 78 14.125 -2.247 -3.586 1.00 27.26 C ANISOU 626 CA GLU A 78 3386 3413 3561 -78 -118 -300 C ATOM 627 C GLU A 78 15.002 -3.471 -3.314 1.00 28.19 C ANISOU 627 C GLU A 78 3503 3530 3678 -78 -120 -304 C ATOM 628 O GLU A 78 15.382 -4.159 -4.278 1.00 27.62 O ANISOU 628 O GLU A 78 3429 3458 3606 -79 -120 -305 O ATOM 629 CB GLU A 78 14.963 -0.980 -3.585 1.00 29.28 C ANISOU 629 CB GLU A 78 3641 3667 3818 -78 -117 -302 C ATOM 630 CG GLU A 78 16.046 -0.978 -4.637 1.00 45.57 C ANISOU 630 CG GLU A 78 5704 5730 5881 -81 -115 -305 C ATOM 631 CD GLU A 78 16.821 0.316 -4.758 1.00 75.99 C ANISOU 631 CD GLU A 78 9556 9582 9736 -82 -112 -307 C ATOM 632 OE1 GLU A 78 16.535 1.277 -4.005 1.00 75.34 O ANISOU 632 OE1 GLU A 78 9473 9498 9654 -80 -113 -305 O ATOM 633 OE2 GLU A 78 17.717 0.368 -5.630 1.00 74.49 O ANISOU 633 OE2 GLU A 78 9366 9391 9545 -85 -110 -310 O ATOM 634 N ASN A 79 15.343 -3.732 -2.037 1.00 23.64 N ANISOU 634 N ASN A 79 2927 2952 3102 -75 -121 -306 N ATOM 635 CA ASN A 79 16.201 -4.871 -1.733 1.00 22.48 C ANISOU 635 CA ASN A 79 2781 2804 2955 -74 -124 -310 C ATOM 636 C ASN A 79 15.475 -6.205 -1.947 1.00 23.67 C ANISOU 636 C ASN A 79 2933 2956 3104 -75 -126 -308 C ATOM 637 O ASN A 79 16.091 -7.164 -2.411 1.00 22.94 O ANISOU 637 O ASN A 79 2841 2864 3012 -76 -129 -311 O ATOM 638 CB ASN A 79 16.882 -4.700 -0.387 1.00 25.40 C ANISOU 638 CB ASN A 79 3154 3171 3327 -71 -126 -314 C ATOM 639 CG ASN A 79 17.829 -3.515 -0.413 1.00 52.31 C ANISOU 639 CG ASN A 79 6560 6578 6739 -70 -124 -317 C ATOM 640 OD1 ASN A 79 18.644 -3.347 -1.333 1.00 48.16 O ANISOU 640 OD1 ASN A 79 6031 6052 6214 -72 -123 -321 O ATOM 641 ND2 ASN A 79 17.677 -2.617 0.545 1.00 47.43 N ANISOU 641 ND2 ASN A 79 5941 5959 6122 -67 -123 -316 N ATOM 642 N SER A 80 14.145 -6.227 -1.752 1.00 18.35 N ANISOU 642 N SER A 80 2260 2282 2429 -76 -125 -303 N ATOM 643 CA SER A 80 13.337 -7.425 -2.017 1.00 17.49 C ANISOU 643 CA SER A 80 2153 2175 2319 -77 -126 -301 C ATOM 644 C SER A 80 13.234 -7.701 -3.519 1.00 18.73 C ANISOU 644 C SER A 80 2306 2334 2477 -78 -125 -301 C ATOM 645 O SER A 80 13.223 -8.869 -3.910 1.00 17.25 O ANISOU 645 O SER A 80 2118 2148 2290 -78 -128 -301 O ATOM 646 CB SER A 80 11.947 -7.289 -1.407 1.00 20.20 C ANISOU 646 CB SER A 80 2496 2517 2661 -77 -123 -298 C ATOM 647 OG SER A 80 12.021 -7.295 0.009 1.00 24.52 O ANISOU 647 OG SER A 80 3047 3062 3206 -76 -123 -299 O ATOM 648 N VAL A 81 13.168 -6.641 -4.356 1.00 17.19 N ANISOU 648 N VAL A 81 1995 2364 2172 8 -90 -302 N ATOM 649 CA VAL A 81 13.134 -6.773 -5.826 1.00 17.40 C ANISOU 649 CA VAL A 81 2025 2388 2199 8 -89 -300 C ATOM 650 C VAL A 81 14.439 -7.447 -6.300 1.00 21.10 C ANISOU 650 C VAL A 81 2493 2856 2666 8 -86 -297 C ATOM 651 O VAL A 81 14.392 -8.399 -7.084 1.00 20.13 O ANISOU 651 O VAL A 81 2373 2733 2542 8 -85 -296 O ATOM 652 CB VAL A 81 12.899 -5.415 -6.556 1.00 22.44 C ANISOU 652 CB VAL A 81 2663 3024 2839 8 -91 -300 C ATOM 653 CG1 VAL A 81 12.952 -5.581 -8.079 1.00 22.84 C ANISOU 653 CG1 VAL A 81 2717 3073 2888 9 -90 -298 C ATOM 654 CG2 VAL A 81 11.570 -4.789 -6.145 1.00 22.40 C ANISOU 654 CG2 VAL A 81 2657 3019 2833 8 -95 -305 C ATOM 655 N LYS A 82 15.597 -6.982 -5.788 1.00 19.52 N ANISOU 655 N LYS A 82 2291 2655 2468 8 -86 -297 N ATOM 656 CA LYS A 82 16.904 -7.547 -6.144 1.00 19.03 C ANISOU 656 CA LYS A 82 2230 2593 2406 8 -84 -295 C ATOM 657 C LYS A 82 16.975 -9.014 -5.728 1.00 21.30 C ANISOU 657 C LYS A 82 2518 2882 2691 9 -83 -295 C ATOM 658 O LYS A 82 17.483 -9.840 -6.486 1.00 20.64 O ANISOU 658 O LYS A 82 2436 2798 2606 8 -82 -294 O ATOM 659 CB LYS A 82 18.045 -6.734 -5.508 1.00 22.28 C ANISOU 659 CB LYS A 82 2639 3004 2822 9 -84 -296 C ATOM 660 CG LYS A 82 18.265 -5.371 -6.169 1.00 39.10 C ANISOU 660 CG LYS A 82 4769 5133 4956 8 -84 -295 C ATOM 661 CD LYS A 82 19.414 -4.603 -5.522 1.00 52.76 C ANISOU 661 CD LYS A 82 6495 6861 6691 9 -84 -297 C ATOM 662 CE LYS A 82 19.491 -3.172 -6.000 1.00 67.78 C ANISOU 662 CE LYS A 82 8396 8760 8599 8 -85 -296 C ATOM 663 NZ LYS A 82 20.524 -2.399 -5.258 1.00 78.31 N ANISOU 663 NZ LYS A 82 9724 10092 9938 10 -84 -300 N ATOM 664 N GLN A 83 16.411 -9.348 -4.546 1.00 17.06 N ANISOU 664 N GLN A 83 1982 2348 2154 9 -84 -296 N ATOM 665 CA GLN A 83 16.393 -10.726 -4.053 1.00 16.15 C ANISOU 665 CA GLN A 83 1868 2233 2037 10 -82 -296 C ATOM 666 C GLN A 83 15.554 -11.614 -4.973 1.00 18.95 C ANISOU 666 C GLN A 83 2223 2587 2390 9 -82 -295 C ATOM 667 O GLN A 83 15.973 -12.725 -5.303 1.00 17.65 O ANISOU 667 O GLN A 83 2060 2422 2225 9 -81 -294 O ATOM 668 CB GLN A 83 15.851 -10.773 -2.624 1.00 16.93 C ANISOU 668 CB GLN A 83 1965 2334 2134 11 -83 -297 C ATOM 669 CG GLN A 83 15.877 -12.171 -2.001 1.00 19.20 C ANISOU 669 CG GLN A 83 2254 2622 2419 11 -81 -295 C ATOM 670 CD GLN A 83 15.254 -12.186 -0.626 1.00 24.73 C ANISOU 670 CD GLN A 83 2953 3325 3117 12 -81 -295 C ATOM 671 OE1 GLN A 83 14.776 -11.166 -0.118 1.00 23.16 O ANISOU 671 OE1 GLN A 83 2752 3129 2919 12 -83 -297 O ATOM 672 NE2 GLN A 83 15.227 -13.349 -0.002 1.00 20.97 N ANISOU 672 NE2 GLN A 83 2479 2850 2639 13 -80 -293 N ATOM 673 N LEU A 84 14.359 -11.125 -5.366 1.00 16.55 N ANISOU 673 N LEU A 84 1920 2283 2087 8 -82 -296 N ATOM 674 CA LEU A 84 13.439 -11.828 -6.259 1.00 16.27 C ANISOU 674 CA LEU A 84 1884 2246 2050 8 -81 -297 C ATOM 675 C LEU A 84 14.132 -12.091 -7.597 1.00 18.86 C ANISOU 675 C LEU A 84 2212 2574 2379 9 -81 -296 C ATOM 676 O LEU A 84 14.099 -13.218 -8.085 1.00 17.79 O ANISOU 676 O LEU A 84 2077 2439 2244 10 -80 -296 O ATOM 677 CB LEU A 84 12.170 -10.960 -6.440 1.00 16.50 C ANISOU 677 CB LEU A 84 1914 2275 2080 8 -82 -300 C ATOM 678 CG LEU A 84 11.043 -11.464 -7.357 1.00 21.35 C ANISOU 678 CG LEU A 84 2529 2890 2695 9 -81 -302 C ATOM 679 CD1 LEU A 84 9.755 -10.737 -7.049 1.00 21.15 C ANISOU 679 CD1 LEU A 84 2504 2865 2669 9 -83 -306 C ATOM 680 CD2 LEU A 84 11.370 -11.238 -8.827 1.00 24.85 C ANISOU 680 CD2 LEU A 84 2972 3333 3138 11 -82 -302 C ATOM 681 N VAL A 85 14.748 -11.052 -8.187 1.00 16.81 N ANISOU 681 N VAL A 85 1954 2315 2120 9 -81 -294 N ATOM 682 CA VAL A 85 15.447 -11.176 -9.480 1.00 16.89 C ANISOU 682 CA VAL A 85 1963 2325 2130 10 -81 -293 C ATOM 683 C VAL A 85 16.516 -12.281 -9.424 1.00 19.26 C ANISOU 683 C VAL A 85 2262 2626 2429 9 -81 -293 C ATOM 684 O VAL A 85 16.545 -13.134 -10.310 1.00 19.16 O ANISOU 684 O VAL A 85 2248 2615 2416 10 -81 -293 O ATOM 685 CB VAL A 85 16.021 -9.817 -9.963 1.00 21.00 C ANISOU 685 CB VAL A 85 2484 2845 2650 9 -81 -291 C ATOM 686 CG1 VAL A 85 16.980 -10.000 -11.142 1.00 21.37 C ANISOU 686 CG1 VAL A 85 2530 2893 2696 10 -80 -289 C ATOM 687 CG2 VAL A 85 14.900 -8.851 -10.337 1.00 20.99 C ANISOU 687 CG2 VAL A 85 2484 2843 2649 10 -82 -292 C ATOM 688 N SER A 86 17.367 -12.279 -8.376 1.00 17.33 N ANISOU 688 N SER A 86 2018 2381 2185 9 -81 -293 N ATOM 689 CA SER A 86 18.420 -13.288 -8.226 1.00 17.40 C ANISOU 689 CA SER A 86 2027 2391 2194 8 -81 -293 C ATOM 690 C SER A 86 17.862 -14.679 -8.001 1.00 22.18 C ANISOU 690 C SER A 86 2632 2996 2799 9 -82 -294 C ATOM 691 O SER A 86 18.385 -15.650 -8.550 1.00 23.26 O ANISOU 691 O SER A 86 2768 3134 2937 9 -83 -294 O ATOM 692 CB SER A 86 19.371 -12.912 -7.092 1.00 22.70 C ANISOU 692 CB SER A 86 2699 3062 2865 8 -82 -294 C ATOM 693 OG SER A 86 19.993 -11.668 -7.370 1.00 35.15 O ANISOU 693 OG SER A 86 4275 4638 4443 8 -81 -294 O ATOM 694 N ASP A 87 16.782 -14.775 -7.219 1.00 18.81 N ANISOU 694 N ASP A 87 2206 2569 2373 9 -81 -293 N ATOM 695 CA ASP A 87 16.147 -16.041 -6.892 1.00 18.27 C ANISOU 695 CA ASP A 87 2137 2499 2306 9 -80 -293 C ATOM 696 C ASP A 87 15.497 -16.638 -8.131 1.00 22.09 C ANISOU 696 C ASP A 87 2618 2983 2791 10 -80 -295 C ATOM 697 O ASP A 87 15.763 -17.785 -8.491 1.00 22.55 O ANISOU 697 O ASP A 87 2674 3041 2851 10 -81 -295 O ATOM 698 CB ASP A 87 15.105 -15.783 -5.785 1.00 19.98 C ANISOU 698 CB ASP A 87 2354 2715 2521 9 -79 -293 C ATOM 699 CG ASP A 87 14.330 -16.960 -5.237 1.00 23.57 C ANISOU 699 CG ASP A 87 2809 3169 2978 8 -77 -292 C ATOM 700 OD1 ASP A 87 14.648 -18.120 -5.606 1.00 23.70 O ANISOU 700 OD1 ASP A 87 2825 3184 2996 9 -78 -292 O ATOM 701 OD2 ASP A 87 13.420 -16.727 -4.426 1.00 23.14 O ANISOU 701 OD2 ASP A 87 2756 3115 2923 8 -76 -292 O ATOM 702 N CYS A 88 14.664 -15.856 -8.805 1.00 18.12 N ANISOU 702 N CYS A 88 2116 2481 2289 11 -80 -296 N ATOM 703 CA CYS A 88 13.973 -16.399 -9.947 0.70 18.21 C ANISOU 703 CA CYS A 88 2124 2493 2301 13 -79 -298 C ATOM 704 C CYS A 88 14.853 -16.574 -11.222 1.00 20.32 C ANISOU 704 C CYS A 88 2389 2764 2569 14 -81 -298 C ATOM 705 O CYS A 88 14.553 -17.428 -12.054 1.00 20.25 O ANISOU 705 O CYS A 88 2376 2756 2562 17 -81 -301 O ATOM 706 CB CYS A 88 12.636 -15.695 -10.159 0.70 19.40 C ANISOU 706 CB CYS A 88 2275 2644 2452 14 -78 -300 C ATOM 707 SG CYS A 88 11.684 -15.446 -8.610 0.70 22.64 S ANISOU 707 SG CYS A 88 2688 3052 2862 12 -77 -301 S ATOM 708 N SER A 89 16.065 -15.955 -11.236 1.00 16.56 N ANISOU 708 N SER A 89 1914 2288 2090 13 -82 -296 N ATOM 709 CA SER A 89 17.040 -16.183 -12.316 1.00 16.39 C ANISOU 709 CA SER A 89 1890 2270 2069 13 -83 -297 C ATOM 710 C SER A 89 17.673 -17.593 -12.223 1.00 20.15 C ANISOU 710 C SER A 89 2363 2747 2547 13 -85 -298 C ATOM 711 O SER A 89 18.284 -18.039 -13.192 1.00 19.87 O ANISOU 711 O SER A 89 2323 2714 2511 14 -87 -300 O ATOM 712 CB SER A 89 18.138 -15.129 -12.288 1.00 18.79 C ANISOU 712 CB SER A 89 2196 2574 2370 12 -83 -295 C ATOM 713 OG SER A 89 17.635 -13.863 -12.674 1.00 25.07 O ANISOU 713 OG SER A 89 2993 3369 3164 12 -82 -293 O ATOM 714 N THR A 90 17.533 -18.289 -11.067 1.00 18.64 N ANISOU 714 N THR A 90 2173 2552 2356 12 -85 -298 N ATOM 715 CA THR A 90 18.100 -19.636 -10.880 1.00 18.25 C ANISOU 715 CA THR A 90 2122 2503 2310 12 -88 -299 C ATOM 716 C THR A 90 17.245 -20.745 -11.472 1.00 23.76 C ANISOU 716 C THR A 90 2814 3200 3012 14 -88 -301 C ATOM 717 O THR A 90 17.727 -21.878 -11.605 1.00 24.27 O ANISOU 717 O THR A 90 2876 3266 3080 14 -91 -303 O ATOM 718 CB THR A 90 18.432 -19.922 -9.405 1.00 24.10 C ANISOU 718 CB THR A 90 2866 3240 3050 11 -88 -297 C ATOM 719 OG1 THR A 90 17.226 -20.001 -8.648 1.00 24.22 O ANISOU 719 OG1 THR A 90 2883 3253 3067 11 -85 -296 O ATOM 720 CG2 THR A 90 19.402 -18.917 -8.805 1.00 25.08 C ANISOU 720 CG2 THR A 90 2994 3365 3170 9 -87 -297 C ATOM 721 N ILE A 91 15.966 -20.439 -11.797 1.00 20.30 N ANISOU 721 N ILE A 91 2482 2637 2595 193 -162 -418 N ATOM 722 CA ILE A 91 15.042 -21.411 -12.383 1.00 20.19 C ANISOU 722 CA ILE A 91 2473 2620 2577 191 -164 -413 C ATOM 723 C ILE A 91 15.526 -21.744 -13.783 1.00 23.82 C ANISOU 723 C ILE A 91 2937 3077 3036 189 -163 -413 C ATOM 724 O ILE A 91 15.658 -20.860 -14.624 1.00 22.31 O ANISOU 724 O ILE A 91 2746 2884 2846 186 -162 -413 O ATOM 725 CB ILE A 91 13.570 -20.918 -12.344 1.00 22.97 C ANISOU 725 CB ILE A 91 2825 2973 2931 189 -166 -411 C ATOM 726 CG1 ILE A 91 13.078 -20.796 -10.878 1.00 23.32 C ANISOU 726 CG1 ILE A 91 2864 3021 2975 191 -168 -411 C ATOM 727 CG2 ILE A 91 12.647 -21.845 -13.172 1.00 23.20 C ANISOU 727 CG2 ILE A 91 2859 2999 2958 187 -168 -407 C ATOM 728 CD1 ILE A 91 11.871 -19.943 -10.711 1.00 27.57 C ANISOU 728 CD1 ILE A 91 3401 3560 3516 189 -170 -411 C ATOM 729 N SER A 92 15.854 -23.013 -13.990 1.00 23.10 N ANISOU 729 N SER A 92 2848 2986 2943 189 -164 -413 N ATOM 730 CA SER A 92 16.356 -23.536 -15.247 1.00 23.97 C ANISOU 730 CA SER A 92 2960 3094 3051 187 -163 -413 C ATOM 731 C SER A 92 15.491 -24.729 -15.567 1.00 27.33 C ANISOU 731 C SER A 92 3389 3519 3477 187 -165 -410 C ATOM 732 O SER A 92 15.405 -25.674 -14.782 1.00 26.77 O ANISOU 732 O SER A 92 3317 3448 3405 189 -167 -409 O ATOM 733 CB SER A 92 17.825 -23.932 -15.114 1.00 29.12 C ANISOU 733 CB SER A 92 3612 3748 3703 189 -163 -419 C ATOM 734 OG SER A 92 18.319 -24.490 -16.320 1.00 37.63 O ANISOU 734 OG SER A 92 4692 4825 4780 186 -163 -420 O ATOM 735 N GLU A 93 14.775 -24.636 -16.675 1.00 24.92 N ANISOU 735 N GLU A 93 3084 3212 3171 185 -166 -408 N ATOM 736 CA GLU A 93 13.827 -25.658 -17.080 1.00 25.22 C ANISOU 736 CA GLU A 93 3124 3249 3209 185 -167 -405 C ATOM 737 C GLU A 93 13.856 -25.773 -18.584 1.00 28.92 C ANISOU 737 C GLU A 93 3593 3717 3677 183 -167 -405 C ATOM 738 O GLU A 93 13.676 -24.763 -19.268 1.00 28.92 O ANISOU 738 O GLU A 93 3595 3717 3677 182 -166 -405 O ATOM 739 CB GLU A 93 12.431 -25.224 -16.596 1.00 27.05 C ANISOU 739 CB GLU A 93 3356 3481 3441 185 -167 -403 C ATOM 740 CG GLU A 93 11.569 -26.301 -15.980 1.00 37.77 C ANISOU 740 CG GLU A 93 4715 4838 4799 186 -168 -402 C ATOM 741 CD GLU A 93 12.230 -27.187 -14.945 1.00 52.20 C ANISOU 741 CD GLU A 93 6541 6666 6626 187 -168 -402 C ATOM 742 OE1 GLU A 93 12.578 -26.688 -13.852 1.00 43.46 O ANISOU 742 OE1 GLU A 93 5434 5561 5519 189 -168 -402 O ATOM 743 OE2 GLU A 93 12.395 -28.391 -15.234 1.00 40.81 O ANISOU 743 OE2 GLU A 93 5100 5223 5184 188 -169 -401 O ATOM 744 N GLU A 94 14.102 -26.993 -19.104 1.00 25.40 N ANISOU 744 N GLU A 94 3147 3272 3231 183 -168 -406 N ATOM 745 CA GLU A 94 14.136 -27.236 -20.550 1.00 25.97 C ANISOU 745 CA GLU A 94 3219 3346 3304 182 -168 -407 C ATOM 746 C GLU A 94 12.717 -27.107 -21.112 1.00 26.83 C ANISOU 746 C GLU A 94 3328 3454 3413 183 -168 -405 C ATOM 747 O GLU A 94 12.550 -26.657 -22.244 1.00 26.88 O ANISOU 747 O GLU A 94 3335 3461 3418 183 -167 -405 O ATOM 748 CB GLU A 94 14.738 -28.615 -20.879 1.00 27.99 C ANISOU 748 CB GLU A 94 3471 3602 3561 183 -170 -409 C ATOM 749 CG GLU A 94 15.142 -28.793 -22.338 1.00 43.85 C ANISOU 749 CG GLU A 94 5478 5614 5569 181 -170 -411 C ATOM 750 CD GLU A 94 16.440 -28.159 -22.811 1.00 73.40 C ANISOU 750 CD GLU A 94 9220 9358 9309 178 -170 -415 C ATOM 751 OE1 GLU A 94 17.356 -27.953 -21.981 1.00 74.13 O ANISOU 751 OE1 GLU A 94 9314 9451 9402 178 -169 -417 O ATOM 752 OE2 GLU A 94 16.561 -27.925 -24.035 1.00 69.59 O ANISOU 752 OE2 GLU A 94 8737 8878 8826 176 -169 -415 O ATOM 753 N ASN A 95 11.698 -27.471 -20.311 1.00 20.46 N ANISOU 753 N ASN A 95 2522 2646 2607 185 -168 -404 N ATOM 754 CA ASN A 95 10.299 -27.337 -20.718 1.00 18.14 C ANISOU 754 CA ASN A 95 2228 2350 2313 186 -168 -403 C ATOM 755 C ASN A 95 9.896 -25.865 -20.463 1.00 19.08 C ANISOU 755 C ASN A 95 2349 2469 2431 185 -168 -403 C ATOM 756 O ASN A 95 9.827 -25.462 -19.300 1.00 17.50 O ANISOU 756 O ASN A 95 2150 2268 2231 185 -168 -402 O ATOM 757 CB ASN A 95 9.422 -28.308 -19.944 1.00 16.57 C ANISOU 757 CB ASN A 95 2028 2150 2116 187 -168 -404 C ATOM 758 CG ASN A 95 7.942 -28.199 -20.269 1.00 22.21 C ANISOU 758 CG ASN A 95 2743 2864 2830 188 -167 -405 C ATOM 759 OD1 ASN A 95 7.454 -27.212 -20.841 1.00 21.25 O ANISOU 759 OD1 ASN A 95 2624 2743 2708 188 -168 -406 O ATOM 760 ND2 ASN A 95 7.196 -29.204 -19.892 1.00 19.76 N ANISOU 760 ND2 ASN A 95 2432 2553 2522 188 -166 -407 N ATOM 761 N PRO A 96 9.646 -25.046 -21.513 1.00 16.83 N ANISOU 761 N PRO A 96 2067 2184 2145 185 -168 -402 N ATOM 762 CA PRO A 96 9.337 -23.622 -21.277 1.00 17.06 C ANISOU 762 CA PRO A 96 2097 2211 2172 185 -169 -402 C ATOM 763 C PRO A 96 8.016 -23.365 -20.553 1.00 19.45 C ANISOU 763 C PRO A 96 2400 2513 2476 186 -170 -403 C ATOM 764 O PRO A 96 7.865 -22.330 -19.906 1.00 18.65 O ANISOU 764 O PRO A 96 2300 2412 2376 185 -172 -403 O ATOM 765 CB PRO A 96 9.362 -23.017 -22.684 1.00 19.25 C ANISOU 765 CB PRO A 96 2377 2489 2448 185 -168 -401 C ATOM 766 CG PRO A 96 9.012 -24.149 -23.580 1.00 23.61 C ANISOU 766 CG PRO A 96 2928 3043 3000 187 -168 -402 C ATOM 767 CD PRO A 96 9.658 -25.355 -22.960 1.00 18.77 C ANISOU 767 CD PRO A 96 2312 2432 2389 186 -168 -403 C ATOM 768 N HIS A 97 7.064 -24.309 -20.658 1.00 16.25 N ANISOU 768 N HIS A 97 1994 2108 2071 187 -170 -405 N ATOM 769 CA HIS A 97 5.768 -24.197 -20.000 1.00 14.82 C ANISOU 769 CA HIS A 97 1814 1927 1891 187 -172 -408 C ATOM 770 C HIS A 97 5.957 -24.419 -18.500 1.00 16.38 C ANISOU 770 C HIS A 97 2010 2125 2089 185 -172 -408 C ATOM 771 O HIS A 97 5.417 -23.664 -17.690 1.00 14.68 O ANISOU 771 O HIS A 97 1793 1909 1873 184 -173 -409 O ATOM 772 CB HIS A 97 4.770 -25.205 -20.585 1.00 15.80 C ANISOU 772 CB HIS A 97 1937 2051 2015 190 -171 -412 C ATOM 773 CG HIS A 97 4.388 -24.942 -22.010 1.00 19.25 C ANISOU 773 CG HIS A 97 2375 2488 2450 193 -171 -414 C ATOM 774 ND1 HIS A 97 4.370 -23.661 -22.537 1.00 21.67 N ANISOU 774 ND1 HIS A 97 2685 2794 2755 193 -173 -413 N ATOM 775 CD2 HIS A 97 3.941 -25.802 -22.949 1.00 20.77 C ANISOU 775 CD2 HIS A 97 2566 2682 2643 195 -170 -417 C ATOM 776 CE1 HIS A 97 3.950 -23.796 -23.785 1.00 20.46 C ANISOU 776 CE1 HIS A 97 2532 2641 2600 197 -173 -415 C ATOM 777 NE2 HIS A 97 3.671 -25.061 -24.072 1.00 20.91 N ANISOU 777 NE2 HIS A 97 2586 2700 2659 198 -171 -417 N ATOM 778 N LEU A 98 6.794 -25.414 -18.126 1.00 15.42 N ANISOU 778 N LEU A 98 1887 2004 1968 185 -170 -406 N ATOM 779 CA LEU A 98 7.086 -25.653 -16.713 1.00 15.34 C ANISOU 779 CA LEU A 98 1876 1995 1959 184 -170 -405 C ATOM 780 C LEU A 98 7.917 -24.505 -16.152 1.00 17.39 C ANISOU 780 C LEU A 98 2134 2255 2218 184 -171 -404 C ATOM 781 O LEU A 98 7.755 -24.134 -14.987 1.00 16.97 O ANISOU 781 O LEU A 98 2079 2204 2165 183 -171 -404 O ATOM 782 CB LEU A 98 7.790 -27.005 -16.518 1.00 15.81 C ANISOU 782 CB LEU A 98 1934 2053 2018 185 -168 -403 C ATOM 783 CG LEU A 98 8.159 -27.404 -15.082 1.00 20.34 C ANISOU 783 CG LEU A 98 2508 2628 2592 185 -168 -401 C ATOM 784 CD1 LEU A 98 6.943 -27.461 -14.181 1.00 20.03 C ANISOU 784 CD1 LEU A 98 2469 2590 2552 183 -168 -402 C ATOM 785 CD2 LEU A 98 8.884 -28.747 -15.074 1.00 22.14 C ANISOU 785 CD2 LEU A 98 2737 2856 2821 186 -167 -400 C ATOM 786 N LYS A 99 8.799 -23.925 -16.983 1.00 15.43 N ANISOU 786 N LYS A 99 1886 2007 1970 184 -170 -403 N ATOM 787 CA LYS A 99 9.597 -22.777 -16.577 1.00 14.40 C ANISOU 787 CA LYS A 99 1755 1877 1840 183 -170 -403 C ATOM 788 C LYS A 99 8.671 -21.624 -16.186 1.00 16.31 C ANISOU 788 C LYS A 99 1996 2119 2083 183 -172 -404 C ATOM 789 O LYS A 99 8.893 -20.993 -15.154 1.00 14.79 O ANISOU 789 O LYS A 99 1800 1928 1892 183 -173 -405 O ATOM 790 CB LYS A 99 10.529 -22.323 -17.703 1.00 17.02 C ANISOU 790 CB LYS A 99 2088 2207 2171 183 -169 -402 C ATOM 791 CG LYS A 99 11.689 -21.501 -17.171 1.00 28.08 C ANISOU 791 CG LYS A 99 3487 3609 3573 182 -167 -403 C ATOM 792 CD LYS A 99 12.179 -20.514 -18.186 1.00 35.16 C ANISOU 792 CD LYS A 99 4386 4504 4470 181 -166 -403 C ATOM 793 CE LYS A 99 13.457 -19.850 -17.740 1.00 34.99 C ANISOU 793 CE LYS A 99 4362 4483 4451 180 -164 -405 C ATOM 794 NZ LYS A 99 14.601 -20.307 -18.566 1.00 44.43 N ANISOU 794 NZ LYS A 99 5558 5678 5644 179 -161 -406 N ATOM 795 N ALA A 100 7.610 -21.387 -16.978 1.00 12.90 N ANISOU 795 N ALA A 100 1566 1685 1651 183 -174 -405 N ATOM 796 CA ALA A 100 6.667 -20.310 -16.701 1.00 12.60 C ANISOU 796 CA ALA A 100 1527 1646 1613 182 -177 -408 C ATOM 797 C ALA A 100 5.927 -20.490 -15.380 1.00 14.02 C ANISOU 797 C ALA A 100 1704 1829 1793 181 -179 -410 C ATOM 798 O ALA A 100 5.815 -19.527 -14.629 1.00 13.23 O ANISOU 798 O ALA A 100 1601 1731 1696 181 -181 -412 O ATOM 799 CB ALA A 100 5.681 -20.161 -17.845 1.00 13.65 C ANISOU 799 CB ALA A 100 1664 1777 1744 184 -179 -409 C ATOM 800 N SER A 101 5.430 -21.713 -15.085 1.00 11.73 N ANISOU 800 N SER A 101 1337 1615 1504 58 -295 -333 N ATOM 801 CA SER A 101 4.714 -21.906 -13.823 1.00 12.45 C ANISOU 801 CA SER A 101 1429 1704 1597 53 -295 -332 C ATOM 802 C SER A 101 5.682 -21.832 -12.645 1.00 14.73 C ANISOU 802 C SER A 101 1717 1997 1883 48 -294 -330 C ATOM 803 O SER A 101 5.334 -21.251 -11.620 1.00 13.23 O ANISOU 803 O SER A 101 1527 1807 1692 43 -291 -330 O ATOM 804 CB SER A 101 3.949 -23.223 -13.822 1.00 14.31 C ANISOU 804 CB SER A 101 1663 1935 1837 55 -300 -331 C ATOM 805 OG SER A 101 4.843 -24.298 -14.053 1.00 15.69 O ANISOU 805 OG SER A 101 1837 2112 2012 59 -307 -331 O ATOM 806 N LYS A 102 6.930 -22.337 -12.805 1.00 12.08 N ANISOU 806 N LYS A 102 1380 1664 1545 50 -296 -331 N ATOM 807 CA LYS A 102 7.919 -22.239 -11.735 1.00 11.88 C ANISOU 807 CA LYS A 102 1354 1642 1517 46 -296 -331 C ATOM 808 C LYS A 102 8.269 -20.779 -11.465 1.00 15.77 C ANISOU 808 C LYS A 102 1847 2137 2009 43 -290 -331 C ATOM 809 O LYS A 102 8.440 -20.400 -10.311 1.00 17.33 O ANISOU 809 O LYS A 102 2045 2335 2206 40 -289 -331 O ATOM 810 CB LYS A 102 9.160 -23.065 -12.059 1.00 14.27 C ANISOU 810 CB LYS A 102 1656 1948 1818 49 -300 -333 C ATOM 811 CG LYS A 102 8.876 -24.546 -11.909 1.00 20.43 C ANISOU 811 CG LYS A 102 2436 2725 2600 51 -309 -333 C ATOM 812 CD LYS A 102 10.095 -25.382 -12.088 1.00 26.87 C ANISOU 812 CD LYS A 102 3251 3545 3414 55 -315 -337 C ATOM 813 CE LYS A 102 9.814 -26.797 -11.644 1.00 33.97 C ANISOU 813 CE LYS A 102 4150 4440 4316 55 -325 -336 C ATOM 814 NZ LYS A 102 11.055 -27.603 -11.624 1.00 44.98 N ANISOU 814 NZ LYS A 102 5545 5837 5708 58 -333 -342 N ATOM 815 N LEU A 103 8.316 -19.953 -12.522 1.00 13.13 N ANISOU 815 N LEU A 103 1513 1804 1674 44 -288 -331 N ATOM 816 CA LEU A 103 8.597 -18.522 -12.368 1.00 12.08 C ANISOU 816 CA LEU A 103 1378 1670 1540 41 -285 -331 C ATOM 817 C LEU A 103 7.478 -17.786 -11.636 1.00 15.03 C ANISOU 817 C LEU A 103 1753 2041 1915 38 -284 -332 C ATOM 818 O LEU A 103 7.762 -16.985 -10.742 1.00 14.23 O ANISOU 818 O LEU A 103 1652 1941 1815 36 -284 -332 O ATOM 819 CB LEU A 103 8.899 -17.860 -13.713 1.00 12.49 C ANISOU 819 CB LEU A 103 1430 1725 1592 42 -284 -330 C ATOM 820 CG LEU A 103 10.323 -18.086 -14.227 1.00 15.77 C ANISOU 820 CG LEU A 103 1843 2146 2004 43 -284 -329 C ATOM 821 CD1 LEU A 103 10.401 -17.815 -15.698 1.00 17.02 C ANISOU 821 CD1 LEU A 103 1999 2307 2161 46 -283 -327 C ATOM 822 CD2 LEU A 103 11.340 -17.238 -13.464 1.00 16.40 C ANISOU 822 CD2 LEU A 103 1921 2227 2085 39 -282 -328 C ATOM 823 N VAL A 104 6.212 -18.052 -11.994 1.00 12.00 N ANISOU 823 N VAL A 104 1372 1655 1534 39 -285 -332 N ATOM 824 CA VAL A 104 5.081 -17.428 -11.304 1.00 11.87 C ANISOU 824 CA VAL A 104 1356 1637 1518 37 -284 -334 C ATOM 825 C VAL A 104 5.082 -17.875 -9.838 1.00 14.73 C ANISOU 825 C VAL A 104 1716 2002 1878 36 -285 -334 C ATOM 826 O VAL A 104 4.854 -17.055 -8.958 1.00 13.85 O ANISOU 826 O VAL A 104 1603 1892 1766 35 -285 -335 O ATOM 827 CB VAL A 104 3.745 -17.711 -12.027 1.00 14.70 C ANISOU 827 CB VAL A 104 1716 1991 1878 39 -285 -336 C ATOM 828 CG1 VAL A 104 2.539 -17.311 -11.172 1.00 14.77 C ANISOU 828 CG1 VAL A 104 1724 2000 1886 37 -285 -339 C ATOM 829 CG2 VAL A 104 3.700 -16.984 -13.372 1.00 14.49 C ANISOU 829 CG2 VAL A 104 1692 1962 1852 41 -285 -337 C ATOM 830 N GLN A 105 5.368 -19.163 -9.575 1.00 12.62 N ANISOU 830 N GLN A 105 1449 1735 1611 37 -286 -331 N ATOM 831 CA GLN A 105 5.450 -19.668 -8.210 1.00 12.80 C ANISOU 831 CA GLN A 105 1471 1761 1632 35 -286 -330 C ATOM 832 C GLN A 105 6.550 -18.916 -7.428 1.00 16.15 C ANISOU 832 C GLN A 105 1893 2187 2054 35 -285 -331 C ATOM 833 O GLN A 105 6.333 -18.537 -6.273 1.00 15.89 O ANISOU 833 O GLN A 105 1860 2159 2021 35 -285 -332 O ATOM 834 CB GLN A 105 5.709 -21.180 -8.236 1.00 13.27 C ANISOU 834 CB GLN A 105 1531 1819 1693 35 -289 -327 C ATOM 835 CG GLN A 105 5.819 -21.806 -6.844 1.00 17.52 C ANISOU 835 CG GLN A 105 2068 2360 2229 33 -290 -324 C ATOM 836 CD GLN A 105 6.133 -23.275 -6.926 1.00 29.65 C ANISOU 836 CD GLN A 105 3605 3894 3766 33 -295 -322 C ATOM 837 OE1 GLN A 105 7.161 -23.688 -7.473 1.00 24.12 O ANISOU 837 OE1 GLN A 105 2906 3192 3066 36 -298 -324 O ATOM 838 NE2 GLN A 105 5.234 -24.098 -6.414 1.00 24.11 N ANISOU 838 NE2 GLN A 105 2903 3192 3065 31 -297 -317 N ATOM 839 N CYS A 106 7.707 -18.655 -8.071 1.00 13.25 N ANISOU 839 N CYS A 106 1526 1819 1688 36 -285 -332 N ATOM 840 CA CYS A 106 8.815 -17.930 -7.456 1.00 15.01 C ANISOU 840 CA CYS A 106 1749 2044 1912 36 -285 -333 C ATOM 841 C CYS A 106 8.425 -16.492 -7.118 1.00 17.04 C ANISOU 841 C CYS A 106 2004 2301 2170 36 -285 -335 C ATOM 842 O CYS A 106 8.628 -16.050 -5.984 1.00 16.53 O ANISOU 842 O CYS A 106 1937 2238 2105 37 -286 -337 O ATOM 843 CB CYS A 106 10.033 -17.971 -8.367 1.00 16.80 C ANISOU 843 CB CYS A 106 1975 2271 2139 37 -285 -333 C ATOM 844 SG CYS A 106 11.526 -17.241 -7.640 1.00 21.80 S ANISOU 844 SG CYS A 106 2607 2905 2773 37 -284 -335 S ATOM 845 N VAL A 107 7.836 -15.771 -8.087 1.00 13.53 N ANISOU 845 N VAL A 107 1560 1855 1727 35 -286 -335 N ATOM 846 CA VAL A 107 7.413 -14.379 -7.867 1.00 13.31 C ANISOU 846 CA VAL A 107 1530 1827 1701 35 -289 -338 C ATOM 847 C VAL A 107 6.359 -14.328 -6.730 1.00 15.84 C ANISOU 847 C VAL A 107 1849 2151 2019 36 -290 -340 C ATOM 848 O VAL A 107 6.393 -13.409 -5.912 1.00 14.42 O ANISOU 848 O VAL A 107 1667 1973 1840 38 -294 -343 O ATOM 849 CB VAL A 107 6.859 -13.719 -9.164 1.00 16.31 C ANISOU 849 CB VAL A 107 1912 2204 2082 33 -290 -338 C ATOM 850 CG1 VAL A 107 6.371 -12.292 -8.894 1.00 15.49 C ANISOU 850 CG1 VAL A 107 1807 2099 1981 33 -295 -341 C ATOM 851 CG2 VAL A 107 7.901 -13.720 -10.288 1.00 15.95 C ANISOU 851 CG2 VAL A 107 1867 2157 2037 32 -288 -334 C ATOM 852 N SER A 108 5.436 -15.310 -6.698 1.00 14.99 N ANISOU 852 N SER A 108 1742 2044 1909 35 -288 -339 N ATOM 853 CA SER A 108 4.330 -15.405 -5.738 1.00 14.37 C ANISOU 853 CA SER A 108 1662 1971 1828 36 -288 -341 C ATOM 854 C SER A 108 4.754 -15.479 -4.283 1.00 19.12 C ANISOU 854 C SER A 108 2261 2578 2427 38 -289 -341 C ATOM 855 O SER A 108 3.969 -15.096 -3.410 1.00 20.74 O ANISOU 855 O SER A 108 2462 2789 2629 40 -290 -343 O ATOM 856 CB SER A 108 3.385 -16.549 -6.086 1.00 16.21 C ANISOU 856 CB SER A 108 1896 2203 2059 34 -286 -338 C ATOM 857 OG SER A 108 2.739 -16.286 -7.323 1.00 17.50 O ANISOU 857 OG SER A 108 2062 2362 2226 34 -286 -340 O ATOM 858 N LYS A 109 5.991 -15.934 -4.019 1.00 15.38 N ANISOU 858 N LYS A 109 1788 2103 1954 39 -288 -339 N ATOM 859 CA LYS A 109 6.549 -15.969 -2.658 1.00 15.66 C ANISOU 859 CA LYS A 109 1820 2142 1987 42 -288 -340 C ATOM 860 C LYS A 109 6.719 -14.538 -2.110 1.00 20.14 C ANISOU 860 C LYS A 109 2385 2712 2557 47 -292 -345 C ATOM 861 O LYS A 109 6.684 -14.341 -0.890 1.00 21.19 O ANISOU 861 O LYS A 109 2513 2850 2687 51 -294 -347 O ATOM 862 CB LYS A 109 7.945 -16.612 -2.647 1.00 17.66 C ANISOU 862 CB LYS A 109 2076 2391 2241 43 -287 -338 C ATOM 863 CG LYS A 109 7.996 -18.100 -2.961 1.00 30.48 C ANISOU 863 CG LYS A 109 3703 4014 3864 40 -285 -334 C ATOM 864 CD LYS A 109 9.391 -18.668 -2.642 1.00 38.53 C ANISOU 864 CD LYS A 109 4724 5030 4883 41 -285 -335 C ATOM 865 CE LYS A 109 10.499 -18.083 -3.493 1.00 45.00 C ANISOU 865 CE LYS A 109 5544 5846 5706 41 -286 -338 C ATOM 866 NZ LYS A 109 11.838 -18.531 -3.037 1.00 52.98 N ANISOU 866 NZ LYS A 109 6557 6856 6718 43 -286 -340 N ATOM 867 N TYR A 110 6.961 -13.559 -3.000 1.00 15.93 N ANISOU 867 N TYR A 110 1851 2173 2027 46 -295 -346 N ATOM 868 CA TYR A 110 7.211 -12.153 -2.646 1.00 15.73 C ANISOU 868 CA TYR A 110 1822 2148 2006 50 -302 -351 C ATOM 869 C TYR A 110 5.915 -11.355 -2.585 1.00 20.19 C ANISOU 869 C TYR A 110 2385 2717 2570 51 -307 -355 C ATOM 870 O TYR A 110 5.654 -10.685 -1.587 1.00 20.94 O ANISOU 870 O TYR A 110 2475 2817 2664 56 -313 -360 O ATOM 871 CB TYR A 110 8.241 -11.531 -3.613 1.00 16.69 C ANISOU 871 CB TYR A 110 1946 2263 2134 48 -303 -349 C ATOM 872 CG TYR A 110 9.579 -12.240 -3.578 1.00 16.99 C ANISOU 872 CG TYR A 110 1985 2299 2173 47 -299 -346 C ATOM 873 CD1 TYR A 110 10.617 -11.769 -2.779 1.00 18.80 C ANISOU 873 CD1 TYR A 110 2211 2526 2406 52 -302 -348 C ATOM 874 CD2 TYR A 110 9.797 -13.404 -4.313 1.00 16.50 C ANISOU 874 CD2 TYR A 110 1927 2235 2108 44 -294 -343 C ATOM 875 CE1 TYR A 110 11.849 -12.418 -2.741 1.00 19.63 C ANISOU 875 CE1 TYR A 110 2318 2628 2512 52 -298 -347 C ATOM 876 CE2 TYR A 110 11.022 -14.068 -4.273 1.00 17.20 C ANISOU 876 CE2 TYR A 110 2017 2322 2197 44 -291 -342 C ATOM 877 CZ TYR A 110 12.031 -13.593 -3.450 1.00 22.69 C ANISOU 877 CZ TYR A 110 2709 3015 2895 48 -293 -345 C ATOM 878 OH TYR A 110 13.244 -14.236 -3.400 1.00 23.04 O ANISOU 878 OH TYR A 110 2756 3059 2941 48 -291 -345 O ATOM 879 N LYS A 111 5.095 -11.439 -3.643 1.00 15.87 N ANISOU 879 N LYS A 111 1943 2214 1872 56 8 -610 N ATOM 880 CA LYS A 111 3.770 -10.812 -3.724 1.00 15.51 C ANISOU 880 CA LYS A 111 1901 2169 1825 55 13 -601 C ATOM 881 C LYS A 111 2.950 -11.621 -4.699 1.00 17.15 C ANISOU 881 C LYS A 111 2104 2378 2034 54 12 -599 C ATOM 882 O LYS A 111 3.453 -11.982 -5.765 1.00 17.36 O ANISOU 882 O LYS A 111 2126 2408 2062 51 11 -604 O ATOM 883 CB LYS A 111 3.807 -9.359 -4.249 1.00 18.43 C ANISOU 883 CB LYS A 111 2271 2542 2191 53 18 -600 C ATOM 884 CG LYS A 111 4.210 -8.276 -3.261 1.00 34.89 C ANISOU 884 CG LYS A 111 4359 4625 4273 54 21 -600 C ATOM 885 CD LYS A 111 3.409 -8.285 -1.961 1.00 46.85 C ANISOU 885 CD LYS A 111 5875 6136 5788 58 21 -594 C ATOM 886 CE LYS A 111 2.432 -7.157 -1.887 1.00 59.72 C ANISOU 886 CE LYS A 111 7507 7767 7417 57 25 -588 C ATOM 887 NZ LYS A 111 2.768 -6.193 -0.813 1.00 68.27 N ANISOU 887 NZ LYS A 111 8591 8850 8500 59 27 -588 N ATOM 888 N THR A 112 1.672 -11.829 -4.374 1.00 14.69 N ANISOU 888 N THR A 112 1795 2066 1722 55 14 -592 N ATOM 889 CA THR A 112 0.764 -12.538 -5.266 1.00 14.64 C ANISOU 889 CA THR A 112 1785 2061 1717 55 15 -590 C ATOM 890 C THR A 112 0.053 -11.522 -6.141 1.00 16.72 C ANISOU 890 C THR A 112 2048 2327 1978 53 19 -587 C ATOM 891 O THR A 112 0.007 -10.337 -5.798 1.00 16.88 O ANISOU 891 O THR A 112 2071 2346 1995 53 21 -585 O ATOM 892 CB THR A 112 -0.251 -13.360 -4.461 1.00 16.07 C ANISOU 892 CB THR A 112 1969 2239 1898 57 14 -586 C ATOM 893 OG1 THR A 112 -1.106 -12.467 -3.747 1.00 16.20 O ANISOU 893 OG1 THR A 112 1990 2254 1912 57 17 -582 O ATOM 894 CG2 THR A 112 0.412 -14.360 -3.500 1.00 16.52 C ANISOU 894 CG2 THR A 112 2028 2292 1957 58 9 -588 C ATOM 895 N MET A 113 -0.543 -11.978 -7.256 1.00 14.17 N ANISOU 895 N MET A 113 1721 2007 1656 52 20 -587 N ATOM 896 CA MET A 113 -1.335 -11.070 -8.096 1.00 12.62 C ANISOU 896 CA MET A 113 1525 1813 1457 52 23 -584 C ATOM 897 C MET A 113 -2.551 -10.583 -7.314 1.00 17.00 C ANISOU 897 C MET A 113 2085 2365 2010 55 25 -580 C ATOM 898 O MET A 113 -2.902 -9.409 -7.411 1.00 17.15 O ANISOU 898 O MET A 113 2106 2382 2026 55 26 -578 O ATOM 899 CB MET A 113 -1.777 -11.770 -9.372 1.00 13.99 C ANISOU 899 CB MET A 113 1693 1992 1633 50 24 -586 C ATOM 900 CG MET A 113 -0.637 -11.983 -10.312 1.00 15.89 C ANISOU 900 CG MET A 113 1928 2236 1874 45 23 -591 C ATOM 901 SD MET A 113 -1.186 -12.528 -11.942 1.00 18.12 S ANISOU 901 SD MET A 113 2201 2525 2157 43 25 -592 S ATOM 902 CE MET A 113 -1.195 -14.290 -11.703 1.00 15.28 C ANISOU 902 CE MET A 113 1833 2166 1805 45 23 -595 C ATOM 903 N LYS A 114 -3.141 -11.459 -6.476 1.00 14.72 N ANISOU 903 N LYS A 114 1796 2074 1722 57 25 -580 N ATOM 904 CA LYS A 114 -4.307 -11.090 -5.662 1.00 14.48 C ANISOU 904 CA LYS A 114 1769 2042 1690 58 26 -578 C ATOM 905 C LYS A 114 -3.988 -9.937 -4.706 1.00 17.72 C ANISOU 905 C LYS A 114 2184 2450 2099 58 26 -577 C ATOM 906 O LYS A 114 -4.841 -9.061 -4.500 1.00 18.59 O ANISOU 906 O LYS A 114 2295 2560 2208 58 26 -577 O ATOM 907 CB LYS A 114 -4.792 -12.291 -4.846 1.00 16.49 C ANISOU 907 CB LYS A 114 2025 2295 1945 58 26 -579 C ATOM 908 CG LYS A 114 -6.111 -12.002 -4.116 1.00 25.91 C ANISOU 908 CG LYS A 114 3221 3488 3136 58 28 -580 C ATOM 909 CD LYS A 114 -6.490 -13.111 -3.189 1.00 36.50 C ANISOU 909 CD LYS A 114 4564 4827 4475 56 29 -580 C ATOM 910 CE LYS A 114 -7.953 -13.068 -2.824 1.00 45.74 C ANISOU 910 CE LYS A 114 5736 5999 5643 55 32 -584 C ATOM 911 NZ LYS A 114 -8.359 -14.258 -2.029 1.00 51.75 N ANISOU 911 NZ LYS A 114 6501 6759 6402 52 33 -585 N ATOM 912 N SER A 115 -2.756 -9.927 -4.148 1.00 14.95 N ANISOU 912 N SER A 115 1834 2098 1749 57 24 -578 N ATOM 913 CA SER A 115 -2.346 -8.921 -3.166 1.00 14.86 C ANISOU 913 CA SER A 115 1825 2086 1737 57 24 -577 C ATOM 914 C SER A 115 -2.523 -7.484 -3.655 1.00 18.17 C ANISOU 914 C SER A 115 2245 2505 2155 57 25 -576 C ATOM 915 O SER A 115 -2.804 -6.591 -2.851 1.00 17.74 O ANISOU 915 O SER A 115 2190 2449 2100 57 26 -576 O ATOM 916 CB SER A 115 -0.906 -9.165 -2.725 1.00 18.33 C ANISOU 916 CB SER A 115 2264 2524 2177 57 22 -579 C ATOM 917 OG SER A 115 0.016 -8.719 -3.703 1.00 21.48 O ANISOU 917 OG SER A 115 2661 2924 2575 56 23 -582 O ATOM 918 N VAL A 116 -2.399 -7.266 -4.981 1.00 15.84 N ANISOU 918 N VAL A 116 1948 2211 1859 56 25 -576 N ATOM 919 CA VAL A 116 -2.518 -5.938 -5.590 1.00 16.83 C ANISOU 919 CA VAL A 116 2076 2336 1983 55 25 -575 C ATOM 920 C VAL A 116 -3.934 -5.336 -5.408 1.00 22.45 C ANISOU 920 C VAL A 116 2789 3047 2696 57 24 -574 C ATOM 921 O VAL A 116 -4.071 -4.116 -5.295 1.00 23.67 O ANISOU 921 O VAL A 116 2945 3199 2850 58 23 -573 O ATOM 922 CB VAL A 116 -2.035 -5.964 -7.068 1.00 19.75 C ANISOU 922 CB VAL A 116 2445 2707 2351 52 25 -575 C ATOM 923 CG1 VAL A 116 -2.011 -4.565 -7.677 1.00 20.22 C ANISOU 923 CG1 VAL A 116 2509 2766 2409 50 24 -573 C ATOM 924 CG2 VAL A 116 -0.649 -6.603 -7.171 1.00 18.97 C ANISOU 924 CG2 VAL A 116 2345 2611 2253 49 25 -579 C ATOM 925 N ASP A 117 -4.963 -6.190 -5.311 1.00 19.92 N ANISOU 925 N ASP A 117 2466 2726 2375 59 24 -575 N ATOM 926 CA ASP A 117 -6.347 -5.724 -5.143 1.00 21.11 C ANISOU 926 CA ASP A 117 2617 2876 2526 61 23 -577 C ATOM 927 C ASP A 117 -6.628 -5.074 -3.792 1.00 28.24 C ANISOU 927 C ASP A 117 3520 3778 3431 61 23 -579 C ATOM 928 O ASP A 117 -7.586 -4.306 -3.683 1.00 29.64 O ANISOU 928 O ASP A 117 3697 3955 3609 62 20 -581 O ATOM 929 CB ASP A 117 -7.337 -6.854 -5.421 1.00 22.98 C ANISOU 929 CB ASP A 117 2853 3116 2764 62 25 -580 C ATOM 930 CG ASP A 117 -7.484 -7.168 -6.897 1.00 37.12 C ANISOU 930 CG ASP A 117 4643 4908 4554 63 25 -579 C ATOM 931 OD1 ASP A 117 -7.039 -6.339 -7.733 1.00 37.22 O ANISOU 931 OD1 ASP A 117 4656 4919 4565 63 24 -577 O ATOM 932 OD2 ASP A 117 -8.077 -8.219 -7.221 1.00 45.36 O ANISOU 932 OD2 ASP A 117 5683 5954 5597 65 28 -581 O ATOM 933 N PHE A 118 -5.802 -5.376 -2.774 1.00 24.27 N ANISOU 933 N PHE A 118 3017 3276 2928 59 24 -578 N ATOM 934 CA PHE A 118 -5.960 -4.825 -1.417 1.00 23.80 C ANISOU 934 CA PHE A 118 2956 3217 2870 57 24 -579 C ATOM 935 C PHE A 118 -5.131 -3.578 -1.168 1.00 31.07 C ANISOU 935 C PHE A 118 3876 4137 3793 58 24 -578 C ATOM 936 O PHE A 118 -5.115 -3.072 -0.042 1.00 31.77 O ANISOU 936 O PHE A 118 3962 4226 3882 57 24 -579 O ATOM 937 CB PHE A 118 -5.636 -5.907 -0.379 1.00 24.38 C ANISOU 937 CB PHE A 118 3030 3291 2942 55 25 -579 C ATOM 938 CG PHE A 118 -6.447 -7.168 -0.562 1.00 24.34 C ANISOU 938 CG PHE A 118 3026 3287 2936 54 26 -581 C ATOM 939 CD1 PHE A 118 -7.838 -7.125 -0.595 1.00 25.64 C ANISOU 939 CD1 PHE A 118 3189 3452 3099 54 26 -585 C ATOM 940 CD2 PHE A 118 -5.825 -8.402 -0.689 1.00 25.53 C ANISOU 940 CD2 PHE A 118 3178 3437 3085 54 26 -579 C ATOM 941 CE1 PHE A 118 -8.589 -8.292 -0.774 1.00 25.75 C ANISOU 941 CE1 PHE A 118 3205 3468 3112 53 28 -588 C ATOM 942 CE2 PHE A 118 -6.580 -9.570 -0.856 1.00 27.27 C ANISOU 942 CE2 PHE A 118 3400 3658 3305 53 27 -580 C ATOM 943 CZ PHE A 118 -7.958 -9.508 -0.890 1.00 25.14 C ANISOU 943 CZ PHE A 118 3129 3390 3034 52 28 -585 C ATOM 944 N LEU A 119 -4.468 -3.069 -2.220 1.00 28.97 N ANISOU 944 N LEU A 119 3613 3869 3526 58 23 -576 N ATOM 945 CA LEU A 119 -3.599 -1.893 -2.186 1.00 32.47 C ANISOU 945 CA LEU A 119 4056 4311 3969 58 24 -574 C ATOM 946 C LEU A 119 -4.297 -0.620 -2.673 1.00 47.29 C ANISOU 946 C LEU A 119 5934 6185 5847 59 21 -574 C ATOM 947 O LEU A 119 -5.534 -0.553 -2.685 1.00 49.93 O ANISOU 947 O LEU A 119 6268 6519 6184 60 17 -576 O ATOM 948 CB LEU A 119 -2.382 -2.132 -3.074 1.00 32.65 C ANISOU 948 CB LEU A 119 4082 4334 3990 57 26 -573 C ATOM 949 CG LEU A 119 -1.358 -3.181 -2.695 1.00 37.28 C ANISOU 949 CG LEU A 119 4667 4922 4575 56 28 -575 C ATOM 950 CD1 LEU A 119 -0.204 -3.097 -3.656 1.00 37.29 C ANISOU 950 CD1 LEU A 119 4670 4924 4574 54 29 -576 C ATOM 951 CD2 LEU A 119 -0.829 -2.981 -1.279 1.00 39.60 C ANISOU 951 CD2 LEU A 119 4960 5217 4871 57 29 -576 C ATOM 952 OXT LEU A 119 -3.586 0.323 -3.099 1.00 71.61 O ANISOU 952 OXT LEU A 119 9017 9264 8927 58 21 -572 O TER 953 LEU A 119 HETATM 954 C1 EOL A 120 2.647 -10.674 -10.663 1.00 22.39 C HETATM 955 O1 EOL A 120 2.898 -13.159 -8.006 1.00 17.52 O HETATM 956 C2 EOL A 120 2.807 -11.494 -11.785 1.00 31.24 C HETATM 957 O2 EOL A 120 2.513 -10.499 -8.241 1.00 17.05 O HETATM 958 C3 EOL A 120 2.691 -11.242 -9.392 1.00 18.06 C HETATM 959 C4 EOL A 120 3.033 -12.859 -11.630 1.00 20.41 C HETATM 960 C5 EOL A 120 2.868 -12.610 -9.251 1.00 15.66 C HETATM 961 C6 EOL A 120 3.059 -13.427 -10.361 1.00 19.96 C HETATM 962 C7 EOL A 120 2.742 -10.915 -13.163 1.00 27.12 C HETATM 963 C8 EOL A 120 3.628 -9.766 -13.473 1.00 37.65 C HETATM 964 C9 EOL A 120 4.805 -9.630 -12.803 1.00 74.99 C HETATM 965 C10 EOL A 120 2.360 -9.130 -8.313 1.00 16.80 C HETATM 966 O HOH A 121 -12.949 -13.058 -10.494 1.00 43.68 O HETATM 967 O HOH A 122 2.775 -22.031 -5.090 1.00 35.38 O HETATM 968 O HOH A 123 -8.050 -13.740 -25.446 1.00 45.51 O HETATM 969 O HOH A 124 19.237 -16.168 -5.193 1.00 49.49 O HETATM 970 O HOH A 125 -1.403 -26.732 -6.072 1.00 51.25 O HETATM 971 O HOH A 126 7.687 0.582 -12.827 1.00 38.12 O HETATM 972 O HOH A 127 7.447 -22.724 -26.939 1.00 39.35 O HETATM 973 O HOH A 128 -5.770 -19.876 -2.850 1.00 32.59 O HETATM 974 O HOH A 129 15.751 -17.420 -17.748 1.00 32.58 O HETATM 975 O HOH A 130 14.258 -6.454 2.127 1.00 34.13 O HETATM 976 O HOH A 131 11.955 -28.821 -17.832 1.00 33.80 O HETATM 977 O HOH A 132 12.174 -30.771 -14.424 1.00 48.79 O HETATM 978 O HOH A 133 16.447 -27.928 -14.129 1.00 52.36 O HETATM 979 O HOH A 134 0.218 -6.083 -3.260 1.00 35.00 O HETATM 980 O HOH A 135 8.295 -24.330 -4.549 1.00 58.23 O HETATM 981 O HOH A 136 -7.877 -22.565 -25.436 1.00 48.70 O HETATM 982 O HOH A 137 20.046 -9.661 -2.484 1.00 51.02 O HETATM 983 O HOH A 138 2.873 -8.006 3.519 1.00 43.64 O HETATM 984 O HOH A 139 -9.760 -14.102 -13.789 1.00 28.38 O HETATM 985 O HOH A 140 -2.158 -12.993 -24.962 1.00 29.38 O HETATM 986 O HOH A 141 9.399 -3.970 -19.775 1.00 33.72 O HETATM 987 O HOH A 142 0.175 -14.721 -7.978 1.00 15.80 O HETATM 988 O HOH A 143 3.263 -13.447 -0.962 1.00 34.79 O HETATM 989 O HOH A 144 6.715 -0.353 -2.313 1.00 51.54 O HETATM 990 O HOH A 145 6.874 -16.353 0.878 1.00 43.48 O HETATM 991 O HOH A 146 -0.546 -1.053 -19.222 1.00 24.98 O HETATM 992 O HOH A 147 -11.495 -20.230 -23.571 1.00 28.60 O HETATM 993 O HOH A 148 11.627 -30.196 -11.905 1.00 58.80 O HETATM 994 O HOH A 149 3.029 -21.708 -25.703 1.00 25.27 O HETATM 995 O HOH A 150 -5.311 -25.163 -23.432 1.00 19.87 O HETATM 996 O HOH A 151 2.395 -29.408 -9.383 1.00 26.59 O HETATM 997 O HOH A 152 -2.623 -23.576 -9.567 1.00 20.36 O HETATM 998 O HOH A 153 -0.037 -4.815 1.573 1.00 32.81 O HETATM 999 O HOH A 154 15.653 -7.515 -18.680 1.00 35.17 O HETATM 1000 O HOH A 155 -7.215 -10.324 -8.449 1.00 30.24 O HETATM 1001 O HOH A 156 19.405 -9.097 -8.424 1.00 36.67 O HETATM 1002 O HOH A 157 17.503 -14.049 -17.050 1.00 34.31 O HETATM 1003 O HOH A 158 -9.161 -11.861 -12.621 1.00 25.96 O HETATM 1004 O HOH A 159 -4.794 -9.330 -9.437 1.00 20.59 O HETATM 1005 O HOH A 160 14.169 -8.738 0.944 1.00 42.55 O HETATM 1006 O HOH A 161 14.547 -5.980 -20.715 1.00 50.31 O HETATM 1007 O HOH A 162 4.188 -29.185 -20.123 1.00 19.22 O HETATM 1008 O HOH A 163 -8.034 -15.327 -14.956 1.00 23.77 O HETATM 1009 O HOH A 164 -8.425 -25.787 -15.824 1.00 24.69 O HETATM 1010 O HOH A 165 0.583 -19.591 -23.071 1.00 22.66 O HETATM 1011 O HOH A 166 20.851 -15.747 -9.738 1.00 22.44 O HETATM 1012 O HOH A 167 12.529 -1.785 -15.289 1.00 43.58 O HETATM 1013 O HOH A 168 14.860 -29.205 -15.956 1.00 42.41 O HETATM 1014 O HOH A 169 5.205 -4.770 -18.027 1.00 40.96 O HETATM 1015 O HOH A 170 -14.318 -22.447 -12.260 1.00 27.43 O HETATM 1016 O HOH A 171 10.458 -20.784 -6.146 1.00 44.70 O HETATM 1017 O HOH A 172 9.348 -22.001 -8.296 1.00 22.80 O HETATM 1018 O HOH A 173 3.785 -31.656 -19.188 1.00 28.04 O HETATM 1019 O HOH A 174 5.680 -27.458 -3.447 1.00 55.92 O HETATM 1020 O HOH A 175 -11.353 -25.281 -21.429 1.00 33.93 O HETATM 1021 O HOH A 176 -14.087 -21.315 -15.954 1.00 24.13 O HETATM 1022 O HOH A 177 -9.157 -19.916 -5.220 1.00 47.44 O HETATM 1023 O HOH A 178 10.350 -0.475 -4.755 1.00 39.38 O HETATM 1024 O HOH A 179 -2.207 -0.619 1.528 1.00 38.68 O HETATM 1025 O HOH A 180 17.615 -18.980 -4.794 1.00 54.33 O HETATM 1026 O HOH A 181 -16.274 -19.730 -15.646 1.00 31.09 O HETATM 1027 O HOH A 182 6.794 -21.115 -25.176 1.00 38.61 O HETATM 1028 O HOH A 183 1.277 -11.357 -1.327 1.00 27.83 O HETATM 1029 O HOH A 184 -6.228 -27.328 -15.202 1.00 28.29 O HETATM 1030 O HOH A 185 -1.064 -12.433 -27.882 1.00 62.97 O HETATM 1031 O HOH A 186 6.527 -14.173 3.793 1.00 56.71 O HETATM 1032 O HOH A 187 -14.979 -17.090 -15.562 1.00 30.98 O HETATM 1033 O HOH A 188 -11.628 -22.859 -23.977 1.00 37.08 O HETATM 1034 O HOH A 189 15.918 -22.823 -18.826 1.00 48.23 O HETATM 1035 O HOH A 190 -10.821 -28.891 -20.088 1.00 49.56 O HETATM 1036 O HOH A 191 4.927 -30.610 -16.421 1.00 34.25 O HETATM 1037 O HOH A 192 7.382 -30.369 -9.511 1.00 60.77 O HETATM 1038 O HOH A 193 3.820 -4.117 -20.316 1.00 19.71 O HETATM 1039 O HOH A 194 12.907 -23.095 -21.321 1.00 31.12 O HETATM 1040 O HOH A 195 -9.564 -16.679 -1.167 1.00 44.26 O HETATM 1041 O HOH A 196 -1.830 -31.105 -16.942 1.00 31.59 O HETATM 1042 O HOH A 197 2.976 -18.150 -2.828 1.00 53.39 O HETATM 1043 O HOH A 198 15.023 -18.213 -14.760 1.00 18.72 O HETATM 1044 O HOH A 199 10.594 -25.038 -5.001 1.00 60.41 O HETATM 1045 O HOH A 200 17.811 -14.217 -3.940 1.00 32.63 O HETATM 1046 O HOH A 201 5.182 -2.495 -16.746 1.00 56.96 O HETATM 1047 O HOH A 202 -10.523 -19.636 -27.623 1.00 55.29 O HETATM 1048 O HOH A 203 -6.531 -30.470 -5.113 1.00 57.40 O HETATM 1049 O HOH A 204 18.730 -7.794 -2.211 1.00 43.34 O HETATM 1050 O HOH A 205 -5.320 -6.683 -9.836 1.00 25.83 O HETATM 1051 O HOH A 206 -1.302 -20.003 -25.058 1.00 24.80 O HETATM 1052 O HOH A 207 4.069 -7.201 -23.758 1.00 23.81 O HETATM 1053 O HOH A 208 -7.143 -29.099 -13.339 1.00 52.66 O HETATM 1054 O HOH A 209 0.948 -16.833 -24.617 1.00 50.68 O HETATM 1055 O HOH A 210 -8.847 -25.471 -8.302 1.00 41.14 O HETATM 1056 O HOH A 211 -1.435 4.514 -7.248 1.00 60.93 O HETATM 1057 O HOH A 212 -10.198 -10.185 -14.814 1.00 26.83 O HETATM 1058 O HOH A 213 8.359 -26.104 -8.078 1.00 43.54 O HETATM 1059 O HOH A 214 1.434 -9.261 0.566 1.00 41.78 O HETATM 1060 O HOH A 215 -3.478 -21.649 -25.258 1.00 24.94 O HETATM 1061 O HOH A 216 5.566 -26.972 -6.365 1.00 28.95 O HETATM 1062 O HOH A 217 4.898 -19.677 -4.265 1.00 29.41 O HETATM 1063 O HOH A 218 4.800 -22.061 -27.648 1.00 31.76 O HETATM 1064 O HOH A 219 -10.230 -13.719 -10.432 1.00 29.73 O HETATM 1065 O HOH A 220 -11.926 -14.461 -19.044 1.00 33.60 O HETATM 1066 O HOH A 221 3.035 -27.372 -7.361 1.00 36.63 O HETATM 1067 O HOH A 222 5.461 -9.700 0.858 1.00 35.25 O HETATM 1068 O HOH A 223 9.026 -21.814 -4.109 1.00 53.79 O HETATM 1069 O HOH A 224 14.490 -20.766 -21.402 1.00 47.66 O HETATM 1070 O HOH A 225 6.174 -21.717 -2.867 1.00 43.03 O HETATM 1071 O HOH A 226 17.071 -16.451 -15.907 1.00 42.73 O HETATM 1072 O HOH A 227 11.351 -6.784 -19.883 1.00 31.97 O HETATM 1073 O HOH A 228 -11.012 -12.431 -22.575 1.00 45.50 O HETATM 1074 O HOH A 229 -12.065 -19.444 -6.503 1.00 37.62 O HETATM 1075 O HOH A 230 -1.899 8.264 -13.274 1.00 59.05 O HETATM 1076 O HOH A 231 20.570 -10.039 -4.890 1.00 54.87 O HETATM 1077 O HOH A 232 -7.856 -15.308 -6.726 1.00 33.03 O HETATM 1078 O HOH A 233 4.088 1.992 -5.328 1.00 44.69 O HETATM 1079 O HOH A 234 -11.323 -14.546 -16.198 1.00 33.38 O HETATM 1080 O HOH A 235 15.549 -3.150 -7.246 1.00 44.56 O HETATM 1081 O HOH A 236 10.536 -11.080 -26.671 1.00 44.32 O HETATM 1082 O HOH A 237 -10.894 -12.403 -15.428 1.00 44.22 O HETATM 1083 O HOH A 238 4.711 -9.295 -25.272 1.00 31.46 O HETATM 1084 O HOH A 239 -10.855 -13.236 -1.354 1.00 35.02 O HETATM 1085 O HOH A 240 7.172 -10.831 -24.146 1.00 37.04 O HETATM 1086 O HOH A 241 12.741 0.438 -1.409 1.00 37.29 O HETATM 1087 O HOH A 242 -6.057 -22.186 -3.729 1.00 35.11 O HETATM 1088 O HOH A 243 13.423 -20.709 -5.595 1.00 58.09 O HETATM 1089 O HOH A 244 -4.052 0.010 -16.586 1.00 31.78 O HETATM 1090 O HOH A 245 -1.782 0.978 -17.864 1.00 37.42 O HETATM 1091 O HOH A 246 -10.113 -26.455 -17.880 1.00 48.08 O HETATM 1092 O HOH A 247 13.539 -24.002 -23.794 1.00 53.23 O HETATM 1093 O HOH A 248 23.023 -14.916 -5.559 1.00 56.03 O HETATM 1094 O HOH A 249 18.786 0.004 1.572 1.00 52.37 O HETATM 1095 O HOH A 250 -9.168 -11.444 -9.776 1.00 48.72 O HETATM 1096 O HOH A 251 -4.348 -29.032 -17.585 1.00 28.66 O HETATM 1097 O HOH A 252 1.813 -30.194 -17.807 1.00 36.13 O HETATM 1098 O HOH A 253 14.506 -24.828 -12.235 1.00 46.00 O HETATM 1099 O HOH A 254 0.912 -14.185 -24.304 1.00 40.78 O HETATM 1100 O HOH A 255 18.676 -12.933 -14.943 1.00 40.11 O HETATM 1101 O HOH A 256 0.838 -28.811 -5.883 1.00 52.62 O HETATM 1102 O HOH A 257 -4.484 -25.372 -8.202 1.00 34.07 O HETATM 1103 O HOH A 258 10.766 -27.759 -25.409 1.00 52.51 O HETATM 1104 O HOH A 259 10.745 -31.122 -17.345 1.00 39.91 O CONECT 138 398 CONECT 398 138 CONECT 707 844 CONECT 844 707 CONECT 954 956 958 CONECT 955 960 CONECT 956 954 959 962 CONECT 957 958 965 CONECT 958 954 957 960 CONECT 959 956 961 CONECT 960 955 958 961 CONECT 961 959 960 CONECT 962 956 963 CONECT 963 962 964 CONECT 964 963 CONECT 965 957 MASTER 439 0 1 7 0 0 3 6 1094 1 16 10 END A second structure was input as follows:HEADER TRANSPORT PROTEIN 13-MAY-11 3S0A TITLE APIS MELLIFERA OBP14, NATIVE APO-PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: OBP14; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 18-135; COMPND 5 SYNONYM: ODORANT BINDING PROTEIN 14; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: APIS MELLIFERA; SOURCE 3 ORGANISM_COMMON: HONEYBEE; SOURCE 4 ORGANISM_TAXID: 7460; SOURCE 5 GENE: NP_001035313; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-5 B(+) KEYWDS ALL HELICAL PROTEIN, UNKNOWN ODORANT MOLECULES, ANTENNAE, TRANSPORT KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.SPINELLI,A.LAGARDE,I.IOVINELLA,M.TEGONI,P.PELOSI,C.CAMBILLAU REVDAT 2 11-JAN-12 3S0A 1 JRNL REVDAT 1 30-NOV-11 3S0A 0 JRNL AUTH S.SPINELLI,A.LAGARDE,I.IOVINELLA,P.LEGRAND,M.TEGONI, JRNL AUTH 2 P.PELOSI,C.CAMBILLAU JRNL TITL CRYSTAL STRUCTURE OF APIS MELLIFERA OBP14, A C-MINUS JRNL TITL 2 ODORANT-BINDING PROTEIN, AND ITS COMPLEXES WITH ODORANT JRNL TITL 3 MOLECULES. JRNL REF INSECT BIOCHEM.MOL.BIOL. V. 42 41 2012 JRNL REFN ISSN 0965-1748 JRNL PMID 22075131 JRNL DOI 10.1016/J.IBMB.2011.10.005 REMARK 2 REMARK 2 RESOLUTION. 1.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 36080 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) : 0.156 REMARK 3 R VALUE (WORKING SET) : 0.155 REMARK 3 FREE R VALUE : 0.178 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1900 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) : 1.15 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2290 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.17 REMARK 3 BIN R VALUE (WORKING SET) : 0.2780 REMARK 3 BIN FREE R VALUE SET COUNT : 128 REMARK 3 BIN FREE R VALUE : 0.3120 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 943 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 174 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 10.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.41 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.27000 REMARK 3 B22 (A**2) : -0.62000 REMARK 3 B33 (A**2) : 0.35000 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : -0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.039 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.142 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1025 ; 0.012 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 700 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1398 ; 1.481 ; 1.990 REMARK 3 BOND ANGLES OTHERS (DEGREES): 1772 ; 0.939 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 142 ; 5.165 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 43 ;39.520 ;27.907 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 228 ;11.282 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ;11.590 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 172 ; 0.091 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1114 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 159 ; 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): 633 ; 1.196 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 251 ; 0.385 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1053 ; 1.938 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 392 ; 3.043 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 332 ; 4.680 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1725 ; 1.132 ; 3.000 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 : 12 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 1 A 10 REMARK 3 ORIGIN FOR THE GROUP (A): 16.0760 3.6486 29.3747 REMARK 3 T TENSOR REMARK 3 T11: 0.0774 T22: 0.0085 REMARK 3 T33: 0.0100 T12: 0.0003 REMARK 3 T13: 0.0154 T23: -0.0037 REMARK 3 L TENSOR REMARK 3 L11: -0.3470 L22: 2.2944 REMARK 3 L33: 2.7862 L12: 0.6833 REMARK 3 L13: 0.8573 L23: 0.9768 REMARK 3 S TENSOR REMARK 3 S11: 0.0657 S12: 0.0239 S13: 0.0535 REMARK 3 S21: 0.2585 S22: -0.0641 S23: 0.0081 REMARK 3 S31: 0.2291 S32: -0.0502 S33: -0.0016 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 11 A 20 REMARK 3 ORIGIN FOR THE GROUP (A): 18.2693 16.6159 24.6320 REMARK 3 T TENSOR REMARK 3 T11: 0.0295 T22: 0.0265 REMARK 3 T33: 0.0278 T12: -0.0023 REMARK 3 T13: 0.0031 T23: 0.0066 REMARK 3 L TENSOR REMARK 3 L11: -0.0020 L22: 2.7770 REMARK 3 L33: 0.3918 L12: -0.3908 REMARK 3 L13: -0.0735 L23: -0.6290 REMARK 3 S TENSOR REMARK 3 S11: -0.0090 S12: 0.0082 S13: 0.0355 REMARK 3 S21: 0.0166 S22: 0.0151 S23: -0.0600 REMARK 3 S31: 0.0316 S32: 0.0454 S33: -0.0061 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 21 A 30 REMARK 3 ORIGIN FOR THE GROUP (A): 19.1875 25.1344 31.7697 REMARK 3 T TENSOR REMARK 3 T11: 0.0192 T22: 0.0266 REMARK 3 T33: 0.0364 T12: 0.0011 REMARK 3 T13: -0.0118 T23: 0.0038 REMARK 3 L TENSOR REMARK 3 L11: 0.1607 L22: 1.7587 REMARK 3 L33: 2.4276 L12: 0.6420 REMARK 3 L13: 0.1966 L23: -0.1157 REMARK 3 S TENSOR REMARK 3 S11: 0.0310 S12: 0.0043 S13: -0.0158 REMARK 3 S21: 0.0705 S22: -0.0402 S23: -0.1415 REMARK 3 S31: -0.0695 S32: 0.0876 S33: 0.0092 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 31 A 40 REMARK 3 ORIGIN FOR THE GROUP (A): 11.5744 24.2945 36.1154 REMARK 3 T TENSOR REMARK 3 T11: 0.0566 T22: 0.0219 REMARK 3 T33: 0.0579 T12: 0.0042 REMARK 3 T13: -0.0028 T23: -0.0142 REMARK 3 L TENSOR REMARK 3 L11: 0.8408 L22: 0.3201 REMARK 3 L33: 1.0361 L12: -0.1701 REMARK 3 L13: 0.9860 L23: -1.0043 REMARK 3 S TENSOR REMARK 3 S11: -0.0156 S12: -0.1472 S13: 0.1476 REMARK 3 S21: 0.1215 S22: 0.0034 S23: 0.0491 REMARK 3 S31: -0.0796 S32: 0.0050 S33: 0.0122 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 41 A 50 REMARK 3 ORIGIN FOR THE GROUP (A): 10.6784 24.3429 26.3656 REMARK 3 T TENSOR REMARK 3 T11: 0.0214 T22: 0.0225 REMARK 3 T33: 0.0454 T12: -0.0092 REMARK 3 T13: -0.0081 T23: 0.0264 REMARK 3 L TENSOR REMARK 3 L11: 1.4060 L22: 0.9172 REMARK 3 L33: 0.4988 L12: -0.0935 REMARK 3 L13: 0.3538 L23: 0.7148 REMARK 3 S TENSOR REMARK 3 S11: -0.0610 S12: 0.0391 S13: 0.0712 REMARK 3 S21: -0.0144 S22: 0.0547 S23: 0.0488 REMARK 3 S31: -0.0087 S32: 0.0235 S33: 0.0063 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 51 A 60 REMARK 3 ORIGIN FOR THE GROUP (A): 4.3997 15.0005 21.3281 REMARK 3 T TENSOR REMARK 3 T11: 0.0255 T22: 0.0038 REMARK 3 T33: 0.0749 T12: -0.0127 REMARK 3 T13: -0.0303 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 2.1937 L22: -0.3164 REMARK 3 L33: 1.9743 L12: 0.1999 REMARK 3 L13: 0.9796 L23: -0.4571 REMARK 3 S TENSOR REMARK 3 S11: 0.0067 S12: 0.0290 S13: -0.1629 REMARK 3 S21: -0.0674 S22: 0.0189 S23: 0.0262 REMARK 3 S31: 0.1007 S32: -0.0519 S33: -0.0256 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 61 A 70 REMARK 3 ORIGIN FOR THE GROUP (A): -1.1393 11.0066 27.0680 REMARK 3 T TENSOR REMARK 3 T11: 0.0405 T22: 0.0775 REMARK 3 T33: 0.0146 T12: -0.0413 REMARK 3 T13: -0.0079 T23: 0.0255 REMARK 3 L TENSOR REMARK 3 L11: 2.3598 L22: 3.4179 REMARK 3 L33: 4.1940 L12: 0.8691 REMARK 3 L13: 3.6595 L23: -2.2502 REMARK 3 S TENSOR REMARK 3 S11: 0.2216 S12: -0.3623 S13: 0.0800 REMARK 3 S21: -0.1807 S22: 0.1599 S23: 0.2098 REMARK 3 S31: 0.4486 S32: -0.5681 S33: -0.3814 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 71 A 80 REMARK 3 ORIGIN FOR THE GROUP (A): 3.8845 3.0878 37.3525 REMARK 3 T TENSOR REMARK 3 T11: 0.0494 T22: 0.0480 REMARK 3 T33: 0.0126 T12: -0.0233 REMARK 3 T13: 0.0192 T23: -0.0133 REMARK 3 L TENSOR REMARK 3 L11: 4.6201 L22: 0.5004 REMARK 3 L33: 1.8780 L12: 0.5827 REMARK 3 L13: -1.6413 L23: 0.0233 REMARK 3 S TENSOR REMARK 3 S11: -0.1759 S12: -0.0839 S13: -0.0687 REMARK 3 S21: -0.0684 S22: 0.1459 S23: -0.1023 REMARK 3 S31: 0.1498 S32: -0.0629 S33: 0.0300 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 81 A 90 REMARK 3 ORIGIN FOR THE GROUP (A): -3.5470 10.9796 37.3931 REMARK 3 T TENSOR REMARK 3 T11: 0.0185 T22: 0.0437 REMARK 3 T33: 0.0370 T12: -0.0031 REMARK 3 T13: 0.0020 T23: 0.0235 REMARK 3 L TENSOR REMARK 3 L11: -0.5537 L22: 3.9922 REMARK 3 L33: 2.0320 L12: -0.4567 REMARK 3 L13: 0.5005 L23: -2.1334 REMARK 3 S TENSOR REMARK 3 S11: -0.0001 S12: -0.0392 S13: 0.0671 REMARK 3 S21: -0.0821 S22: 0.0504 S23: 0.0872 REMARK 3 S31: 0.0884 S32: -0.1081 S33: -0.0503 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 91 A 100 REMARK 3 ORIGIN FOR THE GROUP (A): -1.1501 25.5966 29.0126 REMARK 3 T TENSOR REMARK 3 T11: 0.0210 T22: 0.0400 REMARK 3 T33: 0.0852 T12: 0.0085 REMARK 3 T13: -0.0174 T23: 0.0516 REMARK 3 L TENSOR REMARK 3 L11: 1.0873 L22: 0.4444 REMARK 3 L33: 1.7911 L12: 0.5537 REMARK 3 L13: -0.5580 L23: -0.4601 REMARK 3 S TENSOR REMARK 3 S11: 0.0321 S12: 0.0006 S13: 0.0563 REMARK 3 S21: -0.0929 S22: 0.0559 S23: 0.1479 REMARK 3 S31: 0.0184 S32: -0.1324 S33: -0.0880 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 101 A 109 REMARK 3 ORIGIN FOR THE GROUP (A): 4.4710 19.2953 36.9108 REMARK 3 T TENSOR REMARK 3 T11: 0.0180 T22: 0.0310 REMARK 3 T33: 0.0409 T12: -0.0049 REMARK 3 T13: 0.0152 T23: 0.0217 REMARK 3 L TENSOR REMARK 3 L11: -0.3429 L22: 2.0393 REMARK 3 L33: 3.2317 L12: 0.0243 REMARK 3 L13: 0.0968 L23: -1.0686 REMARK 3 S TENSOR REMARK 3 S11: 0.0262 S12: -0.0174 S13: 0.0632 REMARK 3 S21: 0.0668 S22: -0.0360 S23: 0.0813 REMARK 3 S31: 0.0515 S32: -0.0630 S33: 0.0098 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 110 A 119 REMARK 3 ORIGIN FOR THE GROUP (A): 14.3636 10.0182 38.8647 REMARK 3 T TENSOR REMARK 3 T11: 0.0650 T22: 0.0308 REMARK 3 T33: 0.0051 T12: 0.0142 REMARK 3 T13: -0.0093 T23: 0.0139 REMARK 3 L TENSOR REMARK 3 L11: 0.5462 L22: 0.6778 REMARK 3 L33: 0.3442 L12: -0.2646 REMARK 3 L13: 0.6123 L23: -0.2323 REMARK 3 S TENSOR REMARK 3 S11: 0.0337 S12: 0.0096 S13: -0.0190 REMARK 3 S21: -0.0090 S22: -0.0139 S23: 0.0040 REMARK 3 S31: 0.0844 S32: 0.0278 S33: -0.0198 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : RESIDUAL ONLY REMARK 4 REMARK 4 3S0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11. REMARK 100 THE RCSB ID CODE IS RCSB065598. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-FEB-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8265 REMARK 200 MONOCHROMATOR : MIRRORS REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37980 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150 REMARK 200 RESOLUTION RANGE LOW (A) : 45.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.04500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.50000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3RZS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 37.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8-1.9 M TRI-SODIUM CITRATE, 25 MM REMARK 280 CHES, PH 9.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 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 16.20500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.19000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.99500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.19000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.20500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 18.99500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 210 O HOH A 246 1.67 REMARK 500 O HOH A 172 O HOH A 173 1.91 REMARK 500 O HOH A 144 O HOH A 146 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 126 DISTANCE = 6.00 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3RZS RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH TA6BR14 REMARK 900 RELATED ID: 3S0B RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE FLUORESCENT PROBE REMARK 900 1-N-PHENYLNAPHTHYLAMINE REMARK 900 RELATED ID: 3S0D RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP 14 IN COMPLEX WITH THE CITRUS ODORANT REMARK 900 CITRALVA REMARK 900 RELATED ID: 3S0E RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14 IN COMPLEX WITH THE ODORANT EUGENOL REMARK 900 RELATED ID: 3S0F RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP14, NATIVE APO, CRYSTAL FORM 2 REMARK 900 RELATED ID: 3S0G RELATED DB: PDB REMARK 900 APIS MELLIFERA OBP 14 DOUBLE MUTANT GLN44CYS, HIS97CYS DBREF 3S0A A 2 119 UNP Q1W640 Q1W640_APIME 18 135 SEQADV 3S0A MET A 1 UNP Q1W640 INITIATING METHIONINE SEQRES 1 A 119 MET THR ILE GLU GLU LEU LYS THR ARG LEU HIS THR GLU SEQRES 2 A 119 GLN SER VAL CYS LYS THR GLU THR GLY ILE ASP GLN GLN SEQRES 3 A 119 LYS ALA ASN ASP VAL ILE GLU GLY ASN ILE ASP VAL GLU SEQRES 4 A 119 ASP LYS LYS VAL GLN LEU TYR CYS GLU CYS ILE LEU LYS SEQRES 5 A 119 ASN PHE ASN ILE LEU ASP LYS ASN ASN VAL PHE LYS PRO SEQRES 6 A 119 GLN GLY ILE LYS ALA VAL MET GLU LEU LEU ILE ASP GLU SEQRES 7 A 119 ASN SER VAL LYS GLN LEU VAL SER ASP CYS SER THR ILE SEQRES 8 A 119 SER GLU GLU ASN PRO HIS LEU LYS ALA SER LYS LEU VAL SEQRES 9 A 119 GLN CYS VAL SER LYS TYR LYS THR MET LYS SER VAL ASP SEQRES 10 A 119 PHE LEU FORMUL 2 HOH *174(H2 O) HELIX 1 1 THR A 2 GLY A 22 1 21 HELIX 2 2 ASP A 24 GLU A 33 1 10 HELIX 3 3 ASP A 40 PHE A 54 1 15 HELIX 4 4 LYS A 64 GLU A 73 1 10 HELIX 5 5 ASP A 77 SER A 89 1 13 HELIX 6 6 ASN A 95 LYS A 109 1 15 HELIX 7 7 THR A 112 ASP A 117 1 6 SSBOND 1 CYS A 17 CYS A 49 1555 1555 2.06 SSBOND 2 CYS A 88 CYS A 106 1555 1555 2.02 CRYST1 32.410 37.990 86.380 90.00 90.00 90.00 P 21 21 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 0.030855 0.000000 0.000000 0.00000 SCALE2 0.000000 0.026323 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011577 0.00000 ATOM 1 N MET A 1 10.739 -2.256 28.043 1.00 17.55 N ANISOU 1 N MET A 1 2181 2106 2378 -99 -83 37 N ATOM 2 CA AMET A 1 11.812 -1.226 28.089 0.50 16.67 C ANISOU 2 CA AMET A 1 2105 2093 2136 -51 -54 29 C ATOM 3 CA BMET A 1 11.809 -1.229 28.100 0.50 16.03 C ANISOU 3 CA BMET A 1 2041 1999 2049 -71 -44 53 C ATOM 4 C MET A 1 12.429 -1.301 29.462 1.00 15.02 C ANISOU 4 C MET A 1 1934 1888 1884 -58 -34 -6 C ATOM 5 O MET A 1 11.738 -1.135 30.470 1.00 16.30 O ANISOU 5 O MET A 1 2023 2174 1995 -57 27 226 O ATOM 6 CB AMET A 1 11.269 0.179 27.825 0.50 17.46 C ANISOU 6 CB AMET A 1 2205 2193 2233 21 -63 -28 C ATOM 7 CB BMET A 1 11.242 0.159 27.884 0.50 16.44 C ANISOU 7 CB BMET A 1 2086 2046 2112 -40 -42 11 C ATOM 8 CG AMET A 1 12.338 1.144 27.334 0.50 18.68 C ANISOU 8 CG AMET A 1 2269 2366 2462 49 -54 -64 C ATOM 9 CG BMET A 1 12.258 1.260 28.084 0.50 15.37 C ANISOU 9 CG BMET A 1 2000 1865 1975 -92 -8 100 C ATOM 10 SD AMET A 1 12.123 2.876 27.781 0.50 20.24 S ANISOU 10 SD AMET A 1 2409 2596 2684 140 -252 -283 S ATOM 11 SD BMET A 1 11.502 2.852 27.794 0.50 17.86 S ANISOU 11 SD BMET A 1 2014 1949 2823 -241 51 174 S ATOM 12 CE AMET A 1 10.963 3.457 26.556 0.50 15.74 C ANISOU 12 CE AMET A 1 2111 2495 1374 9 271 -370 C ATOM 13 CE BMET A 1 12.782 3.704 26.900 0.50 13.71 C ANISOU 13 CE BMET A 1 2044 1503 1661 -857 -436 385 C ATOM 14 N THR A 2 13.719 -1.566 29.502 1.00 11.92 N ANISOU 14 N THR A 2 1724 1402 1400 -229 6 63 N ATOM 15 CA THR A 2 14.361 -1.752 30.776 1.00 10.56 C ANISOU 15 CA THR A 2 1554 1257 1199 -237 -7 78 C ATOM 16 C THR A 2 14.629 -0.369 31.397 1.00 9.90 C ANISOU 16 C THR A 2 1482 1149 1128 -200 46 60 C ATOM 17 O THR A 2 14.598 0.692 30.730 1.00 10.06 O ANISOU 17 O THR A 2 1520 1224 1077 -311 -59 78 O ATOM 18 CB THR A 2 15.678 -2.499 30.635 1.00 10.62 C ANISOU 18 CB THR A 2 1631 1210 1193 -243 67 118 C ATOM 19 OG1 THR A 2 16.608 -1.663 29.938 1.00 11.16 O ANISOU 19 OG1 THR A 2 1611 1190 1440 -191 70 216 O ATOM 20 CG2 THR A 2 15.487 -3.840 29.902 1.00 11.58 C ANISOU 20 CG2 THR A 2 1726 1238 1434 -320 95 45 C ATOM 21 N ILE A 3 14.910 -0.366 32.695 1.00 9.78 N ANISOU 21 N ILE A 3 1459 1117 1140 -201 29 110 N ATOM 22 CA AILE A 3 15.268 0.875 33.370 0.50 9.85 C ANISOU 22 CA AILE A 3 1436 1242 1063 -103 41 54 C ATOM 23 CA BILE A 3 15.262 0.869 33.367 0.50 9.89 C ANISOU 23 CA BILE A 3 1421 1240 1095 -99 33 67 C ATOM 24 C ILE A 3 16.509 1.477 32.728 1.00 9.69 C ANISOU 24 C ILE A 3 1419 1192 1069 -31 16 94 C ATOM 25 O ILE A 3 16.580 2.694 32.558 1.00 9.12 O ANISOU 25 O ILE A 3 1502 962 1001 -78 -3 106 O ATOM 26 CB AILE A 3 15.520 0.641 34.869 0.50 10.19 C ANISOU 26 CB AILE A 3 1459 1348 1064 -78 36 102 C ATOM 27 CB BILE A 3 15.438 0.621 34.882 0.50 10.16 C ANISOU 27 CB BILE A 3 1428 1336 1095 -87 27 119 C ATOM 28 CG1AILE A 3 14.215 0.332 35.608 0.50 11.33 C ANISOU 28 CG1AILE A 3 1523 1580 1203 -64 154 14 C ATOM 29 CG1BILE A 3 15.628 1.944 35.618 0.50 10.50 C ANISOU 29 CG1BILE A 3 1363 1442 1181 -151 -82 16 C ATOM 30 CG2AILE A 3 16.174 1.854 35.490 0.50 10.07 C ANISOU 30 CG2AILE A 3 1482 1391 951 -133 -21 56 C ATOM 31 CG2BILE A 3 16.587 -0.358 35.166 0.50 11.72 C ANISOU 31 CG2BILE A 3 1525 1550 1376 31 95 165 C ATOM 32 CD1AILE A 3 13.148 1.341 35.418 0.50 11.60 C ANISOU 32 CD1AILE A 3 1478 2063 866 94 87 60 C ATOM 33 CD1BILE A 3 14.482 2.855 35.434 0.50 12.40 C ANISOU 33 CD1BILE A 3 1525 1745 1441 39 -173 -10 C ATOM 34 N GLU A 4 17.472 0.633 32.347 1.00 10.49 N ANISOU 34 N GLU A 4 1555 1216 1212 40 -12 73 N ATOM 35 CA GLU A 4 18.694 1.153 31.739 1.00 11.41 C ANISOU 35 CA GLU A 4 1539 1325 1471 140 5 94 C ATOM 36 C GLU A 4 18.374 1.768 30.372 1.00 9.90 C ANISOU 36 C GLU A 4 1413 1133 1213 61 73 16 C ATOM 37 O GLU A 4 18.937 2.794 30.027 1.00 9.81 O ANISOU 37 O GLU A 4 1150 1190 1388 58 46 68 O ATOM 38 CB GLU A 4 19.806 0.089 31.655 1.00 13.15 C ANISOU 38 CB GLU A 4 1704 1501 1789 173 55 83 C ATOM 39 CG GLU A 4 20.461 -0.248 33.001 1.00 18.12 C ANISOU 39 CG GLU A 4 2134 2426 2324 282 -102 213 C ATOM 40 CD GLU A 4 21.154 0.926 33.682 1.00 22.89 C ANISOU 40 CD GLU A 4 2815 3020 2859 197 -122 123 C ATOM 41 OE1 GLU A 4 21.982 1.620 33.045 1.00 26.46 O ANISOU 41 OE1 GLU A 4 3053 3646 3354 84 -14 279 O ATOM 42 OE2 GLU A 4 20.888 1.141 34.890 1.00 26.76 O ANISOU 42 OE2 GLU A 4 3354 3793 3017 246 -34 -63 O ATOM 43 N GLU A 5 17.460 1.159 29.615 1.00 8.48 N ANISOU 43 N GLU A 5 1252 884 1083 66 125 88 N ATOM 44 CA GLU A 5 17.039 1.755 28.346 1.00 8.15 C ANISOU 44 CA GLU A 5 1225 934 937 4 93 -28 C ATOM 45 C GLU A 5 16.325 3.086 28.540 1.00 6.89 C ANISOU 45 C GLU A 5 1058 774 785 -3 140 -24 C ATOM 46 O GLU A 5 16.540 4.006 27.756 1.00 7.27 O ANISOU 46 O GLU A 5 1198 753 809 -23 159 45 O ATOM 47 CB GLU A 5 16.181 0.780 27.567 1.00 8.65 C ANISOU 47 CB GLU A 5 1272 890 1123 -64 79 -28 C ATOM 48 CG GLU A 5 17.005 -0.382 26.983 1.00 10.42 C ANISOU 48 CG GLU A 5 1707 985 1265 -54 239 -127 C ATOM 49 CD GLU A 5 16.210 -1.615 26.661 1.00 11.47 C ANISOU 49 CD GLU A 5 1949 936 1470 18 223 -193 C ATOM 50 OE1 GLU A 5 14.965 -1.641 26.835 1.00 12.08 O ANISOU 50 OE1 GLU A 5 2063 1187 1337 -343 60 -159 O ATOM 51 OE2 GLU A 5 16.865 -2.557 26.181 1.00 17.89 O ANISOU 51 OE2 GLU A 5 2822 1347 2626 16 537 -516 O ATOM 52 N LEU A 6 15.483 3.189 29.566 1.00 6.69 N ANISOU 52 N LEU A 6 931 712 896 -98 119 84 N ATOM 53 CA LEU A 6 14.810 4.448 29.855 1.00 6.72 C ANISOU 53 CA LEU A 6 908 812 834 -75 71 64 C ATOM 54 C LEU A 6 15.806 5.513 30.263 1.00 6.01 C ANISOU 54 C LEU A 6 805 768 707 7 60 -25 C ATOM 55 O LEU A 6 15.682 6.654 29.821 1.00 6.23 O ANISOU 55 O LEU A 6 897 712 759 1 52 -59 O ATOM 56 CB LEU A 6 13.721 4.268 30.925 1.00 7.29 C ANISOU 56 CB LEU A 6 958 1003 806 -76 121 102 C ATOM 57 CG LEU A 6 13.011 5.563 31.347 1.00 8.69 C ANISOU 57 CG LEU A 6 1009 1220 1072 -77 149 43 C ATOM 58 CD1 LEU A 6 12.227 6.165 30.192 1.00 9.79 C ANISOU 58 CD1 LEU A 6 1102 1262 1353 48 78 34 C ATOM 59 CD2 LEU A 6 12.088 5.282 32.531 1.00 9.71 C ANISOU 59 CD2 LEU A 6 858 1593 1236 -112 77 -133 C ATOM 60 N LYS A 7 16.797 5.164 31.092 1.00 6.69 N ANISOU 60 N LYS A 7 978 733 829 22 -43 100 N ATOM 61 CA LYS A 7 17.814 6.133 31.454 1.00 7.03 C ANISOU 61 CA LYS A 7 944 848 878 60 -45 28 C ATOM 62 C LYS A 7 18.461 6.703 30.204 1.00 6.75 C ANISOU 62 C LYS A 7 943 795 824 -15 -19 46 C ATOM 63 O LYS A 7 18.680 7.897 30.094 1.00 7.15 O ANISOU 63 O LYS A 7 1014 843 860 80 -34 62 O ATOM 64 CB LYS A 7 18.904 5.494 32.319 1.00 7.63 C ANISOU 64 CB LYS A 7 991 1038 869 124 -118 74 C ATOM 65 CG LYS A 7 18.531 5.159 33.730 1.00 9.63 C ANISOU 65 CG LYS A 7 1315 1241 1100 190 -222 101 C ATOM 66 CD LYS A 7 19.735 4.544 34.454 1.00 13.92 C ANISOU 66 CD LYS A 7 1619 1932 1737 295 -241 153 C ATOM 67 CE LYS A 7 19.362 3.834 35.748 1.00 15.59 C ANISOU 67 CE LYS A 7 1685 2185 2051 327 -111 294 C ATOM 68 NZ LYS A 7 20.592 3.258 36.357 1.00 18.68 N ANISOU 68 NZ LYS A 7 1731 2666 2701 578 -213 506 N ATOM 69 N THR A 8 18.837 5.812 29.289 1.00 6.75 N ANISOU 69 N THR A 8 949 771 845 41 -114 51 N ATOM 70 CA THR A 8 19.507 6.189 28.065 1.00 7.00 C ANISOU 70 CA THR A 8 843 848 967 145 2 11 C ATOM 71 C THR A 8 18.609 7.051 27.169 1.00 5.96 C ANISOU 71 C THR A 8 774 671 817 -1 42 -72 C ATOM 72 O THR A 8 19.059 8.063 26.636 1.00 6.34 O ANISOU 72 O THR A 8 775 755 879 14 -10 39 O ATOM 73 CB THR A 8 19.991 4.914 27.359 1.00 8.06 C ANISOU 73 CB THR A 8 890 997 1173 201 32 58 C ATOM 74 OG1 THR A 8 20.852 4.182 28.234 1.00 10.49 O ANISOU 74 OG1 THR A 8 1356 1331 1296 509 -67 21 O ATOM 75 CG2 THR A 8 20.742 5.255 26.109 1.00 9.54 C ANISOU 75 CG2 THR A 8 1047 1233 1345 237 112 98 C ATOM 76 N ARG A 9 17.355 6.635 27.019 1.00 4.68 N ANISOU 76 N ARG A 9 634 503 638 -5 72 -34 N ATOM 77 CA ARG A 9 16.415 7.390 26.219 1.00 5.09 C ANISOU 77 CA ARG A 9 666 613 654 -6 80 22 C ATOM 78 C ARG A 9 16.231 8.790 26.765 1.00 4.34 C ANISOU 78 C ARG A 9 609 595 444 44 -6 -46 C ATOM 79 O ARG A 9 16.161 9.760 26.011 1.00 4.63 O ANISOU 79 O ARG A 9 588 641 530 21 -6 2 O ATOM 80 CB ARG A 9 15.086 6.643 26.164 1.00 5.43 C ANISOU 80 CB ARG A 9 748 620 695 -30 57 22 C ATOM 81 CG ARG A 9 13.939 7.355 25.469 1.00 4.92 C ANISOU 81 CG ARG A 9 664 583 620 -110 109 -10 C ATOM 82 CD ARG A 9 14.145 7.507 23.978 1.00 5.43 C ANISOU 82 CD ARG A 9 671 676 716 31 91 -101 C ATOM 83 NE ARG A 9 13.036 8.216 23.359 1.00 5.25 N ANISOU 83 NE ARG A 9 587 712 695 -21 100 -90 N ATOM 84 CZ ARG A 9 11.864 7.681 23.068 1.00 6.09 C ANISOU 84 CZ ARG A 9 533 707 1074 79 219 0 C ATOM 85 NH1 ARG A 9 11.627 6.400 23.252 1.00 7.97 N ANISOU 85 NH1 ARG A 9 596 885 1544 71 -68 24 N ATOM 86 NH2 ARG A 9 10.912 8.441 22.553 1.00 7.53 N ANISOU 86 NH2 ARG A 9 728 884 1248 63 -103 -30 N ATOM 87 N LEU A 10 16.119 8.906 28.076 1.00 4.67 N ANISOU 87 N LEU A 10 656 591 527 -29 8 49 N ATOM 88 CA LEU A 10 15.990 10.222 28.701 1.00 4.61 C ANISOU 88 CA LEU A 10 618 622 512 7 -55 -52 C ATOM 89 C LEU A 10 17.199 11.098 28.402 1.00 4.57 C ANISOU 89 C LEU A 10 597 679 459 20 -80 -77 C ATOM 90 O LEU A 10 17.041 12.244 28.056 1.00 4.46 O ANISOU 90 O LEU A 10 549 638 506 22 19 -36 O ATOM 91 CB LEU A 10 15.762 10.091 30.205 1.00 5.53 C ANISOU 91 CB LEU A 10 702 790 610 -15 12 -57 C ATOM 92 CG LEU A 10 14.373 9.665 30.647 1.00 6.11 C ANISOU 92 CG LEU A 10 857 834 630 -22 58 -92 C ATOM 93 CD1 LEU A 10 14.407 9.263 32.106 1.00 7.71 C ANISOU 93 CD1 LEU A 10 1069 1262 596 -247 282 8 C ATOM 94 CD2 LEU A 10 13.360 10.767 30.402 1.00 8.40 C ANISOU 94 CD2 LEU A 10 949 1268 975 83 145 81 C ATOM 95 N HIS A 11 18.397 10.548 28.540 1.00 4.41 N ANISOU 95 N HIS A 11 683 484 506 59 -53 28 N ATOM 96 CA HIS A 11 19.568 11.324 28.230 1.00 5.03 C ANISOU 96 CA HIS A 11 739 614 555 -34 -81 -92 C ATOM 97 C HIS A 11 19.559 11.783 26.768 1.00 4.83 C ANISOU 97 C HIS A 11 660 597 576 111 -109 -81 C ATOM 98 O HIS A 11 19.933 12.909 26.484 1.00 4.97 O ANISOU 98 O HIS A 11 606 654 626 -29 1 -27 O ATOM 99 CB HIS A 11 20.842 10.529 28.511 1.00 6.07 C ANISOU 99 CB HIS A 11 850 718 737 -28 27 -86 C ATOM 100 CG HIS A 11 21.131 10.292 29.961 1.00 9.55 C ANISOU 100 CG HIS A 11 1124 1296 1207 37 80 89 C ATOM 101 ND1 HIS A 11 20.613 11.011 31.025 1.00 12.40 N ANISOU 101 ND1 HIS A 11 1555 1885 1268 80 -311 413 N ATOM 102 CD2 HIS A 11 21.977 9.390 30.496 1.00 9.95 C ANISOU 102 CD2 HIS A 11 1050 1332 1396 348 88 268 C ATOM 103 CE1 HIS A 11 21.113 10.526 32.150 1.00 10.20 C ANISOU 103 CE1 HIS A 11 1323 1640 911 272 84 81 C ATOM 104 NE2 HIS A 11 21.948 9.550 31.856 1.00 14.46 N ANISOU 104 NE2 HIS A 11 1847 2148 1497 231 -47 190 N ATOM 105 N THR A 12 19.154 10.906 25.853 1.00 4.62 N ANISOU 105 N THR A 12 599 555 601 6 68 -55 N ATOM 106 CA THR A 12 19.084 11.238 24.456 1.00 4.54 C ANISOU 106 CA THR A 12 585 586 551 46 19 -56 C ATOM 107 C THR A 12 18.101 12.361 24.195 1.00 4.61 C ANISOU 107 C THR A 12 635 507 610 34 70 -77 C ATOM 108 O THR A 12 18.427 13.315 23.489 1.00 4.63 O ANISOU 108 O THR A 12 575 579 605 28 87 -21 O ATOM 109 CB THR A 12 18.792 9.988 23.613 1.00 4.50 C ANISOU 109 CB THR A 12 512 594 601 111 76 -43 C ATOM 110 OG1 THR A 12 19.966 9.181 23.695 1.00 5.26 O ANISOU 110 OG1 THR A 12 580 714 702 95 -17 -167 O ATOM 111 CG2 THR A 12 18.501 10.330 22.163 1.00 5.70 C ANISOU 111 CG2 THR A 12 763 836 565 -40 -54 -121 C ATOM 112 N GLU A 13 16.897 12.260 24.748 1.00 3.91 N ANISOU 112 N GLU A 13 572 442 470 20 80 21 N ATOM 113 CA GLU A 13 15.910 13.286 24.519 1.00 3.81 C ANISOU 113 CA GLU A 13 513 499 433 30 36 -69 C ATOM 114 C GLU A 13 16.293 14.593 25.176 1.00 3.94 C ANISOU 114 C GLU A 13 515 452 528 18 34 -41 C ATOM 115 O GLU A 13 16.024 15.665 24.630 1.00 4.60 O ANISOU 115 O GLU A 13 670 498 577 20 21 -31 O ATOM 116 CB GLU A 13 14.498 12.844 24.935 1.00 4.44 C ANISOU 116 CB GLU A 13 575 585 525 -6 83 -65 C ATOM 117 CG GLU A 13 13.964 11.600 24.241 1.00 5.24 C ANISOU 117 CG GLU A 13 636 632 721 -63 -23 27 C ATOM 118 CD GLU A 13 13.798 11.660 22.722 1.00 5.09 C ANISOU 118 CD GLU A 13 524 628 781 1 54 -45 C ATOM 119 OE1 GLU A 13 14.244 12.636 22.083 1.00 6.57 O ANISOU 119 OE1 GLU A 13 784 947 765 -193 8 -50 O ATOM 120 OE2 GLU A 13 13.204 10.684 22.212 1.00 6.34 O ANISOU 120 OE2 GLU A 13 776 812 821 -38 -24 -57 O ATOM 121 N GLN A 14 16.885 14.538 26.365 1.00 3.52 N ANISOU 121 N GLN A 14 507 364 464 -10 24 -30 N ATOM 122 CA GLN A 14 17.410 15.726 27.001 1.00 4.08 C ANISOU 122 CA GLN A 14 624 397 525 8 -17 -31 C ATOM 123 C GLN A 14 18.412 16.421 26.100 1.00 4.76 C ANISOU 123 C GLN A 14 636 523 650 8 -19 -22 C ATOM 124 O GLN A 14 18.410 17.645 25.970 1.00 5.29 O ANISOU 124 O GLN A 14 734 566 707 -54 38 12 O ATOM 125 CB GLN A 14 18.047 15.337 28.328 1.00 4.32 C ANISOU 125 CB GLN A 14 638 430 573 -8 -88 -113 C ATOM 126 CG GLN A 14 17.025 15.000 29.398 1.00 4.25 C ANISOU 126 CG GLN A 14 596 578 438 -30 -135 -114 C ATOM 127 CD GLN A 14 17.564 14.126 30.516 1.00 5.00 C ANISOU 127 CD GLN A 14 737 637 524 -76 -22 -156 C ATOM 128 OE1 GLN A 14 18.751 13.880 30.591 1.00 6.52 O ANISOU 128 OE1 GLN A 14 887 986 603 203 12 -27 O ATOM 129 NE2 GLN A 14 16.682 13.646 31.369 1.00 5.63 N ANISOU 129 NE2 GLN A 14 863 639 637 -58 37 -107 N ATOM 130 N SER A 15 19.285 15.647 25.468 1.00 5.08 N ANISOU 130 N SER A 15 633 600 696 -13 -6 3 N ATOM 131 CA ASER A 15 20.296 16.215 24.583 0.50 5.36 C ANISOU 131 CA ASER A 15 654 730 649 -52 22 23 C ATOM 132 CA BSER A 15 20.298 16.223 24.595 0.50 5.92 C ANISOU 132 CA BSER A 15 727 802 719 -42 5 13 C ATOM 133 C SER A 15 19.684 16.870 23.355 1.00 5.28 C ANISOU 133 C SER A 15 682 645 679 -92 81 24 C ATOM 134 O SER A 15 20.001 18.012 23.039 1.00 5.74 O ANISOU 134 O SER A 15 780 669 732 -42 14 31 O ATOM 135 CB ASER A 15 21.281 15.137 24.142 0.50 5.91 C ANISOU 135 CB ASER A 15 666 845 732 -56 46 111 C ATOM 136 CB BSER A 15 21.321 15.149 24.221 0.50 6.74 C ANISOU 136 CB BSER A 15 776 949 836 -36 45 73 C ATOM 137 OG ASER A 15 22.165 15.673 23.174 0.50 6.76 O ANISOU 137 OG ASER A 15 723 1000 846 -6 242 250 O ATOM 138 OG BSER A 15 22.015 14.704 25.378 0.50 11.01 O ANISOU 138 OG BSER A 15 1284 1613 1287 84 -24 139 O ATOM 139 N VAL A 16 18.805 16.149 22.663 1.00 4.91 N ANISOU 139 N VAL A 16 637 559 666 -39 53 -37 N ATOM 140 CA VAL A 16 18.254 16.709 21.439 1.00 5.83 C ANISOU 140 CA VAL A 16 813 676 725 -24 2 34 C ATOM 141 C VAL A 16 17.321 17.897 21.743 1.00 5.05 C ANISOU 141 C VAL A 16 711 653 553 -24 28 26 C ATOM 142 O VAL A 16 17.272 18.848 20.971 1.00 5.30 O ANISOU 142 O VAL A 16 737 648 627 -77 74 113 O ATOM 143 CB VAL A 16 17.614 15.665 20.495 1.00 7.34 C ANISOU 143 CB VAL A 16 865 933 991 104 -77 -50 C ATOM 144 CG1 VAL A 16 18.611 14.559 20.133 1.00 9.85 C ANISOU 144 CG1 VAL A 16 1234 1160 1349 70 -9 -260 C ATOM 145 CG2 VAL A 16 16.422 15.114 21.060 1.00 7.97 C ANISOU 145 CG2 VAL A 16 1032 1162 833 24 -38 108 C ATOM 146 N CYS A 17 16.618 17.857 22.864 1.00 4.38 N ANISOU 146 N CYS A 17 553 608 501 3 -38 111 N ATOM 147 CA CYS A 17 15.766 18.964 23.214 1.00 4.28 C ANISOU 147 CA CYS A 17 434 630 562 -1 7 80 C ATOM 148 C CYS A 17 16.552 20.182 23.686 1.00 4.33 C ANISOU 148 C CYS A 17 521 534 588 4 41 56 C ATOM 149 O CYS A 17 16.112 21.317 23.463 1.00 5.10 O ANISOU 149 O CYS A 17 622 566 748 -7 7 76 O ATOM 150 CB CYS A 17 14.705 18.526 24.212 1.00 5.17 C ANISOU 150 CB CYS A 17 593 643 727 -8 67 59 C ATOM 151 SG CYS A 17 13.487 17.403 23.483 1.00 5.76 S ANISOU 151 SG CYS A 17 641 796 748 -43 -53 26 S ATOM 152 N LYS A 18 17.702 19.988 24.306 1.00 4.78 N ANISOU 152 N LYS A 18 693 490 629 49 -67 38 N ATOM 153 CA LYS A 18 18.547 21.112 24.646 1.00 5.28 C ANISOU 153 CA LYS A 18 687 654 664 -11 -10 -37 C ATOM 154 C LYS A 18 18.985 21.831 23.360 1.00 5.42 C ANISOU 154 C LYS A 18 687 612 760 46 -45 -25 C ATOM 155 O LYS A 18 18.941 23.047 23.280 1.00 5.77 O ANISOU 155 O LYS A 18 730 650 810 -18 -84 -18 O ATOM 156 CB LYS A 18 19.730 20.668 25.496 1.00 6.05 C ANISOU 156 CB LYS A 18 816 739 741 -34 -131 59 C ATOM 157 CG LYS A 18 20.604 21.832 25.904 1.00 7.52 C ANISOU 157 CG LYS A 18 783 1084 989 -78 46 -6 C ATOM 158 CD LYS A 18 21.736 21.441 26.825 1.00 11.14 C ANISOU 158 CD LYS A 18 1376 1551 1303 -173 -240 -63 C ATOM 159 CE LYS A 18 22.627 22.636 27.169 1.00 12.93 C ANISOU 159 CE LYS A 18 1501 1633 1779 -117 -206 -62 C ATOM 160 NZ LYS A 18 23.348 23.131 25.981 1.00 17.32 N ANISOU 160 NZ LYS A 18 2526 2158 1897 -107 -34 -34 N ATOM 161 N THR A 19 19.419 21.065 22.355 1.00 5.69 N ANISOU 161 N THR A 19 708 710 742 76 8 26 N ATOM 162 CA ATHR A 19 19.858 21.594 21.073 0.50 6.33 C ANISOU 162 CA ATHR A 19 796 810 797 -1 80 1 C ATOM 163 CA BTHR A 19 19.867 21.736 21.139 0.50 6.01 C ANISOU 163 CA BTHR A 19 692 750 839 18 73 -19 C ATOM 164 C THR A 19 18.714 22.273 20.301 1.00 5.83 C ANISOU 164 C THR A 19 700 716 797 54 139 39 C ATOM 165 O THR A 19 18.901 23.260 19.617 1.00 6.08 O ANISOU 165 O THR A 19 780 590 939 -18 128 57 O ATOM 166 CB ATHR A 19 20.486 20.417 20.270 0.50 6.92 C ANISOU 166 CB ATHR A 19 867 872 890 -15 135 -41 C ATOM 167 CB BTHR A 19 20.878 20.922 20.314 0.50 6.19 C ANISOU 167 CB BTHR A 19 575 823 951 82 106 41 C ATOM 168 OG1ATHR A 19 21.555 19.847 21.041 0.50 9.31 O ANISOU 168 OG1ATHR A 19 1102 1130 1306 -85 180 238 O ATOM 169 OG1BTHR A 19 20.341 19.640 20.007 0.50 7.06 O ANISOU 169 OG1BTHR A 19 780 734 1169 101 296 -95 O ATOM 170 CG2ATHR A 19 21.003 20.863 18.955 0.50 8.32 C ANISOU 170 CG2ATHR A 19 1347 1042 772 39 65 34 C ATOM 171 CG2BTHR A 19 22.173 20.759 21.087 0.50 8.56 C ANISOU 171 CG2BTHR A 19 666 1083 1503 146 -180 -182 C ATOM 172 N GLU A 20 17.520 21.698 20.374 1.00 4.60 N ANISOU 172 N GLU A 20 658 510 578 -73 54 34 N ATOM 173 CA GLU A 20 16.381 22.254 19.669 1.00 4.66 C ANISOU 173 CA GLU A 20 716 589 463 -68 51 5 C ATOM 174 C GLU A 20 15.975 23.607 20.238 1.00 4.09 C ANISOU 174 C GLU A 20 534 501 520 -115 2 58 C ATOM 175 O GLU A 20 15.474 24.450 19.487 1.00 5.00 O ANISOU 175 O GLU A 20 701 670 527 20 -12 91 O ATOM 176 CB GLU A 20 15.223 21.266 19.714 1.00 5.29 C ANISOU 176 CB GLU A 20 809 579 622 -68 -30 -67 C ATOM 177 CG GLU A 20 13.994 21.778 18.986 1.00 6.85 C ANISOU 177 CG GLU A 20 999 845 758 -37 -91 -92 C ATOM 178 CD GLU A 20 12.833 20.822 18.981 1.00 7.01 C ANISOU 178 CD GLU A 20 909 839 915 73 -85 -131 C ATOM 179 OE1 GLU A 20 13.011 19.654 18.654 1.00 8.75 O ANISOU 179 OE1 GLU A 20 1097 935 1290 89 -79 -325 O ATOM 180 OE2 GLU A 20 11.707 21.244 19.270 1.00 12.23 O ANISOU 180 OE2 GLU A 20 1132 1071 2442 -116 342 -438 O ATOM 181 N THR A 21 16.107 23.772 21.549 1.00 4.17 N ANISOU 181 N THR A 21 497 602 483 43 16 102 N ATOM 182 CA THR A 21 15.532 24.923 22.243 1.00 4.81 C ANISOU 182 CA THR A 21 674 624 527 53 86 81 C ATOM 183 C THR A 21 16.564 25.978 22.594 1.00 5.09 C ANISOU 183 C THR A 21 764 585 584 83 93 128 C ATOM 184 O THR A 21 16.193 27.120 22.831 1.00 6.34 O ANISOU 184 O THR A 21 963 711 736 142 -74 23 O ATOM 185 CB THR A 21 14.812 24.498 23.528 1.00 5.43 C ANISOU 185 CB THR A 21 861 686 515 122 80 47 C ATOM 186 OG1 THR A 21 15.770 23.935 24.463 1.00 5.91 O ANISOU 186 OG1 THR A 21 890 849 505 57 -1 23 O ATOM 187 CG2 THR A 21 13.730 23.492 23.219 1.00 6.63 C ANISOU 187 CG2 THR A 21 666 952 899 110 85 265 C ATOM 188 N GLY A 22 17.848 25.611 22.663 1.00 5.05 N ANISOU 188 N GLY A 22 682 641 596 -5 -15 -10 N ATOM 189 CA GLY A 22 18.847 26.543 23.151 1.00 5.56 C ANISOU 189 CA GLY A 22 737 722 651 -80 9 83 C ATOM 190 C GLY A 22 18.781 26.845 24.632 1.00 5.69 C ANISOU 190 C GLY A 22 656 806 698 -55 22 11 C ATOM 191 O GLY A 22 19.377 27.832 25.068 1.00 6.85 O ANISOU 191 O GLY A 22 783 922 897 -248 -57 -8 O ATOM 192 N ILE A 23 18.076 26.039 25.412 1.00 5.64 N ANISOU 192 N ILE A 23 821 746 574 -54 -14 18 N ATOM 193 CA ILE A 23 18.004 26.252 26.841 1.00 5.91 C ANISOU 193 CA ILE A 23 777 824 641 -20 -45 39 C ATOM 194 C ILE A 23 19.403 26.193 27.454 1.00 6.01 C ANISOU 194 C ILE A 23 773 782 728 -6 19 -23 C ATOM 195 O ILE A 23 20.222 25.352 27.079 1.00 6.93 O ANISOU 195 O ILE A 23 849 952 832 64 -7 -52 O ATOM 196 CB ILE A 23 17.038 25.230 27.483 1.00 5.72 C ANISOU 196 CB ILE A 23 687 815 667 -31 -89 38 C ATOM 197 CG1 ILE A 23 16.739 25.567 28.942 1.00 5.45 C ANISOU 197 CG1 ILE A 23 602 843 625 -56 81 -109 C ATOM 198 CG2 ILE A 23 17.536 23.803 27.363 1.00 6.69 C ANISOU 198 CG2 ILE A 23 1021 866 654 0 5 11 C ATOM 199 CD1 ILE A 23 15.645 24.729 29.541 1.00 7.93 C ANISOU 199 CD1 ILE A 23 778 1214 1021 -250 -69 45 C ATOM 200 N ASP A 24 19.639 27.029 28.460 1.00 5.94 N ANISOU 200 N ASP A 24 683 830 741 -48 -74 -41 N ATOM 201 CA ASP A 24 20.889 26.948 29.241 1.00 7.01 C ANISOU 201 CA ASP A 24 858 976 827 -66 -118 -34 C ATOM 202 C ASP A 24 20.976 25.582 29.908 1.00 6.37 C ANISOU 202 C ASP A 24 775 852 792 13 -84 -148 C ATOM 203 O ASP A 24 19.978 25.053 30.408 1.00 6.31 O ANISOU 203 O ASP A 24 727 947 720 -82 -104 -48 O ATOM 204 CB ASP A 24 20.885 27.968 30.403 1.00 8.61 C ANISOU 204 CB ASP A 24 1151 1140 977 -103 -288 -50 C ATOM 205 CG ASP A 24 21.037 29.396 29.981 1.00 11.10 C ANISOU 205 CG ASP A 24 1450 1450 1315 -1 -267 -145 C ATOM 206 OD1 ASP A 24 21.407 29.674 28.827 1.00 13.76 O ANISOU 206 OD1 ASP A 24 1931 1397 1899 -399 -137 259 O ATOM 207 OD2 ASP A 24 20.784 30.243 30.880 1.00 13.45 O ANISOU 207 OD2 ASP A 24 2150 1502 1459 96 -453 -261 O ATOM 208 N GLN A 25 22.192 25.045 30.036 1.00 7.03 N ANISOU 208 N GLN A 25 794 1050 824 19 -15 -157 N ATOM 209 CA GLN A 25 22.378 23.791 30.748 1.00 7.52 C ANISOU 209 CA GLN A 25 853 1040 962 134 -65 -154 C ATOM 210 C GLN A 25 21.859 23.873 32.175 1.00 6.76 C ANISOU 210 C GLN A 25 764 904 897 101 -84 -114 C ATOM 211 O GLN A 25 21.283 22.917 32.662 1.00 6.96 O ANISOU 211 O GLN A 25 817 876 947 157 -122 -8 O ATOM 212 CB GLN A 25 23.840 23.343 30.794 1.00 8.71 C ANISOU 212 CB GLN A 25 990 1216 1101 212 -9 -229 C ATOM 213 CG GLN A 25 24.032 21.977 31.564 1.00 11.77 C ANISOU 213 CG GLN A 25 1423 1699 1348 196 125 -101 C ATOM 214 CD GLN A 25 23.509 20.787 30.771 1.00 14.34 C ANISOU 214 CD GLN A 25 1802 1904 1741 190 181 -218 C ATOM 215 OE1 GLN A 25 22.558 20.091 31.162 1.00 15.39 O ANISOU 215 OE1 GLN A 25 2023 2070 1753 154 236 -260 O ATOM 216 NE2 GLN A 25 24.117 20.564 29.625 1.00 16.42 N ANISOU 216 NE2 GLN A 25 2364 2355 1520 117 216 -553 N ATOM 217 N GLN A 26 22.050 25.007 32.851 1.00 6.19 N ANISOU 217 N GLN A 26 719 813 820 56 -87 -43 N ATOM 218 CA GLN A 26 21.593 25.132 34.221 1.00 6.60 C ANISOU 218 CA GLN A 26 797 914 796 -52 -139 -7 C ATOM 219 C GLN A 26 20.076 24.921 34.304 1.00 6.07 C ANISOU 219 C GLN A 26 763 765 778 -97 -59 -31 C ATOM 220 O GLN A 26 19.572 24.256 35.218 1.00 6.38 O ANISOU 220 O GLN A 26 813 868 743 -6 -117 -23 O ATOM 221 CB GLN A 26 21.923 26.517 34.745 1.00 8.46 C ANISOU 221 CB GLN A 26 1044 1139 1030 -31 -31 -218 C ATOM 222 CG GLN A 26 21.361 26.789 36.118 1.00 11.47 C ANISOU 222 CG GLN A 26 1347 1760 1249 -81 20 -385 C ATOM 223 CD GLN A 26 21.979 25.921 37.158 1.00 15.67 C ANISOU 223 CD GLN A 26 1899 2383 1672 51 -26 -192 C ATOM 224 OE1 GLN A 26 23.201 25.907 37.314 1.00 19.09 O ANISOU 224 OE1 GLN A 26 1957 3276 2019 103 -287 43 O ATOM 225 NE2 GLN A 26 21.155 25.188 37.895 1.00 18.42 N ANISOU 225 NE2 GLN A 26 2209 2924 1865 -202 -391 133 N ATOM 226 N LYS A 27 19.343 25.539 33.376 1.00 5.48 N ANISOU 226 N LYS A 27 695 680 707 -27 -32 28 N ATOM 227 CA LYS A 27 17.893 25.430 33.405 1.00 5.24 C ANISOU 227 CA LYS A 27 680 631 679 -35 34 57 C ATOM 228 C LYS A 27 17.432 24.039 33.003 1.00 5.42 C ANISOU 228 C LYS A 27 734 650 675 17 -8 28 C ATOM 229 O LYS A 27 16.447 23.525 33.569 1.00 6.27 O ANISOU 229 O LYS A 27 769 768 844 50 41 93 O ATOM 230 CB LYS A 27 17.255 26.516 32.550 1.00 5.66 C ANISOU 230 CB LYS A 27 753 677 720 -40 -12 8 C ATOM 231 CG LYS A 27 17.516 27.895 33.071 1.00 6.92 C ANISOU 231 CG LYS A 27 818 772 1039 -17 20 -41 C ATOM 232 CD LYS A 27 16.872 28.971 32.217 1.00 7.82 C ANISOU 232 CD LYS A 27 1016 862 1092 49 27 -47 C ATOM 233 CE LYS A 27 17.137 30.357 32.809 1.00 9.24 C ANISOU 233 CE LYS A 27 1122 837 1551 186 75 -92 C ATOM 234 NZ LYS A 27 16.551 31.432 31.994 1.00 11.36 N ANISOU 234 NZ LYS A 27 1578 967 1772 166 -189 31 N ATOM 235 N ALA A 28 18.095 23.412 32.030 1.00 5.41 N ANISOU 235 N ALA A 28 696 713 643 -34 37 -20 N ATOM 236 CA ALA A 28 17.795 22.016 31.732 1.00 5.57 C ANISOU 236 CA ALA A 28 747 661 707 -45 -85 3 C ATOM 237 C ALA A 28 18.013 21.151 32.957 1.00 5.57 C ANISOU 237 C ALA A 28 675 670 770 -2 -73 -26 C ATOM 238 O ALA A 28 17.188 20.300 33.252 1.00 5.62 O ANISOU 238 O ALA A 28 729 677 729 35 -24 14 O ATOM 239 CB ALA A 28 18.634 21.530 30.555 1.00 6.73 C ANISOU 239 CB ALA A 28 841 886 828 27 25 -78 C ATOM 240 N ASN A 29 19.120 21.374 33.658 1.00 5.95 N ANISOU 240 N ASN A 29 692 714 855 26 -121 32 N ATOM 241 CA ASN A 29 19.383 20.613 34.892 1.00 6.22 C ANISOU 241 CA ASN A 29 789 723 849 -27 -84 93 C ATOM 242 C ASN A 29 18.300 20.821 35.929 1.00 6.40 C ANISOU 242 C ASN A 29 905 782 743 -1 -93 -27 C ATOM 243 O ASN A 29 17.916 19.881 36.607 1.00 6.31 O ANISOU 243 O ASN A 29 865 803 729 -17 -96 46 O ATOM 244 CB ASN A 29 20.698 20.997 35.551 1.00 7.45 C ANISOU 244 CB ASN A 29 945 923 960 -37 -234 126 C ATOM 245 CG ASN A 29 21.879 20.595 34.810 1.00 9.32 C ANISOU 245 CG ASN A 29 1131 1348 1062 -101 -197 251 C ATOM 246 OD1 ASN A 29 22.987 21.073 35.143 1.00 13.44 O ANISOU 246 OD1 ASN A 29 1115 1807 2182 -270 -153 232 O ATOM 247 ND2 ASN A 29 21.741 19.722 33.866 1.00 8.02 N ANISOU 247 ND2 ASN A 29 617 1208 1221 -54 271 254 N ATOM 248 N ASP A 30 17.823 22.051 36.064 1.00 6.45 N ANISOU 248 N ASP A 30 951 681 818 7 -91 49 N ATOM 249 CA ASP A 30 16.742 22.332 36.989 1.00 6.72 C ANISOU 249 CA ASP A 30 1006 697 849 -6 -56 19 C ATOM 250 C ASP A 30 15.511 21.496 36.633 1.00 5.97 C ANISOU 250 C ASP A 30 886 652 730 130 -4 -41 C ATOM 251 O ASP A 30 14.895 20.888 37.502 1.00 6.40 O ANISOU 251 O ASP A 30 888 774 766 82 -11 45 O ATOM 252 CB ASP A 30 16.368 23.820 36.967 1.00 7.48 C ANISOU 252 CB ASP A 30 1066 757 1017 -44 21 -107 C ATOM 253 CG ASP A 30 17.426 24.730 37.536 1.00 11.45 C ANISOU 253 CG ASP A 30 1553 1253 1542 -145 70 -201 C ATOM 254 OD1 ASP A 30 18.288 24.264 38.305 1.00 14.06 O ANISOU 254 OD1 ASP A 30 1832 1599 1908 -314 -501 -663 O ATOM 255 OD2 ASP A 30 17.403 25.930 37.182 1.00 13.52 O ANISOU 255 OD2 ASP A 30 1778 1226 2133 -92 92 -428 O ATOM 256 N VAL A 31 15.137 21.490 35.356 1.00 4.97 N ANISOU 256 N VAL A 31 679 641 567 97 -99 94 N ATOM 257 CA VAL A 31 13.999 20.695 34.905 1.00 5.06 C ANISOU 257 CA VAL A 31 679 630 614 55 -60 58 C ATOM 258 C VAL A 31 14.236 19.216 35.203 1.00 5.13 C ANISOU 258 C VAL A 31 633 651 662 29 -69 71 C ATOM 259 O VAL A 31 13.362 18.522 35.733 1.00 5.30 O ANISOU 259 O VAL A 31 635 774 604 32 -122 160 O ATOM 260 CB VAL A 31 13.713 20.912 33.414 1.00 4.74 C ANISOU 260 CB VAL A 31 576 641 584 110 -57 35 C ATOM 261 CG1 VAL A 31 12.696 19.915 32.910 1.00 6.41 C ANISOU 261 CG1 VAL A 31 753 1013 668 -78 -99 38 C ATOM 262 CG2 VAL A 31 13.276 22.336 33.134 1.00 5.67 C ANISOU 262 CG2 VAL A 31 632 752 771 123 13 180 C ATOM 263 N ILE A 32 15.422 18.722 34.864 1.00 4.75 N ANISOU 263 N ILE A 32 678 487 637 41 -93 83 N ATOM 264 CA ILE A 32 15.757 17.330 35.103 1.00 4.93 C ANISOU 264 CA ILE A 32 697 526 648 14 -46 27 C ATOM 265 C ILE A 32 15.643 16.957 36.578 1.00 4.96 C ANISOU 265 C ILE A 32 639 544 700 -20 -125 77 C ATOM 266 O ILE A 32 15.158 15.893 36.908 1.00 5.26 O ANISOU 266 O ILE A 32 705 560 731 -5 -27 112 O ATOM 267 CB ILE A 32 17.150 17.034 34.486 1.00 4.44 C ANISOU 267 CB ILE A 32 615 481 588 -86 -69 50 C ATOM 268 CG1 ILE A 32 17.091 17.125 32.963 1.00 4.94 C ANISOU 268 CG1 ILE A 32 705 623 548 -82 -69 -148 C ATOM 269 CG2 ILE A 32 17.680 15.684 34.893 1.00 6.37 C ANISOU 269 CG2 ILE A 32 836 727 855 136 80 200 C ATOM 270 CD1 ILE A 32 18.454 17.208 32.289 1.00 6.34 C ANISOU 270 CD1 ILE A 32 869 780 760 -14 180 -48 C ATOM 271 N GLU A 33 16.041 17.859 37.454 1.00 5.32 N ANISOU 271 N GLU A 33 800 575 643 27 -119 56 N ATOM 272 CA GLU A 33 15.939 17.650 38.901 1.00 6.18 C ANISOU 272 CA GLU A 33 925 800 621 -23 -177 68 C ATOM 273 C GLU A 33 14.559 17.908 39.477 1.00 6.53 C ANISOU 273 C GLU A 33 999 791 688 22 -112 90 C ATOM 274 O GLU A 33 14.340 17.691 40.660 1.00 7.46 O ANISOU 274 O GLU A 33 1087 977 768 -44 19 111 O ATOM 275 CB GLU A 33 16.942 18.541 39.623 1.00 8.03 C ANISOU 275 CB GLU A 33 1161 1238 651 8 -217 147 C ATOM 276 CG GLU A 33 18.325 18.073 39.349 1.00 11.10 C ANISOU 276 CG GLU A 33 1404 1520 1293 56 -331 29 C ATOM 277 CD GLU A 33 19.423 18.982 39.833 1.00 14.59 C ANISOU 277 CD GLU A 33 1761 2045 1735 -154 -437 78 C ATOM 278 OE1 GLU A 33 19.116 20.003 40.493 1.00 14.98 O ANISOU 278 OE1 GLU A 33 1995 1934 1761 -393 -661 -60 O ATOM 279 OE2 GLU A 33 20.619 18.640 39.558 1.00 16.47 O ANISOU 279 OE2 GLU A 33 1769 2363 2124 -190 -227 217 O ATOM 280 N GLY A 34 13.613 18.328 38.650 1.00 6.07 N ANISOU 280 N GLY A 34 844 744 715 67 4 136 N ATOM 281 CA GLY A 34 12.216 18.501 39.052 1.00 6.47 C ANISOU 281 CA GLY A 34 869 766 823 15 16 116 C ATOM 282 C GLY A 34 11.857 19.887 39.562 1.00 7.70 C ANISOU 282 C GLY A 34 1123 862 937 73 80 164 C ATOM 283 O GLY A 34 10.822 20.049 40.188 1.00 9.61 O ANISOU 283 O GLY A 34 1278 1063 1308 213 305 86 O ATOM 284 N ASN A 35 12.700 20.886 39.319 1.00 7.24 N ANISOU 284 N ASN A 35 987 816 948 77 -11 82 N ATOM 285 CA ASN A 35 12.411 22.266 39.704 1.00 8.07 C ANISOU 285 CA ASN A 35 1185 860 1021 26 -43 110 C ATOM 286 C ASN A 35 12.146 23.051 38.452 1.00 8.18 C ANISOU 286 C ASN A 35 1125 982 999 19 -47 165 C ATOM 287 O ASN A 35 13.074 23.540 37.785 1.00 9.09 O ANISOU 287 O ASN A 35 1053 1080 1318 38 -98 449 O ATOM 288 CB ASN A 35 13.566 22.794 40.495 1.00 8.67 C ANISOU 288 CB ASN A 35 1240 1062 992 78 -91 94 C ATOM 289 CG ASN A 35 13.737 22.007 41.748 1.00 10.33 C ANISOU 289 CG ASN A 35 1527 1196 1199 203 -157 169 C ATOM 290 OD1 ASN A 35 12.788 21.883 42.519 1.00 12.30 O ANISOU 290 OD1 ASN A 35 1721 1554 1398 305 -159 461 O ATOM 291 ND2 ASN A 35 14.907 21.388 41.929 1.00 12.62 N ANISOU 291 ND2 ASN A 35 1628 1703 1462 445 -162 128 N ATOM 292 N ILE A 36 10.863 23.123 38.116 1.00 8.73 N ANISOU 292 N ILE A 36 1019 1198 1098 50 7 146 N ATOM 293 CA AILE A 36 10.423 23.699 36.845 0.50 8.84 C ANISOU 293 CA AILE A 36 1061 1168 1128 15 -14 153 C ATOM 294 CA BILE A 36 10.444 23.677 36.837 0.50 9.04 C ANISOU 294 CA BILE A 36 1099 1196 1137 47 -7 150 C ATOM 295 C ILE A 36 10.001 25.139 37.039 1.00 8.97 C ANISOU 295 C ILE A 36 1070 1189 1149 21 -24 117 C ATOM 296 O ILE A 36 9.077 25.416 37.784 1.00 10.32 O ANISOU 296 O ILE A 36 1232 1325 1364 58 61 70 O ATOM 297 CB AILE A 36 9.190 22.970 36.244 0.50 8.40 C ANISOU 297 CB AILE A 36 914 1072 1205 41 -2 124 C ATOM 298 CB BILE A 36 9.305 22.820 36.159 0.50 8.72 C ANISOU 298 CB BILE A 36 992 1132 1189 68 11 107 C ATOM 299 CG1AILE A 36 9.330 21.463 36.379 0.50 7.55 C ANISOU 299 CG1AILE A 36 868 945 1056 -90 31 147 C ATOM 300 CG1BILE A 36 9.832 21.460 35.634 0.50 9.14 C ANISOU 300 CG1BILE A 36 1124 1081 1266 -9 -7 121 C ATOM 301 CG2AILE A 36 8.993 23.381 34.786 0.50 8.22 C ANISOU 301 CG2AILE A 36 921 1036 1166 -117 -27 126 C ATOM 302 CG2BILE A 36 8.689 23.595 34.999 0.50 8.26 C ANISOU 302 CG2BILE A 36 945 1127 1066 144 100 114 C ATOM 303 CD1AILE A 36 10.673 20.956 35.999 0.50 9.10 C ANISOU 303 CD1AILE A 36 965 1218 1274 115 142 189 C ATOM 304 CD1BILE A 36 10.089 20.376 36.684 0.50 7.82 C ANISOU 304 CD1BILE A 36 984 774 1211 -102 121 17 C ATOM 305 N ASP A 37 10.686 26.064 36.374 1.00 8.63 N ANISOU 305 N ASP A 37 1059 1015 1203 64 -102 119 N ATOM 306 CA ASP A 37 10.286 27.467 36.352 1.00 9.12 C ANISOU 306 CA ASP A 37 1201 1037 1227 72 -110 43 C ATOM 307 C ASP A 37 9.286 27.591 35.209 1.00 8.39 C ANISOU 307 C ASP A 37 1107 960 1120 126 -119 48 C ATOM 308 O ASP A 37 9.660 27.775 34.048 1.00 7.87 O ANISOU 308 O ASP A 37 791 950 1247 189 -67 134 O ATOM 309 CB ASP A 37 11.516 28.338 36.123 1.00 10.55 C ANISOU 309 CB ASP A 37 1431 1226 1350 -31 -122 71 C ATOM 310 CG ASP A 37 11.196 29.820 36.076 1.00 14.73 C ANISOU 310 CG ASP A 37 2008 1499 2089 -84 -49 -18 C ATOM 311 OD1 ASP A 37 12.155 30.606 35.940 1.00 18.70 O ANISOU 311 OD1 ASP A 37 2755 1612 2735 -491 -165 158 O ATOM 312 OD2 ASP A 37 10.003 30.190 36.134 1.00 18.38 O ANISOU 312 OD2 ASP A 37 2582 1701 2697 139 134 -12 O ATOM 313 N VAL A 38 8.008 27.399 35.544 1.00 8.02 N ANISOU 313 N VAL A 38 1060 830 1157 67 -96 17 N ATOM 314 CA VAL A 38 6.999 27.135 34.530 1.00 8.42 C ANISOU 314 CA VAL A 38 1043 1001 1155 74 -12 123 C ATOM 315 C VAL A 38 6.805 28.319 33.572 1.00 7.18 C ANISOU 315 C VAL A 38 881 767 1079 118 59 118 C ATOM 316 O VAL A 38 6.408 28.092 32.442 1.00 7.87 O ANISOU 316 O VAL A 38 1041 896 1053 30 0 169 O ATOM 317 CB VAL A 38 5.630 26.715 35.150 1.00 8.87 C ANISOU 317 CB VAL A 38 1028 1055 1287 130 37 138 C ATOM 318 CG1 VAL A 38 5.751 25.383 35.906 1.00 9.75 C ANISOU 318 CG1 VAL A 38 1140 1251 1312 136 -65 251 C ATOM 319 CG2 VAL A 38 5.040 27.820 36.045 1.00 10.56 C ANISOU 319 CG2 VAL A 38 1163 1351 1496 115 42 -89 C ATOM 320 N GLU A 39 7.149 29.539 33.996 1.00 8.18 N ANISOU 320 N GLU A 39 992 994 1121 28 -26 114 N ATOM 321 CA GLU A 39 6.964 30.746 33.173 1.00 8.51 C ANISOU 321 CA GLU A 39 1071 879 1283 171 24 89 C ATOM 322 C GLU A 39 8.107 31.033 32.206 1.00 9.11 C ANISOU 322 C GLU A 39 1059 1066 1334 120 19 114 C ATOM 323 O GLU A 39 7.994 31.923 31.378 1.00 10.15 O ANISOU 323 O GLU A 39 1223 1060 1571 54 86 228 O ATOM 324 CB GLU A 39 6.740 31.983 34.058 1.00 9.70 C ANISOU 324 CB GLU A 39 1291 1025 1368 194 30 -54 C ATOM 325 CG GLU A 39 5.542 31.891 34.996 1.00 12.49 C ANISOU 325 CG GLU A 39 1681 1286 1778 252 124 -24 C ATOM 326 CD GLU A 39 4.200 31.940 34.290 1.00 16.98 C ANISOU 326 CD GLU A 39 2196 2063 2192 6 -48 -185 C ATOM 327 OE1 GLU A 39 4.110 32.464 33.156 1.00 19.30 O ANISOU 327 OE1 GLU A 39 2210 2591 2533 375 -202 213 O ATOM 328 OE2 GLU A 39 3.210 31.475 34.899 1.00 19.79 O ANISOU 328 OE2 GLU A 39 2346 2607 2565 96 336 -290 O ATOM 329 N ASP A 40 9.204 30.295 32.309 1.00 8.14 N ANISOU 329 N ASP A 40 979 870 1243 69 -49 88 N ATOM 330 CA ASP A 40 10.396 30.583 31.521 1.00 8.35 C ANISOU 330 CA ASP A 40 1008 947 1216 21 -59 86 C ATOM 331 C ASP A 40 10.183 30.003 30.121 1.00 8.22 C ANISOU 331 C ASP A 40 987 961 1174 77 -34 81 C ATOM 332 O ASP A 40 9.848 28.819 29.984 1.00 8.07 O ANISOU 332 O ASP A 40 1010 831 1224 46 -92 82 O ATOM 333 CB ASP A 40 11.602 29.980 32.246 1.00 8.65 C ANISOU 333 CB ASP A 40 1060 1001 1224 7 -112 -26 C ATOM 334 CG ASP A 40 12.920 30.190 31.527 1.00 9.54 C ANISOU 334 CG ASP A 40 1099 984 1538 -143 48 -59 C ATOM 335 OD1 ASP A 40 13.815 30.895 32.087 1.00 13.08 O ANISOU 335 OD1 ASP A 40 1321 1679 1970 -376 133 -325 O ATOM 336 OD2 ASP A 40 13.117 29.603 30.445 1.00 9.61 O ANISOU 336 OD2 ASP A 40 1002 1293 1354 -153 -76 131 O ATOM 337 N LYS A 41 10.364 30.825 29.092 1.00 8.41 N ANISOU 337 N LYS A 41 1101 810 1281 56 -3 57 N ATOM 338 CA ALYS A 41 10.064 30.432 27.710 0.50 8.27 C ANISOU 338 CA ALYS A 41 1017 889 1234 86 -52 100 C ATOM 339 CA BLYS A 41 10.039 30.427 27.739 0.50 8.97 C ANISOU 339 CA BLYS A 41 1121 981 1306 75 -46 75 C ATOM 340 C LYS A 41 10.854 29.210 27.260 1.00 7.71 C ANISOU 340 C LYS A 41 955 816 1156 53 -32 137 C ATOM 341 O LYS A 41 10.279 28.282 26.698 1.00 7.53 O ANISOU 341 O LYS A 41 839 957 1064 -120 -29 58 O ATOM 342 CB ALYS A 41 10.301 31.594 26.721 0.50 9.00 C ANISOU 342 CB ALYS A 41 1134 996 1288 101 -78 141 C ATOM 343 CB BLYS A 41 10.196 31.615 26.778 0.50 10.13 C ANISOU 343 CB BLYS A 41 1308 1153 1388 72 -76 121 C ATOM 344 CG ALYS A 41 10.070 31.234 25.220 0.50 9.84 C ANISOU 344 CG ALYS A 41 1252 1116 1367 139 -41 172 C ATOM 345 CG BLYS A 41 9.343 32.862 27.110 0.50 14.57 C ANISOU 345 CG BLYS A 41 1907 1659 1967 139 -13 -60 C ATOM 346 CD ALYS A 41 10.437 32.378 24.274 0.50 13.42 C ANISOU 346 CD ALYS A 41 1768 1644 1685 -25 6 346 C ATOM 347 CD BLYS A 41 7.854 32.556 27.201 0.50 17.56 C ANISOU 347 CD BLYS A 41 2152 2137 2381 88 -19 -55 C ATOM 348 CE ALYS A 41 10.609 31.895 22.823 0.50 16.00 C ANISOU 348 CE ALYS A 41 2088 2070 1919 -72 44 202 C ATOM 349 CE BLYS A 41 7.433 32.361 28.635 0.50 18.98 C ANISOU 349 CE BLYS A 41 2326 2414 2469 57 21 -40 C ATOM 350 NZ ALYS A 41 9.335 31.775 22.066 0.50 17.14 N ANISOU 350 NZ ALYS A 41 2252 2226 2033 -176 7 282 N ATOM 351 NZ BLYS A 41 6.011 32.745 28.901 0.50 20.67 N ANISOU 351 NZ BLYS A 41 2575 2574 2705 223 -2 -111 N ATOM 352 N LYS A 42 12.182 29.211 27.449 1.00 7.28 N ANISOU 352 N LYS A 42 822 836 1107 -161 -23 19 N ATOM 353 CA LYS A 42 12.963 28.052 27.001 1.00 6.63 C ANISOU 353 CA LYS A 42 791 823 904 -59 -50 65 C ATOM 354 C LYS A 42 12.670 26.819 27.865 1.00 5.85 C ANISOU 354 C LYS A 42 707 721 794 -6 -24 21 C ATOM 355 O LYS A 42 12.747 25.730 27.364 1.00 6.55 O ANISOU 355 O LYS A 42 809 755 923 -127 -97 23 O ATOM 356 CB LYS A 42 14.450 28.375 26.796 1.00 7.23 C ANISOU 356 CB LYS A 42 936 820 989 -64 68 54 C ATOM 357 CG LYS A 42 14.688 29.186 25.489 1.00 8.16 C ANISOU 357 CG LYS A 42 1140 972 989 17 96 -1 C ATOM 358 CD LYS A 42 16.127 29.564 25.295 1.00 5.18 C ANISOU 358 CD LYS A 42 763 742 463 94 53 -170 C ATOM 359 CE LYS A 42 16.341 30.187 23.946 1.00 6.25 C ANISOU 359 CE LYS A 42 1108 672 591 74 -21 -139 C ATOM 360 NZ LYS A 42 17.647 30.918 23.793 1.00 10.84 N ANISOU 360 NZ LYS A 42 1289 1844 984 -294 57 -32 N ATOM 361 N VAL A 43 12.388 27.005 29.145 1.00 6.18 N ANISOU 361 N VAL A 43 801 629 917 -26 -16 -10 N ATOM 362 CA VAL A 43 11.951 25.876 29.970 1.00 6.00 C ANISOU 362 CA VAL A 43 778 608 891 36 45 -31 C ATOM 363 C VAL A 43 10.684 25.264 29.377 1.00 5.39 C ANISOU 363 C VAL A 43 672 564 809 32 36 -18 C ATOM 364 O VAL A 43 10.571 24.044 29.261 1.00 5.07 O ANISOU 364 O VAL A 43 647 552 727 25 4 -8 O ATOM 365 CB VAL A 43 11.744 26.273 31.436 1.00 5.76 C ANISOU 365 CB VAL A 43 607 721 860 49 21 -55 C ATOM 366 CG1 VAL A 43 10.991 25.210 32.216 1.00 7.09 C ANISOU 366 CG1 VAL A 43 813 811 1069 -54 43 -61 C ATOM 367 CG2 VAL A 43 13.093 26.572 32.094 1.00 7.47 C ANISOU 367 CG2 VAL A 43 873 971 994 58 -132 -178 C ATOM 368 N GLN A 44 9.724 26.109 29.020 1.00 5.35 N ANISOU 368 N GLN A 44 700 584 747 37 27 -63 N ATOM 369 CA GLN A 44 8.495 25.634 28.383 1.00 5.35 C ANISOU 369 CA GLN A 44 638 631 763 -2 14 -23 C ATOM 370 C GLN A 44 8.806 24.859 27.121 1.00 4.79 C ANISOU 370 C GLN A 44 509 674 637 34 34 17 C ATOM 371 O GLN A 44 8.264 23.777 26.902 1.00 4.98 O ANISOU 371 O GLN A 44 597 660 633 9 103 49 O ATOM 372 CB GLN A 44 7.573 26.796 28.027 1.00 5.56 C ANISOU 372 CB GLN A 44 670 650 790 52 9 -37 C ATOM 373 CG GLN A 44 6.956 27.453 29.236 1.00 6.19 C ANISOU 373 CG GLN A 44 897 631 823 49 -63 -14 C ATOM 374 CD GLN A 44 6.306 28.769 28.956 1.00 7.35 C ANISOU 374 CD GLN A 44 984 967 842 143 -72 -14 C ATOM 375 OE1 GLN A 44 6.260 29.214 27.819 1.00 8.67 O ANISOU 375 OE1 GLN A 44 1231 1006 1058 196 -76 74 O ATOM 376 NE2 GLN A 44 5.792 29.395 30.010 1.00 8.63 N ANISOU 376 NE2 GLN A 44 1371 740 1169 317 175 106 N ATOM 377 N LEU A 45 9.659 25.422 26.271 1.00 4.97 N ANISOU 377 N LEU A 45 602 618 667 28 26 29 N ATOM 378 CA LEU A 45 9.991 24.772 25.014 1.00 4.73 C ANISOU 378 CA LEU A 45 540 714 542 38 39 57 C ATOM 379 C LEU A 45 10.702 23.436 25.262 1.00 4.61 C ANISOU 379 C LEU A 45 547 641 561 51 13 16 C ATOM 380 O LEU A 45 10.456 22.456 24.573 1.00 5.19 O ANISOU 380 O LEU A 45 581 713 675 13 -48 61 O ATOM 381 CB LEU A 45 10.864 25.674 24.168 1.00 5.30 C ANISOU 381 CB LEU A 45 532 787 693 2 47 35 C ATOM 382 CG LEU A 45 10.184 26.920 23.591 1.00 6.38 C ANISOU 382 CG LEU A 45 770 887 767 144 151 109 C ATOM 383 CD1 LEU A 45 11.212 27.859 22.985 1.00 8.89 C ANISOU 383 CD1 LEU A 45 1117 1295 964 -52 295 104 C ATOM 384 CD2 LEU A 45 9.143 26.509 22.564 1.00 10.00 C ANISOU 384 CD2 LEU A 45 1332 1191 1277 80 -297 291 C ATOM 385 N TYR A 46 11.592 23.404 26.253 1.00 4.63 N ANISOU 385 N TYR A 46 537 653 567 -6 -36 21 N ATOM 386 CA TYR A 46 12.314 22.170 26.565 1.00 4.31 C ANISOU 386 CA TYR A 46 510 620 505 40 -5 2 C ATOM 387 C TYR A 46 11.346 21.093 27.066 1.00 4.42 C ANISOU 387 C TYR A 46 508 604 567 54 -43 -36 C ATOM 388 O TYR A 46 11.400 19.953 26.639 1.00 4.73 O ANISOU 388 O TYR A 46 476 696 625 -30 -40 -29 O ATOM 389 CB TYR A 46 13.388 22.507 27.600 1.00 4.55 C ANISOU 389 CB TYR A 46 576 653 500 83 122 -23 C ATOM 390 CG TYR A 46 14.260 21.383 28.037 1.00 4.52 C ANISOU 390 CG TYR A 46 521 664 529 -84 2 33 C ATOM 391 CD1 TYR A 46 15.286 20.900 27.231 1.00 5.04 C ANISOU 391 CD1 TYR A 46 646 778 492 29 -30 15 C ATOM 392 CD2 TYR A 46 14.105 20.821 29.298 1.00 5.55 C ANISOU 392 CD2 TYR A 46 792 646 670 73 183 33 C ATOM 393 CE1 TYR A 46 16.126 19.874 27.671 1.00 4.94 C ANISOU 393 CE1 TYR A 46 640 710 524 -17 117 -159 C ATOM 394 CE2 TYR A 46 14.956 19.835 29.750 1.00 5.94 C ANISOU 394 CE2 TYR A 46 1077 790 388 110 13 57 C ATOM 395 CZ TYR A 46 15.965 19.385 28.953 1.00 4.66 C ANISOU 395 CZ TYR A 46 640 539 590 7 -127 -3 C ATOM 396 OH TYR A 46 16.788 18.387 29.445 1.00 5.91 O ANISOU 396 OH TYR A 46 1032 584 630 56 -212 -146 O ATOM 397 N CYS A 47 10.444 21.487 27.963 1.00 4.87 N ANISOU 397 N CYS A 47 541 687 622 -43 22 7 N ATOM 398 CA CYS A 47 9.421 20.560 28.457 1.00 5.11 C ANISOU 398 CA CYS A 47 640 673 627 -32 -9 60 C ATOM 399 C CYS A 47 8.526 20.052 27.327 1.00 4.62 C ANISOU 399 C CYS A 47 509 617 629 7 69 10 C ATOM 400 O CYS A 47 8.250 18.855 27.230 1.00 5.37 O ANISOU 400 O CYS A 47 641 666 731 -62 35 98 O ATOM 401 CB CYS A 47 8.584 21.246 29.534 1.00 5.27 C ANISOU 401 CB CYS A 47 688 800 512 -2 11 -4 C ATOM 402 SG CYS A 47 9.439 21.512 31.090 1.00 5.44 S ANISOU 402 SG CYS A 47 649 778 637 2 25 10 S ATOM 403 N GLU A 48 8.072 20.959 26.480 1.00 4.75 N ANISOU 403 N GLU A 48 581 640 580 -58 75 4 N ATOM 404 CA GLU A 48 7.271 20.592 25.327 1.00 5.43 C ANISOU 404 CA GLU A 48 571 724 765 -1 -50 -43 C ATOM 405 C GLU A 48 7.991 19.589 24.444 1.00 5.16 C ANISOU 405 C GLU A 48 613 668 677 8 -150 -4 C ATOM 406 O GLU A 48 7.412 18.630 23.971 1.00 5.66 O ANISOU 406 O GLU A 48 658 649 841 -76 -38 -14 O ATOM 407 CB GLU A 48 6.910 21.839 24.541 1.00 6.07 C ANISOU 407 CB GLU A 48 748 781 776 2 -155 -42 C ATOM 408 CG GLU A 48 6.044 21.569 23.308 1.00 6.48 C ANISOU 408 CG GLU A 48 756 751 953 27 -177 -167 C ATOM 409 CD GLU A 48 5.870 22.768 22.410 1.00 8.06 C ANISOU 409 CD GLU A 48 942 943 1176 135 -315 -110 C ATOM 410 OE1 GLU A 48 6.826 23.528 22.192 1.00 9.14 O ANISOU 410 OE1 GLU A 48 1121 1245 1105 -18 -102 290 O ATOM 411 OE2 GLU A 48 4.749 22.972 21.911 1.00 10.75 O ANISOU 411 OE2 GLU A 48 1146 1255 1683 -104 -406 222 O ATOM 412 N CYS A 49 9.264 19.853 24.185 1.00 4.62 N ANISOU 412 N CYS A 49 526 581 647 -8 -10 -69 N ATOM 413 CA CYS A 49 10.049 18.992 23.333 1.00 4.79 C ANISOU 413 CA CYS A 49 614 603 602 -17 -12 -70 C ATOM 414 C CYS A 49 10.170 17.582 23.883 1.00 5.30 C ANISOU 414 C CYS A 49 673 698 640 -26 -22 -85 C ATOM 415 O CYS A 49 10.005 16.588 23.174 1.00 6.31 O ANISOU 415 O CYS A 49 777 681 937 17 -16 -36 O ATOM 416 CB CYS A 49 11.414 19.624 23.103 1.00 5.41 C ANISOU 416 CB CYS A 49 810 534 709 82 47 -19 C ATOM 417 SG CYS A 49 12.579 18.661 22.125 1.00 6.14 S ANISOU 417 SG CYS A 49 840 805 687 -10 62 -38 S ATOM 418 N ILE A 50 10.454 17.472 25.165 1.00 5.04 N ANISOU 418 N ILE A 50 543 637 734 -2 11 17 N ATOM 419 CA AILE A 50 10.578 16.153 25.760 0.50 5.94 C ANISOU 419 CA AILE A 50 692 761 804 -35 26 126 C ATOM 420 CA BILE A 50 10.580 16.145 25.760 0.50 6.38 C ANISOU 420 CA BILE A 50 742 793 889 -5 -12 115 C ATOM 421 C ILE A 50 9.233 15.404 25.677 1.00 6.15 C ANISOU 421 C ILE A 50 751 748 835 -52 24 107 C ATOM 422 O ILE A 50 9.175 14.233 25.307 1.00 6.73 O ANISOU 422 O ILE A 50 810 674 1069 -4 -22 121 O ATOM 423 CB AILE A 50 11.126 16.287 27.177 0.50 6.26 C ANISOU 423 CB AILE A 50 729 779 867 -84 -19 181 C ATOM 424 CB BILE A 50 11.059 16.182 27.214 0.50 7.14 C ANISOU 424 CB BILE A 50 817 904 991 -20 -58 151 C ATOM 425 CG1AILE A 50 12.648 16.538 27.097 0.50 5.48 C ANISOU 425 CG1AILE A 50 679 827 575 -34 110 15 C ATOM 426 CG1BILE A 50 12.371 16.981 27.359 0.50 7.85 C ANISOU 426 CG1BILE A 50 912 781 1287 92 -145 131 C ATOM 427 CG2AILE A 50 10.731 15.083 28.079 0.50 6.58 C ANISOU 427 CG2AILE A 50 689 818 992 -71 158 333 C ATOM 428 CG2BILE A 50 11.249 14.737 27.718 0.50 7.49 C ANISOU 428 CG2BILE A 50 863 964 1017 102 -35 142 C ATOM 429 CD1AILE A 50 13.173 17.011 28.424 0.50 4.72 C ANISOU 429 CD1AILE A 50 742 788 262 -49 8 -70 C ATOM 430 CD1BILE A 50 13.566 16.105 27.433 0.50 9.80 C ANISOU 430 CD1BILE A 50 974 1371 1379 285 134 -47 C ATOM 431 N LEU A 51 8.140 16.083 25.989 1.00 7.01 N ANISOU 431 N LEU A 51 865 860 939 -27 59 98 N ATOM 432 CA LEU A 51 6.827 15.443 25.898 1.00 7.05 C ANISOU 432 CA LEU A 51 935 767 975 -84 82 199 C ATOM 433 C LEU A 51 6.490 15.023 24.476 1.00 7.41 C ANISOU 433 C LEU A 51 770 981 1065 -28 92 91 C ATOM 434 O LEU A 51 5.929 13.952 24.266 1.00 8.03 O ANISOU 434 O LEU A 51 849 977 1222 -225 111 24 O ATOM 435 CB LEU A 51 5.758 16.394 26.396 1.00 7.91 C ANISOU 435 CB LEU A 51 1001 1043 958 -33 108 86 C ATOM 436 CG LEU A 51 5.810 16.653 27.891 1.00 8.98 C ANISOU 436 CG LEU A 51 1032 1214 1163 -177 214 101 C ATOM 437 CD1 LEU A 51 4.923 17.843 28.269 1.00 11.16 C ANISOU 437 CD1 LEU A 51 1168 1588 1482 36 311 222 C ATOM 438 CD2 LEU A 51 5.427 15.458 28.719 1.00 13.75 C ANISOU 438 CD2 LEU A 51 2035 1745 1443 -469 500 397 C ATOM 439 N LYS A 52 6.764 15.864 23.506 1.00 7.04 N ANISOU 439 N LYS A 52 892 797 984 0 -13 30 N ATOM 440 CA LYS A 52 6.489 15.526 22.103 1.00 7.69 C ANISOU 440 CA LYS A 52 838 1046 1035 33 -97 -87 C ATOM 441 C LYS A 52 7.352 14.370 21.627 1.00 7.81 C ANISOU 441 C LYS A 52 895 927 1145 10 -108 -104 C ATOM 442 O LYS A 52 6.893 13.495 20.857 1.00 8.68 O ANISOU 442 O LYS A 52 1020 1012 1265 11 -127 -177 O ATOM 443 CB LYS A 52 6.662 16.724 21.200 1.00 8.21 C ANISOU 443 CB LYS A 52 990 1021 1108 103 -32 -54 C ATOM 444 CG LYS A 52 5.484 17.692 21.221 1.00 7.83 C ANISOU 444 CG LYS A 52 986 1034 955 15 -92 -82 C ATOM 445 CD LYS A 52 5.607 18.827 20.226 1.00 10.42 C ANISOU 445 CD LYS A 52 1543 1190 1225 59 -107 24 C ATOM 446 CE LYS A 52 4.417 19.772 20.375 1.00 11.71 C ANISOU 446 CE LYS A 52 1535 1330 1583 108 -460 41 C ATOM 447 NZ LYS A 52 4.444 20.889 19.388 1.00 13.93 N ANISOU 447 NZ LYS A 52 1930 1557 1805 134 -305 168 N ATOM 448 N ASN A 53 8.601 14.325 22.088 1.00 7.70 N ANISOU 448 N ASN A 53 880 909 1137 40 -25 -100 N ATOM 449 CA ASN A 53 9.484 13.265 21.636 1.00 8.23 C ANISOU 449 CA ASN A 53 1007 931 1189 63 -20 5 C ATOM 450 C ASN A 53 9.119 11.907 22.210 1.00 8.88 C ANISOU 450 C ASN A 53 1034 1029 1311 51 -9 -38 C ATOM 451 O ASN A 53 9.456 10.870 21.626 1.00 10.00 O ANISOU 451 O ASN A 53 1221 994 1584 48 56 -94 O ATOM 452 CB ASN A 53 10.939 13.599 21.890 1.00 8.20 C ANISOU 452 CB ASN A 53 956 1012 1148 50 16 -52 C ATOM 453 CG ASN A 53 11.453 14.701 20.980 1.00 8.67 C ANISOU 453 CG ASN A 53 1036 1156 1100 78 -81 136 C ATOM 454 OD1 ASN A 53 10.689 15.316 20.223 1.00 11.67 O ANISOU 454 OD1 ASN A 53 1352 1686 1393 102 -194 71 O ATOM 455 ND2 ASN A 53 12.743 15.001 21.078 1.00 8.35 N ANISOU 455 ND2 ASN A 53 1113 1190 869 68 -136 0 N ATOM 456 N PHE A 54 8.419 11.904 23.334 1.00 8.63 N ANISOU 456 N PHE A 54 1129 872 1278 47 -2 26 N ATOM 457 CA PHE A 54 7.812 10.698 23.892 1.00 10.06 C ANISOU 457 CA PHE A 54 1279 1101 1441 25 -14 95 C ATOM 458 C PHE A 54 6.369 10.488 23.388 1.00 11.15 C ANISOU 458 C PHE A 54 1334 1249 1653 -36 -58 186 C ATOM 459 O PHE A 54 5.708 9.554 23.834 1.00 12.79 O ANISOU 459 O PHE A 54 1430 1332 2094 -137 -115 307 O ATOM 460 CB PHE A 54 7.823 10.776 25.419 1.00 9.29 C ANISOU 460 CB PHE A 54 1085 1023 1420 85 116 71 C ATOM 461 CG PHE A 54 9.136 10.342 26.056 1.00 8.26 C ANISOU 461 CG PHE A 54 1119 1013 1003 54 273 61 C ATOM 462 CD1 PHE A 54 9.343 9.011 26.362 1.00 9.37 C ANISOU 462 CD1 PHE A 54 1243 1181 1135 208 435 -42 C ATOM 463 CD2 PHE A 54 10.131 11.260 26.378 1.00 10.07 C ANISOU 463 CD2 PHE A 54 1180 1305 1341 174 242 193 C ATOM 464 CE1 PHE A 54 10.520 8.601 26.942 1.00 8.86 C ANISOU 464 CE1 PHE A 54 1394 1081 888 201 343 154 C ATOM 465 CE2 PHE A 54 11.316 10.854 26.971 1.00 8.64 C ANISOU 465 CE2 PHE A 54 1167 1382 731 127 365 245 C ATOM 466 CZ PHE A 54 11.498 9.505 27.259 1.00 7.31 C ANISOU 466 CZ PHE A 54 1043 1279 456 366 315 -111 C ATOM 467 N ASN A 55 5.887 11.338 22.478 1.00 10.92 N ANISOU 467 N ASN A 55 1304 1247 1597 -52 -73 2 N ATOM 468 CA ASN A 55 4.559 11.208 21.850 1.00 11.46 C ANISOU 468 CA ASN A 55 1393 1432 1526 -93 -45 -110 C ATOM 469 C ASN A 55 3.426 11.393 22.837 1.00 11.03 C ANISOU 469 C ASN A 55 1354 1365 1472 -189 12 -15 C ATOM 470 O ASN A 55 2.265 11.053 22.536 1.00 11.51 O ANISOU 470 O ASN A 55 1354 1559 1458 -249 -29 94 O ATOM 471 CB ASN A 55 4.463 9.926 21.001 1.00 11.91 C ANISOU 471 CB ASN A 55 1406 1548 1569 -119 -18 -185 C ATOM 472 CG ASN A 55 5.519 9.920 19.916 1.00 14.24 C ANISOU 472 CG ASN A 55 1730 1921 1758 -54 46 -372 C ATOM 473 OD1 ASN A 55 5.533 10.814 19.070 1.00 15.38 O ANISOU 473 OD1 ASN A 55 2151 2392 1299 -169 253 -696 O ATOM 474 ND2 ASN A 55 6.450 8.971 19.978 1.00 16.99 N ANISOU 474 ND2 ASN A 55 1862 2326 2267 124 79 -408 N ATOM 475 N ILE A 56 3.743 11.993 23.978 1.00 11.30 N ANISOU 475 N ILE A 56 1240 1535 1516 -117 1 27 N ATOM 476 CA ILE A 56 2.752 12.375 24.981 1.00 11.33 C ANISOU 476 CA ILE A 56 1392 1453 1458 -164 69 122 C ATOM 477 C ILE A 56 1.961 13.635 24.610 1.00 11.36 C ANISOU 477 C ILE A 56 1285 1504 1524 -111 19 37 C ATOM 478 O ILE A 56 0.824 13.818 25.027 1.00 13.03 O ANISOU 478 O ILE A 56 1476 1862 1611 -43 181 157 O ATOM 479 CB ILE A 56 3.444 12.520 26.344 1.00 12.00 C ANISOU 479 CB ILE A 56 1471 1560 1525 -202 8 194 C ATOM 480 CG1 ILE A 56 3.968 11.174 26.834 1.00 13.89 C ANISOU 480 CG1 ILE A 56 1670 1990 1617 -35 69 318 C ATOM 481 CG2 ILE A 56 2.556 13.155 27.400 1.00 13.38 C ANISOU 481 CG2 ILE A 56 1582 1698 1803 -84 26 181 C ATOM 482 CD1 ILE A 56 4.885 11.315 28.002 1.00 14.84 C ANISOU 482 CD1 ILE A 56 1752 2285 1598 -68 -4 570 C ATOM 483 N LEU A 57 2.594 14.523 23.869 1.00 10.59 N ANISOU 483 N LEU A 57 1241 1359 1421 -147 -41 -17 N ATOM 484 CA LEU A 57 1.900 15.568 23.154 1.00 9.89 C ANISOU 484 CA LEU A 57 1123 1402 1230 -121 -113 2 C ATOM 485 C LEU A 57 2.059 15.225 21.689 1.00 10.25 C ANISOU 485 C LEU A 57 1258 1416 1220 -67 -176 -36 C ATOM 486 O LEU A 57 3.169 14.875 21.274 1.00 11.18 O ANISOU 486 O LEU A 57 1412 1485 1349 -18 -261 -45 O ATOM 487 CB LEU A 57 2.527 16.942 23.413 1.00 10.30 C ANISOU 487 CB LEU A 57 1314 1369 1229 -102 33 40 C ATOM 488 CG LEU A 57 2.364 17.500 24.825 1.00 9.74 C ANISOU 488 CG LEU A 57 991 1459 1249 -110 -7 -47 C ATOM 489 CD1 LEU A 57 3.206 18.740 24.961 1.00 10.93 C ANISOU 489 CD1 LEU A 57 1372 1318 1460 -159 -96 118 C ATOM 490 CD2 LEU A 57 0.911 17.821 25.111 1.00 12.25 C ANISOU 490 CD2 LEU A 57 1356 1660 1637 -50 233 3 C ATOM 491 N ASP A 58 0.982 15.314 20.896 1.00 9.91 N ANISOU 491 N ASP A 58 1180 1404 1179 -30 -203 0 N ATOM 492 CA ASP A 58 1.147 15.171 19.450 1.00 10.62 C ANISOU 492 CA ASP A 58 1379 1430 1227 34 -147 14 C ATOM 493 C ASP A 58 1.685 16.486 18.910 1.00 10.81 C ANISOU 493 C ASP A 58 1426 1342 1339 54 -102 -1 C ATOM 494 O ASP A 58 1.958 17.433 19.666 1.00 10.50 O ANISOU 494 O ASP A 58 1285 1337 1367 -114 -168 85 O ATOM 495 CB ASP A 58 -0.127 14.651 18.725 1.00 11.31 C ANISOU 495 CB ASP A 58 1503 1507 1287 6 -206 23 C ATOM 496 CG ASP A 58 -1.203 15.709 18.509 1.00 11.92 C ANISOU 496 CG ASP A 58 1661 1499 1367 -109 -177 -40 C ATOM 497 OD1 ASP A 58 -1.039 16.880 18.871 1.00 11.85 O ANISOU 497 OD1 ASP A 58 1486 1393 1621 81 -341 10 O ATOM 498 OD2 ASP A 58 -2.251 15.335 17.926 1.00 14.63 O ANISOU 498 OD2 ASP A 58 1658 1745 2153 -250 -273 74 O ATOM 499 N LYS A 59 1.913 16.542 17.605 1.00 11.36 N ANISOU 499 N LYS A 59 1548 1412 1354 43 -105 8 N ATOM 500 CA LYS A 59 2.548 17.709 17.005 1.00 12.34 C ANISOU 500 CA LYS A 59 1639 1528 1522 10 -54 55 C ATOM 501 C LYS A 59 1.726 18.990 17.181 1.00 12.36 C ANISOU 501 C LYS A 59 1548 1503 1641 -34 -13 58 C ATOM 502 O LYS A 59 2.293 20.072 17.144 1.00 13.77 O ANISOU 502 O LYS A 59 1714 1573 1943 -107 20 49 O ATOM 503 CB LYS A 59 2.857 17.446 15.525 1.00 13.46 C ANISOU 503 CB LYS A 59 1902 1628 1584 -4 -15 67 C ATOM 504 CG LYS A 59 1.630 17.335 14.638 1.00 14.85 C ANISOU 504 CG LYS A 59 2170 1813 1658 1 -19 106 C ATOM 505 CD LYS A 59 2.015 16.989 13.200 1.00 18.48 C ANISOU 505 CD LYS A 59 2844 2214 1962 39 73 32 C ATOM 506 CE LYS A 59 0.784 16.838 12.331 1.00 20.52 C ANISOU 506 CE LYS A 59 2970 2447 2377 -65 -30 89 C ATOM 507 NZ LYS A 59 1.101 16.585 10.886 1.00 22.60 N ANISOU 507 NZ LYS A 59 3590 2518 2476 -197 -26 -155 N ATOM 508 N ASN A 60 0.411 18.850 17.368 1.00 12.37 N ANISOU 508 N ASN A 60 1468 1519 1712 19 -58 60 N ATOM 509 CA ASN A 60 -0.510 19.961 17.640 1.00 12.58 C ANISOU 509 CA ASN A 60 1515 1550 1716 59 -62 66 C ATOM 510 C ASN A 60 -0.827 20.165 19.115 1.00 12.98 C ANISOU 510 C ASN A 60 1499 1625 1805 64 -41 28 C ATOM 511 O ASN A 60 -1.793 20.852 19.456 1.00 13.88 O ANISOU 511 O ASN A 60 1575 1805 1890 128 67 13 O ATOM 512 CB ASN A 60 -1.824 19.744 16.876 1.00 12.82 C ANISOU 512 CB ASN A 60 1561 1568 1739 106 -84 69 C ATOM 513 CG ASN A 60 -1.636 19.688 15.359 1.00 14.64 C ANISOU 513 CG ASN A 60 1919 1787 1855 65 -156 -85 C ATOM 514 OD1 ASN A 60 -2.278 18.876 14.670 1.00 17.37 O ANISOU 514 OD1 ASN A 60 2441 2224 1934 124 -346 -364 O ATOM 515 ND2 ASN A 60 -0.797 20.557 14.833 1.00 14.85 N ANISOU 515 ND2 ASN A 60 1891 2080 1670 205 -368 285 N ATOM 516 N ASN A 61 0.002 19.590 19.989 1.00 12.60 N ANISOU 516 N ASN A 61 1456 1572 1758 28 -25 11 N ATOM 517 CA ASN A 61 -0.110 19.741 21.456 1.00 12.89 C ANISOU 517 CA ASN A 61 1487 1657 1751 -16 5 20 C ATOM 518 C ASN A 61 -1.351 19.096 22.041 1.00 14.06 C ANISOU 518 C ASN A 61 1660 1872 1807 -104 89 -45 C ATOM 519 O ASN A 61 -1.772 19.458 23.136 1.00 15.46 O ANISOU 519 O ASN A 61 1861 2164 1847 -258 296 -56 O ATOM 520 CB ASN A 61 0.037 21.203 21.919 1.00 13.15 C ANISOU 520 CB ASN A 61 1555 1704 1736 50 43 -55 C ATOM 521 CG ASN A 61 1.426 21.727 21.704 1.00 12.30 C ANISOU 521 CG ASN A 61 1502 1543 1626 123 15 27 C ATOM 522 OD1 ASN A 61 2.213 21.844 22.655 1.00 15.68 O ANISOU 522 OD1 ASN A 61 1763 2073 2119 -14 -14 -296 O ATOM 523 ND2 ASN A 61 1.770 22.001 20.452 1.00 12.59 N ANISOU 523 ND2 ASN A 61 1696 1502 1586 -73 18 -163 N ATOM 524 N VAL A 62 -1.888 18.092 21.354 1.00 13.99 N ANISOU 524 N VAL A 62 1608 1899 1806 -153 77 -21 N ATOM 525 CA VAL A 62 -2.945 17.277 21.928 1.00 14.24 C ANISOU 525 CA VAL A 62 1644 1894 1871 -123 35 15 C ATOM 526 C VAL A 62 -2.294 16.318 22.917 1.00 14.18 C ANISOU 526 C VAL A 62 1679 1886 1821 -83 57 50 C ATOM 527 O VAL A 62 -1.339 15.584 22.591 1.00 13.35 O ANISOU 527 O VAL A 62 1563 1777 1729 -54 -112 81 O ATOM 528 CB VAL A 62 -3.749 16.506 20.869 1.00 13.76 C ANISOU 528 CB VAL A 62 1473 1951 1802 -161 -15 -2 C ATOM 529 CG1 VAL A 62 -4.828 15.627 21.528 1.00 14.49 C ANISOU 529 CG1 VAL A 62 1485 2090 1931 -114 183 136 C ATOM 530 CG2 VAL A 62 -4.390 17.489 19.870 1.00 14.43 C ANISOU 530 CG2 VAL A 62 1494 1973 2013 155 -21 8 C ATOM 531 N PHE A 63 -2.790 16.366 24.147 1.00 15.02 N ANISOU 531 N PHE A 63 1876 1940 1891 -17 90 88 N ATOM 532 CA PHE A 63 -2.238 15.606 25.248 1.00 15.92 C ANISOU 532 CA PHE A 63 1958 2049 2038 -64 -5 20 C ATOM 533 C PHE A 63 -2.788 14.166 25.250 1.00 15.19 C ANISOU 533 C PHE A 63 1766 1994 2010 -138 66 -3 C ATOM 534 O PHE A 63 -4.003 13.944 25.109 1.00 15.72 O ANISOU 534 O PHE A 63 1709 2179 2084 -168 60 35 O ATOM 535 CB PHE A 63 -2.544 16.335 26.555 1.00 16.60 C ANISOU 535 CB PHE A 63 2062 2078 2167 -122 73 -39 C ATOM 536 CG PHE A 63 -2.209 15.550 27.778 1.00 19.24 C ANISOU 536 CG PHE A 63 2536 2301 2472 -86 -63 28 C ATOM 537 CD1 PHE A 63 -0.908 15.186 28.050 1.00 21.42 C ANISOU 537 CD1 PHE A 63 2759 2716 2661 -107 -86 16 C ATOM 538 CD2 PHE A 63 -3.200 15.172 28.663 1.00 22.00 C ANISOU 538 CD2 PHE A 63 2875 2792 2691 -6 72 11 C ATOM 539 CE1 PHE A 63 -0.601 14.463 29.183 1.00 23.48 C ANISOU 539 CE1 PHE A 63 3170 2802 2948 -113 -33 139 C ATOM 540 CE2 PHE A 63 -2.898 14.445 29.784 1.00 23.81 C ANISOU 540 CE2 PHE A 63 3161 2985 2898 -18 36 98 C ATOM 541 CZ PHE A 63 -1.602 14.098 30.052 1.00 23.61 C ANISOU 541 CZ PHE A 63 3119 3032 2819 -3 28 9 C ATOM 542 N LYS A 64 -1.886 13.200 25.433 1.00 14.54 N ANISOU 542 N LYS A 64 1672 1888 1965 -183 38 36 N ATOM 543 CA LYS A 64 -2.175 11.765 25.401 1.00 15.96 C ANISOU 543 CA LYS A 64 1928 1993 2141 -120 6 -43 C ATOM 544 C LYS A 64 -1.780 11.121 26.737 1.00 16.36 C ANISOU 544 C LYS A 64 1901 2106 2209 -128 -59 -82 C ATOM 545 O LYS A 64 -0.627 10.703 26.925 1.00 16.55 O ANISOU 545 O LYS A 64 1806 1991 2489 -130 -99 -259 O ATOM 546 CB LYS A 64 -1.349 11.084 24.314 1.00 16.21 C ANISOU 546 CB LYS A 64 2004 2067 2086 -76 1 -8 C ATOM 547 CG LYS A 64 -1.397 11.726 22.958 1.00 18.18 C ANISOU 547 CG LYS A 64 2392 2269 2245 10 57 -64 C ATOM 548 CD LYS A 64 -2.721 11.490 22.288 1.00 17.83 C ANISOU 548 CD LYS A 64 2195 2343 2236 46 183 -133 C ATOM 549 CE LYS A 64 -2.710 12.099 20.881 1.00 16.36 C ANISOU 549 CE LYS A 64 2087 2155 1973 1 132 -383 C ATOM 550 NZ LYS A 64 -2.005 11.294 19.818 1.00 15.88 N ANISOU 550 NZ LYS A 64 1895 2057 2081 355 210 -300 N ATOM 551 N PRO A 65 -2.731 10.988 27.670 1.00 18.04 N ANISOU 551 N PRO A 65 2187 2386 2281 -38 -3 -24 N ATOM 552 CA PRO A 65 -2.420 10.371 28.973 1.00 18.62 C ANISOU 552 CA PRO A 65 2281 2477 2317 -41 -39 -1 C ATOM 553 C PRO A 65 -1.771 8.976 28.923 1.00 18.72 C ANISOU 553 C PRO A 65 2295 2521 2295 -31 -56 -27 C ATOM 554 O PRO A 65 -0.950 8.658 29.774 1.00 18.86 O ANISOU 554 O PRO A 65 2199 2703 2262 -23 -115 -31 O ATOM 555 CB PRO A 65 -3.782 10.290 29.666 1.00 19.45 C ANISOU 555 CB PRO A 65 2385 2574 2429 10 -14 10 C ATOM 556 CG PRO A 65 -4.646 11.289 28.969 1.00 19.59 C ANISOU 556 CG PRO A 65 2459 2556 2429 16 -3 46 C ATOM 557 CD PRO A 65 -4.130 11.446 27.579 1.00 18.13 C ANISOU 557 CD PRO A 65 2169 2434 2285 -14 -40 1 C ATOM 558 N GLN A 66 -2.131 8.146 27.948 1.00 18.38 N ANISOU 558 N GLN A 66 2300 2401 2283 -74 -94 -60 N ATOM 559 CA GLN A 66 -1.547 6.804 27.831 1.00 18.58 C ANISOU 559 CA GLN A 66 2393 2376 2289 -34 -101 -37 C ATOM 560 C GLN A 66 -0.025 6.817 27.663 1.00 17.25 C ANISOU 560 C GLN A 66 2298 2152 2101 -19 -91 -61 C ATOM 561 O GLN A 66 0.653 5.892 28.103 1.00 17.37 O ANISOU 561 O GLN A 66 2490 2023 2087 19 -180 -70 O ATOM 562 CB GLN A 66 -2.199 6.029 26.671 1.00 19.53 C ANISOU 562 CB GLN A 66 2534 2452 2432 -31 -125 -68 C ATOM 563 CG GLN A 66 -1.844 4.522 26.609 1.00 22.98 C ANISOU 563 CG GLN A 66 2979 2738 3015 99 -6 -57 C ATOM 564 CD GLN A 66 -2.383 3.724 27.786 1.00 24.75 C ANISOU 564 CD GLN A 66 3283 2962 3158 85 -22 -46 C ATOM 565 OE1 GLN A 66 -3.575 3.773 28.093 1.00 28.47 O ANISOU 565 OE1 GLN A 66 3393 3621 3802 190 14 -179 O ATOM 566 NE2 GLN A 66 -1.512 2.969 28.438 1.00 25.15 N ANISOU 566 NE2 GLN A 66 3181 3034 3337 194 -239 -394 N ATOM 567 N GLY A 67 0.515 7.869 27.047 1.00 15.40 N ANISOU 567 N GLY A 67 2160 2016 1673 30 -92 -6 N ATOM 568 CA GLY A 67 1.950 8.015 26.893 1.00 15.06 C ANISOU 568 CA GLY A 67 2115 1944 1660 84 71 62 C ATOM 569 C GLY A 67 2.630 8.174 28.227 1.00 14.68 C ANISOU 569 C GLY A 67 1975 1960 1643 61 112 95 C ATOM 570 O GLY A 67 3.733 7.681 28.427 1.00 15.71 O ANISOU 570 O GLY A 67 2200 2133 1637 247 278 113 O ATOM 571 N ILE A 68 1.989 8.899 29.142 1.00 13.27 N ANISOU 571 N ILE A 68 1799 1641 1602 62 45 58 N ATOM 572 CA ILE A 68 2.531 9.040 30.482 1.00 13.26 C ANISOU 572 CA ILE A 68 1767 1695 1573 35 -55 5 C ATOM 573 C ILE A 68 2.484 7.703 31.208 1.00 12.37 C ANISOU 573 C ILE A 68 1676 1631 1392 -3 -65 -1 C ATOM 574 O ILE A 68 3.449 7.324 31.846 1.00 11.35 O ANISOU 574 O ILE A 68 1497 1346 1467 30 -81 52 O ATOM 575 CB ILE A 68 1.770 10.091 31.314 1.00 14.13 C ANISOU 575 CB ILE A 68 1890 1858 1617 110 -188 -129 C ATOM 576 CG1 ILE A 68 1.998 11.485 30.759 1.00 16.50 C ANISOU 576 CG1 ILE A 68 2319 2114 1835 247 -99 -48 C ATOM 577 CG2 ILE A 68 2.250 10.082 32.764 1.00 16.12 C ANISOU 577 CG2 ILE A 68 2067 2245 1812 211 -335 -65 C ATOM 578 CD1 ILE A 68 1.215 12.576 31.517 1.00 18.54 C ANISOU 578 CD1 ILE A 68 2514 2282 2248 560 -94 -221 C ATOM 579 N LYS A 69 1.370 6.984 31.091 1.00 13.10 N ANISOU 579 N LYS A 69 1757 1703 1514 -37 -4 158 N ATOM 580 CA LYS A 69 1.246 5.675 31.742 1.00 14.28 C ANISOU 580 CA LYS A 69 1893 1797 1736 -90 8 148 C ATOM 581 C LYS A 69 2.329 4.710 31.296 1.00 14.39 C ANISOU 581 C LYS A 69 1899 1780 1789 -93 -75 116 C ATOM 582 O LYS A 69 2.926 4.016 32.134 1.00 14.96 O ANISOU 582 O LYS A 69 2005 1757 1918 -93 -189 215 O ATOM 583 CB LYS A 69 -0.099 5.039 31.443 1.00 15.02 C ANISOU 583 CB LYS A 69 1970 1903 1834 -146 74 159 C ATOM 584 CG LYS A 69 -1.288 5.784 31.975 1.00 18.42 C ANISOU 584 CG LYS A 69 2360 2235 2401 54 84 -11 C ATOM 585 CD LYS A 69 -2.557 4.908 31.905 1.00 22.61 C ANISOU 585 CD LYS A 69 2746 2783 3062 -136 91 -92 C ATOM 586 CE LYS A 69 -3.747 5.706 31.376 1.00 25.08 C ANISOU 586 CE LYS A 69 3046 3092 3389 -29 25 -78 C ATOM 587 NZ LYS A 69 -4.957 4.868 31.145 1.00 26.94 N ANISOU 587 NZ LYS A 69 3133 3378 3723 -56 5 -104 N ATOM 588 N ALA A 70 2.593 4.664 29.995 1.00 15.48 N ANISOU 588 N ALA A 70 2021 1930 1930 -28 -138 -52 N ATOM 589 CA ALA A 70 3.579 3.732 29.448 1.00 16.15 C ANISOU 589 CA ALA A 70 2110 2012 2015 32 -87 -69 C ATOM 590 C ALA A 70 4.938 3.917 30.090 1.00 15.77 C ANISOU 590 C ALA A 70 2088 1923 1979 26 -44 -47 C ATOM 591 O ALA A 70 5.597 2.943 30.423 1.00 17.70 O ANISOU 591 O ALA A 70 2272 2149 2301 138 -70 -104 O ATOM 592 CB ALA A 70 3.692 3.887 27.932 1.00 16.88 C ANISOU 592 CB ALA A 70 2196 2180 2037 71 -94 -155 C ATOM 593 N VAL A 71 5.361 5.166 30.260 1.00 13.40 N ANISOU 593 N VAL A 71 1887 1614 1589 25 -47 0 N ATOM 594 CA VAL A 71 6.657 5.440 30.873 1.00 12.13 C ANISOU 594 CA VAL A 71 1684 1500 1425 35 63 117 C ATOM 595 C VAL A 71 6.613 5.228 32.415 1.00 9.78 C ANISOU 595 C VAL A 71 1342 1143 1230 12 -10 110 C ATOM 596 O VAL A 71 7.492 4.575 32.998 1.00 9.82 O ANISOU 596 O VAL A 71 1367 1211 1153 89 -94 91 O ATOM 597 CB VAL A 71 7.179 6.865 30.527 1.00 12.76 C ANISOU 597 CB VAL A 71 1761 1602 1483 70 139 164 C ATOM 598 CG1 VAL A 71 8.472 7.115 31.251 1.00 14.14 C ANISOU 598 CG1 VAL A 71 1819 1701 1853 79 69 310 C ATOM 599 CG2 VAL A 71 7.384 7.035 29.016 1.00 14.94 C ANISOU 599 CG2 VAL A 71 2124 2014 1538 216 259 354 C ATOM 600 N MET A 72 5.606 5.786 33.072 1.00 8.74 N ANISOU 600 N MET A 72 1244 997 1078 -69 -73 157 N ATOM 601 CA MET A 72 5.585 5.815 34.525 1.00 8.81 C ANISOU 601 CA MET A 72 1184 1087 1076 -49 -106 130 C ATOM 602 C MET A 72 5.353 4.447 35.141 1.00 9.44 C ANISOU 602 C MET A 72 1251 1117 1219 0 -120 59 C ATOM 603 O MET A 72 5.786 4.202 36.262 1.00 9.70 O ANISOU 603 O MET A 72 1271 1270 1143 14 -138 110 O ATOM 604 CB MET A 72 4.602 6.865 35.032 1.00 8.73 C ANISOU 604 CB MET A 72 1090 1126 1099 -39 -22 119 C ATOM 605 CG MET A 72 4.921 8.302 34.597 1.00 9.42 C ANISOU 605 CG MET A 72 1312 1198 1066 -31 -102 36 C ATOM 606 SD MET A 72 6.576 8.872 35.027 1.00 11.27 S ANISOU 606 SD MET A 72 1356 1252 1672 54 -208 8 S ATOM 607 CE MET A 72 6.394 8.647 36.732 1.00 11.55 C ANISOU 607 CE MET A 72 923 1968 1495 125 -422 138 C ATOM 608 N GLU A 73 4.701 3.533 34.420 1.00 10.46 N ANISOU 608 N GLU A 73 1407 1123 1444 -54 -142 100 N ATOM 609 CA AGLU A 73 4.509 2.208 35.000 0.50 10.83 C ANISOU 609 CA AGLU A 73 1424 1228 1460 -77 -75 100 C ATOM 610 CA BGLU A 73 4.509 2.119 34.821 0.50 11.08 C ANISOU 610 CA BGLU A 73 1470 1255 1483 -47 -87 110 C ATOM 611 C GLU A 73 5.845 1.430 35.094 1.00 10.46 C ANISOU 611 C GLU A 73 1372 1175 1426 -81 -2 98 C ATOM 612 O GLU A 73 5.910 0.420 35.797 1.00 11.23 O ANISOU 612 O GLU A 73 1483 1245 1539 -64 -10 248 O ATOM 613 CB AGLU A 73 3.399 1.434 34.289 0.50 11.03 C ANISOU 613 CB AGLU A 73 1434 1236 1521 -81 -54 79 C ATOM 614 CB BGLU A 73 3.744 1.310 33.733 0.50 11.52 C ANISOU 614 CB BGLU A 73 1530 1307 1538 -7 -84 120 C ATOM 615 CG AGLU A 73 1.997 1.955 34.622 0.50 12.17 C ANISOU 615 CG AGLU A 73 1488 1431 1704 -103 -128 -91 C ATOM 616 CG BGLU A 73 4.586 0.875 32.517 0.50 13.13 C ANISOU 616 CG BGLU A 73 1748 1651 1590 85 -159 24 C ATOM 617 CD AGLU A 73 0.893 1.180 33.936 0.50 13.51 C ANISOU 617 CD AGLU A 73 1621 1642 1869 -34 -233 -298 C ATOM 618 CD BGLU A 73 3.846 -0.009 31.496 0.50 14.51 C ANISOU 618 CD BGLU A 73 2064 1986 1464 123 -260 21 C ATOM 619 OE1AGLU A 73 -0.269 1.305 34.381 0.50 14.24 O ANISOU 619 OE1AGLU A 73 1762 1686 1962 243 -103 -395 O ATOM 620 OE1BGLU A 73 2.598 -0.035 31.482 0.50 15.60 O ANISOU 620 OE1BGLU A 73 2176 2287 1462 204 -508 43 O ATOM 621 OE2AGLU A 73 1.187 0.451 32.958 0.50 15.79 O ANISOU 621 OE2AGLU A 73 1699 2131 2170 121 -242 -648 O ATOM 622 OE2BGLU A 73 4.540 -0.683 30.703 0.50 14.95 O ANISOU 622 OE2BGLU A 73 2064 2233 1380 320 -544 8 O ATOM 623 N LEU A 74 6.922 1.933 34.481 1.00 10.76 N ANISOU 623 N LEU A 74 1469 1285 1332 -30 13 -15 N ATOM 624 CA LEU A 74 8.243 1.364 34.694 1.00 10.52 C ANISOU 624 CA LEU A 74 1463 1186 1348 -6 34 -38 C ATOM 625 C LEU A 74 8.872 1.798 36.023 1.00 10.97 C ANISOU 625 C LEU A 74 1420 1298 1447 2 -63 -17 C ATOM 626 O LEU A 74 9.840 1.197 36.487 1.00 11.40 O ANISOU 626 O LEU A 74 1464 1250 1615 138 -41 -66 O ATOM 627 CB LEU A 74 9.183 1.776 33.559 1.00 11.71 C ANISOU 627 CB LEU A 74 1624 1265 1558 7 80 -20 C ATOM 628 CG LEU A 74 8.747 1.470 32.135 1.00 14.37 C ANISOU 628 CG LEU A 74 2085 1611 1762 -59 41 -28 C ATOM 629 CD1 LEU A 74 9.796 2.014 31.160 1.00 15.08 C ANISOU 629 CD1 LEU A 74 2251 1610 1866 -147 209 -37 C ATOM 630 CD2 LEU A 74 8.548 -0.023 31.929 1.00 15.47 C ANISOU 630 CD2 LEU A 74 2414 1593 1872 -144 53 -179 C ATOM 631 N LEU A 75 8.334 2.863 36.615 1.00 9.39 N ANISOU 631 N LEU A 75 1124 1103 1338 -50 24 9 N ATOM 632 CA LEU A 75 8.958 3.566 37.739 1.00 9.27 C ANISOU 632 CA LEU A 75 1168 1169 1184 -6 67 12 C ATOM 633 C LEU A 75 8.191 3.510 39.052 1.00 9.77 C ANISOU 633 C LEU A 75 1239 1206 1265 -59 49 83 C ATOM 634 O LEU A 75 8.806 3.549 40.108 1.00 11.77 O ANISOU 634 O LEU A 75 1488 1674 1310 -40 -11 34 O ATOM 635 CB LEU A 75 9.137 5.028 37.347 1.00 8.71 C ANISOU 635 CB LEU A 75 1066 1121 1121 -30 106 -42 C ATOM 636 CG LEU A 75 10.002 5.269 36.106 1.00 9.26 C ANISOU 636 CG LEU A 75 1331 1092 1095 0 8 -67 C ATOM 637 CD1 LEU A 75 9.994 6.721 35.711 1.00 10.01 C ANISOU 637 CD1 LEU A 75 1416 1011 1375 10 216 -14 C ATOM 638 CD2 LEU A 75 11.413 4.783 36.350 1.00 10.52 C ANISOU 638 CD2 LEU A 75 1230 1447 1317 120 188 155 C ATOM 639 N ILE A 76 6.868 3.483 39.001 1.00 9.38 N ANISOU 639 N ILE A 76 1249 1111 1203 -63 66 125 N ATOM 640 CA ILE A 76 6.048 3.508 40.208 1.00 9.51 C ANISOU 640 CA ILE A 76 1221 1098 1292 -5 118 156 C ATOM 641 C ILE A 76 4.940 2.508 40.015 1.00 9.02 C ANISOU 641 C ILE A 76 1220 1018 1188 20 116 182 C ATOM 642 O ILE A 76 4.664 2.051 38.915 1.00 9.25 O ANISOU 642 O ILE A 76 1211 1002 1299 -16 136 106 O ATOM 643 CB ILE A 76 5.496 4.938 40.502 1.00 10.30 C ANISOU 643 CB ILE A 76 1346 1202 1365 -66 173 42 C ATOM 644 CG1 ILE A 76 4.546 5.419 39.410 1.00 11.17 C ANISOU 644 CG1 ILE A 76 1529 1133 1581 20 254 91 C ATOM 645 CG2 ILE A 76 6.640 5.923 40.673 1.00 12.14 C ANISOU 645 CG2 ILE A 76 1473 1232 1906 -178 179 41 C ATOM 646 CD1 ILE A 76 3.994 6.817 39.635 1.00 14.08 C ANISOU 646 CD1 ILE A 76 2087 1334 1927 303 463 121 C ATOM 647 N ASP A 77 4.273 2.184 41.107 1.00 8.80 N ANISOU 647 N ASP A 77 1152 1125 1067 12 85 200 N ATOM 648 CA ASP A 77 3.247 1.153 41.090 1.00 9.52 C ANISOU 648 CA ASP A 77 1261 1091 1265 -3 92 182 C ATOM 649 C ASP A 77 2.011 1.574 40.270 1.00 9.22 C ANISOU 649 C ASP A 77 1274 1099 1127 42 188 210 C ATOM 650 O ASP A 77 1.741 2.759 40.085 1.00 8.98 O ANISOU 650 O ASP A 77 1195 967 1249 60 252 216 O ATOM 651 CB ASP A 77 2.848 0.809 42.525 1.00 9.25 C ANISOU 651 CB ASP A 77 1243 1050 1220 37 24 365 C ATOM 652 CG ASP A 77 2.118 1.942 43.196 1.00 9.66 C ANISOU 652 CG ASP A 77 1360 1162 1145 17 29 251 C ATOM 653 OD1 ASP A 77 2.782 2.857 43.708 1.00 10.43 O ANISOU 653 OD1 ASP A 77 1612 1155 1192 -68 -175 512 O ATOM 654 OD2 ASP A 77 0.873 1.920 43.198 1.00 9.71 O ANISOU 654 OD2 ASP A 77 1186 1109 1392 37 15 487 O ATOM 655 N GLU A 78 1.237 0.593 39.825 1.00 9.59 N ANISOU 655 N GLU A 78 1350 1108 1183 75 88 144 N ATOM 656 CA GLU A 78 0.119 0.811 38.914 1.00 10.72 C ANISOU 656 CA GLU A 78 1400 1308 1365 54 49 117 C ATOM 657 C GLU A 78 -0.903 1.802 39.475 1.00 9.31 C ANISOU 657 C GLU A 78 1321 1140 1074 73 72 117 C ATOM 658 O GLU A 78 -1.379 2.684 38.754 1.00 9.61 O ANISOU 658 O GLU A 78 1394 1190 1067 258 -61 139 O ATOM 659 CB GLU A 78 -0.556 -0.528 38.592 1.00 12.88 C ANISOU 659 CB GLU A 78 1597 1591 1706 73 -39 -60 C ATOM 660 CG GLU A 78 -1.654 -0.448 37.562 1.00 17.43 C ANISOU 660 CG GLU A 78 2087 2237 2295 68 -224 -63 C ATOM 661 CD GLU A 78 -2.439 -1.748 37.444 1.00 23.65 C ANISOU 661 CD GLU A 78 2950 2681 3352 -87 -418 -204 C ATOM 662 OE1 GLU A 78 -1.904 -2.816 37.820 1.00 28.25 O ANISOU 662 OE1 GLU A 78 3558 3033 4139 143 -541 -216 O ATOM 663 OE2 GLU A 78 -3.601 -1.694 36.991 1.00 28.47 O ANISOU 663 OE2 GLU A 78 3329 3377 4109 -51 -745 -351 O ATOM 664 N ASN A 79 -1.265 1.673 40.738 1.00 7.78 N ANISOU 664 N ASN A 79 1110 940 905 80 82 103 N ATOM 665 CA ASN A 79 -2.260 2.578 41.277 1.00 7.74 C ANISOU 665 CA ASN A 79 1063 937 940 10 45 58 C ATOM 666 C ASN A 79 -1.747 4.003 41.355 1.00 7.87 C ANISOU 666 C ASN A 79 1077 1022 890 18 70 102 C ATOM 667 O ASN A 79 -2.505 4.933 41.135 1.00 7.93 O ANISOU 667 O ASN A 79 945 1077 991 100 0 280 O ATOM 668 CB ASN A 79 -2.772 2.105 42.630 1.00 7.31 C ANISOU 668 CB ASN A 79 1040 859 876 -116 48 79 C ATOM 669 CG ASN A 79 -3.482 0.758 42.557 1.00 8.14 C ANISOU 669 CG ASN A 79 1111 1005 976 -274 -126 -227 C ATOM 670 OD1 ASN A 79 -4.010 0.369 41.513 1.00 12.35 O ANISOU 670 OD1 ASN A 79 1703 1762 1227 -496 -236 -215 O ATOM 671 ND2 ASN A 79 -3.460 0.033 43.652 1.00 8.89 N ANISOU 671 ND2 ASN A 79 1327 920 1129 -164 34 -94 N ATOM 672 N SER A 80 -0.472 4.174 41.684 1.00 7.26 N ANISOU 672 N SER A 80 1011 940 804 -6 46 157 N ATOM 673 CA SER A 80 0.134 5.496 41.708 1.00 7.63 C ANISOU 673 CA SER A 80 992 1010 895 -72 -3 160 C ATOM 674 C SER A 80 0.130 6.112 40.318 1.00 7.74 C ANISOU 674 C SER A 80 1082 971 889 7 -68 79 C ATOM 675 O SER A 80 -0.081 7.307 40.186 1.00 8.27 O ANISOU 675 O SER A 80 1228 935 979 -33 -175 270 O ATOM 676 CB SER A 80 1.553 5.457 42.292 1.00 7.81 C ANISOU 676 CB SER A 80 995 1014 956 -38 41 246 C ATOM 677 OG SER A 80 1.511 5.110 43.673 1.00 8.08 O ANISOU 677 OG SER A 80 1153 1088 827 -284 37 375 O ATOM 678 N VAL A 81 0.375 5.319 39.281 1.00 8.29 N ANISOU 678 N VAL A 81 1085 1138 927 -121 26 94 N ATOM 679 CA VAL A 81 0.311 5.831 37.902 1.00 9.41 C ANISOU 679 CA VAL A 81 1245 1340 989 -60 -47 30 C ATOM 680 C VAL A 81 -1.105 6.339 37.585 1.00 8.44 C ANISOU 680 C VAL A 81 1115 1214 876 -73 59 55 C ATOM 681 O VAL A 81 -1.276 7.413 37.002 1.00 8.44 O ANISOU 681 O VAL A 81 1129 1171 907 -31 -50 33 O ATOM 682 CB VAL A 81 0.750 4.764 36.873 1.00 9.30 C ANISOU 682 CB VAL A 81 1104 1560 869 10 162 98 C ATOM 683 CG1 VAL A 81 0.558 5.274 35.459 1.00 11.60 C ANISOU 683 CG1 VAL A 81 1483 1864 1058 144 169 97 C ATOM 684 CG2 VAL A 81 2.188 4.345 37.103 1.00 11.84 C ANISOU 684 CG2 VAL A 81 1123 1980 1392 129 141 303 C ATOM 685 N LYS A 82 -2.125 5.575 37.970 1.00 8.76 N ANISOU 685 N LYS A 82 1142 1134 1052 -74 37 55 N ATOM 686 CA LYS A 82 -3.513 6.044 37.776 1.00 10.41 C ANISOU 686 CA LYS A 82 1309 1416 1227 -26 15 129 C ATOM 687 C LYS A 82 -3.761 7.377 38.483 1.00 9.99 C ANISOU 687 C LYS A 82 1148 1412 1233 29 35 112 C ATOM 688 O LYS A 82 -4.389 8.292 37.937 1.00 9.67 O ANISOU 688 O LYS A 82 1014 1498 1161 -44 -38 62 O ATOM 689 CB LYS A 82 -4.507 5.012 38.300 1.00 12.09 C ANISOU 689 CB LYS A 82 1459 1671 1460 -51 125 126 C ATOM 690 CG LYS A 82 -4.589 3.714 37.520 1.00 18.39 C ANISOU 690 CG LYS A 82 2359 2225 2402 74 62 -27 C ATOM 691 CD LYS A 82 -5.658 2.822 38.159 1.00 23.88 C ANISOU 691 CD LYS A 82 2909 2862 3301 -175 78 17 C ATOM 692 CE LYS A 82 -5.692 1.402 37.596 1.00 27.75 C ANISOU 692 CE LYS A 82 3513 3211 3819 -47 63 -49 C ATOM 693 NZ LYS A 82 -6.521 0.513 38.471 1.00 30.46 N ANISOU 693 NZ LYS A 82 3746 3657 4167 -85 182 99 N ATOM 694 N GLN A 83 -3.255 7.491 39.719 1.00 9.82 N ANISOU 694 N GLN A 83 1264 1359 1105 58 89 57 N ATOM 695 CA GLN A 83 -3.357 8.727 40.515 1.00 10.65 C ANISOU 695 CA GLN A 83 1357 1418 1269 4 143 -14 C ATOM 696 C GLN A 83 -2.674 9.887 39.871 1.00 9.69 C ANISOU 696 C GLN A 83 1329 1334 1018 74 -6 -81 C ATOM 697 O GLN A 83 -3.217 10.984 39.833 1.00 10.47 O ANISOU 697 O GLN A 83 1255 1350 1373 90 -88 -137 O ATOM 698 CB GLN A 83 -2.785 8.520 41.934 1.00 11.92 C ANISOU 698 CB GLN A 83 1511 1627 1392 -5 165 -97 C ATOM 699 CG GLN A 83 -3.608 7.590 42.816 1.00 11.92 C ANISOU 699 CG GLN A 83 1467 1710 1352 -353 207 -159 C ATOM 700 CD GLN A 83 -4.965 8.150 43.172 1.00 14.16 C ANISOU 700 CD GLN A 83 1790 1838 1752 -174 424 -357 C ATOM 701 OE1 GLN A 83 -5.126 9.352 43.354 1.00 16.84 O ANISOU 701 OE1 GLN A 83 1998 1960 2439 -186 971 -677 O ATOM 702 NE2 GLN A 83 -5.960 7.276 43.249 1.00 14.09 N ANISOU 702 NE2 GLN A 83 1941 2098 1315 -446 508 -105 N ATOM 703 N LEU A 84 -1.479 9.637 39.357 1.00 9.74 N ANISOU 703 N LEU A 84 1211 1228 1259 114 -87 -296 N ATOM 704 CA LEU A 84 -0.728 10.628 38.620 1.00 10.31 C ANISOU 704 CA LEU A 84 1344 1181 1392 43 -52 -241 C ATOM 705 C LEU A 84 -1.514 11.123 37.422 1.00 10.19 C ANISOU 705 C LEU A 84 1315 1163 1391 -22 38 -93 C ATOM 706 O LEU A 84 -1.629 12.321 37.205 1.00 11.34 O ANISOU 706 O LEU A 84 1306 1230 1770 -1 44 -41 O ATOM 707 CB LEU A 84 0.616 10.035 38.147 1.00 10.11 C ANISOU 707 CB LEU A 84 1215 1256 1367 -45 -120 -276 C ATOM 708 CG LEU A 84 1.562 10.888 37.289 1.00 11.64 C ANISOU 708 CG LEU A 84 1354 1378 1688 -65 95 -443 C ATOM 709 CD1 LEU A 84 2.945 10.257 37.286 1.00 13.22 C ANISOU 709 CD1 LEU A 84 1251 1734 2036 -76 391 -761 C ATOM 710 CD2 LEU A 84 1.090 11.067 35.885 1.00 12.55 C ANISOU 710 CD2 LEU A 84 1606 1519 1643 -344 290 -160 C ATOM 711 N VAL A 85 -2.071 10.202 36.643 1.00 9.92 N ANISOU 711 N VAL A 85 1275 1177 1316 -47 -10 -21 N ATOM 712 CA VAL A 85 -2.806 10.589 35.462 1.00 10.26 C ANISOU 712 CA VAL A 85 1406 1302 1191 -193 17 94 C ATOM 713 C VAL A 85 -4.018 11.436 35.847 1.00 10.52 C ANISOU 713 C VAL A 85 1436 1342 1217 -96 -78 131 C ATOM 714 O VAL A 85 -4.253 12.482 35.237 1.00 11.61 O ANISOU 714 O VAL A 85 1472 1337 1600 -83 -15 266 O ATOM 715 CB VAL A 85 -3.210 9.361 34.619 1.00 10.59 C ANISOU 715 CB VAL A 85 1508 1423 1092 -124 -72 6 C ATOM 716 CG1 VAL A 85 -4.212 9.728 33.532 1.00 13.33 C ANISOU 716 CG1 VAL A 85 1752 1923 1386 -195 -178 21 C ATOM 717 CG2 VAL A 85 -1.987 8.727 33.992 1.00 12.09 C ANISOU 717 CG2 VAL A 85 1753 1591 1247 -177 110 -47 C ATOM 718 N SER A 86 -4.745 11.051 36.891 1.00 10.96 N ANISOU 718 N SER A 86 1429 1431 1303 -34 -121 127 N ATOM 719 CA SER A 86 -5.895 11.838 37.312 1.00 11.72 C ANISOU 719 CA SER A 86 1481 1561 1409 38 -86 94 C ATOM 720 C SER A 86 -5.464 13.220 37.822 1.00 11.91 C ANISOU 720 C SER A 86 1483 1504 1537 124 -96 73 C ATOM 721 O SER A 86 -6.141 14.230 37.583 1.00 14.40 O ANISOU 721 O SER A 86 1715 1719 2036 266 -218 90 O ATOM 722 CB SER A 86 -6.660 11.095 38.385 1.00 12.49 C ANISOU 722 CB SER A 86 1658 1596 1490 -29 -55 86 C ATOM 723 OG SER A 86 -7.206 9.904 37.858 1.00 15.72 O ANISOU 723 OG SER A 86 2034 2120 1816 -168 -30 -81 O ATOM 724 N ASP A 87 -4.337 13.264 38.521 1.00 11.01 N ANISOU 724 N ASP A 87 1344 1381 1456 75 39 97 N ATOM 725 CA ASP A 87 -3.799 14.498 39.083 1.00 11.11 C ANISOU 725 CA ASP A 87 1350 1422 1448 97 42 26 C ATOM 726 C ASP A 87 -3.343 15.473 37.994 1.00 11.48 C ANISOU 726 C ASP A 87 1518 1351 1491 193 34 95 C ATOM 727 O ASP A 87 -3.589 16.687 38.088 1.00 13.83 O ANISOU 727 O ASP A 87 2003 1467 1785 227 187 161 O ATOM 728 CB ASP A 87 -2.613 14.141 40.006 1.00 10.40 C ANISOU 728 CB ASP A 87 1307 1276 1369 64 36 -7 C ATOM 729 CG ASP A 87 -2.095 15.317 40.842 1.00 10.37 C ANISOU 729 CG ASP A 87 1486 1221 1232 130 7 -13 C ATOM 730 OD1 ASP A 87 -2.779 16.349 40.990 1.00 15.90 O ANISOU 730 OD1 ASP A 87 2064 1769 2207 435 -313 -183 O ATOM 731 OD2 ASP A 87 -0.963 15.167 41.364 1.00 9.80 O ANISOU 731 OD2 ASP A 87 1405 1205 1111 33 122 14 O ATOM 732 N CYS A 88 -2.673 14.955 36.965 1.00 11.95 N ANISOU 732 N CYS A 88 1514 1431 1595 -58 149 84 N ATOM 733 CA CYS A 88 -1.944 15.789 36.009 1.00 11.63 C ANISOU 733 CA CYS A 88 1514 1453 1449 -11 77 117 C ATOM 734 C CYS A 88 -2.566 15.932 34.622 1.00 12.85 C ANISOU 734 C CYS A 88 1671 1588 1622 -16 41 147 C ATOM 735 O CYS A 88 -2.007 16.676 33.797 1.00 14.95 O ANISOU 735 O CYS A 88 1862 1886 1932 56 30 349 O ATOM 736 CB CYS A 88 -0.532 15.224 35.820 1.00 10.92 C ANISOU 736 CB CYS A 88 1558 1355 1234 -139 204 69 C ATOM 737 SG CYS A 88 0.498 15.108 37.289 1.00 10.56 S ANISOU 737 SG CYS A 88 1330 1416 1264 4 -76 188 S ATOM 738 N SER A 89 -3.710 15.292 34.335 1.00 13.80 N ANISOU 738 N SER A 89 1711 1686 1843 39 -21 77 N ATOM 739 CA ASER A 89 -4.190 15.250 32.932 0.50 14.45 C ANISOU 739 CA ASER A 89 1805 1798 1885 37 0 48 C ATOM 740 CA BSER A 89 -4.261 15.207 32.956 0.50 13.86 C ANISOU 740 CA BSER A 89 1767 1713 1786 57 -19 57 C ATOM 741 C SER A 89 -5.064 16.416 32.453 1.00 14.20 C ANISOU 741 C SER A 89 1790 1779 1823 46 -9 39 C ATOM 742 O SER A 89 -5.323 16.540 31.252 1.00 14.86 O ANISOU 742 O SER A 89 1885 1755 2005 -4 58 60 O ATOM 743 CB ASER A 89 -4.942 13.956 32.654 0.50 15.05 C ANISOU 743 CB ASER A 89 1897 1870 1951 42 -40 18 C ATOM 744 CB BSER A 89 -5.158 13.960 32.803 0.50 14.15 C ANISOU 744 CB BSER A 89 1809 1750 1816 81 -54 23 C ATOM 745 OG ASER A 89 -6.146 13.945 33.374 0.50 16.72 O ANISOU 745 OG ASER A 89 1943 2154 2255 -34 72 39 O ATOM 746 OG BSER A 89 -4.398 12.775 32.608 0.50 12.64 O ANISOU 746 OG BSER A 89 1799 1598 1405 215 -145 84 O ATOM 747 N THR A 90 -5.518 17.251 33.372 1.00 13.90 N ANISOU 747 N THR A 90 1785 1660 1835 23 57 -1 N ATOM 748 CA THR A 90 -6.417 18.345 33.031 1.00 14.28 C ANISOU 748 CA THR A 90 1784 1688 1952 7 37 -11 C ATOM 749 C THR A 90 -6.000 19.625 33.763 1.00 13.49 C ANISOU 749 C THR A 90 1604 1607 1914 -43 -2 -31 C ATOM 750 O THR A 90 -6.795 20.309 34.413 1.00 13.38 O ANISOU 750 O THR A 90 1442 1627 2013 6 17 73 O ATOM 751 CB THR A 90 -7.861 17.983 33.359 1.00 14.36 C ANISOU 751 CB THR A 90 1776 1746 1933 -48 50 -50 C ATOM 752 OG1 THR A 90 -7.941 17.548 34.720 1.00 15.27 O ANISOU 752 OG1 THR A 90 1968 1851 1980 54 229 124 O ATOM 753 CG2 THR A 90 -8.367 16.873 32.427 1.00 15.76 C ANISOU 753 CG2 THR A 90 2151 1697 2139 64 13 -197 C ATOM 754 N ILE A 91 -4.717 19.929 33.664 1.00 13.87 N ANISOU 754 N ILE A 91 1583 1664 2023 -24 55 -105 N ATOM 755 CA ILE A 91 -4.181 21.145 34.251 1.00 13.57 C ANISOU 755 CA ILE A 91 1406 1751 1998 -110 76 -119 C ATOM 756 C ILE A 91 -4.918 22.310 33.622 1.00 12.55 C ANISOU 756 C ILE A 91 1187 1845 1735 -93 43 -22 C ATOM 757 O ILE A 91 -5.155 22.382 32.391 1.00 13.97 O ANISOU 757 O ILE A 91 1417 1986 1902 -62 -4 -41 O ATOM 758 CB ILE A 91 -2.660 21.207 34.047 1.00 14.25 C ANISOU 758 CB ILE A 91 1398 1876 2140 3 111 -193 C ATOM 759 CG1 ILE A 91 -2.001 20.116 34.879 1.00 15.43 C ANISOU 759 CG1 ILE A 91 1617 1852 2393 76 224 -213 C ATOM 760 CG2 ILE A 91 -2.085 22.562 34.423 1.00 15.40 C ANISOU 760 CG2 ILE A 91 1413 1979 2456 -215 37 -112 C ATOM 761 CD1 ILE A 91 -0.528 19.926 34.585 1.00 16.58 C ANISOU 761 CD1 ILE A 91 1403 2123 2773 152 66 -360 C ATOM 762 N SER A 92 -5.289 23.258 34.444 1.00 11.84 N ANISOU 762 N SER A 92 1275 1611 1611 -54 14 97 N ATOM 763 CA ASER A 92 -6.117 24.345 33.946 0.50 12.78 C ANISOU 763 CA ASER A 92 1500 1669 1685 -48 21 94 C ATOM 764 CA BSER A 92 -6.115 24.356 33.971 0.50 12.54 C ANISOU 764 CA BSER A 92 1485 1633 1645 -35 40 111 C ATOM 765 C SER A 92 -5.207 25.406 33.340 1.00 12.41 C ANISOU 765 C SER A 92 1459 1617 1637 -100 59 81 C ATOM 766 O SER A 92 -4.843 26.348 34.013 1.00 14.74 O ANISOU 766 O SER A 92 1763 1979 1856 -288 175 -2 O ATOM 767 CB ASER A 92 -6.996 24.917 35.060 0.50 13.40 C ANISOU 767 CB ASER A 92 1614 1740 1736 -51 56 87 C ATOM 768 CB BSER A 92 -6.924 24.949 35.134 0.50 13.13 C ANISOU 768 CB BSER A 92 1610 1700 1676 -29 60 101 C ATOM 769 OG ASER A 92 -6.212 25.335 36.160 0.50 15.10 O ANISOU 769 OG ASER A 92 1872 1941 1923 -53 -67 -72 O ATOM 770 OG BSER A 92 -7.823 23.999 35.687 0.50 13.13 O ANISOU 770 OG BSER A 92 1701 1637 1648 23 137 82 O ATOM 771 N GLU A 93 -4.863 25.228 32.053 1.00 11.56 N ANISOU 771 N GLU A 93 1316 1414 1659 -23 -8 130 N ATOM 772 CA GLU A 93 -3.965 26.162 31.339 1.00 11.50 C ANISOU 772 CA GLU A 93 1372 1386 1609 19 32 96 C ATOM 773 C GLU A 93 -4.243 26.179 29.834 1.00 12.35 C ANISOU 773 C GLU A 93 1530 1492 1668 139 -51 137 C ATOM 774 O GLU A 93 -4.176 25.146 29.181 1.00 15.63 O ANISOU 774 O GLU A 93 2214 1821 1901 354 -238 79 O ATOM 775 CB GLU A 93 -2.495 25.753 31.606 1.00 11.65 C ANISOU 775 CB GLU A 93 1282 1467 1675 -17 108 20 C ATOM 776 CG GLU A 93 -1.483 26.648 30.943 1.00 11.61 C ANISOU 776 CG GLU A 93 1240 1544 1626 17 58 84 C ATOM 777 CD GLU A 93 -1.697 28.094 31.290 1.00 12.42 C ANISOU 777 CD GLU A 93 1365 1683 1669 5 183 8 C ATOM 778 OE1 GLU A 93 -1.622 28.412 32.498 1.00 12.45 O ANISOU 778 OE1 GLU A 93 1563 1328 1838 320 208 -226 O ATOM 779 OE2 GLU A 93 -1.937 28.902 30.371 1.00 13.46 O ANISOU 779 OE2 GLU A 93 1643 1497 1975 96 238 -41 O ATOM 780 N GLU A 94 -4.578 27.346 29.277 1.00 11.67 N ANISOU 780 N GLU A 94 1154 1556 1724 124 199 205 N ATOM 781 CA GLU A 94 -4.907 27.462 27.845 1.00 12.32 C ANISOU 781 CA GLU A 94 1131 1839 1711 22 161 125 C ATOM 782 C GLU A 94 -3.701 27.626 26.908 1.00 11.71 C ANISOU 782 C GLU A 94 1093 1845 1511 -4 141 29 C ATOM 783 O GLU A 94 -3.769 27.275 25.711 1.00 13.63 O ANISOU 783 O GLU A 94 1211 2368 1599 3 -18 -70 O ATOM 784 CB GLU A 94 -5.880 28.639 27.623 1.00 13.18 C ANISOU 784 CB GLU A 94 1170 1957 1878 107 156 197 C ATOM 785 CG GLU A 94 -7.154 28.565 28.474 1.00 16.43 C ANISOU 785 CG GLU A 94 1433 2487 2321 157 229 121 C ATOM 786 CD GLU A 94 -7.819 27.242 28.303 1.00 17.75 C ANISOU 786 CD GLU A 94 1156 2986 2600 60 -91 -115 C ATOM 787 OE1 GLU A 94 -8.109 26.877 27.144 1.00 24.00 O ANISOU 787 OE1 GLU A 94 2325 4138 2655 174 -38 -286 O ATOM 788 OE2 GLU A 94 -8.001 26.538 29.304 1.00 17.60 O ANISOU 788 OE2 GLU A 94 921 3428 2337 -297 246 -220 O ATOM 789 N ASN A 95 -2.619 28.175 27.442 1.00 9.77 N ANISOU 789 N ASN A 95 1021 1355 1335 79 70 137 N ATOM 790 CA ASN A 95 -1.422 28.436 26.666 1.00 9.26 C ANISOU 790 CA ASN A 95 1171 1183 1163 63 140 105 C ATOM 791 C ASN A 95 -0.660 27.122 26.561 1.00 8.06 C ANISOU 791 C ASN A 95 834 1092 1137 102 6 139 C ATOM 792 O ASN A 95 -0.237 26.581 27.603 1.00 8.43 O ANISOU 792 O ASN A 95 956 1210 1035 218 190 141 O ATOM 793 CB ASN A 95 -0.588 29.465 27.414 1.00 9.15 C ANISOU 793 CB ASN A 95 1210 1092 1175 103 90 65 C ATOM 794 CG ASN A 95 0.749 29.754 26.761 1.00 10.55 C ANISOU 794 CG ASN A 95 1497 1112 1397 -149 350 29 C ATOM 795 OD1 ASN A 95 1.315 28.939 26.022 1.00 11.32 O ANISOU 795 OD1 ASN A 95 1569 1177 1553 -108 492 -48 O ATOM 796 ND2 ASN A 95 1.271 30.917 27.048 1.00 14.38 N ANISOU 796 ND2 ASN A 95 2037 1361 2062 -261 613 -505 N ATOM 797 N PRO A 96 -0.506 26.564 25.341 1.00 8.97 N ANISOU 797 N PRO A 96 1032 1183 1193 12 -52 86 N ATOM 798 CA PRO A 96 0.105 25.239 25.247 1.00 8.89 C ANISOU 798 CA PRO A 96 951 1209 1215 47 -6 42 C ATOM 799 C PRO A 96 1.516 25.141 25.826 1.00 7.91 C ANISOU 799 C PRO A 96 854 1080 1071 -36 -2 51 C ATOM 800 O PRO A 96 1.924 24.080 26.285 1.00 7.42 O ANISOU 800 O PRO A 96 835 1028 953 -74 -31 35 O ATOM 801 CB PRO A 96 0.134 24.962 23.731 1.00 10.46 C ANISOU 801 CB PRO A 96 1155 1433 1385 -13 -43 -71 C ATOM 802 CG PRO A 96 0.103 26.291 23.113 1.00 12.40 C ANISOU 802 CG PRO A 96 1492 1700 1520 91 50 -9 C ATOM 803 CD PRO A 96 -0.854 27.071 24.000 1.00 9.77 C ANISOU 803 CD PRO A 96 1120 1313 1279 185 -37 120 C ATOM 804 N HIS A 97 2.273 26.232 25.767 1.00 7.20 N ANISOU 804 N HIS A 97 795 908 1030 30 -32 101 N ATOM 805 CA HIS A 97 3.643 26.215 26.277 1.00 7.34 C ANISOU 805 CA HIS A 97 854 924 1008 15 53 91 C ATOM 806 C HIS A 97 3.685 26.172 27.787 1.00 7.16 C ANISOU 806 C HIS A 97 829 832 1057 34 -7 -57 C ATOM 807 O HIS A 97 4.467 25.419 28.357 1.00 6.89 O ANISOU 807 O HIS A 97 781 927 907 22 32 46 O ATOM 808 CB HIS A 97 4.373 27.407 25.714 1.00 8.27 C ANISOU 808 CB HIS A 97 853 1081 1207 -14 3 92 C ATOM 809 CG HIS A 97 4.561 27.302 24.243 1.00 10.22 C ANISOU 809 CG HIS A 97 1233 1330 1318 -75 241 243 C ATOM 810 ND1 HIS A 97 5.483 26.454 23.678 1.00 16.27 N ANISOU 810 ND1 HIS A 97 2303 2262 1617 199 309 38 N ATOM 811 CD2 HIS A 97 3.858 27.837 23.218 1.00 14.15 C ANISOU 811 CD2 HIS A 97 2042 1952 1381 401 206 -36 C ATOM 812 CE1 HIS A 97 5.409 26.554 22.362 1.00 15.78 C ANISOU 812 CE1 HIS A 97 2147 2534 1315 36 263 -249 C ATOM 813 NE2 HIS A 97 4.429 27.379 22.057 1.00 18.02 N ANISOU 813 NE2 HIS A 97 2890 2676 1278 166 284 -166 N ATOM 814 N LEU A 98 2.830 26.953 28.436 1.00 7.64 N ANISOU 814 N LEU A 98 952 925 1025 167 19 -55 N ATOM 815 CA LEU A 98 2.705 26.887 29.884 1.00 8.62 C ANISOU 815 CA LEU A 98 1072 1050 1153 257 57 -36 C ATOM 816 C LEU A 98 2.093 25.560 30.337 1.00 8.34 C ANISOU 816 C LEU A 98 1120 1082 966 278 142 -14 C ATOM 817 O LEU A 98 2.459 25.036 31.417 1.00 9.14 O ANISOU 817 O LEU A 98 1253 1293 925 326 120 -6 O ATOM 818 CB LEU A 98 1.908 28.091 30.394 1.00 10.30 C ANISOU 818 CB LEU A 98 1241 1283 1388 331 107 -54 C ATOM 819 CG LEU A 98 1.849 28.366 31.893 1.00 13.20 C ANISOU 819 CG LEU A 98 1747 1503 1763 317 248 -197 C ATOM 820 CD1 LEU A 98 3.187 28.307 32.565 1.00 15.27 C ANISOU 820 CD1 LEU A 98 1859 1989 1952 210 241 -334 C ATOM 821 CD2 LEU A 98 1.208 29.739 32.105 1.00 16.29 C ANISOU 821 CD2 LEU A 98 2046 1794 2347 519 353 -553 C ATOM 822 N LYS A 99 1.194 24.993 29.533 1.00 8.10 N ANISOU 822 N LYS A 99 1031 992 1055 234 148 75 N ATOM 823 CA LYS A 99 0.676 23.691 29.869 1.00 8.66 C ANISOU 823 CA LYS A 99 1067 1117 1105 147 140 118 C ATOM 824 C LYS A 99 1.803 22.643 29.849 1.00 6.97 C ANISOU 824 C LYS A 99 772 942 933 87 113 91 C ATOM 825 O LYS A 99 1.829 21.732 30.674 1.00 7.12 O ANISOU 825 O LYS A 99 795 1038 869 24 227 107 O ATOM 826 CB LYS A 99 -0.420 23.270 28.917 1.00 9.25 C ANISOU 826 CB LYS A 99 986 1208 1321 187 61 219 C ATOM 827 CG LYS A 99 -1.054 21.987 29.375 1.00 13.73 C ANISOU 827 CG LYS A 99 1628 1588 1999 26 -116 142 C ATOM 828 CD LYS A 99 -2.544 21.931 29.096 1.00 18.70 C ANISOU 828 CD LYS A 99 2047 2514 2541 17 -234 53 C ATOM 829 CE LYS A 99 -3.245 20.945 30.033 1.00 22.41 C ANISOU 829 CE LYS A 99 3021 2720 2773 30 -213 238 C ATOM 830 NZ LYS A 99 -4.714 20.769 29.801 1.00 25.16 N ANISOU 830 NZ LYS A 99 3342 3055 3161 -136 -113 30 N ATOM 831 N ALA A 100 2.739 22.765 28.913 1.00 6.18 N ANISOU 831 N ALA A 100 779 822 745 77 96 42 N ATOM 832 CA ALA A 100 3.818 21.792 28.813 1.00 5.80 C ANISOU 832 CA ALA A 100 736 743 723 -31 67 1 C ATOM 833 C ALA A 100 4.724 21.846 30.044 1.00 5.20 C ANISOU 833 C ALA A 100 609 711 656 -101 66 48 C ATOM 834 O ALA A 100 5.075 20.808 30.612 1.00 5.23 O ANISOU 834 O ALA A 100 567 698 720 -29 52 -72 O ATOM 835 CB ALA A 100 4.629 22.021 27.532 1.00 6.01 C ANISOU 835 CB ALA A 100 832 876 575 -13 227 -14 C ATOM 836 N SER A 101 5.135 23.033 30.464 1.00 5.73 N ANISOU 836 N SER A 101 698 706 770 23 -39 96 N ATOM 837 CA SER A 101 5.944 23.131 31.659 1.00 5.86 C ANISOU 837 CA SER A 101 754 662 809 37 42 -29 C ATOM 838 C SER A 101 5.174 22.686 32.905 1.00 6.05 C ANISOU 838 C SER A 101 649 788 861 -30 -57 1 C ATOM 839 O SER A 101 5.730 22.005 33.763 1.00 6.24 O ANISOU 839 O SER A 101 805 750 813 -4 3 57 O ATOM 840 CB SER A 101 6.551 24.505 31.829 1.00 5.90 C ANISOU 840 CB SER A 101 679 767 795 18 -1 -58 C ATOM 841 OG SER A 101 5.557 25.497 31.902 1.00 6.70 O ANISOU 841 OG SER A 101 759 796 991 136 -20 32 O ATOM 842 N LYS A 102 3.890 23.028 32.997 1.00 6.49 N ANISOU 842 N LYS A 102 745 888 830 104 -10 -11 N ATOM 843 CA LYS A 102 3.109 22.597 34.144 1.00 6.70 C ANISOU 843 CA LYS A 102 825 817 901 66 54 -6 C ATOM 844 C LYS A 102 2.947 21.072 34.160 1.00 6.25 C ANISOU 844 C LYS A 102 772 832 769 41 10 58 C ATOM 845 O LYS A 102 2.901 20.485 35.259 1.00 6.87 O ANISOU 845 O LYS A 102 893 964 752 74 117 109 O ATOM 846 CB LYS A 102 1.759 23.317 34.177 1.00 7.14 C ANISOU 846 CB LYS A 102 876 881 955 -16 78 22 C ATOM 847 CG LYS A 102 1.892 24.776 34.577 1.00 8.55 C ANISOU 847 CG LYS A 102 1202 958 1088 76 28 -24 C ATOM 848 CD LYS A 102 0.538 25.493 34.518 1.00 10.03 C ANISOU 848 CD LYS A 102 1176 1244 1388 51 37 -46 C ATOM 849 CE LYS A 102 0.607 26.898 35.093 1.00 11.16 C ANISOU 849 CE LYS A 102 1412 1338 1489 182 74 -181 C ATOM 850 NZ LYS A 102 -0.726 27.598 35.129 1.00 13.43 N ANISOU 850 NZ LYS A 102 1582 1661 1857 430 -301 -336 N ATOM 851 N LEU A 103 2.804 20.452 32.996 1.00 6.52 N ANISOU 851 N LEU A 103 846 813 815 34 -15 78 N ATOM 852 CA ALEU A 103 2.707 18.993 32.896 0.50 6.42 C ANISOU 852 CA ALEU A 103 774 799 866 40 -27 33 C ATOM 853 CA BLEU A 103 2.690 19.011 32.935 0.50 6.20 C ANISOU 853 CA BLEU A 103 744 778 834 39 -8 31 C ATOM 854 C LEU A 103 3.982 18.330 33.418 1.00 6.06 C ANISOU 854 C LEU A 103 750 824 728 10 -89 109 C ATOM 855 O LEU A 103 3.914 17.413 34.248 1.00 6.18 O ANISOU 855 O LEU A 103 782 754 811 -32 -37 81 O ATOM 856 CB ALEU A 103 2.422 18.531 31.462 0.50 7.04 C ANISOU 856 CB ALEU A 103 814 908 952 96 -111 72 C ATOM 857 CB BLEU A 103 2.311 18.573 31.535 0.50 6.59 C ANISOU 857 CB BLEU A 103 747 877 879 77 -56 84 C ATOM 858 CG ALEU A 103 0.965 18.599 31.012 0.50 8.03 C ANISOU 858 CG ALEU A 103 799 1049 1201 29 -66 50 C ATOM 859 CG BLEU A 103 2.085 17.088 31.349 0.50 6.49 C ANISOU 859 CG BLEU A 103 628 902 934 60 52 13 C ATOM 860 CD1ALEU A 103 0.855 18.456 29.500 0.50 8.41 C ANISOU 860 CD1ALEU A 103 872 1084 1237 189 -225 84 C ATOM 861 CD1BLEU A 103 1.079 16.544 32.354 0.50 8.30 C ANISOU 861 CD1BLEU A 103 1189 762 1201 -128 59 148 C ATOM 862 CD2ALEU A 103 0.153 17.522 31.728 0.50 9.35 C ANISOU 862 CD2ALEU A 103 771 1309 1470 -71 -66 181 C ATOM 863 CD2BLEU A 103 1.624 16.855 29.947 0.50 7.36 C ANISOU 863 CD2BLEU A 103 853 1054 888 -22 177 -107 C ATOM 864 N VAL A 104 5.138 18.796 32.953 1.00 5.60 N ANISOU 864 N VAL A 104 673 727 727 48 -141 101 N ATOM 865 CA VAL A 104 6.379 18.223 33.443 1.00 5.78 C ANISOU 865 CA VAL A 104 779 687 728 32 -58 51 C ATOM 866 C VAL A 104 6.525 18.459 34.950 1.00 5.54 C ANISOU 866 C VAL A 104 707 676 720 -6 -114 54 C ATOM 867 O VAL A 104 6.990 17.572 35.680 1.00 6.21 O ANISOU 867 O VAL A 104 756 721 879 19 -73 55 O ATOM 868 CB VAL A 104 7.595 18.744 32.636 1.00 5.95 C ANISOU 868 CB VAL A 104 743 699 815 1 -79 100 C ATOM 869 CG1 VAL A 104 8.905 18.362 33.319 1.00 6.82 C ANISOU 869 CG1 VAL A 104 877 823 889 -10 -135 -5 C ATOM 870 CG2 VAL A 104 7.530 18.196 31.207 1.00 6.99 C ANISOU 870 CG2 VAL A 104 861 1055 738 -5 -9 1 C ATOM 871 N GLN A 105 6.125 19.628 35.444 1.00 5.96 N ANISOU 871 N GLN A 105 838 711 714 68 -49 93 N ATOM 872 CA GLN A 105 6.186 19.890 36.868 1.00 6.28 C ANISOU 872 CA GLN A 105 706 852 827 19 -80 -32 C ATOM 873 C GLN A 105 5.321 18.885 37.660 1.00 6.57 C ANISOU 873 C GLN A 105 921 724 851 20 -125 38 C ATOM 874 O GLN A 105 5.735 18.355 38.698 1.00 7.02 O ANISOU 874 O GLN A 105 873 975 819 14 -70 -21 O ATOM 875 CB GLN A 105 5.708 21.298 37.159 1.00 6.95 C ANISOU 875 CB GLN A 105 948 833 857 -58 -8 -13 C ATOM 876 CG GLN A 105 5.620 21.627 38.621 1.00 9.27 C ANISOU 876 CG GLN A 105 1387 1119 1014 72 -31 -22 C ATOM 877 CD GLN A 105 5.274 23.081 38.845 1.00 11.47 C ANISOU 877 CD GLN A 105 1530 1296 1528 136 50 -221 C ATOM 878 OE1 GLN A 105 4.169 23.529 38.530 1.00 13.09 O ANISOU 878 OE1 GLN A 105 1561 1656 1756 323 332 63 O ATOM 879 NE2 GLN A 105 6.244 23.841 39.323 1.00 12.34 N ANISOU 879 NE2 GLN A 105 1627 1510 1551 -63 200 -369 N ATOM 880 N CYS A 106 4.108 18.639 37.171 1.00 6.66 N ANISOU 880 N CYS A 106 871 809 851 -14 -28 76 N ATOM 881 CA CYS A 106 3.210 17.736 37.844 1.00 7.28 C ANISOU 881 CA CYS A 106 896 915 955 -85 50 23 C ATOM 882 C CYS A 106 3.760 16.303 37.874 1.00 6.19 C ANISOU 882 C CYS A 106 766 853 732 -112 -85 52 C ATOM 883 O CYS A 106 3.761 15.667 38.919 1.00 7.63 O ANISOU 883 O CYS A 106 1115 916 866 7 86 87 O ATOM 884 CB CYS A 106 1.851 17.793 37.153 1.00 7.19 C ANISOU 884 CB CYS A 106 839 802 1089 -112 68 82 C ATOM 885 SG CYS A 106 0.521 16.970 38.067 1.00 10.40 S ANISOU 885 SG CYS A 106 1207 1489 1254 -126 91 166 S ATOM 886 N VAL A 107 4.209 15.804 36.727 1.00 5.86 N ANISOU 886 N VAL A 107 685 822 718 -31 -50 72 N ATOM 887 CA VAL A 107 4.730 14.456 36.642 1.00 6.12 C ANISOU 887 CA VAL A 107 881 811 633 -87 -98 26 C ATOM 888 C VAL A 107 5.961 14.313 37.543 1.00 5.51 C ANISOU 888 C VAL A 107 774 719 600 2 -84 39 C ATOM 889 O VAL A 107 6.159 13.274 38.195 1.00 5.81 O ANISOU 889 O VAL A 107 847 670 687 -26 -37 -14 O ATOM 890 CB VAL A 107 5.070 14.071 35.197 1.00 7.25 C ANISOU 890 CB VAL A 107 1115 858 782 50 -171 16 C ATOM 891 CG1 VAL A 107 5.759 12.741 35.124 1.00 9.05 C ANISOU 891 CG1 VAL A 107 1300 1017 1121 171 -98 -107 C ATOM 892 CG2 VAL A 107 3.819 14.094 34.326 1.00 8.73 C ANISOU 892 CG2 VAL A 107 1311 1194 811 -142 -414 -126 C ATOM 893 N SER A 108 6.768 15.364 37.612 1.00 5.45 N ANISOU 893 N SER A 108 725 664 680 8 -97 47 N ATOM 894 CA SER A 108 8.003 15.348 38.389 1.00 5.47 C ANISOU 894 CA SER A 108 684 654 738 54 -28 23 C ATOM 895 C SER A 108 7.780 15.272 39.879 1.00 5.75 C ANISOU 895 C SER A 108 748 681 754 -28 -35 70 C ATOM 896 O SER A 108 8.700 14.874 40.573 1.00 6.55 O ANISOU 896 O SER A 108 794 937 756 61 -77 85 O ATOM 897 CB SER A 108 8.871 16.553 38.057 1.00 6.19 C ANISOU 897 CB SER A 108 720 765 866 1 -77 25 C ATOM 898 OG SER A 108 9.340 16.521 36.721 1.00 7.24 O ANISOU 898 OG SER A 108 820 970 959 86 93 211 O ATOM 899 N LYS A 109 6.567 15.525 40.371 1.00 6.17 N ANISOU 899 N LYS A 109 834 784 724 -20 -27 6 N ATOM 900 CA LYS A 109 6.247 15.273 41.770 1.00 7.07 C ANISOU 900 CA LYS A 109 935 1009 741 -37 11 -60 C ATOM 901 C LYS A 109 6.347 13.778 42.074 1.00 7.19 C ANISOU 901 C LYS A 109 989 1071 670 -70 -5 41 C ATOM 902 O LYS A 109 6.614 13.371 43.198 1.00 8.66 O ANISOU 902 O LYS A 109 1370 1294 627 -184 -54 79 O ATOM 903 CB LYS A 109 4.810 15.708 42.090 1.00 7.21 C ANISOU 903 CB LYS A 109 1044 1026 667 16 25 -41 C ATOM 904 CG LYS A 109 4.526 17.168 41.916 1.00 9.39 C ANISOU 904 CG LYS A 109 1410 1168 990 55 58 -109 C ATOM 905 CD LYS A 109 3.157 17.549 42.458 1.00 10.52 C ANISOU 905 CD LYS A 109 1456 1332 1209 159 42 -145 C ATOM 906 CE LYS A 109 2.040 16.716 41.843 1.00 11.28 C ANISOU 906 CE LYS A 109 1350 1381 1553 50 158 -316 C ATOM 907 NZ LYS A 109 0.669 17.226 42.198 1.00 11.25 N ANISOU 907 NZ LYS A 109 1425 1348 1501 170 -17 -130 N ATOM 908 N TYR A 110 6.083 12.951 41.074 1.00 6.38 N ANISOU 908 N TYR A 110 885 839 700 -83 32 2 N ATOM 909 CA TYR A 110 6.020 11.509 41.240 1.00 6.09 C ANISOU 909 CA TYR A 110 894 779 640 -95 54 29 C ATOM 910 C TYR A 110 7.407 10.898 41.033 1.00 6.42 C ANISOU 910 C TYR A 110 827 840 772 -103 -28 -3 C ATOM 911 O TYR A 110 7.910 10.172 41.894 1.00 8.04 O ANISOU 911 O TYR A 110 1037 1006 1011 38 11 230 O ATOM 912 CB TYR A 110 4.974 10.925 40.266 1.00 6.73 C ANISOU 912 CB TYR A 110 918 912 724 -41 55 96 C ATOM 913 CG TYR A 110 3.574 11.376 40.633 1.00 6.48 C ANISOU 913 CG TYR A 110 799 813 848 -171 38 52 C ATOM 914 CD1 TYR A 110 2.734 10.561 41.372 1.00 7.06 C ANISOU 914 CD1 TYR A 110 748 915 1017 -99 20 189 C ATOM 915 CD2 TYR A 110 3.090 12.624 40.264 1.00 6.65 C ANISOU 915 CD2 TYR A 110 757 944 823 -61 148 -13 C ATOM 916 CE1 TYR A 110 1.473 11.000 41.752 1.00 7.93 C ANISOU 916 CE1 TYR A 110 814 949 1247 -170 233 275 C ATOM 917 CE2 TYR A 110 1.819 13.065 40.637 1.00 6.02 C ANISOU 917 CE2 TYR A 110 818 830 637 -60 -83 73 C ATOM 918 CZ TYR A 110 1.024 12.247 41.407 1.00 7.30 C ANISOU 918 CZ TYR A 110 723 1080 970 -91 68 130 C ATOM 919 OH TYR A 110 -0.249 12.622 41.807 1.00 8.25 O ANISOU 919 OH TYR A 110 922 1285 926 159 279 72 O ATOM 920 N LYS A 111 8.044 11.192 39.900 1.00 5.96 N ANISOU 920 N LYS A 111 703 843 719 -97 -11 -95 N ATOM 921 CA LYS A 111 9.453 10.851 39.682 1.00 6.60 C ANISOU 921 CA LYS A 111 779 825 902 -184 -35 -60 C ATOM 922 C LYS A 111 10.058 11.966 38.867 1.00 5.71 C ANISOU 922 C LYS A 111 683 739 745 -51 16 -119 C ATOM 923 O LYS A 111 9.492 12.372 37.860 1.00 6.86 O ANISOU 923 O LYS A 111 760 1021 822 -80 -63 61 O ATOM 924 CB LYS A 111 9.633 9.545 38.872 1.00 8.46 C ANISOU 924 CB LYS A 111 1051 1013 1148 -132 57 -123 C ATOM 925 CG LYS A 111 9.191 8.245 39.504 1.00 11.66 C ANISOU 925 CG LYS A 111 1327 1394 1709 -186 72 -57 C ATOM 926 CD LYS A 111 9.992 7.873 40.731 1.00 13.63 C ANISOU 926 CD LYS A 111 1799 1578 1802 -113 -40 7 C ATOM 927 CE LYS A 111 11.477 7.649 40.490 1.00 13.39 C ANISOU 927 CE LYS A 111 1826 1673 1589 -406 -75 -66 C ATOM 928 NZ LYS A 111 12.096 7.059 41.740 1.00 14.56 N ANISOU 928 NZ LYS A 111 2027 1780 1725 -69 -168 -3 N ATOM 929 N THR A 112 11.235 12.428 39.263 1.00 5.77 N ANISOU 929 N THR A 112 573 837 782 -38 -40 10 N ATOM 930 CA THR A 112 11.963 13.381 38.441 1.00 5.59 C ANISOU 930 CA THR A 112 584 736 801 19 2 -33 C ATOM 931 C THR A 112 12.796 12.641 37.419 1.00 5.17 C ANISOU 931 C THR A 112 519 715 729 -33 3 -22 C ATOM 932 O THR A 112 13.142 11.475 37.608 1.00 5.76 O ANISOU 932 O THR A 112 761 681 745 33 -34 9 O ATOM 933 CB THR A 112 12.871 14.259 39.292 1.00 5.82 C ANISOU 933 CB THR A 112 574 827 808 -30 -58 -9 C ATOM 934 OG1 THR A 112 13.949 13.467 39.786 1.00 6.24 O ANISOU 934 OG1 THR A 112 668 794 909 30 42 7 O ATOM 935 CG2 THR A 112 12.104 14.949 40.419 1.00 6.54 C ANISOU 935 CG2 THR A 112 818 818 848 27 -17 -222 C ATOM 936 N MET A 113 13.174 13.307 36.331 1.00 5.18 N ANISOU 936 N MET A 113 569 713 685 85 38 55 N ATOM 937 CA MET A 113 14.039 12.656 35.358 1.00 5.17 C ANISOU 937 CA MET A 113 655 673 634 -4 -20 -79 C ATOM 938 C MET A 113 15.381 12.294 35.997 1.00 5.09 C ANISOU 938 C MET A 113 620 658 656 28 -41 7 C ATOM 939 O MET A 113 15.920 11.220 35.742 1.00 5.44 O ANISOU 939 O MET A 113 701 601 764 110 171 7 O ATOM 940 CB MET A 113 14.249 13.525 34.127 1.00 5.42 C ANISOU 940 CB MET A 113 767 617 674 -76 -6 -23 C ATOM 941 CG MET A 113 12.992 13.631 33.276 1.00 5.66 C ANISOU 941 CG MET A 113 674 828 647 -74 17 -166 C ATOM 942 SD MET A 113 13.223 14.446 31.690 1.00 6.73 S ANISOU 942 SD MET A 113 963 828 764 -60 -150 -32 S ATOM 943 CE MET A 113 13.161 16.084 32.237 1.00 8.55 C ANISOU 943 CE MET A 113 1363 1127 756 -327 -252 -103 C ATOM 944 N LYS A 114 15.912 13.147 36.877 1.00 5.37 N ANISOU 944 N LYS A 114 652 675 710 63 -29 -41 N ATOM 945 CA ALYS A 114 17.199 12.847 37.477 0.50 6.36 C ANISOU 945 CA ALYS A 114 713 810 894 24 -21 46 C ATOM 946 CA BLYS A 114 17.189 12.890 37.533 0.50 6.14 C ANISOU 946 CA BLYS A 114 665 774 891 42 -19 29 C ATOM 947 C LYS A 114 17.112 11.601 38.325 1.00 6.24 C ANISOU 947 C LYS A 114 718 781 872 10 -26 67 C ATOM 948 O LYS A 114 18.050 10.799 38.373 1.00 6.82 O ANISOU 948 O LYS A 114 751 880 961 121 -9 52 O ATOM 949 CB ALYS A 114 17.669 14.003 38.350 0.50 6.52 C ANISOU 949 CB ALYS A 114 804 865 807 -72 -6 63 C ATOM 950 CB BLYS A 114 17.513 14.057 38.485 0.50 6.06 C ANISOU 950 CB BLYS A 114 693 774 834 -45 -43 55 C ATOM 951 CG ALYS A 114 18.990 13.745 39.073 0.50 8.55 C ANISOU 951 CG ALYS A 114 1030 1125 1093 42 -112 180 C ATOM 952 CG BLYS A 114 18.841 13.952 39.268 0.50 7.39 C ANISOU 952 CG BLYS A 114 784 927 1097 167 -93 -50 C ATOM 953 CD ALYS A 114 19.480 15.015 39.699 0.50 10.46 C ANISOU 953 CD ALYS A 114 1235 1455 1282 -54 -36 70 C ATOM 954 CD BLYS A 114 20.047 13.958 38.318 0.50 10.90 C ANISOU 954 CD BLYS A 114 1138 1567 1434 65 -86 -170 C ATOM 955 CE ALYS A 114 20.749 14.866 40.485 0.50 11.71 C ANISOU 955 CE ALYS A 114 1342 1594 1511 -69 -111 44 C ATOM 956 CE BLYS A 114 21.371 14.271 39.023 0.50 13.54 C ANISOU 956 CE BLYS A 114 1430 1885 1827 -60 -178 -141 C ATOM 957 NZ ALYS A 114 21.160 16.195 41.010 0.50 9.70 N ANISOU 957 NZ ALYS A 114 1110 1468 1104 -113 -2 68 N ATOM 958 NZ BLYS A 114 22.473 14.419 38.031 0.50 15.72 N ANISOU 958 NZ BLYS A 114 1861 2138 1972 -247 -62 -257 N ATOM 959 N SER A 115 15.990 11.420 38.995 1.00 6.20 N ANISOU 959 N SER A 115 749 787 819 31 -4 128 N ATOM 960 CA ASER A 115 15.881 10.299 39.930 0.50 6.14 C ANISOU 960 CA ASER A 115 783 814 734 -47 26 149 C ATOM 961 CA BSER A 115 15.849 10.290 39.918 0.50 6.91 C ANISOU 961 CA BSER A 115 878 906 841 -24 16 139 C ATOM 962 C SER A 115 15.924 8.950 39.218 1.00 6.89 C ANISOU 962 C SER A 115 949 853 815 -38 70 152 C ATOM 963 O SER A 115 16.323 7.946 39.816 1.00 7.62 O ANISOU 963 O SER A 115 1118 927 848 144 30 246 O ATOM 964 CB ASER A 115 14.629 10.417 40.799 0.50 6.71 C ANISOU 964 CB ASER A 115 784 915 850 -31 72 113 C ATOM 965 CB BSER A 115 14.544 10.386 40.699 0.50 7.86 C ANISOU 965 CB BSER A 115 914 1078 993 -2 76 151 C ATOM 966 OG ASER A 115 13.454 10.248 40.030 0.50 6.42 O ANISOU 966 OG ASER A 115 801 839 798 -208 77 245 O ATOM 967 OG BSER A 115 14.644 11.407 41.665 0.50 11.40 O ANISOU 967 OG BSER A 115 1354 1480 1495 -10 -22 35 O ATOM 968 N VAL A 116 15.572 8.923 37.934 1.00 7.37 N ANISOU 968 N VAL A 116 1036 889 874 -111 -145 111 N ATOM 969 CA VAL A 116 15.611 7.695 37.163 1.00 8.13 C ANISOU 969 CA VAL A 116 1183 965 937 -107 -89 107 C ATOM 970 C VAL A 116 17.035 7.170 37.088 1.00 8.44 C ANISOU 970 C VAL A 116 1308 1047 852 16 -90 98 C ATOM 971 O VAL A 116 17.255 5.963 37.053 1.00 9.69 O ANISOU 971 O VAL A 116 1572 1011 1097 -1 -79 -88 O ATOM 972 CB VAL A 116 15.019 7.879 35.752 1.00 7.84 C ANISOU 972 CB VAL A 116 1130 871 977 -157 -98 120 C ATOM 973 CG1 VAL A 116 15.091 6.573 34.963 1.00 9.13 C ANISOU 973 CG1 VAL A 116 1131 1216 1121 -265 -173 -11 C ATOM 974 CG2 VAL A 116 13.590 8.291 35.875 1.00 8.84 C ANISOU 974 CG2 VAL A 116 1058 1103 1198 -351 -80 35 C ATOM 975 N ASP A 117 18.015 8.064 37.059 1.00 9.18 N ANISOU 975 N ASP A 117 1281 1173 1033 65 6 -18 N ATOM 976 CA ASP A 117 19.416 7.639 36.959 1.00 11.11 C ANISOU 976 CA ASP A 117 1385 1437 1397 76 44 -97 C ATOM 977 C ASP A 117 19.945 6.846 38.126 1.00 12.68 C ANISOU 977 C ASP A 117 1483 1696 1636 146 -54 -79 C ATOM 978 O ASP A 117 20.959 6.160 38.004 1.00 14.24 O ANISOU 978 O ASP A 117 1481 1875 2055 396 -3 -94 O ATOM 979 CB ASP A 117 20.311 8.844 36.776 1.00 11.62 C ANISOU 979 CB ASP A 117 1331 1516 1566 69 113 -167 C ATOM 980 CG ASP A 117 20.393 9.270 35.357 1.00 12.49 C ANISOU 980 CG ASP A 117 1443 1523 1776 0 -164 135 C ATOM 981 OD1 ASP A 117 20.049 8.462 34.466 1.00 15.75 O ANISOU 981 OD1 ASP A 117 2158 2166 1657 -241 -244 18 O ATOM 982 OD2 ASP A 117 20.836 10.393 35.121 1.00 15.94 O ANISOU 982 OD2 ASP A 117 1668 1787 2600 251 -80 354 O ATOM 983 N PHE A 118 19.283 6.927 39.268 1.00 12.26 N ANISOU 983 N PHE A 118 1589 1626 1443 142 -148 -34 N ATOM 984 CA PHE A 118 19.764 6.224 40.455 1.00 13.25 C ANISOU 984 CA PHE A 118 1810 1755 1468 77 -294 -20 C ATOM 985 C PHE A 118 19.222 4.794 40.520 1.00 14.35 C ANISOU 985 C PHE A 118 2003 1818 1628 35 -236 8 C ATOM 986 O PHE A 118 19.624 4.000 41.365 1.00 16.47 O ANISOU 986 O PHE A 118 2370 1890 1995 109 -375 76 O ATOM 987 CB PHE A 118 19.350 6.980 41.712 1.00 12.47 C ANISOU 987 CB PHE A 118 1798 1663 1277 113 -240 3 C ATOM 988 CG PHE A 118 19.833 8.429 41.795 1.00 13.24 C ANISOU 988 CG PHE A 118 1769 1781 1479 188 -298 56 C ATOM 989 CD1 PHE A 118 21.173 8.741 41.902 1.00 13.58 C ANISOU 989 CD1 PHE A 118 1759 1861 1537 197 -151 292 C ATOM 990 CD2 PHE A 118 18.918 9.466 41.865 1.00 12.75 C ANISOU 990 CD2 PHE A 118 1795 1702 1346 245 -535 15 C ATOM 991 CE1 PHE A 118 21.591 10.028 42.054 1.00 14.92 C ANISOU 991 CE1 PHE A 118 1832 2062 1772 92 -184 346 C ATOM 992 CE2 PHE A 118 19.321 10.780 41.980 1.00 12.57 C ANISOU 992 CE2 PHE A 118 1834 1706 1235 271 -74 221 C ATOM 993 CZ PHE A 118 20.655 11.070 42.080 1.00 14.25 C ANISOU 993 CZ PHE A 118 2029 1571 1815 -26 -131 304 C ATOM 994 N LEU A 119 18.313 4.443 39.623 1.00 15.24 N ANISOU 994 N LEU A 119 2109 1907 1773 25 -250 16 N ATOM 995 CA LEU A 119 17.624 3.163 39.715 1.00 16.59 C ANISOU 995 CA LEU A 119 2211 2001 2090 7 -50 4 C ATOM 996 C LEU A 119 18.398 1.986 39.116 1.00 18.30 C ANISOU 996 C LEU A 119 2483 2101 2367 22 42 40 C ATOM 997 O LEU A 119 19.328 2.146 38.321 1.00 19.97 O ANISOU 997 O LEU A 119 2494 2316 2776 107 126 9 O ATOM 998 CB LEU A 119 16.237 3.289 39.078 1.00 15.82 C ANISOU 998 CB LEU A 119 2192 1870 1949 -39 -101 -13 C ATOM 999 CG LEU A 119 15.319 4.257 39.837 1.00 15.62 C ANISOU 999 CG LEU A 119 2266 1746 1922 -12 16 109 C ATOM 1000 CD1 LEU A 119 13.971 4.354 39.183 1.00 16.47 C ANISOU 1000 CD1 LEU A 119 2130 1889 2237 -313 124 143 C ATOM 1001 CD2 LEU A 119 15.184 3.842 41.311 1.00 17.01 C ANISOU 1001 CD2 LEU A 119 2681 1710 2070 47 197 262 C ATOM 1002 OXT LEU A 119 18.102 0.833 39.456 1.00 20.50 O ANISOU 1002 OXT LEU A 119 2730 2320 2737 -17 118 51 O TER 1003 LEU A 119 HETATM 1004 O HOH A 120 -5.185 5.836 34.241 1.00 23.55 O ANISOU 1004 O HOH A 120 3252 1843 3853 1859 -906 513 O HETATM 1005 O HOH A 121 10.688 23.387 43.047 1.00 65.22 O ANISOU 1005 O HOH A 121 9080 6707 8993 -2033 2424 -2296 O HETATM 1006 O HOH A 122 2.449 24.222 41.772 1.00 54.52 O ANISOU 1006 O HOH A 122 10253 4190 6273 2797 3086 1188 O HETATM 1007 O HOH A 123 19.834 -0.016 36.852 1.00 51.40 O ANISOU 1007 O HOH A 123 9318 4857 5352 -212 90 -2078 O HETATM 1008 O HOH A 124 -6.800 8.494 31.134 1.00 31.39 O ANISOU 1008 O HOH A 124 2529 4946 4451 -556 -1132 -558 O HETATM 1009 O HOH A 125 0.399 24.060 19.214 1.00 83.81 O ANISOU 1009 O HOH A 125 8687 15737 7420 -5144 -1084 1135 O HETATM 1010 O HOH A 126 -1.191 27.702 19.487 1.00 15.21 O ANISOU 1010 O HOH A 126 2174 1980 1623 229 514 -1278 O HETATM 1011 O HOH A 127 21.533 3.020 31.002 1.00 23.59 O ANISOU 1011 O HOH A 127 1930 3793 3239 275 -196 329 O HETATM 1012 O HOH A 128 16.557 -5.072 25.862 1.00 13.33 O ANISOU 1012 O HOH A 128 1453 1481 2128 -191 -214 -267 O HETATM 1013 O HOH A 129 22.011 14.203 27.708 1.00 18.40 O ANISOU 1013 O HOH A 129 1756 2447 2785 -570 -15 -743 O HETATM 1014 O HOH A 130 6.790 14.947 45.372 1.00 28.46 O ANISOU 1014 O HOH A 130 4681 3690 2440 -731 -689 -1030 O HETATM 1015 O HOH A 131 -5.069 17.892 36.071 1.00 21.44 O ANISOU 1015 O HOH A 131 2748 2681 2716 861 -24 730 O HETATM 1016 O HOH A 132 -4.630 18.250 29.370 1.00 62.99 O ANISOU 1016 O HOH A 132 5018 9082 9833 -489 281 -3004 O HETATM 1017 O HOH A 133 -7.164 15.011 35.204 1.00 28.66 O ANISOU 1017 O HOH A 133 4859 2474 3556 289 -1811 93 O HETATM 1018 O HOH A 134 18.713 -2.817 29.053 1.00 37.21 O ANISOU 1018 O HOH A 134 4619 3519 5997 568 -1483 -1147 O HETATM 1019 O HOH A 135 22.098 34.729 31.835 1.00 40.09 O ANISOU 1019 O HOH A 135 3288 6509 5433 605 832 -532 O HETATM 1020 O HOH A 136 -0.043 23.409 37.728 1.00 32.78 O ANISOU 1020 O HOH A 136 3787 5102 3565 1822 -255 -480 O HETATM 1021 O HOH A 137 22.800 1.866 26.184 1.00 49.24 O ANISOU 1021 O HOH A 137 8582 4441 5683 -639 -1025 -211 O HETATM 1022 O HOH A 138 23.430 20.314 39.004 1.00 42.63 O ANISOU 1022 O HOH A 138 6783 5373 4039 2417 -263 -700 O HETATM 1023 O HOH A 139 27.141 4.343 26.186 1.00 32.45 O ANISOU 1023 O HOH A 139 3448 4097 4783 -857 -1747 -1712 O HETATM 1024 O HOH A 140 8.450 12.172 29.676 1.00 34.64 O ANISOU 1024 O HOH A 140 3710 4941 4510 -180 911 818 O HETATM 1025 O HOH A 141 8.345 -1.819 38.459 1.00 41.72 O ANISOU 1025 O HOH A 141 3840 7728 4281 -1158 486 -2629 O HETATM 1026 O HOH A 142 21.726 2.168 40.797 1.00 29.64 O ANISOU 1026 O HOH A 142 4627 3128 3507 1465 -40 -58 O HETATM 1027 O HOH A 143 21.160 11.078 39.027 1.00 31.98 O ANISOU 1027 O HOH A 143 4806 4698 2644 310 -435 467 O HETATM 1028 O HOH A 144 20.094 17.787 36.788 1.00 19.88 O ANISOU 1028 O HOH A 144 2616 2837 2097 -391 -404 719 O HETATM 1029 O HOH A 145 22.810 22.538 37.762 1.00 25.99 O ANISOU 1029 O HOH A 145 3681 3460 2731 -500 -1681 -467 O HETATM 1030 O HOH A 146 21.111 17.102 34.968 1.00 22.19 O ANISOU 1030 O HOH A 146 4184 1520 2725 -377 -781 174 O HETATM 1031 O HOH A 147 13.889 26.431 38.794 1.00 23.19 O ANISOU 1031 O HOH A 147 3105 3021 2683 265 -63 -269 O HETATM 1032 O HOH A 148 9.413 8.851 19.430 1.00 33.99 O ANISOU 1032 O HOH A 148 3463 6860 2590 694 110 394 O HETATM 1033 O HOH A 149 -6.717 21.605 37.125 1.00 32.94 O ANISOU 1033 O HOH A 149 4728 4353 3432 -1614 -416 471 O HETATM 1034 O HOH A 150 -5.292 17.910 24.466 1.00 28.88 O ANISOU 1034 O HOH A 150 3361 3653 3955 689 1657 259 O HETATM 1035 O HOH A 151 21.144 21.061 42.159 1.00 34.27 O ANISOU 1035 O HOH A 151 4352 4954 3712 -613 93 578 O HETATM 1036 O HOH A 152 1.784 21.016 44.038 1.00 28.56 O ANISOU 1036 O HOH A 152 4872 3560 2418 -149 1041 80 O HETATM 1037 O HOH A 153 -8.958 13.058 34.340 1.00 30.20 O ANISOU 1037 O HOH A 153 2207 2720 6548 316 -298 25 O HETATM 1038 O HOH A 154 -6.252 19.468 14.299 1.00 26.02 O ANISOU 1038 O HOH A 154 2989 2103 4794 358 -382 177 O HETATM 1039 O HOH A 155 -3.096 24.050 26.656 1.00 43.58 O ANISOU 1039 O HOH A 155 3984 7187 5388 -1113 -935 -534 O HETATM 1040 O HOH A 156 23.023 31.821 30.900 1.00 31.02 O ANISOU 1040 O HOH A 156 2821 3505 5460 -319 -1039 336 O HETATM 1041 O HOH A 157 21.607 24.012 40.956 1.00 37.15 O ANISOU 1041 O HOH A 157 4585 5311 4219 546 -1677 -328 O HETATM 1042 O HOH A 158 3.133 -2.819 30.078 1.00 28.83 O ANISOU 1042 O HOH A 158 4165 3111 3677 1320 -1961 -414 O HETATM 1043 O HOH A 159 2.739 25.831 38.585 1.00 51.44 O ANISOU 1043 O HOH A 159 6629 6971 5942 692 -1156 1790 O HETATM 1044 O HOH A 160 7.541 4.879 24.929 1.00 55.86 O ANISOU 1044 O HOH A 160 6056 6434 8733 1046 2923 -542 O HETATM 1045 O HOH A 161 0.529 20.368 12.355 1.00 42.49 O ANISOU 1045 O HOH A 161 7219 4097 4826 -1294 1441 -8 O HETATM 1046 O HOH A 162 24.470 16.004 24.534 1.00 45.42 O ANISOU 1046 O HOH A 162 1372 7174 8711 -942 7 -655 O HETATM 1047 O HOH A 163 10.933 4.324 41.639 1.00 24.66 O ANISOU 1047 O HOH A 163 3675 1245 4448 -324 -1629 863 O HETATM 1048 O HOH A 164 24.851 18.060 22.332 1.00 35.29 O ANISOU 1048 O HOH A 164 1935 6188 5284 755 604 -612 O HETATM 1049 O HOH A 165 4.696 -2.763 41.513 1.00 33.52 O ANISOU 1049 O HOH A 165 3977 6924 1832 2299 -314 -74 O HETATM 1050 O HOH A 166 5.734 -2.495 32.332 1.00 30.89 O ANISOU 1050 O HOH A 166 4014 4327 3395 645 -1744 -645 O HETATM 1051 O HOH A 167 -4.625 25.175 24.255 1.00 29.72 O ANISOU 1051 O HOH A 167 4304 2693 4294 -1007 -486 -1093 O HETATM 1052 O HOH A 168 13.066 -2.719 36.539 1.00 25.79 O ANISOU 1052 O HOH A 168 3731 2874 3195 -49 1058 -393 O HETATM 1053 O HOH A 169 0.486 30.468 35.605 1.00 47.34 O ANISOU 1053 O HOH A 169 7567 3343 7076 441 -1444 -1296 O HETATM 1054 O HOH A 170 19.436 6.663 23.039 1.00 6.95 O ANISOU 1054 O HOH A 170 737 804 1099 81 -232 -117 O HETATM 1055 O HOH A 171 8.748 14.389 33.900 1.00 31.33 O ANISOU 1055 O HOH A 171 3536 4629 3736 -2913 488 -1401 O HETATM 1056 O HOH A 172 9.595 12.411 34.507 1.00 21.83 O ANISOU 1056 O HOH A 172 1602 4192 2499 -1171 -861 1350 O HETATM 1057 O HOH A 173 10.360 10.678 34.777 1.00 23.35 O ANISOU 1057 O HOH A 173 2104 3061 3706 -522 592 -1945 O HETATM 1058 O HOH A 174 10.137 11.613 32.325 1.00 26.18 O ANISOU 1058 O HOH A 174 1946 3706 4292 -980 1125 -1315 O HETATM 1059 O HOH A 175 9.287 13.584 31.679 1.00 39.16 O ANISOU 1059 O HOH A 175 5422 5189 4269 -1921 -68 303 O HETATM 1060 O HOH A 176 19.256 18.741 28.529 1.00 7.62 O ANISOU 1060 O HOH A 176 1038 860 997 -22 -45 -192 O HETATM 1061 O HOH A 177 12.034 15.932 35.974 1.00 6.28 O ANISOU 1061 O HOH A 177 771 805 811 38 31 48 O HETATM 1062 O HOH A 178 9.372 22.696 22.075 1.00 7.69 O ANISOU 1062 O HOH A 178 915 1293 714 -52 105 173 O HETATM 1063 O HOH A 179 15.567 14.960 41.294 1.00 7.84 O ANISOU 1063 O HOH A 179 1020 1179 776 -1 -119 -58 O HETATM 1064 O HOH A 180 11.036 23.687 20.219 1.00 7.26 O ANISOU 1064 O HOH A 180 794 936 1028 -208 160 67 O HETATM 1065 O HOH A 181 17.862 29.257 28.702 1.00 9.65 O ANISOU 1065 O HOH A 181 1150 1220 1295 211 59 -239 O HETATM 1066 O HOH A 182 13.225 25.114 35.416 1.00 9.44 O ANISOU 1066 O HOH A 182 1296 1052 1236 266 -206 -20 O HETATM 1067 O HOH A 183 17.398 11.599 33.424 1.00 7.61 O ANISOU 1067 O HOH A 183 912 1183 794 172 22 78 O HETATM 1068 O HOH A 184 14.866 7.268 42.112 1.00 10.48 O ANISOU 1068 O HOH A 184 1004 1521 1454 -272 -126 304 O HETATM 1069 O HOH A 185 1.178 21.557 25.391 1.00 13.37 O ANISOU 1069 O HOH A 185 1763 1399 1916 -358 299 -13 O HETATM 1070 O HOH A 186 7.340 19.496 40.515 1.00 13.29 O ANISOU 1070 O HOH A 186 1597 1660 1791 -76 -395 -182 O HETATM 1071 O HOH A 187 18.300 9.153 32.646 1.00 11.45 O ANISOU 1071 O HOH A 187 1750 1316 1285 215 -130 -277 O HETATM 1072 O HOH A 188 2.129 21.865 37.553 1.00 12.36 O ANISOU 1072 O HOH A 188 1589 1785 1320 169 159 -376 O HETATM 1073 O HOH A 189 12.104 10.879 19.715 1.00 12.62 O ANISOU 1073 O HOH A 189 1816 1534 1441 218 -385 15 O HETATM 1074 O HOH A 190 15.511 30.507 29.479 1.00 11.00 O ANISOU 1074 O HOH A 190 829 1329 2019 55 29 -454 O HETATM 1075 O HOH A 191 24.059 26.875 32.011 1.00 13.31 O ANISOU 1075 O HOH A 191 1133 2126 1797 -470 -45 282 O HETATM 1076 O HOH A 192 15.767 19.332 43.753 1.00 11.97 O ANISOU 1076 O HOH A 192 1538 1484 1526 404 -144 443 O HETATM 1077 O HOH A 193 9.242 20.334 20.305 1.00 16.97 O ANISOU 1077 O HOH A 193 2806 1624 2018 -239 -978 331 O HETATM 1078 O HOH A 194 6.771 25.280 20.193 1.00 13.66 O ANISOU 1078 O HOH A 194 1454 2130 1604 330 52 546 O HETATM 1079 O HOH A 195 22.654 18.870 23.887 1.00 15.50 O ANISOU 1079 O HOH A 195 1364 2073 2451 -248 -124 103 O HETATM 1080 O HOH A 196 23.213 6.307 24.295 1.00 12.34 O ANISOU 1080 O HOH A 196 1229 1804 1656 -163 -49 -364 O HETATM 1081 O HOH A 197 4.749 14.360 19.128 1.00 15.87 O ANISOU 1081 O HOH A 197 1430 2614 1983 134 -291 -701 O HETATM 1082 O HOH A 198 -5.056 11.713 41.877 1.00 13.68 O ANISOU 1082 O HOH A 198 1548 2172 1479 140 39 -55 O HETATM 1083 O HOH A 199 8.785 22.320 40.013 1.00 12.67 O ANISOU 1083 O HOH A 199 1497 1819 1497 153 231 147 O HETATM 1084 O HOH A 200 22.024 8.364 25.863 1.00 16.54 O ANISOU 1084 O HOH A 200 1639 2239 2407 691 -481 -546 O HETATM 1085 O HOH A 201 21.676 28.714 26.281 1.00 18.46 O ANISOU 1085 O HOH A 201 1581 3091 2339 -750 2 -79 O HETATM 1086 O HOH A 202 -7.431 10.287 42.175 1.00 16.38 O ANISOU 1086 O HOH A 202 2152 2588 1484 -407 -365 473 O HETATM 1087 O HOH A 203 9.836 16.120 42.850 1.00 12.02 O ANISOU 1087 O HOH A 203 1421 2066 1080 519 -45 -220 O HETATM 1088 O HOH A 204 3.651 -0.025 37.380 1.00 17.41 O ANISOU 1088 O HOH A 204 2689 1578 2347 -480 76 105 O HETATM 1089 O HOH A 205 -5.287 4.766 41.904 1.00 15.68 O ANISOU 1089 O HOH A 205 1789 1891 2277 359 262 835 O HETATM 1090 O HOH A 206 14.004 17.068 19.304 1.00 20.16 O ANISOU 1090 O HOH A 206 2758 1923 2978 653 1256 542 O HETATM 1091 O HOH A 207 7.826 30.345 37.064 1.00 25.62 O ANISOU 1091 O HOH A 207 3377 1884 4470 -328 -642 -1236 O HETATM 1092 O HOH A 208 21.871 17.059 20.724 1.00 16.95 O ANISOU 1092 O HOH A 208 1956 2221 2263 135 311 -347 O HETATM 1093 O HOH A 209 14.096 0.023 24.844 1.00 14.33 O ANISOU 1093 O HOH A 209 1543 2644 1257 563 349 -253 O HETATM 1094 O HOH A 210 7.856 6.162 22.559 1.00 17.33 O ANISOU 1094 O HOH A 210 1858 1007 3718 -172 483 -551 O HETATM 1095 O HOH A 211 14.326 -2.912 34.039 1.00 12.34 O ANISOU 1095 O HOH A 211 1548 1583 1557 -90 225 178 O HETATM 1096 O HOH A 212 17.810 -1.811 32.709 1.00 54.96 O ANISOU 1096 O HOH A 212 7619 6030 7231 -549 1803 413 O HETATM 1097 O HOH A 213 -0.918 30.499 23.161 1.00 14.28 O ANISOU 1097 O HOH A 213 2071 1457 1894 -196 -613 -154 O HETATM 1098 O HOH A 214 3.340 31.877 25.394 1.00 16.32 O ANISOU 1098 O HOH A 214 2013 1838 2349 635 -149 -150 O HETATM 1099 O HOH A 215 -1.870 31.568 30.713 1.00 19.20 O ANISOU 1099 O HOH A 215 2252 1832 3209 -205 334 -340 O HETATM 1100 O HOH A 216 5.762 20.881 42.279 1.00 18.82 O ANISOU 1100 O HOH A 216 2716 2723 1711 329 -129 -331 O HETATM 1101 O HOH A 217 11.693 33.364 29.661 1.00 16.55 O ANISOU 1101 O HOH A 217 2271 1384 2633 -223 817 -258 O HETATM 1102 O HOH A 218 9.408 18.633 41.906 1.00 17.24 O ANISOU 1102 O HOH A 218 1799 2647 2103 328 -396 938 O HETATM 1103 O HOH A 219 0.342 13.654 14.351 1.00 19.40 O ANISOU 1103 O HOH A 219 2926 2464 1979 -405 780 697 O HETATM 1104 O HOH A 220 21.189 14.685 33.784 1.00 14.95 O ANISOU 1104 O HOH A 220 1553 1638 2489 -251 515 174 O HETATM 1105 O HOH A 221 23.026 7.638 28.293 1.00 22.44 O ANISOU 1105 O HOH A 221 2327 2424 3775 549 0 -298 O HETATM 1106 O HOH A 222 15.150 26.989 36.004 1.00 19.62 O ANISOU 1106 O HOH A 222 1940 1763 3750 -356 -306 -56 O HETATM 1107 O HOH A 223 20.143 22.162 38.788 1.00 20.82 O ANISOU 1107 O HOH A 223 2528 2608 2775 382 -35 426 O HETATM 1108 O HOH A 224 18.804 32.055 30.209 1.00 16.24 O ANISOU 1108 O HOH A 224 1943 1764 2462 309 0 -419 O HETATM 1109 O HOH A 225 8.703 14.913 18.339 1.00 22.20 O ANISOU 1109 O HOH A 225 2813 4052 1567 -781 -148 466 O HETATM 1110 O HOH A 226 10.538 12.355 18.182 1.00 26.27 O ANISOU 1110 O HOH A 226 3128 4624 2228 1778 -679 -514 O HETATM 1111 O HOH A 227 2.141 20.282 39.815 1.00 20.97 O ANISOU 1111 O HOH A 227 3993 1843 2130 717 797 135 O HETATM 1112 O HOH A 228 0.471 18.635 44.693 1.00 18.09 O ANISOU 1112 O HOH A 228 2786 1602 2482 4 499 -460 O HETATM 1113 O HOH A 229 -0.092 19.529 40.833 1.00 20.26 O ANISOU 1113 O HOH A 229 3326 1861 2508 141 -357 574 O HETATM 1114 O HOH A 230 13.369 -3.848 26.564 1.00 34.16 O ANISOU 1114 O HOH A 230 5210 3779 3988 -217 -1673 428 O HETATM 1115 O HOH A 231 16.746 33.597 33.833 1.00 15.28 O ANISOU 1115 O HOH A 231 2285 1700 1819 -312 -15 -281 O HETATM 1116 O HOH A 232 -2.813 18.518 31.856 1.00 18.44 O ANISOU 1116 O HOH A 232 2265 2399 2339 -23 421 346 O HETATM 1117 O HOH A 233 19.165 29.930 35.856 1.00 23.58 O ANISOU 1117 O HOH A 233 3811 2377 2770 -170 -661 -65 O HETATM 1118 O HOH A 234 2.359 -2.098 40.115 1.00 20.54 O ANISOU 1118 O HOH A 234 3305 1192 3305 319 -515 410 O HETATM 1119 O HOH A 235 22.433 6.881 34.039 1.00 21.53 O ANISOU 1119 O HOH A 235 1862 3081 3236 281 -39 552 O HETATM 1120 O HOH A 236 1.961 4.425 24.939 1.00 25.07 O ANISOU 1120 O HOH A 236 3443 3577 2503 -26 161 -634 O HETATM 1121 O HOH A 237 12.517 33.416 32.503 1.00 17.24 O ANISOU 1121 O HOH A 237 2672 1584 2291 -586 63 -227 O HETATM 1122 O HOH A 238 21.378 17.696 29.834 1.00 15.74 O ANISOU 1122 O HOH A 238 1067 2702 2210 454 -103 85 O HETATM 1123 O HOH A 239 -6.214 7.542 35.881 1.00 19.17 O ANISOU 1123 O HOH A 239 2027 2577 2678 -435 -638 -437 O HETATM 1124 O HOH A 240 3.302 21.474 41.739 1.00 22.50 O ANISOU 1124 O HOH A 240 3444 2752 2351 622 785 -259 O HETATM 1125 O HOH A 241 13.507 31.897 28.219 1.00 14.37 O ANISOU 1125 O HOH A 241 1769 1409 2282 -49 -484 -44 O HETATM 1126 O HOH A 242 20.832 29.841 33.678 1.00 19.61 O ANISOU 1126 O HOH A 242 2739 2494 2217 20 -406 -83 O HETATM 1127 O HOH A 243 -6.631 10.961 31.893 1.00 58.41 O ANISOU 1127 O HOH A 243 9562 5346 7281 -469 -3886 839 O HETATM 1128 O HOH A 244 10.407 32.843 34.567 1.00 22.22 O ANISOU 1128 O HOH A 244 3088 1580 3772 -70 539 -220 O HETATM 1129 O HOH A 245 3.566 30.416 37.678 1.00 33.49 O ANISOU 1129 O HOH A 245 4594 3582 4546 1181 1913 502 O HETATM 1130 O HOH A 246 8.227 7.579 21.764 1.00 27.66 O ANISOU 1130 O HOH A 246 2014 3053 5441 -424 -773 32 O HETATM 1131 O HOH A 247 9.807 17.792 19.709 1.00 39.10 O ANISOU 1131 O HOH A 247 5537 4156 5163 995 -2430 -4211 O HETATM 1132 O HOH A 248 22.680 11.497 36.554 1.00 30.32 O ANISOU 1132 O HOH A 248 2865 3931 4721 -1511 -1436 57 O HETATM 1133 O HOH A 249 19.609 12.691 34.600 1.00 10.88 O ANISOU 1133 O HOH A 249 1299 1463 1371 -250 -221 202 O HETATM 1134 O HOH A 250 17.502 22.071 40.796 1.00 42.46 O ANISOU 1134 O HOH A 250 4326 8060 3746 184 2432 -1477 O HETATM 1135 O HOH A 251 7.482 12.339 18.242 1.00 26.59 O ANISOU 1135 O HOH A 251 2606 4499 2996 -1059 60 -149 O HETATM 1136 O HOH A 252 10.622 -1.359 35.624 1.00 23.32 O ANISOU 1136 O HOH A 252 3663 1748 3448 1400 545 306 O HETATM 1137 O HOH A 253 23.091 5.100 29.115 1.00 25.57 O ANISOU 1137 O HOH A 253 2540 2626 4550 637 -1891 -368 O HETATM 1138 O HOH A 254 7.473 27.921 38.530 1.00 25.01 O ANISOU 1138 O HOH A 254 2397 4867 2237 904 308 234 O HETATM 1139 O HOH A 255 -2.917 26.176 36.080 1.00 26.01 O ANISOU 1139 O HOH A 255 2541 4058 3284 -139 419 -7 O HETATM 1140 O HOH A 256 22.067 16.848 27.472 1.00 26.64 O ANISOU 1140 O HOH A 256 4702 3231 2188 -933 -154 -737 O HETATM 1141 O HOH A 257 -7.451 8.372 40.189 1.00 19.32 O ANISOU 1141 O HOH A 257 2941 3011 1386 233 403 149 O HETATM 1142 O HOH A 258 18.541 31.739 27.526 1.00 16.71 O ANISOU 1142 O HOH A 258 2596 1841 1911 476 403 481 O HETATM 1143 O HOH A 259 -2.281 18.120 43.202 1.00 29.83 O ANISOU 1143 O HOH A 259 4328 3553 3452 -1109 516 -1524 O HETATM 1144 O HOH A 260 10.911 6.011 18.544 1.00 22.40 O ANISOU 1144 O HOH A 260 3008 3213 2289 -1024 478 49 O HETATM 1145 O HOH A 261 24.464 4.507 26.047 1.00 33.37 O ANISOU 1145 O HOH A 261 3011 5807 3861 -519 -1505 774 O HETATM 1146 O HOH A 262 5.381 7.469 26.138 1.00 21.81 O ANISOU 1146 O HOH A 262 3308 2395 2583 539 1889 -351 O HETATM 1147 O HOH A 263 7.676 28.958 25.447 1.00 18.86 O ANISOU 1147 O HOH A 263 2149 2461 2557 -202 -21 669 O HETATM 1148 O HOH A 264 11.636 -2.075 24.818 1.00 25.68 O ANISOU 1148 O HOH A 264 3176 2656 3925 -1000 434 -1398 O HETATM 1149 O HOH A 265 2.385 6.390 23.282 1.00 36.05 O ANISOU 1149 O HOH A 265 4932 4951 3814 -314 89 492 O HETATM 1150 O HOH A 266 5.944 19.208 44.730 1.00 33.41 O ANISOU 1150 O HOH A 266 4908 5283 2503 319 -593 -710 O HETATM 1151 O HOH A 267 -4.690 23.379 37.170 1.00 25.94 O ANISOU 1151 O HOH A 267 4065 3874 1917 759 -233 -1007 O HETATM 1152 O HOH A 268 7.110 21.849 19.201 1.00 22.39 O ANISOU 1152 O HOH A 268 2705 2282 3519 -423 -513 278 O HETATM 1153 O HOH A 269 -5.423 29.716 31.314 1.00 90.59 O ANISOU 1153 O HOH A 269 7051 6713 20656 -915 2627 -1716 O HETATM 1154 O HOH A 270 -1.289 7.759 23.134 1.00 64.91 O ANISOU 1154 O HOH A 270 7050 3384 14228 -2738 2990 -4577 O HETATM 1155 O HOH A 271 7.345 28.407 20.266 1.00 46.12 O ANISOU 1155 O HOH A 271 4157 8434 4932 1033 -824 799 O HETATM 1156 O HOH A 272 5.403 20.166 16.725 1.00 30.09 O ANISOU 1156 O HOH A 272 4147 4708 2577 -1523 267 110 O HETATM 1157 O HOH A 273 8.795 34.690 35.543 1.00 21.53 O ANISOU 1157 O HOH A 273 2068 2039 4071 -562 919 -609 O HETATM 1158 O HOH A 274 -8.430 12.658 41.237 1.00 47.14 O ANISOU 1158 O HOH A 274 9141 3726 5042 256 -1170 2748 O HETATM 1159 O HOH A 275 -6.925 15.665 29.223 1.00 24.05 O ANISOU 1159 O HOH A 275 2599 4243 2295 -658 -1227 -867 O HETATM 1160 O HOH A 276 8.113 17.057 44.809 1.00 26.97 O ANISOU 1160 O HOH A 276 3357 3668 3222 -447 -349 -845 O HETATM 1161 O HOH A 277 12.112 15.462 17.426 1.00 33.69 O ANISOU 1161 O HOH A 277 3937 4278 4583 -206 -949 -2023 O HETATM 1162 O HOH A 278 18.519 28.236 37.711 1.00 24.09 O ANISOU 1162 O HOH A 278 3796 1929 3427 -449 -157 -750 O HETATM 1163 O HOH A 279 5.250 26.724 39.824 1.00 26.73 O ANISOU 1163 O HOH A 279 4633 2199 3323 548 663 -523 O HETATM 1164 O HOH A 280 3.892 24.576 19.842 1.00 53.13 O ANISOU 1164 O HOH A 280 8798 4333 7053 -1862 -548 -1256 O HETATM 1165 O HOH A 281 8.185 34.670 31.501 1.00 24.64 O ANISOU 1165 O HOH A 281 4608 1614 3140 54 322 489 O HETATM 1166 O HOH A 282 2.173 13.993 16.163 1.00 18.81 O ANISOU 1166 O HOH A 282 3793 1874 1478 -258 341 -66 O HETATM 1167 O HOH A 283 21.068 15.044 30.789 1.00 18.71 O ANISOU 1167 O HOH A 283 1066 2340 3703 340 121 -189 O HETATM 1168 O HOH A 284 -3.001 30.987 25.020 1.00 17.90 O ANISOU 1168 O HOH A 284 3782 1398 1621 102 -328 -163 O HETATM 1169 O HOH A 285 -1.758 2.589 35.934 1.00 22.83 O ANISOU 1169 O HOH A 285 3311 3242 2118 55 -505 -334 O HETATM 1170 O HOH A 286 5.907 16.248 17.371 1.00 25.83 O ANISOU 1170 O HOH A 286 2988 4690 2137 455 93 -248 O HETATM 1171 O HOH A 287 -3.930 16.912 16.375 1.00 21.83 O ANISOU 1171 O HOH A 287 3056 2460 2776 -376 -857 -35 O HETATM 1172 O HOH A 288 -1.476 20.554 25.622 1.00 26.14 O ANISOU 1172 O HOH A 288 1674 5561 2697 -1358 541 -233 O HETATM 1173 O HOH A 289 8.383 13.275 45.458 1.00 26.16 O ANISOU 1173 O HOH A 289 2551 3574 3813 355 1059 368 O HETATM 1174 O HOH A 290 6.350 35.661 35.008 1.00 22.15 O ANISOU 1174 O HOH A 290 2938 2429 3047 118 806 369 O HETATM 1175 O HOH A 291 14.513 29.847 35.052 1.00 27.08 O ANISOU 1175 O HOH A 291 2708 3665 3916 -1470 855 -835 O HETATM 1176 O HOH A 292 -5.394 19.265 16.846 1.00 26.30 O ANISOU 1176 O HOH A 292 3467 2884 3639 -505 645 490 O HETATM 1177 O HOH A 293 26.529 23.068 29.754 1.00 93.21 O ANISOU 1177 O HOH A 293 9163 10602 15648 -5833 10826 -10912 O CONECT 151 417 CONECT 417 151 CONECT 737 885 CONECT 885 737 MASTER 488 0 0 7 0 0 0 6 1117 1 4 10 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