HEADER SIGNALING PROTEIN 10-DEC-10 3PXO TITLE CRYSTAL STRUCTURE OF METARHODOPSIN II COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ACTIVE METARHODOPSIN II WITH ALL-TRANS RETINAL SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913 KEYWDS PROTEIN, RETINAL PROTEIN, PHOTORECEPTOR, ACTIVE STATE, CHROMOPHORE, KEYWDS 2 G-PROTEIN COUPLED RECEPTOR, GLYCOPROTEIN, LIPOPROTEIN, PALMITATE, KEYWDS 3 PHOSPHOPROTEIN, PHOTORECEPTOR PROTEIN, SENSORY TRANSDUCTION, KEYWDS 4 TRANSDUCER, TRANSMEMBRANE, VISION, SIGNALING PROTEIN, G-PROTEIN, KEYWDS 5 TRANSDUCIN, GALPHA SUBUNIT, MEMBRANE, RECEPTOR, GTP-BINDING, KEYWDS 6 MYRISTATE, NUCLEOTIDE-BINDING, G-PROTEIN-COUPLED RECEPTOR, KEYWDS 7 RHODOPSIN, OPSIN EXPDTA X-RAY DIFFRACTION AUTHOR H.-W.CHOE,Y.J.KIM,J.H.PARK,T.MORIZUMI,E.F.PAI,N.KRAUSS,K.P.HOFMANN, AUTHOR 2 P.SCHEERER,O.P.ERNST REVDAT 4 29-JUL-20 3PXO 1 COMPND REMARK HETNAM LINK REVDAT 4 2 1 SITE ATOM REVDAT 3 06-APR-11 3PXO 1 JRNL REVDAT 2 23-MAR-11 3PXO 1 JRNL REVDAT 1 09-MAR-11 3PXO 0 JRNL AUTH H.W.CHOE,Y.J.KIM,J.H.PARK,T.MORIZUMI,E.F.PAI,N.KRAUSS, JRNL AUTH 2 K.P.HOFMANN,P.SCHEERER,O.P.ERNST JRNL TITL CRYSTAL STRUCTURE OF METARHODOPSIN II. JRNL REF NATURE V. 471 651 2011 JRNL REFN ISSN 0028-0836 JRNL PMID 21389988 JRNL DOI 10.1038/NATURE09789 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0072 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.52 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 23795 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) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1253 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08 REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2840 REMARK 3 BIN FREE R VALUE SET COUNT : 91 REMARK 3 BIN FREE R VALUE : 0.3060 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2592 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 155 REMARK 3 SOLVENT ATOMS : 5 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.71000 REMARK 3 B22 (A**2) : -3.71000 REMARK 3 B33 (A**2) : 5.56000 REMARK 3 B12 (A**2) : -1.85000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.009 ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.320 ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 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 326 REMARK 3 ORIGIN FOR THE GROUP (A): -39.4545 -8.6444 38.9985 REMARK 3 T TENSOR REMARK 3 T11: 0.0061 T22: 0.0332 REMARK 3 T33: 0.0201 T12: -0.0018 REMARK 3 T13: 0.0017 T23: -0.0229 REMARK 3 L TENSOR REMARK 3 L11: 0.7678 L22: 0.0904 REMARK 3 L33: 0.1403 L12: 0.0298 REMARK 3 L13: -0.0461 L23: -0.0693 REMARK 3 S TENSOR REMARK 3 S11: 0.0017 S12: 0.0682 S13: -0.0192 REMARK 3 S21: -0.0220 S22: 0.0025 S23: 0.0035 REMARK 3 S31: 0.0210 S32: 0.0172 S33: -0.0041 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 401 A 404 REMARK 3 ORIGIN FOR THE GROUP (A): -79.8194 -7.3238 37.5689 REMARK 3 T TENSOR REMARK 3 T11: 0.0016 T22: 0.0180 REMARK 3 T33: 0.0237 T12: -0.0008 REMARK 3 T13: -0.0032 T23: 0.0016 REMARK 3 L TENSOR REMARK 3 L11: 4.2189 L22: 1.4198 REMARK 3 L33: 6.0659 L12: -2.4413 REMARK 3 L13: 1.1994 L23: -0.8955 REMARK 3 S TENSOR REMARK 3 S11: 0.0478 S12: -0.0314 S13: 0.1042 REMARK 3 S21: -0.0287 S22: 0.0286 S23: -0.0569 REMARK 3 S31: 0.0338 S32: -0.3219 S33: -0.0764 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 501 A 502 REMARK 3 ORIGIN FOR THE GROUP (A): -62.9277 -29.5065 43.6239 REMARK 3 T TENSOR REMARK 3 T11: 0.1712 T22: 0.0251 REMARK 3 T33: 0.0238 T12: 0.0421 REMARK 3 T13: 0.0473 T23: 0.0214 REMARK 3 L TENSOR REMARK 3 L11: 5.1807 L22: 0.1041 REMARK 3 L33: 2.1795 L12: 0.7344 REMARK 3 L13: 3.3601 L23: 0.4763 REMARK 3 S TENSOR REMARK 3 S11: 0.0032 S12: 0.1222 S13: -0.0514 REMARK 3 S21: 0.0009 S22: 0.0233 S23: -0.0066 REMARK 3 S31: -0.0005 S32: 0.0810 S33: -0.0264 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 601 A 602 REMARK 3 ORIGIN FOR THE GROUP (A): -41.0523 -9.2945 47.5285 REMARK 3 T TENSOR REMARK 3 T11: 0.0645 T22: 0.0266 REMARK 3 T33: 0.1464 T12: -0.0085 REMARK 3 T13: 0.0796 T23: -0.0446 REMARK 3 L TENSOR REMARK 3 L11: 3.6743 L22: 3.8618 REMARK 3 L33: 2.2519 L12: -3.7146 REMARK 3 L13: -2.5150 L23: 2.3753 REMARK 3 S TENSOR REMARK 3 S11: -0.2492 S12: 0.0682 S13: -0.4333 REMARK 3 S21: 0.2554 S22: -0.0188 S23: 0.3758 REMARK 3 S31: 0.0502 S32: -0.1127 S33: 0.2679 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 701 A 701 REMARK 3 ORIGIN FOR THE GROUP (A): -31.6963 10.1993 58.8064 REMARK 3 T TENSOR REMARK 3 T11: 0.0295 T22: 0.0487 REMARK 3 T33: 0.0112 T12: -0.0222 REMARK 3 T13: 0.0017 T23: 0.0128 REMARK 3 L TENSOR REMARK 3 L11: 6.0753 L22: 1.0716 REMARK 3 L33: 3.2677 L12: -0.0895 REMARK 3 L13: -1.3285 L23: 1.8046 REMARK 3 S TENSOR REMARK 3 S11: -0.0415 S12: 0.4057 S13: 0.0873 REMARK 3 S21: -0.1720 S22: 0.1049 S23: -0.0276 REMARK 3 S31: -0.2786 S32: 0.0945 S33: -0.0634 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 801 A 801 REMARK 3 ORIGIN FOR THE GROUP (A): -44.9266 -12.7341 35.9796 REMARK 3 T TENSOR REMARK 3 T11: 0.0156 T22: 0.0486 REMARK 3 T33: 0.0336 T12: 0.0200 REMARK 3 T13: 0.0021 T23: -0.0014 REMARK 3 L TENSOR REMARK 3 L11: 4.7813 L22: 0.2758 REMARK 3 L33: 1.7979 L12: -1.1463 REMARK 3 L13: -2.9103 L23: 0.6996 REMARK 3 S TENSOR REMARK 3 S11: -0.1250 S12: -0.0816 S13: -0.1023 REMARK 3 S21: 0.0339 S22: 0.0306 S23: 0.0254 REMARK 3 S31: 0.0834 S32: 0.0539 S33: 0.0944 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 349 A 353 REMARK 3 ORIGIN FOR THE GROUP (A): -47.6234 -8.0579 39.9536 REMARK 3 T TENSOR REMARK 3 T11: 0.0065 T22: 0.0075 REMARK 3 T33: 0.0209 T12: -0.0054 REMARK 3 T13: 0.0088 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 6.1444 L22: 0.1052 REMARK 3 L33: 0.7651 L12: -0.5084 REMARK 3 L13: -2.0146 L23: 0.0861 REMARK 3 S TENSOR REMARK 3 S11: 0.0651 S12: 0.0625 S13: 0.0476 REMARK 3 S21: 0.0014 S22: -0.0063 S23: 0.0276 REMARK 3 S31: -0.0330 S32: -0.0152 S33: -0.0587 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3PXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10. REMARK 100 THE DEPOSITION ID IS D_1000062939. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : BESSY REMARK 200 BEAMLINE : 14.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841 REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL - DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25082 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 33.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.700 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : 0.06600 REMARK 200 FOR THE DATA SET : 19.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.70 REMARK 200 R MERGE FOR SHELL (I) : 0.46300 REMARK 200 R SYM FOR SHELL (I) : 0.46300 REMARK 200 FOR SHELL : 3.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3DQB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 84.74 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 8.06 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0-3.4 M AMMONIUM SULFATE, 0.1 M REMARK 280 SODIUM ACETATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 120.91000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.80742 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.26667 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 120.91000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.80742 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.26667 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 120.91000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.80742 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.26667 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 120.91000 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 69.80742 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.26667 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 120.91000 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 69.80742 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.26667 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 120.91000 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 69.80742 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.26667 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 139.61484 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.53333 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 139.61484 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.53333 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 139.61484 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.53333 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 139.61484 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.53333 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 139.61484 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.53333 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 139.61484 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.53333 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8780 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31740 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 111.80000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 28 37.11 -93.18 REMARK 500 TYR A 29 4.90 -68.87 REMARK 500 ALA A 32 141.78 -172.66 REMARK 500 ARG A 69 39.40 -80.76 REMARK 500 SER A 176 -170.54 48.51 REMARK 500 HIS A 195 107.36 -15.92 REMARK 500 ASN A 199 47.82 89.54 REMARK 500 PHE A 212 -54.46 -129.87 REMARK 500 GLN A 237 41.32 -140.77 REMARK 500 GLN A 238 0.27 -62.33 REMARK 500 CYS A 323 -39.23 61.34 REMARK 500 LYS A 325 -105.08 -142.90 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3PQR RELATED DB: PDB DBREF 3PXO A 1 348 UNP P02699 OPSD_BOVIN 1 348 SEQRES 1 A 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE SEQRES 2 A 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA SEQRES 3 A 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET SEQRES 4 A 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE SEQRES 5 A 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS SEQRES 6 A 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN SEQRES 7 A 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE SEQRES 8 A 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL SEQRES 9 A 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA SEQRES 10 A 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL SEQRES 11 A 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET SEQRES 12 A 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY SEQRES 13 A 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA SEQRES 14 A 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY SEQRES 15 A 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS SEQRES 16 A 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE SEQRES 17 A 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE SEQRES 18 A 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA SEQRES 19 A 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU SEQRES 20 A 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA SEQRES 21 A 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE SEQRES 22 A 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE SEQRES 23 A 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA SEQRES 24 A 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN SEQRES 25 A 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS SEQRES 26 A 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER SEQRES 27 A 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA MODRES 3PXO ASN A 15 ASN GLYCOSYLATION SITE MODRES 3PXO ASN A 2 ASN GLYCOSYLATION SITE HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET MAN B 4 11 HET NAG C 1 14 HET NAG C 2 14 HET BOG A 601 20 HET BOG A 602 20 HET PLM A 701 17 HET RET A 801 20 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM PLM PALMITIC ACID HETNAM RET RETINAL FORMUL 2 NAG 4(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN C6 H12 O6 FORMUL 4 BOG 2(C14 H28 O6) FORMUL 6 PLM C16 H32 O2 FORMUL 7 RET C20 H28 O FORMUL 8 HOH *5(H2 O) HELIX 1 1 SER A 14 GLY A 18 5 5 HELIX 2 2 GLU A 33 HIS A 65 1 33 HELIX 3 3 LYS A 66 ARG A 69 5 4 HELIX 4 4 THR A 70 LEU A 72 5 3 HELIX 5 5 ASN A 73 GLY A 90 1 18 HELIX 6 6 GLY A 90 GLY A 101 1 12 HELIX 7 7 PHE A 105 LYS A 141 1 37 HELIX 8 8 GLY A 149 ALA A 169 1 21 HELIX 9 9 PRO A 170 GLY A 174 5 5 HELIX 10 10 ASN A 199 HIS A 211 1 13 HELIX 11 11 PHE A 212 GLN A 236 1 25 HELIX 12 12 SER A 240 HIS A 278 1 39 HELIX 13 13 ILE A 286 MET A 288 5 3 HELIX 14 14 THR A 289 THR A 297 1 9 HELIX 15 15 THR A 297 ILE A 307 1 11 HELIX 16 16 ASN A 310 CYS A 322 1 13 SHEET 1 A 2 THR A 4 GLY A 6 0 SHEET 2 A 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 B 2 TYR A 178 GLU A 181 0 SHEET 2 B 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.04 LINK ND2 ASN A 2 C1 NAG C 1 1555 1555 1.34 LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.34 LINK NZ LYS A 296 C15 RET A 801 1555 1555 1.33 LINK SG CYS A 323 C1 PLM A 701 1555 1555 1.84 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.42 LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.46 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.47 CRYST1 241.820 241.820 111.800 90.00 90.00 120.00 H 3 2 18 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 0.004135 0.002388 0.000000 0.00000 SCALE2 0.000000 0.004775 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008945 0.00000 ATOM 1 N MET A 1 -68.006 -25.087 40.399 1.00 98.21 N ANISOU 1 N MET A 1 12094 12286 12934 -262 -161 -231 N ATOM 2 CA MET A 1 -68.070 -23.619 40.104 1.00 98.63 C ANISOU 2 CA MET A 1 12164 12391 12921 -252 -159 -222 C ATOM 3 C MET A 1 -67.472 -22.788 41.240 1.00 95.86 C ANISOU 3 C MET A 1 11827 12046 12548 -230 -145 -179 C ATOM 4 O MET A 1 -68.144 -22.494 42.235 1.00 96.49 O ANISOU 4 O MET A 1 11901 12130 12630 -226 -141 -136 O ATOM 5 CB MET A 1 -69.514 -23.189 39.839 1.00 99.34 C ANISOU 5 CB MET A 1 12242 12507 12995 -264 -169 -209 C ATOM 6 CG MET A 1 -70.005 -23.438 38.417 1.00110.18 C ANISOU 6 CG MET A 1 13605 13901 14358 -284 -184 -257 C ATOM 7 SD MET A 1 -69.710 -22.064 37.270 1.00122.34 S ANISOU 7 SD MET A 1 15157 15501 15824 -277 -187 -273 S ATOM 8 CE MET A 1 -70.654 -20.741 38.023 1.00122.78 C ANISOU 8 CE MET A 1 15214 15584 15851 -266 -182 -213 C ATOM 9 N ASN A 2 -66.207 -22.405 41.083 1.00 92.87 N ANISOU 9 N ASN A 2 11465 11671 12148 -216 -137 -194 N ATOM 10 CA ASN A 2 -65.467 -21.735 42.156 1.00 88.01 C ANISOU 10 CA ASN A 2 10862 11060 11516 -197 -123 -160 C ATOM 11 C ASN A 2 -65.226 -20.242 41.943 1.00 78.56 C ANISOU 11 C ASN A 2 9682 9903 10266 -185 -118 -156 C ATOM 12 O ASN A 2 -64.795 -19.546 42.853 1.00 75.00 O ANISOU 12 O ASN A 2 9238 9460 9799 -171 -108 -130 O ATOM 13 CB ASN A 2 -64.153 -22.470 42.430 1.00 90.25 C ANISOU 13 CB ASN A 2 11150 11315 11826 -189 -116 -170 C ATOM 14 CG ASN A 2 -64.359 -23.742 43.238 1.00103.65 C ANISOU 14 CG ASN A 2 12828 12972 13581 -194 -115 -148 C ATOM 15 OD1 ASN A 2 -65.108 -23.749 44.221 1.00112.14 O ANISOU 15 OD1 ASN A 2 13892 14050 14667 -195 -114 -105 O ATOM 16 ND2 ASN A 2 -63.685 -24.824 42.834 1.00120.87 N ANISOU 16 ND2 ASN A 2 15002 15117 15804 -198 -116 -175 N ATOM 17 N GLY A 3 -65.520 -19.763 40.740 1.00 71.30 N ANISOU 17 N GLY A 3 8763 9007 9319 -192 -126 -182 N ATOM 18 CA GLY A 3 -65.362 -18.366 40.411 1.00 63.04 C ANISOU 18 CA GLY A 3 7728 7995 8229 -182 -123 -175 C ATOM 19 C GLY A 3 -66.597 -17.728 39.812 1.00 57.70 C ANISOU 19 C GLY A 3 7041 7347 7533 -190 -131 -167 C ATOM 20 O GLY A 3 -67.678 -18.309 39.812 1.00 61.08 O ANISOU 20 O GLY A 3 7455 7771 7981 -203 -140 -163 O ATOM 21 N THR A 4 -66.426 -16.512 39.312 1.00 52.44 N ANISOU 21 N THR A 4 6382 6711 6833 -182 -128 -162 N ATOM 22 CA THR A 4 -67.484 -15.774 38.659 1.00 47.17 C ANISOU 22 CA THR A 4 5702 6074 6146 -187 -135 -150 C ATOM 23 C THR A 4 -66.876 -15.099 37.439 1.00 53.20 C ANISOU 23 C THR A 4 6469 6870 6876 -186 -138 -165 C ATOM 24 O THR A 4 -66.077 -14.185 37.582 1.00 55.82 O ANISOU 24 O THR A 4 6812 7206 7193 -171 -128 -155 O ATOM 25 CB THR A 4 -68.043 -14.694 39.592 1.00 44.92 C ANISOU 25 CB THR A 4 5417 5793 5857 -174 -126 -111 C ATOM 26 OG1 THR A 4 -68.624 -15.301 40.754 1.00 42.79 O ANISOU 26 OG1 THR A 4 5142 5502 5615 -175 -122 -94 O ATOM 27 CG2 THR A 4 -69.072 -13.840 38.885 1.00 21.26 C ANISOU 27 CG2 THR A 4 2407 2828 2844 -178 -132 -95 C ATOM 28 N GLU A 5 -67.228 -15.559 36.241 1.00 55.45 N ANISOU 28 N GLU A 5 6742 7178 7149 -201 -152 -190 N ATOM 29 CA GLU A 5 -66.668 -14.978 35.030 1.00 53.98 C ANISOU 29 CA GLU A 5 6553 7030 6926 -201 -155 -203 C ATOM 30 C GLU A 5 -67.409 -13.723 34.644 1.00 55.35 C ANISOU 30 C GLU A 5 6715 7238 7077 -197 -156 -167 C ATOM 31 O GLU A 5 -68.538 -13.486 35.080 1.00 60.55 O ANISOU 31 O GLU A 5 7364 7895 7747 -199 -158 -142 O ATOM 32 CB GLU A 5 -66.700 -15.958 33.870 1.00 55.21 C ANISOU 32 CB GLU A 5 6697 7206 7074 -219 -168 -248 C ATOM 33 CG GLU A 5 -65.927 -17.248 34.091 1.00 62.96 C ANISOU 33 CG GLU A 5 7686 8151 8084 -223 -166 -288 C ATOM 34 CD GLU A 5 -66.371 -18.331 33.127 1.00 78.81 C ANISOU 34 CD GLU A 5 9677 10171 10097 -244 -180 -335 C ATOM 35 OE1 GLU A 5 -67.588 -18.646 33.116 1.00 90.56 O ANISOU 35 OE1 GLU A 5 11150 11662 11597 -259 -190 -330 O ATOM 36 OE2 GLU A 5 -65.518 -18.855 32.373 1.00 76.80 O ANISOU 36 OE2 GLU A 5 9423 9925 9834 -247 -180 -379 O ATOM 37 N GLY A 6 -66.745 -12.922 33.821 1.00 57.31 N ANISOU 37 N GLY A 6 6962 7517 7295 -191 -154 -164 N ATOM 38 CA GLY A 6 -67.210 -11.616 33.397 1.00 54.66 C ANISOU 38 CA GLY A 6 6613 7213 6941 -185 -153 -125 C ATOM 39 C GLY A 6 -66.445 -11.338 32.127 1.00 58.48 C ANISOU 39 C GLY A 6 7090 7740 7389 -187 -157 -136 C ATOM 40 O GLY A 6 -65.439 -12.009 31.859 1.00 57.62 O ANISOU 40 O GLY A 6 6991 7627 7273 -189 -156 -172 O ATOM 41 N PRO A 7 -66.930 -10.384 31.308 1.00 63.66 N ANISOU 41 N PRO A 7 7726 8440 8022 -187 -162 -103 N ATOM 42 CA PRO A 7 -66.292 -10.082 30.025 1.00 64.78 C ANISOU 42 CA PRO A 7 7854 8633 8125 -190 -166 -107 C ATOM 43 C PRO A 7 -64.806 -9.733 30.155 1.00 69.78 C ANISOU 43 C PRO A 7 8504 9252 8755 -176 -153 -113 C ATOM 44 O PRO A 7 -63.994 -10.162 29.318 1.00 75.25 O ANISOU 44 O PRO A 7 9196 9975 9422 -181 -156 -142 O ATOM 45 CB PRO A 7 -67.093 -8.888 29.493 1.00 61.30 C ANISOU 45 CB PRO A 7 7388 8231 7672 -187 -169 -53 C ATOM 46 CG PRO A 7 -67.971 -8.446 30.605 1.00 66.59 C ANISOU 46 CG PRO A 7 8062 8860 8379 -179 -162 -24 C ATOM 47 CD PRO A 7 -68.182 -9.628 31.483 1.00 65.30 C ANISOU 47 CD PRO A 7 7916 8655 8238 -185 -164 -60 C ATOM 48 N ASN A 8 -64.445 -9.010 31.215 1.00 67.88 N ANISOU 48 N ASN A 8 8280 8969 8543 -160 -139 -89 N ATOM 49 CA ASN A 8 -63.102 -8.460 31.331 1.00 64.62 C ANISOU 49 CA ASN A 8 7879 8545 8128 -148 -127 -87 C ATOM 50 C ASN A 8 -62.312 -8.901 32.561 1.00 63.81 C ANISOU 50 C ASN A 8 7803 8388 8052 -139 -117 -108 C ATOM 51 O ASN A 8 -61.371 -8.199 32.973 1.00 63.72 O ANISOU 51 O ASN A 8 7802 8360 8048 -127 -105 -98 O ATOM 52 CB ASN A 8 -63.212 -6.941 31.356 1.00 68.31 C ANISOU 52 CB ASN A 8 8335 9016 8604 -136 -119 -35 C ATOM 53 CG ASN A 8 -62.993 -6.324 30.007 1.00 69.29 C ANISOU 53 CG ASN A 8 8435 9196 8695 -138 -124 -12 C ATOM 54 OD1 ASN A 8 -62.491 -6.973 29.093 1.00 66.26 O ANISOU 54 OD1 ASN A 8 8047 8850 8278 -147 -132 -39 O ATOM 55 ND2 ASN A 8 -63.354 -5.052 29.874 1.00 72.05 N ANISOU 55 ND2 ASN A 8 8766 9552 9056 -130 -120 40 N ATOM 56 N PHE A 9 -62.686 -10.034 33.161 1.00 57.48 N ANISOU 56 N PHE A 9 7011 7561 7267 -146 -120 -136 N ATOM 57 CA PHE A 9 -62.203 -10.351 34.501 1.00 55.92 C ANISOU 57 CA PHE A 9 6833 7315 7098 -138 -110 -143 C ATOM 58 C PHE A 9 -62.645 -11.716 35.045 1.00 57.83 C ANISOU 58 C PHE A 9 7081 7532 7360 -147 -115 -169 C ATOM 59 O PHE A 9 -63.505 -12.381 34.471 1.00 61.55 O ANISOU 59 O PHE A 9 7540 8019 7829 -161 -127 -181 O ATOM 60 CB PHE A 9 -62.669 -9.262 35.470 1.00 53.99 C ANISOU 60 CB PHE A 9 6589 7051 6872 -127 -100 -107 C ATOM 61 CG PHE A 9 -64.151 -9.270 35.715 1.00 55.20 C ANISOU 61 CG PHE A 9 6730 7206 7037 -132 -106 -90 C ATOM 62 CD1 PHE A 9 -64.730 -10.226 36.551 1.00 50.05 C ANISOU 62 CD1 PHE A 9 6083 6530 6404 -137 -108 -101 C ATOM 63 CD2 PHE A 9 -64.974 -8.333 35.100 1.00 55.30 C ANISOU 63 CD2 PHE A 9 6724 7245 7043 -132 -109 -58 C ATOM 64 CE1 PHE A 9 -66.105 -10.236 36.767 1.00 52.81 C ANISOU 64 CE1 PHE A 9 6419 6882 6763 -143 -113 -84 C ATOM 65 CE2 PHE A 9 -66.358 -8.339 35.318 1.00 47.50 C ANISOU 65 CE2 PHE A 9 5723 6259 6065 -137 -114 -41 C ATOM 66 CZ PHE A 9 -66.920 -9.284 36.152 1.00 42.54 C ANISOU 66 CZ PHE A 9 5101 5608 5455 -142 -116 -55 C ATOM 67 N TYR A 10 -62.073 -12.109 36.182 1.00 54.95 N ANISOU 67 N TYR A 10 6731 7130 7018 -140 -107 -174 N ATOM 68 CA TYR A 10 -62.418 -13.361 36.820 1.00 51.26 C ANISOU 68 CA TYR A 10 6265 6634 6576 -147 -110 -189 C ATOM 69 C TYR A 10 -62.300 -13.214 38.335 1.00 51.31 C ANISOU 69 C TYR A 10 6282 6611 6605 -136 -99 -169 C ATOM 70 O TYR A 10 -61.202 -13.108 38.870 1.00 54.72 O ANISOU 70 O TYR A 10 6725 7029 7038 -126 -90 -172 O ATOM 71 CB TYR A 10 -61.540 -14.509 36.290 1.00 48.16 C ANISOU 71 CB TYR A 10 5877 6235 6187 -153 -113 -229 C ATOM 72 CG TYR A 10 -61.835 -15.837 36.956 1.00 55.33 C ANISOU 72 CG TYR A 10 6784 7108 7131 -160 -115 -243 C ATOM 73 CD1 TYR A 10 -62.861 -16.666 36.494 1.00 57.60 C ANISOU 73 CD1 TYR A 10 7058 7397 7432 -176 -127 -258 C ATOM 74 CD2 TYR A 10 -61.118 -16.244 38.081 1.00 59.02 C ANISOU 74 CD2 TYR A 10 7261 7541 7622 -150 -106 -236 C ATOM 75 CE1 TYR A 10 -63.147 -17.869 37.125 1.00 58.42 C ANISOU 75 CE1 TYR A 10 7157 7465 7575 -183 -129 -266 C ATOM 76 CE2 TYR A 10 -61.401 -17.436 38.722 1.00 63.06 C ANISOU 76 CE2 TYR A 10 7768 8021 8172 -156 -108 -240 C ATOM 77 CZ TYR A 10 -62.414 -18.245 38.241 1.00 65.00 C ANISOU 77 CZ TYR A 10 7999 8263 8434 -172 -119 -254 C ATOM 78 OH TYR A 10 -62.685 -19.421 38.893 1.00 67.09 O ANISOU 78 OH TYR A 10 8257 8493 8743 -178 -120 -255 O ATOM 79 N VAL A 11 -63.434 -13.195 39.023 1.00 50.05 N ANISOU 79 N VAL A 11 6114 6444 6459 -139 -100 -149 N ATOM 80 CA VAL A 11 -63.436 -13.102 40.470 1.00 52.54 C ANISOU 80 CA VAL A 11 6434 6739 6791 -130 -89 -131 C ATOM 81 C VAL A 11 -63.377 -14.510 41.052 1.00 58.22 C ANISOU 81 C VAL A 11 7152 7433 7535 -136 -92 -140 C ATOM 82 O VAL A 11 -64.300 -15.300 40.849 1.00 61.27 O ANISOU 82 O VAL A 11 7528 7816 7938 -148 -101 -142 O ATOM 83 CB VAL A 11 -64.709 -12.397 40.996 1.00 53.34 C ANISOU 83 CB VAL A 11 6524 6847 6895 -128 -87 -104 C ATOM 84 CG1 VAL A 11 -64.659 -12.239 42.517 1.00 51.34 C ANISOU 84 CG1 VAL A 11 6272 6581 6653 -118 -75 -88 C ATOM 85 CG2 VAL A 11 -64.910 -11.048 40.314 1.00 52.86 C ANISOU 85 CG2 VAL A 11 6458 6808 6817 -123 -86 -91 C ATOM 86 N PRO A 12 -62.303 -14.824 41.804 1.00 59.73 N ANISOU 86 N PRO A 12 7352 7607 7734 -128 -84 -142 N ATOM 87 CA PRO A 12 -62.150 -16.129 42.467 1.00 55.38 C ANISOU 87 CA PRO A 12 6798 7032 7213 -132 -84 -142 C ATOM 88 C PRO A 12 -63.109 -16.335 43.641 1.00 54.62 C ANISOU 88 C PRO A 12 6690 6930 7133 -132 -82 -112 C ATOM 89 O PRO A 12 -62.680 -16.703 44.729 1.00 57.35 O ANISOU 89 O PRO A 12 7034 7267 7490 -127 -75 -95 O ATOM 90 CB PRO A 12 -60.717 -16.080 42.994 1.00 54.24 C ANISOU 90 CB PRO A 12 6663 6879 7065 -120 -75 -145 C ATOM 91 CG PRO A 12 -60.461 -14.629 43.220 1.00 55.74 C ANISOU 91 CG PRO A 12 6860 7089 7228 -110 -67 -135 C ATOM 92 CD PRO A 12 -61.160 -13.932 42.082 1.00 58.92 C ANISOU 92 CD PRO A 12 7261 7510 7615 -115 -73 -141 C ATOM 93 N PHE A 13 -64.397 -16.108 43.430 1.00 52.07 N ANISOU 93 N PHE A 13 6357 6618 6810 -140 -88 -102 N ATOM 94 CA PHE A 13 -65.373 -16.344 44.479 1.00 53.10 C ANISOU 94 CA PHE A 13 6474 6747 6955 -141 -85 -73 C ATOM 95 C PHE A 13 -66.676 -16.728 43.794 1.00 59.05 C ANISOU 95 C PHE A 13 7215 7502 7719 -156 -98 -73 C ATOM 96 O PHE A 13 -66.961 -16.259 42.679 1.00 61.11 O ANISOU 96 O PHE A 13 7478 7778 7964 -161 -105 -89 O ATOM 97 CB PHE A 13 -65.538 -15.091 45.342 1.00 52.37 C ANISOU 97 CB PHE A 13 6382 6674 6841 -128 -74 -54 C ATOM 98 CG PHE A 13 -66.328 -15.307 46.611 1.00 50.94 C ANISOU 98 CG PHE A 13 6187 6498 6671 -127 -68 -24 C ATOM 99 CD1 PHE A 13 -65.739 -15.889 47.727 1.00 48.49 C ANISOU 99 CD1 PHE A 13 5872 6184 6368 -122 -61 -10 C ATOM 100 CD2 PHE A 13 -67.652 -14.879 46.706 1.00 52.38 C ANISOU 100 CD2 PHE A 13 6357 6694 6852 -129 -69 -9 C ATOM 101 CE1 PHE A 13 -66.472 -16.086 48.901 1.00 47.31 C ANISOU 101 CE1 PHE A 13 5705 6046 6224 -121 -56 21 C ATOM 102 CE2 PHE A 13 -68.387 -15.052 47.889 1.00 42.51 C ANISOU 102 CE2 PHE A 13 5091 5453 5608 -128 -63 18 C ATOM 103 CZ PHE A 13 -67.802 -15.667 48.977 1.00 42.05 C ANISOU 103 CZ PHE A 13 5027 5393 5556 -124 -56 33 C ATOM 104 N SER A 14 -67.446 -17.604 44.439 1.00 58.81 N ANISOU 104 N SER A 14 7170 7459 7717 -164 -100 -55 N ATOM 105 CA SER A 14 -68.650 -18.148 43.828 1.00 58.48 C ANISOU 105 CA SER A 14 7114 7416 7691 -180 -113 -57 C ATOM 106 C SER A 14 -69.822 -17.195 43.981 1.00 58.52 C ANISOU 106 C SER A 14 7111 7446 7678 -178 -112 -35 C ATOM 107 O SER A 14 -70.125 -16.756 45.096 1.00 57.73 O ANISOU 107 O SER A 14 7006 7354 7576 -168 -102 -7 O ATOM 108 CB SER A 14 -68.999 -19.510 44.430 1.00 58.20 C ANISOU 108 CB SER A 14 7063 7353 7699 -191 -116 -43 C ATOM 109 OG SER A 14 -70.386 -19.783 44.320 1.00 53.69 O ANISOU 109 OG SER A 14 6474 6785 7141 -204 -125 -31 O ATOM 110 N ASN A 15 -70.499 -16.912 42.865 1.00 56.80 N ANISOU 110 N ASN A 15 6889 7244 7450 -188 -123 -47 N ATOM 111 CA ASN A 15 -71.655 -16.025 42.897 1.00 54.79 C ANISOU 111 CA ASN A 15 6623 7012 7182 -186 -122 -25 C ATOM 112 C ASN A 15 -72.975 -16.719 43.204 1.00 57.25 C ANISOU 112 C ASN A 15 6915 7321 7518 -199 -130 -7 C ATOM 113 O ASN A 15 -74.045 -16.196 42.888 1.00 59.14 O ANISOU 113 O ASN A 15 7142 7580 7749 -202 -134 6 O ATOM 114 CB ASN A 15 -71.778 -15.193 41.620 1.00 52.52 C ANISOU 114 CB ASN A 15 6337 6749 6869 -187 -129 -38 C ATOM 115 CG ASN A 15 -72.614 -13.948 41.829 1.00 52.61 C ANISOU 115 CG ASN A 15 6340 6782 6868 -177 -123 -10 C ATOM 116 OD1 ASN A 15 -72.839 -13.531 42.966 1.00 59.83 O ANISOU 116 OD1 ASN A 15 7253 7693 7788 -166 -110 10 O ATOM 117 ND2 ASN A 15 -73.074 -13.346 40.745 1.00 53.76 N ANISOU 117 ND2 ASN A 15 6478 6952 6997 -181 -131 -10 N ATOM 118 N LYS A 16 -72.916 -17.876 43.855 1.00 60.13 N ANISOU 118 N LYS A 16 7272 7661 7912 -206 -130 -1 N ATOM 119 CA LYS A 16 -74.148 -18.598 44.170 1.00 60.65 C ANISOU 119 CA LYS A 16 7317 7722 8006 -219 -137 20 C ATOM 120 C LYS A 16 -75.022 -17.903 45.209 1.00 57.76 C ANISOU 120 C LYS A 16 6940 7375 7631 -209 -127 58 C ATOM 121 O LYS A 16 -76.192 -18.198 45.311 1.00 63.18 O ANISOU 121 O LYS A 16 7607 8066 8332 -219 -133 76 O ATOM 122 CB LYS A 16 -73.877 -20.063 44.526 1.00 58.57 C ANISOU 122 CB LYS A 16 7045 7423 7785 -231 -141 19 C ATOM 123 CG LYS A 16 -73.681 -20.356 45.978 1.00 65.37 C ANISOU 123 CG LYS A 16 7900 8277 8661 -221 -129 55 C ATOM 124 CD LYS A 16 -72.794 -21.592 46.137 1.00 82.95 C ANISOU 124 CD LYS A 16 10125 10467 10926 -226 -130 48 C ATOM 125 CE LYS A 16 -72.186 -21.669 47.536 1.00 89.73 C ANISOU 125 CE LYS A 16 10980 11326 11787 -212 -116 83 C ATOM 126 NZ LYS A 16 -70.783 -22.162 47.481 1.00 91.88 N ANISOU 126 NZ LYS A 16 11264 11575 12071 -206 -113 66 N ATOM 127 N THR A 17 -74.468 -16.963 45.958 1.00 60.19 N ANISOU 127 N THR A 17 7258 7696 7917 -190 -112 67 N ATOM 128 CA THR A 17 -75.267 -16.232 46.941 1.00 59.71 C ANISOU 128 CA THR A 17 7185 7656 7847 -179 -100 96 C ATOM 129 C THR A 17 -75.570 -14.833 46.425 1.00 59.19 C ANISOU 129 C THR A 17 7122 7610 7756 -168 -96 91 C ATOM 130 O THR A 17 -76.211 -14.034 47.108 1.00 59.81 O ANISOU 130 O THR A 17 7191 7706 7827 -157 -84 109 O ATOM 131 CB THR A 17 -74.594 -16.177 48.348 1.00 59.90 C ANISOU 131 CB THR A 17 7209 7684 7865 -165 -84 112 C ATOM 132 OG1 THR A 17 -73.535 -15.210 48.346 1.00 70.12 O ANISOU 132 OG1 THR A 17 8523 8985 9136 -150 -74 92 O ATOM 133 CG2 THR A 17 -74.037 -17.544 48.752 1.00 46.47 C ANISOU 133 CG2 THR A 17 5504 5961 6191 -173 -88 119 C ATOM 134 N GLY A 18 -75.106 -14.549 45.211 1.00 59.14 N ANISOU 134 N GLY A 18 7129 7603 7740 -172 -104 67 N ATOM 135 CA GLY A 18 -75.525 -13.353 44.475 1.00 59.85 C ANISOU 135 CA GLY A 18 7216 7712 7812 -165 -104 68 C ATOM 136 C GLY A 18 -74.792 -12.074 44.831 1.00 61.27 C ANISOU 136 C GLY A 18 7407 7896 7976 -145 -88 65 C ATOM 137 O GLY A 18 -75.138 -11.002 44.331 1.00 63.45 O ANISOU 137 O GLY A 18 7678 8184 8245 -138 -85 71 O ATOM 138 N VAL A 19 -73.756 -12.193 45.666 1.00 60.75 N ANISOU 138 N VAL A 19 7354 7820 7908 -137 -77 56 N ATOM 139 CA VAL A 19 -73.053 -11.035 46.252 1.00 53.59 C ANISOU 139 CA VAL A 19 6455 6917 6990 -118 -61 51 C ATOM 140 C VAL A 19 -71.869 -10.501 45.427 1.00 53.78 C ANISOU 140 C VAL A 19 6496 6935 7003 -114 -61 30 C ATOM 141 O VAL A 19 -71.491 -9.333 45.568 1.00 53.23 O ANISOU 141 O VAL A 19 6429 6867 6928 -101 -50 27 O ATOM 142 CB VAL A 19 -72.567 -11.331 47.698 1.00 52.76 C ANISOU 142 CB VAL A 19 6350 6813 6885 -111 -48 54 C ATOM 143 CG1 VAL A 19 -73.719 -11.799 48.577 1.00 42.89 C ANISOU 143 CG1 VAL A 19 5079 5575 5643 -114 -46 79 C ATOM 144 CG2 VAL A 19 -71.409 -12.343 47.709 1.00 49.29 C ANISOU 144 CG2 VAL A 19 5924 6358 6446 -117 -53 42 C ATOM 145 N VAL A 20 -71.289 -11.359 44.585 1.00 51.80 N ANISOU 145 N VAL A 20 6256 6676 6751 -126 -74 15 N ATOM 146 CA VAL A 20 -70.171 -10.984 43.708 1.00 50.93 C ANISOU 146 CA VAL A 20 6159 6563 6627 -124 -76 -4 C ATOM 147 C VAL A 20 -70.469 -9.810 42.776 1.00 50.20 C ANISOU 147 C VAL A 20 6062 6486 6527 -119 -77 3 C ATOM 148 O VAL A 20 -71.483 -9.802 42.099 1.00 52.00 O ANISOU 148 O VAL A 20 6276 6728 6755 -127 -86 15 O ATOM 149 CB VAL A 20 -69.699 -12.185 42.868 1.00 49.94 C ANISOU 149 CB VAL A 20 6040 6431 6503 -138 -90 -24 C ATOM 150 CG1 VAL A 20 -68.592 -11.778 41.923 1.00 40.12 C ANISOU 150 CG1 VAL A 20 4810 5192 5243 -136 -92 -43 C ATOM 151 CG2 VAL A 20 -69.221 -13.298 43.790 1.00 56.63 C ANISOU 151 CG2 VAL A 20 6892 7259 7366 -141 -88 -27 C ATOM 152 N ARG A 21 -69.587 -8.813 42.763 1.00 52.40 N ANISOU 152 N ARG A 21 6348 6762 6799 -107 -66 -2 N ATOM 153 CA ARG A 21 -69.704 -7.681 41.827 1.00 54.83 C ANISOU 153 CA ARG A 21 6648 7081 7103 -102 -66 10 C ATOM 154 C ARG A 21 -68.444 -7.565 40.997 1.00 54.31 C ANISOU 154 C ARG A 21 6594 7017 7023 -102 -69 -5 C ATOM 155 O ARG A 21 -67.411 -8.105 41.366 1.00 57.45 O ANISOU 155 O ARG A 21 7008 7403 7417 -102 -67 -24 O ATOM 156 CB ARG A 21 -69.930 -6.360 42.563 1.00 50.75 C ANISOU 156 CB ARG A 21 6123 6557 6601 -86 -49 22 C ATOM 157 CG ARG A 21 -71.029 -6.412 43.599 1.00 54.39 C ANISOU 157 CG ARG A 21 6572 7018 7074 -82 -43 33 C ATOM 158 CD ARG A 21 -72.397 -6.091 43.024 1.00 51.57 C ANISOU 158 CD ARG A 21 6195 6675 6725 -85 -48 58 C ATOM 159 NE ARG A 21 -73.453 -6.277 44.022 1.00 59.24 N ANISOU 159 NE ARG A 21 7154 7648 7707 -83 -42 67 N ATOM 160 CZ ARG A 21 -74.019 -7.448 44.313 1.00 66.40 C ANISOU 160 CZ ARG A 21 8059 8559 8611 -95 -51 69 C ATOM 161 NH1 ARG A 21 -73.641 -8.562 43.686 1.00 68.20 N ANISOU 161 NH1 ARG A 21 8296 8786 8830 -110 -67 59 N ATOM 162 NH2 ARG A 21 -74.967 -7.510 45.240 1.00 63.65 N ANISOU 162 NH2 ARG A 21 7697 8216 8272 -91 -44 82 N ATOM 163 N SER A 22 -68.543 -6.867 39.872 1.00 56.37 N ANISOU 163 N SER A 22 6846 7295 7277 -103 -74 9 N ATOM 164 CA SER A 22 -67.387 -6.514 39.055 1.00 56.88 C ANISOU 164 CA SER A 22 6918 7367 7328 -101 -74 1 C ATOM 165 C SER A 22 -66.283 -5.875 39.904 1.00 61.53 C ANISOU 165 C SER A 22 7520 7933 7926 -88 -59 -8 C ATOM 166 O SER A 22 -66.549 -4.956 40.690 1.00 63.95 O ANISOU 166 O SER A 22 7821 8227 8252 -77 -46 2 O ATOM 167 CB SER A 22 -67.819 -5.522 37.983 1.00 54.99 C ANISOU 167 CB SER A 22 6659 7150 7085 -99 -78 30 C ATOM 168 OG SER A 22 -66.756 -5.188 37.122 1.00 54.06 O ANISOU 168 OG SER A 22 6544 7045 6952 -99 -79 28 O ATOM 169 N PRO A 23 -65.033 -6.351 39.747 1.00 60.93 N ANISOU 169 N PRO A 23 7460 7854 7838 -90 -60 -29 N ATOM 170 CA PRO A 23 -63.919 -5.694 40.422 1.00 59.67 C ANISOU 170 CA PRO A 23 7309 7677 7684 -79 -47 -37 C ATOM 171 C PRO A 23 -63.671 -4.277 39.868 1.00 57.92 C ANISOU 171 C PRO A 23 7078 7458 7472 -71 -40 -18 C ATOM 172 O PRO A 23 -62.911 -3.510 40.458 1.00 58.27 O ANISOU 172 O PRO A 23 7126 7486 7529 -62 -28 -24 O ATOM 173 CB PRO A 23 -62.739 -6.611 40.099 1.00 61.52 C ANISOU 173 CB PRO A 23 7560 7913 7903 -84 -52 -61 C ATOM 174 CG PRO A 23 -63.090 -7.177 38.766 1.00 60.42 C ANISOU 174 CG PRO A 23 7414 7797 7746 -95 -66 -61 C ATOM 175 CD PRO A 23 -64.572 -7.416 38.840 1.00 58.24 C ANISOU 175 CD PRO A 23 7125 7527 7477 -101 -73 -48 C ATOM 176 N PHE A 24 -64.300 -3.938 38.745 1.00 52.53 N ANISOU 176 N PHE A 24 6379 6796 6784 -74 -48 5 N ATOM 177 CA PHE A 24 -64.255 -2.578 38.252 1.00 52.96 C ANISOU 177 CA PHE A 24 6417 6851 6854 -66 -41 33 C ATOM 178 C PHE A 24 -65.367 -1.685 38.827 1.00 55.53 C ANISOU 178 C PHE A 24 6725 7162 7210 -58 -32 53 C ATOM 179 O PHE A 24 -65.345 -0.482 38.627 1.00 58.73 O ANISOU 179 O PHE A 24 7115 7559 7640 -49 -23 76 O ATOM 180 CB PHE A 24 -64.306 -2.539 36.724 1.00 52.48 C ANISOU 180 CB PHE A 24 6342 6826 6772 -73 -53 54 C ATOM 181 CG PHE A 24 -63.210 -3.309 36.056 1.00 57.18 C ANISOU 181 CG PHE A 24 6950 7438 7337 -81 -61 32 C ATOM 182 CD1 PHE A 24 -61.878 -3.094 36.391 1.00 65.06 C ANISOU 182 CD1 PHE A 24 7962 8420 8337 -75 -52 17 C ATOM 183 CD2 PHE A 24 -63.506 -4.250 35.076 1.00 56.96 C ANISOU 183 CD2 PHE A 24 6919 7445 7279 -94 -76 24 C ATOM 184 CE1 PHE A 24 -60.851 -3.820 35.762 1.00 56.27 C ANISOU 184 CE1 PHE A 24 6859 7323 7197 -81 -58 -4 C ATOM 185 CE2 PHE A 24 -62.491 -4.978 34.445 1.00 57.92 C ANISOU 185 CE2 PHE A 24 7049 7583 7373 -100 -81 -2 C ATOM 186 CZ PHE A 24 -61.160 -4.756 34.790 1.00 51.73 C ANISOU 186 CZ PHE A 24 6280 6781 6593 -92 -72 -14 C ATOM 187 N GLU A 25 -66.328 -2.244 39.555 1.00 57.75 N ANISOU 187 N GLU A 25 7007 7441 7495 -59 -33 47 N ATOM 188 CA GLU A 25 -67.505 -1.451 39.936 1.00 56.29 C ANISOU 188 CA GLU A 25 6802 7248 7337 -52 -25 68 C ATOM 189 C GLU A 25 -67.823 -1.350 41.426 1.00 53.32 C ANISOU 189 C GLU A 25 6429 6851 6979 -44 -11 50 C ATOM 190 O GLU A 25 -68.528 -0.444 41.836 1.00 55.35 O ANISOU 190 O GLU A 25 6669 7096 7264 -33 0 62 O ATOM 191 CB GLU A 25 -68.749 -1.925 39.175 1.00 60.90 C ANISOU 191 CB GLU A 25 7371 7858 7910 -60 -39 91 C ATOM 192 CG GLU A 25 -68.703 -1.712 37.657 1.00 69.63 C ANISOU 192 CG GLU A 25 8462 8994 9000 -67 -51 117 C ATOM 193 CD GLU A 25 -68.610 -0.248 37.274 1.00 84.55 C ANISOU 193 CD GLU A 25 10332 10877 10918 -55 -41 151 C ATOM 194 OE1 GLU A 25 -69.232 0.592 37.963 1.00 92.91 O ANISOU 194 OE1 GLU A 25 11377 11911 12012 -43 -28 163 O ATOM 195 OE2 GLU A 25 -67.915 0.067 36.284 1.00 91.43 O ANISOU 195 OE2 GLU A 25 11197 11765 11777 -57 -46 167 O ATOM 196 N ALA A 26 -67.319 -2.264 42.244 1.00 50.60 N ANISOU 196 N ALA A 26 6104 6504 6619 -48 -12 22 N ATOM 197 CA ALA A 26 -67.714 -2.273 43.651 1.00 47.63 C ANISOU 197 CA ALA A 26 5726 6119 6252 -41 0 8 C ATOM 198 C ALA A 26 -66.757 -3.046 44.578 1.00 48.41 C ANISOU 198 C ALA A 26 5843 6215 6334 -44 3 -20 C ATOM 199 O ALA A 26 -66.061 -3.978 44.159 1.00 45.25 O ANISOU 199 O ALA A 26 5459 5820 5915 -53 -8 -27 O ATOM 200 CB ALA A 26 -69.147 -2.801 43.789 1.00 45.74 C ANISOU 200 CB ALA A 26 5475 5891 6013 -46 -5 23 C ATOM 201 N PRO A 27 -66.733 -2.668 45.863 1.00 49.78 N ANISOU 201 N PRO A 27 6013 6384 6516 -36 17 -36 N ATOM 202 CA PRO A 27 -65.789 -3.274 46.813 1.00 50.80 C ANISOU 202 CA PRO A 27 6156 6517 6629 -37 20 -59 C ATOM 203 C PRO A 27 -65.929 -4.792 46.934 1.00 52.62 C ANISOU 203 C PRO A 27 6394 6758 6840 -48 8 -54 C ATOM 204 O PRO A 27 -67.037 -5.312 47.031 1.00 59.87 O ANISOU 204 O PRO A 27 7304 7684 7760 -52 4 -40 O ATOM 205 CB PRO A 27 -66.155 -2.603 48.129 1.00 48.34 C ANISOU 205 CB PRO A 27 5832 6209 6328 -28 37 -74 C ATOM 206 CG PRO A 27 -66.775 -1.308 47.709 1.00 51.88 C ANISOU 206 CG PRO A 27 6264 6643 6806 -19 46 -66 C ATOM 207 CD PRO A 27 -67.518 -1.582 46.472 1.00 42.44 C ANISOU 207 CD PRO A 27 5065 5449 5612 -25 32 -36 C ATOM 208 N GLN A 28 -64.806 -5.490 46.943 1.00 52.07 N ANISOU 208 N GLN A 28 6340 6688 6757 -52 4 -66 N ATOM 209 CA GLN A 28 -64.805 -6.940 46.943 1.00 49.87 C ANISOU 209 CA GLN A 28 6068 6413 6469 -62 -8 -61 C ATOM 210 C GLN A 28 -64.738 -7.514 48.347 1.00 50.78 C ANISOU 210 C GLN A 28 6179 6538 6578 -60 -1 -62 C ATOM 211 O GLN A 28 -64.094 -8.546 48.563 1.00 52.30 O ANISOU 211 O GLN A 28 6378 6729 6764 -65 -6 -62 O ATOM 212 CB GLN A 28 -63.619 -7.444 46.130 1.00 46.03 C ANISOU 212 CB GLN A 28 5597 5919 5973 -66 -16 -71 C ATOM 213 CG GLN A 28 -63.594 -6.882 44.748 1.00 47.66 C ANISOU 213 CG GLN A 28 5805 6124 6181 -68 -22 -68 C ATOM 214 CD GLN A 28 -64.631 -7.533 43.838 1.00 57.51 C ANISOU 214 CD GLN A 28 7045 7377 7427 -78 -35 -56 C ATOM 215 OE1 GLN A 28 -65.340 -6.849 43.092 1.00 53.41 O ANISOU 215 OE1 GLN A 28 6516 6866 6912 -78 -38 -43 O ATOM 216 NE2 GLN A 28 -64.711 -8.866 43.883 1.00 48.30 N ANISOU 216 NE2 GLN A 28 5883 6209 6259 -88 -45 -61 N ATOM 217 N TYR A 29 -65.408 -6.871 49.300 1.00 51.30 N ANISOU 217 N TYR A 29 6231 6616 6646 -53 11 -62 N ATOM 218 CA TYR A 29 -65.267 -7.276 50.707 1.00 51.75 C ANISOU 218 CA TYR A 29 6279 6692 6691 -51 19 -63 C ATOM 219 C TYR A 29 -65.878 -8.640 51.036 1.00 53.49 C ANISOU 219 C TYR A 29 6493 6919 6910 -59 11 -40 C ATOM 220 O TYR A 29 -65.858 -9.070 52.184 1.00 57.05 O ANISOU 220 O TYR A 29 6934 7392 7352 -58 16 -32 O ATOM 221 CB TYR A 29 -65.753 -6.180 51.675 1.00 49.45 C ANISOU 221 CB TYR A 29 5972 6417 6400 -41 35 -75 C ATOM 222 CG TYR A 29 -65.073 -4.820 51.493 1.00 51.66 C ANISOU 222 CG TYR A 29 6255 6685 6688 -33 45 -101 C ATOM 223 CD1 TYR A 29 -63.677 -4.692 51.489 1.00 58.86 C ANISOU 223 CD1 TYR A 29 7179 7592 7592 -33 46 -118 C ATOM 224 CD2 TYR A 29 -65.825 -3.666 51.340 1.00 46.04 C ANISOU 224 CD2 TYR A 29 5531 5965 5996 -26 55 -106 C ATOM 225 CE1 TYR A 29 -63.064 -3.452 51.323 1.00 45.68 C ANISOU 225 CE1 TYR A 29 5510 5910 5936 -27 55 -140 C ATOM 226 CE2 TYR A 29 -65.224 -2.427 51.183 1.00 50.74 C ANISOU 226 CE2 TYR A 29 6126 6545 6608 -19 64 -127 C ATOM 227 CZ TYR A 29 -63.847 -2.321 51.181 1.00 51.89 C ANISOU 227 CZ TYR A 29 6283 6685 6746 -20 64 -145 C ATOM 228 OH TYR A 29 -63.272 -1.079 51.003 1.00 48.99 O ANISOU 228 OH TYR A 29 5914 6301 6400 -15 74 -165 O ATOM 229 N TYR A 30 -66.370 -9.346 50.021 1.00 56.28 N ANISOU 229 N TYR A 30 6851 7258 7275 -68 -3 -28 N ATOM 230 CA TYR A 30 -66.818 -10.738 50.188 1.00 57.49 C ANISOU 230 CA TYR A 30 6998 7409 7436 -78 -13 -8 C ATOM 231 C TYR A 30 -65.729 -11.779 49.910 1.00 59.28 C ANISOU 231 C TYR A 30 7237 7622 7666 -84 -21 -11 C ATOM 232 O TYR A 30 -65.878 -12.943 50.279 1.00 62.30 O ANISOU 232 O TYR A 30 7611 8000 8060 -91 -26 6 O ATOM 233 CB TYR A 30 -68.010 -11.031 49.291 1.00 56.39 C ANISOU 233 CB TYR A 30 6854 7262 7310 -87 -24 3 C ATOM 234 CG TYR A 30 -67.777 -10.617 47.868 1.00 55.03 C ANISOU 234 CG TYR A 30 6693 7077 7138 -90 -32 -11 C ATOM 235 CD1 TYR A 30 -66.990 -11.397 47.006 1.00 47.28 C ANISOU 235 CD1 TYR A 30 5724 6081 6159 -98 -43 -22 C ATOM 236 CD2 TYR A 30 -68.320 -9.431 47.385 1.00 41.73 C ANISOU 236 CD2 TYR A 30 5004 5397 5453 -84 -28 -11 C ATOM 237 CE1 TYR A 30 -66.776 -11.008 45.692 1.00 42.02 C ANISOU 237 CE1 TYR A 30 5066 5412 5488 -101 -50 -34 C ATOM 238 CE2 TYR A 30 -68.110 -9.031 46.080 1.00 39.96 C ANISOU 238 CE2 TYR A 30 4787 5167 5228 -87 -36 -17 C ATOM 239 CZ TYR A 30 -67.343 -9.812 45.239 1.00 48.28 C ANISOU 239 CZ TYR A 30 5853 6214 6278 -96 -47 -29 C ATOM 240 OH TYR A 30 -67.150 -9.380 43.945 1.00 57.21 O ANISOU 240 OH TYR A 30 6987 7348 7402 -98 -54 -34 O ATOM 241 N LEU A 31 -64.649 -11.375 49.248 1.00 59.44 N ANISOU 241 N LEU A 31 7273 7632 7681 -81 -21 -32 N ATOM 242 CA LEU A 31 -63.526 -12.291 49.046 1.00 59.07 C ANISOU 242 CA LEU A 31 7236 7572 7637 -84 -26 -37 C ATOM 243 C LEU A 31 -62.365 -12.043 50.006 1.00 56.95 C ANISOU 243 C LEU A 31 6969 7315 7355 -76 -16 -42 C ATOM 244 O LEU A 31 -61.391 -12.793 49.999 1.00 59.77 O ANISOU 244 O LEU A 31 7332 7663 7716 -77 -19 -43 O ATOM 245 CB LEU A 31 -63.060 -12.324 47.575 1.00 57.44 C ANISOU 245 CB LEU A 31 7044 7348 7433 -89 -36 -56 C ATOM 246 CG LEU A 31 -62.728 -11.013 46.880 1.00 56.15 C ANISOU 246 CG LEU A 31 6889 7189 7257 -83 -32 -70 C ATOM 247 CD1 LEU A 31 -61.498 -10.432 47.495 1.00 76.99 C ANISOU 247 CD1 LEU A 31 9535 9833 9886 -74 -22 -81 C ATOM 248 CD2 LEU A 31 -62.495 -11.228 45.417 1.00 64.71 C ANISOU 248 CD2 LEU A 31 7981 8266 8341 -89 -43 -83 C ATOM 249 N ALA A 32 -62.477 -10.999 50.827 1.00 57.71 N ANISOU 249 N ALA A 32 7058 7431 7436 -68 -5 -46 N ATOM 250 CA ALA A 32 -61.492 -10.692 51.884 1.00 56.47 C ANISOU 250 CA ALA A 32 6899 7295 7263 -62 5 -53 C ATOM 251 C ALA A 32 -62.008 -9.550 52.751 1.00 56.00 C ANISOU 251 C ALA A 32 6827 7259 7191 -55 18 -62 C ATOM 252 O ALA A 32 -62.607 -8.596 52.233 1.00 58.74 O ANISOU 252 O ALA A 32 7176 7599 7545 -52 21 -73 O ATOM 253 CB ALA A 32 -60.141 -10.316 51.276 1.00 56.32 C ANISOU 253 CB ALA A 32 6897 7263 7239 -59 5 -74 C ATOM 254 N GLU A 33 -61.762 -9.632 54.058 1.00 51.97 N ANISOU 254 N GLU A 33 6302 6782 6663 -52 26 -58 N ATOM 255 CA GLU A 33 -62.239 -8.624 55.011 1.00 49.25 C ANISOU 255 CA GLU A 33 5942 6467 6305 -45 40 -73 C ATOM 256 C GLU A 33 -61.627 -7.252 54.742 1.00 53.35 C ANISOU 256 C GLU A 33 6469 6976 6825 -40 48 -109 C ATOM 257 O GLU A 33 -60.480 -7.169 54.291 1.00 60.95 O ANISOU 257 O GLU A 33 7446 7926 7787 -41 45 -120 O ATOM 258 CB GLU A 33 -61.847 -9.029 56.416 1.00 47.06 C ANISOU 258 CB GLU A 33 5646 6232 6003 -44 46 -65 C ATOM 259 CG GLU A 33 -62.341 -10.364 56.854 1.00 55.91 C ANISOU 259 CG GLU A 33 6753 7365 7125 -49 40 -24 C ATOM 260 CD GLU A 33 -63.783 -10.338 57.259 1.00 75.33 C ANISOU 260 CD GLU A 33 9195 9842 9587 -49 44 -9 C ATOM 261 OE1 GLU A 33 -64.550 -9.492 56.740 1.00 75.58 O ANISOU 261 OE1 GLU A 33 9231 9858 9628 -47 47 -26 O ATOM 262 OE2 GLU A 33 -64.151 -11.185 58.098 1.00 93.79 O ANISOU 262 OE2 GLU A 33 11512 12207 11916 -52 44 24 O ATOM 263 N PRO A 34 -62.356 -6.157 55.054 1.00 52.26 N ANISOU 263 N PRO A 34 6320 6846 6691 -34 59 -127 N ATOM 264 CA PRO A 34 -61.679 -4.864 54.886 1.00 50.47 C ANISOU 264 CA PRO A 34 6097 6607 6472 -29 68 -162 C ATOM 265 C PRO A 34 -60.270 -4.774 55.506 1.00 49.46 C ANISOU 265 C PRO A 34 5971 6496 6326 -30 71 -181 C ATOM 266 O PRO A 34 -59.383 -4.207 54.883 1.00 49.76 O ANISOU 266 O PRO A 34 6021 6512 6374 -30 70 -197 O ATOM 267 CB PRO A 34 -62.644 -3.870 55.535 1.00 46.56 C ANISOU 267 CB PRO A 34 5582 6126 5984 -23 82 -180 C ATOM 268 CG PRO A 34 -63.951 -4.484 55.375 1.00 40.01 C ANISOU 268 CG PRO A 34 4746 5298 5159 -24 78 -151 C ATOM 269 CD PRO A 34 -63.767 -5.980 55.439 1.00 47.61 C ANISOU 269 CD PRO A 34 5713 6269 6106 -31 65 -119 C ATOM 270 N TRP A 35 -60.030 -5.334 56.689 1.00 51.75 N ANISOU 270 N TRP A 35 6246 6828 6589 -32 74 -178 N ATOM 271 CA TRP A 35 -58.701 -5.109 57.277 1.00 54.63 C ANISOU 271 CA TRP A 35 6609 7212 6934 -33 77 -199 C ATOM 272 C TRP A 35 -57.609 -5.686 56.400 1.00 56.18 C ANISOU 272 C TRP A 35 6827 7382 7137 -36 65 -187 C ATOM 273 O TRP A 35 -56.546 -5.092 56.244 1.00 59.57 O ANISOU 273 O TRP A 35 7263 7803 7566 -36 67 -209 O ATOM 274 CB TRP A 35 -58.580 -5.601 58.714 1.00 49.31 C ANISOU 274 CB TRP A 35 5913 6597 6226 -34 82 -194 C ATOM 275 CG TRP A 35 -58.668 -7.046 58.850 1.00 52.87 C ANISOU 275 CG TRP A 35 6361 7058 6668 -37 72 -148 C ATOM 276 CD1 TRP A 35 -59.794 -7.773 59.046 1.00 50.58 C ANISOU 276 CD1 TRP A 35 6060 6776 6380 -38 70 -116 C ATOM 277 CD2 TRP A 35 -57.578 -7.979 58.834 1.00 56.97 C ANISOU 277 CD2 TRP A 35 6886 7579 7181 -40 63 -126 C ATOM 278 NE1 TRP A 35 -59.482 -9.109 59.157 1.00 48.61 N ANISOU 278 NE1 TRP A 35 5809 6532 6130 -42 60 -75 N ATOM 279 CE2 TRP A 35 -58.128 -9.263 59.032 1.00 49.49 C ANISOU 279 CE2 TRP A 35 5930 6639 6236 -42 56 -81 C ATOM 280 CE3 TRP A 35 -56.192 -7.852 58.671 1.00 52.27 C ANISOU 280 CE3 TRP A 35 6301 6979 6580 -41 61 -140 C ATOM 281 CZ2 TRP A 35 -57.347 -10.420 59.056 1.00 50.70 C ANISOU 281 CZ2 TRP A 35 6084 6791 6391 -45 48 -48 C ATOM 282 CZ3 TRP A 35 -55.415 -9.000 58.714 1.00 56.43 C ANISOU 282 CZ3 TRP A 35 6828 7508 7104 -43 52 -108 C ATOM 283 CH2 TRP A 35 -55.997 -10.271 58.903 1.00 49.93 C ANISOU 283 CH2 TRP A 35 5996 6689 6288 -44 46 -63 C ATOM 284 N GLN A 36 -57.897 -6.831 55.795 1.00 57.56 N ANISOU 284 N GLN A 36 7011 7540 7319 -39 54 -153 N ATOM 285 CA GLN A 36 -56.990 -7.434 54.840 1.00 53.72 C ANISOU 285 CA GLN A 36 6544 7025 6841 -41 43 -143 C ATOM 286 C GLN A 36 -56.712 -6.533 53.625 1.00 53.13 C ANISOU 286 C GLN A 36 6485 6915 6785 -40 42 -162 C ATOM 287 O GLN A 36 -55.585 -6.494 53.131 1.00 55.19 O ANISOU 287 O GLN A 36 6758 7165 7047 -41 39 -169 O ATOM 288 CB GLN A 36 -57.532 -8.779 54.410 1.00 53.05 C ANISOU 288 CB GLN A 36 6462 6928 6768 -45 33 -110 C ATOM 289 CG GLN A 36 -57.808 -9.684 55.578 1.00 58.27 C ANISOU 289 CG GLN A 36 7103 7621 7415 -46 34 -84 C ATOM 290 CD GLN A 36 -58.446 -10.985 55.159 1.00 64.33 C ANISOU 290 CD GLN A 36 7870 8369 8201 -51 24 -50 C ATOM 291 OE1 GLN A 36 -59.527 -11.009 54.558 1.00 69.96 O ANISOU 291 OE1 GLN A 36 8585 9065 8930 -53 20 -46 O ATOM 292 NE2 GLN A 36 -57.780 -12.080 55.473 1.00 64.08 N ANISOU 292 NE2 GLN A 36 7834 8341 8173 -52 20 -27 N ATOM 293 N PHE A 37 -57.706 -5.791 53.148 1.00 49.01 N ANISOU 293 N PHE A 37 5962 6379 6280 -39 45 -167 N ATOM 294 CA PHE A 37 -57.405 -4.791 52.126 1.00 48.77 C ANISOU 294 CA PHE A 37 5942 6321 6268 -37 46 -180 C ATOM 295 C PHE A 37 -56.440 -3.731 52.648 1.00 48.77 C ANISOU 295 C PHE A 37 5937 6326 6267 -35 56 -210 C ATOM 296 O PHE A 37 -55.562 -3.258 51.898 1.00 50.72 O ANISOU 296 O PHE A 37 6194 6554 6524 -35 54 -218 O ATOM 297 CB PHE A 37 -58.669 -4.175 51.523 1.00 44.29 C ANISOU 297 CB PHE A 37 5370 5738 5721 -35 48 -174 C ATOM 298 CG PHE A 37 -59.337 -5.073 50.556 1.00 54.84 C ANISOU 298 CG PHE A 37 6713 7062 7060 -39 35 -149 C ATOM 299 CD1 PHE A 37 -59.063 -4.970 49.193 1.00 52.61 C ANISOU 299 CD1 PHE A 37 6442 6759 6787 -41 27 -143 C ATOM 300 CD2 PHE A 37 -60.189 -6.088 51.006 1.00 59.70 C ANISOU 300 CD2 PHE A 37 7323 7691 7670 -42 31 -131 C ATOM 301 CE1 PHE A 37 -59.664 -5.847 48.274 1.00 55.04 C ANISOU 301 CE1 PHE A 37 6755 7061 7096 -47 15 -125 C ATOM 302 CE2 PHE A 37 -60.793 -6.966 50.098 1.00 64.42 C ANISOU 302 CE2 PHE A 37 7926 8275 8274 -48 18 -111 C ATOM 303 CZ PHE A 37 -60.526 -6.847 48.726 1.00 55.83 C ANISOU 303 CZ PHE A 37 6850 7169 7193 -51 10 -111 C ATOM 304 N SER A 38 -56.596 -3.386 53.931 1.00 45.03 N ANISOU 304 N SER A 38 5446 5881 5781 -33 66 -229 N ATOM 305 CA SER A 38 -55.737 -2.413 54.603 1.00 41.80 C ANISOU 305 CA SER A 38 5029 5483 5370 -33 76 -264 C ATOM 306 C SER A 38 -54.315 -2.938 54.716 1.00 41.84 C ANISOU 306 C SER A 38 5041 5498 5356 -37 70 -264 C ATOM 307 O SER A 38 -53.359 -2.211 54.419 1.00 36.75 O ANISOU 307 O SER A 38 4401 4841 4722 -38 72 -283 O ATOM 308 CB SER A 38 -56.258 -2.117 56.000 1.00 40.98 C ANISOU 308 CB SER A 38 4902 5418 5250 -31 87 -285 C ATOM 309 OG SER A 38 -57.399 -1.307 55.945 1.00 34.85 O ANISOU 309 OG SER A 38 4116 4629 4497 -26 96 -296 O ATOM 310 N MET A 39 -54.186 -4.193 55.159 1.00 41.17 N ANISOU 310 N MET A 39 4957 5437 5249 -39 64 -240 N ATOM 311 CA MET A 39 -52.896 -4.865 55.173 1.00 45.13 C ANISOU 311 CA MET A 39 5465 5947 5737 -41 57 -232 C ATOM 312 C MET A 39 -52.262 -4.847 53.781 1.00 47.69 C ANISOU 312 C MET A 39 5810 6232 6080 -41 50 -227 C ATOM 313 O MET A 39 -51.065 -4.591 53.646 1.00 48.80 O ANISOU 313 O MET A 39 5955 6370 6217 -42 50 -238 O ATOM 314 CB MET A 39 -53.000 -6.291 55.706 1.00 42.52 C ANISOU 314 CB MET A 39 5129 5639 5389 -42 51 -199 C ATOM 315 CG MET A 39 -53.049 -6.398 57.232 1.00 52.71 C ANISOU 315 CG MET A 39 6395 6983 6650 -43 57 -200 C ATOM 316 SD MET A 39 -52.211 -5.066 58.129 1.00 64.28 S ANISOU 316 SD MET A 39 7845 8479 8098 -45 68 -249 S ATOM 317 CE MET A 39 -50.489 -5.345 57.720 1.00 54.78 C ANISOU 317 CE MET A 39 6654 7268 6892 -47 61 -247 C ATOM 318 N LEU A 40 -53.063 -5.093 52.746 1.00 47.28 N ANISOU 318 N LEU A 40 5768 6152 6043 -40 45 -210 N ATOM 319 CA LEU A 40 -52.561 -4.946 51.400 1.00 47.65 C ANISOU 319 CA LEU A 40 5831 6170 6105 -41 39 -207 C ATOM 320 C LEU A 40 -52.043 -3.511 51.209 1.00 50.72 C ANISOU 320 C LEU A 40 6217 6547 6507 -40 47 -231 C ATOM 321 O LEU A 40 -50.925 -3.313 50.726 1.00 56.24 O ANISOU 321 O LEU A 40 6922 7238 7207 -41 45 -235 O ATOM 322 CB LEU A 40 -53.613 -5.327 50.353 1.00 47.04 C ANISOU 322 CB LEU A 40 5759 6073 6039 -41 32 -189 C ATOM 323 CG LEU A 40 -53.226 -5.075 48.886 1.00 44.32 C ANISOU 323 CG LEU A 40 5427 5706 5706 -42 27 -185 C ATOM 324 CD1 LEU A 40 -52.112 -5.964 48.468 1.00 36.98 C ANISOU 324 CD1 LEU A 40 4508 4776 4767 -43 20 -182 C ATOM 325 CD2 LEU A 40 -54.401 -5.256 47.947 1.00 52.93 C ANISOU 325 CD2 LEU A 40 6518 6786 6805 -43 20 -170 C ATOM 326 N ALA A 41 -52.824 -2.514 51.614 1.00 49.28 N ANISOU 326 N ALA A 41 6023 6364 6339 -38 56 -245 N ATOM 327 CA ALA A 41 -52.363 -1.124 51.522 1.00 47.95 C ANISOU 327 CA ALA A 41 5847 6179 6192 -38 64 -269 C ATOM 328 C ALA A 41 -51.076 -0.923 52.316 1.00 48.87 C ANISOU 328 C ALA A 41 5959 6313 6295 -41 68 -293 C ATOM 329 O ALA A 41 -50.145 -0.257 51.849 1.00 51.46 O ANISOU 329 O ALA A 41 6290 6626 6638 -43 69 -302 O ATOM 330 CB ALA A 41 -53.434 -0.159 52.000 1.00 45.55 C ANISOU 330 CB ALA A 41 5527 5871 5909 -35 75 -285 C ATOM 331 N ALA A 42 -51.027 -1.502 53.516 1.00 45.92 N ANISOU 331 N ALA A 42 5577 5976 5895 -43 69 -300 N ATOM 332 CA ALA A 42 -49.848 -1.397 54.362 1.00 42.17 C ANISOU 332 CA ALA A 42 5094 5527 5401 -47 71 -321 C ATOM 333 C ALA A 42 -48.582 -1.897 53.631 1.00 44.91 C ANISOU 333 C ALA A 42 5455 5864 5743 -48 63 -306 C ATOM 334 O ALA A 42 -47.556 -1.218 53.601 1.00 46.70 O ANISOU 334 O ALA A 42 5680 6087 5977 -52 65 -324 O ATOM 335 CB ALA A 42 -50.069 -2.144 55.650 1.00 35.87 C ANISOU 335 CB ALA A 42 4282 4776 4570 -48 72 -319 C ATOM 336 N TYR A 43 -48.671 -3.067 53.007 1.00 45.80 N ANISOU 336 N TYR A 43 5582 5971 5849 -46 54 -274 N ATOM 337 CA TYR A 43 -47.520 -3.658 52.353 1.00 44.30 C ANISOU 337 CA TYR A 43 5404 5774 5655 -46 47 -262 C ATOM 338 C TYR A 43 -47.083 -2.847 51.125 1.00 47.08 C ANISOU 338 C TYR A 43 5765 6095 6029 -46 47 -265 C ATOM 339 O TYR A 43 -45.888 -2.700 50.872 1.00 49.99 O ANISOU 339 O TYR A 43 6136 6463 6396 -48 46 -269 O ATOM 340 CB TYR A 43 -47.782 -5.128 51.998 1.00 42.94 C ANISOU 340 CB TYR A 43 5240 5600 5474 -44 38 -232 C ATOM 341 CG TYR A 43 -46.514 -5.882 51.686 1.00 45.53 C ANISOU 341 CG TYR A 43 5575 5929 5795 -43 33 -222 C ATOM 342 CD1 TYR A 43 -45.673 -6.324 52.716 1.00 53.16 C ANISOU 342 CD1 TYR A 43 6530 6925 6743 -43 34 -220 C ATOM 343 CD2 TYR A 43 -46.118 -6.104 50.365 1.00 41.24 C ANISOU 343 CD2 TYR A 43 5045 5361 5262 -41 29 -216 C ATOM 344 CE1 TYR A 43 -44.473 -6.990 52.442 1.00 48.04 C ANISOU 344 CE1 TYR A 43 5886 6277 6091 -41 30 -210 C ATOM 345 CE2 TYR A 43 -44.925 -6.772 50.076 1.00 52.65 C ANISOU 345 CE2 TYR A 43 6495 6807 6702 -39 26 -210 C ATOM 346 CZ TYR A 43 -44.105 -7.209 51.121 1.00 58.67 C ANISOU 346 CZ TYR A 43 7248 7595 7451 -39 27 -206 C ATOM 347 OH TYR A 43 -42.924 -7.864 50.842 1.00 59.50 O ANISOU 347 OH TYR A 43 7355 7699 7554 -36 25 -198 O ATOM 348 N MET A 44 -48.034 -2.318 50.362 1.00 45.89 N ANISOU 348 N MET A 44 5616 5922 5898 -45 48 -260 N ATOM 349 CA MET A 44 -47.674 -1.437 49.259 1.00 48.14 C ANISOU 349 CA MET A 44 5904 6182 6205 -45 49 -257 C ATOM 350 C MET A 44 -46.964 -0.198 49.812 1.00 50.77 C ANISOU 350 C MET A 44 6224 6511 6555 -49 57 -284 C ATOM 351 O MET A 44 -46.046 0.349 49.193 1.00 50.33 O ANISOU 351 O MET A 44 6169 6443 6511 -51 58 -283 O ATOM 352 CB MET A 44 -48.910 -0.991 48.462 1.00 48.47 C ANISOU 352 CB MET A 44 5945 6205 6268 -43 49 -244 C ATOM 353 CG MET A 44 -49.573 -2.037 47.578 1.00 51.45 C ANISOU 353 CG MET A 44 6332 6581 6634 -41 39 -219 C ATOM 354 SD MET A 44 -48.471 -2.986 46.518 1.00 49.07 S ANISOU 354 SD MET A 44 6045 6283 6317 -42 30 -207 S ATOM 355 CE MET A 44 -48.310 -4.433 47.585 1.00 39.62 C ANISOU 355 CE MET A 44 4852 5103 5098 -42 27 -210 C ATOM 356 N PHE A 45 -47.422 0.262 50.971 1.00 51.61 N ANISOU 356 N PHE A 45 6317 6629 6662 -50 65 -308 N ATOM 357 CA PHE A 45 -46.863 1.454 51.570 1.00 50.69 C ANISOU 357 CA PHE A 45 6186 6510 6565 -54 74 -341 C ATOM 358 C PHE A 45 -45.391 1.207 51.987 1.00 49.89 C ANISOU 358 C PHE A 45 6085 6429 6443 -60 71 -352 C ATOM 359 O PHE A 45 -44.493 1.990 51.643 1.00 49.50 O ANISOU 359 O PHE A 45 6031 6363 6413 -64 73 -362 O ATOM 360 CB PHE A 45 -47.741 1.921 52.732 1.00 48.13 C ANISOU 360 CB PHE A 45 5845 6200 6242 -54 83 -371 C ATOM 361 CG PHE A 45 -47.217 3.139 53.426 1.00 53.37 C ANISOU 361 CG PHE A 45 6490 6861 6927 -60 93 -414 C ATOM 362 CD1 PHE A 45 -47.211 4.376 52.776 1.00 47.25 C ANISOU 362 CD1 PHE A 45 5708 6044 6202 -60 100 -421 C ATOM 363 CD2 PHE A 45 -46.700 3.050 54.720 1.00 46.70 C ANISOU 363 CD2 PHE A 45 5633 6057 6055 -65 96 -446 C ATOM 364 CE1 PHE A 45 -46.706 5.511 53.414 1.00 44.53 C ANISOU 364 CE1 PHE A 45 5343 5692 5884 -67 109 -465 C ATOM 365 CE2 PHE A 45 -46.194 4.184 55.363 1.00 47.85 C ANISOU 365 CE2 PHE A 45 5758 6201 6220 -72 105 -493 C ATOM 366 CZ PHE A 45 -46.193 5.409 54.711 1.00 42.82 C ANISOU 366 CZ PHE A 45 5115 5516 5639 -73 112 -504 C ATOM 367 N LEU A 46 -45.153 0.110 52.699 1.00 45.76 N ANISOU 367 N LEU A 46 5564 5940 5884 -59 66 -346 N ATOM 368 CA LEU A 46 -43.807 -0.351 52.991 1.00 47.60 C ANISOU 368 CA LEU A 46 5797 6193 6095 -63 62 -346 C ATOM 369 C LEU A 46 -42.927 -0.398 51.736 1.00 51.73 C ANISOU 369 C LEU A 46 6333 6692 6630 -62 57 -327 C ATOM 370 O LEU A 46 -41.828 0.159 51.720 1.00 55.93 O ANISOU 370 O LEU A 46 6860 7224 7168 -66 58 -339 O ATOM 371 CB LEU A 46 -43.862 -1.738 53.627 1.00 46.71 C ANISOU 371 CB LEU A 46 5685 6113 5948 -60 56 -326 C ATOM 372 CG LEU A 46 -42.539 -2.323 54.101 1.00 45.84 C ANISOU 372 CG LEU A 46 5571 6031 5814 -62 52 -322 C ATOM 373 CD1 LEU A 46 -41.926 -1.349 55.058 1.00 53.44 C ANISOU 373 CD1 LEU A 46 6516 7018 6773 -70 58 -359 C ATOM 374 CD2 LEU A 46 -42.728 -3.677 54.785 1.00 42.24 C ANISOU 374 CD2 LEU A 46 5112 5606 5332 -58 47 -297 C ATOM 375 N LEU A 47 -43.418 -1.067 50.690 1.00 54.02 N ANISOU 375 N LEU A 47 6638 6966 6922 -56 52 -299 N ATOM 376 CA LEU A 47 -42.691 -1.230 49.427 1.00 49.17 C ANISOU 376 CA LEU A 47 6035 6336 6313 -54 48 -280 C ATOM 377 C LEU A 47 -42.367 0.092 48.757 1.00 47.92 C ANISOU 377 C LEU A 47 5869 6153 6184 -57 52 -286 C ATOM 378 O LEU A 47 -41.333 0.215 48.144 1.00 53.87 O ANISOU 378 O LEU A 47 6625 6904 6940 -58 51 -279 O ATOM 379 CB LEU A 47 -43.471 -2.130 48.466 1.00 50.29 C ANISOU 379 CB LEU A 47 6189 6468 6450 -49 42 -256 C ATOM 380 CG LEU A 47 -43.025 -3.580 48.210 1.00 50.11 C ANISOU 380 CG LEU A 47 6176 6455 6407 -45 35 -241 C ATOM 381 CD1 LEU A 47 -42.379 -4.258 49.401 1.00 47.71 C ANISOU 381 CD1 LEU A 47 5866 6175 6085 -45 34 -244 C ATOM 382 CD2 LEU A 47 -44.200 -4.384 47.738 1.00 48.88 C ANISOU 382 CD2 LEU A 47 6028 6293 6252 -42 30 -227 C ATOM 383 N ILE A 48 -43.248 1.079 48.870 1.00 48.52 N ANISOU 383 N ILE A 48 5936 6212 6287 -58 58 -295 N ATOM 384 CA ILE A 48 -42.953 2.441 48.407 1.00 47.50 C ANISOU 384 CA ILE A 48 5795 6056 6195 -62 65 -300 C ATOM 385 C ILE A 48 -41.906 3.155 49.279 1.00 50.17 C ANISOU 385 C ILE A 48 6120 6400 6542 -70 69 -332 C ATOM 386 O ILE A 48 -40.929 3.720 48.763 1.00 49.68 O ANISOU 386 O ILE A 48 6054 6327 6497 -74 70 -328 O ATOM 387 CB ILE A 48 -44.234 3.312 48.342 1.00 48.31 C ANISOU 387 CB ILE A 48 5888 6136 6332 -60 71 -302 C ATOM 388 CG1 ILE A 48 -45.332 2.572 47.554 1.00 44.39 C ANISOU 388 CG1 ILE A 48 5403 5640 5824 -53 65 -273 C ATOM 389 CG2 ILE A 48 -43.906 4.715 47.774 1.00 37.03 C ANISOU 389 CG2 ILE A 48 4444 4675 4952 -63 78 -301 C ATOM 390 CD1 ILE A 48 -46.674 3.300 47.437 1.00 38.67 C ANISOU 390 CD1 ILE A 48 4667 4895 5129 -50 71 -268 C ATOM 391 N MET A 49 -42.117 3.141 50.595 1.00 50.54 N ANISOU 391 N MET A 49 6158 6467 6576 -73 73 -363 N ATOM 392 CA MET A 49 -41.209 3.828 51.518 1.00 50.50 C ANISOU 392 CA MET A 49 6137 6473 6576 -82 77 -400 C ATOM 393 C MET A 49 -39.786 3.306 51.419 1.00 50.78 C ANISOU 393 C MET A 49 6178 6528 6590 -86 71 -392 C ATOM 394 O MET A 49 -38.861 4.103 51.448 1.00 50.65 O ANISOU 394 O MET A 49 6149 6502 6592 -94 73 -408 O ATOM 395 CB MET A 49 -41.701 3.760 52.962 1.00 49.41 C ANISOU 395 CB MET A 49 5988 6368 6419 -85 81 -435 C ATOM 396 CG MET A 49 -43.024 4.445 53.182 1.00 53.85 C ANISOU 396 CG MET A 49 6540 6912 7007 -82 90 -451 C ATOM 397 SD MET A 49 -42.875 6.238 53.174 1.00 64.98 S ANISOU 397 SD MET A 49 7927 8280 8481 -89 102 -489 S ATOM 398 CE MET A 49 -43.257 6.692 51.488 1.00 50.26 C ANISOU 398 CE MET A 49 6071 6364 6662 -82 101 -441 C ATOM 399 N LEU A 50 -39.600 1.989 51.295 1.00 48.00 N ANISOU 399 N LEU A 50 5839 6197 6200 -80 63 -367 N ATOM 400 CA LEU A 50 -38.252 1.448 51.078 1.00 50.12 C ANISOU 400 CA LEU A 50 6113 6481 6451 -81 58 -355 C ATOM 401 C LEU A 50 -37.860 1.478 49.589 1.00 52.84 C ANISOU 401 C LEU A 50 6467 6799 6810 -77 56 -326 C ATOM 402 O LEU A 50 -36.788 1.967 49.221 1.00 52.93 O ANISOU 402 O LEU A 50 6473 6805 6832 -81 56 -325 O ATOM 403 CB LEU A 50 -38.102 0.039 51.645 1.00 46.48 C ANISOU 403 CB LEU A 50 5658 6053 5951 -76 52 -341 C ATOM 404 CG LEU A 50 -38.519 -0.175 53.102 1.00 52.25 C ANISOU 404 CG LEU A 50 6376 6820 6659 -79 53 -361 C ATOM 405 CD1 LEU A 50 -38.563 -1.663 53.463 1.00 42.79 C ANISOU 405 CD1 LEU A 50 5182 5649 5429 -72 47 -334 C ATOM 406 CD2 LEU A 50 -37.615 0.577 54.061 1.00 52.88 C ANISOU 406 CD2 LEU A 50 6435 6924 6733 -90 56 -395 C ATOM 407 N GLY A 51 -38.750 0.988 48.736 1.00 51.99 N ANISOU 407 N GLY A 51 6373 6680 6703 -69 54 -302 N ATOM 408 CA GLY A 51 -38.463 0.867 47.311 1.00 50.37 C ANISOU 408 CA GLY A 51 6175 6461 6503 -65 51 -274 C ATOM 409 C GLY A 51 -38.069 2.153 46.616 1.00 52.78 C ANISOU 409 C GLY A 51 6469 6744 6843 -70 56 -270 C ATOM 410 O GLY A 51 -37.227 2.137 45.720 1.00 52.98 O ANISOU 410 O GLY A 51 6495 6769 6867 -69 54 -251 O ATOM 411 N PHE A 52 -38.665 3.275 47.014 1.00 54.86 N ANISOU 411 N PHE A 52 6719 6987 7139 -74 62 -285 N ATOM 412 CA PHE A 52 -38.385 4.527 46.317 1.00 55.64 C ANISOU 412 CA PHE A 52 6804 7058 7281 -79 67 -275 C ATOM 413 C PHE A 52 -36.996 5.055 46.659 1.00 57.56 C ANISOU 413 C PHE A 52 7035 7302 7533 -87 69 -290 C ATOM 414 O PHE A 52 -36.177 5.263 45.771 1.00 54.66 O ANISOU 414 O PHE A 52 6665 6931 7173 -88 68 -267 O ATOM 415 CB PHE A 52 -39.441 5.589 46.595 1.00 53.58 C ANISOU 415 CB PHE A 52 6528 6768 7061 -80 74 -287 C ATOM 416 CG PHE A 52 -39.129 6.909 45.961 1.00 59.88 C ANISOU 416 CG PHE A 52 7307 7533 7912 -85 80 -275 C ATOM 417 CD1 PHE A 52 -39.376 7.118 44.603 1.00 58.33 C ANISOU 417 CD1 PHE A 52 7108 7326 7729 -80 79 -229 C ATOM 418 CD2 PHE A 52 -38.556 7.940 46.711 1.00 60.30 C ANISOU 418 CD2 PHE A 52 7340 7568 8002 -95 87 -307 C ATOM 419 CE1 PHE A 52 -39.072 8.341 44.001 1.00 60.44 C ANISOU 419 CE1 PHE A 52 7353 7563 8049 -84 85 -210 C ATOM 420 CE2 PHE A 52 -38.254 9.173 46.121 1.00 59.59 C ANISOU 420 CE2 PHE A 52 7230 7442 7970 -99 93 -293 C ATOM 421 CZ PHE A 52 -38.507 9.370 44.761 1.00 62.61 C ANISOU 421 CZ PHE A 52 7608 7812 8367 -94 92 -241 C ATOM 422 N PRO A 53 -36.718 5.271 47.955 1.00 59.44 N ANISOU 422 N PRO A 53 7264 7550 7769 -95 71 -330 N ATOM 423 CA PRO A 53 -35.374 5.717 48.293 1.00 57.67 C ANISOU 423 CA PRO A 53 7029 7331 7552 -104 71 -345 C ATOM 424 C PRO A 53 -34.278 4.797 47.730 1.00 56.98 C ANISOU 424 C PRO A 53 6952 7267 7431 -101 65 -320 C ATOM 425 O PRO A 53 -33.451 5.272 46.971 1.00 62.40 O ANISOU 425 O PRO A 53 7631 7942 8135 -104 65 -303 O ATOM 426 CB PRO A 53 -35.387 5.728 49.822 1.00 57.39 C ANISOU 426 CB PRO A 53 6985 7319 7503 -111 72 -391 C ATOM 427 CG PRO A 53 -36.797 5.954 50.164 1.00 55.51 C ANISOU 427 CG PRO A 53 6746 7068 7277 -108 77 -403 C ATOM 428 CD PRO A 53 -37.563 5.151 49.154 1.00 56.82 C ANISOU 428 CD PRO A 53 6930 7229 7427 -95 73 -362 C ATOM 429 N ILE A 54 -34.282 3.505 48.056 1.00 55.04 N ANISOU 429 N ILE A 54 6722 7051 7142 -94 59 -316 N ATOM 430 CA ILE A 54 -33.249 2.588 47.548 1.00 54.49 C ANISOU 430 CA ILE A 54 6660 7001 7044 -89 55 -295 C ATOM 431 C ILE A 54 -32.984 2.782 46.052 1.00 56.84 C ANISOU 431 C ILE A 54 6960 7283 7353 -85 55 -263 C ATOM 432 O ILE A 54 -31.837 2.896 45.621 1.00 57.36 O ANISOU 432 O ILE A 54 7021 7355 7420 -87 55 -252 O ATOM 433 CB ILE A 54 -33.633 1.118 47.744 1.00 52.89 C ANISOU 433 CB ILE A 54 6473 6819 6803 -79 50 -286 C ATOM 434 CG1 ILE A 54 -34.219 0.874 49.143 1.00 66.41 C ANISOU 434 CG1 ILE A 54 8181 8549 8501 -81 49 -310 C ATOM 435 CG2 ILE A 54 -32.445 0.233 47.495 1.00 53.52 C ANISOU 435 CG2 ILE A 54 6556 6919 6860 -74 46 -272 C ATOM 436 CD1 ILE A 54 -33.226 0.389 50.209 1.00 73.54 C ANISOU 436 CD1 ILE A 54 9075 9487 9378 -85 46 -321 C ATOM 437 N ASN A 55 -34.043 2.819 45.254 1.00 56.05 N ANISOU 437 N ASN A 55 6867 7170 7262 -79 56 -245 N ATOM 438 CA ASN A 55 -33.870 2.842 43.808 1.00 57.36 C ANISOU 438 CA ASN A 55 7032 7332 7429 -74 56 -212 C ATOM 439 C ASN A 55 -33.580 4.219 43.253 1.00 57.89 C ANISOU 439 C ASN A 55 7080 7377 7537 -81 61 -197 C ATOM 440 O ASN A 55 -32.861 4.349 42.271 1.00 63.39 O ANISOU 440 O ASN A 55 7771 8081 8234 -80 61 -171 O ATOM 441 CB ASN A 55 -35.072 2.210 43.089 1.00 57.47 C ANISOU 441 CB ASN A 55 7058 7348 7429 -66 53 -196 C ATOM 442 CG ASN A 55 -35.136 0.703 43.279 1.00 61.65 C ANISOU 442 CG ASN A 55 7605 7898 7922 -58 48 -202 C ATOM 443 OD1 ASN A 55 -35.967 0.192 44.035 1.00 58.66 O ANISOU 443 OD1 ASN A 55 7233 7519 7534 -56 46 -215 O ATOM 444 ND2 ASN A 55 -34.242 -0.017 42.603 1.00 61.60 N ANISOU 444 ND2 ASN A 55 7602 7909 7894 -53 47 -192 N ATOM 445 N PHE A 56 -34.158 5.246 43.861 1.00 60.50 N ANISOU 445 N PHE A 56 7399 7682 7907 -88 65 -214 N ATOM 446 CA PHE A 56 -33.903 6.617 43.439 1.00 63.10 C ANISOU 446 CA PHE A 56 7706 7983 8287 -96 71 -201 C ATOM 447 C PHE A 56 -32.488 7.018 43.849 1.00 64.20 C ANISOU 447 C PHE A 56 7833 8124 8435 -105 72 -214 C ATOM 448 O PHE A 56 -31.720 7.556 43.051 1.00 65.12 O ANISOU 448 O PHE A 56 7936 8235 8571 -109 73 -187 O ATOM 449 CB PHE A 56 -34.914 7.583 44.055 1.00 63.34 C ANISOU 449 CB PHE A 56 7724 7980 8361 -100 77 -220 C ATOM 450 CG PHE A 56 -34.658 9.012 43.697 1.00 69.51 C ANISOU 450 CG PHE A 56 8479 8726 9207 -107 83 -208 C ATOM 451 CD1 PHE A 56 -35.004 9.496 42.426 1.00 65.29 C ANISOU 451 CD1 PHE A 56 7933 8179 8696 -103 85 -158 C ATOM 452 CD2 PHE A 56 -34.037 9.869 44.609 1.00 66.49 C ANISOU 452 CD2 PHE A 56 8079 8324 8860 -120 88 -244 C ATOM 453 CE1 PHE A 56 -34.750 10.811 42.069 1.00 58.73 C ANISOU 453 CE1 PHE A 56 7074 7313 7930 -110 92 -139 C ATOM 454 CE2 PHE A 56 -33.781 11.192 44.271 1.00 64.55 C ANISOU 454 CE2 PHE A 56 7806 8038 8680 -128 95 -233 C ATOM 455 CZ PHE A 56 -34.132 11.665 42.991 1.00 67.48 C ANISOU 455 CZ PHE A 56 8165 8393 9080 -122 97 -177 C ATOM 456 N LEU A 57 -32.153 6.735 45.099 1.00 62.56 N ANISOU 456 N LEU A 57 7629 7929 8213 -111 70 -254 N ATOM 457 CA LEU A 57 -30.798 6.875 45.587 1.00 64.78 C ANISOU 457 CA LEU A 57 7899 8221 8491 -120 69 -269 C ATOM 458 C LEU A 57 -29.773 6.304 44.611 1.00 63.82 C ANISOU 458 C LEU A 57 7783 8120 8346 -115 66 -235 C ATOM 459 O LEU A 57 -28.773 6.948 44.324 1.00 66.56 O ANISOU 459 O LEU A 57 8114 8462 8715 -122 68 -226 O ATOM 460 CB LEU A 57 -30.669 6.185 46.943 1.00 66.78 C ANISOU 460 CB LEU A 57 8159 8503 8710 -122 65 -307 C ATOM 461 CG LEU A 57 -29.896 6.885 48.056 1.00 70.98 C ANISOU 461 CG LEU A 57 8672 9039 9257 -137 66 -347 C ATOM 462 CD1 LEU A 57 -29.692 8.367 47.736 1.00 74.50 C ANISOU 462 CD1 LEU A 57 9096 9445 9767 -149 73 -352 C ATOM 463 CD2 LEU A 57 -30.663 6.689 49.367 1.00 74.60 C ANISOU 463 CD2 LEU A 57 9132 9514 9700 -139 67 -388 C ATOM 464 N THR A 58 -30.019 5.102 44.098 1.00 62.84 N ANISOU 464 N THR A 58 7678 8019 8180 -102 63 -218 N ATOM 465 CA THR A 58 -29.088 4.482 43.159 1.00 60.73 C ANISOU 465 CA THR A 58 7414 7774 7888 -95 61 -191 C ATOM 466 C THR A 58 -28.833 5.392 41.960 1.00 64.76 C ANISOU 466 C THR A 58 7908 8272 8428 -98 65 -156 C ATOM 467 O THR A 58 -27.680 5.736 41.666 1.00 68.35 O ANISOU 467 O THR A 58 8349 8731 8888 -103 67 -144 O ATOM 468 CB THR A 58 -29.564 3.104 42.694 1.00 56.71 C ANISOU 468 CB THR A 58 6925 7285 7336 -81 58 -182 C ATOM 469 OG1 THR A 58 -29.514 2.200 43.793 1.00 52.05 O ANISOU 469 OG1 THR A 58 6346 6709 6721 -79 54 -207 O ATOM 470 CG2 THR A 58 -28.665 2.568 41.606 1.00 56.84 C ANISOU 470 CG2 THR A 58 6942 7323 7332 -74 58 -157 C ATOM 471 N LEU A 59 -29.909 5.800 41.292 1.00 65.89 N ANISOU 471 N LEU A 59 8049 8399 8587 -95 67 -136 N ATOM 472 CA LEU A 59 -29.812 6.719 40.157 1.00 65.55 C ANISOU 472 CA LEU A 59 7985 8346 8574 -97 71 -95 C ATOM 473 C LEU A 59 -29.050 7.983 40.534 1.00 66.09 C ANISOU 473 C LEU A 59 8030 8387 8695 -111 75 -98 C ATOM 474 O LEU A 59 -28.113 8.381 39.847 1.00 67.14 O ANISOU 474 O LEU A 59 8147 8526 8838 -114 77 -69 O ATOM 475 CB LEU A 59 -31.203 7.090 39.645 1.00 62.44 C ANISOU 475 CB LEU A 59 7589 7936 8198 -93 72 -76 C ATOM 476 CG LEU A 59 -31.991 5.967 38.978 1.00 59.03 C ANISOU 476 CG LEU A 59 7177 7533 7721 -81 67 -67 C ATOM 477 CD1 LEU A 59 -33.153 6.579 38.192 1.00 49.12 C ANISOU 477 CD1 LEU A 59 5910 6266 6487 -79 69 -35 C ATOM 478 CD2 LEU A 59 -31.080 5.117 38.078 1.00 46.39 C ANISOU 478 CD2 LEU A 59 5579 5970 6076 -75 66 -50 C ATOM 479 N TYR A 60 -29.444 8.585 41.650 1.00 66.60 N ANISOU 479 N TYR A 60 8090 8423 8791 -119 77 -134 N ATOM 480 CA TYR A 60 -28.932 9.882 42.059 1.00 66.71 C ANISOU 480 CA TYR A 60 8078 8404 8865 -134 81 -144 C ATOM 481 C TYR A 60 -27.447 9.842 42.394 1.00 66.33 C ANISOU 481 C TYR A 60 8023 8371 8809 -142 79 -155 C ATOM 482 O TYR A 60 -26.690 10.708 41.962 1.00 71.15 O ANISOU 482 O TYR A 60 8609 8965 9458 -151 83 -134 O ATOM 483 CB TYR A 60 -29.734 10.414 43.244 1.00 66.31 C ANISOU 483 CB TYR A 60 8024 8324 8844 -140 84 -191 C ATOM 484 CG TYR A 60 -29.331 11.795 43.672 1.00 71.94 C ANISOU 484 CG TYR A 60 8709 8998 9628 -155 90 -208 C ATOM 485 CD1 TYR A 60 -29.672 12.904 42.905 1.00 79.12 C ANISOU 485 CD1 TYR A 60 9594 9867 10601 -158 97 -173 C ATOM 486 CD2 TYR A 60 -28.609 11.996 44.846 1.00 77.62 C ANISOU 486 CD2 TYR A 60 9421 9720 10352 -169 89 -259 C ATOM 487 CE1 TYR A 60 -29.310 14.175 43.296 1.00 85.12 C ANISOU 487 CE1 TYR A 60 10324 10584 11434 -172 103 -191 C ATOM 488 CE2 TYR A 60 -28.245 13.266 45.250 1.00 77.70 C ANISOU 488 CE2 TYR A 60 9402 9691 10429 -184 95 -282 C ATOM 489 CZ TYR A 60 -28.597 14.350 44.469 1.00 87.11 C ANISOU 489 CZ TYR A 60 10570 10836 11690 -186 102 -248 C ATOM 490 OH TYR A 60 -28.227 15.617 44.852 1.00 94.85 O ANISOU 490 OH TYR A 60 11520 11773 12747 -202 108 -271 O ATOM 491 N VAL A 61 -27.034 8.835 43.155 1.00 63.12 N ANISOU 491 N VAL A 61 7634 7996 8354 -140 74 -184 N ATOM 492 CA VAL A 61 -25.633 8.678 43.532 1.00 61.34 C ANISOU 492 CA VAL A 61 7402 7790 8115 -147 72 -195 C ATOM 493 C VAL A 61 -24.753 8.453 42.296 1.00 64.48 C ANISOU 493 C VAL A 61 7795 8207 8499 -142 73 -149 C ATOM 494 O VAL A 61 -23.608 8.885 42.250 1.00 64.16 O ANISOU 494 O VAL A 61 7737 8168 8473 -151 73 -142 O ATOM 495 CB VAL A 61 -25.460 7.545 44.577 1.00 59.65 C ANISOU 495 CB VAL A 61 7206 7610 7849 -143 66 -228 C ATOM 496 CG1 VAL A 61 -24.017 7.137 44.728 1.00 51.83 C ANISOU 496 CG1 VAL A 61 6210 6647 6836 -146 63 -227 C ATOM 497 CG2 VAL A 61 -26.013 7.988 45.920 1.00 59.20 C ANISOU 497 CG2 VAL A 61 7145 7542 7808 -153 66 -277 C ATOM 498 N THR A 62 -25.301 7.805 41.278 1.00 67.74 N ANISOU 498 N THR A 62 8220 8633 8883 -127 73 -117 N ATOM 499 CA THR A 62 -24.566 7.614 40.035 1.00 68.22 C ANISOU 499 CA THR A 62 8274 8718 8929 -121 75 -74 C ATOM 500 C THR A 62 -24.335 8.945 39.323 1.00 70.04 C ANISOU 500 C THR A 62 8474 8924 9213 -131 80 -38 C ATOM 501 O THR A 62 -23.258 9.180 38.772 1.00 73.52 O ANISOU 501 O THR A 62 8899 9379 9657 -134 81 -12 O ATOM 502 CB THR A 62 -25.256 6.578 39.120 1.00 66.72 C ANISOU 502 CB THR A 62 8102 8555 8694 -105 74 -56 C ATOM 503 OG1 THR A 62 -25.074 5.277 39.686 1.00 70.12 O ANISOU 503 OG1 THR A 62 8555 9009 9079 -96 70 -83 O ATOM 504 CG2 THR A 62 -24.661 6.590 37.719 1.00 63.75 C ANISOU 504 CG2 THR A 62 7712 8204 8304 -99 77 -11 C ATOM 505 N VAL A 63 -25.321 9.832 39.348 1.00 70.78 N ANISOU 505 N VAL A 63 8558 8982 9353 -135 82 -33 N ATOM 506 CA VAL A 63 -25.130 11.133 38.717 1.00 73.23 C ANISOU 506 CA VAL A 63 8836 9264 9724 -144 88 5 C ATOM 507 C VAL A 63 -23.997 11.907 39.413 1.00 75.41 C ANISOU 507 C VAL A 63 9091 9519 10040 -161 89 -14 C ATOM 508 O VAL A 63 -23.266 12.659 38.774 1.00 78.49 O ANISOU 508 O VAL A 63 9454 9901 10465 -169 92 23 O ATOM 509 CB VAL A 63 -26.459 11.936 38.609 1.00 72.21 C ANISOU 509 CB VAL A 63 8697 9096 9642 -144 91 16 C ATOM 510 CG1 VAL A 63 -26.226 13.435 38.749 1.00 70.92 C ANISOU 510 CG1 VAL A 63 8499 8883 9564 -159 97 26 C ATOM 511 CG2 VAL A 63 -27.138 11.636 37.285 1.00 67.64 C ANISOU 511 CG2 VAL A 63 8118 8543 9039 -132 91 69 C ATOM 512 N GLN A 64 -23.811 11.653 40.704 1.00 76.55 N ANISOU 512 N GLN A 64 9248 9661 10176 -168 85 -71 N ATOM 513 CA GLN A 64 -22.830 12.378 41.515 1.00 75.89 C ANISOU 513 CA GLN A 64 9145 9561 10130 -186 85 -100 C ATOM 514 C GLN A 64 -21.434 11.746 41.663 1.00 73.69 C ANISOU 514 C GLN A 64 8868 9320 9812 -188 81 -104 C ATOM 515 O GLN A 64 -20.547 12.379 42.227 1.00 76.22 O ANISOU 515 O GLN A 64 9168 9629 10163 -205 80 -123 O ATOM 516 CB GLN A 64 -23.402 12.631 42.907 1.00 75.55 C ANISOU 516 CB GLN A 64 9105 9496 10104 -195 84 -164 C ATOM 517 CG GLN A 64 -24.256 13.873 43.020 1.00 80.23 C ANISOU 517 CG GLN A 64 9678 10035 10772 -203 91 -171 C ATOM 518 CD GLN A 64 -24.589 14.187 44.467 1.00 92.74 C ANISOU 518 CD GLN A 64 11260 11603 12373 -214 91 -242 C ATOM 519 OE1 GLN A 64 -24.021 13.595 45.392 1.00 91.21 O ANISOU 519 OE1 GLN A 64 11075 11442 12137 -219 85 -282 O ATOM 520 NE2 GLN A 64 -25.514 15.119 44.673 1.00 95.81 N ANISOU 520 NE2 GLN A 64 11635 11946 12824 -218 98 -257 N ATOM 521 N HIS A 65 -21.238 10.514 41.194 1.00 70.50 N ANISOU 521 N HIS A 65 8486 8959 9343 -172 78 -88 N ATOM 522 CA HIS A 65 -19.961 9.823 41.387 1.00 68.56 C ANISOU 522 CA HIS A 65 8241 8749 9058 -172 75 -93 C ATOM 523 C HIS A 65 -19.426 9.171 40.126 1.00 72.08 C ANISOU 523 C HIS A 65 8690 9230 9469 -158 77 -47 C ATOM 524 O HIS A 65 -19.808 8.054 39.785 1.00 71.99 O ANISOU 524 O HIS A 65 8700 9245 9407 -141 77 -44 O ATOM 525 CB HIS A 65 -20.060 8.782 42.492 1.00 65.82 C ANISOU 525 CB HIS A 65 7918 8426 8665 -167 69 -136 C ATOM 526 CG HIS A 65 -20.323 9.365 43.841 1.00 66.35 C ANISOU 526 CG HIS A 65 7978 8473 8758 -182 67 -187 C ATOM 527 ND1 HIS A 65 -19.315 9.657 44.734 1.00 67.89 N ANISOU 527 ND1 HIS A 65 8157 8677 8960 -198 63 -216 N ATOM 528 CD2 HIS A 65 -21.481 9.721 44.449 1.00 69.45 C ANISOU 528 CD2 HIS A 65 8376 8842 9171 -185 68 -216 C ATOM 529 CE1 HIS A 65 -19.841 10.165 45.835 1.00 77.42 C ANISOU 529 CE1 HIS A 65 9360 9869 10188 -210 62 -264 C ATOM 530 NE2 HIS A 65 -21.155 10.208 45.690 1.00 73.04 N ANISOU 530 NE2 HIS A 65 8818 9294 9642 -202 65 -265 N ATOM 531 N LYS A 66 -18.512 9.873 39.461 1.00 76.91 N ANISOU 531 N LYS A 66 9274 9840 10106 -166 81 -12 N ATOM 532 CA LYS A 66 -17.851 9.399 38.237 1.00 77.27 C ANISOU 532 CA LYS A 66 9315 9923 10120 -154 84 33 C ATOM 533 C LYS A 66 -17.481 7.906 38.254 1.00 74.68 C ANISOU 533 C LYS A 66 9012 9639 9725 -138 83 18 C ATOM 534 O LYS A 66 -17.780 7.191 37.311 1.00 74.95 O ANISOU 534 O LYS A 66 9056 9701 9723 -122 86 39 O ATOM 535 CB LYS A 66 -16.622 10.280 37.934 1.00 78.91 C ANISOU 535 CB LYS A 66 9491 10128 10364 -168 87 61 C ATOM 536 CG LYS A 66 -15.660 9.766 36.845 1.00 84.11 C ANISOU 536 CG LYS A 66 10140 10832 10985 -158 91 102 C ATOM 537 CD LYS A 66 -16.034 10.288 35.462 1.00 88.73 C ANISOU 537 CD LYS A 66 10706 11426 11583 -153 97 160 C ATOM 538 CE LYS A 66 -14.853 10.263 34.504 1.00 87.13 C ANISOU 538 CE LYS A 66 10480 11262 11363 -151 103 204 C ATOM 539 NZ LYS A 66 -15.167 11.099 33.312 1.00 89.00 N ANISOU 539 NZ LYS A 66 10688 11502 11626 -152 108 266 N ATOM 540 N LYS A 67 -16.850 7.439 39.328 1.00 75.53 N ANISOU 540 N LYS A 67 9127 9754 9819 -141 78 -17 N ATOM 541 CA LYS A 67 -16.348 6.062 39.393 1.00 76.37 C ANISOU 541 CA LYS A 67 9250 9897 9870 -125 78 -27 C ATOM 542 C LYS A 67 -17.423 4.988 39.188 1.00 76.65 C ANISOU 542 C LYS A 67 9314 9942 9870 -108 77 -37 C ATOM 543 O LYS A 67 -17.125 3.892 38.709 1.00 79.80 O ANISOU 543 O LYS A 67 9722 10369 10229 -92 80 -33 O ATOM 544 CB LYS A 67 -15.622 5.816 40.717 1.00 77.45 C ANISOU 544 CB LYS A 67 9387 10040 10002 -134 72 -61 C ATOM 545 CG LYS A 67 -14.343 6.622 40.895 1.00 84.04 C ANISOU 545 CG LYS A 67 10193 10875 10863 -150 71 -54 C ATOM 546 CD LYS A 67 -13.259 6.188 39.920 1.00 86.90 C ANISOU 546 CD LYS A 67 10546 11270 11203 -140 77 -19 C ATOM 547 CE LYS A 67 -11.880 6.425 40.500 1.00 89.10 C ANISOU 547 CE LYS A 67 10804 11561 11489 -152 74 -23 C ATOM 548 NZ LYS A 67 -10.864 5.573 39.820 1.00 95.59 N ANISOU 548 NZ LYS A 67 11623 12423 12276 -136 79 0 N ATOM 549 N LEU A 68 -18.665 5.303 39.550 1.00 74.04 N ANISOU 549 N LEU A 68 8993 9584 9555 -111 75 -52 N ATOM 550 CA LEU A 68 -19.786 4.383 39.371 1.00 68.16 C ANISOU 550 CA LEU A 68 8272 8844 8781 -97 74 -60 C ATOM 551 C LEU A 68 -20.211 4.239 37.917 1.00 67.18 C ANISOU 551 C LEU A 68 8147 8735 8643 -86 79 -27 C ATOM 552 O LEU A 68 -20.774 3.222 37.535 1.00 68.08 O ANISOU 552 O LEU A 68 8279 8865 8724 -72 79 -34 O ATOM 553 CB LEU A 68 -20.980 4.850 40.188 1.00 66.46 C ANISOU 553 CB LEU A 68 8065 8597 8590 -104 71 -84 C ATOM 554 CG LEU A 68 -20.777 4.894 41.704 1.00 66.34 C ANISOU 554 CG LEU A 68 8051 8575 8581 -114 66 -123 C ATOM 555 CD1 LEU A 68 -21.939 5.637 42.369 1.00 60.47 C ANISOU 555 CD1 LEU A 68 7308 7798 7867 -123 65 -145 C ATOM 556 CD2 LEU A 68 -20.590 3.493 42.310 1.00 51.70 C ANISOU 556 CD2 LEU A 68 6214 6746 6682 -103 63 -141 C ATOM 557 N ARG A 69 -19.925 5.252 37.107 1.00 65.37 N ANISOU 557 N ARG A 69 7895 8504 8440 -93 83 8 N ATOM 558 CA ARG A 69 -20.494 5.362 35.771 1.00 62.17 C ANISOU 558 CA ARG A 69 7483 8115 8025 -86 86 44 C ATOM 559 C ARG A 69 -19.808 4.523 34.706 1.00 64.62 C ANISOU 559 C ARG A 69 7790 8474 8291 -73 91 60 C ATOM 560 O ARG A 69 -19.662 4.962 33.567 1.00 65.85 O ANISOU 560 O ARG A 69 7924 8651 8443 -72 95 100 O ATOM 561 CB ARG A 69 -20.534 6.818 35.341 1.00 59.20 C ANISOU 561 CB ARG A 69 7078 7718 7699 -99 89 81 C ATOM 562 CG ARG A 69 -21.853 7.476 35.624 1.00 61.36 C ANISOU 562 CG ARG A 69 7354 7954 8007 -104 87 79 C ATOM 563 CD ARG A 69 -21.905 8.882 35.062 1.00 71.51 C ANISOU 563 CD ARG A 69 8607 9217 9347 -115 91 123 C ATOM 564 NE ARG A 69 -21.698 9.876 36.111 1.00 78.05 N ANISOU 564 NE ARG A 69 9423 9997 10234 -132 90 102 N ATOM 565 CZ ARG A 69 -20.569 10.546 36.300 1.00 70.54 C ANISOU 565 CZ ARG A 69 8450 9036 9315 -144 92 110 C ATOM 566 NH1 ARG A 69 -20.479 11.426 37.283 1.00 71.46 N ANISOU 566 NH1 ARG A 69 8556 9109 9486 -160 91 82 N ATOM 567 NH2 ARG A 69 -19.534 10.337 35.505 1.00 78.41 N ANISOU 567 NH2 ARG A 69 9434 10069 10288 -141 94 142 N ATOM 568 N THR A 70 -19.415 3.308 35.068 1.00 68.45 N ANISOU 568 N THR A 70 8293 8975 8741 -62 91 31 N ATOM 569 CA THR A 70 -18.775 2.390 34.128 1.00 72.08 C ANISOU 569 CA THR A 70 8749 9478 9159 -47 96 37 C ATOM 570 C THR A 70 -19.823 1.614 33.323 1.00 74.94 C ANISOU 570 C THR A 70 9124 9859 9490 -35 97 31 C ATOM 571 O THR A 70 -20.964 1.484 33.768 1.00 77.27 O ANISOU 571 O THR A 70 9437 10132 9792 -36 92 14 O ATOM 572 CB THR A 70 -17.852 1.402 34.865 1.00 73.08 C ANISOU 572 CB THR A 70 8886 9611 9269 -39 97 9 C ATOM 573 OG1 THR A 70 -18.640 0.480 35.630 1.00 74.53 O ANISOU 573 OG1 THR A 70 9095 9778 9443 -33 92 -25 O ATOM 574 CG2 THR A 70 -16.892 2.155 35.799 1.00 75.53 C ANISOU 574 CG2 THR A 70 9184 9904 9609 -53 94 10 C ATOM 575 N PRO A 71 -19.449 1.108 32.127 1.00 77.05 N ANISOU 575 N PRO A 71 9382 10173 9722 -24 103 42 N ATOM 576 CA PRO A 71 -20.356 0.299 31.291 1.00 75.09 C ANISOU 576 CA PRO A 71 9142 9949 9440 -14 104 30 C ATOM 577 C PRO A 71 -20.991 -0.923 31.984 1.00 71.25 C ANISOU 577 C PRO A 71 8684 9444 8944 -5 100 -15 C ATOM 578 O PRO A 71 -22.183 -1.200 31.785 1.00 69.68 O ANISOU 578 O PRO A 71 8497 9241 8738 -4 97 -25 O ATOM 579 CB PRO A 71 -19.461 -0.134 30.114 1.00 75.05 C ANISOU 579 CB PRO A 71 9118 9999 9398 -3 113 41 C ATOM 580 CG PRO A 71 -18.077 0.340 30.455 1.00 75.10 C ANISOU 580 CG PRO A 71 9109 10005 9421 -7 117 57 C ATOM 581 CD PRO A 71 -18.247 1.491 31.370 1.00 76.79 C ANISOU 581 CD PRO A 71 9322 10173 9682 -24 111 73 C ATOM 582 N LEU A 72 -20.203 -1.624 32.799 1.00 68.41 N ANISOU 582 N LEU A 72 8333 9073 8586 1 102 -38 N ATOM 583 CA LEU A 72 -20.659 -2.811 33.525 1.00 64.41 C ANISOU 583 CA LEU A 72 7850 8548 8076 9 99 -75 C ATOM 584 C LEU A 72 -21.698 -2.484 34.608 1.00 65.94 C ANISOU 584 C LEU A 72 8059 8700 8293 0 90 -83 C ATOM 585 O LEU A 72 -22.235 -3.381 35.283 1.00 65.84 O ANISOU 585 O LEU A 72 8064 8671 8280 5 87 -109 O ATOM 586 CB LEU A 72 -19.460 -3.527 34.138 1.00 62.56 C ANISOU 586 CB LEU A 72 7615 8314 7842 17 103 -88 C ATOM 587 CG LEU A 72 -19.616 -5.007 34.484 1.00 66.77 C ANISOU 587 CG LEU A 72 8163 8839 8368 32 104 -120 C ATOM 588 CD1 LEU A 72 -20.288 -5.795 33.357 1.00 72.04 C ANISOU 588 CD1 LEU A 72 8833 9526 9013 42 108 -138 C ATOM 589 CD2 LEU A 72 -18.267 -5.601 34.834 1.00 64.09 C ANISOU 589 CD2 LEU A 72 7815 8507 8029 41 110 -124 C ATOM 590 N ASN A 73 -21.993 -1.195 34.756 1.00 64.19 N ANISOU 590 N ASN A 73 7829 8465 8095 -14 87 -61 N ATOM 591 CA ASN A 73 -22.963 -0.741 35.732 1.00 59.94 C ANISOU 591 CA ASN A 73 7303 7891 7581 -23 80 -70 C ATOM 592 C ASN A 73 -24.251 -0.276 35.101 1.00 59.18 C ANISOU 592 C ASN A 73 7207 7791 7488 -27 78 -58 C ATOM 593 O ASN A 73 -25.263 -0.152 35.777 1.00 61.27 O ANISOU 593 O ASN A 73 7484 8030 7767 -31 73 -70 O ATOM 594 CB ASN A 73 -22.369 0.382 36.567 1.00 60.59 C ANISOU 594 CB ASN A 73 7374 7953 7696 -37 79 -62 C ATOM 595 CG ASN A 73 -21.576 -0.127 37.749 1.00 59.47 C ANISOU 595 CG ASN A 73 7237 7804 7554 -37 77 -83 C ATOM 596 OD1 ASN A 73 -21.489 -1.336 37.986 1.00 59.68 O ANISOU 596 OD1 ASN A 73 7276 7840 7561 -26 77 -101 O ATOM 597 ND2 ASN A 73 -20.999 0.798 38.511 1.00 59.56 N ANISOU 597 ND2 ASN A 73 7237 7803 7591 -51 75 -82 N ATOM 598 N TYR A 74 -24.211 -0.011 33.802 1.00 62.06 N ANISOU 598 N TYR A 74 7557 8186 7838 -24 82 -33 N ATOM 599 CA TYR A 74 -25.398 0.424 33.056 1.00 63.13 C ANISOU 599 CA TYR A 74 7688 8327 7972 -27 79 -15 C ATOM 600 C TYR A 74 -26.628 -0.449 33.357 1.00 61.34 C ANISOU 600 C TYR A 74 7483 8088 7734 -22 74 -44 C ATOM 601 O TYR A 74 -27.714 0.073 33.589 1.00 60.05 O ANISOU 601 O TYR A 74 7323 7904 7589 -28 70 -38 O ATOM 602 CB TYR A 74 -25.115 0.427 31.548 1.00 64.20 C ANISOU 602 CB TYR A 74 7803 8513 8078 -22 84 11 C ATOM 603 CG TYR A 74 -24.244 1.564 31.033 1.00 72.82 C ANISOU 603 CG TYR A 74 8866 9617 9184 -29 89 55 C ATOM 604 CD1 TYR A 74 -23.322 2.214 31.864 1.00 77.88 C ANISOU 604 CD1 TYR A 74 9502 10231 9858 -37 90 59 C ATOM 605 CD2 TYR A 74 -24.315 1.959 29.695 1.00 80.17 C ANISOU 605 CD2 TYR A 74 9773 10593 10096 -29 92 92 C ATOM 606 CE1 TYR A 74 -22.513 3.240 31.380 1.00 75.65 C ANISOU 606 CE1 TYR A 74 9191 9957 9594 -44 94 100 C ATOM 607 CE2 TYR A 74 -23.511 2.977 29.200 1.00 84.02 C ANISOU 607 CE2 TYR A 74 10231 11094 10599 -35 97 138 C ATOM 608 CZ TYR A 74 -22.613 3.612 30.044 1.00 84.58 C ANISOU 608 CZ TYR A 74 10298 11131 10708 -43 98 141 C ATOM 609 OH TYR A 74 -21.821 4.621 29.542 1.00 83.44 O ANISOU 609 OH TYR A 74 10122 10997 10584 -50 102 188 O ATOM 610 N ILE A 75 -26.440 -1.772 33.367 1.00 60.91 N ANISOU 610 N ILE A 75 7441 8045 7655 -12 75 -74 N ATOM 611 CA ILE A 75 -27.529 -2.720 33.599 1.00 57.84 C ANISOU 611 CA ILE A 75 7072 7647 7259 -8 70 -101 C ATOM 612 C ILE A 75 -28.140 -2.577 34.992 1.00 57.59 C ANISOU 612 C ILE A 75 7055 7572 7253 -13 65 -113 C ATOM 613 O ILE A 75 -29.341 -2.768 35.158 1.00 59.61 O ANISOU 613 O ILE A 75 7321 7816 7512 -14 60 -121 O ATOM 614 CB ILE A 75 -27.093 -4.202 33.352 1.00 59.31 C ANISOU 614 CB ILE A 75 7266 7848 7422 5 74 -132 C ATOM 615 CG1 ILE A 75 -28.284 -5.076 32.918 1.00 58.43 C ANISOU 615 CG1 ILE A 75 7164 7741 7296 8 70 -154 C ATOM 616 CG2 ILE A 75 -26.434 -4.801 34.592 1.00 56.96 C ANISOU 616 CG2 ILE A 75 6979 7524 7139 9 74 -150 C ATOM 617 CD1 ILE A 75 -28.905 -4.675 31.599 1.00 48.88 C ANISOU 617 CD1 ILE A 75 5941 6568 6064 5 69 -139 C ATOM 618 N LEU A 76 -27.325 -2.248 35.991 1.00 55.78 N ANISOU 618 N LEU A 76 6825 7326 7041 -17 66 -115 N ATOM 619 CA LEU A 76 -27.847 -2.025 37.339 1.00 55.11 C ANISOU 619 CA LEU A 76 6750 7210 6978 -23 61 -128 C ATOM 620 C LEU A 76 -28.614 -0.703 37.421 1.00 56.35 C ANISOU 620 C LEU A 76 6900 7349 7162 -34 60 -112 C ATOM 621 O LEU A 76 -29.551 -0.560 38.205 1.00 56.56 O ANISOU 621 O LEU A 76 6934 7353 7201 -38 57 -123 O ATOM 622 CB LEU A 76 -26.733 -2.060 38.375 1.00 52.31 C ANISOU 622 CB LEU A 76 6394 6850 6631 -25 62 -136 C ATOM 623 CG LEU A 76 -25.988 -3.383 38.557 1.00 55.64 C ANISOU 623 CG LEU A 76 6821 7284 7036 -13 64 -150 C ATOM 624 CD1 LEU A 76 -24.757 -3.136 39.403 1.00 54.26 C ANISOU 624 CD1 LEU A 76 6638 7111 6868 -17 65 -149 C ATOM 625 CD2 LEU A 76 -26.846 -4.489 39.154 1.00 46.80 C ANISOU 625 CD2 LEU A 76 5717 6153 5913 -7 61 -169 C ATOM 626 N LEU A 77 -28.217 0.265 36.605 1.00 57.28 N ANISOU 626 N LEU A 77 7000 7476 7289 -39 63 -84 N ATOM 627 CA LEU A 77 -28.986 1.487 36.479 1.00 58.24 C ANISOU 627 CA LEU A 77 7111 7579 7441 -47 63 -63 C ATOM 628 C LEU A 77 -30.345 1.126 35.912 1.00 57.99 C ANISOU 628 C LEU A 77 7086 7552 7396 -43 60 -61 C ATOM 629 O LEU A 77 -31.377 1.664 36.325 1.00 58.37 O ANISOU 629 O LEU A 77 7135 7576 7467 -48 58 -60 O ATOM 630 CB LEU A 77 -28.269 2.473 35.560 1.00 59.93 C ANISOU 630 CB LEU A 77 7299 7805 7667 -52 67 -26 C ATOM 631 CG LEU A 77 -27.617 3.698 36.197 1.00 62.81 C ANISOU 631 CG LEU A 77 7648 8142 8075 -63 70 -18 C ATOM 632 CD1 LEU A 77 -27.066 3.387 37.572 1.00 69.50 C ANISOU 632 CD1 LEU A 77 8507 8974 8927 -67 68 -55 C ATOM 633 CD2 LEU A 77 -26.530 4.237 35.284 1.00 73.43 C ANISOU 633 CD2 LEU A 77 8970 9508 9423 -65 74 16 C ATOM 634 N ASN A 78 -30.329 0.193 34.965 1.00 56.63 N ANISOU 634 N ASN A 78 6916 7412 7187 -35 59 -62 N ATOM 635 CA ASN A 78 -31.532 -0.262 34.291 1.00 55.42 C ANISOU 635 CA ASN A 78 6768 7272 7017 -32 56 -61 C ATOM 636 C ASN A 78 -32.421 -0.965 35.300 1.00 54.79 C ANISOU 636 C ASN A 78 6709 7167 6942 -31 51 -91 C ATOM 637 O ASN A 78 -33.624 -0.725 35.348 1.00 56.04 O ANISOU 637 O ASN A 78 6869 7314 7109 -33 47 -87 O ATOM 638 CB ASN A 78 -31.142 -1.224 33.173 1.00 57.25 C ANISOU 638 CB ASN A 78 6996 7546 7208 -24 57 -67 C ATOM 639 CG ASN A 78 -32.270 -1.508 32.223 1.00 57.62 C ANISOU 639 CG ASN A 78 7041 7618 7234 -23 53 -63 C ATOM 640 OD1 ASN A 78 -32.913 -0.592 31.723 1.00 57.57 O ANISOU 640 OD1 ASN A 78 7020 7618 7237 -28 52 -31 O ATOM 641 ND2 ASN A 78 -32.501 -2.789 31.940 1.00 54.86 N ANISOU 641 ND2 ASN A 78 6702 7284 6858 -17 51 -94 N ATOM 642 N LEU A 79 -31.806 -1.800 36.135 1.00 50.91 N ANISOU 642 N LEU A 79 6230 6667 6445 -27 51 -117 N ATOM 643 CA LEU A 79 -32.509 -2.479 37.207 1.00 48.86 C ANISOU 643 CA LEU A 79 5987 6386 6191 -26 48 -141 C ATOM 644 C LEU A 79 -33.281 -1.485 38.042 1.00 51.74 C ANISOU 644 C LEU A 79 6351 6725 6584 -34 46 -137 C ATOM 645 O LEU A 79 -34.457 -1.696 38.335 1.00 55.63 O ANISOU 645 O LEU A 79 6852 7206 7079 -34 43 -143 O ATOM 646 CB LEU A 79 -31.534 -3.225 38.105 1.00 47.65 C ANISOU 646 CB LEU A 79 5841 6229 6035 -22 49 -159 C ATOM 647 CG LEU A 79 -32.171 -3.931 39.297 1.00 46.36 C ANISOU 647 CG LEU A 79 5691 6048 5877 -21 45 -177 C ATOM 648 CD1 LEU A 79 -33.196 -4.936 38.792 1.00 44.35 C ANISOU 648 CD1 LEU A 79 5445 5795 5611 -16 42 -186 C ATOM 649 CD2 LEU A 79 -31.115 -4.609 40.179 1.00 41.04 C ANISOU 649 CD2 LEU A 79 5018 5376 5201 -17 47 -187 C ATOM 650 N ALA A 80 -32.621 -0.395 38.417 1.00 51.13 N ANISOU 650 N ALA A 80 6262 6636 6529 -40 50 -128 N ATOM 651 CA ALA A 80 -33.236 0.591 39.293 1.00 52.25 C ANISOU 651 CA ALA A 80 6399 6750 6702 -48 50 -131 C ATOM 652 C ALA A 80 -34.420 1.285 38.621 1.00 54.33 C ANISOU 652 C ALA A 80 6656 7006 6981 -50 50 -111 C ATOM 653 O ALA A 80 -35.402 1.624 39.293 1.00 57.06 O ANISOU 653 O ALA A 80 7005 7332 7346 -52 49 -120 O ATOM 654 CB ALA A 80 -32.197 1.619 39.792 1.00 48.11 C ANISOU 654 CB ALA A 80 5861 6215 6203 -56 54 -130 C ATOM 655 N VAL A 81 -34.327 1.504 37.306 1.00 52.56 N ANISOU 655 N VAL A 81 6420 6802 6749 -48 50 -82 N ATOM 656 CA VAL A 81 -35.400 2.176 36.583 1.00 51.39 C ANISOU 656 CA VAL A 81 6261 6652 6614 -50 50 -55 C ATOM 657 C VAL A 81 -36.594 1.226 36.484 1.00 50.22 C ANISOU 657 C VAL A 81 6128 6512 6443 -45 44 -68 C ATOM 658 O VAL A 81 -37.743 1.635 36.654 1.00 49.67 O ANISOU 658 O VAL A 81 6056 6427 6391 -47 43 -62 O ATOM 659 CB VAL A 81 -34.950 2.673 35.182 1.00 54.42 C ANISOU 659 CB VAL A 81 6624 7064 6991 -49 51 -16 C ATOM 660 CG1 VAL A 81 -36.128 3.253 34.402 1.00 52.92 C ANISOU 660 CG1 VAL A 81 6419 6878 6811 -50 50 17 C ATOM 661 CG2 VAL A 81 -33.873 3.729 35.313 1.00 54.60 C ANISOU 661 CG2 VAL A 81 6628 7072 7045 -55 57 1 C ATOM 662 N ALA A 82 -36.315 -0.054 36.260 1.00 47.83 N ANISOU 662 N ALA A 82 5838 6231 6106 -40 41 -87 N ATOM 663 CA ALA A 82 -37.367 -1.058 36.240 1.00 48.62 C ANISOU 663 CA ALA A 82 5951 6335 6188 -37 35 -103 C ATOM 664 C ALA A 82 -38.095 -1.046 37.575 1.00 52.12 C ANISOU 664 C ALA A 82 6405 6747 6650 -39 35 -121 C ATOM 665 O ALA A 82 -39.324 -1.030 37.628 1.00 55.28 O ANISOU 665 O ALA A 82 6807 7141 7056 -40 31 -119 O ATOM 666 CB ALA A 82 -36.790 -2.429 35.962 1.00 44.58 C ANISOU 666 CB ALA A 82 5450 5843 5646 -31 34 -126 C ATOM 667 N ASP A 83 -37.320 -1.036 38.656 1.00 52.87 N ANISOU 667 N ASP A 83 6505 6828 6754 -39 37 -137 N ATOM 668 CA ASP A 83 -37.880 -1.049 39.984 1.00 51.44 C ANISOU 668 CA ASP A 83 6331 6626 6586 -41 37 -156 C ATOM 669 C ASP A 83 -38.788 0.155 40.182 1.00 53.02 C ANISOU 669 C ASP A 83 6521 6807 6817 -46 40 -146 C ATOM 670 O ASP A 83 -39.763 0.082 40.919 1.00 58.06 O ANISOU 670 O ASP A 83 7164 7434 7462 -46 39 -157 O ATOM 671 CB ASP A 83 -36.775 -1.051 41.037 1.00 52.11 C ANISOU 671 CB ASP A 83 6417 6709 6675 -43 40 -172 C ATOM 672 CG ASP A 83 -36.046 -2.394 41.151 1.00 54.53 C ANISOU 672 CG ASP A 83 6732 7029 6956 -37 38 -183 C ATOM 673 OD1 ASP A 83 -36.554 -3.425 40.669 1.00 60.23 O ANISOU 673 OD1 ASP A 83 7463 7758 7663 -32 35 -185 O ATOM 674 OD2 ASP A 83 -34.949 -2.419 41.750 1.00 65.46 O ANISOU 674 OD2 ASP A 83 8114 8418 8339 -37 40 -189 O ATOM 675 N LEU A 84 -38.480 1.267 39.527 1.00 53.01 N ANISOU 675 N LEU A 84 6503 6801 6836 -49 43 -124 N ATOM 676 CA LEU A 84 -39.274 2.470 39.732 1.00 54.38 C ANISOU 676 CA LEU A 84 6663 6950 7048 -53 47 -114 C ATOM 677 C LEU A 84 -40.576 2.395 38.949 1.00 56.24 C ANISOU 677 C LEU A 84 6897 7192 7281 -50 44 -93 C ATOM 678 O LEU A 84 -41.629 2.792 39.443 1.00 58.29 O ANISOU 678 O LEU A 84 7153 7432 7560 -50 45 -96 O ATOM 679 CB LEU A 84 -38.474 3.744 39.426 1.00 54.90 C ANISOU 679 CB LEU A 84 6709 7003 7148 -58 53 -95 C ATOM 680 CG LEU A 84 -37.419 4.149 40.480 1.00 57.74 C ANISOU 680 CG LEU A 84 7066 7348 7524 -63 57 -121 C ATOM 681 CD1 LEU A 84 -36.530 5.266 39.971 1.00 53.20 C ANISOU 681 CD1 LEU A 84 6470 6763 6982 -69 62 -99 C ATOM 682 CD2 LEU A 84 -38.025 4.542 41.831 1.00 49.24 C ANISOU 682 CD2 LEU A 84 5990 6249 6470 -67 60 -153 C ATOM 683 N PHE A 85 -40.519 1.835 37.747 1.00 58.94 N ANISOU 683 N PHE A 85 7238 7563 7594 -47 39 -75 N ATOM 684 CA PHE A 85 -41.744 1.511 37.017 1.00 59.47 C ANISOU 684 CA PHE A 85 7304 7644 7649 -46 34 -60 C ATOM 685 C PHE A 85 -42.698 0.701 37.901 1.00 59.67 C ANISOU 685 C PHE A 85 7346 7659 7667 -45 30 -87 C ATOM 686 O PHE A 85 -43.896 0.966 37.930 1.00 59.91 O ANISOU 686 O PHE A 85 7372 7681 7709 -45 29 -78 O ATOM 687 CB PHE A 85 -41.427 0.749 35.730 1.00 59.32 C ANISOU 687 CB PHE A 85 7283 7665 7589 -44 29 -50 C ATOM 688 CG PHE A 85 -41.128 1.638 34.563 1.00 66.21 C ANISOU 688 CG PHE A 85 8133 8558 8467 -45 31 -9 C ATOM 689 CD1 PHE A 85 -40.040 2.492 34.583 1.00 72.45 C ANISOU 689 CD1 PHE A 85 8910 9339 9278 -47 37 6 C ATOM 690 CD2 PHE A 85 -41.935 1.624 33.447 1.00 76.16 C ANISOU 690 CD2 PHE A 85 9379 9849 9710 -46 26 17 C ATOM 691 CE1 PHE A 85 -39.767 3.315 33.516 1.00 70.79 C ANISOU 691 CE1 PHE A 85 8675 9149 9074 -48 39 49 C ATOM 692 CE2 PHE A 85 -41.666 2.450 32.378 1.00 78.51 C ANISOU 692 CE2 PHE A 85 9650 10171 10009 -47 27 61 C ATOM 693 CZ PHE A 85 -40.582 3.294 32.416 1.00 77.32 C ANISOU 693 CZ PHE A 85 9487 10009 9881 -48 34 79 C ATOM 694 N MET A 86 -42.163 -0.272 38.635 1.00 57.11 N ANISOU 694 N MET A 86 7039 7336 7326 -43 29 -115 N ATOM 695 CA MET A 86 -42.992 -1.072 39.511 1.00 55.85 C ANISOU 695 CA MET A 86 6892 7169 7162 -42 26 -136 C ATOM 696 C MET A 86 -43.566 -0.241 40.645 1.00 58.00 C ANISOU 696 C MET A 86 7159 7415 7461 -44 31 -143 C ATOM 697 O MET A 86 -44.716 -0.434 41.040 1.00 58.96 O ANISOU 697 O MET A 86 7283 7531 7586 -44 29 -147 O ATOM 698 CB MET A 86 -42.217 -2.257 40.059 1.00 54.58 C ANISOU 698 CB MET A 86 6744 7013 6980 -40 24 -158 C ATOM 699 CG MET A 86 -42.205 -3.439 39.122 1.00 55.46 C ANISOU 699 CG MET A 86 6863 7145 7067 -38 19 -161 C ATOM 700 SD MET A 86 -41.216 -4.787 39.775 1.00 65.58 S ANISOU 700 SD MET A 86 8155 8426 8335 -33 19 -184 S ATOM 701 CE MET A 86 -42.473 -5.703 40.650 1.00 71.94 C ANISOU 701 CE MET A 86 8970 9220 9146 -34 14 -194 C ATOM 702 N VAL A 87 -42.766 0.696 41.146 1.00 57.88 N ANISOU 702 N VAL A 87 7136 7387 7468 -46 38 -148 N ATOM 703 CA VAL A 87 -43.143 1.517 42.289 1.00 57.43 C ANISOU 703 CA VAL A 87 7072 7309 7439 -49 44 -164 C ATOM 704 C VAL A 87 -44.281 2.472 41.929 1.00 59.05 C ANISOU 704 C VAL A 87 7264 7497 7676 -48 47 -146 C ATOM 705 O VAL A 87 -45.280 2.557 42.644 1.00 63.74 O ANISOU 705 O VAL A 87 7858 8082 8280 -47 49 -158 O ATOM 706 CB VAL A 87 -41.920 2.292 42.851 1.00 59.03 C ANISOU 706 CB VAL A 87 7266 7502 7659 -53 50 -177 C ATOM 707 CG1 VAL A 87 -42.360 3.481 43.693 1.00 60.49 C ANISOU 707 CG1 VAL A 87 7437 7662 7884 -56 58 -193 C ATOM 708 CG2 VAL A 87 -41.024 1.365 43.670 1.00 53.73 C ANISOU 708 CG2 VAL A 87 6607 6849 6961 -53 48 -200 C ATOM 709 N PHE A 88 -44.144 3.165 40.805 1.00 58.24 N ANISOU 709 N PHE A 88 7148 7393 7588 -48 48 -115 N ATOM 710 CA PHE A 88 -45.145 4.137 40.389 1.00 57.78 C ANISOU 710 CA PHE A 88 7071 7318 7563 -47 51 -91 C ATOM 711 C PHE A 88 -46.283 3.527 39.567 1.00 59.11 C ANISOU 711 C PHE A 88 7243 7506 7711 -44 43 -69 C ATOM 712 O PHE A 88 -47.435 3.914 39.714 1.00 63.67 O ANISOU 712 O PHE A 88 7812 8072 8309 -42 45 -62 O ATOM 713 CB PHE A 88 -44.478 5.308 39.669 1.00 54.78 C ANISOU 713 CB PHE A 88 6670 6926 7218 -49 56 -62 C ATOM 714 CG PHE A 88 -43.636 6.149 40.581 1.00 67.20 C ANISOU 714 CG PHE A 88 8235 8471 8825 -53 65 -86 C ATOM 715 CD1 PHE A 88 -44.235 7.007 41.507 1.00 70.93 C ANISOU 715 CD1 PHE A 88 8697 8911 9341 -54 73 -106 C ATOM 716 CD2 PHE A 88 -42.246 6.044 40.566 1.00 70.70 C ANISOU 716 CD2 PHE A 88 8682 8923 9258 -57 64 -93 C ATOM 717 CE1 PHE A 88 -43.464 7.770 42.377 1.00 61.87 C ANISOU 717 CE1 PHE A 88 7540 7741 8226 -59 81 -136 C ATOM 718 CE2 PHE A 88 -41.463 6.806 41.432 1.00 67.18 C ANISOU 718 CE2 PHE A 88 8228 8455 8844 -63 71 -118 C ATOM 719 CZ PHE A 88 -42.077 7.674 42.335 1.00 65.89 C ANISOU 719 CZ PHE A 88 8052 8260 8724 -65 79 -141 C ATOM 720 N GLY A 89 -45.969 2.565 38.716 1.00 57.77 N ANISOU 720 N GLY A 89 7082 7367 7501 -44 35 -62 N ATOM 721 CA GLY A 89 -47.000 1.860 37.983 1.00 57.21 C ANISOU 721 CA GLY A 89 7013 7318 7406 -44 27 -50 C ATOM 722 C GLY A 89 -47.789 0.922 38.880 1.00 58.71 C ANISOU 722 C GLY A 89 7219 7504 7583 -43 24 -77 C ATOM 723 O GLY A 89 -49.015 0.986 38.922 1.00 60.28 O ANISOU 723 O GLY A 89 7414 7699 7791 -43 22 -70 O ATOM 724 N GLY A 90 -47.096 0.044 39.598 1.00 58.33 N ANISOU 724 N GLY A 90 7188 7457 7518 -43 23 -106 N ATOM 725 CA GLY A 90 -47.775 -0.946 40.436 1.00 58.53 C ANISOU 725 CA GLY A 90 7227 7482 7532 -43 20 -126 C ATOM 726 C GLY A 90 -48.131 -0.459 41.838 1.00 58.32 C ANISOU 726 C GLY A 90 7198 7435 7526 -42 27 -143 C ATOM 727 O GLY A 90 -49.313 -0.247 42.155 1.00 57.93 O ANISOU 727 O GLY A 90 7143 7378 7488 -42 28 -140 O ATOM 728 N PHE A 91 -47.104 -0.264 42.664 1.00 54.57 N ANISOU 728 N PHE A 91 6726 6955 7054 -43 32 -161 N ATOM 729 CA PHE A 91 -47.278 -0.035 44.096 1.00 54.45 C ANISOU 729 CA PHE A 91 6708 6932 7048 -43 38 -184 C ATOM 730 C PHE A 91 -48.219 1.124 44.449 1.00 54.67 C ANISOU 730 C PHE A 91 6721 6941 7109 -42 46 -185 C ATOM 731 O PHE A 91 -49.086 0.973 45.320 1.00 53.24 O ANISOU 731 O PHE A 91 6539 6761 6928 -41 48 -197 O ATOM 732 CB PHE A 91 -45.926 0.141 44.816 1.00 54.48 C ANISOU 732 CB PHE A 91 6713 6938 7050 -45 42 -204 C ATOM 733 CG PHE A 91 -44.909 -0.937 44.516 1.00 61.33 C ANISOU 733 CG PHE A 91 7593 7822 7890 -45 37 -202 C ATOM 734 CD1 PHE A 91 -45.222 -2.023 43.694 1.00 69.23 C ANISOU 734 CD1 PHE A 91 8603 8832 8871 -43 29 -191 C ATOM 735 CD2 PHE A 91 -43.638 -0.874 45.076 1.00 59.55 C ANISOU 735 CD2 PHE A 91 7365 7601 7658 -47 39 -216 C ATOM 736 CE1 PHE A 91 -44.275 -3.008 43.424 1.00 65.17 C ANISOU 736 CE1 PHE A 91 8097 8329 8336 -41 25 -193 C ATOM 737 CE2 PHE A 91 -42.688 -1.857 44.818 1.00 61.18 C ANISOU 737 CE2 PHE A 91 7581 7821 7843 -45 35 -214 C ATOM 738 CZ PHE A 91 -43.008 -2.928 43.991 1.00 63.28 C ANISOU 738 CZ PHE A 91 7857 8094 8094 -41 29 -203 C ATOM 739 N THR A 92 -48.051 2.283 43.813 1.00 54.05 N ANISOU 739 N THR A 92 6630 6846 7061 -42 51 -171 N ATOM 740 CA THR A 92 -48.857 3.438 44.224 1.00 56.11 C ANISOU 740 CA THR A 92 6873 7083 7362 -40 60 -174 C ATOM 741 C THR A 92 -50.312 3.230 43.839 1.00 55.95 C ANISOU 741 C THR A 92 6850 7065 7343 -37 57 -155 C ATOM 742 O THR A 92 -51.215 3.450 44.655 1.00 54.13 O ANISOU 742 O THR A 92 6614 6827 7125 -34 63 -169 O ATOM 743 CB THR A 92 -48.357 4.779 43.660 1.00 54.60 C ANISOU 743 CB THR A 92 6664 6868 7215 -41 67 -160 C ATOM 744 OG1 THR A 92 -48.306 4.699 42.236 1.00 61.78 O ANISOU 744 OG1 THR A 92 7570 7786 8116 -41 60 -120 O ATOM 745 CG2 THR A 92 -46.990 5.107 44.204 1.00 49.72 C ANISOU 745 CG2 THR A 92 6045 6245 6601 -46 71 -184 C ATOM 746 N THR A 93 -50.525 2.779 42.603 1.00 56.15 N ANISOU 746 N THR A 93 6878 7103 7352 -37 48 -124 N ATOM 747 CA THR A 93 -51.860 2.408 42.125 1.00 55.46 C ANISOU 747 CA THR A 93 6789 7024 7258 -35 42 -105 C ATOM 748 C THR A 93 -52.562 1.397 43.051 1.00 53.58 C ANISOU 748 C THR A 93 6563 6795 6998 -35 40 -126 C ATOM 749 O THR A 93 -53.724 1.592 43.428 1.00 51.50 O ANISOU 749 O THR A 93 6292 6527 6748 -33 42 -124 O ATOM 750 CB THR A 93 -51.803 1.847 40.697 1.00 55.36 C ANISOU 750 CB THR A 93 6778 7035 7221 -37 31 -77 C ATOM 751 OG1 THR A 93 -50.847 2.590 39.946 1.00 52.44 O ANISOU 751 OG1 THR A 93 6398 6664 6862 -38 34 -59 O ATOM 752 CG2 THR A 93 -53.157 1.958 40.023 1.00 56.25 C ANISOU 752 CG2 THR A 93 6879 7155 7338 -36 27 -50 C ATOM 753 N THR A 94 -51.857 0.334 43.426 1.00 48.70 N ANISOU 753 N THR A 94 5962 6192 6351 -38 35 -143 N ATOM 754 CA THR A 94 -52.451 -0.666 44.303 1.00 51.13 C ANISOU 754 CA THR A 94 6278 6509 6641 -38 32 -156 C ATOM 755 C THR A 94 -52.820 -0.131 45.677 1.00 51.03 C ANISOU 755 C THR A 94 6257 6491 6642 -36 42 -177 C ATOM 756 O THR A 94 -53.810 -0.567 46.264 1.00 51.60 O ANISOU 756 O THR A 94 6327 6569 6708 -35 42 -179 O ATOM 757 CB THR A 94 -51.551 -1.880 44.493 1.00 50.60 C ANISOU 757 CB THR A 94 6225 6455 6545 -41 26 -167 C ATOM 758 OG1 THR A 94 -51.142 -2.362 43.210 1.00 60.71 O ANISOU 758 OG1 THR A 94 7511 7743 7812 -43 18 -154 O ATOM 759 CG2 THR A 94 -52.304 -2.980 45.252 1.00 44.00 C ANISOU 759 CG2 THR A 94 5394 5628 5695 -42 22 -171 C ATOM 760 N LEU A 95 -52.009 0.789 46.193 1.00 53.15 N ANISOU 760 N LEU A 95 6519 6749 6927 -36 51 -195 N ATOM 761 CA LEU A 95 -52.260 1.405 47.496 1.00 52.07 C ANISOU 761 CA LEU A 95 6370 6610 6803 -34 62 -223 C ATOM 762 C LEU A 95 -53.594 2.137 47.435 1.00 51.29 C ANISOU 762 C LEU A 95 6257 6497 6733 -30 68 -216 C ATOM 763 O LEU A 95 -54.453 2.000 48.323 1.00 49.08 O ANISOU 763 O LEU A 95 5972 6226 6450 -28 73 -229 O ATOM 764 CB LEU A 95 -51.129 2.382 47.854 1.00 52.80 C ANISOU 764 CB LEU A 95 6455 6691 6914 -37 70 -246 C ATOM 765 CG LEU A 95 -51.264 3.322 49.061 1.00 44.46 C ANISOU 765 CG LEU A 95 5382 5631 5880 -36 84 -282 C ATOM 766 CD1 LEU A 95 -51.545 2.565 50.336 1.00 41.77 C ANISOU 766 CD1 LEU A 95 5042 5322 5507 -37 84 -303 C ATOM 767 CD2 LEU A 95 -49.986 4.106 49.221 1.00 44.99 C ANISOU 767 CD2 LEU A 95 5443 5687 5964 -41 88 -303 C ATOM 768 N TYR A 96 -53.761 2.885 46.352 1.00 47.10 N ANISOU 768 N TYR A 96 5719 5947 6230 -28 68 -192 N ATOM 769 CA TYR A 96 -54.951 3.664 46.133 1.00 48.66 C ANISOU 769 CA TYR A 96 5900 6128 6460 -23 74 -179 C ATOM 770 C TYR A 96 -56.190 2.768 45.975 1.00 51.27 C ANISOU 770 C TYR A 96 6235 6475 6770 -22 67 -161 C ATOM 771 O TYR A 96 -57.186 2.932 46.700 1.00 54.87 O ANISOU 771 O TYR A 96 6681 6930 7235 -18 73 -171 O ATOM 772 CB TYR A 96 -54.744 4.555 44.917 1.00 47.24 C ANISOU 772 CB TYR A 96 5709 5928 6312 -22 74 -148 C ATOM 773 CG TYR A 96 -55.851 5.546 44.690 1.00 56.34 C ANISOU 773 CG TYR A 96 6838 7059 7509 -15 82 -130 C ATOM 774 CD1 TYR A 96 -55.968 6.678 45.486 1.00 59.13 C ANISOU 774 CD1 TYR A 96 7173 7384 7909 -11 98 -155 C ATOM 775 CD2 TYR A 96 -56.780 5.355 43.671 1.00 62.44 C ANISOU 775 CD2 TYR A 96 7606 7840 8280 -13 74 -90 C ATOM 776 CE1 TYR A 96 -56.975 7.587 45.274 1.00 61.71 C ANISOU 776 CE1 TYR A 96 7477 7687 8283 -3 107 -138 C ATOM 777 CE2 TYR A 96 -57.788 6.265 43.448 1.00 59.27 C ANISOU 777 CE2 TYR A 96 7182 7419 7921 -6 82 -69 C ATOM 778 CZ TYR A 96 -57.881 7.375 44.253 1.00 62.46 C ANISOU 778 CZ TYR A 96 7568 7790 8375 -1 98 -92 C ATOM 779 OH TYR A 96 -58.892 8.276 44.048 1.00 67.58 O ANISOU 779 OH TYR A 96 8191 8416 9072 8 107 -71 O ATOM 780 N THR A 97 -56.119 1.801 45.062 1.00 47.75 N ANISOU 780 N THR A 97 5802 6044 6295 -26 53 -139 N ATOM 781 CA THR A 97 -57.238 0.897 44.861 1.00 43.43 C ANISOU 781 CA THR A 97 5259 5513 5730 -27 44 -125 C ATOM 782 C THR A 97 -57.534 0.028 46.099 1.00 44.10 C ANISOU 782 C THR A 97 5351 5612 5795 -28 45 -146 C ATOM 783 O THR A 97 -58.688 -0.103 46.496 1.00 44.66 O ANISOU 783 O THR A 97 5414 5686 5869 -27 47 -142 O ATOM 784 CB THR A 97 -57.065 -0.004 43.614 1.00 43.01 C ANISOU 784 CB THR A 97 5216 5475 5651 -33 30 -104 C ATOM 785 OG1 THR A 97 -56.025 -0.952 43.842 1.00 37.39 O ANISOU 785 OG1 THR A 97 4521 4773 4913 -37 25 -121 O ATOM 786 CG2 THR A 97 -56.755 0.806 42.370 1.00 45.51 C ANISOU 786 CG2 THR A 97 5522 5788 5982 -33 28 -79 C ATOM 787 N SER A 98 -56.517 -0.574 46.709 1.00 42.71 N ANISOU 787 N SER A 98 5186 5445 5598 -31 44 -164 N ATOM 788 CA SER A 98 -56.779 -1.469 47.837 1.00 46.78 C ANISOU 788 CA SER A 98 5704 5979 6093 -32 45 -175 C ATOM 789 C SER A 98 -57.685 -0.818 48.892 1.00 48.70 C ANISOU 789 C SER A 98 5931 6224 6349 -28 56 -189 C ATOM 790 O SER A 98 -58.477 -1.490 49.557 1.00 48.10 O ANISOU 790 O SER A 98 5852 6165 6260 -28 56 -186 O ATOM 791 CB SER A 98 -55.480 -1.970 48.476 1.00 45.62 C ANISOU 791 CB SER A 98 5565 5842 5925 -35 44 -192 C ATOM 792 OG SER A 98 -54.689 -0.890 48.942 1.00 55.23 O ANISOU 792 OG SER A 98 6775 7054 7156 -33 55 -214 O ATOM 793 N LEU A 99 -57.559 0.497 49.024 1.00 52.27 N ANISOU 793 N LEU A 99 6371 6660 6829 -23 68 -204 N ATOM 794 CA LEU A 99 -58.287 1.254 50.025 1.00 53.21 C ANISOU 794 CA LEU A 99 6472 6781 6965 -18 82 -226 C ATOM 795 C LEU A 99 -59.727 1.545 49.584 1.00 55.77 C ANISOU 795 C LEU A 99 6785 7095 7310 -13 83 -205 C ATOM 796 O LEU A 99 -60.585 1.855 50.419 1.00 54.21 O ANISOU 796 O LEU A 99 6573 6904 7120 -8 93 -218 O ATOM 797 CB LEU A 99 -57.547 2.563 50.312 1.00 55.56 C ANISOU 797 CB LEU A 99 6758 7060 7293 -16 94 -254 C ATOM 798 CG LEU A 99 -56.239 2.494 51.105 1.00 53.16 C ANISOU 798 CG LEU A 99 6458 6770 6970 -21 96 -285 C ATOM 799 CD1 LEU A 99 -55.541 3.847 51.068 1.00 47.22 C ANISOU 799 CD1 LEU A 99 5693 5991 6256 -20 107 -309 C ATOM 800 CD2 LEU A 99 -56.461 2.017 52.547 1.00 35.54 C ANISOU 800 CD2 LEU A 99 4218 4575 4708 -21 102 -309 C ATOM 801 N HIS A 100 -59.968 1.486 48.272 1.00 55.19 N ANISOU 801 N HIS A 100 6716 7009 7245 -14 73 -173 N ATOM 802 CA HIS A 100 -61.322 1.451 47.716 1.00 52.41 C ANISOU 802 CA HIS A 100 6356 6656 6904 -12 70 -146 C ATOM 803 C HIS A 100 -61.942 0.043 47.717 1.00 52.89 C ANISOU 803 C HIS A 100 6425 6738 6931 -18 57 -131 C ATOM 804 O HIS A 100 -63.161 -0.098 47.579 1.00 58.37 O ANISOU 804 O HIS A 100 7111 7437 7631 -17 56 -114 O ATOM 805 CB HIS A 100 -61.336 1.983 46.293 1.00 48.27 C ANISOU 805 CB HIS A 100 5827 6116 6399 -12 64 -115 C ATOM 806 CG HIS A 100 -61.091 3.453 46.185 1.00 54.74 C ANISOU 806 CG HIS A 100 6629 6907 7264 -5 77 -118 C ATOM 807 ND1 HIS A 100 -59.829 3.989 46.034 1.00 67.97 N ANISOU 807 ND1 HIS A 100 8308 8569 8950 -6 80 -129 N ATOM 808 CD2 HIS A 100 -61.949 4.499 46.144 1.00 58.59 C ANISOU 808 CD2 HIS A 100 7094 7374 7794 4 88 -109 C ATOM 809 CE1 HIS A 100 -59.919 5.304 45.927 1.00 66.19 C ANISOU 809 CE1 HIS A 100 8061 8314 8773 0 92 -127 C ATOM 810 NE2 HIS A 100 -61.195 5.640 45.997 1.00 64.94 N ANISOU 810 NE2 HIS A 100 7886 8150 8637 7 97 -115 N ATOM 811 N GLY A 101 -61.115 -0.991 47.847 1.00 50.81 N ANISOU 811 N GLY A 101 6179 6488 6639 -24 49 -137 N ATOM 812 CA GLY A 101 -61.602 -2.376 47.849 1.00 50.28 C ANISOU 812 CA GLY A 101 6119 6436 6548 -31 38 -124 C ATOM 813 C GLY A 101 -61.934 -2.960 46.484 1.00 51.63 C ANISOU 813 C GLY A 101 6296 6606 6715 -37 23 -101 C ATOM 814 O GLY A 101 -62.566 -4.004 46.378 1.00 54.51 O ANISOU 814 O GLY A 101 6663 6980 7069 -44 13 -90 O ATOM 815 N TYR A 102 -61.509 -2.287 45.424 1.00 54.37 N ANISOU 815 N TYR A 102 6644 6944 7072 -37 21 -92 N ATOM 816 CA TYR A 102 -61.673 -2.804 44.064 1.00 51.45 C ANISOU 816 CA TYR A 102 6276 6580 6691 -44 7 -74 C ATOM 817 C TYR A 102 -60.892 -1.929 43.099 1.00 51.47 C ANISOU 817 C TYR A 102 6277 6578 6702 -41 7 -66 C ATOM 818 O TYR A 102 -60.394 -0.868 43.480 1.00 51.64 O ANISOU 818 O TYR A 102 6293 6584 6743 -35 19 -72 O ATOM 819 CB TYR A 102 -63.149 -2.874 43.673 1.00 48.74 C ANISOU 819 CB TYR A 102 5920 6244 6354 -45 1 -53 C ATOM 820 CG TYR A 102 -63.828 -1.535 43.475 1.00 49.98 C ANISOU 820 CG TYR A 102 6058 6392 6539 -37 10 -36 C ATOM 821 CD1 TYR A 102 -64.053 -1.030 42.197 1.00 50.74 C ANISOU 821 CD1 TYR A 102 6143 6493 6641 -38 4 -9 C ATOM 822 CD2 TYR A 102 -64.261 -0.779 44.564 1.00 51.90 C ANISOU 822 CD2 TYR A 102 6291 6624 6805 -28 25 -46 C ATOM 823 CE1 TYR A 102 -64.681 0.192 42.003 1.00 45.67 C ANISOU 823 CE1 TYR A 102 5480 5841 6031 -30 12 12 C ATOM 824 CE2 TYR A 102 -64.894 0.449 44.380 1.00 45.85 C ANISOU 824 CE2 TYR A 102 5505 5845 6073 -20 34 -31 C ATOM 825 CZ TYR A 102 -65.098 0.927 43.098 1.00 48.16 C ANISOU 825 CZ TYR A 102 5786 6138 6375 -20 28 0 C ATOM 826 OH TYR A 102 -65.726 2.139 42.910 1.00 49.98 O ANISOU 826 OH TYR A 102 5994 6353 6645 -11 38 20 O ATOM 827 N PHE A 103 -60.784 -2.364 41.852 1.00 51.88 N ANISOU 827 N PHE A 103 6331 6643 6738 -48 -5 -53 N ATOM 828 CA PHE A 103 -59.921 -1.666 40.909 1.00 53.57 C ANISOU 828 CA PHE A 103 6541 6859 6953 -47 -4 -42 C ATOM 829 C PHE A 103 -60.654 -0.506 40.275 1.00 53.15 C ANISOU 829 C PHE A 103 6466 6804 6924 -42 -1 -11 C ATOM 830 O PHE A 103 -61.223 -0.639 39.188 1.00 57.43 O ANISOU 830 O PHE A 103 6999 7368 7456 -47 -11 13 O ATOM 831 CB PHE A 103 -59.349 -2.612 39.840 1.00 53.47 C ANISOU 831 CB PHE A 103 6538 6869 6911 -55 -17 -44 C ATOM 832 CG PHE A 103 -58.228 -2.003 39.051 1.00 55.39 C ANISOU 832 CG PHE A 103 6779 7116 7150 -53 -16 -37 C ATOM 833 CD1 PHE A 103 -56.907 -2.217 39.425 1.00 52.52 C ANISOU 833 CD1 PHE A 103 6429 6745 6780 -52 -11 -58 C ATOM 834 CD2 PHE A 103 -58.494 -1.169 37.962 1.00 51.73 C ANISOU 834 CD2 PHE A 103 6297 6667 6692 -53 -17 -5 C ATOM 835 CE1 PHE A 103 -55.866 -1.630 38.715 1.00 55.98 C ANISOU 835 CE1 PHE A 103 6865 7190 7217 -51 -9 -49 C ATOM 836 CE2 PHE A 103 -57.460 -0.573 37.253 1.00 54.54 C ANISOU 836 CE2 PHE A 103 6647 7029 7046 -51 -15 7 C ATOM 837 CZ PHE A 103 -56.143 -0.806 37.626 1.00 53.87 C ANISOU 837 CZ PHE A 103 6578 6936 6955 -50 -11 -17 C ATOM 838 N VAL A 104 -60.621 0.637 40.949 1.00 53.90 N ANISOU 838 N VAL A 104 6551 6875 7053 -33 13 -12 N ATOM 839 CA VAL A 104 -61.437 1.788 40.540 1.00 55.07 C ANISOU 839 CA VAL A 104 6675 7014 7235 -27 19 19 C ATOM 840 C VAL A 104 -61.118 2.430 39.189 1.00 57.17 C ANISOU 840 C VAL A 104 6925 7291 7507 -28 14 56 C ATOM 841 O VAL A 104 -61.893 3.243 38.728 1.00 62.78 O ANISOU 841 O VAL A 104 7613 7998 8244 -23 17 89 O ATOM 842 CB VAL A 104 -61.443 2.904 41.587 1.00 51.26 C ANISOU 842 CB VAL A 104 6182 6499 6796 -17 37 5 C ATOM 843 CG1 VAL A 104 -62.112 2.435 42.837 1.00 48.20 C ANISOU 843 CG1 VAL A 104 5800 6109 6404 -15 42 -22 C ATOM 844 CG2 VAL A 104 -60.027 3.385 41.856 1.00 50.80 C ANISOU 844 CG2 VAL A 104 6130 6425 6746 -17 44 -14 C ATOM 845 N PHE A 105 -60.004 2.093 38.552 1.00 58.55 N ANISOU 845 N PHE A 105 7110 7480 7657 -33 8 53 N ATOM 846 CA PHE A 105 -59.664 2.766 37.300 1.00 62.05 C ANISOU 846 CA PHE A 105 7534 7937 8103 -33 6 91 C ATOM 847 C PHE A 105 -60.255 2.079 36.072 1.00 64.31 C ANISOU 847 C PHE A 105 7813 8269 8353 -41 -10 114 C ATOM 848 O PHE A 105 -59.941 2.434 34.935 1.00 63.96 O ANISOU 848 O PHE A 105 7752 8250 8299 -43 -15 146 O ATOM 849 CB PHE A 105 -58.145 2.971 37.161 1.00 64.38 C ANISOU 849 CB PHE A 105 7837 8228 8395 -33 9 82 C ATOM 850 CG PHE A 105 -57.557 3.846 38.233 1.00 66.23 C ANISOU 850 CG PHE A 105 8073 8422 8670 -27 25 63 C ATOM 851 CD1 PHE A 105 -57.973 5.170 38.375 1.00 61.38 C ANISOU 851 CD1 PHE A 105 7434 7778 8110 -19 36 84 C ATOM 852 CD2 PHE A 105 -56.606 3.341 39.119 1.00 65.54 C ANISOU 852 CD2 PHE A 105 8008 8325 8570 -29 28 21 C ATOM 853 CE1 PHE A 105 -57.457 5.976 39.382 1.00 56.14 C ANISOU 853 CE1 PHE A 105 6769 7076 7486 -15 51 59 C ATOM 854 CE2 PHE A 105 -56.077 4.142 40.130 1.00 59.98 C ANISOU 854 CE2 PHE A 105 7302 7588 7900 -24 41 -1 C ATOM 855 CZ PHE A 105 -56.504 5.464 40.257 1.00 57.81 C ANISOU 855 CZ PHE A 105 7003 7284 7679 -18 53 14 C ATOM 856 N GLY A 106 -61.114 1.093 36.296 1.00 66.74 N ANISOU 856 N GLY A 106 8130 8588 8639 -46 -19 98 N ATOM 857 CA GLY A 106 -61.788 0.428 35.185 1.00 70.55 C ANISOU 857 CA GLY A 106 8602 9114 9088 -55 -34 114 C ATOM 858 C GLY A 106 -60.856 -0.383 34.305 1.00 72.64 C ANISOU 858 C GLY A 106 8877 9412 9311 -64 -44 100 C ATOM 859 O GLY A 106 -59.685 -0.561 34.635 1.00 74.76 O ANISOU 859 O GLY A 106 9162 9667 9576 -63 -39 76 O ATOM 860 N PRO A 107 -61.373 -0.899 33.178 1.00 75.14 N ANISOU 860 N PRO A 107 9180 9774 9594 -74 -58 111 N ATOM 861 CA PRO A 107 -60.576 -1.819 32.358 1.00 72.74 C ANISOU 861 CA PRO A 107 8883 9505 9248 -82 -67 87 C ATOM 862 C PRO A 107 -59.390 -1.169 31.657 1.00 70.71 C ANISOU 862 C PRO A 107 8618 9264 8983 -79 -62 105 C ATOM 863 O PRO A 107 -58.366 -1.822 31.492 1.00 73.19 O ANISOU 863 O PRO A 107 8948 9587 9275 -82 -63 75 O ATOM 864 CB PRO A 107 -61.582 -2.344 31.329 1.00 71.39 C ANISOU 864 CB PRO A 107 8694 9383 9046 -94 -82 97 C ATOM 865 CG PRO A 107 -62.914 -2.143 31.977 1.00 74.37 C ANISOU 865 CG PRO A 107 9066 9741 9450 -92 -82 111 C ATOM 866 CD PRO A 107 -62.778 -0.860 32.740 1.00 74.24 C ANISOU 866 CD PRO A 107 9045 9683 9479 -78 -66 137 C ATOM 867 N THR A 108 -59.500 0.088 31.239 1.00 69.22 N ANISOU 867 N THR A 108 8404 9080 8815 -73 -57 154 N ATOM 868 CA THR A 108 -58.351 0.680 30.552 1.00 69.10 C ANISOU 868 CA THR A 108 8379 9082 8793 -70 -53 174 C ATOM 869 C THR A 108 -57.220 1.009 31.531 1.00 66.66 C ANISOU 869 C THR A 108 8091 8724 8512 -63 -40 153 C ATOM 870 O THR A 108 -56.043 0.895 31.182 1.00 66.85 O ANISOU 870 O THR A 108 8120 8760 8520 -63 -38 144 O ATOM 871 CB THR A 108 -58.693 1.858 29.571 1.00 68.84 C ANISOU 871 CB THR A 108 8307 9079 8772 -67 -53 241 C ATOM 872 OG1 THR A 108 -58.713 3.100 30.270 1.00 68.18 O ANISOU 872 OG1 THR A 108 8215 8944 8748 -56 -39 269 O ATOM 873 CG2 THR A 108 -60.017 1.634 28.871 1.00 67.98 C ANISOU 873 CG2 THR A 108 8176 9012 8642 -74 -65 264 C ATOM 874 N GLY A 109 -57.588 1.380 32.758 1.00 63.35 N ANISOU 874 N GLY A 109 7682 8254 8134 -56 -31 142 N ATOM 875 CA GLY A 109 -56.628 1.502 33.851 1.00 57.80 C ANISOU 875 CA GLY A 109 7000 7509 7452 -51 -20 111 C ATOM 876 C GLY A 109 -55.987 0.157 34.124 1.00 58.61 C ANISOU 876 C GLY A 109 7130 7619 7520 -57 -25 64 C ATOM 877 O GLY A 109 -54.783 0.058 34.346 1.00 59.38 O ANISOU 877 O GLY A 109 7240 7708 7614 -55 -20 46 O ATOM 878 N CYS A 110 -56.800 -0.892 34.081 1.00 59.01 N ANISOU 878 N CYS A 110 7189 7685 7549 -63 -35 46 N ATOM 879 CA CYS A 110 -56.318 -2.246 34.267 1.00 57.96 C ANISOU 879 CA CYS A 110 7078 7556 7389 -68 -40 4 C ATOM 880 C CYS A 110 -55.271 -2.583 33.231 1.00 57.79 C ANISOU 880 C CYS A 110 7055 7568 7335 -71 -44 -2 C ATOM 881 O CYS A 110 -54.349 -3.342 33.497 1.00 61.65 O ANISOU 881 O CYS A 110 7560 8050 7812 -71 -43 -34 O ATOM 882 CB CYS A 110 -57.469 -3.235 34.170 1.00 55.86 C ANISOU 882 CB CYS A 110 6813 7303 7109 -76 -51 -9 C ATOM 883 SG CYS A 110 -57.029 -4.906 34.669 1.00 70.17 S ANISOU 883 SG CYS A 110 8651 9106 8906 -82 -56 -60 S ATOM 884 N ASN A 111 -55.412 -2.028 32.037 1.00 60.61 N ANISOU 884 N ASN A 111 7388 7964 7677 -74 -48 31 N ATOM 885 CA ASN A 111 -54.422 -2.275 31.003 1.00 62.83 C ANISOU 885 CA ASN A 111 7663 8285 7924 -76 -51 28 C ATOM 886 C ASN A 111 -53.154 -1.501 31.307 1.00 62.12 C ANISOU 886 C ASN A 111 7577 8175 7853 -69 -39 37 C ATOM 887 O ASN A 111 -52.064 -2.073 31.330 1.00 64.28 O ANISOU 887 O ASN A 111 7863 8449 8110 -68 -37 10 O ATOM 888 CB ASN A 111 -54.964 -1.941 29.607 1.00 62.36 C ANISOU 888 CB ASN A 111 7572 8284 7836 -82 -59 63 C ATOM 889 CG ASN A 111 -55.826 -3.052 29.035 1.00 58.79 C ANISOU 889 CG ASN A 111 7118 7867 7351 -93 -73 38 C ATOM 890 OD1 ASN A 111 -55.511 -4.238 29.143 1.00 53.91 O ANISOU 890 OD1 ASN A 111 6518 7249 6718 -97 -76 -11 O ATOM 891 ND2 ASN A 111 -56.921 -2.667 28.412 1.00 79.36 N ANISOU 891 ND2 ASN A 111 9699 10505 9950 -97 -80 71 N ATOM 892 N LEU A 112 -53.317 -0.206 31.570 1.00 61.09 N ANISOU 892 N LEU A 112 7431 8022 7758 -63 -32 75 N ATOM 893 CA LEU A 112 -52.211 0.661 31.943 1.00 59.41 C ANISOU 893 CA LEU A 112 7218 7783 7571 -57 -20 86 C ATOM 894 C LEU A 112 -51.401 0.106 33.123 1.00 59.54 C ANISOU 894 C LEU A 112 7264 7763 7596 -55 -15 41 C ATOM 895 O LEU A 112 -50.223 -0.213 32.960 1.00 59.31 O ANISOU 895 O LEU A 112 7243 7743 7551 -55 -13 26 O ATOM 896 CB LEU A 112 -52.710 2.085 32.207 1.00 59.87 C ANISOU 896 CB LEU A 112 7256 7812 7679 -52 -12 127 C ATOM 897 CG LEU A 112 -52.842 2.964 30.949 1.00 64.69 C ANISOU 897 CG LEU A 112 7831 8459 8290 -52 -14 186 C ATOM 898 CD1 LEU A 112 -53.774 4.149 31.187 1.00 54.76 C ANISOU 898 CD1 LEU A 112 6550 7172 7084 -47 -8 227 C ATOM 899 CD2 LEU A 112 -51.467 3.448 30.432 1.00 63.69 C ANISOU 899 CD2 LEU A 112 7695 8344 8161 -51 -9 203 C ATOM 900 N GLU A 113 -52.033 -0.049 34.289 1.00 58.63 N ANISOU 900 N GLU A 113 7162 7612 7502 -53 -12 21 N ATOM 901 CA GLU A 113 -51.340 -0.548 35.473 1.00 57.41 C ANISOU 901 CA GLU A 113 7030 7428 7353 -51 -7 -17 C ATOM 902 C GLU A 113 -50.693 -1.907 35.212 1.00 59.42 C ANISOU 902 C GLU A 113 7302 7702 7573 -54 -13 -48 C ATOM 903 O GLU A 113 -49.561 -2.164 35.634 1.00 62.27 O ANISOU 903 O GLU A 113 7674 8054 7931 -52 -9 -67 O ATOM 904 CB GLU A 113 -52.285 -0.613 36.674 1.00 57.67 C ANISOU 904 CB GLU A 113 7072 7432 7408 -50 -5 -31 C ATOM 905 CG GLU A 113 -51.619 -0.981 38.018 1.00 63.89 C ANISOU 905 CG GLU A 113 7878 8195 8203 -47 1 -64 C ATOM 906 CD GLU A 113 -51.560 -2.493 38.280 1.00 73.11 C ANISOU 906 CD GLU A 113 9064 9370 9345 -50 -5 -92 C ATOM 907 OE1 GLU A 113 -50.513 -2.999 38.746 1.00 80.07 O ANISOU 907 OE1 GLU A 113 9956 10247 10218 -49 -3 -112 O ATOM 908 OE2 GLU A 113 -52.565 -3.183 38.024 1.00 82.68 O ANISOU 908 OE2 GLU A 113 10275 10592 10546 -54 -13 -92 O ATOM 909 N GLY A 114 -51.407 -2.776 34.508 1.00 58.41 N ANISOU 909 N GLY A 114 7172 7601 7419 -60 -23 -54 N ATOM 910 CA GLY A 114 -50.899 -4.108 34.230 1.00 56.58 C ANISOU 910 CA GLY A 114 6953 7384 7160 -63 -28 -87 C ATOM 911 C GLY A 114 -49.672 -4.036 33.350 1.00 56.50 C ANISOU 911 C GLY A 114 6937 7400 7129 -61 -26 -87 C ATOM 912 O GLY A 114 -48.700 -4.757 33.562 1.00 57.92 O ANISOU 912 O GLY A 114 7129 7575 7301 -59 -24 -113 O ATOM 913 N PHE A 115 -49.712 -3.159 32.357 1.00 55.92 N ANISOU 913 N PHE A 115 6842 7356 7047 -62 -27 -53 N ATOM 914 CA PHE A 115 -48.573 -2.991 31.466 1.00 58.10 C ANISOU 914 CA PHE A 115 7109 7664 7302 -61 -24 -46 C ATOM 915 C PHE A 115 -47.330 -2.504 32.240 1.00 57.59 C ANISOU 915 C PHE A 115 7054 7569 7258 -55 -14 -48 C ATOM 916 O PHE A 115 -46.320 -3.202 32.309 1.00 58.19 O ANISOU 916 O PHE A 115 7142 7647 7322 -53 -12 -74 O ATOM 917 CB PHE A 115 -48.930 -2.055 30.309 1.00 53.92 C ANISOU 917 CB PHE A 115 6550 7175 6761 -63 -27 0 C ATOM 918 CG PHE A 115 -47.800 -1.808 29.348 1.00 62.47 C ANISOU 918 CG PHE A 115 7618 8297 7820 -62 -24 14 C ATOM 919 CD1 PHE A 115 -47.522 -2.718 28.326 1.00 71.34 C ANISOU 919 CD1 PHE A 115 8737 9473 8897 -66 -29 -9 C ATOM 920 CD2 PHE A 115 -47.039 -0.646 29.434 1.00 59.99 C ANISOU 920 CD2 PHE A 115 7294 7971 7531 -58 -15 49 C ATOM 921 CE1 PHE A 115 -46.484 -2.483 27.419 1.00 67.41 C ANISOU 921 CE1 PHE A 115 8222 9017 8373 -65 -25 4 C ATOM 922 CE2 PHE A 115 -46.006 -0.399 28.531 1.00 59.45 C ANISOU 922 CE2 PHE A 115 7209 7941 7440 -57 -12 66 C ATOM 923 CZ PHE A 115 -45.722 -1.321 27.526 1.00 59.20 C ANISOU 923 CZ PHE A 115 7171 7964 7356 -60 -17 45 C ATOM 924 N PHE A 116 -47.421 -1.330 32.853 1.00 56.56 N ANISOU 924 N PHE A 116 6918 7409 7164 -53 -8 -22 N ATOM 925 CA PHE A 116 -46.258 -0.730 33.487 1.00 57.73 C ANISOU 925 CA PHE A 116 7070 7531 7333 -49 1 -23 C ATOM 926 C PHE A 116 -45.669 -1.577 34.632 1.00 60.70 C ANISOU 926 C PHE A 116 7470 7882 7711 -47 4 -63 C ATOM 927 O PHE A 116 -44.441 -1.731 34.739 1.00 60.27 O ANISOU 927 O PHE A 116 7421 7827 7650 -45 8 -74 O ATOM 928 CB PHE A 116 -46.559 0.707 33.910 1.00 54.58 C ANISOU 928 CB PHE A 116 6657 7104 6979 -48 8 8 C ATOM 929 CG PHE A 116 -46.573 1.671 32.763 1.00 57.24 C ANISOU 929 CG PHE A 116 6965 7465 7319 -48 9 57 C ATOM 930 CD1 PHE A 116 -45.452 1.812 31.943 1.00 63.24 C ANISOU 930 CD1 PHE A 116 7714 8254 8061 -49 10 72 C ATOM 931 CD2 PHE A 116 -47.701 2.422 32.477 1.00 61.68 C ANISOU 931 CD2 PHE A 116 7508 8026 7903 -48 8 91 C ATOM 932 CE1 PHE A 116 -45.453 2.694 30.847 1.00 55.47 C ANISOU 932 CE1 PHE A 116 6699 7298 7079 -49 11 123 C ATOM 933 CE2 PHE A 116 -47.706 3.313 31.393 1.00 69.43 C ANISOU 933 CE2 PHE A 116 8457 9032 8889 -49 8 144 C ATOM 934 CZ PHE A 116 -46.574 3.447 30.581 1.00 57.32 C ANISOU 934 CZ PHE A 116 6913 7531 7337 -50 10 161 C ATOM 935 N ALA A 117 -46.535 -2.155 35.461 1.00 58.84 N ANISOU 935 N ALA A 117 7247 7627 7482 -47 1 -82 N ATOM 936 CA ALA A 117 -46.073 -3.122 36.437 1.00 55.47 C ANISOU 936 CA ALA A 117 6840 7183 7053 -46 2 -115 C ATOM 937 C ALA A 117 -45.378 -4.294 35.738 1.00 57.41 C ANISOU 937 C ALA A 117 7092 7452 7271 -45 -2 -135 C ATOM 938 O ALA A 117 -44.222 -4.577 36.034 1.00 61.18 O ANISOU 938 O ALA A 117 7575 7925 7745 -42 2 -148 O ATOM 939 CB ALA A 117 -47.205 -3.597 37.304 1.00 55.51 C ANISOU 939 CB ALA A 117 6853 7169 7067 -47 -1 -126 C ATOM 940 N THR A 118 -46.048 -4.953 34.790 1.00 56.85 N ANISOU 940 N THR A 118 7016 7406 7178 -49 -9 -140 N ATOM 941 CA THR A 118 -45.430 -6.093 34.106 1.00 55.28 C ANISOU 941 CA THR A 118 6821 7229 6956 -48 -11 -167 C ATOM 942 C THR A 118 -44.129 -5.696 33.393 1.00 57.30 C ANISOU 942 C THR A 118 7068 7507 7196 -45 -6 -160 C ATOM 943 O THR A 118 -43.097 -6.372 33.533 1.00 56.05 O ANISOU 943 O THR A 118 6917 7347 7033 -41 -2 -181 O ATOM 944 CB THR A 118 -46.378 -6.783 33.107 1.00 55.15 C ANISOU 944 CB THR A 118 6796 7241 6918 -55 -20 -177 C ATOM 945 OG1 THR A 118 -47.567 -7.212 33.777 1.00 53.61 O ANISOU 945 OG1 THR A 118 6608 7024 6739 -58 -25 -183 O ATOM 946 CG2 THR A 118 -45.703 -8.016 32.485 1.00 53.50 C ANISOU 946 CG2 THR A 118 6588 7049 6689 -54 -21 -214 C ATOM 947 N LEU A 119 -44.174 -4.593 32.647 1.00 56.41 N ANISOU 947 N LEU A 119 6938 7418 7078 -47 -5 -126 N ATOM 948 CA LEU A 119 -42.995 -4.115 31.938 1.00 55.40 C ANISOU 948 CA LEU A 119 6798 7315 6937 -44 0 -113 C ATOM 949 C LEU A 119 -41.831 -3.955 32.900 1.00 57.06 C ANISOU 949 C LEU A 119 7019 7494 7165 -39 8 -120 C ATOM 950 O LEU A 119 -40.709 -4.355 32.586 1.00 59.17 O ANISOU 950 O LEU A 119 7287 7776 7418 -36 12 -132 O ATOM 951 CB LEU A 119 -43.270 -2.797 31.211 1.00 55.15 C ANISOU 951 CB LEU A 119 6743 7304 6908 -46 1 -66 C ATOM 952 CG LEU A 119 -42.138 -2.275 30.311 1.00 52.61 C ANISOU 952 CG LEU A 119 6403 7016 6569 -45 6 -44 C ATOM 953 CD1 LEU A 119 -41.891 -3.212 29.135 1.00 48.40 C ANISOU 953 CD1 LEU A 119 5862 6538 5989 -45 3 -64 C ATOM 954 CD2 LEU A 119 -42.411 -0.850 29.820 1.00 43.90 C ANISOU 954 CD2 LEU A 119 5275 5922 5482 -47 7 11 C ATOM 955 N GLY A 120 -42.114 -3.386 34.074 1.00 58.86 N ANISOU 955 N GLY A 120 7255 7684 7426 -40 10 -115 N ATOM 956 CA GLY A 120 -41.106 -3.154 35.112 1.00 56.38 C ANISOU 956 CA GLY A 120 6948 7343 7129 -37 16 -122 C ATOM 957 C GLY A 120 -40.434 -4.433 35.565 1.00 56.69 C ANISOU 957 C GLY A 120 7003 7379 7158 -33 17 -154 C ATOM 958 O GLY A 120 -39.224 -4.613 35.386 1.00 57.87 O ANISOU 958 O GLY A 120 7151 7537 7299 -29 21 -160 O ATOM 959 N GLY A 121 -41.224 -5.337 36.135 1.00 55.11 N ANISOU 959 N GLY A 121 6815 7165 6962 -33 12 -173 N ATOM 960 CA GLY A 121 -40.689 -6.583 36.675 1.00 56.74 C ANISOU 960 CA GLY A 121 7032 7361 7167 -28 13 -199 C ATOM 961 C GLY A 121 -39.993 -7.423 35.626 1.00 58.11 C ANISOU 961 C GLY A 121 7202 7558 7319 -25 14 -215 C ATOM 962 O GLY A 121 -39.152 -8.251 35.950 1.00 59.52 O ANISOU 962 O GLY A 121 7385 7729 7500 -19 17 -232 O ATOM 963 N GLU A 122 -40.364 -7.217 34.366 1.00 60.94 N ANISOU 963 N GLU A 122 7550 7948 7658 -28 11 -210 N ATOM 964 CA GLU A 122 -39.764 -7.937 33.242 1.00 61.68 C ANISOU 964 CA GLU A 122 7636 8073 7726 -25 12 -230 C ATOM 965 C GLU A 122 -38.389 -7.394 32.902 1.00 59.74 C ANISOU 965 C GLU A 122 7382 7845 7471 -20 20 -218 C ATOM 966 O GLU A 122 -37.435 -8.158 32.776 1.00 60.08 O ANISOU 966 O GLU A 122 7426 7893 7508 -14 24 -240 O ATOM 967 CB GLU A 122 -40.667 -7.862 32.010 1.00 63.53 C ANISOU 967 CB GLU A 122 7857 8345 7936 -31 6 -228 C ATOM 968 CG GLU A 122 -41.684 -8.969 31.953 1.00 64.31 C ANISOU 968 CG GLU A 122 7960 8437 8036 -35 0 -257 C ATOM 969 CD GLU A 122 -41.051 -10.304 31.647 1.00 67.36 C ANISOU 969 CD GLU A 122 8349 8826 8419 -30 2 -299 C ATOM 970 OE1 GLU A 122 -40.418 -10.412 30.584 1.00 73.60 O ANISOU 970 OE1 GLU A 122 9126 9655 9182 -28 6 -311 O ATOM 971 OE2 GLU A 122 -41.178 -11.241 32.462 1.00 71.68 O ANISOU 971 OE2 GLU A 122 8907 9337 8992 -28 2 -319 O ATOM 972 N ILE A 123 -38.300 -6.073 32.742 1.00 56.94 N ANISOU 972 N ILE A 123 7017 7498 7118 -23 21 -184 N ATOM 973 CA ILE A 123 -37.013 -5.396 32.601 1.00 53.81 C ANISOU 973 CA ILE A 123 6612 7112 6720 -21 28 -167 C ATOM 974 C ILE A 123 -36.075 -5.787 33.747 1.00 54.57 C ANISOU 974 C ILE A 123 6722 7178 6835 -16 32 -182 C ATOM 975 O ILE A 123 -34.922 -6.147 33.510 1.00 54.86 O ANISOU 975 O ILE A 123 6756 7228 6863 -10 38 -190 O ATOM 976 CB ILE A 123 -37.177 -3.870 32.546 1.00 51.33 C ANISOU 976 CB ILE A 123 6286 6797 6421 -26 29 -126 C ATOM 977 CG1 ILE A 123 -37.949 -3.466 31.293 1.00 51.24 C ANISOU 977 CG1 ILE A 123 6256 6824 6389 -30 25 -103 C ATOM 978 CG2 ILE A 123 -35.827 -3.192 32.554 1.00 49.83 C ANISOU 978 CG2 ILE A 123 6087 6610 6237 -24 36 -110 C ATOM 979 CD1 ILE A 123 -38.334 -2.001 31.244 1.00 53.66 C ANISOU 979 CD1 ILE A 123 6547 7124 6719 -34 26 -58 C ATOM 980 N ALA A 124 -36.580 -5.742 34.980 1.00 53.55 N ANISOU 980 N ALA A 124 6604 7013 6729 -18 30 -184 N ATOM 981 CA ALA A 124 -35.819 -6.206 36.141 1.00 53.43 C ANISOU 981 CA ALA A 124 6598 6975 6728 -14 33 -197 C ATOM 982 C ALA A 124 -35.310 -7.631 35.939 1.00 53.94 C ANISOU 982 C ALA A 124 6667 7044 6784 -6 35 -223 C ATOM 983 O ALA A 124 -34.128 -7.901 36.115 1.00 56.88 O ANISOU 983 O ALA A 124 7038 7418 7156 0 40 -227 O ATOM 984 CB ALA A 124 -36.659 -6.109 37.422 1.00 50.98 C ANISOU 984 CB ALA A 124 6298 6636 6438 -17 30 -198 C ATOM 985 N LEU A 125 -36.206 -8.528 35.543 1.00 56.33 N ANISOU 985 N LEU A 125 6973 7347 7083 -6 30 -241 N ATOM 986 CA LEU A 125 -35.875 -9.931 35.307 1.00 59.56 C ANISOU 986 CA LEU A 125 7384 7754 7492 1 32 -270 C ATOM 987 C LEU A 125 -34.758 -10.116 34.273 1.00 60.55 C ANISOU 987 C LEU A 125 7499 7909 7599 8 39 -280 C ATOM 988 O LEU A 125 -33.751 -10.755 34.565 1.00 59.76 O ANISOU 988 O LEU A 125 7398 7801 7506 16 45 -291 O ATOM 989 CB LEU A 125 -37.146 -10.715 34.923 1.00 61.01 C ANISOU 989 CB LEU A 125 7570 7934 7677 -3 26 -289 C ATOM 990 CG LEU A 125 -37.152 -12.081 34.218 1.00 62.23 C ANISOU 990 CG LEU A 125 7721 8092 7832 1 27 -326 C ATOM 991 CD1 LEU A 125 -36.137 -13.040 34.777 1.00 59.66 C ANISOU 991 CD1 LEU A 125 7396 7744 7527 12 34 -340 C ATOM 992 CD2 LEU A 125 -38.547 -12.686 34.318 1.00 68.83 C ANISOU 992 CD2 LEU A 125 8561 8913 8680 -5 19 -338 C ATOM 993 N TRP A 126 -34.926 -9.542 33.083 1.00 62.57 N ANISOU 993 N TRP A 126 7743 8201 7828 4 39 -275 N ATOM 994 CA TRP A 126 -33.924 -9.680 32.021 1.00 65.15 C ANISOU 994 CA TRP A 126 8057 8566 8131 10 46 -284 C ATOM 995 C TRP A 126 -32.619 -8.935 32.330 1.00 64.84 C ANISOU 995 C TRP A 126 8013 8528 8093 13 52 -261 C ATOM 996 O TRP A 126 -31.537 -9.349 31.897 1.00 67.30 O ANISOU 996 O TRP A 126 8317 8858 8396 21 60 -273 O ATOM 997 CB TRP A 126 -34.498 -9.296 30.643 1.00 65.97 C ANISOU 997 CB TRP A 126 8146 8717 8202 4 43 -281 C ATOM 998 CG TRP A 126 -35.398 -10.371 30.076 1.00 69.45 C ANISOU 998 CG TRP A 126 8587 9167 8635 2 39 -319 C ATOM 999 CD1 TRP A 126 -36.763 -10.373 30.057 1.00 68.81 C ANISOU 999 CD1 TRP A 126 8508 9081 8555 -7 30 -319 C ATOM 1000 CD2 TRP A 126 -34.991 -11.618 29.487 1.00 73.06 C ANISOU 1000 CD2 TRP A 126 9038 9635 9086 8 44 -365 C ATOM 1001 NE1 TRP A 126 -37.230 -11.529 29.482 1.00 65.63 N ANISOU 1001 NE1 TRP A 126 8102 8687 8146 -7 28 -362 N ATOM 1002 CE2 TRP A 126 -36.163 -12.313 29.128 1.00 73.35 C ANISOU 1002 CE2 TRP A 126 9075 9673 9121 2 37 -393 C ATOM 1003 CE3 TRP A 126 -33.750 -12.212 29.226 1.00 69.49 C ANISOU 1003 CE3 TRP A 126 8580 9192 8632 19 54 -388 C ATOM 1004 CZ2 TRP A 126 -36.130 -13.569 28.519 1.00 73.91 C ANISOU 1004 CZ2 TRP A 126 9139 9752 9191 5 40 -446 C ATOM 1005 CZ3 TRP A 126 -33.721 -13.458 28.624 1.00 63.98 C ANISOU 1005 CZ3 TRP A 126 7875 8501 7933 24 58 -439 C ATOM 1006 CH2 TRP A 126 -34.901 -14.123 28.281 1.00 68.76 C ANISOU 1006 CH2 TRP A 126 8480 9106 8540 16 51 -469 C ATOM 1007 N SER A 127 -32.721 -7.853 33.095 1.00 61.21 N ANISOU 1007 N SER A 127 7557 8051 7649 7 50 -231 N ATOM 1008 CA SER A 127 -31.541 -7.175 33.594 1.00 57.24 C ANISOU 1008 CA SER A 127 7051 7544 7155 8 54 -212 C ATOM 1009 C SER A 127 -30.684 -8.140 34.394 1.00 56.63 C ANISOU 1009 C SER A 127 6980 7448 7090 17 58 -231 C ATOM 1010 O SER A 127 -29.469 -8.181 34.218 1.00 59.40 O ANISOU 1010 O SER A 127 7323 7811 7436 23 65 -230 O ATOM 1011 CB SER A 127 -31.926 -5.974 34.443 1.00 54.95 C ANISOU 1011 CB SER A 127 6762 7231 6885 -1 51 -187 C ATOM 1012 OG SER A 127 -32.300 -4.899 33.606 1.00 58.23 O ANISOU 1012 OG SER A 127 7164 7666 7293 -7 50 -160 O ATOM 1013 N LEU A 128 -31.308 -8.929 35.262 1.00 53.56 N ANISOU 1013 N LEU A 128 6602 7028 6718 18 55 -245 N ATOM 1014 CA LEU A 128 -30.549 -9.892 36.065 1.00 55.32 C ANISOU 1014 CA LEU A 128 6829 7234 6958 27 58 -257 C ATOM 1015 C LEU A 128 -29.937 -11.000 35.212 1.00 57.46 C ANISOU 1015 C LEU A 128 7093 7517 7223 38 65 -283 C ATOM 1016 O LEU A 128 -29.024 -11.700 35.653 1.00 58.63 O ANISOU 1016 O LEU A 128 7238 7655 7384 47 70 -288 O ATOM 1017 CB LEU A 128 -31.405 -10.500 37.177 1.00 50.88 C ANISOU 1017 CB LEU A 128 6277 6639 6417 26 53 -260 C ATOM 1018 CG LEU A 128 -31.835 -9.524 38.257 1.00 46.97 C ANISOU 1018 CG LEU A 128 5786 6132 5929 16 48 -240 C ATOM 1019 CD1 LEU A 128 -32.430 -10.290 39.412 1.00 53.98 C ANISOU 1019 CD1 LEU A 128 6679 6995 6834 17 45 -241 C ATOM 1020 CD2 LEU A 128 -30.651 -8.691 38.707 1.00 50.36 C ANISOU 1020 CD2 LEU A 128 6209 6570 6357 15 51 -225 C ATOM 1021 N VAL A 129 -30.458 -11.165 34.002 1.00 57.91 N ANISOU 1021 N VAL A 129 7145 7598 7261 37 65 -299 N ATOM 1022 CA VAL A 129 -29.944 -12.170 33.094 1.00 57.64 C ANISOU 1022 CA VAL A 129 7101 7580 7219 47 73 -332 C ATOM 1023 C VAL A 129 -28.749 -11.564 32.395 1.00 56.39 C ANISOU 1023 C VAL A 129 6930 7458 7038 51 80 -321 C ATOM 1024 O VAL A 129 -27.639 -12.091 32.491 1.00 56.89 O ANISOU 1024 O VAL A 129 6988 7520 7109 61 88 -330 O ATOM 1025 CB VAL A 129 -30.999 -12.627 32.046 1.00 58.24 C ANISOU 1025 CB VAL A 129 7174 7674 7279 43 69 -360 C ATOM 1026 CG1 VAL A 129 -30.335 -13.413 30.928 1.00 52.93 C ANISOU 1026 CG1 VAL A 129 6488 7032 6592 51 78 -396 C ATOM 1027 CG2 VAL A 129 -32.069 -13.465 32.700 1.00 53.58 C ANISOU 1027 CG2 VAL A 129 6595 7045 6716 40 63 -375 C ATOM 1028 N VAL A 130 -28.980 -10.444 31.713 1.00 53.97 N ANISOU 1028 N VAL A 130 6617 7183 6707 42 78 -299 N ATOM 1029 CA VAL A 130 -27.927 -9.765 30.959 1.00 54.24 C ANISOU 1029 CA VAL A 130 6635 7257 6718 44 84 -282 C ATOM 1030 C VAL A 130 -26.646 -9.601 31.798 1.00 57.11 C ANISOU 1030 C VAL A 130 6998 7603 7098 50 90 -267 C ATOM 1031 O VAL A 130 -25.552 -9.908 31.319 1.00 62.24 O ANISOU 1031 O VAL A 130 7635 8274 7738 59 99 -275 O ATOM 1032 CB VAL A 130 -28.426 -8.420 30.394 1.00 53.49 C ANISOU 1032 CB VAL A 130 6531 7187 6605 33 80 -247 C ATOM 1033 CG1 VAL A 130 -27.272 -7.551 29.933 1.00 51.12 C ANISOU 1033 CG1 VAL A 130 6213 6917 6292 34 86 -218 C ATOM 1034 CG2 VAL A 130 -29.421 -8.661 29.262 1.00 51.28 C ANISOU 1034 CG2 VAL A 130 6244 6943 6298 30 77 -261 C ATOM 1035 N LEU A 131 -26.794 -9.165 33.051 1.00 55.76 N ANISOU 1035 N LEU A 131 6838 7396 6951 44 84 -249 N ATOM 1036 CA LEU A 131 -25.680 -9.063 33.986 1.00 55.65 C ANISOU 1036 CA LEU A 131 6823 7367 6953 48 87 -237 C ATOM 1037 C LEU A 131 -24.882 -10.375 34.100 1.00 58.06 C ANISOU 1037 C LEU A 131 7127 7667 7269 62 94 -261 C ATOM 1038 O LEU A 131 -23.660 -10.390 33.924 1.00 58.70 O ANISOU 1038 O LEU A 131 7196 7763 7345 70 102 -256 O ATOM 1039 CB LEU A 131 -26.171 -8.597 35.368 1.00 56.14 C ANISOU 1039 CB LEU A 131 6897 7396 7038 39 79 -223 C ATOM 1040 CG LEU A 131 -25.093 -8.226 36.410 1.00 59.28 C ANISOU 1040 CG LEU A 131 7291 7785 7448 38 80 -207 C ATOM 1041 CD1 LEU A 131 -24.190 -7.113 35.899 1.00 58.27 C ANISOU 1041 CD1 LEU A 131 7149 7680 7311 33 83 -186 C ATOM 1042 CD2 LEU A 131 -25.679 -7.848 37.774 1.00 50.91 C ANISOU 1042 CD2 LEU A 131 6239 6698 6405 29 72 -200 C ATOM 1043 N ALA A 132 -25.569 -11.475 34.392 1.00 58.49 N ANISOU 1043 N ALA A 132 7189 7696 7339 67 93 -284 N ATOM 1044 CA ALA A 132 -24.921 -12.777 34.448 1.00 57.93 C ANISOU 1044 CA ALA A 132 7113 7614 7286 82 101 -307 C ATOM 1045 C ALA A 132 -24.164 -13.072 33.146 1.00 60.42 C ANISOU 1045 C ALA A 132 7413 7964 7580 92 112 -329 C ATOM 1046 O ALA A 132 -23.038 -13.561 33.185 1.00 62.63 O ANISOU 1046 O ALA A 132 7683 8246 7868 104 121 -333 O ATOM 1047 CB ALA A 132 -25.936 -13.870 34.742 1.00 56.17 C ANISOU 1047 CB ALA A 132 6897 7358 7086 84 98 -330 C ATOM 1048 N ILE A 133 -24.775 -12.785 31.995 1.00 60.28 N ANISOU 1048 N ILE A 133 7391 7978 7534 86 111 -342 N ATOM 1049 CA ILE A 133 -24.077 -12.950 30.717 1.00 60.97 C ANISOU 1049 CA ILE A 133 7461 8111 7595 94 122 -361 C ATOM 1050 C ILE A 133 -22.803 -12.087 30.724 1.00 64.05 C ANISOU 1050 C ILE A 133 7841 8524 7973 96 127 -329 C ATOM 1051 O ILE A 133 -21.676 -12.611 30.636 1.00 63.17 O ANISOU 1051 O ILE A 133 7717 8418 7866 108 137 -339 O ATOM 1052 CB ILE A 133 -24.992 -12.623 29.489 1.00 59.88 C ANISOU 1052 CB ILE A 133 7317 8014 7421 86 118 -374 C ATOM 1053 CG1 ILE A 133 -26.101 -13.671 29.363 1.00 58.03 C ANISOU 1053 CG1 ILE A 133 7089 7759 7199 85 115 -414 C ATOM 1054 CG2 ILE A 133 -24.185 -12.582 28.186 1.00 53.83 C ANISOU 1054 CG2 ILE A 133 6528 7306 6618 92 129 -387 C ATOM 1055 CD1 ILE A 133 -27.288 -13.239 28.510 1.00 41.06 C ANISOU 1055 CD1 ILE A 133 4937 5642 5020 73 107 -418 C ATOM 1056 N GLU A 134 -22.989 -10.775 30.887 1.00 61.74 N ANISOU 1056 N GLU A 134 7549 8239 7669 82 120 -291 N ATOM 1057 CA GLU A 134 -21.881 -9.820 30.875 1.00 58.68 C ANISOU 1057 CA GLU A 134 7150 7872 7274 80 123 -258 C ATOM 1058 C GLU A 134 -20.754 -10.185 31.838 1.00 57.89 C ANISOU 1058 C GLU A 134 7050 7749 7198 89 127 -253 C ATOM 1059 O GLU A 134 -19.588 -10.134 31.472 1.00 56.81 O ANISOU 1059 O GLU A 134 6898 7636 7053 96 136 -247 O ATOM 1060 CB GLU A 134 -22.388 -8.404 31.131 1.00 54.19 C ANISOU 1060 CB GLU A 134 6584 7301 6706 64 114 -219 C ATOM 1061 CG GLU A 134 -23.384 -7.951 30.090 1.00 54.97 C ANISOU 1061 CG GLU A 134 6676 7429 6780 57 111 -215 C ATOM 1062 CD GLU A 134 -23.889 -6.548 30.325 1.00 65.55 C ANISOU 1062 CD GLU A 134 8016 8763 8128 42 103 -174 C ATOM 1063 OE1 GLU A 134 -23.753 -6.047 31.456 1.00 79.37 O ANISOU 1063 OE1 GLU A 134 9775 10476 9905 36 98 -160 O ATOM 1064 OE2 GLU A 134 -24.437 -5.941 29.383 1.00 68.46 O ANISOU 1064 OE2 GLU A 134 8373 9163 8476 36 101 -157 O ATOM 1065 N ARG A 135 -21.097 -10.575 33.058 1.00 58.78 N ANISOU 1065 N ARG A 135 7176 7819 7339 88 121 -254 N ATOM 1066 CA ARG A 135 -20.072 -10.946 34.022 1.00 61.57 C ANISOU 1066 CA ARG A 135 7526 8155 7713 95 124 -245 C ATOM 1067 C ARG A 135 -19.295 -12.149 33.534 1.00 64.80 C ANISOU 1067 C ARG A 135 7924 8570 8127 114 136 -271 C ATOM 1068 O ARG A 135 -18.069 -12.129 33.493 1.00 69.85 O ANISOU 1068 O ARG A 135 8550 9224 8766 121 144 -262 O ATOM 1069 CB ARG A 135 -20.675 -11.220 35.395 1.00 60.92 C ANISOU 1069 CB ARG A 135 7457 8032 7656 91 115 -240 C ATOM 1070 CG ARG A 135 -20.970 -9.962 36.160 1.00 57.33 C ANISOU 1070 CG ARG A 135 7008 7572 7201 74 105 -213 C ATOM 1071 CD ARG A 135 -21.941 -10.228 37.253 1.00 57.10 C ANISOU 1071 CD ARG A 135 6993 7512 7189 68 96 -214 C ATOM 1072 NE ARG A 135 -22.039 -9.088 38.158 1.00 60.75 N ANISOU 1072 NE ARG A 135 7457 7970 7654 53 89 -194 N ATOM 1073 CZ ARG A 135 -22.779 -9.077 39.260 1.00 59.05 C ANISOU 1073 CZ ARG A 135 7251 7735 7451 47 81 -192 C ATOM 1074 NH1 ARG A 135 -23.512 -10.137 39.600 1.00 52.80 N ANISOU 1074 NH1 ARG A 135 6466 6924 6669 53 80 -203 N ATOM 1075 NH2 ARG A 135 -22.782 -8.005 40.024 1.00 57.05 N ANISOU 1075 NH2 ARG A 135 6996 7481 7199 33 75 -180 N ATOM 1076 N TYR A 136 -20.018 -13.191 33.150 1.00 66.95 N ANISOU 1076 N TYR A 136 8201 8830 8408 121 139 -305 N ATOM 1077 CA TYR A 136 -19.415 -14.396 32.600 1.00 66.97 C ANISOU 1077 CA TYR A 136 8191 8834 8422 139 152 -339 C ATOM 1078 C TYR A 136 -18.514 -14.075 31.416 1.00 66.35 C ANISOU 1078 C TYR A 136 8094 8805 8311 145 163 -345 C ATOM 1079 O TYR A 136 -17.395 -14.564 31.337 1.00 68.73 O ANISOU 1079 O TYR A 136 8381 9112 8621 159 174 -351 O ATOM 1080 CB TYR A 136 -20.515 -15.370 32.186 1.00 67.18 C ANISOU 1080 CB TYR A 136 8224 8843 8460 142 152 -379 C ATOM 1081 CG TYR A 136 -20.153 -16.304 31.062 1.00 66.44 C ANISOU 1081 CG TYR A 136 8114 8768 8363 156 166 -426 C ATOM 1082 CD1 TYR A 136 -19.496 -17.499 31.322 1.00 65.71 C ANISOU 1082 CD1 TYR A 136 8011 8647 8308 174 177 -447 C ATOM 1083 CD2 TYR A 136 -20.493 -16.006 29.740 1.00 61.90 C ANISOU 1083 CD2 TYR A 136 7531 8241 7748 152 168 -449 C ATOM 1084 CE1 TYR A 136 -19.175 -18.371 30.308 1.00 69.13 C ANISOU 1084 CE1 TYR A 136 8428 9096 8744 187 191 -496 C ATOM 1085 CE2 TYR A 136 -20.185 -16.876 28.715 1.00 63.68 C ANISOU 1085 CE2 TYR A 136 7740 8489 7968 164 182 -499 C ATOM 1086 CZ TYR A 136 -19.527 -18.060 29.012 1.00 70.17 C ANISOU 1086 CZ TYR A 136 8553 9278 8832 182 193 -525 C ATOM 1087 OH TYR A 136 -19.203 -18.947 28.023 1.00 68.38 O ANISOU 1087 OH TYR A 136 8307 9070 8604 195 208 -581 O ATOM 1088 N VAL A 137 -19.006 -13.252 30.496 1.00 65.88 N ANISOU 1088 N VAL A 137 8033 8783 8216 134 160 -342 N ATOM 1089 CA VAL A 137 -18.208 -12.835 29.340 1.00 63.65 C ANISOU 1089 CA VAL A 137 7729 8556 7898 138 170 -341 C ATOM 1090 C VAL A 137 -16.898 -12.177 29.794 1.00 65.55 C ANISOU 1090 C VAL A 137 7960 8804 8141 140 173 -304 C ATOM 1091 O VAL A 137 -15.826 -12.518 29.301 1.00 69.13 O ANISOU 1091 O VAL A 137 8396 9283 8588 153 186 -313 O ATOM 1092 CB VAL A 137 -19.020 -11.903 28.386 1.00 61.66 C ANISOU 1092 CB VAL A 137 7475 8347 7608 124 164 -330 C ATOM 1093 CG1 VAL A 137 -18.112 -10.958 27.639 1.00 52.51 C ANISOU 1093 CG1 VAL A 137 6295 7239 6418 122 170 -300 C ATOM 1094 CG2 VAL A 137 -19.854 -12.723 27.415 1.00 58.46 C ANISOU 1094 CG2 VAL A 137 7065 7961 7185 128 167 -378 C ATOM 1095 N VAL A 138 -16.993 -11.266 30.760 1.00 64.29 N ANISOU 1095 N VAL A 138 7811 8622 7994 126 162 -266 N ATOM 1096 CA VAL A 138 -15.844 -10.521 31.258 1.00 62.04 C ANISOU 1096 CA VAL A 138 7517 8344 7713 123 163 -231 C ATOM 1097 C VAL A 138 -14.858 -11.352 32.090 1.00 65.70 C ANISOU 1097 C VAL A 138 7976 8785 8203 137 168 -235 C ATOM 1098 O VAL A 138 -13.664 -11.079 32.086 1.00 68.99 O ANISOU 1098 O VAL A 138 8377 9220 8616 141 174 -217 O ATOM 1099 CB VAL A 138 -16.308 -9.300 32.060 1.00 60.42 C ANISOU 1099 CB VAL A 138 7322 8120 7516 103 149 -197 C ATOM 1100 CG1 VAL A 138 -15.171 -8.708 32.862 1.00 53.48 C ANISOU 1100 CG1 VAL A 138 6434 7237 6649 99 148 -168 C ATOM 1101 CG2 VAL A 138 -16.905 -8.264 31.124 1.00 59.49 C ANISOU 1101 CG2 VAL A 138 7198 8031 7373 91 146 -180 C ATOM 1102 N VAL A 139 -15.348 -12.372 32.785 1.00 67.89 N ANISOU 1102 N VAL A 139 8264 9023 8507 144 166 -254 N ATOM 1103 CA VAL A 139 -14.513 -13.152 33.697 1.00 67.87 C ANISOU 1103 CA VAL A 139 8256 8997 8534 156 170 -250 C ATOM 1104 C VAL A 139 -14.002 -14.436 33.062 1.00 72.12 C ANISOU 1104 C VAL A 139 8781 9536 9086 179 186 -284 C ATOM 1105 O VAL A 139 -12.882 -14.855 33.329 1.00 75.72 O ANISOU 1105 O VAL A 139 9222 9993 9556 192 194 -276 O ATOM 1106 CB VAL A 139 -15.261 -13.480 35.017 1.00 67.24 C ANISOU 1106 CB VAL A 139 8192 8875 8483 151 159 -242 C ATOM 1107 CG1 VAL A 139 -14.596 -14.631 35.773 1.00 61.41 C ANISOU 1107 CG1 VAL A 139 7444 8111 7779 168 165 -241 C ATOM 1108 CG2 VAL A 139 -15.335 -12.248 35.899 1.00 62.68 C ANISOU 1108 CG2 VAL A 139 7621 8297 7899 131 146 -208 C ATOM 1109 N CYS A 140 -14.826 -15.069 32.235 1.00 76.35 N ANISOU 1109 N CYS A 140 9320 10072 9618 183 190 -323 N ATOM 1110 CA CYS A 140 -14.473 -16.350 31.628 1.00 76.87 C ANISOU 1110 CA CYS A 140 9373 10134 9702 204 205 -365 C ATOM 1111 C CYS A 140 -13.837 -16.157 30.260 1.00 80.21 C ANISOU 1111 C CYS A 140 9776 10610 10088 211 219 -386 C ATOM 1112 O CYS A 140 -13.206 -17.069 29.723 1.00 81.46 O ANISOU 1112 O CYS A 140 9918 10775 10258 229 234 -419 O ATOM 1113 CB CYS A 140 -15.703 -17.242 31.522 1.00 73.69 C ANISOU 1113 CB CYS A 140 8981 9700 9320 204 203 -402 C ATOM 1114 SG CYS A 140 -16.382 -17.704 33.128 1.00 78.67 S ANISOU 1114 SG CYS A 140 9627 10268 9997 200 191 -378 S ATOM 1115 N LYS A 141 -14.004 -14.958 29.710 1.00 84.23 N ANISOU 1115 N LYS A 141 10286 11160 10555 195 213 -364 N ATOM 1116 CA LYS A 141 -13.419 -14.589 28.421 1.00 88.53 C ANISOU 1116 CA LYS A 141 10811 11767 11059 199 224 -372 C ATOM 1117 C LYS A 141 -13.647 -15.659 27.355 1.00 92.84 C ANISOU 1117 C LYS A 141 11345 12332 11598 213 237 -434 C ATOM 1118 O LYS A 141 -12.696 -16.223 26.819 1.00 95.74 O ANISOU 1118 O LYS A 141 11692 12721 11965 230 254 -457 O ATOM 1119 CB LYS A 141 -11.929 -14.269 28.583 1.00 86.53 C ANISOU 1119 CB LYS A 141 10540 11531 10805 207 232 -344 C ATOM 1120 CG LYS A 141 -11.670 -12.878 29.111 1.00 82.64 C ANISOU 1120 CG LYS A 141 10051 11046 10302 189 220 -288 C ATOM 1121 CD LYS A 141 -10.396 -12.806 29.918 1.00 80.94 C ANISOU 1121 CD LYS A 141 9825 10820 10106 194 223 -260 C ATOM 1122 CE LYS A 141 -10.155 -11.371 30.361 1.00 88.38 C ANISOU 1122 CE LYS A 141 10769 11772 11040 174 211 -210 C ATOM 1123 NZ LYS A 141 -8.709 -11.073 30.531 1.00 95.24 N ANISOU 1123 NZ LYS A 141 11618 12660 11910 178 218 -183 N ATOM 1124 N PRO A 142 -14.918 -15.943 27.039 1.00 96.76 N ANISOU 1124 N PRO A 142 11853 12822 12091 205 231 -463 N ATOM 1125 CA PRO A 142 -15.186 -17.050 26.129 1.00 99.49 C ANISOU 1125 CA PRO A 142 12186 13179 12435 217 243 -529 C ATOM 1126 C PRO A 142 -14.917 -16.690 24.660 1.00101.55 C ANISOU 1126 C PRO A 142 12424 13521 12639 218 252 -548 C ATOM 1127 O PRO A 142 -14.980 -17.563 23.799 1.00102.14 O ANISOU 1127 O PRO A 142 12483 13618 12707 228 265 -608 O ATOM 1128 CB PRO A 142 -16.675 -17.328 26.361 1.00 98.01 C ANISOU 1128 CB PRO A 142 12019 12959 12261 205 230 -546 C ATOM 1129 CG PRO A 142 -17.250 -16.003 26.728 1.00 96.19 C ANISOU 1129 CG PRO A 142 11804 12736 12008 185 213 -492 C ATOM 1130 CD PRO A 142 -16.142 -15.184 27.361 1.00 96.93 C ANISOU 1130 CD PRO A 142 11895 12831 12103 185 213 -439 C ATOM 1131 N MET A 143 -14.625 -15.419 24.389 1.00103.73 N ANISOU 1131 N MET A 143 12695 13842 12876 206 247 -498 N ATOM 1132 CA MET A 143 -14.339 -14.952 23.033 1.00107.26 C ANISOU 1132 CA MET A 143 13116 14372 13264 206 256 -503 C ATOM 1133 C MET A 143 -12.961 -14.300 22.959 1.00110.99 C ANISOU 1133 C MET A 143 13571 14878 13724 211 265 -462 C ATOM 1134 O MET A 143 -12.663 -13.361 23.706 1.00112.19 O ANISOU 1134 O MET A 143 13731 15009 13886 201 255 -404 O ATOM 1135 CB MET A 143 -15.394 -13.954 22.567 1.00105.72 C ANISOU 1135 CB MET A 143 12926 14212 13032 185 242 -475 C ATOM 1136 CG MET A 143 -16.815 -14.460 22.650 1.00108.45 C ANISOU 1136 CG MET A 143 13288 14528 13388 177 231 -508 C ATOM 1137 SD MET A 143 -17.987 -13.160 22.233 1.00114.68 S ANISOU 1137 SD MET A 143 14081 15354 14138 153 214 -462 S ATOM 1138 CE MET A 143 -17.752 -12.002 23.580 1.00115.89 C ANISOU 1138 CE MET A 143 14256 15452 14326 142 201 -387 C ATOM 1139 N SER A 144 -12.133 -14.799 22.044 1.00113.02 N ANISOU 1139 N SER A 144 13800 15185 13957 227 283 -495 N ATOM 1140 CA SER A 144 -10.762 -14.329 21.897 1.00113.52 C ANISOU 1140 CA SER A 144 13841 15281 14008 235 294 -462 C ATOM 1141 C SER A 144 -10.702 -12.869 21.430 1.00113.32 C ANISOU 1141 C SER A 144 13805 15310 13940 218 286 -399 C ATOM 1142 O SER A 144 -11.428 -12.470 20.511 1.00111.86 O ANISOU 1142 O SER A 144 13610 15179 13711 208 283 -400 O ATOM 1143 CB SER A 144 -10.005 -15.235 20.926 1.00114.49 C ANISOU 1143 CB SER A 144 13936 15453 14114 256 317 -518 C ATOM 1144 OG SER A 144 -8.617 -14.961 20.957 1.00119.44 O ANISOU 1144 OG SER A 144 14543 16100 14738 267 328 -489 O ATOM 1145 N ASN A 145 -9.840 -12.084 22.079 1.00112.74 N ANISOU 1145 N ASN A 145 13731 15222 13882 214 283 -343 N ATOM 1146 CA ASN A 145 -9.656 -10.664 21.753 1.00111.93 C ANISOU 1146 CA ASN A 145 13615 15161 13752 197 277 -277 C ATOM 1147 C ASN A 145 -10.952 -9.863 21.791 1.00108.71 C ANISOU 1147 C ASN A 145 13223 14745 13338 176 259 -251 C ATOM 1148 O ASN A 145 -11.350 -9.257 20.792 1.00109.01 O ANISOU 1148 O ASN A 145 13241 14843 13332 168 259 -233 O ATOM 1149 CB ASN A 145 -8.965 -10.495 20.391 1.00114.94 C ANISOU 1149 CB ASN A 145 13958 15635 14079 204 293 -276 C ATOM 1150 CG ASN A 145 -7.474 -10.231 20.519 1.00119.48 C ANISOU 1150 CG ASN A 145 14512 16224 14659 213 303 -246 C ATOM 1151 OD1 ASN A 145 -7.056 -9.157 20.962 1.00122.93 O ANISOU 1151 OD1 ASN A 145 14948 16652 15109 199 295 -184 O ATOM 1152 ND2 ASN A 145 -6.663 -11.207 20.117 1.00122.42 N ANISOU 1152 ND2 ASN A 145 14868 16620 15027 235 322 -291 N ATOM 1153 N PHE A 146 -11.607 -9.879 22.948 1.00105.05 N ANISOU 1153 N PHE A 146 12790 14207 12916 168 245 -248 N ATOM 1154 CA PHE A 146 -12.845 -9.134 23.163 1.00 99.71 C ANISOU 1154 CA PHE A 146 12131 13512 12242 149 229 -224 C ATOM 1155 C PHE A 146 -12.751 -8.318 24.446 1.00 96.43 C ANISOU 1155 C PHE A 146 11734 13037 11869 137 216 -180 C ATOM 1156 O PHE A 146 -12.332 -8.833 25.483 1.00 94.40 O ANISOU 1156 O PHE A 146 11492 12730 11647 143 215 -191 O ATOM 1157 CB PHE A 146 -14.042 -10.087 23.243 1.00 98.97 C ANISOU 1157 CB PHE A 146 12058 13390 12155 152 224 -276 C ATOM 1158 CG PHE A 146 -15.347 -9.395 23.524 1.00100.13 C ANISOU 1158 CG PHE A 146 12222 13515 12307 134 207 -253 C ATOM 1159 CD1 PHE A 146 -16.170 -8.989 22.484 1.00 98.79 C ANISOU 1159 CD1 PHE A 146 12040 13399 12098 125 204 -248 C ATOM 1160 CD2 PHE A 146 -15.748 -9.141 24.830 1.00100.86 C ANISOU 1160 CD2 PHE A 146 12342 13537 12443 125 195 -236 C ATOM 1161 CE1 PHE A 146 -17.373 -8.348 22.737 1.00 95.85 C ANISOU 1161 CE1 PHE A 146 11681 13004 11732 109 189 -225 C ATOM 1162 CE2 PHE A 146 -16.944 -8.495 25.090 1.00 98.06 C ANISOU 1162 CE2 PHE A 146 12002 13162 12094 110 180 -217 C ATOM 1163 CZ PHE A 146 -17.759 -8.098 24.039 1.00 97.72 C ANISOU 1163 CZ PHE A 146 11947 13168 12016 102 178 -210 C ATOM 1164 N ARG A 147 -13.138 -7.049 24.377 1.00 93.05 N ANISOU 1164 N ARG A 147 11301 12616 11437 119 206 -129 N ATOM 1165 CA ARG A 147 -13.223 -6.232 25.579 1.00 92.05 C ANISOU 1165 CA ARG A 147 11192 12433 11352 104 193 -95 C ATOM 1166 C ARG A 147 -14.605 -5.592 25.709 1.00 88.90 C ANISOU 1166 C ARG A 147 10807 12013 10959 89 180 -81 C ATOM 1167 O ARG A 147 -15.017 -4.808 24.857 1.00 89.29 O ANISOU 1167 O ARG A 147 10839 12100 10986 80 179 -50 O ATOM 1168 CB ARG A 147 -12.111 -5.173 25.626 1.00 92.48 C ANISOU 1168 CB ARG A 147 11225 12501 11413 97 195 -44 C ATOM 1169 CG ARG A 147 -11.704 -4.760 27.060 1.00102.93 C ANISOU 1169 CG ARG A 147 12562 13764 12781 88 187 -29 C ATOM 1170 CD ARG A 147 -11.092 -3.352 27.130 1.00111.95 C ANISOU 1170 CD ARG A 147 13685 14911 13939 71 183 27 C ATOM 1171 NE ARG A 147 -11.991 -2.334 26.577 1.00116.81 N ANISOU 1171 NE ARG A 147 14294 15537 14552 57 177 60 N ATOM 1172 CZ ARG A 147 -12.656 -1.427 27.291 1.00113.88 C ANISOU 1172 CZ ARG A 147 13932 15121 14214 40 165 80 C ATOM 1173 NH1 ARG A 147 -12.528 -1.377 28.611 1.00111.38 N ANISOU 1173 NH1 ARG A 147 13634 14751 13933 34 158 68 N ATOM 1174 NH2 ARG A 147 -13.448 -0.557 26.675 1.00113.27 N ANISOU 1174 NH2 ARG A 147 13844 15056 14136 29 162 113 N ATOM 1175 N PHE A 148 -15.319 -5.952 26.775 1.00 84.47 N ANISOU 1175 N PHE A 148 10275 11393 10428 86 170 -102 N ATOM 1176 CA PHE A 148 -16.631 -5.390 27.058 1.00 79.98 C ANISOU 1176 CA PHE A 148 9721 10798 9871 73 158 -91 C ATOM 1177 C PHE A 148 -16.532 -3.884 27.259 1.00 78.69 C ANISOU 1177 C PHE A 148 9547 10627 9725 56 152 -36 C ATOM 1178 O PHE A 148 -15.844 -3.418 28.164 1.00 78.81 O ANISOU 1178 O PHE A 148 9564 10611 9770 50 149 -21 O ATOM 1179 CB PHE A 148 -17.245 -6.050 28.303 1.00 78.45 C ANISOU 1179 CB PHE A 148 9557 10542 9708 73 150 -120 C ATOM 1180 CG PHE A 148 -18.650 -5.592 28.603 1.00 77.24 C ANISOU 1180 CG PHE A 148 9420 10362 9566 61 138 -114 C ATOM 1181 CD1 PHE A 148 -19.743 -6.187 27.971 1.00 72.18 C ANISOU 1181 CD1 PHE A 148 8785 9735 8905 63 136 -141 C ATOM 1182 CD2 PHE A 148 -18.881 -4.555 29.506 1.00 71.63 C ANISOU 1182 CD2 PHE A 148 8717 9615 8886 46 129 -85 C ATOM 1183 CE1 PHE A 148 -21.043 -5.761 28.235 1.00 66.89 C ANISOU 1183 CE1 PHE A 148 8128 9042 8245 52 126 -133 C ATOM 1184 CE2 PHE A 148 -20.177 -4.118 29.770 1.00 69.02 C ANISOU 1184 CE2 PHE A 148 8398 9260 8566 36 120 -81 C ATOM 1185 CZ PHE A 148 -21.262 -4.724 29.128 1.00 67.72 C ANISOU 1185 CZ PHE A 148 8240 9110 8381 40 118 -102 C ATOM 1186 N GLY A 149 -17.224 -3.127 26.416 1.00 77.50 N ANISOU 1186 N GLY A 149 9382 10506 9560 47 149 -7 N ATOM 1187 CA GLY A 149 -17.260 -1.677 26.557 1.00 76.62 C ANISOU 1187 CA GLY A 149 9257 10382 9474 31 144 47 C ATOM 1188 C GLY A 149 -18.644 -1.088 26.378 1.00 78.29 C ANISOU 1188 C GLY A 149 9472 10583 9691 21 135 63 C ATOM 1189 O GLY A 149 -19.634 -1.814 26.260 1.00 80.12 O ANISOU 1189 O GLY A 149 9720 10814 9907 25 132 31 O ATOM 1190 N GLU A 150 -18.699 0.240 26.328 1.00 79.64 N ANISOU 1190 N GLU A 150 9626 10747 9889 8 132 115 N ATOM 1191 CA GLU A 150 -19.950 0.999 26.287 1.00 80.38 C ANISOU 1191 CA GLU A 150 9719 10822 10000 -3 124 139 C ATOM 1192 C GLU A 150 -21.020 0.433 25.343 1.00 81.29 C ANISOU 1192 C GLU A 150 9834 10979 10074 3 123 127 C ATOM 1193 O GLU A 150 -22.132 0.139 25.776 1.00 82.11 O ANISOU 1193 O GLU A 150 9960 11053 10186 1 116 104 O ATOM 1194 CB GLU A 150 -19.662 2.457 25.940 1.00 78.91 C ANISOU 1194 CB GLU A 150 9502 10639 9842 -15 125 204 C ATOM 1195 CG GLU A 150 -20.312 3.436 26.880 1.00 84.03 C ANISOU 1195 CG GLU A 150 10158 11221 10548 -28 118 218 C ATOM 1196 CD GLU A 150 -20.703 4.731 26.195 1.00 93.71 C ANISOU 1196 CD GLU A 150 11351 12456 11798 -39 117 283 C ATOM 1197 OE1 GLU A 150 -20.152 5.027 25.114 1.00 96.46 O ANISOU 1197 OE1 GLU A 150 11667 12860 12124 -37 124 326 O ATOM 1198 OE2 GLU A 150 -21.567 5.454 26.738 1.00 96.20 O ANISOU 1198 OE2 GLU A 150 11671 12724 12158 -47 112 294 O ATOM 1199 N ASN A 151 -20.684 0.283 24.063 1.00 84.14 N ANISOU 1199 N ASN A 151 10168 11412 10389 8 130 143 N ATOM 1200 CA ASN A 151 -21.641 -0.199 23.053 1.00 84.64 C ANISOU 1200 CA ASN A 151 10224 11528 10408 11 128 133 C ATOM 1201 C ASN A 151 -22.356 -1.470 23.454 1.00 83.09 C ANISOU 1201 C ASN A 151 10059 11310 10201 18 125 66 C ATOM 1202 O ASN A 151 -23.550 -1.614 23.204 1.00 85.60 O ANISOU 1202 O ASN A 151 10383 11634 10509 15 118 58 O ATOM 1203 CB ASN A 151 -20.962 -0.438 21.703 1.00 85.58 C ANISOU 1203 CB ASN A 151 10309 11735 10472 18 138 143 C ATOM 1204 CG ASN A 151 -20.439 0.832 21.083 1.00 87.89 C ANISOU 1204 CG ASN A 151 10563 12061 10770 10 142 219 C ATOM 1205 OD1 ASN A 151 -21.109 1.873 21.082 1.00 73.70 O ANISOU 1205 OD1 ASN A 151 8754 10248 9001 -1 135 270 O ATOM 1206 ND2 ASN A 151 -19.226 0.758 20.548 1.00 99.53 N ANISOU 1206 ND2 ASN A 151 12015 13582 12221 16 152 229 N ATOM 1207 N HIS A 152 -21.623 -2.398 24.053 1.00 80.23 N ANISOU 1207 N HIS A 152 9716 10925 9843 28 130 20 N ATOM 1208 CA HIS A 152 -22.215 -3.653 24.485 1.00 81.39 C ANISOU 1208 CA HIS A 152 9891 11047 9988 35 127 -41 C ATOM 1209 C HIS A 152 -23.219 -3.406 25.606 1.00 81.10 C ANISOU 1209 C HIS A 152 9880 10942 9990 27 116 -42 C ATOM 1210 O HIS A 152 -24.353 -3.881 25.549 1.00 80.69 O ANISOU 1210 O HIS A 152 9841 10885 9932 26 110 -65 O ATOM 1211 CB HIS A 152 -21.129 -4.638 24.901 1.00 81.30 C ANISOU 1211 CB HIS A 152 9888 11024 9979 48 136 -80 C ATOM 1212 CG HIS A 152 -20.090 -4.848 23.845 1.00 90.21 C ANISOU 1212 CG HIS A 152 10988 12217 11069 57 148 -80 C ATOM 1213 ND1 HIS A 152 -19.067 -3.950 23.619 1.00 94.80 N ANISOU 1213 ND1 HIS A 152 11547 12821 11651 54 153 -33 N ATOM 1214 CD2 HIS A 152 -19.941 -5.827 22.922 1.00 88.49 C ANISOU 1214 CD2 HIS A 152 10759 12051 10812 68 157 -122 C ATOM 1215 CE1 HIS A 152 -18.323 -4.376 22.617 1.00 86.44 C ANISOU 1215 CE1 HIS A 152 10464 11826 10552 64 165 -44 C ATOM 1216 NE2 HIS A 152 -18.829 -5.515 22.179 1.00 87.30 N ANISOU 1216 NE2 HIS A 152 10580 11955 10636 73 168 -100 N ATOM 1217 N ALA A 153 -22.809 -2.620 26.599 1.00 80.11 N ANISOU 1217 N ALA A 153 9761 10770 9906 20 113 -18 N ATOM 1218 CA ALA A 153 -23.695 -2.228 27.685 1.00 75.90 C ANISOU 1218 CA ALA A 153 9250 10178 9412 12 104 -17 C ATOM 1219 C ALA A 153 -25.036 -1.705 27.161 1.00 74.60 C ANISOU 1219 C ALA A 153 9080 10023 9243 4 97 4 C ATOM 1220 O ALA A 153 -26.095 -2.058 27.694 1.00 73.50 O ANISOU 1220 O ALA A 153 8961 9853 9114 3 90 -18 O ATOM 1221 CB ALA A 153 -23.022 -1.193 28.559 1.00 75.50 C ANISOU 1221 CB ALA A 153 9196 10090 9401 3 103 12 C ATOM 1222 N ILE A 154 -24.980 -0.873 26.121 1.00 71.79 N ANISOU 1222 N ILE A 154 8694 9712 8871 0 100 49 N ATOM 1223 CA ILE A 154 -26.182 -0.314 25.501 1.00 71.45 C ANISOU 1223 CA ILE A 154 8638 9686 8822 -6 94 78 C ATOM 1224 C ILE A 154 -27.031 -1.439 24.899 1.00 71.68 C ANISOU 1224 C ILE A 154 8675 9749 8810 -1 91 37 C ATOM 1225 O ILE A 154 -28.243 -1.508 25.124 1.00 68.00 O ANISOU 1225 O ILE A 154 8221 9263 8351 -5 83 29 O ATOM 1226 CB ILE A 154 -25.838 0.745 24.406 1.00 73.13 C ANISOU 1226 CB ILE A 154 8811 9951 9024 -11 98 142 C ATOM 1227 CG1 ILE A 154 -24.773 1.746 24.895 1.00 74.31 C ANISOU 1227 CG1 ILE A 154 8948 10071 9214 -16 102 179 C ATOM 1228 CG2 ILE A 154 -27.099 1.456 23.910 1.00 64.37 C ANISOU 1228 CG2 ILE A 154 7687 8853 7918 -18 91 181 C ATOM 1229 CD1 ILE A 154 -25.286 2.851 25.799 1.00 74.50 C ANISOU 1229 CD1 ILE A 154 8976 10030 9299 -27 97 205 C ATOM 1230 N MET A 155 -26.384 -2.326 24.150 1.00 72.16 N ANISOU 1230 N MET A 155 8729 9860 8830 8 98 8 N ATOM 1231 CA MET A 155 -27.059 -3.491 23.597 1.00 75.62 C ANISOU 1231 CA MET A 155 9172 10327 9231 12 96 -42 C ATOM 1232 C MET A 155 -27.757 -4.275 24.690 1.00 73.80 C ANISOU 1232 C MET A 155 8977 10033 9030 13 90 -86 C ATOM 1233 O MET A 155 -28.947 -4.550 24.586 1.00 77.31 O ANISOU 1233 O MET A 155 9428 10475 9469 9 82 -99 O ATOM 1234 CB MET A 155 -26.077 -4.396 22.854 1.00 78.94 C ANISOU 1234 CB MET A 155 9580 10798 9613 23 107 -77 C ATOM 1235 CG MET A 155 -26.264 -4.415 21.350 1.00 90.50 C ANISOU 1235 CG MET A 155 11012 12353 11021 23 109 -71 C ATOM 1236 SD MET A 155 -24.751 -3.943 20.492 1.00112.71 S ANISOU 1236 SD MET A 155 13790 15232 13804 28 122 -37 S ATOM 1237 CE MET A 155 -25.081 -2.199 20.170 1.00109.81 C ANISOU 1237 CE MET A 155 13394 14880 13449 15 117 58 C ATOM 1238 N GLY A 156 -27.014 -4.627 25.738 1.00 72.92 N ANISOU 1238 N GLY A 156 8885 9872 8949 19 93 -105 N ATOM 1239 CA GLY A 156 -27.579 -5.293 26.915 1.00 69.60 C ANISOU 1239 CA GLY A 156 8495 9390 8559 19 88 -137 C ATOM 1240 C GLY A 156 -28.839 -4.613 27.448 1.00 68.80 C ANISOU 1240 C GLY A 156 8403 9255 8481 9 78 -116 C ATOM 1241 O GLY A 156 -29.851 -5.273 27.706 1.00 68.30 O ANISOU 1241 O GLY A 156 8355 9174 8421 8 72 -144 O ATOM 1242 N VAL A 157 -28.790 -3.292 27.604 1.00 63.11 N ANISOU 1242 N VAL A 157 7672 8526 7781 1 76 -68 N ATOM 1243 CA VAL A 157 -29.932 -2.570 28.137 1.00 59.74 C ANISOU 1243 CA VAL A 157 7252 8065 7381 -7 69 -48 C ATOM 1244 C VAL A 157 -31.109 -2.682 27.180 1.00 63.67 C ANISOU 1244 C VAL A 157 7740 8600 7852 -10 63 -44 C ATOM 1245 O VAL A 157 -32.218 -3.040 27.590 1.00 65.69 O ANISOU 1245 O VAL A 157 8011 8832 8117 -13 56 -61 O ATOM 1246 CB VAL A 157 -29.598 -1.091 28.444 1.00 58.06 C ANISOU 1246 CB VAL A 157 7026 7833 7203 -15 70 1 C ATOM 1247 CG1 VAL A 157 -30.855 -0.295 28.707 1.00 43.10 C ANISOU 1247 CG1 VAL A 157 5131 5912 5334 -23 63 24 C ATOM 1248 CG2 VAL A 157 -28.677 -1.004 29.646 1.00 58.74 C ANISOU 1248 CG2 VAL A 157 7125 7874 7319 -15 72 -11 C ATOM 1249 N ALA A 158 -30.855 -2.395 25.904 1.00 64.66 N ANISOU 1249 N ALA A 158 7837 8788 7942 -10 66 -19 N ATOM 1250 CA ALA A 158 -31.890 -2.445 24.873 1.00 62.86 C ANISOU 1250 CA ALA A 158 7593 8609 7682 -14 61 -11 C ATOM 1251 C ALA A 158 -32.510 -3.834 24.777 1.00 61.14 C ANISOU 1251 C ALA A 158 7391 8397 7441 -11 57 -71 C ATOM 1252 O ALA A 158 -33.729 -3.966 24.665 1.00 64.06 O ANISOU 1252 O ALA A 158 7763 8768 7807 -16 49 -75 O ATOM 1253 CB ALA A 158 -31.324 -2.017 23.517 1.00 62.82 C ANISOU 1253 CB ALA A 158 7551 8682 7637 -14 66 24 C ATOM 1254 N PHE A 159 -31.674 -4.865 24.830 1.00 55.91 N ANISOU 1254 N PHE A 159 6738 7737 6768 -3 63 -117 N ATOM 1255 CA PHE A 159 -32.151 -6.238 24.763 1.00 58.07 C ANISOU 1255 CA PHE A 159 7024 8010 7029 0 61 -177 C ATOM 1256 C PHE A 159 -33.171 -6.495 25.868 1.00 61.06 C ANISOU 1256 C PHE A 159 7429 8325 7444 -3 53 -190 C ATOM 1257 O PHE A 159 -34.159 -7.209 25.700 1.00 62.67 O ANISOU 1257 O PHE A 159 7639 8531 7641 -7 47 -219 O ATOM 1258 CB PHE A 159 -30.978 -7.192 24.925 1.00 53.17 C ANISOU 1258 CB PHE A 159 6410 7383 6408 12 71 -218 C ATOM 1259 CG PHE A 159 -31.377 -8.625 24.986 1.00 54.97 C ANISOU 1259 CG PHE A 159 6651 7598 6638 16 71 -281 C ATOM 1260 CD1 PHE A 159 -31.793 -9.291 23.838 1.00 54.19 C ANISOU 1260 CD1 PHE A 159 6535 7555 6500 14 70 -317 C ATOM 1261 CD2 PHE A 159 -31.338 -9.319 26.191 1.00 53.53 C ANISOU 1261 CD2 PHE A 159 6494 7349 6496 20 70 -304 C ATOM 1262 CE1 PHE A 159 -32.167 -10.642 23.892 1.00 59.11 C ANISOU 1262 CE1 PHE A 159 7168 8160 7131 17 70 -379 C ATOM 1263 CE2 PHE A 159 -31.696 -10.670 26.252 1.00 56.12 C ANISOU 1263 CE2 PHE A 159 6831 7660 6834 24 70 -359 C ATOM 1264 CZ PHE A 159 -32.108 -11.331 25.097 1.00 56.55 C ANISOU 1264 CZ PHE A 159 6869 7763 6855 22 71 -398 C ATOM 1265 N THR A 160 -32.897 -5.894 27.013 1.00 64.47 N ANISOU 1265 N THR A 160 7876 8703 7915 -3 54 -167 N ATOM 1266 CA THR A 160 -33.746 -5.970 28.173 1.00 62.79 C ANISOU 1266 CA THR A 160 7686 8433 7737 -7 47 -173 C ATOM 1267 C THR A 160 -35.121 -5.366 27.875 1.00 64.35 C ANISOU 1267 C THR A 160 7878 8639 7934 -16 39 -149 C ATOM 1268 O THR A 160 -36.146 -5.978 28.175 1.00 67.50 O ANISOU 1268 O THR A 160 8289 9019 8338 -18 32 -172 O ATOM 1269 CB THR A 160 -33.026 -5.298 29.357 1.00 62.04 C ANISOU 1269 CB THR A 160 7601 8291 7678 -6 50 -153 C ATOM 1270 OG1 THR A 160 -32.492 -6.311 30.228 1.00 63.70 O ANISOU 1270 OG1 THR A 160 7830 8470 7904 1 53 -188 O ATOM 1271 CG2 THR A 160 -33.934 -4.346 30.111 1.00 59.52 C ANISOU 1271 CG2 THR A 160 7289 7938 7390 -14 45 -126 C ATOM 1272 N TRP A 161 -35.139 -4.193 27.246 1.00 63.41 N ANISOU 1272 N TRP A 161 7737 8548 7808 -20 39 -101 N ATOM 1273 CA ATRP A 161 -36.409 -3.563 26.933 0.50 62.84 C ANISOU 1273 CA ATRP A 161 7655 8485 7736 -27 31 -73 C ATOM 1274 CA BTRP A 161 -36.362 -3.493 26.851 0.50 61.88 C ANISOU 1274 CA BTRP A 161 7531 8367 7613 -27 32 -69 C ATOM 1275 C TRP A 161 -37.166 -4.308 25.830 1.00 63.77 C ANISOU 1275 C TRP A 161 7761 8658 7812 -30 26 -94 C ATOM 1276 O TRP A 161 -38.399 -4.299 25.809 1.00 66.55 O ANISOU 1276 O TRP A 161 8113 9007 8165 -36 18 -90 O ATOM 1277 CB ATRP A 161 -36.227 -2.084 26.600 0.50 62.83 C ANISOU 1277 CB ATRP A 161 7630 8495 7748 -31 34 -10 C ATOM 1278 CB BTRP A 161 -35.998 -2.134 26.233 0.50 61.17 C ANISOU 1278 CB BTRP A 161 7413 8304 7525 -30 35 -9 C ATOM 1279 CG ATRP A 161 -36.124 -1.195 27.821 0.50 63.82 C ANISOU 1279 CG ATRP A 161 7766 8556 7926 -32 36 9 C ATOM 1280 CG BTRP A 161 -35.313 -1.153 27.171 0.50 58.21 C ANISOU 1280 CG BTRP A 161 7042 7879 7196 -30 40 18 C ATOM 1281 CD1ATRP A 161 -35.161 -1.239 28.791 0.50 61.45 C ANISOU 1281 CD1ATRP A 161 7482 8216 7650 -29 41 -8 C ATOM 1282 CD1BTRP A 161 -34.889 -1.396 28.448 0.50 57.43 C ANISOU 1282 CD1BTRP A 161 6968 7724 7128 -28 42 -9 C ATOM 1283 CD2ATRP A 161 -37.012 -0.123 28.189 0.50 65.41 C ANISOU 1283 CD2ATRP A 161 7961 8727 8164 -37 33 45 C ATOM 1284 CD2BTRP A 161 -34.952 0.212 26.884 0.50 49.68 C ANISOU 1284 CD2BTRP A 161 5936 6802 6136 -34 44 75 C ATOM 1285 NE1ATRP A 161 -35.394 -0.268 29.737 0.50 56.58 N ANISOU 1285 NE1ATRP A 161 6869 7551 7079 -33 41 12 N ATOM 1286 NE1BTRP A 161 -34.312 -0.267 28.980 0.50 55.89 N ANISOU 1286 NE1BTRP A 161 6766 7500 6969 -31 46 22 N ATOM 1287 CE2ATRP A 161 -36.521 0.432 29.392 0.50 61.31 C ANISOU 1287 CE2ATRP A 161 7454 8152 7689 -37 37 43 C ATOM 1288 CE2BTRP A 161 -34.332 0.733 28.041 0.50 51.96 C ANISOU 1288 CE2BTRP A 161 6237 7034 6470 -34 48 74 C ATOM 1289 CE3ATRP A 161 -38.173 0.419 27.620 0.50 62.56 C ANISOU 1289 CE3ATRP A 161 7583 8384 7803 -41 28 78 C ATOM 1290 CE3BTRP A 161 -35.107 1.045 25.771 0.50 41.75 C ANISOU 1290 CE3BTRP A 161 4898 5846 5120 -37 44 130 C ATOM 1291 CZ2ATRP A 161 -37.149 1.503 30.033 0.50 58.08 C ANISOU 1291 CZ2ATRP A 161 7040 7701 7325 -41 38 68 C ATOM 1292 CZ2BTRP A 161 -33.856 2.050 28.113 0.50 45.02 C ANISOU 1292 CZ2BTRP A 161 5339 6139 5629 -38 52 120 C ATOM 1293 CZ3ATRP A 161 -38.792 1.479 28.260 0.50 60.83 C ANISOU 1293 CZ3ATRP A 161 7360 8120 7632 -44 28 108 C ATOM 1294 CZ3BTRP A 161 -34.639 2.355 25.847 0.50 44.24 C ANISOU 1294 CZ3BTRP A 161 5192 6143 5474 -40 49 182 C ATOM 1295 CH2ATRP A 161 -38.279 2.009 29.455 0.50 56.81 C ANISOU 1295 CH2ATRP A 161 6864 7554 7169 -44 34 100 C ATOM 1296 CH2BTRP A 161 -34.022 2.842 27.010 0.50 40.22 C ANISOU 1296 CH2BTRP A 161 4698 5572 5014 -41 53 175 C ATOM 1297 N VAL A 162 -36.455 -4.990 24.941 1.00 64.11 N ANISOU 1297 N VAL A 162 7792 8751 7816 -26 30 -119 N ATOM 1298 CA VAL A 162 -37.125 -5.753 23.890 1.00 62.43 C ANISOU 1298 CA VAL A 162 7566 8594 7561 -30 25 -149 C ATOM 1299 C VAL A 162 -37.751 -7.009 24.491 1.00 63.86 C ANISOU 1299 C VAL A 162 7772 8737 7757 -30 21 -207 C ATOM 1300 O VAL A 162 -38.926 -7.272 24.280 1.00 65.59 O ANISOU 1300 O VAL A 162 7989 8963 7968 -38 12 -216 O ATOM 1301 CB VAL A 162 -36.181 -6.053 22.662 1.00 63.52 C ANISOU 1301 CB VAL A 162 7678 8806 7649 -27 32 -161 C ATOM 1302 CG1 VAL A 162 -36.661 -7.252 21.847 1.00 56.93 C ANISOU 1302 CG1 VAL A 162 6836 8017 6776 -29 29 -221 C ATOM 1303 CG2 VAL A 162 -36.067 -4.828 21.765 1.00 54.36 C ANISOU 1303 CG2 VAL A 162 6485 7705 6465 -30 33 -96 C ATOM 1304 N MET A 163 -36.986 -7.761 25.276 1.00 64.27 N ANISOU 1304 N MET A 163 7844 8744 7832 -23 27 -241 N ATOM 1305 CA MET A 163 -37.522 -8.958 25.919 1.00 66.83 C ANISOU 1305 CA MET A 163 8189 9026 8179 -22 24 -290 C ATOM 1306 C MET A 163 -38.747 -8.673 26.788 1.00 69.28 C ANISOU 1306 C MET A 163 8513 9291 8518 -29 15 -273 C ATOM 1307 O MET A 163 -39.658 -9.504 26.890 1.00 70.48 O ANISOU 1307 O MET A 163 8673 9431 8677 -33 8 -304 O ATOM 1308 CB MET A 163 -36.452 -9.644 26.755 1.00 66.34 C ANISOU 1308 CB MET A 163 8143 8919 8143 -12 32 -315 C ATOM 1309 CG MET A 163 -35.476 -10.468 25.945 1.00 75.35 C ANISOU 1309 CG MET A 163 9272 10096 9261 -5 41 -355 C ATOM 1310 SD MET A 163 -36.307 -11.539 24.761 1.00 73.98 S ANISOU 1310 SD MET A 163 9083 9971 9055 -11 37 -412 S ATOM 1311 CE MET A 163 -36.588 -10.367 23.438 1.00 66.26 C ANISOU 1311 CE MET A 163 8075 9080 8022 -19 33 -369 C ATOM 1312 N ALA A 164 -38.758 -7.496 27.411 1.00 68.65 N ANISOU 1312 N ALA A 164 8437 9188 8460 -29 15 -225 N ATOM 1313 CA ALA A 164 -39.847 -7.097 28.289 1.00 67.50 C ANISOU 1313 CA ALA A 164 8304 9000 8343 -34 8 -207 C ATOM 1314 C ALA A 164 -41.103 -6.798 27.480 1.00 67.68 C ANISOU 1314 C ALA A 164 8311 9059 8346 -43 -1 -191 C ATOM 1315 O ALA A 164 -42.151 -7.384 27.729 1.00 71.12 O ANISOU 1315 O ALA A 164 8755 9480 8789 -48 -8 -211 O ATOM 1316 CB ALA A 164 -39.444 -5.901 29.118 1.00 67.63 C ANISOU 1316 CB ALA A 164 8323 8984 8388 -33 12 -166 C ATOM 1317 N LEU A 165 -40.987 -5.886 26.515 1.00 65.66 N ANISOU 1317 N LEU A 165 8030 8852 8065 -45 0 -153 N ATOM 1318 CA LEU A 165 -42.040 -5.640 25.526 1.00 62.92 C ANISOU 1318 CA LEU A 165 7660 8556 7690 -53 -8 -135 C ATOM 1319 C LEU A 165 -42.609 -6.934 24.902 1.00 62.93 C ANISOU 1319 C LEU A 165 7661 8589 7662 -58 -15 -189 C ATOM 1320 O LEU A 165 -43.817 -7.042 24.694 1.00 63.46 O ANISOU 1320 O LEU A 165 7722 8666 7724 -66 -24 -189 O ATOM 1321 CB LEU A 165 -41.523 -4.702 24.433 1.00 60.92 C ANISOU 1321 CB LEU A 165 7376 8364 7407 -54 -5 -89 C ATOM 1322 CG LEU A 165 -41.954 -3.233 24.355 1.00 64.43 C ANISOU 1322 CG LEU A 165 7801 8810 7870 -56 -6 -19 C ATOM 1323 CD1 LEU A 165 -42.635 -2.717 25.622 1.00 64.89 C ANISOU 1323 CD1 LEU A 165 7879 8794 7982 -55 -7 -6 C ATOM 1324 CD2 LEU A 165 -40.768 -2.341 23.958 1.00 64.54 C ANISOU 1324 CD2 LEU A 165 7796 8844 7882 -52 2 22 C ATOM 1325 N ALA A 166 -41.750 -7.917 24.624 1.00 60.85 N ANISOU 1325 N ALA A 166 7400 8336 7383 -54 -9 -237 N ATOM 1326 CA ALA A 166 -42.209 -9.200 24.084 1.00 60.75 C ANISOU 1326 CA ALA A 166 7385 8346 7351 -59 -14 -297 C ATOM 1327 C ALA A 166 -43.128 -9.933 25.057 1.00 62.88 C ANISOU 1327 C ALA A 166 7678 8555 7659 -63 -20 -322 C ATOM 1328 O ALA A 166 -43.833 -10.867 24.669 1.00 61.79 O ANISOU 1328 O ALA A 166 7536 8429 7512 -70 -27 -365 O ATOM 1329 CB ALA A 166 -41.031 -10.088 23.697 1.00 58.47 C ANISOU 1329 CB ALA A 166 7094 8073 7048 -52 -5 -345 C ATOM 1330 N CYS A 167 -43.097 -9.521 26.326 1.00 64.57 N ANISOU 1330 N CYS A 167 7913 8705 7915 -58 -18 -297 N ATOM 1331 CA CYS A 167 -44.001 -10.066 27.330 1.00 65.58 C ANISOU 1331 CA CYS A 167 8060 8778 8079 -61 -23 -310 C ATOM 1332 C CYS A 167 -45.214 -9.166 27.593 1.00 63.79 C ANISOU 1332 C CYS A 167 7830 8545 7860 -67 -31 -268 C ATOM 1333 O CYS A 167 -46.348 -9.640 27.595 1.00 64.90 O ANISOU 1333 O CYS A 167 7971 8682 8004 -75 -39 -281 O ATOM 1334 CB CYS A 167 -43.261 -10.366 28.633 1.00 66.30 C ANISOU 1334 CB CYS A 167 8174 8807 8210 -52 -16 -316 C ATOM 1335 SG CYS A 167 -44.363 -10.588 30.074 1.00 77.93 S ANISOU 1335 SG CYS A 167 9667 10216 9726 -54 -21 -309 S ATOM 1336 N ALA A 168 -44.978 -7.874 27.799 1.00 62.79 N ANISOU 1336 N ALA A 168 7699 8416 7740 -64 -27 -218 N ATOM 1337 CA ALA A 168 -46.029 -6.971 28.273 1.00 64.87 C ANISOU 1337 CA ALA A 168 7962 8661 8024 -67 -31 -178 C ATOM 1338 C ALA A 168 -46.927 -6.384 27.169 1.00 68.02 C ANISOU 1338 C ALA A 168 8335 9115 8396 -74 -39 -148 C ATOM 1339 O ALA A 168 -48.032 -5.899 27.449 1.00 67.40 O ANISOU 1339 O ALA A 168 8253 9024 8332 -78 -44 -123 O ATOM 1340 CB ALA A 168 -45.429 -5.864 29.113 1.00 63.22 C ANISOU 1340 CB ALA A 168 7760 8416 7845 -60 -23 -143 C ATOM 1341 N ALA A 169 -46.456 -6.428 25.924 1.00 68.71 N ANISOU 1341 N ALA A 169 8401 9266 8441 -76 -39 -150 N ATOM 1342 CA ALA A 169 -47.209 -5.859 24.805 1.00 67.77 C ANISOU 1342 CA ALA A 169 8251 9210 8289 -84 -47 -116 C ATOM 1343 C ALA A 169 -48.312 -6.781 24.250 1.00 68.24 C ANISOU 1343 C ALA A 169 8302 9301 8324 -95 -59 -151 C ATOM 1344 O ALA A 169 -49.459 -6.347 24.106 1.00 68.36 O ANISOU 1344 O ALA A 169 8306 9328 8340 -101 -67 -122 O ATOM 1345 CB ALA A 169 -46.274 -5.378 23.704 1.00 62.74 C ANISOU 1345 CB ALA A 169 7587 8636 7614 -82 -42 -94 C ATOM 1346 N PRO A 170 -47.980 -8.053 23.952 1.00 69.20 N ANISOU 1346 N PRO A 170 8430 9435 8429 -97 -59 -214 N ATOM 1347 CA PRO A 170 -48.983 -8.980 23.415 1.00 70.70 C ANISOU 1347 CA PRO A 170 8611 9653 8599 -110 -71 -254 C ATOM 1348 C PRO A 170 -50.378 -8.907 24.065 1.00 72.61 C ANISOU 1348 C PRO A 170 8861 9860 8869 -116 -79 -239 C ATOM 1349 O PRO A 170 -51.372 -8.867 23.338 1.00 73.17 O ANISOU 1349 O PRO A 170 8910 9978 8914 -126 -90 -232 O ATOM 1350 CB PRO A 170 -48.349 -10.353 23.650 1.00 69.84 C ANISOU 1350 CB PRO A 170 8519 9517 8499 -108 -66 -325 C ATOM 1351 CG PRO A 170 -46.892 -10.094 23.537 1.00 69.66 C ANISOU 1351 CG PRO A 170 8498 9502 8469 -97 -54 -321 C ATOM 1352 CD PRO A 170 -46.650 -8.687 24.037 1.00 69.50 C ANISOU 1352 CD PRO A 170 8479 9462 8465 -90 -49 -252 C ATOM 1353 N PRO A 171 -50.464 -8.890 25.418 1.00 72.69 N ANISOU 1353 N PRO A 171 8897 9793 8927 -109 -75 -234 N ATOM 1354 CA PRO A 171 -51.799 -8.934 26.024 1.00 70.75 C ANISOU 1354 CA PRO A 171 8657 9517 8706 -115 -83 -224 C ATOM 1355 C PRO A 171 -52.621 -7.690 25.732 1.00 70.40 C ANISOU 1355 C PRO A 171 8594 9498 8657 -117 -87 -163 C ATOM 1356 O PRO A 171 -53.847 -7.752 25.757 1.00 75.49 O ANISOU 1356 O PRO A 171 9231 10144 9305 -124 -96 -156 O ATOM 1357 CB PRO A 171 -51.510 -9.039 27.523 1.00 67.38 C ANISOU 1357 CB PRO A 171 8260 9012 8328 -106 -75 -226 C ATOM 1358 CG PRO A 171 -50.108 -9.547 27.602 1.00 71.84 C ANISOU 1358 CG PRO A 171 8837 9567 8893 -99 -66 -256 C ATOM 1359 CD PRO A 171 -49.413 -8.897 26.450 1.00 71.95 C ANISOU 1359 CD PRO A 171 8829 9642 8867 -98 -64 -238 C ATOM 1360 N LEU A 172 -51.957 -6.578 25.441 1.00 67.18 N ANISOU 1360 N LEU A 172 8175 9108 8244 -109 -80 -118 N ATOM 1361 CA LEU A 172 -52.661 -5.356 25.099 1.00 66.43 C ANISOU 1361 CA LEU A 172 8056 9035 8150 -110 -83 -55 C ATOM 1362 C LEU A 172 -53.453 -5.549 23.818 1.00 68.73 C ANISOU 1362 C LEU A 172 8316 9405 8395 -121 -95 -50 C ATOM 1363 O LEU A 172 -54.425 -4.836 23.572 1.00 70.66 O ANISOU 1363 O LEU A 172 8540 9668 8641 -124 -101 -4 O ATOM 1364 CB LEU A 172 -51.689 -4.180 24.930 1.00 64.40 C ANISOU 1364 CB LEU A 172 7787 8783 7898 -100 -73 -7 C ATOM 1365 CG LEU A 172 -51.152 -3.482 26.187 1.00 63.33 C ANISOU 1365 CG LEU A 172 7673 8574 7815 -90 -61 9 C ATOM 1366 CD1 LEU A 172 -50.623 -2.098 25.822 1.00 62.70 C ANISOU 1366 CD1 LEU A 172 7571 8506 7745 -84 -54 69 C ATOM 1367 CD2 LEU A 172 -52.193 -3.384 27.330 1.00 51.34 C ANISOU 1367 CD2 LEU A 172 6170 6998 6338 -89 -62 10 C ATOM 1368 N VAL A 173 -53.036 -6.518 23.003 1.00 69.14 N ANISOU 1368 N VAL A 173 8361 9504 8405 -128 -99 -99 N ATOM 1369 CA VAL A 173 -53.531 -6.612 21.630 1.00 65.21 C ANISOU 1369 CA VAL A 173 7827 9097 7852 -140 -110 -96 C ATOM 1370 C VAL A 173 -53.899 -8.027 21.149 1.00 67.90 C ANISOU 1370 C VAL A 173 8167 9467 8165 -153 -119 -170 C ATOM 1371 O VAL A 173 -53.715 -8.347 19.981 1.00 72.30 O ANISOU 1371 O VAL A 173 8698 10104 8669 -161 -123 -191 O ATOM 1372 CB VAL A 173 -52.548 -5.935 20.613 1.00 64.44 C ANISOU 1372 CB VAL A 173 7702 9067 7714 -136 -104 -64 C ATOM 1373 CG1 VAL A 173 -52.433 -4.419 20.871 1.00 56.17 C ANISOU 1373 CG1 VAL A 173 6645 8002 6696 -126 -97 19 C ATOM 1374 CG2 VAL A 173 -51.180 -6.620 20.615 1.00 52.75 C ANISOU 1374 CG2 VAL A 173 6238 7581 6225 -130 -94 -114 C ATOM 1375 N GLY A 174 -54.421 -8.876 22.025 1.00 66.90 N ANISOU 1375 N GLY A 174 8066 9279 8074 -156 -121 -211 N ATOM 1376 CA GLY A 174 -54.974 -10.138 21.555 1.00 65.49 C ANISOU 1376 CA GLY A 174 7882 9125 7877 -171 -132 -276 C ATOM 1377 C GLY A 174 -54.370 -11.425 22.080 1.00 67.87 C ANISOU 1377 C GLY A 174 8207 9375 8204 -170 -126 -348 C ATOM 1378 O GLY A 174 -55.065 -12.440 22.183 1.00 69.68 O ANISOU 1378 O GLY A 174 8440 9589 8446 -182 -134 -395 O ATOM 1379 N TRP A 175 -53.080 -11.416 22.391 1.00 67.70 N ANISOU 1379 N TRP A 175 8202 9328 8193 -157 -113 -355 N ATOM 1380 CA TRP A 175 -52.448 -12.626 22.924 1.00 68.32 C ANISOU 1380 CA TRP A 175 8301 9355 8301 -155 -107 -418 C ATOM 1381 C TRP A 175 -52.350 -12.529 24.456 1.00 69.00 C ANISOU 1381 C TRP A 175 8421 9350 8446 -144 -100 -396 C ATOM 1382 O TRP A 175 -51.643 -11.673 24.986 1.00 71.10 O ANISOU 1382 O TRP A 175 8698 9594 8723 -131 -91 -356 O ATOM 1383 CB TRP A 175 -51.096 -12.891 22.236 1.00 67.31 C ANISOU 1383 CB TRP A 175 8167 9262 8145 -148 -97 -449 C ATOM 1384 CG TRP A 175 -50.552 -14.284 22.423 1.00 61.20 C ANISOU 1384 CG TRP A 175 7404 8452 7395 -148 -92 -524 C ATOM 1385 CD1 TRP A 175 -51.254 -15.414 22.781 1.00 64.43 C ANISOU 1385 CD1 TRP A 175 7821 8823 7839 -157 -98 -572 C ATOM 1386 CD2 TRP A 175 -49.197 -14.700 22.239 1.00 55.96 C ANISOU 1386 CD2 TRP A 175 6744 7790 6729 -137 -80 -557 C ATOM 1387 NE1 TRP A 175 -50.409 -16.500 22.851 1.00 54.96 N ANISOU 1387 NE1 TRP A 175 6627 7594 6661 -152 -90 -631 N ATOM 1388 CE2 TRP A 175 -49.141 -16.091 22.526 1.00 57.31 C ANISOU 1388 CE2 TRP A 175 6922 7916 6935 -140 -78 -624 C ATOM 1389 CE3 TRP A 175 -48.016 -14.031 21.880 1.00 58.30 C ANISOU 1389 CE3 TRP A 175 7036 8118 6999 -126 -69 -534 C ATOM 1390 CZ2 TRP A 175 -47.950 -16.823 22.456 1.00 54.72 C ANISOU 1390 CZ2 TRP A 175 6599 7575 6619 -130 -66 -670 C ATOM 1391 CZ3 TRP A 175 -46.829 -14.761 21.808 1.00 54.67 C ANISOU 1391 CZ3 TRP A 175 6579 7647 6545 -117 -58 -580 C ATOM 1392 CH2 TRP A 175 -46.809 -16.144 22.091 1.00 57.94 C ANISOU 1392 CH2 TRP A 175 7002 8017 6996 -118 -56 -648 C ATOM 1393 N SER A 176 -53.085 -13.407 25.144 1.00 69.12 N ANISOU 1393 N SER A 176 8448 9316 8497 -150 -105 -423 N ATOM 1394 CA SER A 176 -53.506 -13.212 26.544 1.00 66.80 C ANISOU 1394 CA SER A 176 8178 8952 8252 -144 -103 -393 C ATOM 1395 C SER A 176 -54.122 -11.823 26.800 1.00 67.01 C ANISOU 1395 C SER A 176 8200 8985 8275 -141 -104 -326 C ATOM 1396 O SER A 176 -54.390 -11.060 25.853 1.00 67.27 O ANISOU 1396 O SER A 176 8211 9078 8272 -144 -109 -299 O ATOM 1397 CB SER A 176 -52.372 -13.523 27.538 1.00 67.43 C ANISOU 1397 CB SER A 176 8281 8973 8366 -130 -90 -402 C ATOM 1398 OG SER A 176 -52.850 -13.539 28.881 1.00 59.22 O ANISOU 1398 OG SER A 176 7259 7872 7369 -127 -89 -381 O ATOM 1399 N ARG A 177 -54.346 -11.501 28.076 1.00 64.38 N ANISOU 1399 N ARG A 177 7887 8593 7982 -133 -100 -300 N ATOM 1400 CA ARG A 177 -54.979 -10.235 28.462 1.00 62.46 C ANISOU 1400 CA ARG A 177 7639 8345 7746 -129 -99 -242 C ATOM 1401 C ARG A 177 -54.591 -9.815 29.877 1.00 61.46 C ANISOU 1401 C ARG A 177 7536 8158 7659 -117 -88 -223 C ATOM 1402 O ARG A 177 -54.003 -10.597 30.624 1.00 60.61 O ANISOU 1402 O ARG A 177 7446 8011 7573 -113 -83 -250 O ATOM 1403 CB ARG A 177 -56.492 -10.373 28.386 1.00 58.12 C ANISOU 1403 CB ARG A 177 7079 7804 7198 -140 -111 -235 C ATOM 1404 CG ARG A 177 -56.975 -11.530 29.194 1.00 60.90 C ANISOU 1404 CG ARG A 177 7445 8110 7582 -145 -113 -269 C ATOM 1405 CD ARG A 177 -58.470 -11.670 29.200 1.00 62.24 C ANISOU 1405 CD ARG A 177 7604 8285 7758 -157 -125 -260 C ATOM 1406 NE ARG A 177 -58.840 -12.762 30.094 1.00 53.43 N ANISOU 1406 NE ARG A 177 6503 7121 6679 -161 -126 -287 N ATOM 1407 CZ ARG A 177 -60.076 -12.996 30.508 1.00 46.83 C ANISOU 1407 CZ ARG A 177 5662 6270 5860 -169 -133 -279 C ATOM 1408 NH1 ARG A 177 -61.061 -12.213 30.086 1.00 53.14 N ANISOU 1408 NH1 ARG A 177 6444 7102 6643 -173 -140 -246 N ATOM 1409 NH2 ARG A 177 -60.322 -14.010 31.335 1.00 39.15 N ANISOU 1409 NH2 ARG A 177 4700 5252 4924 -172 -133 -300 N ATOM 1410 N TYR A 178 -54.933 -8.577 30.232 1.00 61.32 N ANISOU 1410 N TYR A 178 7515 8134 7652 -111 -85 -175 N ATOM 1411 CA TYR A 178 -54.740 -8.062 31.586 1.00 57.55 C ANISOU 1411 CA TYR A 178 7054 7603 7209 -101 -75 -158 C ATOM 1412 C TYR A 178 -56.053 -8.071 32.369 1.00 57.51 C ANISOU 1412 C TYR A 178 7050 7573 7227 -104 -79 -147 C ATOM 1413 O TYR A 178 -57.032 -7.431 31.983 1.00 62.27 O ANISOU 1413 O TYR A 178 7637 8196 7827 -107 -84 -118 O ATOM 1414 CB TYR A 178 -54.145 -6.637 31.560 1.00 55.74 C ANISOU 1414 CB TYR A 178 6818 7377 6983 -92 -67 -119 C ATOM 1415 CG TYR A 178 -52.676 -6.583 31.188 1.00 54.46 C ANISOU 1415 CG TYR A 178 6659 7226 6808 -87 -60 -128 C ATOM 1416 CD1 TYR A 178 -51.719 -7.282 31.932 1.00 59.13 C ANISOU 1416 CD1 TYR A 178 7270 7787 7410 -82 -54 -158 C ATOM 1417 CD2 TYR A 178 -52.241 -5.831 30.098 1.00 51.34 C ANISOU 1417 CD2 TYR A 178 6244 6875 6389 -87 -60 -102 C ATOM 1418 CE1 TYR A 178 -50.367 -7.242 31.589 1.00 62.02 C ANISOU 1418 CE1 TYR A 178 7637 8163 7763 -77 -48 -166 C ATOM 1419 CE2 TYR A 178 -50.902 -5.786 29.743 1.00 56.79 C ANISOU 1419 CE2 TYR A 178 6935 7577 7064 -82 -53 -109 C ATOM 1420 CZ TYR A 178 -49.967 -6.491 30.493 1.00 62.85 C ANISOU 1420 CZ TYR A 178 7724 8312 7844 -77 -47 -142 C ATOM 1421 OH TYR A 178 -48.637 -6.443 30.143 1.00 58.92 O ANISOU 1421 OH TYR A 178 7226 7828 7333 -72 -41 -148 O ATOM 1422 N ILE A 179 -56.084 -8.784 33.480 1.00 54.29 N ANISOU 1422 N ILE A 179 6658 7124 6843 -103 -76 -165 N ATOM 1423 CA ILE A 179 -57.281 -8.773 34.307 1.00 55.16 C ANISOU 1423 CA ILE A 179 6770 7213 6976 -104 -78 -153 C ATOM 1424 C ILE A 179 -56.878 -8.603 35.759 1.00 55.60 C ANISOU 1424 C ILE A 179 6840 7226 7058 -95 -67 -150 C ATOM 1425 O ILE A 179 -55.776 -8.994 36.140 1.00 57.25 O ANISOU 1425 O ILE A 179 7062 7422 7269 -90 -62 -167 O ATOM 1426 CB ILE A 179 -58.153 -10.055 34.097 1.00 55.45 C ANISOU 1426 CB ILE A 179 6803 7251 7013 -117 -89 -178 C ATOM 1427 CG1 ILE A 179 -57.362 -11.324 34.417 1.00 52.36 C ANISOU 1427 CG1 ILE A 179 6424 6837 6632 -118 -88 -216 C ATOM 1428 CG2 ILE A 179 -58.655 -10.138 32.651 1.00 54.75 C ANISOU 1428 CG2 ILE A 179 6695 7212 6894 -128 -101 -183 C ATOM 1429 CD1 ILE A 179 -58.210 -12.542 34.537 1.00 48.25 C ANISOU 1429 CD1 ILE A 179 5901 6304 6127 -129 -96 -238 C ATOM 1430 N PRO A 180 -57.755 -8.001 36.575 1.00 56.29 N ANISOU 1430 N PRO A 180 6925 7298 7164 -92 -64 -128 N ATOM 1431 CA PRO A 180 -57.482 -7.907 38.014 1.00 54.92 C ANISOU 1431 CA PRO A 180 6763 7093 7011 -84 -54 -129 C ATOM 1432 C PRO A 180 -57.080 -9.266 38.601 1.00 53.54 C ANISOU 1432 C PRO A 180 6599 6901 6841 -87 -56 -153 C ATOM 1433 O PRO A 180 -57.732 -10.267 38.313 1.00 52.38 O ANISOU 1433 O PRO A 180 6449 6755 6696 -96 -64 -165 O ATOM 1434 CB PRO A 180 -58.826 -7.460 38.583 1.00 55.52 C ANISOU 1434 CB PRO A 180 6831 7163 7102 -84 -54 -110 C ATOM 1435 CG PRO A 180 -59.447 -6.668 37.466 1.00 55.21 C ANISOU 1435 CG PRO A 180 6774 7148 7054 -87 -59 -88 C ATOM 1436 CD PRO A 180 -59.031 -7.363 36.206 1.00 55.42 C ANISOU 1436 CD PRO A 180 6800 7204 7055 -95 -68 -103 C ATOM 1437 N GLU A 181 -56.001 -9.313 39.386 1.00 54.52 N ANISOU 1437 N GLU A 181 6734 7010 6971 -80 -48 -160 N ATOM 1438 CA GLU A 181 -55.617 -10.569 40.047 1.00 54.81 C ANISOU 1438 CA GLU A 181 6778 7029 7019 -81 -48 -176 C ATOM 1439 C GLU A 181 -55.938 -10.646 41.536 1.00 50.05 C ANISOU 1439 C GLU A 181 6176 6411 6431 -77 -42 -165 C ATOM 1440 O GLU A 181 -56.391 -9.681 42.131 1.00 50.64 O ANISOU 1440 O GLU A 181 6247 6487 6508 -73 -36 -150 O ATOM 1441 CB GLU A 181 -54.170 -11.005 39.737 1.00 55.35 C ANISOU 1441 CB GLU A 181 6854 7096 7081 -77 -45 -194 C ATOM 1442 CG GLU A 181 -53.057 -10.130 40.280 1.00 61.86 C ANISOU 1442 CG GLU A 181 7683 7918 7901 -68 -35 -188 C ATOM 1443 CD GLU A 181 -51.647 -10.640 39.904 1.00 73.57 C ANISOU 1443 CD GLU A 181 9172 9402 9378 -64 -33 -204 C ATOM 1444 OE1 GLU A 181 -51.357 -11.856 40.021 1.00 67.34 O ANISOU 1444 OE1 GLU A 181 8386 8602 8599 -65 -35 -219 O ATOM 1445 OE2 GLU A 181 -50.810 -9.805 39.510 1.00 82.31 O ANISOU 1445 OE2 GLU A 181 10280 10520 10473 -60 -29 -202 O ATOM 1446 N GLY A 182 -55.754 -11.827 42.108 1.00 49.28 N ANISOU 1446 N GLY A 182 6079 6298 6346 -79 -43 -170 N ATOM 1447 CA GLY A 182 -55.901 -12.033 43.540 1.00 49.91 C ANISOU 1447 CA GLY A 182 6157 6370 6437 -75 -38 -157 C ATOM 1448 C GLY A 182 -57.078 -11.303 44.128 1.00 52.48 C ANISOU 1448 C GLY A 182 6474 6702 6763 -75 -35 -140 C ATOM 1449 O GLY A 182 -58.223 -11.598 43.790 1.00 56.96 O ANISOU 1449 O GLY A 182 7036 7270 7337 -82 -42 -135 O ATOM 1450 N MET A 183 -56.802 -10.337 45.004 1.00 53.08 N ANISOU 1450 N MET A 183 6550 6785 6834 -68 -26 -135 N ATOM 1451 CA MET A 183 -57.865 -9.574 45.662 1.00 49.35 C ANISOU 1451 CA MET A 183 6068 6318 6363 -66 -21 -124 C ATOM 1452 C MET A 183 -58.520 -8.523 44.770 1.00 48.79 C ANISOU 1452 C MET A 183 5994 6252 6293 -66 -22 -121 C ATOM 1453 O MET A 183 -59.281 -7.696 45.259 1.00 46.99 O ANISOU 1453 O MET A 183 5757 6026 6070 -63 -16 -113 O ATOM 1454 CB MET A 183 -57.336 -8.924 46.924 1.00 48.41 C ANISOU 1454 CB MET A 183 5946 6207 6239 -59 -9 -126 C ATOM 1455 CG MET A 183 -57.287 -9.866 48.088 1.00 56.95 C ANISOU 1455 CG MET A 183 7021 7295 7321 -59 -8 -117 C ATOM 1456 SD MET A 183 -56.034 -9.400 49.281 1.00 60.89 S ANISOU 1456 SD MET A 183 7519 7810 7806 -53 3 -125 S ATOM 1457 CE MET A 183 -56.686 -7.863 49.930 1.00 58.51 C ANISOU 1457 CE MET A 183 7208 7522 7503 -49 14 -136 C ATOM 1458 N GLN A 184 -58.201 -8.548 43.475 1.00 50.26 N ANISOU 1458 N GLN A 184 6184 6439 6473 -70 -29 -125 N ATOM 1459 CA GLN A 184 -58.882 -7.736 42.463 1.00 52.64 C ANISOU 1459 CA GLN A 184 6478 6749 6773 -71 -32 -116 C ATOM 1460 C GLN A 184 -58.523 -6.250 42.498 1.00 54.40 C ANISOU 1460 C GLN A 184 6697 6970 7001 -63 -22 -109 C ATOM 1461 O GLN A 184 -59.188 -5.421 41.873 1.00 52.65 O ANISOU 1461 O GLN A 184 6465 6754 6786 -62 -22 -94 O ATOM 1462 CB GLN A 184 -60.402 -7.930 42.559 1.00 57.50 C ANISOU 1462 CB GLN A 184 7083 7367 7396 -76 -37 -102 C ATOM 1463 CG GLN A 184 -60.857 -9.387 42.436 1.00 56.17 C ANISOU 1463 CG GLN A 184 6916 7198 7230 -86 -47 -108 C ATOM 1464 CD GLN A 184 -60.379 -10.017 41.142 1.00 57.19 C ANISOU 1464 CD GLN A 184 7048 7333 7348 -93 -57 -123 C ATOM 1465 OE1 GLN A 184 -59.488 -10.863 41.147 1.00 54.11 O ANISOU 1465 OE1 GLN A 184 6666 6934 6958 -94 -58 -139 O ATOM 1466 NE2 GLN A 184 -60.941 -9.572 40.019 1.00 50.57 N ANISOU 1466 NE2 GLN A 184 6202 6514 6500 -98 -64 -117 N ATOM 1467 N CYS A 185 -57.452 -5.917 43.209 1.00 58.18 N ANISOU 1467 N CYS A 185 7182 7443 7481 -58 -13 -120 N ATOM 1468 CA CYS A 185 -57.044 -4.531 43.356 1.00 58.68 C ANISOU 1468 CA CYS A 185 7240 7501 7556 -51 -3 -119 C ATOM 1469 C CYS A 185 -55.934 -4.180 42.411 1.00 59.57 C ANISOU 1469 C CYS A 185 7356 7615 7662 -51 -4 -119 C ATOM 1470 O CYS A 185 -55.693 -3.006 42.169 1.00 66.38 O ANISOU 1470 O CYS A 185 8211 8473 8538 -47 2 -111 O ATOM 1471 CB CYS A 185 -56.596 -4.250 44.775 1.00 58.24 C ANISOU 1471 CB CYS A 185 7185 7440 7505 -47 7 -133 C ATOM 1472 SG CYS A 185 -57.959 -4.271 45.902 1.00 67.42 S ANISOU 1472 SG CYS A 185 8336 8605 8674 -45 12 -131 S ATOM 1473 N SER A 186 -55.236 -5.183 41.891 1.00 58.01 N ANISOU 1473 N SER A 186 7168 7425 7447 -55 -12 -127 N ATOM 1474 CA SER A 186 -54.209 -4.916 40.892 1.00 57.82 C ANISOU 1474 CA SER A 186 7146 7408 7413 -55 -13 -127 C ATOM 1475 C SER A 186 -54.329 -5.845 39.702 1.00 59.18 C ANISOU 1475 C SER A 186 7319 7599 7567 -61 -24 -129 C ATOM 1476 O SER A 186 -54.817 -6.962 39.823 1.00 63.52 O ANISOU 1476 O SER A 186 7873 8147 8113 -66 -30 -139 O ATOM 1477 CB SER A 186 -52.816 -5.022 41.501 1.00 54.64 C ANISOU 1477 CB SER A 186 6753 7000 7008 -52 -7 -142 C ATOM 1478 OG SER A 186 -52.605 -6.324 41.988 1.00 52.19 O ANISOU 1478 OG SER A 186 6451 6688 6690 -53 -11 -155 O ATOM 1479 N CYS A 187 -53.848 -5.385 38.555 1.00 60.59 N ANISOU 1479 N CYS A 187 7492 7794 7734 -62 -26 -121 N ATOM 1480 CA CYS A 187 -53.961 -6.135 37.314 1.00 61.33 C ANISOU 1480 CA CYS A 187 7583 7914 7807 -68 -36 -126 C ATOM 1481 C CYS A 187 -52.647 -6.780 36.891 1.00 59.62 C ANISOU 1481 C CYS A 187 7374 7705 7574 -67 -35 -147 C ATOM 1482 O CYS A 187 -51.590 -6.168 36.975 1.00 63.61 O ANISOU 1482 O CYS A 187 7881 8207 8080 -62 -28 -143 O ATOM 1483 CB CYS A 187 -54.469 -5.211 36.214 1.00 60.61 C ANISOU 1483 CB CYS A 187 7473 7847 7708 -70 -39 -99 C ATOM 1484 SG CYS A 187 -56.159 -4.642 36.494 1.00 68.09 S ANISOU 1484 SG CYS A 187 8408 8790 8674 -71 -41 -75 S ATOM 1485 N GLY A 188 -52.724 -8.015 36.421 1.00 59.58 N ANISOU 1485 N GLY A 188 7371 7708 7558 -73 -43 -170 N ATOM 1486 CA GLY A 188 -51.562 -8.707 35.879 1.00 60.27 C ANISOU 1486 CA GLY A 188 7463 7805 7631 -72 -42 -192 C ATOM 1487 C GLY A 188 -51.909 -9.468 34.619 1.00 59.22 C ANISOU 1487 C GLY A 188 7322 7702 7478 -80 -51 -211 C ATOM 1488 O GLY A 188 -52.963 -9.273 34.050 1.00 59.11 O ANISOU 1488 O GLY A 188 7297 7708 7456 -87 -58 -201 O ATOM 1489 N ILE A 189 -51.004 -10.331 34.180 1.00 62.66 N ANISOU 1489 N ILE A 189 7760 8143 7905 -79 -50 -240 N ATOM 1490 CA ILE A 189 -51.220 -11.178 33.015 1.00 62.61 C ANISOU 1490 CA ILE A 189 7744 8166 7879 -87 -58 -270 C ATOM 1491 C ILE A 189 -52.139 -12.322 33.396 1.00 64.78 C ANISOU 1491 C ILE A 189 8020 8418 8175 -95 -64 -291 C ATOM 1492 O ILE A 189 -51.956 -12.937 34.450 1.00 65.72 O ANISOU 1492 O ILE A 189 8150 8497 8322 -91 -61 -296 O ATOM 1493 CB ILE A 189 -49.890 -11.789 32.536 1.00 63.07 C ANISOU 1493 CB ILE A 189 7804 8232 7928 -83 -52 -299 C ATOM 1494 CG1 ILE A 189 -49.160 -10.837 31.595 1.00 60.62 C ANISOU 1494 CG1 ILE A 189 7483 7964 7586 -80 -49 -283 C ATOM 1495 CG2 ILE A 189 -50.113 -13.140 31.865 1.00 65.18 C ANISOU 1495 CG2 ILE A 189 8065 8507 8194 -90 -58 -345 C ATOM 1496 CD1 ILE A 189 -47.736 -11.281 31.319 1.00 65.65 C ANISOU 1496 CD1 ILE A 189 8122 8605 8215 -72 -41 -307 C ATOM 1497 N ASP A 190 -53.124 -12.600 32.542 1.00 67.58 N ANISOU 1497 N ASP A 190 8362 8799 8516 -106 -75 -302 N ATOM 1498 CA ASP A 190 -54.019 -13.739 32.744 1.00 69.19 C ANISOU 1498 CA ASP A 190 8565 8984 8742 -116 -82 -326 C ATOM 1499 C ASP A 190 -53.296 -15.037 32.386 1.00 69.41 C ANISOU 1499 C ASP A 190 8592 9002 8779 -118 -81 -374 C ATOM 1500 O ASP A 190 -53.111 -15.365 31.212 1.00 72.20 O ANISOU 1500 O ASP A 190 8933 9392 9108 -123 -85 -406 O ATOM 1501 CB ASP A 190 -55.319 -13.588 31.939 1.00 66.76 C ANISOU 1501 CB ASP A 190 8240 8710 8416 -129 -94 -323 C ATOM 1502 CG ASP A 190 -56.284 -14.756 32.157 1.00 70.01 C ANISOU 1502 CG ASP A 190 8649 9101 8853 -141 -102 -347 C ATOM 1503 OD1 ASP A 190 -55.936 -15.707 32.912 1.00 59.34 O ANISOU 1503 OD1 ASP A 190 7305 7705 7535 -138 -98 -365 O ATOM 1504 OD2 ASP A 190 -57.386 -14.726 31.560 1.00 68.27 O ANISOU 1504 OD2 ASP A 190 8414 8906 8620 -153 -113 -347 O ATOM 1505 N TYR A 191 -52.877 -15.761 33.414 1.00 68.81 N ANISOU 1505 N TYR A 191 8527 8879 8739 -112 -75 -378 N ATOM 1506 CA TYR A 191 -52.068 -16.956 33.226 1.00 68.38 C ANISOU 1506 CA TYR A 191 8471 8806 8705 -110 -71 -419 C ATOM 1507 C TYR A 191 -52.746 -18.144 33.889 1.00 68.88 C ANISOU 1507 C TYR A 191 8532 8825 8813 -116 -75 -432 C ATOM 1508 O TYR A 191 -52.154 -19.210 33.990 1.00 71.34 O ANISOU 1508 O TYR A 191 8842 9109 9157 -114 -71 -460 O ATOM 1509 CB TYR A 191 -50.640 -16.761 33.799 1.00 66.64 C ANISOU 1509 CB TYR A 191 8261 8569 8489 -95 -59 -410 C ATOM 1510 CG TYR A 191 -50.602 -16.636 35.306 1.00 56.84 C ANISOU 1510 CG TYR A 191 7032 7290 7276 -88 -55 -375 C ATOM 1511 CD1 TYR A 191 -50.575 -17.765 36.112 1.00 54.61 C ANISOU 1511 CD1 TYR A 191 6748 6964 7035 -86 -53 -381 C ATOM 1512 CD2 TYR A 191 -50.650 -15.392 35.919 1.00 52.93 C ANISOU 1512 CD2 TYR A 191 6543 6802 6765 -83 -52 -336 C ATOM 1513 CE1 TYR A 191 -50.579 -17.664 37.494 1.00 61.77 C ANISOU 1513 CE1 TYR A 191 7661 7845 7962 -80 -49 -347 C ATOM 1514 CE2 TYR A 191 -50.654 -15.271 37.295 1.00 56.79 C ANISOU 1514 CE2 TYR A 191 7039 7263 7275 -77 -47 -309 C ATOM 1515 CZ TYR A 191 -50.616 -16.412 38.081 1.00 64.22 C ANISOU 1515 CZ TYR A 191 7979 8169 8251 -76 -46 -313 C ATOM 1516 OH TYR A 191 -50.628 -16.304 39.452 1.00 59.06 O ANISOU 1516 OH TYR A 191 7329 7498 7613 -71 -42 -284 O ATOM 1517 N TYR A 192 -53.982 -17.960 34.342 1.00 69.65 N ANISOU 1517 N TYR A 192 8627 8916 8918 -124 -82 -409 N ATOM 1518 CA TYR A 192 -54.659 -18.984 35.142 1.00 71.61 C ANISOU 1518 CA TYR A 192 8873 9123 9214 -130 -85 -409 C ATOM 1519 C TYR A 192 -56.031 -19.348 34.589 1.00 74.73 C ANISOU 1519 C TYR A 192 9255 9528 9612 -147 -97 -423 C ATOM 1520 O TYR A 192 -56.526 -20.449 34.815 1.00 76.55 O ANISOU 1520 O TYR A 192 9476 9726 9882 -155 -101 -440 O ATOM 1521 CB TYR A 192 -54.781 -18.541 36.606 1.00 71.35 C ANISOU 1521 CB TYR A 192 8849 9065 9196 -121 -80 -361 C ATOM 1522 CG TYR A 192 -55.142 -17.080 36.794 1.00 72.57 C ANISOU 1522 CG TYR A 192 9010 9247 9317 -117 -79 -326 C ATOM 1523 CD1 TYR A 192 -54.157 -16.094 36.741 1.00 71.63 C ANISOU 1523 CD1 TYR A 192 8899 9145 9172 -106 -71 -314 C ATOM 1524 CD2 TYR A 192 -56.464 -16.681 37.015 1.00 67.80 C ANISOU 1524 CD2 TYR A 192 8400 8649 8711 -125 -85 -304 C ATOM 1525 CE1 TYR A 192 -54.470 -14.755 36.902 1.00 78.72 C ANISOU 1525 CE1 TYR A 192 9799 10062 10048 -103 -70 -284 C ATOM 1526 CE2 TYR A 192 -56.790 -15.334 37.176 1.00 73.95 C ANISOU 1526 CE2 TYR A 192 9182 9449 9466 -120 -83 -273 C ATOM 1527 CZ TYR A 192 -55.782 -14.374 37.128 1.00 81.07 C ANISOU 1527 CZ TYR A 192 10092 10364 10347 -109 -75 -264 C ATOM 1528 OH TYR A 192 -56.060 -13.030 37.291 1.00 80.09 O ANISOU 1528 OH TYR A 192 9968 10255 10208 -104 -72 -235 O ATOM 1529 N THR A 193 -56.633 -18.412 33.864 1.00 78.57 N ANISOU 1529 N THR A 193 9736 10059 10056 -152 -104 -413 N ATOM 1530 CA THR A 193 -57.961 -18.591 33.277 1.00 79.01 C ANISOU 1530 CA THR A 193 9779 10135 10108 -169 -117 -422 C ATOM 1531 C THR A 193 -57.875 -19.168 31.861 1.00 82.32 C ANISOU 1531 C THR A 193 10183 10589 10508 -181 -123 -476 C ATOM 1532 O THR A 193 -57.061 -18.710 31.049 1.00 80.80 O ANISOU 1532 O THR A 193 9988 10433 10278 -176 -120 -489 O ATOM 1533 CB THR A 193 -58.755 -17.255 33.317 1.00 79.79 C ANISOU 1533 CB THR A 193 9876 10264 10175 -168 -120 -377 C ATOM 1534 OG1 THR A 193 -59.820 -17.381 34.262 1.00 85.70 O ANISOU 1534 OG1 THR A 193 10625 10986 10952 -171 -123 -351 O ATOM 1535 CG2 THR A 193 -59.318 -16.858 31.954 1.00 61.17 C ANISOU 1535 CG2 THR A 193 7502 7964 7777 -179 -130 -390 C ATOM 1536 N PRO A 194 -58.701 -20.196 31.570 1.00 85.70 N ANISOU 1536 N PRO A 194 10597 11006 10961 -197 -133 -510 N ATOM 1537 CA PRO A 194 -58.660 -20.922 30.291 1.00 84.89 C ANISOU 1537 CA PRO A 194 10475 10933 10845 -211 -139 -572 C ATOM 1538 C PRO A 194 -59.038 -20.090 29.054 1.00 84.03 C ANISOU 1538 C PRO A 194 10353 10901 10673 -219 -148 -575 C ATOM 1539 O PRO A 194 -58.752 -20.502 27.942 1.00 85.74 O ANISOU 1539 O PRO A 194 10555 11157 10867 -227 -151 -626 O ATOM 1540 CB PRO A 194 -59.659 -22.063 30.509 1.00 85.47 C ANISOU 1540 CB PRO A 194 10537 10972 10968 -228 -148 -597 C ATOM 1541 CG PRO A 194 -59.708 -22.246 32.000 1.00 84.23 C ANISOU 1541 CG PRO A 194 10393 10753 10859 -218 -141 -553 C ATOM 1542 CD PRO A 194 -59.605 -20.851 32.536 1.00 86.15 C ANISOU 1542 CD PRO A 194 10651 11015 11065 -204 -136 -494 C ATOM 1543 N HIS A 195 -59.660 -18.933 29.253 1.00 82.65 N ANISOU 1543 N HIS A 195 10181 10751 10473 -216 -151 -520 N ATOM 1544 CA HIS A 195 -60.004 -17.988 28.172 1.00 83.32 C ANISOU 1544 CA HIS A 195 10249 10908 10499 -221 -158 -507 C ATOM 1545 C HIS A 195 -59.299 -18.184 26.818 1.00 83.03 C ANISOU 1545 C HIS A 195 10198 10931 10421 -226 -159 -554 C ATOM 1546 O HIS A 195 -58.133 -17.840 26.672 1.00 82.60 O ANISOU 1546 O HIS A 195 10150 10884 10350 -212 -149 -553 O ATOM 1547 CB HIS A 195 -59.762 -16.565 28.668 1.00 83.25 C ANISOU 1547 CB HIS A 195 10253 10904 10474 -204 -151 -442 C ATOM 1548 CG HIS A 195 -60.516 -15.519 27.913 1.00 83.38 C ANISOU 1548 CG HIS A 195 10251 10981 10448 -209 -159 -407 C ATOM 1549 ND1 HIS A 195 -59.924 -14.716 26.960 1.00 83.12 N ANISOU 1549 ND1 HIS A 195 10208 11006 10369 -205 -157 -396 N ATOM 1550 CD2 HIS A 195 -61.809 -15.123 27.990 1.00 81.76 C ANISOU 1550 CD2 HIS A 195 10035 10787 10242 -217 -168 -377 C ATOM 1551 CE1 HIS A 195 -60.821 -13.874 26.477 1.00 79.27 C ANISOU 1551 CE1 HIS A 195 9702 10563 9856 -210 -165 -357 C ATOM 1552 NE2 HIS A 195 -61.974 -14.103 27.083 1.00 88.42 N ANISOU 1552 NE2 HIS A 195 10861 11694 11041 -217 -172 -346 N ATOM 1553 N GLU A 196 -60.030 -18.672 25.812 1.00 86.73 N ANISOU 1553 N GLU A 196 10641 11445 10866 -245 -172 -593 N ATOM 1554 CA GLU A 196 -59.423 -19.038 24.511 1.00 87.21 C ANISOU 1554 CA GLU A 196 10682 11566 10886 -252 -174 -649 C ATOM 1555 C GLU A 196 -59.496 -17.996 23.384 1.00 84.14 C ANISOU 1555 C GLU A 196 10273 11270 10427 -254 -179 -624 C ATOM 1556 O GLU A 196 -58.728 -18.072 22.432 1.00 83.12 O ANISOU 1556 O GLU A 196 10129 11194 10258 -255 -176 -658 O ATOM 1557 CB GLU A 196 -59.953 -20.387 24.017 1.00 87.50 C ANISOU 1557 CB GLU A 196 10702 11601 10944 -273 -183 -724 C ATOM 1558 CG GLU A 196 -59.355 -21.588 24.745 1.00 97.74 C ANISOU 1558 CG GLU A 196 12013 12818 12308 -268 -173 -766 C ATOM 1559 CD GLU A 196 -60.418 -22.565 25.239 1.00108.40 C ANISOU 1559 CD GLU A 196 13356 14117 13713 -285 -182 -787 C ATOM 1560 OE1 GLU A 196 -61.286 -22.961 24.430 1.00115.61 O ANISOU 1560 OE1 GLU A 196 14245 15070 14610 -306 -196 -825 O ATOM 1561 OE2 GLU A 196 -60.389 -22.934 26.438 1.00104.31 O ANISOU 1561 OE2 GLU A 196 12856 13523 13254 -276 -176 -762 O ATOM 1562 N GLU A 197 -60.407 -17.031 23.484 1.00 83.99 N ANISOU 1562 N GLU A 197 10248 11272 10391 -256 -186 -563 N ATOM 1563 CA GLU A 197 -60.484 -15.950 22.490 1.00 86.14 C ANISOU 1563 CA GLU A 197 10497 11629 10601 -256 -191 -526 C ATOM 1564 C GLU A 197 -59.148 -15.237 22.342 1.00 83.83 C ANISOU 1564 C GLU A 197 10213 11352 10289 -238 -177 -504 C ATOM 1565 O GLU A 197 -58.860 -14.680 21.293 1.00 82.76 O ANISOU 1565 O GLU A 197 10054 11294 10099 -240 -179 -494 O ATOM 1566 CB GLU A 197 -61.564 -14.917 22.858 1.00 88.03 C ANISOU 1566 CB GLU A 197 10732 11872 10842 -255 -197 -453 C ATOM 1567 CG GLU A 197 -63.012 -15.369 22.647 1.00 99.63 C ANISOU 1567 CG GLU A 197 12183 13358 12312 -275 -213 -464 C ATOM 1568 CD GLU A 197 -63.374 -16.610 23.467 1.00117.73 C ANISOU 1568 CD GLU A 197 14492 15579 14663 -283 -215 -510 C ATOM 1569 OE1 GLU A 197 -63.293 -16.565 24.723 1.00111.63 O ANISOU 1569 OE1 GLU A 197 13745 14730 13938 -271 -206 -484 O ATOM 1570 OE2 GLU A 197 -63.738 -17.636 22.842 1.00125.97 O ANISOU 1570 OE2 GLU A 197 15518 16643 15702 -303 -225 -573 O ATOM 1571 N THR A 198 -58.348 -15.252 23.410 1.00 85.16 N ANISOU 1571 N THR A 198 10412 11447 10500 -222 -164 -494 N ATOM 1572 CA THR A 198 -57.076 -14.517 23.477 1.00 81.65 C ANISOU 1572 CA THR A 198 9977 11003 10044 -204 -150 -468 C ATOM 1573 C THR A 198 -55.867 -15.449 23.405 1.00 82.40 C ANISOU 1573 C THR A 198 10081 11080 10148 -199 -140 -527 C ATOM 1574 O THR A 198 -54.768 -15.026 23.023 1.00 80.90 O ANISOU 1574 O THR A 198 9890 10915 9934 -188 -131 -521 O ATOM 1575 CB THR A 198 -56.969 -13.680 24.762 1.00 79.09 C ANISOU 1575 CB THR A 198 9678 10614 9757 -188 -141 -409 C ATOM 1576 OG1 THR A 198 -57.476 -14.441 25.865 1.00 77.78 O ANISOU 1576 OG1 THR A 198 9531 10378 9644 -189 -142 -424 O ATOM 1577 CG2 THR A 198 -57.753 -12.382 24.626 1.00 69.79 C ANISOU 1577 CG2 THR A 198 8486 9466 8563 -187 -146 -341 C ATOM 1578 N ASN A 199 -56.079 -16.709 23.783 1.00 80.61 N ANISOU 1578 N ASN A 199 9861 10806 9960 -206 -142 -581 N ATOM 1579 CA ASN A 199 -55.075 -17.750 23.604 1.00 80.82 C ANISOU 1579 CA ASN A 199 9891 10816 10001 -203 -133 -645 C ATOM 1580 C ASN A 199 -54.142 -17.873 24.781 1.00 79.46 C ANISOU 1580 C ASN A 199 9747 10568 9877 -185 -120 -631 C ATOM 1581 O ASN A 199 -52.921 -17.955 24.630 1.00 78.38 O ANISOU 1581 O ASN A 199 9614 10432 9734 -173 -108 -647 O ATOM 1582 CB ASN A 199 -54.265 -17.510 22.337 1.00 82.77 C ANISOU 1582 CB ASN A 199 10116 11142 10189 -202 -130 -669 C ATOM 1583 CG ASN A 199 -54.911 -18.113 21.128 1.00 80.57 C ANISOU 1583 CG ASN A 199 9807 10933 9874 -222 -142 -725 C ATOM 1584 OD1 ASN A 199 -55.189 -17.418 20.146 1.00 77.58 O ANISOU 1584 OD1 ASN A 199 9403 10639 9435 -229 -149 -706 O ATOM 1585 ND2 ASN A 199 -55.170 -19.418 21.191 1.00 70.05 N ANISOU 1585 ND2 ASN A 199 8472 9565 8579 -233 -144 -794 N ATOM 1586 N ASN A 200 -54.737 -17.914 25.959 1.00 78.24 N ANISOU 1586 N ASN A 200 9609 10350 9767 -183 -121 -601 N ATOM 1587 CA ASN A 200 -53.973 -17.961 27.182 1.00 79.38 C ANISOU 1587 CA ASN A 200 9779 10428 9954 -167 -109 -579 C ATOM 1588 C ASN A 200 -53.001 -19.135 27.276 1.00 80.89 C ANISOU 1588 C ASN A 200 9974 10583 10179 -162 -100 -632 C ATOM 1589 O ASN A 200 -51.868 -18.963 27.723 1.00 85.84 O ANISOU 1589 O ASN A 200 10613 11188 10814 -146 -88 -620 O ATOM 1590 CB ASN A 200 -54.905 -17.874 28.393 1.00 75.94 C ANISOU 1590 CB ASN A 200 9355 9939 9557 -168 -113 -540 C ATOM 1591 CG ASN A 200 -55.656 -16.551 28.444 1.00 69.75 C ANISOU 1591 CG ASN A 200 8571 9185 8747 -168 -117 -482 C ATOM 1592 OD1 ASN A 200 -55.520 -15.701 27.551 1.00 54.66 O ANISOU 1592 OD1 ASN A 200 6647 7332 6790 -168 -119 -467 O ATOM 1593 ND2 ASN A 200 -56.454 -16.369 29.486 1.00 74.71 N ANISOU 1593 ND2 ASN A 200 9209 9773 9405 -167 -119 -448 N ATOM 1594 N GLU A 201 -53.418 -20.306 26.814 1.00 80.56 N ANISOU 1594 N GLU A 201 9917 10534 10156 -175 -105 -691 N ATOM 1595 CA GLU A 201 -52.608 -21.507 26.973 1.00 82.01 C ANISOU 1595 CA GLU A 201 10101 10673 10385 -170 -96 -742 C ATOM 1596 C GLU A 201 -51.258 -21.400 26.246 1.00 81.93 C ANISOU 1596 C GLU A 201 10088 10699 10345 -158 -85 -768 C ATOM 1597 O GLU A 201 -50.210 -21.764 26.800 1.00 82.50 O ANISOU 1597 O GLU A 201 10170 10729 10448 -144 -72 -771 O ATOM 1598 CB GLU A 201 -53.384 -22.741 26.515 1.00 84.00 C ANISOU 1598 CB GLU A 201 10335 10914 10668 -188 -104 -805 C ATOM 1599 CG GLU A 201 -53.028 -24.019 27.258 1.00 90.59 C ANISOU 1599 CG GLU A 201 11172 11669 11580 -184 -96 -834 C ATOM 1600 CD GLU A 201 -53.427 -25.259 26.486 1.00100.17 C ANISOU 1600 CD GLU A 201 12361 12878 12820 -201 -101 -914 C ATOM 1601 OE1 GLU A 201 -54.623 -25.395 26.157 1.00108.11 O ANISOU 1601 OE1 GLU A 201 13354 13901 13821 -220 -114 -926 O ATOM 1602 OE2 GLU A 201 -52.545 -26.094 26.198 1.00100.77 O ANISOU 1602 OE2 GLU A 201 12429 12934 12924 -195 -90 -968 O ATOM 1603 N SER A 202 -51.274 -20.884 25.019 1.00 78.82 N ANISOU 1603 N SER A 202 9676 10385 9888 -165 -89 -784 N ATOM 1604 CA SER A 202 -50.027 -20.744 24.274 1.00 76.36 C ANISOU 1604 CA SER A 202 9358 10115 9542 -155 -78 -807 C ATOM 1605 C SER A 202 -49.131 -19.652 24.877 1.00 76.17 C ANISOU 1605 C SER A 202 9351 10084 9505 -137 -69 -743 C ATOM 1606 O SER A 202 -47.909 -19.798 24.912 1.00 79.72 O ANISOU 1606 O SER A 202 9805 10524 9959 -123 -56 -754 O ATOM 1607 CB SER A 202 -50.279 -20.522 22.776 1.00 72.98 C ANISOU 1607 CB SER A 202 8900 9782 9046 -167 -85 -840 C ATOM 1608 OG SER A 202 -50.700 -19.201 22.512 1.00 74.22 O ANISOU 1608 OG SER A 202 9054 9992 9153 -169 -92 -777 O ATOM 1609 N PHE A 203 -49.739 -18.579 25.383 1.00 72.89 N ANISOU 1609 N PHE A 203 8947 9670 9079 -137 -75 -677 N ATOM 1610 CA PHE A 203 -48.985 -17.502 26.022 1.00 68.09 C ANISOU 1610 CA PHE A 203 8355 9052 8466 -122 -67 -617 C ATOM 1611 C PHE A 203 -48.284 -17.953 27.311 1.00 64.88 C ANISOU 1611 C PHE A 203 7969 8568 8113 -109 -57 -609 C ATOM 1612 O PHE A 203 -47.111 -17.659 27.527 1.00 62.24 O ANISOU 1612 O PHE A 203 7643 8229 7777 -95 -46 -597 O ATOM 1613 CB PHE A 203 -49.890 -16.309 26.290 1.00 66.74 C ANISOU 1613 CB PHE A 203 8185 8893 8278 -126 -75 -555 C ATOM 1614 CG PHE A 203 -49.152 -15.066 26.684 1.00 71.57 C ANISOU 1614 CG PHE A 203 8808 9508 8879 -113 -67 -499 C ATOM 1615 CD1 PHE A 203 -48.630 -14.220 25.718 1.00 71.09 C ANISOU 1615 CD1 PHE A 203 8731 9510 8770 -111 -65 -481 C ATOM 1616 CD2 PHE A 203 -48.993 -14.731 28.033 1.00 73.87 C ANISOU 1616 CD2 PHE A 203 9120 9738 9208 -103 -62 -463 C ATOM 1617 CE1 PHE A 203 -47.959 -13.052 26.088 1.00 79.79 C ANISOU 1617 CE1 PHE A 203 9839 10608 9868 -100 -58 -428 C ATOM 1618 CE2 PHE A 203 -48.331 -13.577 28.415 1.00 64.75 C ANISOU 1618 CE2 PHE A 203 7973 8584 8046 -93 -55 -416 C ATOM 1619 CZ PHE A 203 -47.806 -12.732 27.442 1.00 75.81 C ANISOU 1619 CZ PHE A 203 9359 10041 9406 -92 -53 -399 C ATOM 1620 N VAL A 204 -48.999 -18.684 28.154 1.00 63.43 N ANISOU 1620 N VAL A 204 7793 8329 7977 -113 -61 -613 N ATOM 1621 CA VAL A 204 -48.426 -19.191 29.395 1.00 65.50 C ANISOU 1621 CA VAL A 204 8071 8525 8291 -102 -53 -602 C ATOM 1622 C VAL A 204 -47.237 -20.116 29.105 1.00 67.99 C ANISOU 1622 C VAL A 204 8382 8827 8625 -93 -42 -648 C ATOM 1623 O VAL A 204 -46.231 -20.102 29.823 1.00 68.27 O ANISOU 1623 O VAL A 204 8427 8832 8680 -78 -32 -630 O ATOM 1624 CB VAL A 204 -49.490 -19.922 30.261 1.00 63.76 C ANISOU 1624 CB VAL A 204 7853 8252 8119 -110 -60 -598 C ATOM 1625 CG1 VAL A 204 -48.875 -20.460 31.538 1.00 66.53 C ANISOU 1625 CG1 VAL A 204 8216 8540 8522 -98 -51 -580 C ATOM 1626 CG2 VAL A 204 -50.638 -18.982 30.601 1.00 66.29 C ANISOU 1626 CG2 VAL A 204 8178 8585 8423 -117 -69 -552 C ATOM 1627 N ILE A 205 -47.359 -20.920 28.050 1.00 70.49 N ANISOU 1627 N ILE A 205 8680 9167 8936 -101 -43 -710 N ATOM 1628 CA ILE A 205 -46.272 -21.799 27.627 1.00 68.32 C ANISOU 1628 CA ILE A 205 8397 8885 8678 -93 -32 -761 C ATOM 1629 C ILE A 205 -45.106 -20.952 27.126 1.00 64.64 C ANISOU 1629 C ILE A 205 7931 8466 8164 -81 -23 -747 C ATOM 1630 O ILE A 205 -43.953 -21.187 27.488 1.00 63.82 O ANISOU 1630 O ILE A 205 7832 8338 8079 -66 -11 -748 O ATOM 1631 CB ILE A 205 -46.737 -22.818 26.553 1.00 70.40 C ANISOU 1631 CB ILE A 205 8636 9168 8943 -106 -35 -839 C ATOM 1632 CG1 ILE A 205 -47.512 -23.959 27.215 1.00 72.10 C ANISOU 1632 CG1 ILE A 205 8850 9315 9229 -114 -40 -859 C ATOM 1633 CG2 ILE A 205 -45.546 -23.394 25.790 1.00 69.14 C ANISOU 1633 CG2 ILE A 205 8464 9027 8780 -96 -22 -895 C ATOM 1634 CD1 ILE A 205 -48.381 -24.746 26.256 1.00 62.75 C ANISOU 1634 CD1 ILE A 205 7643 8152 8046 -133 -48 -926 C ATOM 1635 N TYR A 206 -45.415 -19.948 26.320 1.00 60.84 N ANISOU 1635 N TYR A 206 7442 8052 7622 -87 -29 -729 N ATOM 1636 CA TYR A 206 -44.397 -19.022 25.862 1.00 63.20 C ANISOU 1636 CA TYR A 206 7740 8398 7877 -77 -22 -706 C ATOM 1637 C TYR A 206 -43.681 -18.353 27.045 1.00 65.64 C ANISOU 1637 C TYR A 206 8069 8664 8206 -63 -15 -649 C ATOM 1638 O TYR A 206 -42.454 -18.409 27.127 1.00 66.41 O ANISOU 1638 O TYR A 206 8169 8757 8307 -50 -4 -652 O ATOM 1639 CB TYR A 206 -45.007 -18.010 24.898 1.00 61.12 C ANISOU 1639 CB TYR A 206 7462 8211 7551 -88 -31 -684 C ATOM 1640 CG TYR A 206 -44.243 -16.721 24.732 1.00 63.98 C ANISOU 1640 CG TYR A 206 7825 8610 7875 -79 -26 -631 C ATOM 1641 CD1 TYR A 206 -42.955 -16.702 24.203 1.00 66.03 C ANISOU 1641 CD1 TYR A 206 8076 8899 8114 -68 -14 -646 C ATOM 1642 CD2 TYR A 206 -44.832 -15.509 25.062 1.00 63.74 C ANISOU 1642 CD2 TYR A 206 7800 8587 7832 -82 -32 -567 C ATOM 1643 CE1 TYR A 206 -42.266 -15.502 24.036 1.00 62.40 C ANISOU 1643 CE1 TYR A 206 7615 8474 7623 -62 -10 -595 C ATOM 1644 CE2 TYR A 206 -44.161 -14.310 24.891 1.00 60.68 C ANISOU 1644 CE2 TYR A 206 7409 8229 7417 -75 -28 -518 C ATOM 1645 CZ TYR A 206 -42.883 -14.311 24.381 1.00 61.69 C ANISOU 1645 CZ TYR A 206 7529 8385 7524 -66 -17 -531 C ATOM 1646 OH TYR A 206 -42.239 -13.104 24.214 1.00 65.04 O ANISOU 1646 OH TYR A 206 7948 8838 7925 -60 -12 -479 O ATOM 1647 N MET A 207 -44.445 -17.761 27.967 1.00 66.48 N ANISOU 1647 N MET A 207 8190 8742 8328 -67 -22 -600 N ATOM 1648 CA MET A 207 -43.888 -17.185 29.202 1.00 65.25 C ANISOU 1648 CA MET A 207 8053 8545 8194 -56 -17 -551 C ATOM 1649 C MET A 207 -43.042 -18.168 30.008 1.00 63.85 C ANISOU 1649 C MET A 207 7882 8313 8064 -45 -7 -568 C ATOM 1650 O MET A 207 -41.915 -17.846 30.400 1.00 63.38 O ANISOU 1650 O MET A 207 7829 8248 8006 -33 1 -550 O ATOM 1651 CB MET A 207 -44.988 -16.623 30.109 1.00 65.51 C ANISOU 1651 CB MET A 207 8098 8553 8241 -62 -25 -509 C ATOM 1652 CG MET A 207 -45.668 -15.374 29.581 1.00 74.01 C ANISOU 1652 CG MET A 207 9168 9674 9278 -69 -32 -474 C ATOM 1653 SD MET A 207 -44.569 -13.966 29.324 1.00 90.21 S ANISOU 1653 SD MET A 207 11218 11760 11296 -60 -25 -433 S ATOM 1654 CE MET A 207 -44.051 -13.627 31.007 1.00 83.94 C ANISOU 1654 CE MET A 207 10446 10906 10542 -50 -18 -398 C ATOM 1655 N PHE A 208 -43.588 -19.352 30.273 1.00 61.51 N ANISOU 1655 N PHE A 208 7583 7978 7810 -49 -10 -599 N ATOM 1656 CA PHE A 208 -42.881 -20.333 31.086 1.00 62.31 C ANISOU 1656 CA PHE A 208 7687 8024 7964 -38 -1 -608 C ATOM 1657 C PHE A 208 -41.554 -20.719 30.460 1.00 66.40 C ANISOU 1657 C PHE A 208 8196 8555 8477 -26 11 -641 C ATOM 1658 O PHE A 208 -40.531 -20.788 31.146 1.00 71.50 O ANISOU 1658 O PHE A 208 8848 9177 9144 -13 20 -622 O ATOM 1659 CB PHE A 208 -43.715 -21.581 31.292 1.00 58.42 C ANISOU 1659 CB PHE A 208 7187 7487 7521 -46 -5 -638 C ATOM 1660 CG PHE A 208 -43.149 -22.523 32.312 1.00 59.47 C ANISOU 1660 CG PHE A 208 7320 7559 7716 -35 3 -631 C ATOM 1661 CD1 PHE A 208 -43.412 -22.341 33.672 1.00 60.38 C ANISOU 1661 CD1 PHE A 208 7447 7639 7856 -33 0 -578 C ATOM 1662 CD2 PHE A 208 -42.374 -23.609 31.924 1.00 60.83 C ANISOU 1662 CD2 PHE A 208 7479 7709 7923 -27 12 -678 C ATOM 1663 CE1 PHE A 208 -42.910 -23.232 34.638 1.00 60.27 C ANISOU 1663 CE1 PHE A 208 7428 7573 7899 -23 7 -565 C ATOM 1664 CE2 PHE A 208 -41.858 -24.498 32.883 1.00 64.54 C ANISOU 1664 CE2 PHE A 208 7946 8121 8456 -16 20 -665 C ATOM 1665 CZ PHE A 208 -42.133 -24.308 34.242 1.00 58.46 C ANISOU 1665 CZ PHE A 208 7185 7319 7708 -15 17 -606 C ATOM 1666 N VAL A 209 -41.572 -20.981 29.159 1.00 67.38 N ANISOU 1666 N VAL A 209 8305 8722 8573 -31 12 -691 N ATOM 1667 CA VAL A 209 -40.364 -21.388 28.457 1.00 65.59 C ANISOU 1667 CA VAL A 209 8066 8514 8339 -20 24 -730 C ATOM 1668 C VAL A 209 -39.430 -20.197 28.235 1.00 64.42 C ANISOU 1668 C VAL A 209 7922 8412 8143 -13 29 -693 C ATOM 1669 O VAL A 209 -38.350 -20.149 28.825 1.00 66.49 O ANISOU 1669 O VAL A 209 8190 8652 8421 1 38 -674 O ATOM 1670 CB VAL A 209 -40.696 -22.133 27.135 1.00 68.07 C ANISOU 1670 CB VAL A 209 8358 8864 8639 -29 24 -803 C ATOM 1671 CG1 VAL A 209 -39.526 -22.083 26.158 1.00 65.37 C ANISOU 1671 CG1 VAL A 209 8003 8573 8263 -20 36 -836 C ATOM 1672 CG2 VAL A 209 -41.114 -23.586 27.432 1.00 66.28 C ANISOU 1672 CG2 VAL A 209 8124 8577 8481 -32 25 -849 C ATOM 1673 N VAL A 210 -39.860 -19.227 27.427 1.00 60.99 N ANISOU 1673 N VAL A 210 7483 8039 7653 -22 22 -680 N ATOM 1674 CA VAL A 210 -38.988 -18.131 27.006 1.00 59.28 C ANISOU 1674 CA VAL A 210 7264 7870 7391 -15 27 -649 C ATOM 1675 C VAL A 210 -38.598 -17.190 28.141 1.00 63.43 C ANISOU 1675 C VAL A 210 7808 8367 7927 -9 28 -585 C ATOM 1676 O VAL A 210 -37.470 -16.682 28.156 1.00 67.07 O ANISOU 1676 O VAL A 210 8268 8840 8375 0 36 -566 O ATOM 1677 CB VAL A 210 -39.597 -17.306 25.845 1.00 60.62 C ANISOU 1677 CB VAL A 210 7418 8114 7499 -27 20 -642 C ATOM 1678 CG1 VAL A 210 -38.793 -16.029 25.595 1.00 52.76 C ANISOU 1678 CG1 VAL A 210 6421 7161 6466 -22 24 -594 C ATOM 1679 CG2 VAL A 210 -39.667 -18.141 24.576 1.00 59.65 C ANISOU 1679 CG2 VAL A 210 7272 8039 7353 -32 22 -710 C ATOM 1680 N HIS A 211 -39.517 -16.955 29.086 1.00 63.07 N ANISOU 1680 N HIS A 211 7776 8284 7905 -16 19 -554 N ATOM 1681 CA HIS A 211 -39.305 -15.953 30.141 1.00 57.49 C ANISOU 1681 CA HIS A 211 7083 7556 7204 -12 19 -497 C ATOM 1682 C HIS A 211 -39.028 -16.497 31.540 1.00 57.32 C ANISOU 1682 C HIS A 211 7075 7474 7231 -5 22 -485 C ATOM 1683 O HIS A 211 -38.859 -15.733 32.488 1.00 56.37 O ANISOU 1683 O HIS A 211 6965 7338 7115 -3 21 -444 O ATOM 1684 CB HIS A 211 -40.471 -14.990 30.198 1.00 53.96 C ANISOU 1684 CB HIS A 211 6639 7122 6740 -23 8 -463 C ATOM 1685 CG HIS A 211 -40.540 -14.063 29.035 1.00 53.85 C ANISOU 1685 CG HIS A 211 6612 7170 6678 -28 6 -452 C ATOM 1686 ND1 HIS A 211 -40.059 -12.775 29.086 1.00 61.73 N ANISOU 1686 ND1 HIS A 211 7609 8186 7659 -26 8 -406 N ATOM 1687 CD2 HIS A 211 -41.052 -14.225 27.794 1.00 57.79 C ANISOU 1687 CD2 HIS A 211 7094 7720 7144 -36 2 -476 C ATOM 1688 CE1 HIS A 211 -40.270 -12.180 27.924 1.00 56.76 C ANISOU 1688 CE1 HIS A 211 6962 7614 6989 -32 6 -398 C ATOM 1689 NE2 HIS A 211 -40.876 -13.037 27.124 1.00 56.93 N ANISOU 1689 NE2 HIS A 211 6974 7662 6997 -38 1 -440 N ATOM 1690 N PHE A 212 -38.978 -17.810 31.685 1.00 58.93 N ANISOU 1690 N PHE A 212 7275 7645 7471 -1 25 -520 N ATOM 1691 CA PHE A 212 -38.556 -18.376 32.959 1.00 61.32 C ANISOU 1691 CA PHE A 212 7585 7896 7819 7 29 -503 C ATOM 1692 C PHE A 212 -37.460 -19.446 32.828 1.00 63.53 C ANISOU 1692 C PHE A 212 7855 8157 8128 20 40 -534 C ATOM 1693 O PHE A 212 -36.411 -19.327 33.465 1.00 63.64 O ANISOU 1693 O PHE A 212 7871 8160 8151 31 47 -511 O ATOM 1694 CB PHE A 212 -39.745 -18.887 33.772 1.00 60.39 C ANISOU 1694 CB PHE A 212 7472 7739 7735 -1 21 -494 C ATOM 1695 CG PHE A 212 -39.343 -19.574 35.035 1.00 59.69 C ANISOU 1695 CG PHE A 212 7385 7603 7693 8 25 -474 C ATOM 1696 CD1 PHE A 212 -38.902 -18.841 36.123 1.00 59.13 C ANISOU 1696 CD1 PHE A 212 7322 7528 7618 12 26 -429 C ATOM 1697 CD2 PHE A 212 -39.361 -20.954 35.122 1.00 63.52 C ANISOU 1697 CD2 PHE A 212 7859 8049 8227 11 28 -500 C ATOM 1698 CE1 PHE A 212 -38.508 -19.471 37.289 1.00 59.59 C ANISOU 1698 CE1 PHE A 212 7377 7550 7713 20 29 -406 C ATOM 1699 CE2 PHE A 212 -38.966 -21.593 36.285 1.00 66.14 C ANISOU 1699 CE2 PHE A 212 8187 8339 8603 20 33 -474 C ATOM 1700 CZ PHE A 212 -38.543 -20.849 37.372 1.00 63.41 C ANISOU 1700 CZ PHE A 212 7850 7997 8247 24 33 -426 C ATOM 1701 N ILE A 213 -37.702 -20.477 32.010 1.00 65.06 N ANISOU 1701 N ILE A 213 8035 8347 8336 18 42 -586 N ATOM 1702 CA ILE A 213 -36.699 -21.522 31.748 1.00 65.84 C ANISOU 1702 CA ILE A 213 8122 8428 8467 31 55 -623 C ATOM 1703 C ILE A 213 -35.430 -20.987 31.046 1.00 66.88 C ANISOU 1703 C ILE A 213 8248 8603 8561 41 65 -629 C ATOM 1704 O ILE A 213 -34.324 -21.141 31.584 1.00 66.42 O ANISOU 1704 O ILE A 213 8189 8527 8521 55 74 -614 O ATOM 1705 CB ILE A 213 -37.293 -22.756 31.001 1.00 67.01 C ANISOU 1705 CB ILE A 213 8255 8561 8645 26 56 -687 C ATOM 1706 CG1 ILE A 213 -38.415 -23.404 31.820 1.00 67.04 C ANISOU 1706 CG1 ILE A 213 8262 8513 8697 18 47 -676 C ATOM 1707 CG2 ILE A 213 -36.212 -23.807 30.749 1.00 63.99 C ANISOU 1707 CG2 ILE A 213 7857 8156 8300 41 70 -727 C ATOM 1708 CD1 ILE A 213 -37.929 -24.127 33.088 1.00 59.26 C ANISOU 1708 CD1 ILE A 213 7276 7467 7774 29 53 -646 C ATOM 1709 N ILE A 214 -35.575 -20.351 29.876 1.00 65.25 N ANISOU 1709 N ILE A 214 8036 8456 8300 34 63 -647 N ATOM 1710 CA ILE A 214 -34.420 -19.692 29.237 1.00 64.89 C ANISOU 1710 CA ILE A 214 7984 8458 8215 43 71 -643 C ATOM 1711 C ILE A 214 -33.631 -18.848 30.255 1.00 67.53 C ANISOU 1711 C ILE A 214 8331 8779 8551 49 73 -584 C ATOM 1712 O ILE A 214 -32.449 -19.107 30.464 1.00 69.87 O ANISOU 1712 O ILE A 214 8622 9066 8860 63 84 -584 O ATOM 1713 CB ILE A 214 -34.773 -18.848 27.956 1.00 66.69 C ANISOU 1713 CB ILE A 214 8202 8759 8378 33 67 -650 C ATOM 1714 CG1 ILE A 214 -35.358 -19.713 26.822 1.00 64.42 C ANISOU 1714 CG1 ILE A 214 7897 8498 8081 26 67 -716 C ATOM 1715 CG2 ILE A 214 -33.564 -18.053 27.456 1.00 55.90 C ANISOU 1715 CG2 ILE A 214 6829 7439 6973 41 76 -632 C ATOM 1716 CD1 ILE A 214 -34.736 -21.061 26.669 1.00 69.42 C ANISOU 1716 CD1 ILE A 214 8518 9102 8755 37 79 -774 C ATOM 1717 N PRO A 215 -34.283 -17.860 30.920 1.00 69.81 N ANISOU 1717 N PRO A 215 8633 9064 8828 40 63 -537 N ATOM 1718 CA PRO A 215 -33.528 -17.080 31.907 1.00 65.81 C ANISOU 1718 CA PRO A 215 8135 8545 8323 45 64 -489 C ATOM 1719 C PRO A 215 -32.858 -17.925 32.974 1.00 65.07 C ANISOU 1719 C PRO A 215 8042 8404 8276 57 70 -484 C ATOM 1720 O PRO A 215 -31.685 -17.711 33.273 1.00 68.26 O ANISOU 1720 O PRO A 215 8445 8812 8681 66 78 -468 O ATOM 1721 CB PRO A 215 -34.593 -16.176 32.520 1.00 62.80 C ANISOU 1721 CB PRO A 215 7767 8159 7936 33 53 -453 C ATOM 1722 CG PRO A 215 -35.517 -15.925 31.383 1.00 67.57 C ANISOU 1722 CG PRO A 215 8365 8801 8508 23 47 -471 C ATOM 1723 CD PRO A 215 -35.619 -17.268 30.690 1.00 69.59 C ANISOU 1723 CD PRO A 215 8610 9053 8779 25 51 -527 C ATOM 1724 N LEU A 216 -33.574 -18.892 33.531 1.00 65.48 N ANISOU 1724 N LEU A 216 8096 8414 8370 56 67 -494 N ATOM 1725 CA LEU A 216 -33.009 -19.704 34.604 1.00 67.11 C ANISOU 1725 CA LEU A 216 8300 8576 8624 66 72 -480 C ATOM 1726 C LEU A 216 -31.796 -20.493 34.110 1.00 68.79 C ANISOU 1726 C LEU A 216 8497 8786 8853 81 86 -509 C ATOM 1727 O LEU A 216 -30.813 -20.651 34.840 1.00 70.96 O ANISOU 1727 O LEU A 216 8768 9045 9147 92 92 -486 O ATOM 1728 CB LEU A 216 -34.069 -20.636 35.193 1.00 67.75 C ANISOU 1728 CB LEU A 216 8380 8613 8748 61 67 -484 C ATOM 1729 CG LEU A 216 -33.955 -20.987 36.674 1.00 72.58 C ANISOU 1729 CG LEU A 216 8992 9186 9398 66 66 -442 C ATOM 1730 CD1 LEU A 216 -35.329 -21.148 37.256 1.00 77.85 C ANISOU 1730 CD1 LEU A 216 9664 9832 10081 55 56 -429 C ATOM 1731 CD2 LEU A 216 -33.157 -22.258 36.884 1.00 81.00 C ANISOU 1731 CD2 LEU A 216 10042 10216 10517 81 77 -454 C ATOM 1732 N ILE A 217 -31.858 -20.977 32.869 1.00 67.91 N ANISOU 1732 N ILE A 217 8376 8693 8733 82 91 -561 N ATOM 1733 CA ILE A 217 -30.738 -21.725 32.289 1.00 67.58 C ANISOU 1733 CA ILE A 217 8318 8652 8706 97 105 -596 C ATOM 1734 C ILE A 217 -29.513 -20.829 32.032 1.00 67.65 C ANISOU 1734 C ILE A 217 8326 8703 8676 104 112 -576 C ATOM 1735 O ILE A 217 -28.412 -21.144 32.496 1.00 67.82 O ANISOU 1735 O ILE A 217 8340 8709 8720 118 121 -564 O ATOM 1736 CB ILE A 217 -31.159 -22.533 31.025 1.00 69.09 C ANISOU 1736 CB ILE A 217 8495 8856 8900 95 110 -665 C ATOM 1737 CG1 ILE A 217 -31.787 -23.867 31.447 1.00 66.37 C ANISOU 1737 CG1 ILE A 217 8144 8450 8623 96 110 -690 C ATOM 1738 CG2 ILE A 217 -29.971 -22.760 30.076 1.00 62.72 C ANISOU 1738 CG2 ILE A 217 7672 8081 8078 108 125 -702 C ATOM 1739 CD1 ILE A 217 -32.689 -24.492 30.385 1.00 61.60 C ANISOU 1739 CD1 ILE A 217 7530 7856 8020 85 108 -754 C ATOM 1740 N VAL A 218 -29.708 -19.715 31.322 1.00 63.31 N ANISOU 1740 N VAL A 218 7779 8204 8069 95 107 -568 N ATOM 1741 CA VAL A 218 -28.638 -18.739 31.129 1.00 61.57 C ANISOU 1741 CA VAL A 218 7557 8022 7813 99 112 -541 C ATOM 1742 C VAL A 218 -27.958 -18.328 32.436 1.00 63.68 C ANISOU 1742 C VAL A 218 7832 8265 8099 103 111 -491 C ATOM 1743 O VAL A 218 -26.730 -18.271 32.489 1.00 65.88 O ANISOU 1743 O VAL A 218 8103 8552 8377 114 120 -483 O ATOM 1744 CB VAL A 218 -29.108 -17.478 30.398 1.00 61.60 C ANISOU 1744 CB VAL A 218 7564 8079 7762 86 104 -525 C ATOM 1745 CG1 VAL A 218 -27.978 -16.473 30.320 1.00 56.74 C ANISOU 1745 CG1 VAL A 218 6944 7495 7119 89 109 -492 C ATOM 1746 CG2 VAL A 218 -29.593 -17.823 28.999 1.00 63.11 C ANISOU 1746 CG2 VAL A 218 7742 8311 7925 82 106 -573 C ATOM 1747 N ILE A 219 -28.737 -18.057 33.487 1.00 63.51 N ANISOU 1747 N ILE A 219 7824 8215 8092 94 100 -460 N ATOM 1748 CA ILE A 219 -28.154 -17.652 34.780 1.00 63.28 C ANISOU 1748 CA ILE A 219 7800 8168 8076 96 98 -415 C ATOM 1749 C ILE A 219 -27.294 -18.745 35.414 1.00 66.43 C ANISOU 1749 C ILE A 219 8188 8534 8518 112 107 -415 C ATOM 1750 O ILE A 219 -26.201 -18.469 35.903 1.00 67.55 O ANISOU 1750 O ILE A 219 8324 8682 8659 119 111 -391 O ATOM 1751 CB ILE A 219 -29.207 -17.122 35.799 1.00 61.35 C ANISOU 1751 CB ILE A 219 7569 7905 7834 84 86 -384 C ATOM 1752 CG1 ILE A 219 -29.780 -15.793 35.319 1.00 61.96 C ANISOU 1752 CG1 ILE A 219 7655 8016 7871 71 79 -373 C ATOM 1753 CG2 ILE A 219 -28.585 -16.906 37.175 1.00 50.13 C ANISOU 1753 CG2 ILE A 219 6149 6470 6428 87 85 -345 C ATOM 1754 CD1 ILE A 219 -30.855 -15.244 36.200 1.00 62.01 C ANISOU 1754 CD1 ILE A 219 7674 8008 7881 59 68 -349 C ATOM 1755 N PHE A 220 -27.782 -19.983 35.394 1.00 70.17 N ANISOU 1755 N PHE A 220 8656 8973 9033 117 109 -442 N ATOM 1756 CA PHE A 220 -27.037 -21.111 35.966 1.00 71.77 C ANISOU 1756 CA PHE A 220 8844 9139 9287 132 119 -439 C ATOM 1757 C PHE A 220 -25.754 -21.425 35.190 1.00 71.18 C ANISOU 1757 C PHE A 220 8754 9080 9211 148 133 -464 C ATOM 1758 O PHE A 220 -24.698 -21.668 35.787 1.00 70.16 O ANISOU 1758 O PHE A 220 8614 8941 9102 160 140 -441 O ATOM 1759 CB PHE A 220 -27.920 -22.355 36.070 1.00 69.73 C ANISOU 1759 CB PHE A 220 8579 8834 9079 133 118 -462 C ATOM 1760 CG PHE A 220 -28.560 -22.518 37.404 1.00 76.55 C ANISOU 1760 CG PHE A 220 9447 9667 9971 128 110 -419 C ATOM 1761 CD1 PHE A 220 -29.755 -21.875 37.700 1.00 81.96 C ANISOU 1761 CD1 PHE A 220 10148 10360 10634 112 97 -405 C ATOM 1762 CD2 PHE A 220 -27.960 -23.302 38.383 1.00 84.12 C ANISOU 1762 CD2 PHE A 220 10391 10593 10977 140 114 -389 C ATOM 1763 CE1 PHE A 220 -30.355 -22.020 38.958 1.00 86.60 C ANISOU 1763 CE1 PHE A 220 10737 10924 11244 108 89 -366 C ATOM 1764 CE2 PHE A 220 -28.550 -23.455 39.643 1.00 85.78 C ANISOU 1764 CE2 PHE A 220 10601 10782 11208 135 106 -345 C ATOM 1765 CZ PHE A 220 -29.751 -22.812 39.929 1.00 85.91 C ANISOU 1765 CZ PHE A 220 10634 10808 11200 119 94 -335 C ATOM 1766 N PHE A 221 -25.848 -21.412 33.864 1.00 69.07 N ANISOU 1766 N PHE A 221 8483 8841 8918 147 138 -510 N ATOM 1767 CA PHE A 221 -24.688 -21.642 33.030 1.00 69.45 C ANISOU 1767 CA PHE A 221 8516 8914 8959 161 152 -537 C ATOM 1768 C PHE A 221 -23.661 -20.557 33.307 1.00 71.08 C ANISOU 1768 C PHE A 221 8724 9153 9130 162 153 -496 C ATOM 1769 O PHE A 221 -22.560 -20.853 33.774 1.00 73.17 O ANISOU 1769 O PHE A 221 8978 9408 9416 175 161 -479 O ATOM 1770 CB PHE A 221 -25.073 -21.644 31.554 1.00 69.17 C ANISOU 1770 CB PHE A 221 8475 8917 8890 157 156 -591 C ATOM 1771 CG PHE A 221 -23.909 -21.813 30.624 1.00 70.43 C ANISOU 1771 CG PHE A 221 8616 9109 9033 170 172 -622 C ATOM 1772 CD1 PHE A 221 -23.345 -23.069 30.413 1.00 68.59 C ANISOU 1772 CD1 PHE A 221 8364 8848 8848 188 187 -663 C ATOM 1773 CD2 PHE A 221 -23.379 -20.714 29.944 1.00 72.10 C ANISOU 1773 CD2 PHE A 221 8827 9382 9186 167 172 -609 C ATOM 1774 CE1 PHE A 221 -22.266 -23.223 29.535 1.00 69.10 C ANISOU 1774 CE1 PHE A 221 8410 8946 8897 201 203 -694 C ATOM 1775 CE2 PHE A 221 -22.300 -20.859 29.058 1.00 68.81 C ANISOU 1775 CE2 PHE A 221 8391 9003 8752 180 188 -635 C ATOM 1776 CZ PHE A 221 -21.744 -22.111 28.855 1.00 61.82 C ANISOU 1776 CZ PHE A 221 7487 8090 7910 197 203 -680 C ATOM 1777 N CYS A 222 -24.044 -19.304 33.051 1.00 69.31 N ANISOU 1777 N CYS A 222 8512 8967 8857 147 143 -477 N ATOM 1778 CA CYS A 222 -23.141 -18.163 33.179 1.00 66.08 C ANISOU 1778 CA CYS A 222 8103 8591 8414 145 143 -441 C ATOM 1779 C CYS A 222 -22.443 -18.104 34.516 1.00 65.12 C ANISOU 1779 C CYS A 222 7981 8445 8317 149 141 -399 C ATOM 1780 O CYS A 222 -21.238 -17.896 34.586 1.00 66.22 O ANISOU 1780 O CYS A 222 8110 8599 8451 157 148 -384 O ATOM 1781 CB CYS A 222 -23.898 -16.870 32.985 1.00 64.97 C ANISOU 1781 CB CYS A 222 7975 8478 8233 127 131 -420 C ATOM 1782 SG CYS A 222 -24.193 -16.507 31.284 1.00 70.06 S ANISOU 1782 SG CYS A 222 8612 9178 8831 123 135 -453 S ATOM 1783 N TYR A 223 -23.205 -18.266 35.585 1.00 65.03 N ANISOU 1783 N TYR A 223 7979 8400 8328 143 132 -378 N ATOM 1784 CA TYR A 223 -22.631 -18.150 36.909 1.00 64.11 C ANISOU 1784 CA TYR A 223 7861 8270 8229 144 129 -336 C ATOM 1785 C TYR A 223 -21.913 -19.419 37.317 1.00 64.56 C ANISOU 1785 C TYR A 223 7901 8297 8333 163 138 -337 C ATOM 1786 O TYR A 223 -20.938 -19.355 38.061 1.00 66.72 O ANISOU 1786 O TYR A 223 8164 8573 8613 169 140 -306 O ATOM 1787 CB TYR A 223 -23.684 -17.735 37.943 1.00 64.28 C ANISOU 1787 CB TYR A 223 7896 8277 8251 130 115 -310 C ATOM 1788 CG TYR A 223 -23.935 -16.239 38.004 1.00 58.80 C ANISOU 1788 CG TYR A 223 7213 7611 7516 114 106 -292 C ATOM 1789 CD1 TYR A 223 -25.220 -15.731 38.148 1.00 52.93 C ANISOU 1789 CD1 TYR A 223 6484 6863 6763 100 96 -291 C ATOM 1790 CD2 TYR A 223 -22.883 -15.336 37.922 1.00 56.66 C ANISOU 1790 CD2 TYR A 223 6937 7368 7222 113 108 -276 C ATOM 1791 CE1 TYR A 223 -25.448 -14.359 38.211 1.00 47.99 C ANISOU 1791 CE1 TYR A 223 5866 6258 6108 86 89 -275 C ATOM 1792 CE2 TYR A 223 -23.105 -13.968 37.974 1.00 62.46 C ANISOU 1792 CE2 TYR A 223 7680 8124 7930 98 101 -260 C ATOM 1793 CZ TYR A 223 -24.387 -13.488 38.120 1.00 54.61 C ANISOU 1793 CZ TYR A 223 6699 7122 6929 85 92 -260 C ATOM 1794 OH TYR A 223 -24.592 -12.134 38.183 1.00 58.61 O ANISOU 1794 OH TYR A 223 7210 7643 7415 71 86 -244 O ATOM 1795 N GLY A 224 -22.390 -20.565 36.827 1.00 64.88 N ANISOU 1795 N GLY A 224 7936 8309 8407 171 145 -372 N ATOM 1796 CA GLY A 224 -21.688 -21.839 37.012 1.00 65.55 C ANISOU 1796 CA GLY A 224 8000 8361 8545 190 157 -378 C ATOM 1797 C GLY A 224 -20.265 -21.735 36.480 1.00 67.19 C ANISOU 1797 C GLY A 224 8194 8594 8741 204 169 -384 C ATOM 1798 O GLY A 224 -19.302 -21.981 37.203 1.00 65.54 O ANISOU 1798 O GLY A 224 7971 8378 8554 214 174 -353 O ATOM 1799 N GLN A 225 -20.136 -21.330 35.220 1.00 66.76 N ANISOU 1799 N GLN A 225 8141 8575 8651 202 175 -420 N ATOM 1800 CA GLN A 225 -18.838 -21.015 34.645 1.00 69.25 C ANISOU 1800 CA GLN A 225 8442 8924 8944 213 186 -423 C ATOM 1801 C GLN A 225 -18.050 -20.030 35.505 1.00 70.46 C ANISOU 1801 C GLN A 225 8598 9098 9076 207 179 -370 C ATOM 1802 O GLN A 225 -16.908 -20.295 35.888 1.00 72.62 O ANISOU 1802 O GLN A 225 8856 9371 9366 220 187 -351 O ATOM 1803 CB GLN A 225 -18.996 -20.452 33.233 1.00 67.25 C ANISOU 1803 CB GLN A 225 8191 8717 8642 207 189 -460 C ATOM 1804 CG GLN A 225 -19.711 -21.383 32.265 1.00 76.33 C ANISOU 1804 CG GLN A 225 9337 9859 9807 211 196 -521 C ATOM 1805 CD GLN A 225 -19.065 -22.762 32.158 1.00 82.22 C ANISOU 1805 CD GLN A 225 10061 10571 10609 233 213 -554 C ATOM 1806 OE1 GLN A 225 -18.413 -23.238 33.090 1.00 82.89 O ANISOU 1806 OE1 GLN A 225 10137 10621 10735 244 216 -523 O ATOM 1807 NE2 GLN A 225 -19.258 -23.413 31.018 1.00 78.26 N ANISOU 1807 NE2 GLN A 225 9548 10078 10109 238 223 -617 N ATOM 1808 N LEU A 226 -18.661 -18.893 35.810 1.00 71.21 N ANISOU 1808 N LEU A 226 8710 9211 9136 188 165 -347 N ATOM 1809 CA LEU A 226 -17.960 -17.845 36.532 1.00 69.94 C ANISOU 1809 CA LEU A 226 8550 9072 8953 180 159 -304 C ATOM 1810 C LEU A 226 -17.295 -18.421 37.782 1.00 72.86 C ANISOU 1810 C LEU A 226 8907 9418 9356 189 159 -271 C ATOM 1811 O LEU A 226 -16.096 -18.219 38.005 1.00 73.26 O ANISOU 1811 O LEU A 226 8944 9487 9404 195 164 -251 O ATOM 1812 CB LEU A 226 -18.900 -16.690 36.876 1.00 63.91 C ANISOU 1812 CB LEU A 226 7806 8318 8161 158 144 -287 C ATOM 1813 CG LEU A 226 -18.173 -15.430 37.336 1.00 59.31 C ANISOU 1813 CG LEU A 226 7221 7762 7551 147 139 -254 C ATOM 1814 CD1 LEU A 226 -18.796 -14.190 36.732 1.00 58.16 C ANISOU 1814 CD1 LEU A 226 7087 7639 7371 131 132 -254 C ATOM 1815 CD2 LEU A 226 -18.122 -15.339 38.855 1.00 59.40 C ANISOU 1815 CD2 LEU A 226 7232 7759 7577 142 129 -220 C ATOM 1816 N VAL A 227 -18.071 -19.164 38.568 1.00 73.83 N ANISOU 1816 N VAL A 227 9032 9505 9512 189 154 -264 N ATOM 1817 CA VAL A 227 -17.574 -19.750 39.808 1.00 74.68 C ANISOU 1817 CA VAL A 227 9126 9596 9653 197 153 -226 C ATOM 1818 C VAL A 227 -16.468 -20.754 39.520 1.00 75.27 C ANISOU 1818 C VAL A 227 9177 9658 9764 220 169 -231 C ATOM 1819 O VAL A 227 -15.452 -20.779 40.205 1.00 75.30 O ANISOU 1819 O VAL A 227 9163 9671 9775 227 170 -198 O ATOM 1820 CB VAL A 227 -18.706 -20.405 40.629 1.00 73.59 C ANISOU 1820 CB VAL A 227 8991 9422 9546 193 146 -214 C ATOM 1821 CG1 VAL A 227 -18.144 -21.386 41.644 1.00 71.57 C ANISOU 1821 CG1 VAL A 227 8712 9144 9336 207 149 -178 C ATOM 1822 CG2 VAL A 227 -19.531 -19.336 41.327 1.00 75.11 C ANISOU 1822 CG2 VAL A 227 9202 9632 9704 172 130 -195 C ATOM 1823 N PHE A 228 -16.660 -21.558 38.482 1.00 77.46 N ANISOU 1823 N PHE A 228 9450 9917 10063 232 181 -276 N ATOM 1824 CA PHE A 228 -15.649 -22.530 38.074 1.00 77.35 C ANISOU 1824 CA PHE A 228 9412 9889 10086 255 198 -291 C ATOM 1825 C PHE A 228 -14.323 -21.837 37.719 1.00 73.51 C ANISOU 1825 C PHE A 228 8918 9446 9568 260 204 -282 C ATOM 1826 O PHE A 228 -13.292 -22.134 38.313 1.00 72.89 O ANISOU 1826 O PHE A 228 8819 9366 9509 272 209 -251 O ATOM 1827 CB PHE A 228 -16.171 -23.392 36.920 1.00 77.12 C ANISOU 1827 CB PHE A 228 9382 9839 10081 264 209 -352 C ATOM 1828 CG PHE A 228 -15.230 -24.487 36.508 1.00 88.18 C ANISOU 1828 CG PHE A 228 10755 11219 11529 289 229 -374 C ATOM 1829 CD1 PHE A 228 -14.935 -25.536 37.380 1.00 91.25 C ANISOU 1829 CD1 PHE A 228 11123 11562 11984 304 234 -346 C ATOM 1830 CD2 PHE A 228 -14.641 -24.473 35.242 1.00 87.96 C ANISOU 1830 CD2 PHE A 228 10720 11218 11481 298 243 -421 C ATOM 1831 CE1 PHE A 228 -14.066 -26.550 37.000 1.00 87.19 C ANISOU 1831 CE1 PHE A 228 10583 11025 11522 328 253 -366 C ATOM 1832 CE2 PHE A 228 -13.780 -25.480 34.853 1.00 81.74 C ANISOU 1832 CE2 PHE A 228 9906 10411 10740 322 263 -446 C ATOM 1833 CZ PHE A 228 -13.489 -26.522 35.733 1.00 88.45 C ANISOU 1833 CZ PHE A 228 10736 11210 11662 338 268 -419 C ATOM 1834 N THR A 229 -14.365 -20.890 36.787 1.00 70.64 N ANISOU 1834 N THR A 229 8566 9121 9153 249 203 -303 N ATOM 1835 CA THR A 229 -13.195 -20.073 36.465 1.00 68.41 C ANISOU 1835 CA THR A 229 8275 8882 8836 250 207 -290 C ATOM 1836 C THR A 229 -12.496 -19.484 37.694 1.00 71.18 C ANISOU 1836 C THR A 229 8621 9243 9182 243 198 -235 C ATOM 1837 O THR A 229 -11.279 -19.562 37.803 1.00 77.62 O ANISOU 1837 O THR A 229 9417 10073 10003 254 206 -218 O ATOM 1838 CB THR A 229 -13.551 -18.945 35.484 1.00 65.69 C ANISOU 1838 CB THR A 229 7944 8578 8437 234 203 -307 C ATOM 1839 OG1 THR A 229 -13.680 -19.490 34.171 1.00 67.72 O ANISOU 1839 OG1 THR A 229 8196 8845 8691 245 217 -358 O ATOM 1840 CG2 THR A 229 -12.480 -17.888 35.459 1.00 51.15 C ANISOU 1840 CG2 THR A 229 6095 6777 6561 229 203 -279 C ATOM 1841 N VAL A 230 -13.259 -18.896 38.611 1.00 71.69 N ANISOU 1841 N VAL A 230 8701 9304 9236 225 182 -210 N ATOM 1842 CA VAL A 230 -12.691 -18.228 39.788 1.00 69.91 C ANISOU 1842 CA VAL A 230 8468 9094 8998 215 171 -164 C ATOM 1843 C VAL A 230 -12.082 -19.242 40.768 1.00 71.94 C ANISOU 1843 C VAL A 230 8704 9333 9298 230 174 -134 C ATOM 1844 O VAL A 230 -11.030 -18.993 41.363 1.00 72.59 O ANISOU 1844 O VAL A 230 8769 9437 9376 232 174 -102 O ATOM 1845 CB VAL A 230 -13.757 -17.311 40.493 1.00 68.85 C ANISOU 1845 CB VAL A 230 8355 8964 8840 191 154 -152 C ATOM 1846 CG1 VAL A 230 -13.299 -16.852 41.882 1.00 59.38 C ANISOU 1846 CG1 VAL A 230 7147 7780 7636 181 143 -110 C ATOM 1847 CG2 VAL A 230 -14.076 -16.106 39.620 1.00 67.04 C ANISOU 1847 CG2 VAL A 230 8142 8760 8571 176 150 -170 C ATOM 1848 N LYS A 231 -12.750 -20.382 40.925 1.00 72.03 N ANISOU 1848 N LYS A 231 8713 9304 9353 241 178 -141 N ATOM 1849 CA LYS A 231 -12.304 -21.439 41.826 1.00 73.91 C ANISOU 1849 CA LYS A 231 8925 9518 9638 257 182 -107 C ATOM 1850 C LYS A 231 -10.998 -22.038 41.305 1.00 76.60 C ANISOU 1850 C LYS A 231 9242 9860 10003 280 199 -111 C ATOM 1851 O LYS A 231 -10.092 -22.376 42.080 1.00 78.42 O ANISOU 1851 O LYS A 231 9448 10095 10253 290 201 -70 O ATOM 1852 CB LYS A 231 -13.367 -22.542 41.901 1.00 74.46 C ANISOU 1852 CB LYS A 231 8997 9540 9756 264 184 -119 C ATOM 1853 CG LYS A 231 -14.566 -22.257 42.798 1.00 73.56 C ANISOU 1853 CG LYS A 231 8898 9421 9632 245 168 -99 C ATOM 1854 CD LYS A 231 -14.475 -23.044 44.092 1.00 82.73 C ANISOU 1854 CD LYS A 231 10036 10567 10832 252 165 -47 C ATOM 1855 CE LYS A 231 -15.831 -23.216 44.727 1.00 82.04 C ANISOU 1855 CE LYS A 231 9958 10461 10752 240 154 -37 C ATOM 1856 NZ LYS A 231 -16.306 -21.942 45.306 1.00 84.24 N ANISOU 1856 NZ LYS A 231 10255 10778 10973 217 138 -27 N ATOM 1857 N GLU A 232 -10.925 -22.166 39.983 1.00 74.57 N ANISOU 1857 N GLU A 232 8990 9602 9743 288 212 -160 N ATOM 1858 CA GLU A 232 -9.778 -22.725 39.303 1.00 76.33 C ANISOU 1858 CA GLU A 232 9189 9826 9985 310 230 -174 C ATOM 1859 C GLU A 232 -8.556 -21.809 39.370 1.00 77.59 C ANISOU 1859 C GLU A 232 9341 10034 10107 307 229 -149 C ATOM 1860 O GLU A 232 -7.438 -22.286 39.572 1.00 84.34 O ANISOU 1860 O GLU A 232 10169 10890 10986 324 239 -129 O ATOM 1861 CB GLU A 232 -10.134 -22.990 37.851 1.00 77.38 C ANISOU 1861 CB GLU A 232 9330 9956 10115 317 243 -238 C ATOM 1862 CG GLU A 232 -9.117 -23.809 37.104 1.00 88.69 C ANISOU 1862 CG GLU A 232 10737 11383 11579 343 265 -264 C ATOM 1863 CD GLU A 232 -9.698 -24.405 35.850 1.00100.79 C ANISOU 1863 CD GLU A 232 12271 12902 13121 350 278 -333 C ATOM 1864 OE1 GLU A 232 -10.588 -23.760 35.257 1.00109.43 O ANISOU 1864 OE1 GLU A 232 13389 14016 14173 333 269 -360 O ATOM 1865 OE2 GLU A 232 -9.277 -25.516 35.463 1.00107.01 O ANISOU 1865 OE2 GLU A 232 13037 13661 13961 373 296 -362 O ATOM 1866 N ALA A 233 -8.767 -20.507 39.176 1.00 73.76 N ANISOU 1866 N ALA A 233 8874 9584 9566 285 218 -150 N ATOM 1867 CA ALA A 233 -7.708 -19.510 39.310 1.00 69.42 C ANISOU 1867 CA ALA A 233 8317 9079 8981 277 214 -124 C ATOM 1868 C ALA A 233 -7.134 -19.429 40.732 1.00 71.73 C ANISOU 1868 C ALA A 233 8594 9379 9282 273 204 -71 C ATOM 1869 O ALA A 233 -5.977 -19.042 40.925 1.00 74.41 O ANISOU 1869 O ALA A 233 8915 9747 9609 274 205 -47 O ATOM 1870 CB ALA A 233 -8.207 -18.160 38.871 1.00 63.07 C ANISOU 1870 CB ALA A 233 7536 8304 8126 253 204 -134 C ATOM 1871 N ALA A 234 -7.938 -19.790 41.727 1.00 72.81 N ANISOU 1871 N ALA A 234 8735 9493 9436 267 194 -51 N ATOM 1872 CA ALA A 234 -7.513 -19.660 43.117 1.00 74.88 C ANISOU 1872 CA ALA A 234 8981 9772 9698 260 182 0 C ATOM 1873 C ALA A 234 -6.773 -20.907 43.587 1.00 76.69 C ANISOU 1873 C ALA A 234 9178 9983 9978 285 192 30 C ATOM 1874 O ALA A 234 -5.864 -20.817 44.416 1.00 77.99 O ANISOU 1874 O ALA A 234 9319 10174 10140 285 188 72 O ATOM 1875 CB ALA A 234 -8.700 -19.347 44.028 1.00 72.97 C ANISOU 1875 CB ALA A 234 8755 9525 9444 241 165 11 C ATOM 1876 N ALA A 235 -7.165 -22.066 43.056 1.00 76.43 N ANISOU 1876 N ALA A 235 9141 9904 9993 305 206 8 N ATOM 1877 CA ALA A 235 -6.438 -23.313 43.299 1.00 74.17 C ANISOU 1877 CA ALA A 235 8822 9593 9766 332 219 31 C ATOM 1878 C ALA A 235 -5.023 -23.204 42.735 1.00 75.76 C ANISOU 1878 C ALA A 235 9004 9819 9963 346 232 30 C ATOM 1879 O ALA A 235 -4.134 -23.981 43.098 1.00 79.00 O ANISOU 1879 O ALA A 235 9381 10220 10413 366 241 61 O ATOM 1880 CB ALA A 235 -7.167 -24.477 42.674 1.00 72.32 C ANISOU 1880 CB ALA A 235 8589 9303 9588 349 232 -4 C ATOM 1881 N GLN A 236 -4.823 -22.218 41.859 1.00 74.13 N ANISOU 1881 N GLN A 236 8815 9644 9708 335 232 -2 N ATOM 1882 CA GLN A 236 -3.524 -21.943 41.255 1.00 71.84 C ANISOU 1882 CA GLN A 236 8507 9382 9404 345 244 -4 C ATOM 1883 C GLN A 236 -2.796 -20.731 41.851 1.00 72.21 C ANISOU 1883 C GLN A 236 8552 9481 9404 324 229 30 C ATOM 1884 O GLN A 236 -1.743 -20.329 41.336 1.00 74.08 O ANISOU 1884 O GLN A 236 8777 9748 9624 329 237 30 O ATOM 1885 CB GLN A 236 -3.679 -21.765 39.746 1.00 72.08 C ANISOU 1885 CB GLN A 236 8553 9417 9418 349 257 -62 C ATOM 1886 CG GLN A 236 -3.798 -23.066 38.995 1.00 71.35 C ANISOU 1886 CG GLN A 236 8449 9283 9377 376 277 -101 C ATOM 1887 CD GLN A 236 -2.559 -23.913 39.143 1.00 73.70 C ANISOU 1887 CD GLN A 236 8709 9572 9719 403 293 -81 C ATOM 1888 OE1 GLN A 236 -1.437 -23.418 39.028 1.00 78.89 O ANISOU 1888 OE1 GLN A 236 9352 10267 10354 406 297 -63 O ATOM 1889 NE2 GLN A 236 -2.750 -25.195 39.425 1.00 74.36 N ANISOU 1889 NE2 GLN A 236 8776 9606 9872 424 303 -79 N ATOM 1890 N GLN A 237 -3.361 -20.146 42.910 1.00 69.50 N ANISOU 1890 N GLN A 237 8218 9149 9039 302 210 57 N ATOM 1891 CA GLN A 237 -2.709 -19.074 43.669 1.00 68.86 C ANISOU 1891 CA GLN A 237 8130 9114 8919 281 195 89 C ATOM 1892 C GLN A 237 -2.948 -19.216 45.161 1.00 71.03 C ANISOU 1892 C GLN A 237 8393 9398 9197 272 180 132 C ATOM 1893 O GLN A 237 -3.200 -18.223 45.849 1.00 72.60 O ANISOU 1893 O GLN A 237 8601 9626 9359 246 163 140 O ATOM 1894 CB GLN A 237 -3.256 -17.716 43.275 1.00 65.30 C ANISOU 1894 CB GLN A 237 7707 8683 8419 254 184 63 C ATOM 1895 CG GLN A 237 -2.798 -17.192 41.962 1.00 76.27 C ANISOU 1895 CG GLN A 237 9103 10086 9791 256 195 34 C ATOM 1896 CD GLN A 237 -2.772 -15.686 41.949 1.00 81.58 C ANISOU 1896 CD GLN A 237 9787 10790 10419 228 182 34 C ATOM 1897 OE1 GLN A 237 -2.305 -15.052 42.901 1.00 82.77 O ANISOU 1897 OE1 GLN A 237 9927 10967 10556 211 169 61 O ATOM 1898 NE2 GLN A 237 -3.278 -15.099 40.872 1.00 85.28 N ANISOU 1898 NE2 GLN A 237 10275 11259 10868 221 186 2 N ATOM 1899 N GLN A 238 -2.881 -20.435 45.676 1.00 70.36 N ANISOU 1899 N GLN A 238 8286 9288 9158 292 186 160 N ATOM 1900 CA GLN A 238 -3.220 -20.642 47.070 1.00 69.06 C ANISOU 1900 CA GLN A 238 8108 9136 8997 284 172 205 C ATOM 1901 C GLN A 238 -2.293 -19.887 48.019 1.00 71.60 C ANISOU 1901 C GLN A 238 8407 9514 9282 268 158 242 C ATOM 1902 O GLN A 238 -2.458 -19.957 49.240 1.00 76.48 O ANISOU 1902 O GLN A 238 9010 10157 9894 259 145 281 O ATOM 1903 CB GLN A 238 -3.227 -22.127 47.393 1.00 67.80 C ANISOU 1903 CB GLN A 238 7922 8938 8900 310 182 235 C ATOM 1904 CG GLN A 238 -3.951 -22.946 46.369 1.00 67.99 C ANISOU 1904 CG GLN A 238 7963 8904 8967 328 198 192 C ATOM 1905 CD GLN A 238 -4.389 -24.267 46.926 1.00 73.35 C ANISOU 1905 CD GLN A 238 8620 9541 9708 346 203 223 C ATOM 1906 OE1 GLN A 238 -3.658 -24.901 47.679 1.00 86.64 O ANISOU 1906 OE1 GLN A 238 10267 11230 11422 359 205 276 O ATOM 1907 NE2 GLN A 238 -5.589 -24.694 46.567 1.00 76.99 N ANISOU 1907 NE2 GLN A 238 9103 9959 10192 345 205 192 N ATOM 1908 N GLU A 239 -1.328 -19.155 47.467 1.00 72.79 N ANISOU 1908 N GLU A 239 8555 9692 9409 264 161 231 N ATOM 1909 CA GLU A 239 -0.391 -18.389 48.293 1.00 75.78 C ANISOU 1909 CA GLU A 239 8912 10127 9755 247 148 262 C ATOM 1910 C GLU A 239 -0.854 -16.951 48.497 1.00 78.56 C ANISOU 1910 C GLU A 239 9288 10506 10057 212 132 237 C ATOM 1911 O GLU A 239 -0.289 -16.227 49.312 1.00 81.41 O ANISOU 1911 O GLU A 239 9632 10913 10388 193 118 255 O ATOM 1912 CB GLU A 239 1.034 -18.427 47.717 1.00 74.79 C ANISOU 1912 CB GLU A 239 8763 10017 9636 261 160 270 C ATOM 1913 CG GLU A 239 1.320 -17.408 46.622 1.00 68.17 C ANISOU 1913 CG GLU A 239 7945 9187 8770 250 164 231 C ATOM 1914 CD GLU A 239 0.948 -17.911 45.235 1.00 71.03 C ANISOU 1914 CD GLU A 239 8326 9508 9154 270 183 190 C ATOM 1915 OE1 GLU A 239 0.400 -19.039 45.132 1.00 59.19 O ANISOU 1915 OE1 GLU A 239 6827 7968 7695 291 193 187 O ATOM 1916 OE2 GLU A 239 1.218 -17.179 44.249 1.00 68.67 O ANISOU 1916 OE2 GLU A 239 8039 9219 8833 264 188 162 O ATOM 1917 N SER A 240 -1.873 -16.541 47.744 1.00 81.39 N ANISOU 1917 N SER A 240 9682 10836 10408 205 133 194 N ATOM 1918 CA SER A 240 -2.496 -15.225 47.907 1.00 81.63 C ANISOU 1918 CA SER A 240 9734 10881 10399 174 119 169 C ATOM 1919 C SER A 240 -3.775 -15.345 48.726 1.00 81.21 C ANISOU 1919 C SER A 240 9695 10819 10343 164 108 169 C ATOM 1920 O SER A 240 -4.740 -15.962 48.263 1.00 80.12 O ANISOU 1920 O SER A 240 9575 10640 10225 175 115 153 O ATOM 1921 CB SER A 240 -2.826 -14.628 46.540 1.00 81.80 C ANISOU 1921 CB SER A 240 9784 10882 10415 172 127 127 C ATOM 1922 OG SER A 240 -3.715 -13.536 46.670 1.00 84.11 O ANISOU 1922 OG SER A 240 10101 11177 10682 146 115 104 O ATOM 1923 N ALA A 241 -3.778 -14.765 49.933 1.00 82.03 N ANISOU 1923 N ALA A 241 9786 10962 10419 142 92 185 N ATOM 1924 CA ALA A 241 -4.954 -14.812 50.835 1.00 80.76 C ANISOU 1924 CA ALA A 241 9633 10802 10249 131 82 186 C ATOM 1925 C ALA A 241 -6.112 -13.943 50.314 1.00 78.55 C ANISOU 1925 C ALA A 241 9391 10499 9955 114 78 141 C ATOM 1926 O ALA A 241 -7.274 -14.348 50.374 1.00 75.04 O ANISOU 1926 O ALA A 241 8963 10028 9520 117 78 134 O ATOM 1927 CB ALA A 241 -4.571 -14.428 52.266 1.00 78.16 C ANISOU 1927 CB ALA A 241 9275 10530 9890 112 66 213 C ATOM 1928 N THR A 242 -5.769 -12.758 49.806 1.00 76.47 N ANISOU 1928 N THR A 242 9136 10245 9672 97 76 115 N ATOM 1929 CA THR A 242 -6.619 -11.991 48.899 1.00 77.42 C ANISOU 1929 CA THR A 242 9289 10337 9788 88 78 77 C ATOM 1930 C THR A 242 -7.408 -12.900 47.959 1.00 78.04 C ANISOU 1930 C THR A 242 9389 10370 9892 109 90 65 C ATOM 1931 O THR A 242 -8.634 -12.953 48.034 1.00 81.32 O ANISOU 1931 O THR A 242 9825 10765 10309 105 87 50 O ATOM 1932 CB THR A 242 -5.761 -11.030 48.035 1.00 79.06 C ANISOU 1932 CB THR A 242 9497 10553 9989 80 81 63 C ATOM 1933 OG1 THR A 242 -5.181 -10.028 48.873 1.00 82.70 O ANISOU 1933 OG1 THR A 242 9942 11052 10429 55 69 65 O ATOM 1934 CG2 THR A 242 -6.583 -10.357 46.924 1.00 77.86 C ANISOU 1934 CG2 THR A 242 9375 10372 9836 74 86 31 C ATOM 1935 N THR A 243 -6.703 -13.601 47.071 1.00 75.84 N ANISOU 1935 N THR A 243 9104 10078 9633 131 104 68 N ATOM 1936 CA THR A 243 -7.338 -14.416 46.034 1.00 72.16 C ANISOU 1936 CA THR A 243 8655 9572 9191 151 117 48 C ATOM 1937 C THR A 243 -8.288 -15.467 46.615 1.00 71.17 C ANISOU 1937 C THR A 243 8532 9421 9089 161 116 57 C ATOM 1938 O THR A 243 -9.342 -15.729 46.041 1.00 70.81 O ANISOU 1938 O THR A 243 8508 9343 9053 164 119 33 O ATOM 1939 CB THR A 243 -6.284 -15.057 45.083 1.00 72.61 C ANISOU 1939 CB THR A 243 8698 9625 9266 174 133 49 C ATOM 1940 OG1 THR A 243 -5.616 -14.024 44.354 1.00 69.91 O ANISOU 1940 OG1 THR A 243 8357 9304 8901 164 135 37 O ATOM 1941 CG2 THR A 243 -6.922 -16.018 44.080 1.00 68.46 C ANISOU 1941 CG2 THR A 243 8185 9060 8767 195 147 23 C ATOM 1942 N GLN A 244 -7.930 -16.047 47.758 1.00 70.28 N ANISOU 1942 N GLN A 244 8394 9323 8985 165 111 95 N ATOM 1943 CA GLN A 244 -8.770 -17.072 48.371 1.00 73.72 C ANISOU 1943 CA GLN A 244 8826 9736 9446 174 110 113 C ATOM 1944 C GLN A 244 -10.051 -16.451 48.912 1.00 76.61 C ANISOU 1944 C GLN A 244 9213 10104 9790 153 98 100 C ATOM 1945 O GLN A 244 -11.112 -17.082 48.912 1.00 75.37 O ANISOU 1945 O GLN A 244 9067 9917 9653 158 99 95 O ATOM 1946 CB GLN A 244 -8.032 -17.795 49.501 1.00 72.09 C ANISOU 1946 CB GLN A 244 8583 9553 9254 183 108 165 C ATOM 1947 CG GLN A 244 -6.765 -18.504 49.083 1.00 71.30 C ANISOU 1947 CG GLN A 244 8459 9451 9183 206 121 183 C ATOM 1948 CD GLN A 244 -6.875 -19.181 47.731 1.00 67.40 C ANISOU 1948 CD GLN A 244 7977 8908 8723 227 138 151 C ATOM 1949 OE1 GLN A 244 -7.649 -20.124 47.551 1.00 70.21 O ANISOU 1949 OE1 GLN A 244 8338 9223 9116 240 144 146 O ATOM 1950 NE2 GLN A 244 -6.081 -18.712 46.773 1.00 64.61 N ANISOU 1950 NE2 GLN A 244 7628 8563 8358 230 146 128 N ATOM 1951 N LYS A 245 -9.917 -15.210 49.379 1.00 80.19 N ANISOU 1951 N LYS A 245 9669 10594 10206 129 86 92 N ATOM 1952 CA LYS A 245 -10.999 -14.435 49.979 1.00 81.37 C ANISOU 1952 CA LYS A 245 9834 10751 10330 108 75 77 C ATOM 1953 C LYS A 245 -11.997 -14.029 48.892 1.00 81.39 C ANISOU 1953 C LYS A 245 9871 10718 10335 105 79 38 C ATOM 1954 O LYS A 245 -13.191 -14.343 48.981 1.00 84.51 O ANISOU 1954 O LYS A 245 10281 11091 10737 104 77 30 O ATOM 1955 CB LYS A 245 -10.417 -13.193 50.665 1.00 80.35 C ANISOU 1955 CB LYS A 245 9695 10668 10167 84 64 74 C ATOM 1956 CG LYS A 245 -11.227 -12.666 51.826 1.00 92.40 C ANISOU 1956 CG LYS A 245 11220 12220 11669 64 51 71 C ATOM 1957 CD LYS A 245 -11.114 -11.143 51.951 1.00103.45 C ANISOU 1957 CD LYS A 245 12624 13642 13041 37 43 41 C ATOM 1958 CE LYS A 245 -12.422 -10.548 52.493 1.00106.92 C ANISOU 1958 CE LYS A 245 13079 14080 13466 21 36 17 C ATOM 1959 NZ LYS A 245 -12.485 -9.063 52.383 1.00105.95 N ANISOU 1959 NZ LYS A 245 12965 13963 13330 -3 31 -19 N ATOM 1960 N ALA A 246 -11.495 -13.353 47.859 1.00 78.07 N ANISOU 1960 N ALA A 246 9460 10295 9908 103 84 16 N ATOM 1961 CA ALA A 246 -12.298 -12.991 46.692 1.00 77.27 C ANISOU 1961 CA ALA A 246 9386 10166 9807 101 89 -17 C ATOM 1962 C ALA A 246 -13.095 -14.179 46.136 1.00 78.89 C ANISOU 1962 C ALA A 246 9602 10334 10040 120 97 -25 C ATOM 1963 O ALA A 246 -14.236 -14.025 45.692 1.00 79.06 O ANISOU 1963 O ALA A 246 9645 10334 10060 115 95 -47 O ATOM 1964 CB ALA A 246 -11.413 -12.386 45.609 1.00 73.48 C ANISOU 1964 CB ALA A 246 8906 9694 9321 102 96 -28 C ATOM 1965 N GLU A 247 -12.489 -15.362 46.169 1.00 79.36 N ANISOU 1965 N GLU A 247 9643 10383 10127 141 105 -7 N ATOM 1966 CA GLU A 247 -13.117 -16.558 45.633 1.00 78.95 C ANISOU 1966 CA GLU A 247 9596 10292 10109 159 114 -17 C ATOM 1967 C GLU A 247 -14.317 -16.967 46.493 1.00 79.13 C ANISOU 1967 C GLU A 247 9624 10300 10141 153 106 -6 C ATOM 1968 O GLU A 247 -15.397 -17.264 45.971 1.00 78.76 O ANISOU 1968 O GLU A 247 9596 10224 10105 154 107 -29 O ATOM 1969 CB GLU A 247 -12.084 -17.684 45.517 1.00 78.30 C ANISOU 1969 CB GLU A 247 9489 10201 10060 183 126 1 C ATOM 1970 CG GLU A 247 -12.645 -19.033 45.109 1.00 81.77 C ANISOU 1970 CG GLU A 247 9928 10596 10547 202 136 -9 C ATOM 1971 CD GLU A 247 -13.130 -19.843 46.302 1.00 90.80 C ANISOU 1971 CD GLU A 247 11056 11726 11717 205 131 28 C ATOM 1972 OE1 GLU A 247 -12.465 -19.803 47.365 1.00 93.28 O ANISOU 1972 OE1 GLU A 247 11348 12070 12026 203 125 70 O ATOM 1973 OE2 GLU A 247 -14.174 -20.520 46.175 1.00 92.91 O ANISOU 1973 OE2 GLU A 247 11332 11959 12011 209 132 17 O ATOM 1974 N LYS A 248 -14.128 -16.963 47.810 1.00 78.75 N ANISOU 1974 N LYS A 248 9558 10276 10086 147 97 29 N ATOM 1975 CA LYS A 248 -15.219 -17.239 48.743 1.00 78.24 C ANISOU 1975 CA LYS A 248 9494 10208 10024 140 89 44 C ATOM 1976 C LYS A 248 -16.329 -16.181 48.631 1.00 76.61 C ANISOU 1976 C LYS A 248 9316 10004 9789 120 81 14 C ATOM 1977 O LYS A 248 -17.514 -16.516 48.554 1.00 74.27 O ANISOU 1977 O LYS A 248 9033 9683 9504 119 80 5 O ATOM 1978 CB LYS A 248 -14.696 -17.360 50.182 1.00 76.98 C ANISOU 1978 CB LYS A 248 9305 10087 9855 137 81 89 C ATOM 1979 CG LYS A 248 -13.748 -18.549 50.402 1.00 87.35 C ANISOU 1979 CG LYS A 248 10588 11396 11206 159 89 128 C ATOM 1980 CD LYS A 248 -13.728 -19.048 51.851 1.00 99.14 C ANISOU 1980 CD LYS A 248 12050 12919 12699 158 82 181 C ATOM 1981 CE LYS A 248 -14.921 -19.960 52.153 1.00110.41 C ANISOU 1981 CE LYS A 248 13478 14315 14158 163 82 196 C ATOM 1982 NZ LYS A 248 -15.083 -20.254 53.610 1.00112.66 N ANISOU 1982 NZ LYS A 248 13733 14638 14433 158 73 248 N ATOM 1983 N GLU A 249 -15.939 -14.909 48.592 1.00 73.97 N ANISOU 1983 N GLU A 249 8987 9696 9422 104 76 0 N ATOM 1984 CA GLU A 249 -16.898 -13.828 48.431 1.00 74.54 C ANISOU 1984 CA GLU A 249 9082 9769 9473 85 70 -28 C ATOM 1985 C GLU A 249 -17.699 -13.957 47.123 1.00 71.44 C ANISOU 1985 C GLU A 249 8714 9340 9092 91 76 -57 C ATOM 1986 O GLU A 249 -18.919 -13.833 47.124 1.00 72.22 O ANISOU 1986 O GLU A 249 8828 9423 9189 84 72 -69 O ATOM 1987 CB GLU A 249 -16.197 -12.464 48.565 1.00 76.67 C ANISOU 1987 CB GLU A 249 9348 10068 9714 68 64 -37 C ATOM 1988 CG GLU A 249 -17.011 -11.234 48.111 1.00 95.55 C ANISOU 1988 CG GLU A 249 11761 12452 12091 51 61 -67 C ATOM 1989 CD GLU A 249 -18.128 -10.808 49.084 1.00113.21 C ANISOU 1989 CD GLU A 249 14003 14695 14316 36 52 -72 C ATOM 1990 OE1 GLU A 249 -18.634 -11.657 49.857 1.00119.44 O ANISOU 1990 OE1 GLU A 249 14785 15486 15110 42 50 -55 O ATOM 1991 OE2 GLU A 249 -18.516 -9.615 49.056 1.00113.72 O ANISOU 1991 OE2 GLU A 249 14076 14762 14369 19 48 -94 O ATOM 1992 N VAL A 250 -17.021 -14.234 46.015 1.00 71.19 N ANISOU 1992 N VAL A 250 8682 9298 9069 103 86 -68 N ATOM 1993 CA VAL A 250 -17.702 -14.408 44.730 1.00 67.26 C ANISOU 1993 CA VAL A 250 8203 8775 8579 109 92 -97 C ATOM 1994 C VAL A 250 -18.664 -15.590 44.753 1.00 68.46 C ANISOU 1994 C VAL A 250 8359 8894 8758 119 94 -100 C ATOM 1995 O VAL A 250 -19.689 -15.588 44.068 1.00 67.46 O ANISOU 1995 O VAL A 250 8250 8749 8633 116 94 -124 O ATOM 1996 CB VAL A 250 -16.703 -14.580 43.565 1.00 66.55 C ANISOU 1996 CB VAL A 250 8107 8687 8491 122 104 -109 C ATOM 1997 CG1 VAL A 250 -17.350 -15.308 42.389 1.00 59.63 C ANISOU 1997 CG1 VAL A 250 7242 7786 7629 133 112 -139 C ATOM 1998 CG2 VAL A 250 -16.162 -13.226 43.129 1.00 61.10 C ANISOU 1998 CG2 VAL A 250 7419 8023 7772 108 102 -114 C ATOM 1999 N THR A 251 -18.336 -16.600 45.546 1.00 69.59 N ANISOU 1999 N THR A 251 8483 9030 8927 130 96 -74 N ATOM 2000 CA THR A 251 -19.166 -17.792 45.592 1.00 69.89 C ANISOU 2000 CA THR A 251 8521 9033 9001 140 98 -73 C ATOM 2001 C THR A 251 -20.414 -17.555 46.430 1.00 71.54 C ANISOU 2001 C THR A 251 8738 9241 9202 126 88 -64 C ATOM 2002 O THR A 251 -21.512 -17.921 46.011 1.00 74.36 O ANISOU 2002 O THR A 251 9109 9572 9573 126 87 -82 O ATOM 2003 CB THR A 251 -18.384 -19.029 46.066 1.00 67.82 C ANISOU 2003 CB THR A 251 8231 8758 8779 159 105 -44 C ATOM 2004 OG1 THR A 251 -17.194 -19.152 45.284 1.00 70.18 O ANISOU 2004 OG1 THR A 251 8522 9062 9083 172 116 -54 O ATOM 2005 CG2 THR A 251 -19.209 -20.279 45.886 1.00 61.32 C ANISOU 2005 CG2 THR A 251 7407 7891 8003 170 110 -48 C ATOM 2006 N ARG A 252 -20.255 -16.924 47.594 1.00 73.31 N ANISOU 2006 N ARG A 252 8954 9498 9402 115 79 -39 N ATOM 2007 CA ARG A 252 -21.406 -16.619 48.441 1.00 73.98 C ANISOU 2007 CA ARG A 252 9045 9590 9475 101 70 -33 C ATOM 2008 C ARG A 252 -22.367 -15.696 47.697 1.00 73.11 C ANISOU 2008 C ARG A 252 8962 9471 9346 89 67 -68 C ATOM 2009 O ARG A 252 -23.577 -15.938 47.683 1.00 74.43 O ANISOU 2009 O ARG A 252 9140 9619 9521 86 64 -75 O ATOM 2010 CB ARG A 252 -20.995 -16.026 49.794 1.00 74.38 C ANISOU 2010 CB ARG A 252 9078 9684 9498 90 61 -6 C ATOM 2011 CG ARG A 252 -22.019 -16.304 50.921 1.00 86.18 C ANISOU 2011 CG ARG A 252 10566 11188 10991 84 54 15 C ATOM 2012 CD ARG A 252 -21.648 -15.638 52.260 1.00101.31 C ANISOU 2012 CD ARG A 252 12463 13158 12872 71 46 34 C ATOM 2013 NE ARG A 252 -21.341 -14.209 52.117 1.00114.12 N ANISOU 2013 NE ARG A 252 14095 14803 14462 54 42 4 N ATOM 2014 CZ ARG A 252 -22.101 -13.202 52.557 1.00116.16 C ANISOU 2014 CZ ARG A 252 14363 15078 14696 37 37 -17 C ATOM 2015 NH1 ARG A 252 -23.247 -13.430 53.197 1.00117.81 N ANISOU 2015 NH1 ARG A 252 14572 15288 14902 34 33 -11 N ATOM 2016 NH2 ARG A 252 -21.705 -11.950 52.358 1.00110.32 N ANISOU 2016 NH2 ARG A 252 13629 14350 13936 24 35 -44 N ATOM 2017 N MET A 253 -21.826 -14.676 47.039 1.00 69.86 N ANISOU 2017 N MET A 253 8558 9072 8912 82 68 -87 N ATOM 2018 CA MET A 253 -22.650 -13.789 46.230 1.00 71.62 C ANISOU 2018 CA MET A 253 8804 9288 9121 72 66 -116 C ATOM 2019 C MET A 253 -23.482 -14.506 45.170 1.00 70.60 C ANISOU 2019 C MET A 253 8688 9128 9010 80 70 -136 C ATOM 2020 O MET A 253 -24.691 -14.288 45.081 1.00 72.62 O ANISOU 2020 O MET A 253 8957 9373 9263 72 66 -147 O ATOM 2021 CB MET A 253 -21.826 -12.657 45.614 1.00 71.66 C ANISOU 2021 CB MET A 253 8810 9311 9105 65 67 -127 C ATOM 2022 CG MET A 253 -21.553 -11.536 46.604 1.00 81.12 C ANISOU 2022 CG MET A 253 10001 10536 10283 49 60 -120 C ATOM 2023 SD MET A 253 -23.055 -10.987 47.459 1.00 91.50 S ANISOU 2023 SD MET A 253 11327 11850 11590 34 52 -126 S ATOM 2024 CE MET A 253 -23.885 -10.118 46.119 1.00 83.59 C ANISOU 2024 CE MET A 253 10346 10828 10586 28 53 -152 C ATOM 2025 N VAL A 254 -22.854 -15.366 44.377 1.00 69.67 N ANISOU 2025 N VAL A 254 8564 8997 8911 95 79 -144 N ATOM 2026 CA VAL A 254 -23.599 -16.077 43.342 1.00 69.70 C ANISOU 2026 CA VAL A 254 8577 8974 8931 102 84 -170 C ATOM 2027 C VAL A 254 -24.728 -16.908 43.964 1.00 68.45 C ANISOU 2027 C VAL A 254 8419 8790 8797 102 80 -162 C ATOM 2028 O VAL A 254 -25.848 -16.924 43.456 1.00 70.17 O ANISOU 2028 O VAL A 254 8651 8994 9016 96 77 -182 O ATOM 2029 CB VAL A 254 -22.679 -16.905 42.388 1.00 70.99 C ANISOU 2029 CB VAL A 254 8731 9130 9113 119 96 -186 C ATOM 2030 CG1 VAL A 254 -23.492 -17.865 41.518 1.00 68.92 C ANISOU 2030 CG1 VAL A 254 8474 8839 8875 126 100 -216 C ATOM 2031 CG2 VAL A 254 -21.880 -15.970 41.499 1.00 68.82 C ANISOU 2031 CG2 VAL A 254 8457 8882 8808 117 100 -198 C ATOM 2032 N ILE A 255 -24.452 -17.556 45.087 1.00 65.95 N ANISOU 2032 N ILE A 255 8086 8471 8500 107 79 -130 N ATOM 2033 CA ILE A 255 -25.481 -18.344 45.749 1.00 65.87 C ANISOU 2033 CA ILE A 255 8073 8439 8515 106 75 -116 C ATOM 2034 C ILE A 255 -26.650 -17.464 46.222 1.00 66.31 C ANISOU 2034 C ILE A 255 8143 8508 8545 89 65 -117 C ATOM 2035 O ILE A 255 -27.818 -17.809 46.018 1.00 67.89 O ANISOU 2035 O ILE A 255 8352 8686 8756 86 63 -127 O ATOM 2036 CB ILE A 255 -24.895 -19.223 46.875 1.00 66.54 C ANISOU 2036 CB ILE A 255 8132 8524 8627 116 76 -74 C ATOM 2037 CG1 ILE A 255 -23.845 -20.175 46.284 1.00 66.22 C ANISOU 2037 CG1 ILE A 255 8077 8464 8621 135 87 -76 C ATOM 2038 CG2 ILE A 255 -26.004 -20.011 47.578 1.00 65.19 C ANISOU 2038 CG2 ILE A 255 7955 8333 8483 115 72 -53 C ATOM 2039 CD1 ILE A 255 -23.225 -21.141 47.261 1.00 62.75 C ANISOU 2039 CD1 ILE A 255 7607 8019 8216 147 90 -31 C ATOM 2040 N ILE A 256 -26.333 -16.309 46.805 1.00 64.06 N ANISOU 2040 N ILE A 256 7859 8255 8225 78 60 -109 N ATOM 2041 CA ILE A 256 -27.349 -15.314 47.136 1.00 58.31 C ANISOU 2041 CA ILE A 256 7144 7538 7472 63 53 -117 C ATOM 2042 C ILE A 256 -28.116 -14.863 45.889 1.00 60.00 C ANISOU 2042 C ILE A 256 7379 7738 7682 59 53 -149 C ATOM 2043 O ILE A 256 -29.347 -14.837 45.899 1.00 62.59 O ANISOU 2043 O ILE A 256 7716 8054 8010 52 49 -155 O ATOM 2044 CB ILE A 256 -26.749 -14.103 47.895 1.00 59.11 C ANISOU 2044 CB ILE A 256 7241 7676 7543 52 49 -111 C ATOM 2045 CG1 ILE A 256 -26.365 -14.513 49.323 1.00 50.79 C ANISOU 2045 CG1 ILE A 256 6164 6646 6487 52 46 -78 C ATOM 2046 CG2 ILE A 256 -27.722 -12.912 47.925 1.00 52.58 C ANISOU 2046 CG2 ILE A 256 6428 6855 6696 36 44 -129 C ATOM 2047 CD1 ILE A 256 -25.239 -13.668 49.915 1.00 41.00 C ANISOU 2047 CD1 ILE A 256 4912 5443 5222 45 44 -74 C ATOM 2048 N MET A 257 -27.410 -14.541 44.807 1.00 57.92 N ANISOU 2048 N MET A 257 7120 7477 7411 62 58 -167 N ATOM 2049 CA MET A 257 -28.090 -14.056 43.599 1.00 58.72 C ANISOU 2049 CA MET A 257 7237 7573 7502 57 58 -192 C ATOM 2050 C MET A 257 -29.040 -15.071 42.983 1.00 59.67 C ANISOU 2050 C MET A 257 7361 7667 7642 62 59 -208 C ATOM 2051 O MET A 257 -30.140 -14.719 42.542 1.00 59.37 O ANISOU 2051 O MET A 257 7335 7626 7598 54 55 -221 O ATOM 2052 CB MET A 257 -27.097 -13.559 42.557 1.00 54.57 C ANISOU 2052 CB MET A 257 6710 7063 6962 61 64 -204 C ATOM 2053 CG MET A 257 -26.466 -12.271 42.983 1.00 60.75 C ANISOU 2053 CG MET A 257 7490 7868 7725 51 62 -193 C ATOM 2054 SD MET A 257 -25.238 -11.630 41.861 1.00 77.45 S ANISOU 2054 SD MET A 257 9600 10003 9825 53 69 -199 S ATOM 2055 CE MET A 257 -24.261 -13.083 41.494 1.00 76.14 C ANISOU 2055 CE MET A 257 9423 9831 9677 73 78 -203 C ATOM 2056 N VAL A 258 -28.611 -16.329 42.975 1.00 60.67 N ANISOU 2056 N VAL A 258 7477 7775 7799 75 65 -208 N ATOM 2057 CA VAL A 258 -29.349 -17.389 42.318 1.00 61.56 C ANISOU 2057 CA VAL A 258 7592 7861 7939 80 66 -229 C ATOM 2058 C VAL A 258 -30.596 -17.711 43.139 1.00 63.78 C ANISOU 2058 C VAL A 258 7875 8125 8234 73 59 -214 C ATOM 2059 O VAL A 258 -31.713 -17.654 42.609 1.00 67.37 O ANISOU 2059 O VAL A 258 8340 8572 8687 65 55 -232 O ATOM 2060 CB VAL A 258 -28.437 -18.621 42.026 1.00 61.60 C ANISOU 2060 CB VAL A 258 7580 7846 7978 96 76 -236 C ATOM 2061 CG1 VAL A 258 -29.247 -19.865 41.683 1.00 61.88 C ANISOU 2061 CG1 VAL A 258 7613 7846 8055 100 78 -254 C ATOM 2062 CG2 VAL A 258 -27.483 -18.294 40.886 1.00 58.41 C ANISOU 2062 CG2 VAL A 258 7177 7461 7556 102 84 -260 C ATOM 2063 N ILE A 259 -30.410 -17.998 44.429 1.00 60.41 N ANISOU 2063 N ILE A 259 7436 7699 7819 74 58 -180 N ATOM 2064 CA ILE A 259 -31.527 -18.135 45.371 1.00 59.52 C ANISOU 2064 CA ILE A 259 7322 7581 7713 67 51 -160 C ATOM 2065 C ILE A 259 -32.526 -16.961 45.316 1.00 60.66 C ANISOU 2065 C ILE A 259 7483 7741 7825 52 44 -170 C ATOM 2066 O ILE A 259 -33.740 -17.166 45.270 1.00 61.90 O ANISOU 2066 O ILE A 259 7646 7884 7990 47 40 -174 O ATOM 2067 CB ILE A 259 -31.010 -18.269 46.802 1.00 60.37 C ANISOU 2067 CB ILE A 259 7412 7704 7822 69 50 -119 C ATOM 2068 CG1 ILE A 259 -30.457 -19.679 47.019 1.00 63.59 C ANISOU 2068 CG1 ILE A 259 7799 8087 8276 83 55 -99 C ATOM 2069 CG2 ILE A 259 -32.107 -17.904 47.816 1.00 53.88 C ANISOU 2069 CG2 ILE A 259 6590 6894 6987 58 42 -100 C ATOM 2070 CD1 ILE A 259 -29.614 -19.827 48.282 1.00 69.77 C ANISOU 2070 CD1 ILE A 259 8559 8893 9057 87 55 -55 C ATOM 2071 N ALA A 260 -32.012 -15.736 45.320 1.00 59.33 N ANISOU 2071 N ALA A 260 7320 7598 7624 47 43 -173 N ATOM 2072 CA ALA A 260 -32.852 -14.550 45.188 1.00 58.05 C ANISOU 2072 CA ALA A 260 7171 7448 7437 34 39 -182 C ATOM 2073 C ALA A 260 -33.726 -14.535 43.918 1.00 58.83 C ANISOU 2073 C ALA A 260 7282 7534 7536 32 38 -207 C ATOM 2074 O ALA A 260 -34.885 -14.126 43.974 1.00 60.46 O ANISOU 2074 O ALA A 260 7495 7739 7737 23 33 -209 O ATOM 2075 CB ALA A 260 -32.001 -13.297 45.263 1.00 57.50 C ANISOU 2075 CB ALA A 260 7102 7403 7342 30 40 -183 C ATOM 2076 N PHE A 261 -33.172 -14.969 42.785 1.00 56.84 N ANISOU 2076 N PHE A 261 7030 7277 7288 39 42 -227 N ATOM 2077 CA PHE A 261 -33.931 -15.064 41.536 1.00 56.64 C ANISOU 2077 CA PHE A 261 7012 7248 7260 36 41 -252 C ATOM 2078 C PHE A 261 -35.037 -16.110 41.660 1.00 60.39 C ANISOU 2078 C PHE A 261 7486 7697 7761 35 38 -258 C ATOM 2079 O PHE A 261 -36.167 -15.909 41.182 1.00 60.21 O ANISOU 2079 O PHE A 261 7471 7673 7732 27 33 -269 O ATOM 2080 CB PHE A 261 -33.005 -15.448 40.382 1.00 57.52 C ANISOU 2080 CB PHE A 261 7119 7365 7369 44 48 -275 C ATOM 2081 CG PHE A 261 -33.636 -15.342 39.021 1.00 50.82 C ANISOU 2081 CG PHE A 261 6275 6527 6506 40 47 -302 C ATOM 2082 CD1 PHE A 261 -33.663 -14.124 38.344 1.00 57.90 C ANISOU 2082 CD1 PHE A 261 7176 7452 7372 33 46 -300 C ATOM 2083 CD2 PHE A 261 -34.160 -16.469 38.393 1.00 53.42 C ANISOU 2083 CD2 PHE A 261 6602 6840 6856 42 48 -330 C ATOM 2084 CE1 PHE A 261 -34.225 -14.024 37.061 1.00 59.28 C ANISOU 2084 CE1 PHE A 261 7351 7645 7529 29 44 -321 C ATOM 2085 CE2 PHE A 261 -34.731 -16.387 37.115 1.00 50.04 C ANISOU 2085 CE2 PHE A 261 6175 6430 6410 37 46 -358 C ATOM 2086 CZ PHE A 261 -34.757 -15.166 36.444 1.00 51.10 C ANISOU 2086 CZ PHE A 261 6312 6599 6507 31 44 -352 C ATOM 2087 N LEU A 262 -34.712 -17.233 42.295 1.00 57.86 N ANISOU 2087 N LEU A 262 7155 7356 7473 43 41 -248 N ATOM 2088 CA LEU A 262 -35.707 -18.260 42.507 1.00 57.56 C ANISOU 2088 CA LEU A 262 7113 7289 7467 41 38 -248 C ATOM 2089 C LEU A 262 -36.838 -17.738 43.387 1.00 59.88 C ANISOU 2089 C LEU A 262 7412 7588 7752 31 30 -226 C ATOM 2090 O LEU A 262 -38.008 -17.789 42.989 1.00 61.60 O ANISOU 2090 O LEU A 262 7635 7798 7972 23 25 -238 O ATOM 2091 CB LEU A 262 -35.075 -19.516 43.090 1.00 58.14 C ANISOU 2091 CB LEU A 262 7170 7337 7583 53 43 -233 C ATOM 2092 CG LEU A 262 -34.250 -20.349 42.105 1.00 60.13 C ANISOU 2092 CG LEU A 262 7415 7574 7858 63 51 -263 C ATOM 2093 CD1 LEU A 262 -33.742 -21.627 42.776 1.00 52.85 C ANISOU 2093 CD1 LEU A 262 6473 6621 6988 75 57 -243 C ATOM 2094 CD2 LEU A 262 -35.054 -20.659 40.830 1.00 53.62 C ANISOU 2094 CD2 LEU A 262 6596 6741 7036 58 50 -307 C ATOM 2095 N ILE A 263 -36.492 -17.204 44.561 1.00 58.74 N ANISOU 2095 N ILE A 263 7263 7460 7595 31 30 -197 N ATOM 2096 CA ILE A 263 -37.483 -16.592 45.441 1.00 58.03 C ANISOU 2096 CA ILE A 263 7175 7381 7492 21 24 -180 C ATOM 2097 C ILE A 263 -38.385 -15.593 44.678 1.00 57.67 C ANISOU 2097 C ILE A 263 7145 7344 7424 12 21 -200 C ATOM 2098 O ILE A 263 -39.596 -15.528 44.883 1.00 56.81 O ANISOU 2098 O ILE A 263 7037 7230 7316 5 16 -197 O ATOM 2099 CB ILE A 263 -36.823 -15.918 46.664 1.00 58.42 C ANISOU 2099 CB ILE A 263 7218 7458 7523 21 25 -157 C ATOM 2100 CG1 ILE A 263 -36.199 -16.976 47.587 1.00 64.44 C ANISOU 2100 CG1 ILE A 263 7960 8216 8307 29 28 -127 C ATOM 2101 CG2 ILE A 263 -37.856 -15.130 47.456 1.00 61.42 C ANISOU 2101 CG2 ILE A 263 7599 7853 7884 11 21 -148 C ATOM 2102 CD1 ILE A 263 -35.472 -16.415 48.845 1.00 50.06 C ANISOU 2102 CD1 ILE A 263 6127 6430 6463 28 28 -103 C ATOM 2103 N CYS A 264 -37.802 -14.837 43.768 1.00 55.82 N ANISOU 2103 N CYS A 264 6917 7122 7169 12 23 -217 N ATOM 2104 CA CYS A 264 -38.573 -13.824 43.095 1.00 55.87 C ANISOU 2104 CA CYS A 264 6933 7139 7157 4 19 -227 C ATOM 2105 C CYS A 264 -39.575 -14.360 42.070 1.00 58.76 C ANISOU 2105 C CYS A 264 7303 7494 7530 1 16 -246 C ATOM 2106 O CYS A 264 -40.713 -13.896 42.027 1.00 62.58 O ANISOU 2106 O CYS A 264 7791 7980 8008 -7 11 -244 O ATOM 2107 CB CYS A 264 -37.660 -12.796 42.454 1.00 53.69 C ANISOU 2107 CB CYS A 264 6659 6881 6859 4 23 -233 C ATOM 2108 SG CYS A 264 -38.596 -11.523 41.642 1.00 57.82 S ANISOU 2108 SG CYS A 264 7188 7416 7363 -5 19 -237 S ATOM 2109 N TRP A 265 -39.167 -15.316 41.236 1.00 59.98 N ANISOU 2109 N TRP A 265 7454 7639 7697 6 18 -266 N ATOM 2110 CA TRP A 265 -40.036 -15.772 40.140 1.00 57.83 C ANISOU 2110 CA TRP A 265 7183 7364 7427 1 14 -291 C ATOM 2111 C TRP A 265 -40.551 -17.211 40.241 1.00 59.10 C ANISOU 2111 C TRP A 265 7337 7495 7625 1 13 -302 C ATOM 2112 O TRP A 265 -41.483 -17.574 39.533 1.00 57.86 O ANISOU 2112 O TRP A 265 7179 7333 7472 -5 8 -322 O ATOM 2113 CB TRP A 265 -39.359 -15.572 38.792 1.00 57.70 C ANISOU 2113 CB TRP A 265 7165 7368 7390 3 17 -316 C ATOM 2114 CG TRP A 265 -38.947 -14.164 38.535 1.00 59.66 C ANISOU 2114 CG TRP A 265 7417 7644 7607 1 18 -302 C ATOM 2115 CD1 TRP A 265 -37.675 -13.677 38.513 1.00 51.68 C ANISOU 2115 CD1 TRP A 265 6404 6647 6585 7 24 -296 C ATOM 2116 CD2 TRP A 265 -39.808 -13.056 38.240 1.00 62.06 C ANISOU 2116 CD2 TRP A 265 7725 7965 7892 -7 13 -292 C ATOM 2117 NE1 TRP A 265 -37.686 -12.337 38.219 1.00 53.70 N ANISOU 2117 NE1 TRP A 265 6662 6924 6818 2 24 -283 N ATOM 2118 CE2 TRP A 265 -38.983 -11.928 38.048 1.00 59.06 C ANISOU 2118 CE2 TRP A 265 7343 7604 7492 -6 17 -279 C ATOM 2119 CE3 TRP A 265 -41.197 -12.910 38.107 1.00 59.74 C ANISOU 2119 CE3 TRP A 265 7432 7669 7597 -16 6 -290 C ATOM 2120 CZ2 TRP A 265 -39.500 -10.663 37.746 1.00 57.87 C ANISOU 2120 CZ2 TRP A 265 7193 7469 7328 -13 15 -263 C ATOM 2121 CZ3 TRP A 265 -41.711 -11.657 37.797 1.00 50.23 C ANISOU 2121 CZ3 TRP A 265 6228 6483 6375 -22 4 -274 C ATOM 2122 CH2 TRP A 265 -40.863 -10.550 37.623 1.00 58.28 C ANISOU 2122 CH2 TRP A 265 7245 7518 7380 -20 8 -261 C ATOM 2123 N LEU A 266 -39.963 -18.033 41.108 1.00 61.77 N ANISOU 2123 N LEU A 266 7666 7811 7992 9 17 -287 N ATOM 2124 CA LEU A 266 -40.412 -19.424 41.225 1.00 63.72 C ANISOU 2124 CA LEU A 266 7903 8024 8284 10 16 -294 C ATOM 2125 C LEU A 266 -41.913 -19.541 41.542 1.00 66.03 C ANISOU 2125 C LEU A 266 8196 8306 8585 -1 8 -286 C ATOM 2126 O LEU A 266 -42.592 -20.385 40.961 1.00 70.70 O ANISOU 2126 O LEU A 266 8782 8878 9202 -6 5 -308 O ATOM 2127 CB LEU A 266 -39.572 -20.230 42.229 1.00 61.27 C ANISOU 2127 CB LEU A 266 7580 7693 8007 21 22 -269 C ATOM 2128 CG LEU A 266 -39.877 -21.734 42.272 1.00 57.94 C ANISOU 2128 CG LEU A 266 7143 7229 7642 23 24 -274 C ATOM 2129 CD1 LEU A 266 -39.729 -22.361 40.888 1.00 54.22 C ANISOU 2129 CD1 LEU A 266 6670 6746 7186 24 27 -326 C ATOM 2130 CD2 LEU A 266 -39.010 -22.473 43.301 1.00 52.89 C ANISOU 2130 CD2 LEU A 266 6487 6572 7037 35 30 -239 C ATOM 2131 N PRO A 267 -42.436 -18.695 42.454 1.00 64.63 N ANISOU 2131 N PRO A 267 8024 8145 8389 -5 5 -256 N ATOM 2132 CA PRO A 267 -43.857 -18.745 42.766 1.00 62.86 C ANISOU 2132 CA PRO A 267 7799 7914 8171 -15 -2 -246 C ATOM 2133 C PRO A 267 -44.754 -18.434 41.565 1.00 63.21 C ANISOU 2133 C PRO A 267 7849 7967 8200 -24 -8 -275 C ATOM 2134 O PRO A 267 -45.707 -19.160 41.318 1.00 62.70 O ANISOU 2134 O PRO A 267 7779 7885 8157 -31 -13 -284 O ATOM 2135 CB PRO A 267 -44.010 -17.665 43.837 1.00 64.83 C ANISOU 2135 CB PRO A 267 8051 8185 8394 -16 -2 -216 C ATOM 2136 CG PRO A 267 -42.691 -17.583 44.471 1.00 63.14 C ANISOU 2136 CG PRO A 267 7833 7979 8176 -7 4 -202 C ATOM 2137 CD PRO A 267 -41.730 -17.753 43.339 1.00 64.45 C ANISOU 2137 CD PRO A 267 8004 8144 8342 -1 8 -231 C ATOM 2138 N TYR A 268 -44.477 -17.362 40.833 1.00 64.57 N ANISOU 2138 N TYR A 268 8030 8167 8335 -25 -7 -285 N ATOM 2139 CA TYR A 268 -45.232 -17.101 39.607 1.00 68.22 C ANISOU 2139 CA TYR A 268 8494 8645 8780 -33 -13 -309 C ATOM 2140 C TYR A 268 -45.150 -18.278 38.625 1.00 70.89 C ANISOU 2140 C TYR A 268 8826 8972 9139 -34 -14 -347 C ATOM 2141 O TYR A 268 -46.169 -18.721 38.098 1.00 73.57 O ANISOU 2141 O TYR A 268 9160 9307 9485 -44 -20 -365 O ATOM 2142 CB TYR A 268 -44.789 -15.798 38.924 1.00 68.21 C ANISOU 2142 CB TYR A 268 8500 8678 8740 -33 -12 -309 C ATOM 2143 CG TYR A 268 -45.729 -14.632 39.148 1.00 71.30 C ANISOU 2143 CG TYR A 268 8894 9083 9112 -39 -16 -287 C ATOM 2144 CD1 TYR A 268 -45.278 -13.450 39.725 1.00 70.97 C ANISOU 2144 CD1 TYR A 268 8857 9052 9057 -35 -12 -266 C ATOM 2145 CD2 TYR A 268 -47.072 -14.713 38.781 1.00 67.55 C ANISOU 2145 CD2 TYR A 268 8417 8610 8638 -48 -23 -290 C ATOM 2146 CE1 TYR A 268 -46.136 -12.380 39.931 1.00 66.70 C ANISOU 2146 CE1 TYR A 268 8317 8520 8506 -40 -14 -249 C ATOM 2147 CE2 TYR A 268 -47.934 -13.656 38.981 1.00 62.81 C ANISOU 2147 CE2 TYR A 268 7818 8022 8025 -52 -26 -270 C ATOM 2148 CZ TYR A 268 -47.465 -12.490 39.559 1.00 69.28 C ANISOU 2148 CZ TYR A 268 8641 8848 8833 -48 -21 -250 C ATOM 2149 OH TYR A 268 -48.329 -11.433 39.769 1.00 68.03 O ANISOU 2149 OH TYR A 268 8481 8697 8669 -51 -22 -232 O ATOM 2150 N ALA A 269 -43.939 -18.786 38.392 1.00 71.63 N ANISOU 2150 N ALA A 269 8915 9059 9241 -25 -6 -363 N ATOM 2151 CA ALA A 269 -43.736 -19.907 37.473 1.00 68.52 C ANISOU 2151 CA ALA A 269 8512 8652 8869 -25 -4 -406 C ATOM 2152 C ALA A 269 -44.349 -21.191 38.020 1.00 67.59 C ANISOU 2152 C ALA A 269 8384 8491 8806 -27 -6 -408 C ATOM 2153 O ALA A 269 -44.989 -21.928 37.277 1.00 69.70 O ANISOU 2153 O ALA A 269 8643 8748 9090 -36 -10 -443 O ATOM 2154 CB ALA A 269 -42.258 -20.101 37.184 1.00 66.63 C ANISOU 2154 CB ALA A 269 8270 8416 8629 -12 6 -419 C ATOM 2155 N GLY A 270 -44.158 -21.438 39.317 1.00 65.06 N ANISOU 2155 N GLY A 270 8062 8146 8511 -22 -3 -369 N ATOM 2156 CA GLY A 270 -44.644 -22.647 39.979 1.00 67.03 C ANISOU 2156 CA GLY A 270 8298 8354 8818 -23 -4 -359 C ATOM 2157 C GLY A 270 -46.157 -22.757 39.962 1.00 72.12 C ANISOU 2157 C GLY A 270 8941 8993 9470 -37 -14 -359 C ATOM 2158 O GLY A 270 -46.714 -23.763 39.522 1.00 74.52 O ANISOU 2158 O GLY A 270 9233 9269 9811 -44 -17 -385 O ATOM 2159 N VAL A 271 -46.820 -21.707 40.438 1.00 74.07 N ANISOU 2159 N VAL A 271 9197 9264 9680 -42 -19 -330 N ATOM 2160 CA VAL A 271 -48.272 -21.606 40.392 1.00 71.13 C ANISOU 2160 CA VAL A 271 8825 8895 9307 -55 -28 -327 C ATOM 2161 C VAL A 271 -48.786 -21.712 38.953 1.00 72.24 C ANISOU 2161 C VAL A 271 8964 9048 9435 -65 -34 -374 C ATOM 2162 O VAL A 271 -49.679 -22.510 38.679 1.00 72.74 O ANISOU 2162 O VAL A 271 9017 9092 9527 -76 -40 -391 O ATOM 2163 CB VAL A 271 -48.769 -20.305 41.076 1.00 71.23 C ANISOU 2163 CB VAL A 271 8848 8936 9281 -56 -30 -292 C ATOM 2164 CG1 VAL A 271 -50.245 -20.032 40.755 1.00 71.55 C ANISOU 2164 CG1 VAL A 271 8887 8986 9312 -69 -39 -294 C ATOM 2165 CG2 VAL A 271 -48.517 -20.366 42.595 1.00 60.17 C ANISOU 2165 CG2 VAL A 271 7442 7527 7894 -49 -25 -248 C ATOM 2166 N ALA A 272 -48.207 -20.940 38.035 1.00 72.24 N ANISOU 2166 N ALA A 272 8972 9084 9393 -63 -32 -394 N ATOM 2167 CA ALA A 272 -48.630 -20.987 36.626 1.00 74.38 C ANISOU 2167 CA ALA A 272 9238 9378 9644 -73 -38 -438 C ATOM 2168 C ALA A 272 -48.620 -22.412 36.091 1.00 76.01 C ANISOU 2168 C ALA A 272 9431 9556 9895 -77 -38 -483 C ATOM 2169 O ALA A 272 -49.546 -22.826 35.382 1.00 77.02 O ANISOU 2169 O ALA A 272 9549 9687 10026 -90 -46 -514 O ATOM 2170 CB ALA A 272 -47.755 -20.092 35.749 1.00 71.38 C ANISOU 2170 CB ALA A 272 8864 9041 9216 -67 -34 -450 C ATOM 2171 N PHE A 273 -47.573 -23.153 36.452 1.00 76.03 N ANISOU 2171 N PHE A 273 9428 9527 9931 -65 -28 -488 N ATOM 2172 CA PHE A 273 -47.371 -24.525 35.994 1.00 78.71 C ANISOU 2172 CA PHE A 273 9752 9832 10323 -66 -25 -533 C ATOM 2173 C PHE A 273 -48.406 -25.492 36.571 1.00 78.87 C ANISOU 2173 C PHE A 273 9760 9807 10400 -76 -30 -525 C ATOM 2174 O PHE A 273 -49.053 -26.220 35.834 1.00 78.92 O ANISOU 2174 O PHE A 273 9753 9802 10429 -88 -35 -569 O ATOM 2175 CB PHE A 273 -45.949 -24.988 36.334 1.00 79.13 C ANISOU 2175 CB PHE A 273 9802 9862 10401 -49 -12 -531 C ATOM 2176 CG PHE A 273 -45.670 -26.423 35.982 1.00 80.50 C ANISOU 2176 CG PHE A 273 9956 9991 10639 -47 -6 -575 C ATOM 2177 CD1 PHE A 273 -45.416 -26.795 34.657 1.00 85.37 C ANISOU 2177 CD1 PHE A 273 10564 10624 11248 -50 -3 -642 C ATOM 2178 CD2 PHE A 273 -45.635 -27.401 36.975 1.00 76.27 C ANISOU 2178 CD2 PHE A 273 9408 9399 10173 -43 -2 -548 C ATOM 2179 CE1 PHE A 273 -45.146 -28.121 34.325 1.00 78.48 C ANISOU 2179 CE1 PHE A 273 9672 9707 10440 -49 3 -689 C ATOM 2180 CE2 PHE A 273 -45.365 -28.724 36.659 1.00 74.64 C ANISOU 2180 CE2 PHE A 273 9180 9144 10034 -40 5 -587 C ATOM 2181 CZ PHE A 273 -45.121 -29.087 35.328 1.00 75.95 C ANISOU 2181 CZ PHE A 273 9339 9322 10196 -44 8 -661 C ATOM 2182 N TYR A 274 -48.550 -25.493 37.891 1.00 80.28 N ANISOU 2182 N TYR A 274 9939 9961 10601 -71 -29 -470 N ATOM 2183 CA TYR A 274 -49.589 -26.265 38.571 1.00 81.57 C ANISOU 2183 CA TYR A 274 10090 10088 10815 -81 -35 -449 C ATOM 2184 C TYR A 274 -50.992 -26.084 37.949 1.00 81.64 C ANISOU 2184 C TYR A 274 10098 10114 10807 -99 -47 -469 C ATOM 2185 O TYR A 274 -51.598 -27.048 37.498 1.00 80.24 O ANISOU 2185 O TYR A 274 9905 9909 10672 -111 -51 -502 O ATOM 2186 CB TYR A 274 -49.604 -25.875 40.046 1.00 80.24 C ANISOU 2186 CB TYR A 274 9926 9917 10647 -73 -33 -380 C ATOM 2187 CG TYR A 274 -50.580 -26.644 40.884 1.00 84.59 C ANISOU 2187 CG TYR A 274 10460 10432 11247 -81 -37 -349 C ATOM 2188 CD1 TYR A 274 -50.136 -27.578 41.812 1.00 89.86 C ANISOU 2188 CD1 TYR A 274 11111 11059 11974 -73 -30 -315 C ATOM 2189 CD2 TYR A 274 -51.950 -26.426 40.767 1.00 89.68 C ANISOU 2189 CD2 TYR A 274 11105 11087 11882 -96 -47 -347 C ATOM 2190 CE1 TYR A 274 -51.030 -28.286 42.597 1.00 97.62 C ANISOU 2190 CE1 TYR A 274 12076 12012 13004 -81 -34 -280 C ATOM 2191 CE2 TYR A 274 -52.854 -27.128 41.545 1.00 98.05 C ANISOU 2191 CE2 TYR A 274 12149 12118 12989 -104 -51 -315 C ATOM 2192 CZ TYR A 274 -52.388 -28.055 42.460 1.00100.22 C ANISOU 2192 CZ TYR A 274 12405 12352 13321 -96 -44 -280 C ATOM 2193 OH TYR A 274 -53.282 -28.752 43.237 1.00105.55 O ANISOU 2193 OH TYR A 274 13061 12999 14044 -104 -47 -243 O ATOM 2194 N ILE A 275 -51.494 -24.849 37.939 1.00 81.30 N ANISOU 2194 N ILE A 275 10070 10115 10705 -102 -53 -447 N ATOM 2195 CA ILE A 275 -52.759 -24.498 37.277 1.00 80.86 C ANISOU 2195 CA ILE A 275 10013 10085 10625 -118 -64 -462 C ATOM 2196 C ILE A 275 -52.856 -25.016 35.832 1.00 83.80 C ANISOU 2196 C ILE A 275 10375 10470 10994 -129 -69 -529 C ATOM 2197 O ILE A 275 -53.899 -25.501 35.412 1.00 86.64 O ANISOU 2197 O ILE A 275 10724 10826 11371 -145 -78 -552 O ATOM 2198 CB ILE A 275 -53.023 -22.956 37.342 1.00 78.82 C ANISOU 2198 CB ILE A 275 9771 9875 10302 -116 -67 -431 C ATOM 2199 CG1 ILE A 275 -53.525 -22.569 38.730 1.00 76.67 C ANISOU 2199 CG1 ILE A 275 9503 9593 10037 -113 -66 -374 C ATOM 2200 CG2 ILE A 275 -54.026 -22.498 36.286 1.00 71.35 C ANISOU 2200 CG2 ILE A 275 8822 8967 9321 -131 -78 -454 C ATOM 2201 CD1 ILE A 275 -53.514 -21.089 38.998 1.00 77.36 C ANISOU 2201 CD1 ILE A 275 9603 9717 10071 -107 -65 -344 C ATOM 2202 N PHE A 276 -51.775 -24.911 35.073 1.00 86.85 N ANISOU 2202 N PHE A 276 10764 10875 11359 -121 -62 -563 N ATOM 2203 CA PHE A 276 -51.742 -25.470 33.726 1.00 90.62 C ANISOU 2203 CA PHE A 276 11228 11369 11833 -130 -64 -632 C ATOM 2204 C PHE A 276 -51.898 -26.995 33.766 1.00 95.49 C ANISOU 2204 C PHE A 276 11826 11929 12527 -137 -63 -669 C ATOM 2205 O PHE A 276 -52.802 -27.541 33.140 1.00 98.03 O ANISOU 2205 O PHE A 276 12134 12251 12863 -154 -72 -708 O ATOM 2206 CB PHE A 276 -50.439 -25.075 33.032 1.00 89.00 C ANISOU 2206 CB PHE A 276 11029 11196 11591 -118 -55 -655 C ATOM 2207 CG PHE A 276 -50.322 -25.561 31.617 1.00 87.30 C ANISOU 2207 CG PHE A 276 10798 11009 11363 -126 -56 -728 C ATOM 2208 CD1 PHE A 276 -50.694 -24.741 30.554 1.00 85.34 C ANISOU 2208 CD1 PHE A 276 10549 10830 11047 -135 -63 -744 C ATOM 2209 CD2 PHE A 276 -49.792 -26.821 31.340 1.00 86.59 C ANISOU 2209 CD2 PHE A 276 10692 10881 11327 -124 -48 -781 C ATOM 2210 CE1 PHE A 276 -50.560 -25.175 29.239 1.00 80.49 C ANISOU 2210 CE1 PHE A 276 9916 10252 10413 -143 -64 -813 C ATOM 2211 CE2 PHE A 276 -49.655 -27.265 30.028 1.00 77.83 C ANISOU 2211 CE2 PHE A 276 9567 9802 10203 -132 -48 -856 C ATOM 2212 CZ PHE A 276 -50.038 -26.439 28.978 1.00 78.83 C ANISOU 2212 CZ PHE A 276 9691 10004 10255 -142 -56 -872 C ATOM 2213 N THR A 277 -51.017 -27.666 34.511 1.00100.34 N ANISOU 2213 N THR A 277 12438 12495 13192 -123 -52 -655 N ATOM 2214 CA THR A 277 -51.068 -29.116 34.729 1.00103.06 C ANISOU 2214 CA THR A 277 12761 12775 13623 -126 -48 -678 C ATOM 2215 C THR A 277 -52.434 -29.573 35.243 1.00106.64 C ANISOU 2215 C THR A 277 13204 13198 14115 -142 -58 -658 C ATOM 2216 O THR A 277 -53.168 -30.246 34.527 1.00110.01 O ANISOU 2216 O THR A 277 13615 13616 14568 -159 -65 -708 O ATOM 2217 CB THR A 277 -49.957 -29.576 35.707 1.00102.63 C ANISOU 2217 CB THR A 277 12705 12675 13615 -106 -35 -643 C ATOM 2218 OG1 THR A 277 -48.684 -29.477 35.061 1.00101.61 O ANISOU 2218 OG1 THR A 277 12579 12564 13466 -93 -24 -677 O ATOM 2219 CG2 THR A 277 -50.167 -31.015 36.139 1.00106.90 C ANISOU 2219 CG2 THR A 277 13221 13144 14254 -109 -31 -649 C ATOM 2220 N HIS A 278 -52.769 -29.207 36.479 1.00110.37 N ANISOU 2220 N HIS A 278 13683 13660 14591 -137 -59 -586 N ATOM 2221 CA HIS A 278 -54.077 -29.515 37.061 1.00113.88 C ANISOU 2221 CA HIS A 278 14119 14084 15067 -152 -69 -557 C ATOM 2222 C HIS A 278 -55.153 -28.610 36.461 1.00117.68 C ANISOU 2222 C HIS A 278 14609 14618 15486 -166 -82 -564 C ATOM 2223 O HIS A 278 -55.428 -27.527 36.984 1.00118.60 O ANISOU 2223 O HIS A 278 14742 14769 15554 -162 -84 -517 O ATOM 2224 CB HIS A 278 -54.040 -29.349 38.583 1.00112.25 C ANISOU 2224 CB HIS A 278 13915 13860 14876 -141 -65 -477 C ATOM 2225 CG HIS A 278 -52.997 -30.184 39.258 1.00112.93 C ANISOU 2225 CG HIS A 278 13989 13898 15020 -126 -53 -458 C ATOM 2226 ND1 HIS A 278 -51.728 -30.351 38.745 1.00114.12 N ANISOU 2226 ND1 HIS A 278 14142 14046 15173 -113 -43 -492 N ATOM 2227 CD2 HIS A 278 -53.029 -30.886 40.415 1.00114.05 C ANISOU 2227 CD2 HIS A 278 14114 13997 15222 -122 -49 -405 C ATOM 2228 CE1 HIS A 278 -51.028 -31.130 39.549 1.00115.20 C ANISOU 2228 CE1 HIS A 278 14264 14137 15370 -101 -33 -461 C ATOM 2229 NE2 HIS A 278 -51.794 -31.468 40.571 1.00117.78 N ANISOU 2229 NE2 HIS A 278 14579 14440 15733 -106 -37 -406 N ATOM 2230 N GLN A 279 -55.758 -29.070 35.367 1.00121.86 N ANISOU 2230 N GLN A 279 15126 15155 16020 -183 -90 -624 N ATOM 2231 CA GLN A 279 -56.692 -28.273 34.560 1.00124.62 C ANISOU 2231 CA GLN A 279 15479 15562 16309 -198 -102 -639 C ATOM 2232 C GLN A 279 -57.749 -27.511 35.379 1.00124.45 C ANISOU 2232 C GLN A 279 15465 15554 16266 -201 -109 -576 C ATOM 2233 O GLN A 279 -57.757 -26.276 35.387 1.00124.56 O ANISOU 2233 O GLN A 279 15496 15615 16217 -195 -110 -547 O ATOM 2234 CB GLN A 279 -57.361 -29.156 33.495 1.00127.63 C ANISOU 2234 CB GLN A 279 15838 15940 16715 -219 -111 -710 C ATOM 2235 CG GLN A 279 -56.385 -29.933 32.600 1.00131.80 C ANISOU 2235 CG GLN A 279 16355 16458 17264 -217 -103 -783 C ATOM 2236 CD GLN A 279 -57.059 -31.053 31.817 1.00137.53 C ANISOU 2236 CD GLN A 279 17055 17163 18038 -239 -111 -854 C ATOM 2237 OE1 GLN A 279 -57.997 -31.697 32.300 1.00136.11 O ANISOU 2237 OE1 GLN A 279 16861 16942 17913 -252 -117 -842 O ATOM 2238 NE2 GLN A 279 -56.572 -31.296 30.603 1.00139.87 N ANISOU 2238 NE2 GLN A 279 17341 17490 18315 -243 -109 -931 N ATOM 2239 N GLY A 280 -58.631 -28.246 36.059 1.00123.33 N ANISOU 2239 N GLY A 280 15310 15372 16179 -211 -114 -555 N ATOM 2240 CA GLY A 280 -59.656 -27.639 36.911 1.00121.20 C ANISOU 2240 CA GLY A 280 15043 15112 15894 -214 -119 -495 C ATOM 2241 C GLY A 280 -59.181 -27.467 38.344 1.00120.74 C ANISOU 2241 C GLY A 280 14993 15032 15852 -197 -109 -430 C ATOM 2242 O GLY A 280 -59.050 -28.444 39.084 1.00119.78 O ANISOU 2242 O GLY A 280 14856 14860 15794 -196 -105 -411 O ATOM 2243 N SER A 281 -58.919 -26.220 38.732 1.00120.10 N ANISOU 2243 N SER A 281 14930 14989 15711 -185 -106 -395 N ATOM 2244 CA SER A 281 -58.361 -25.901 40.052 1.00118.35 C ANISOU 2244 CA SER A 281 14716 14760 15492 -168 -96 -339 C ATOM 2245 C SER A 281 -59.102 -24.734 40.687 1.00114.94 C ANISOU 2245 C SER A 281 14294 14364 15015 -166 -97 -295 C ATOM 2246 O SER A 281 -59.567 -23.837 39.987 1.00115.87 O ANISOU 2246 O SER A 281 14420 14519 15085 -170 -103 -308 O ATOM 2247 CB SER A 281 -56.882 -25.527 39.927 1.00118.47 C ANISOU 2247 CB SER A 281 14745 14785 15484 -151 -85 -349 C ATOM 2248 OG SER A 281 -56.135 -26.568 39.322 1.00123.78 O ANISOU 2248 OG SER A 281 15408 15425 16198 -151 -82 -392 O ATOM 2249 N ASP A 282 -59.202 -24.726 42.011 1.00109.81 N ANISOU 2249 N ASP A 282 13639 13704 14378 -159 -92 -242 N ATOM 2250 CA ASP A 282 -59.771 -23.564 42.681 1.00104.88 C ANISOU 2250 CA ASP A 282 13023 13115 13711 -154 -91 -205 C ATOM 2251 C ASP A 282 -58.808 -22.933 43.685 1.00100.87 C ANISOU 2251 C ASP A 282 12524 12620 13180 -137 -80 -172 C ATOM 2252 O ASP A 282 -58.517 -23.494 44.749 1.00 99.30 O ANISOU 2252 O ASP A 282 12315 12404 13010 -131 -74 -138 O ATOM 2253 CB ASP A 282 -61.132 -23.882 43.307 1.00106.31 C ANISOU 2253 CB ASP A 282 13189 13290 13915 -165 -96 -173 C ATOM 2254 CG ASP A 282 -61.118 -23.824 44.822 1.00110.44 C ANISOU 2254 CG ASP A 282 13704 13814 14444 -156 -88 -117 C ATOM 2255 OD1 ASP A 282 -60.794 -24.849 45.454 1.00116.47 O ANISOU 2255 OD1 ASP A 282 14452 14546 15254 -154 -85 -96 O ATOM 2256 OD2 ASP A 282 -61.453 -22.758 45.382 1.00114.29 O ANISOU 2256 OD2 ASP A 282 14199 14336 14891 -149 -85 -94 O ATOM 2257 N PHE A 283 -58.297 -21.765 43.312 1.00 94.02 N ANISOU 2257 N PHE A 283 11675 11785 12264 -129 -77 -184 N ATOM 2258 CA PHE A 283 -57.420 -21.008 44.173 1.00 86.60 C ANISOU 2258 CA PHE A 283 10744 10862 11299 -115 -67 -160 C ATOM 2259 C PHE A 283 -58.078 -19.697 44.565 1.00 80.73 C ANISOU 2259 C PHE A 283 10007 10152 10514 -113 -66 -142 C ATOM 2260 O PHE A 283 -58.651 -19.002 43.726 1.00 76.87 O ANISOU 2260 O PHE A 283 9524 9681 10003 -118 -71 -158 O ATOM 2261 CB PHE A 283 -56.091 -20.756 43.470 1.00 88.71 C ANISOU 2261 CB PHE A 283 11024 11133 11548 -107 -63 -189 C ATOM 2262 CG PHE A 283 -55.172 -21.949 43.463 1.00 96.62 C ANISOU 2262 CG PHE A 283 12018 12102 12592 -103 -59 -199 C ATOM 2263 CD1 PHE A 283 -54.753 -22.514 42.262 1.00101.07 C ANISOU 2263 CD1 PHE A 283 12583 12652 13167 -107 -62 -245 C ATOM 2264 CD2 PHE A 283 -54.728 -22.513 44.661 1.00 98.52 C ANISOU 2264 CD2 PHE A 283 12248 12327 12859 -96 -53 -162 C ATOM 2265 CE1 PHE A 283 -53.898 -23.616 42.257 1.00103.67 C ANISOU 2265 CE1 PHE A 283 12903 12948 13541 -102 -57 -256 C ATOM 2266 CE2 PHE A 283 -53.876 -23.617 44.663 1.00 96.08 C ANISOU 2266 CE2 PHE A 283 11928 11983 12593 -91 -49 -167 C ATOM 2267 CZ PHE A 283 -53.459 -24.168 43.463 1.00 96.98 C ANISOU 2267 CZ PHE A 283 12044 12079 12724 -94 -51 -215 C ATOM 2268 N GLY A 284 -57.991 -19.363 45.848 1.00 76.11 N ANISOU 2268 N GLY A 284 9418 9579 9923 -105 -58 -107 N ATOM 2269 CA GLY A 284 -58.606 -18.147 46.366 1.00 72.44 C ANISOU 2269 CA GLY A 284 8956 9144 9425 -102 -55 -93 C ATOM 2270 C GLY A 284 -57.906 -16.845 46.006 1.00 70.45 C ANISOU 2270 C GLY A 284 8719 8912 9136 -94 -50 -109 C ATOM 2271 O GLY A 284 -56.802 -16.845 45.439 1.00 67.41 O ANISOU 2271 O GLY A 284 8343 8523 8745 -90 -49 -128 O ATOM 2272 N PRO A 285 -58.536 -15.711 46.359 1.00 68.02 N ANISOU 2272 N PRO A 285 8412 8626 8806 -91 -46 -100 N ATOM 2273 CA PRO A 285 -57.961 -14.405 46.060 1.00 67.52 C ANISOU 2273 CA PRO A 285 8360 8580 8716 -84 -41 -112 C ATOM 2274 C PRO A 285 -56.648 -14.150 46.825 1.00 66.02 C ANISOU 2274 C PRO A 285 8174 8395 8515 -75 -32 -111 C ATOM 2275 O PRO A 285 -55.747 -13.505 46.295 1.00 65.55 O ANISOU 2275 O PRO A 285 8124 8339 8441 -71 -30 -127 O ATOM 2276 CB PRO A 285 -59.063 -13.435 46.506 1.00 66.04 C ANISOU 2276 CB PRO A 285 8167 8409 8518 -84 -38 -100 C ATOM 2277 CG PRO A 285 -59.777 -14.160 47.579 1.00 64.14 C ANISOU 2277 CG PRO A 285 7911 8168 8290 -86 -37 -76 C ATOM 2278 CD PRO A 285 -59.746 -15.604 47.191 1.00 65.29 C ANISOU 2278 CD PRO A 285 8053 8291 8463 -94 -45 -76 C ATOM 2279 N ILE A 286 -56.545 -14.650 48.053 1.00 65.08 N ANISOU 2279 N ILE A 286 8045 8281 8403 -72 -28 -90 N ATOM 2280 CA ILE A 286 -55.347 -14.435 48.862 1.00 67.22 C ANISOU 2280 CA ILE A 286 8315 8564 8661 -65 -21 -87 C ATOM 2281 C ILE A 286 -54.150 -15.269 48.354 1.00 68.76 C ANISOU 2281 C ILE A 286 8516 8741 8869 -62 -23 -95 C ATOM 2282 O ILE A 286 -53.066 -14.722 48.100 1.00 66.80 O ANISOU 2282 O ILE A 286 8277 8498 8607 -57 -19 -110 O ATOM 2283 CB ILE A 286 -55.630 -14.653 50.381 1.00 67.60 C ANISOU 2283 CB ILE A 286 8346 8633 8706 -62 -15 -59 C ATOM 2284 CG1 ILE A 286 -56.373 -13.450 50.972 1.00 66.37 C ANISOU 2284 CG1 ILE A 286 8186 8502 8528 -61 -9 -61 C ATOM 2285 CG2 ILE A 286 -54.355 -14.924 51.159 1.00 62.75 C ANISOU 2285 CG2 ILE A 286 7727 8031 8085 -57 -10 -50 C ATOM 2286 CD1 ILE A 286 -55.494 -12.244 51.252 1.00 84.63 C ANISOU 2286 CD1 ILE A 286 10504 10833 10818 -55 -1 -81 C ATOM 2287 N PHE A 287 -54.363 -16.574 48.178 1.00 68.22 N ANISOU 2287 N PHE A 287 8440 8649 8831 -67 -28 -87 N ATOM 2288 CA PHE A 287 -53.370 -17.453 47.553 1.00 69.05 C ANISOU 2288 CA PHE A 287 8548 8732 8956 -65 -29 -100 C ATOM 2289 C PHE A 287 -52.800 -16.838 46.271 1.00 67.02 C ANISOU 2289 C PHE A 287 8307 8475 8682 -64 -30 -134 C ATOM 2290 O PHE A 287 -51.585 -16.725 46.095 1.00 66.36 O ANISOU 2290 O PHE A 287 8230 8393 8592 -57 -26 -144 O ATOM 2291 CB PHE A 287 -53.996 -18.818 47.230 1.00 71.26 C ANISOU 2291 CB PHE A 287 8817 8981 9278 -72 -35 -97 C ATOM 2292 CG PHE A 287 -53.057 -19.771 46.529 1.00 71.66 C ANISOU 2292 CG PHE A 287 8868 9004 9356 -70 -36 -116 C ATOM 2293 CD1 PHE A 287 -52.355 -20.731 47.254 1.00 69.15 C ANISOU 2293 CD1 PHE A 287 8536 8670 9068 -64 -32 -93 C ATOM 2294 CD2 PHE A 287 -52.875 -19.702 45.149 1.00 70.29 C ANISOU 2294 CD2 PHE A 287 8706 8824 9177 -73 -40 -156 C ATOM 2295 CE1 PHE A 287 -51.483 -21.606 46.621 1.00 68.34 C ANISOU 2295 CE1 PHE A 287 8432 8538 8995 -61 -31 -112 C ATOM 2296 CE2 PHE A 287 -52.001 -20.568 44.506 1.00 73.24 C ANISOU 2296 CE2 PHE A 287 9078 9175 9575 -70 -38 -178 C ATOM 2297 CZ PHE A 287 -51.303 -21.523 45.244 1.00 72.12 C ANISOU 2297 CZ PHE A 287 8923 9011 9469 -64 -34 -158 C ATOM 2298 N MET A 288 -53.699 -16.444 45.380 1.00 66.55 N ANISOU 2298 N MET A 288 8252 8417 8615 -71 -36 -149 N ATOM 2299 CA MET A 288 -53.327 -15.904 44.084 1.00 63.06 C ANISOU 2299 CA MET A 288 7821 7983 8157 -72 -38 -176 C ATOM 2300 C MET A 288 -52.625 -14.568 44.199 1.00 60.82 C ANISOU 2300 C MET A 288 7545 7718 7844 -65 -32 -175 C ATOM 2301 O MET A 288 -52.119 -14.043 43.202 1.00 59.87 O ANISOU 2301 O MET A 288 7432 7607 7708 -64 -32 -192 O ATOM 2302 CB MET A 288 -54.561 -15.783 43.187 1.00 63.27 C ANISOU 2302 CB MET A 288 7846 8013 8181 -81 -47 -185 C ATOM 2303 CG MET A 288 -55.071 -17.123 42.709 1.00 61.38 C ANISOU 2303 CG MET A 288 7598 7753 7971 -90 -54 -198 C ATOM 2304 SD MET A 288 -53.869 -17.967 41.656 1.00 65.87 S ANISOU 2304 SD MET A 288 8170 8309 8549 -89 -54 -235 S ATOM 2305 CE MET A 288 -54.125 -17.066 40.122 1.00 54.16 C ANISOU 2305 CE MET A 288 6691 6858 7028 -94 -60 -260 C ATOM 2306 N THR A 289 -52.595 -14.021 45.414 1.00 59.41 N ANISOU 2306 N THR A 289 7364 7551 7659 -60 -26 -157 N ATOM 2307 CA THR A 289 -51.843 -12.792 45.671 1.00 61.38 C ANISOU 2307 CA THR A 289 7618 7815 7887 -55 -19 -159 C ATOM 2308 C THR A 289 -50.349 -13.073 45.972 1.00 62.37 C ANISOU 2308 C THR A 289 7745 7940 8010 -48 -14 -162 C ATOM 2309 O THR A 289 -49.488 -12.230 45.693 1.00 61.33 O ANISOU 2309 O THR A 289 7620 7818 7865 -45 -11 -171 O ATOM 2310 CB THR A 289 -52.521 -11.910 46.759 1.00 60.25 C ANISOU 2310 CB THR A 289 7469 7687 7736 -54 -14 -147 C ATOM 2311 OG1 THR A 289 -53.690 -11.277 46.209 1.00 60.58 O ANISOU 2311 OG1 THR A 289 7510 7730 7777 -58 -16 -147 O ATOM 2312 CG2 THR A 289 -51.578 -10.830 47.250 1.00 58.75 C ANISOU 2312 CG2 THR A 289 7280 7510 7531 -49 -6 -153 C ATOM 2313 N ILE A 290 -50.052 -14.279 46.469 1.00 60.16 N ANISOU 2313 N ILE A 290 7459 7650 7749 -47 -15 -152 N ATOM 2314 CA ILE A 290 -48.713 -14.634 46.939 1.00 61.18 C ANISOU 2314 CA ILE A 290 7586 7780 7879 -40 -11 -148 C ATOM 2315 C ILE A 290 -47.606 -14.470 45.870 1.00 65.09 C ANISOU 2315 C ILE A 290 8091 8272 8369 -37 -9 -170 C ATOM 2316 O ILE A 290 -46.513 -13.960 46.175 1.00 61.47 O ANISOU 2316 O ILE A 290 7634 7825 7897 -32 -5 -170 O ATOM 2317 CB ILE A 290 -48.697 -16.053 47.599 1.00 63.31 C ANISOU 2317 CB ILE A 290 7843 8035 8178 -39 -11 -127 C ATOM 2318 CG1 ILE A 290 -49.549 -16.057 48.876 1.00 64.36 C ANISOU 2318 CG1 ILE A 290 7962 8183 8309 -41 -10 -99 C ATOM 2319 CG2 ILE A 290 -47.262 -16.523 47.930 1.00 58.98 C ANISOU 2319 CG2 ILE A 290 7289 7486 7635 -31 -7 -121 C ATOM 2320 CD1 ILE A 290 -49.874 -17.467 49.415 1.00 64.47 C ANISOU 2320 CD1 ILE A 290 7959 8180 8357 -42 -13 -72 C ATOM 2321 N PRO A 291 -47.880 -14.889 44.613 1.00 67.89 N ANISOU 2321 N PRO A 291 8450 8614 8730 -40 -14 -190 N ATOM 2322 CA PRO A 291 -46.870 -14.661 43.564 1.00 66.51 C ANISOU 2322 CA PRO A 291 8282 8443 8544 -36 -12 -210 C ATOM 2323 C PRO A 291 -46.459 -13.187 43.414 1.00 64.30 C ANISOU 2323 C PRO A 291 8008 8185 8238 -35 -9 -210 C ATOM 2324 O PRO A 291 -45.270 -12.899 43.268 1.00 65.51 O ANISOU 2324 O PRO A 291 8164 8345 8383 -30 -5 -215 O ATOM 2325 CB PRO A 291 -47.556 -15.174 42.290 1.00 63.73 C ANISOU 2325 CB PRO A 291 7930 8086 8198 -43 -18 -232 C ATOM 2326 CG PRO A 291 -48.538 -16.184 42.780 1.00 64.66 C ANISOU 2326 CG PRO A 291 8041 8184 8343 -47 -23 -224 C ATOM 2327 CD PRO A 291 -49.027 -15.676 44.110 1.00 67.82 C ANISOU 2327 CD PRO A 291 8438 8591 8740 -47 -21 -195 C ATOM 2328 N ALA A 292 -47.423 -12.268 43.463 1.00 62.68 N ANISOU 2328 N ALA A 292 7804 7988 8024 -40 -10 -204 N ATOM 2329 CA ALA A 292 -47.115 -10.839 43.342 1.00 60.79 C ANISOU 2329 CA ALA A 292 7566 7762 7769 -39 -7 -202 C ATOM 2330 C ALA A 292 -46.333 -10.340 44.547 1.00 61.18 C ANISOU 2330 C ALA A 292 7613 7816 7815 -36 0 -196 C ATOM 2331 O ALA A 292 -45.459 -9.483 44.408 1.00 62.02 O ANISOU 2331 O ALA A 292 7721 7931 7914 -34 4 -199 O ATOM 2332 CB ALA A 292 -48.376 -10.016 43.151 1.00 59.90 C ANISOU 2332 CB ALA A 292 7451 7653 7654 -44 -9 -196 C ATOM 2333 N PHE A 293 -46.652 -10.869 45.729 1.00 59.64 N ANISOU 2333 N PHE A 293 7413 7622 7626 -35 1 -185 N ATOM 2334 CA PHE A 293 -45.941 -10.494 46.940 1.00 56.93 C ANISOU 2334 CA PHE A 293 7063 7292 7275 -33 6 -180 C ATOM 2335 C PHE A 293 -44.463 -10.755 46.688 1.00 57.62 C ANISOU 2335 C PHE A 293 7152 7380 7360 -28 8 -184 C ATOM 2336 O PHE A 293 -43.658 -9.831 46.761 1.00 62.13 O ANISOU 2336 O PHE A 293 7724 7962 7922 -28 12 -191 O ATOM 2337 CB PHE A 293 -46.495 -11.247 48.155 1.00 57.59 C ANISOU 2337 CB PHE A 293 7136 7381 7363 -33 6 -163 C ATOM 2338 CG PHE A 293 -45.558 -11.305 49.346 1.00 66.51 C ANISOU 2338 CG PHE A 293 8256 8531 8484 -30 10 -155 C ATOM 2339 CD1 PHE A 293 -45.674 -10.396 50.385 1.00 70.81 C ANISOU 2339 CD1 PHE A 293 8792 9100 9013 -33 14 -158 C ATOM 2340 CD2 PHE A 293 -44.598 -12.312 49.456 1.00 72.48 C ANISOU 2340 CD2 PHE A 293 9007 9284 9247 -26 9 -144 C ATOM 2341 CE1 PHE A 293 -44.817 -10.472 51.494 1.00 69.97 C ANISOU 2341 CE1 PHE A 293 8672 9020 8893 -31 17 -151 C ATOM 2342 CE2 PHE A 293 -43.745 -12.383 50.557 1.00 66.61 C ANISOU 2342 CE2 PHE A 293 8251 8565 8493 -23 12 -132 C ATOM 2343 CZ PHE A 293 -43.856 -11.466 51.572 1.00 59.02 C ANISOU 2343 CZ PHE A 293 7281 7632 7510 -27 15 -135 C ATOM 2344 N PHE A 294 -44.113 -11.979 46.296 1.00 56.13 N ANISOU 2344 N PHE A 294 6964 7180 7184 -25 6 -183 N ATOM 2345 CA PHE A 294 -42.710 -12.328 46.071 1.00 52.63 C ANISOU 2345 CA PHE A 294 6520 6737 6740 -19 8 -186 C ATOM 2346 C PHE A 294 -41.994 -11.472 45.005 1.00 53.22 C ANISOU 2346 C PHE A 294 6602 6817 6803 -19 10 -201 C ATOM 2347 O PHE A 294 -40.881 -10.975 45.247 1.00 53.90 O ANISOU 2347 O PHE A 294 6686 6914 6880 -16 14 -201 O ATOM 2348 CB PHE A 294 -42.559 -13.823 45.806 1.00 50.11 C ANISOU 2348 CB PHE A 294 6197 6399 6443 -15 7 -184 C ATOM 2349 CG PHE A 294 -42.547 -14.648 47.058 1.00 58.15 C ANISOU 2349 CG PHE A 294 7203 7418 7476 -12 8 -160 C ATOM 2350 CD1 PHE A 294 -41.380 -14.796 47.797 1.00 61.07 C ANISOU 2350 CD1 PHE A 294 7564 7799 7842 -6 11 -146 C ATOM 2351 CD2 PHE A 294 -43.708 -15.248 47.526 1.00 64.54 C ANISOU 2351 CD2 PHE A 294 8005 8217 8298 -16 4 -146 C ATOM 2352 CE1 PHE A 294 -41.371 -15.538 48.969 1.00 56.26 C ANISOU 2352 CE1 PHE A 294 6937 7195 7243 -4 12 -117 C ATOM 2353 CE2 PHE A 294 -43.700 -15.997 48.699 1.00 57.08 C ANISOU 2353 CE2 PHE A 294 7044 7277 7366 -13 5 -117 C ATOM 2354 CZ PHE A 294 -42.537 -16.136 49.421 1.00 51.76 C ANISOU 2354 CZ PHE A 294 6360 6618 6688 -7 9 -101 C ATOM 2355 N ALA A 295 -42.639 -11.271 43.856 1.00 48.07 N ANISOU 2355 N ALA A 295 5955 6161 6148 -22 7 -211 N ATOM 2356 CA ALA A 295 -42.035 -10.509 42.764 1.00 48.92 C ANISOU 2356 CA ALA A 295 6065 6277 6243 -22 9 -219 C ATOM 2357 C ALA A 295 -41.863 -9.023 43.096 1.00 51.13 C ANISOU 2357 C ALA A 295 6344 6566 6515 -25 12 -213 C ATOM 2358 O ALA A 295 -40.764 -8.463 42.979 1.00 50.09 O ANISOU 2358 O ALA A 295 6211 6442 6379 -23 16 -214 O ATOM 2359 CB ALA A 295 -42.845 -10.674 41.487 1.00 47.77 C ANISOU 2359 CB ALA A 295 5922 6133 6094 -25 4 -228 C ATOM 2360 N LYS A 296 -42.967 -8.391 43.480 1.00 52.65 N ANISOU 2360 N LYS A 296 6536 6757 6712 -29 11 -208 N ATOM 2361 CA LYS A 296 -42.981 -6.983 43.856 1.00 52.90 C ANISOU 2361 CA LYS A 296 6563 6791 6745 -32 15 -206 C ATOM 2362 C LYS A 296 -41.962 -6.650 44.946 1.00 52.48 C ANISOU 2362 C LYS A 296 6506 6745 6691 -32 20 -210 C ATOM 2363 O LYS A 296 -41.294 -5.616 44.873 1.00 51.17 O ANISOU 2363 O LYS A 296 6335 6580 6526 -34 24 -212 O ATOM 2364 CB LYS A 296 -44.382 -6.566 44.320 1.00 53.84 C ANISOU 2364 CB LYS A 296 6680 6906 6872 -36 14 -202 C ATOM 2365 CG LYS A 296 -45.372 -6.366 43.199 1.00 58.12 C ANISOU 2365 CG LYS A 296 7222 7445 7416 -38 10 -196 C ATOM 2366 CD LYS A 296 -46.658 -5.732 43.699 1.00 63.55 C ANISOU 2366 CD LYS A 296 7904 8127 8114 -40 11 -191 C ATOM 2367 CE LYS A 296 -47.574 -5.346 42.554 1.00 51.57 C ANISOU 2367 CE LYS A 296 6384 6610 6599 -42 8 -181 C ATOM 2368 NZ LYS A 296 -47.822 -6.494 41.658 1.00 64.53 N ANISOU 2368 NZ LYS A 296 8030 8258 8229 -44 0 -183 N ATOM 2369 N THR A 297 -41.842 -7.499 45.965 1.00 47.43 N ANISOU 2369 N THR A 297 5863 6109 6048 -30 19 -208 N ATOM 2370 CA THR A 297 -40.983 -7.122 47.078 1.00 50.89 C ANISOU 2370 CA THR A 297 6294 6563 6481 -31 23 -211 C ATOM 2371 C THR A 297 -39.481 -7.147 46.693 1.00 50.46 C ANISOU 2371 C THR A 297 6238 6512 6421 -28 25 -212 C ATOM 2372 O THR A 297 -38.607 -6.681 47.439 1.00 49.45 O ANISOU 2372 O THR A 297 6103 6398 6289 -31 27 -217 O ATOM 2373 CB THR A 297 -41.367 -7.843 48.417 1.00 49.00 C ANISOU 2373 CB THR A 297 6046 6335 6236 -31 22 -204 C ATOM 2374 OG1 THR A 297 -40.190 -8.149 49.186 1.00 54.03 O ANISOU 2374 OG1 THR A 297 6674 6990 6864 -29 24 -200 O ATOM 2375 CG2 THR A 297 -42.109 -9.099 48.144 1.00 50.50 C ANISOU 2375 CG2 THR A 297 6239 6514 6433 -27 18 -192 C ATOM 2376 N SER A 298 -39.209 -7.617 45.480 1.00 50.61 N ANISOU 2376 N SER A 298 6264 6523 6441 -24 23 -211 N ATOM 2377 CA SER A 298 -37.852 -7.633 44.950 1.00 48.78 C ANISOU 2377 CA SER A 298 6031 6297 6206 -21 26 -212 C ATOM 2378 C SER A 298 -37.421 -6.237 44.527 1.00 48.98 C ANISOU 2378 C SER A 298 6054 6325 6232 -26 29 -214 C ATOM 2379 O SER A 298 -36.234 -5.976 44.400 1.00 53.02 O ANISOU 2379 O SER A 298 6561 6844 6741 -25 31 -214 O ATOM 2380 CB SER A 298 -37.729 -8.615 43.775 1.00 48.74 C ANISOU 2380 CB SER A 298 6031 6286 6200 -15 24 -214 C ATOM 2381 OG SER A 298 -38.201 -8.047 42.562 1.00 42.59 O ANISOU 2381 OG SER A 298 5256 5508 5418 -17 23 -216 O ATOM 2382 N ALA A 299 -38.373 -5.336 44.306 1.00 46.49 N ANISOU 2382 N ALA A 299 5738 6002 5925 -31 29 -214 N ATOM 2383 CA ALA A 299 -38.018 -3.940 44.063 1.00 46.51 C ANISOU 2383 CA ALA A 299 5733 6001 5937 -36 32 -213 C ATOM 2384 C ALA A 299 -37.220 -3.375 45.251 1.00 47.99 C ANISOU 2384 C ALA A 299 5912 6195 6128 -41 35 -224 C ATOM 2385 O ALA A 299 -36.545 -2.358 45.133 1.00 52.23 O ANISOU 2385 O ALA A 299 6440 6729 6676 -46 39 -226 O ATOM 2386 CB ALA A 299 -39.255 -3.103 43.781 1.00 41.96 C ANISOU 2386 CB ALA A 299 5154 5413 5375 -40 33 -209 C ATOM 2387 N VAL A 300 -37.291 -4.059 46.387 1.00 48.32 N ANISOU 2387 N VAL A 300 5953 6247 6160 -40 34 -230 N ATOM 2388 CA VAL A 300 -36.460 -3.745 47.530 1.00 48.37 C ANISOU 2388 CA VAL A 300 5949 6269 6162 -45 36 -241 C ATOM 2389 C VAL A 300 -35.223 -4.673 47.596 1.00 52.23 C ANISOU 2389 C VAL A 300 6436 6772 6637 -40 34 -233 C ATOM 2390 O VAL A 300 -34.088 -4.188 47.571 1.00 53.08 O ANISOU 2390 O VAL A 300 6538 6887 6745 -42 36 -236 O ATOM 2391 CB VAL A 300 -37.274 -3.809 48.836 1.00 49.94 C ANISOU 2391 CB VAL A 300 6140 6479 6354 -48 36 -251 C ATOM 2392 CG1 VAL A 300 -36.396 -3.532 50.055 1.00 48.76 C ANISOU 2392 CG1 VAL A 300 5976 6356 6193 -53 37 -264 C ATOM 2393 CG2 VAL A 300 -38.424 -2.830 48.789 1.00 51.66 C ANISOU 2393 CG2 VAL A 300 6357 6682 6588 -52 39 -261 C ATOM 2394 N TYR A 301 -35.416 -5.994 47.654 1.00 50.00 N ANISOU 2394 N TYR A 301 6159 6492 6347 -32 32 -222 N ATOM 2395 CA TYR A 301 -34.258 -6.869 47.864 1.00 49.57 C ANISOU 2395 CA TYR A 301 6099 6450 6285 -26 31 -212 C ATOM 2396 C TYR A 301 -33.245 -6.959 46.720 1.00 51.02 C ANISOU 2396 C TYR A 301 6286 6628 6471 -21 33 -210 C ATOM 2397 O TYR A 301 -32.055 -7.187 46.975 1.00 53.60 O ANISOU 2397 O TYR A 301 6605 6968 6792 -19 35 -205 O ATOM 2398 CB TYR A 301 -34.608 -8.251 48.446 1.00 47.98 C ANISOU 2398 CB TYR A 301 5896 6252 6083 -19 29 -198 C ATOM 2399 CG TYR A 301 -35.515 -9.135 47.620 1.00 50.97 C ANISOU 2399 CG TYR A 301 6285 6608 6473 -13 28 -194 C ATOM 2400 CD1 TYR A 301 -35.051 -9.747 46.461 1.00 57.39 C ANISOU 2400 CD1 TYR A 301 7104 7408 7292 -6 29 -195 C ATOM 2401 CD2 TYR A 301 -36.823 -9.407 48.035 1.00 48.06 C ANISOU 2401 CD2 TYR A 301 5918 6234 6107 -15 25 -191 C ATOM 2402 CE1 TYR A 301 -35.866 -10.574 45.708 1.00 48.58 C ANISOU 2402 CE1 TYR A 301 5996 6275 6187 -3 27 -197 C ATOM 2403 CE2 TYR A 301 -37.647 -10.229 47.300 1.00 54.89 C ANISOU 2403 CE2 TYR A 301 6792 7080 6985 -12 23 -189 C ATOM 2404 CZ TYR A 301 -37.161 -10.814 46.126 1.00 64.11 C ANISOU 2404 CZ TYR A 301 7965 8235 8160 -6 24 -194 C ATOM 2405 OH TYR A 301 -37.965 -11.635 45.362 1.00 62.81 O ANISOU 2405 OH TYR A 301 7806 8053 8007 -4 21 -199 O ATOM 2406 N ASN A 302 -33.692 -6.763 45.479 1.00 49.34 N ANISOU 2406 N ASN A 302 6082 6402 6263 -20 34 -211 N ATOM 2407 CA ASN A 302 -32.754 -6.716 44.349 1.00 49.12 C ANISOU 2407 CA ASN A 302 6055 6376 6234 -16 37 -209 C ATOM 2408 C ASN A 302 -31.690 -5.628 44.521 1.00 48.84 C ANISOU 2408 C ASN A 302 6009 6349 6198 -22 39 -209 C ATOM 2409 O ASN A 302 -30.510 -5.942 44.605 1.00 49.06 O ANISOU 2409 O ASN A 302 6031 6389 6221 -18 41 -206 O ATOM 2410 CB ASN A 302 -33.462 -6.560 43.003 1.00 49.70 C ANISOU 2410 CB ASN A 302 6134 6442 6307 -15 37 -209 C ATOM 2411 CG ASN A 302 -33.965 -7.888 42.428 1.00 54.62 C ANISOU 2411 CG ASN A 302 6764 7059 6928 -7 35 -213 C ATOM 2412 OD1 ASN A 302 -33.540 -8.977 42.834 1.00 44.31 O ANISOU 2412 OD1 ASN A 302 5457 5751 5626 0 36 -214 O ATOM 2413 ND2 ASN A 302 -34.890 -7.791 41.473 1.00 61.52 N ANISOU 2413 ND2 ASN A 302 7643 7931 7801 -8 33 -216 N ATOM 2414 N PRO A 303 -32.098 -4.348 44.605 1.00 47.39 N ANISOU 2414 N PRO A 303 5821 6159 6024 -32 40 -213 N ATOM 2415 CA PRO A 303 -31.054 -3.334 44.839 1.00 47.42 C ANISOU 2415 CA PRO A 303 5814 6169 6034 -39 42 -215 C ATOM 2416 C PRO A 303 -30.266 -3.506 46.157 1.00 49.53 C ANISOU 2416 C PRO A 303 6072 6454 6295 -43 41 -223 C ATOM 2417 O PRO A 303 -29.100 -3.134 46.213 1.00 50.54 O ANISOU 2417 O PRO A 303 6190 6592 6422 -46 42 -223 O ATOM 2418 CB PRO A 303 -31.818 -1.997 44.811 1.00 47.53 C ANISOU 2418 CB PRO A 303 5823 6167 6068 -49 43 -220 C ATOM 2419 CG PRO A 303 -33.291 -2.351 44.876 1.00 44.16 C ANISOU 2419 CG PRO A 303 5406 5730 5641 -46 41 -222 C ATOM 2420 CD PRO A 303 -33.434 -3.758 44.388 1.00 45.46 C ANISOU 2420 CD PRO A 303 5582 5901 5790 -36 39 -215 C ATOM 2421 N VAL A 304 -30.870 -4.068 47.203 1.00 50.93 N ANISOU 2421 N VAL A 304 6249 6638 6463 -42 38 -228 N ATOM 2422 CA VAL A 304 -30.092 -4.375 48.408 1.00 51.24 C ANISOU 2422 CA VAL A 304 6276 6703 6490 -45 37 -231 C ATOM 2423 C VAL A 304 -28.936 -5.304 48.034 1.00 53.86 C ANISOU 2423 C VAL A 304 6606 7044 6814 -35 37 -215 C ATOM 2424 O VAL A 304 -27.785 -5.025 48.367 1.00 54.80 O ANISOU 2424 O VAL A 304 6713 7179 6929 -39 37 -215 O ATOM 2425 CB VAL A 304 -30.945 -4.996 49.563 1.00 49.46 C ANISOU 2425 CB VAL A 304 6048 6491 6254 -44 34 -231 C ATOM 2426 CG1 VAL A 304 -30.076 -5.769 50.532 1.00 45.06 C ANISOU 2426 CG1 VAL A 304 5477 5964 5680 -42 32 -220 C ATOM 2427 CG2 VAL A 304 -31.675 -3.924 50.320 1.00 47.60 C ANISOU 2427 CG2 VAL A 304 5806 6259 6021 -56 35 -253 C ATOM 2428 N ILE A 305 -29.254 -6.380 47.311 1.00 54.28 N ANISOU 2428 N ILE A 305 6669 7085 6869 -23 38 -204 N ATOM 2429 CA ILE A 305 -28.281 -7.405 46.918 1.00 53.15 C ANISOU 2429 CA ILE A 305 6523 6945 6724 -11 40 -191 C ATOM 2430 C ILE A 305 -27.298 -6.939 45.835 1.00 54.04 C ANISOU 2430 C ILE A 305 6635 7058 6839 -10 44 -191 C ATOM 2431 O ILE A 305 -26.097 -7.056 46.012 1.00 56.92 O ANISOU 2431 O ILE A 305 6990 7438 7200 -8 45 -185 O ATOM 2432 CB ILE A 305 -29.005 -8.691 46.458 1.00 55.80 C ANISOU 2432 CB ILE A 305 6869 7265 7068 0 40 -186 C ATOM 2433 CG1 ILE A 305 -29.599 -9.428 47.664 1.00 55.07 C ANISOU 2433 CG1 ILE A 305 6770 7178 6976 1 37 -175 C ATOM 2434 CG2 ILE A 305 -28.081 -9.596 45.637 1.00 51.84 C ANISOU 2434 CG2 ILE A 305 6366 6761 6572 13 45 -181 C ATOM 2435 CD1 ILE A 305 -30.465 -10.593 47.289 1.00 46.56 C ANISOU 2435 CD1 ILE A 305 5699 6079 5911 10 37 -171 C ATOM 2436 N TYR A 306 -27.806 -6.408 44.725 1.00 55.03 N ANISOU 2436 N TYR A 306 6769 7171 6968 -11 45 -196 N ATOM 2437 CA TYR A 306 -26.970 -6.025 43.581 1.00 56.88 C ANISOU 2437 CA TYR A 306 7000 7409 7201 -9 50 -191 C ATOM 2438 C TYR A 306 -26.315 -4.645 43.682 1.00 58.78 C ANISOU 2438 C TYR A 306 7231 7656 7448 -21 50 -190 C ATOM 2439 O TYR A 306 -25.327 -4.383 43.002 1.00 61.37 O ANISOU 2439 O TYR A 306 7550 7992 7774 -20 54 -182 O ATOM 2440 CB TYR A 306 -27.753 -6.106 42.263 1.00 54.98 C ANISOU 2440 CB TYR A 306 6769 7162 6960 -5 51 -193 C ATOM 2441 CG TYR A 306 -28.134 -7.505 41.872 1.00 58.85 C ANISOU 2441 CG TYR A 306 7267 7647 7447 7 52 -198 C ATOM 2442 CD1 TYR A 306 -29.242 -8.126 42.448 1.00 65.71 C ANISOU 2442 CD1 TYR A 306 8143 8502 8322 7 48 -203 C ATOM 2443 CD2 TYR A 306 -27.404 -8.207 40.922 1.00 53.13 C ANISOU 2443 CD2 TYR A 306 6539 6930 6718 18 57 -201 C ATOM 2444 CE1 TYR A 306 -29.604 -9.410 42.101 1.00 64.19 C ANISOU 2444 CE1 TYR A 306 7955 8300 8134 17 49 -209 C ATOM 2445 CE2 TYR A 306 -27.763 -9.503 40.566 1.00 61.70 C ANISOU 2445 CE2 TYR A 306 7629 8008 7807 28 59 -212 C ATOM 2446 CZ TYR A 306 -28.861 -10.093 41.164 1.00 62.50 C ANISOU 2446 CZ TYR A 306 7737 8091 7918 27 54 -216 C ATOM 2447 OH TYR A 306 -29.230 -11.368 40.843 1.00 73.51 O ANISOU 2447 OH TYR A 306 9134 9473 9324 36 56 -228 O ATOM 2448 N ILE A 307 -26.869 -3.753 44.491 1.00 60.31 N ANISOU 2448 N ILE A 307 7422 7844 7650 -33 47 -199 N ATOM 2449 CA ILE A 307 -26.331 -2.398 44.572 1.00 61.18 C ANISOU 2449 CA ILE A 307 7519 7952 7774 -46 48 -201 C ATOM 2450 C ILE A 307 -25.653 -2.170 45.915 1.00 62.61 C ANISOU 2450 C ILE A 307 7688 8148 7953 -55 46 -213 C ATOM 2451 O ILE A 307 -24.505 -1.758 45.969 1.00 64.11 O ANISOU 2451 O ILE A 307 7866 8349 8145 -60 46 -211 O ATOM 2452 CB ILE A 307 -27.414 -1.316 44.360 1.00 61.52 C ANISOU 2452 CB ILE A 307 7563 7974 7836 -55 49 -205 C ATOM 2453 CG1 ILE A 307 -28.231 -1.573 43.087 1.00 62.60 C ANISOU 2453 CG1 ILE A 307 7711 8103 7972 -47 50 -192 C ATOM 2454 CG2 ILE A 307 -26.792 0.059 44.310 1.00 63.66 C ANISOU 2454 CG2 ILE A 307 7819 8238 8132 -67 51 -206 C ATOM 2455 CD1 ILE A 307 -27.437 -1.464 41.829 1.00 68.37 C ANISOU 2455 CD1 ILE A 307 8435 8843 8699 -43 54 -174 C ATOM 2456 N MET A 308 -26.350 -2.470 47.001 1.00 64.42 N ANISOU 2456 N MET A 308 7918 8382 8175 -57 42 -225 N ATOM 2457 CA MET A 308 -25.889 -2.044 48.314 1.00 65.68 C ANISOU 2457 CA MET A 308 8063 8563 8330 -68 39 -241 C ATOM 2458 C MET A 308 -24.840 -2.930 48.948 1.00 66.31 C ANISOU 2458 C MET A 308 8133 8671 8390 -64 37 -231 C ATOM 2459 O MET A 308 -24.111 -2.477 49.826 1.00 66.35 O ANISOU 2459 O MET A 308 8121 8700 8390 -74 34 -242 O ATOM 2460 CB MET A 308 -27.066 -1.836 49.253 1.00 66.62 C ANISOU 2460 CB MET A 308 8183 8682 8448 -74 38 -259 C ATOM 2461 CG MET A 308 -28.091 -0.899 48.662 1.00 77.64 C ANISOU 2461 CG MET A 308 9585 10047 9867 -78 41 -268 C ATOM 2462 SD MET A 308 -28.602 0.361 49.820 1.00 99.60 S ANISOU 2462 SD MET A 308 12352 12829 12664 -95 42 -304 S ATOM 2463 CE MET A 308 -27.029 1.039 50.381 1.00 95.16 C ANISOU 2463 CE MET A 308 11767 12286 12103 -108 40 -319 C ATOM 2464 N MET A 309 -24.754 -4.185 48.511 1.00 68.48 N ANISOU 2464 N MET A 309 8416 8947 8657 -48 38 -211 N ATOM 2465 CA MET A 309 -23.725 -5.090 49.023 1.00 74.19 C ANISOU 2465 CA MET A 309 9128 9694 9367 -41 37 -196 C ATOM 2466 C MET A 309 -22.400 -4.846 48.313 1.00 77.38 C ANISOU 2466 C MET A 309 9524 10102 9775 -40 40 -188 C ATOM 2467 O MET A 309 -21.357 -5.343 48.729 1.00 78.18 O ANISOU 2467 O MET A 309 9612 10225 9867 -36 39 -176 O ATOM 2468 CB MET A 309 -24.139 -6.550 48.870 1.00 73.74 C ANISOU 2468 CB MET A 309 9078 9630 9308 -24 38 -178 C ATOM 2469 CG MET A 309 -25.539 -6.834 49.347 1.00 81.60 C ANISOU 2469 CG MET A 309 10082 10618 10303 -25 36 -182 C ATOM 2470 SD MET A 309 -25.597 -8.218 50.479 1.00 93.22 S ANISOU 2470 SD MET A 309 11542 12111 11768 -16 33 -159 S ATOM 2471 CE MET A 309 -25.019 -7.426 51.995 1.00 94.43 C ANISOU 2471 CE MET A 309 11671 12311 11897 -32 28 -166 C ATOM 2472 N ASN A 310 -22.471 -4.080 47.230 1.00 81.47 N ANISOU 2472 N ASN A 310 10049 10600 10305 -42 43 -192 N ATOM 2473 CA ASN A 310 -21.315 -3.619 46.481 1.00 84.71 C ANISOU 2473 CA ASN A 310 10451 11015 10721 -44 47 -184 C ATOM 2474 C ASN A 310 -20.563 -2.536 47.256 1.00 87.46 C ANISOU 2474 C ASN A 310 10781 11376 11073 -61 43 -195 C ATOM 2475 O ASN A 310 -21.165 -1.568 47.729 1.00 87.45 O ANISOU 2475 O ASN A 310 10777 11367 11084 -76 41 -214 O ATOM 2476 CB ASN A 310 -21.818 -3.069 45.149 1.00 85.94 C ANISOU 2476 CB ASN A 310 10617 11149 10888 -42 51 -181 C ATOM 2477 CG ASN A 310 -20.716 -2.532 44.267 1.00 90.84 C ANISOU 2477 CG ASN A 310 11227 11776 11514 -44 55 -168 C ATOM 2478 OD1 ASN A 310 -19.708 -1.994 44.746 1.00 81.18 O ANISOU 2478 OD1 ASN A 310 9987 10565 10294 -53 54 -169 O ATOM 2479 ND2 ASN A 310 -20.928 -2.635 42.949 1.00 95.06 N ANISOU 2479 ND2 ASN A 310 11767 12304 12048 -35 60 -158 N ATOM 2480 N LYS A 311 -19.248 -2.704 47.377 1.00 90.87 N ANISOU 2480 N LYS A 311 11198 11830 11499 -61 43 -185 N ATOM 2481 CA LYS A 311 -18.410 -1.807 48.184 1.00 93.71 C ANISOU 2481 CA LYS A 311 11537 12207 11861 -79 39 -197 C ATOM 2482 C LYS A 311 -18.413 -0.347 47.708 1.00 92.48 C ANISOU 2482 C LYS A 311 11376 12031 11733 -95 40 -209 C ATOM 2483 O LYS A 311 -18.557 0.581 48.516 1.00 89.92 O ANISOU 2483 O LYS A 311 11040 11706 11419 -113 37 -234 O ATOM 2484 CB LYS A 311 -16.975 -2.343 48.249 1.00 96.67 C ANISOU 2484 CB LYS A 311 11896 12609 12225 -74 39 -180 C ATOM 2485 CG LYS A 311 -16.592 -2.957 49.591 1.00104.40 C ANISOU 2485 CG LYS A 311 12861 13624 13184 -75 33 -179 C ATOM 2486 CD LYS A 311 -16.146 -1.883 50.588 1.00111.11 C ANISOU 2486 CD LYS A 311 13689 14495 14032 -99 26 -203 C ATOM 2487 CE LYS A 311 -15.782 -2.483 51.941 1.00111.64 C ANISOU 2487 CE LYS A 311 13738 14609 14073 -101 19 -200 C ATOM 2488 NZ LYS A 311 -15.292 -1.445 52.889 1.00108.98 N ANISOU 2488 NZ LYS A 311 13377 14299 13732 -126 13 -229 N ATOM 2489 N GLN A 312 -18.250 -0.161 46.398 1.00 91.10 N ANISOU 2489 N GLN A 312 11205 11838 11569 -89 46 -191 N ATOM 2490 CA GLN A 312 -18.258 1.162 45.777 1.00 89.32 C ANISOU 2490 CA GLN A 312 10973 11592 11374 -101 49 -191 C ATOM 2491 C GLN A 312 -19.561 1.920 46.037 1.00 88.99 C ANISOU 2491 C GLN A 312 10937 11523 11353 -110 48 -210 C ATOM 2492 O GLN A 312 -19.549 2.935 46.756 1.00 87.61 O ANISOU 2492 O GLN A 312 10748 11340 11200 -128 46 -233 O ATOM 2493 CB GLN A 312 -18.017 1.057 44.266 1.00 90.06 C ANISOU 2493 CB GLN A 312 11069 11679 11469 -90 55 -162 C ATOM 2494 CG GLN A 312 -16.568 0.847 43.872 1.00 89.58 C ANISOU 2494 CG GLN A 312 10994 11640 11401 -87 58 -144 C ATOM 2495 CD GLN A 312 -16.076 1.921 42.931 1.00 93.79 C ANISOU 2495 CD GLN A 312 11513 12164 11958 -96 62 -125 C ATOM 2496 OE1 GLN A 312 -16.818 2.398 42.075 1.00101.49 O ANISOU 2496 OE1 GLN A 312 12492 13122 12947 -95 65 -113 O ATOM 2497 NE2 GLN A 312 -14.826 2.328 43.099 1.00 99.01 N ANISOU 2497 NE2 GLN A 312 12154 12839 12626 -105 61 -119 N ATOM 2498 N PHE A 313 -20.667 1.422 45.455 1.00 84.22 N ANISOU 2498 N PHE A 313 10352 10906 10743 -98 50 -202 N ATOM 2499 CA PHE A 313 -21.976 2.079 45.546 0.50 77.24 C ANISOU 2499 CA PHE A 313 9475 9996 9879 -103 50 -215 C ATOM 2500 C PHE A 313 -22.191 2.510 46.985 1.00 78.49 C ANISOU 2500 C PHE A 313 9624 10158 10041 -117 46 -249 C ATOM 2501 O PHE A 313 -22.512 3.668 47.252 1.00 80.27 O ANISOU 2501 O PHE A 313 9838 10363 10298 -131 48 -268 O ATOM 2502 CB PHE A 313 -23.119 1.158 45.090 0.50 72.29 C ANISOU 2502 CB PHE A 313 8869 9364 9235 -88 51 -208 C ATOM 2503 CG PHE A 313 -23.388 1.183 43.594 0.50 62.81 C ANISOU 2503 CG PHE A 313 7673 8153 8037 -79 55 -182 C ATOM 2504 CD1 PHE A 313 -24.136 2.207 43.021 0.50 48.21 C ANISOU 2504 CD1 PHE A 313 5821 6280 6216 -86 58 -174 C ATOM 2505 CD2 PHE A 313 -22.928 0.151 42.765 0.50 49.94 C ANISOU 2505 CD2 PHE A 313 6051 6541 6384 -65 58 -165 C ATOM 2506 CE1 PHE A 313 -24.394 2.222 41.639 0.50 39.23 C ANISOU 2506 CE1 PHE A 313 4685 5143 5078 -78 61 -147 C ATOM 2507 CE2 PHE A 313 -23.183 0.157 41.398 0.50 36.36 C ANISOU 2507 CE2 PHE A 313 4333 4821 4661 -57 62 -145 C ATOM 2508 CZ PHE A 313 -23.918 1.199 40.829 0.50 32.39 C ANISOU 2508 CZ PHE A 313 3824 4300 4181 -65 63 -134 C ATOM 2509 N ARG A 314 -21.944 1.593 47.915 1.00 78.04 N ANISOU 2509 N ARG A 314 9567 10130 9952 -113 42 -257 N ATOM 2510 CA ARG A 314 -22.120 1.872 49.338 1.00 78.75 C ANISOU 2510 CA ARG A 314 9646 10238 10037 -125 38 -289 C ATOM 2511 C ARG A 314 -21.405 3.154 49.779 1.00 81.55 C ANISOU 2511 C ARG A 314 9978 10590 10417 -146 37 -314 C ATOM 2512 O ARG A 314 -22.023 4.025 50.402 1.00 81.24 O ANISOU 2512 O ARG A 314 9930 10539 10398 -159 38 -347 O ATOM 2513 CB ARG A 314 -21.645 0.686 50.174 1.00 78.58 C ANISOU 2513 CB ARG A 314 9623 10257 9978 -118 33 -283 C ATOM 2514 CG ARG A 314 -22.484 0.414 51.415 1.00 77.90 C ANISOU 2514 CG ARG A 314 9535 10191 9873 -121 30 -304 C ATOM 2515 CD ARG A 314 -21.768 -0.537 52.376 1.00 79.75 C ANISOU 2515 CD ARG A 314 9756 10473 10073 -118 25 -294 C ATOM 2516 NE ARG A 314 -21.709 -1.906 51.864 1.00 82.95 N ANISOU 2516 NE ARG A 314 10174 10878 10465 -98 26 -258 N ATOM 2517 CZ ARG A 314 -20.626 -2.476 51.340 1.00 88.14 C ANISOU 2517 CZ ARG A 314 10829 11542 11119 -89 27 -234 C ATOM 2518 NH1 ARG A 314 -20.684 -3.726 50.901 1.00 94.84 N ANISOU 2518 NH1 ARG A 314 11687 12386 11962 -70 29 -207 N ATOM 2519 NH2 ARG A 314 -19.485 -1.807 51.253 1.00 92.89 N ANISOU 2519 NH2 ARG A 314 11415 12152 11726 -99 26 -238 N ATOM 2520 N ASN A 315 -20.113 3.267 49.445 1.00 83.59 N ANISOU 2520 N ASN A 315 10225 10859 10678 -150 37 -301 N ATOM 2521 CA ASN A 315 -19.295 4.433 49.812 1.00 81.04 C ANISOU 2521 CA ASN A 315 9877 10533 10382 -171 35 -323 C ATOM 2522 C ASN A 315 -19.918 5.737 49.344 1.00 79.74 C ANISOU 2522 C ASN A 315 9706 10323 10268 -181 40 -334 C ATOM 2523 O ASN A 315 -20.148 6.657 50.127 1.00 80.74 O ANISOU 2523 O ASN A 315 9818 10441 10420 -198 40 -373 O ATOM 2524 CB ASN A 315 -17.890 4.317 49.220 1.00 81.65 C ANISOU 2524 CB ASN A 315 9943 10622 10457 -171 35 -296 C ATOM 2525 CG ASN A 315 -17.029 3.284 49.929 1.00 86.67 C ANISOU 2525 CG ASN A 315 10573 11305 11051 -165 30 -290 C ATOM 2526 OD1 ASN A 315 -17.498 2.551 50.796 1.00 89.14 O ANISOU 2526 OD1 ASN A 315 10891 11643 11336 -160 26 -300 O ATOM 2527 ND2 ASN A 315 -15.758 3.217 49.549 1.00 90.42 N ANISOU 2527 ND2 ASN A 315 11036 11793 11525 -166 29 -271 N ATOM 2528 N CYS A 316 -20.199 5.802 48.053 1.00 77.24 N ANISOU 2528 N CYS A 316 9401 9979 9969 -171 46 -300 N ATOM 2529 CA CYS A 316 -20.763 6.994 47.460 1.00 77.52 C ANISOU 2529 CA CYS A 316 9429 9971 10056 -179 51 -298 C ATOM 2530 C CYS A 316 -22.094 7.363 48.077 1.00 80.12 C ANISOU 2530 C CYS A 316 9763 10281 10400 -181 53 -329 C ATOM 2531 O CYS A 316 -22.384 8.541 48.270 1.00 80.57 O ANISOU 2531 O CYS A 316 9803 10306 10504 -195 56 -351 O ATOM 2532 CB CYS A 316 -20.931 6.784 45.966 1.00 78.79 C ANISOU 2532 CB CYS A 316 9599 10118 10219 -164 55 -251 C ATOM 2533 SG CYS A 316 -19.400 6.319 45.169 1.00 72.09 S ANISOU 2533 SG CYS A 316 8744 9296 9351 -159 55 -215 S ATOM 2534 N MET A 317 -22.908 6.351 48.370 1.00 82.94 N ANISOU 2534 N MET A 317 10140 10656 10718 -168 51 -330 N ATOM 2535 CA MET A 317 -24.209 6.563 49.002 1.00 83.80 C ANISOU 2535 CA MET A 317 10254 10752 10834 -168 52 -357 C ATOM 2536 C MET A 317 -24.005 7.297 50.322 1.00 81.79 C ANISOU 2536 C MET A 317 9978 10507 10591 -187 51 -410 C ATOM 2537 O MET A 317 -24.675 8.287 50.594 1.00 80.80 O ANISOU 2537 O MET A 317 9842 10353 10507 -196 56 -438 O ATOM 2538 CB MET A 317 -24.920 5.221 49.233 1.00 86.54 C ANISOU 2538 CB MET A 317 10623 11124 11133 -152 49 -349 C ATOM 2539 CG MET A 317 -26.322 5.112 48.614 1.00 95.19 C ANISOU 2539 CG MET A 317 11736 12195 12237 -141 53 -335 C ATOM 2540 SD MET A 317 -26.701 3.469 47.923 1.00110.05 S ANISOU 2540 SD MET A 317 13645 14095 14075 -119 50 -299 S ATOM 2541 CE MET A 317 -25.724 3.393 46.412 1.00 82.93 C ANISOU 2541 CE MET A 317 10211 10656 10645 -112 52 -260 C ATOM 2542 N VAL A 318 -23.048 6.823 51.117 1.00 81.05 N ANISOU 2542 N VAL A 318 9875 10455 10464 -193 45 -422 N ATOM 2543 CA VAL A 318 -22.768 7.412 52.424 1.00 83.14 C ANISOU 2543 CA VAL A 318 10117 10742 10730 -212 43 -475 C ATOM 2544 C VAL A 318 -22.258 8.843 52.297 1.00 84.11 C ANISOU 2544 C VAL A 318 10215 10830 10912 -231 46 -499 C ATOM 2545 O VAL A 318 -22.663 9.725 53.061 1.00 85.92 O ANISOU 2545 O VAL A 318 10428 11049 11170 -246 49 -549 O ATOM 2546 CB VAL A 318 -21.770 6.565 53.242 1.00 83.04 C ANISOU 2546 CB VAL A 318 10097 10789 10666 -214 35 -476 C ATOM 2547 CG1 VAL A 318 -21.429 7.261 54.560 1.00 81.75 C ANISOU 2547 CG1 VAL A 318 9904 10654 10502 -236 32 -533 C ATOM 2548 CG2 VAL A 318 -22.344 5.181 53.501 1.00 81.47 C ANISOU 2548 CG2 VAL A 318 9917 10621 10417 -195 32 -453 C ATOM 2549 N THR A 319 -21.373 9.066 51.329 1.00 82.73 N ANISOU 2549 N THR A 319 10038 10638 10759 -232 47 -464 N ATOM 2550 CA THR A 319 -20.919 10.412 51.000 1.00 82.63 C ANISOU 2550 CA THR A 319 10001 10584 10811 -249 51 -475 C ATOM 2551 C THR A 319 -22.090 11.313 50.602 1.00 82.33 C ANISOU 2551 C THR A 319 9961 10491 10828 -248 59 -481 C ATOM 2552 O THR A 319 -22.252 12.397 51.149 1.00 86.29 O ANISOU 2552 O THR A 319 10440 10966 11379 -265 63 -525 O ATOM 2553 CB THR A 319 -19.886 10.390 49.861 1.00 83.06 C ANISOU 2553 CB THR A 319 10054 10631 10876 -246 51 -424 C ATOM 2554 OG1 THR A 319 -18.745 9.622 50.266 1.00 88.37 O ANISOU 2554 OG1 THR A 319 10723 11352 11502 -247 43 -420 O ATOM 2555 CG2 THR A 319 -19.451 11.799 49.498 1.00 79.22 C ANISOU 2555 CG2 THR A 319 9539 10099 10462 -264 55 -429 C ATOM 2556 N THR A 320 -22.910 10.856 49.661 1.00 80.51 N ANISOU 2556 N THR A 320 9753 10246 10592 -229 62 -438 N ATOM 2557 CA THR A 320 -24.009 11.665 49.150 1.00 77.92 C ANISOU 2557 CA THR A 320 9423 9868 10317 -226 70 -433 C ATOM 2558 C THR A 320 -25.016 11.960 50.249 1.00 80.81 C ANISOU 2558 C THR A 320 9786 10230 10690 -231 73 -488 C ATOM 2559 O THR A 320 -25.549 13.063 50.328 1.00 82.57 O ANISOU 2559 O THR A 320 9991 10409 10975 -239 81 -511 O ATOM 2560 CB THR A 320 -24.714 10.977 47.972 1.00 75.16 C ANISOU 2560 CB THR A 320 9098 9514 9948 -205 72 -377 C ATOM 2561 OG1 THR A 320 -23.760 10.699 46.941 1.00 75.36 O ANISOU 2561 OG1 THR A 320 9123 9548 9963 -201 70 -329 O ATOM 2562 CG2 THR A 320 -25.804 11.864 47.412 1.00 67.00 C ANISOU 2562 CG2 THR A 320 8057 8430 8970 -203 79 -366 C ATOM 2563 N LEU A 321 -25.251 10.976 51.109 1.00 82.94 N ANISOU 2563 N LEU A 321 10069 10546 10897 -225 68 -508 N ATOM 2564 CA LEU A 321 -26.201 11.122 52.203 1.00 86.84 C ANISOU 2564 CA LEU A 321 10560 11049 11387 -228 71 -559 C ATOM 2565 C LEU A 321 -25.679 11.990 53.350 1.00 91.19 C ANISOU 2565 C LEU A 321 11081 11609 11960 -251 72 -626 C ATOM 2566 O LEU A 321 -26.430 12.783 53.922 1.00 90.76 O ANISOU 2566 O LEU A 321 11012 11533 11941 -258 79 -673 O ATOM 2567 CB LEU A 321 -26.637 9.749 52.720 1.00 86.11 C ANISOU 2567 CB LEU A 321 10489 11007 11221 -215 65 -552 C ATOM 2568 CG LEU A 321 -27.675 9.037 51.845 1.00 82.80 C ANISOU 2568 CG LEU A 321 10097 10574 10789 -194 67 -507 C ATOM 2569 CD1 LEU A 321 -28.304 7.879 52.612 1.00 73.12 C ANISOU 2569 CD1 LEU A 321 8886 9392 9504 -184 63 -511 C ATOM 2570 CD2 LEU A 321 -28.746 10.018 51.337 1.00 66.17 C ANISOU 2570 CD2 LEU A 321 7986 8414 8742 -193 76 -508 C ATOM 2571 N CYS A 322 -24.397 11.844 53.680 1.00 95.51 N ANISOU 2571 N CYS A 322 11616 12188 12485 -263 65 -632 N ATOM 2572 CA CYS A 322 -23.765 12.690 54.689 1.00 99.52 C ANISOU 2572 CA CYS A 322 12092 12707 13014 -287 64 -696 C ATOM 2573 C CYS A 322 -23.267 14.021 54.135 1.00102.16 C ANISOU 2573 C CYS A 322 12403 12982 13433 -302 70 -704 C ATOM 2574 O CYS A 322 -22.307 14.589 54.658 1.00104.24 O ANISOU 2574 O CYS A 322 12639 13254 13712 -323 67 -740 O ATOM 2575 CB CYS A 322 -22.624 11.952 55.370 1.00 97.95 C ANISOU 2575 CB CYS A 322 11887 12574 12755 -294 54 -701 C ATOM 2576 SG CYS A 322 -23.200 10.603 56.366 1.00109.62 S ANISOU 2576 SG CYS A 322 13380 14125 14146 -281 48 -705 S ATOM 2577 N CYS A 323 -23.927 14.515 53.085 1.00104.37 N ANISOU 2577 N CYS A 323 12689 13202 13766 -292 77 -667 N ATOM 2578 CA CYS A 323 -23.734 15.882 52.584 1.00107.53 C ANISOU 2578 CA CYS A 323 13062 13536 14259 -306 85 -672 C ATOM 2579 C CYS A 323 -22.299 16.160 52.108 1.00108.88 C ANISOU 2579 C CYS A 323 13217 13704 14447 -318 80 -647 C ATOM 2580 O CYS A 323 -22.093 16.831 51.098 1.00109.71 O ANISOU 2580 O CYS A 323 13312 13762 14613 -319 85 -606 O ATOM 2581 CB CYS A 323 -24.172 16.920 53.635 1.00106.65 C ANISOU 2581 CB CYS A 323 12921 13403 14197 -323 92 -754 C ATOM 2582 SG CYS A 323 -25.724 16.541 54.537 1.00113.91 S ANISOU 2582 SG CYS A 323 13855 14344 15083 -311 98 -798 S ATOM 2583 N GLY A 324 -21.316 15.634 52.834 1.00110.18 N ANISOU 2583 N GLY A 324 13379 13926 14561 -328 71 -670 N ATOM 2584 CA GLY A 324 -19.913 15.920 52.566 1.00112.35 C ANISOU 2584 CA GLY A 324 13635 14203 14850 -343 66 -656 C ATOM 2585 C GLY A 324 -19.039 14.685 52.549 1.00113.39 C ANISOU 2585 C GLY A 324 13783 14398 14902 -334 56 -623 C ATOM 2586 O GLY A 324 -18.553 14.293 51.492 1.00112.82 O ANISOU 2586 O GLY A 324 13722 14322 14822 -323 55 -560 O ATOM 2587 N LYS A 325 -18.837 14.074 53.718 1.00115.63 N ANISOU 2587 N LYS A 325 14066 14742 15126 -339 49 -664 N ATOM 2588 CA LYS A 325 -17.992 12.880 53.831 1.00119.84 C ANISOU 2588 CA LYS A 325 14611 15337 15585 -331 39 -633 C ATOM 2589 C LYS A 325 -18.506 11.835 54.843 1.00121.79 C ANISOU 2589 C LYS A 325 14871 15645 15759 -322 34 -653 C ATOM 2590 O LYS A 325 -19.468 11.125 54.561 1.00123.08 O ANISOU 2590 O LYS A 325 15061 15807 15897 -302 37 -627 O ATOM 2591 CB LYS A 325 -16.541 13.274 54.131 1.00121.80 C ANISOU 2591 CB LYS A 325 14831 15605 15842 -353 32 -648 C ATOM 2592 CG LYS A 325 -15.499 12.221 53.737 1.00124.36 C ANISOU 2592 CG LYS A 325 15166 15973 16113 -342 25 -595 C ATOM 2593 CD LYS A 325 -14.171 12.445 54.466 1.00127.05 C ANISOU 2593 CD LYS A 325 15477 16354 16444 -364 17 -623 C ATOM 2594 CE LYS A 325 -14.320 12.217 55.973 1.00128.28 C ANISOU 2594 CE LYS A 325 15619 16569 16553 -376 10 -683 C ATOM 2595 NZ LYS A 325 -13.095 12.559 56.747 1.00127.05 N ANISOU 2595 NZ LYS A 325 15429 16455 16390 -402 1 -717 N ATOM 2596 N ASN A 326 -17.865 11.744 56.011 1.00125.05 N ANISOU 2596 N ASN A 326 15263 16114 16137 -338 27 -695 N ATOM 2597 CA ASN A 326 -18.132 10.662 56.980 1.00126.31 C ANISOU 2597 CA ASN A 326 15429 16343 16220 -330 21 -702 C ATOM 2598 C ASN A 326 -18.812 11.088 58.285 1.00127.13 C ANISOU 2598 C ASN A 326 15514 16477 16314 -344 22 -774 C ATOM 2599 O ASN A 326 -19.541 10.313 58.909 1.00126.52 O ANISOU 2599 O ASN A 326 15446 16441 16186 -333 21 -776 O ATOM 2600 CB ASN A 326 -16.840 9.911 57.318 1.00125.61 C ANISOU 2600 CB ASN A 326 15330 16314 16082 -333 10 -681 C ATOM 2601 CG ASN A 326 -16.351 9.046 56.177 1.00125.13 C ANISOU 2601 CG ASN A 326 15293 16242 16009 -312 10 -607 C ATOM 2602 OD1 ASN A 326 -17.108 8.702 55.268 1.00121.18 O ANISOU 2602 OD1 ASN A 326 14820 15704 15519 -292 16 -570 O ATOM 2603 ND2 ASN A 326 -15.077 8.682 56.224 1.00125.54 N ANISOU 2603 ND2 ASN A 326 15332 16329 16039 -316 3 -587 N TER 2604 ASN A 326 HETATM 2605 C1 NAG B 1 -73.773 -12.212 40.843 1.00 43.52 C ANISOU 2605 C1 NAG B 1 5670 5433 5433 255 -113 -77 C HETATM 2606 C2 NAG B 1 -73.620 -11.430 39.538 1.00 46.18 C ANISOU 2606 C2 NAG B 1 5938 5785 5824 228 -94 -86 C HETATM 2607 C3 NAG B 1 -74.514 -10.201 39.566 1.00 52.07 C ANISOU 2607 C3 NAG B 1 6594 6525 6664 117 -79 -86 C HETATM 2608 C4 NAG B 1 -75.968 -10.556 39.867 1.00 50.65 C ANISOU 2608 C4 NAG B 1 6467 6310 6470 43 -93 -54 C HETATM 2609 C5 NAG B 1 -76.100 -11.483 41.076 1.00 58.52 C ANISOU 2609 C5 NAG B 1 7517 7313 7405 57 -107 -21 C HETATM 2610 C6 NAG B 1 -77.463 -12.171 40.979 1.00 61.46 C ANISOU 2610 C6 NAG B 1 7936 7649 7766 -63 -126 63 C HETATM 2611 C7 NAG B 1 -71.482 -10.943 38.357 1.00 51.70 C ANISOU 2611 C7 NAG B 1 6472 6688 6483 369 -49 -64 C HETATM 2612 C8 NAG B 1 -70.045 -10.482 38.611 1.00 55.85 C ANISOU 2612 C8 NAG B 1 6817 7402 7002 407 -34 -50 C HETATM 2613 N2 NAG B 1 -72.217 -11.002 39.460 1.00 48.35 N ANISOU 2613 N2 NAG B 1 6096 6184 6091 303 -76 -100 N HETATM 2614 O3 NAG B 1 -74.426 -9.462 38.328 1.00 55.31 O ANISOU 2614 O3 NAG B 1 6953 6939 7121 101 -50 -57 O HETATM 2615 O4 NAG B 1 -76.586 -9.333 40.225 1.00 56.27 O ANISOU 2615 O4 NAG B 1 7088 7066 7227 19 -80 -71 O HETATM 2616 O5 NAG B 1 -75.123 -12.546 41.145 1.00 55.07 O ANISOU 2616 O5 NAG B 1 7186 6828 6909 149 -124 -21 O HETATM 2617 O6 NAG B 1 -77.377 -13.206 39.980 1.00 83.64 O ANISOU 2617 O6 NAG B 1 10891 10316 10571 -91 -178 62 O HETATM 2618 O7 NAG B 1 -71.877 -11.188 37.218 1.00 60.84 O ANISOU 2618 O7 NAG B 1 7693 7816 7607 404 -41 -39 O HETATM 2619 C1 NAG B 2 -77.779 -9.065 39.494 1.00 42.93 C ANISOU 2619 C1 NAG B 2 5389 5386 5536 -30 -72 -35 C HETATM 2620 C2 NAG B 2 -78.582 -8.138 40.381 1.00 40.38 C ANISOU 2620 C2 NAG B 2 4999 5144 5199 4 -69 -49 C HETATM 2621 C3 NAG B 2 -79.873 -7.778 39.706 1.00 45.93 C ANISOU 2621 C3 NAG B 2 5666 5916 5870 -11 -56 -6 C HETATM 2622 C4 NAG B 2 -79.611 -7.263 38.284 1.00 51.72 C ANISOU 2622 C4 NAG B 2 6419 6579 6652 -2 -38 -3 C HETATM 2623 C5 NAG B 2 -78.760 -8.266 37.511 1.00 41.69 C ANISOU 2623 C5 NAG B 2 5208 5245 5389 -36 -47 2 C HETATM 2624 C6 NAG B 2 -78.471 -7.736 36.113 1.00 44.05 C ANISOU 2624 C6 NAG B 2 5501 5538 5700 15 -15 30 C HETATM 2625 C7 NAG B 2 -78.230 -8.518 42.797 1.00 55.20 C ANISOU 2625 C7 NAG B 2 6843 7150 6980 110 -91 -83 C HETATM 2626 C8 NAG B 2 -78.559 -9.432 43.985 1.00 43.34 C ANISOU 2626 C8 NAG B 2 5325 5770 5372 143 -78 -4 C HETATM 2627 N2 NAG B 2 -78.838 -8.835 41.654 1.00 55.97 N ANISOU 2627 N2 NAG B 2 6961 7205 7100 17 -76 -21 N HETATM 2628 O3 NAG B 2 -80.504 -6.781 40.505 1.00 61.90 O ANISOU 2628 O3 NAG B 2 7638 8030 7850 91 -56 -33 O HETATM 2629 O4 NAG B 2 -80.839 -7.127 37.572 1.00 68.40 O ANISOU 2629 O4 NAG B 2 8492 8792 8704 1 -32 36 O HETATM 2630 O5 NAG B 2 -77.537 -8.495 38.201 1.00 44.37 O ANISOU 2630 O5 NAG B 2 5563 5538 5757 -17 -51 -28 O HETATM 2631 O6 NAG B 2 -77.627 -8.664 35.436 1.00 55.76 O ANISOU 2631 O6 NAG B 2 7036 7006 7146 48 -28 22 O HETATM 2632 O7 NAG B 2 -77.451 -7.570 42.923 1.00 66.12 O ANISOU 2632 O7 NAG B 2 8215 8484 8424 159 -122 -188 O HETATM 2633 C1 BMA B 3 -81.335 -5.792 37.571 1.00 90.63 C ANISOU 2633 C1 BMA B 3 11285 11637 11512 112 -9 33 C HETATM 2634 C2 BMA B 3 -82.002 -5.579 36.201 1.00 99.12 C ANISOU 2634 C2 BMA B 3 12341 12781 12540 149 13 79 C HETATM 2635 C3 BMA B 3 -82.749 -4.254 36.200 1.00106.78 C ANISOU 2635 C3 BMA B 3 13304 13799 13466 306 37 92 C HETATM 2636 C4 BMA B 3 -83.724 -4.267 37.385 1.00107.76 C ANISOU 2636 C4 BMA B 3 13357 14100 13485 358 16 74 C HETATM 2637 C5 BMA B 3 -82.914 -4.308 38.701 1.00105.22 C ANISOU 2637 C5 BMA B 3 13080 13678 13223 343 -11 10 C HETATM 2638 C6 BMA B 3 -83.721 -4.167 40.020 1.00103.14 C ANISOU 2638 C6 BMA B 3 12748 13615 12826 465 -26 -6 C HETATM 2639 O2 BMA B 3 -82.936 -6.644 35.985 1.00102.21 O ANISOU 2639 O2 BMA B 3 12668 13319 12847 58 -26 94 O HETATM 2640 O3 BMA B 3 -83.380 -3.936 34.927 1.00114.68 O ANISOU 2640 O3 BMA B 3 14282 14893 14399 387 67 146 O HETATM 2641 O4 BMA B 3 -84.557 -3.116 37.342 1.00124.28 O ANISOU 2641 O4 BMA B 3 15454 16280 15487 564 30 77 O HETATM 2642 O5 BMA B 3 -82.197 -5.564 38.739 1.00 96.05 O ANISOU 2642 O5 BMA B 3 11918 12462 12115 176 -21 23 O HETATM 2643 O6 BMA B 3 -83.566 -2.836 40.534 1.00 97.94 O ANISOU 2643 O6 BMA B 3 12187 12858 12166 667 -62 -105 O HETATM 2644 C1 MAN B 4 -83.963 -5.065 34.204 1.00122.37 C ANISOU 2644 C1 MAN B 4 15179 16023 15291 297 33 147 C HETATM 2645 C2 MAN B 4 -83.326 -5.188 32.821 1.00123.31 C ANISOU 2645 C2 MAN B 4 15340 16093 15421 331 51 168 C HETATM 2646 C3 MAN B 4 -83.653 -3.936 32.006 1.00121.75 C ANISOU 2646 C3 MAN B 4 15148 15936 15175 521 119 245 C HETATM 2647 C4 MAN B 4 -85.164 -3.812 31.814 1.00126.11 C ANISOU 2647 C4 MAN B 4 15598 16751 15566 612 98 240 C HETATM 2648 C5 MAN B 4 -85.913 -3.939 33.161 1.00128.34 C ANISOU 2648 C5 MAN B 4 15813 17134 15818 559 64 207 C HETATM 2649 C6 MAN B 4 -87.424 -4.158 32.912 1.00130.56 C ANISOU 2649 C6 MAN B 4 15920 17768 15918 596 30 219 C HETATM 2650 O2 MAN B 4 -83.861 -6.351 32.170 1.00120.46 O ANISOU 2650 O2 MAN B 4 14936 15854 14979 252 -26 118 O HETATM 2651 O3 MAN B 4 -83.011 -3.983 30.734 1.00114.68 O ANISOU 2651 O3 MAN B 4 14272 15036 14267 585 156 301 O HETATM 2652 O4 MAN B 4 -85.441 -2.543 31.211 1.00130.86 O ANISOU 2652 O4 MAN B 4 16239 17369 16114 837 168 321 O HETATM 2653 O5 MAN B 4 -85.418 -5.014 34.029 1.00126.94 O ANISOU 2653 O5 MAN B 4 15636 16869 15725 349 16 166 O HETATM 2654 O6 MAN B 4 -88.057 -2.912 32.574 1.00132.51 O ANISOU 2654 O6 MAN B 4 16170 18133 16046 872 86 263 O HETATM 2655 C1 NAG C 1 -64.309 -25.962 42.506 1.00135.28 C ANISOU 2655 C1 NAG C 1 18122 16574 16706 358 348 305 C HETATM 2656 C2 NAG C 1 -63.455 -26.779 41.508 1.00137.81 C ANISOU 2656 C2 NAG C 1 18411 17008 16944 317 398 336 C HETATM 2657 C3 NAG C 1 -63.587 -28.281 41.803 1.00142.36 C ANISOU 2657 C3 NAG C 1 18989 17601 17502 374 460 259 C HETATM 2658 C4 NAG C 1 -63.108 -28.596 43.225 1.00145.12 C ANISOU 2658 C4 NAG C 1 19359 17904 17875 404 469 236 C HETATM 2659 C5 NAG C 1 -63.866 -27.752 44.267 1.00141.35 C ANISOU 2659 C5 NAG C 1 18895 17387 17426 419 450 228 C HETATM 2660 C6 NAG C 1 -62.839 -27.241 45.288 1.00135.79 C ANISOU 2660 C6 NAG C 1 18189 16675 16730 426 439 219 C HETATM 2661 C7 NAG C 1 -63.606 -25.369 39.449 1.00140.63 C ANISOU 2661 C7 NAG C 1 18706 17456 17271 155 280 520 C HETATM 2662 C8 NAG C 1 -64.083 -25.338 37.996 1.00139.52 C ANISOU 2662 C8 NAG C 1 18510 17439 17062 73 262 596 C HETATM 2663 N2 NAG C 1 -63.846 -26.514 40.102 1.00136.79 N ANISOU 2663 N2 NAG C 1 18246 16951 16777 254 372 398 N HETATM 2664 O3 NAG C 1 -62.819 -29.032 40.860 1.00145.83 O ANISOU 2664 O3 NAG C 1 19372 18151 17886 373 474 219 O HETATM 2665 O4 NAG C 1 -63.261 -30.001 43.519 1.00153.43 O ANISOU 2665 O4 NAG C 1 20410 18943 18946 427 468 206 O HETATM 2666 O5 NAG C 1 -64.714 -26.673 43.735 1.00140.15 O ANISOU 2666 O5 NAG C 1 18743 17199 17311 418 399 229 O HETATM 2667 O6 NAG C 1 -63.513 -26.847 46.485 1.00134.90 O ANISOU 2667 O6 NAG C 1 18051 16588 16618 461 426 161 O HETATM 2668 O7 NAG C 1 -63.068 -24.378 39.941 1.00142.54 O ANISOU 2668 O7 NAG C 1 18960 17622 17578 117 191 583 O HETATM 2669 C1 NAG C 2 -61.965 -30.550 43.925 1.00159.45 C ANISOU 2669 C1 NAG C 2 21159 19705 19719 440 454 180 C HETATM 2670 C2 NAG C 2 -62.071 -31.433 45.193 1.00159.96 C ANISOU 2670 C2 NAG C 2 21235 19714 19830 430 414 212 C HETATM 2671 C3 NAG C 2 -61.457 -32.821 44.971 1.00160.91 C ANISOU 2671 C3 NAG C 2 21333 19772 20031 458 324 164 C HETATM 2672 C4 NAG C 2 -61.846 -33.453 43.627 1.00162.70 C ANISOU 2672 C4 NAG C 2 21528 20002 20290 505 287 75 C HETATM 2673 C5 NAG C 2 -61.606 -32.507 42.430 1.00160.59 C ANISOU 2673 C5 NAG C 2 21226 19871 19920 517 369 25 C HETATM 2674 C6 NAG C 2 -62.822 -32.466 41.478 1.00158.29 C ANISOU 2674 C6 NAG C 2 20931 19602 19610 512 384 27 C HETATM 2675 C7 NAG C 2 -61.904 -30.469 47.484 1.00157.47 C ANISOU 2675 C7 NAG C 2 20916 19458 19458 389 443 275 C HETATM 2676 C8 NAG C 2 -60.950 -29.831 48.506 1.00152.66 C ANISOU 2676 C8 NAG C 2 20300 18877 18828 391 457 268 C HETATM 2677 N2 NAG C 2 -61.342 -30.800 46.317 1.00159.98 N ANISOU 2677 N2 NAG C 2 21244 19733 19809 417 434 237 N HETATM 2678 O3 NAG C 2 -61.856 -33.687 46.037 1.00160.95 O ANISOU 2678 O3 NAG C 2 21345 19710 20097 406 240 255 O HETATM 2679 O4 NAG C 2 -61.068 -34.643 43.449 1.00165.63 O ANISOU 2679 O4 NAG C 2 21854 20312 20765 565 165 -31 O HETATM 2680 O5 NAG C 2 -61.220 -31.156 42.816 1.00160.48 O ANISOU 2680 O5 NAG C 2 21235 19901 19837 470 437 100 O HETATM 2681 O6 NAG C 2 -62.380 -32.205 40.143 1.00153.12 O ANISOU 2681 O6 NAG C 2 20197 19109 18871 523 408 -48 O HETATM 2682 O7 NAG C 2 -63.095 -30.634 47.751 1.00158.29 O ANISOU 2682 O7 NAG C 2 20998 19611 19534 363 440 302 O HETATM 2683 C1 BOG A 601 -18.466 -24.783 46.928 1.00132.48 C ANISOU 2683 C1 BOG A 601 16930 17240 16165 2018 509 -507 C HETATM 2684 O1 BOG A 601 -19.796 -24.444 46.494 1.00127.04 O ANISOU 2684 O1 BOG A 601 16278 16329 15664 1704 658 -370 O HETATM 2685 C2 BOG A 601 -18.308 -24.264 48.364 1.00131.39 C ANISOU 2685 C2 BOG A 601 16836 17327 15761 2430 359 -633 C HETATM 2686 O2 BOG A 601 -18.375 -22.836 48.368 1.00127.45 O ANISOU 2686 O2 BOG A 601 16110 16904 15413 2220 150 -865 O HETATM 2687 C3 BOG A 601 -16.977 -24.703 48.979 1.00136.17 C ANISOU 2687 C3 BOG A 601 17415 18213 16111 2874 185 -812 C HETATM 2688 O3 BOG A 601 -17.007 -24.410 50.378 1.00130.01 O ANISOU 2688 O3 BOG A 601 16737 17646 15016 3354 77 -899 O HETATM 2689 C4 BOG A 601 -16.694 -26.204 48.741 1.00142.62 C ANISOU 2689 C4 BOG A 601 18446 18939 16806 3057 411 -579 C HETATM 2690 O4 BOG A 601 -15.345 -26.525 49.104 1.00144.81 O ANISOU 2690 O4 BOG A 601 18648 19501 16873 3432 209 -788 O HETATM 2691 C5 BOG A 601 -16.918 -26.604 47.271 1.00142.83 C ANISOU 2691 C5 BOG A 601 18404 18711 17155 2563 561 -457 C HETATM 2692 O5 BOG A 601 -18.251 -26.222 46.833 1.00139.86 O ANISOU 2692 O5 BOG A 601 18055 18089 16996 2202 718 -316 O HETATM 2693 C6 BOG A 601 -16.701 -28.124 47.135 1.00142.98 C ANISOU 2693 C6 BOG A 601 18645 18618 17063 2763 812 -234 C HETATM 2694 O6 BOG A 601 -16.416 -28.449 45.772 1.00141.54 O ANISOU 2694 O6 BOG A 601 18330 18314 17137 2385 836 -237 O HETATM 2695 C1' BOG A 601 -19.898 -24.467 45.056 1.00113.65 C ANISOU 2695 C1' BOG A 601 14462 14493 14225 1308 692 -362 C HETATM 2696 C2' BOG A 601 -21.290 -23.983 44.641 1.00 97.52 C ANISOU 2696 C2' BOG A 601 12428 12274 12352 1031 795 -281 C HETATM 2697 C3' BOG A 601 -21.235 -23.292 43.282 1.00 91.03 C ANISOU 2697 C3' BOG A 601 11431 11417 11740 685 709 -372 C HETATM 2698 C4' BOG A 601 -22.251 -22.158 43.209 1.00 85.20 C ANISOU 2698 C4' BOG A 601 10649 10631 11093 510 680 -393 C HETATM 2699 C5' BOG A 601 -23.514 -22.636 42.506 1.00 82.02 C ANISOU 2699 C5' BOG A 601 10296 10055 10813 344 837 -293 C HETATM 2700 C6' BOG A 601 -23.573 -22.097 41.083 1.00 83.34 C ANISOU 2700 C6' BOG A 601 10352 10205 11110 115 778 -356 C HETATM 2701 C7' BOG A 601 -24.993 -22.214 40.532 1.00 83.26 C ANISOU 2701 C7' BOG A 601 10347 10083 11204 -8 864 -342 C HETATM 2702 C8' BOG A 601 -25.225 -21.182 39.429 1.00 84.30 C ANISOU 2702 C8' BOG A 601 10402 10248 11380 -138 772 -406 C HETATM 2703 C1 BOG A 602 -64.287 5.163 49.599 1.00 97.42 C ANISOU 2703 C1 BOG A 602 10903 13421 12689 1854 61 -2403 C HETATM 2704 O1 BOG A 602 -62.859 5.401 49.771 1.00 84.42 O ANISOU 2704 O1 BOG A 602 9626 11615 10836 1752 127 -1994 O HETATM 2705 C2 BOG A 602 -65.194 6.370 49.778 1.00103.64 C ANISOU 2705 C2 BOG A 602 11765 14346 13267 2091 -10 -2397 C HETATM 2706 O2 BOG A 602 -64.745 7.125 50.892 1.00110.59 O ANISOU 2706 O2 BOG A 602 12973 15007 14038 1963 154 -1979 O HETATM 2707 C3 BOG A 602 -66.595 5.854 50.067 1.00112.07 C ANISOU 2707 C3 BOG A 602 12401 15467 14712 2055 20 -2805 C HETATM 2708 O3 BOG A 602 -67.507 6.948 50.181 1.00122.16 O ANISOU 2708 O3 BOG A 602 13720 16902 15794 2299 -67 -2836 O HETATM 2709 C4 BOG A 602 -67.077 4.930 48.953 1.00118.49 C ANISOU 2709 C4 BOG A 602 12789 16504 15729 2163 -156 -3343 C HETATM 2710 O4 BOG A 602 -68.215 4.237 49.453 1.00120.39 O ANISOU 2710 O4 BOG A 602 12588 16676 16477 2006 -25 -3721 O HETATM 2711 C5 BOG A 602 -65.999 3.915 48.502 1.00122.38 C ANISOU 2711 C5 BOG A 602 13286 16895 16318 1992 -128 -3311 C HETATM 2712 O5 BOG A 602 -64.675 4.523 48.362 1.00115.08 O ANISOU 2712 O5 BOG A 602 12828 15909 14987 2030 -141 -2844 O HETATM 2713 C6 BOG A 602 -66.476 3.217 47.191 1.00127.09 C ANISOU 2713 C6 BOG A 602 13483 17792 17015 2202 -377 -3884 C HETATM 2714 O6 BOG A 602 -65.395 3.074 46.259 1.00121.42 O ANISOU 2714 O6 BOG A 602 12964 17163 16009 2321 -511 -3768 O HETATM 2715 C1' BOG A 602 -62.187 6.477 49.086 1.00 73.48 C ANISOU 2715 C1' BOG A 602 8566 10327 9026 1990 20 -1779 C HETATM 2716 C2' BOG A 602 -60.722 6.014 49.190 1.00 70.13 C ANISOU 2716 C2' BOG A 602 8322 9709 8614 1776 113 -1530 C HETATM 2717 C3' BOG A 602 -59.698 7.141 49.422 1.00 66.52 C ANISOU 2717 C3' BOG A 602 8259 9127 7890 1800 183 -1157 C HETATM 2718 C4' BOG A 602 -58.263 6.591 49.309 1.00 68.00 C ANISOU 2718 C4' BOG A 602 8555 9169 8111 1621 242 -1002 C HETATM 2719 C5' BOG A 602 -57.193 7.694 49.376 1.00 75.09 C ANISOU 2719 C5' BOG A 602 9787 9935 8811 1645 326 -710 C HETATM 2720 C6' BOG A 602 -55.768 7.110 49.259 1.00 73.96 C ANISOU 2720 C6' BOG A 602 9708 9658 8735 1466 378 -603 C HETATM 2721 C7' BOG A 602 -54.685 8.196 49.388 1.00 68.06 C ANISOU 2721 C7' BOG A 602 9234 8744 7882 1457 496 -375 C HETATM 2722 C8' BOG A 602 -53.312 7.602 49.747 1.00 62.13 C ANISOU 2722 C8' BOG A 602 8496 7841 7268 1222 547 -303 C HETATM 2723 C1 PLM A 701 -25.546 15.424 55.984 1.00121.11 C ANISOU 2723 C1 PLM A 701 15477 15517 15021 -1033 583 300 C HETATM 2724 O2 PLM A 701 -24.441 15.377 56.587 1.00118.20 O ANISOU 2724 O2 PLM A 701 15013 15197 14700 -1131 636 91 O HETATM 2725 C2 PLM A 701 -26.783 14.884 56.781 1.00115.55 C ANISOU 2725 C2 PLM A 701 14783 14746 14374 -834 443 299 C HETATM 2726 C3 PLM A 701 -26.610 13.446 57.358 1.00112.18 C ANISOU 2726 C3 PLM A 701 14233 14468 13920 -745 348 111 C HETATM 2727 C4 PLM A 701 -27.578 13.116 58.534 1.00104.25 C ANISOU 2727 C4 PLM A 701 13235 13369 13006 -600 257 91 C HETATM 2728 C5 PLM A 701 -28.283 11.739 58.391 1.00 94.58 C ANISOU 2728 C5 PLM A 701 11965 12231 11741 -481 171 70 C HETATM 2729 C6 PLM A 701 -28.437 10.943 59.714 1.00 84.75 C ANISOU 2729 C6 PLM A 701 10669 10966 10567 -380 119 -10 C HETATM 2730 C7 PLM A 701 -29.915 10.820 60.192 1.00 77.62 C ANISOU 2730 C7 PLM A 701 9812 9976 9706 -284 66 60 C HETATM 2731 C8 PLM A 701 -30.505 9.384 60.147 1.00 73.40 C ANISOU 2731 C8 PLM A 701 9232 9469 9187 -209 36 31 C HETATM 2732 C9 PLM A 701 -32.036 9.415 59.899 1.00 71.90 C ANISOU 2732 C9 PLM A 701 9075 9244 8999 -166 4 80 C HETATM 2733 CA PLM A 701 -32.719 8.039 59.671 1.00 71.01 C ANISOU 2733 CA PLM A 701 8903 9149 8928 -134 8 12 C HETATM 2734 CB PLM A 701 -34.256 8.198 59.762 1.00 72.27 C ANISOU 2734 CB PLM A 701 9073 9295 9090 -97 -19 26 C HETATM 2735 CC PLM A 701 -35.090 6.972 59.317 1.00 71.23 C ANISOU 2735 CC PLM A 701 8861 9197 9006 -103 9 -85 C HETATM 2736 CD PLM A 701 -36.597 7.203 59.607 1.00 65.17 C ANISOU 2736 CD PLM A 701 8084 8442 8237 -72 -15 -98 C HETATM 2737 CE PLM A 701 -37.513 6.286 58.777 1.00 72.13 C ANISOU 2737 CE PLM A 701 8853 9423 9129 -101 14 -258 C HETATM 2738 CF PLM A 701 -38.962 6.206 59.311 1.00 69.05 C ANISOU 2738 CF PLM A 701 8423 9042 8769 -91 18 -318 C HETATM 2739 CG PLM A 701 -39.965 6.876 58.360 1.00 70.19 C ANISOU 2739 CG PLM A 701 8496 9395 8777 -36 -58 -373 C HETATM 2740 C1 RET A 801 -43.137 -16.091 34.573 1.00 69.47 C ANISOU 2740 C1 RET A 801 8637 8838 8921 212 205 15 C HETATM 2741 C2 RET A 801 -43.403 -17.632 34.691 1.00 69.47 C ANISOU 2741 C2 RET A 801 8633 8724 9040 220 370 26 C HETATM 2742 C3 RET A 801 -44.631 -18.091 34.082 1.00 75.42 C ANISOU 2742 C3 RET A 801 9352 9426 9877 133 432 -101 C HETATM 2743 C4 RET A 801 -45.849 -17.295 34.371 1.00 74.23 C ANISOU 2743 C4 RET A 801 9194 9330 9679 110 360 -139 C HETATM 2744 C5 RET A 801 -45.641 -15.813 34.274 1.00 71.94 C ANISOU 2744 C5 RET A 801 8918 9151 9267 126 205 -110 C HETATM 2745 C6 RET A 801 -44.446 -15.269 34.526 1.00 75.28 C ANISOU 2745 C6 RET A 801 9363 9602 9637 171 151 -39 C HETATM 2746 C7 RET A 801 -44.266 -13.812 34.735 1.00 75.47 C ANISOU 2746 C7 RET A 801 9390 9689 9596 182 58 -25 C HETATM 2747 C8 RET A 801 -44.965 -13.011 35.523 1.00 67.93 C ANISOU 2747 C8 RET A 801 8435 8752 8624 189 30 -21 C HETATM 2748 C9 RET A 801 -44.749 -11.577 35.697 1.00 64.73 C ANISOU 2748 C9 RET A 801 8018 8372 8204 186 -12 -30 C HETATM 2749 C10 RET A 801 -45.313 -10.999 36.765 1.00 63.51 C ANISOU 2749 C10 RET A 801 7853 8233 8044 192 -19 -42 C HETATM 2750 C11 RET A 801 -45.282 -9.635 37.198 1.00 61.37 C ANISOU 2750 C11 RET A 801 7555 7966 7798 176 -20 -84 C HETATM 2751 C12 RET A 801 -46.021 -9.215 38.247 1.00 69.10 C ANISOU 2751 C12 RET A 801 8517 8966 8773 176 -21 -112 C HETATM 2752 C13 RET A 801 -46.084 -7.886 38.802 1.00 74.14 C ANISOU 2752 C13 RET A 801 9111 9596 9463 144 6 -187 C HETATM 2753 C14 RET A 801 -46.966 -7.644 39.806 1.00 71.07 C ANISOU 2753 C14 RET A 801 8706 9236 9063 145 1 -214 C HETATM 2754 C15 RET A 801 -47.183 -6.386 40.492 1.00 71.44 C ANISOU 2754 C15 RET A 801 8696 9271 9176 104 47 -314 C HETATM 2755 C16 RET A 801 -42.251 -15.672 33.449 1.00 62.43 C ANISOU 2755 C16 RET A 801 7738 7982 7999 183 146 -18 C HETATM 2756 C17 RET A 801 -42.398 -15.898 35.883 1.00 70.66 C ANISOU 2756 C17 RET A 801 8789 9050 9010 305 198 111 C HETATM 2757 C18 RET A 801 -46.870 -15.038 33.849 1.00 67.10 C ANISOU 2757 C18 RET A 801 8272 8612 8610 92 147 -175 C HETATM 2758 C19 RET A 801 -43.915 -10.860 34.676 1.00 63.33 C ANISOU 2758 C19 RET A 801 7833 8190 8041 176 -18 -32 C HETATM 2759 C20 RET A 801 -45.164 -6.837 38.241 1.00 77.12 C ANISOU 2759 C20 RET A 801 9455 9918 9931 109 66 -240 C HETATM 2760 O HOH A 349 -58.333 -13.027 38.924 1.00 57.46 O ANISOU 2760 O HOH A 349 6829 7344 7660 -144 132 -475 O HETATM 2761 O HOH A 350 -25.504 -3.861 29.858 1.00 59.12 O ANISOU 2761 O HOH A 350 7183 7464 7818 98 394 310 O HETATM 2762 O HOH A 351 -33.751 -11.689 42.039 1.00 63.97 O ANISOU 2762 O HOH A 351 7806 8587 7913 9 86 114 O HETATM 2763 O HOH A 352 -60.602 -1.121 51.287 1.00 38.19 O ANISOU 2763 O HOH A 352 4341 4966 5203 -214 493 -693 O HETATM 2764 O HOH A 353 -60.254 -10.376 37.581 1.00 50.25 O ANISOU 2764 O HOH A 353 5872 6862 6358 -43 52 -319 O CONECT 16 2655 CONECT 117 2605 CONECT 883 1484 CONECT 1484 883 CONECT 2368 2754 CONECT 2582 2723 CONECT 2605 117 2606 2616 CONECT 2606 2605 2607 2613 CONECT 2607 2606 2608 2614 CONECT 2608 2607 2609 2615 CONECT 2609 2608 2610 2616 CONECT 2610 2609 2617 CONECT 2611 2612 2613 2618 CONECT 2612 2611 CONECT 2613 2606 2611 CONECT 2614 2607 CONECT 2615 2608 2619 CONECT 2616 2605 2609 CONECT 2617 2610 CONECT 2618 2611 CONECT 2619 2615 2620 2630 CONECT 2620 2619 2621 2627 CONECT 2621 2620 2622 2628 CONECT 2622 2621 2623 2629 CONECT 2623 2622 2624 2630 CONECT 2624 2623 2631 CONECT 2625 2626 2627 2632 CONECT 2626 2625 CONECT 2627 2620 2625 CONECT 2628 2621 CONECT 2629 2622 2633 CONECT 2630 2619 2623 CONECT 2631 2624 CONECT 2632 2625 CONECT 2633 2629 2634 2642 CONECT 2634 2633 2635 2639 CONECT 2635 2634 2636 2640 CONECT 2636 2635 2637 2641 CONECT 2637 2636 2638 2642 CONECT 2638 2637 2643 CONECT 2639 2634 CONECT 2640 2635 2644 CONECT 2641 2636 CONECT 2642 2633 2637 CONECT 2643 2638 CONECT 2644 2640 2645 2653 CONECT 2645 2644 2646 2650 CONECT 2646 2645 2647 2651 CONECT 2647 2646 2648 2652 CONECT 2648 2647 2649 2653 CONECT 2649 2648 2654 CONECT 2650 2645 CONECT 2651 2646 CONECT 2652 2647 CONECT 2653 2644 2648 CONECT 2654 2649 CONECT 2655 16 2656 2666 CONECT 2656 2655 2657 2663 CONECT 2657 2656 2658 2664 CONECT 2658 2657 2659 2665 CONECT 2659 2658 2660 2666 CONECT 2660 2659 2667 CONECT 2661 2662 2663 2668 CONECT 2662 2661 CONECT 2663 2656 2661 CONECT 2664 2657 CONECT 2665 2658 2669 CONECT 2666 2655 2659 CONECT 2667 2660 CONECT 2668 2661 CONECT 2669 2665 2670 2680 CONECT 2670 2669 2671 2677 CONECT 2671 2670 2672 2678 CONECT 2672 2671 2673 2679 CONECT 2673 2672 2674 2680 CONECT 2674 2673 2681 CONECT 2675 2676 2677 2682 CONECT 2676 2675 CONECT 2677 2670 2675 CONECT 2678 2671 CONECT 2679 2672 CONECT 2680 2669 2673 CONECT 2681 2674 CONECT 2682 2675 CONECT 2683 2684 2685 2692 CONECT 2684 2683 2695 CONECT 2685 2683 2686 2687 CONECT 2686 2685 CONECT 2687 2685 2688 2689 CONECT 2688 2687 CONECT 2689 2687 2690 2691 CONECT 2690 2689 CONECT 2691 2689 2692 2693 CONECT 2692 2683 2691 CONECT 2693 2691 2694 CONECT 2694 2693 CONECT 2695 2684 2696 CONECT 2696 2695 2697 CONECT 2697 2696 2698 CONECT 2698 2697 2699 CONECT 2699 2698 2700 CONECT 2700 2699 2701 CONECT 2701 2700 2702 CONECT 2702 2701 CONECT 2703 2704 2705 2712 CONECT 2704 2703 2715 CONECT 2705 2703 2706 2707 CONECT 2706 2705 CONECT 2707 2705 2708 2709 CONECT 2708 2707 CONECT 2709 2707 2710 2711 CONECT 2710 2709 CONECT 2711 2709 2712 2713 CONECT 2712 2703 2711 CONECT 2713 2711 2714 CONECT 2714 2713 CONECT 2715 2704 2716 CONECT 2716 2715 2717 CONECT 2717 2716 2718 CONECT 2718 2717 2719 CONECT 2719 2718 2720 CONECT 2720 2719 2721 CONECT 2721 2720 2722 CONECT 2722 2721 CONECT 2723 2582 2724 2725 CONECT 2724 2723 CONECT 2725 2723 2726 CONECT 2726 2725 2727 CONECT 2727 2726 2728 CONECT 2728 2727 2729 CONECT 2729 2728 2730 CONECT 2730 2729 2731 CONECT 2731 2730 2732 CONECT 2732 2731 2733 CONECT 2733 2732 2734 CONECT 2734 2733 2735 CONECT 2735 2734 2736 CONECT 2736 2735 2737 CONECT 2737 2736 2738 CONECT 2738 2737 2739 CONECT 2739 2738 CONECT 2740 2741 2745 2755 2756 CONECT 2741 2740 2742 CONECT 2742 2741 2743 CONECT 2743 2742 2744 CONECT 2744 2743 2745 2757 CONECT 2745 2740 2744 2746 CONECT 2746 2745 2747 CONECT 2747 2746 2748 CONECT 2748 2747 2749 2758 CONECT 2749 2748 2750 CONECT 2750 2749 2751 CONECT 2751 2750 2752 CONECT 2752 2751 2753 2759 CONECT 2753 2752 2754 CONECT 2754 2368 2753 CONECT 2755 2740 CONECT 2756 2740 CONECT 2757 2744 CONECT 2758 2748 CONECT 2759 2752 MASTER 486 0 10 16 4 0 0 6 2752 1 161 27 END