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*** VIRAL PROTEIN 04-MAY-16 5JQ7 ***elNémo ID: 2411211922381880042Job options:ID = 2411211922381880042 JOBID = VIRAL PROTEIN 04-MAY-16 5JQ7 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER VIRAL PROTEIN 04-MAY-16 5JQ7 TITLE CRYSTAL STRUCTURE OF EBOLA GLYCOPROTEIN IN COMPLEX WITH TOREMIFENE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN 1,ENVELOPE GLYCOPROTEIN 1,ENVELOPE COMPND 3 GLYCOPROTEIN 1; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: GP1,2,GP,GP1,2,GP,GP1,2,GP; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ENVELOPE GLYCOPROTEIN 2; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: GP1,2,GP; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: EBOLA VIRUS - MAYINGA, ZAIRE, 1976; SOURCE 3 ORGANISM_TAXID: 128952; SOURCE 4 GENE: GP; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: EBOLA VIRUS - MAYINGA, ZAIRE, 1976; SOURCE 11 ORGANISM_TAXID: 128952; SOURCE 12 GENE: GP; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293T KEYWDS EBOLA VIRUS, FILOVIRIDAE, ENVELOPE GLYCOPROTEIN, PROTEIN INHIBITOR KEYWDS 2 COMPLEX, IBUPROFEN, TOREMIFENE, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.ZHAO,J.REN,D.I.STUART REVDAT 4 10-JAN-24 5JQ7 1 HETSYN LINK REVDAT 3 29-JUL-20 5JQ7 1 COMPND REMARK HETNAM LINK REVDAT 3 2 1 SITE ATOM REVDAT 2 13-JUL-16 5JQ7 1 JRNL REVDAT 1 29-JUN-16 5JQ7 0 JRNL AUTH Y.ZHAO,J.REN,K.HARLOS,D.M.JONES,A.ZELTINA,T.A.BOWDEN, JRNL AUTH 2 S.PADILLA-PARRA,E.E.FRY,D.I.STUART JRNL TITL TOREMIFENE INTERACTS WITH AND DESTABILIZES THE EBOLA VIRUS JRNL TITL 2 GLYCOPROTEIN. JRNL REF NATURE V. 535 168 2016 JRNL REFN ESSN 1476-4687 JRNL PMID 27362232 JRNL DOI 10.1038/NATURE18615 REMARK 2 REMARK 2 RESOLUTION. 2.69 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0135 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.15 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 20449 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) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.245 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1090 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.69 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1502 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.3000 REMARK 3 BIN FREE R VALUE SET COUNT : 88 REMARK 3 BIN FREE R VALUE : 0.3310 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3034 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 151 REMARK 3 SOLVENT ATOMS : 53 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.64 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.47000 REMARK 3 B22 (A**2) : 2.47000 REMARK 3 B33 (A**2) : -8.00000 REMARK 3 B12 (A**2) : 1.23000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.365 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.267 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.209 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.978 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3268 ; 0.007 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3004 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4448 ; 1.286 ; 1.992 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6910 ; 0.867 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 382 ; 6.173 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;37.173 ;24.110 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 485 ;12.318 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.229 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 507 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3618 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 756 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1546 ; 1.779 ; 6.179 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1545 ; 1.778 ; 6.175 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1922 ; 3.229 ; 9.233 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1923 ; 3.229 ; 9.238 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1722 ; 2.037 ; 6.696 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1723 ; 2.036 ; 6.701 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2527 ; 3.508 ; 9.972 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3392 ; 6.456 ;49.423 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3393 ; 6.455 ;49.439 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 : 4 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 30 A 190 REMARK 3 ORIGIN FOR THE GROUP (A): -55.5806 13.1695 -19.6225 REMARK 3 T TENSOR REMARK 3 T11: 0.1625 T22: 0.0203 REMARK 3 T33: 0.3222 T12: -0.0253 REMARK 3 T13: 0.0870 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 0.8661 L22: 2.0242 REMARK 3 L33: 3.2696 L12: -0.1770 REMARK 3 L13: 0.4511 L23: 0.3945 REMARK 3 S TENSOR REMARK 3 S11: -0.1196 S12: -0.0139 S13: -0.0889 REMARK 3 S21: 0.0614 S22: -0.0682 S23: 0.0857 REMARK 3 S31: 0.5259 S32: -0.2162 S33: 0.1878 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 211 A 477 REMARK 3 ORIGIN FOR THE GROUP (A): -46.6782 -5.4402 -38.8177 REMARK 3 T TENSOR REMARK 3 T11: 1.0075 T22: 0.1592 REMARK 3 T33: 0.4377 T12: 0.1955 REMARK 3 T13: 0.1508 T23: -0.0943 REMARK 3 L TENSOR REMARK 3 L11: 0.4045 L22: 4.0995 REMARK 3 L33: 4.0630 L12: 0.0457 REMARK 3 L13: -0.7834 L23: 2.9841 REMARK 3 S TENSOR REMARK 3 S11: -0.4267 S12: 0.0602 S13: -0.2758 REMARK 3 S21: 0.0090 S22: 0.2319 S23: -0.3448 REMARK 3 S31: 1.2604 S32: 0.2080 S33: 0.1948 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 : B 502 B 610 REMARK 3 ORIGIN FOR THE GROUP (A): -51.8364 17.9591 -8.2679 REMARK 3 T TENSOR REMARK 3 T11: 0.1718 T22: 0.0161 REMARK 3 T33: 0.3790 T12: -0.0132 REMARK 3 T13: 0.0379 T23: 0.0423 REMARK 3 L TENSOR REMARK 3 L11: 0.2987 L22: 1.1580 REMARK 3 L33: 2.2358 L12: 0.0474 REMARK 3 L13: 0.3968 L23: 0.2587 REMARK 3 S TENSOR REMARK 3 S11: -0.0078 S12: -0.0463 S13: -0.0340 REMARK 3 S21: 0.2444 S22: -0.0926 S23: -0.0599 REMARK 3 S31: 0.4820 S32: -0.0643 S33: 0.1003 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 : B 611 B 632 REMARK 3 ORIGIN FOR THE GROUP (A): -50.0384 30.9769 36.4189 REMARK 3 T TENSOR REMARK 3 T11: 1.1702 T22: 0.4870 REMARK 3 T33: 0.3200 T12: -0.1982 REMARK 3 T13: -0.1293 T23: 0.0810 REMARK 3 L TENSOR REMARK 3 L11: 1.0915 L22: 0.3693 REMARK 3 L33: 0.0314 L12: -0.1191 REMARK 3 L13: 0.1624 L23: -0.0429 REMARK 3 S TENSOR REMARK 3 S11: 0.4039 S12: -0.0678 S13: 0.1146 REMARK 3 S21: 0.2349 S22: -0.3979 S23: -0.1251 REMARK 3 S31: 0.0933 S32: 0.0299 S33: -0.0060 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 5JQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAY-16. REMARK 100 THE DEPOSITION ID IS D_1000221052. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-NOV-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9700 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21539 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 51.150 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 9.800 REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 5JQ3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 9% (W/V) PEG 6000 AND 0.1 M SODIUM REMARK 280 CITRATE TRIBASIC DIHYDRATE, PH 5.2, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K 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 56.72500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 32.75019 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 102.29000 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 56.72500 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 32.75019 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 102.29000 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 56.72500 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 32.75019 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 102.29000 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 56.72500 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 32.75019 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 102.29000 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 56.72500 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 32.75019 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 102.29000 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 56.72500 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 32.75019 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 102.29000 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 65.50039 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 204.58000 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 65.50039 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 204.58000 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 65.50039 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 204.58000 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 65.50039 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 204.58000 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 65.50039 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 204.58000 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 65.50039 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 204.58000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 37690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 55690 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 -0.500000 -0.866025 0.000000 -56.72500 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 98.25058 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -113.45000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 820 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 28 REMARK 465 THR A 29 REMARK 465 LYS A 191 REMARK 465 ASP A 192 REMARK 465 PHE A 193 REMARK 465 PHE A 194 REMARK 465 SER A 195 REMARK 465 SER A 196 REMARK 465 HIS A 197 REMARK 465 PRO A 198 REMARK 465 LEU A 199 REMARK 465 ARG A 200 REMARK 465 GLU A 201 REMARK 465 PRO A 202 REMARK 465 VAL A 203 REMARK 465 ASN A 204 REMARK 465 ALA A 205 REMARK 465 THR A 206 REMARK 465 GLU A 207 REMARK 465 ASP A 208 REMARK 465 PRO A 209 REMARK 465 SER A 210 REMARK 465 THR A 284 REMARK 465 ILE A 285 REMARK 465 GLY A 286 REMARK 465 LYS A 294 REMARK 465 LYS A 295 REMARK 465 ASN A 296 REMARK 465 LEU A 297 REMARK 465 THR A 298 REMARK 465 ARG A 299 REMARK 465 LYS A 300 REMARK 465 ILE A 301 REMARK 465 ARG A 302 REMARK 465 SER A 432 REMARK 465 THR A 433 REMARK 465 HIS A 434 REMARK 465 HIS A 435 REMARK 465 GLN A 436 REMARK 465 ASP A 437 REMARK 465 THR A 438 REMARK 465 GLY A 439 REMARK 465 GLU A 440 REMARK 465 GLU A 441 REMARK 465 SER A 442 REMARK 465 ALA A 443 REMARK 465 SER A 444 REMARK 465 SER A 445 REMARK 465 GLY A 446 REMARK 465 LYS A 447 REMARK 465 LEU A 448 REMARK 465 GLY A 449 REMARK 465 LEU A 450 REMARK 465 ILE A 451 REMARK 465 THR A 452 REMARK 465 ASN A 453 REMARK 465 THR A 454 REMARK 465 ILE A 455 REMARK 465 ALA A 456 REMARK 465 GLY A 457 REMARK 465 VAL A 458 REMARK 465 ALA A 459 REMARK 465 GLY A 460 REMARK 465 LEU A 461 REMARK 465 ILE A 462 REMARK 465 THR A 463 REMARK 465 GLY A 464 REMARK 465 GLY A 465 REMARK 465 ARG A 466 REMARK 465 ARG A 467 REMARK 465 THR A 468 REMARK 465 ARG A 469 REMARK 465 ARG A 470 REMARK 465 GLY B 633 REMARK 465 SER B 634 REMARK 465 GLY B 635 REMARK 465 TYR B 636 REMARK 465 ILE B 637 REMARK 465 PRO B 638 REMARK 465 GLU B 639 REMARK 465 ALA B 640 REMARK 465 PRO B 641 REMARK 465 ARG B 642 REMARK 465 ASP B 643 REMARK 465 GLY B 644 REMARK 465 GLN B 645 REMARK 465 ALA B 646 REMARK 465 TYR B 647 REMARK 465 VAL B 648 REMARK 465 ARG B 649 REMARK 465 LYS B 650 REMARK 465 ASP B 651 REMARK 465 GLY B 652 REMARK 465 GLU B 653 REMARK 465 TRP B 654 REMARK 465 VAL B 655 REMARK 465 LEU B 656 REMARK 465 LEU B 657 REMARK 465 SER B 658 REMARK 465 THR B 659 REMARK 465 PHE B 660 REMARK 465 LEU B 661 REMARK 465 GLY B 662 REMARK 465 THR B 663 REMARK 465 HIS B 664 REMARK 465 HIS B 665 REMARK 465 HIS B 666 REMARK 465 HIS B 667 REMARK 465 HIS B 668 REMARK 465 HIS B 669 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 190 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 162 -161.33 -109.97 REMARK 500 PRO A 187 -165.29 -69.36 REMARK 500 GLU A 229 72.55 -112.48 REMARK 500 ASN A 268 47.82 -106.67 REMARK 500 GLU A 304 67.30 -113.64 REMARK 500 UNK A 472 98.18 -161.54 REMARK 500 ASN B 550 43.51 -85.70 REMARK 500 HIS B 613 -65.48 -28.35 REMARK 500 ILE B 626 -39.79 -137.34 REMARK 500 ASP B 629 46.83 -94.61 REMARK 500 REMARK 500 REMARK: NULL DBREF 5JQ7 A 32 432 UNP Q05320 VGP_EBOZM 32 312 DBREF 5JQ7 A 433 470 UNP Q05320 VGP_EBOZM 464 501 DBREF 5JQ7 A 471 477 PDB 5JQ7 5JQ7 471 477 DBREF 5JQ7 B 502 632 UNP Q05320 VGP_EBOZM 502 632 SEQADV 5JQ7 GLU A 28 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 THR A 29 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLY A 30 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ARG A 31 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ALA A 42 UNP Q05320 THR 42 ENGINEERED MUTATION SEQADV 5JQ7 GLY B 633 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 SER B 634 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLY B 635 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 TYR B 636 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ILE B 637 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 PRO B 638 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLU B 639 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ALA B 640 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 PRO B 641 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ARG B 642 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ASP B 643 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLY B 644 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLN B 645 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ALA B 646 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 TYR B 647 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 VAL B 648 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ARG B 649 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 LYS B 650 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 ASP B 651 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLY B 652 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLU B 653 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 TRP B 654 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 VAL B 655 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 LEU B 656 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 LEU B 657 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 SER B 658 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 THR B 659 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 PHE B 660 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 LEU B 661 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 GLY B 662 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 THR B 663 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 664 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 665 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 666 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 667 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 668 UNP Q05320 EXPRESSION TAG SEQADV 5JQ7 HIS B 669 UNP Q05320 EXPRESSION TAG SEQRES 1 A 330 GLU THR GLY ARG SER ILE PRO LEU GLY VAL ILE HIS ASN SEQRES 2 A 330 SER ALA LEU GLN VAL SER ASP VAL ASP LYS LEU VAL CYS SEQRES 3 A 330 ARG ASP LYS LEU SER SER THR ASN GLN LEU ARG SER VAL SEQRES 4 A 330 GLY LEU ASN LEU GLU GLY ASN GLY VAL ALA THR ASP VAL SEQRES 5 A 330 PRO SER ALA THR LYS ARG TRP GLY PHE ARG SER GLY VAL SEQRES 6 A 330 PRO PRO LYS VAL VAL ASN TYR GLU ALA GLY GLU TRP ALA SEQRES 7 A 330 GLU ASN CYS TYR ASN LEU GLU ILE LYS LYS PRO ASP GLY SEQRES 8 A 330 SER GLU CYS LEU PRO ALA ALA PRO ASP GLY ILE ARG GLY SEQRES 9 A 330 PHE PRO ARG CYS ARG TYR VAL HIS LYS VAL SER GLY THR SEQRES 10 A 330 GLY PRO CYS ALA GLY ASP PHE ALA PHE HIS LYS GLU GLY SEQRES 11 A 330 ALA PHE PHE LEU TYR ASP ARG LEU ALA SER THR VAL ILE SEQRES 12 A 330 TYR ARG GLY THR THR PHE ALA GLU GLY VAL VAL ALA PHE SEQRES 13 A 330 LEU ILE LEU PRO GLN ALA LYS LYS ASP PHE PHE SER SER SEQRES 14 A 330 HIS PRO LEU ARG GLU PRO VAL ASN ALA THR GLU ASP PRO SEQRES 15 A 330 SER SER GLY TYR TYR SER THR THR ILE ARG TYR GLN ALA SEQRES 16 A 330 THR GLY PHE GLY THR ASN GLU THR GLU TYR LEU PHE GLU SEQRES 17 A 330 VAL ASP ASN LEU THR TYR VAL GLN LEU GLU SER ARG PHE SEQRES 18 A 330 THR PRO GLN PHE LEU LEU GLN LEU ASN GLU THR ILE TYR SEQRES 19 A 330 THR SER GLY LYS ARG SER ASN THR THR GLY LYS LEU ILE SEQRES 20 A 330 TRP LYS VAL ASN PRO GLU ILE ASP THR THR ILE GLY GLU SEQRES 21 A 330 TRP ALA PHE TRP GLU THR LYS LYS ASN LEU THR ARG LYS SEQRES 22 A 330 ILE ARG SER GLU GLU LEU SER PHE THR VAL VAL SER THR SEQRES 23 A 330 HIS HIS GLN ASP THR GLY GLU GLU SER ALA SER SER GLY SEQRES 24 A 330 LYS LEU GLY LEU ILE THR ASN THR ILE ALA GLY VAL ALA SEQRES 25 A 330 GLY LEU ILE THR GLY GLY ARG ARG THR ARG ARG UNK UNK SEQRES 26 A 330 UNK UNK UNK UNK UNK SEQRES 1 B 168 GLU ALA ILE VAL ASN ALA GLN PRO LYS CYS ASN PRO ASN SEQRES 2 B 168 LEU HIS TYR TRP THR THR GLN ASP GLU GLY ALA ALA ILE SEQRES 3 B 168 GLY LEU ALA TRP ILE PRO TYR PHE GLY PRO ALA ALA GLU SEQRES 4 B 168 GLY ILE TYR ILE GLU GLY LEU MET HIS ASN GLN ASP GLY SEQRES 5 B 168 LEU ILE CYS GLY LEU ARG GLN LEU ALA ASN GLU THR THR SEQRES 6 B 168 GLN ALA LEU GLN LEU PHE LEU ARG ALA THR THR GLU LEU SEQRES 7 B 168 ARG THR PHE SER ILE LEU ASN ARG LYS ALA ILE ASP PHE SEQRES 8 B 168 LEU LEU GLN ARG TRP GLY GLY THR CYS HIS ILE LEU GLY SEQRES 9 B 168 PRO ASP CYS CYS ILE GLU PRO HIS ASP TRP THR LYS ASN SEQRES 10 B 168 ILE THR ASP LYS ILE ASP GLN ILE ILE HIS ASP PHE VAL SEQRES 11 B 168 ASP GLY SER GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY SEQRES 12 B 168 GLN ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SEQRES 13 B 168 SER THR PHE LEU GLY THR HIS HIS HIS HIS HIS HIS HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET GOL A 605 6 HET GOL A 606 6 HET DMS A 607 4 HET T0R B 705 29 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GOL GLYCEROL HETNAM DMS DIMETHYL SULFOXIDE HETNAM T0R TOREMIFENE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 NAG 6(C8 H15 N O6) FORMUL 3 BMA C6 H12 O6 FORMUL 3 MAN C6 H12 O6 FORMUL 8 GOL 2(C3 H8 O3) FORMUL 10 DMS C2 H6 O S FORMUL 11 T0R C26 H28 CL N O FORMUL 12 HOH *53(H2 O) HELIX 1 AA1 SER A 59 ASN A 61 5 3 HELIX 2 AA2 GLU A 71 GLY A 74 5 4 HELIX 3 AA3 ASP A 78 LYS A 84 1 7 HELIX 4 AA4 THR A 249 GLY A 264 1 16 HELIX 5 AA5 ALA B 538 GLY B 541 5 4 HELIX 6 AA6 ASN B 550 ASP B 552 5 3 HELIX 7 AA7 GLY B 553 THR B 576 1 24 HELIX 8 AA8 SER B 583 GLY B 598 1 16 HELIX 9 AA9 PRO B 612 THR B 620 1 9 HELIX 10 AB1 ASP B 621 ILE B 626 5 6 SHEET 1 AA1 2 GLY A 36 HIS A 39 0 SHEET 2 AA1 2 ALA A 42 VAL A 45 -1 O GLN A 44 N VAL A 37 SHEET 1 AA2 6 LEU A 63 ASN A 69 0 SHEET 2 AA2 6 ALA A 177 ILE A 185 -1 O LEU A 184 N ARG A 64 SHEET 3 AA2 6 PHE A 159 LEU A 161 -1 N LEU A 161 O ALA A 177 SHEET 4 AA2 6 LEU A 165 SER A 167 -1 O SER A 167 N PHE A 160 SHEET 5 AA2 6 VAL A 96 ASN A 98 -1 N VAL A 97 O ALA A 166 SHEET 6 AA2 6 ARG B 580 THR B 581 1 O THR B 581 N VAL A 96 SHEET 1 AA3 2 TRP A 86 ARG A 89 0 SHEET 2 AA3 2 PHE A 151 HIS A 154 -1 O PHE A 153 N GLY A 87 SHEET 1 AA4 3 ALA A 101 GLU A 103 0 SHEET 2 AA4 3 LEU B 515 THR B 520 -1 O TRP B 518 N GLY A 102 SHEET 3 AA4 3 TYR B 543 MET B 548 -1 O ILE B 544 N THR B 519 SHEET 1 AA5 8 ALA A 105 LYS A 114 0 SHEET 2 AA5 8 CYS A 135 THR A 144 1 O HIS A 139 N CYS A 108 SHEET 3 AA5 8 THR A 216 THR A 223 1 O TYR A 220 N SER A 142 SHEET 4 AA5 8 GLU A 231 ASP A 237 -1 O GLU A 235 N ARG A 219 SHEET 5 AA5 8 THR A 240 GLN A 243 -1 O VAL A 242 N PHE A 234 SHEET 6 AA5 8 LEU A 273 VAL A 277 1 O LEU A 273 N TYR A 241 SHEET 7 AA5 8 UNK A 472 UNK A 476 1 O UNK A 474 N LYS A 276 SHEET 8 AA5 8 PHE A 308 THR A 309 -1 N THR A 309 O UNK A 475 SSBOND 1 CYS A 53 CYS B 609 1555 1555 2.03 SSBOND 2 CYS A 108 CYS A 135 1555 1555 2.04 SSBOND 3 CYS A 121 CYS A 147 1555 1555 2.03 SSBOND 4 CYS B 511 CYS B 556 1555 1555 2.05 SSBOND 5 CYS B 601 CYS B 608 1555 1555 2.04 LINK ND2 ASN A 228 C1 NAG A 602 1555 1555 1.45 LINK ND2 ASN A 238 C1 NAG A 603 1555 1555 1.45 LINK ND2 ASN A 257 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 268 C1 NAG A 604 1555 1555 1.45 LINK ND2 ASN B 563 C1 NAG C 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O6 BMA C 3 C1 MAN C 4 1555 1555 1.45 CRYST1 113.450 113.450 306.870 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 0.008814 0.005089 0.000000 0.00000 SCALE2 0.000000 0.010178 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003259 0.00000 ATOM 1 N GLY A 30 -73.703 17.659 -10.933 1.00111.61 N ANISOU 1 N GLY A 30 11466 15420 15520 -953 1777 -1251 N ATOM 2 CA GLY A 30 -72.420 18.220 -10.401 1.00111.67 C ANISOU 2 CA GLY A 30 11756 15186 15486 -754 1711 -1160 C ATOM 3 C GLY A 30 -72.035 17.658 -9.038 1.00114.79 C ANISOU 3 C GLY A 30 12348 15507 15760 -846 1894 -1081 C ATOM 4 O GLY A 30 -72.909 17.278 -8.255 1.00120.00 O ANISOU 4 O GLY A 30 12886 16356 16350 -979 2085 -1125 O ATOM 5 N ARG A 31 -70.728 17.590 -8.765 1.00112.77 N ANISOU 5 N ARG A 31 12391 14984 15471 -779 1837 -966 N ATOM 6 CA ARG A 31 -70.199 17.166 -7.452 1.00113.07 C ANISOU 6 CA ARG A 31 12657 14921 15381 -819 1972 -885 C ATOM 7 C ARG A 31 -68.750 17.652 -7.263 1.00105.44 C ANISOU 7 C ARG A 31 11948 13705 14407 -630 1830 -797 C ATOM 8 O ARG A 31 -68.013 17.819 -8.243 1.00104.01 O ANISOU 8 O ARG A 31 11820 13383 14315 -567 1668 -760 O ATOM 9 CB ARG A 31 -70.288 15.635 -7.293 1.00118.70 C ANISOU 9 CB ARG A 31 13501 15564 16035 -1131 2128 -805 C ATOM 10 CG ARG A 31 -69.889 15.067 -5.924 1.00123.25 C ANISOU 10 CG ARG A 31 14326 16045 16458 -1199 2282 -719 C ATOM 11 CD ARG A 31 -70.702 15.618 -4.750 1.00127.63 C ANISOU 11 CD ARG A 31 14758 16821 16912 -1146 2436 -793 C ATOM 12 NE ARG A 31 -72.150 15.416 -4.899 1.00133.70 N ANISOU 12 NE ARG A 31 15219 17883 17697 -1316 2581 -895 N ATOM 13 CZ ARG A 31 -72.928 14.616 -4.153 1.00138.56 C ANISOU 13 CZ ARG A 31 15811 18628 18207 -1563 2818 -890 C ATOM 14 NH1 ARG A 31 -72.445 13.885 -3.145 1.00140.22 N ANISOU 14 NH1 ARG A 31 16320 18688 18268 -1676 2949 -780 N ATOM 15 NH2 ARG A 31 -74.232 14.548 -4.420 1.00141.02 N ANISOU 15 NH2 ARG A 31 15789 19233 18556 -1706 2926 -998 N ATOM 16 N SER A 32 -68.370 17.894 -6.004 1.00 97.96 N ANISOU 16 N SER A 32 11150 12719 13349 -544 1892 -768 N ATOM 17 CA SER A 32 -67.029 18.365 -5.618 1.00 89.79 C ANISOU 17 CA SER A 32 10350 11472 12294 -376 1763 -693 C ATOM 18 C SER A 32 -65.875 17.524 -6.185 1.00 81.81 C ANISOU 18 C SER A 32 9543 10223 11317 -454 1688 -572 C ATOM 19 O SER A 32 -65.896 16.293 -6.108 1.00 82.55 O ANISOU 19 O SER A 32 9746 10253 11364 -650 1799 -509 O ATOM 20 CB SER A 32 -66.922 18.398 -4.087 1.00 91.59 C ANISOU 20 CB SER A 32 10730 11702 12367 -336 1876 -675 C ATOM 21 OG SER A 32 -65.660 18.885 -3.660 1.00 93.08 O ANISOU 21 OG SER A 32 11130 11701 12532 -175 1738 -613 O ATOM 22 N ILE A 33 -64.868 18.198 -6.737 1.00 73.38 N ANISOU 22 N ILE A 33 8531 9024 10325 -299 1503 -543 N ATOM 23 CA ILE A 33 -63.693 17.520 -7.283 1.00 67.77 C ANISOU 23 CA ILE A 33 7991 8108 9649 -335 1427 -438 C ATOM 24 C ILE A 33 -62.880 16.945 -6.124 1.00 66.23 C ANISOU 24 C ILE A 33 8044 7780 9339 -334 1474 -350 C ATOM 25 O ILE A 33 -62.496 17.687 -5.230 1.00 63.73 O ANISOU 25 O ILE A 33 7792 7454 8968 -194 1429 -356 O ATOM 26 CB ILE A 33 -62.804 18.455 -8.127 1.00 64.40 C ANISOU 26 CB ILE A 33 7545 7596 9325 -177 1230 -429 C ATOM 27 CG1 ILE A 33 -63.566 18.929 -9.368 1.00 63.65 C ANISOU 27 CG1 ILE A 33 7243 7610 9331 -178 1171 -505 C ATOM 28 CG2 ILE A 33 -61.528 17.740 -8.565 1.00 63.32 C ANISOU 28 CG2 ILE A 33 7574 7270 9212 -199 1170 -324 C ATOM 29 CD1 ILE A 33 -62.921 20.092 -10.082 1.00 62.32 C ANISOU 29 CD1 ILE A 33 7051 7384 9244 -17 988 -509 C ATOM 30 N PRO A 34 -62.617 15.625 -6.138 1.00 65.52 N ANISOU 30 N PRO A 34 8110 7577 9204 -482 1552 -272 N ATOM 31 CA PRO A 34 -61.850 15.028 -5.049 1.00 65.45 C ANISOU 31 CA PRO A 34 8359 7432 9075 -468 1584 -185 C ATOM 32 C PRO A 34 -60.429 15.544 -4.951 1.00 63.86 C ANISOU 32 C PRO A 34 8263 7097 8901 -282 1411 -134 C ATOM 33 O PRO A 34 -59.807 15.830 -5.971 1.00 63.37 O ANISOU 33 O PRO A 34 8134 6987 8955 -224 1289 -127 O ATOM 34 CB PRO A 34 -61.805 13.537 -5.405 1.00 66.39 C ANISOU 34 CB PRO A 34 8627 7433 9164 -649 1669 -116 C ATOM 35 CG PRO A 34 -62.872 13.336 -6.407 1.00 67.82 C ANISOU 35 CG PRO A 34 8611 7732 9423 -803 1727 -182 C ATOM 36 CD PRO A 34 -62.990 14.623 -7.151 1.00 66.25 C ANISOU 36 CD PRO A 34 8177 7648 9346 -660 1601 -261 C ATOM 37 N LEU A 35 -59.938 15.635 -3.721 1.00 64.49 N ANISOU 37 N LEU A 35 8509 7125 8868 -202 1406 -99 N ATOM 38 CA LEU A 35 -58.571 15.999 -3.413 1.00 63.53 C ANISOU 38 CA LEU A 35 8503 6882 8751 -43 1245 -48 C ATOM 39 C LEU A 35 -57.942 14.842 -2.642 1.00 65.13 C ANISOU 39 C LEU A 35 8973 6942 8832 -67 1282 46 C ATOM 40 O LEU A 35 -58.470 14.410 -1.622 1.00 66.41 O ANISOU 40 O LEU A 35 9268 7114 8848 -130 1405 59 O ATOM 41 CB LEU A 35 -58.569 17.272 -2.571 1.00 63.69 C ANISOU 41 CB LEU A 35 8493 6970 8734 94 1175 -105 C ATOM 42 CG LEU A 35 -57.230 17.867 -2.133 1.00 63.16 C ANISOU 42 CG LEU A 35 8524 6803 8670 250 990 -70 C ATOM 43 CD1 LEU A 35 -56.344 18.185 -3.325 1.00 60.97 C ANISOU 43 CD1 LEU A 35 8140 6475 8551 291 845 -50 C ATOM 44 CD2 LEU A 35 -57.481 19.121 -1.305 1.00 63.09 C ANISOU 44 CD2 LEU A 35 8497 6864 8611 363 938 -145 C ATOM 45 N GLY A 36 -56.825 14.333 -3.145 1.00 66.10 N ANISOU 45 N GLY A 36 9175 6934 9005 -12 1179 111 N ATOM 46 CA GLY A 36 -56.093 13.255 -2.492 1.00 68.07 C ANISOU 46 CA GLY A 36 9689 7031 9143 7 1179 201 C ATOM 47 C GLY A 36 -55.254 13.759 -1.331 1.00 69.13 C ANISOU 47 C GLY A 36 9945 7129 9191 164 1065 223 C ATOM 48 O GLY A 36 -54.579 14.770 -1.443 1.00 69.81 O ANISOU 48 O GLY A 36 9915 7248 9359 287 915 195 O ATOM 49 N VAL A 37 -55.296 13.039 -0.217 1.00 71.68 N ANISOU 49 N VAL A 37 10516 7377 9341 149 1130 275 N ATOM 50 CA VAL A 37 -54.478 13.337 0.957 1.00 72.43 C ANISOU 50 CA VAL A 37 10773 7420 9326 298 1014 303 C ATOM 51 C VAL A 37 -54.094 12.011 1.629 1.00 74.92 C ANISOU 51 C VAL A 37 11405 7574 9484 296 1048 399 C ATOM 52 O VAL A 37 -54.801 11.011 1.480 1.00 75.49 O ANISOU 52 O VAL A 37 11590 7596 9495 141 1207 433 O ATOM 53 CB VAL A 37 -55.239 14.286 1.918 1.00 72.63 C ANISOU 53 CB VAL A 37 10774 7562 9259 302 1068 237 C ATOM 54 CG1 VAL A 37 -56.538 13.655 2.407 1.00 74.43 C ANISOU 54 CG1 VAL A 37 11087 7839 9352 131 1306 237 C ATOM 55 CG2 VAL A 37 -54.363 14.719 3.089 1.00 73.09 C ANISOU 55 CG2 VAL A 37 10996 7569 9204 462 922 253 C ATOM 56 N ILE A 38 -52.977 12.007 2.349 1.00 77.31 N ANISOU 56 N ILE A 38 11858 7794 9720 464 888 442 N ATOM 57 CA ILE A 38 -52.484 10.809 3.036 1.00 81.05 C ANISOU 57 CA ILE A 38 12659 8101 10035 506 881 535 C ATOM 58 C ILE A 38 -52.828 10.822 4.535 1.00 84.63 C ANISOU 58 C ILE A 38 13356 8537 10260 509 932 557 C ATOM 59 O ILE A 38 -52.372 11.700 5.258 1.00 84.30 O ANISOU 59 O ILE A 38 13301 8544 10183 636 804 525 O ATOM 60 CB ILE A 38 -50.960 10.647 2.819 1.00 80.85 C ANISOU 60 CB ILE A 38 12650 7995 10075 712 659 570 C ATOM 61 CG1 ILE A 38 -50.682 10.381 1.331 1.00 79.82 C ANISOU 61 CG1 ILE A 38 12328 7867 10133 696 651 559 C ATOM 62 CG2 ILE A 38 -50.400 9.508 3.665 1.00 83.50 C ANISOU 62 CG2 ILE A 38 13342 8155 10226 803 619 661 C ATOM 63 CD1 ILE A 38 -49.245 10.593 0.904 1.00 79.51 C ANISOU 63 CD1 ILE A 38 12176 7825 10207 889 444 564 C ATOM 64 N HIS A 39 -53.634 9.849 4.979 1.00 89.22 N ANISOU 64 N HIS A 39 14170 9047 10683 358 1120 610 N ATOM 65 CA HIS A 39 -53.878 9.579 6.407 1.00 93.50 C ANISOU 65 CA HIS A 39 15015 9537 10971 353 1185 657 C ATOM 66 C HIS A 39 -53.591 8.111 6.714 1.00 95.04 C ANISOU 66 C HIS A 39 15581 9516 11012 330 1214 772 C ATOM 67 O HIS A 39 -53.887 7.238 5.889 1.00 95.28 O ANISOU 67 O HIS A 39 15632 9469 11100 203 1305 802 O ATOM 68 CB HIS A 39 -55.332 9.865 6.796 1.00 97.86 C ANISOU 68 CB HIS A 39 15513 10229 11440 155 1429 612 C ATOM 69 CG HIS A 39 -55.731 11.301 6.658 1.00100.58 C ANISOU 69 CG HIS A 39 15543 10775 11895 196 1410 495 C ATOM 70 ND1 HIS A 39 -57.006 11.687 6.296 1.00102.46 N ANISOU 70 ND1 HIS A 39 15562 11182 12184 37 1599 421 N ATOM 71 CD2 HIS A 39 -55.025 12.444 6.827 1.00 99.96 C ANISOU 71 CD2 HIS A 39 15343 10750 11884 381 1216 436 C ATOM 72 CE1 HIS A 39 -57.068 13.006 6.254 1.00101.28 C ANISOU 72 CE1 HIS A 39 15186 11171 12123 144 1520 322 C ATOM 73 NE2 HIS A 39 -55.878 13.488 6.567 1.00100.12 N ANISOU 73 NE2 HIS A 39 15103 10948 11987 340 1290 332 N ATOM 74 N ASN A 40 -53.038 7.846 7.903 1.00 95.59 N ANISOU 74 N ASN A 40 15963 9479 10876 453 1131 833 N ATOM 75 CA ASN A 40 -52.761 6.478 8.382 1.00 97.09 C ANISOU 75 CA ASN A 40 16570 9441 10877 453 1146 950 C ATOM 76 C ASN A 40 -52.018 5.611 7.353 1.00 95.05 C ANISOU 76 C ASN A 40 16330 9039 10743 527 1046 987 C ATOM 77 O ASN A 40 -52.400 4.470 7.091 1.00 96.93 O ANISOU 77 O ASN A 40 16790 9125 10913 394 1165 1052 O ATOM 78 CB ASN A 40 -54.065 5.790 8.808 1.00 99.18 C ANISOU 78 CB ASN A 40 17036 9679 10968 174 1433 996 C ATOM 79 CG ASN A 40 -54.763 6.506 9.945 1.00101.44 C ANISOU 79 CG ASN A 40 17355 10097 11087 121 1549 967 C ATOM 80 OD1 ASN A 40 -54.124 7.064 10.832 1.00102.87 O ANISOU 80 OD1 ASN A 40 17633 10283 11168 311 1401 962 O ATOM 81 ND2 ASN A 40 -56.086 6.470 9.938 1.00103.50 N ANISOU 81 ND2 ASN A 40 17541 10474 11310 -138 1817 945 N ATOM 82 N SER A 41 -50.962 6.178 6.775 1.00 91.58 N ANISOU 82 N SER A 41 15658 8654 10483 735 831 941 N ATOM 83 CA SER A 41 -50.169 5.533 5.732 1.00 89.81 C ANISOU 83 CA SER A 41 15390 8337 10397 841 728 956 C ATOM 84 C SER A 41 -51.025 5.040 4.556 1.00 89.68 C ANISOU 84 C SER A 41 15264 8315 10494 622 909 939 C ATOM 85 O SER A 41 -50.796 3.950 4.033 1.00 93.26 O ANISOU 85 O SER A 41 15897 8601 10935 629 916 987 O ATOM 86 CB SER A 41 -49.326 4.396 6.328 1.00 90.99 C ANISOU 86 CB SER A 41 15939 8257 10374 1015 611 1051 C ATOM 87 OG SER A 41 -48.484 4.873 7.361 1.00 90.03 O ANISOU 87 OG SER A 41 15898 8152 10154 1230 416 1059 O ATOM 88 N ALA A 42 -52.003 5.850 4.150 1.00 88.35 N ANISOU 88 N ALA A 42 14810 8328 10430 442 1043 866 N ATOM 89 CA ALA A 42 -52.895 5.523 3.030 1.00 87.79 C ANISOU 89 CA ALA A 42 14595 8286 10474 225 1202 835 C ATOM 90 C ALA A 42 -53.433 6.780 2.322 1.00 86.52 C ANISOU 90 C ALA A 42 14007 8360 10504 161 1229 729 C ATOM 91 O ALA A 42 -53.789 7.765 2.968 1.00 86.26 O ANISOU 91 O ALA A 42 13857 8468 10447 163 1242 684 O ATOM 92 CB ALA A 42 -54.053 4.677 3.520 1.00 89.06 C ANISOU 92 CB ALA A 42 15005 8370 10463 -34 1428 884 C ATOM 93 N LEU A 43 -53.493 6.734 0.995 1.00 84.79 N ANISOU 93 N LEU A 43 13581 8172 10462 114 1233 689 N ATOM 94 CA LEU A 43 -54.113 7.798 0.223 1.00 82.98 C ANISOU 94 CA LEU A 43 12983 8142 10400 37 1267 596 C ATOM 95 C LEU A 43 -55.621 7.706 0.411 1.00 84.73 C ANISOU 95 C LEU A 43 13181 8452 10561 -219 1485 569 C ATOM 96 O LEU A 43 -56.189 6.615 0.389 1.00 85.80 O ANISOU 96 O LEU A 43 13511 8481 10606 -394 1618 614 O ATOM 97 CB LEU A 43 -53.748 7.680 -1.257 1.00 81.00 C ANISOU 97 CB LEU A 43 12554 7889 10332 57 1212 567 C ATOM 98 CG LEU A 43 -54.134 8.848 -2.164 1.00 79.97 C ANISOU 98 CG LEU A 43 12053 7947 10383 27 1198 478 C ATOM 99 CD1 LEU A 43 -53.368 10.126 -1.822 1.00 78.69 C ANISOU 99 CD1 LEU A 43 11727 7884 10284 206 1040 446 C ATOM 100 CD2 LEU A 43 -53.901 8.456 -3.613 1.00 79.24 C ANISOU 100 CD2 LEU A 43 11857 7824 10426 13 1178 463 C ATOM 101 N GLN A 44 -56.254 8.856 0.629 1.00 86.68 N ANISOU 101 N GLN A 44 13193 8893 10849 -239 1520 493 N ATOM 102 CA GLN A 44 -57.702 8.947 0.817 1.00 87.64 C ANISOU 102 CA GLN A 44 13222 9150 10924 -457 1724 448 C ATOM 103 C GLN A 44 -58.228 10.167 0.099 1.00 85.53 C ANISOU 103 C GLN A 44 12582 9090 10823 -444 1704 339 C ATOM 104 O GLN A 44 -57.484 11.108 -0.131 1.00 82.94 O ANISOU 104 O GLN A 44 12118 8796 10597 -263 1541 307 O ATOM 105 CB GLN A 44 -58.038 9.069 2.297 1.00 90.38 C ANISOU 105 CB GLN A 44 13746 9523 11069 -465 1813 470 C ATOM 106 CG GLN A 44 -57.353 8.039 3.166 1.00 93.81 C ANISOU 106 CG GLN A 44 14584 9742 11316 -423 1791 583 C ATOM 107 CD GLN A 44 -57.916 7.989 4.561 1.00 97.78 C ANISOU 107 CD GLN A 44 15290 10269 11591 -489 1927 612 C ATOM 108 OE1 GLN A 44 -58.331 9.012 5.118 1.00100.57 O ANISOU 108 OE1 GLN A 44 15497 10792 11923 -446 1956 543 O ATOM 109 NE2 GLN A 44 -57.930 6.795 5.144 1.00100.39 N ANISOU 109 NE2 GLN A 44 15983 10423 11738 -591 2012 714 N ATOM 110 N VAL A 45 -59.509 10.143 -0.255 1.00 88.42 N ANISOU 110 N VAL A 45 12788 9592 11213 -641 1865 283 N ATOM 111 CA VAL A 45 -60.208 11.349 -0.684 1.00 88.70 C ANISOU 111 CA VAL A 45 12491 9843 11366 -618 1864 173 C ATOM 112 C VAL A 45 -60.510 12.150 0.563 1.00 89.17 C ANISOU 112 C VAL A 45 12564 10009 11306 -540 1907 139 C ATOM 113 O VAL A 45 -61.178 11.649 1.464 1.00 89.20 O ANISOU 113 O VAL A 45 12702 10040 11149 -664 2078 160 O ATOM 114 CB VAL A 45 -61.541 11.056 -1.408 1.00 90.72 C ANISOU 114 CB VAL A 45 12553 10235 11678 -845 2018 114 C ATOM 115 CG1 VAL A 45 -62.295 12.357 -1.707 1.00 91.36 C ANISOU 115 CG1 VAL A 45 12305 10548 11860 -784 2008 -5 C ATOM 116 CG2 VAL A 45 -61.291 10.262 -2.686 1.00 89.85 C ANISOU 116 CG2 VAL A 45 12446 10016 11678 -928 1971 138 C ATOM 117 N SER A 46 -60.015 13.387 0.593 1.00 90.86 N ANISOU 117 N SER A 46 12651 10278 11592 -341 1756 84 N ATOM 118 CA SER A 46 -60.282 14.332 1.674 1.00 93.66 C ANISOU 118 CA SER A 46 13003 10737 11846 -235 1771 30 C ATOM 119 C SER A 46 -61.786 14.575 1.781 1.00 97.49 C ANISOU 119 C SER A 46 13303 11436 12302 -361 1970 -56 C ATOM 120 O SER A 46 -62.412 15.035 0.824 1.00 96.36 O ANISOU 120 O SER A 46 12891 11418 12302 -388 1968 -133 O ATOM 121 CB SER A 46 -59.544 15.649 1.410 1.00 91.68 C ANISOU 121 CB SER A 46 12627 10498 11709 -25 1558 -23 C ATOM 122 OG SER A 46 -59.807 16.610 2.414 1.00 93.29 O ANISOU 122 OG SER A 46 12841 10789 11813 86 1559 -88 O ATOM 123 N ASP A 47 -62.353 14.242 2.940 1.00103.61 N ANISOU 123 N ASP A 47 14220 12259 12886 -434 2140 -43 N ATOM 124 CA ASP A 47 -63.796 14.342 3.160 1.00109.50 C ANISOU 124 CA ASP A 47 14790 13230 13583 -569 2361 -122 C ATOM 125 C ASP A 47 -64.201 15.813 3.323 1.00109.47 C ANISOU 125 C ASP A 47 14569 13404 13618 -381 2312 -251 C ATOM 126 O ASP A 47 -63.730 16.493 4.234 1.00108.49 O ANISOU 126 O ASP A 47 14576 13251 13394 -208 2243 -265 O ATOM 127 CB ASP A 47 -64.202 13.520 4.389 1.00115.25 C ANISOU 127 CB ASP A 47 15762 13950 14075 -710 2570 -59 C ATOM 128 CG ASP A 47 -65.689 13.214 4.421 1.00121.16 C ANISOU 128 CG ASP A 47 16325 14923 14784 -936 2832 -115 C ATOM 129 OD1 ASP A 47 -66.066 12.108 3.976 1.00125.63 O ANISOU 129 OD1 ASP A 47 16927 15448 15358 -1185 2942 -59 O ATOM 130 OD2 ASP A 47 -66.480 14.077 4.872 1.00122.46 O ANISOU 130 OD2 ASP A 47 16306 15311 14912 -866 2924 -222 O ATOM 131 N VAL A 48 -65.076 16.287 2.436 1.00111.25 N ANISOU 131 N VAL A 48 14481 13806 13983 -408 2339 -349 N ATOM 132 CA VAL A 48 -65.421 17.718 2.341 1.00112.49 C ANISOU 132 CA VAL A 48 14427 14107 14204 -203 2255 -476 C ATOM 133 C VAL A 48 -66.140 18.225 3.592 1.00114.54 C ANISOU 133 C VAL A 48 14701 14528 14290 -133 2407 -550 C ATOM 134 O VAL A 48 -65.825 19.306 4.087 1.00113.16 O ANISOU 134 O VAL A 48 14563 14350 14081 88 2296 -611 O ATOM 135 CB VAL A 48 -66.291 18.019 1.088 1.00112.87 C ANISOU 135 CB VAL A 48 14139 14317 14428 -246 2252 -565 C ATOM 136 CG1 VAL A 48 -66.765 19.475 1.066 1.00112.71 C ANISOU 136 CG1 VAL A 48 13923 14448 14452 -20 2177 -702 C ATOM 137 CG2 VAL A 48 -65.523 17.696 -0.189 1.00111.74 C ANISOU 137 CG2 VAL A 48 13989 14015 14451 -279 2085 -504 C ATOM 138 N ASP A 49 -67.090 17.435 4.091 1.00117.66 N ANISOU 138 N ASP A 49 15077 15060 14568 -331 2662 -544 N ATOM 139 CA ASP A 49 -67.948 17.839 5.212 1.00121.63 C ANISOU 139 CA ASP A 49 15553 15762 14897 -290 2854 -623 C ATOM 140 C ASP A 49 -67.235 17.907 6.568 1.00120.79 C ANISOU 140 C ASP A 49 15789 15527 14578 -184 2849 -569 C ATOM 141 O ASP A 49 -67.677 18.639 7.453 1.00121.40 O ANISOU 141 O ASP A 49 15863 15737 14523 -48 2929 -656 O ATOM 142 CB ASP A 49 -69.163 16.905 5.321 1.00127.01 C ANISOU 142 CB ASP A 49 16106 16638 15512 -572 3145 -625 C ATOM 143 CG ASP A 49 -70.040 16.920 4.069 1.00129.09 C ANISOU 143 CG ASP A 49 15998 17078 15972 -672 3157 -704 C ATOM 144 OD1 ASP A 49 -70.706 15.894 3.803 1.00131.74 O ANISOU 144 OD1 ASP A 49 16262 17487 16306 -959 3325 -669 O ATOM 145 OD2 ASP A 49 -70.063 17.947 3.351 1.00128.79 O ANISOU 145 OD2 ASP A 49 15754 17098 16082 -470 2989 -801 O ATOM 146 N LYS A 50 -66.149 17.150 6.729 1.00119.54 N ANISOU 146 N LYS A 50 15925 15115 14378 -232 2751 -433 N ATOM 147 CA LYS A 50 -65.370 17.142 7.971 1.00119.33 C ANISOU 147 CA LYS A 50 16243 14947 14149 -129 2711 -372 C ATOM 148 C LYS A 50 -64.097 17.976 7.828 1.00115.28 C ANISOU 148 C LYS A 50 15819 14259 13721 108 2402 -373 C ATOM 149 O LYS A 50 -63.514 18.063 6.743 1.00113.31 O ANISOU 149 O LYS A 50 15461 13919 13672 128 2226 -355 O ATOM 150 CB LYS A 50 -65.031 15.705 8.381 1.00121.62 C ANISOU 150 CB LYS A 50 16827 15074 14306 -331 2808 -220 C ATOM 151 CG LYS A 50 -66.256 14.800 8.434 1.00126.11 C ANISOU 151 CG LYS A 50 17316 15797 14801 -617 3113 -207 C ATOM 152 CD LYS A 50 -66.102 13.626 9.393 1.00129.18 C ANISOU 152 CD LYS A 50 18077 16052 14953 -786 3260 -72 C ATOM 153 CE LYS A 50 -67.433 12.917 9.621 1.00132.70 C ANISOU 153 CE LYS A 50 18432 16688 15296 -1082 3591 -75 C ATOM 154 NZ LYS A 50 -68.409 13.722 10.415 1.00135.30 N ANISOU 154 NZ LYS A 50 18601 17301 15504 -1022 3784 -193 N ATOM 155 N LEU A 51 -63.689 18.591 8.935 1.00114.08 N ANISOU 155 N LEU A 51 15866 14070 13407 276 2343 -397 N ATOM 156 CA LEU A 51 -62.514 19.457 8.997 1.00111.12 C ANISOU 156 CA LEU A 51 15591 13544 13084 490 2053 -408 C ATOM 157 C LEU A 51 -61.484 18.758 9.864 1.00110.09 C ANISOU 157 C LEU A 51 15816 13218 12796 496 1975 -289 C ATOM 158 O LEU A 51 -61.787 18.375 10.994 1.00112.31 O ANISOU 158 O LEU A 51 16313 13518 12841 467 2123 -265 O ATOM 159 CB LEU A 51 -62.894 20.810 9.619 1.00112.39 C ANISOU 159 CB LEU A 51 15712 13818 13173 694 2025 -548 C ATOM 160 CG LEU A 51 -61.992 22.034 9.413 1.00110.55 C ANISOU 160 CG LEU A 51 15486 13475 13042 904 1729 -605 C ATOM 161 CD1 LEU A 51 -62.605 23.231 10.124 1.00111.23 C ANISOU 161 CD1 LEU A 51 15563 13679 13018 1090 1752 -751 C ATOM 162 CD2 LEU A 51 -60.567 21.815 9.896 1.00109.89 C ANISOU 162 CD2 LEU A 51 15674 13172 12907 954 1515 -510 C ATOM 163 N VAL A 52 -60.272 18.594 9.338 1.00106.45 N ANISOU 163 N VAL A 52 15412 12577 12455 540 1743 -218 N ATOM 164 CA VAL A 52 -59.170 18.007 10.093 1.00105.72 C ANISOU 164 CA VAL A 52 15637 12299 12232 586 1619 -114 C ATOM 165 C VAL A 52 -58.102 19.086 10.299 1.00102.15 C ANISOU 165 C VAL A 52 15220 11766 11826 792 1329 -159 C ATOM 166 O VAL A 52 -57.332 19.387 9.388 1.00 99.09 O ANISOU 166 O VAL A 52 14695 11314 11640 831 1137 -152 O ATOM 167 CB VAL A 52 -58.583 16.765 9.375 1.00106.76 C ANISOU 167 CB VAL A 52 15823 12290 12452 467 1592 11 C ATOM 168 CG1 VAL A 52 -57.770 15.921 10.353 1.00108.45 C ANISOU 168 CG1 VAL A 52 16403 12334 12469 498 1535 122 C ATOM 169 CG2 VAL A 52 -59.687 15.930 8.732 1.00107.01 C ANISOU 169 CG2 VAL A 52 15724 12411 12524 243 1840 28 C ATOM 170 N CYS A 53 -58.074 19.677 11.493 1.00102.09 N ANISOU 170 N CYS A 53 15399 11767 11624 912 1303 -208 N ATOM 171 CA CYS A 53 -57.078 20.706 11.833 1.00102.01 C ANISOU 171 CA CYS A 53 15456 11673 11628 1092 1022 -257 C ATOM 172 C CYS A 53 -55.635 20.179 11.831 1.00104.25 C ANISOU 172 C CYS A 53 15881 11782 11945 1127 787 -154 C ATOM 173 O CYS A 53 -54.698 20.957 11.651 1.00103.55 O ANISOU 173 O CYS A 53 15748 11633 11960 1230 533 -185 O ATOM 174 CB CYS A 53 -57.391 21.349 13.190 1.00102.47 C ANISOU 174 CB CYS A 53 15722 11770 11439 1210 1052 -333 C ATOM 175 SG CYS A 53 -58.888 22.365 13.231 1.00102.11 S ANISOU 175 SG CYS A 53 15487 11940 11368 1255 1256 -495 S ATOM 176 N ARG A 54 -55.464 18.872 12.046 1.00109.53 N ANISOU 176 N ARG A 54 16722 12374 12520 1044 871 -36 N ATOM 177 CA ARG A 54 -54.157 18.209 11.926 1.00111.57 C ANISOU 177 CA ARG A 54 17092 12478 12819 1089 666 62 C ATOM 178 C ARG A 54 -53.568 18.341 10.512 1.00106.38 C ANISOU 178 C ARG A 54 16156 11809 12452 1071 538 68 C ATOM 179 O ARG A 54 -52.350 18.447 10.371 1.00104.26 O ANISOU 179 O ARG A 54 15889 11461 12264 1161 299 95 O ATOM 180 CB ARG A 54 -54.253 16.725 12.352 1.00117.80 C ANISOU 180 CB ARG A 54 18136 13177 13443 1002 807 186 C ATOM 181 CG ARG A 54 -52.990 15.888 12.129 1.00121.98 C ANISOU 181 CG ARG A 54 18778 13550 14018 1064 614 289 C ATOM 182 CD ARG A 54 -53.052 14.518 12.801 1.00128.09 C ANISOU 182 CD ARG A 54 19889 14202 14575 1013 727 408 C ATOM 183 NE ARG A 54 -52.578 14.553 14.194 1.00133.89 N ANISOU 183 NE ARG A 54 20952 14866 15054 1140 619 430 N ATOM 184 CZ ARG A 54 -53.190 14.020 15.264 1.00139.39 C ANISOU 184 CZ ARG A 54 21961 15533 15468 1089 790 476 C ATOM 185 NH1 ARG A 54 -52.621 14.142 16.465 1.00141.81 N ANISOU 185 NH1 ARG A 54 22561 15770 15550 1230 649 490 N ATOM 186 NH2 ARG A 54 -54.346 13.358 15.170 1.00140.99 N ANISOU 186 NH2 ARG A 54 22193 15777 15598 891 1098 510 N ATOM 187 N ASP A 55 -54.419 18.331 9.481 1.00103.52 N ANISOU 187 N ASP A 55 15555 11538 12240 954 696 40 N ATOM 188 CA ASP A 55 -53.959 18.530 8.099 1.00100.53 C ANISOU 188 CA ASP A 55 14915 11157 12122 933 592 40 C ATOM 189 C ASP A 55 -53.356 19.921 7.956 1.00 96.67 C ANISOU 189 C ASP A 55 14302 10685 11743 1044 372 -40 C ATOM 190 O ASP A 55 -53.897 20.893 8.488 1.00 95.17 O ANISOU 190 O ASP A 55 14118 10558 11485 1097 381 -133 O ATOM 191 CB ASP A 55 -55.099 18.362 7.078 1.00101.85 C ANISOU 191 CB ASP A 55 14861 11429 12408 793 796 11 C ATOM 192 CG ASP A 55 -55.555 16.909 6.912 1.00104.24 C ANISOU 192 CG ASP A 55 15259 11694 12652 645 988 99 C ATOM 193 OD1 ASP A 55 -56.640 16.692 6.323 1.00105.47 O ANISOU 193 OD1 ASP A 55 15267 11949 12858 509 1178 71 O ATOM 194 OD2 ASP A 55 -54.843 15.976 7.345 1.00104.59 O ANISOU 194 OD2 ASP A 55 15529 11607 12600 662 942 194 O ATOM 195 N LYS A 56 -52.236 20.001 7.240 1.00 92.57 N ANISOU 195 N LYS A 56 13678 10107 11386 1075 179 -7 N ATOM 196 CA LYS A 56 -51.488 21.242 7.106 1.00 91.24 C ANISOU 196 CA LYS A 56 13411 9934 11320 1151 -48 -67 C ATOM 197 C LYS A 56 -51.181 21.583 5.640 1.00 85.18 C ANISOU 197 C LYS A 56 12375 9188 10800 1096 -104 -67 C ATOM 198 O LYS A 56 -50.538 20.804 4.941 1.00 85.59 O ANISOU 198 O LYS A 56 12363 9208 10950 1067 -125 6 O ATOM 199 CB LYS A 56 -50.200 21.146 7.919 1.00 95.27 C ANISOU 199 CB LYS A 56 14082 10360 11755 1251 -272 -29 C ATOM 200 CG LYS A 56 -49.496 22.482 8.088 1.00101.10 C ANISOU 200 CG LYS A 56 14769 11091 12552 1313 -510 -101 C ATOM 201 CD LYS A 56 -48.609 22.524 9.321 1.00106.34 C ANISOU 201 CD LYS A 56 15650 11693 13061 1417 -706 -96 C ATOM 202 CE LYS A 56 -48.100 23.939 9.549 1.00109.69 C ANISOU 202 CE LYS A 56 16044 12106 13527 1453 -929 -184 C ATOM 203 NZ LYS A 56 -47.243 24.041 10.763 1.00113.34 N ANISOU 203 NZ LYS A 56 16717 12513 13834 1549 -1142 -191 N ATOM 204 N LEU A 57 -51.663 22.738 5.178 1.00 80.06 N ANISOU 204 N LEU A 57 11588 8590 10240 1092 -122 -150 N ATOM 205 CA LEU A 57 -51.275 23.295 3.876 1.00 76.44 C ANISOU 205 CA LEU A 57 10908 8139 9996 1047 -209 -154 C ATOM 206 C LEU A 57 -50.501 24.599 4.101 1.00 75.74 C ANISOU 206 C LEU A 57 10820 8010 9947 1100 -442 -206 C ATOM 207 O LEU A 57 -51.089 25.676 4.208 1.00 75.41 O ANISOU 207 O LEU A 57 10779 7980 9894 1130 -461 -292 O ATOM 208 CB LEU A 57 -52.510 23.520 2.995 1.00 74.06 C ANISOU 208 CB LEU A 57 10452 7917 9769 987 -44 -201 C ATOM 209 CG LEU A 57 -52.289 23.920 1.532 1.00 71.52 C ANISOU 209 CG LEU A 57 9919 7604 9651 930 -94 -194 C ATOM 210 CD1 LEU A 57 -51.674 22.800 0.707 1.00 70.11 C ANISOU 210 CD1 LEU A 57 9669 7405 9561 864 -62 -101 C ATOM 211 CD2 LEU A 57 -53.611 24.335 0.908 1.00 71.74 C ANISOU 211 CD2 LEU A 57 9827 7714 9716 905 38 -263 C ATOM 212 N SER A 58 -49.179 24.487 4.206 1.00 75.34 N ANISOU 212 N SER A 58 10775 7910 9937 1114 -624 -157 N ATOM 213 CA SER A 58 -48.320 25.646 4.470 1.00 76.30 C ANISOU 213 CA SER A 58 10902 7991 10096 1135 -863 -200 C ATOM 214 C SER A 58 -47.976 26.428 3.201 1.00 73.05 C ANISOU 214 C SER A 58 10286 7583 9883 1051 -935 -203 C ATOM 215 O SER A 58 -47.542 27.580 3.269 1.00 72.66 O ANISOU 215 O SER A 58 10242 7493 9872 1037 -1106 -250 O ATOM 216 CB SER A 58 -47.037 25.209 5.181 1.00 78.51 C ANISOU 216 CB SER A 58 11259 8239 10331 1180 -1040 -153 C ATOM 217 OG SER A 58 -46.220 24.438 4.321 1.00 81.33 O ANISOU 217 OG SER A 58 11459 8620 10820 1145 -1052 -72 O ATOM 218 N SER A 59 -48.161 25.801 2.050 1.00 70.39 N ANISOU 218 N SER A 59 9792 7287 9664 988 -809 -151 N ATOM 219 CA SER A 59 -47.822 26.430 0.788 1.00 70.08 C ANISOU 219 CA SER A 59 9572 7254 9800 905 -860 -141 C ATOM 220 C SER A 59 -48.631 25.828 -0.334 1.00 67.86 C ANISOU 220 C SER A 59 9171 7020 9592 857 -668 -116 C ATOM 221 O SER A 59 -49.054 24.674 -0.274 1.00 67.23 O ANISOU 221 O SER A 59 9116 6966 9460 865 -518 -81 O ATOM 222 CB SER A 59 -46.325 26.251 0.502 1.00 71.19 C ANISOU 222 CB SER A 59 9611 7399 10038 869 -1010 -79 C ATOM 223 OG SER A 59 -46.043 26.277 -0.885 1.00 70.09 O ANISOU 223 OG SER A 59 9282 7291 10056 782 -975 -38 O ATOM 224 N THR A 60 -48.790 26.612 -1.384 1.00 66.73 N ANISOU 224 N THR A 60 8912 6877 9564 797 -686 -131 N ATOM 225 CA THR A 60 -49.553 26.196 -2.542 1.00 66.87 C ANISOU 225 CA THR A 60 8814 6939 9654 750 -532 -117 C ATOM 226 C THR A 60 -48.745 25.219 -3.433 1.00 67.20 C ANISOU 226 C THR A 60 8738 7003 9789 696 -496 -31 C ATOM 227 O THR A 60 -49.309 24.597 -4.326 1.00 66.54 O ANISOU 227 O THR A 60 8581 6951 9748 659 -361 -13 O ATOM 228 CB THR A 60 -50.095 27.444 -3.277 1.00 67.39 C ANISOU 228 CB THR A 60 8832 6987 9785 728 -575 -170 C ATOM 229 OG1 THR A 60 -51.263 27.110 -4.023 1.00 70.16 O ANISOU 229 OG1 THR A 60 9112 7394 10152 721 -418 -190 O ATOM 230 CG2 THR A 60 -49.074 28.053 -4.177 1.00 66.85 C ANISOU 230 CG2 THR A 60 8672 6885 9840 645 -699 -126 C ATOM 231 N ASN A 61 -47.439 25.087 -3.172 1.00 70.21 N ANISOU 231 N ASN A 61 9102 7375 10198 701 -621 12 N ATOM 232 CA ASN A 61 -46.599 24.000 -3.717 1.00 71.80 C ANISOU 232 CA ASN A 61 9217 7606 10456 699 -587 84 C ATOM 233 C ASN A 61 -46.965 22.613 -3.252 1.00 69.06 C ANISOU 233 C ASN A 61 8972 7252 10014 757 -462 112 C ATOM 234 O ASN A 61 -46.692 21.663 -3.952 1.00 69.53 O ANISOU 234 O ASN A 61 8977 7323 10115 755 -385 160 O ATOM 235 CB ASN A 61 -45.127 24.174 -3.323 1.00 77.19 C ANISOU 235 CB ASN A 61 9854 8301 11173 717 -764 112 C ATOM 236 CG ASN A 61 -44.478 25.341 -4.010 1.00 81.31 C ANISOU 236 CG ASN A 61 10247 8835 11810 620 -881 109 C ATOM 237 OD1 ASN A 61 -44.814 25.665 -5.155 1.00 86.51 O ANISOU 237 OD1 ASN A 61 10816 9503 12549 545 -810 117 O ATOM 238 ND2 ASN A 61 -43.536 25.987 -3.320 1.00 83.71 N ANISOU 238 ND2 ASN A 61 10551 9136 12116 611 -1066 98 N ATOM 239 N GLN A 62 -47.511 22.489 -2.051 1.00 68.47 N ANISOU 239 N GLN A 62 9063 7149 9801 810 -445 85 N ATOM 240 CA GLN A 62 -47.986 21.198 -1.560 1.00 68.70 C ANISOU 240 CA GLN A 62 9225 7157 9720 842 -311 115 C ATOM 241 C GLN A 62 -49.164 20.648 -2.371 1.00 65.60 C ANISOU 241 C GLN A 62 8795 6785 9343 766 -113 110 C ATOM 242 O GLN A 62 -49.471 19.465 -2.269 1.00 63.69 O ANISOU 242 O GLN A 62 8646 6516 9037 758 4 147 O ATOM 243 CB GLN A 62 -48.399 21.289 -0.085 1.00 72.54 C ANISOU 243 CB GLN A 62 9907 7616 10036 900 -321 86 C ATOM 244 CG GLN A 62 -47.274 21.546 0.908 1.00 74.75 C ANISOU 244 CG GLN A 62 10272 7866 10261 985 -518 94 C ATOM 245 CD GLN A 62 -47.784 21.610 2.341 1.00 77.89 C ANISOU 245 CD GLN A 62 10891 8234 10467 1044 -513 62 C ATOM 246 OE1 GLN A 62 -47.609 22.620 3.028 1.00 80.92 O ANISOU 246 OE1 GLN A 62 11324 8611 10810 1076 -645 7 O ATOM 247 NE2 GLN A 62 -48.440 20.542 2.793 1.00 77.38 N ANISOU 247 NE2 GLN A 62 10975 8147 10276 1048 -354 95 N ATOM 248 N LEU A 63 -49.842 21.512 -3.130 1.00 64.00 N ANISOU 248 N LEU A 63 8474 6622 9218 709 -88 62 N ATOM 249 CA LEU A 63 -50.922 21.096 -4.015 1.00 62.76 C ANISOU 249 CA LEU A 63 8251 6502 9093 635 70 48 C ATOM 250 C LEU A 63 -50.349 20.705 -5.358 1.00 62.65 C ANISOU 250 C LEU A 63 8115 6487 9199 594 73 92 C ATOM 251 O LEU A 63 -49.485 21.400 -5.887 1.00 63.34 O ANISOU 251 O LEU A 63 8107 6579 9379 598 -41 104 O ATOM 252 CB LEU A 63 -51.975 22.204 -4.153 1.00 61.64 C ANISOU 252 CB LEU A 63 8047 6410 8962 621 85 -32 C ATOM 253 CG LEU A 63 -52.816 22.349 -2.882 1.00 62.38 C ANISOU 253 CG LEU A 63 8259 6526 8914 663 144 -85 C ATOM 254 CD1 LEU A 63 -53.629 23.624 -2.912 1.00 62.40 C ANISOU 254 CD1 LEU A 63 8207 6574 8926 697 116 -175 C ATOM 255 CD2 LEU A 63 -53.730 21.142 -2.695 1.00 63.03 C ANISOU 255 CD2 LEU A 63 8391 6640 8916 600 339 -72 C ATOM 256 N ARG A 64 -50.812 19.578 -5.893 1.00 63.73 N ANISOU 256 N ARG A 64 8268 6619 9328 547 209 115 N ATOM 257 CA ARG A 64 -50.309 19.049 -7.155 1.00 64.45 C ANISOU 257 CA ARG A 64 8272 6704 9512 519 229 152 C ATOM 258 C ARG A 64 -51.444 18.492 -7.988 1.00 63.60 C ANISOU 258 C ARG A 64 8138 6615 9411 429 371 130 C ATOM 259 O ARG A 64 -52.385 17.929 -7.454 1.00 63.46 O ANISOU 259 O ARG A 64 8203 6597 9310 384 478 112 O ATOM 260 CB ARG A 64 -49.289 17.925 -6.915 1.00 66.27 C ANISOU 260 CB ARG A 64 8588 6878 9711 586 216 215 C ATOM 261 CG ARG A 64 -48.086 18.281 -6.050 1.00 68.48 C ANISOU 261 CG ARG A 64 8889 7151 9979 685 63 238 C ATOM 262 CD ARG A 64 -47.147 19.278 -6.714 1.00 70.32 C ANISOU 262 CD ARG A 64 8948 7436 10332 683 -58 238 C ATOM 263 NE ARG A 64 -46.197 19.850 -5.765 1.00 73.17 N ANISOU 263 NE ARG A 64 9318 7804 10679 747 -219 241 N ATOM 264 CZ ARG A 64 -45.112 19.239 -5.285 1.00 75.04 C ANISOU 264 CZ ARG A 64 9576 8037 10896 844 -300 278 C ATOM 265 NH1 ARG A 64 -44.783 18.004 -5.657 1.00 76.39 N ANISOU 265 NH1 ARG A 64 9780 8187 11057 905 -232 317 N ATOM 266 NH2 ARG A 64 -44.342 19.877 -4.413 1.00 77.01 N ANISOU 266 NH2 ARG A 64 9823 8302 11132 888 -463 270 N ATOM 267 N SER A 65 -51.335 18.665 -9.300 1.00 63.99 N ANISOU 267 N SER A 65 8072 6686 9555 392 369 131 N ATOM 268 CA SER A 65 -52.238 18.064 -10.270 1.00 63.67 C ANISOU 268 CA SER A 65 8002 6659 9528 307 480 111 C ATOM 269 C SER A 65 -51.409 17.171 -11.177 1.00 63.58 C ANISOU 269 C SER A 65 8001 6604 9552 318 499 159 C ATOM 270 O SER A 65 -50.325 17.538 -11.636 1.00 62.34 O ANISOU 270 O SER A 65 7775 6454 9456 370 422 189 O ATOM 271 CB SER A 65 -52.947 19.126 -11.093 1.00 62.09 C ANISOU 271 CB SER A 65 7673 6524 9391 270 453 60 C ATOM 272 OG SER A 65 -51.992 19.972 -11.675 1.00 63.72 O ANISOU 272 OG SER A 65 7808 6728 9674 304 345 85 O ATOM 273 N VAL A 66 -51.960 16.009 -11.472 1.00 63.88 N ANISOU 273 N VAL A 66 8121 6602 9548 260 607 160 N ATOM 274 CA VAL A 66 -51.156 14.880 -11.855 1.00 63.54 C ANISOU 274 CA VAL A 66 8165 6484 9492 304 632 205 C ATOM 275 C VAL A 66 -51.913 14.058 -12.896 1.00 62.63 C ANISOU 275 C VAL A 66 8078 6343 9373 207 730 183 C ATOM 276 O VAL A 66 -53.128 13.922 -12.810 1.00 64.40 O ANISOU 276 O VAL A 66 8313 6587 9567 95 800 144 O ATOM 277 CB VAL A 66 -50.805 14.141 -10.546 1.00 65.43 C ANISOU 277 CB VAL A 66 8574 6649 9635 366 634 242 C ATOM 278 CG1 VAL A 66 -51.125 12.662 -10.583 1.00 67.88 C ANISOU 278 CG1 VAL A 66 9069 6853 9866 327 735 261 C ATOM 279 CG2 VAL A 66 -49.362 14.406 -10.158 1.00 65.95 C ANISOU 279 CG2 VAL A 66 8617 6715 9726 508 516 281 C ATOM 280 N GLY A 67 -51.196 13.545 -13.887 1.00 60.80 N ANISOU 280 N GLY A 67 7848 6079 9171 250 734 201 N ATOM 281 CA GLY A 67 -51.792 12.719 -14.937 1.00 61.51 C ANISOU 281 CA GLY A 67 7989 6130 9249 167 812 177 C ATOM 282 C GLY A 67 -51.308 11.276 -14.885 1.00 62.26 C ANISOU 282 C GLY A 67 8279 6098 9276 215 861 206 C ATOM 283 O GLY A 67 -50.100 11.011 -14.954 1.00 60.61 O ANISOU 283 O GLY A 67 8091 5863 9075 357 823 240 O ATOM 284 N LEU A 68 -52.254 10.349 -14.764 1.00 63.21 N ANISOU 284 N LEU A 68 8544 6143 9329 96 943 189 N ATOM 285 CA LEU A 68 -51.966 8.912 -14.784 1.00 64.14 C ANISOU 285 CA LEU A 68 8894 6106 9368 120 991 212 C ATOM 286 C LEU A 68 -52.550 8.285 -16.054 1.00 64.15 C ANISOU 286 C LEU A 68 8938 6068 9368 16 1044 169 C ATOM 287 O LEU A 68 -53.689 8.574 -16.434 1.00 64.95 O ANISOU 287 O LEU A 68 8956 6232 9488 -144 1075 122 O ATOM 288 CB LEU A 68 -52.548 8.226 -13.539 1.00 64.95 C ANISOU 288 CB LEU A 68 9186 6121 9370 44 1044 237 C ATOM 289 CG LEU A 68 -51.877 8.426 -12.171 1.00 65.37 C ANISOU 289 CG LEU A 68 9300 6160 9377 165 992 288 C ATOM 290 CD1 LEU A 68 -50.363 8.274 -12.210 1.00 65.81 C ANISOU 290 CD1 LEU A 68 9373 6181 9448 389 904 324 C ATOM 291 CD2 LEU A 68 -52.225 9.772 -11.589 1.00 64.54 C ANISOU 291 CD2 LEU A 68 9003 6200 9318 142 955 268 C ATOM 292 N ASN A 69 -51.773 7.407 -16.684 1.00 64.54 N ANISOU 292 N ASN A 69 9118 6014 9389 119 1050 178 N ATOM 293 CA ASN A 69 -52.122 6.821 -17.980 1.00 65.12 C ANISOU 293 CA ASN A 69 9248 6040 9452 52 1086 133 C ATOM 294 C ASN A 69 -53.015 5.595 -17.825 1.00 66.90 C ANISOU 294 C ASN A 69 9715 6116 9589 -104 1152 117 C ATOM 295 O ASN A 69 -52.855 4.844 -16.869 1.00 67.66 O ANISOU 295 O ASN A 69 10009 6089 9608 -83 1172 158 O ATOM 296 CB ASN A 69 -50.840 6.434 -18.735 1.00 65.42 C ANISOU 296 CB ASN A 69 9327 6039 9489 251 1070 142 C ATOM 297 CG ASN A 69 -49.914 7.622 -18.968 1.00 64.22 C ANISOU 297 CG ASN A 69 8930 6043 9425 377 1015 160 C ATOM 298 OD1 ASN A 69 -50.366 8.767 -19.066 1.00 63.32 O ANISOU 298 OD1 ASN A 69 8625 6054 9376 294 987 150 O ATOM 299 ND2 ASN A 69 -48.614 7.357 -19.067 1.00 64.53 N ANISOU 299 ND2 ASN A 69 8975 6078 9465 576 998 184 N ATOM 300 N LEU A 70 -53.933 5.390 -18.774 1.00 68.46 N ANISOU 300 N LEU A 70 9905 6318 9787 -266 1178 59 N ATOM 301 CA LEU A 70 -54.836 4.225 -18.761 1.00 71.84 C ANISOU 301 CA LEU A 70 10554 6605 10134 -456 1236 36 C ATOM 302 C LEU A 70 -54.122 2.884 -18.891 1.00 73.45 C ANISOU 302 C LEU A 70 11074 6586 10244 -359 1251 55 C ATOM 303 O LEU A 70 -54.597 1.878 -18.367 1.00 74.59 O ANISOU 303 O LEU A 70 11466 6573 10302 -483 1295 68 O ATOM 304 CB LEU A 70 -55.875 4.302 -19.883 1.00 73.26 C ANISOU 304 CB LEU A 70 10648 6847 10340 -638 1238 -40 C ATOM 305 CG LEU A 70 -57.018 5.315 -19.848 1.00 74.62 C ANISOU 305 CG LEU A 70 10557 7213 10581 -792 1229 -82 C ATOM 306 CD1 LEU A 70 -58.215 4.709 -20.573 1.00 76.13 C ANISOU 306 CD1 LEU A 70 10787 7391 10749 -1029 1246 -154 C ATOM 307 CD2 LEU A 70 -57.424 5.723 -18.437 1.00 75.17 C ANISOU 307 CD2 LEU A 70 10559 7350 10650 -842 1265 -48 C ATOM 308 N GLU A 71 -53.038 2.870 -19.662 1.00 74.40 N ANISOU 308 N GLU A 71 11191 6696 10378 -146 1217 50 N ATOM 309 CA GLU A 71 -52.046 1.785 -19.673 1.00 75.35 C ANISOU 309 CA GLU A 71 11576 6633 10418 43 1216 70 C ATOM 310 C GLU A 71 -51.856 1.106 -18.331 1.00 74.71 C ANISOU 310 C GLU A 71 11717 6409 10259 78 1221 133 C ATOM 311 O GLU A 71 -51.949 -0.113 -18.232 1.00 75.60 O ANISOU 311 O GLU A 71 12153 6304 10267 54 1242 137 O ATOM 312 CB GLU A 71 -50.689 2.367 -20.036 1.00 77.30 C ANISOU 312 CB GLU A 71 11662 6986 10720 315 1177 83 C ATOM 313 CG GLU A 71 -50.314 2.257 -21.485 1.00 78.87 C ANISOU 313 CG GLU A 71 11841 7202 10921 393 1188 29 C ATOM 314 CD GLU A 71 -48.984 2.915 -21.767 1.00 80.24 C ANISOU 314 CD GLU A 71 11820 7514 11151 636 1167 48 C ATOM 315 OE1 GLU A 71 -48.393 3.565 -20.874 1.00 79.34 O ANISOU 315 OE1 GLU A 71 11558 7495 11090 727 1128 98 O ATOM 316 OE2 GLU A 71 -48.516 2.778 -22.907 1.00 84.35 O ANISOU 316 OE2 GLU A 71 12334 8055 11659 730 1190 9 O ATOM 317 N GLY A 72 -51.579 1.918 -17.309 1.00 71.96 N ANISOU 317 N GLY A 72 11212 6176 9952 138 1194 182 N ATOM 318 CA GLY A 72 -51.286 1.434 -15.962 1.00 72.12 C ANISOU 318 CA GLY A 72 11426 6083 9891 201 1184 248 C ATOM 319 C GLY A 72 -52.453 0.810 -15.212 1.00 72.35 C ANISOU 319 C GLY A 72 11659 5997 9833 -54 1253 267 C ATOM 320 O GLY A 72 -52.270 0.328 -14.097 1.00 72.88 O ANISOU 320 O GLY A 72 11932 5949 9809 -18 1253 328 O ATOM 321 N ASN A 73 -53.648 0.858 -15.803 1.00 72.12 N ANISOU 321 N ASN A 73 11561 6012 9826 -315 1309 216 N ATOM 322 CA ASN A 73 -54.826 0.136 -15.319 1.00 73.38 C ANISOU 322 CA ASN A 73 11908 6069 9903 -601 1390 221 C ATOM 323 C ASN A 73 -55.095 -1.167 -16.069 1.00 74.60 C ANISOU 323 C ASN A 73 12367 6000 9975 -708 1413 192 C ATOM 324 O ASN A 73 -56.054 -1.879 -15.743 1.00 76.24 O ANISOU 324 O ASN A 73 12757 6101 10107 -973 1480 197 O ATOM 325 CB ASN A 73 -56.071 1.018 -15.434 1.00 72.74 C ANISOU 325 CB ASN A 73 11534 6202 9899 -840 1434 173 C ATOM 326 CG ASN A 73 -55.938 2.329 -14.704 1.00 69.89 C ANISOU 326 CG ASN A 73 10895 6050 9611 -750 1411 191 C ATOM 327 OD1 ASN A 73 -56.628 3.280 -15.031 1.00 70.63 O ANISOU 327 OD1 ASN A 73 10707 6338 9791 -840 1412 141 O ATOM 328 ND2 ASN A 73 -55.066 2.387 -13.712 1.00 69.91 N ANISOU 328 ND2 ASN A 73 10984 6005 9570 -568 1380 257 N ATOM 329 N GLY A 74 -54.277 -1.461 -17.080 1.00 74.10 N ANISOU 329 N GLY A 74 12357 5872 9923 -515 1361 159 N ATOM 330 CA GLY A 74 -54.312 -2.745 -17.788 1.00 75.27 C ANISOU 330 CA GLY A 74 12843 5778 9978 -554 1366 127 C ATOM 331 C GLY A 74 -55.138 -2.777 -19.059 1.00 74.26 C ANISOU 331 C GLY A 74 12638 5692 9886 -749 1374 38 C ATOM 332 O GLY A 74 -55.479 -3.854 -19.537 1.00 77.06 O ANISOU 332 O GLY A 74 13285 5838 10153 -869 1383 6 O ATOM 333 N VAL A 75 -55.442 -1.614 -19.625 1.00 72.01 N ANISOU 333 N VAL A 75 11982 5658 9718 -776 1358 -3 N ATOM 334 CA VAL A 75 -56.270 -1.556 -20.828 1.00 72.31 C ANISOU 334 CA VAL A 75 11930 5756 9787 -956 1348 -89 C ATOM 335 C VAL A 75 -55.463 -2.005 -22.040 1.00 73.07 C ANISOU 335 C VAL A 75 12157 5755 9852 -764 1310 -136 C ATOM 336 O VAL A 75 -54.233 -1.857 -22.076 1.00 72.93 O ANISOU 336 O VAL A 75 12134 5737 9839 -465 1290 -109 O ATOM 337 CB VAL A 75 -56.862 -0.149 -21.097 1.00 70.93 C ANISOU 337 CB VAL A 75 11338 5876 9737 -1025 1330 -121 C ATOM 338 CG1 VAL A 75 -57.618 0.366 -19.875 1.00 70.54 C ANISOU 338 CG1 VAL A 75 11143 5942 9714 -1179 1376 -84 C ATOM 339 CG2 VAL A 75 -55.788 0.846 -21.543 1.00 69.56 C ANISOU 339 CG2 VAL A 75 10949 5842 9639 -743 1283 -110 C ATOM 340 N ALA A 76 -56.166 -2.561 -23.022 1.00 73.58 N ANISOU 340 N ALA A 76 12333 5744 9879 -939 1299 -212 N ATOM 341 CA ALA A 76 -55.569 -2.904 -24.298 1.00 73.39 C ANISOU 341 CA ALA A 76 12417 5651 9816 -782 1266 -273 C ATOM 342 C ALA A 76 -55.009 -1.633 -24.942 1.00 71.92 C ANISOU 342 C ALA A 76 11887 5711 9727 -601 1243 -281 C ATOM 343 O ALA A 76 -55.704 -0.621 -25.031 1.00 70.98 O ANISOU 343 O ALA A 76 11473 5798 9695 -730 1226 -293 O ATOM 344 CB ALA A 76 -56.608 -3.546 -25.198 1.00 74.37 C ANISOU 344 CB ALA A 76 12681 5686 9890 -1046 1245 -360 C ATOM 345 N THR A 77 -53.749 -1.686 -25.356 1.00 72.46 N ANISOU 345 N THR A 77 11998 5758 9775 -302 1244 -273 N ATOM 346 CA THR A 77 -53.063 -0.538 -25.960 1.00 71.12 C ANISOU 346 CA THR A 77 11529 5808 9683 -129 1235 -270 C ATOM 347 C THR A 77 -52.782 -0.679 -27.464 1.00 71.98 C ANISOU 347 C THR A 77 11690 5916 9743 -46 1232 -342 C ATOM 348 O THR A 77 -52.294 0.269 -28.084 1.00 71.49 O ANISOU 348 O THR A 77 11396 6034 9731 64 1233 -339 O ATOM 349 CB THR A 77 -51.735 -0.274 -25.235 1.00 70.64 C ANISOU 349 CB THR A 77 11399 5789 9651 152 1248 -201 C ATOM 350 OG1 THR A 77 -50.793 -1.316 -25.538 1.00 72.90 O ANISOU 350 OG1 THR A 77 11951 5905 9843 380 1264 -218 O ATOM 351 CG2 THR A 77 -51.960 -0.218 -23.741 1.00 70.14 C ANISOU 351 CG2 THR A 77 11332 5706 9611 87 1245 -131 C ATOM 352 N ASP A 78 -53.063 -1.849 -28.044 1.00 73.25 N ANISOU 352 N ASP A 78 12168 5867 9793 -100 1230 -405 N ATOM 353 CA ASP A 78 -53.024 -2.019 -29.500 1.00 74.38 C ANISOU 353 CA ASP A 78 12387 6001 9871 -64 1221 -487 C ATOM 354 C ASP A 78 -53.942 -1.018 -30.220 1.00 73.32 C ANISOU 354 C ASP A 78 12000 6060 9798 -254 1176 -521 C ATOM 355 O ASP A 78 -55.001 -0.647 -29.705 1.00 72.61 O ANISOU 355 O ASP A 78 11778 6037 9770 -491 1143 -515 O ATOM 356 CB ASP A 78 -53.398 -3.450 -29.895 1.00 77.44 C ANISOU 356 CB ASP A 78 13183 6111 10127 -145 1207 -557 C ATOM 357 CG ASP A 78 -54.808 -3.831 -29.469 1.00 79.49 C ANISOU 357 CG ASP A 78 13520 6290 10390 -507 1170 -575 C ATOM 358 OD1 ASP A 78 -55.000 -4.201 -28.293 1.00 80.85 O ANISOU 358 OD1 ASP A 78 13775 6373 10572 -590 1189 -517 O ATOM 359 OD2 ASP A 78 -55.724 -3.768 -30.313 1.00 81.24 O ANISOU 359 OD2 ASP A 78 13720 6546 10599 -712 1122 -648 O ATOM 360 N VAL A 79 -53.524 -0.583 -31.406 1.00 73.59 N ANISOU 360 N VAL A 79 11969 6186 9803 -138 1177 -558 N ATOM 361 CA VAL A 79 -54.245 0.456 -32.154 1.00 73.37 C ANISOU 361 CA VAL A 79 11711 6345 9821 -269 1125 -582 C ATOM 362 C VAL A 79 -55.726 0.128 -32.387 1.00 74.72 C ANISOU 362 C VAL A 79 11940 6472 9978 -572 1047 -652 C ATOM 363 O VAL A 79 -56.574 0.983 -32.144 1.00 73.61 O ANISOU 363 O VAL A 79 11556 6489 9924 -727 998 -645 O ATOM 364 CB VAL A 79 -53.525 0.809 -33.485 1.00 73.77 C ANISOU 364 CB VAL A 79 11753 6469 9807 -96 1146 -612 C ATOM 365 CG1 VAL A 79 -54.444 1.545 -34.458 1.00 73.69 C ANISOU 365 CG1 VAL A 79 11625 6579 9794 -252 1069 -659 C ATOM 366 CG2 VAL A 79 -52.293 1.655 -33.193 1.00 72.54 C ANISOU 366 CG2 VAL A 79 11386 6462 9714 130 1212 -531 C ATOM 367 N PRO A 80 -56.042 -1.100 -32.851 1.00 77.33 N ANISOU 367 N PRO A 80 12589 6594 10198 -656 1031 -726 N ATOM 368 CA PRO A 80 -57.452 -1.458 -33.072 1.00 78.60 C ANISOU 368 CA PRO A 80 12795 6720 10346 -971 951 -798 C ATOM 369 C PRO A 80 -58.340 -1.304 -31.838 1.00 78.20 C ANISOU 369 C PRO A 80 12597 6724 10392 -1195 950 -758 C ATOM 370 O PRO A 80 -59.450 -0.802 -31.956 1.00 78.51 O ANISOU 370 O PRO A 80 12442 6902 10485 -1407 886 -796 O ATOM 371 CB PRO A 80 -57.384 -2.931 -33.485 1.00 80.16 C ANISOU 371 CB PRO A 80 13411 6639 10407 -998 950 -865 C ATOM 372 CG PRO A 80 -56.025 -3.100 -34.051 1.00 80.35 C ANISOU 372 CG PRO A 80 13566 6607 10355 -665 1010 -859 C ATOM 373 CD PRO A 80 -55.139 -2.194 -33.255 1.00 78.39 C ANISOU 373 CD PRO A 80 13055 6520 10210 -465 1077 -755 C ATOM 374 N SER A 81 -57.842 -1.731 -30.680 1.00 78.46 N ANISOU 374 N SER A 81 12722 6653 10435 -1134 1020 -686 N ATOM 375 CA SER A 81 -58.590 -1.666 -29.422 1.00 78.75 C ANISOU 375 CA SER A 81 12655 6725 10538 -1333 1042 -641 C ATOM 376 C SER A 81 -58.662 -0.242 -28.877 1.00 77.98 C ANISOU 376 C SER A 81 12169 6891 10567 -1284 1043 -588 C ATOM 377 O SER A 81 -59.682 0.159 -28.305 1.00 79.22 O ANISOU 377 O SER A 81 12140 7171 10789 -1490 1033 -592 O ATOM 378 CB SER A 81 -57.954 -2.588 -28.380 1.00 79.22 C ANISOU 378 CB SER A 81 12978 6574 10546 -1259 1111 -576 C ATOM 379 OG SER A 81 -57.925 -3.928 -28.847 1.00 83.06 O ANISOU 379 OG SER A 81 13860 6791 10907 -1305 1102 -628 O ATOM 380 N ALA A 82 -57.576 0.509 -29.055 1.00 76.29 N ANISOU 380 N ALA A 82 11839 6764 10383 -1014 1059 -542 N ATOM 381 CA ALA A 82 -57.479 1.878 -28.570 1.00 74.33 C ANISOU 381 CA ALA A 82 11260 6736 10244 -943 1053 -489 C ATOM 382 C ALA A 82 -58.414 2.831 -29.314 1.00 74.42 C ANISOU 382 C ALA A 82 11033 6936 10305 -1059 975 -542 C ATOM 383 O ALA A 82 -59.079 3.664 -28.702 1.00 73.92 O ANISOU 383 O ALA A 82 10730 7028 10325 -1143 955 -530 O ATOM 384 CB ALA A 82 -56.041 2.364 -28.685 1.00 73.07 C ANISOU 384 CB ALA A 82 11058 6610 10095 -649 1086 -431 C ATOM 385 N THR A 83 -58.464 2.708 -30.633 1.00 75.69 N ANISOU 385 N THR A 83 11271 7082 10406 -1049 925 -606 N ATOM 386 CA THR A 83 -59.277 3.608 -31.449 1.00 76.12 C ANISOU 386 CA THR A 83 11125 7305 10489 -1127 832 -657 C ATOM 387 C THR A 83 -60.778 3.393 -31.242 1.00 77.97 C ANISOU 387 C THR A 83 11280 7595 10751 -1407 772 -725 C ATOM 388 O THR A 83 -61.553 4.345 -31.359 1.00 77.25 O ANISOU 388 O THR A 83 10937 7689 10724 -1462 700 -751 O ATOM 389 CB THR A 83 -58.946 3.472 -32.941 1.00 76.19 C ANISOU 389 CB THR A 83 11267 7276 10404 -1044 791 -709 C ATOM 390 OG1 THR A 83 -59.053 2.096 -33.322 1.00 79.33 O ANISOU 390 OG1 THR A 83 11969 7473 10699 -1127 799 -770 O ATOM 391 CG2 THR A 83 -57.542 3.974 -33.214 1.00 75.09 C ANISOU 391 CG2 THR A 83 11122 7155 10251 -777 854 -642 C ATOM 392 N LYS A 84 -61.181 2.161 -30.920 1.00 79.48 N ANISOU 392 N LYS A 84 11679 7626 10891 -1581 802 -756 N ATOM 393 CA LYS A 84 -62.586 1.867 -30.629 1.00 81.05 C ANISOU 393 CA LYS A 84 11795 7884 11117 -1880 763 -818 C ATOM 394 C LYS A 84 -63.096 2.558 -29.364 1.00 78.22 C ANISOU 394 C LYS A 84 11175 7686 10859 -1942 808 -773 C ATOM 395 O LYS A 84 -64.305 2.676 -29.183 1.00 78.84 O ANISOU 395 O LYS A 84 11078 7896 10979 -2159 773 -830 O ATOM 396 CB LYS A 84 -62.841 0.351 -30.548 1.00 86.62 C ANISOU 396 CB LYS A 84 12818 8357 11733 -2075 793 -852 C ATOM 397 CG LYS A 84 -62.854 -0.357 -31.905 1.00 90.27 C ANISOU 397 CG LYS A 84 13516 8689 12092 -2103 716 -939 C ATOM 398 CD LYS A 84 -63.808 -1.536 -31.937 1.00 95.36 C ANISOU 398 CD LYS A 84 14352 9197 12680 -2425 688 -1012 C ATOM 399 CE LYS A 84 -63.281 -2.721 -31.143 1.00 98.86 C ANISOU 399 CE LYS A 84 15135 9371 13055 -2450 787 -960 C ATOM 400 NZ LYS A 84 -62.384 -3.576 -31.973 1.00101.00 N ANISOU 400 NZ LYS A 84 15778 9395 13200 -2286 778 -987 N ATOM 401 N ARG A 85 -62.184 3.006 -28.498 1.00 75.76 N ANISOU 401 N ARG A 85 10831 7371 10581 -1752 881 -679 N ATOM 402 CA ARG A 85 -62.530 3.863 -27.347 1.00 73.49 C ANISOU 402 CA ARG A 85 10293 7247 10382 -1759 917 -637 C ATOM 403 C ARG A 85 -62.794 5.346 -27.666 1.00 71.28 C ANISOU 403 C ARG A 85 9705 7196 10182 -1652 838 -652 C ATOM 404 O ARG A 85 -63.213 6.084 -26.772 1.00 71.15 O ANISOU 404 O ARG A 85 9479 7321 10232 -1660 857 -635 O ATOM 405 CB ARG A 85 -61.436 3.788 -26.272 1.00 71.82 C ANISOU 405 CB ARG A 85 10181 6939 10168 -1594 1007 -535 C ATOM 406 CG ARG A 85 -61.267 2.408 -25.659 1.00 72.41 C ANISOU 406 CG ARG A 85 10559 6791 10162 -1693 1085 -508 C ATOM 407 CD ARG A 85 -60.434 2.456 -24.389 1.00 70.95 C ANISOU 407 CD ARG A 85 10426 6552 9980 -1552 1160 -411 C ATOM 408 NE ARG A 85 -59.017 2.691 -24.665 1.00 69.38 N ANISOU 408 NE ARG A 85 10288 6298 9775 -1259 1150 -361 N ATOM 409 CZ ARG A 85 -58.073 1.753 -24.757 1.00 69.44 C ANISOU 409 CZ ARG A 85 10573 6104 9706 -1131 1176 -335 C ATOM 410 NH1 ARG A 85 -56.822 2.117 -24.995 1.00 67.68 N ANISOU 410 NH1 ARG A 85 10334 5887 9492 -862 1171 -297 N ATOM 411 NH2 ARG A 85 -58.348 0.456 -24.614 1.00 71.52 N ANISOU 411 NH2 ARG A 85 11133 6161 9881 -1263 1207 -348 N ATOM 412 N TRP A 86 -62.530 5.793 -28.897 1.00 69.71 N ANISOU 412 N TRP A 86 9498 7022 9964 -1544 753 -681 N ATOM 413 CA TRP A 86 -62.738 7.195 -29.279 1.00 67.76 C ANISOU 413 CA TRP A 86 9006 6961 9776 -1434 667 -689 C ATOM 414 C TRP A 86 -63.836 7.290 -30.323 1.00 68.39 C ANISOU 414 C TRP A 86 9002 7138 9842 -1557 546 -791 C ATOM 415 O TRP A 86 -64.053 6.353 -31.072 1.00 71.21 O ANISOU 415 O TRP A 86 9530 7396 10130 -1670 520 -846 O ATOM 416 CB TRP A 86 -61.439 7.838 -29.792 1.00 66.19 C ANISOU 416 CB TRP A 86 8858 6727 9564 -1191 668 -622 C ATOM 417 CG TRP A 86 -60.220 7.399 -29.032 1.00 64.95 C ANISOU 417 CG TRP A 86 8838 6442 9397 -1072 776 -537 C ATOM 418 CD1 TRP A 86 -60.125 7.189 -27.688 1.00 64.48 C ANISOU 418 CD1 TRP A 86 8769 6360 9371 -1092 850 -490 C ATOM 419 CD2 TRP A 86 -58.933 7.103 -29.575 1.00 64.20 C ANISOU 419 CD2 TRP A 86 8907 6238 9248 -904 818 -494 C ATOM 420 NE1 TRP A 86 -58.864 6.765 -27.360 1.00 63.98 N ANISOU 420 NE1 TRP A 86 8857 6171 9279 -943 918 -421 N ATOM 421 CE2 TRP A 86 -58.108 6.705 -28.502 1.00 64.85 C ANISOU 421 CE2 TRP A 86 9062 6236 9341 -822 904 -425 C ATOM 422 CE3 TRP A 86 -58.394 7.135 -30.862 1.00 64.69 C ANISOU 422 CE3 TRP A 86 9060 6274 9245 -809 794 -509 C ATOM 423 CZ2 TRP A 86 -56.762 6.336 -28.682 1.00 65.01 C ANISOU 423 CZ2 TRP A 86 9218 6159 9320 -638 960 -378 C ATOM 424 CZ3 TRP A 86 -57.059 6.762 -31.040 1.00 65.16 C ANISOU 424 CZ3 TRP A 86 9256 6240 9260 -635 870 -461 C ATOM 425 CH2 TRP A 86 -56.261 6.371 -29.952 1.00 64.30 C ANISOU 425 CH2 TRP A 86 9193 6062 9175 -547 948 -399 C ATOM 426 N GLY A 87 -64.531 8.423 -30.350 1.00 68.11 N ANISOU 426 N GLY A 87 8712 7297 9869 -1525 460 -820 N ATOM 427 CA GLY A 87 -65.665 8.637 -31.252 1.00 68.79 C ANISOU 427 CA GLY A 87 8676 7510 9950 -1622 322 -923 C ATOM 428 C GLY A 87 -66.015 10.105 -31.473 1.00 68.34 C ANISOU 428 C GLY A 87 8391 7631 9944 -1476 212 -933 C ATOM 429 O GLY A 87 -65.756 10.963 -30.622 1.00 66.10 O ANISOU 429 O GLY A 87 7982 7410 9720 -1358 249 -879 O ATOM 430 N PHE A 88 -66.626 10.377 -32.622 1.00 69.55 N ANISOU 430 N PHE A 88 8508 7855 10061 -1481 65 -1007 N ATOM 431 CA PHE A 88 -66.969 11.731 -33.034 1.00 69.53 C ANISOU 431 CA PHE A 88 8339 7996 10083 -1328 -66 -1022 C ATOM 432 C PHE A 88 -68.355 12.173 -32.537 1.00 70.50 C ANISOU 432 C PHE A 88 8164 8340 10282 -1399 -143 -1112 C ATOM 433 O PHE A 88 -69.289 11.382 -32.491 1.00 72.86 O ANISOU 433 O PHE A 88 8384 8706 10589 -1604 -154 -1197 O ATOM 434 CB PHE A 88 -66.846 11.856 -34.554 1.00 70.46 C ANISOU 434 CB PHE A 88 8593 8071 10104 -1268 -194 -1048 C ATOM 435 CG PHE A 88 -65.426 11.791 -35.036 1.00 70.16 C ANISOU 435 CG PHE A 88 8798 7863 9993 -1142 -114 -953 C ATOM 436 CD1 PHE A 88 -64.832 10.571 -35.345 1.00 70.91 C ANISOU 436 CD1 PHE A 88 9127 7797 10019 -1216 -25 -949 C ATOM 437 CD2 PHE A 88 -64.661 12.949 -35.145 1.00 69.46 C ANISOU 437 CD2 PHE A 88 8707 7777 9906 -949 -121 -869 C ATOM 438 CE1 PHE A 88 -63.505 10.509 -35.772 1.00 70.05 C ANISOU 438 CE1 PHE A 88 9216 7556 9842 -1081 59 -869 C ATOM 439 CE2 PHE A 88 -63.335 12.889 -35.576 1.00 68.93 C ANISOU 439 CE2 PHE A 88 8834 7580 9775 -847 -33 -783 C ATOM 440 CZ PHE A 88 -62.758 11.666 -35.886 1.00 68.48 C ANISOU 440 CZ PHE A 88 8981 7388 9651 -905 61 -785 C ATOM 441 N ARG A 89 -68.462 13.450 -32.167 1.00 69.44 N ANISOU 441 N ARG A 89 7866 8318 10198 -1226 -193 -1094 N ATOM 442 CA ARG A 89 -69.673 14.016 -31.572 1.00 69.25 C ANISOU 442 CA ARG A 89 7544 8517 10248 -1237 -251 -1178 C ATOM 443 C ARG A 89 -69.688 15.522 -31.807 1.00 69.16 C ANISOU 443 C ARG A 89 7445 8581 10249 -990 -379 -1168 C ATOM 444 O ARG A 89 -68.644 16.183 -31.697 1.00 68.16 O ANISOU 444 O ARG A 89 7448 8337 10110 -836 -345 -1068 O ATOM 445 CB ARG A 89 -69.698 13.711 -30.062 1.00 68.00 C ANISOU 445 CB ARG A 89 7296 8388 10153 -1317 -79 -1150 C ATOM 446 CG ARG A 89 -70.738 14.433 -29.206 1.00 67.60 C ANISOU 446 CG ARG A 89 6939 8570 10175 -1283 -93 -1219 C ATOM 447 CD ARG A 89 -72.155 13.979 -29.501 1.00 69.73 C ANISOU 447 CD ARG A 89 6986 9041 10466 -1459 -166 -1353 C ATOM 448 NE ARG A 89 -73.147 14.891 -28.925 1.00 70.16 N ANISOU 448 NE ARG A 89 6725 9348 10585 -1361 -212 -1433 N ATOM 449 CZ ARG A 89 -73.501 14.946 -27.643 1.00 69.32 C ANISOU 449 CZ ARG A 89 6457 9355 10523 -1397 -74 -1440 C ATOM 450 NH1 ARG A 89 -74.413 15.830 -27.259 1.00 70.35 N ANISOU 450 NH1 ARG A 89 6301 9725 10702 -1273 -131 -1527 N ATOM 451 NH2 ARG A 89 -72.955 14.138 -26.737 1.00 68.65 N ANISOU 451 NH2 ARG A 89 6505 9150 10428 -1540 117 -1365 N ATOM 452 N SER A 90 -70.876 16.048 -32.116 1.00 69.69 N ANISOU 452 N SER A 90 7294 8845 10339 -957 -530 -1275 N ATOM 453 CA SER A 90 -71.103 17.483 -32.268 1.00 68.32 C ANISOU 453 CA SER A 90 7026 8755 10175 -714 -671 -1285 C ATOM 454 C SER A 90 -71.870 18.025 -31.068 1.00 67.70 C ANISOU 454 C SER A 90 6676 8862 10182 -661 -634 -1340 C ATOM 455 O SER A 90 -72.394 17.259 -30.259 1.00 67.17 O ANISOU 455 O SER A 90 6467 8893 10162 -836 -513 -1383 O ATOM 456 CB SER A 90 -71.873 17.769 -33.557 1.00 70.46 C ANISOU 456 CB SER A 90 7261 9112 10394 -663 -895 -1372 C ATOM 457 OG SER A 90 -71.076 17.501 -34.700 1.00 70.67 O ANISOU 457 OG SER A 90 7567 8961 10322 -664 -933 -1312 O ATOM 458 N GLY A 91 -71.892 19.354 -30.948 1.00 66.83 N ANISOU 458 N GLY A 91 6519 8789 10081 -418 -731 -1334 N ATOM 459 CA GLY A 91 -72.665 20.055 -29.925 1.00 66.72 C ANISOU 459 CA GLY A 91 6254 8960 10133 -310 -724 -1401 C ATOM 460 C GLY A 91 -72.013 20.203 -28.566 1.00 65.38 C ANISOU 460 C GLY A 91 6113 8728 9998 -291 -544 -1328 C ATOM 461 O GLY A 91 -72.612 20.791 -27.667 1.00 67.41 O ANISOU 461 O GLY A 91 6181 9132 10298 -192 -524 -1385 O ATOM 462 N VAL A 92 -70.796 19.688 -28.405 1.00 63.33 N ANISOU 462 N VAL A 92 6087 8259 9717 -370 -418 -1209 N ATOM 463 CA VAL A 92 -70.096 19.717 -27.129 1.00 62.27 C ANISOU 463 CA VAL A 92 6000 8053 9607 -364 -256 -1135 C ATOM 464 C VAL A 92 -68.806 20.521 -27.310 1.00 61.80 C ANISOU 464 C VAL A 92 6164 7795 9519 -213 -285 -1019 C ATOM 465 O VAL A 92 -67.919 20.090 -28.049 1.00 62.61 O ANISOU 465 O VAL A 92 6463 7743 9582 -266 -273 -943 O ATOM 466 CB VAL A 92 -69.775 18.286 -26.661 1.00 61.46 C ANISOU 466 CB VAL A 92 5969 7882 9501 -604 -77 -1098 C ATOM 467 CG1 VAL A 92 -69.002 18.301 -25.339 1.00 59.37 C ANISOU 467 CG1 VAL A 92 5773 7534 9248 -586 76 -1017 C ATOM 468 CG2 VAL A 92 -71.063 17.469 -26.555 1.00 63.33 C ANISOU 468 CG2 VAL A 92 5992 8308 9759 -796 -49 -1210 C ATOM 469 N PRO A 93 -68.693 21.697 -26.664 1.00 62.46 N ANISOU 469 N PRO A 93 6224 7887 9621 -28 -323 -1009 N ATOM 470 CA PRO A 93 -67.440 22.448 -26.828 1.00 61.77 C ANISOU 470 CA PRO A 93 6351 7610 9509 78 -350 -895 C ATOM 471 C PRO A 93 -66.253 21.748 -26.163 1.00 61.30 C ANISOU 471 C PRO A 93 6424 7413 9455 -25 -185 -793 C ATOM 472 O PRO A 93 -66.401 21.230 -25.067 1.00 61.83 O ANISOU 472 O PRO A 93 6417 7527 9547 -95 -61 -805 O ATOM 473 CB PRO A 93 -67.726 23.775 -26.124 1.00 60.79 C ANISOU 473 CB PRO A 93 6165 7530 9402 279 -425 -925 C ATOM 474 CG PRO A 93 -69.201 23.886 -26.095 1.00 62.59 C ANISOU 474 CG PRO A 93 6152 7978 9650 330 -495 -1064 C ATOM 475 CD PRO A 93 -69.705 22.488 -25.949 1.00 63.54 C ANISOU 475 CD PRO A 93 6149 8201 9789 104 -370 -1106 C ATOM 476 N PRO A 94 -65.086 21.724 -26.821 1.00 62.54 N ANISOU 476 N PRO A 94 6773 7409 9579 -31 -181 -693 N ATOM 477 CA PRO A 94 -63.930 21.104 -26.163 1.00 62.36 C ANISOU 477 CA PRO A 94 6857 7271 9563 -101 -39 -602 C ATOM 478 C PRO A 94 -63.466 21.867 -24.921 1.00 60.92 C ANISOU 478 C PRO A 94 6668 7066 9413 -10 -10 -567 C ATOM 479 O PRO A 94 -63.662 23.077 -24.823 1.00 62.68 O ANISOU 479 O PRO A 94 6872 7302 9640 124 -115 -582 O ATOM 480 CB PRO A 94 -62.850 21.112 -27.252 1.00 61.44 C ANISOU 480 CB PRO A 94 6917 7022 9404 -98 -57 -517 C ATOM 481 CG PRO A 94 -63.274 22.170 -28.207 1.00 62.63 C ANISOU 481 CG PRO A 94 7083 7190 9524 6 -218 -538 C ATOM 482 CD PRO A 94 -64.770 22.139 -28.198 1.00 63.84 C ANISOU 482 CD PRO A 94 7063 7501 9691 14 -295 -661 C ATOM 483 N LYS A 95 -62.892 21.136 -23.975 1.00 58.42 N ANISOU 483 N LYS A 95 6382 6707 9107 -81 120 -525 N ATOM 484 CA LYS A 95 -62.418 21.699 -22.732 1.00 57.56 C ANISOU 484 CA LYS A 95 6278 6573 9017 -11 152 -494 C ATOM 485 C LYS A 95 -61.049 21.129 -22.424 1.00 56.71 C ANISOU 485 C LYS A 95 6300 6340 8906 -53 237 -394 C ATOM 486 O LYS A 95 -60.740 19.987 -22.777 1.00 56.59 O ANISOU 486 O LYS A 95 6343 6284 8874 -151 317 -370 O ATOM 487 CB LYS A 95 -63.395 21.389 -21.594 1.00 57.90 C ANISOU 487 CB LYS A 95 6191 6739 9067 -39 226 -568 C ATOM 488 CG LYS A 95 -64.716 22.126 -21.692 1.00 59.37 C ANISOU 488 CG LYS A 95 6214 7079 9263 42 140 -677 C ATOM 489 CD LYS A 95 -64.561 23.593 -21.335 1.00 60.24 C ANISOU 489 CD LYS A 95 6345 7167 9377 228 34 -681 C ATOM 490 CE LYS A 95 -65.733 24.418 -21.810 1.00 62.02 C ANISOU 490 CE LYS A 95 6443 7516 9603 352 -92 -784 C ATOM 491 NZ LYS A 95 -67.009 23.943 -21.217 1.00 64.17 N ANISOU 491 NZ LYS A 95 6503 7991 9885 316 -20 -893 N ATOM 492 N VAL A 96 -60.243 21.953 -21.762 1.00 56.49 N ANISOU 492 N VAL A 96 6317 6253 8891 28 209 -342 N ATOM 493 CA VAL A 96 -58.854 21.666 -21.463 1.00 54.79 C ANISOU 493 CA VAL A 96 6201 5937 8680 15 260 -250 C ATOM 494 C VAL A 96 -58.581 22.062 -20.022 1.00 55.53 C ANISOU 494 C VAL A 96 6292 6024 8782 66 272 -242 C ATOM 495 O VAL A 96 -59.043 23.113 -19.564 1.00 55.97 O ANISOU 495 O VAL A 96 6312 6111 8842 148 197 -282 O ATOM 496 CB VAL A 96 -57.935 22.445 -22.415 1.00 54.27 C ANISOU 496 CB VAL A 96 6204 5798 8617 50 184 -184 C ATOM 497 CG1 VAL A 96 -56.482 22.412 -21.949 1.00 54.36 C ANISOU 497 CG1 VAL A 96 6274 5735 8643 51 220 -97 C ATOM 498 CG2 VAL A 96 -58.079 21.892 -23.826 1.00 54.21 C ANISOU 498 CG2 VAL A 96 6227 5789 8580 -1 190 -186 C ATOM 499 N VAL A 97 -57.836 21.209 -19.319 1.00 55.63 N ANISOU 499 N VAL A 97 6359 5991 8787 29 359 -194 N ATOM 500 CA VAL A 97 -57.405 21.459 -17.937 1.00 55.51 C ANISOU 500 CA VAL A 97 6368 5958 8766 75 368 -177 C ATOM 501 C VAL A 97 -55.930 21.104 -17.850 1.00 55.35 C ANISOU 501 C VAL A 97 6422 5852 8754 78 380 -90 C ATOM 502 O VAL A 97 -55.474 20.222 -18.581 1.00 55.85 O ANISOU 502 O VAL A 97 6520 5885 8815 35 433 -56 O ATOM 503 CB VAL A 97 -58.206 20.623 -16.925 1.00 55.30 C ANISOU 503 CB VAL A 97 6327 5984 8701 29 471 -219 C ATOM 504 CG1 VAL A 97 -58.035 19.124 -17.166 1.00 55.54 C ANISOU 504 CG1 VAL A 97 6421 5973 8707 -69 576 -190 C ATOM 505 CG2 VAL A 97 -57.817 20.978 -15.499 1.00 54.60 C ANISOU 505 CG2 VAL A 97 6281 5877 8586 90 471 -206 C ATOM 506 N ASN A 98 -55.182 21.768 -16.974 1.00 54.70 N ANISOU 506 N ASN A 98 6364 5738 8679 134 327 -60 N ATOM 507 CA ASN A 98 -53.745 21.554 -16.958 1.00 56.18 C ANISOU 507 CA ASN A 98 6588 5870 8885 143 319 16 C ATOM 508 C ASN A 98 -53.341 20.569 -15.873 1.00 56.07 C ANISOU 508 C ASN A 98 6631 5834 8838 156 382 37 C ATOM 509 O ASN A 98 -54.087 20.356 -14.920 1.00 56.31 O ANISOU 509 O ASN A 98 6685 5883 8826 157 418 0 O ATOM 510 CB ASN A 98 -52.990 22.885 -16.856 1.00 57.01 C ANISOU 510 CB ASN A 98 6686 5950 9024 175 204 44 C ATOM 511 CG ASN A 98 -52.794 23.337 -15.438 1.00 57.76 C ANISOU 511 CG ASN A 98 6811 6031 9102 223 154 33 C ATOM 512 OD1 ASN A 98 -53.735 23.739 -14.779 1.00 58.89 O ANISOU 512 OD1 ASN A 98 6962 6197 9215 258 142 -27 O ATOM 513 ND2 ASN A 98 -51.562 23.254 -14.957 1.00 58.96 N ANISOU 513 ND2 ASN A 98 6975 6156 9269 233 123 87 N ATOM 514 N TYR A 99 -52.169 19.957 -16.060 1.00 56.17 N ANISOU 514 N TYR A 99 6667 5811 8861 172 398 96 N ATOM 515 CA TYR A 99 -51.538 19.116 -15.045 1.00 58.05 C ANISOU 515 CA TYR A 99 6975 6015 9065 215 427 126 C ATOM 516 C TYR A 99 -49.996 19.267 -15.061 1.00 57.77 C ANISOU 516 C TYR A 99 6909 5972 9067 271 368 185 C ATOM 517 O TYR A 99 -49.398 19.435 -16.110 1.00 57.21 O ANISOU 517 O TYR A 99 6777 5920 9037 259 366 210 O ATOM 518 CB TYR A 99 -51.995 17.648 -15.205 1.00 58.72 C ANISOU 518 CB TYR A 99 7144 6064 9100 181 540 121 C ATOM 519 CG TYR A 99 -51.454 16.937 -16.423 1.00 57.76 C ANISOU 519 CG TYR A 99 7031 5920 8995 180 582 144 C ATOM 520 CD1 TYR A 99 -52.103 17.010 -17.648 1.00 57.51 C ANISOU 520 CD1 TYR A 99 6964 5911 8976 116 605 114 C ATOM 521 CD2 TYR A 99 -50.293 16.180 -16.340 1.00 59.41 C ANISOU 521 CD2 TYR A 99 7287 6090 9196 257 595 190 C ATOM 522 CE1 TYR A 99 -51.603 16.361 -18.766 1.00 57.92 C ANISOU 522 CE1 TYR A 99 7041 5940 9026 122 647 130 C ATOM 523 CE2 TYR A 99 -49.772 15.524 -17.449 1.00 59.79 C ANISOU 523 CE2 TYR A 99 7346 6123 9248 277 642 203 C ATOM 524 CZ TYR A 99 -50.431 15.615 -18.661 1.00 59.33 C ANISOU 524 CZ TYR A 99 7266 6081 9195 205 673 173 C ATOM 525 OH TYR A 99 -49.917 14.961 -19.757 1.00 58.87 O ANISOU 525 OH TYR A 99 7235 6006 9124 231 723 180 O ATOM 526 N GLU A 100 -49.378 19.186 -13.885 1.00 60.19 N ANISOU 526 N GLU A 100 7253 6263 9352 331 323 204 N ATOM 527 CA GLU A 100 -47.953 19.523 -13.666 1.00 62.15 C ANISOU 527 CA GLU A 100 7443 6531 9641 383 238 247 C ATOM 528 C GLU A 100 -46.969 18.375 -13.886 1.00 61.41 C ANISOU 528 C GLU A 100 7356 6433 9543 457 280 286 C ATOM 529 O GLU A 100 -45.786 18.616 -14.115 1.00 61.54 O ANISOU 529 O GLU A 100 7274 6498 9609 492 229 317 O ATOM 530 CB GLU A 100 -47.742 19.980 -12.222 1.00 65.37 C ANISOU 530 CB GLU A 100 7894 6926 10018 427 146 241 C ATOM 531 CG GLU A 100 -48.621 21.134 -11.769 1.00 68.76 C ANISOU 531 CG GLU A 100 8335 7353 10436 390 94 194 C ATOM 532 CD GLU A 100 -48.674 21.303 -10.257 1.00 72.34 C ANISOU 532 CD GLU A 100 8878 7785 10822 442 36 176 C ATOM 533 OE1 GLU A 100 -49.310 22.293 -9.798 1.00 75.18 O ANISOU 533 OE1 GLU A 100 9258 8143 11164 434 -13 130 O ATOM 534 OE2 GLU A 100 -48.081 20.465 -9.535 1.00 71.03 O ANISOU 534 OE2 GLU A 100 8776 7600 10612 503 35 204 O ATOM 535 N ALA A 101 -47.446 17.140 -13.752 1.00 60.39 N ANISOU 535 N ALA A 101 7346 6247 9351 482 367 280 N ATOM 536 CA ALA A 101 -46.584 15.957 -13.784 1.00 60.44 C ANISOU 536 CA ALA A 101 7407 6224 9334 584 398 309 C ATOM 537 C ALA A 101 -47.312 14.796 -14.409 1.00 59.27 C ANISOU 537 C ALA A 101 7378 6005 9134 558 514 294 C ATOM 538 O ALA A 101 -48.514 14.650 -14.239 1.00 58.58 O ANISOU 538 O ALA A 101 7367 5881 9007 468 565 266 O ATOM 539 CB ALA A 101 -46.151 15.580 -12.381 1.00 61.41 C ANISOU 539 CB ALA A 101 7623 6309 9400 676 336 327 C ATOM 540 N GLY A 102 -46.578 13.957 -15.120 1.00 59.72 N ANISOU 540 N GLY A 102 7452 6047 9191 637 554 309 N ATOM 541 CA GLY A 102 -47.189 12.828 -15.792 1.00 60.65 C ANISOU 541 CA GLY A 102 7706 6081 9255 612 654 290 C ATOM 542 C GLY A 102 -46.347 11.590 -15.706 1.00 61.73 C ANISOU 542 C GLY A 102 7964 6146 9343 759 673 309 C ATOM 543 O GLY A 102 -45.281 11.583 -15.081 1.00 62.00 O ANISOU 543 O GLY A 102 7961 6208 9385 893 604 336 O ATOM 544 N GLU A 103 -46.854 10.550 -16.352 1.00 62.17 N ANISOU 544 N GLU A 103 8169 6107 9345 734 757 289 N ATOM 545 CA GLU A 103 -46.283 9.221 -16.313 1.00 63.70 C ANISOU 545 CA GLU A 103 8542 6190 9469 872 783 297 C ATOM 546 C GLU A 103 -45.714 8.923 -17.690 1.00 64.07 C ANISOU 546 C GLU A 103 8541 6268 9535 941 832 275 C ATOM 547 O GLU A 103 -46.360 9.204 -18.700 1.00 63.79 O ANISOU 547 O GLU A 103 8463 6257 9516 822 881 246 O ATOM 548 CB GLU A 103 -47.374 8.217 -15.944 1.00 63.80 C ANISOU 548 CB GLU A 103 8805 6045 9388 770 843 288 C ATOM 549 CG GLU A 103 -46.937 6.767 -16.030 1.00 66.81 C ANISOU 549 CG GLU A 103 9430 6270 9682 895 872 293 C ATOM 550 CD GLU A 103 -47.852 5.808 -15.290 1.00 67.35 C ANISOU 550 CD GLU A 103 9776 6167 9644 791 914 304 C ATOM 551 OE1 GLU A 103 -47.329 4.785 -14.805 1.00 70.11 O ANISOU 551 OE1 GLU A 103 10350 6376 9909 925 900 329 O ATOM 552 OE2 GLU A 103 -49.079 6.055 -15.189 1.00 64.98 O ANISOU 552 OE2 GLU A 103 9475 5874 9341 578 962 287 O ATOM 553 N TRP A 104 -44.513 8.351 -17.727 1.00 63.99 N ANISOU 553 N TRP A 104 8538 6261 9512 1144 817 285 N ATOM 554 CA TRP A 104 -43.897 7.945 -18.983 1.00 64.14 C ANISOU 554 CA TRP A 104 8528 6312 9531 1241 879 259 C ATOM 555 C TRP A 104 -44.808 6.882 -19.595 1.00 65.24 C ANISOU 555 C TRP A 104 8916 6287 9585 1174 954 222 C ATOM 556 O TRP A 104 -45.233 5.950 -18.899 1.00 65.55 O ANISOU 556 O TRP A 104 9193 6165 9547 1177 952 227 O ATOM 557 CB TRP A 104 -42.514 7.311 -18.753 1.00 66.13 C ANISOU 557 CB TRP A 104 8771 6586 9768 1503 850 266 C ATOM 558 CG TRP A 104 -41.391 8.232 -18.373 1.00 65.83 C ANISOU 558 CG TRP A 104 8460 6734 9816 1586 777 291 C ATOM 559 CD1 TRP A 104 -41.370 9.148 -17.355 1.00 65.35 C ANISOU 559 CD1 TRP A 104 8285 6736 9807 1518 682 323 C ATOM 560 CD2 TRP A 104 -40.100 8.281 -18.978 1.00 66.58 C ANISOU 560 CD2 TRP A 104 8365 6979 9951 1751 792 282 C ATOM 561 NE1 TRP A 104 -40.153 9.783 -17.309 1.00 65.65 N ANISOU 561 NE1 TRP A 104 8074 6948 9919 1611 626 334 N ATOM 562 CE2 TRP A 104 -39.351 9.269 -18.291 1.00 66.72 C ANISOU 562 CE2 TRP A 104 8143 7152 10053 1752 697 311 C ATOM 563 CE3 TRP A 104 -39.499 7.592 -20.041 1.00 67.71 C ANISOU 563 CE3 TRP A 104 8513 7150 10062 1897 880 246 C ATOM 564 CZ2 TRP A 104 -38.029 9.581 -18.629 1.00 67.83 C ANISOU 564 CZ2 TRP A 104 8028 7486 10255 1875 690 309 C ATOM 565 CZ3 TRP A 104 -38.186 7.904 -20.383 1.00 68.89 C ANISOU 565 CZ3 TRP A 104 8406 7499 10267 2040 886 242 C ATOM 566 CH2 TRP A 104 -37.465 8.893 -19.676 1.00 69.13 C ANISOU 566 CH2 TRP A 104 8179 7695 10390 2019 792 275 C ATOM 567 N ALA A 105 -45.109 7.021 -20.882 1.00 64.90 N ANISOU 567 N ALA A 105 8833 6278 9545 1102 1016 187 N ATOM 568 CA ALA A 105 -45.963 6.061 -21.576 1.00 65.60 C ANISOU 568 CA ALA A 105 9150 6220 9554 1024 1075 142 C ATOM 569 C ALA A 105 -45.150 5.062 -22.387 1.00 67.42 C ANISOU 569 C ALA A 105 9506 6389 9719 1216 1125 109 C ATOM 570 O ALA A 105 -44.052 5.366 -22.863 1.00 68.39 O ANISOU 570 O ALA A 105 9469 6642 9874 1373 1141 111 O ATOM 571 CB ALA A 105 -46.936 6.790 -22.481 1.00 65.01 C ANISOU 571 CB ALA A 105 8984 6207 9508 823 1097 114 C ATOM 572 N GLU A 106 -45.694 3.857 -22.505 1.00 68.85 N ANISOU 572 N GLU A 106 9980 6373 9805 1201 1152 77 N ATOM 573 CA GLU A 106 -45.297 2.923 -23.547 1.00 71.57 C ANISOU 573 CA GLU A 106 10488 6635 10070 1334 1207 24 C ATOM 574 C GLU A 106 -45.996 3.218 -24.871 1.00 69.53 C ANISOU 574 C GLU A 106 10202 6412 9802 1180 1254 -23 C ATOM 575 O GLU A 106 -45.399 3.060 -25.928 1.00 72.50 O ANISOU 575 O GLU A 106 10570 6832 10144 1301 1306 -60 O ATOM 576 CB GLU A 106 -45.576 1.475 -23.131 1.00 74.90 C ANISOU 576 CB GLU A 106 11279 6799 10381 1379 1203 8 C ATOM 577 CG GLU A 106 -44.445 0.872 -22.329 1.00 78.47 C ANISOU 577 CG GLU A 106 11811 7202 10802 1658 1165 34 C ATOM 578 CD GLU A 106 -43.420 0.156 -23.172 1.00 81.91 C ANISOU 578 CD GLU A 106 12320 7622 11180 1935 1203 -16 C ATOM 579 OE1 GLU A 106 -43.804 -0.764 -23.927 1.00 84.35 O ANISOU 579 OE1 GLU A 106 12893 7762 11392 1929 1243 -72 O ATOM 580 OE2 GLU A 106 -42.224 0.493 -23.044 1.00 85.67 O ANISOU 580 OE2 GLU A 106 12591 8256 11702 2162 1190 -4 O ATOM 581 N ASN A 107 -47.253 3.633 -24.812 1.00 66.31 N ANISOU 581 N ASN A 107 9782 5994 9416 927 1234 -27 N ATOM 582 CA ASN A 107 -48.089 3.740 -25.990 1.00 66.63 C ANISOU 582 CA ASN A 107 9845 6038 9430 772 1255 -80 C ATOM 583 C ASN A 107 -48.751 5.105 -26.031 1.00 65.19 C ANISOU 583 C ASN A 107 9414 6018 9337 601 1220 -61 C ATOM 584 O ASN A 107 -49.492 5.494 -25.121 1.00 64.17 O ANISOU 584 O ASN A 107 9229 5899 9253 466 1181 -38 O ATOM 585 CB ASN A 107 -49.156 2.642 -26.009 1.00 67.93 C ANISOU 585 CB ASN A 107 10297 6000 9513 621 1253 -126 C ATOM 586 CG ASN A 107 -48.560 1.254 -26.011 1.00 69.84 C ANISOU 586 CG ASN A 107 10839 6045 9652 791 1278 -149 C ATOM 587 OD1 ASN A 107 -48.213 0.712 -27.059 1.00 69.67 O ANISOU 587 OD1 ASN A 107 10940 5971 9557 892 1312 -204 O ATOM 588 ND2 ASN A 107 -48.435 0.667 -24.825 1.00 71.44 N ANISOU 588 ND2 ASN A 107 11182 6127 9834 834 1258 -109 N ATOM 589 N CYS A 108 -48.445 5.830 -27.094 1.00 65.35 N ANISOU 589 N CYS A 108 9296 6163 9371 621 1237 -70 N ATOM 590 CA CYS A 108 -49.103 7.068 -27.417 1.00 64.59 C ANISOU 590 CA CYS A 108 9010 6194 9334 472 1198 -61 C ATOM 591 C CYS A 108 -49.626 6.947 -28.842 1.00 64.88 C ANISOU 591 C CYS A 108 9126 6221 9302 404 1212 -119 C ATOM 592 O CYS A 108 -49.243 6.034 -29.580 1.00 65.30 O ANISOU 592 O CYS A 108 9350 6192 9268 496 1262 -160 O ATOM 593 CB CYS A 108 -48.107 8.214 -27.311 1.00 65.09 C ANISOU 593 CB CYS A 108 8837 6421 9471 561 1196 -3 C ATOM 594 SG CYS A 108 -47.343 8.421 -25.684 1.00 65.48 S ANISOU 594 SG CYS A 108 8785 6498 9595 658 1160 58 S ATOM 595 N TYR A 109 -50.510 7.863 -29.217 1.00 64.15 N ANISOU 595 N TYR A 109 8922 6208 9241 255 1158 -127 N ATOM 596 CA TYR A 109 -51.143 7.841 -30.532 1.00 65.32 C ANISOU 596 CA TYR A 109 9142 6354 9322 177 1145 -183 C ATOM 597 C TYR A 109 -51.098 9.230 -31.170 1.00 65.77 C ANISOU 597 C TYR A 109 9022 6556 9410 154 1112 -152 C ATOM 598 O TYR A 109 -51.138 10.240 -30.471 1.00 64.15 O ANISOU 598 O TYR A 109 8646 6435 9291 126 1070 -104 O ATOM 599 CB TYR A 109 -52.579 7.321 -30.413 1.00 65.07 C ANISOU 599 CB TYR A 109 9207 6242 9273 -9 1088 -245 C ATOM 600 CG TYR A 109 -52.643 6.063 -29.592 1.00 65.08 C ANISOU 600 CG TYR A 109 9390 6090 9247 -16 1118 -258 C ATOM 601 CD1 TYR A 109 -52.557 4.817 -30.190 1.00 65.94 C ANISOU 601 CD1 TYR A 109 9753 6046 9254 9 1151 -312 C ATOM 602 CD2 TYR A 109 -52.729 6.122 -28.208 1.00 64.53 C ANISOU 602 CD2 TYR A 109 9264 6014 9240 -39 1115 -214 C ATOM 603 CE1 TYR A 109 -52.576 3.662 -29.434 1.00 67.02 C ANISOU 603 CE1 TYR A 109 10093 6017 9354 5 1174 -317 C ATOM 604 CE2 TYR A 109 -52.745 4.971 -27.442 1.00 65.59 C ANISOU 604 CE2 TYR A 109 9595 5993 9333 -45 1144 -215 C ATOM 605 CZ TYR A 109 -52.666 3.747 -28.062 1.00 66.57 C ANISOU 605 CZ TYR A 109 9979 5955 9357 -24 1171 -264 C ATOM 606 OH TYR A 109 -52.696 2.611 -27.306 1.00 68.91 O ANISOU 606 OH TYR A 109 10505 6074 9603 -34 1193 -260 O ATOM 607 N ASN A 110 -51.004 9.246 -32.500 1.00 68.13 N ANISOU 607 N ASN A 110 9391 6870 9624 170 1132 -179 N ATOM 608 CA ASN A 110 -50.889 10.464 -33.298 1.00 67.87 C ANISOU 608 CA ASN A 110 9247 6952 9588 154 1110 -145 C ATOM 609 C ASN A 110 -51.718 10.274 -34.570 1.00 68.34 C ANISOU 609 C ASN A 110 9439 6981 9544 80 1068 -210 C ATOM 610 O ASN A 110 -51.335 9.508 -35.438 1.00 70.69 O ANISOU 610 O ASN A 110 9893 7227 9736 145 1130 -248 O ATOM 611 CB ASN A 110 -49.409 10.705 -33.617 1.00 68.45 C ANISOU 611 CB ASN A 110 9261 7100 9646 295 1214 -88 C ATOM 612 CG ASN A 110 -49.152 12.059 -34.256 1.00 68.06 C ANISOU 612 CG ASN A 110 9093 7166 9598 259 1203 -30 C ATOM 613 OD1 ASN A 110 -49.607 12.328 -35.365 1.00 67.93 O ANISOU 613 OD1 ASN A 110 9157 7154 9497 211 1181 -51 O ATOM 614 ND2 ASN A 110 -48.379 12.903 -33.571 1.00 67.15 N ANISOU 614 ND2 ASN A 110 8805 7136 9571 281 1213 43 N ATOM 615 N LEU A 111 -52.846 10.972 -34.679 1.00 68.71 N ANISOU 615 N LEU A 111 9427 7063 9615 -41 955 -230 N ATOM 616 CA LEU A 111 -53.829 10.706 -35.739 1.00 70.50 C ANISOU 616 CA LEU A 111 9774 7261 9751 -125 881 -307 C ATOM 617 C LEU A 111 -53.817 11.755 -36.847 1.00 71.89 C ANISOU 617 C LEU A 111 9937 7513 9865 -116 838 -282 C ATOM 618 O LEU A 111 -53.847 12.958 -36.563 1.00 73.06 O ANISOU 618 O LEU A 111 9943 7738 10076 -125 788 -224 O ATOM 619 CB LEU A 111 -55.234 10.618 -35.141 1.00 69.90 C ANISOU 619 CB LEU A 111 9643 7180 9735 -269 773 -364 C ATOM 620 CG LEU A 111 -55.407 9.704 -33.927 1.00 69.62 C ANISOU 620 CG LEU A 111 9620 7070 9759 -314 811 -378 C ATOM 621 CD1 LEU A 111 -56.878 9.622 -33.562 1.00 70.07 C ANISOU 621 CD1 LEU A 111 9619 7149 9855 -482 715 -443 C ATOM 622 CD2 LEU A 111 -54.846 8.315 -34.183 1.00 71.10 C ANISOU 622 CD2 LEU A 111 10028 7122 9863 -264 896 -409 C ATOM 623 N GLU A 112 -53.749 11.284 -38.098 1.00 73.03 N ANISOU 623 N GLU A 112 10252 7622 9872 -95 856 -324 N ATOM 624 CA GLU A 112 -53.958 12.108 -39.299 1.00 73.93 C ANISOU 624 CA GLU A 112 10413 7786 9889 -104 797 -315 C ATOM 625 C GLU A 112 -55.110 11.472 -40.068 1.00 73.49 C ANISOU 625 C GLU A 112 10499 7676 9745 -187 686 -421 C ATOM 626 O GLU A 112 -54.900 10.656 -40.953 1.00 76.10 O ANISOU 626 O GLU A 112 11020 7943 9948 -157 728 -473 O ATOM 627 CB GLU A 112 -52.694 12.150 -40.169 1.00 75.76 C ANISOU 627 CB GLU A 112 10731 8040 10014 3 936 -266 C ATOM 628 CG GLU A 112 -51.490 12.839 -39.533 1.00 77.14 C ANISOU 628 CG GLU A 112 10747 8291 10269 69 1043 -162 C ATOM 629 CD GLU A 112 -51.519 14.364 -39.602 1.00 79.08 C ANISOU 629 CD GLU A 112 10884 8613 10547 22 981 -79 C ATOM 630 OE1 GLU A 112 -52.490 14.957 -40.136 1.00 80.21 O ANISOU 630 OE1 GLU A 112 11074 8751 10649 -40 847 -99 O ATOM 631 OE2 GLU A 112 -50.544 14.981 -39.112 1.00 80.27 O ANISOU 631 OE2 GLU A 112 10908 8826 10763 50 1058 4 O ATOM 632 N ILE A 113 -56.332 11.834 -39.703 1.00 72.26 N ANISOU 632 N ILE A 113 10243 7552 9658 -289 540 -462 N ATOM 633 CA ILE A 113 -57.534 11.230 -40.266 1.00 73.63 C ANISOU 633 CA ILE A 113 10504 7697 9773 -394 415 -571 C ATOM 634 C ILE A 113 -58.263 12.254 -41.129 1.00 75.87 C ANISOU 634 C ILE A 113 10767 8056 10001 -405 261 -581 C ATOM 635 O ILE A 113 -58.486 13.387 -40.702 1.00 76.19 O ANISOU 635 O ILE A 113 10653 8175 10121 -387 198 -531 O ATOM 636 CB ILE A 113 -58.475 10.711 -39.152 1.00 72.33 C ANISOU 636 CB ILE A 113 10223 7529 9728 -517 366 -625 C ATOM 637 CG1 ILE A 113 -57.744 9.720 -38.241 1.00 71.85 C ANISOU 637 CG1 ILE A 113 10211 7375 9711 -499 509 -605 C ATOM 638 CG2 ILE A 113 -59.733 10.076 -39.728 1.00 73.31 C ANISOU 638 CG2 ILE A 113 10414 7640 9800 -655 233 -744 C ATOM 639 CD1 ILE A 113 -57.136 8.519 -38.932 1.00 73.25 C ANISOU 639 CD1 ILE A 113 10638 7426 9767 -455 593 -646 C ATOM 640 N LYS A 114 -58.623 11.841 -42.342 1.00 79.11 N ANISOU 640 N LYS A 114 11357 8432 10267 -423 194 -649 N ATOM 641 CA LYS A 114 -59.402 12.654 -43.264 1.00 81.73 C ANISOU 641 CA LYS A 114 11709 8824 10521 -427 23 -674 C ATOM 642 C LYS A 114 -60.685 11.936 -43.639 1.00 83.82 C ANISOU 642 C LYS A 114 12008 9085 10754 -546 -134 -806 C ATOM 643 O LYS A 114 -60.823 10.735 -43.437 1.00 83.98 O ANISOU 643 O LYS A 114 12101 9031 10775 -631 -92 -875 O ATOM 644 CB LYS A 114 -58.600 12.923 -44.533 1.00 84.45 C ANISOU 644 CB LYS A 114 12259 9140 10686 -336 77 -629 C ATOM 645 CG LYS A 114 -57.359 13.771 -44.333 1.00 85.78 C ANISOU 645 CG LYS A 114 12386 9334 10871 -242 222 -496 C ATOM 646 CD LYS A 114 -56.743 14.134 -45.676 1.00 89.57 C ANISOU 646 CD LYS A 114 13067 9807 11158 -177 265 -453 C ATOM 647 CE LYS A 114 -55.573 15.095 -45.531 1.00 91.46 C ANISOU 647 CE LYS A 114 13251 10086 11410 -119 402 -316 C ATOM 648 NZ LYS A 114 -54.479 14.516 -44.696 1.00 92.58 N ANISOU 648 NZ LYS A 114 13302 10229 11645 -81 599 -280 N ATOM 649 N LYS A 115 -61.633 12.687 -44.180 1.00 86.83 N ANISOU 649 N LYS A 115 12339 9545 11105 -555 -325 -843 N ATOM 650 CA LYS A 115 -62.801 12.092 -44.820 1.00 91.75 C ANISOU 650 CA LYS A 115 13009 10183 11668 -661 -500 -974 C ATOM 651 C LYS A 115 -62.370 11.584 -46.204 1.00 95.17 C ANISOU 651 C LYS A 115 13741 10526 11890 -625 -495 -1003 C ATOM 652 O LYS A 115 -61.316 11.995 -46.710 1.00 95.99 O ANISOU 652 O LYS A 115 13977 10595 11898 -507 -379 -913 O ATOM 653 CB LYS A 115 -63.947 13.111 -44.936 1.00 93.30 C ANISOU 653 CB LYS A 115 13036 10511 11900 -652 -721 -1009 C ATOM 654 CG LYS A 115 -64.681 13.383 -43.622 1.00 92.99 C ANISOU 654 CG LYS A 115 12698 10578 12057 -709 -748 -1027 C ATOM 655 CD LYS A 115 -66.121 13.859 -43.827 1.00 95.10 C ANISOU 655 CD LYS A 115 12794 10987 12350 -739 -989 -1127 C ATOM 656 CE LYS A 115 -66.298 15.357 -43.649 1.00 95.38 C ANISOU 656 CE LYS A 115 12700 11111 12427 -587 -1085 -1069 C ATOM 657 NZ LYS A 115 -66.510 15.718 -42.223 1.00 94.34 N ANISOU 657 NZ LYS A 115 12309 11058 12476 -592 -1021 -1050 N ATOM 658 N PRO A 116 -63.170 10.691 -46.830 1.00 97.89 N ANISOU 658 N PRO A 116 14199 10840 12154 -734 -617 -1129 N ATOM 659 CA PRO A 116 -62.835 10.269 -48.203 1.00 99.01 C ANISOU 659 CA PRO A 116 14645 10898 12075 -690 -633 -1167 C ATOM 660 C PRO A 116 -62.840 11.407 -49.249 1.00 99.12 C ANISOU 660 C PRO A 116 14743 10966 11951 -575 -743 -1121 C ATOM 661 O PRO A 116 -62.237 11.249 -50.308 1.00100.11 O ANISOU 661 O PRO A 116 15128 11026 11883 -504 -695 -1112 O ATOM 662 CB PRO A 116 -63.893 9.200 -48.523 1.00100.90 C ANISOU 662 CB PRO A 116 14951 11105 12281 -856 -784 -1322 C ATOM 663 CG PRO A 116 -64.987 9.418 -47.538 1.00101.38 C ANISOU 663 CG PRO A 116 14702 11284 12532 -979 -897 -1362 C ATOM 664 CD PRO A 116 -64.331 9.952 -46.301 1.00 99.22 C ANISOU 664 CD PRO A 116 14237 11039 12420 -914 -728 -1244 C ATOM 665 N ASP A 117 -63.495 12.533 -48.947 1.00 98.49 N ANISOU 665 N ASP A 117 14464 10999 11958 -548 -884 -1091 N ATOM 666 CA ASP A 117 -63.381 13.751 -49.764 1.00 98.50 C ANISOU 666 CA ASP A 117 14553 11033 11840 -423 -974 -1019 C ATOM 667 C ASP A 117 -62.156 14.644 -49.445 1.00 95.94 C ANISOU 667 C ASP A 117 14227 10691 11533 -317 -784 -857 C ATOM 668 O ASP A 117 -62.070 15.765 -49.949 1.00 95.92 O ANISOU 668 O ASP A 117 14284 10707 11451 -230 -853 -780 O ATOM 669 CB ASP A 117 -64.701 14.562 -49.723 1.00100.54 C ANISOU 669 CB ASP A 117 14633 11410 12156 -420 -1244 -1074 C ATOM 670 CG ASP A 117 -64.951 15.287 -48.389 1.00 98.99 C ANISOU 670 CG ASP A 117 14128 11300 12181 -407 -1232 -1029 C ATOM 671 OD1 ASP A 117 -64.069 15.331 -47.504 1.00 96.18 O ANISOU 671 OD1 ASP A 117 13702 10911 11930 -397 -1027 -939 O ATOM 672 OD2 ASP A 117 -66.066 15.831 -48.236 1.00100.07 O ANISOU 672 OD2 ASP A 117 14090 11549 12383 -396 -1440 -1092 O ATOM 673 N GLY A 118 -61.236 14.173 -48.599 1.00 93.47 N ANISOU 673 N GLY A 118 13848 10342 11323 -327 -559 -804 N ATOM 674 CA GLY A 118 -59.980 14.885 -48.326 1.00 91.93 C ANISOU 674 CA GLY A 118 13648 10138 11143 -245 -368 -659 C ATOM 675 C GLY A 118 -59.980 15.984 -47.265 1.00 90.16 C ANISOU 675 C GLY A 118 13193 9973 11091 -223 -380 -574 C ATOM 676 O GLY A 118 -58.921 16.559 -46.980 1.00 88.92 O ANISOU 676 O GLY A 118 13022 9808 10955 -178 -227 -457 O ATOM 677 N SER A 119 -61.142 16.288 -46.677 1.00 89.28 N ANISOU 677 N SER A 119 12896 9926 11098 -256 -558 -637 N ATOM 678 CA SER A 119 -61.225 17.294 -45.615 1.00 86.79 C ANISOU 678 CA SER A 119 12369 9663 10943 -223 -577 -573 C ATOM 679 C SER A 119 -60.759 16.695 -44.297 1.00 85.03 C ANISOU 679 C SER A 119 11979 9438 10888 -272 -412 -561 C ATOM 680 O SER A 119 -60.965 15.509 -44.040 1.00 81.98 O ANISOU 680 O SER A 119 11583 9033 10532 -351 -365 -639 O ATOM 681 CB SER A 119 -62.646 17.821 -45.470 1.00 86.79 C ANISOU 681 CB SER A 119 12224 9750 11000 -216 -820 -656 C ATOM 682 OG SER A 119 -63.555 16.753 -45.361 1.00 87.15 O ANISOU 682 OG SER A 119 12191 9837 11084 -318 -889 -789 O ATOM 683 N GLU A 120 -60.140 17.535 -43.466 1.00 85.22 N ANISOU 683 N GLU A 120 11893 9473 11014 -228 -335 -462 N ATOM 684 CA GLU A 120 -59.572 17.100 -42.184 1.00 82.59 C ANISOU 684 CA GLU A 120 11415 9137 10829 -256 -182 -435 C ATOM 685 C GLU A 120 -60.681 16.761 -41.182 1.00 81.18 C ANISOU 685 C GLU A 120 11037 9018 10789 -320 -266 -524 C ATOM 686 O GLU A 120 -61.704 17.451 -41.118 1.00 82.11 O ANISOU 686 O GLU A 120 11049 9208 10940 -304 -434 -568 O ATOM 687 CB GLU A 120 -58.654 18.183 -41.610 1.00 81.50 C ANISOU 687 CB GLU A 120 11217 8998 10752 -199 -104 -310 C ATOM 688 CG GLU A 120 -57.416 18.483 -42.456 1.00 82.61 C ANISOU 688 CG GLU A 120 11521 9096 10768 -163 19 -211 C ATOM 689 CD GLU A 120 -56.317 17.435 -42.356 1.00 83.67 C ANISOU 689 CD GLU A 120 11690 9205 10893 -166 229 -196 C ATOM 690 OE1 GLU A 120 -56.441 16.476 -41.565 1.00 84.52 O ANISOU 690 OE1 GLU A 120 11717 9304 11092 -193 278 -252 O ATOM 691 OE2 GLU A 120 -55.308 17.569 -43.080 1.00 85.40 O ANISOU 691 OE2 GLU A 120 12026 9415 11007 -137 350 -127 O ATOM 692 N CYS A 121 -60.476 15.690 -40.421 1.00 78.60 N ANISOU 692 N CYS A 121 10666 8663 10533 -387 -146 -551 N ATOM 693 CA CYS A 121 -61.430 15.264 -39.384 1.00 77.04 C ANISOU 693 CA CYS A 121 10289 8521 10461 -473 -186 -626 C ATOM 694 C CYS A 121 -61.151 15.866 -38.013 1.00 74.04 C ANISOU 694 C CYS A 121 9735 8174 10220 -440 -122 -565 C ATOM 695 O CYS A 121 -62.074 16.053 -37.222 1.00 74.95 O ANISOU 695 O CYS A 121 9675 8371 10430 -476 -189 -616 O ATOM 696 CB CYS A 121 -61.426 13.745 -39.256 1.00 77.22 C ANISOU 696 CB CYS A 121 10392 8475 10472 -579 -97 -686 C ATOM 697 SG CYS A 121 -62.229 12.958 -40.648 1.00 78.60 S ANISOU 697 SG CYS A 121 10732 8627 10504 -661 -224 -803 S ATOM 698 N LEU A 122 -59.877 16.131 -37.726 1.00 70.32 N ANISOU 698 N LEU A 122 9308 7651 9759 -374 8 -462 N ATOM 699 CA LEU A 122 -59.450 16.663 -36.442 1.00 67.31 C ANISOU 699 CA LEU A 122 8789 7287 9497 -342 69 -400 C ATOM 700 C LEU A 122 -58.932 18.092 -36.632 1.00 65.49 C ANISOU 700 C LEU A 122 8558 7065 9258 -253 28 -313 C ATOM 701 O LEU A 122 -58.422 18.426 -37.714 1.00 65.44 O ANISOU 701 O LEU A 122 8690 7027 9146 -221 26 -269 O ATOM 702 CB LEU A 122 -58.365 15.768 -35.858 1.00 66.54 C ANISOU 702 CB LEU A 122 8735 7122 9422 -345 243 -356 C ATOM 703 CG LEU A 122 -58.717 14.277 -35.796 1.00 68.15 C ANISOU 703 CG LEU A 122 9010 7275 9608 -431 293 -432 C ATOM 704 CD1 LEU A 122 -57.458 13.443 -35.557 1.00 69.24 C ANISOU 704 CD1 LEU A 122 9249 7328 9729 -385 454 -383 C ATOM 705 CD2 LEU A 122 -59.778 13.999 -34.742 1.00 67.34 C ANISOU 705 CD2 LEU A 122 8766 7220 9598 -525 254 -493 C ATOM 706 N PRO A 123 -59.071 18.945 -35.600 1.00 62.87 N ANISOU 706 N PRO A 123 8091 6769 9028 -220 -5 -288 N ATOM 707 CA PRO A 123 -58.587 20.322 -35.696 1.00 62.68 C ANISOU 707 CA PRO A 123 8087 6730 8997 -149 -53 -206 C ATOM 708 C PRO A 123 -57.100 20.427 -35.420 1.00 61.64 C ANISOU 708 C PRO A 123 7989 6551 8879 -144 89 -100 C ATOM 709 O PRO A 123 -56.538 19.581 -34.740 1.00 61.25 O ANISOU 709 O PRO A 123 7896 6494 8879 -165 209 -96 O ATOM 710 CB PRO A 123 -59.373 21.042 -34.608 1.00 61.83 C ANISOU 710 CB PRO A 123 7825 6676 8991 -113 -143 -240 C ATOM 711 CG PRO A 123 -59.602 20.010 -33.576 1.00 61.85 C ANISOU 711 CG PRO A 123 7716 6708 9073 -173 -54 -290 C ATOM 712 CD PRO A 123 -59.674 18.679 -34.283 1.00 62.81 C ANISOU 712 CD PRO A 123 7922 6809 9132 -250 3 -336 C ATOM 713 N ALA A 124 -56.470 21.462 -35.961 1.00 63.69 N ANISOU 713 N ALA A 124 8328 6781 9088 -119 70 -16 N ATOM 714 CA ALA A 124 -55.058 21.745 -35.687 1.00 62.86 C ANISOU 714 CA ALA A 124 8224 6654 9003 -130 194 85 C ATOM 715 C ALA A 124 -54.877 21.973 -34.201 1.00 62.62 C ANISOU 715 C ALA A 124 8051 6636 9105 -122 205 93 C ATOM 716 O ALA A 124 -55.764 22.543 -33.545 1.00 63.51 O ANISOU 716 O ALA A 124 8096 6759 9273 -95 92 51 O ATOM 717 CB ALA A 124 -54.594 22.977 -36.453 1.00 62.12 C ANISOU 717 CB ALA A 124 8242 6525 8835 -133 152 173 C ATOM 718 N ALA A 125 -53.742 21.529 -33.668 1.00 61.74 N ANISOU 718 N ALA A 125 7892 6528 9037 -133 336 142 N ATOM 719 CA ALA A 125 -53.437 21.761 -32.258 1.00 60.99 C ANISOU 719 CA ALA A 125 7677 6440 9054 -124 343 157 C ATOM 720 C ALA A 125 -53.534 23.259 -31.954 1.00 60.05 C ANISOU 720 C ALA A 125 7556 6297 8961 -120 230 198 C ATOM 721 O ALA A 125 -52.910 24.063 -32.630 1.00 60.73 O ANISOU 721 O ALA A 125 7718 6356 8998 -148 225 273 O ATOM 722 CB ALA A 125 -52.055 21.237 -31.905 1.00 60.61 C ANISOU 722 CB ALA A 125 7587 6407 9034 -125 481 214 C ATOM 723 N PRO A 126 -54.346 23.641 -30.961 1.00 60.32 N ANISOU 723 N PRO A 126 7520 6337 9062 -85 140 148 N ATOM 724 CA PRO A 126 -54.349 25.044 -30.535 1.00 60.94 C ANISOU 724 CA PRO A 126 7613 6375 9166 -65 33 182 C ATOM 725 C PRO A 126 -52.960 25.521 -30.129 1.00 61.93 C ANISOU 725 C PRO A 126 7730 6474 9325 -114 91 275 C ATOM 726 O PRO A 126 -52.083 24.713 -29.836 1.00 63.28 O ANISOU 726 O PRO A 126 7837 6680 9526 -138 209 298 O ATOM 727 CB PRO A 126 -55.280 25.045 -29.319 1.00 60.22 C ANISOU 727 CB PRO A 126 7422 6313 9145 -10 -24 102 C ATOM 728 CG PRO A 126 -56.175 23.866 -29.514 1.00 60.93 C ANISOU 728 CG PRO A 126 7465 6463 9223 -14 10 18 C ATOM 729 CD PRO A 126 -55.392 22.847 -30.286 1.00 60.71 C ANISOU 729 CD PRO A 126 7488 6428 9151 -67 130 53 C ATOM 730 N ASP A 127 -52.769 26.829 -30.113 1.00 63.72 N ANISOU 730 N ASP A 127 8024 6639 9546 -129 0 325 N ATOM 731 CA ASP A 127 -51.491 27.408 -29.748 1.00 64.75 C ANISOU 731 CA ASP A 127 8143 6746 9710 -203 35 411 C ATOM 732 C ASP A 127 -51.159 27.002 -28.313 1.00 64.07 C ANISOU 732 C ASP A 127 7928 6694 9720 -182 62 385 C ATOM 733 O ASP A 127 -51.972 27.193 -27.409 1.00 64.04 O ANISOU 733 O ASP A 127 7898 6679 9752 -117 -14 321 O ATOM 734 CB ASP A 127 -51.574 28.926 -29.895 1.00 68.42 C ANISOU 734 CB ASP A 127 8736 7112 10146 -226 -96 456 C ATOM 735 CG ASP A 127 -50.260 29.639 -29.626 1.00 72.06 C ANISOU 735 CG ASP A 127 9200 7543 10635 -342 -70 550 C ATOM 736 OD1 ASP A 127 -49.190 28.992 -29.511 1.00 73.73 O ANISOU 736 OD1 ASP A 127 9301 7831 10882 -403 56 588 O ATOM 737 OD2 ASP A 127 -50.314 30.889 -29.545 1.00 76.56 O ANISOU 737 OD2 ASP A 127 9890 8010 11188 -370 -187 583 O ATOM 738 N GLY A 128 -49.983 26.409 -28.119 1.00 61.86 N ANISOU 738 N GLY A 128 7567 6465 9472 -226 174 430 N ATOM 739 CA GLY A 128 -49.519 26.034 -26.791 1.00 60.69 C ANISOU 739 CA GLY A 128 7311 6345 9403 -203 191 416 C ATOM 740 C GLY A 128 -49.769 24.586 -26.404 1.00 60.98 C ANISOU 740 C GLY A 128 7285 6430 9451 -139 279 360 C ATOM 741 O GLY A 128 -49.363 24.168 -25.320 1.00 59.05 O ANISOU 741 O GLY A 128 6971 6205 9258 -110 296 352 O ATOM 742 N ILE A 129 -50.434 23.817 -27.270 1.00 61.70 N ANISOU 742 N ILE A 129 7421 6532 9488 -120 325 322 N ATOM 743 CA ILE A 129 -50.657 22.399 -27.012 1.00 61.74 C ANISOU 743 CA ILE A 129 7402 6561 9492 -79 410 273 C ATOM 744 C ILE A 129 -49.666 21.598 -27.845 1.00 62.49 C ANISOU 744 C ILE A 129 7504 6688 9552 -79 531 309 C ATOM 745 O ILE A 129 -49.702 21.630 -29.076 1.00 62.74 O ANISOU 745 O ILE A 129 7601 6722 9515 -102 559 321 O ATOM 746 CB ILE A 129 -52.114 21.982 -27.279 1.00 62.17 C ANISOU 746 CB ILE A 129 7498 6609 9515 -68 375 192 C ATOM 747 CG1 ILE A 129 -53.019 22.642 -26.231 1.00 62.46 C ANISOU 747 CG1 ILE A 129 7496 6642 9593 -44 279 146 C ATOM 748 CG2 ILE A 129 -52.262 20.459 -27.215 1.00 62.00 C ANISOU 748 CG2 ILE A 129 7488 6592 9477 -57 471 150 C ATOM 749 CD1 ILE A 129 -54.493 22.610 -26.562 1.00 64.17 C ANISOU 749 CD1 ILE A 129 7718 6879 9783 -34 219 65 C ATOM 750 N ARG A 130 -48.771 20.905 -27.144 1.00 62.56 N ANISOU 750 N ARG A 130 7448 6724 9599 -39 597 324 N ATOM 751 CA ARG A 130 -47.720 20.108 -27.751 1.00 62.92 C ANISOU 751 CA ARG A 130 7476 6812 9615 -4 715 350 C ATOM 752 C ARG A 130 -47.964 18.662 -27.395 1.00 62.60 C ANISOU 752 C ARG A 130 7480 6744 9561 69 774 296 C ATOM 753 O ARG A 130 -48.747 18.364 -26.506 1.00 60.68 O ANISOU 753 O ARG A 130 7256 6458 9339 75 730 256 O ATOM 754 CB ARG A 130 -46.361 20.540 -27.217 1.00 64.01 C ANISOU 754 CB ARG A 130 7493 7014 9812 -3 731 410 C ATOM 755 CG ARG A 130 -45.875 21.874 -27.753 1.00 65.66 C ANISOU 755 CG ARG A 130 7674 7249 10023 -104 699 476 C ATOM 756 CD ARG A 130 -44.679 22.385 -26.961 1.00 67.46 C ANISOU 756 CD ARG A 130 7765 7539 10324 -131 683 525 C ATOM 757 NE ARG A 130 -45.052 22.540 -25.559 1.00 68.43 N ANISOU 757 NE ARG A 130 7873 7618 10508 -101 579 496 N ATOM 758 CZ ARG A 130 -45.742 23.560 -25.045 1.00 68.06 C ANISOU 758 CZ ARG A 130 7875 7504 10479 -150 459 489 C ATOM 759 NH1 ARG A 130 -46.141 24.590 -25.796 1.00 68.87 N ANISOU 759 NH1 ARG A 130 8054 7563 10550 -231 411 514 N ATOM 760 NH2 ARG A 130 -46.032 23.547 -23.748 1.00 67.89 N ANISOU 760 NH2 ARG A 130 7843 7454 10499 -105 386 456 N ATOM 761 N GLY A 131 -47.272 17.761 -28.081 1.00 64.13 N ANISOU 761 N GLY A 131 7700 6958 9708 127 879 296 N ATOM 762 CA GLY A 131 -47.441 16.332 -27.844 1.00 65.13 C ANISOU 762 CA GLY A 131 7908 7031 9804 203 934 246 C ATOM 763 C GLY A 131 -46.946 15.878 -26.484 1.00 64.14 C ANISOU 763 C GLY A 131 7738 6896 9733 276 923 254 C ATOM 764 O GLY A 131 -46.087 16.525 -25.885 1.00 65.19 O ANISOU 764 O GLY A 131 7751 7092 9926 292 895 299 O ATOM 765 N PHE A 132 -47.491 14.756 -26.020 1.00 63.12 N ANISOU 765 N PHE A 132 7720 6685 9577 310 939 209 N ATOM 766 CA PHE A 132 -47.125 14.131 -24.746 1.00 62.41 C ANISOU 766 CA PHE A 132 7641 6559 9511 388 929 215 C ATOM 767 C PHE A 132 -45.617 13.920 -24.686 1.00 62.31 C ANISOU 767 C PHE A 132 7544 6614 9515 518 968 250 C ATOM 768 O PHE A 132 -45.032 13.462 -25.660 1.00 63.67 O ANISOU 768 O PHE A 132 7729 6814 9645 582 1048 244 O ATOM 769 CB PHE A 132 -47.826 12.778 -24.613 1.00 63.03 C ANISOU 769 CB PHE A 132 7897 6521 9528 399 967 167 C ATOM 770 CG PHE A 132 -47.825 12.216 -23.221 1.00 63.57 C ANISOU 770 CG PHE A 132 8022 6528 9603 442 944 174 C ATOM 771 CD1 PHE A 132 -48.734 12.673 -22.282 1.00 62.10 C ANISOU 771 CD1 PHE A 132 7823 6330 9441 350 890 168 C ATOM 772 CD2 PHE A 132 -46.942 11.194 -22.857 1.00 65.16 C ANISOU 772 CD2 PHE A 132 8303 6680 9774 587 978 183 C ATOM 773 CE1 PHE A 132 -48.754 12.147 -21.001 1.00 63.01 C ANISOU 773 CE1 PHE A 132 8012 6386 9542 384 878 179 C ATOM 774 CE2 PHE A 132 -46.958 10.665 -21.574 1.00 64.38 C ANISOU 774 CE2 PHE A 132 8287 6509 9664 630 949 195 C ATOM 775 CZ PHE A 132 -47.870 11.143 -20.649 1.00 63.97 C ANISOU 775 CZ PHE A 132 8230 6446 9628 519 904 197 C ATOM 776 N PRO A 133 -44.982 14.245 -23.554 1.00 62.30 N ANISOU 776 N PRO A 133 7451 6649 9571 564 911 282 N ATOM 777 CA PRO A 133 -43.516 14.335 -23.583 1.00 63.94 C ANISOU 777 CA PRO A 133 7517 6965 9811 667 931 314 C ATOM 778 C PRO A 133 -42.738 13.019 -23.572 1.00 64.21 C ANISOU 778 C PRO A 133 7608 6983 9804 852 991 295 C ATOM 779 O PRO A 133 -41.619 12.988 -24.072 1.00 65.44 O ANISOU 779 O PRO A 133 7642 7251 9969 944 1043 306 O ATOM 780 CB PRO A 133 -43.180 15.155 -22.325 1.00 64.24 C ANISOU 780 CB PRO A 133 7445 7042 9921 647 824 346 C ATOM 781 CG PRO A 133 -44.486 15.477 -21.659 1.00 63.39 C ANISOU 781 CG PRO A 133 7435 6842 9807 548 762 328 C ATOM 782 CD PRO A 133 -45.507 14.533 -22.210 1.00 62.64 C ANISOU 782 CD PRO A 133 7507 6649 9644 530 826 284 C ATOM 783 N ARG A 134 -43.305 11.962 -22.999 1.00 64.13 N ANISOU 783 N ARG A 134 7782 6838 9743 907 986 266 N ATOM 784 CA ARG A 134 -42.605 10.677 -22.881 1.00 65.98 C ANISOU 784 CA ARG A 134 8116 7024 9927 1103 1025 247 C ATOM 785 C ARG A 134 -43.428 9.507 -23.446 1.00 65.87 C ANISOU 785 C ARG A 134 8354 6853 9819 1104 1086 199 C ATOM 786 O ARG A 134 -44.348 9.012 -22.790 1.00 65.47 O ANISOU 786 O ARG A 134 8470 6668 9736 1039 1057 189 O ATOM 787 CB ARG A 134 -42.240 10.429 -21.416 1.00 66.42 C ANISOU 787 CB ARG A 134 8186 7048 10000 1196 938 268 C ATOM 788 CG ARG A 134 -41.252 11.433 -20.835 1.00 66.43 C ANISOU 788 CG ARG A 134 7945 7205 10088 1216 863 306 C ATOM 789 CD ARG A 134 -39.850 11.181 -21.353 1.00 67.79 C ANISOU 789 CD ARG A 134 7964 7516 10277 1385 905 303 C ATOM 790 NE ARG A 134 -38.883 12.163 -20.866 1.00 68.00 N ANISOU 790 NE ARG A 134 7734 7709 10393 1375 832 336 N ATOM 791 CZ ARG A 134 -38.566 13.306 -21.469 1.00 67.54 C ANISOU 791 CZ ARG A 134 7480 7787 10395 1238 849 361 C ATOM 792 NH1 ARG A 134 -37.657 14.089 -20.913 1.00 68.53 N ANISOU 792 NH1 ARG A 134 7388 8050 10597 1223 771 388 N ATOM 793 NH2 ARG A 134 -39.138 13.687 -22.611 1.00 67.10 N ANISOU 793 NH2 ARG A 134 7453 7724 10317 1108 935 362 N ATOM 794 N CYS A 135 -43.091 9.102 -24.672 1.00 66.08 N ANISOU 794 N CYS A 135 8407 6901 9797 1167 1173 169 N ATOM 795 CA CYS A 135 -43.709 7.980 -25.370 1.00 67.31 C ANISOU 795 CA CYS A 135 8808 6911 9855 1180 1229 115 C ATOM 796 C CYS A 135 -42.643 7.014 -25.891 1.00 69.43 C ANISOU 796 C CYS A 135 9137 7179 10062 1416 1299 84 C ATOM 797 O CYS A 135 -41.793 7.414 -26.689 1.00 69.06 O ANISOU 797 O CYS A 135 8931 7282 10024 1488 1363 85 O ATOM 798 CB CYS A 135 -44.494 8.511 -26.562 1.00 66.80 C ANISOU 798 CB CYS A 135 8740 6869 9768 1019 1262 94 C ATOM 799 SG CYS A 135 -45.794 9.668 -26.125 1.00 65.56 S ANISOU 799 SG CYS A 135 8508 6724 9676 774 1178 114 S ATOM 800 N ARG A 136 -42.682 5.755 -25.453 1.00 71.31 N ANISOU 800 N ARG A 136 9610 7251 10231 1539 1292 56 N ATOM 801 CA ARG A 136 -41.762 4.727 -25.995 1.00 74.86 C ANISOU 801 CA ARG A 136 10163 7674 10604 1792 1355 12 C ATOM 802 C ARG A 136 -42.125 4.349 -27.435 1.00 73.47 C ANISOU 802 C ARG A 136 10116 7457 10341 1762 1444 -46 C ATOM 803 O ARG A 136 -41.240 4.122 -28.255 1.00 73.40 O ANISOU 803 O ARG A 136 10061 7537 10291 1935 1525 -78 O ATOM 804 CB ARG A 136 -41.730 3.475 -25.106 1.00 76.55 C ANISOU 804 CB ARG A 136 10641 7689 10755 1939 1309 0 C ATOM 805 CG ARG A 136 -40.799 2.361 -25.577 1.00 80.77 C ANISOU 805 CG ARG A 136 11312 8173 11202 2236 1358 -52 C ATOM 806 CD ARG A 136 -39.316 2.706 -25.475 1.00 83.91 C ANISOU 806 CD ARG A 136 11433 8792 11656 2476 1368 -43 C ATOM 807 NE ARG A 136 -38.503 1.770 -26.264 1.00 87.42 N ANISOU 807 NE ARG A 136 11974 9230 12012 2755 1445 -111 N ATOM 808 CZ ARG A 136 -38.257 1.863 -27.575 1.00 88.19 C ANISOU 808 CZ ARG A 136 12012 9426 12067 2782 1562 -157 C ATOM 809 NH1 ARG A 136 -37.512 0.927 -28.165 1.00 90.87 N ANISOU 809 NH1 ARG A 136 12462 9748 12313 3068 1629 -227 N ATOM 810 NH2 ARG A 136 -38.737 2.873 -28.311 1.00 86.82 N ANISOU 810 NH2 ARG A 136 11687 9368 11932 2542 1612 -136 N ATOM 811 N TYR A 137 -43.426 4.274 -27.716 1.00 71.99 N ANISOU 811 N TYR A 137 10087 7144 10121 1547 1425 -66 N ATOM 812 CA TYR A 137 -43.944 4.018 -29.059 1.00 71.43 C ANISOU 812 CA TYR A 137 10144 7030 9965 1480 1482 -124 C ATOM 813 C TYR A 137 -45.023 5.037 -29.395 1.00 68.85 C ANISOU 813 C TYR A 137 9718 6758 9681 1213 1446 -108 C ATOM 814 O TYR A 137 -45.962 5.219 -28.623 1.00 69.27 O ANISOU 814 O TYR A 137 9791 6748 9778 1049 1375 -91 O ATOM 815 CB TYR A 137 -44.534 2.613 -29.144 1.00 72.27 C ANISOU 815 CB TYR A 137 10608 6888 9962 1499 1476 -186 C ATOM 816 CG TYR A 137 -43.551 1.542 -28.768 1.00 74.66 C ANISOU 816 CG TYR A 137 11057 7102 10209 1782 1495 -205 C ATOM 817 CD1 TYR A 137 -42.429 1.310 -29.549 1.00 75.99 C ANISOU 817 CD1 TYR A 137 11177 7366 10329 2029 1578 -242 C ATOM 818 CD2 TYR A 137 -43.730 0.766 -27.622 1.00 75.82 C ANISOU 818 CD2 TYR A 137 11394 7073 10341 1816 1432 -188 C ATOM 819 CE1 TYR A 137 -41.512 0.330 -29.209 1.00 78.59 C ANISOU 819 CE1 TYR A 137 11633 7622 10604 2323 1586 -269 C ATOM 820 CE2 TYR A 137 -42.814 -0.220 -27.275 1.00 78.02 C ANISOU 820 CE2 TYR A 137 11828 7257 10558 2102 1432 -206 C ATOM 821 CZ TYR A 137 -41.708 -0.431 -28.074 1.00 78.98 C ANISOU 821 CZ TYR A 137 11886 7481 10640 2366 1505 -251 C ATOM 822 OH TYR A 137 -40.797 -1.398 -27.747 1.00 81.30 O ANISOU 822 OH TYR A 137 12325 7693 10871 2680 1498 -278 O ATOM 823 N VAL A 138 -44.885 5.705 -30.534 1.00 67.21 N ANISOU 823 N VAL A 138 9409 6671 9454 1180 1496 -114 N ATOM 824 CA VAL A 138 -45.910 6.617 -31.020 1.00 66.05 C ANISOU 824 CA VAL A 138 9203 6565 9328 956 1451 -108 C ATOM 825 C VAL A 138 -46.587 5.907 -32.170 1.00 68.44 C ANISOU 825 C VAL A 138 9731 6759 9511 911 1471 -184 C ATOM 826 O VAL A 138 -45.960 5.660 -33.203 1.00 70.82 O ANISOU 826 O VAL A 138 10084 7096 9726 1027 1553 -214 O ATOM 827 CB VAL A 138 -45.322 7.974 -31.481 1.00 64.22 C ANISOU 827 CB VAL A 138 8720 6532 9147 931 1477 -51 C ATOM 828 CG1 VAL A 138 -46.401 8.854 -32.098 1.00 62.28 C ANISOU 828 CG1 VAL A 138 8458 6306 8900 730 1420 -51 C ATOM 829 CG2 VAL A 138 -44.657 8.686 -30.309 1.00 62.84 C ANISOU 829 CG2 VAL A 138 8327 6456 9090 959 1441 16 C ATOM 830 N HIS A 139 -47.856 5.562 -31.981 1.00 69.66 N ANISOU 830 N HIS A 139 10020 6790 9655 740 1398 -219 N ATOM 831 CA HIS A 139 -48.639 4.905 -33.022 1.00 72.33 C ANISOU 831 CA HIS A 139 10574 7021 9884 661 1389 -298 C ATOM 832 C HIS A 139 -49.247 5.970 -33.923 1.00 73.42 C ANISOU 832 C HIS A 139 10601 7274 10021 525 1351 -297 C ATOM 833 O HIS A 139 -50.268 6.577 -33.587 1.00 71.18 O ANISOU 833 O HIS A 139 10230 7014 9799 352 1264 -290 O ATOM 834 CB HIS A 139 -49.712 4.016 -32.406 1.00 72.44 C ANISOU 834 CB HIS A 139 10774 6859 9887 519 1327 -339 C ATOM 835 CG HIS A 139 -49.156 2.934 -31.539 1.00 73.46 C ANISOU 835 CG HIS A 139 11066 6847 9999 651 1355 -335 C ATOM 836 ND1 HIS A 139 -48.853 3.131 -30.212 1.00 74.04 N ANISOU 836 ND1 HIS A 139 11033 6939 10157 684 1340 -270 N ATOM 837 CD2 HIS A 139 -48.822 1.654 -31.813 1.00 74.32 C ANISOU 837 CD2 HIS A 139 11453 6783 10001 773 1389 -389 C ATOM 838 CE1 HIS A 139 -48.375 2.011 -29.703 1.00 74.03 C ANISOU 838 CE1 HIS A 139 11242 6783 10103 820 1360 -280 C ATOM 839 NE2 HIS A 139 -48.341 1.101 -30.655 1.00 74.55 N ANISOU 839 NE2 HIS A 139 11545 6725 10053 880 1390 -352 N ATOM 840 N LYS A 140 -48.589 6.208 -35.057 1.00 76.30 N ANISOU 840 N LYS A 140 10968 7714 10308 619 1420 -303 N ATOM 841 CA LYS A 140 -48.997 7.254 -35.971 1.00 78.37 C ANISOU 841 CA LYS A 140 11147 8081 10548 517 1389 -290 C ATOM 842 C LYS A 140 -49.935 6.671 -37.025 1.00 78.62 C ANISOU 842 C LYS A 140 11397 8015 10459 430 1340 -378 C ATOM 843 O LYS A 140 -49.495 6.002 -37.964 1.00 80.72 O ANISOU 843 O LYS A 140 11836 8236 10598 533 1409 -428 O ATOM 844 CB LYS A 140 -47.780 7.936 -36.605 1.00 82.74 C ANISOU 844 CB LYS A 140 11579 8782 11074 638 1495 -236 C ATOM 845 CG LYS A 140 -48.129 9.273 -37.235 1.00 86.95 C ANISOU 845 CG LYS A 140 12001 9426 11610 519 1452 -190 C ATOM 846 CD LYS A 140 -46.948 9.945 -37.910 1.00 91.52 C ANISOU 846 CD LYS A 140 12476 10148 12148 602 1571 -130 C ATOM 847 CE LYS A 140 -47.426 11.179 -38.664 1.00 94.29 C ANISOU 847 CE LYS A 140 12792 10565 12467 472 1517 -87 C ATOM 848 NZ LYS A 140 -46.311 11.972 -39.258 1.00 97.05 N ANISOU 848 NZ LYS A 140 13036 11058 12780 508 1636 -12 N ATOM 849 N VAL A 141 -51.232 6.928 -36.858 1.00 76.72 N ANISOU 849 N VAL A 141 11143 7749 10256 244 1218 -403 N ATOM 850 CA VAL A 141 -52.258 6.414 -37.759 1.00 76.98 C ANISOU 850 CA VAL A 141 11357 7700 10189 131 1141 -493 C ATOM 851 C VAL A 141 -52.667 7.477 -38.784 1.00 78.04 C ANISOU 851 C VAL A 141 11431 7943 10278 74 1078 -486 C ATOM 852 O VAL A 141 -53.212 8.527 -38.430 1.00 77.22 O ANISOU 852 O VAL A 141 11147 7930 10261 -12 997 -445 O ATOM 853 CB VAL A 141 -53.500 5.944 -36.979 1.00 76.38 C ANISOU 853 CB VAL A 141 11300 7543 10176 -48 1041 -538 C ATOM 854 CG1 VAL A 141 -54.487 5.247 -37.914 1.00 78.27 C ANISOU 854 CG1 VAL A 141 11738 7691 10309 -173 958 -642 C ATOM 855 CG2 VAL A 141 -53.090 5.020 -35.837 1.00 76.16 C ANISOU 855 CG2 VAL A 141 11340 7403 10193 0 1100 -524 C ATOM 856 N SER A 142 -52.378 7.200 -40.054 1.00 80.09 N ANISOU 856 N SER A 142 11858 8184 10387 137 1116 -526 N ATOM 857 CA SER A 142 -52.900 7.982 -41.173 1.00 79.80 C ANISOU 857 CA SER A 142 11841 8213 10265 77 1039 -535 C ATOM 858 C SER A 142 -54.015 7.184 -41.829 1.00 79.95 C ANISOU 858 C SER A 142 12057 8129 10191 -33 924 -650 C ATOM 859 O SER A 142 -53.969 5.962 -41.841 1.00 81.88 O ANISOU 859 O SER A 142 12489 8240 10378 -17 956 -719 O ATOM 860 CB SER A 142 -51.791 8.280 -42.174 1.00 81.32 C ANISOU 860 CB SER A 142 12092 8470 10335 215 1167 -498 C ATOM 861 OG SER A 142 -50.825 9.136 -41.590 1.00 81.82 O ANISOU 861 OG SER A 142 11945 8648 10492 281 1258 -391 O ATOM 862 N GLY A 143 -55.027 7.861 -42.355 1.00 79.51 N ANISOU 862 N GLY A 143 11965 8126 10118 -147 779 -673 N ATOM 863 CA GLY A 143 -56.140 7.156 -42.979 1.00 81.09 C ANISOU 863 CA GLY A 143 12325 8248 10236 -271 647 -788 C ATOM 864 C GLY A 143 -57.426 7.943 -43.118 1.00 81.29 C ANISOU 864 C GLY A 143 12223 8360 10303 -407 459 -814 C ATOM 865 O GLY A 143 -57.432 9.173 -43.035 1.00 80.50 O ANISOU 865 O GLY A 143 11955 8373 10256 -380 423 -742 O ATOM 866 N THR A 144 -58.519 7.209 -43.326 1.00 81.76 N ANISOU 866 N THR A 144 12366 8362 10336 -553 333 -923 N ATOM 867 CA THR A 144 -59.820 7.799 -43.606 1.00 81.31 C ANISOU 867 CA THR A 144 12196 8397 10300 -676 136 -975 C ATOM 868 C THR A 144 -60.950 7.164 -42.801 1.00 80.85 C ANISOU 868 C THR A 144 12040 8329 10347 -870 50 -1051 C ATOM 869 O THR A 144 -60.834 6.037 -42.314 1.00 80.53 O ANISOU 869 O THR A 144 12113 8166 10317 -937 122 -1084 O ATOM 870 CB THR A 144 -60.169 7.673 -45.100 1.00 83.54 C ANISOU 870 CB THR A 144 12687 8657 10397 -678 25 -1052 C ATOM 871 OG1 THR A 144 -60.102 6.295 -45.497 1.00 85.15 O ANISOU 871 OG1 THR A 144 13146 8708 10496 -722 55 -1143 O ATOM 872 CG2 THR A 144 -59.214 8.488 -45.941 1.00 83.22 C ANISOU 872 CG2 THR A 144 12723 8653 10241 -510 101 -970 C ATOM 873 N GLY A 145 -62.045 7.912 -42.687 1.00 79.98 N ANISOU 873 N GLY A 145 11724 8352 10309 -957 -105 -1079 N ATOM 874 CA GLY A 145 -63.273 7.458 -42.023 1.00 79.67 C ANISOU 874 CA GLY A 145 11547 8355 10368 -1159 -199 -1160 C ATOM 875 C GLY A 145 -64.385 8.482 -42.209 1.00 79.41 C ANISOU 875 C GLY A 145 11285 8501 10384 -1191 -385 -1197 C ATOM 876 O GLY A 145 -64.124 9.601 -42.672 1.00 78.96 O ANISOU 876 O GLY A 145 11185 8516 10298 -1045 -431 -1141 O ATOM 877 N PRO A 146 -65.630 8.121 -41.846 1.00 79.36 N ANISOU 877 N PRO A 146 11131 8573 10449 -1381 -495 -1291 N ATOM 878 CA PRO A 146 -66.745 9.043 -42.062 1.00 81.27 C ANISOU 878 CA PRO A 146 11140 9003 10733 -1393 -687 -1344 C ATOM 879 C PRO A 146 -66.691 10.310 -41.186 1.00 81.12 C ANISOU 879 C PRO A 146 10868 9113 10839 -1266 -663 -1262 C ATOM 880 O PRO A 146 -67.076 11.371 -41.664 1.00 82.06 O ANISOU 880 O PRO A 146 10894 9342 10944 -1158 -803 -1264 O ATOM 881 CB PRO A 146 -67.980 8.191 -41.759 1.00 81.90 C ANISOU 881 CB PRO A 146 11109 9140 10867 -1646 -772 -1466 C ATOM 882 CG PRO A 146 -67.502 7.129 -40.844 1.00 81.32 C ANISOU 882 CG PRO A 146 11132 8927 10836 -1759 -588 -1435 C ATOM 883 CD PRO A 146 -66.050 6.894 -41.152 1.00 80.42 C ANISOU 883 CD PRO A 146 11292 8632 10630 -1591 -440 -1348 C ATOM 884 N CYS A 147 -66.211 10.194 -39.944 1.00 80.33 N ANISOU 884 N CYS A 147 10687 8988 10847 -1272 -499 -1193 N ATOM 885 CA CYS A 147 -66.044 11.342 -39.028 1.00 80.46 C ANISOU 885 CA CYS A 147 10493 9101 10973 -1150 -462 -1114 C ATOM 886 C CYS A 147 -67.350 12.112 -38.806 1.00 80.55 C ANISOU 886 C CYS A 147 10226 9313 11063 -1171 -623 -1187 C ATOM 887 O CYS A 147 -67.442 13.308 -39.086 1.00 78.41 O ANISOU 887 O CYS A 147 9878 9122 10790 -1016 -725 -1162 O ATOM 888 CB CYS A 147 -64.936 12.287 -39.519 1.00 80.60 C ANISOU 888 CB CYS A 147 10621 9070 10933 -944 -428 -1007 C ATOM 889 SG CYS A 147 -63.323 11.497 -39.761 1.00 82.41 S ANISOU 889 SG CYS A 147 11129 9107 11076 -883 -226 -923 S ATOM 890 N ALA A 148 -68.355 11.407 -38.292 1.00 82.44 N ANISOU 890 N ALA A 148 10320 9634 11366 -1363 -643 -1278 N ATOM 891 CA ALA A 148 -69.704 11.958 -38.137 1.00 83.68 C ANISOU 891 CA ALA A 148 10187 10011 11595 -1401 -796 -1373 C ATOM 892 C ALA A 148 -69.823 12.793 -36.854 1.00 81.78 C ANISOU 892 C ALA A 148 9705 9885 11479 -1318 -725 -1330 C ATOM 893 O ALA A 148 -70.542 12.424 -35.922 1.00 83.18 O ANISOU 893 O ALA A 148 9687 10171 11745 -1458 -671 -1378 O ATOM 894 CB ALA A 148 -70.731 10.829 -38.159 1.00 86.14 C ANISOU 894 CB ALA A 148 10430 10379 11918 -1668 -839 -1493 C ATOM 895 N GLY A 149 -69.125 13.927 -36.827 1.00 78.85 N ANISOU 895 N GLY A 149 9362 9490 11106 -1097 -725 -1241 N ATOM 896 CA GLY A 149 -69.084 14.792 -35.659 1.00 76.53 C ANISOU 896 CA GLY A 149 8890 9273 10913 -993 -663 -1195 C ATOM 897 C GLY A 149 -67.925 15.768 -35.712 1.00 75.62 C ANISOU 897 C GLY A 149 8908 9050 10773 -791 -627 -1073 C ATOM 898 O GLY A 149 -66.893 15.492 -36.327 1.00 74.61 O ANISOU 898 O GLY A 149 9012 8769 10566 -767 -566 -1001 O ATOM 899 N ASP A 150 -68.091 16.901 -35.028 1.00 75.31 N ANISOU 899 N ASP A 150 8719 9094 10799 -652 -659 -1053 N ATOM 900 CA ASP A 150 -67.115 17.998 -35.064 1.00 72.33 C ANISOU 900 CA ASP A 150 8454 8626 10402 -472 -653 -944 C ATOM 901 C ASP A 150 -65.814 17.700 -34.333 1.00 69.37 C ANISOU 901 C ASP A 150 8190 8116 10050 -485 -459 -833 C ATOM 902 O ASP A 150 -64.750 18.127 -34.774 1.00 70.42 O ANISOU 902 O ASP A 150 8486 8137 10131 -403 -428 -738 O ATOM 903 CB ASP A 150 -67.724 19.269 -34.480 1.00 72.25 C ANISOU 903 CB ASP A 150 8267 8731 10453 -321 -753 -966 C ATOM 904 CG ASP A 150 -68.887 19.784 -35.289 1.00 74.71 C ANISOU 904 CG ASP A 150 8479 9173 10732 -248 -972 -1068 C ATOM 905 OD1 ASP A 150 -69.067 19.355 -36.450 1.00 77.10 O ANISOU 905 OD1 ASP A 150 8890 9456 10948 -295 -1065 -1101 O ATOM 906 OD2 ASP A 150 -69.628 20.628 -34.757 1.00 75.94 O ANISOU 906 OD2 ASP A 150 8452 9456 10943 -129 -1058 -1120 O ATOM 907 N PHE A 151 -65.903 16.996 -33.209 1.00 67.50 N ANISOU 907 N PHE A 151 7862 7899 9886 -587 -332 -843 N ATOM 908 CA PHE A 151 -64.727 16.624 -32.426 1.00 64.05 C ANISOU 908 CA PHE A 151 7522 7343 9470 -593 -161 -748 C ATOM 909 C PHE A 151 -64.767 15.165 -32.006 1.00 63.41 C ANISOU 909 C PHE A 151 7485 7215 9393 -763 -39 -772 C ATOM 910 O PHE A 151 -65.851 14.583 -31.881 1.00 63.78 O ANISOU 910 O PHE A 151 7424 7351 9458 -898 -66 -863 O ATOM 911 CB PHE A 151 -64.632 17.495 -31.186 1.00 62.09 C ANISOU 911 CB PHE A 151 7146 7142 9302 -504 -129 -712 C ATOM 912 CG PHE A 151 -64.504 18.951 -31.486 1.00 61.72 C ANISOU 912 CG PHE A 151 7092 7108 9249 -337 -245 -681 C ATOM 913 CD1 PHE A 151 -63.265 19.505 -31.775 1.00 60.12 C ANISOU 913 CD1 PHE A 151 7040 6786 9015 -257 -217 -574 C ATOM 914 CD2 PHE A 151 -65.627 19.777 -31.486 1.00 62.55 C ANISOU 914 CD2 PHE A 151 7042 7345 9376 -259 -386 -760 C ATOM 915 CE1 PHE A 151 -63.150 20.855 -32.052 1.00 60.06 C ANISOU 915 CE1 PHE A 151 7055 6769 8992 -124 -326 -539 C ATOM 916 CE2 PHE A 151 -65.515 21.129 -31.758 1.00 61.40 C ANISOU 916 CE2 PHE A 151 6928 7185 9215 -94 -505 -730 C ATOM 917 CZ PHE A 151 -64.274 21.667 -32.043 1.00 60.51 C ANISOU 917 CZ PHE A 151 6994 6931 9066 -38 -475 -615 C ATOM 918 N ALA A 152 -63.577 14.605 -31.774 1.00 61.65 N ANISOU 918 N ALA A 152 7420 6852 9149 -754 90 -690 N ATOM 919 CA ALA A 152 -63.412 13.212 -31.356 1.00 62.74 C ANISOU 919 CA ALA A 152 7660 6901 9276 -887 209 -696 C ATOM 920 C ALA A 152 -63.178 13.172 -29.859 1.00 62.26 C ANISOU 920 C ALA A 152 7529 6841 9282 -891 318 -651 C ATOM 921 O ALA A 152 -62.206 13.749 -29.390 1.00 61.93 O ANISOU 921 O ALA A 152 7508 6759 9263 -766 362 -568 O ATOM 922 CB ALA A 152 -62.232 12.579 -32.077 1.00 62.59 C ANISOU 922 CB ALA A 152 7872 6728 9179 -842 276 -642 C ATOM 923 N PHE A 153 -64.062 12.494 -29.121 1.00 63.07 N ANISOU 923 N PHE A 153 7556 6994 9412 -1044 361 -705 N ATOM 924 CA PHE A 153 -63.981 12.390 -27.653 1.00 62.21 C ANISOU 924 CA PHE A 153 7393 6893 9349 -1065 469 -668 C ATOM 925 C PHE A 153 -63.615 10.975 -27.229 1.00 63.15 C ANISOU 925 C PHE A 153 7698 6867 9428 -1189 588 -644 C ATOM 926 O PHE A 153 -63.527 10.072 -28.060 1.00 65.19 O ANISOU 926 O PHE A 153 8116 7024 9628 -1264 583 -667 O ATOM 927 CB PHE A 153 -65.327 12.739 -27.027 1.00 63.57 C ANISOU 927 CB PHE A 153 7333 7249 9572 -1150 444 -746 C ATOM 928 CG PHE A 153 -65.764 14.150 -27.270 1.00 63.54 C ANISOU 928 CG PHE A 153 7149 7385 9606 -1004 322 -778 C ATOM 929 CD1 PHE A 153 -66.420 14.493 -28.445 1.00 64.32 C ANISOU 929 CD1 PHE A 153 7189 7560 9688 -992 180 -847 C ATOM 930 CD2 PHE A 153 -65.535 15.136 -26.322 1.00 62.36 C ANISOU 930 CD2 PHE A 153 6909 7283 9499 -870 337 -742 C ATOM 931 CE1 PHE A 153 -66.835 15.794 -28.674 1.00 64.44 C ANISOU 931 CE1 PHE A 153 7065 7689 9728 -839 54 -876 C ATOM 932 CE2 PHE A 153 -65.952 16.437 -26.545 1.00 63.24 C ANISOU 932 CE2 PHE A 153 6886 7504 9638 -724 216 -775 C ATOM 933 CZ PHE A 153 -66.599 16.769 -27.723 1.00 63.49 C ANISOU 933 CZ PHE A 153 6867 7603 9652 -703 73 -840 C ATOM 934 N HIS A 154 -63.397 10.796 -25.931 1.00 62.31 N ANISOU 934 N HIS A 154 7592 6740 9342 -1199 689 -597 N ATOM 935 CA HIS A 154 -63.172 9.485 -25.343 1.00 63.33 C ANISOU 935 CA HIS A 154 7907 6730 9426 -1319 799 -570 C ATOM 936 C HIS A 154 -64.519 8.930 -24.890 1.00 66.10 C ANISOU 936 C HIS A 154 8165 7169 9780 -1555 832 -641 C ATOM 937 O HIS A 154 -65.196 9.544 -24.066 1.00 66.04 O ANISOU 937 O HIS A 154 7961 7313 9816 -1574 852 -660 O ATOM 938 CB HIS A 154 -62.212 9.594 -24.157 1.00 62.28 C ANISOU 938 CB HIS A 154 7837 6527 9299 -1203 881 -479 C ATOM 939 CG HIS A 154 -61.431 8.344 -23.897 1.00 62.76 C ANISOU 939 CG HIS A 154 8160 6389 9296 -1222 964 -428 C ATOM 940 ND1 HIS A 154 -61.935 7.292 -23.167 1.00 64.54 N ANISOU 940 ND1 HIS A 154 8502 6540 9477 -1398 1047 -431 N ATOM 941 CD2 HIS A 154 -60.182 7.981 -24.267 1.00 62.00 C ANISOU 941 CD2 HIS A 154 8238 6152 9164 -1079 975 -374 C ATOM 942 CE1 HIS A 154 -61.032 6.334 -23.097 1.00 65.23 C ANISOU 942 CE1 HIS A 154 8848 6432 9504 -1350 1094 -380 C ATOM 943 NE2 HIS A 154 -59.958 6.727 -23.757 1.00 64.26 N ANISOU 943 NE2 HIS A 154 8750 6275 9387 -1147 1051 -350 N ATOM 944 N LYS A 155 -64.902 7.768 -25.415 1.00 69.21 N ANISOU 944 N LYS A 155 8702 7470 10122 -1739 843 -682 N ATOM 945 CA LYS A 155 -66.208 7.162 -25.112 1.00 71.90 C ANISOU 945 CA LYS A 155 8954 7899 10465 -2008 873 -753 C ATOM 946 C LYS A 155 -66.363 6.755 -23.644 1.00 72.50 C ANISOU 946 C LYS A 155 9050 7964 10529 -2112 1014 -706 C ATOM 947 O LYS A 155 -67.476 6.660 -23.129 1.00 73.42 O ANISOU 947 O LYS A 155 9005 8226 10664 -2304 1059 -758 O ATOM 948 CB LYS A 155 -66.448 5.939 -25.994 1.00 74.26 C ANISOU 948 CB LYS A 155 9453 8061 10699 -2193 849 -801 C ATOM 949 CG LYS A 155 -66.568 6.244 -27.475 1.00 75.60 C ANISOU 949 CG LYS A 155 9598 8263 10860 -2138 705 -868 C ATOM 950 CD LYS A 155 -66.922 4.981 -28.235 1.00 78.39 C ANISOU 950 CD LYS A 155 10158 8483 11144 -2350 681 -928 C ATOM 951 CE LYS A 155 -67.036 5.236 -29.726 1.00 79.81 C ANISOU 951 CE LYS A 155 10340 8686 11295 -2294 533 -998 C ATOM 952 NZ LYS A 155 -67.702 4.087 -30.407 1.00 83.27 N ANISOU 952 NZ LYS A 155 10928 9038 11672 -2546 485 -1083 N ATOM 953 N GLU A 156 -65.240 6.480 -22.996 1.00 72.39 N ANISOU 953 N GLU A 156 9241 7782 10480 -1988 1084 -610 N ATOM 954 CA GLU A 156 -65.206 6.169 -21.565 1.00 74.23 C ANISOU 954 CA GLU A 156 9533 7986 10686 -2045 1210 -549 C ATOM 955 C GLU A 156 -64.995 7.379 -20.628 1.00 72.67 C ANISOU 955 C GLU A 156 9151 7925 10535 -1866 1224 -516 C ATOM 956 O GLU A 156 -64.839 7.211 -19.416 1.00 73.28 O ANISOU 956 O GLU A 156 9292 7972 10577 -1878 1321 -460 O ATOM 957 CB GLU A 156 -64.165 5.068 -21.327 1.00 75.45 C ANISOU 957 CB GLU A 156 10040 7868 10758 -2015 1266 -469 C ATOM 958 CG GLU A 156 -64.522 3.781 -22.071 1.00 78.24 C ANISOU 958 CG GLU A 156 10608 8069 11049 -2223 1265 -509 C ATOM 959 CD GLU A 156 -63.405 2.759 -22.123 1.00 79.74 C ANISOU 959 CD GLU A 156 11163 7978 11155 -2134 1289 -446 C ATOM 960 OE1 GLU A 156 -63.617 1.700 -22.763 1.00 81.86 O ANISOU 960 OE1 GLU A 156 11647 8093 11362 -2283 1279 -481 O ATOM 961 OE2 GLU A 156 -62.324 3.006 -21.538 1.00 79.55 O ANISOU 961 OE2 GLU A 156 11212 7887 11124 -1910 1308 -367 O ATOM 962 N GLY A 157 -65.018 8.594 -21.180 1.00 71.52 N ANISOU 962 N GLY A 157 8797 7918 10456 -1706 1121 -551 N ATOM 963 CA GLY A 157 -64.935 9.826 -20.388 1.00 68.92 C ANISOU 963 CA GLY A 157 8294 7721 10171 -1543 1114 -536 C ATOM 964 C GLY A 157 -63.543 10.237 -19.945 1.00 65.83 C ANISOU 964 C GLY A 157 8025 7210 9774 -1324 1107 -443 C ATOM 965 O GLY A 157 -63.400 11.221 -19.228 1.00 65.94 O ANISOU 965 O GLY A 157 7928 7308 9816 -1196 1096 -429 O ATOM 966 N ALA A 158 -62.517 9.509 -20.371 1.00 63.19 N ANISOU 966 N ALA A 158 7914 6690 9405 -1276 1107 -387 N ATOM 967 CA ALA A 158 -61.150 9.828 -19.994 1.00 61.63 C ANISOU 967 CA ALA A 158 7812 6396 9205 -1074 1096 -304 C ATOM 968 C ALA A 158 -60.630 10.987 -20.845 1.00 60.60 C ANISOU 968 C ALA A 158 7561 6330 9134 -907 989 -307 C ATOM 969 O ALA A 158 -61.345 11.494 -21.716 1.00 61.18 O ANISOU 969 O ALA A 158 7502 6504 9237 -938 921 -370 O ATOM 970 CB ALA A 158 -60.262 8.604 -20.140 1.00 61.89 C ANISOU 970 CB ALA A 158 8114 6224 9176 -1065 1137 -252 C ATOM 971 N PHE A 159 -59.393 11.404 -20.578 1.00 58.83 N ANISOU 971 N PHE A 159 7385 6046 8919 -737 971 -237 N ATOM 972 CA PHE A 159 -58.782 12.538 -21.260 1.00 58.04 C ANISOU 972 CA PHE A 159 7189 5995 8869 -595 882 -224 C ATOM 973 C PHE A 159 -57.698 12.117 -22.237 1.00 57.93 C ANISOU 973 C PHE A 159 7293 5881 8836 -518 875 -187 C ATOM 974 O PHE A 159 -57.060 11.065 -22.094 1.00 57.95 O ANISOU 974 O PHE A 159 7461 5763 8793 -506 933 -155 O ATOM 975 CB PHE A 159 -58.172 13.506 -20.241 1.00 57.58 C ANISOU 975 CB PHE A 159 7066 5970 8842 -472 859 -177 C ATOM 976 CG PHE A 159 -59.188 14.182 -19.368 1.00 58.76 C ANISOU 976 CG PHE A 159 7083 6236 9006 -507 857 -222 C ATOM 977 CD1 PHE A 159 -59.859 15.314 -19.813 1.00 59.29 C ANISOU 977 CD1 PHE A 159 6991 6421 9115 -474 775 -275 C ATOM 978 CD2 PHE A 159 -59.486 13.685 -18.117 1.00 59.54 C ANISOU 978 CD2 PHE A 159 7228 6329 9066 -562 939 -214 C ATOM 979 CE1 PHE A 159 -60.807 15.936 -19.025 1.00 59.30 C ANISOU 979 CE1 PHE A 159 6864 6540 9125 -479 776 -328 C ATOM 980 CE2 PHE A 159 -60.431 14.307 -17.322 1.00 61.13 C ANISOU 980 CE2 PHE A 159 7301 6655 9271 -586 954 -262 C ATOM 981 CZ PHE A 159 -61.094 15.434 -17.778 1.00 60.46 C ANISOU 981 CZ PHE A 159 7040 6696 9233 -536 873 -324 C ATOM 982 N PHE A 160 -57.494 12.975 -23.225 1.00 57.39 N ANISOU 982 N PHE A 160 7147 5865 8793 -455 804 -192 N ATOM 983 CA PHE A 160 -56.327 12.918 -24.077 1.00 57.53 C ANISOU 983 CA PHE A 160 7236 5826 8796 -356 803 -149 C ATOM 984 C PHE A 160 -55.263 13.828 -23.449 1.00 56.84 C ANISOU 984 C PHE A 160 7081 5761 8752 -232 782 -81 C ATOM 985 O PHE A 160 -55.431 15.047 -23.359 1.00 54.67 O ANISOU 985 O PHE A 160 6689 5562 8519 -207 714 -78 O ATOM 986 CB PHE A 160 -56.709 13.312 -25.507 1.00 58.01 C ANISOU 986 CB PHE A 160 7271 5928 8842 -376 745 -187 C ATOM 987 CG PHE A 160 -57.827 12.479 -26.052 1.00 59.37 C ANISOU 987 CG PHE A 160 7493 6090 8974 -512 744 -263 C ATOM 988 CD1 PHE A 160 -57.585 11.180 -26.490 1.00 59.65 C ANISOU 988 CD1 PHE A 160 7705 6011 8947 -552 802 -276 C ATOM 989 CD2 PHE A 160 -59.138 12.956 -26.050 1.00 59.73 C ANISOU 989 CD2 PHE A 160 7408 6241 9043 -600 682 -330 C ATOM 990 CE1 PHE A 160 -58.614 10.387 -26.957 1.00 60.75 C ANISOU 990 CE1 PHE A 160 7902 6131 9049 -701 793 -349 C ATOM 991 CE2 PHE A 160 -60.176 12.167 -26.518 1.00 60.28 C ANISOU 991 CE2 PHE A 160 7502 6318 9082 -746 674 -406 C ATOM 992 CZ PHE A 160 -59.914 10.879 -26.966 1.00 61.63 C ANISOU 992 CZ PHE A 160 7861 6364 9191 -811 728 -414 C ATOM 993 N LEU A 161 -54.194 13.200 -22.969 1.00 58.18 N ANISOU 993 N LEU A 161 7334 5860 8909 -154 832 -31 N ATOM 994 CA LEU A 161 -53.124 13.893 -22.282 1.00 58.33 C ANISOU 994 CA LEU A 161 7290 5902 8968 -48 807 28 C ATOM 995 C LEU A 161 -52.097 14.344 -23.294 1.00 57.54 C ANISOU 995 C LEU A 161 7153 5828 8880 23 798 63 C ATOM 996 O LEU A 161 -51.544 13.536 -24.024 1.00 58.44 O ANISOU 996 O LEU A 161 7349 5900 8954 64 853 65 O ATOM 997 CB LEU A 161 -52.456 12.976 -21.259 1.00 59.57 C ANISOU 997 CB LEU A 161 7548 5983 9101 14 852 61 C ATOM 998 CG LEU A 161 -53.328 12.395 -20.149 1.00 60.18 C ANISOU 998 CG LEU A 161 7698 6020 9146 -63 883 43 C ATOM 999 CD1 LEU A 161 -52.438 11.594 -19.213 1.00 61.22 C ANISOU 999 CD1 LEU A 161 7952 6065 9242 30 909 90 C ATOM 1000 CD2 LEU A 161 -54.084 13.481 -19.392 1.00 59.88 C ANISOU 1000 CD2 LEU A 161 7534 6073 9143 -105 838 25 C ATOM 1001 N TYR A 162 -51.862 15.646 -23.326 1.00 57.31 N ANISOU 1001 N TYR A 162 7010 5867 8897 35 734 88 N ATOM 1002 CA TYR A 162 -50.863 16.262 -24.173 1.00 57.74 C ANISOU 1002 CA TYR A 162 7016 5959 8963 76 729 132 C ATOM 1003 C TYR A 162 -49.750 16.752 -23.243 1.00 58.12 C ANISOU 1003 C TYR A 162 6987 6034 9061 141 705 186 C ATOM 1004 O TYR A 162 -49.654 16.269 -22.113 1.00 60.03 O ANISOU 1004 O TYR A 162 7253 6248 9308 178 707 187 O ATOM 1005 CB TYR A 162 -51.533 17.386 -24.965 1.00 57.74 C ANISOU 1005 CB TYR A 162 6973 5998 8966 18 662 120 C ATOM 1006 CG TYR A 162 -52.614 16.876 -25.884 1.00 58.49 C ANISOU 1006 CG TYR A 162 7134 6080 9010 -39 667 60 C ATOM 1007 CD1 TYR A 162 -52.301 16.379 -27.143 1.00 59.45 C ANISOU 1007 CD1 TYR A 162 7328 6186 9073 -35 713 58 C ATOM 1008 CD2 TYR A 162 -53.949 16.878 -25.495 1.00 58.35 C ANISOU 1008 CD2 TYR A 162 7099 6074 8996 -98 624 -1 C ATOM 1009 CE1 TYR A 162 -53.290 15.906 -27.991 1.00 60.24 C ANISOU 1009 CE1 TYR A 162 7497 6271 9120 -93 701 -3 C ATOM 1010 CE2 TYR A 162 -54.941 16.408 -26.338 1.00 58.33 C ANISOU 1010 CE2 TYR A 162 7137 6072 8951 -163 615 -63 C ATOM 1011 CZ TYR A 162 -54.610 15.916 -27.575 1.00 59.29 C ANISOU 1011 CZ TYR A 162 7346 6166 9014 -163 645 -64 C ATOM 1012 OH TYR A 162 -55.600 15.452 -28.405 1.00 59.79 O ANISOU 1012 OH TYR A 162 7458 6229 9030 -232 619 -131 O ATOM 1013 N ASP A 163 -48.898 17.673 -23.691 1.00 57.41 N ANISOU 1013 N ASP A 163 6814 5997 8999 145 681 233 N ATOM 1014 CA ASP A 163 -47.851 18.206 -22.822 1.00 57.50 C ANISOU 1014 CA ASP A 163 6737 6045 9063 184 642 278 C ATOM 1015 C ASP A 163 -48.424 19.111 -21.733 1.00 57.21 C ANISOU 1015 C ASP A 163 6679 5997 9060 152 545 268 C ATOM 1016 O ASP A 163 -48.643 20.288 -21.956 1.00 56.71 O ANISOU 1016 O ASP A 163 6585 5945 9017 100 477 276 O ATOM 1017 CB ASP A 163 -46.793 18.958 -23.633 1.00 57.63 C ANISOU 1017 CB ASP A 163 6666 6129 9100 164 650 331 C ATOM 1018 CG ASP A 163 -45.781 19.655 -22.757 1.00 57.27 C ANISOU 1018 CG ASP A 163 6512 6131 9116 170 589 373 C ATOM 1019 OD1 ASP A 163 -45.363 20.765 -23.136 1.00 57.66 O ANISOU 1019 OD1 ASP A 163 6501 6216 9191 94 550 412 O ATOM 1020 OD2 ASP A 163 -45.431 19.117 -21.677 1.00 56.32 O ANISOU 1020 OD2 ASP A 163 6380 6005 9011 244 570 367 O ATOM 1021 N ARG A 164 -48.664 18.538 -20.556 1.00 59.54 N ANISOU 1021 N ARG A 164 7012 6261 9348 192 541 249 N ATOM 1022 CA ARG A 164 -49.181 19.270 -19.382 1.00 60.77 C ANISOU 1022 CA ARG A 164 7162 6409 9518 182 463 232 C ATOM 1023 C ARG A 164 -50.550 19.943 -19.598 1.00 59.43 C ANISOU 1023 C ARG A 164 7002 6239 9339 125 430 182 C ATOM 1024 O ARG A 164 -50.919 20.867 -18.867 1.00 59.31 O ANISOU 1024 O ARG A 164 6971 6226 9337 127 355 165 O ATOM 1025 CB ARG A 164 -48.146 20.287 -18.872 1.00 63.30 C ANISOU 1025 CB ARG A 164 7405 6758 9887 192 376 273 C ATOM 1026 CG ARG A 164 -46.899 19.637 -18.290 1.00 65.72 C ANISOU 1026 CG ARG A 164 7679 7084 10204 267 383 308 C ATOM 1027 CD ARG A 164 -45.783 20.655 -18.141 1.00 68.24 C ANISOU 1027 CD ARG A 164 7892 7456 10580 245 301 348 C ATOM 1028 NE ARG A 164 -45.302 21.077 -19.456 1.00 69.43 N ANISOU 1028 NE ARG A 164 7974 7652 10751 184 338 380 N ATOM 1029 CZ ARG A 164 -44.746 22.257 -19.741 1.00 70.01 C ANISOU 1029 CZ ARG A 164 7979 7757 10864 99 277 415 C ATOM 1030 NH1 ARG A 164 -44.372 22.502 -20.990 1.00 68.52 N ANISOU 1030 NH1 ARG A 164 7751 7608 10674 39 336 449 N ATOM 1031 NH2 ARG A 164 -44.557 23.196 -18.807 1.00 71.72 N ANISOU 1031 NH2 ARG A 164 8182 7957 11110 66 160 418 N ATOM 1032 N LEU A 165 -51.297 19.468 -20.592 1.00 57.95 N ANISOU 1032 N LEU A 165 6842 6049 9124 87 478 152 N ATOM 1033 CA LEU A 165 -52.664 19.906 -20.830 1.00 57.32 C ANISOU 1033 CA LEU A 165 6756 5988 9033 48 446 93 C ATOM 1034 C LEU A 165 -53.445 18.646 -21.167 1.00 56.53 C ANISOU 1034 C LEU A 165 6704 5879 8892 5 527 50 C ATOM 1035 O LEU A 165 -53.010 17.850 -22.002 1.00 55.56 O ANISOU 1035 O LEU A 165 6631 5731 8748 0 583 65 O ATOM 1036 CB LEU A 165 -52.747 20.929 -21.973 1.00 56.30 C ANISOU 1036 CB LEU A 165 6609 5871 8910 29 382 101 C ATOM 1037 CG LEU A 165 -52.120 22.302 -21.692 1.00 56.44 C ANISOU 1037 CG LEU A 165 6604 5879 8961 43 289 141 C ATOM 1038 CD1 LEU A 165 -51.879 23.097 -22.966 1.00 57.07 C ANISOU 1038 CD1 LEU A 165 6704 5949 9030 11 250 175 C ATOM 1039 CD2 LEU A 165 -52.972 23.117 -20.735 1.00 55.95 C ANISOU 1039 CD2 LEU A 165 6533 5818 8905 75 210 91 C ATOM 1040 N ALA A 166 -54.565 18.458 -20.477 1.00 55.70 N ANISOU 1040 N ALA A 166 6591 5797 8775 -27 538 -4 N ATOM 1041 CA ALA A 166 -55.462 17.342 -20.709 1.00 56.77 C ANISOU 1041 CA ALA A 166 6765 5930 8874 -104 608 -51 C ATOM 1042 C ALA A 166 -56.674 17.904 -21.423 1.00 57.74 C ANISOU 1042 C ALA A 166 6814 6124 9001 -146 556 -117 C ATOM 1043 O ALA A 166 -57.298 18.837 -20.914 1.00 57.57 O ANISOU 1043 O ALA A 166 6713 6162 8999 -117 499 -151 O ATOM 1044 CB ALA A 166 -55.867 16.718 -19.388 1.00 56.66 C ANISOU 1044 CB ALA A 166 6785 5908 8836 -131 667 -63 C ATOM 1045 N SER A 167 -56.988 17.367 -22.606 1.00 57.82 N ANISOU 1045 N SER A 167 6853 6128 8988 -198 564 -141 N ATOM 1046 CA SER A 167 -58.168 17.794 -23.361 1.00 56.74 C ANISOU 1046 CA SER A 167 6644 6064 8848 -234 499 -210 C ATOM 1047 C SER A 167 -59.217 16.691 -23.451 1.00 58.25 C ANISOU 1047 C SER A 167 6835 6282 9014 -354 551 -277 C ATOM 1048 O SER A 167 -58.910 15.493 -23.384 1.00 56.99 O ANISOU 1048 O SER A 167 6781 6049 8824 -416 635 -262 O ATOM 1049 CB SER A 167 -57.803 18.238 -24.773 1.00 55.80 C ANISOU 1049 CB SER A 167 6561 5927 8712 -207 439 -192 C ATOM 1050 OG SER A 167 -58.933 18.782 -25.435 1.00 55.34 O ANISOU 1050 OG SER A 167 6438 5941 8647 -216 349 -259 O ATOM 1051 N THR A 168 -60.459 17.133 -23.646 1.00 58.12 N ANISOU 1051 N THR A 168 6701 6372 9007 -383 492 -355 N ATOM 1052 CA THR A 168 -61.579 16.243 -23.838 1.00 58.17 C ANISOU 1052 CA THR A 168 6670 6435 8997 -519 522 -430 C ATOM 1053 C THR A 168 -61.620 15.688 -25.263 1.00 58.81 C ANISOU 1053 C THR A 168 6827 6475 9041 -572 485 -451 C ATOM 1054 O THR A 168 -62.395 14.757 -25.523 1.00 61.79 O ANISOU 1054 O THR A 168 7209 6871 9397 -709 510 -509 O ATOM 1055 CB THR A 168 -62.923 16.943 -23.508 1.00 58.74 C ANISOU 1055 CB THR A 168 6552 6668 9097 -520 467 -518 C ATOM 1056 OG1 THR A 168 -63.117 18.081 -24.355 1.00 58.26 O ANISOU 1056 OG1 THR A 168 6435 6653 9048 -409 331 -541 O ATOM 1057 CG2 THR A 168 -62.956 17.382 -22.051 1.00 58.20 C ANISOU 1057 CG2 THR A 168 6424 6642 9047 -472 519 -510 C ATOM 1058 N VAL A 169 -60.804 16.244 -26.170 1.00 57.63 N ANISOU 1058 N VAL A 169 6745 6273 8877 -478 430 -404 N ATOM 1059 CA VAL A 169 -60.817 15.879 -27.593 1.00 58.79 C ANISOU 1059 CA VAL A 169 6977 6388 8971 -506 388 -424 C ATOM 1060 C VAL A 169 -59.429 15.647 -28.206 1.00 58.06 C ANISOU 1060 C VAL A 169 7035 6184 8840 -444 437 -345 C ATOM 1061 O VAL A 169 -58.418 16.044 -27.637 1.00 57.18 O ANISOU 1061 O VAL A 169 6933 6038 8754 -365 477 -272 O ATOM 1062 CB VAL A 169 -61.559 16.939 -28.444 1.00 60.04 C ANISOU 1062 CB VAL A 169 7053 6634 9125 -454 245 -469 C ATOM 1063 CG1 VAL A 169 -62.945 17.197 -27.869 1.00 60.95 C ANISOU 1063 CG1 VAL A 169 6988 6888 9280 -491 194 -559 C ATOM 1064 CG2 VAL A 169 -60.752 18.241 -28.565 1.00 59.08 C ANISOU 1064 CG2 VAL A 169 6949 6487 9011 -318 191 -397 C ATOM 1065 N ILE A 170 -59.409 15.016 -29.382 1.00 59.80 N ANISOU 1065 N ILE A 170 7365 6362 8994 -480 432 -368 N ATOM 1066 CA ILE A 170 -58.167 14.697 -30.099 1.00 60.77 C ANISOU 1066 CA ILE A 170 7628 6397 9064 -417 492 -309 C ATOM 1067 C ILE A 170 -57.823 15.818 -31.073 1.00 61.13 C ANISOU 1067 C ILE A 170 7674 6470 9079 -342 422 -274 C ATOM 1068 O ILE A 170 -58.673 16.213 -31.880 1.00 62.67 O ANISOU 1068 O ILE A 170 7859 6710 9240 -362 318 -324 O ATOM 1069 CB ILE A 170 -58.267 13.365 -30.883 1.00 61.55 C ANISOU 1069 CB ILE A 170 7880 6418 9085 -485 533 -357 C ATOM 1070 CG1 ILE A 170 -58.538 12.199 -29.929 1.00 62.59 C ANISOU 1070 CG1 ILE A 170 8055 6492 9233 -574 608 -381 C ATOM 1071 CG2 ILE A 170 -56.980 13.101 -31.657 1.00 61.70 C ANISOU 1071 CG2 ILE A 170 8034 6367 9041 -393 604 -304 C ATOM 1072 CD1 ILE A 170 -58.875 10.893 -30.613 1.00 64.41 C ANISOU 1072 CD1 ILE A 170 8452 6633 9388 -671 628 -442 C ATOM 1073 N TYR A 171 -56.587 16.317 -31.012 1.00 60.49 N ANISOU 1073 N TYR A 171 7611 6367 9006 -262 472 -188 N ATOM 1074 CA TYR A 171 -56.101 17.290 -32.007 1.00 61.41 C ANISOU 1074 CA TYR A 171 7762 6493 9075 -214 431 -139 C ATOM 1075 C TYR A 171 -55.319 16.579 -33.110 1.00 61.57 C ANISOU 1075 C TYR A 171 7920 6469 9002 -199 514 -123 C ATOM 1076 O TYR A 171 -54.729 15.518 -32.897 1.00 61.01 O ANISOU 1076 O TYR A 171 7903 6354 8922 -186 617 -125 O ATOM 1077 CB TYR A 171 -55.264 18.405 -31.366 1.00 61.22 C ANISOU 1077 CB TYR A 171 7669 6482 9110 -162 430 -56 C ATOM 1078 CG TYR A 171 -55.951 19.067 -30.190 1.00 61.01 C ANISOU 1078 CG TYR A 171 7526 6489 9165 -158 358 -77 C ATOM 1079 CD1 TYR A 171 -57.062 19.880 -30.376 1.00 61.64 C ANISOU 1079 CD1 TYR A 171 7563 6610 9245 -150 231 -125 C ATOM 1080 CD2 TYR A 171 -55.502 18.862 -28.895 1.00 60.84 C ANISOU 1080 CD2 TYR A 171 7443 6462 9210 -145 414 -55 C ATOM 1081 CE1 TYR A 171 -57.701 20.480 -29.307 1.00 62.24 C ANISOU 1081 CE1 TYR A 171 7533 6728 9387 -126 175 -155 C ATOM 1082 CE2 TYR A 171 -56.133 19.453 -27.817 1.00 62.03 C ANISOU 1082 CE2 TYR A 171 7501 6645 9419 -134 357 -80 C ATOM 1083 CZ TYR A 171 -57.234 20.259 -28.028 1.00 63.34 C ANISOU 1083 CZ TYR A 171 7620 6859 9585 -122 244 -133 C ATOM 1084 OH TYR A 171 -57.857 20.857 -26.956 1.00 67.56 O ANISOU 1084 OH TYR A 171 8063 7436 10171 -91 197 -166 O ATOM 1085 N ARG A 172 -55.338 17.177 -34.296 1.00 62.31 N ANISOU 1085 N ARG A 172 8085 6573 9015 -189 465 -110 N ATOM 1086 CA ARG A 172 -54.737 16.581 -35.476 1.00 63.14 C ANISOU 1086 CA ARG A 172 8334 6648 9008 -172 540 -105 C ATOM 1087 C ARG A 172 -53.231 16.483 -35.318 1.00 60.89 C ANISOU 1087 C ARG A 172 8042 6363 8728 -113 682 -27 C ATOM 1088 O ARG A 172 -52.586 17.429 -34.879 1.00 57.89 O ANISOU 1088 O ARG A 172 7574 6017 8403 -99 688 47 O ATOM 1089 CB ARG A 172 -55.054 17.424 -36.711 1.00 65.54 C ANISOU 1089 CB ARG A 172 8722 6966 9214 -172 453 -94 C ATOM 1090 CG ARG A 172 -54.553 16.847 -38.029 1.00 68.90 C ANISOU 1090 CG ARG A 172 9316 7365 9497 -155 525 -97 C ATOM 1091 CD ARG A 172 -54.421 17.932 -39.073 1.00 72.25 C ANISOU 1091 CD ARG A 172 9825 7803 9823 -146 475 -41 C ATOM 1092 NE ARG A 172 -55.685 18.651 -39.223 1.00 74.54 N ANISOU 1092 NE ARG A 172 10105 8103 10113 -163 287 -82 N ATOM 1093 CZ ARG A 172 -55.818 19.913 -39.624 1.00 75.86 C ANISOU 1093 CZ ARG A 172 10307 8271 10243 -147 190 -28 C ATOM 1094 NH1 ARG A 172 -54.760 20.658 -39.944 1.00 77.08 N ANISOU 1094 NH1 ARG A 172 10516 8414 10354 -145 270 79 N ATOM 1095 NH2 ARG A 172 -57.037 20.440 -39.699 1.00 77.19 N ANISOU 1095 NH2 ARG A 172 10457 8453 10415 -135 8 -83 N ATOM 1096 N GLY A 173 -52.687 15.325 -35.681 1.00 61.64 N ANISOU 1096 N GLY A 173 8231 6423 8765 -76 789 -52 N ATOM 1097 CA GLY A 173 -51.245 15.149 -35.826 1.00 61.93 C ANISOU 1097 CA GLY A 173 8264 6484 8781 2 930 7 C ATOM 1098 C GLY A 173 -50.441 15.541 -34.603 1.00 60.53 C ANISOU 1098 C GLY A 173 7930 6344 8721 32 964 69 C ATOM 1099 O GLY A 173 -49.335 16.050 -34.729 1.00 59.61 O ANISOU 1099 O GLY A 173 7749 6289 8609 64 1038 139 O ATOM 1100 N THR A 174 -51.014 15.292 -33.426 1.00 60.83 N ANISOU 1100 N THR A 174 7908 6353 8849 12 910 42 N ATOM 1101 CA THR A 174 -50.428 15.670 -32.149 1.00 59.94 C ANISOU 1101 CA THR A 174 7661 6267 8843 37 915 90 C ATOM 1102 C THR A 174 -50.463 14.455 -31.235 1.00 59.98 C ANISOU 1102 C THR A 174 7699 6214 8877 76 952 52 C ATOM 1103 O THR A 174 -51.497 13.799 -31.098 1.00 60.15 O ANISOU 1103 O THR A 174 7793 6177 8883 22 916 -11 O ATOM 1104 CB THR A 174 -51.200 16.831 -31.508 1.00 59.61 C ANISOU 1104 CB THR A 174 7531 6245 8872 -25 794 102 C ATOM 1105 OG1 THR A 174 -51.357 17.886 -32.467 1.00 59.29 O ANISOU 1105 OG1 THR A 174 7514 6229 8785 -60 740 130 O ATOM 1106 CG2 THR A 174 -50.452 17.360 -30.289 1.00 59.84 C ANISOU 1106 CG2 THR A 174 7437 6302 8996 0 793 156 C ATOM 1107 N THR A 175 -49.325 14.167 -30.616 1.00 59.75 N ANISOU 1107 N THR A 175 7615 6202 8882 165 1021 91 N ATOM 1108 CA THR A 175 -49.133 12.919 -29.904 1.00 59.12 C ANISOU 1108 CA THR A 175 7607 6051 8802 234 1066 63 C ATOM 1109 C THR A 175 -49.811 12.991 -28.545 1.00 59.00 C ANISOU 1109 C THR A 175 7552 6005 8858 183 999 59 C ATOM 1110 O THR A 175 -49.649 13.978 -27.828 1.00 58.69 O ANISOU 1110 O THR A 175 7385 6023 8890 169 949 101 O ATOM 1111 CB THR A 175 -47.639 12.602 -29.746 1.00 58.74 C ANISOU 1111 CB THR A 175 7507 6048 8761 375 1150 103 C ATOM 1112 OG1 THR A 175 -47.086 12.368 -31.036 1.00 59.46 O ANISOU 1112 OG1 THR A 175 7651 6171 8768 428 1235 94 O ATOM 1113 CG2 THR A 175 -47.421 11.362 -28.897 1.00 59.77 C ANISOU 1113 CG2 THR A 175 7731 6090 8888 470 1176 79 C ATOM 1114 N PHE A 176 -50.554 11.939 -28.192 1.00 58.67 N ANISOU 1114 N PHE A 176 7634 5870 8788 149 1004 9 N ATOM 1115 CA PHE A 176 -51.262 11.907 -26.920 1.00 58.07 C ANISOU 1115 CA PHE A 176 7536 5767 8759 88 963 3 C ATOM 1116 C PHE A 176 -51.215 10.538 -26.273 1.00 58.26 C ANISOU 1116 C PHE A 176 7713 5675 8745 116 1011 -13 C ATOM 1117 O PHE A 176 -51.119 9.526 -26.961 1.00 60.10 O ANISOU 1117 O PHE A 176 8102 5826 8907 141 1057 -47 O ATOM 1118 CB PHE A 176 -52.726 12.360 -27.097 1.00 57.89 C ANISOU 1118 CB PHE A 176 7482 5770 8744 -52 895 -46 C ATOM 1119 CG PHE A 176 -53.577 11.417 -27.901 1.00 58.15 C ANISOU 1119 CG PHE A 176 7649 5739 8707 -137 904 -115 C ATOM 1120 CD1 PHE A 176 -54.147 10.284 -27.314 1.00 59.37 C ANISOU 1120 CD1 PHE A 176 7920 5800 8835 -208 934 -151 C ATOM 1121 CD2 PHE A 176 -53.832 11.668 -29.236 1.00 58.72 C ANISOU 1121 CD2 PHE A 176 7744 5836 8730 -159 877 -145 C ATOM 1122 CE1 PHE A 176 -54.935 9.411 -28.056 1.00 60.04 C ANISOU 1122 CE1 PHE A 176 8136 5818 8855 -311 932 -219 C ATOM 1123 CE2 PHE A 176 -54.619 10.800 -29.980 1.00 60.28 C ANISOU 1123 CE2 PHE A 176 8071 5973 8859 -244 869 -217 C ATOM 1124 CZ PHE A 176 -55.176 9.673 -29.390 1.00 60.15 C ANISOU 1124 CZ PHE A 176 8162 5865 8827 -327 894 -257 C ATOM 1125 N ALA A 177 -51.288 10.533 -24.945 1.00 57.31 N ANISOU 1125 N ALA A 177 7572 5540 8662 114 996 11 N ATOM 1126 CA ALA A 177 -51.579 9.345 -24.163 1.00 58.63 C ANISOU 1126 CA ALA A 177 7904 5585 8785 95 1028 0 C ATOM 1127 C ALA A 177 -52.998 9.471 -23.608 1.00 58.45 C ANISOU 1127 C ALA A 177 7863 5570 8772 -79 1006 -34 C ATOM 1128 O ALA A 177 -53.450 10.570 -23.285 1.00 57.12 O ANISOU 1128 O ALA A 177 7532 5508 8661 -121 958 -31 O ATOM 1129 CB ALA A 177 -50.584 9.205 -23.030 1.00 58.83 C ANISOU 1129 CB ALA A 177 7933 5592 8827 227 1030 54 C ATOM 1130 N GLU A 178 -53.701 8.346 -23.528 1.00 59.15 N ANISOU 1130 N GLU A 178 8120 5550 8802 -181 1042 -69 N ATOM 1131 CA GLU A 178 -54.980 8.302 -22.843 1.00 59.49 C ANISOU 1131 CA GLU A 178 8143 5609 8848 -355 1043 -98 C ATOM 1132 C GLU A 178 -54.688 8.349 -21.370 1.00 60.50 C ANISOU 1132 C GLU A 178 8279 5723 8983 -313 1060 -45 C ATOM 1133 O GLU A 178 -53.731 7.731 -20.911 1.00 61.52 O ANISOU 1133 O GLU A 178 8539 5757 9079 -191 1080 -1 O ATOM 1134 CB GLU A 178 -55.728 7.017 -23.132 1.00 60.56 C ANISOU 1134 CB GLU A 178 8474 5622 8912 -501 1083 -144 C ATOM 1135 CG GLU A 178 -56.304 6.923 -24.516 1.00 61.36 C ANISOU 1135 CG GLU A 178 8578 5740 8996 -584 1053 -212 C ATOM 1136 CD GLU A 178 -56.723 5.511 -24.831 1.00 64.10 C ANISOU 1136 CD GLU A 178 9168 5925 9260 -703 1086 -253 C ATOM 1137 OE1 GLU A 178 -57.946 5.266 -24.977 1.00 65.07 O ANISOU 1137 OE1 GLU A 178 9276 6069 9375 -913 1074 -311 O ATOM 1138 OE2 GLU A 178 -55.825 4.639 -24.902 1.00 65.17 O ANISOU 1138 OE2 GLU A 178 9513 5912 9335 -586 1121 -231 O ATOM 1139 N GLY A 179 -55.516 9.067 -20.620 1.00 60.97 N ANISOU 1139 N GLY A 179 8206 5881 9077 -401 1049 -55 N ATOM 1140 CA GLY A 179 -55.316 9.155 -19.185 1.00 59.97 C ANISOU 1140 CA GLY A 179 8098 5746 8941 -367 1065 -10 C ATOM 1141 C GLY A 179 -56.375 9.932 -18.447 1.00 58.74 C ANISOU 1141 C GLY A 179 7796 5710 8810 -468 1066 -38 C ATOM 1142 O GLY A 179 -57.380 10.367 -19.016 1.00 59.07 O ANISOU 1142 O GLY A 179 7710 5850 8882 -571 1051 -98 O ATOM 1143 N VAL A 180 -56.114 10.105 -17.163 1.00 57.19 N ANISOU 1143 N VAL A 180 7623 5511 8596 -419 1077 2 N ATOM 1144 CA VAL A 180 -57.038 10.731 -16.240 1.00 56.25 C ANISOU 1144 CA VAL A 180 7398 5497 8477 -494 1097 -22 C ATOM 1145 C VAL A 180 -56.230 11.593 -15.266 1.00 55.58 C ANISOU 1145 C VAL A 180 7271 5439 8406 -345 1045 20 C ATOM 1146 O VAL A 180 -55.002 11.462 -15.181 1.00 55.43 O ANISOU 1146 O VAL A 180 7323 5349 8387 -210 1004 73 O ATOM 1147 CB VAL A 180 -57.872 9.659 -15.499 1.00 56.88 C ANISOU 1147 CB VAL A 180 7620 5518 8473 -660 1203 -23 C ATOM 1148 CG1 VAL A 180 -59.059 9.221 -16.348 1.00 56.98 C ANISOU 1148 CG1 VAL A 180 7584 5573 8491 -853 1240 -92 C ATOM 1149 CG2 VAL A 180 -57.012 8.463 -15.134 1.00 56.80 C ANISOU 1149 CG2 VAL A 180 7876 5318 8385 -613 1233 40 C ATOM 1150 N VAL A 181 -56.918 12.469 -14.540 1.00 55.85 N ANISOU 1150 N VAL A 181 7187 5584 8449 -364 1041 -9 N ATOM 1151 CA VAL A 181 -56.259 13.480 -13.714 1.00 55.05 C ANISOU 1151 CA VAL A 181 7033 5517 8363 -231 972 14 C ATOM 1152 C VAL A 181 -56.649 13.344 -12.249 1.00 56.28 C ANISOU 1152 C VAL A 181 7267 5678 8439 -254 1029 23 C ATOM 1153 O VAL A 181 -57.782 12.987 -11.930 1.00 58.16 O ANISOU 1153 O VAL A 181 7500 5964 8632 -386 1123 -13 O ATOM 1154 CB VAL A 181 -56.566 14.893 -14.230 1.00 53.87 C ANISOU 1154 CB VAL A 181 6691 5484 8291 -190 890 -31 C ATOM 1155 CG1 VAL A 181 -55.972 15.951 -13.321 1.00 54.08 C ANISOU 1155 CG1 VAL A 181 6687 5533 8326 -73 812 -15 C ATOM 1156 CG2 VAL A 181 -56.014 15.049 -15.635 1.00 53.31 C ANISOU 1156 CG2 VAL A 181 6575 5398 8281 -160 833 -24 C ATOM 1157 N ALA A 182 -55.677 13.614 -11.379 1.00 56.72 N ANISOU 1157 N ALA A 182 7391 5690 8470 -129 972 71 N ATOM 1158 CA ALA A 182 -55.842 13.612 -9.934 1.00 57.67 C ANISOU 1158 CA ALA A 182 7604 5807 8500 -118 1006 85 C ATOM 1159 C ALA A 182 -55.283 14.911 -9.342 1.00 57.89 C ANISOU 1159 C ALA A 182 7550 5887 8555 13 894 78 C ATOM 1160 O ALA A 182 -54.452 15.584 -9.959 1.00 57.75 O ANISOU 1160 O ALA A 182 7447 5873 8620 97 787 87 O ATOM 1161 CB ALA A 182 -55.117 12.417 -9.336 1.00 58.56 C ANISOU 1161 CB ALA A 182 7950 5775 8524 -90 1032 157 C ATOM 1162 N PHE A 183 -55.742 15.237 -8.135 1.00 59.28 N ANISOU 1162 N PHE A 183 7768 6101 8652 18 924 61 N ATOM 1163 CA PHE A 183 -55.263 16.387 -7.379 1.00 58.64 C ANISOU 1163 CA PHE A 183 7657 6051 8570 137 818 49 C ATOM 1164 C PHE A 183 -54.865 15.941 -5.975 1.00 60.32 C ANISOU 1164 C PHE A 183 8059 6201 8657 184 828 92 C ATOM 1165 O PHE A 183 -55.622 15.224 -5.332 1.00 62.33 O ANISOU 1165 O PHE A 183 8421 6451 8807 100 955 95 O ATOM 1166 CB PHE A 183 -56.355 17.447 -7.318 1.00 57.63 C ANISOU 1166 CB PHE A 183 7389 6048 8457 123 833 -35 C ATOM 1167 CG PHE A 183 -56.855 17.859 -8.664 1.00 57.39 C ANISOU 1167 CG PHE A 183 7192 6080 8533 83 816 -78 C ATOM 1168 CD1 PHE A 183 -58.019 17.301 -9.192 1.00 58.60 C ANISOU 1168 CD1 PHE A 183 7276 6301 8686 -39 928 -120 C ATOM 1169 CD2 PHE A 183 -56.147 18.786 -9.428 1.00 56.50 C ANISOU 1169 CD2 PHE A 183 6997 5955 8514 158 684 -75 C ATOM 1170 CE1 PHE A 183 -58.474 17.676 -10.447 1.00 59.07 C ANISOU 1170 CE1 PHE A 183 7191 6418 8835 -65 893 -162 C ATOM 1171 CE2 PHE A 183 -56.592 19.167 -10.683 1.00 55.76 C ANISOU 1171 CE2 PHE A 183 6777 5907 8500 127 662 -109 C ATOM 1172 CZ PHE A 183 -57.755 18.612 -11.197 1.00 57.80 C ANISOU 1172 CZ PHE A 183 6971 6234 8755 26 760 -154 C ATOM 1173 N LEU A 184 -53.701 16.379 -5.495 1.00 60.98 N ANISOU 1173 N LEU A 184 8184 6239 8744 309 693 123 N ATOM 1174 CA LEU A 184 -53.160 15.930 -4.214 1.00 64.20 C ANISOU 1174 CA LEU A 184 8786 6577 9028 377 670 168 C ATOM 1175 C LEU A 184 -52.757 17.074 -3.319 1.00 65.79 C ANISOU 1175 C LEU A 184 8982 6809 9205 476 547 140 C ATOM 1176 O LEU A 184 -52.313 18.098 -3.807 1.00 66.13 O ANISOU 1176 O LEU A 184 8887 6888 9351 519 431 113 O ATOM 1177 CB LEU A 184 -51.889 15.122 -4.447 1.00 66.23 C ANISOU 1177 CB LEU A 184 9126 6735 9302 456 594 238 C ATOM 1178 CG LEU A 184 -51.878 13.998 -5.471 1.00 65.26 C ANISOU 1178 CG LEU A 184 9028 6551 9214 402 670 269 C ATOM 1179 CD1 LEU A 184 -50.433 13.647 -5.751 1.00 66.19 C ANISOU 1179 CD1 LEU A 184 9161 6611 9374 536 555 317 C ATOM 1180 CD2 LEU A 184 -52.650 12.798 -4.954 1.00 66.44 C ANISOU 1180 CD2 LEU A 184 9385 6624 9235 305 813 296 C ATOM 1181 N ILE A 185 -52.891 16.877 -2.011 1.00 71.18 N ANISOU 1181 N ILE A 185 9837 7467 9741 507 571 149 N ATOM 1182 CA ILE A 185 -52.139 17.641 -1.021 1.00 75.79 C ANISOU 1182 CA ILE A 185 10485 8037 10273 623 422 142 C ATOM 1183 C ILE A 185 -51.031 16.702 -0.571 1.00 78.17 C ANISOU 1183 C ILE A 185 10946 8238 10516 701 347 221 C ATOM 1184 O ILE A 185 -51.305 15.616 -0.077 1.00 79.57 O ANISOU 1184 O ILE A 185 11309 8349 10573 675 448 267 O ATOM 1185 CB ILE A 185 -52.946 18.026 0.246 1.00 79.00 C ANISOU 1185 CB ILE A 185 11010 8480 10526 632 485 98 C ATOM 1186 CG1 ILE A 185 -54.362 18.489 -0.078 1.00 81.18 C ANISOU 1186 CG1 ILE A 185 11159 8867 10816 548 629 22 C ATOM 1187 CG2 ILE A 185 -52.229 19.133 1.012 1.00 79.32 C ANISOU 1187 CG2 ILE A 185 11077 8515 10543 748 304 65 C ATOM 1188 CD1 ILE A 185 -55.185 18.802 1.162 1.00 84.05 C ANISOU 1188 CD1 ILE A 185 11629 9286 11017 564 719 -25 C ATOM 1189 N LEU A 186 -49.789 17.127 -0.730 1.00 82.38 N ANISOU 1189 N LEU A 186 11410 8762 11129 796 168 235 N ATOM 1190 CA LEU A 186 -48.647 16.408 -0.184 1.00 87.39 C ANISOU 1190 CA LEU A 186 12174 9323 11707 909 59 295 C ATOM 1191 C LEU A 186 -48.338 16.940 1.214 1.00 95.10 C ANISOU 1191 C LEU A 186 13287 10288 12557 993 -58 281 C ATOM 1192 O LEU A 186 -48.763 18.044 1.564 1.00 96.91 O ANISOU 1192 O LEU A 186 13468 10569 12781 974 -87 218 O ATOM 1193 CB LEU A 186 -47.433 16.630 -1.064 1.00 85.71 C ANISOU 1193 CB LEU A 186 11781 9137 11648 967 -75 309 C ATOM 1194 CG LEU A 186 -47.649 16.301 -2.532 1.00 85.80 C ANISOU 1194 CG LEU A 186 11643 9168 11786 893 23 314 C ATOM 1195 CD1 LEU A 186 -46.510 16.907 -3.328 1.00 86.46 C ANISOU 1195 CD1 LEU A 186 11520 9313 12018 934 -107 314 C ATOM 1196 CD2 LEU A 186 -47.773 14.798 -2.749 1.00 86.82 C ANISOU 1196 CD2 LEU A 186 11922 9210 11854 900 135 365 C ATOM 1197 N PRO A 187 -47.585 16.173 2.019 1.00104.35 N ANISOU 1197 N PRO A 187 14644 11386 13619 1099 -139 334 N ATOM 1198 CA PRO A 187 -46.972 16.759 3.226 1.00110.87 C ANISOU 1198 CA PRO A 187 15573 12206 14346 1201 -311 319 C ATOM 1199 C PRO A 187 -45.842 17.766 2.901 1.00117.26 C ANISOU 1199 C PRO A 187 16175 13079 15299 1250 -528 287 C ATOM 1200 O PRO A 187 -45.735 18.226 1.759 1.00117.11 O ANISOU 1200 O PRO A 187 15929 13117 15451 1186 -519 270 O ATOM 1201 CB PRO A 187 -46.420 15.531 3.962 1.00112.58 C ANISOU 1201 CB PRO A 187 16035 12322 14418 1310 -346 392 C ATOM 1202 CG PRO A 187 -47.212 14.374 3.442 1.00110.06 C ANISOU 1202 CG PRO A 187 15811 11938 14067 1225 -134 438 C ATOM 1203 CD PRO A 187 -47.493 14.701 2.012 1.00106.19 C ANISOU 1203 CD PRO A 187 15054 11520 13773 1126 -60 407 C ATOM 1204 N GLN A 188 -45.029 18.120 3.902 1.00128.04 N ANISOU 1204 N GLN A 188 17625 14435 16589 1350 -721 279 N ATOM 1205 CA GLN A 188 -43.780 18.890 3.686 1.00134.48 C ANISOU 1205 CA GLN A 188 18251 15311 17532 1390 -946 258 C ATOM 1206 C GLN A 188 -42.492 18.037 3.744 1.00139.61 C ANISOU 1206 C GLN A 188 18888 15961 18195 1526 -1085 309 C ATOM 1207 O GLN A 188 -41.424 18.518 3.351 1.00139.78 O ANISOU 1207 O GLN A 188 18700 16061 18347 1545 -1245 297 O ATOM 1208 CB GLN A 188 -43.662 20.039 4.692 1.00136.65 C ANISOU 1208 CB GLN A 188 18591 15592 17734 1400 -1106 195 C ATOM 1209 CG GLN A 188 -44.822 21.025 4.675 1.00136.58 C ANISOU 1209 CG GLN A 188 18589 15590 17714 1302 -1001 128 C ATOM 1210 CD GLN A 188 -45.891 20.703 5.708 1.00138.24 C ANISOU 1210 CD GLN A 188 19055 15755 17714 1324 -866 117 C ATOM 1211 OE1 GLN A 188 -46.363 19.565 5.804 1.00136.67 O ANISOU 1211 OE1 GLN A 188 18980 15520 17426 1329 -710 172 O ATOM 1212 NE2 GLN A 188 -46.278 21.708 6.491 1.00138.67 N ANISOU 1212 NE2 GLN A 188 19200 15808 17679 1333 -920 43 N ATOM 1213 N ALA A 189 -42.589 16.799 4.243 1.00143.72 N ANISOU 1213 N ALA A 189 19633 16397 18576 1620 -1027 365 N ATOM 1214 CA ALA A 189 -41.450 15.868 4.296 1.00147.30 C ANISOU 1214 CA ALA A 189 20103 16838 19024 1784 -1151 413 C ATOM 1215 C ALA A 189 -41.927 14.407 4.265 1.00148.61 C ANISOU 1215 C ALA A 189 20502 16883 19077 1834 -994 480 C ATOM 1216 O ALA A 189 -42.599 13.955 5.195 1.00151.53 O ANISOU 1216 O ALA A 189 21163 17154 19255 1836 -926 507 O ATOM 1217 CB ALA A 189 -40.617 16.125 5.545 1.00148.27 C ANISOU 1217 CB ALA A 189 20336 16963 19036 1914 -1394 401 C ATOM 1218 N LYS A 190 -41.585 13.681 3.197 1.00147.21 N ANISOU 1218 N LYS A 190 20211 16710 19010 1865 -933 507 N ATOM 1219 CA LYS A 190 -41.956 12.264 3.052 1.00145.16 C ANISOU 1219 CA LYS A 190 20182 16318 18654 1910 -798 567 C ATOM 1220 C LYS A 190 -41.011 11.531 2.094 1.00142.31 C ANISOU 1220 C LYS A 190 19689 15975 18405 2041 -837 584 C ATOM 1221 O LYS A 190 -41.432 10.979 1.075 1.00137.67 O ANISOU 1221 O LYS A 190 19069 15355 17882 1978 -680 594 O ATOM 1222 CB LYS A 190 -43.408 12.138 2.576 1.00141.93 C ANISOU 1222 CB LYS A 190 19832 15863 18232 1709 -543 567 C ATOM 1223 N SER A 211 -30.894 5.519 -17.476 1.00132.97 N ANISOU 1223 N SER A 211 17009 16310 17200 7782 -3305 -2821 N ATOM 1224 CA SER A 211 -31.411 5.386 -18.833 1.00130.80 C ANISOU 1224 CA SER A 211 16719 15955 17022 7374 -2890 -2703 C ATOM 1225 C SER A 211 -32.053 6.690 -19.332 1.00127.24 C ANISOU 1225 C SER A 211 15992 15649 16701 6750 -2565 -2591 C ATOM 1226 O SER A 211 -32.708 7.425 -18.568 1.00123.86 O ANISOU 1226 O SER A 211 15672 15214 16173 6557 -2595 -2408 O ATOM 1227 CB SER A 211 -32.424 4.241 -18.913 1.00129.63 C ANISOU 1227 CB SER A 211 17291 15375 16584 7384 -2800 -2349 C ATOM 1228 OG SER A 211 -31.850 3.028 -18.462 1.00133.67 O ANISOU 1228 OG SER A 211 18136 15710 16942 7970 -3091 -2439 O ATOM 1229 N GLY A 212 -31.856 6.962 -20.622 1.00124.47 N ANISOU 1229 N GLY A 212 15321 15411 16560 6449 -2254 -2709 N ATOM 1230 CA GLY A 212 -32.386 8.157 -21.260 1.00119.17 C ANISOU 1230 CA GLY A 212 14430 14852 15998 5887 -1938 -2627 C ATOM 1231 C GLY A 212 -33.798 7.916 -21.752 1.00113.84 C ANISOU 1231 C GLY A 212 14214 13892 15147 5550 -1711 -2233 C ATOM 1232 O GLY A 212 -34.530 7.085 -21.198 1.00114.23 O ANISOU 1232 O GLY A 212 14763 13673 14965 5691 -1814 -1988 O ATOM 1233 N TYR A 213 -34.168 8.640 -22.805 1.00107.55 N ANISOU 1233 N TYR A 213 13262 13148 14452 5104 -1398 -2198 N ATOM 1234 CA TYR A 213 -35.508 8.585 -23.366 1.00101.55 C ANISOU 1234 CA TYR A 213 12857 12169 13556 4759 -1192 -1875 C ATOM 1235 C TYR A 213 -35.445 8.246 -24.851 1.00100.99 C ANISOU 1235 C TYR A 213 12760 12050 13560 4575 -922 -1927 C ATOM 1236 O TYR A 213 -35.028 9.070 -25.665 1.00100.25 O ANISOU 1236 O TYR A 213 12356 12114 13618 4324 -723 -2084 O ATOM 1237 CB TYR A 213 -36.224 9.920 -23.127 1.00 96.78 C ANISOU 1237 CB TYR A 213 12166 11648 12955 4395 -1111 -1745 C ATOM 1238 CG TYR A 213 -37.479 10.107 -23.938 1.00 92.08 C ANISOU 1238 CG TYR A 213 11808 10898 12279 4016 -888 -1499 C ATOM 1239 CD1 TYR A 213 -38.470 9.121 -23.975 1.00 90.79 C ANISOU 1239 CD1 TYR A 213 12073 10476 11945 4020 -876 -1275 C ATOM 1240 CD2 TYR A 213 -37.679 11.268 -24.676 1.00 90.10 C ANISOU 1240 CD2 TYR A 213 11370 10750 12111 3658 -692 -1513 C ATOM 1241 CE1 TYR A 213 -39.620 9.290 -24.730 1.00 88.18 C ANISOU 1241 CE1 TYR A 213 11916 10032 11556 3687 -698 -1098 C ATOM 1242 CE2 TYR A 213 -38.827 11.451 -25.428 1.00 88.01 C ANISOU 1242 CE2 TYR A 213 11326 10349 11763 3358 -537 -1312 C ATOM 1243 CZ TYR A 213 -39.793 10.462 -25.454 1.00 87.12 C ANISOU 1243 CZ TYR A 213 11575 10016 11507 3378 -552 -1118 C ATOM 1244 OH TYR A 213 -40.929 10.657 -26.202 1.00 85.26 O ANISOU 1244 OH TYR A 213 11513 9675 11204 3093 -424 -965 O ATOM 1245 N TYR A 214 -35.872 7.031 -25.186 1.00101.85 N ANISOU 1245 N TYR A 214 13236 11919 13541 4686 -901 -1798 N ATOM 1246 CA TYR A 214 -35.958 6.572 -26.571 1.00102.65 C ANISOU 1246 CA TYR A 214 13397 11932 13672 4513 -652 -1811 C ATOM 1247 C TYR A 214 -37.416 6.611 -27.014 1.00 96.37 C ANISOU 1247 C TYR A 214 12938 10949 12728 4165 -508 -1514 C ATOM 1248 O TYR A 214 -38.315 6.399 -26.200 1.00 97.07 O ANISOU 1248 O TYR A 214 13314 10901 12664 4170 -611 -1306 O ATOM 1249 CB TYR A 214 -35.441 5.139 -26.688 1.00108.21 C ANISOU 1249 CB TYR A 214 14288 12489 14334 4878 -723 -1891 C ATOM 1250 CG TYR A 214 -34.098 4.890 -26.041 1.00115.55 C ANISOU 1250 CG TYR A 214 14942 13578 15382 5331 -954 -2190 C ATOM 1251 CD1 TYR A 214 -34.003 4.537 -24.691 1.00119.22 C ANISOU 1251 CD1 TYR A 214 15580 13994 15725 5703 -1273 -2151 C ATOM 1252 CD2 TYR A 214 -32.916 4.979 -26.782 1.00121.09 C ANISOU 1252 CD2 TYR A 214 15223 14474 16312 5399 -856 -2538 C ATOM 1253 CE1 TYR A 214 -32.769 4.289 -24.097 1.00125.27 C ANISOU 1253 CE1 TYR A 214 16093 14911 16589 6168 -1535 -2452 C ATOM 1254 CE2 TYR A 214 -31.675 4.729 -26.201 1.00126.03 C ANISOU 1254 CE2 TYR A 214 15544 15272 17069 5840 -1090 -2868 C ATOM 1255 CZ TYR A 214 -31.604 4.385 -24.859 1.00128.30 C ANISOU 1255 CZ TYR A 214 15999 15519 17230 6244 -1453 -2824 C ATOM 1256 OH TYR A 214 -30.376 4.143 -24.281 1.00132.75 O ANISOU 1256 OH TYR A 214 16258 16263 17917 6723 -1732 -3175 O ATOM 1257 N SER A 215 -37.648 6.888 -28.294 1.00 91.19 N ANISOU 1257 N SER A 215 12249 10287 12112 3864 -270 -1519 N ATOM 1258 CA SER A 215 -39.002 6.895 -28.858 1.00 85.23 C ANISOU 1258 CA SER A 215 11783 9373 11227 3557 -155 -1286 C ATOM 1259 C SER A 215 -38.978 6.422 -30.302 1.00 84.12 C ANISOU 1259 C SER A 215 11729 9145 11086 3411 58 -1330 C ATOM 1260 O SER A 215 -38.168 6.896 -31.094 1.00 85.33 O ANISOU 1260 O SER A 215 11649 9413 11358 3329 201 -1513 O ATOM 1261 CB SER A 215 -39.613 8.288 -28.787 1.00 81.67 C ANISOU 1261 CB SER A 215 11207 9030 10790 3265 -130 -1206 C ATOM 1262 OG SER A 215 -40.953 8.261 -29.232 1.00 78.59 O ANISOU 1262 OG SER A 215 11075 8502 10281 3020 -69 -1014 O ATOM 1263 N THR A 216 -39.880 5.499 -30.629 1.00 81.75 N ANISOU 1263 N THR A 216 11779 8636 10647 3357 96 -1178 N ATOM 1264 CA THR A 216 -39.951 4.873 -31.944 1.00 80.79 C ANISOU 1264 CA THR A 216 11800 8399 10494 3236 282 -1205 C ATOM 1265 C THR A 216 -41.345 5.084 -32.514 1.00 78.21 C ANISOU 1265 C THR A 216 11692 7975 10048 2918 342 -1033 C ATOM 1266 O THR A 216 -42.337 4.875 -31.827 1.00 78.08 O ANISOU 1266 O THR A 216 11852 7877 9938 2882 253 -889 O ATOM 1267 CB THR A 216 -39.672 3.363 -31.827 1.00 82.46 C ANISOU 1267 CB THR A 216 12253 8435 10643 3508 264 -1221 C ATOM 1268 OG1 THR A 216 -38.380 3.167 -31.250 1.00 84.87 O ANISOU 1268 OG1 THR A 216 12342 8841 11061 3861 156 -1410 O ATOM 1269 CG2 THR A 216 -39.728 2.673 -33.182 1.00 82.64 C ANISOU 1269 CG2 THR A 216 12434 8334 10632 3382 464 -1256 C ATOM 1270 N THR A 217 -41.420 5.504 -33.769 1.00 77.44 N ANISOU 1270 N THR A 217 11588 7885 9949 2688 494 -1072 N ATOM 1271 CA THR A 217 -42.697 5.780 -34.414 1.00 75.59 C ANISOU 1271 CA THR A 217 11540 7578 9602 2415 514 -948 C ATOM 1272 C THR A 217 -43.107 4.563 -35.217 1.00 76.40 C ANISOU 1272 C THR A 217 11921 7501 9606 2378 608 -931 C ATOM 1273 O THR A 217 -42.275 3.942 -35.863 1.00 80.09 O ANISOU 1273 O THR A 217 12408 7920 10100 2462 732 -1037 O ATOM 1274 CB THR A 217 -42.599 7.018 -35.320 1.00 74.40 C ANISOU 1274 CB THR A 217 11294 7512 9462 2197 600 -994 C ATOM 1275 OG1 THR A 217 -42.297 8.162 -34.514 1.00 73.06 O ANISOU 1275 OG1 THR A 217 10887 7497 9372 2211 522 -1007 O ATOM 1276 CG2 THR A 217 -43.902 7.268 -36.058 1.00 73.78 C ANISOU 1276 CG2 THR A 217 11427 7355 9251 1970 574 -890 C ATOM 1277 N ILE A 218 -44.390 4.226 -35.158 1.00 75.42 N ANISOU 1277 N ILE A 218 11994 7283 9376 2244 560 -822 N ATOM 1278 CA ILE A 218 -44.942 3.052 -35.826 1.00 75.75 C ANISOU 1278 CA ILE A 218 12314 7152 9314 2175 648 -814 C ATOM 1279 C ILE A 218 -46.108 3.551 -36.655 1.00 75.78 C ANISOU 1279 C ILE A 218 12390 7162 9240 1903 628 -786 C ATOM 1280 O ILE A 218 -47.037 4.143 -36.108 1.00 74.52 O ANISOU 1280 O ILE A 218 12172 7064 9075 1810 509 -734 O ATOM 1281 CB ILE A 218 -45.420 2.009 -34.800 1.00 75.51 C ANISOU 1281 CB ILE A 218 12479 6988 9221 2279 614 -752 C ATOM 1282 CG1 ILE A 218 -44.267 1.635 -33.868 1.00 76.65 C ANISOU 1282 CG1 ILE A 218 12572 7128 9421 2608 569 -780 C ATOM 1283 CG2 ILE A 218 -45.970 0.767 -35.490 1.00 76.54 C ANISOU 1283 CG2 ILE A 218 12915 6926 9238 2184 738 -762 C ATOM 1284 CD1 ILE A 218 -44.588 0.522 -32.898 1.00 78.19 C ANISOU 1284 CD1 ILE A 218 13065 7135 9508 2748 550 -720 C ATOM 1285 N ARG A 219 -46.060 3.306 -37.963 1.00 78.40 N ANISOU 1285 N ARG A 219 12851 7429 9508 1792 733 -839 N ATOM 1286 CA ARG A 219 -46.973 3.947 -38.904 1.00 79.49 C ANISOU 1286 CA ARG A 219 13060 7584 9558 1576 680 -839 C ATOM 1287 C ARG A 219 -48.028 2.982 -39.405 1.00 79.65 C ANISOU 1287 C ARG A 219 13298 7491 9474 1444 687 -857 C ATOM 1288 O ARG A 219 -47.734 1.825 -39.699 1.00 81.01 O ANISOU 1288 O ARG A 219 13635 7533 9611 1476 818 -885 O ATOM 1289 CB ARG A 219 -46.197 4.553 -40.068 1.00 81.95 C ANISOU 1289 CB ARG A 219 13399 7897 9839 1519 786 -899 C ATOM 1290 CG ARG A 219 -45.241 5.638 -39.614 1.00 84.19 C ANISOU 1290 CG ARG A 219 13456 8304 10226 1591 802 -920 C ATOM 1291 CD ARG A 219 -44.647 6.418 -40.776 1.00 88.66 C ANISOU 1291 CD ARG A 219 14099 8854 10734 1467 937 -992 C ATOM 1292 NE ARG A 219 -44.284 7.777 -40.355 1.00 91.02 N ANISOU 1292 NE ARG A 219 14230 9269 11084 1448 911 -996 N ATOM 1293 CZ ARG A 219 -43.162 8.124 -39.713 1.00 92.75 C ANISOU 1293 CZ ARG A 219 14199 9591 11448 1543 995 -1077 C ATOM 1294 NH1 ARG A 219 -42.976 9.402 -39.381 1.00 94.32 N ANISOU 1294 NH1 ARG A 219 14278 9885 11673 1486 976 -1083 N ATOM 1295 NH2 ARG A 219 -42.224 7.225 -39.394 1.00 92.91 N ANISOU 1295 NH2 ARG A 219 14087 9625 11587 1704 1088 -1172 N ATOM 1296 N TYR A 220 -49.258 3.480 -39.497 1.00 78.87 N ANISOU 1296 N TYR A 220 13186 7447 9332 1301 543 -862 N ATOM 1297 CA TYR A 220 -50.414 2.679 -39.855 1.00 79.23 C ANISOU 1297 CA TYR A 220 13374 7427 9301 1150 527 -926 C ATOM 1298 C TYR A 220 -51.257 3.407 -40.887 1.00 79.58 C ANISOU 1298 C TYR A 220 13448 7529 9260 1019 377 -989 C ATOM 1299 O TYR A 220 -51.493 4.608 -40.753 1.00 78.89 O ANISOU 1299 O TYR A 220 13231 7552 9189 1038 224 -968 O ATOM 1300 CB TYR A 220 -51.298 2.458 -38.630 1.00 79.04 C ANISOU 1300 CB TYR A 220 13266 7432 9333 1114 475 -929 C ATOM 1301 CG TYR A 220 -50.664 1.759 -37.449 1.00 78.20 C ANISOU 1301 CG TYR A 220 13195 7245 9272 1256 583 -864 C ATOM 1302 CD1 TYR A 220 -49.987 2.476 -36.463 1.00 76.71 C ANISOU 1302 CD1 TYR A 220 12836 7139 9168 1419 524 -785 C ATOM 1303 CD2 TYR A 220 -50.797 0.389 -37.285 1.00 79.38 C ANISOU 1303 CD2 TYR A 220 13580 7221 9357 1232 732 -889 C ATOM 1304 CE1 TYR A 220 -49.432 1.835 -35.362 1.00 76.58 C ANISOU 1304 CE1 TYR A 220 12889 7040 9167 1582 581 -735 C ATOM 1305 CE2 TYR A 220 -50.245 -0.259 -36.193 1.00 79.74 C ANISOU 1305 CE2 TYR A 220 13733 7158 9404 1394 808 -828 C ATOM 1306 CZ TYR A 220 -49.567 0.464 -35.234 1.00 78.31 C ANISOU 1306 CZ TYR A 220 13385 7067 9302 1582 716 -752 C ATOM 1307 OH TYR A 220 -49.030 -0.210 -34.162 1.00 78.28 O ANISOU 1307 OH TYR A 220 13529 6941 9270 1775 757 -700 O ATOM 1308 N GLN A 221 -51.708 2.679 -41.905 1.00 81.86 N ANISOU 1308 N GLN A 221 13927 7734 9441 904 409 -1072 N ATOM 1309 CA GLN A 221 -52.809 3.134 -42.758 1.00 83.43 C ANISOU 1309 CA GLN A 221 14166 7987 9545 791 215 -1173 C ATOM 1310 C GLN A 221 -54.116 2.667 -42.128 1.00 83.45 C ANISOU 1310 C GLN A 221 14050 8051 9603 677 136 -1290 C ATOM 1311 O GLN A 221 -54.140 1.665 -41.412 1.00 82.98 O ANISOU 1311 O GLN A 221 14012 7921 9593 633 299 -1298 O ATOM 1312 CB GLN A 221 -52.712 2.569 -44.169 1.00 86.55 C ANISOU 1312 CB GLN A 221 14827 8268 9788 712 275 -1235 C ATOM 1313 CG GLN A 221 -51.888 3.387 -45.148 1.00 87.91 C ANISOU 1313 CG GLN A 221 15157 8394 9852 757 287 -1184 C ATOM 1314 CD GLN A 221 -51.951 2.808 -46.557 1.00 90.88 C ANISOU 1314 CD GLN A 221 15834 8645 10051 659 335 -1258 C ATOM 1315 OE1 GLN A 221 -52.573 1.767 -46.790 1.00 91.50 O ANISOU 1315 OE1 GLN A 221 15980 8683 10102 561 358 -1349 O ATOM 1316 NE2 GLN A 221 -51.310 3.481 -47.505 1.00 92.99 N ANISOU 1316 NE2 GLN A 221 16309 8837 10186 665 371 -1232 N ATOM 1317 N ALA A 222 -55.200 3.383 -42.415 1.00 83.65 N ANISOU 1317 N ALA A 222 13972 8197 9612 630 -104 -1404 N ATOM 1318 CA ALA A 222 -56.512 3.049 -41.872 1.00 85.02 C ANISOU 1318 CA ALA A 222 13979 8462 9863 499 -179 -1580 C ATOM 1319 C ALA A 222 -57.637 3.417 -42.831 1.00 87.22 C ANISOU 1319 C ALA A 222 14227 8839 10071 445 -443 -1781 C ATOM 1320 O ALA A 222 -57.611 4.484 -43.446 1.00 87.31 O ANISOU 1320 O ALA A 222 14271 8897 10003 567 -662 -1753 O ATOM 1321 CB ALA A 222 -56.715 3.760 -40.551 1.00 84.72 C ANISOU 1321 CB ALA A 222 13693 8529 9966 553 -226 -1537 C ATOM 1322 N THR A 223 -58.617 2.524 -42.957 1.00 88.68 N ANISOU 1322 N THR A 223 14372 9048 10272 266 -422 -2001 N ATOM 1323 CA THR A 223 -59.863 2.827 -43.656 1.00 90.61 C ANISOU 1323 CA THR A 223 14502 9434 10491 220 -707 -2264 C ATOM 1324 C THR A 223 -61.029 2.602 -42.700 1.00 91.72 C ANISOU 1324 C THR A 223 14330 9713 10806 67 -703 -2501 C ATOM 1325 O THR A 223 -60.952 1.749 -41.811 1.00 90.68 O ANISOU 1325 O THR A 223 14196 9504 10752 -80 -415 -2492 O ATOM 1326 CB THR A 223 -60.032 1.961 -44.911 1.00 92.27 C ANISOU 1326 CB THR A 223 14937 9566 10553 114 -697 -2389 C ATOM 1327 OG1 THR A 223 -60.040 0.577 -44.545 1.00 94.18 O ANISOU 1327 OG1 THR A 223 15242 9705 10833 -92 -384 -2445 O ATOM 1328 CG2 THR A 223 -58.901 2.213 -45.883 1.00 91.42 C ANISOU 1328 CG2 THR A 223 15154 9312 10268 241 -674 -2178 C ATOM 1329 N GLY A 224 -62.097 3.378 -42.883 1.00 93.64 N ANISOU 1329 N GLY A 224 14331 10147 11101 112 -1018 -2728 N ATOM 1330 CA GLY A 224 -63.286 3.286 -42.041 1.00 95.72 C ANISOU 1330 CA GLY A 224 14246 10571 11551 -38 -1027 -3017 C ATOM 1331 C GLY A 224 -62.973 3.505 -40.575 1.00 95.56 C ANISOU 1331 C GLY A 224 14108 10531 11668 -53 -825 -2869 C ATOM 1332 O GLY A 224 -63.399 2.728 -39.722 1.00 97.69 O ANISOU 1332 O GLY A 224 14299 10780 12039 -277 -569 -2995 O ATOM 1333 N PHE A 225 -62.214 4.565 -40.295 1.00 94.76 N ANISOU 1333 N PHE A 225 14031 10422 11551 172 -927 -2608 N ATOM 1334 CA PHE A 225 -61.754 4.889 -38.942 1.00 92.06 C ANISOU 1334 CA PHE A 225 13609 10056 11314 197 -766 -2434 C ATOM 1335 C PHE A 225 -62.935 5.253 -38.056 1.00 95.23 C ANISOU 1335 C PHE A 225 13663 10623 11895 98 -824 -2686 C ATOM 1336 O PHE A 225 -63.785 6.050 -38.453 1.00 96.29 O ANISOU 1336 O PHE A 225 13577 10930 12078 183 -1127 -2889 O ATOM 1337 CB PHE A 225 -60.749 6.051 -38.982 1.00 87.94 C ANISOU 1337 CB PHE A 225 13165 9512 10734 450 -890 -2149 C ATOM 1338 CG PHE A 225 -60.210 6.437 -37.634 1.00 84.78 C ANISOU 1338 CG PHE A 225 12683 9097 10431 493 -753 -1973 C ATOM 1339 CD1 PHE A 225 -60.788 7.483 -36.905 1.00 83.54 C ANISOU 1339 CD1 PHE A 225 12272 9080 10389 554 -905 -2031 C ATOM 1340 CD2 PHE A 225 -59.131 5.757 -37.085 1.00 82.77 C ANISOU 1340 CD2 PHE A 225 12610 8690 10148 491 -487 -1764 C ATOM 1341 CE1 PHE A 225 -60.301 7.832 -35.659 1.00 80.66 C ANISOU 1341 CE1 PHE A 225 11846 8698 10101 585 -780 -1875 C ATOM 1342 CE2 PHE A 225 -58.633 6.109 -35.839 1.00 80.80 C ANISOU 1342 CE2 PHE A 225 12297 8429 9971 550 -392 -1617 C ATOM 1343 CZ PHE A 225 -59.220 7.147 -35.125 1.00 79.83 C ANISOU 1343 CZ PHE A 225 11933 8444 9956 584 -532 -1667 C ATOM 1344 N GLY A 226 -62.975 4.671 -36.859 1.00 98.33 N ANISOU 1344 N GLY A 226 14032 10952 12375 -69 -534 -2685 N ATOM 1345 CA GLY A 226 -64.032 4.957 -35.890 1.00102.53 C ANISOU 1345 CA GLY A 226 14254 11618 13083 -204 -512 -2930 C ATOM 1346 C GLY A 226 -65.402 4.435 -36.287 1.00108.18 C ANISOU 1346 C GLY A 226 14741 12470 13891 -433 -539 -3377 C ATOM 1347 O GLY A 226 -66.411 5.109 -36.070 1.00109.07 O ANISOU 1347 O GLY A 226 14501 12784 14156 -438 -716 -3656 O ATOM 1348 N THR A 227 -65.430 3.242 -36.881 1.00113.23 N ANISOU 1348 N THR A 227 15569 13006 14446 -617 -365 -3469 N ATOM 1349 CA THR A 227 -66.672 2.547 -37.225 1.00120.31 C ANISOU 1349 CA THR A 227 16267 14016 15426 -892 -323 -3924 C ATOM 1350 C THR A 227 -66.531 1.066 -36.873 1.00127.76 C ANISOU 1350 C THR A 227 17494 14742 16304 -1206 126 -3946 C ATOM 1351 O THR A 227 -65.466 0.621 -36.446 1.00126.83 O ANISOU 1351 O THR A 227 17731 14392 16067 -1154 347 -3602 O ATOM 1352 CB THR A 227 -67.021 2.696 -38.724 1.00120.33 C ANISOU 1352 CB THR A 227 16219 14143 15357 -774 -671 -4087 C ATOM 1353 OG1 THR A 227 -66.009 2.075 -39.526 1.00118.09 O ANISOU 1353 OG1 THR A 227 16336 13661 14869 -715 -592 -3813 O ATOM 1354 CG2 THR A 227 -67.148 4.157 -39.114 1.00118.80 C ANISOU 1354 CG2 THR A 227 15838 14119 15181 -435 -1125 -4057 C ATOM 1355 N ASN A 228 -67.618 0.319 -37.038 1.00139.43 N ANISOU 1355 N ASN A 228 18820 16296 17860 -1525 258 -4375 N ATOM 1356 CA ASN A 228 -67.631 -1.129 -36.772 1.00147.79 C ANISOU 1356 CA ASN A 228 20179 17133 18841 -1867 709 -4453 C ATOM 1357 C ASN A 228 -66.680 -1.970 -37.651 1.00146.20 C ANISOU 1357 C ASN A 228 20406 16717 18425 -1798 781 -4198 C ATOM 1358 O ASN A 228 -66.149 -2.974 -37.173 1.00148.10 O ANISOU 1358 O ASN A 228 21031 16686 18550 -1934 1149 -4051 O ATOM 1359 CB ASN A 228 -69.064 -1.686 -36.854 1.00159.93 C ANISOU 1359 CB ASN A 228 21420 18824 20520 -2256 836 -5032 C ATOM 1360 CG ASN A 228 -69.753 -1.382 -38.186 1.00171.91 C ANISOU 1360 CG ASN A 228 22632 20602 22081 -2174 435 -5340 C ATOM 1361 OD1 ASN A 228 -69.191 -0.686 -39.033 1.00172.01 O ANISOU 1361 OD1 ASN A 228 22689 20664 22002 -1822 60 -5105 O ATOM 1362 ND2 ASN A 228 -70.975 -1.890 -38.378 1.00187.35 N ANISOU 1362 ND2 ASN A 228 24292 22721 24168 -2500 513 -5889 N ATOM 1363 N GLU A 229 -66.479 -1.574 -38.914 1.00143.20 N ANISOU 1363 N GLU A 229 19989 16440 17979 -1585 440 -4157 N ATOM 1364 CA GLU A 229 -65.554 -2.268 -39.837 1.00139.76 C ANISOU 1364 CA GLU A 229 19941 15814 17345 -1504 493 -3924 C ATOM 1365 C GLU A 229 -64.326 -1.405 -40.194 1.00131.43 C ANISOU 1365 C GLU A 229 19025 14715 16195 -1115 267 -3502 C ATOM 1366 O GLU A 229 -64.205 -0.908 -41.317 1.00131.00 O ANISOU 1366 O GLU A 229 18964 14743 16066 -943 -27 -3483 O ATOM 1367 CB GLU A 229 -66.287 -2.727 -41.115 1.00145.48 C ANISOU 1367 CB GLU A 229 20595 16647 18030 -1637 352 -4250 C ATOM 1368 CG GLU A 229 -67.135 -3.992 -40.965 1.00151.37 C ANISOU 1368 CG GLU A 229 21365 17340 18805 -2070 698 -4620 C ATOM 1369 CD GLU A 229 -68.635 -3.736 -41.031 1.00156.42 C ANISOU 1369 CD GLU A 229 21515 18279 19634 -2276 549 -5169 C ATOM 1370 OE1 GLU A 229 -69.337 -4.023 -40.037 1.00159.45 O ANISOU 1370 OE1 GLU A 229 21744 18681 20156 -2567 830 -5422 O ATOM 1371 OE2 GLU A 229 -69.114 -3.254 -42.081 1.00157.99 O ANISOU 1371 OE2 GLU A 229 21495 18693 19840 -2145 151 -5369 O ATOM 1372 N THR A 230 -63.420 -1.247 -39.229 1.00123.57 N ANISOU 1372 N THR A 230 18174 13581 15193 -990 421 -3186 N ATOM 1373 CA THR A 230 -62.160 -0.521 -39.425 1.00117.38 C ANISOU 1373 CA THR A 230 17519 12743 14334 -662 282 -2811 C ATOM 1374 C THR A 230 -61.053 -1.502 -39.810 1.00113.94 C ANISOU 1374 C THR A 230 17481 12062 13748 -623 506 -2591 C ATOM 1375 O THR A 230 -60.810 -2.468 -39.088 1.00114.74 O ANISOU 1375 O THR A 230 17804 11974 13818 -735 814 -2545 O ATOM 1376 CB THR A 230 -61.720 0.226 -38.142 1.00115.23 C ANISOU 1376 CB THR A 230 17156 12476 14147 -527 305 -2611 C ATOM 1377 OG1 THR A 230 -62.835 0.908 -37.557 1.00117.13 O ANISOU 1377 OG1 THR A 230 17045 12913 14544 -618 187 -2850 O ATOM 1378 CG2 THR A 230 -60.636 1.246 -38.448 1.00112.40 C ANISOU 1378 CG2 THR A 230 16823 12136 13745 -212 104 -2315 C ATOM 1379 N GLU A 231 -60.385 -1.245 -40.934 1.00110.14 N ANISOU 1379 N GLU A 231 17116 11568 13164 -458 357 -2466 N ATOM 1380 CA GLU A 231 -59.265 -2.068 -41.400 1.00107.01 C ANISOU 1380 CA GLU A 231 17064 10955 12639 -391 551 -2273 C ATOM 1381 C GLU A 231 -57.961 -1.281 -41.226 1.00 99.94 C ANISOU 1381 C GLU A 231 16202 10032 11738 -103 493 -1970 C ATOM 1382 O GLU A 231 -57.846 -0.164 -41.723 1.00 98.18 O ANISOU 1382 O GLU A 231 15855 9933 11514 33 251 -1923 O ATOM 1383 CB GLU A 231 -59.444 -2.454 -42.874 1.00110.72 C ANISOU 1383 CB GLU A 231 17664 11414 12988 -457 474 -2391 C ATOM 1384 CG GLU A 231 -60.839 -2.930 -43.278 1.00115.79 C ANISOU 1384 CG GLU A 231 18184 12162 13648 -725 427 -2753 C ATOM 1385 CD GLU A 231 -61.165 -4.342 -42.811 1.00119.46 C ANISOU 1385 CD GLU A 231 18822 12466 14102 -998 786 -2884 C ATOM 1386 OE1 GLU A 231 -62.198 -4.528 -42.127 1.00122.20 O ANISOU 1386 OE1 GLU A 231 18984 12893 14552 -1223 863 -3135 O ATOM 1387 OE2 GLU A 231 -60.398 -5.273 -43.139 1.00121.09 O ANISOU 1387 OE2 GLU A 231 19365 12453 14191 -998 1009 -2755 O ATOM 1388 N TYR A 232 -56.994 -1.871 -40.524 1.00 95.47 N ANISOU 1388 N TYR A 232 15817 9297 11159 -9 714 -1789 N ATOM 1389 CA TYR A 232 -55.679 -1.271 -40.285 1.00 91.61 C ANISOU 1389 CA TYR A 232 15338 8786 10684 254 692 -1548 C ATOM 1390 C TYR A 232 -54.570 -2.021 -41.024 1.00 91.36 C ANISOU 1390 C TYR A 232 15568 8587 10558 351 846 -1451 C ATOM 1391 O TYR A 232 -54.663 -3.230 -41.229 1.00 93.25 O ANISOU 1391 O TYR A 232 16040 8666 10724 247 1035 -1511 O ATOM 1392 CB TYR A 232 -55.376 -1.272 -38.788 1.00 90.94 C ANISOU 1392 CB TYR A 232 15220 8661 10671 340 782 -1442 C ATOM 1393 CG TYR A 232 -56.229 -0.312 -38.006 1.00 90.03 C ANISOU 1393 CG TYR A 232 14824 8720 10663 287 632 -1506 C ATOM 1394 CD1 TYR A 232 -57.285 -0.763 -37.210 1.00 90.39 C ANISOU 1394 CD1 TYR A 232 14841 8755 10747 78 735 -1662 C ATOM 1395 CD2 TYR A 232 -55.993 1.059 -38.074 1.00 88.94 C ANISOU 1395 CD2 TYR A 232 14463 8744 10585 430 410 -1429 C ATOM 1396 CE1 TYR A 232 -58.075 0.129 -36.499 1.00 90.44 C ANISOU 1396 CE1 TYR A 232 14570 8925 10868 26 610 -1747 C ATOM 1397 CE2 TYR A 232 -56.777 1.957 -37.372 1.00 88.65 C ANISOU 1397 CE2 TYR A 232 14172 8862 10649 397 269 -1493 C ATOM 1398 CZ TYR A 232 -57.817 1.491 -36.587 1.00 89.86 C ANISOU 1398 CZ TYR A 232 14266 9018 10856 202 364 -1655 C ATOM 1399 OH TYR A 232 -58.588 2.401 -35.895 1.00 91.71 O ANISOU 1399 OH TYR A 232 14229 9410 11205 170 235 -1741 O ATOM 1400 N LEU A 233 -53.526 -1.292 -41.417 1.00 89.96 N ANISOU 1400 N LEU A 233 15353 8441 10385 538 784 -1322 N ATOM 1401 CA LEU A 233 -52.340 -1.864 -42.070 1.00 89.66 C ANISOU 1401 CA LEU A 233 15510 8264 10289 650 939 -1251 C ATOM 1402 C LEU A 233 -51.073 -1.276 -41.462 1.00 88.29 C ANISOU 1402 C LEU A 233 15224 8118 10201 891 950 -1114 C ATOM 1403 O LEU A 233 -50.899 -0.058 -41.477 1.00 88.40 O ANISOU 1403 O LEU A 233 15053 8271 10261 942 811 -1075 O ATOM 1404 CB LEU A 233 -52.336 -1.536 -43.565 1.00 90.08 C ANISOU 1404 CB LEU A 233 15649 8333 10244 582 876 -1305 C ATOM 1405 CG LEU A 233 -53.430 -2.121 -44.456 1.00 91.85 C ANISOU 1405 CG LEU A 233 16000 8535 10362 365 842 -1467 C ATOM 1406 CD1 LEU A 233 -53.303 -1.548 -45.859 1.00 91.96 C ANISOU 1406 CD1 LEU A 233 16122 8562 10255 349 735 -1494 C ATOM 1407 CD2 LEU A 233 -53.373 -3.643 -44.479 1.00 93.35 C ANISOU 1407 CD2 LEU A 233 16429 8537 10502 280 1087 -1513 C ATOM 1408 N PHE A 234 -50.190 -2.126 -40.939 1.00 87.73 N ANISOU 1408 N PHE A 234 15270 7915 10145 1046 1107 -1061 N ATOM 1409 CA PHE A 234 -48.870 -1.678 -40.463 1.00 87.32 C ANISOU 1409 CA PHE A 234 15090 7902 10184 1296 1115 -984 C ATOM 1410 C PHE A 234 -47.948 -1.403 -41.655 1.00 88.70 C ANISOU 1410 C PHE A 234 15272 8078 10348 1325 1188 -1016 C ATOM 1411 O PHE A 234 -47.888 -2.210 -42.579 1.00 89.85 O ANISOU 1411 O PHE A 234 15627 8099 10411 1256 1316 -1070 O ATOM 1412 CB PHE A 234 -48.256 -2.723 -39.531 1.00 87.79 C ANISOU 1412 CB PHE A 234 15293 7812 10249 1495 1222 -948 C ATOM 1413 CG PHE A 234 -46.800 -2.506 -39.237 1.00 87.48 C ANISOU 1413 CG PHE A 234 15127 7806 10304 1781 1231 -929 C ATOM 1414 CD1 PHE A 234 -46.359 -1.312 -38.685 1.00 85.75 C ANISOU 1414 CD1 PHE A 234 14615 7769 10194 1873 1103 -899 C ATOM 1415 CD2 PHE A 234 -45.866 -3.508 -39.499 1.00 89.52 C ANISOU 1415 CD2 PHE A 234 15545 7919 10548 1964 1368 -968 C ATOM 1416 CE1 PHE A 234 -45.016 -1.114 -38.406 1.00 86.59 C ANISOU 1416 CE1 PHE A 234 14563 7931 10405 2124 1113 -932 C ATOM 1417 CE2 PHE A 234 -44.521 -3.314 -39.221 1.00 90.06 C ANISOU 1417 CE2 PHE A 234 15444 8044 10727 2243 1361 -1006 C ATOM 1418 CZ PHE A 234 -44.095 -2.115 -38.671 1.00 88.40 C ANISOU 1418 CZ PHE A 234 14915 8036 10637 2315 1234 -999 C ATOM 1419 N GLU A 235 -47.233 -0.274 -41.621 1.00 89.07 N ANISOU 1419 N GLU A 235 15110 8257 10475 1406 1133 -997 N ATOM 1420 CA GLU A 235 -46.378 0.175 -42.737 1.00 90.61 C ANISOU 1420 CA GLU A 235 15317 8454 10655 1385 1236 -1052 C ATOM 1421 C GLU A 235 -44.912 -0.244 -42.564 1.00 92.59 C ANISOU 1421 C GLU A 235 15492 8675 11010 1595 1394 -1107 C ATOM 1422 O GLU A 235 -44.273 0.126 -41.580 1.00 92.45 O ANISOU 1422 O GLU A 235 15255 8753 11116 1774 1343 -1099 O ATOM 1423 CB GLU A 235 -46.459 1.695 -42.867 1.00 90.08 C ANISOU 1423 CB GLU A 235 15101 8527 10596 1318 1120 -1032 C ATOM 1424 CG GLU A 235 -45.628 2.304 -43.988 1.00 92.58 C ANISOU 1424 CG GLU A 235 15482 8824 10869 1252 1256 -1098 C ATOM 1425 CD GLU A 235 -45.895 3.789 -44.173 1.00 93.07 C ANISOU 1425 CD GLU A 235 15500 8976 10884 1163 1142 -1071 C ATOM 1426 OE1 GLU A 235 -46.802 4.141 -44.960 1.00 94.67 O ANISOU 1426 OE1 GLU A 235 15897 9141 10932 1030 1029 -1061 O ATOM 1427 OE2 GLU A 235 -45.196 4.607 -43.535 1.00 92.89 O ANISOU 1427 OE2 GLU A 235 15265 9056 10971 1236 1157 -1072 O ATOM 1428 N VAL A 236 -44.394 -1.003 -43.531 1.00 94.95 N ANISOU 1428 N VAL A 236 15962 8851 11264 1578 1577 -1185 N ATOM 1429 CA VAL A 236 -42.977 -1.370 -43.587 1.00 97.20 C ANISOU 1429 CA VAL A 236 16154 9117 11660 1769 1742 -1292 C ATOM 1430 C VAL A 236 -42.226 -0.308 -44.398 1.00 97.95 C ANISOU 1430 C VAL A 236 16132 9295 11789 1662 1857 -1389 C ATOM 1431 O VAL A 236 -41.214 0.228 -43.950 1.00 97.61 O ANISOU 1431 O VAL A 236 15823 9367 11895 1788 1898 -1479 O ATOM 1432 CB VAL A 236 -42.790 -2.769 -44.215 1.00 99.78 C ANISOU 1432 CB VAL A 236 16737 9251 11922 1804 1908 -1347 C ATOM 1433 CG1 VAL A 236 -41.313 -3.118 -44.347 1.00102.34 C ANISOU 1433 CG1 VAL A 236 16936 9568 12379 2017 2075 -1499 C ATOM 1434 CG2 VAL A 236 -43.528 -3.827 -43.399 1.00 99.73 C ANISOU 1434 CG2 VAL A 236 16909 9126 11856 1883 1835 -1262 C ATOM 1435 N ASP A 237 -42.720 -0.046 -45.606 1.00 99.75 N ANISOU 1435 N ASP A 237 16586 9449 11863 1421 1919 -1390 N ATOM 1436 CA ASP A 237 -42.347 1.135 -46.408 1.00101.82 C ANISOU 1436 CA ASP A 237 16856 9748 12080 1256 2010 -1448 C ATOM 1437 C ASP A 237 -43.592 1.603 -47.168 1.00103.92 C ANISOU 1437 C ASP A 237 17392 9960 12131 1045 1871 -1360 C ATOM 1438 O ASP A 237 -44.667 1.025 -46.993 1.00103.57 O ANISOU 1438 O ASP A 237 17442 9888 12019 1029 1711 -1286 O ATOM 1439 CB ASP A 237 -41.138 0.864 -47.340 1.00103.32 C ANISOU 1439 CB ASP A 237 17094 9860 12302 1221 2323 -1625 C ATOM 1440 CG ASP A 237 -41.373 -0.267 -48.352 1.00104.02 C ANISOU 1440 CG ASP A 237 17499 9763 12260 1143 2450 -1649 C ATOM 1441 OD1 ASP A 237 -42.496 -0.439 -48.868 1.00103.03 O ANISOU 1441 OD1 ASP A 237 17638 9557 11951 1003 2331 -1554 O ATOM 1442 OD2 ASP A 237 -40.396 -0.981 -48.656 1.00105.05 O ANISOU 1442 OD2 ASP A 237 17601 9834 12479 1226 2674 -1790 O ATOM 1443 N ASN A 238 -43.463 2.624 -48.011 1.00108.79 N ANISOU 1443 N ASN A 238 18150 10553 12632 888 1931 -1390 N ATOM 1444 CA ASN A 238 -44.632 3.191 -48.707 1.00111.47 C ANISOU 1444 CA ASN A 238 18761 10842 12749 742 1743 -1319 C ATOM 1445 C ASN A 238 -45.355 2.239 -49.666 1.00108.63 C ANISOU 1445 C ASN A 238 18708 10345 12219 646 1726 -1332 C ATOM 1446 O ASN A 238 -46.494 2.513 -50.045 1.00106.56 O ANISOU 1446 O ASN A 238 18610 10076 11799 574 1498 -1294 O ATOM 1447 CB ASN A 238 -44.261 4.505 -49.420 1.00117.64 C ANISOU 1447 CB ASN A 238 19715 11582 13401 612 1823 -1348 C ATOM 1448 CG ASN A 238 -44.156 5.681 -48.461 1.00124.04 C ANISOU 1448 CG ASN A 238 20277 12537 14316 672 1717 -1302 C ATOM 1449 OD1 ASN A 238 -44.660 5.627 -47.337 1.00124.21 O ANISOU 1449 OD1 ASN A 238 20033 12692 14467 800 1514 -1226 O ATOM 1450 ND2 ASN A 238 -43.507 6.757 -48.903 1.00135.01 N ANISOU 1450 ND2 ASN A 238 21779 13884 15635 560 1876 -1357 N ATOM 1451 N LEU A 239 -44.706 1.136 -50.045 1.00107.82 N ANISOU 1451 N LEU A 239 18673 10142 12152 656 1954 -1405 N ATOM 1452 CA LEU A 239 -45.323 0.098 -50.883 1.00107.95 C ANISOU 1452 CA LEU A 239 18969 10023 12021 562 1968 -1428 C ATOM 1453 C LEU A 239 -45.481 -1.283 -50.222 1.00105.75 C ANISOU 1453 C LEU A 239 18604 9724 11851 665 1992 -1424 C ATOM 1454 O LEU A 239 -46.095 -2.163 -50.821 1.00106.32 O ANISOU 1454 O LEU A 239 18899 9691 11804 571 1999 -1450 O ATOM 1455 CB LEU A 239 -44.517 -0.053 -52.180 1.00110.52 C ANISOU 1455 CB LEU A 239 19579 10187 12226 439 2250 -1529 C ATOM 1456 CG LEU A 239 -44.315 1.229 -52.994 1.00111.38 C ANISOU 1456 CG LEU A 239 19904 10246 12167 301 2289 -1547 C ATOM 1457 CD1 LEU A 239 -43.363 0.993 -54.159 1.00113.71 C ANISOU 1457 CD1 LEU A 239 20471 10366 12366 163 2642 -1671 C ATOM 1458 CD2 LEU A 239 -45.651 1.776 -53.483 1.00111.37 C ANISOU 1458 CD2 LEU A 239 20157 10228 11928 227 1971 -1478 C ATOM 1459 N THR A 240 -44.948 -1.474 -49.011 1.00102.89 N ANISOU 1459 N THR A 240 17958 9445 11690 856 2003 -1399 N ATOM 1460 CA THR A 240 -45.006 -2.765 -48.311 1.00101.41 C ANISOU 1460 CA THR A 240 17757 9195 11575 983 2039 -1389 C ATOM 1461 C THR A 240 -45.751 -2.620 -46.978 1.00 99.25 C ANISOU 1461 C THR A 240 17300 9030 11379 1063 1826 -1298 C ATOM 1462 O THR A 240 -45.377 -1.803 -46.137 1.00 97.98 O ANISOU 1462 O THR A 240 16888 9001 11338 1178 1741 -1260 O ATOM 1463 CB THR A 240 -43.593 -3.320 -48.047 1.00102.26 C ANISOU 1463 CB THR A 240 17755 9263 11833 1190 2251 -1466 C ATOM 1464 OG1 THR A 240 -42.807 -3.227 -49.239 1.00104.04 O ANISOU 1464 OG1 THR A 240 18100 9414 12015 1095 2479 -1580 O ATOM 1465 CG2 THR A 240 -43.652 -4.780 -47.596 1.00103.09 C ANISOU 1465 CG2 THR A 240 17987 9234 11948 1324 2310 -1462 C ATOM 1466 N TYR A 241 -46.794 -3.428 -46.792 1.00 98.91 N ANISOU 1466 N TYR A 241 17391 8924 11264 980 1763 -1284 N ATOM 1467 CA TYR A 241 -47.665 -3.346 -45.618 1.00 97.52 C ANISOU 1467 CA TYR A 241 17086 8827 11137 994 1597 -1227 C ATOM 1468 C TYR A 241 -47.945 -4.713 -45.006 1.00 99.87 C ANISOU 1468 C TYR A 241 17546 8978 11419 1027 1697 -1230 C ATOM 1469 O TYR A 241 -47.636 -5.751 -45.595 1.00101.54 O ANISOU 1469 O TYR A 241 17989 9026 11565 1020 1873 -1276 O ATOM 1470 CB TYR A 241 -48.983 -2.672 -45.995 1.00 96.49 C ANISOU 1470 CB TYR A 241 16945 8795 10921 792 1394 -1250 C ATOM 1471 CG TYR A 241 -48.801 -1.220 -46.346 1.00 95.54 C ANISOU 1471 CG TYR A 241 16702 8799 10797 793 1263 -1225 C ATOM 1472 CD1 TYR A 241 -48.461 -0.831 -47.641 1.00 96.60 C ANISOU 1472 CD1 TYR A 241 17016 8879 10807 712 1315 -1264 C ATOM 1473 CD2 TYR A 241 -48.945 -0.235 -45.379 1.00 94.06 C ANISOU 1473 CD2 TYR A 241 16266 8761 10711 870 1108 -1163 C ATOM 1474 CE1 TYR A 241 -48.280 0.504 -47.963 1.00 96.92 C ANISOU 1474 CE1 TYR A 241 17021 8992 10809 704 1223 -1241 C ATOM 1475 CE2 TYR A 241 -48.766 1.103 -45.687 1.00 94.47 C ANISOU 1475 CE2 TYR A 241 16248 8902 10743 868 1007 -1140 C ATOM 1476 CZ TYR A 241 -48.434 1.470 -46.978 1.00 95.25 C ANISOU 1476 CZ TYR A 241 16560 8927 10703 785 1069 -1179 C ATOM 1477 OH TYR A 241 -48.255 2.796 -47.270 1.00 94.55 O ANISOU 1477 OH TYR A 241 16473 8887 10562 775 993 -1156 O ATOM 1478 N VAL A 242 -48.524 -4.688 -43.808 1.00 99.60 N ANISOU 1478 N VAL A 242 17422 8988 11433 1054 1602 -1184 N ATOM 1479 CA VAL A 242 -48.922 -5.890 -43.085 1.00100.77 C ANISOU 1479 CA VAL A 242 17777 8973 11536 1055 1707 -1187 C ATOM 1480 C VAL A 242 -50.320 -5.669 -42.525 1.00100.54 C ANISOU 1480 C VAL A 242 17688 9019 11493 844 1600 -1221 C ATOM 1481 O VAL A 242 -50.575 -4.625 -41.935 1.00 99.03 O ANISOU 1481 O VAL A 242 17246 8996 11384 864 1433 -1184 O ATOM 1482 CB VAL A 242 -47.958 -6.195 -41.918 1.00101.27 C ANISOU 1482 CB VAL A 242 17836 8970 11671 1362 1739 -1111 C ATOM 1483 CG1 VAL A 242 -48.322 -7.518 -41.251 1.00102.87 C ANISOU 1483 CG1 VAL A 242 18372 8940 11773 1370 1874 -1109 C ATOM 1484 CG2 VAL A 242 -46.514 -6.219 -42.406 1.00101.85 C ANISOU 1484 CG2 VAL A 242 17860 9029 11809 1595 1816 -1128 C ATOM 1485 N GLN A 243 -51.215 -6.643 -42.708 1.00102.78 N ANISOU 1485 N GLN A 243 18191 9179 11681 633 1712 -1316 N ATOM 1486 CA GLN A 243 -52.566 -6.571 -42.135 1.00103.08 C ANISOU 1486 CA GLN A 243 18159 9282 11722 404 1659 -1408 C ATOM 1487 C GLN A 243 -52.464 -6.628 -40.626 1.00101.69 C ANISOU 1487 C GLN A 243 17990 9057 11591 522 1689 -1326 C ATOM 1488 O GLN A 243 -51.860 -7.539 -40.081 1.00102.05 O ANISOU 1488 O GLN A 243 18304 8892 11576 665 1847 -1264 O ATOM 1489 CB GLN A 243 -53.471 -7.706 -42.627 1.00106.74 C ANISOU 1489 CB GLN A 243 18868 9612 12076 127 1823 -1568 C ATOM 1490 CG GLN A 243 -54.109 -7.466 -43.985 1.00108.69 C ANISOU 1490 CG GLN A 243 19051 9968 12275 -65 1718 -1709 C ATOM 1491 CD GLN A 243 -55.099 -8.559 -44.356 1.00113.07 C ANISOU 1491 CD GLN A 243 19803 10419 12737 -366 1874 -1909 C ATOM 1492 OE1 GLN A 243 -56.058 -8.815 -43.624 1.00116.56 O ANISOU 1492 OE1 GLN A 243 20208 10874 13205 -561 1931 -2037 O ATOM 1493 NE2 GLN A 243 -54.870 -9.212 -45.492 1.00113.93 N ANISOU 1493 NE2 GLN A 243 20127 10422 12739 -428 1966 -1957 N ATOM 1494 N LEU A 244 -53.051 -5.643 -39.957 1.00102.28 N ANISOU 1494 N LEU A 244 17793 9312 11755 479 1529 -1329 N ATOM 1495 CA LEU A 244 -52.913 -5.507 -38.510 1.00102.12 C ANISOU 1495 CA LEU A 244 17763 9261 11774 599 1533 -1242 C ATOM 1496 C LEU A 244 -53.909 -6.405 -37.782 1.00104.25 C ANISOU 1496 C LEU A 244 18264 9376 11969 367 1720 -1347 C ATOM 1497 O LEU A 244 -54.950 -6.773 -38.326 1.00106.88 O ANISOU 1497 O LEU A 244 18612 9722 12275 69 1790 -1527 O ATOM 1498 CB LEU A 244 -53.105 -4.045 -38.096 1.00 99.02 C ANISOU 1498 CB LEU A 244 16995 9120 11509 640 1304 -1207 C ATOM 1499 CG LEU A 244 -52.731 -3.662 -36.660 1.00 98.44 C ANISOU 1499 CG LEU A 244 16869 9047 11484 812 1267 -1094 C ATOM 1500 CD1 LEU A 244 -51.241 -3.858 -36.406 1.00 98.68 C ANISOU 1500 CD1 LEU A 244 16990 8992 11510 1151 1276 -958 C ATOM 1501 CD2 LEU A 244 -53.150 -2.228 -36.384 1.00 96.33 C ANISOU 1501 CD2 LEU A 244 16235 9028 11337 789 1056 -1092 C ATOM 1502 N GLU A 245 -53.557 -6.770 -36.556 1.00105.35 N ANISOU 1502 N GLU A 245 18603 9359 12063 502 1807 -1253 N ATOM 1503 CA GLU A 245 -54.448 -7.490 -35.655 1.00108.08 C ANISOU 1503 CA GLU A 245 19209 9532 12322 278 2012 -1343 C ATOM 1504 C GLU A 245 -54.236 -6.961 -34.241 1.00106.68 C ANISOU 1504 C GLU A 245 19013 9354 12165 431 1949 -1231 C ATOM 1505 O GLU A 245 -53.207 -6.339 -33.954 1.00105.73 O ANISOU 1505 O GLU A 245 18760 9312 12099 757 1773 -1076 O ATOM 1506 CB GLU A 245 -54.185 -8.997 -35.724 1.00111.66 C ANISOU 1506 CB GLU A 245 20189 9644 12591 272 2280 -1347 C ATOM 1507 CG GLU A 245 -54.518 -9.618 -37.076 1.00113.53 C ANISOU 1507 CG GLU A 245 20481 9862 12792 70 2377 -1481 C ATOM 1508 CD GLU A 245 -54.452 -11.137 -37.077 1.00118.80 C ANISOU 1508 CD GLU A 245 21700 10172 13266 5 2680 -1512 C ATOM 1509 OE1 GLU A 245 -54.895 -11.766 -36.088 1.00121.80 O ANISOU 1509 OE1 GLU A 245 22421 10329 13528 -115 2887 -1543 O ATOM 1510 OE2 GLU A 245 -53.965 -11.711 -38.078 1.00120.49 O ANISOU 1510 OE2 GLU A 245 22042 10308 13430 62 2730 -1512 O ATOM 1511 N SER A 246 -55.215 -7.199 -33.372 1.00106.96 N ANISOU 1511 N SER A 246 19178 9304 12158 178 2106 -1336 N ATOM 1512 CA SER A 246 -55.166 -6.717 -31.986 1.00105.72 C ANISOU 1512 CA SER A 246 19041 9127 11998 273 2073 -1249 C ATOM 1513 C SER A 246 -54.052 -7.355 -31.165 1.00106.14 C ANISOU 1513 C SER A 246 19523 8911 11892 622 2105 -1064 C ATOM 1514 O SER A 246 -53.465 -6.706 -30.300 1.00105.14 O ANISOU 1514 O SER A 246 19315 8839 11791 871 1945 -935 O ATOM 1515 CB SER A 246 -56.506 -6.950 -31.286 1.00108.13 C ANISOU 1515 CB SER A 246 19439 9366 12277 -122 2296 -1441 C ATOM 1516 OG SER A 246 -57.507 -6.108 -31.827 1.00108.17 O ANISOU 1516 OG SER A 246 18957 9675 12466 -371 2187 -1630 O ATOM 1517 N ARG A 247 -53.770 -8.623 -31.441 1.00108.16 N ANISOU 1517 N ARG A 247 20242 8875 11976 653 2299 -1064 N ATOM 1518 CA ARG A 247 -52.752 -9.370 -30.700 1.00109.93 C ANISOU 1518 CA ARG A 247 20944 8805 12019 1019 2319 -913 C ATOM 1519 C ARG A 247 -51.289 -8.967 -30.966 1.00106.65 C ANISOU 1519 C ARG A 247 20326 8507 11686 1499 2050 -774 C ATOM 1520 O ARG A 247 -50.414 -9.362 -30.194 1.00109.33 O ANISOU 1520 O ARG A 247 20972 8662 11905 1864 1987 -669 O ATOM 1521 CB ARG A 247 -52.936 -10.883 -30.909 1.00114.83 C ANISOU 1521 CB ARG A 247 22172 9046 12412 908 2623 -969 C ATOM 1522 CG ARG A 247 -52.665 -11.392 -32.319 1.00116.71 C ANISOU 1522 CG ARG A 247 22355 9304 12683 893 2660 -1021 C ATOM 1523 CD ARG A 247 -53.318 -12.748 -32.549 1.00121.64 C ANISOU 1523 CD ARG A 247 23516 9596 13106 606 3015 -1140 C ATOM 1524 NE ARG A 247 -53.170 -13.208 -33.932 1.00123.75 N ANISOU 1524 NE ARG A 247 23717 9894 13405 546 3059 -1207 N ATOM 1525 CZ ARG A 247 -52.064 -13.742 -34.461 1.00126.32 C ANISOU 1525 CZ ARG A 247 24210 10102 13684 890 3012 -1114 C ATOM 1526 NH1 ARG A 247 -52.062 -14.120 -35.739 1.00127.57 N ANISOU 1526 NH1 ARG A 247 24305 10294 13872 774 3079 -1194 N ATOM 1527 NH2 ARG A 247 -50.955 -13.899 -33.736 1.00127.95 N ANISOU 1527 NH2 ARG A 247 24635 10164 13817 1360 2890 -961 N ATOM 1528 N PHE A 248 -51.012 -8.196 -32.022 1.00101.82 N ANISOU 1528 N PHE A 248 19226 8191 11268 1506 1896 -796 N ATOM 1529 CA PHE A 248 -49.631 -7.756 -32.301 1.00 99.55 C ANISOU 1529 CA PHE A 248 18709 8033 11082 1909 1684 -713 C ATOM 1530 C PHE A 248 -49.176 -6.646 -31.350 1.00 97.65 C ANISOU 1530 C PHE A 248 18177 7981 10942 2115 1455 -635 C ATOM 1531 O PHE A 248 -49.826 -5.602 -31.250 1.00 96.20 O ANISOU 1531 O PHE A 248 17648 8025 10878 1911 1376 -652 O ATOM 1532 CB PHE A 248 -49.465 -7.246 -33.736 1.00 98.01 C ANISOU 1532 CB PHE A 248 18136 8066 11037 1819 1631 -772 C ATOM 1533 CG PHE A 248 -49.816 -8.241 -34.814 1.00 99.41 C ANISOU 1533 CG PHE A 248 18550 8092 11128 1628 1829 -857 C ATOM 1534 CD1 PHE A 248 -49.810 -9.620 -34.595 1.00101.79 C ANISOU 1534 CD1 PHE A 248 19383 8053 11239 1661 2035 -863 C ATOM 1535 CD2 PHE A 248 -50.115 -7.779 -36.088 1.00 98.44 C ANISOU 1535 CD2 PHE A 248 18147 8155 11099 1427 1804 -933 C ATOM 1536 CE1 PHE A 248 -50.131 -10.496 -35.615 1.00102.75 C ANISOU 1536 CE1 PHE A 248 19710 8044 11285 1468 2224 -950 C ATOM 1537 CE2 PHE A 248 -50.432 -8.653 -37.110 1.00 99.02 C ANISOU 1537 CE2 PHE A 248 18428 8102 11090 1248 1972 -1020 C ATOM 1538 CZ PHE A 248 -50.440 -10.012 -36.873 1.00101.60 C ANISOU 1538 CZ PHE A 248 19245 8109 11247 1258 2188 -1032 C ATOM 1539 N THR A 249 -48.050 -6.877 -30.675 1.00 97.90 N ANISOU 1539 N THR A 249 18348 7924 10926 2534 1336 -565 N ATOM 1540 CA THR A 249 -47.428 -5.891 -29.794 1.00 96.24 C ANISOU 1540 CA THR A 249 17864 7893 10807 2777 1102 -510 C ATOM 1541 C THR A 249 -46.525 -4.971 -30.620 1.00 95.16 C ANISOU 1541 C THR A 249 17204 8059 10890 2906 949 -549 C ATOM 1542 O THR A 249 -46.172 -5.319 -31.750 1.00 96.02 O ANISOU 1542 O THR A 249 17265 8176 11043 2897 1024 -607 O ATOM 1543 CB THR A 249 -46.560 -6.578 -28.727 1.00 98.46 C ANISOU 1543 CB THR A 249 18531 7949 10931 3209 1008 -455 C ATOM 1544 OG1 THR A 249 -45.576 -7.403 -29.365 1.00100.11 O ANISOU 1544 OG1 THR A 249 18869 8049 11119 3509 1006 -497 O ATOM 1545 CG2 THR A 249 -47.411 -7.437 -27.813 1.00100.08 C ANISOU 1545 CG2 THR A 249 19335 7812 10878 3076 1183 -411 C ATOM 1546 N PRO A 250 -46.142 -3.800 -30.067 1.00 93.08 N ANISOU 1546 N PRO A 250 16574 8034 10756 3006 760 -529 N ATOM 1547 CA PRO A 250 -45.135 -2.948 -30.704 1.00 92.39 C ANISOU 1547 CA PRO A 250 16036 8206 10861 3146 642 -590 C ATOM 1548 C PRO A 250 -43.824 -3.667 -31.051 1.00 96.17 C ANISOU 1548 C PRO A 250 16562 8620 11356 3509 622 -668 C ATOM 1549 O PRO A 250 -43.324 -3.505 -32.163 1.00 97.25 O ANISOU 1549 O PRO A 250 16477 8865 11606 3473 683 -754 O ATOM 1550 CB PRO A 250 -44.880 -1.868 -29.654 1.00 91.49 C ANISOU 1550 CB PRO A 250 15663 8272 10824 3255 453 -558 C ATOM 1551 CG PRO A 250 -46.161 -1.763 -28.914 1.00 90.22 C ANISOU 1551 CG PRO A 250 15680 8033 10567 2996 502 -481 C ATOM 1552 CD PRO A 250 -46.762 -3.135 -28.908 1.00 91.95 C ANISOU 1552 CD PRO A 250 16408 7935 10592 2919 685 -468 C ATOM 1553 N GLN A 251 -43.304 -4.476 -30.123 1.00 99.73 N ANISOU 1553 N GLN A 251 17331 8879 11683 3858 541 -653 N ATOM 1554 CA GLN A 251 -42.005 -5.151 -30.297 1.00102.07 C ANISOU 1554 CA GLN A 251 17656 9122 12003 4281 471 -759 C ATOM 1555 C GLN A 251 -42.077 -6.210 -31.390 1.00101.98 C ANISOU 1555 C GLN A 251 17895 8922 11929 4210 678 -795 C ATOM 1556 O GLN A 251 -41.090 -6.454 -32.085 1.00103.93 O ANISOU 1556 O GLN A 251 17986 9221 12282 4417 684 -922 O ATOM 1557 CB GLN A 251 -41.515 -5.809 -28.993 1.00106.58 C ANISOU 1557 CB GLN A 251 18585 9497 12413 4714 297 -733 C ATOM 1558 CG GLN A 251 -41.187 -4.853 -27.841 1.00108.08 C ANISOU 1558 CG GLN A 251 18541 9869 12656 4880 53 -725 C ATOM 1559 CD GLN A 251 -42.409 -4.371 -27.055 1.00108.00 C ANISOU 1559 CD GLN A 251 18678 9815 12540 4558 95 -578 C ATOM 1560 OE1 GLN A 251 -43.527 -4.852 -27.257 1.00108.13 O ANISOU 1560 OE1 GLN A 251 19007 9646 12429 4229 306 -498 O ATOM 1561 NE2 GLN A 251 -42.199 -3.401 -26.164 1.00108.42 N ANISOU 1561 NE2 GLN A 251 18483 10052 12657 4640 -93 -569 N ATOM 1562 N PHE A 252 -43.238 -6.847 -31.526 1.00 99.89 N ANISOU 1562 N PHE A 252 18011 8441 11498 3906 862 -708 N ATOM 1563 CA PHE A 252 -43.463 -7.804 -32.605 1.00 99.90 C ANISOU 1563 CA PHE A 252 18254 8269 11432 3768 1078 -744 C ATOM 1564 C PHE A 252 -43.466 -7.117 -33.963 1.00 97.99 C ANISOU 1564 C PHE A 252 17609 8260 11363 3505 1154 -816 C ATOM 1565 O PHE A 252 -42.943 -7.667 -34.929 1.00 99.75 O ANISOU 1565 O PHE A 252 17861 8429 11610 3558 1263 -897 O ATOM 1566 CB PHE A 252 -44.780 -8.559 -32.412 1.00 99.77 C ANISOU 1566 CB PHE A 252 18706 7992 11208 3448 1272 -671 C ATOM 1567 CG PHE A 252 -45.126 -9.465 -33.561 1.00100.13 C ANISOU 1567 CG PHE A 252 18976 7881 11187 3245 1502 -721 C ATOM 1568 CD1 PHE A 252 -44.453 -10.671 -33.737 1.00103.02 C ANISOU 1568 CD1 PHE A 252 19723 7982 11435 3525 1580 -750 C ATOM 1569 CD2 PHE A 252 -46.109 -9.105 -34.478 1.00 97.94 C ANISOU 1569 CD2 PHE A 252 18531 7722 10960 2796 1623 -754 C ATOM 1570 CE1 PHE A 252 -44.762 -11.506 -34.799 1.00103.87 C ANISOU 1570 CE1 PHE A 252 20046 7940 11477 3329 1803 -800 C ATOM 1571 CE2 PHE A 252 -46.424 -9.934 -35.541 1.00 99.14 C ANISOU 1571 CE2 PHE A 252 18889 7736 11042 2606 1822 -813 C ATOM 1572 CZ PHE A 252 -45.749 -11.136 -35.703 1.00102.20 C ANISOU 1572 CZ PHE A 252 19660 7856 11315 2857 1927 -831 C ATOM 1573 N LEU A 253 -44.069 -5.931 -34.035 1.00 95.23 N ANISOU 1573 N LEU A 253 16926 8143 11113 3228 1101 -788 N ATOM 1574 CA LEU A 253 -44.117 -5.164 -35.279 1.00 93.02 C ANISOU 1574 CA LEU A 253 16321 8061 10958 2985 1154 -847 C ATOM 1575 C LEU A 253 -42.720 -4.706 -35.707 1.00 93.32 C ANISOU 1575 C LEU A 253 16032 8263 11162 3226 1109 -961 C ATOM 1576 O LEU A 253 -42.392 -4.770 -36.889 1.00 93.10 O ANISOU 1576 O LEU A 253 15937 8257 11180 3131 1236 -1045 O ATOM 1577 CB LEU A 253 -45.073 -3.965 -35.155 1.00 89.95 C ANISOU 1577 CB LEU A 253 15690 7865 10619 2685 1078 -796 C ATOM 1578 CG LEU A 253 -46.563 -4.278 -34.968 1.00 88.91 C ANISOU 1578 CG LEU A 253 15784 7629 10369 2370 1149 -751 C ATOM 1579 CD1 LEU A 253 -47.333 -3.015 -34.620 1.00 86.53 C ANISOU 1579 CD1 LEU A 253 15195 7537 10144 2174 1028 -723 C ATOM 1580 CD2 LEU A 253 -47.164 -4.928 -36.204 1.00 89.26 C ANISOU 1580 CD2 LEU A 253 15993 7578 10343 2118 1310 -811 C ATOM 1581 N LEU A 254 -41.905 -4.265 -34.749 1.00 94.29 N ANISOU 1581 N LEU A 254 15956 8497 11372 3523 940 -989 N ATOM 1582 CA LEU A 254 -40.523 -3.863 -35.030 1.00 96.76 C ANISOU 1582 CA LEU A 254 15917 8982 11863 3763 903 -1155 C ATOM 1583 C LEU A 254 -39.619 -5.049 -35.405 1.00101.84 C ANISOU 1583 C LEU A 254 16725 9468 12500 4066 974 -1278 C ATOM 1584 O LEU A 254 -38.689 -4.884 -36.196 1.00103.42 O ANISOU 1584 O LEU A 254 16667 9781 12847 4124 1057 -1452 O ATOM 1585 CB LEU A 254 -39.920 -3.095 -33.845 1.00 96.61 C ANISOU 1585 CB LEU A 254 15626 9138 11941 4006 682 -1185 C ATOM 1586 CG LEU A 254 -40.593 -1.779 -33.442 1.00 94.20 C ANISOU 1586 CG LEU A 254 15096 9018 11676 3749 606 -1094 C ATOM 1587 CD1 LEU A 254 -39.837 -1.132 -32.289 1.00 94.64 C ANISOU 1587 CD1 LEU A 254 14891 9238 11826 4022 395 -1152 C ATOM 1588 CD2 LEU A 254 -40.705 -0.820 -34.618 1.00 92.70 C ANISOU 1588 CD2 LEU A 254 14652 8986 11581 3422 736 -1141 C ATOM 1589 N GLN A 255 -39.887 -6.228 -34.841 1.00105.14 N ANISOU 1589 N GLN A 255 17589 9615 12742 4252 958 -1202 N ATOM 1590 CA GLN A 255 -39.196 -7.461 -35.253 1.00109.54 C ANISOU 1590 CA GLN A 255 18391 9973 13256 4529 1039 -1301 C ATOM 1591 C GLN A 255 -39.666 -7.962 -36.620 1.00109.17 C ANISOU 1591 C GLN A 255 18502 9815 13162 4213 1299 -1304 C ATOM 1592 O GLN A 255 -38.852 -8.391 -37.438 1.00111.68 O ANISOU 1592 O GLN A 255 18756 10118 13559 4336 1408 -1453 O ATOM 1593 CB GLN A 255 -39.356 -8.566 -34.202 1.00113.27 C ANISOU 1593 CB GLN A 255 19378 10143 13512 4832 948 -1211 C ATOM 1594 CG GLN A 255 -38.505 -8.336 -32.964 1.00116.46 C ANISOU 1594 CG GLN A 255 19670 10624 13955 5294 662 -1267 C ATOM 1595 CD GLN A 255 -38.674 -9.422 -31.921 1.00120.19 C ANISOU 1595 CD GLN A 255 20747 10754 14162 5608 567 -1169 C ATOM 1596 OE1 GLN A 255 -38.310 -10.577 -32.146 1.00123.86 O ANISOU 1596 OE1 GLN A 255 21578 10965 14515 5864 620 -1214 O ATOM 1597 NE2 GLN A 255 -39.213 -9.052 -30.764 1.00120.48 N ANISOU 1597 NE2 GLN A 255 20929 10762 14083 5595 434 -1039 N ATOM 1598 N LEU A 256 -40.973 -7.920 -36.857 1.00107.40 N ANISOU 1598 N LEU A 256 18476 9519 12812 3813 1395 -1166 N ATOM 1599 CA LEU A 256 -41.546 -8.310 -38.149 1.00108.17 C ANISOU 1599 CA LEU A 256 18717 9530 12850 3483 1613 -1175 C ATOM 1600 C LEU A 256 -41.018 -7.421 -39.275 1.00108.50 C ANISOU 1600 C LEU A 256 18376 9794 13053 3332 1681 -1288 C ATOM 1601 O LEU A 256 -40.648 -7.919 -40.338 1.00110.17 O ANISOU 1601 O LEU A 256 18657 9932 13268 3289 1852 -1382 O ATOM 1602 CB LEU A 256 -43.073 -8.236 -38.093 1.00106.99 C ANISOU 1602 CB LEU A 256 18759 9325 12567 3086 1656 -1052 C ATOM 1603 CG LEU A 256 -43.880 -8.733 -39.288 1.00107.31 C ANISOU 1603 CG LEU A 256 18997 9263 12511 2734 1847 -1069 C ATOM 1604 CD1 LEU A 256 -43.664 -10.220 -39.503 1.00110.85 C ANISOU 1604 CD1 LEU A 256 19884 9408 12825 2865 2012 -1098 C ATOM 1605 CD2 LEU A 256 -45.351 -8.441 -39.063 1.00106.31 C ANISOU 1605 CD2 LEU A 256 18935 9156 12302 2372 1835 -1002 C ATOM 1606 N ASN A 257 -40.987 -6.112 -39.024 1.00107.97 N ANISOU 1606 N ASN A 257 17943 9976 13103 3244 1565 -1282 N ATOM 1607 CA ASN A 257 -40.366 -5.127 -39.921 1.00108.81 C ANISOU 1607 CA ASN A 257 17704 10284 13352 3118 1635 -1401 C ATOM 1608 C ASN A 257 -38.900 -5.471 -40.240 1.00110.65 C ANISOU 1608 C ASN A 257 17767 10544 13731 3405 1720 -1613 C ATOM 1609 O ASN A 257 -38.522 -5.582 -41.409 1.00109.91 O ANISOU 1609 O ASN A 257 17666 10429 13663 3276 1920 -1727 O ATOM 1610 CB ASN A 257 -40.456 -3.733 -39.281 1.00108.27 C ANISOU 1610 CB ASN A 257 17307 10451 13377 3053 1480 -1364 C ATOM 1611 CG ASN A 257 -39.801 -2.657 -40.119 1.00110.55 C ANISOU 1611 CG ASN A 257 17288 10923 13791 2907 1577 -1493 C ATOM 1612 OD1 ASN A 257 -40.318 -2.286 -41.167 1.00107.08 O ANISOU 1612 OD1 ASN A 257 16936 10469 13280 2602 1689 -1472 O ATOM 1613 ND2 ASN A 257 -38.662 -2.149 -39.655 1.00116.96 N ANISOU 1613 ND2 ASN A 257 17761 11901 14778 3121 1538 -1645 N ATOM 1614 N GLU A 258 -38.105 -5.634 -39.181 1.00112.38 N ANISOU 1614 N GLU A 258 17852 10810 14038 3798 1561 -1682 N ATOM 1615 CA GLU A 258 -36.697 -6.073 -39.247 1.00115.71 C ANISOU 1615 CA GLU A 258 18082 11267 14614 4162 1584 -1926 C ATOM 1616 C GLU A 258 -36.526 -7.308 -40.140 1.00116.77 C ANISOU 1616 C GLU A 258 18515 11174 14678 4210 1778 -1988 C ATOM 1617 O GLU A 258 -35.671 -7.326 -41.027 1.00117.50 O ANISOU 1617 O GLU A 258 18420 11321 14900 4216 1952 -2200 O ATOM 1618 CB GLU A 258 -36.174 -6.325 -37.809 1.00119.16 C ANISOU 1618 CB GLU A 258 18475 11721 15078 4627 1311 -1950 C ATOM 1619 CG GLU A 258 -34.997 -7.289 -37.609 1.00125.17 C ANISOU 1619 CG GLU A 258 19232 12413 15915 5131 1252 -2164 C ATOM 1620 CD GLU A 258 -33.637 -6.665 -37.873 1.00128.12 C ANISOU 1620 CD GLU A 258 19044 13062 16572 5289 1268 -2499 C ATOM 1621 OE1 GLU A 258 -32.912 -7.170 -38.758 1.00131.64 O ANISOU 1621 OE1 GLU A 258 19416 13482 17119 5355 1451 -2713 O ATOM 1622 OE2 GLU A 258 -33.285 -5.682 -37.184 1.00127.64 O ANISOU 1622 OE2 GLU A 258 18613 13244 16639 5337 1112 -2573 O ATOM 1623 N THR A 259 -37.354 -8.322 -39.897 1.00116.27 N ANISOU 1623 N THR A 259 18924 10846 14405 4220 1772 -1817 N ATOM 1624 CA THR A 259 -37.328 -9.580 -40.657 1.00117.01 C ANISOU 1624 CA THR A 259 19377 10685 14396 4255 1958 -1849 C ATOM 1625 C THR A 259 -37.702 -9.384 -42.131 1.00115.67 C ANISOU 1625 C THR A 259 19226 10517 14206 3827 2209 -1870 C ATOM 1626 O THR A 259 -37.155 -10.061 -42.996 1.00117.41 O ANISOU 1626 O THR A 259 19532 10632 14446 3871 2396 -2003 O ATOM 1627 CB THR A 259 -38.262 -10.635 -40.013 1.00116.68 C ANISOU 1627 CB THR A 259 19880 10345 14105 4292 1923 -1658 C ATOM 1628 OG1 THR A 259 -37.889 -10.830 -38.644 1.00117.47 O ANISOU 1628 OG1 THR A 259 20040 10408 14185 4706 1688 -1636 O ATOM 1629 CG2 THR A 259 -38.190 -11.969 -40.734 1.00119.02 C ANISOU 1629 CG2 THR A 259 20577 10358 14285 4346 2121 -1699 C ATOM 1630 N ILE A 260 -38.626 -8.465 -42.408 1.00113.13 N ANISOU 1630 N ILE A 260 18842 10304 13836 3434 2202 -1748 N ATOM 1631 CA ILE A 260 -39.027 -8.144 -43.788 1.00112.39 C ANISOU 1631 CA ILE A 260 18793 10216 13694 3039 2394 -1764 C ATOM 1632 C ILE A 260 -37.896 -7.456 -44.566 1.00112.75 C ANISOU 1632 C ILE A 260 18508 10417 13913 3027 2539 -1978 C ATOM 1633 O ILE A 260 -37.611 -7.836 -45.706 1.00112.60 O ANISOU 1633 O ILE A 260 18604 10307 13872 2899 2767 -2083 O ATOM 1634 CB ILE A 260 -40.344 -7.317 -43.822 1.00109.82 C ANISOU 1634 CB ILE A 260 18501 9964 13259 2674 2300 -1596 C ATOM 1635 CG1 ILE A 260 -41.526 -8.240 -43.497 1.00109.80 C ANISOU 1635 CG1 ILE A 260 18883 9764 13070 2577 2275 -1457 C ATOM 1636 CG2 ILE A 260 -40.578 -6.664 -45.184 1.00109.12 C ANISOU 1636 CG2 ILE A 260 18407 9925 13128 2324 2436 -1637 C ATOM 1637 CD1 ILE A 260 -42.803 -7.525 -43.119 1.00108.24 C ANISOU 1637 CD1 ILE A 260 18665 9658 12804 2313 2133 -1327 C ATOM 1638 N TYR A 261 -37.267 -6.452 -43.955 1.00112.17 N ANISOU 1638 N TYR A 261 18040 10571 14006 3133 2432 -2057 N ATOM 1639 CA TYR A 261 -36.163 -5.727 -44.603 1.00113.58 C ANISOU 1639 CA TYR A 261 17883 10908 14363 3088 2603 -2301 C ATOM 1640 C TYR A 261 -34.944 -6.616 -44.880 1.00118.15 C ANISOU 1640 C TYR A 261 18374 11436 15081 3383 2749 -2560 C ATOM 1641 O TYR A 261 -34.414 -6.608 -45.994 1.00120.61 O ANISOU 1641 O TYR A 261 18661 11726 15437 3220 3021 -2735 O ATOM 1642 CB TYR A 261 -35.731 -4.514 -43.779 1.00111.58 C ANISOU 1642 CB TYR A 261 17219 10911 14265 3147 2461 -2358 C ATOM 1643 CG TYR A 261 -36.407 -3.220 -44.158 1.00108.48 C ANISOU 1643 CG TYR A 261 16800 10615 13802 2763 2475 -2249 C ATOM 1644 CD1 TYR A 261 -37.600 -2.827 -43.553 1.00106.37 C ANISOU 1644 CD1 TYR A 261 16657 10350 13406 2654 2262 -1999 C ATOM 1645 CD2 TYR A 261 -35.835 -2.362 -45.096 1.00108.74 C ANISOU 1645 CD2 TYR A 261 16697 10725 13891 2515 2709 -2417 C ATOM 1646 CE1 TYR A 261 -38.213 -1.622 -43.888 1.00104.04 C ANISOU 1646 CE1 TYR A 261 16345 10139 13044 2348 2248 -1912 C ATOM 1647 CE2 TYR A 261 -36.438 -1.157 -45.436 1.00106.62 C ANISOU 1647 CE2 TYR A 261 16470 10513 13527 2193 2710 -2315 C ATOM 1648 CZ TYR A 261 -37.627 -0.791 -44.826 1.00103.90 C ANISOU 1648 CZ TYR A 261 16239 10177 13059 2132 2461 -2060 C ATOM 1649 OH TYR A 261 -38.237 0.394 -45.148 1.00101.50 O ANISOU 1649 OH TYR A 261 15988 9920 12655 1859 2434 -1968 O ATOM 1650 N THR A 262 -34.514 -7.375 -43.872 1.00120.66 N ANISOU 1650 N THR A 262 18667 11721 15456 3825 2567 -2595 N ATOM 1651 CA THR A 262 -33.326 -8.236 -43.991 1.00124.70 C ANISOU 1651 CA THR A 262 19070 12194 16113 4194 2646 -2866 C ATOM 1652 C THR A 262 -33.543 -9.462 -44.885 1.00126.18 C ANISOU 1652 C THR A 262 19672 12105 16165 4158 2846 -2846 C ATOM 1653 O THR A 262 -32.663 -9.808 -45.671 1.00128.69 O ANISOU 1653 O THR A 262 19880 12411 16604 4215 3065 -3099 O ATOM 1654 CB THR A 262 -32.822 -8.704 -42.611 1.00126.38 C ANISOU 1654 CB THR A 262 19194 12431 16392 4735 2341 -2909 C ATOM 1655 OG1 THR A 262 -33.893 -9.327 -41.894 1.00125.23 O ANISOU 1655 OG1 THR A 262 19503 12072 16004 4782 2172 -2602 O ATOM 1656 CG2 THR A 262 -32.281 -7.521 -41.807 1.00125.33 C ANISOU 1656 CG2 THR A 262 18566 12605 16445 4817 2167 -3028 C ATOM 1657 N SER A 263 -34.704 -10.109 -44.770 1.00125.45 N ANISOU 1657 N SER A 263 20044 11792 15827 4046 2792 -2570 N ATOM 1658 CA SER A 263 -35.053 -11.245 -45.644 1.00127.58 C ANISOU 1658 CA SER A 263 20744 11789 15941 3950 2994 -2535 C ATOM 1659 C SER A 263 -35.358 -10.842 -47.096 1.00127.04 C ANISOU 1659 C SER A 263 20734 11717 15818 3478 3265 -2558 C ATOM 1660 O SER A 263 -35.402 -11.704 -47.975 1.00128.94 O ANISOU 1660 O SER A 263 21265 11760 15965 3397 3470 -2595 O ATOM 1661 CB SER A 263 -36.245 -12.034 -45.083 1.00127.05 C ANISOU 1661 CB SER A 263 21158 11490 15624 3922 2884 -2266 C ATOM 1662 OG SER A 263 -36.036 -12.409 -43.730 1.00128.43 O ANISOU 1662 OG SER A 263 21377 11622 15795 4341 2642 -2223 O ATOM 1663 N GLY A 264 -35.588 -9.550 -47.339 1.00126.33 N ANISOU 1663 N GLY A 264 20419 11820 15760 3175 3260 -2533 N ATOM 1664 CA GLY A 264 -35.815 -9.030 -48.686 1.00127.06 C ANISOU 1664 CA GLY A 264 20599 11902 15775 2750 3494 -2564 C ATOM 1665 C GLY A 264 -37.219 -9.317 -49.184 1.00126.24 C ANISOU 1665 C GLY A 264 20917 11641 15407 2436 3470 -2333 C ATOM 1666 O GLY A 264 -37.395 -9.809 -50.301 1.00128.74 O ANISOU 1666 O GLY A 264 21508 11803 15601 2230 3674 -2365 O ATOM 1667 N LYS A 265 -38.215 -9.002 -48.355 1.00123.84 N ANISOU 1667 N LYS A 265 20649 11383 15019 2395 3224 -2126 N ATOM 1668 CA LYS A 265 -39.626 -9.254 -48.673 1.00121.62 C ANISOU 1668 CA LYS A 265 20706 10989 14513 2109 3167 -1947 C ATOM 1669 C LYS A 265 -40.406 -7.954 -48.902 1.00117.91 C ANISOU 1669 C LYS A 265 20142 10675 13982 1812 3043 -1855 C ATOM 1670 O LYS A 265 -41.623 -7.910 -48.707 1.00115.02 O ANISOU 1670 O LYS A 265 19917 10298 13486 1648 2892 -1717 O ATOM 1671 CB LYS A 265 -40.277 -10.088 -47.559 1.00121.46 C ANISOU 1671 CB LYS A 265 20860 10860 14426 2279 3014 -1813 C ATOM 1672 CG LYS A 265 -39.506 -11.343 -47.165 1.00124.75 C ANISOU 1672 CG LYS A 265 21423 11097 14877 2639 3092 -1888 C ATOM 1673 CD LYS A 265 -39.233 -12.260 -48.352 1.00127.33 C ANISOU 1673 CD LYS A 265 22013 11231 15132 2559 3355 -1994 C ATOM 1674 CE LYS A 265 -38.557 -13.554 -47.926 1.00129.77 C ANISOU 1674 CE LYS A 265 22519 11334 15454 2944 3416 -2063 C ATOM 1675 NZ LYS A 265 -38.342 -14.455 -49.089 1.00131.26 N ANISOU 1675 NZ LYS A 265 22979 11325 15567 2851 3684 -2164 N ATOM 1676 N ARG A 266 -39.705 -6.908 -49.338 1.00117.60 N ANISOU 1676 N ARG A 266 19879 10770 14033 1740 3120 -1956 N ATOM 1677 CA ARG A 266 -40.339 -5.635 -49.658 1.00116.77 C ANISOU 1677 CA ARG A 266 19741 10779 13845 1479 3019 -1882 C ATOM 1678 C ARG A 266 -40.876 -5.687 -51.074 1.00118.03 C ANISOU 1678 C ARG A 266 20241 10808 13794 1174 3139 -1889 C ATOM 1679 O ARG A 266 -40.490 -6.557 -51.860 1.00121.02 O ANISOU 1679 O ARG A 266 20819 11032 14129 1150 3354 -1983 O ATOM 1680 CB ARG A 266 -39.341 -4.487 -49.538 1.00117.02 C ANISOU 1680 CB ARG A 266 19449 10977 14034 1508 3085 -2000 C ATOM 1681 CG ARG A 266 -38.752 -4.312 -48.148 1.00116.67 C ANISOU 1681 CG ARG A 266 19038 11089 14199 1815 2941 -2021 C ATOM 1682 CD ARG A 266 -37.548 -3.393 -48.190 1.00117.93 C ANISOU 1682 CD ARG A 266 18863 11403 14539 1836 3082 -2222 C ATOM 1683 NE ARG A 266 -37.907 -2.048 -48.636 1.00116.94 N ANISOU 1683 NE ARG A 266 18757 11348 14325 1547 3086 -2178 N ATOM 1684 CZ ARG A 266 -37.041 -1.086 -48.961 1.00118.05 C ANISOU 1684 CZ ARG A 266 18717 11581 14555 1433 3272 -2351 C ATOM 1685 NH1 ARG A 266 -35.724 -1.291 -48.905 1.00120.77 N ANISOU 1685 NH1 ARG A 266 18775 11995 15115 1573 3476 -2619 N ATOM 1686 NH2 ARG A 266 -37.501 0.101 -49.352 1.00116.79 N ANISOU 1686 NH2 ARG A 266 18672 11437 14263 1177 3261 -2279 N ATOM 1687 N SER A 267 -41.765 -4.751 -51.390 1.00117.15 N ANISOU 1687 N SER A 267 20212 10753 13544 960 2984 -1798 N ATOM 1688 CA SER A 267 -42.302 -4.618 -52.741 1.00119.56 C ANISOU 1688 CA SER A 267 20863 10943 13618 689 3044 -1809 C ATOM 1689 C SER A 267 -41.201 -4.160 -53.694 1.00124.85 C ANISOU 1689 C SER A 267 21595 11556 14286 590 3338 -1958 C ATOM 1690 O SER A 267 -40.677 -3.053 -53.549 1.00124.12 O ANISOU 1690 O SER A 267 21336 11565 14258 567 3369 -1996 O ATOM 1691 CB SER A 267 -43.458 -3.614 -52.766 1.00117.27 C ANISOU 1691 CB SER A 267 20630 10740 13188 546 2763 -1699 C ATOM 1692 OG SER A 267 -43.939 -3.395 -54.082 1.00117.42 O ANISOU 1692 OG SER A 267 21009 10644 12958 321 2779 -1722 O ATOM 1693 N ASN A 268 -40.860 -5.020 -54.658 1.00132.04 N ANISOU 1693 N ASN A 268 22756 12294 15117 511 3580 -2057 N ATOM 1694 CA ASN A 268 -39.912 -4.675 -55.740 1.00137.69 C ANISOU 1694 CA ASN A 268 23608 12914 15791 356 3910 -2221 C ATOM 1695 C ASN A 268 -40.656 -4.475 -57.068 1.00134.51 C ANISOU 1695 C ASN A 268 23689 12352 15065 71 3918 -2187 C ATOM 1696 O ASN A 268 -40.281 -5.024 -58.101 1.00137.02 O ANISOU 1696 O ASN A 268 24285 12498 15278 -56 4178 -2294 O ATOM 1697 CB ASN A 268 -38.767 -5.702 -55.859 1.00146.12 C ANISOU 1697 CB ASN A 268 24579 13908 17031 494 4215 -2405 C ATOM 1698 CG ASN A 268 -39.253 -7.138 -55.880 1.00155.89 C ANISOU 1698 CG ASN A 268 26001 15013 18216 582 4186 -2354 C ATOM 1699 OD1 ASN A 268 -40.365 -7.421 -56.327 1.00155.12 O ANISOU 1699 OD1 ASN A 268 26207 14830 17901 427 4048 -2238 O ATOM 1700 ND2 ASN A 268 -38.415 -8.053 -55.387 1.00170.90 N ANISOU 1700 ND2 ASN A 268 27723 16894 20314 843 4312 -2463 N ATOM 1701 N THR A 269 -41.733 -3.696 -56.999 1.00129.67 N ANISOU 1701 N THR A 269 23177 11797 14293 -5 3609 -2048 N ATOM 1702 CA THR A 269 -42.476 -3.207 -58.158 1.00127.98 C ANISOU 1702 CA THR A 269 23413 11457 13753 -229 3530 -2018 C ATOM 1703 C THR A 269 -43.021 -1.836 -57.762 1.00125.07 C ANISOU 1703 C THR A 269 22990 11207 13323 -229 3258 -1919 C ATOM 1704 O THR A 269 -42.771 -1.370 -56.644 1.00122.65 O ANISOU 1704 O THR A 269 22294 11070 13233 -83 3177 -1880 O ATOM 1705 CB THR A 269 -43.646 -4.146 -58.534 1.00127.83 C ANISOU 1705 CB THR A 269 23624 11373 13572 -276 3332 -1967 C ATOM 1706 OG1 THR A 269 -44.452 -4.407 -57.379 1.00126.98 O ANISOU 1706 OG1 THR A 269 23221 11425 13601 -132 3046 -1872 O ATOM 1707 CG2 THR A 269 -43.138 -5.463 -59.086 1.00129.28 C ANISOU 1707 CG2 THR A 269 23951 11400 13768 -305 3620 -2066 C ATOM 1708 N THR A 270 -43.758 -1.192 -58.664 1.00124.71 N ANISOU 1708 N THR A 270 23349 11063 12972 -372 3105 -1883 N ATOM 1709 CA THR A 270 -44.484 0.045 -58.336 1.00122.53 C ANISOU 1709 CA THR A 270 23073 10880 12600 -341 2786 -1785 C ATOM 1710 C THR A 270 -45.748 -0.224 -57.496 1.00119.51 C ANISOU 1710 C THR A 270 22448 10670 12289 -211 2377 -1694 C ATOM 1711 O THR A 270 -46.304 0.708 -56.905 1.00115.43 O ANISOU 1711 O THR A 270 21796 10277 11783 -135 2109 -1621 O ATOM 1712 CB THR A 270 -44.905 0.820 -59.610 1.00124.44 C ANISOU 1712 CB THR A 270 23890 10935 12454 -494 2714 -1789 C ATOM 1713 OG1 THR A 270 -43.970 0.576 -60.667 1.00125.59 O ANISOU 1713 OG1 THR A 270 24381 10863 12474 -671 3121 -1900 O ATOM 1714 CG2 THR A 270 -44.988 2.333 -59.335 1.00124.23 C ANISOU 1714 CG2 THR A 270 23907 10944 12348 -470 2572 -1725 C ATOM 1715 N GLY A 271 -46.198 -1.485 -57.460 1.00119.23 N ANISOU 1715 N GLY A 271 22375 10629 12297 -203 2356 -1718 N ATOM 1716 CA GLY A 271 -47.444 -1.872 -56.799 1.00117.10 C ANISOU 1716 CA GLY A 271 21921 10495 12074 -142 2029 -1683 C ATOM 1717 C GLY A 271 -47.387 -2.035 -55.289 1.00113.80 C ANISOU 1717 C GLY A 271 21042 10247 11948 14 1983 -1623 C ATOM 1718 O GLY A 271 -46.314 -2.203 -54.700 1.00111.83 O ANISOU 1718 O GLY A 271 20587 10008 11893 112 2213 -1617 O ATOM 1719 N LYS A 272 -48.574 -2.004 -54.683 1.00112.04 N ANISOU 1719 N LYS A 272 20665 10156 11749 38 1679 -1603 N ATOM 1720 CA LYS A 272 -48.752 -2.113 -53.238 1.00109.78 C ANISOU 1720 CA LYS A 272 19995 10019 11698 163 1602 -1547 C ATOM 1721 C LYS A 272 -48.720 -3.593 -52.828 1.00109.52 C ANISOU 1721 C LYS A 272 19933 9918 11760 169 1767 -1577 C ATOM 1722 O LYS A 272 -49.338 -4.427 -53.486 1.00111.99 O ANISOU 1722 O LYS A 272 20454 10146 11949 40 1773 -1654 O ATOM 1723 CB LYS A 272 -50.085 -1.465 -52.835 1.00109.53 C ANISOU 1723 CB LYS A 272 19834 10141 11640 157 1236 -1551 C ATOM 1724 CG LYS A 272 -50.114 -0.914 -51.420 1.00108.26 C ANISOU 1724 CG LYS A 272 19303 10140 11688 286 1139 -1473 C ATOM 1725 CD LYS A 272 -51.476 -0.325 -51.074 1.00108.17 C ANISOU 1725 CD LYS A 272 19155 10280 11661 272 794 -1512 C ATOM 1726 CE LYS A 272 -51.499 0.248 -49.660 1.00106.21 C ANISOU 1726 CE LYS A 272 18558 10180 11615 387 717 -1436 C ATOM 1727 NZ LYS A 272 -52.876 0.547 -49.181 1.00105.38 N ANISOU 1727 NZ LYS A 272 18273 10225 11539 359 429 -1513 N ATOM 1728 N LEU A 273 -48.001 -3.903 -51.747 1.00108.07 N ANISOU 1728 N LEU A 273 19521 9761 11778 326 1892 -1524 N ATOM 1729 CA LEU A 273 -47.801 -5.282 -51.273 1.00108.17 C ANISOU 1729 CA LEU A 273 19564 9670 11866 383 2065 -1539 C ATOM 1730 C LEU A 273 -48.271 -5.417 -49.825 1.00107.09 C ANISOU 1730 C LEU A 273 19199 9623 11865 482 1951 -1482 C ATOM 1731 O LEU A 273 -47.759 -4.732 -48.944 1.00105.89 O ANISOU 1731 O LEU A 273 18806 9577 11851 639 1898 -1414 O ATOM 1732 CB LEU A 273 -46.319 -5.653 -51.370 1.00108.71 C ANISOU 1732 CB LEU A 273 19635 9641 12027 530 2342 -1556 C ATOM 1733 CG LEU A 273 -45.854 -7.013 -50.832 1.00109.91 C ANISOU 1733 CG LEU A 273 19838 9662 12258 673 2521 -1570 C ATOM 1734 CD1 LEU A 273 -46.625 -8.169 -51.462 1.00110.95 C ANISOU 1734 CD1 LEU A 273 20280 9638 12238 503 2594 -1622 C ATOM 1735 CD2 LEU A 273 -44.355 -7.172 -51.051 1.00111.00 C ANISOU 1735 CD2 LEU A 273 19929 9742 12504 842 2757 -1634 C ATOM 1736 N ILE A 274 -49.223 -6.319 -49.585 1.00107.81 N ANISOU 1736 N ILE A 274 19389 9663 11911 372 1936 -1525 N ATOM 1737 CA ILE A 274 -49.824 -6.508 -48.265 1.00107.47 C ANISOU 1737 CA ILE A 274 19198 9674 11962 408 1860 -1494 C ATOM 1738 C ILE A 274 -49.569 -7.941 -47.784 1.00110.35 C ANISOU 1738 C ILE A 274 19764 9839 12322 461 2083 -1499 C ATOM 1739 O ILE A 274 -50.142 -8.891 -48.321 1.00111.84 O ANISOU 1739 O ILE A 274 20189 9903 12399 286 2190 -1587 O ATOM 1740 CB ILE A 274 -51.344 -6.209 -48.302 1.00106.91 C ANISOU 1740 CB ILE A 274 19059 9721 11838 194 1651 -1586 C ATOM 1741 CG1 ILE A 274 -51.589 -4.744 -48.693 1.00106.59 C ANISOU 1741 CG1 ILE A 274 18852 9858 11786 200 1398 -1574 C ATOM 1742 CG2 ILE A 274 -51.991 -6.517 -46.954 1.00106.18 C ANISOU 1742 CG2 ILE A 274 18848 9657 11835 182 1638 -1586 C ATOM 1743 CD1 ILE A 274 -53.040 -4.393 -48.966 1.00107.19 C ANISOU 1743 CD1 ILE A 274 18860 10063 11802 31 1149 -1708 C ATOM 1744 N TRP A 275 -48.707 -8.081 -46.775 1.00111.89 N ANISOU 1744 N TRP A 275 19887 9998 12625 711 2143 -1414 N ATOM 1745 CA TRP A 275 -48.432 -9.373 -46.137 1.00114.71 C ANISOU 1745 CA TRP A 275 20479 10144 12960 826 2321 -1403 C ATOM 1746 C TRP A 275 -49.459 -9.662 -45.052 1.00116.75 C ANISOU 1746 C TRP A 275 20775 10383 13199 724 2281 -1397 C ATOM 1747 O TRP A 275 -49.681 -8.836 -44.175 1.00114.34 O ANISOU 1747 O TRP A 275 20237 10225 12981 775 2125 -1343 O ATOM 1748 CB TRP A 275 -47.037 -9.389 -45.502 1.00114.87 C ANISOU 1748 CB TRP A 275 20420 10132 13092 1186 2362 -1340 C ATOM 1749 CG TRP A 275 -45.924 -9.316 -46.488 1.00115.86 C ANISOU 1749 CG TRP A 275 20522 10246 13253 1284 2474 -1393 C ATOM 1750 CD1 TRP A 275 -45.156 -8.228 -46.780 1.00115.27 C ANISOU 1750 CD1 TRP A 275 20177 10335 13284 1356 2421 -1405 C ATOM 1751 CD2 TRP A 275 -45.445 -10.380 -47.312 1.00118.11 C ANISOU 1751 CD2 TRP A 275 21077 10333 13466 1299 2692 -1464 C ATOM 1752 NE1 TRP A 275 -44.227 -8.547 -47.740 1.00117.46 N ANISOU 1752 NE1 TRP A 275 20530 10532 13566 1399 2609 -1494 N ATOM 1753 CE2 TRP A 275 -44.383 -9.863 -48.086 1.00118.65 C ANISOU 1753 CE2 TRP A 275 21002 10464 13612 1377 2767 -1527 C ATOM 1754 CE3 TRP A 275 -45.812 -11.722 -47.475 1.00120.48 C ANISOU 1754 CE3 TRP A 275 21741 10397 13639 1237 2855 -1493 C ATOM 1755 CZ2 TRP A 275 -43.682 -10.640 -49.011 1.00121.30 C ANISOU 1755 CZ2 TRP A 275 21526 10644 13915 1405 2992 -1621 C ATOM 1756 CZ3 TRP A 275 -45.115 -12.498 -48.397 1.00122.73 C ANISOU 1756 CZ3 TRP A 275 22226 10522 13882 1280 3062 -1569 C ATOM 1757 CH2 TRP A 275 -44.060 -11.952 -49.153 1.00123.15 C ANISOU 1757 CH2 TRP A 275 22109 10653 14027 1368 3125 -1634 C ATOM 1758 N LYS A 276 -50.082 -10.836 -45.111 1.00122.64 N ANISOU 1758 N LYS A 276 21832 10937 13827 560 2450 -1468 N ATOM 1759 CA LYS A 276 -50.926 -11.315 -44.024 1.00126.14 C ANISOU 1759 CA LYS A 276 22395 11297 14234 451 2502 -1485 C ATOM 1760 C LYS A 276 -50.132 -12.302 -43.178 1.00127.82 C ANISOU 1760 C LYS A 276 22926 11246 14392 713 2663 -1401 C ATOM 1761 O LYS A 276 -49.274 -13.012 -43.693 1.00131.19 O ANISOU 1761 O LYS A 276 23558 11511 14774 879 2789 -1391 O ATOM 1762 CB LYS A 276 -52.201 -11.965 -44.562 1.00130.16 C ANISOU 1762 CB LYS A 276 23060 11757 14638 65 2607 -1656 C ATOM 1763 CG LYS A 276 -53.286 -12.102 -43.506 1.00134.65 C ANISOU 1763 CG LYS A 276 23638 12318 15202 -135 2646 -1731 C ATOM 1764 CD LYS A 276 -54.652 -12.432 -44.091 1.00139.10 C ANISOU 1764 CD LYS A 276 24203 12933 15716 -550 2699 -1968 C ATOM 1765 CE LYS A 276 -55.751 -12.214 -43.056 1.00141.42 C ANISOU 1765 CE LYS A 276 24368 13303 16060 -763 2703 -2083 C ATOM 1766 NZ LYS A 276 -57.111 -12.490 -43.598 1.00144.47 N ANISOU 1766 NZ LYS A 276 24681 13780 16431 -1173 2745 -2378 N ATOM 1767 N VAL A 277 -50.405 -12.312 -41.878 1.00130.03 N ANISOU 1767 N VAL A 277 23260 11477 14667 768 2649 -1349 N ATOM 1768 CA VAL A 277 -49.811 -13.262 -40.941 1.00134.35 C ANISOU 1768 CA VAL A 277 24192 11740 15115 1023 2776 -1273 C ATOM 1769 C VAL A 277 -50.873 -14.316 -40.630 1.00139.89 C ANISOU 1769 C VAL A 277 25309 12196 15645 716 3019 -1363 C ATOM 1770 O VAL A 277 -52.037 -13.978 -40.400 1.00138.39 O ANISOU 1770 O VAL A 277 24994 12116 15470 383 3023 -1459 O ATOM 1771 CB VAL A 277 -49.362 -12.560 -39.639 1.00133.33 C ANISOU 1771 CB VAL A 277 23908 11689 15060 1299 2601 -1157 C ATOM 1772 CG1 VAL A 277 -48.638 -13.534 -38.712 1.00135.69 C ANISOU 1772 CG1 VAL A 277 24647 11679 15229 1634 2685 -1081 C ATOM 1773 CG2 VAL A 277 -48.470 -11.364 -39.957 1.00130.47 C ANISOU 1773 CG2 VAL A 277 23078 11610 14884 1516 2377 -1110 C ATOM 1774 N ASN A 278 -50.474 -15.587 -40.624 1.00148.26 N ANISOU 1774 N ASN A 278 26866 12921 16544 823 3235 -1355 N ATOM 1775 CA ASN A 278 -51.406 -16.688 -40.360 1.00154.63 C ANISOU 1775 CA ASN A 278 28147 13444 17159 513 3524 -1454 C ATOM 1776 C ASN A 278 -51.721 -16.746 -38.858 1.00157.51 C ANISOU 1776 C ASN A 278 28743 13664 17439 547 3564 -1398 C ATOM 1777 O ASN A 278 -50.859 -16.392 -38.044 1.00155.72 O ANISOU 1777 O ASN A 278 28497 13430 17237 946 3397 -1251 O ATOM 1778 CB ASN A 278 -50.831 -18.024 -40.844 1.00158.86 C ANISOU 1778 CB ASN A 278 29195 13635 17527 634 3752 -1457 C ATOM 1779 CG ASN A 278 -50.543 -18.033 -42.340 1.00160.20 C ANISOU 1779 CG ASN A 278 29185 13921 17762 571 3748 -1524 C ATOM 1780 OD1 ASN A 278 -50.465 -16.980 -42.983 1.00156.96 O ANISOU 1780 OD1 ASN A 278 28284 13834 17518 548 3540 -1531 O ATOM 1781 ND2 ASN A 278 -50.374 -19.228 -42.899 1.00164.04 N ANISOU 1781 ND2 ASN A 278 30112 14118 18097 543 3990 -1572 N ATOM 1782 N PRO A 279 -52.947 -17.187 -38.481 1.00161.98 N ANISOU 1782 N PRO A 279 29532 14114 17900 120 3795 -1537 N ATOM 1783 CA PRO A 279 -53.331 -17.210 -37.053 1.00164.50 C ANISOU 1783 CA PRO A 279 30100 14279 18122 96 3874 -1503 C ATOM 1784 C PRO A 279 -52.429 -18.047 -36.122 1.00168.79 C ANISOU 1784 C PRO A 279 31263 14421 18445 500 3948 -1341 C ATOM 1785 O PRO A 279 -52.374 -17.769 -34.920 1.00167.39 O ANISOU 1785 O PRO A 279 31216 14173 18212 640 3890 -1253 O ATOM 1786 CB PRO A 279 -54.755 -17.789 -37.076 1.00165.83 C ANISOU 1786 CB PRO A 279 30462 14346 18201 -483 4197 -1742 C ATOM 1787 CG PRO A 279 -55.255 -17.537 -38.453 1.00164.35 C ANISOU 1787 CG PRO A 279 29863 14430 18151 -751 4141 -1907 C ATOM 1788 CD PRO A 279 -54.053 -17.659 -39.340 1.00163.12 C ANISOU 1788 CD PRO A 279 29694 14270 18014 -378 4003 -1764 C ATOM 1789 N GLU A 280 -51.743 -19.053 -36.675 1.00173.99 N ANISOU 1789 N GLU A 280 32317 14817 18973 699 4063 -1312 N ATOM 1790 CA GLU A 280 -50.841 -19.925 -35.902 1.00178.00 C ANISOU 1790 CA GLU A 280 33453 14923 19255 1144 4104 -1178 C ATOM 1791 C GLU A 280 -49.636 -19.198 -35.278 1.00177.36 C ANISOU 1791 C GLU A 280 33127 14981 19281 1727 3736 -1015 C ATOM 1792 O GLU A 280 -49.166 -19.593 -34.207 1.00179.39 O ANISOU 1792 O GLU A 280 33845 14962 19353 2065 3701 -914 O ATOM 1793 CB GLU A 280 -50.354 -21.101 -36.768 1.00179.36 C ANISOU 1793 CB GLU A 280 34038 14816 19294 1246 4286 -1206 C ATOM 1794 CG GLU A 280 -51.454 -22.090 -37.139 1.00181.77 C ANISOU 1794 CG GLU A 280 34784 14864 19415 712 4700 -1369 C ATOM 1795 CD GLU A 280 -50.939 -23.302 -37.902 1.00184.68 C ANISOU 1795 CD GLU A 280 35634 14913 19624 833 4896 -1385 C ATOM 1796 OE1 GLU A 280 -51.290 -24.440 -37.521 1.00187.60 O ANISOU 1796 OE1 GLU A 280 36740 14834 19703 700 5226 -1422 O ATOM 1797 OE2 GLU A 280 -50.184 -23.126 -38.882 1.00183.35 O ANISOU 1797 OE2 GLU A 280 35134 14921 19608 1051 4742 -1369 O ATOM 1798 N ILE A 281 -49.154 -18.143 -35.938 1.00174.47 N ANISOU 1798 N ILE A 281 32063 15030 19194 1835 3470 -1008 N ATOM 1799 CA ILE A 281 -48.022 -17.346 -35.439 1.00172.65 C ANISOU 1799 CA ILE A 281 31502 14991 19106 2335 3132 -902 C ATOM 1800 C ILE A 281 -48.475 -16.483 -34.257 1.00170.44 C ANISOU 1800 C ILE A 281 31073 14834 18850 2283 3000 -843 C ATOM 1801 O ILE A 281 -49.080 -15.429 -34.455 1.00166.10 O ANISOU 1801 O ILE A 281 29999 14623 18489 2000 2913 -879 O ATOM 1802 CB ILE A 281 -47.423 -16.444 -36.550 1.00170.39 C ANISOU 1802 CB ILE A 281 30540 15098 19102 2394 2946 -938 C ATOM 1803 CG1 ILE A 281 -46.849 -17.301 -37.686 1.00172.21 C ANISOU 1803 CG1 ILE A 281 30932 15193 19307 2483 3080 -1000 C ATOM 1804 CG2 ILE A 281 -46.339 -15.520 -35.988 1.00169.16 C ANISOU 1804 CG2 ILE A 281 29990 15170 19112 2839 2625 -872 C ATOM 1805 CD1 ILE A 281 -46.733 -16.567 -39.004 1.00170.28 C ANISOU 1805 CD1 ILE A 281 30146 15275 19276 2313 3027 -1072 C ATOM 1806 N ASP A 282 -48.171 -16.933 -33.038 1.00172.93 N ANISOU 1806 N ASP A 282 31879 14862 18961 2572 2978 -756 N ATOM 1807 CA ASP A 282 -48.602 -16.237 -31.806 1.00171.45 C ANISOU 1807 CA ASP A 282 31662 14730 18751 2525 2884 -697 C ATOM 1808 C ASP A 282 -47.795 -14.961 -31.517 1.00166.83 C ANISOU 1808 C ASP A 282 30458 14522 18405 2848 2507 -636 C ATOM 1809 O ASP A 282 -46.829 -14.650 -32.222 1.00166.43 O ANISOU 1809 O ASP A 282 30026 14674 18532 3127 2328 -649 O ATOM 1810 CB ASP A 282 -48.572 -17.190 -30.593 1.00174.88 C ANISOU 1810 CB ASP A 282 32927 14683 18836 2715 3002 -626 C ATOM 1811 CG ASP A 282 -47.163 -17.585 -30.178 1.00176.93 C ANISOU 1811 CG ASP A 282 33440 14782 19002 3412 2748 -538 C ATOM 1812 OD1 ASP A 282 -46.418 -18.110 -31.031 1.00178.26 O ANISOU 1812 OD1 ASP A 282 33595 14919 19213 3654 2726 -573 O ATOM 1813 OD2 ASP A 282 -46.809 -17.383 -28.997 1.00177.36 O ANISOU 1813 OD2 ASP A 282 33711 14740 18937 3724 2566 -454 O ATOM 1814 N THR A 283 -48.221 -14.219 -30.494 1.00163.67 N ANISOU 1814 N THR A 283 29963 14212 18010 2772 2418 -589 N ATOM 1815 CA THR A 283 -47.548 -12.985 -30.058 1.00160.12 C ANISOU 1815 CA THR A 283 28972 14100 17763 3042 2081 -536 C ATOM 1816 C THR A 283 -47.890 -12.664 -28.600 1.00160.50 C ANISOU 1816 C THR A 283 29249 14051 17680 3067 2026 -463 C ATOM 1817 O THR A 283 -47.689 -13.488 -27.708 1.00163.60 O ANISOU 1817 O THR A 283 30292 14072 17795 3296 2069 -406 O ATOM 1818 CB THR A 283 -47.946 -11.777 -30.934 1.00154.46 C ANISOU 1818 CB THR A 283 27512 13828 17346 2733 2009 -595 C ATOM 1819 OG1 THR A 283 -47.610 -12.033 -32.304 1.00153.29 O ANISOU 1819 OG1 THR A 283 27181 13759 17299 2704 2061 -662 O ATOM 1820 CG2 THR A 283 -47.231 -10.508 -30.478 1.00151.06 C ANISOU 1820 CG2 THR A 283 26563 13723 17111 2991 1694 -549 C ATOM 1821 N GLU A 287 -51.510 -12.937 -21.646 1.00164.85 N ANISOU 1821 N GLU A 287 32306 13299 17029 2203 2775 -314 N ATOM 1822 CA GLU A 287 -52.292 -11.948 -20.905 1.00162.74 C ANISOU 1822 CA GLU A 287 31747 13217 16866 1883 2816 -356 C ATOM 1823 C GLU A 287 -51.427 -11.228 -19.865 1.00158.03 C ANISOU 1823 C GLU A 287 31124 12690 16227 2353 2440 -208 C ATOM 1824 O GLU A 287 -51.704 -11.266 -18.659 1.00159.38 O ANISOU 1824 O GLU A 287 31801 12604 16152 2320 2529 -169 O ATOM 1825 CB GLU A 287 -53.517 -12.619 -20.259 1.00168.34 C ANISOU 1825 CB GLU A 287 33094 13546 17321 1354 3315 -475 C ATOM 1826 CG GLU A 287 -54.545 -13.123 -21.264 1.00169.81 C ANISOU 1826 CG GLU A 287 33154 13753 17612 798 3692 -686 C ATOM 1827 CD GLU A 287 -55.215 -11.994 -22.032 1.00166.35 C ANISOU 1827 CD GLU A 287 31738 13863 17605 474 3606 -828 C ATOM 1828 OE1 GLU A 287 -55.899 -11.162 -21.397 1.00166.99 O ANISOU 1828 OE1 GLU A 287 31544 14108 17796 220 3643 -902 O ATOM 1829 OE2 GLU A 287 -55.053 -11.934 -23.271 1.00163.18 O ANISOU 1829 OE2 GLU A 287 30867 13713 17418 487 3495 -869 O ATOM 1830 N TRP A 288 -50.377 -10.576 -20.365 1.00150.56 N ANISOU 1830 N TRP A 288 29589 12095 15520 2773 2034 -146 N ATOM 1831 CA TRP A 288 -49.399 -9.866 -19.542 1.00146.74 C ANISOU 1831 CA TRP A 288 28969 11743 15042 3260 1630 -41 C ATOM 1832 C TRP A 288 -49.261 -8.422 -20.020 1.00137.36 C ANISOU 1832 C TRP A 288 26808 11117 14266 3204 1393 -69 C ATOM 1833 O TRP A 288 -49.107 -8.173 -21.220 1.00132.88 O ANISOU 1833 O TRP A 288 25697 10829 13960 3145 1353 -124 O ATOM 1834 CB TRP A 288 -48.028 -10.552 -19.615 1.00150.48 C ANISOU 1834 CB TRP A 288 29721 12069 15385 3914 1343 21 C ATOM 1835 CG TRP A 288 -47.921 -11.846 -18.846 1.00156.25 C ANISOU 1835 CG TRP A 288 31507 12211 15648 4136 1464 80 C ATOM 1836 CD1 TRP A 288 -48.202 -12.041 -17.521 1.00158.82 C ANISOU 1836 CD1 TRP A 288 32525 12189 15630 4161 1524 146 C ATOM 1837 CD2 TRP A 288 -47.469 -13.111 -19.351 1.00159.33 C ANISOU 1837 CD2 TRP A 288 32427 12269 15841 4387 1535 80 C ATOM 1838 NE1 TRP A 288 -47.970 -13.349 -17.176 1.00164.17 N ANISOU 1838 NE1 TRP A 288 34168 12319 15889 4410 1631 191 N ATOM 1839 CE2 TRP A 288 -47.517 -14.030 -18.276 1.00165.23 C ANISOU 1839 CE2 TRP A 288 34216 12454 16108 4561 1636 152 C ATOM 1840 CE3 TRP A 288 -47.033 -13.559 -20.610 1.00159.36 C ANISOU 1840 CE3 TRP A 288 32160 12377 16012 4478 1536 23 C ATOM 1841 CZ2 TRP A 288 -47.146 -15.383 -18.420 1.00170.36 C ANISOU 1841 CZ2 TRP A 288 35655 12636 16437 4840 1727 173 C ATOM 1842 CZ3 TRP A 288 -46.664 -14.905 -20.757 1.00164.72 C ANISOU 1842 CZ3 TRP A 288 33579 12611 16394 4745 1632 38 C ATOM 1843 CH2 TRP A 288 -46.725 -15.800 -19.663 1.00169.67 C ANISOU 1843 CH2 TRP A 288 35249 12674 16540 4932 1722 113 C ATOM 1844 N ALA A 289 -49.305 -7.483 -19.075 1.00131.15 N ANISOU 1844 N ALA A 289 25851 10468 13510 3226 1245 -29 N ATOM 1845 CA ALA A 289 -49.110 -6.065 -19.374 1.00122.90 C ANISOU 1845 CA ALA A 289 23957 9920 12818 3206 1012 -46 C ATOM 1846 C ALA A 289 -47.624 -5.764 -19.573 1.00118.84 C ANISOU 1846 C ALA A 289 23127 9611 12416 3766 615 -17 C ATOM 1847 O ALA A 289 -46.766 -6.493 -19.066 1.00119.23 O ANISOU 1847 O ALA A 289 23638 9418 12244 4223 455 22 O ATOM 1848 CB ALA A 289 -49.687 -5.208 -18.259 1.00122.46 C ANISOU 1848 CB ALA A 289 23867 9918 12744 3025 1016 -26 C ATOM 1849 N PHE A 290 -47.338 -4.682 -20.304 1.00112.27 N ANISOU 1849 N PHE A 290 21521 9214 11920 3725 463 -61 N ATOM 1850 CA PHE A 290 -45.955 -4.297 -20.680 1.00109.32 C ANISOU 1850 CA PHE A 290 20729 9092 11715 4172 140 -92 C ATOM 1851 C PHE A 290 -44.926 -4.236 -19.533 1.00111.45 C ANISOU 1851 C PHE A 290 21184 9311 11851 4688 -182 -70 C ATOM 1852 O PHE A 290 -43.767 -4.617 -19.710 1.00114.67 O ANISOU 1852 O PHE A 290 21566 9735 12266 5150 -405 -127 O ATOM 1853 CB PHE A 290 -45.949 -2.970 -21.457 1.00103.87 C ANISOU 1853 CB PHE A 290 19236 8854 11375 3971 72 -146 C ATOM 1854 CG PHE A 290 -46.427 -1.776 -20.665 1.00100.70 C ANISOU 1854 CG PHE A 290 18571 8638 11051 3790 9 -116 C ATOM 1855 CD1 PHE A 290 -45.556 -1.066 -19.831 1.00100.37 C ANISOU 1855 CD1 PHE A 290 18348 8747 11039 4111 -275 -112 C ATOM 1856 CD2 PHE A 290 -47.738 -1.335 -20.778 1.00 98.22 C ANISOU 1856 CD2 PHE A 290 18156 8366 10796 3305 227 -118 C ATOM 1857 CE1 PHE A 290 -45.993 0.050 -19.121 1.00 98.13 C ANISOU 1857 CE1 PHE A 290 17826 8631 10827 3935 -321 -86 C ATOM 1858 CE2 PHE A 290 -48.181 -0.228 -20.066 1.00 96.03 C ANISOU 1858 CE2 PHE A 290 17631 8257 10599 3150 175 -101 C ATOM 1859 CZ PHE A 290 -47.310 0.469 -19.237 1.00 95.59 C ANISOU 1859 CZ PHE A 290 17430 8331 10558 3457 -90 -73 C ATOM 1860 N TRP A 291 -45.359 -3.769 -18.365 1.00110.14 N ANISOU 1860 N TRP A 291 21201 9086 11561 4614 -212 -8 N ATOM 1861 CA TRP A 291 -44.467 -3.565 -17.216 1.00110.61 C ANISOU 1861 CA TRP A 291 21413 9124 11488 5078 -544 4 C ATOM 1862 C TRP A 291 -44.064 -4.825 -16.441 1.00117.28 C ANISOU 1862 C TRP A 291 23104 9516 11941 5490 -623 49 C ATOM 1863 O TRP A 291 -43.231 -4.726 -15.535 1.00118.30 O ANISOU 1863 O TRP A 291 23379 9625 11944 5948 -953 39 O ATOM 1864 CB TRP A 291 -45.097 -2.575 -16.232 1.00106.54 C ANISOU 1864 CB TRP A 291 20815 8698 10967 4839 -541 55 C ATOM 1865 CG TRP A 291 -46.285 -3.117 -15.492 1.00104.84 C ANISOU 1865 CG TRP A 291 21260 8106 10468 4506 -234 132 C ATOM 1866 CD1 TRP A 291 -46.271 -3.917 -14.391 1.00107.05 C ANISOU 1866 CD1 TRP A 291 22354 7964 10354 4709 -236 198 C ATOM 1867 CD2 TRP A 291 -47.659 -2.888 -15.806 1.00101.19 C ANISOU 1867 CD2 TRP A 291 20705 7650 10089 3905 129 119 C ATOM 1868 NE1 TRP A 291 -47.550 -4.205 -14.001 1.00106.62 N ANISOU 1868 NE1 TRP A 291 22732 7644 10136 4230 149 225 N ATOM 1869 CE2 TRP A 291 -48.425 -3.586 -14.853 1.00102.93 C ANISOU 1869 CE2 TRP A 291 21682 7450 9973 3733 374 161 C ATOM 1870 CE3 TRP A 291 -48.319 -2.154 -16.799 1.00 97.20 C ANISOU 1870 CE3 TRP A 291 19563 7462 9904 3505 266 56 C ATOM 1871 CZ2 TRP A 291 -49.822 -3.569 -14.857 1.00102.12 C ANISOU 1871 CZ2 TRP A 291 21656 7263 9880 3152 768 109 C ATOM 1872 CZ3 TRP A 291 -49.705 -2.138 -16.807 1.00 96.08 C ANISOU 1872 CZ3 TRP A 291 19496 7244 9767 2977 606 12 C ATOM 1873 CH2 TRP A 291 -50.444 -2.845 -15.844 1.00 98.66 C ANISOU 1873 CH2 TRP A 291 20522 7176 9788 2793 864 23 C ATOM 1874 N GLU A 292 -44.673 -5.977 -16.750 1.00122.84 N ANISOU 1874 N GLU A 292 24392 9848 12433 5329 -329 87 N ATOM 1875 CA GLU A 292 -44.365 -7.254 -16.049 1.00131.46 C ANISOU 1875 CA GLU A 292 26408 10437 13101 5705 -363 138 C ATOM 1876 C GLU A 292 -43.649 -8.321 -16.905 1.00136.08 C ANISOU 1876 C GLU A 292 27166 10883 13655 6041 -400 86 C ATOM 1877 O GLU A 292 -43.179 -9.326 -16.366 1.00140.43 O ANISOU 1877 O GLU A 292 28443 11044 13869 6468 -508 113 O ATOM 1878 CB GLU A 292 -45.609 -7.834 -15.329 1.00133.14 C ANISOU 1878 CB GLU A 292 27402 10208 12975 5295 20 224 C ATOM 1879 CG GLU A 292 -46.923 -7.890 -16.110 1.00131.16 C ANISOU 1879 CG GLU A 292 27010 9969 12853 4605 488 191 C ATOM 1880 CD GLU A 292 -48.125 -8.228 -15.231 1.00132.81 C ANISOU 1880 CD GLU A 292 27881 9808 12773 4169 864 220 C ATOM 1881 OE1 GLU A 292 -49.271 -7.953 -15.655 1.00131.64 O ANISOU 1881 OE1 GLU A 292 27473 9760 12782 3577 1206 149 O ATOM 1882 OE2 GLU A 292 -47.939 -8.761 -14.117 1.00136.23 O ANISOU 1882 OE2 GLU A 292 29099 9844 12816 4414 824 291 O ATOM 1883 N THR A 293 -43.551 -8.089 -18.216 1.00138.12 N ANISOU 1883 N THR A 293 26788 11443 14246 5867 -320 7 N ATOM 1884 CA THR A 293 -42.727 -8.907 -19.117 1.00142.78 C ANISOU 1884 CA THR A 293 27379 11989 14880 6201 -385 -70 C ATOM 1885 C THR A 293 -41.400 -8.198 -19.399 1.00143.70 C ANISOU 1885 C THR A 293 26782 12523 15295 6636 -771 -209 C ATOM 1886 O THR A 293 -41.342 -6.965 -19.482 1.00139.99 O ANISOU 1886 O THR A 293 25621 12461 15108 6464 -860 -251 O ATOM 1887 CB THR A 293 -43.450 -9.172 -20.456 1.00141.27 C ANISOU 1887 CB THR A 293 26978 11845 14852 5717 -24 -92 C ATOM 1888 OG1 THR A 293 -44.007 -7.949 -20.957 1.00134.88 O ANISOU 1888 OG1 THR A 293 25437 11447 14365 5266 52 -113 O ATOM 1889 CG2 THR A 293 -44.567 -10.198 -20.273 1.00143.53 C ANISOU 1889 CG2 THR A 293 28047 11666 14819 5367 365 -16 C ATOM 1890 N SER A 303 -35.553 -13.750 -35.083 1.00190.43 N ANISOU 1890 N SER A 303 30261 18995 23099 6727 968 -1783 N ATOM 1891 CA SER A 303 -34.914 -14.861 -35.785 1.00195.69 C ANISOU 1891 CA SER A 303 31142 19459 23750 6996 1083 -1925 C ATOM 1892 C SER A 303 -35.485 -15.034 -37.200 1.00195.88 C ANISOU 1892 C SER A 303 31188 19446 23790 6481 1449 -1899 C ATOM 1893 O SER A 303 -36.411 -14.316 -37.594 1.00191.63 O ANISOU 1893 O SER A 303 30525 19029 23256 5944 1582 -1769 O ATOM 1894 CB SER A 303 -35.060 -16.154 -34.970 1.00197.62 C ANISOU 1894 CB SER A 303 32157 19259 23670 7385 998 -1818 C ATOM 1895 OG SER A 303 -36.422 -16.479 -34.746 1.00194.91 O ANISOU 1895 OG SER A 303 32355 18653 23049 6966 1178 -1554 O ATOM 1896 N GLU A 304 -34.908 -15.970 -37.959 1.00200.97 N ANISOU 1896 N GLU A 304 31989 19926 24442 6672 1590 -2039 N ATOM 1897 CA GLU A 304 -35.365 -16.308 -39.316 1.00201.70 C ANISOU 1897 CA GLU A 304 32177 19938 24519 6238 1934 -2032 C ATOM 1898 C GLU A 304 -35.934 -17.736 -39.372 1.00203.05 C ANISOU 1898 C GLU A 304 33103 19655 24389 6265 2093 -1912 C ATOM 1899 O GLU A 304 -35.355 -18.637 -39.994 1.00201.34 O ANISOU 1899 O GLU A 304 33066 19264 24167 6481 2218 -2041 O ATOM 1900 CB GLU A 304 -34.222 -16.137 -40.325 1.00204.41 C ANISOU 1900 CB GLU A 304 32045 20480 25140 6349 2038 -2323 C ATOM 1901 CG GLU A 304 -33.737 -14.701 -40.472 1.00202.04 C ANISOU 1901 CG GLU A 304 31030 20610 25126 6199 1976 -2462 C ATOM 1902 CD GLU A 304 -32.666 -14.532 -41.540 1.00203.55 C ANISOU 1902 CD GLU A 304 30783 20976 25580 6224 2155 -2777 C ATOM 1903 OE1 GLU A 304 -32.201 -15.543 -42.115 1.00204.96 O ANISOU 1903 OE1 GLU A 304 31170 20960 25743 6422 2294 -2905 O ATOM 1904 OE2 GLU A 304 -32.287 -13.372 -41.807 1.00201.19 O ANISOU 1904 OE2 GLU A 304 29944 21000 25499 6028 2179 -2909 O ATOM 1905 N GLU A 305 -37.068 -17.916 -38.694 1.00201.81 N ANISOU 1905 N GLU A 305 33387 19306 23983 6034 2105 -1681 N ATOM 1906 CA GLU A 305 -37.849 -19.162 -38.715 1.00201.61 C ANISOU 1906 CA GLU A 305 34112 18845 23645 5918 2312 -1557 C ATOM 1907 C GLU A 305 -39.084 -19.079 -39.628 1.00196.17 C ANISOU 1907 C GLU A 305 33490 18154 22890 5227 2605 -1466 C ATOM 1908 O GLU A 305 -39.508 -20.098 -40.181 1.00196.46 O ANISOU 1908 O GLU A 305 34000 17896 22749 5071 2850 -1451 O ATOM 1909 CB GLU A 305 -38.285 -19.528 -37.292 1.00203.74 C ANISOU 1909 CB GLU A 305 34904 18856 23651 6119 2166 -1401 C ATOM 1910 CG GLU A 305 -37.132 -19.876 -36.358 1.00207.99 C ANISOU 1910 CG GLU A 305 35553 19302 24169 6864 1857 -1490 C ATOM 1911 CD GLU A 305 -37.543 -19.913 -34.895 1.00209.07 C ANISOU 1911 CD GLU A 305 36124 19250 24061 7036 1670 -1333 C ATOM 1912 OE1 GLU A 305 -38.016 -18.877 -34.378 1.00205.19 O ANISOU 1912 OE1 GLU A 305 35307 19007 23647 6789 1568 -1252 O ATOM 1913 OE2 GLU A 305 -37.381 -20.975 -34.258 1.00213.31 O ANISOU 1913 OE2 GLU A 305 37360 19373 24312 7427 1627 -1294 O ATOM 1914 N LEU A 306 -39.654 -17.878 -39.777 1.00189.14 N ANISOU 1914 N LEU A 306 32138 17588 22136 4833 2564 -1421 N ATOM 1915 CA LEU A 306 -40.843 -17.658 -40.612 1.00183.54 C ANISOU 1915 CA LEU A 306 31429 16925 21380 4210 2774 -1363 C ATOM 1916 C LEU A 306 -40.507 -17.734 -42.098 1.00180.63 C ANISOU 1916 C LEU A 306 30878 16631 21120 4039 2958 -1487 C ATOM 1917 O LEU A 306 -39.381 -17.433 -42.501 1.00179.22 O ANISOU 1917 O LEU A 306 30347 16609 21138 4304 2908 -1626 O ATOM 1918 CB LEU A 306 -41.469 -16.289 -40.319 1.00180.35 C ANISOU 1918 CB LEU A 306 30577 16850 21094 3911 2633 -1295 C ATOM 1919 CG LEU A 306 -41.922 -15.993 -38.886 1.00180.32 C ANISOU 1919 CG LEU A 306 30686 16823 21004 3993 2462 -1174 C ATOM 1920 CD1 LEU A 306 -42.375 -14.544 -38.766 1.00175.88 C ANISOU 1920 CD1 LEU A 306 29601 16621 20602 3726 2324 -1138 C ATOM 1921 CD2 LEU A 306 -43.028 -16.945 -38.453 1.00182.05 C ANISOU 1921 CD2 LEU A 306 31530 16698 20942 3760 2644 -1085 C ATOM 1922 N SER A 307 -41.498 -18.124 -42.900 1.00178.54 N ANISOU 1922 N SER A 307 30852 16258 20725 3581 3179 -1460 N ATOM 1923 CA SER A 307 -41.345 -18.283 -44.350 1.00178.80 C ANISOU 1923 CA SER A 307 30812 16318 20805 3364 3375 -1565 C ATOM 1924 C SER A 307 -42.443 -17.519 -45.094 1.00176.51 C ANISOU 1924 C SER A 307 30332 16220 20512 2809 3414 -1537 C ATOM 1925 O SER A 307 -43.630 -17.720 -44.831 1.00175.96 O ANISOU 1925 O SER A 307 30491 16070 20296 2495 3455 -1469 O ATOM 1926 CB SER A 307 -41.391 -19.764 -44.728 1.00180.72 C ANISOU 1926 CB SER A 307 31632 16179 20854 3405 3612 -1594 C ATOM 1927 OG SER A 307 -42.583 -20.371 -44.268 1.00180.73 O ANISOU 1927 OG SER A 307 32090 15956 20622 3127 3715 -1498 O ATOM 1928 N PHE A 308 -42.027 -16.659 -46.026 1.00175.63 N ANISOU 1928 N PHE A 308 29823 16352 20555 2697 3407 -1614 N ATOM 1929 CA PHE A 308 -42.918 -15.756 -46.762 1.00173.30 C ANISOU 1929 CA PHE A 308 29323 16262 20260 2247 3385 -1599 C ATOM 1930 C PHE A 308 -43.053 -16.209 -48.216 1.00171.15 C ANISOU 1930 C PHE A 308 29220 15900 19906 1983 3597 -1687 C ATOM 1931 O PHE A 308 -42.049 -16.536 -48.851 1.00172.96 O ANISOU 1931 O PHE A 308 29446 16071 20200 2156 3730 -1788 O ATOM 1932 CB PHE A 308 -42.347 -14.333 -46.732 1.00173.73 C ANISOU 1932 CB PHE A 308 28860 16635 20513 2309 3218 -1615 C ATOM 1933 CG PHE A 308 -42.270 -13.731 -45.353 1.00176.08 C ANISOU 1933 CG PHE A 308 28951 17056 20894 2529 2992 -1533 C ATOM 1934 CD1 PHE A 308 -43.260 -12.859 -44.901 1.00176.05 C ANISOU 1934 CD1 PHE A 308 28797 17214 20878 2289 2840 -1440 C ATOM 1935 CD2 PHE A 308 -41.204 -14.026 -44.506 1.00179.59 C ANISOU 1935 CD2 PHE A 308 29350 17458 21427 2994 2917 -1567 C ATOM 1936 CE1 PHE A 308 -43.193 -12.300 -43.630 1.00176.12 C ANISOU 1936 CE1 PHE A 308 28632 17328 20956 2479 2645 -1365 C ATOM 1937 CE2 PHE A 308 -41.132 -13.472 -43.234 1.00180.80 C ANISOU 1937 CE2 PHE A 308 29336 17721 21639 3200 2696 -1496 C ATOM 1938 CZ PHE A 308 -42.127 -12.607 -42.795 1.00178.47 C ANISOU 1938 CZ PHE A 308 28910 17576 21325 2928 2573 -1387 C ATOM 1939 N THR A 309 -44.283 -16.225 -48.737 1.00167.61 N ANISOU 1939 N THR A 309 28909 15451 19323 1568 3625 -1674 N ATOM 1940 CA THR A 309 -44.555 -16.619 -50.132 1.00167.56 C ANISOU 1940 CA THR A 309 29087 15367 19209 1283 3798 -1762 C ATOM 1941 C THR A 309 -45.712 -15.803 -50.729 1.00165.30 C ANISOU 1941 C THR A 309 28677 15267 18861 879 3673 -1769 C ATOM 1942 O THR A 309 -46.732 -15.598 -50.069 1.00161.83 O ANISOU 1942 O THR A 309 28202 14897 18388 727 3546 -1732 O ATOM 1943 CB THR A 309 -44.890 -18.126 -50.248 1.00169.60 C ANISOU 1943 CB THR A 309 29844 15302 19294 1226 4022 -1794 C ATOM 1944 OG1 THR A 309 -45.896 -18.473 -49.289 1.00169.53 O ANISOU 1944 OG1 THR A 309 30008 15215 19187 1107 3984 -1739 O ATOM 1945 CG2 THR A 309 -43.652 -18.992 -50.013 1.00170.64 C ANISOU 1945 CG2 THR A 309 30148 15220 19464 1646 4156 -1820 C ATOM 1946 N VAL A 310 -45.548 -15.364 -51.982 1.00167.26 N ANISOU 1946 N VAL A 310 28883 15584 19083 718 3712 -1836 N ATOM 1947 CA VAL A 310 -46.508 -14.470 -52.659 1.00167.70 C ANISOU 1947 CA VAL A 310 28833 15819 19066 402 3547 -1855 C ATOM 1948 C VAL A 310 -47.624 -15.276 -53.334 1.00170.15 C ANISOU 1948 C VAL A 310 29442 16017 19190 75 3613 -1943 C ATOM 1949 O VAL A 310 -47.365 -16.024 -54.280 1.00174.88 O ANISOU 1949 O VAL A 310 30310 16448 19685 -6 3811 -2015 O ATOM 1950 CB VAL A 310 -45.818 -13.577 -53.727 1.00167.45 C ANISOU 1950 CB VAL A 310 28691 15883 19049 375 3558 -1892 C ATOM 1951 CG1 VAL A 310 -46.817 -12.599 -54.349 1.00165.72 C ANISOU 1951 CG1 VAL A 310 28413 15827 18723 107 3339 -1903 C ATOM 1952 CG2 VAL A 310 -44.632 -12.823 -53.128 1.00167.57 C ANISOU 1952 CG2 VAL A 310 28395 16011 19262 668 3540 -1858 C ATOM 1953 N VAL A 311 -48.860 -15.103 -52.860 1.00169.23 N ANISOU 1953 N VAL A 311 29259 16002 19038 -121 3455 -1962 N ATOM 1954 CA VAL A 311 -50.013 -15.845 -53.382 1.00170.12 C ANISOU 1954 CA VAL A 311 29598 16044 18996 -453 3506 -2095 C ATOM 1955 C VAL A 311 -50.538 -15.165 -54.646 1.00168.44 C ANISOU 1955 C VAL A 311 29346 15970 18681 -671 3346 -2187 C ATOM 1956 O VAL A 311 -51.135 -14.092 -54.586 1.00164.86 O ANISOU 1956 O VAL A 311 28638 15742 18257 -722 3072 -2194 O ATOM 1957 CB VAL A 311 -51.145 -15.971 -52.329 1.00170.01 C ANISOU 1957 CB VAL A 311 29507 16087 19001 -596 3428 -2135 C ATOM 1958 CG1 VAL A 311 -52.335 -16.744 -52.898 1.00171.83 C ANISOU 1958 CG1 VAL A 311 29934 16264 19089 -971 3503 -2330 C ATOM 1959 CG2 VAL A 311 -50.625 -16.644 -51.062 1.00170.22 C ANISOU 1959 CG2 VAL A 311 29661 15934 19080 -369 3583 -2033 C ATOM 1960 N UNK A 471 -52.248 -4.038 -56.618 1.00138.82 N ATOM 1961 CA UNK A 471 -52.260 -4.758 -55.348 1.00139.71 C ATOM 1962 C UNK A 471 -51.787 -6.203 -55.521 1.00138.41 C ATOM 1963 O UNK A 471 -51.883 -6.772 -56.612 1.00137.52 O ATOM 1964 CB UNK A 471 -53.655 -4.725 -54.737 1.00138.44 C ATOM 1965 N UNK A 472 -51.274 -6.784 -54.438 1.00136.18 N ATOM 1966 CA UNK A 472 -50.793 -8.169 -54.439 1.00133.93 C ATOM 1967 C UNK A 472 -50.690 -8.715 -53.011 1.00133.63 C ATOM 1968 O UNK A 472 -49.707 -8.459 -52.312 1.00134.32 O ATOM 1969 CB UNK A 472 -49.445 -8.258 -55.145 1.00131.94 C ATOM 1970 N UNK A 473 -51.711 -9.462 -52.589 1.00132.59 N ATOM 1971 CA UNK A 473 -51.752 -10.060 -51.247 1.00129.98 C ATOM 1972 C UNK A 473 -50.787 -11.242 -51.124 1.00129.74 C ATOM 1973 O UNK A 473 -50.341 -11.804 -52.129 1.00130.10 O ATOM 1974 CB UNK A 473 -53.170 -10.498 -50.901 1.00126.78 C ATOM 1975 N UNK A 474 -50.471 -11.607 -49.883 1.00128.79 N ATOM 1976 CA UNK A 474 -49.562 -12.723 -49.600 1.00128.30 C ATOM 1977 C UNK A 474 -49.684 -13.213 -48.155 1.00128.00 C ATOM 1978 O UNK A 474 -50.307 -12.554 -47.318 1.00129.81 O ATOM 1979 CB UNK A 474 -48.126 -12.317 -49.901 1.00127.66 C ATOM 1980 N UNK A 475 -49.084 -14.371 -47.880 1.00126.56 N ATOM 1981 CA UNK A 475 -49.129 -15.001 -46.558 1.00124.79 C ATOM 1982 C UNK A 475 -47.722 -15.200 -45.987 1.00124.72 C ATOM 1983 O UNK A 475 -46.753 -15.352 -46.734 1.00121.37 O ATOM 1984 CB UNK A 475 -49.861 -16.332 -46.639 1.00122.82 C ATOM 1985 N UNK A 476 -47.632 -15.183 -44.657 1.00128.93 N ATOM 1986 CA UNK A 476 -46.397 -15.462 -43.921 1.00132.87 C ATOM 1987 C UNK A 476 -46.686 -16.578 -42.916 1.00138.35 C ATOM 1988 O UNK A 476 -47.547 -16.416 -42.048 1.00143.52 O ATOM 1989 CB UNK A 476 -45.916 -14.210 -43.204 1.00132.16 C ATOM 1990 N UNK A 477 -45.977 -17.703 -43.043 1.00139.66 N ATOM 1991 CA UNK A 477 -46.223 -18.896 -42.222 1.00136.39 C ATOM 1992 C UNK A 477 -44.915 -19.485 -41.707 1.00134.92 C ATOM 1993 O UNK A 477 -44.325 -18.974 -40.756 1.00132.97 O ATOM 1994 CB UNK A 477 -46.988 -19.936 -43.028 1.00134.99 C TER 1995 UNK A 477 ATOM 1996 N GLU B 502 -63.723 9.707 2.204 1.00111.19 N ANISOU 1996 N GLU B 502 15363 12336 14548 -2265 1353 220 N ATOM 1997 CA GLU B 502 -63.837 8.274 1.771 1.00111.61 C ANISOU 1997 CA GLU B 502 15647 12250 14509 -2416 1357 255 C ATOM 1998 C GLU B 502 -62.476 7.582 1.666 1.00109.34 C ANISOU 1998 C GLU B 502 15607 11727 14208 -2264 1239 330 C ATOM 1999 O GLU B 502 -61.436 8.239 1.657 1.00108.34 O ANISOU 1999 O GLU B 502 15425 11566 14171 -2036 1148 351 O ATOM 2000 CB GLU B 502 -64.548 8.171 0.417 1.00112.89 C ANISOU 2000 CB GLU B 502 15642 12505 14745 -2487 1373 210 C ATOM 2001 CG GLU B 502 -65.988 8.650 0.417 1.00115.80 C ANISOU 2001 CG GLU B 502 15772 13111 15115 -2657 1487 131 C ATOM 2002 CD GLU B 502 -66.665 8.446 -0.928 1.00117.66 C ANISOU 2002 CD GLU B 502 15865 13424 15414 -2733 1489 89 C ATOM 2003 OE1 GLU B 502 -67.789 7.899 -0.955 1.00121.49 O ANISOU 2003 OE1 GLU B 502 16332 14003 15823 -2976 1577 54 O ATOM 2004 OE2 GLU B 502 -66.073 8.825 -1.962 1.00116.64 O ANISOU 2004 OE2 GLU B 502 15643 13266 15405 -2556 1402 92 O ATOM 2005 N ALA B 503 -62.507 6.252 1.582 1.00108.63 N ANISOU 2005 N ALA B 503 15791 11481 14001 -2393 1238 368 N ATOM 2006 CA ALA B 503 -61.313 5.439 1.320 1.00105.91 C ANISOU 2006 CA ALA B 503 15692 10911 13634 -2249 1125 431 C ATOM 2007 C ALA B 503 -61.181 5.122 -0.176 1.00101.90 C ANISOU 2007 C ALA B 503 15126 10379 13212 -2192 1081 420 C ATOM 2008 O ALA B 503 -62.179 5.118 -0.906 1.00101.32 O ANISOU 2008 O ALA B 503 14916 10419 13161 -2341 1145 374 O ATOM 2009 CB ALA B 503 -61.366 4.155 2.128 1.00108.12 C ANISOU 2009 CB ALA B 503 16345 11011 13723 -2404 1138 479 C ATOM 2010 N ILE B 504 -59.949 4.857 -0.615 1.00 96.95 N ANISOU 2010 N ILE B 504 14600 9609 12625 -1976 972 460 N ATOM 2011 CA ILE B 504 -59.639 4.568 -2.023 1.00 93.11 C ANISOU 2011 CA ILE B 504 14076 9086 12215 -1887 924 453 C ATOM 2012 C ILE B 504 -59.484 3.065 -2.247 1.00 91.34 C ANISOU 2012 C ILE B 504 14194 8648 11859 -1956 893 488 C ATOM 2013 O ILE B 504 -58.488 2.469 -1.843 1.00 91.18 O ANISOU 2013 O ILE B 504 14408 8455 11779 -1821 814 536 O ATOM 2014 CB ILE B 504 -58.342 5.285 -2.472 1.00 90.99 C ANISOU 2014 CB ILE B 504 13677 8813 12080 -1591 827 469 C ATOM 2015 CG1 ILE B 504 -58.493 6.809 -2.343 1.00 90.13 C ANISOU 2015 CG1 ILE B 504 13242 8903 12100 -1525 848 433 C ATOM 2016 CG2 ILE B 504 -57.958 4.899 -3.899 1.00 89.02 C ANISOU 2016 CG2 ILE B 504 13417 8515 11891 -1494 783 464 C ATOM 2017 CD1 ILE B 504 -59.602 7.401 -3.183 1.00 89.29 C ANISOU 2017 CD1 ILE B 504 12887 8970 12067 -1636 917 372 C ATOM 2018 N VAL B 505 -60.468 2.472 -2.912 1.00 89.61 N ANISOU 2018 N VAL B 505 14006 8445 11596 -2161 949 461 N ATOM 2019 CA VAL B 505 -60.460 1.051 -3.250 1.00 90.10 C ANISOU 2019 CA VAL B 505 14398 8306 11529 -2254 922 488 C ATOM 2020 C VAL B 505 -60.113 0.905 -4.730 1.00 87.89 C ANISOU 2020 C VAL B 505 14058 8001 11334 -2130 870 470 C ATOM 2021 O VAL B 505 -60.951 1.206 -5.592 1.00 88.12 O ANISOU 2021 O VAL B 505 13895 8162 11425 -2240 916 424 O ATOM 2022 CB VAL B 505 -61.849 0.419 -2.989 1.00 91.37 C ANISOU 2022 CB VAL B 505 14651 8498 11564 -2602 1020 469 C ATOM 2023 CG1 VAL B 505 -61.846 -1.070 -3.331 1.00 93.34 C ANISOU 2023 CG1 VAL B 505 15274 8521 11667 -2713 985 499 C ATOM 2024 CG2 VAL B 505 -62.278 0.663 -1.547 1.00 91.89 C ANISOU 2024 CG2 VAL B 505 14746 8621 11547 -2735 1091 479 C ATOM 2025 N ASN B 506 -58.894 0.451 -5.035 1.00 85.69 N ANISOU 2025 N ASN B 506 13940 7561 11056 -1898 775 504 N ATOM 2026 CA ASN B 506 -58.515 0.188 -6.432 1.00 83.66 C ANISOU 2026 CA ASN B 506 13664 7262 10858 -1777 729 489 C ATOM 2027 C ASN B 506 -59.406 -0.909 -7.023 1.00 83.62 C ANISOU 2027 C ASN B 506 13866 7165 10741 -2006 756 475 C ATOM 2028 O ASN B 506 -59.428 -2.033 -6.522 1.00 85.34 O ANISOU 2028 O ASN B 506 14427 7195 10801 -2106 739 507 O ATOM 2029 CB ASN B 506 -57.034 -0.169 -6.583 1.00 82.90 C ANISOU 2029 CB ASN B 506 13713 7016 10769 -1482 628 524 C ATOM 2030 CG ASN B 506 -56.578 -0.137 -8.040 1.00 83.15 C ANISOU 2030 CG ASN B 506 13648 7055 10888 -1326 594 500 C ATOM 2031 OD1 ASN B 506 -57.020 -0.953 -8.853 1.00 84.67 O ANISOU 2031 OD1 ASN B 506 13989 7162 11017 -1422 598 485 O ATOM 2032 ND2 ASN B 506 -55.701 0.810 -8.381 1.00 80.80 N ANISOU 2032 ND2 ASN B 506 13108 6860 10729 -1095 563 497 N ATOM 2033 N ALA B 507 -60.146 -0.549 -8.073 1.00 82.78 N ANISOU 2033 N ALA B 507 13551 7188 10711 -2093 792 428 N ATOM 2034 CA ALA B 507 -61.120 -1.425 -8.732 1.00 84.95 C ANISOU 2034 CA ALA B 507 13963 7415 10898 -2334 818 406 C ATOM 2035 C ALA B 507 -60.815 -1.541 -10.226 1.00 83.21 C ANISOU 2035 C ALA B 507 13704 7169 10743 -2209 771 382 C ATOM 2036 O ALA B 507 -61.732 -1.684 -11.038 1.00 83.64 O ANISOU 2036 O ALA B 507 13696 7285 10797 -2380 798 344 O ATOM 2037 CB ALA B 507 -62.532 -0.880 -8.528 1.00 85.42 C ANISOU 2037 CB ALA B 507 13792 7685 10975 -2602 913 363 C ATOM 2038 N GLN B 508 -59.527 -1.480 -10.575 1.00 81.51 N ANISOU 2038 N GLN B 508 13522 6869 10578 -1912 702 403 N ATOM 2039 CA GLN B 508 -59.073 -1.588 -11.961 1.00 79.55 C ANISOU 2039 CA GLN B 508 13250 6589 10385 -1761 660 383 C ATOM 2040 C GLN B 508 -58.616 -3.023 -12.254 1.00 80.00 C ANISOU 2040 C GLN B 508 13709 6389 10298 -1726 601 404 C ATOM 2041 O GLN B 508 -58.219 -3.747 -11.338 1.00 80.69 O ANISOU 2041 O GLN B 508 14069 6316 10270 -1715 572 443 O ATOM 2042 CB GLN B 508 -57.924 -0.612 -12.224 1.00 77.13 C ANISOU 2042 CB GLN B 508 12718 6366 10220 -1457 627 389 C ATOM 2043 CG GLN B 508 -58.230 0.839 -11.885 1.00 75.87 C ANISOU 2043 CG GLN B 508 12192 6437 10196 -1462 671 372 C ATOM 2044 CD GLN B 508 -59.482 1.376 -12.566 1.00 75.36 C ANISOU 2044 CD GLN B 508 11907 6538 10187 -1650 724 321 C ATOM 2045 OE1 GLN B 508 -60.332 1.987 -11.925 1.00 75.75 O ANISOU 2045 OE1 GLN B 508 11794 6729 10258 -1802 777 303 O ATOM 2046 NE2 GLN B 508 -59.602 1.142 -13.859 1.00 74.97 N ANISOU 2046 NE2 GLN B 508 11854 6474 10155 -1636 707 295 N ATOM 2047 N PRO B 509 -58.661 -3.438 -13.531 1.00 79.60 N ANISOU 2047 N PRO B 509 13711 6288 10244 -1701 579 377 N ATOM 2048 CA PRO B 509 -58.212 -4.793 -13.875 1.00 81.64 C ANISOU 2048 CA PRO B 509 14365 6293 10361 -1649 519 391 C ATOM 2049 C PRO B 509 -56.794 -5.095 -13.391 1.00 81.98 C ANISOU 2049 C PRO B 509 14567 6200 10379 -1350 453 427 C ATOM 2050 O PRO B 509 -56.552 -6.151 -12.801 1.00 84.00 O ANISOU 2050 O PRO B 509 15182 6246 10487 -1359 409 456 O ATOM 2051 CB PRO B 509 -58.277 -4.814 -15.406 1.00 81.33 C ANISOU 2051 CB PRO B 509 14261 6272 10367 -1596 507 351 C ATOM 2052 CG PRO B 509 -59.229 -3.727 -15.776 1.00 80.17 C ANISOU 2052 CG PRO B 509 13746 6369 10343 -1744 567 315 C ATOM 2053 CD PRO B 509 -59.131 -2.684 -14.711 1.00 78.73 C ANISOU 2053 CD PRO B 509 13318 6344 10252 -1714 603 332 C ATOM 2054 N LYS B 510 -55.882 -4.160 -13.634 1.00 80.87 N ANISOU 2054 N LYS B 510 14162 6184 10379 -1093 444 424 N ATOM 2055 CA LYS B 510 -54.495 -4.278 -13.210 1.00 82.00 C ANISOU 2055 CA LYS B 510 14385 6246 10524 -794 381 452 C ATOM 2056 C LYS B 510 -54.001 -2.962 -12.633 1.00 78.86 C ANISOU 2056 C LYS B 510 13647 6042 10272 -676 397 462 C ATOM 2057 O LYS B 510 -54.638 -1.933 -12.811 1.00 78.72 O ANISOU 2057 O LYS B 510 13328 6217 10365 -786 454 443 O ATOM 2058 CB LYS B 510 -53.629 -4.682 -14.398 1.00 84.32 C ANISOU 2058 CB LYS B 510 14745 6467 10823 -550 339 431 C ATOM 2059 CG LYS B 510 -54.111 -5.950 -15.084 1.00 88.08 C ANISOU 2059 CG LYS B 510 15564 6746 11154 -657 318 415 C ATOM 2060 CD LYS B 510 -53.020 -6.639 -15.882 1.00 90.90 C ANISOU 2060 CD LYS B 510 16101 6968 11468 -367 259 402 C ATOM 2061 CE LYS B 510 -53.218 -8.146 -15.869 1.00 95.27 C ANISOU 2061 CE LYS B 510 17129 7244 11823 -433 205 405 C ATOM 2062 NZ LYS B 510 -52.121 -8.818 -16.621 1.00 98.45 N ANISOU 2062 NZ LYS B 510 17712 7515 12177 -121 146 386 N ATOM 2063 N CYS B 511 -52.879 -3.018 -11.919 1.00 77.95 N ANISOU 2063 N CYS B 511 13595 5871 10151 -455 339 492 N ATOM 2064 CA CYS B 511 -52.173 -1.836 -11.432 1.00 75.53 C ANISOU 2064 CA CYS B 511 12988 5729 9978 -305 336 504 C ATOM 2065 C CYS B 511 -50.699 -1.969 -11.756 1.00 74.19 C ANISOU 2065 C CYS B 511 12826 5524 9839 26 268 509 C ATOM 2066 O CYS B 511 -50.050 -2.891 -11.297 1.00 74.50 O ANISOU 2066 O CYS B 511 13140 5394 9772 154 200 528 O ATOM 2067 CB CYS B 511 -52.319 -1.677 -9.913 1.00 76.75 C ANISOU 2067 CB CYS B 511 13194 5875 10090 -393 330 538 C ATOM 2068 SG CYS B 511 -51.357 -0.277 -9.259 1.00 78.22 S ANISOU 2068 SG CYS B 511 13047 6243 10428 -199 307 553 S ATOM 2069 N ASN B 512 -50.158 -1.037 -12.527 1.00 73.32 N ANISOU 2069 N ASN B 512 12414 5576 9868 166 285 492 N ATOM 2070 CA ASN B 512 -48.708 -0.910 -12.620 1.00 72.53 C ANISOU 2070 CA ASN B 512 12244 5497 9816 472 229 499 C ATOM 2071 C ASN B 512 -48.238 -0.306 -11.296 1.00 71.81 C ANISOU 2071 C ASN B 512 12059 5463 9760 515 192 532 C ATOM 2072 O ASN B 512 -48.414 0.887 -11.071 1.00 69.26 O ANISOU 2072 O ASN B 512 11452 5312 9551 453 226 535 O ATOM 2073 CB ASN B 512 -48.286 -0.050 -13.814 1.00 70.39 C ANISOU 2073 CB ASN B 512 11675 5393 9676 583 266 474 C ATOM 2074 CG ASN B 512 -46.780 -0.027 -14.019 1.00 70.43 C ANISOU 2074 CG ASN B 512 11609 5428 9720 894 217 476 C ATOM 2075 OD1 ASN B 512 -46.008 -0.392 -13.130 1.00 72.14 O ANISOU 2075 OD1 ASN B 512 11934 5580 9894 1035 148 497 O ATOM 2076 ND2 ASN B 512 -46.353 0.403 -15.195 1.00 69.62 N ANISOU 2076 ND2 ASN B 512 11324 5432 9694 1001 251 452 N ATOM 2077 N PRO B 513 -47.628 -1.133 -10.418 1.00 73.60 N ANISOU 2077 N PRO B 513 12541 5539 9883 629 115 556 N ATOM 2078 CA PRO B 513 -47.260 -0.631 -9.090 1.00 73.07 C ANISOU 2078 CA PRO B 513 12420 5510 9832 652 73 589 C ATOM 2079 C PRO B 513 -46.135 0.418 -9.085 1.00 72.52 C ANISOU 2079 C PRO B 513 12036 5614 9902 858 42 592 C ATOM 2080 O PRO B 513 -45.846 0.969 -8.028 1.00 71.91 O ANISOU 2080 O PRO B 513 11885 5586 9851 867 6 616 O ATOM 2081 CB PRO B 513 -46.785 -1.897 -8.380 1.00 74.49 C ANISOU 2081 CB PRO B 513 12977 5468 9856 757 -14 609 C ATOM 2082 CG PRO B 513 -46.144 -2.674 -9.469 1.00 74.71 C ANISOU 2082 CG PRO B 513 13116 5416 9854 958 -41 583 C ATOM 2083 CD PRO B 513 -47.019 -2.456 -10.670 1.00 73.80 C ANISOU 2083 CD PRO B 513 12890 5366 9784 799 49 552 C ATOM 2084 N ASN B 514 -45.501 0.678 -10.231 1.00 72.90 N ANISOU 2084 N ASN B 514 11912 5754 10033 1013 56 568 N ATOM 2085 CA ASN B 514 -44.433 1.673 -10.322 1.00 73.49 C ANISOU 2085 CA ASN B 514 11680 6004 10237 1188 34 570 C ATOM 2086 C ASN B 514 -44.836 2.870 -11.162 1.00 72.24 C ANISOU 2086 C ASN B 514 11204 6031 10210 1086 114 554 C ATOM 2087 O ASN B 514 -45.400 2.728 -12.253 1.00 72.10 O ANISOU 2087 O ASN B 514 11185 6014 10195 1016 174 529 O ATOM 2088 CB ASN B 514 -43.182 1.043 -10.908 1.00 74.77 C ANISOU 2088 CB ASN B 514 11886 6140 10383 1478 -18 555 C ATOM 2089 CG ASN B 514 -42.700 -0.119 -10.082 1.00 77.12 C ANISOU 2089 CG ASN B 514 12503 6251 10548 1612 -113 568 C ATOM 2090 OD1 ASN B 514 -42.266 0.059 -8.946 1.00 78.18 O ANISOU 2090 OD1 ASN B 514 12645 6384 10676 1659 -182 594 O ATOM 2091 ND2 ASN B 514 -42.812 -1.319 -10.627 1.00 78.09 N ANISOU 2091 ND2 ASN B 514 12911 6203 10555 1668 -122 550 N ATOM 2092 N LEU B 515 -44.516 4.046 -10.637 1.00 71.72 N ANISOU 2092 N LEU B 515 10887 6114 10247 1082 105 570 N ATOM 2093 CA LEU B 515 -44.745 5.299 -11.315 1.00 71.14 C ANISOU 2093 CA LEU B 515 10512 6216 10299 1007 164 560 C ATOM 2094 C LEU B 515 -43.400 5.883 -11.750 1.00 70.44 C ANISOU 2094 C LEU B 515 10200 6260 10301 1214 136 562 C ATOM 2095 O LEU B 515 -42.683 6.497 -10.952 1.00 68.57 O ANISOU 2095 O LEU B 515 9839 6099 10113 1281 82 583 O ATOM 2096 CB LEU B 515 -45.489 6.255 -10.384 1.00 70.82 C ANISOU 2096 CB LEU B 515 10365 6244 10299 827 177 573 C ATOM 2097 CG LEU B 515 -45.766 7.662 -10.909 1.00 70.99 C ANISOU 2097 CG LEU B 515 10089 6438 10444 747 224 563 C ATOM 2098 CD1 LEU B 515 -46.509 7.590 -12.235 1.00 71.50 C ANISOU 2098 CD1 LEU B 515 10129 6518 10521 666 295 533 C ATOM 2099 CD2 LEU B 515 -46.532 8.490 -9.882 1.00 70.42 C ANISOU 2099 CD2 LEU B 515 9951 6412 10391 585 232 570 C ATOM 2100 N HIS B 516 -43.062 5.645 -13.016 1.00 70.57 N ANISOU 2100 N HIS B 516 10176 6304 10333 1309 173 539 N ATOM 2101 CA HIS B 516 -41.982 6.354 -13.699 1.00 70.65 C ANISOU 2101 CA HIS B 516 9933 6473 10436 1456 178 536 C ATOM 2102 C HIS B 516 -42.561 7.686 -14.177 1.00 69.03 C ANISOU 2102 C HIS B 516 9488 6407 10333 1295 237 537 C ATOM 2103 O HIS B 516 -43.344 7.721 -15.133 1.00 68.20 O ANISOU 2103 O HIS B 516 9387 6297 10227 1194 301 517 O ATOM 2104 CB HIS B 516 -41.459 5.519 -14.875 1.00 71.42 C ANISOU 2104 CB HIS B 516 10104 6539 10491 1618 204 508 C ATOM 2105 CG HIS B 516 -40.177 6.025 -15.463 1.00 72.20 C ANISOU 2105 CG HIS B 516 9969 6799 10665 1799 208 504 C ATOM 2106 ND1 HIS B 516 -39.720 5.625 -16.700 1.00 72.63 N ANISOU 2106 ND1 HIS B 516 10012 6879 10705 1927 256 475 N ATOM 2107 CD2 HIS B 516 -39.261 6.905 -14.991 1.00 71.94 C ANISOU 2107 CD2 HIS B 516 9701 6915 10716 1865 172 523 C ATOM 2108 CE1 HIS B 516 -38.572 6.225 -16.958 1.00 72.59 C ANISOU 2108 CE1 HIS B 516 9767 7041 10771 2063 257 476 C ATOM 2109 NE2 HIS B 516 -38.274 7.011 -15.940 1.00 72.23 N ANISOU 2109 NE2 HIS B 516 9580 7073 10788 2022 204 507 N ATOM 2110 N TYR B 517 -42.204 8.775 -13.498 1.00 67.85 N ANISOU 2110 N TYR B 517 9145 6372 10263 1270 208 559 N ATOM 2111 CA TYR B 517 -42.841 10.063 -13.765 1.00 67.56 C ANISOU 2111 CA TYR B 517 8915 6444 10310 1110 250 561 C ATOM 2112 C TYR B 517 -41.960 11.105 -14.446 1.00 66.44 C ANISOU 2112 C TYR B 517 8511 6466 10264 1172 262 568 C ATOM 2113 O TYR B 517 -40.739 11.049 -14.368 1.00 66.01 O ANISOU 2113 O TYR B 517 8375 6474 10229 1329 226 578 O ATOM 2114 CB TYR B 517 -43.473 10.637 -12.488 1.00 68.67 C ANISOU 2114 CB TYR B 517 9060 6574 10457 976 219 576 C ATOM 2115 CG TYR B 517 -42.544 11.151 -11.402 1.00 68.26 C ANISOU 2115 CG TYR B 517 8919 6576 10437 1052 143 604 C ATOM 2116 CD1 TYR B 517 -42.116 12.468 -11.402 1.00 67.72 C ANISOU 2116 CD1 TYR B 517 8617 6648 10465 1029 131 617 C ATOM 2117 CD2 TYR B 517 -42.158 10.338 -10.345 1.00 70.61 C ANISOU 2117 CD2 TYR B 517 9385 6777 10665 1132 76 618 C ATOM 2118 CE1 TYR B 517 -41.298 12.957 -10.406 1.00 69.24 C ANISOU 2118 CE1 TYR B 517 8731 6889 10685 1084 55 641 C ATOM 2119 CE2 TYR B 517 -41.335 10.816 -9.336 1.00 71.63 C ANISOU 2119 CE2 TYR B 517 9437 6956 10821 1198 -3 642 C ATOM 2120 CZ TYR B 517 -40.913 12.130 -9.371 1.00 70.94 C ANISOU 2120 CZ TYR B 517 9105 7016 10833 1170 -13 653 C ATOM 2121 OH TYR B 517 -40.101 12.623 -8.380 1.00 72.42 O ANISOU 2121 OH TYR B 517 9216 7254 11046 1223 -99 676 O ATOM 2122 N TRP B 518 -42.617 12.038 -15.132 1.00 65.16 N ANISOU 2122 N TRP B 518 8225 6374 10157 1043 312 561 N ATOM 2123 CA TRP B 518 -41.974 13.233 -15.660 1.00 65.64 C ANISOU 2123 CA TRP B 518 8049 6585 10306 1048 322 574 C ATOM 2124 C TRP B 518 -42.630 14.485 -15.084 1.00 65.02 C ANISOU 2124 C TRP B 518 7868 6554 10282 895 307 584 C ATOM 2125 O TRP B 518 -43.820 14.482 -14.761 1.00 65.20 O ANISOU 2125 O TRP B 518 7980 6513 10280 769 320 570 O ATOM 2126 CB TRP B 518 -42.011 13.272 -17.191 1.00 65.87 C ANISOU 2126 CB TRP B 518 8028 6656 10344 1058 393 556 C ATOM 2127 CG TRP B 518 -43.365 13.172 -17.808 1.00 65.25 C ANISOU 2127 CG TRP B 518 8042 6511 10237 923 439 531 C ATOM 2128 CD1 TRP B 518 -43.945 12.052 -18.303 1.00 66.30 C ANISOU 2128 CD1 TRP B 518 8359 6533 10295 926 467 506 C ATOM 2129 CD2 TRP B 518 -44.301 14.236 -18.015 1.00 64.90 C ANISOU 2129 CD2 TRP B 518 7910 6510 10238 768 454 527 C ATOM 2130 NE1 TRP B 518 -45.189 12.341 -18.799 1.00 66.02 N ANISOU 2130 NE1 TRP B 518 8344 6480 10258 775 499 486 N ATOM 2131 CE2 TRP B 518 -45.434 13.677 -18.634 1.00 64.59 C ANISOU 2131 CE2 TRP B 518 7994 6394 10151 684 491 496 C ATOM 2132 CE3 TRP B 518 -44.294 15.607 -17.729 1.00 64.99 C ANISOU 2132 CE3 TRP B 518 7758 6614 10321 695 434 543 C ATOM 2133 CZ2 TRP B 518 -46.558 14.437 -18.967 1.00 64.23 C ANISOU 2133 CZ2 TRP B 518 7899 6372 10130 542 506 479 C ATOM 2134 CZ3 TRP B 518 -45.407 16.366 -18.064 1.00 64.16 C ANISOU 2134 CZ3 TRP B 518 7622 6520 10235 561 450 526 C ATOM 2135 CH2 TRP B 518 -46.529 15.777 -18.674 1.00 63.91 C ANISOU 2135 CH2 TRP B 518 7701 6422 10159 491 485 493 C ATOM 2136 N THR B 519 -41.843 15.550 -14.964 1.00 64.89 N ANISOU 2136 N THR B 519 7667 6654 10335 905 280 607 N ATOM 2137 CA THR B 519 -42.348 16.857 -14.541 1.00 64.77 C ANISOU 2137 CA THR B 519 7551 6687 10371 774 261 616 C ATOM 2138 C THR B 519 -41.307 17.923 -14.855 1.00 66.78 C ANISOU 2138 C THR B 519 7606 7072 10694 793 243 641 C ATOM 2139 O THR B 519 -40.294 17.623 -15.479 1.00 66.89 O ANISOU 2139 O THR B 519 7548 7150 10715 898 258 648 O ATOM 2140 CB THR B 519 -42.694 16.872 -13.040 1.00 64.40 C ANISOU 2140 CB THR B 519 7583 6583 10302 732 204 622 C ATOM 2141 OG1 THR B 519 -43.390 18.074 -12.712 1.00 62.28 O ANISOU 2141 OG1 THR B 519 7243 6347 10070 606 195 620 O ATOM 2142 CG2 THR B 519 -41.433 16.732 -12.170 1.00 65.30 C ANISOU 2142 CG2 THR B 519 7661 6727 10422 846 130 649 C ATOM 2143 N THR B 520 -41.562 19.160 -14.434 1.00 69.14 N ANISOU 2143 N THR B 520 7820 7412 11036 688 212 652 N ATOM 2144 CA THR B 520 -40.597 20.244 -14.587 1.00 72.89 C ANISOU 2144 CA THR B 520 8121 8002 11569 678 184 680 C ATOM 2145 C THR B 520 -39.799 20.405 -13.294 1.00 80.35 C ANISOU 2145 C THR B 520 9031 8970 12526 716 99 702 C ATOM 2146 O THR B 520 -40.222 19.934 -12.234 1.00 77.69 O ANISOU 2146 O THR B 520 8813 8552 12154 721 62 696 O ATOM 2147 CB THR B 520 -41.289 21.565 -14.962 1.00 69.71 C ANISOU 2147 CB THR B 520 7662 7623 11199 544 190 679 C ATOM 2148 OG1 THR B 520 -42.152 21.980 -13.902 1.00 69.04 O ANISOU 2148 OG1 THR B 520 7646 7479 11107 471 148 669 O ATOM 2149 CG2 THR B 520 -42.097 21.404 -16.226 1.00 68.36 C ANISOU 2149 CG2 THR B 520 7531 7429 11013 512 262 655 C ATOM 2150 N GLN B 521 -38.644 21.065 -13.388 1.00 91.03 N ANISOU 2150 N GLN B 521 10224 10437 13923 733 67 729 N ATOM 2151 CA GLN B 521 -37.813 21.347 -12.209 1.00 99.94 C ANISOU 2151 CA GLN B 521 11299 11603 15068 758 -25 751 C ATOM 2152 C GLN B 521 -38.475 22.410 -11.319 1.00105.99 C ANISOU 2152 C GLN B 521 12094 12331 15844 632 -78 756 C ATOM 2153 O GLN B 521 -38.927 23.443 -11.826 1.00107.62 O ANISOU 2153 O GLN B 521 12258 12557 16076 524 -59 758 O ATOM 2154 CB GLN B 521 -36.427 21.828 -12.640 1.00103.44 C ANISOU 2154 CB GLN B 521 11546 12198 15557 790 -41 775 C ATOM 2155 CG GLN B 521 -35.412 21.917 -11.511 1.00106.84 C ANISOU 2155 CG GLN B 521 11907 12684 16002 840 -144 795 C ATOM 2156 CD GLN B 521 -34.874 20.561 -11.100 1.00109.36 C ANISOU 2156 CD GLN B 521 12286 12979 16284 1017 -169 783 C ATOM 2157 OE1 GLN B 521 -33.954 20.035 -11.727 1.00111.32 O ANISOU 2157 OE1 GLN B 521 12435 13321 16539 1135 -145 778 O ATOM 2158 NE2 GLN B 521 -35.435 19.995 -10.034 1.00109.61 N ANISOU 2158 NE2 GLN B 521 12487 12887 16270 1042 -218 776 N ATOM 2159 N ASP B 522 -38.551 22.133 -10.012 1.00113.90 N ANISOU 2159 N ASP B 522 13184 13272 16818 653 -145 757 N ATOM 2160 CA ASP B 522 -39.063 23.093 -9.003 1.00118.82 C ANISOU 2160 CA ASP B 522 13843 13861 17442 552 -203 760 C ATOM 2161 C ASP B 522 -38.009 23.614 -7.996 1.00125.31 C ANISOU 2161 C ASP B 522 14593 14736 18281 563 -310 787 C ATOM 2162 O ASP B 522 -38.183 24.703 -7.439 1.00124.79 O ANISOU 2162 O ASP B 522 14517 14670 18228 468 -361 794 O ATOM 2163 CB ASP B 522 -40.292 22.513 -8.262 1.00116.88 C ANISOU 2163 CB ASP B 522 13778 13494 17136 532 -183 733 C ATOM 2164 CG ASP B 522 -39.942 21.395 -7.263 1.00118.68 C ANISOU 2164 CG ASP B 522 14119 13661 17311 627 -227 738 C ATOM 2165 OD1 ASP B 522 -40.773 21.157 -6.360 1.00116.91 O ANISOU 2165 OD1 ASP B 522 14035 13349 17034 589 -231 725 O ATOM 2166 OD2 ASP B 522 -38.870 20.748 -7.371 1.00118.87 O ANISOU 2166 OD2 ASP B 522 14099 13724 17340 742 -258 753 O ATOM 2167 N GLU B 523 -36.941 22.838 -7.770 1.00133.89 N ANISOU 2167 N GLU B 523 15638 15867 19367 682 -351 800 N ATOM 2168 CA GLU B 523 -35.873 23.175 -6.816 1.00140.78 C ANISOU 2168 CA GLU B 523 16436 16799 20253 708 -463 823 C ATOM 2169 C GLU B 523 -34.509 23.165 -7.521 1.00144.25 C ANISOU 2169 C GLU B 523 16678 17390 20741 773 -473 839 C ATOM 2170 O GLU B 523 -34.304 22.414 -8.480 1.00148.33 O ANISOU 2170 O GLU B 523 17160 17940 21257 860 -400 829 O ATOM 2171 CB GLU B 523 -35.883 22.170 -5.649 1.00143.79 C ANISOU 2171 CB GLU B 523 16967 17091 20576 806 -523 818 C ATOM 2172 CG GLU B 523 -34.959 22.487 -4.468 1.00146.46 C ANISOU 2172 CG GLU B 523 17267 17465 20914 831 -654 839 C ATOM 2173 CD GLU B 523 -35.320 23.763 -3.707 1.00147.12 C ANISOU 2173 CD GLU B 523 17363 17530 21003 690 -710 847 C ATOM 2174 OE1 GLU B 523 -36.463 24.258 -3.826 1.00144.12 O ANISOU 2174 OE1 GLU B 523 17064 17082 20610 591 -651 831 O ATOM 2175 OE2 GLU B 523 -34.447 24.275 -2.973 1.00149.97 O ANISOU 2175 OE2 GLU B 523 17654 17948 21380 684 -819 866 O ATOM 2176 N GLY B 524 -33.590 24.003 -7.039 1.00144.74 N ANISOU 2176 N GLY B 524 16608 17547 20837 728 -561 863 N ATOM 2177 CA GLY B 524 -32.218 24.073 -7.553 1.00144.64 C ANISOU 2177 CA GLY B 524 16383 17703 20868 775 -580 878 C ATOM 2178 C GLY B 524 -31.983 25.282 -8.443 1.00144.46 C ANISOU 2178 C GLY B 524 16214 17782 20892 628 -542 897 C ATOM 2179 O GLY B 524 -32.823 25.617 -9.287 1.00142.13 O ANISOU 2179 O GLY B 524 15969 17439 20595 552 -455 891 O ATOM 2180 N ALA B 525 -30.833 25.933 -8.254 1.00145.28 N ANISOU 2180 N ALA B 525 16141 18024 21031 584 -613 921 N ATOM 2181 CA ALA B 525 -30.434 27.084 -9.069 1.00142.73 C ANISOU 2181 CA ALA B 525 15674 17809 20744 430 -585 944 C ATOM 2182 C ALA B 525 -30.001 26.627 -10.463 1.00139.02 C ANISOU 2182 C ALA B 525 15079 17451 20288 484 -468 939 C ATOM 2183 O ALA B 525 -29.461 25.530 -10.631 1.00139.37 O ANISOU 2183 O ALA B 525 15070 17553 20328 652 -445 920 O ATOM 2184 CB ALA B 525 -29.307 27.855 -8.392 1.00143.59 C ANISOU 2184 CB ALA B 525 15634 18040 20882 354 -700 971 C ATOM 2185 N ALA B 526 -30.244 27.480 -11.454 1.00133.96 N ANISOU 2185 N ALA B 526 14405 16836 19657 346 -398 953 N ATOM 2186 CA ALA B 526 -29.896 27.195 -12.849 1.00130.80 C ANISOU 2186 CA ALA B 526 13898 16539 19260 371 -278 949 C ATOM 2187 C ALA B 526 -28.386 27.279 -13.068 1.00127.70 C ANISOU 2187 C ALA B 526 13255 16367 18898 381 -289 964 C ATOM 2188 O ALA B 526 -27.719 28.151 -12.502 1.00124.28 O ANISOU 2188 O ALA B 526 12718 16013 18486 264 -376 991 O ATOM 2189 CB ALA B 526 -30.617 28.158 -13.782 1.00129.27 C ANISOU 2189 CB ALA B 526 13761 16298 19058 210 -211 963 C ATOM 2190 N ILE B 527 -27.866 26.380 -13.906 1.00124.51 N ANISOU 2190 N ILE B 527 12753 16065 18488 519 -200 943 N ATOM 2191 CA ILE B 527 -26.424 26.276 -14.152 1.00125.64 C ANISOU 2191 CA ILE B 527 12640 16440 18656 565 -197 946 C ATOM 2192 C ILE B 527 -25.992 27.387 -15.126 1.00120.42 C ANISOU 2192 C ILE B 527 11838 15909 18004 365 -129 978 C ATOM 2193 O ILE B 527 -26.137 27.248 -16.347 1.00120.15 O ANISOU 2193 O ILE B 527 11795 15906 17950 364 -2 972 O ATOM 2194 CB ILE B 527 -26.019 24.863 -14.682 1.00128.25 C ANISOU 2194 CB ILE B 527 12925 16833 18969 808 -125 905 C ATOM 2195 CG1 ILE B 527 -26.434 23.753 -13.687 1.00128.15 C ANISOU 2195 CG1 ILE B 527 13080 16676 18935 997 -201 877 C ATOM 2196 CG2 ILE B 527 -24.516 24.794 -14.969 1.00128.77 C ANISOU 2196 CG2 ILE B 527 12702 17164 19060 864 -115 901 C ATOM 2197 CD1 ILE B 527 -27.768 23.086 -13.976 1.00127.31 C ANISOU 2197 CD1 ILE B 527 13229 16357 18785 1046 -139 857 C ATOM 2198 N GLY B 528 -25.479 28.490 -14.576 1.00113.31 N ANISOU 2198 N GLY B 528 10848 15077 17128 189 -216 1012 N ATOM 2199 CA GLY B 528 -25.012 29.621 -15.379 1.00109.43 C ANISOU 2199 CA GLY B 528 10237 14705 16637 -27 -168 1049 C ATOM 2200 C GLY B 528 -26.146 30.363 -16.074 1.00103.65 C ANISOU 2200 C GLY B 528 9696 13810 15873 -170 -110 1066 C ATOM 2201 O GLY B 528 -27.034 30.895 -15.407 1.00 99.24 O ANISOU 2201 O GLY B 528 9320 13076 15308 -238 -186 1073 O ATOM 2202 N LEU B 529 -26.120 30.373 -17.412 1.00 98.94 N ANISOU 2202 N LEU B 529 9063 13276 15253 -202 21 1068 N ATOM 2203 CA LEU B 529 -27.101 31.101 -18.241 1.00 93.74 C ANISOU 2203 CA LEU B 529 8573 12483 14557 -337 78 1085 C ATOM 2204 C LEU B 529 -28.297 30.265 -18.743 1.00 88.09 C ANISOU 2204 C LEU B 529 8047 11605 13817 -197 148 1049 C ATOM 2205 O LEU B 529 -29.078 30.753 -19.557 1.00 85.46 O ANISOU 2205 O LEU B 529 7840 11179 13452 -285 201 1057 O ATOM 2206 CB LEU B 529 -26.397 31.698 -19.465 1.00 95.54 C ANISOU 2206 CB LEU B 529 8670 12869 14762 -480 181 1113 C ATOM 2207 CG LEU B 529 -25.161 32.573 -19.247 1.00 98.39 C ANISOU 2207 CG LEU B 529 8826 13420 15138 -658 138 1152 C ATOM 2208 CD1 LEU B 529 -24.601 33.003 -20.600 1.00 99.19 C ANISOU 2208 CD1 LEU B 529 8819 13667 15200 -790 269 1176 C ATOM 2209 CD2 LEU B 529 -25.482 33.779 -18.373 1.00 97.57 C ANISOU 2209 CD2 LEU B 529 8836 13199 15036 -845 4 1186 C ATOM 2210 N ALA B 530 -28.454 29.031 -18.262 1.00 83.56 N ANISOU 2210 N ALA B 530 7503 10993 13252 11 141 1010 N ATOM 2211 CA ALA B 530 -29.455 28.107 -18.805 1.00 79.57 C ANISOU 2211 CA ALA B 530 7158 10357 12718 142 213 975 C ATOM 2212 C ALA B 530 -30.903 28.572 -18.594 1.00 76.47 C ANISOU 2212 C ALA B 530 6991 9753 12310 69 179 972 C ATOM 2213 O ALA B 530 -31.799 28.154 -19.319 1.00 76.00 O ANISOU 2213 O ALA B 530 7057 9595 12221 112 247 951 O ATOM 2214 CB ALA B 530 -29.258 26.718 -18.217 1.00 79.77 C ANISOU 2214 CB ALA B 530 7183 10377 12748 369 197 937 C ATOM 2215 N TRP B 531 -31.125 29.408 -17.585 1.00 73.92 N ANISOU 2215 N TRP B 531 6716 9366 12004 -31 70 990 N ATOM 2216 CA TRP B 531 -32.430 30.052 -17.344 1.00 69.75 C ANISOU 2216 CA TRP B 531 6382 8658 11460 -111 31 986 C ATOM 2217 C TRP B 531 -32.888 31.044 -18.418 1.00 68.61 C ANISOU 2217 C TRP B 531 6296 8483 11289 -256 77 1005 C ATOM 2218 O TRP B 531 -34.086 31.267 -18.553 1.00 68.44 O ANISOU 2218 O TRP B 531 6436 8320 11248 -270 74 987 O ATOM 2219 CB TRP B 531 -32.425 30.774 -15.995 1.00 68.67 C ANISOU 2219 CB TRP B 531 6277 8473 11340 -181 -97 999 C ATOM 2220 CG TRP B 531 -31.407 31.878 -15.879 1.00 68.24 C ANISOU 2220 CG TRP B 531 6097 8531 11299 -339 -152 1042 C ATOM 2221 CD1 TRP B 531 -30.127 31.761 -15.442 1.00 68.64 C ANISOU 2221 CD1 TRP B 531 5964 8737 11376 -335 -191 1058 C ATOM 2222 CD2 TRP B 531 -31.602 33.259 -16.185 1.00 67.68 C ANISOU 2222 CD2 TRP B 531 6084 8422 11210 -531 -181 1072 C ATOM 2223 NE1 TRP B 531 -29.504 32.978 -15.461 1.00 69.44 N ANISOU 2223 NE1 TRP B 531 5997 8907 11477 -527 -239 1098 N ATOM 2224 CE2 TRP B 531 -30.385 33.921 -15.912 1.00 68.61 C ANISOU 2224 CE2 TRP B 531 6050 8676 11342 -652 -234 1109 C ATOM 2225 CE3 TRP B 531 -32.685 34.003 -16.665 1.00 66.02 C ANISOU 2225 CE3 TRP B 531 6043 8074 10967 -608 -174 1070 C ATOM 2226 CZ2 TRP B 531 -30.217 35.293 -16.100 1.00 68.13 C ANISOU 2226 CZ2 TRP B 531 6019 8607 11260 -861 -278 1148 C ATOM 2227 CZ3 TRP B 531 -32.516 35.371 -16.858 1.00 66.38 C ANISOU 2227 CZ3 TRP B 531 6123 8106 10990 -797 -221 1106 C ATOM 2228 CH2 TRP B 531 -31.287 36.000 -16.570 1.00 67.52 C ANISOU 2228 CH2 TRP B 531 6130 8377 11145 -928 -272 1147 C ATOM 2229 N ILE B 532 -31.942 31.656 -19.136 1.00 69.00 N ANISOU 2229 N ILE B 532 6216 8666 11333 -366 114 1039 N ATOM 2230 CA ILE B 532 -32.235 32.615 -20.220 1.00 68.03 C ANISOU 2230 CA ILE B 532 6154 8520 11173 -515 158 1064 C ATOM 2231 C ILE B 532 -32.876 31.859 -21.384 1.00 67.51 C ANISOU 2231 C ILE B 532 6157 8416 11076 -422 269 1036 C ATOM 2232 O ILE B 532 -32.237 30.958 -21.922 1.00 69.63 O ANISOU 2232 O ILE B 532 6316 8795 11343 -322 355 1025 O ATOM 2233 CB ILE B 532 -30.945 33.307 -20.733 1.00 68.71 C ANISOU 2233 CB ILE B 532 6072 8780 11252 -660 187 1108 C ATOM 2234 CG1 ILE B 532 -30.368 34.220 -19.659 1.00 69.69 C ANISOU 2234 CG1 ILE B 532 6148 8931 11400 -787 66 1139 C ATOM 2235 CG2 ILE B 532 -31.192 34.109 -22.003 1.00 68.33 C ANISOU 2235 CG2 ILE B 532 6097 8712 11151 -800 252 1134 C ATOM 2236 CD1 ILE B 532 -28.961 34.698 -19.957 1.00 72.26 C ANISOU 2236 CD1 ILE B 532 6268 9459 11726 -921 87 1178 C ATOM 2237 N PRO B 533 -34.120 32.226 -21.790 1.00 66.55 N ANISOU 2237 N PRO B 533 6214 8144 10926 -451 265 1023 N ATOM 2238 CA PRO B 533 -34.813 31.414 -22.821 1.00 65.26 C ANISOU 2238 CA PRO B 533 6127 7935 10733 -355 358 992 C ATOM 2239 C PRO B 533 -34.057 31.286 -24.154 1.00 66.11 C ANISOU 2239 C PRO B 533 6147 8164 10806 -380 472 1009 C ATOM 2240 O PRO B 533 -34.137 30.245 -24.807 1.00 65.35 O ANISOU 2240 O PRO B 533 6051 8085 10692 -257 557 980 O ATOM 2241 CB PRO B 533 -36.147 32.146 -23.020 1.00 63.69 C ANISOU 2241 CB PRO B 533 6112 7576 10508 -417 314 981 C ATOM 2242 CG PRO B 533 -36.350 32.935 -21.771 1.00 63.83 C ANISOU 2242 CG PRO B 533 6168 7532 10552 -476 196 988 C ATOM 2243 CD PRO B 533 -34.972 33.342 -21.325 1.00 65.58 C ANISOU 2243 CD PRO B 533 6235 7886 10794 -555 171 1029 C ATOM 2244 N TYR B 534 -33.328 32.332 -24.535 1.00 66.94 N ANISOU 2244 N TYR B 534 6187 8351 10893 -542 476 1054 N ATOM 2245 CA TYR B 534 -32.486 32.292 -25.729 1.00 68.91 C ANISOU 2245 CA TYR B 534 6337 8740 11104 -586 591 1074 C ATOM 2246 C TYR B 534 -31.444 31.164 -25.690 1.00 69.52 C ANISOU 2246 C TYR B 534 6226 8985 11203 -446 663 1055 C ATOM 2247 O TYR B 534 -31.179 30.533 -26.714 1.00 70.99 O ANISOU 2247 O TYR B 534 6377 9242 11353 -378 777 1041 O ATOM 2248 CB TYR B 534 -31.778 33.637 -25.924 1.00 70.58 C ANISOU 2248 CB TYR B 534 6501 9023 11293 -807 572 1131 C ATOM 2249 CG TYR B 534 -30.899 33.695 -27.150 1.00 72.18 C ANISOU 2249 CG TYR B 534 6599 9379 11445 -880 698 1155 C ATOM 2250 CD1 TYR B 534 -29.512 33.748 -27.034 1.00 74.16 C ANISOU 2250 CD1 TYR B 534 6624 9842 11710 -938 736 1178 C ATOM 2251 CD2 TYR B 534 -31.455 33.675 -28.430 1.00 72.22 C ANISOU 2251 CD2 TYR B 534 6726 9328 11385 -889 781 1151 C ATOM 2252 CE1 TYR B 534 -28.700 33.797 -28.157 1.00 75.73 C ANISOU 2252 CE1 TYR B 534 6716 10198 11857 -1009 864 1197 C ATOM 2253 CE2 TYR B 534 -30.651 33.719 -29.559 1.00 74.10 C ANISOU 2253 CE2 TYR B 534 6877 9709 11567 -958 906 1173 C ATOM 2254 CZ TYR B 534 -29.274 33.782 -29.416 1.00 75.80 C ANISOU 2254 CZ TYR B 534 6863 10142 11796 -1019 952 1195 C ATOM 2255 OH TYR B 534 -28.470 33.831 -30.526 1.00 77.29 O ANISOU 2255 OH TYR B 534 6953 10489 11923 -1092 1086 1214 O ATOM 2256 N PHE B 535 -30.865 30.923 -24.517 1.00 68.76 N ANISOU 2256 N PHE B 535 6018 8947 11161 -394 592 1052 N ATOM 2257 CA PHE B 535 -29.793 29.940 -24.354 1.00 69.40 C ANISOU 2257 CA PHE B 535 5910 9195 11264 -253 638 1033 C ATOM 2258 C PHE B 535 -30.259 28.593 -23.821 1.00 69.67 C ANISOU 2258 C PHE B 535 6006 9149 11315 -29 624 984 C ATOM 2259 O PHE B 535 -29.576 27.590 -24.016 1.00 72.02 O ANISOU 2259 O PHE B 535 6198 9553 11610 126 683 957 O ATOM 2260 CB PHE B 535 -28.722 30.485 -23.415 1.00 69.04 C ANISOU 2260 CB PHE B 535 5687 9284 11261 -332 561 1061 C ATOM 2261 CG PHE B 535 -27.899 31.579 -24.013 1.00 69.15 C ANISOU 2261 CG PHE B 535 5585 9435 11252 -544 596 1109 C ATOM 2262 CD1 PHE B 535 -26.996 31.296 -25.033 1.00 70.30 C ANISOU 2262 CD1 PHE B 535 5571 9770 11367 -539 725 1110 C ATOM 2263 CD2 PHE B 535 -28.004 32.887 -23.552 1.00 68.36 C ANISOU 2263 CD2 PHE B 535 5541 9278 11152 -752 503 1151 C ATOM 2264 CE1 PHE B 535 -26.216 32.299 -25.593 1.00 71.70 C ANISOU 2264 CE1 PHE B 535 5640 10085 11514 -754 767 1156 C ATOM 2265 CE2 PHE B 535 -27.225 33.895 -24.108 1.00 70.29 C ANISOU 2265 CE2 PHE B 535 5694 9646 11367 -967 534 1199 C ATOM 2266 CZ PHE B 535 -26.329 33.602 -25.130 1.00 71.62 C ANISOU 2266 CZ PHE B 535 5697 10010 11505 -977 669 1203 C ATOM 2267 N GLY B 536 -31.404 28.565 -23.148 1.00 68.58 N ANISOU 2267 N GLY B 536 6043 8825 11187 -11 547 970 N ATOM 2268 CA GLY B 536 -31.849 27.377 -22.430 1.00 67.84 C ANISOU 2268 CA GLY B 536 6021 8646 11107 169 516 929 C ATOM 2269 C GLY B 536 -32.337 26.253 -23.322 1.00 67.36 C ANISOU 2269 C GLY B 536 6051 8534 11005 308 609 890 C ATOM 2270 O GLY B 536 -32.241 26.339 -24.545 1.00 66.83 O ANISOU 2270 O GLY B 536 5976 8515 10901 278 705 892 O ATOM 2271 N PRO B 537 -32.874 25.190 -22.712 1.00 67.66 N ANISOU 2271 N PRO B 537 6192 8470 11044 452 580 855 N ATOM 2272 CA PRO B 537 -33.328 24.046 -23.486 1.00 69.89 C ANISOU 2272 CA PRO B 537 6578 8692 11282 584 657 816 C ATOM 2273 C PRO B 537 -34.596 24.337 -24.283 1.00 71.07 C ANISOU 2273 C PRO B 537 6891 8710 11399 500 687 809 C ATOM 2274 O PRO B 537 -35.349 25.253 -23.947 1.00 70.13 O ANISOU 2274 O PRO B 537 6837 8512 11295 372 627 824 O ATOM 2275 CB PRO B 537 -33.593 22.977 -22.419 1.00 69.19 C ANISOU 2275 CB PRO B 537 6573 8513 11200 727 596 788 C ATOM 2276 CG PRO B 537 -33.908 23.746 -21.187 1.00 68.41 C ANISOU 2276 CG PRO B 537 6488 8362 11142 629 487 810 C ATOM 2277 CD PRO B 537 -33.110 25.014 -21.267 1.00 68.24 C ANISOU 2277 CD PRO B 537 6308 8468 11149 488 472 851 C ATOM 2278 N ALA B 538 -34.795 23.556 -25.342 1.00 73.69 N ANISOU 2278 N ALA B 538 7288 9026 11682 580 774 782 N ATOM 2279 CA ALA B 538 -36.020 23.586 -26.124 1.00 74.59 C ANISOU 2279 CA ALA B 538 7565 9013 11759 530 798 765 C ATOM 2280 C ALA B 538 -37.124 22.890 -25.336 1.00 76.18 C ANISOU 2280 C ALA B 538 7919 9062 11965 578 738 735 C ATOM 2281 O ALA B 538 -36.851 22.255 -24.309 1.00 78.47 O ANISOU 2281 O ALA B 538 8199 9341 12274 666 692 726 O ATOM 2282 CB ALA B 538 -35.808 22.890 -27.459 1.00 74.72 C ANISOU 2282 CB ALA B 538 7609 9064 11716 607 907 744 C ATOM 2283 N ALA B 539 -38.357 22.985 -25.837 1.00 75.61 N ANISOU 2283 N ALA B 539 7984 8876 11867 519 738 717 N ATOM 2284 CA ALA B 539 -39.524 22.340 -25.216 1.00 75.61 C ANISOU 2284 CA ALA B 539 8125 8739 11862 541 692 685 C ATOM 2285 C ALA B 539 -39.307 20.874 -24.830 1.00 76.17 C ANISOU 2285 C ALA B 539 8257 8774 11910 689 706 657 C ATOM 2286 O ALA B 539 -39.783 20.426 -23.788 1.00 77.39 O ANISOU 2286 O ALA B 539 8481 8851 12073 708 650 646 O ATOM 2287 CB ALA B 539 -40.738 22.459 -26.131 1.00 75.95 C ANISOU 2287 CB ALA B 539 8291 8696 11871 477 709 662 C ATOM 2288 N GLU B 540 -38.573 20.142 -25.662 1.00 77.57 N ANISOU 2288 N GLU B 540 8418 9005 12050 797 779 646 N ATOM 2289 CA GLU B 540 -38.282 18.725 -25.421 1.00 78.31 C ANISOU 2289 CA GLU B 540 8586 9058 12108 958 791 617 C ATOM 2290 C GLU B 540 -37.392 18.461 -24.193 1.00 75.36 C ANISOU 2290 C GLU B 540 8130 8734 11767 1047 735 629 C ATOM 2291 O GLU B 540 -37.426 17.350 -23.640 1.00 75.38 O ANISOU 2291 O GLU B 540 8238 8662 11742 1163 711 607 O ATOM 2292 CB GLU B 540 -37.629 18.090 -26.663 1.00 83.49 C ANISOU 2292 CB GLU B 540 9238 9773 12711 1066 885 599 C ATOM 2293 CG GLU B 540 -38.578 17.811 -27.833 1.00 87.54 C ANISOU 2293 CG GLU B 540 9896 10196 13166 1028 934 573 C ATOM 2294 CD GLU B 540 -38.968 19.039 -28.657 1.00 90.14 C ANISOU 2294 CD GLU B 540 10183 10560 13505 876 954 595 C ATOM 2295 OE1 GLU B 540 -39.985 18.950 -29.386 1.00 90.82 O ANISOU 2295 OE1 GLU B 540 10396 10555 13553 822 963 575 O ATOM 2296 OE2 GLU B 540 -38.275 20.087 -28.590 1.00 92.84 O ANISOU 2296 OE2 GLU B 540 10374 11015 13885 808 955 631 O ATOM 2297 N GLY B 541 -36.606 19.462 -23.775 1.00 71.22 N ANISOU 2297 N GLY B 541 7434 8330 11296 991 707 663 N ATOM 2298 CA GLY B 541 -35.585 19.286 -22.741 1.00 69.94 C ANISOU 2298 CA GLY B 541 7164 8243 11164 1078 653 675 C ATOM 2299 C GLY B 541 -35.762 20.037 -21.439 1.00 67.33 C ANISOU 2299 C GLY B 541 6805 7893 10884 986 555 700 C ATOM 2300 O GLY B 541 -34.772 20.324 -20.765 1.00 67.25 O ANISOU 2300 O GLY B 541 6657 7985 10908 1014 509 720 O ATOM 2301 N ILE B 542 -37.007 20.327 -21.064 1.00 66.13 N ANISOU 2301 N ILE B 542 6779 7615 10731 882 521 696 N ATOM 2302 CA ILE B 542 -37.313 21.006 -19.786 1.00 65.12 C ANISOU 2302 CA ILE B 542 6650 7452 10639 800 430 714 C ATOM 2303 C ILE B 542 -37.745 20.048 -18.675 1.00 65.06 C ANISOU 2303 C ILE B 542 6777 7334 10608 873 379 696 C ATOM 2304 O ILE B 542 -38.079 20.487 -17.582 1.00 66.50 O ANISOU 2304 O ILE B 542 6981 7476 10808 813 309 706 O ATOM 2305 CB ILE B 542 -38.394 22.099 -19.959 1.00 64.49 C ANISOU 2305 CB ILE B 542 6612 7318 10572 637 419 719 C ATOM 2306 CG1 ILE B 542 -39.789 21.491 -20.250 1.00 65.42 C ANISOU 2306 CG1 ILE B 542 6899 7304 10651 623 444 684 C ATOM 2307 CG2 ILE B 542 -37.980 23.064 -21.053 1.00 64.00 C ANISOU 2307 CG2 ILE B 542 6445 7348 10520 556 464 740 C ATOM 2308 CD1 ILE B 542 -40.920 22.495 -20.382 1.00 63.44 C ANISOU 2308 CD1 ILE B 542 6687 7006 10411 487 426 679 C ATOM 2309 N TYR B 543 -37.724 18.745 -18.943 1.00 66.50 N ANISOU 2309 N TYR B 543 7061 7463 10743 1001 411 671 N ATOM 2310 CA TYR B 543 -38.274 17.747 -18.031 1.00 65.35 C ANISOU 2310 CA TYR B 543 7084 7189 10557 1055 371 654 C ATOM 2311 C TYR B 543 -37.232 17.093 -17.135 1.00 66.21 C ANISOU 2311 C TYR B 543 7173 7323 10659 1200 311 660 C ATOM 2312 O TYR B 543 -36.079 16.935 -17.518 1.00 66.48 O ANISOU 2312 O TYR B 543 7084 7469 10703 1313 324 662 O ATOM 2313 CB TYR B 543 -38.986 16.663 -18.832 1.00 65.46 C ANISOU 2313 CB TYR B 543 7263 7101 10508 1098 431 621 C ATOM 2314 CG TYR B 543 -40.051 17.232 -19.724 1.00 64.71 C ANISOU 2314 CG TYR B 543 7192 6979 10415 964 479 611 C ATOM 2315 CD1 TYR B 543 -41.259 17.673 -19.198 1.00 63.41 C ANISOU 2315 CD1 TYR B 543 7094 6741 10255 832 452 605 C ATOM 2316 CD2 TYR B 543 -39.842 17.363 -21.087 1.00 65.53 C ANISOU 2316 CD2 TYR B 543 7248 7139 10511 973 549 604 C ATOM 2317 CE1 TYR B 543 -42.235 18.213 -20.009 1.00 62.77 C ANISOU 2317 CE1 TYR B 543 7027 6644 10175 723 486 591 C ATOM 2318 CE2 TYR B 543 -40.811 17.902 -21.905 1.00 65.05 C ANISOU 2318 CE2 TYR B 543 7216 7051 10447 857 582 595 C ATOM 2319 CZ TYR B 543 -42.004 18.325 -21.358 1.00 63.27 C ANISOU 2319 CZ TYR B 543 7053 6754 10232 736 545 587 C ATOM 2320 OH TYR B 543 -42.959 18.857 -22.174 1.00 63.65 O ANISOU 2320 OH TYR B 543 7122 6782 10276 636 567 573 O ATOM 2321 N ILE B 544 -37.668 16.734 -15.933 1.00 66.76 N ANISOU 2321 N ILE B 544 7363 7293 10706 1195 246 661 N ATOM 2322 CA ILE B 544 -36.935 15.851 -15.039 1.00 67.79 C ANISOU 2322 CA ILE B 544 7548 7399 10807 1343 181 661 C ATOM 2323 C ILE B 544 -37.758 14.584 -14.874 1.00 69.31 C ANISOU 2323 C ILE B 544 7989 7424 10919 1383 190 638 C ATOM 2324 O ILE B 544 -38.914 14.521 -15.300 1.00 66.83 O ANISOU 2324 O ILE B 544 7781 7028 10582 1273 240 624 O ATOM 2325 CB ILE B 544 -36.655 16.484 -13.656 1.00 67.64 C ANISOU 2325 CB ILE B 544 7482 7398 10818 1302 84 686 C ATOM 2326 CG1 ILE B 544 -37.948 16.889 -12.930 1.00 66.31 C ANISOU 2326 CG1 ILE B 544 7434 7121 10637 1146 71 688 C ATOM 2327 CG2 ILE B 544 -35.735 17.684 -13.810 1.00 67.46 C ANISOU 2327 CG2 ILE B 544 7220 7541 10868 1259 66 710 C ATOM 2328 CD1 ILE B 544 -37.743 17.208 -11.463 1.00 66.31 C ANISOU 2328 CD1 ILE B 544 7448 7104 10639 1130 -24 707 C ATOM 2329 N GLU B 545 -37.147 13.575 -14.264 1.00 73.03 N ANISOU 2329 N GLU B 545 8557 7846 11343 1539 137 633 N ATOM 2330 CA GLU B 545 -37.815 12.308 -14.026 1.00 74.33 C ANISOU 2330 CA GLU B 545 8982 7839 11418 1580 135 615 C ATOM 2331 C GLU B 545 -37.589 11.816 -12.614 1.00 73.76 C ANISOU 2331 C GLU B 545 9031 7689 11306 1639 39 627 C ATOM 2332 O GLU B 545 -36.645 12.221 -11.944 1.00 75.45 O ANISOU 2332 O GLU B 545 9119 7990 11556 1709 -31 644 O ATOM 2333 CB GLU B 545 -37.353 11.248 -15.028 1.00 77.27 C ANISOU 2333 CB GLU B 545 9425 8192 11740 1744 179 586 C ATOM 2334 CG GLU B 545 -35.866 10.948 -14.996 1.00 80.82 C ANISOU 2334 CG GLU B 545 9759 8748 12200 1961 138 583 C ATOM 2335 CD GLU B 545 -35.499 9.704 -15.780 1.00 85.23 C ANISOU 2335 CD GLU B 545 10445 9252 12686 2150 169 548 C ATOM 2336 OE1 GLU B 545 -36.223 8.684 -15.698 1.00 86.38 O ANISOU 2336 OE1 GLU B 545 10855 9220 12746 2158 166 533 O ATOM 2337 OE2 GLU B 545 -34.462 9.739 -16.471 1.00 89.79 O ANISOU 2337 OE2 GLU B 545 10860 9968 13287 2291 196 533 O ATOM 2338 N GLY B 546 -38.483 10.941 -12.175 1.00 72.78 N ANISOU 2338 N GLY B 546 9155 7397 11098 1598 36 620 N ATOM 2339 CA GLY B 546 -38.334 10.232 -10.920 1.00 72.68 C ANISOU 2339 CA GLY B 546 9317 7276 11019 1662 -48 631 C ATOM 2340 C GLY B 546 -39.035 8.905 -11.030 1.00 73.21 C ANISOU 2340 C GLY B 546 9677 7163 10977 1675 -29 614 C ATOM 2341 O GLY B 546 -39.817 8.690 -11.953 1.00 70.84 O ANISOU 2341 O GLY B 546 9431 6823 10660 1593 48 595 O ATOM 2342 N LEU B 547 -38.720 8.013 -10.096 1.00 76.84 N ANISOU 2342 N LEU B 547 10330 7508 11355 1778 -109 621 N ATOM 2343 CA LEU B 547 -39.321 6.691 -10.026 1.00 79.13 C ANISOU 2343 CA LEU B 547 10937 7604 11524 1787 -108 610 C ATOM 2344 C LEU B 547 -39.841 6.489 -8.621 1.00 80.90 C ANISOU 2344 C LEU B 547 11343 7712 11680 1692 -164 633 C ATOM 2345 O LEU B 547 -39.110 6.694 -7.657 1.00 81.41 O ANISOU 2345 O LEU B 547 11376 7804 11753 1777 -252 653 O ATOM 2346 CB LEU B 547 -38.294 5.613 -10.372 1.00 81.23 C ANISOU 2346 CB LEU B 547 11307 7824 11733 2047 -155 592 C ATOM 2347 CG LEU B 547 -38.776 4.158 -10.437 1.00 83.03 C ANISOU 2347 CG LEU B 547 11889 7835 11822 2085 -163 578 C ATOM 2348 CD1 LEU B 547 -39.991 4.001 -11.344 1.00 82.48 C ANISOU 2348 CD1 LEU B 547 11903 7704 11730 1901 -62 561 C ATOM 2349 CD2 LEU B 547 -37.641 3.258 -10.913 1.00 84.74 C ANISOU 2349 CD2 LEU B 547 12166 8034 11995 2374 -209 552 C ATOM 2350 N MET B 548 -41.107 6.095 -8.523 1.00 83.29 N ANISOU 2350 N MET B 548 11835 7895 11915 1510 -112 631 N ATOM 2351 CA MET B 548 -41.792 5.884 -7.255 1.00 84.62 C ANISOU 2351 CA MET B 548 12190 7954 12006 1382 -142 651 C ATOM 2352 C MET B 548 -42.348 4.473 -7.207 1.00 83.22 C ANISOU 2352 C MET B 548 12359 7572 11686 1361 -141 646 C ATOM 2353 O MET B 548 -42.966 4.020 -8.169 1.00 82.09 O ANISOU 2353 O MET B 548 12285 7385 11520 1298 -73 625 O ATOM 2354 CB MET B 548 -42.943 6.861 -7.135 1.00 87.96 C ANISOU 2354 CB MET B 548 12495 8445 12478 1140 -67 650 C ATOM 2355 CG MET B 548 -42.607 8.135 -6.391 1.00 92.11 C ANISOU 2355 CG MET B 548 12806 9101 13090 1115 -101 667 C ATOM 2356 SD MET B 548 -42.907 7.976 -4.624 1.00100.21 S ANISOU 2356 SD MET B 548 14022 10026 14024 1040 -162 693 S ATOM 2357 CE MET B 548 -44.625 7.469 -4.575 1.00100.47 C ANISOU 2357 CE MET B 548 14251 9955 13966 790 -61 679 C ATOM 2358 N HIS B 549 -42.143 3.798 -6.079 1.00 82.09 N ANISOU 2358 N HIS B 549 12446 7299 11442 1406 -220 668 N ATOM 2359 CA HIS B 549 -42.658 2.448 -5.872 1.00 81.64 C ANISOU 2359 CA HIS B 549 12759 7028 11233 1372 -231 670 C ATOM 2360 C HIS B 549 -43.898 2.491 -4.996 1.00 79.50 C ANISOU 2360 C HIS B 549 12623 6688 10892 1108 -187 686 C ATOM 2361 O HIS B 549 -44.220 3.539 -4.440 1.00 77.09 O ANISOU 2361 O HIS B 549 12135 6499 10656 993 -163 695 O ATOM 2362 CB HIS B 549 -41.564 1.571 -5.279 1.00 83.71 C ANISOU 2362 CB HIS B 549 13215 7178 11412 1614 -354 681 C ATOM 2363 CG HIS B 549 -40.326 1.531 -6.120 1.00 84.78 C ANISOU 2363 CG HIS B 549 13195 7404 11613 1884 -392 659 C ATOM 2364 ND1 HIS B 549 -40.331 1.076 -7.421 1.00 84.46 N ANISOU 2364 ND1 HIS B 549 13158 7356 11575 1947 -336 627 N ATOM 2365 CD2 HIS B 549 -39.054 1.914 -5.860 1.00 85.50 C ANISOU 2365 CD2 HIS B 549 13108 7607 11769 2101 -476 660 C ATOM 2366 CE1 HIS B 549 -39.112 1.167 -7.921 1.00 85.32 C ANISOU 2366 CE1 HIS B 549 13102 7572 11744 2197 -376 609 C ATOM 2367 NE2 HIS B 549 -38.318 1.672 -6.994 1.00 85.58 N ANISOU 2367 NE2 HIS B 549 13013 7683 11817 2292 -462 628 N ATOM 2368 N ASN B 550 -44.583 1.353 -4.863 1.00 80.07 N ANISOU 2368 N ASN B 550 13023 6574 10823 1011 -176 689 N ATOM 2369 CA ASN B 550 -45.932 1.306 -4.277 1.00 79.23 C ANISOU 2369 CA ASN B 550 13040 6417 10645 724 -106 698 C ATOM 2370 C ASN B 550 -45.940 1.203 -2.747 1.00 81.08 C ANISOU 2370 C ASN B 550 13444 6573 10789 677 -160 732 C ATOM 2371 O ASN B 550 -46.731 0.447 -2.181 1.00 83.71 O ANISOU 2371 O ASN B 550 14054 6764 10985 510 -138 745 O ATOM 2372 CB ASN B 550 -46.735 0.149 -4.907 1.00 79.11 C ANISOU 2372 CB ASN B 550 13295 6246 10515 606 -62 685 C ATOM 2373 CG ASN B 550 -48.246 0.316 -4.768 1.00 78.21 C ANISOU 2373 CG ASN B 550 13193 6152 10369 285 42 678 C ATOM 2374 OD1 ASN B 550 -48.769 1.429 -4.775 1.00 76.64 O ANISOU 2374 OD1 ASN B 550 12719 6125 10274 171 106 666 O ATOM 2375 ND2 ASN B 550 -48.954 -0.805 -4.645 1.00 79.71 N ANISOU 2375 ND2 ASN B 550 13707 6169 10410 139 56 685 N ATOM 2376 N GLN B 551 -45.086 1.983 -2.081 1.00 81.89 N ANISOU 2376 N GLN B 551 13380 6771 10963 808 -227 746 N ATOM 2377 CA GLN B 551 -45.057 2.059 -0.620 1.00 83.10 C ANISOU 2377 CA GLN B 551 13662 6869 11040 766 -281 777 C ATOM 2378 C GLN B 551 -46.375 2.665 -0.155 1.00 81.23 C ANISOU 2378 C GLN B 551 13372 6693 10797 480 -173 773 C ATOM 2379 O GLN B 551 -46.869 3.607 -0.770 1.00 79.66 O ANISOU 2379 O GLN B 551 12898 6654 10715 391 -93 748 O ATOM 2380 CB GLN B 551 -43.856 2.900 -0.151 1.00 84.80 C ANISOU 2380 CB GLN B 551 13665 7201 11353 963 -377 787 C ATOM 2381 CG GLN B 551 -43.731 3.121 1.360 1.00 88.12 C ANISOU 2381 CG GLN B 551 14192 7582 11707 936 -444 817 C ATOM 2382 CD GLN B 551 -43.588 1.839 2.190 1.00 92.03 C ANISOU 2382 CD GLN B 551 15095 7850 12020 980 -526 845 C ATOM 2383 OE1 GLN B 551 -43.179 0.777 1.694 1.00 94.23 O ANISOU 2383 OE1 GLN B 551 15570 8000 12232 1116 -573 842 O ATOM 2384 NE2 GLN B 551 -43.915 1.944 3.477 1.00 93.30 N ANISOU 2384 NE2 GLN B 551 15400 7956 12093 871 -545 871 N ATOM 2385 N ASP B 552 -46.948 2.095 0.905 1.00 81.96 N ANISOU 2385 N ASP B 552 13737 6657 10744 341 -171 796 N ATOM 2386 CA ASP B 552 -48.275 2.476 1.425 1.00 82.44 C ANISOU 2386 CA ASP B 552 13789 6765 10766 58 -59 790 C ATOM 2387 C ASP B 552 -49.418 2.280 0.418 1.00 81.60 C ANISOU 2387 C ASP B 552 13640 6693 10671 -133 59 759 C ATOM 2388 O ASP B 552 -50.503 2.842 0.581 1.00 81.26 O ANISOU 2388 O ASP B 552 13483 6751 10641 -346 161 740 O ATOM 2389 CB ASP B 552 -48.268 3.928 1.946 1.00 81.50 C ANISOU 2389 CB ASP B 552 13376 6830 10761 41 -42 782 C ATOM 2390 CG ASP B 552 -47.312 4.137 3.111 1.00 83.45 C ANISOU 2390 CG ASP B 552 13686 7041 10979 183 -157 813 C ATOM 2391 OD1 ASP B 552 -46.833 5.285 3.269 1.00 83.96 O ANISOU 2391 OD1 ASP B 552 13491 7249 11161 257 -185 807 O ATOM 2392 OD2 ASP B 552 -47.044 3.175 3.872 1.00 84.38 O ANISOU 2392 OD2 ASP B 552 14119 6986 10953 216 -225 844 O ATOM 2393 N GLY B 553 -49.180 1.462 -0.608 1.00 81.41 N ANISOU 2393 N GLY B 553 13714 6584 10634 -53 42 751 N ATOM 2394 CA GLY B 553 -50.104 1.323 -1.725 1.00 80.37 C ANISOU 2394 CA GLY B 553 13515 6492 10527 -201 137 718 C ATOM 2395 C GLY B 553 -50.445 2.610 -2.449 1.00 77.66 C ANISOU 2395 C GLY B 553 12783 6370 10351 -233 204 683 C ATOM 2396 O GLY B 553 -51.498 2.696 -3.077 1.00 76.52 O ANISOU 2396 O GLY B 553 12565 6287 10222 -414 294 654 O ATOM 2397 N LEU B 554 -49.537 3.588 -2.388 1.00 77.62 N ANISOU 2397 N LEU B 554 12541 6481 10467 -57 154 686 N ATOM 2398 CA LEU B 554 -49.789 4.961 -2.861 1.00 74.91 C ANISOU 2398 CA LEU B 554 11842 6342 10275 -84 205 659 C ATOM 2399 C LEU B 554 -49.986 5.028 -4.368 1.00 72.32 C ANISOU 2399 C LEU B 554 11372 6076 10028 -73 249 628 C ATOM 2400 O LEU B 554 -50.911 5.668 -4.824 1.00 71.62 O ANISOU 2400 O LEU B 554 11114 6102 9997 -215 325 598 O ATOM 2401 CB LEU B 554 -48.655 5.900 -2.426 1.00 75.52 C ANISOU 2401 CB LEU B 554 11737 6508 10449 100 127 675 C ATOM 2402 CG LEU B 554 -48.605 7.335 -2.977 1.00 76.04 C ANISOU 2402 CG LEU B 554 11452 6767 10672 118 153 653 C ATOM 2403 CD1 LEU B 554 -49.896 8.122 -2.751 1.00 75.72 C ANISOU 2403 CD1 LEU B 554 11290 6828 10649 -91 245 625 C ATOM 2404 CD2 LEU B 554 -47.428 8.073 -2.356 1.00 76.60 C ANISOU 2404 CD2 LEU B 554 11403 6894 10806 282 62 675 C ATOM 2405 N ILE B 555 -49.141 4.337 -5.127 1.00 72.55 N ANISOU 2405 N ILE B 555 11484 6029 10053 99 198 632 N ATOM 2406 CA ILE B 555 -49.223 4.344 -6.593 1.00 70.94 C ANISOU 2406 CA ILE B 555 11166 5873 9915 128 235 604 C ATOM 2407 C ILE B 555 -50.549 3.773 -7.070 1.00 70.92 C ANISOU 2407 C ILE B 555 11274 5825 9845 -95 313 580 C ATOM 2408 O ILE B 555 -51.193 4.363 -7.917 1.00 71.28 O ANISOU 2408 O ILE B 555 11132 5983 9967 -181 372 550 O ATOM 2409 CB ILE B 555 -48.059 3.557 -7.264 1.00 71.01 C ANISOU 2409 CB ILE B 555 11278 5793 9908 365 169 609 C ATOM 2410 CG1 ILE B 555 -46.691 4.130 -6.860 1.00 70.97 C ANISOU 2410 CG1 ILE B 555 11130 5858 9975 592 89 628 C ATOM 2411 CG2 ILE B 555 -48.203 3.536 -8.785 1.00 69.72 C ANISOU 2411 CG2 ILE B 555 11016 5675 9798 384 216 578 C ATOM 2412 CD1 ILE B 555 -46.547 5.626 -7.055 1.00 69.99 C ANISOU 2412 CD1 ILE B 555 10657 5934 9999 588 112 622 C ATOM 2413 N CYS B 556 -50.957 2.632 -6.535 1.00 73.28 N ANISOU 2413 N CYS B 556 11884 5960 9998 -194 308 594 N ATOM 2414 CA CYS B 556 -52.216 2.020 -6.963 1.00 74.49 C ANISOU 2414 CA CYS B 556 12156 6070 10077 -428 378 573 C ATOM 2415 C CYS B 556 -53.426 2.855 -6.542 1.00 73.88 C ANISOU 2415 C CYS B 556 11899 6138 10033 -657 462 552 C ATOM 2416 O CYS B 556 -54.402 2.933 -7.287 1.00 74.65 O ANISOU 2416 O CYS B 556 11911 6302 10149 -812 525 518 O ATOM 2417 CB CYS B 556 -52.335 0.577 -6.466 1.00 76.58 C ANISOU 2417 CB CYS B 556 12819 6112 10164 -493 349 596 C ATOM 2418 SG CYS B 556 -51.168 -0.579 -7.243 1.00 79.08 S ANISOU 2418 SG CYS B 556 13379 6245 10422 -236 258 603 S ATOM 2419 N GLY B 557 -53.357 3.489 -5.372 1.00 73.37 N ANISOU 2419 N GLY B 557 11773 6127 9974 -669 459 568 N ATOM 2420 CA GLY B 557 -54.409 4.414 -4.924 1.00 72.12 C ANISOU 2420 CA GLY B 557 11421 6126 9856 -849 538 543 C ATOM 2421 C GLY B 557 -54.508 5.638 -5.819 1.00 69.97 C ANISOU 2421 C GLY B 557 10808 6035 9740 -797 560 508 C ATOM 2422 O GLY B 557 -55.598 6.077 -6.182 1.00 69.60 O ANISOU 2422 O GLY B 557 10617 6103 9724 -953 629 469 O ATOM 2423 N LEU B 558 -53.348 6.173 -6.169 1.00 68.48 N ANISOU 2423 N LEU B 558 10498 5873 9645 -576 497 522 N ATOM 2424 CA LEU B 558 -53.216 7.293 -7.091 1.00 67.11 C ANISOU 2424 CA LEU B 558 10033 5849 9615 -501 504 497 C ATOM 2425 C LEU B 558 -53.908 7.017 -8.432 1.00 66.25 C ANISOU 2425 C LEU B 558 9886 5761 9523 -578 547 463 C ATOM 2426 O LEU B 558 -54.634 7.865 -8.945 1.00 64.85 O ANISOU 2426 O LEU B 558 9500 5719 9421 -652 588 428 O ATOM 2427 CB LEU B 558 -51.723 7.572 -7.315 1.00 68.30 C ANISOU 2427 CB LEU B 558 10121 5995 9835 -256 426 524 C ATOM 2428 CG LEU B 558 -51.189 8.982 -7.516 1.00 69.48 C ANISOU 2428 CG LEU B 558 9986 6293 10119 -157 407 521 C ATOM 2429 CD1 LEU B 558 -51.777 9.978 -6.527 1.00 69.19 C ANISOU 2429 CD1 LEU B 558 9835 6349 10104 -255 428 512 C ATOM 2430 CD2 LEU B 558 -49.673 8.920 -7.367 1.00 71.07 C ANISOU 2430 CD2 LEU B 558 10194 6461 10346 60 325 555 C ATOM 2431 N ARG B 559 -53.690 5.829 -8.990 1.00 66.71 N ANISOU 2431 N ARG B 559 10158 5681 9506 -554 530 471 N ATOM 2432 CA ARG B 559 -54.357 5.436 -10.237 1.00 66.93 C ANISOU 2432 CA ARG B 559 10189 5709 9532 -636 564 439 C ATOM 2433 C ARG B 559 -55.868 5.433 -10.073 1.00 67.34 C ANISOU 2433 C ARG B 559 10220 5822 9544 -895 633 406 C ATOM 2434 O ARG B 559 -56.586 5.964 -10.921 1.00 67.85 O ANISOU 2434 O ARG B 559 10108 5997 9671 -966 666 368 O ATOM 2435 CB ARG B 559 -53.896 4.061 -10.715 1.00 67.21 C ANISOU 2435 CB ARG B 559 10504 5563 9468 -575 530 452 C ATOM 2436 CG ARG B 559 -52.449 4.044 -11.143 1.00 67.28 C ANISOU 2436 CG ARG B 559 10503 5538 9522 -305 469 472 C ATOM 2437 CD ARG B 559 -52.030 2.734 -11.786 1.00 68.38 C ANISOU 2437 CD ARG B 559 10907 5507 9567 -222 438 473 C ATOM 2438 NE ARG B 559 -50.582 2.678 -11.920 1.00 67.87 N ANISOU 2438 NE ARG B 559 10836 5417 9531 49 378 491 N ATOM 2439 CZ ARG B 559 -49.867 3.389 -12.790 1.00 67.79 C ANISOU 2439 CZ ARG B 559 10608 5520 9630 202 378 481 C ATOM 2440 NH1 ARG B 559 -48.543 3.259 -12.795 1.00 68.24 N ANISOU 2440 NH1 ARG B 559 10663 5561 9701 443 325 496 N ATOM 2441 NH2 ARG B 559 -50.452 4.240 -13.648 1.00 67.22 N ANISOU 2441 NH2 ARG B 559 10314 5579 9645 119 429 456 N ATOM 2442 N GLN B 560 -56.328 4.845 -8.973 1.00 67.81 N ANISOU 2442 N GLN B 560 10455 5812 9495 -1033 653 421 N ATOM 2443 CA GLN B 560 -57.745 4.810 -8.636 1.00 68.61 C ANISOU 2443 CA GLN B 560 10536 5986 9547 -1292 727 390 C ATOM 2444 C GLN B 560 -58.315 6.182 -8.335 1.00 67.22 C ANISOU 2444 C GLN B 560 10059 6011 9468 -1325 768 358 C ATOM 2445 O GLN B 560 -59.463 6.451 -8.673 1.00 67.49 O ANISOU 2445 O GLN B 560 9963 6162 9516 -1485 824 313 O ATOM 2446 CB GLN B 560 -57.978 3.893 -7.435 1.00 70.64 C ANISOU 2446 CB GLN B 560 11063 6120 9655 -1424 742 419 C ATOM 2447 CG GLN B 560 -59.434 3.694 -7.045 1.00 72.05 C ANISOU 2447 CG GLN B 560 11243 6370 9760 -1715 828 390 C ATOM 2448 CD GLN B 560 -60.278 3.086 -8.147 1.00 73.63 C ANISOU 2448 CD GLN B 560 11470 6569 9937 -1868 852 357 C ATOM 2449 OE1 GLN B 560 -59.787 2.321 -8.983 1.00 74.30 O ANISOU 2449 OE1 GLN B 560 11713 6520 9995 -1793 804 369 O ATOM 2450 NE2 GLN B 560 -61.562 3.422 -8.154 1.00 74.70 N ANISOU 2450 NE2 GLN B 560 11447 6859 10076 -2080 926 311 N ATOM 2451 N LEU B 561 -57.527 7.039 -7.691 1.00 66.68 N ANISOU 2451 N LEU B 561 9885 5984 9463 -1174 736 378 N ATOM 2452 CA LEU B 561 -57.978 8.383 -7.344 1.00 66.12 C ANISOU 2452 CA LEU B 561 9553 6088 9479 -1185 765 348 C ATOM 2453 C LEU B 561 -58.287 9.178 -8.597 1.00 66.53 C ANISOU 2453 C LEU B 561 9371 6261 9643 -1148 767 308 C ATOM 2454 O LEU B 561 -59.350 9.807 -8.703 1.00 67.31 O ANISOU 2454 O LEU B 561 9301 6500 9773 -1258 814 260 O ATOM 2455 CB LEU B 561 -56.931 9.118 -6.509 1.00 65.02 C ANISOU 2455 CB LEU B 561 9369 5950 9384 -1018 714 380 C ATOM 2456 CG LEU B 561 -57.246 10.566 -6.102 1.00 63.90 C ANISOU 2456 CG LEU B 561 8981 5969 9326 -1003 730 352 C ATOM 2457 CD1 LEU B 561 -58.548 10.670 -5.322 1.00 63.77 C ANISOU 2457 CD1 LEU B 561 8940 6039 9248 -1197 812 314 C ATOM 2458 CD2 LEU B 561 -56.100 11.150 -5.295 1.00 63.29 C ANISOU 2458 CD2 LEU B 561 8897 5867 9281 -844 666 389 C ATOM 2459 N ALA B 562 -57.348 9.139 -9.540 1.00 66.92 N ANISOU 2459 N ALA B 562 9417 6260 9749 -987 714 327 N ATOM 2460 CA ALA B 562 -57.501 9.811 -10.831 1.00 65.11 C ANISOU 2460 CA ALA B 562 8999 6122 9616 -940 708 296 C ATOM 2461 C ALA B 562 -58.720 9.300 -11.610 1.00 65.07 C ANISOU 2461 C ALA B 562 9002 6146 9575 -1112 749 253 C ATOM 2462 O ALA B 562 -59.417 10.080 -12.238 1.00 66.47 O ANISOU 2462 O ALA B 562 8985 6450 9818 -1146 762 211 O ATOM 2463 CB ALA B 562 -56.231 9.664 -11.660 1.00 63.83 C ANISOU 2463 CB ALA B 562 8868 5889 9496 -748 655 327 C ATOM 2464 N ASN B 563 -58.972 8.000 -11.555 1.00 65.05 N ANISOU 2464 N ASN B 563 9229 6022 9463 -1222 763 263 N ATOM 2465 CA ASN B 563 -60.140 7.416 -12.195 1.00 67.43 C ANISOU 2465 CA ASN B 563 9559 6344 9717 -1412 798 224 C ATOM 2466 C ASN B 563 -61.429 7.988 -11.595 1.00 66.98 C ANISOU 2466 C ASN B 563 9341 6446 9660 -1588 858 178 C ATOM 2467 O ASN B 563 -62.342 8.367 -12.329 1.00 66.00 O ANISOU 2467 O ASN B 563 9057 6442 9577 -1670 873 128 O ATOM 2468 CB ASN B 563 -60.090 5.874 -12.074 1.00 70.75 C ANISOU 2468 CB ASN B 563 10296 6582 10002 -1505 796 250 C ATOM 2469 CG ASN B 563 -61.395 5.195 -12.453 1.00 73.45 C ANISOU 2469 CG ASN B 563 10690 6943 10272 -1754 836 212 C ATOM 2470 OD1 ASN B 563 -62.285 5.066 -11.626 1.00 72.21 O ANISOU 2470 OD1 ASN B 563 10537 6842 10055 -1944 890 198 O ATOM 2471 ND2 ASN B 563 -61.506 4.758 -13.697 1.00 78.92 N ANISOU 2471 ND2 ASN B 563 11423 7596 10966 -1758 811 195 N ATOM 2472 N GLU B 564 -61.487 8.031 -10.265 1.00 66.94 N ANISOU 2472 N GLU B 564 9381 6445 9606 -1639 889 194 N ATOM 2473 CA GLU B 564 -62.657 8.535 -9.532 1.00 66.82 C ANISOU 2473 CA GLU B 564 9225 6586 9578 -1798 957 149 C ATOM 2474 C GLU B 564 -62.860 10.039 -9.656 1.00 64.57 C ANISOU 2474 C GLU B 564 8646 6475 9411 -1696 953 110 C ATOM 2475 O GLU B 564 -63.976 10.524 -9.530 1.00 64.44 O ANISOU 2475 O GLU B 564 8463 6615 9403 -1808 1001 54 O ATOM 2476 CB GLU B 564 -62.541 8.183 -8.055 1.00 68.83 C ANISOU 2476 CB GLU B 564 9629 6784 9737 -1861 992 181 C ATOM 2477 CG GLU B 564 -62.702 6.699 -7.780 1.00 71.87 C ANISOU 2477 CG GLU B 564 10312 7014 9979 -2023 1010 210 C ATOM 2478 CD GLU B 564 -62.497 6.347 -6.324 1.00 74.67 C ANISOU 2478 CD GLU B 564 10843 7296 10231 -2074 1036 247 C ATOM 2479 OE1 GLU B 564 -62.322 7.281 -5.498 1.00 76.79 O ANISOU 2479 OE1 GLU B 564 10984 7649 10540 -1996 1046 244 O ATOM 2480 OE2 GLU B 564 -62.511 5.136 -6.008 1.00 75.56 O ANISOU 2480 OE2 GLU B 564 11235 7259 10215 -2193 1042 279 O ATOM 2481 N THR B 565 -61.772 10.770 -9.880 1.00 62.66 N ANISOU 2481 N THR B 565 8346 6206 9256 -1484 893 137 N ATOM 2482 CA THR B 565 -61.812 12.218 -10.084 1.00 60.73 C ANISOU 2482 CA THR B 565 7854 6097 9120 -1371 874 107 C ATOM 2483 C THR B 565 -62.538 12.619 -11.383 1.00 59.76 C ANISOU 2483 C THR B 565 7570 6075 9060 -1389 863 56 C ATOM 2484 O THR B 565 -63.086 13.722 -11.481 1.00 57.53 O ANISOU 2484 O THR B 565 7082 5933 8843 -1359 862 10 O ATOM 2485 CB THR B 565 -60.369 12.774 -10.081 1.00 59.07 C ANISOU 2485 CB THR B 565 7649 5818 8976 -1158 808 157 C ATOM 2486 OG1 THR B 565 -59.779 12.527 -8.802 1.00 61.27 O ANISOU 2486 OG1 THR B 565 8057 6023 9199 -1139 809 197 O ATOM 2487 CG2 THR B 565 -60.322 14.255 -10.362 1.00 57.30 C ANISOU 2487 CG2 THR B 565 7202 5711 8857 -1047 778 132 C ATOM 2488 N THR B 566 -62.558 11.719 -12.363 1.00 60.32 N ANISOU 2488 N THR B 566 7745 6069 9104 -1435 850 62 N ATOM 2489 CA THR B 566 -62.940 12.076 -13.718 1.00 61.24 C ANISOU 2489 CA THR B 566 7739 6248 9281 -1413 820 26 C ATOM 2490 C THR B 566 -64.356 12.620 -13.854 1.00 62.24 C ANISOU 2490 C THR B 566 7671 6552 9425 -1530 847 -47 C ATOM 2491 O THR B 566 -64.575 13.569 -14.595 1.00 61.97 O ANISOU 2491 O THR B 566 7465 6610 9469 -1448 811 -81 O ATOM 2492 CB THR B 566 -62.764 10.893 -14.683 1.00 62.24 C ANISOU 2492 CB THR B 566 8040 6250 9357 -1456 804 42 C ATOM 2493 OG1 THR B 566 -61.545 10.208 -14.381 1.00 62.41 O ANISOU 2493 OG1 THR B 566 8263 6108 9340 -1358 787 105 O ATOM 2494 CG2 THR B 566 -62.717 11.385 -16.135 1.00 62.82 C ANISOU 2494 CG2 THR B 566 8008 6357 9501 -1370 758 22 C ATOM 2495 N GLN B 567 -65.309 12.028 -13.146 1.00 65.01 N ANISOU 2495 N GLN B 567 8048 6953 9698 -1720 908 -74 N ATOM 2496 CA GLN B 567 -66.702 12.468 -13.242 1.00 66.91 C ANISOU 2496 CA GLN B 567 8089 7384 9949 -1838 939 -151 C ATOM 2497 C GLN B 567 -66.889 13.927 -12.788 1.00 65.33 C ANISOU 2497 C GLN B 567 7669 7327 9824 -1716 934 -189 C ATOM 2498 O GLN B 567 -67.389 14.764 -13.547 1.00 63.38 O ANISOU 2498 O GLN B 567 7241 7192 9645 -1655 897 -239 O ATOM 2499 CB GLN B 567 -67.621 11.544 -12.442 1.00 69.86 C ANISOU 2499 CB GLN B 567 8534 7793 10217 -2077 1018 -169 C ATOM 2500 CG GLN B 567 -69.044 12.076 -12.362 1.00 72.93 C ANISOU 2500 CG GLN B 567 8683 8409 10615 -2191 1059 -255 C ATOM 2501 CD GLN B 567 -70.055 11.086 -11.842 1.00 76.22 C ANISOU 2501 CD GLN B 567 9153 8881 10924 -2461 1138 -278 C ATOM 2502 OE1 GLN B 567 -69.797 9.889 -11.725 1.00 77.96 O ANISOU 2502 OE1 GLN B 567 9612 8954 11055 -2587 1153 -231 O ATOM 2503 NE2 GLN B 567 -71.230 11.594 -11.525 1.00 78.47 N ANISOU 2503 NE2 GLN B 567 9216 9385 11212 -2553 1188 -354 N ATOM 2504 N ALA B 568 -66.508 14.198 -11.542 1.00 64.90 N ANISOU 2504 N ALA B 568 7649 7259 9747 -1684 968 -166 N ATOM 2505 CA ALA B 568 -66.553 15.548 -10.977 1.00 64.70 C ANISOU 2505 CA ALA B 568 7459 7343 9781 -1559 961 -196 C ATOM 2506 C ALA B 568 -65.794 16.543 -11.840 1.00 63.45 C ANISOU 2506 C ALA B 568 7226 7157 9722 -1359 876 -183 C ATOM 2507 O ALA B 568 -66.273 17.657 -12.075 1.00 63.81 O ANISOU 2507 O ALA B 568 7094 7322 9826 -1280 849 -234 O ATOM 2508 CB ALA B 568 -65.978 15.560 -9.567 1.00 65.06 C ANISOU 2508 CB ALA B 568 7607 7331 9779 -1541 996 -157 C ATOM 2509 N LEU B 569 -64.617 16.135 -12.309 1.00 62.43 N ANISOU 2509 N LEU B 569 7239 6874 9607 -1278 833 -115 N ATOM 2510 CA LEU B 569 -63.777 17.008 -13.120 1.00 61.14 C ANISOU 2510 CA LEU B 569 7023 6679 9529 -1104 760 -94 C ATOM 2511 C LEU B 569 -64.459 17.319 -14.441 1.00 60.83 C ANISOU 2511 C LEU B 569 6868 6713 9532 -1103 725 -141 C ATOM 2512 O LEU B 569 -64.502 18.470 -14.850 1.00 60.79 O ANISOU 2512 O LEU B 569 6734 6772 9591 -994 678 -165 O ATOM 2513 CB LEU B 569 -62.388 16.392 -13.346 1.00 59.81 C ANISOU 2513 CB LEU B 569 7021 6345 9356 -1026 733 -16 C ATOM 2514 CG LEU B 569 -61.384 17.247 -14.113 1.00 59.08 C ANISOU 2514 CG LEU B 569 6881 6222 9344 -858 668 13 C ATOM 2515 CD1 LEU B 569 -61.246 18.631 -13.513 1.00 59.42 C ANISOU 2515 CD1 LEU B 569 6802 6334 9439 -764 641 3 C ATOM 2516 CD2 LEU B 569 -60.031 16.569 -14.167 1.00 59.53 C ANISOU 2516 CD2 LEU B 569 7090 6140 9389 -783 653 84 C ATOM 2517 N GLN B 570 -65.006 16.293 -15.090 1.00 61.82 N ANISOU 2517 N GLN B 570 7051 6822 9612 -1228 741 -154 N ATOM 2518 CA GLN B 570 -65.696 16.467 -16.374 1.00 61.84 C ANISOU 2518 CA GLN B 570 6959 6890 9645 -1241 701 -200 C ATOM 2519 C GLN B 570 -66.920 17.368 -16.238 1.00 60.96 C ANISOU 2519 C GLN B 570 6635 6965 9560 -1258 699 -282 C ATOM 2520 O GLN B 570 -67.131 18.237 -17.079 1.00 60.67 O ANISOU 2520 O GLN B 570 6485 6986 9580 -1163 638 -313 O ATOM 2521 CB GLN B 570 -66.094 15.115 -17.015 1.00 63.30 C ANISOU 2521 CB GLN B 570 7263 7019 9766 -1392 717 -201 C ATOM 2522 CG GLN B 570 -64.943 14.299 -17.590 1.00 63.38 C ANISOU 2522 CG GLN B 570 7475 6850 9756 -1338 699 -134 C ATOM 2523 CD GLN B 570 -64.366 14.850 -18.887 1.00 63.75 C ANISOU 2523 CD GLN B 570 7492 6865 9862 -1200 637 -123 C ATOM 2524 OE1 GLN B 570 -64.557 16.022 -19.239 1.00 65.22 O ANISOU 2524 OE1 GLN B 570 7524 7142 10114 -1110 598 -151 O ATOM 2525 NE2 GLN B 570 -63.630 14.004 -19.598 1.00 63.66 N ANISOU 2525 NE2 GLN B 570 7645 6722 9821 -1177 627 -83 N ATOM 2526 N LEU B 571 -67.705 17.168 -15.181 1.00 61.06 N ANISOU 2526 N LEU B 571 6599 7071 9527 -1372 765 -317 N ATOM 2527 CA LEU B 571 -68.871 18.030 -14.910 1.00 61.74 C ANISOU 2527 CA LEU B 571 6471 7353 9632 -1375 773 -403 C ATOM 2528 C LEU B 571 -68.471 19.482 -14.649 1.00 61.08 C ANISOU 2528 C LEU B 571 6296 7299 9613 -1180 727 -411 C ATOM 2529 O LEU B 571 -69.174 20.405 -15.049 1.00 61.75 O ANISOU 2529 O LEU B 571 6218 7505 9738 -1107 685 -476 O ATOM 2530 CB LEU B 571 -69.688 17.499 -13.733 1.00 61.77 C ANISOU 2530 CB LEU B 571 6451 7453 9564 -1537 868 -435 C ATOM 2531 CG LEU B 571 -70.374 16.169 -14.032 1.00 63.27 C ANISOU 2531 CG LEU B 571 6704 7649 9683 -1759 910 -444 C ATOM 2532 CD1 LEU B 571 -70.910 15.550 -12.752 1.00 64.98 C ANISOU 2532 CD1 LEU B 571 6952 7922 9813 -1932 1013 -454 C ATOM 2533 CD2 LEU B 571 -71.480 16.334 -15.061 1.00 63.46 C ANISOU 2533 CD2 LEU B 571 6556 7819 9734 -1807 870 -521 C ATOM 2534 N PHE B 572 -67.340 19.675 -13.983 1.00 59.85 N ANISOU 2534 N PHE B 572 6251 7026 9462 -1097 728 -346 N ATOM 2535 CA PHE B 572 -66.826 21.005 -13.741 1.00 58.54 C ANISOU 2535 CA PHE B 572 6029 6863 9350 -926 678 -343 C ATOM 2536 C PHE B 572 -66.446 21.679 -15.055 1.00 59.22 C ANISOU 2536 C PHE B 572 6088 6912 9500 -807 589 -335 C ATOM 2537 O PHE B 572 -66.770 22.845 -15.263 1.00 60.23 O ANISOU 2537 O PHE B 572 6106 7110 9667 -698 536 -377 O ATOM 2538 CB PHE B 572 -65.640 20.947 -12.786 1.00 57.34 C ANISOU 2538 CB PHE B 572 6011 6589 9185 -881 692 -270 C ATOM 2539 CG PHE B 572 -64.902 22.239 -12.665 1.00 56.57 C ANISOU 2539 CG PHE B 572 5886 6464 9141 -717 629 -253 C ATOM 2540 CD1 PHE B 572 -65.339 23.222 -11.790 1.00 56.87 C ANISOU 2540 CD1 PHE B 572 5839 6589 9179 -659 632 -300 C ATOM 2541 CD2 PHE B 572 -63.772 22.475 -13.425 1.00 55.41 C ANISOU 2541 CD2 PHE B 572 5805 6207 9041 -625 568 -192 C ATOM 2542 CE1 PHE B 572 -64.663 24.416 -11.678 1.00 55.89 C ANISOU 2542 CE1 PHE B 572 5710 6428 9097 -517 566 -284 C ATOM 2543 CE2 PHE B 572 -63.092 23.669 -13.319 1.00 54.94 C ANISOU 2543 CE2 PHE B 572 5727 6123 9025 -495 509 -174 C ATOM 2544 CZ PHE B 572 -63.535 24.641 -12.444 1.00 55.33 C ANISOU 2544 CZ PHE B 572 5706 6244 9071 -444 503 -218 C ATOM 2545 N LEU B 573 -65.784 20.938 -15.942 1.00 59.86 N ANISOU 2545 N LEU B 573 6280 6882 9583 -826 573 -282 N ATOM 2546 CA LEU B 573 -65.394 21.466 -17.252 1.00 59.20 C ANISOU 2546 CA LEU B 573 6187 6758 9546 -729 498 -270 C ATOM 2547 C LEU B 573 -66.592 21.755 -18.170 1.00 60.49 C ANISOU 2547 C LEU B 573 6225 7037 9721 -746 457 -346 C ATOM 2548 O LEU B 573 -66.541 22.680 -18.978 1.00 60.51 O ANISOU 2548 O LEU B 573 6180 7047 9763 -638 384 -358 O ATOM 2549 CB LEU B 573 -64.395 20.528 -17.935 1.00 58.30 C ANISOU 2549 CB LEU B 573 6226 6503 9420 -744 501 -200 C ATOM 2550 CG LEU B 573 -63.039 20.410 -17.228 1.00 58.67 C ANISOU 2550 CG LEU B 573 6386 6438 9469 -685 517 -124 C ATOM 2551 CD1 LEU B 573 -62.160 19.381 -17.923 1.00 59.05 C ANISOU 2551 CD1 LEU B 573 6576 6362 9496 -692 525 -67 C ATOM 2552 CD2 LEU B 573 -62.316 21.753 -17.150 1.00 57.85 C ANISOU 2552 CD2 LEU B 573 6232 6327 9418 -547 465 -103 C ATOM 2553 N ARG B 574 -67.664 20.973 -18.051 1.00 61.83 N ANISOU 2553 N ARG B 574 6343 7297 9850 -887 500 -397 N ATOM 2554 CA ARG B 574 -68.911 21.267 -18.761 1.00 62.03 C ANISOU 2554 CA ARG B 574 6220 7462 9885 -907 459 -480 C ATOM 2555 C ARG B 574 -69.494 22.617 -18.316 1.00 62.98 C ANISOU 2555 C ARG B 574 6183 7709 10037 -787 425 -545 C ATOM 2556 O ARG B 574 -69.999 23.384 -19.145 1.00 64.76 O ANISOU 2556 O ARG B 574 6316 7997 10293 -699 346 -593 O ATOM 2557 CB ARG B 574 -69.930 20.148 -18.530 1.00 63.91 C ANISOU 2557 CB ARG B 574 6425 7788 10067 -1103 521 -522 C ATOM 2558 CG ARG B 574 -71.313 20.406 -19.124 1.00 65.86 C ANISOU 2558 CG ARG B 574 6489 8211 10321 -1139 482 -618 C ATOM 2559 CD ARG B 574 -72.290 19.347 -18.681 1.00 66.98 C ANISOU 2559 CD ARG B 574 6588 8457 10405 -1354 555 -658 C ATOM 2560 NE ARG B 574 -71.937 18.052 -19.244 1.00 68.27 N ANISOU 2560 NE ARG B 574 6923 8492 10525 -1491 569 -606 N ATOM 2561 CZ ARG B 574 -72.485 16.890 -18.890 1.00 69.36 C ANISOU 2561 CZ ARG B 574 7105 8653 10595 -1703 634 -613 C ATOM 2562 NH1 ARG B 574 -73.422 16.844 -17.952 1.00 72.14 N ANISOU 2562 NH1 ARG B 574 7327 9166 10915 -1816 703 -669 N ATOM 2563 NH2 ARG B 574 -72.084 15.761 -19.474 1.00 68.39 N ANISOU 2563 NH2 ARG B 574 7166 8388 10428 -1806 633 -565 N ATOM 2564 N ALA B 575 -69.425 22.898 -17.015 1.00 61.59 N ANISOU 2564 N ALA B 575 5990 7563 9848 -776 480 -547 N ATOM 2565 CA ALA B 575 -70.014 24.112 -16.452 1.00 61.32 C ANISOU 2565 CA ALA B 575 5819 7648 9830 -662 457 -615 C ATOM 2566 C ALA B 575 -69.157 25.379 -16.598 1.00 59.90 C ANISOU 2566 C ALA B 575 5684 7380 9693 -478 378 -583 C ATOM 2567 O ALA B 575 -69.675 26.479 -16.431 1.00 60.63 O ANISOU 2567 O ALA B 575 5678 7555 9800 -359 332 -644 O ATOM 2568 CB ALA B 575 -70.368 23.887 -14.994 1.00 61.40 C ANISOU 2568 CB ALA B 575 5797 7734 9796 -732 553 -637 C ATOM 2569 N THR B 576 -67.867 25.243 -16.888 1.00 58.80 N ANISOU 2569 N THR B 576 5693 7077 9570 -453 362 -492 N ATOM 2570 CA THR B 576 -67.012 26.424 -17.108 1.00 59.48 C ANISOU 2570 CA THR B 576 5827 7079 9693 -303 286 -457 C ATOM 2571 C THR B 576 -67.019 26.817 -18.575 1.00 60.45 C ANISOU 2571 C THR B 576 5952 7173 9842 -243 200 -458 C ATOM 2572 O THR B 576 -67.163 25.959 -19.436 1.00 62.74 O ANISOU 2572 O THR B 576 6263 7450 10124 -322 207 -450 O ATOM 2573 CB THR B 576 -65.557 26.221 -16.622 1.00 58.85 C ANISOU 2573 CB THR B 576 5888 6854 9617 -300 309 -360 C ATOM 2574 OG1 THR B 576 -64.865 27.468 -16.667 1.00 59.28 O ANISOU 2574 OG1 THR B 576 5971 6851 9700 -173 238 -336 O ATOM 2575 CG2 THR B 576 -64.777 25.214 -17.476 1.00 59.39 C ANISOU 2575 CG2 THR B 576 6061 6818 9686 -362 322 -292 C ATOM 2576 N THR B 577 -66.893 28.114 -18.842 1.00 61.55 N ANISOU 2576 N THR B 577 6084 7299 10003 -107 117 -470 N ATOM 2577 CA THR B 577 -66.723 28.636 -20.203 1.00 62.47 C ANISOU 2577 CA THR B 577 6236 7363 10136 -39 28 -459 C ATOM 2578 C THR B 577 -65.270 28.965 -20.532 1.00 61.53 C ANISOU 2578 C THR B 577 6252 7095 10032 -5 8 -364 C ATOM 2579 O THR B 577 -64.993 29.340 -21.672 1.00 62.01 O ANISOU 2579 O THR B 577 6361 7100 10097 35 -53 -344 O ATOM 2580 CB THR B 577 -67.542 29.924 -20.430 1.00 64.25 C ANISOU 2580 CB THR B 577 6384 7660 10365 94 -65 -535 C ATOM 2581 OG1 THR B 577 -67.149 30.908 -19.466 1.00 63.64 O ANISOU 2581 OG1 THR B 577 6334 7556 10290 183 -80 -530 O ATOM 2582 CG2 THR B 577 -69.033 29.646 -20.304 1.00 66.01 C ANISOU 2582 CG2 THR B 577 6448 8057 10577 71 -56 -639 C ATOM 2583 N GLU B 578 -64.357 28.867 -19.554 1.00 60.73 N ANISOU 2583 N GLU B 578 6207 6934 9933 -21 57 -309 N ATOM 2584 CA GLU B 578 -62.915 28.928 -19.839 1.00 60.89 C ANISOU 2584 CA GLU B 578 6337 6830 9966 -13 53 -216 C ATOM 2585 C GLU B 578 -62.517 27.788 -20.760 1.00 59.38 C ANISOU 2585 C GLU B 578 6199 6593 9769 -85 91 -175 C ATOM 2586 O GLU B 578 -62.903 26.631 -20.548 1.00 57.63 O ANISOU 2586 O GLU B 578 5969 6398 9529 -173 154 -188 O ATOM 2587 CB GLU B 578 -62.058 28.798 -18.577 1.00 63.37 C ANISOU 2587 CB GLU B 578 6692 7103 10282 -30 100 -168 C ATOM 2588 CG GLU B 578 -62.023 30.009 -17.684 1.00 65.01 C ANISOU 2588 CG GLU B 578 6892 7316 10492 47 57 -185 C ATOM 2589 CD GLU B 578 -60.742 30.105 -16.881 1.00 65.31 C ANISOU 2589 CD GLU B 578 7003 7275 10537 42 70 -112 C ATOM 2590 OE1 GLU B 578 -59.783 30.745 -17.366 1.00 66.82 O ANISOU 2590 OE1 GLU B 578 7250 7393 10743 74 22 -57 O ATOM 2591 OE2 GLU B 578 -60.712 29.571 -15.754 1.00 65.41 O ANISOU 2591 OE2 GLU B 578 7016 7302 10534 3 125 -111 O ATOM 2592 N LEU B 579 -61.711 28.118 -21.756 1.00 59.27 N ANISOU 2592 N LEU B 579 6251 6504 9763 -52 55 -125 N ATOM 2593 CA LEU B 579 -61.242 27.134 -22.719 1.00 60.00 C ANISOU 2593 CA LEU B 579 6405 6547 9843 -101 89 -86 C ATOM 2594 C LEU B 579 -60.201 26.240 -22.057 1.00 59.53 C ANISOU 2594 C LEU B 579 6402 6432 9782 -141 162 -25 C ATOM 2595 O LEU B 579 -60.228 25.019 -22.228 1.00 61.48 O ANISOU 2595 O LEU B 579 6687 6663 10008 -203 214 -19 O ATOM 2596 CB LEU B 579 -60.675 27.827 -23.961 1.00 60.11 C ANISOU 2596 CB LEU B 579 6475 6506 9858 -51 35 -53 C ATOM 2597 CG LEU B 579 -61.655 28.768 -24.679 1.00 61.72 C ANISOU 2597 CG LEU B 579 6645 6748 10054 2 -53 -111 C ATOM 2598 CD1 LEU B 579 -60.969 29.406 -25.875 1.00 62.21 C ANISOU 2598 CD1 LEU B 579 6791 6740 10104 39 -100 -66 C ATOM 2599 CD2 LEU B 579 -62.938 28.053 -25.095 1.00 61.92 C ANISOU 2599 CD2 LEU B 579 6611 6849 10064 -39 -57 -182 C ATOM 2600 N ARG B 580 -59.319 26.858 -21.277 1.00 57.13 N ANISOU 2600 N ARG B 580 6110 6099 9498 -103 157 17 N ATOM 2601 CA ARG B 580 -58.287 26.160 -20.543 1.00 56.08 C ANISOU 2601 CA ARG B 580 6022 5919 9364 -121 210 73 C ATOM 2602 C ARG B 580 -58.344 26.583 -19.092 1.00 55.27 C ANISOU 2602 C ARG B 580 5893 5839 9268 -114 210 64 C ATOM 2603 O ARG B 580 -58.254 27.769 -18.794 1.00 56.41 O ANISOU 2603 O ARG B 580 6015 5989 9427 -64 158 60 O ATOM 2604 CB ARG B 580 -56.926 26.522 -21.114 1.00 56.95 C ANISOU 2604 CB ARG B 580 6174 5973 9490 -82 199 143 C ATOM 2605 CG ARG B 580 -56.868 26.390 -22.618 1.00 57.96 C ANISOU 2605 CG ARG B 580 6332 6082 9607 -78 192 150 C ATOM 2606 CD ARG B 580 -55.461 26.597 -23.119 1.00 59.24 C ANISOU 2606 CD ARG B 580 6528 6204 9777 -51 202 219 C ATOM 2607 NE ARG B 580 -55.457 26.629 -24.566 1.00 60.89 N ANISOU 2607 NE ARG B 580 6771 6398 9966 -46 195 223 N ATOM 2608 CZ ARG B 580 -54.375 26.716 -25.324 1.00 62.02 C ANISOU 2608 CZ ARG B 580 6944 6517 10103 -31 215 276 C ATOM 2609 NH1 ARG B 580 -53.160 26.777 -24.788 1.00 62.16 N ANISOU 2609 NH1 ARG B 580 6947 6532 10139 -18 240 329 N ATOM 2610 NH2 ARG B 580 -54.521 26.744 -26.642 1.00 63.71 N ANISOU 2610 NH2 ARG B 580 7200 6718 10289 -31 210 272 N ATOM 2611 N THR B 581 -58.451 25.611 -18.193 1.00 54.86 N ANISOU 2611 N THR B 581 5860 5788 9194 -165 266 62 N ATOM 2612 CA THR B 581 -58.578 25.872 -16.772 1.00 54.59 C ANISOU 2612 CA THR B 581 5813 5775 9152 -167 276 51 C ATOM 2613 C THR B 581 -57.261 25.608 -16.023 1.00 54.72 C ANISOU 2613 C THR B 581 5890 5727 9172 -152 286 119 C ATOM 2614 O THR B 581 -56.793 24.476 -15.944 1.00 56.54 O ANISOU 2614 O THR B 581 6182 5917 9384 -180 329 151 O ATOM 2615 CB THR B 581 -59.719 25.032 -16.178 1.00 55.58 C ANISOU 2615 CB THR B 581 5920 5957 9240 -246 331 -2 C ATOM 2616 OG1 THR B 581 -60.948 25.344 -16.854 1.00 55.52 O ANISOU 2616 OG1 THR B 581 5833 6028 9232 -255 313 -71 O ATOM 2617 CG2 THR B 581 -59.874 25.310 -14.700 1.00 56.33 C ANISOU 2617 CG2 THR B 581 6008 6076 9316 -250 348 -16 C ATOM 2618 N PHE B 582 -56.690 26.675 -15.467 1.00 54.29 N ANISOU 2618 N PHE B 582 5824 5664 9138 -103 239 139 N ATOM 2619 CA PHE B 582 -55.473 26.631 -14.653 1.00 52.88 C ANISOU 2619 CA PHE B 582 5687 5440 8965 -85 231 198 C ATOM 2620 C PHE B 582 -55.696 26.948 -13.166 1.00 54.00 C ANISOU 2620 C PHE B 582 5839 5592 9086 -88 226 180 C ATOM 2621 O PHE B 582 -54.752 26.934 -12.404 1.00 54.25 O ANISOU 2621 O PHE B 582 5907 5588 9118 -74 211 225 O ATOM 2622 CB PHE B 582 -54.465 27.630 -15.210 1.00 52.01 C ANISOU 2622 CB PHE B 582 5564 5307 8890 -42 173 243 C ATOM 2623 CG PHE B 582 -53.974 27.296 -16.588 1.00 51.83 C ANISOU 2623 CG PHE B 582 5542 5270 8881 -37 185 272 C ATOM 2624 CD1 PHE B 582 -52.812 26.554 -16.758 1.00 51.58 C ANISOU 2624 CD1 PHE B 582 5532 5210 8853 -26 211 327 C ATOM 2625 CD2 PHE B 582 -54.653 27.739 -17.713 1.00 52.36 C ANISOU 2625 CD2 PHE B 582 5590 5354 8950 -35 168 241 C ATOM 2626 CE1 PHE B 582 -52.337 26.251 -18.013 1.00 51.68 C ANISOU 2626 CE1 PHE B 582 5548 5216 8872 -15 230 350 C ATOM 2627 CE2 PHE B 582 -54.192 27.424 -18.985 1.00 52.92 C ANISOU 2627 CE2 PHE B 582 5673 5408 9023 -32 183 268 C ATOM 2628 CZ PHE B 582 -53.025 26.675 -19.131 1.00 52.80 C ANISOU 2628 CZ PHE B 582 5679 5369 9010 -23 219 322 C ATOM 2629 N SER B 583 -56.931 27.206 -12.739 1.00 55.78 N ANISOU 2629 N SER B 583 6030 5874 9288 -104 241 114 N ATOM 2630 CA SER B 583 -57.188 27.739 -11.392 1.00 56.01 C ANISOU 2630 CA SER B 583 6067 5921 9292 -94 234 90 C ATOM 2631 C SER B 583 -57.682 26.726 -10.349 1.00 54.85 C ANISOU 2631 C SER B 583 5957 5789 9093 -158 305 73 C ATOM 2632 O SER B 583 -57.900 27.098 -9.201 1.00 55.16 O ANISOU 2632 O SER B 583 6011 5844 9102 -154 308 52 O ATOM 2633 CB SER B 583 -58.192 28.884 -11.505 1.00 57.81 C ANISOU 2633 CB SER B 583 6233 6209 9522 -51 200 21 C ATOM 2634 OG SER B 583 -59.385 28.426 -12.140 1.00 62.36 O ANISOU 2634 OG SER B 583 6747 6855 10089 -82 239 -37 O ATOM 2635 N ILE B 584 -57.837 25.456 -10.710 1.00 54.31 N ANISOU 2635 N ILE B 584 5919 5709 9005 -221 360 82 N ATOM 2636 CA ILE B 584 -58.384 24.469 -9.767 1.00 54.78 C ANISOU 2636 CA ILE B 584 6032 5779 9003 -301 429 66 C ATOM 2637 C ILE B 584 -57.601 24.388 -8.455 1.00 55.29 C ANISOU 2637 C ILE B 584 6182 5788 9037 -289 421 106 C ATOM 2638 O ILE B 584 -58.213 24.449 -7.388 1.00 57.62 O ANISOU 2638 O ILE B 584 6491 6118 9283 -324 455 73 O ATOM 2639 CB ILE B 584 -58.532 23.053 -10.387 1.00 55.35 C ANISOU 2639 CB ILE B 584 6158 5820 9050 -376 480 79 C ATOM 2640 CG1 ILE B 584 -59.637 23.043 -11.448 1.00 55.13 C ANISOU 2640 CG1 ILE B 584 6046 5865 9034 -415 496 23 C ATOM 2641 CG2 ILE B 584 -58.876 22.009 -9.316 1.00 56.56 C ANISOU 2641 CG2 ILE B 584 6404 5957 9128 -468 544 78 C ATOM 2642 CD1 ILE B 584 -59.665 21.775 -12.288 1.00 55.61 C ANISOU 2642 CD1 ILE B 584 6169 5883 9075 -480 528 39 C ATOM 2643 N LEU B 585 -56.275 24.261 -8.514 1.00 55.88 N ANISOU 2643 N LEU B 585 6308 5786 9135 -241 377 173 N ATOM 2644 CA LEU B 585 -55.485 24.164 -7.275 1.00 57.12 C ANISOU 2644 CA LEU B 585 6548 5892 9262 -225 356 212 C ATOM 2645 C LEU B 585 -55.507 25.427 -6.412 1.00 57.64 C ANISOU 2645 C LEU B 585 6588 5982 9329 -186 311 193 C ATOM 2646 O LEU B 585 -55.645 25.324 -5.187 1.00 58.36 O ANISOU 2646 O LEU B 585 6743 6066 9366 -207 326 186 O ATOM 2647 CB LEU B 585 -54.048 23.718 -7.552 1.00 58.39 C ANISOU 2647 CB LEU B 585 6754 5982 9449 -173 312 283 C ATOM 2648 CG LEU B 585 -53.910 22.279 -8.088 1.00 59.65 C ANISOU 2648 CG LEU B 585 6986 6094 9584 -198 355 304 C ATOM 2649 CD1 LEU B 585 -52.440 21.948 -8.255 1.00 60.01 C ANISOU 2649 CD1 LEU B 585 7063 6084 9654 -121 307 367 C ATOM 2650 CD2 LEU B 585 -54.615 21.221 -7.235 1.00 59.31 C ANISOU 2650 CD2 LEU B 585 7052 6024 9457 -280 415 289 C ATOM 2651 N ASN B 586 -55.398 26.609 -7.024 1.00 57.78 N ANISOU 2651 N ASN B 586 6530 6023 9398 -133 256 183 N ATOM 2652 CA ASN B 586 -55.525 27.869 -6.260 1.00 58.10 C ANISOU 2652 CA ASN B 586 6563 6079 9432 -94 209 157 C ATOM 2653 C ASN B 586 -56.881 27.986 -5.578 1.00 58.25 C ANISOU 2653 C ASN B 586 6566 6167 9399 -118 266 80 C ATOM 2654 O ASN B 586 -56.969 28.448 -4.446 1.00 56.75 O ANISOU 2654 O ASN B 586 6417 5977 9167 -104 259 63 O ATOM 2655 CB ASN B 586 -55.299 29.096 -7.141 1.00 58.45 C ANISOU 2655 CB ASN B 586 6548 6127 9531 -40 139 155 C ATOM 2656 CG ASN B 586 -53.831 29.369 -7.414 1.00 59.42 C ANISOU 2656 CG ASN B 586 6688 6194 9695 -18 71 229 C ATOM 2657 OD1 ASN B 586 -52.932 28.728 -6.859 1.00 62.06 O ANISOU 2657 OD1 ASN B 586 7068 6491 10022 -26 65 278 O ATOM 2658 ND2 ASN B 586 -53.581 30.333 -8.277 1.00 59.98 N ANISOU 2658 ND2 ASN B 586 6720 6262 9805 7 17 236 N ATOM 2659 N ARG B 587 -57.932 27.551 -6.266 1.00 59.95 N ANISOU 2659 N ARG B 587 6718 6448 9613 -155 325 33 N ATOM 2660 CA ARG B 587 -59.265 27.570 -5.695 1.00 60.74 C ANISOU 2660 CA ARG B 587 6776 6639 9662 -186 390 -43 C ATOM 2661 C ARG B 587 -59.383 26.591 -4.533 1.00 61.20 C ANISOU 2661 C ARG B 587 6918 6687 9645 -266 461 -35 C ATOM 2662 O ARG B 587 -60.044 26.895 -3.552 1.00 62.81 O ANISOU 2662 O ARG B 587 7124 6944 9795 -275 499 -82 O ATOM 2663 CB ARG B 587 -60.328 27.299 -6.749 1.00 62.79 C ANISOU 2663 CB ARG B 587 6937 6980 9939 -217 428 -96 C ATOM 2664 CG ARG B 587 -61.719 27.680 -6.271 1.00 67.17 C ANISOU 2664 CG ARG B 587 7408 7659 10455 -222 478 -189 C ATOM 2665 CD ARG B 587 -62.788 27.466 -7.328 1.00 70.53 C ANISOU 2665 CD ARG B 587 7719 8180 10900 -248 502 -246 C ATOM 2666 NE ARG B 587 -64.122 27.398 -6.727 1.00 74.08 N ANISOU 2666 NE ARG B 587 8083 8766 11297 -290 578 -332 N ATOM 2667 CZ ARG B 587 -65.265 27.331 -7.407 1.00 76.82 C ANISOU 2667 CZ ARG B 587 8303 9232 11650 -311 602 -402 C ATOM 2668 NH1 ARG B 587 -66.422 27.298 -6.742 1.00 77.86 N ANISOU 2668 NH1 ARG B 587 8345 9505 11731 -349 676 -482 N ATOM 2669 NH2 ARG B 587 -65.268 27.264 -8.740 1.00 78.40 N ANISOU 2669 NH2 ARG B 587 8463 9421 11904 -299 554 -394 N ATOM 2670 N LYS B 588 -58.740 25.429 -4.624 1.00 61.07 N ANISOU 2670 N LYS B 588 6984 6600 9619 -320 478 24 N ATOM 2671 CA LYS B 588 -58.708 24.493 -3.486 1.00 61.40 C ANISOU 2671 CA LYS B 588 7142 6606 9580 -392 531 43 C ATOM 2672 C LYS B 588 -57.973 25.066 -2.267 1.00 60.24 C ANISOU 2672 C LYS B 588 7074 6409 9405 -342 484 68 C ATOM 2673 O LYS B 588 -58.425 24.877 -1.135 1.00 61.02 O ANISOU 2673 O LYS B 588 7234 6523 9424 -388 533 47 O ATOM 2674 CB LYS B 588 -58.101 23.145 -3.888 1.00 62.23 C ANISOU 2674 CB LYS B 588 7339 6628 9675 -441 544 101 C ATOM 2675 CG LYS B 588 -59.037 22.325 -4.742 1.00 63.98 C ANISOU 2675 CG LYS B 588 7525 6896 9888 -529 610 70 C ATOM 2676 CD LYS B 588 -58.591 20.885 -4.844 1.00 66.15 C ANISOU 2676 CD LYS B 588 7934 7077 10121 -590 632 120 C ATOM 2677 CE LYS B 588 -59.610 20.058 -5.602 1.00 67.06 C ANISOU 2677 CE LYS B 588 8028 7236 10214 -701 698 85 C ATOM 2678 NZ LYS B 588 -60.905 20.001 -4.877 1.00 68.22 N ANISOU 2678 NZ LYS B 588 8141 7482 10295 -813 781 23 N ATOM 2679 N ALA B 589 -56.861 25.768 -2.503 1.00 57.57 N ANISOU 2679 N ALA B 589 6733 6014 9124 -258 389 113 N ATOM 2680 CA ALA B 589 -56.159 26.498 -1.439 1.00 56.39 C ANISOU 2680 CA ALA B 589 6646 5822 8954 -208 325 132 C ATOM 2681 C ALA B 589 -57.074 27.515 -0.776 1.00 56.02 C ANISOU 2681 C ALA B 589 6568 5843 8873 -187 342 61 C ATOM 2682 O ALA B 589 -57.130 27.599 0.442 1.00 56.89 O ANISOU 2682 O ALA B 589 6758 5941 8913 -196 353 52 O ATOM 2683 CB ALA B 589 -54.923 27.190 -1.988 1.00 55.76 C ANISOU 2683 CB ALA B 589 6543 5693 8950 -137 221 184 C ATOM 2684 N ILE B 590 -57.823 28.265 -1.579 1.00 56.01 N ANISOU 2684 N ILE B 590 6455 5912 8911 -153 343 7 N ATOM 2685 CA ILE B 590 -58.753 29.261 -1.037 1.00 55.87 C ANISOU 2685 CA ILE B 590 6400 5968 8860 -109 356 -71 C ATOM 2686 C ILE B 590 -59.833 28.577 -0.198 1.00 56.51 C ANISOU 2686 C ILE B 590 6488 6126 8855 -183 471 -123 C ATOM 2687 O ILE B 590 -60.093 28.992 0.928 1.00 57.13 O ANISOU 2687 O ILE B 590 6617 6222 8867 -167 489 -156 O ATOM 2688 CB ILE B 590 -59.363 30.155 -2.141 1.00 54.55 C ANISOU 2688 CB ILE B 590 6117 5860 8750 -45 326 -122 C ATOM 2689 CG1 ILE B 590 -58.268 31.020 -2.776 1.00 53.09 C ANISOU 2689 CG1 ILE B 590 5948 5591 8630 18 211 -70 C ATOM 2690 CG2 ILE B 590 -60.464 31.051 -1.574 1.00 55.36 C ANISOU 2690 CG2 ILE B 590 6175 6050 8806 13 349 -216 C ATOM 2691 CD1 ILE B 590 -58.626 31.557 -4.147 1.00 52.38 C ANISOU 2691 CD1 ILE B 590 5769 5533 8600 60 179 -93 C ATOM 2692 N ASP B 591 -60.433 27.518 -0.733 1.00 57.52 N ANISOU 2692 N ASP B 591 6575 6300 8978 -271 549 -130 N ATOM 2693 CA ASP B 591 -61.418 26.734 0.025 1.00 59.76 C ANISOU 2693 CA ASP B 591 6871 6659 9173 -374 666 -172 C ATOM 2694 C ASP B 591 -60.843 26.097 1.291 1.00 60.82 C ANISOU 2694 C ASP B 591 7168 6713 9225 -427 686 -124 C ATOM 2695 O ASP B 591 -61.528 26.039 2.306 1.00 62.81 O ANISOU 2695 O ASP B 591 7450 7022 9390 -473 762 -166 O ATOM 2696 CB ASP B 591 -62.081 25.672 -0.854 1.00 60.31 C ANISOU 2696 CB ASP B 591 6883 6779 9252 -477 734 -180 C ATOM 2697 CG ASP B 591 -63.054 26.266 -1.853 1.00 61.33 C ANISOU 2697 CG ASP B 591 6841 7026 9433 -440 737 -253 C ATOM 2698 OD1 ASP B 591 -63.628 27.330 -1.585 1.00 62.80 O ANISOU 2698 OD1 ASP B 591 6950 7292 9616 -357 728 -320 O ATOM 2699 OD2 ASP B 591 -63.249 25.667 -2.922 1.00 64.57 O ANISOU 2699 OD2 ASP B 591 7201 7447 9882 -487 744 -246 O ATOM 2700 N PHE B 592 -59.593 25.643 1.241 1.00 60.75 N ANISOU 2700 N PHE B 592 7262 6578 9240 -415 617 -39 N ATOM 2701 CA PHE B 592 -58.902 25.162 2.442 1.00 61.50 C ANISOU 2701 CA PHE B 592 7521 6584 9260 -440 607 9 C ATOM 2702 C PHE B 592 -58.934 26.236 3.536 1.00 62.12 C ANISOU 2702 C PHE B 592 7630 6676 9294 -378 582 -23 C ATOM 2703 O PHE B 592 -59.343 25.967 4.657 1.00 64.34 O ANISOU 2703 O PHE B 592 7999 6970 9475 -430 644 -42 O ATOM 2704 CB PHE B 592 -57.453 24.757 2.114 1.00 61.12 C ANISOU 2704 CB PHE B 592 7548 6412 9261 -397 511 97 C ATOM 2705 CG PHE B 592 -56.701 24.190 3.283 1.00 62.28 C ANISOU 2705 CG PHE B 592 7867 6465 9332 -412 485 149 C ATOM 2706 CD1 PHE B 592 -56.617 22.814 3.470 1.00 62.47 C ANISOU 2706 CD1 PHE B 592 8013 6427 9295 -490 527 187 C ATOM 2707 CD2 PHE B 592 -56.070 25.037 4.205 1.00 63.13 C ANISOU 2707 CD2 PHE B 592 8029 6534 9421 -346 409 159 C ATOM 2708 CE1 PHE B 592 -55.926 22.288 4.549 1.00 62.91 C ANISOU 2708 CE1 PHE B 592 8241 6387 9272 -494 493 234 C ATOM 2709 CE2 PHE B 592 -55.383 24.517 5.291 1.00 63.69 C ANISOU 2709 CE2 PHE B 592 8263 6518 9418 -355 376 205 C ATOM 2710 CZ PHE B 592 -55.308 23.138 5.458 1.00 64.19 C ANISOU 2710 CZ PHE B 592 8446 6522 9421 -425 417 243 C ATOM 2711 N LEU B 593 -58.515 27.449 3.192 1.00 61.26 N ANISOU 2711 N LEU B 593 7461 6560 9252 -272 491 -31 N ATOM 2712 CA LEU B 593 -58.518 28.566 4.136 1.00 61.40 C ANISOU 2712 CA LEU B 593 7518 6580 9230 -204 453 -65 C ATOM 2713 C LEU B 593 -59.925 28.956 4.600 1.00 63.58 C ANISOU 2713 C LEU B 593 7734 6981 9440 -208 552 -164 C ATOM 2714 O LEU B 593 -60.130 29.176 5.792 1.00 65.53 O ANISOU 2714 O LEU B 593 8065 7233 9597 -208 582 -189 O ATOM 2715 CB LEU B 593 -57.818 29.783 3.526 1.00 59.67 C ANISOU 2715 CB LEU B 593 7254 6322 9095 -102 331 -54 C ATOM 2716 CG LEU B 593 -56.317 29.594 3.302 1.00 58.00 C ANISOU 2716 CG LEU B 593 7099 6001 8936 -91 226 38 C ATOM 2717 CD1 LEU B 593 -55.776 30.590 2.297 1.00 57.13 C ANISOU 2717 CD1 LEU B 593 6912 5875 8920 -26 131 51 C ATOM 2718 CD2 LEU B 593 -55.575 29.703 4.624 1.00 58.73 C ANISOU 2718 CD2 LEU B 593 7331 6018 8962 -85 172 70 C ATOM 2719 N LEU B 594 -60.889 29.038 3.679 1.00 64.47 N ANISOU 2719 N LEU B 594 7699 7200 9593 -208 603 -221 N ATOM 2720 CA LEU B 594 -62.262 29.448 4.046 1.00 65.76 C ANISOU 2720 CA LEU B 594 7774 7509 9701 -198 696 -324 C ATOM 2721 C LEU B 594 -62.970 28.457 4.977 1.00 67.69 C ANISOU 2721 C LEU B 594 8064 7816 9836 -324 831 -344 C ATOM 2722 O LEU B 594 -63.743 28.868 5.835 1.00 69.22 O ANISOU 2722 O LEU B 594 8249 8101 9950 -310 901 -414 O ATOM 2723 CB LEU B 594 -63.127 29.701 2.807 1.00 64.59 C ANISOU 2723 CB LEU B 594 7449 7469 9623 -169 711 -382 C ATOM 2724 CG LEU B 594 -62.761 30.908 1.948 1.00 64.07 C ANISOU 2724 CG LEU B 594 7332 7368 9642 -36 592 -389 C ATOM 2725 CD1 LEU B 594 -63.618 30.909 0.693 1.00 63.81 C ANISOU 2725 CD1 LEU B 594 7139 7436 9669 -25 609 -439 C ATOM 2726 CD2 LEU B 594 -62.891 32.234 2.691 1.00 64.57 C ANISOU 2726 CD2 LEU B 594 7431 7435 9666 87 545 -445 C ATOM 2727 N GLN B 595 -62.699 27.164 4.805 1.00 68.89 N ANISOU 2727 N GLN B 595 8277 7919 9977 -445 868 -282 N ATOM 2728 CA GLN B 595 -63.238 26.123 5.685 1.00 71.69 C ANISOU 2728 CA GLN B 595 8714 8306 10218 -587 988 -284 C ATOM 2729 C GLN B 595 -62.831 26.359 7.141 1.00 71.89 C ANISOU 2729 C GLN B 595 8900 8271 10144 -572 986 -272 C ATOM 2730 O GLN B 595 -63.624 26.128 8.055 1.00 73.33 O ANISOU 2730 O GLN B 595 9111 8533 10216 -646 1097 -317 O ATOM 2731 CB GLN B 595 -62.760 24.745 5.224 1.00 74.14 C ANISOU 2731 CB GLN B 595 9108 8527 10534 -701 994 -207 C ATOM 2732 CG GLN B 595 -63.469 23.565 5.875 1.00 78.96 C ANISOU 2732 CG GLN B 595 9799 9174 11028 -875 1123 -210 C ATOM 2733 CD GLN B 595 -63.034 22.207 5.321 1.00 82.24 C ANISOU 2733 CD GLN B 595 10313 9487 11445 -980 1119 -137 C ATOM 2734 OE1 GLN B 595 -63.682 21.191 5.583 1.00 86.57 O ANISOU 2734 OE1 GLN B 595 10921 10064 11907 -1139 1220 -140 O ATOM 2735 NE2 GLN B 595 -61.931 22.178 4.563 1.00 82.26 N ANISOU 2735 NE2 GLN B 595 10342 9373 11539 -893 1004 -73 N ATOM 2736 N ARG B 596 -61.603 26.843 7.338 1.00 70.84 N ANISOU 2736 N ARG B 596 8866 8004 10046 -481 858 -212 N ATOM 2737 CA ARG B 596 -61.037 27.079 8.664 1.00 70.63 C ANISOU 2737 CA ARG B 596 9006 7897 9931 -460 826 -190 C ATOM 2738 C ARG B 596 -61.240 28.488 9.168 1.00 69.55 C ANISOU 2738 C ARG B 596 8844 7799 9781 -339 791 -254 C ATOM 2739 O ARG B 596 -61.613 28.665 10.313 1.00 72.52 O ANISOU 2739 O ARG B 596 9304 8201 10047 -348 847 -290 O ATOM 2740 CB ARG B 596 -59.545 26.756 8.669 1.00 70.91 C ANISOU 2740 CB ARG B 596 9168 7769 10005 -434 699 -89 C ATOM 2741 CG ARG B 596 -59.273 25.269 8.615 1.00 72.56 C ANISOU 2741 CG ARG B 596 9477 7913 10180 -545 734 -25 C ATOM 2742 CD ARG B 596 -57.829 24.976 8.252 1.00 73.51 C ANISOU 2742 CD ARG B 596 9665 7896 10367 -492 602 64 C ATOM 2743 NE ARG B 596 -57.589 23.540 8.139 1.00 75.00 N ANISOU 2743 NE ARG B 596 9959 8016 10521 -579 630 120 N ATOM 2744 CZ ARG B 596 -57.974 22.770 7.120 1.00 77.15 C ANISOU 2744 CZ ARG B 596 10165 8314 10834 -639 681 123 C ATOM 2745 NH1 ARG B 596 -58.629 23.266 6.063 1.00 76.74 N ANISOU 2745 NH1 ARG B 596 9927 8364 10867 -624 710 73 N ATOM 2746 NH2 ARG B 596 -57.681 21.473 7.150 1.00 79.36 N ANISOU 2746 NH2 ARG B 596 10580 8508 11064 -712 694 175 N ATOM 2747 N TRP B 597 -60.991 29.484 8.324 1.00 67.56 N ANISOU 2747 N TRP B 597 8491 7545 9631 -228 697 -268 N ATOM 2748 CA TRP B 597 -60.939 30.888 8.756 1.00 67.28 C ANISOU 2748 CA TRP B 597 8472 7505 9587 -100 628 -316 C ATOM 2749 C TRP B 597 -62.046 31.787 8.177 1.00 67.20 C ANISOU 2749 C TRP B 597 8301 7625 9603 -13 663 -418 C ATOM 2750 O TRP B 597 -61.975 33.010 8.290 1.00 65.31 O ANISOU 2750 O TRP B 597 8074 7369 9371 107 587 -457 O ATOM 2751 CB TRP B 597 -59.556 31.441 8.415 1.00 66.23 C ANISOU 2751 CB TRP B 597 8398 7233 9534 -37 463 -242 C ATOM 2752 CG TRP B 597 -58.475 30.545 8.903 1.00 66.16 C ANISOU 2752 CG TRP B 597 8522 7109 9504 -105 420 -148 C ATOM 2753 CD1 TRP B 597 -57.734 29.683 8.162 1.00 65.49 C ANISOU 2753 CD1 TRP B 597 8425 6968 9489 -151 385 -72 C ATOM 2754 CD2 TRP B 597 -58.048 30.380 10.262 1.00 67.44 C ANISOU 2754 CD2 TRP B 597 8859 7203 9562 -125 407 -125 C ATOM 2755 NE1 TRP B 597 -56.847 29.004 8.963 1.00 66.35 N ANISOU 2755 NE1 TRP B 597 8685 6978 9547 -188 344 -4 N ATOM 2756 CE2 TRP B 597 -57.019 29.409 10.259 1.00 66.96 C ANISOU 2756 CE2 TRP B 597 8882 7043 9517 -178 353 -33 C ATOM 2757 CE3 TRP B 597 -58.424 30.969 11.479 1.00 68.59 C ANISOU 2757 CE3 TRP B 597 9104 7359 9596 -96 431 -176 C ATOM 2758 CZ2 TRP B 597 -56.358 29.006 11.427 1.00 67.42 C ANISOU 2758 CZ2 TRP B 597 9120 7011 9486 -202 315 11 C ATOM 2759 CZ3 TRP B 597 -57.764 30.573 12.647 1.00 69.77 C ANISOU 2759 CZ3 TRP B 597 9438 7415 9653 -131 398 -129 C ATOM 2760 CH2 TRP B 597 -56.739 29.595 12.608 1.00 68.64 C ANISOU 2760 CH2 TRP B 597 9376 7173 9531 -184 337 -35 C ATOM 2761 N GLY B 598 -63.074 31.179 7.593 1.00 67.97 N ANISOU 2761 N GLY B 598 8260 7854 9711 -75 773 -462 N ATOM 2762 CA GLY B 598 -64.131 31.912 6.911 1.00 70.14 C ANISOU 2762 CA GLY B 598 8364 8265 10021 9 799 -558 C ATOM 2763 C GLY B 598 -65.164 32.577 7.803 1.00 73.95 C ANISOU 2763 C GLY B 598 8817 8872 10406 77 880 -667 C ATOM 2764 O GLY B 598 -65.963 33.381 7.332 1.00 74.76 O ANISOU 2764 O GLY B 598 8791 9080 10532 187 879 -755 O ATOM 2765 N GLY B 599 -65.181 32.219 9.081 1.00 77.99 N ANISOU 2765 N GLY B 599 9449 9379 10803 17 953 -666 N ATOM 2766 CA GLY B 599 -66.045 32.866 10.060 1.00 81.25 C ANISOU 2766 CA GLY B 599 9858 9902 11108 87 1034 -767 C ATOM 2767 C GLY B 599 -65.231 33.266 11.267 1.00 83.73 C ANISOU 2767 C GLY B 599 10387 10085 11340 120 978 -734 C ATOM 2768 O GLY B 599 -64.021 33.495 11.164 1.00 84.18 O ANISOU 2768 O GLY B 599 10562 9974 11448 142 839 -651 O ATOM 2769 N THR B 600 -65.907 33.364 12.408 1.00 86.98 N ANISOU 2769 N THR B 600 10844 10582 11621 121 1086 -801 N ATOM 2770 CA THR B 600 -65.256 33.641 13.681 1.00 87.87 C ANISOU 2770 CA THR B 600 11173 10581 11631 137 1051 -776 C ATOM 2771 C THR B 600 -64.723 32.318 14.232 1.00 88.33 C ANISOU 2771 C THR B 600 11361 10564 11635 -38 1096 -682 C ATOM 2772 O THR B 600 -65.428 31.311 14.221 1.00 88.76 O ANISOU 2772 O THR B 600 11352 10722 11650 -173 1234 -690 O ATOM 2773 CB THR B 600 -66.229 34.327 14.666 1.00 89.41 C ANISOU 2773 CB THR B 600 11371 10902 11698 223 1152 -894 C ATOM 2774 OG1 THR B 600 -66.520 35.645 14.190 1.00 88.32 O ANISOU 2774 OG1 THR B 600 11157 10791 11607 414 1074 -972 O ATOM 2775 CG2 THR B 600 -65.634 34.441 16.064 1.00 91.07 C ANISOU 2775 CG2 THR B 600 11819 11001 11781 215 1136 -867 C ATOM 2776 N CYS B 601 -63.478 32.330 14.702 1.00 89.27 N ANISOU 2776 N CYS B 601 11667 10502 11750 -38 973 -595 N ATOM 2777 CA CYS B 601 -62.849 31.135 15.261 1.00 91.09 C ANISOU 2777 CA CYS B 601 12049 10637 11924 -179 988 -504 C ATOM 2778 C CYS B 601 -63.217 31.011 16.754 1.00 94.35 C ANISOU 2778 C CYS B 601 12620 11069 12161 -221 1084 -536 C ATOM 2779 O CYS B 601 -62.626 31.684 17.603 1.00 94.04 O ANISOU 2779 O CYS B 601 12735 10932 12061 -147 1000 -531 O ATOM 2780 CB CYS B 601 -61.324 31.188 15.050 1.00 89.35 C ANISOU 2780 CB CYS B 601 11940 10227 11782 -151 804 -399 C ATOM 2781 SG CYS B 601 -60.548 29.585 14.742 1.00 89.38 S ANISOU 2781 SG CYS B 601 12014 10133 11812 -296 792 -281 S ATOM 2782 N HIS B 602 -64.208 30.168 17.059 1.00 97.58 N ANISOU 2782 N HIS B 602 12990 11605 12480 -347 1261 -570 N ATOM 2783 CA HIS B 602 -64.607 29.889 18.451 1.00101.34 C ANISOU 2783 CA HIS B 602 13621 12108 12775 -416 1376 -595 C ATOM 2784 C HIS B 602 -63.581 28.960 19.106 1.00101.07 C ANISOU 2784 C HIS B 602 13827 11896 12679 -519 1315 -483 C ATOM 2785 O HIS B 602 -63.538 27.770 18.780 1.00101.66 O ANISOU 2785 O HIS B 602 13919 11949 12758 -658 1357 -422 O ATOM 2786 CB HIS B 602 -66.004 29.237 18.510 1.00104.44 C ANISOU 2786 CB HIS B 602 13884 12706 13089 -542 1592 -666 C ATOM 2787 CG HIS B 602 -67.130 30.168 18.170 1.00106.80 C ANISOU 2787 CG HIS B 602 13962 13207 13410 -430 1669 -794 C ATOM 2788 ND1 HIS B 602 -67.521 30.424 16.872 1.00106.68 N ANISOU 2788 ND1 HIS B 602 13717 13279 13537 -375 1643 -828 N ATOM 2789 CD2 HIS B 602 -67.956 30.894 18.961 1.00107.98 C ANISOU 2789 CD2 HIS B 602 14087 13489 13450 -352 1769 -902 C ATOM 2790 CE1 HIS B 602 -68.530 31.278 16.878 1.00107.11 C ANISOU 2790 CE1 HIS B 602 13614 13509 13572 -261 1715 -950 C ATOM 2791 NE2 HIS B 602 -68.814 31.578 18.133 1.00108.27 N ANISOU 2791 NE2 HIS B 602 13878 13691 13568 -242 1796 -999 N ATOM 2792 N ILE B 603 -62.780 29.489 20.036 1.00100.92 N ANISOU 2792 N ILE B 603 14001 11747 12595 -447 1211 -458 N ATOM 2793 CA ILE B 603 -61.657 28.726 20.612 1.00101.70 C ANISOU 2793 CA ILE B 603 14328 11663 12648 -512 1114 -350 C ATOM 2794 C ILE B 603 -62.185 27.532 21.423 1.00105.68 C ANISOU 2794 C ILE B 603 14971 12190 12993 -685 1264 -332 C ATOM 2795 O ILE B 603 -63.200 27.636 22.124 1.00106.71 O ANISOU 2795 O ILE B 603 15101 12446 12995 -730 1423 -408 O ATOM 2796 CB ILE B 603 -60.701 29.592 21.472 1.00100.56 C ANISOU 2796 CB ILE B 603 14362 11383 12463 -402 961 -331 C ATOM 2797 CG1 ILE B 603 -60.124 30.754 20.655 1.00 99.42 C ANISOU 2797 CG1 ILE B 603 14099 11205 12470 -253 805 -340 C ATOM 2798 CG2 ILE B 603 -59.543 28.747 22.001 1.00100.31 C ANISOU 2798 CG2 ILE B 603 14546 11175 12391 -462 850 -221 C ATOM 2799 CD1 ILE B 603 -59.259 31.710 21.452 1.00 99.92 C ANISOU 2799 CD1 ILE B 603 14326 11145 12493 -154 652 -331 C ATOM 2800 N LEU B 604 -61.494 26.398 21.284 1.00107.80 N ANISOU 2800 N LEU B 604 15354 12336 13267 -781 1214 -234 N ATOM 2801 CA LEU B 604 -61.942 25.083 21.774 1.00111.06 C ANISOU 2801 CA LEU B 604 15901 12749 13547 -967 1344 -201 C ATOM 2802 C LEU B 604 -63.222 24.531 21.102 1.00112.25 C ANISOU 2802 C LEU B 604 15864 13078 13704 -1095 1529 -254 C ATOM 2803 O LEU B 604 -63.733 23.491 21.522 1.00113.54 O ANISOU 2803 O LEU B 604 16132 13260 13745 -1271 1655 -236 O ATOM 2804 CB LEU B 604 -62.036 25.044 23.320 1.00114.71 C ANISOU 2804 CB LEU B 604 16608 13172 13803 -1013 1400 -208 C ATOM 2805 CG LEU B 604 -60.794 24.552 24.082 1.00115.37 C ANISOU 2805 CG LEU B 604 16976 13038 13819 -1009 1251 -109 C ATOM 2806 CD1 LEU B 604 -60.465 23.090 23.769 1.00115.25 C ANISOU 2806 CD1 LEU B 604 17073 12924 13791 -1139 1246 -19 C ATOM 2807 CD2 LEU B 604 -59.594 25.453 23.820 1.00113.94 C ANISOU 2807 CD2 LEU B 604 16778 12748 13765 -833 1031 -79 C ATOM 2808 N GLY B 605 -63.708 25.187 20.044 1.00112.65 N ANISOU 2808 N GLY B 605 15649 13256 13895 -1017 1536 -315 N ATOM 2809 CA GLY B 605 -64.765 24.628 19.205 1.00114.96 C ANISOU 2809 CA GLY B 605 15746 13707 14225 -1131 1674 -356 C ATOM 2810 C GLY B 605 -64.164 23.598 18.256 1.00116.25 C ANISOU 2810 C GLY B 605 15926 13762 14481 -1203 1602 -266 C ATOM 2811 O GLY B 605 -62.945 23.587 18.046 1.00116.08 O ANISOU 2811 O GLY B 605 16000 13570 14532 -1118 1435 -189 O ATOM 2812 N PRO B 606 -65.008 22.727 17.668 1.00116.77 N ANISOU 2812 N PRO B 606 15896 13928 14543 -1359 1725 -278 N ATOM 2813 CA PRO B 606 -64.499 21.677 16.774 1.00114.87 C ANISOU 2813 CA PRO B 606 15690 13579 14374 -1433 1664 -197 C ATOM 2814 C PRO B 606 -63.986 22.183 15.419 1.00111.43 C ANISOU 2814 C PRO B 606 15072 13127 14138 -1294 1536 -189 C ATOM 2815 O PRO B 606 -63.156 21.516 14.804 1.00109.50 O ANISOU 2815 O PRO B 606 14895 12748 13959 -1294 1438 -111 O ATOM 2816 CB PRO B 606 -65.719 20.772 16.576 1.00116.88 C ANISOU 2816 CB PRO B 606 15878 13973 14556 -1646 1844 -231 C ATOM 2817 CG PRO B 606 -66.883 21.694 16.709 1.00118.07 C ANISOU 2817 CG PRO B 606 15807 14357 14696 -1615 1966 -350 C ATOM 2818 CD PRO B 606 -66.483 22.745 17.710 1.00117.64 C ANISOU 2818 CD PRO B 606 15836 14269 14591 -1464 1918 -375 C ATOM 2819 N ASP B 607 -64.468 23.344 14.971 1.00110.14 N ANISOU 2819 N ASP B 607 14691 13097 14061 -1172 1537 -271 N ATOM 2820 CA ASP B 607 -64.138 23.880 13.647 1.00108.98 C ANISOU 2820 CA ASP B 607 14362 12951 14091 -1053 1432 -272 C ATOM 2821 C ASP B 607 -63.132 25.044 13.670 1.00104.18 C ANISOU 2821 C ASP B 607 13768 12249 13564 -859 1269 -258 C ATOM 2822 O ASP B 607 -63.015 25.776 12.682 1.00103.23 O ANISOU 2822 O ASP B 607 13488 12157 13576 -749 1195 -278 O ATOM 2823 CB ASP B 607 -65.434 24.312 12.944 1.00112.47 C ANISOU 2823 CB ASP B 607 14543 13608 14579 -1059 1536 -373 C ATOM 2824 CG ASP B 607 -66.344 23.136 12.627 1.00115.68 C ANISOU 2824 CG ASP B 607 14905 14110 14937 -1262 1674 -381 C ATOM 2825 OD1 ASP B 607 -65.958 22.297 11.785 1.00116.14 O ANISOU 2825 OD1 ASP B 607 14984 14085 15057 -1326 1629 -319 O ATOM 2826 OD2 ASP B 607 -67.443 23.053 13.216 1.00119.56 O ANISOU 2826 OD2 ASP B 607 15341 14761 15323 -1362 1827 -451 O ATOM 2827 N CYS B 608 -62.393 25.197 14.773 1.00 99.43 N ANISOU 2827 N CYS B 608 13366 11533 12880 -826 1209 -220 N ATOM 2828 CA CYS B 608 -61.447 26.301 14.945 1.00 94.91 C ANISOU 2828 CA CYS B 608 12826 10870 12363 -663 1055 -207 C ATOM 2829 C CYS B 608 -60.058 25.770 15.282 1.00 93.57 C ANISOU 2829 C CYS B 608 12848 10511 12191 -657 920 -102 C ATOM 2830 O CYS B 608 -59.831 25.287 16.385 1.00 94.31 O ANISOU 2830 O CYS B 608 13143 10532 12156 -712 933 -72 O ATOM 2831 CB CYS B 608 -61.927 27.233 16.055 1.00 94.00 C ANISOU 2831 CB CYS B 608 12759 10813 12142 -605 1100 -280 C ATOM 2832 SG CYS B 608 -60.766 28.549 16.482 1.00 90.72 S ANISOU 2832 SG CYS B 608 12435 10270 11763 -432 908 -263 S ATOM 2833 N CYS B 609 -59.123 25.901 14.344 1.00 91.90 N ANISOU 2833 N CYS B 609 12574 10227 12117 -582 788 -50 N ATOM 2834 CA CYS B 609 -57.786 25.329 14.491 1.00 91.31 C ANISOU 2834 CA CYS B 609 12644 9992 12056 -566 656 45 C ATOM 2835 C CYS B 609 -56.836 26.286 15.219 1.00 92.27 C ANISOU 2835 C CYS B 609 12853 10030 12172 -458 514 62 C ATOM 2836 O CYS B 609 -55.858 26.786 14.645 1.00 91.02 O ANISOU 2836 O CYS B 609 12638 9817 12125 -372 375 99 O ATOM 2837 CB CYS B 609 -57.234 24.928 13.120 1.00 89.41 C ANISOU 2837 CB CYS B 609 12285 9726 11958 -544 593 91 C ATOM 2838 SG CYS B 609 -58.406 23.987 12.113 1.00 88.70 S ANISOU 2838 SG CYS B 609 12071 9742 11887 -665 746 61 S ATOM 2839 N ILE B 610 -57.141 26.528 16.492 1.00 93.78 N ANISOU 2839 N ILE B 610 13187 10216 12226 -474 553 33 N ATOM 2840 CA ILE B 610 -56.287 27.303 17.391 1.00 94.87 C ANISOU 2840 CA ILE B 610 13454 10264 12327 -393 422 50 C ATOM 2841 C ILE B 610 -55.939 26.391 18.566 1.00 97.22 C ANISOU 2841 C ILE B 610 13997 10462 12478 -461 421 99 C ATOM 2842 O ILE B 610 -56.826 25.756 19.137 1.00100.47 O ANISOU 2842 O ILE B 610 14489 10916 12765 -562 566 74 O ATOM 2843 CB ILE B 610 -56.990 28.589 17.885 1.00 94.51 C ANISOU 2843 CB ILE B 610 13375 10297 12238 -329 460 -40 C ATOM 2844 CG1 ILE B 610 -57.194 29.564 16.715 1.00 92.52 C ANISOU 2844 CG1 ILE B 610 12906 10118 12129 -243 428 -83 C ATOM 2845 CG2 ILE B 610 -56.181 29.253 18.998 1.00 95.60 C ANISOU 2845 CG2 ILE B 610 13690 10330 12302 -268 334 -23 C ATOM 2846 CD1 ILE B 610 -58.039 30.781 17.034 1.00 92.55 C ANISOU 2846 CD1 ILE B 610 12863 10209 12093 -166 475 -182 C ATOM 2847 N GLU B 611 -54.652 26.325 18.907 1.00119.42 N ANISOU 2847 N GLU B 611 19558 14121 11695 556 -1188 613 N ATOM 2848 CA GLU B 611 -54.164 25.541 20.040 1.00118.79 C ANISOU 2848 CA GLU B 611 19553 13955 11624 401 -1281 613 C ATOM 2849 C GLU B 611 -53.677 26.490 21.148 1.00119.60 C ANISOU 2849 C GLU B 611 19683 13997 11760 228 -1231 682 C ATOM 2850 O GLU B 611 -52.655 27.158 20.979 1.00117.69 O ANISOU 2850 O GLU B 611 19393 13778 11544 265 -1197 780 O ATOM 2851 CB GLU B 611 -53.038 24.599 19.585 1.00118.07 C ANISOU 2851 CB GLU B 611 19438 13891 11531 505 -1377 652 C ATOM 2852 CG GLU B 611 -52.479 23.672 20.661 1.00117.76 C ANISOU 2852 CG GLU B 611 19470 13767 11506 361 -1485 658 C ATOM 2853 CD GLU B 611 -53.545 22.809 21.315 1.00117.19 C ANISOU 2853 CD GLU B 611 19471 13630 11423 251 -1545 555 C ATOM 2854 OE1 GLU B 611 -53.964 23.122 22.449 1.00115.54 O ANISOU 2854 OE1 GLU B 611 19325 13353 11218 64 -1525 546 O ATOM 2855 OE2 GLU B 611 -53.984 21.827 20.683 1.00117.93 O ANISOU 2855 OE2 GLU B 611 19557 13743 11506 353 -1610 482 O ATOM 2856 N PRO B 612 -54.416 26.564 22.278 1.00122.68 N ANISOU 2856 N PRO B 612 20148 14313 12150 41 -1225 628 N ATOM 2857 CA PRO B 612 -53.945 27.320 23.441 1.00125.94 C ANISOU 2857 CA PRO B 612 20594 14667 12588 -133 -1194 679 C ATOM 2858 C PRO B 612 -53.069 26.528 24.439 1.00130.98 C ANISOU 2858 C PRO B 612 21292 15247 13226 -259 -1297 712 C ATOM 2859 O PRO B 612 -52.767 27.054 25.501 1.00132.01 O ANISOU 2859 O PRO B 612 21459 15328 13368 -418 -1281 741 O ATOM 2860 CB PRO B 612 -55.252 27.788 24.096 1.00124.44 C ANISOU 2860 CB PRO B 612 20448 14439 12392 -261 -1132 595 C ATOM 2861 CG PRO B 612 -56.265 26.760 23.723 1.00122.91 C ANISOU 2861 CG PRO B 612 20281 14252 12167 -212 -1183 499 C ATOM 2862 CD PRO B 612 -55.785 26.050 22.488 1.00122.47 C ANISOU 2862 CD PRO B 612 20170 14261 12101 -9 -1236 515 C ATOM 2863 N HIS B 613 -52.677 25.293 24.099 1.00138.11 N ANISOU 2863 N HIS B 613 22202 16157 14116 -187 -1402 707 N ATOM 2864 CA HIS B 613 -51.752 24.442 24.896 1.00143.33 C ANISOU 2864 CA HIS B 613 22908 16766 14782 -281 -1510 749 C ATOM 2865 C HIS B 613 -50.731 25.203 25.761 1.00143.90 C ANISOU 2865 C HIS B 613 22989 16807 14878 -401 -1492 839 C ATOM 2866 O HIS B 613 -50.797 25.134 26.985 1.00145.70 O ANISOU 2866 O HIS B 613 23284 16975 15097 -585 -1519 832 O ATOM 2867 CB HIS B 613 -51.028 23.445 23.961 1.00147.80 C ANISOU 2867 CB HIS B 613 23433 17371 15352 -115 -1596 768 C ATOM 2868 CG HIS B 613 -49.986 22.600 24.636 1.00152.41 C ANISOU 2868 CG HIS B 613 24050 17907 15952 -189 -1707 820 C ATOM 2869 ND1 HIS B 613 -50.299 21.530 25.448 1.00155.17 N ANISOU 2869 ND1 HIS B 613 24468 18192 16296 -307 -1804 779 N ATOM 2870 CD2 HIS B 613 -48.633 22.654 24.595 1.00154.00 C ANISOU 2870 CD2 HIS B 613 24220 18113 16178 -158 -1737 914 C ATOM 2871 CE1 HIS B 613 -49.186 20.973 25.892 1.00155.63 C ANISOU 2871 CE1 HIS B 613 24537 18218 16375 -348 -1890 846 C ATOM 2872 NE2 HIS B 613 -48.161 21.636 25.388 1.00155.94 N ANISOU 2872 NE2 HIS B 613 24518 18298 16433 -259 -1852 926 N ATOM 2873 N ASP B 614 -49.808 25.926 25.128 1.00145.21 N ANISOU 2873 N ASP B 614 23083 17013 15074 -297 -1447 922 N ATOM 2874 CA ASP B 614 -48.806 26.720 25.860 1.00146.57 C ANISOU 2874 CA ASP B 614 23253 17155 15280 -397 -1427 1009 C ATOM 2875 C ASP B 614 -49.436 27.912 26.587 1.00148.89 C ANISOU 2875 C ASP B 614 23564 17422 15585 -529 -1331 985 C ATOM 2876 O ASP B 614 -48.968 28.303 27.656 1.00149.15 O ANISOU 2876 O ASP B 614 23632 17407 15631 -683 -1338 1014 O ATOM 2877 CB ASP B 614 -47.689 27.208 24.924 1.00146.29 C ANISOU 2877 CB ASP B 614 23127 17172 15282 -241 -1399 1107 C ATOM 2878 CG ASP B 614 -46.830 26.070 24.380 1.00145.98 C ANISOU 2878 CG ASP B 614 23070 17154 15239 -131 -1500 1140 C ATOM 2879 OD1 ASP B 614 -46.517 25.125 25.135 1.00146.16 O ANISOU 2879 OD1 ASP B 614 23153 17125 15254 -229 -1603 1132 O ATOM 2880 OD2 ASP B 614 -46.453 26.128 23.191 1.00144.70 O ANISOU 2880 OD2 ASP B 614 22832 17065 15083 55 -1477 1174 O ATOM 2881 N TRP B 615 -50.490 28.480 26.002 1.00152.61 N ANISOU 2881 N TRP B 615 24008 17925 16052 -467 -1243 929 N ATOM 2882 CA TRP B 615 -51.256 29.562 26.630 1.00156.35 C ANISOU 2882 CA TRP B 615 24495 18371 16537 -584 -1150 890 C ATOM 2883 C TRP B 615 -52.047 29.120 27.883 1.00157.63 C ANISOU 2883 C TRP B 615 24753 18477 16660 -779 -1184 809 C ATOM 2884 O TRP B 615 -52.356 29.957 28.735 1.00156.58 O ANISOU 2884 O TRP B 615 24642 18311 16537 -916 -1127 786 O ATOM 2885 CB TRP B 615 -52.180 30.221 25.588 1.00159.67 C ANISOU 2885 CB TRP B 615 24856 18842 16968 -453 -1052 855 C ATOM 2886 CG TRP B 615 -52.951 31.397 26.094 1.00164.17 C ANISOU 2886 CG TRP B 615 25426 19386 17564 -554 -950 816 C ATOM 2887 CD1 TRP B 615 -54.308 31.556 26.079 1.00166.09 C ANISOU 2887 CD1 TRP B 615 25688 19628 17790 -577 -898 723 C ATOM 2888 CD2 TRP B 615 -52.415 32.573 26.707 1.00167.86 C ANISOU 2888 CD2 TRP B 615 25871 19821 18087 -646 -890 865 C ATOM 2889 NE1 TRP B 615 -54.650 32.763 26.640 1.00167.84 N ANISOU 2889 NE1 TRP B 615 25899 19819 18052 -677 -807 709 N ATOM 2890 CE2 TRP B 615 -53.507 33.407 27.035 1.00169.17 C ANISOU 2890 CE2 TRP B 615 26041 19967 18266 -720 -802 793 C ATOM 2891 CE3 TRP B 615 -51.114 33.008 27.009 1.00170.57 C ANISOU 2891 CE3 TRP B 615 26185 20147 18474 -671 -904 959 C ATOM 2892 CZ2 TRP B 615 -53.339 34.655 27.652 1.00171.69 C ANISOU 2892 CZ2 TRP B 615 26337 20250 18645 -818 -729 808 C ATOM 2893 CZ3 TRP B 615 -50.947 34.248 27.623 1.00171.77 C ANISOU 2893 CZ3 TRP B 615 26315 20262 18685 -770 -833 976 C ATOM 2894 CH2 TRP B 615 -52.055 35.055 27.936 1.00172.02 C ANISOU 2894 CH2 TRP B 615 26351 20275 18732 -841 -747 899 C ATOM 2895 N THR B 616 -52.358 27.824 28.002 1.00159.42 N ANISOU 2895 N THR B 616 25032 18693 16847 -790 -1277 766 N ATOM 2896 CA THR B 616 -52.980 27.275 29.222 1.00160.26 C ANISOU 2896 CA THR B 616 25227 18749 16914 -975 -1322 707 C ATOM 2897 C THR B 616 -51.950 27.283 30.357 1.00160.87 C ANISOU 2897 C THR B 616 25343 18787 16992 -1123 -1375 769 C ATOM 2898 O THR B 616 -52.203 27.836 31.426 1.00160.45 O ANISOU 2898 O THR B 616 25331 18705 16925 -1287 -1343 747 O ATOM 2899 CB THR B 616 -53.531 25.826 29.055 1.00160.94 C ANISOU 2899 CB THR B 616 25352 18828 16969 -948 -1415 654 C ATOM 2900 OG1 THR B 616 -52.456 24.877 29.071 1.00162.80 O ANISOU 2900 OG1 THR B 616 25594 19053 17210 -923 -1526 716 O ATOM 2901 CG2 THR B 616 -54.346 25.646 27.765 1.00160.23 C ANISOU 2901 CG2 THR B 616 25214 18783 16880 -770 -1384 598 C ATOM 2902 N LYS B 617 -50.785 26.685 30.091 1.00162.18 N ANISOU 2902 N LYS B 617 25492 18956 17174 -1059 -1456 846 N ATOM 2903 CA LYS B 617 -49.670 26.614 31.054 1.00164.10 C ANISOU 2903 CA LYS B 617 25763 19163 17422 -1180 -1518 916 C ATOM 2904 C LYS B 617 -48.761 27.864 31.073 1.00164.65 C ANISOU 2904 C LYS B 617 25781 19237 17540 -1177 -1454 986 C ATOM 2905 O LYS B 617 -47.630 27.799 31.555 1.00163.95 O ANISOU 2905 O LYS B 617 25695 19128 17469 -1227 -1509 1059 O ATOM 2906 CB LYS B 617 -48.836 25.330 30.832 1.00165.52 C ANISOU 2906 CB LYS B 617 25949 19335 17603 -1122 -1643 965 C ATOM 2907 CG LYS B 617 -48.034 25.267 29.533 1.00167.11 C ANISOU 2907 CG LYS B 617 26071 19580 17844 -916 -1646 1022 C ATOM 2908 CD LYS B 617 -47.039 24.115 29.531 1.00167.81 C ANISOU 2908 CD LYS B 617 26166 19652 17943 -888 -1771 1076 C ATOM 2909 CE LYS B 617 -46.223 24.101 28.245 1.00167.66 C ANISOU 2909 CE LYS B 617 26061 19682 17957 -681 -1768 1129 C ATOM 2910 NZ LYS B 617 -45.060 23.172 28.311 1.00167.64 N ANISOU 2910 NZ LYS B 617 26058 19661 17977 -661 -1881 1193 N ATOM 2911 N ASN B 618 -49.234 28.976 30.506 1.00165.81 N ANISOU 2911 N ASN B 618 25875 19409 17717 -1111 -1341 969 N ATOM 2912 CA ASN B 618 -48.703 30.309 30.806 1.00166.80 C ANISOU 2912 CA ASN B 618 25959 19522 17893 -1157 -1266 1012 C ATOM 2913 C ASN B 618 -49.577 31.003 31.856 1.00170.31 C ANISOU 2913 C ASN B 618 26450 19938 18321 -1328 -1208 934 C ATOM 2914 O ASN B 618 -49.055 31.717 32.708 1.00173.80 O ANISOU 2914 O ASN B 618 26898 20351 18785 -1446 -1194 954 O ATOM 2915 CB ASN B 618 -48.617 31.164 29.534 1.00164.31 C ANISOU 2915 CB ASN B 618 25546 19251 17633 -978 -1176 1051 C ATOM 2916 CG ASN B 618 -47.744 32.397 29.711 1.00162.14 C ANISOU 2916 CG ASN B 618 25214 18960 17431 -1000 -1119 1124 C ATOM 2917 OD1 ASN B 618 -48.125 33.353 30.386 1.00161.19 O ANISOU 2917 OD1 ASN B 618 25099 18811 17335 -1112 -1055 1088 O ATOM 2918 ND2 ASN B 618 -46.568 32.383 29.094 1.00161.30 N ANISOU 2918 ND2 ASN B 618 25048 18872 17365 -890 -1144 1225 N ATOM 2919 N ILE B 619 -50.896 30.800 31.787 1.00172.71 N ANISOU 2919 N ILE B 619 26783 20250 18587 -1339 -1174 842 N ATOM 2920 CA ILE B 619 -51.841 31.403 32.736 1.00174.69 C ANISOU 2920 CA ILE B 619 27077 20479 18818 -1495 -1115 758 C ATOM 2921 C ILE B 619 -51.963 30.568 34.018 1.00177.03 C ANISOU 2921 C ILE B 619 27467 20749 19046 -1673 -1196 727 C ATOM 2922 O ILE B 619 -51.819 31.110 35.118 1.00176.01 O ANISOU 2922 O ILE B 619 27369 20600 18906 -1829 -1184 713 O ATOM 2923 CB ILE B 619 -53.235 31.619 32.085 1.00173.96 C ANISOU 2923 CB ILE B 619 26969 20406 18720 -1427 -1036 675 C ATOM 2924 CG1 ILE B 619 -53.122 32.536 30.854 1.00172.91 C ANISOU 2924 CG1 ILE B 619 26738 20303 18653 -1256 -950 713 C ATOM 2925 CG2 ILE B 619 -54.239 32.187 33.087 1.00174.33 C ANISOU 2925 CG2 ILE B 619 27060 20431 18744 -1589 -976 583 C ATOM 2926 CD1 ILE B 619 -52.541 33.913 31.121 1.00173.12 C ANISOU 2926 CD1 ILE B 619 26713 20312 18751 -1295 -877 754 C ATOM 2927 N THR B 620 -52.221 29.264 33.875 1.00180.19 N ANISOU 2927 N THR B 620 27907 21153 19403 -1649 -1280 718 N ATOM 2928 CA THR B 620 -52.342 28.353 35.034 1.00182.31 C ANISOU 2928 CA THR B 620 28260 21399 19610 -1810 -1365 702 C ATOM 2929 C THR B 620 -51.010 28.112 35.769 1.00184.79 C ANISOU 2929 C THR B 620 28593 21695 19922 -1891 -1449 785 C ATOM 2930 O THR B 620 -51.011 27.720 36.938 1.00186.09 O ANISOU 2930 O THR B 620 28823 21845 20037 -2054 -1502 779 O ATOM 2931 CB THR B 620 -52.951 26.980 34.651 1.00180.53 C ANISOU 2931 CB THR B 620 28064 21174 19354 -1758 -1438 675 C ATOM 2932 OG1 THR B 620 -52.146 26.346 33.649 1.00180.69 O ANISOU 2932 OG1 THR B 620 28041 21204 19407 -1597 -1500 737 O ATOM 2933 CG2 THR B 620 -54.379 27.136 34.139 1.00179.05 C ANISOU 2933 CG2 THR B 620 27870 21000 19159 -1710 -1364 582 C ATOM 2934 N ASP B 621 -49.892 28.333 35.078 1.00186.47 N ANISOU 2934 N ASP B 621 28748 21912 20189 -1775 -1463 866 N ATOM 2935 CA ASP B 621 -48.558 28.273 35.682 1.00186.73 C ANISOU 2935 CA ASP B 621 28786 21926 20234 -1839 -1533 950 C ATOM 2936 C ASP B 621 -48.235 29.555 36.473 1.00188.68 C ANISOU 2936 C ASP B 621 29025 22162 20501 -1952 -1470 948 C ATOM 2937 O ASP B 621 -47.651 29.476 37.557 1.00191.24 O ANISOU 2937 O ASP B 621 29390 22469 20800 -2095 -1526 972 O ATOM 2938 CB ASP B 621 -47.510 28.023 34.587 1.00184.74 C ANISOU 2938 CB ASP B 621 28469 21684 20037 -1664 -1568 1035 C ATOM 2939 CG ASP B 621 -46.153 27.604 35.133 1.00182.88 C ANISOU 2939 CG ASP B 621 28245 21426 19814 -1716 -1665 1124 C ATOM 2940 OD1 ASP B 621 -46.098 26.737 36.030 1.00181.88 O ANISOU 2940 OD1 ASP B 621 28184 21279 19640 -1838 -1755 1126 O ATOM 2941 OD2 ASP B 621 -45.132 28.125 34.635 1.00181.32 O ANISOU 2941 OD2 ASP B 621 27985 21231 19674 -1631 -1653 1197 O ATOM 2942 N LYS B 622 -48.631 30.718 35.941 1.00188.61 N ANISOU 2942 N LYS B 622 28959 22162 20540 -1890 -1358 919 N ATOM 2943 CA LYS B 622 -48.358 32.023 36.580 1.00189.13 C ANISOU 2943 CA LYS B 622 29003 22213 20645 -1983 -1292 910 C ATOM 2944 C LYS B 622 -49.403 32.480 37.625 1.00190.93 C ANISOU 2944 C LYS B 622 29282 22437 20824 -2147 -1240 806 C ATOM 2945 O LYS B 622 -49.358 33.630 38.077 1.00189.87 O ANISOU 2945 O LYS B 622 29122 22290 20726 -2214 -1174 778 O ATOM 2946 CB LYS B 622 -48.152 33.111 35.512 1.00188.14 C ANISOU 2946 CB LYS B 622 28779 22093 20610 -1836 -1198 941 C ATOM 2947 CG LYS B 622 -46.908 32.897 34.659 1.00187.90 C ANISOU 2947 CG LYS B 622 28690 22070 20633 -1695 -1241 1054 C ATOM 2948 CD LYS B 622 -46.817 33.887 33.506 1.00186.82 C ANISOU 2948 CD LYS B 622 28453 21950 20580 -1538 -1145 1092 C ATOM 2949 CE LYS B 622 -46.378 35.263 33.976 1.00186.48 C ANISOU 2949 CE LYS B 622 28363 21876 20614 -1606 -1080 1106 C ATOM 2950 NZ LYS B 622 -46.224 36.201 32.831 1.00185.50 N ANISOU 2950 NZ LYS B 622 28134 21767 20581 -1450 -991 1160 N ATOM 2951 N ILE B 623 -50.329 31.595 38.012 1.00192.46 N ANISOU 2951 N ILE B 623 29543 22641 20940 -2211 -1271 748 N ATOM 2952 CA ILE B 623 -51.138 31.803 39.232 1.00192.89 C ANISOU 2952 CA ILE B 623 29658 22698 20931 -2393 -1248 662 C ATOM 2953 C ILE B 623 -50.307 31.682 40.518 1.00195.43 C ANISOU 2953 C ILE B 623 30028 23014 21211 -2556 -1321 692 C ATOM 2954 O ILE B 623 -50.714 32.197 41.558 1.00197.69 O ANISOU 2954 O ILE B 623 30348 23309 21457 -2705 -1289 626 O ATOM 2955 CB ILE B 623 -52.369 30.856 39.329 1.00190.89 C ANISOU 2955 CB ILE B 623 29462 22458 20607 -2423 -1262 598 C ATOM 2956 CG1 ILE B 623 -51.959 29.375 39.504 1.00189.97 C ANISOU 2956 CG1 ILE B 623 29396 22340 20445 -2435 -1389 656 C ATOM 2957 CG2 ILE B 623 -53.293 31.054 38.132 1.00189.20 C ANISOU 2957 CG2 ILE B 623 29202 22252 20431 -2273 -1185 555 C ATOM 2958 CD1 ILE B 623 -52.025 28.856 40.930 1.00189.63 C ANISOU 2958 CD1 ILE B 623 29430 22301 20319 -2631 -1451 646 C ATOM 2959 N ASP B 624 -49.156 31.004 40.443 1.00195.79 N ANISOU 2959 N ASP B 624 30074 23050 21265 -2525 -1419 788 N ATOM 2960 CA ASP B 624 -48.213 30.903 41.569 1.00195.43 C ANISOU 2960 CA ASP B 624 30066 22999 21189 -2664 -1496 831 C ATOM 2961 C ASP B 624 -47.197 32.070 41.634 1.00197.01 C ANISOU 2961 C ASP B 624 30207 23181 21464 -2661 -1465 865 C ATOM 2962 O ASP B 624 -46.079 31.902 42.133 1.00196.89 O ANISOU 2962 O ASP B 624 30199 23155 21453 -2711 -1542 933 O ATOM 2963 CB ASP B 624 -47.497 29.545 41.535 1.00192.71 C ANISOU 2963 CB ASP B 624 29752 22648 20820 -2645 -1624 917 C ATOM 2964 CG ASP B 624 -48.469 28.377 41.543 1.00189.97 C ANISOU 2964 CG ASP B 624 29458 22311 20410 -2658 -1662 885 C ATOM 2965 OD1 ASP B 624 -48.994 28.031 40.464 1.00185.11 O ANISOU 2965 OD1 ASP B 624 28814 21695 19823 -2516 -1639 872 O ATOM 2966 OD2 ASP B 624 -48.709 27.810 42.629 1.00188.53 O ANISOU 2966 OD2 ASP B 624 29341 22139 20151 -2809 -1716 875 O ATOM 2967 N GLN B 625 -47.580 33.231 41.094 1.00196.94 N ANISOU 2967 N GLN B 625 30138 23166 21522 -2597 -1354 822 N ATOM 2968 CA GLN B 625 -46.984 34.522 41.444 1.00196.93 C ANISOU 2968 CA GLN B 625 30088 23146 21590 -2639 -1306 818 C ATOM 2969 C GLN B 625 -48.055 35.524 41.932 1.00198.85 C ANISOU 2969 C GLN B 625 30330 23393 21829 -2724 -1202 699 C ATOM 2970 O GLN B 625 -47.822 36.737 41.923 1.00199.25 O ANISOU 2970 O GLN B 625 30321 23422 21962 -2722 -1135 680 O ATOM 2971 CB GLN B 625 -46.217 35.086 40.245 1.00194.81 C ANISOU 2971 CB GLN B 625 29724 22856 21435 -2467 -1272 898 C ATOM 2972 CG GLN B 625 -45.028 34.240 39.826 1.00193.22 C ANISOU 2972 CG GLN B 625 29515 22650 21247 -2388 -1370 1014 C ATOM 2973 CD GLN B 625 -44.249 34.861 38.684 1.00191.52 C ANISOU 2973 CD GLN B 625 29202 22422 21143 -2223 -1330 1096 C ATOM 2974 OE1 GLN B 625 -44.818 35.211 37.650 1.00189.92 O ANISOU 2974 OE1 GLN B 625 28947 22232 20980 -2091 -1252 1087 O ATOM 2975 NE2 GLN B 625 -42.939 34.995 38.863 1.00190.73 N ANISOU 2975 NE2 GLN B 625 29073 22300 21092 -2227 -1385 1181 N ATOM 2976 N ILE B 626 -49.222 35.014 42.344 1.00200.67 N ANISOU 2976 N ILE B 626 30623 23650 21973 -2795 -1189 620 N ATOM 2977 CA ILE B 626 -50.265 35.828 43.002 1.00201.81 C ANISOU 2977 CA ILE B 626 30778 23804 22096 -2900 -1102 499 C ATOM 2978 C ILE B 626 -50.915 35.119 44.217 1.00205.29 C ANISOU 2978 C ILE B 626 31311 24280 22408 -3070 -1143 438 C ATOM 2979 O ILE B 626 -51.181 35.777 45.228 1.00205.85 O ANISOU 2979 O ILE B 626 31399 24365 22446 -3207 -1110 359 O ATOM 2980 CB ILE B 626 -51.320 36.354 41.979 1.00199.10 C ANISOU 2980 CB ILE B 626 30385 23455 21809 -2781 -993 447 C ATOM 2981 CG1 ILE B 626 -51.997 37.638 42.487 1.00197.59 C ANISOU 2981 CG1 ILE B 626 30167 23256 21651 -2861 -890 340 C ATOM 2982 CG2 ILE B 626 -52.361 35.299 41.618 1.00198.02 C ANISOU 2982 CG2 ILE B 626 30295 23340 21601 -2746 -1004 421 C ATOM 2983 CD1 ILE B 626 -51.178 38.894 42.273 1.00195.78 C ANISOU 2983 CD1 ILE B 626 29853 22989 21542 -2824 -847 365 C ATOM 2984 N ILE B 627 -51.169 33.806 44.122 1.00208.55 N ANISOU 2984 N ILE B 627 31777 24709 22751 -3059 -1214 474 N ATOM 2985 CA ILE B 627 -51.635 32.995 45.267 1.00210.76 C ANISOU 2985 CA ILE B 627 32143 25025 22912 -3217 -1268 444 C ATOM 2986 C ILE B 627 -50.474 32.426 46.107 1.00212.80 C ANISOU 2986 C ILE B 627 32438 25290 23124 -3311 -1384 524 C ATOM 2987 O ILE B 627 -50.611 32.283 47.325 1.00213.51 O ANISOU 2987 O ILE B 627 32583 25415 23124 -3473 -1413 492 O ATOM 2988 CB ILE B 627 -52.613 31.862 44.826 1.00209.67 C ANISOU 2988 CB ILE B 627 32040 24895 22727 -3173 -1286 438 C ATOM 2989 CG1 ILE B 627 -53.484 31.409 46.007 1.00209.17 C ANISOU 2989 CG1 ILE B 627 32051 24873 22551 -3342 -1294 376 C ATOM 2990 CG2 ILE B 627 -51.885 30.664 44.213 1.00209.01 C ANISOU 2990 CG2 ILE B 627 31962 24795 22654 -3078 -1393 545 C ATOM 2991 CD1 ILE B 627 -54.551 30.401 45.632 1.00208.43 C ANISOU 2991 CD1 ILE B 627 31988 24784 22422 -3308 -1302 360 C ATOM 2992 N HIS B 628 -49.351 32.099 45.460 1.00213.97 N ANISOU 2992 N HIS B 628 32555 25411 23333 -3208 -1450 627 N ATOM 2993 CA HIS B 628 -48.130 31.667 46.160 1.00214.76 C ANISOU 2993 CA HIS B 628 32679 25510 23409 -3282 -1558 709 C ATOM 2994 C HIS B 628 -47.437 32.864 46.821 1.00214.64 C ANISOU 2994 C HIS B 628 32635 25492 23426 -3360 -1532 686 C ATOM 2995 O HIS B 628 -46.906 32.737 47.927 1.00214.34 O ANISOU 2995 O HIS B 628 32637 25474 23326 -3498 -1597 697 O ATOM 2996 CB HIS B 628 -47.168 30.954 45.198 1.00215.11 C ANISOU 2996 CB HIS B 628 32691 25522 23515 -3139 -1632 823 C ATOM 2997 CG HIS B 628 -45.928 30.420 45.854 1.00216.29 C ANISOU 2997 CG HIS B 628 32865 25668 23647 -3208 -1749 913 C ATOM 2998 ND1 HIS B 628 -45.922 29.274 46.621 1.00216.57 N ANISOU 2998 ND1 HIS B 628 32968 25722 23596 -3309 -1848 949 N ATOM 2999 CD2 HIS B 628 -44.651 30.874 45.849 1.00216.08 C ANISOU 2999 CD2 HIS B 628 32798 25617 23682 -3188 -1784 979 C ATOM 3000 CE1 HIS B 628 -44.698 29.048 47.063 1.00215.88 C ANISOU 3000 CE1 HIS B 628 32883 25624 23515 -3350 -1939 1031 C ATOM 3001 NE2 HIS B 628 -43.908 30.004 46.609 1.00216.07 N ANISOU 3001 NE2 HIS B 628 32844 25623 23630 -3278 -1903 1049 N ATOM 3002 N ASP B 629 -47.451 34.016 46.141 1.00213.12 N ANISOU 3002 N ASP B 629 32369 25271 23332 -3271 -1438 654 N ATOM 3003 CA ASP B 629 -46.957 35.284 46.699 1.00211.62 C ANISOU 3003 CA ASP B 629 32141 25071 23193 -3338 -1398 613 C ATOM 3004 C ASP B 629 -48.096 36.113 47.325 1.00211.50 C ANISOU 3004 C ASP B 629 32135 25079 23144 -3436 -1302 475 C ATOM 3005 O ASP B 629 -48.204 37.320 47.083 1.00212.90 O ANISOU 3005 O ASP B 629 32249 25231 23409 -3406 -1215 421 O ATOM 3006 CB ASP B 629 -46.234 36.102 45.613 1.00208.91 C ANISOU 3006 CB ASP B 629 31703 24679 22992 -3186 -1355 668 C ATOM 3007 CG ASP B 629 -45.045 35.368 45.002 1.00206.78 C ANISOU 3007 CG ASP B 629 31416 24389 22760 -3087 -1445 801 C ATOM 3008 OD1 ASP B 629 -44.652 34.297 45.512 1.00206.53 O ANISOU 3008 OD1 ASP B 629 31445 24374 22653 -3147 -1549 852 O ATOM 3009 OD2 ASP B 629 -44.495 35.874 44.002 1.00203.76 O ANISOU 3009 OD2 ASP B 629 30956 23975 22486 -2947 -1412 858 O ATOM 3010 N PHE B 630 -48.934 35.456 48.132 1.00209.14 N ANISOU 3010 N PHE B 630 31912 24827 22724 -3553 -1318 421 N ATOM 3011 CA PHE B 630 -49.995 36.108 48.902 1.00205.46 C ANISOU 3011 CA PHE B 630 31465 24395 22206 -3667 -1237 289 C ATOM 3012 C PHE B 630 -49.450 36.258 50.325 1.00203.98 C ANISOU 3012 C PHE B 630 31316 24247 21938 -3841 -1293 264 C ATOM 3013 O PHE B 630 -49.948 35.653 51.277 1.00203.36 O ANISOU 3013 O PHE B 630 31307 24226 21734 -3970 -1324 232 O ATOM 3014 CB PHE B 630 -51.282 35.266 48.843 1.00203.38 C ANISOU 3014 CB PHE B 630 31253 24162 21858 -3678 -1217 251 C ATOM 3015 CG PHE B 630 -52.514 35.982 49.337 1.00201.34 C ANISOU 3015 CG PHE B 630 31000 23931 21567 -3758 -1114 114 C ATOM 3016 CD1 PHE B 630 -53.153 36.932 48.540 1.00198.66 C ANISOU 3016 CD1 PHE B 630 30596 23558 21324 -3664 -1003 49 C ATOM 3017 CD2 PHE B 630 -53.054 35.690 50.591 1.00200.27 C ANISOU 3017 CD2 PHE B 630 30929 23858 21303 -3926 -1127 52 C ATOM 3018 CE1 PHE B 630 -54.293 37.587 48.990 1.00197.89 C ANISOU 3018 CE1 PHE B 630 30501 23483 21203 -3737 -908 -78 C ATOM 3019 CE2 PHE B 630 -54.193 36.342 51.044 1.00199.22 C ANISOU 3019 CE2 PHE B 630 30798 23754 21139 -3998 -1029 -77 C ATOM 3020 CZ PHE B 630 -54.814 37.292 50.243 1.00198.81 C ANISOU 3020 CZ PHE B 630 30683 23662 21191 -3903 -920 -146 C ATOM 3021 N VAL B 631 -48.411 37.084 50.444 1.00202.09 N ANISOU 3021 N VAL B 631 31028 23979 21777 -3840 -1305 280 N ATOM 3022 CA VAL B 631 -47.586 37.166 51.651 1.00201.91 C ANISOU 3022 CA VAL B 631 31034 23987 21695 -3982 -1380 281 C ATOM 3023 C VAL B 631 -48.178 38.174 52.639 1.00201.48 C ANISOU 3023 C VAL B 631 30979 23969 21605 -4111 -1312 135 C ATOM 3024 O VAL B 631 -48.376 39.340 52.288 1.00201.77 O ANISOU 3024 O VAL B 631 30948 23967 21745 -4067 -1223 63 O ATOM 3025 CB VAL B 631 -46.130 37.582 51.311 1.00201.29 C ANISOU 3025 CB VAL B 631 30898 23856 21726 -3918 -1432 368 C ATOM 3026 CG1 VAL B 631 -45.243 37.538 52.556 1.00201.78 C ANISOU 3026 CG1 VAL B 631 30994 23951 21721 -4063 -1523 376 C ATOM 3027 CG2 VAL B 631 -45.558 36.697 50.204 1.00199.05 C ANISOU 3027 CG2 VAL B 631 30603 23535 21493 -3771 -1486 503 C ATOM 3028 N ASP B 632 -48.449 37.719 53.865 1.00199.60 N ANISOU 3028 N ASP B 632 30812 23806 21222 -4269 -1354 94 N ATOM 3029 CA ASP B 632 -48.960 38.581 54.940 1.00197.90 C ANISOU 3029 CA ASP B 632 30602 23641 20950 -4405 -1301 -47 C ATOM 3030 C ASP B 632 -47.817 39.035 55.849 1.00196.97 C ANISOU 3030 C ASP B 632 30476 23537 20824 -4500 -1372 -48 C ATOM 3031 O ASP B 632 -48.038 39.697 56.861 1.00195.51 O ANISOU 3031 O ASP B 632 30297 23403 20584 -4623 -1348 -163 O ATOM 3032 CB ASP B 632 -50.060 37.867 55.748 1.00197.20 C ANISOU 3032 CB ASP B 632 30589 23637 20698 -4522 -1292 -102 C ATOM 3033 CG ASP B 632 -49.514 36.809 56.702 1.00197.04 C ANISOU 3033 CG ASP B 632 30642 23683 20541 -4636 -1412 -24 C ATOM 3034 OD1 ASP B 632 -48.711 35.960 56.265 1.00196.72 O ANISOU 3034 OD1 ASP B 632 30612 23611 20520 -4576 -1503 110 O ATOM 3035 OD2 ASP B 632 -49.897 36.826 57.890 1.00196.43 O ANISOU 3035 OD2 ASP B 632 30608 23691 20335 -4786 -1415 -97 O TER 3036 ASP B 632 HETATM 3037 C1 NAG C 1 -62.679 4.071 -14.174 1.00 67.12 C HETATM 3038 C2 NAG C 1 -62.882 4.288 -15.666 1.00 71.45 C HETATM 3039 C3 NAG C 1 -64.058 3.466 -16.172 1.00 74.49 C HETATM 3040 C4 NAG C 1 -63.818 1.987 -15.864 1.00 78.43 C HETATM 3041 C5 NAG C 1 -63.510 1.814 -14.377 1.00 75.97 C HETATM 3042 C6 NAG C 1 -63.103 0.387 -14.018 1.00 75.34 C HETATM 3043 C7 NAG C 1 -62.332 6.411 -16.763 1.00 70.61 C HETATM 3044 C8 NAG C 1 -62.754 7.836 -16.955 1.00 68.70 C HETATM 3045 N2 NAG C 1 -63.121 5.689 -15.965 1.00 71.25 N HETATM 3046 O3 NAG C 1 -64.199 3.724 -17.574 1.00 74.72 O HETATM 3047 O4 NAG C 1 -64.970 1.182 -16.153 1.00 90.65 O HETATM 3048 O5 NAG C 1 -62.445 2.675 -13.975 1.00 73.58 O HETATM 3049 O6 NAG C 1 -61.919 0.004 -14.734 1.00 73.20 O HETATM 3050 O7 NAG C 1 -61.328 5.967 -17.302 1.00 72.37 O HETATM 3051 C1 NAG C 2 -65.161 0.882 -17.549 1.00103.66 C HETATM 3052 C2 NAG C 2 -65.446 -0.611 -17.737 1.00111.21 C HETATM 3053 C3 NAG C 2 -65.675 -0.894 -19.218 1.00117.08 C HETATM 3054 C4 NAG C 2 -66.813 -0.006 -19.716 1.00121.95 C HETATM 3055 C5 NAG C 2 -66.506 1.466 -19.452 1.00118.09 C HETATM 3056 C6 NAG C 2 -67.675 2.347 -19.908 1.00117.99 C HETATM 3057 C7 NAG C 2 -64.529 -2.303 -16.184 1.00109.85 C HETATM 3058 C8 NAG C 2 -63.306 -3.084 -15.795 1.00109.60 C HETATM 3059 N2 NAG C 2 -64.376 -1.453 -17.211 1.00111.57 N HETATM 3060 O3 NAG C 2 -66.000 -2.279 -19.405 1.00117.63 O HETATM 3061 O4 NAG C 2 -67.059 -0.197 -21.124 1.00132.08 O HETATM 3062 O5 NAG C 2 -66.254 1.649 -18.057 1.00110.60 O HETATM 3063 O6 NAG C 2 -67.611 3.666 -19.349 1.00116.81 O HETATM 3064 O7 NAG C 2 -65.579 -2.451 -15.576 1.00108.48 O HETATM 3065 C1 BMA C 3 -68.283 -0.924 -21.378 1.00135.30 C HETATM 3066 C2 BMA C 3 -68.874 -0.531 -22.731 1.00133.26 C HETATM 3067 C3 BMA C 3 -70.144 -1.341 -22.999 1.00134.93 C HETATM 3068 C4 BMA C 3 -69.889 -2.837 -22.818 1.00138.04 C HETATM 3069 C5 BMA C 3 -69.238 -3.113 -21.458 1.00141.93 C HETATM 3070 C6 BMA C 3 -68.849 -4.573 -21.248 1.00146.77 C HETATM 3071 O2 BMA C 3 -67.916 -0.747 -23.774 1.00127.33 O HETATM 3072 O3 BMA C 3 -70.625 -1.080 -24.324 1.00132.61 O HETATM 3073 O4 BMA C 3 -71.128 -3.548 -22.924 1.00137.11 O HETATM 3074 O5 BMA C 3 -68.053 -2.332 -21.318 1.00139.98 O HETATM 3075 O6 BMA C 3 -67.917 -4.996 -22.259 1.00154.27 O HETATM 3076 C1 MAN C 4 -67.527 -6.395 -22.218 1.00162.50 C HETATM 3077 C2 MAN C 4 -68.462 -7.223 -23.114 1.00166.17 C HETATM 3078 C3 MAN C 4 -69.655 -7.843 -22.386 1.00167.87 C HETATM 3079 C4 MAN C 4 -69.229 -8.535 -21.098 1.00168.66 C HETATM 3080 C5 MAN C 4 -68.395 -7.621 -20.201 1.00170.46 C HETATM 3081 C6 MAN C 4 -67.778 -8.431 -19.062 1.00170.62 C HETATM 3082 O2 MAN C 4 -67.692 -8.262 -23.735 1.00170.28 O HETATM 3083 O3 MAN C 4 -70.310 -8.794 -23.235 1.00167.40 O HETATM 3084 O4 MAN C 4 -70.405 -8.956 -20.394 1.00167.19 O HETATM 3085 O5 MAN C 4 -67.326 -6.958 -20.903 1.00166.93 O HETATM 3086 O6 MAN C 4 -67.091 -7.559 -18.158 1.00172.64 O HETATM 3087 C1 NAG A 601 -37.904 -1.126 -40.328 1.00 85.54 C HETATM 3088 C2 NAG A 601 -37.907 0.135 -39.467 1.00 91.70 C HETATM 3089 C3 NAG A 601 -37.027 1.196 -40.120 1.00 92.80 C HETATM 3090 C4 NAG A 601 -35.624 0.630 -40.318 1.00 92.85 C HETATM 3091 C5 NAG A 601 -35.713 -0.634 -41.180 1.00 92.44 C HETATM 3092 C6 NAG A 601 -34.367 -1.301 -41.470 1.00 92.28 C HETATM 3093 C7 NAG A 601 -39.812 0.969 -38.127 1.00 96.46 C HETATM 3094 C8 NAG A 601 -41.247 1.417 -38.191 1.00 97.38 C HETATM 3095 N2 NAG A 601 -39.274 0.607 -39.299 1.00 93.00 N HETATM 3096 O3 NAG A 601 -36.978 2.369 -39.302 1.00 96.91 O HETATM 3097 O4 NAG A 601 -34.761 1.598 -40.925 1.00 93.22 O HETATM 3098 O5 NAG A 601 -36.561 -1.582 -40.524 1.00 90.36 O HETATM 3099 O6 NAG A 601 -33.425 -1.120 -40.405 1.00 92.91 O HETATM 3100 O7 NAG A 601 -39.208 0.953 -37.063 1.00 96.11 O HETATM 3101 C1 NAG A 602 -71.730 -2.719 -37.459 1.00142.83 C HETATM 3102 C2 NAG A 602 -73.218 -2.400 -37.634 1.00151.36 C HETATM 3103 C3 NAG A 602 -74.133 -3.498 -37.073 1.00152.72 C HETATM 3104 C4 NAG A 602 -73.415 -4.568 -36.237 1.00153.46 C HETATM 3105 C5 NAG A 602 -72.053 -5.014 -36.798 1.00150.94 C HETATM 3106 C6 NAG A 602 -72.138 -6.392 -37.453 1.00148.98 C HETATM 3107 C7 NAG A 602 -74.040 -0.060 -37.625 1.00153.99 C HETATM 3108 C8 NAG A 602 -74.257 1.157 -36.771 1.00152.56 C HETATM 3109 N2 NAG A 602 -73.510 -1.119 -36.997 1.00152.76 N HETATM 3110 O3 NAG A 602 -74.814 -4.138 -38.162 1.00153.23 O HETATM 3111 O4 NAG A 602 -73.235 -4.066 -34.906 1.00152.87 O HETATM 3112 O5 NAG A 602 -71.526 -4.100 -37.767 1.00147.30 O HETATM 3113 O6 NAG A 602 -72.226 -7.412 -36.452 1.00146.85 O HETATM 3114 O7 NAG A 602 -74.337 -0.051 -38.810 1.00154.71 O HETATM 3115 C1 NAG A 603 -43.368 7.933 -48.071 1.00109.96 C HETATM 3116 C2 NAG A 603 -42.334 8.895 -48.658 1.00116.68 C HETATM 3117 C3 NAG A 603 -42.321 10.245 -47.946 1.00117.47 C HETATM 3118 C4 NAG A 603 -43.732 10.800 -47.793 1.00118.83 C HETATM 3119 C5 NAG A 603 -44.617 9.762 -47.103 1.00119.04 C HETATM 3120 C6 NAG A 603 -46.047 10.255 -46.876 1.00119.37 C HETATM 3121 C7 NAG A 603 -40.345 7.776 -49.588 1.00118.24 C HETATM 3122 C8 NAG A 603 -39.000 7.204 -49.250 1.00116.32 C HETATM 3123 N2 NAG A 603 -41.014 8.292 -48.555 1.00118.25 N HETATM 3124 O3 NAG A 603 -41.513 11.165 -48.689 1.00117.57 O HETATM 3125 O4 NAG A 603 -43.690 12.018 -47.042 1.00119.63 O HETATM 3126 O5 NAG A 603 -44.641 8.575 -47.904 1.00114.76 O HETATM 3127 O6 NAG A 603 -46.672 10.573 -48.126 1.00119.89 O HETATM 3128 O7 NAG A 603 -40.772 7.758 -50.732 1.00119.91 O HETATM 3129 C1 NAG A 604 -38.675 -9.480 -55.291 1.00134.22 C HETATM 3130 C2 NAG A 604 -37.815 -9.984 -54.110 1.00144.03 C HETATM 3131 C3 NAG A 604 -38.438 -11.202 -53.434 1.00145.83 C HETATM 3132 C4 NAG A 604 -39.851 -10.831 -53.011 1.00145.40 C HETATM 3133 C5 NAG A 604 -40.713 -10.609 -54.245 1.00143.31 C HETATM 3134 C6 NAG A 604 -42.022 -9.934 -53.838 1.00141.72 C HETATM 3135 C7 NAG A 604 -35.365 -10.146 -53.749 1.00141.92 C HETATM 3136 C8 NAG A 604 -34.044 -10.447 -54.392 1.00141.69 C HETATM 3137 N2 NAG A 604 -36.441 -10.243 -54.547 1.00142.93 N HETATM 3138 O3 NAG A 604 -37.676 -11.609 -52.290 1.00146.20 O HETATM 3139 O4 NAG A 604 -40.430 -11.866 -52.208 1.00148.74 O HETATM 3140 O5 NAG A 604 -40.082 -9.831 -55.282 1.00140.14 O HETATM 3141 O6 NAG A 604 -42.842 -9.719 -54.991 1.00141.90 O HETATM 3142 O7 NAG A 604 -35.420 -9.838 -52.569 1.00140.61 O HETATM 3143 C1 GOL A 605 -61.136 20.426 -39.332 1.00 91.99 C HETATM 3144 O1 GOL A 605 -60.750 21.619 -38.640 1.00 90.92 O HETATM 3145 C2 GOL A 605 -62.091 19.601 -38.474 1.00 92.02 C HETATM 3146 O2 GOL A 605 -61.805 19.808 -37.089 1.00 91.61 O HETATM 3147 C3 GOL A 605 -63.537 19.993 -38.762 1.00 96.85 C HETATM 3148 O3 GOL A 605 -64.426 19.303 -37.872 1.00 99.53 O HETATM 3149 C1 GOL A 606 -47.066 15.345 -37.450 1.00127.02 C HETATM 3150 O1 GOL A 606 -48.045 14.307 -37.587 1.00122.31 O HETATM 3151 C2 GOL A 606 -45.869 14.846 -36.638 1.00126.76 C HETATM 3152 O2 GOL A 606 -44.653 15.331 -37.226 1.00125.91 O HETATM 3153 C3 GOL A 606 -45.972 15.320 -35.189 1.00125.29 C HETATM 3154 O3 GOL A 606 -44.864 14.830 -34.425 1.00122.07 O HETATM 3155 S DMS A 607 -36.246 11.485 -29.062 1.00151.21 S HETATM 3156 O DMS A 607 -36.491 10.089 -28.631 1.00148.48 O HETATM 3157 C1 DMS A 607 -37.731 12.323 -29.158 1.00148.78 C HETATM 3158 C2 DMS A 607 -35.486 12.348 -27.799 1.00148.73 C HETATM 3159 C11 T0R B 705 -43.402 16.175 -8.908 1.00 82.56 C HETATM 3160 C14 T0R B 705 -47.533 11.816 -8.955 1.00 71.20 C HETATM 3161 CL T0R B 705 -47.280 11.880 -5.173 1.00 97.87 CL HETATM 3162 C9 T0R B 705 -46.443 10.521 -5.965 1.00 90.39 C HETATM 3163 C4 T0R B 705 -45.249 10.920 -6.834 1.00 88.47 C HETATM 3164 C2 T0R B 705 -44.982 12.396 -7.127 1.00 82.70 C HETATM 3165 C6 T0R B 705 -44.087 13.098 -6.138 1.00 81.54 C HETATM 3166 C16 T0R B 705 -42.722 12.804 -6.134 1.00 82.97 C HETATM 3167 C22 T0R B 705 -41.860 13.440 -5.239 1.00 83.58 C HETATM 3168 C24 T0R B 705 -42.362 14.379 -4.341 1.00 83.20 C HETATM 3169 C21 T0R B 705 -43.724 14.675 -4.344 1.00 83.26 C HETATM 3170 C15 T0R B 705 -44.587 14.040 -5.239 1.00 81.73 C HETATM 3171 C1 T0R B 705 -45.443 13.051 -8.227 1.00 78.47 C HETATM 3172 C5 T0R B 705 -46.310 12.405 -9.276 1.00 72.72 C HETATM 3173 C20 T0R B 705 -48.314 11.233 -9.953 1.00 70.78 C HETATM 3174 C23 T0R B 705 -47.889 11.244 -11.284 1.00 71.81 C HETATM 3175 C19 T0R B 705 -46.672 11.836 -11.612 1.00 71.13 C HETATM 3176 C13 T0R B 705 -45.889 12.417 -10.610 1.00 71.54 C HETATM 3177 C3 T0R B 705 -45.101 14.497 -8.514 1.00 80.61 C HETATM 3178 C8 T0R B 705 -46.082 15.468 -8.736 1.00 81.06 C HETATM 3179 C12 T0R B 705 -45.723 16.792 -9.027 1.00 81.06 C HETATM 3180 C10 T0R B 705 -44.372 17.151 -9.115 1.00 83.77 C HETATM 3181 C7 T0R B 705 -43.759 14.865 -8.628 1.00 80.96 C HETATM 3182 O T0R B 705 -43.895 18.415 -9.384 1.00 88.78 O HETATM 3183 C18 T0R B 705 -44.631 19.551 -9.822 1.00 95.58 C HETATM 3184 C17 T0R B 705 -43.765 20.788 -9.593 1.00 97.67 C HETATM 3185 N T0R B 705 -44.212 21.878 -10.483 1.00101.57 N HETATM 3186 C26 T0R B 705 -43.088 22.765 -10.838 1.00103.81 C HETATM 3187 C25 T0R B 705 -45.296 22.659 -9.857 1.00101.71 C HETATM 3188 O HOH A 701 -48.415 25.800 -23.543 1.00 67.76 O HETATM 3189 O HOH A 702 -48.966 21.666 -24.170 1.00 53.88 O HETATM 3190 O HOH A 703 -42.201 12.182 -27.973 1.00 75.79 O HETATM 3191 O HOH A 704 -65.679 18.695 -23.876 1.00 57.09 O HETATM 3192 O HOH A 705 -47.641 4.452 -18.455 1.00 72.40 O HETATM 3193 O HOH A 706 -61.525 16.336 -32.223 1.00 64.07 O HETATM 3194 O HOH A 707 -59.763 18.679 6.664 1.00 83.31 O HETATM 3195 O HOH A 708 -57.611 15.462 -39.092 1.00 73.19 O HETATM 3196 O HOH A 709 -49.261 10.895 -17.608 1.00 54.79 O HETATM 3197 O HOH A 710 -54.796 14.285 -41.752 1.00 75.27 O HETATM 3198 O HOH A 711 -53.434 4.592 -14.124 1.00 60.42 O HETATM 3199 O HOH A 712 -64.674 25.180 -26.349 1.00 65.92 O HETATM 3200 O HOH A 713 -53.697 12.762 -32.701 1.00 69.67 O HETATM 3201 O HOH A 714 -49.201 6.952 -40.832 1.00 68.14 O HETATM 3202 O HOH A 715 -39.740 5.892 -23.808 1.00 67.38 O HETATM 3203 O HOH A 716 -49.750 8.702 7.281 1.00 82.91 O HETATM 3204 O HOH A 717 -48.940 19.415 -32.309 1.00 72.95 O HETATM 3205 O HOH A 718 -64.786 16.038 -38.212 1.00 70.79 O HETATM 3206 O HOH A 719 -51.979 20.258 -35.574 1.00 69.88 O HETATM 3207 O HOH A 720 -72.986 14.317 -33.241 1.00 76.47 O HETATM 3208 O HOH A 721 -58.212 24.012 -32.735 1.00 71.59 O HETATM 3209 O HOH A 722 -52.502 16.616 -42.664 1.00 77.88 O HETATM 3210 O HOH A 723 -67.221 7.942 -34.292 1.00 60.92 O HETATM 3211 O HOH A 724 -46.969 16.001 -31.326 1.00 62.11 O HETATM 3212 O HOH A 725 -49.131 24.068 -30.894 1.00 73.79 O HETATM 3213 O HOH A 726 -45.647 18.735 -30.603 1.00 65.07 O HETATM 3214 O HOH A 727 -43.085 17.854 -26.203 1.00 63.59 O HETATM 3215 O HOH A 728 -68.609 22.199 -30.518 1.00 71.74 O HETATM 3216 O HOH A 729 -42.314 3.196 -20.658 1.00 71.20 O HETATM 3217 O HOH A 730 -35.361 12.792 -18.497 1.00 65.56 O HETATM 3218 O HOH A 731 -51.910 16.882 5.393 1.00 82.68 O HETATM 3219 O HOH A 732 -60.127 23.181 -30.572 1.00 78.98 O HETATM 3220 O HOH B 801 -55.495 23.017 9.499 1.00 67.46 O HETATM 3221 O HOH B 802 -52.357 27.071 -22.340 1.00 61.45 O HETATM 3222 O HOH B 803 -58.048 28.926 -15.189 1.00 58.71 O HETATM 3223 O HOH B 804 -61.568 24.454 -19.284 1.00 59.75 O HETATM 3224 O HOH B 805 -44.658 4.359 -14.737 1.00 66.03 O HETATM 3225 O HOH B 806 -62.402 27.156 -15.523 1.00 53.39 O HETATM 3226 O HOH B 807 -62.706 3.879 -3.525 1.00 80.12 O HETATM 3227 O HOH B 808 -58.193 4.859 1.482 1.00 82.89 O HETATM 3228 O HOH B 809 -36.199 18.247 -8.033 1.00 90.85 O HETATM 3229 O HOH B 810 -57.436 27.519 -26.466 1.00 75.98 O HETATM 3230 O HOH B 811 -26.888 34.142 -15.013 1.00 83.23 O HETATM 3231 O HOH B 812 -60.627 24.238 -25.045 1.00 61.44 O HETATM 3232 O HOH B 813 -29.146 29.893 -28.858 1.00 77.61 O HETATM 3233 O HOH B 814 -61.131 31.112 -22.012 1.00 56.80 O HETATM 3234 O HOH B 815 -65.427 29.106 9.622 1.00 72.74 O HETATM 3235 O HOH B 816 -65.280 27.822 15.006 1.00 82.93 O HETATM 3236 O HOH B 817 -65.346 10.191 -5.093 1.00 75.32 O HETATM 3237 O HOH B 818 -55.101 30.510 -12.526 1.00 65.15 O HETATM 3238 O HOH B 819 -57.746 29.894 -22.792 1.00 57.87 O HETATM 3239 O HOH B 820 -56.728 32.751 -16.406 0.33 57.39 O HETATM 3240 O HOH B 821 -55.050 30.617 -23.757 1.00 67.83 O CONECT 175 2838 CONECT 594 799 CONECT 697 889 CONECT 799 594 CONECT 889 697 CONECT 1362 3101 CONECT 1450 3115 CONECT 1613 3087 CONECT 1700 3129 CONECT 2068 2418 CONECT 2418 2068 CONECT 2471 3037 CONECT 2781 2832 CONECT 2832 2781 CONECT 2838 175 CONECT 3037 2471 3038 3048 CONECT 3038 3037 3039 3045 CONECT 3039 3038 3040 3046 CONECT 3040 3039 3041 3047 CONECT 3041 3040 3042 3048 CONECT 3042 3041 3049 CONECT 3043 3044 3045 3050 CONECT 3044 3043 CONECT 3045 3038 3043 CONECT 3046 3039 CONECT 3047 3040 3051 CONECT 3048 3037 3041 CONECT 3049 3042 CONECT 3050 3043 CONECT 3051 3047 3052 3062 CONECT 3052 3051 3053 3059 CONECT 3053 3052 3054 3060 CONECT 3054 3053 3055 3061 CONECT 3055 3054 3056 3062 CONECT 3056 3055 3063 CONECT 3057 3058 3059 3064 CONECT 3058 3057 CONECT 3059 3052 3057 CONECT 3060 3053 CONECT 3061 3054 3065 CONECT 3062 3051 3055 CONECT 3063 3056 CONECT 3064 3057 CONECT 3065 3061 3066 3074 CONECT 3066 3065 3067 3071 CONECT 3067 3066 3068 3072 CONECT 3068 3067 3069 3073 CONECT 3069 3068 3070 3074 CONECT 3070 3069 3075 CONECT 3071 3066 CONECT 3072 3067 CONECT 3073 3068 CONECT 3074 3065 3069 CONECT 3075 3070 3076 CONECT 3076 3075 3077 3085 CONECT 3077 3076 3078 3082 CONECT 3078 3077 3079 3083 CONECT 3079 3078 3080 3084 CONECT 3080 3079 3081 3085 CONECT 3081 3080 3086 CONECT 3082 3077 CONECT 3083 3078 CONECT 3084 3079 CONECT 3085 3076 3080 CONECT 3086 3081 CONECT 3087 1613 3088 3098 CONECT 3088 3087 3089 3095 CONECT 3089 3088 3090 3096 CONECT 3090 3089 3091 3097 CONECT 3091 3090 3092 3098 CONECT 3092 3091 3099 CONECT 3093 3094 3095 3100 CONECT 3094 3093 CONECT 3095 3088 3093 CONECT 3096 3089 CONECT 3097 3090 CONECT 3098 3087 3091 CONECT 3099 3092 CONECT 3100 3093 CONECT 3101 1362 3102 3112 CONECT 3102 3101 3103 3109 CONECT 3103 3102 3104 3110 CONECT 3104 3103 3105 3111 CONECT 3105 3104 3106 3112 CONECT 3106 3105 3113 CONECT 3107 3108 3109 3114 CONECT 3108 3107 CONECT 3109 3102 3107 CONECT 3110 3103 CONECT 3111 3104 CONECT 3112 3101 3105 CONECT 3113 3106 CONECT 3114 3107 CONECT 3115 1450 3116 3126 CONECT 3116 3115 3117 3123 CONECT 3117 3116 3118 3124 CONECT 3118 3117 3119 3125 CONECT 3119 3118 3120 3126 CONECT 3120 3119 3127 CONECT 3121 3122 3123 3128 CONECT 3122 3121 CONECT 3123 3116 3121 CONECT 3124 3117 CONECT 3125 3118 CONECT 3126 3115 3119 CONECT 3127 3120 CONECT 3128 3121 CONECT 3129 1700 3130 3140 CONECT 3130 3129 3131 3137 CONECT 3131 3130 3132 3138 CONECT 3132 3131 3133 3139 CONECT 3133 3132 3134 3140 CONECT 3134 3133 3141 CONECT 3135 3136 3137 3142 CONECT 3136 3135 CONECT 3137 3130 3135 CONECT 3138 3131 CONECT 3139 3132 CONECT 3140 3129 3133 CONECT 3141 3134 CONECT 3142 3135 CONECT 3143 3144 3145 CONECT 3144 3143 CONECT 3145 3143 3146 3147 CONECT 3146 3145 CONECT 3147 3145 3148 CONECT 3148 3147 CONECT 3149 3150 3151 CONECT 3150 3149 CONECT 3151 3149 3152 3153 CONECT 3152 3151 CONECT 3153 3151 3154 CONECT 3154 3153 CONECT 3155 3156 3157 3158 CONECT 3156 3155 CONECT 3157 3155 CONECT 3158 3155 CONECT 3159 3180 3181 CONECT 3160 3172 3173 CONECT 3161 3162 CONECT 3162 3161 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 3171 CONECT 3165 3164 3166 3170 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 CONECT 3169 3168 3170 CONECT 3170 3165 3169 CONECT 3171 3164 3172 3177 CONECT 3172 3160 3171 3176 CONECT 3173 3160 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3172 3175 CONECT 3177 3171 3178 3181 CONECT 3178 3177 3179 CONECT 3179 3178 3180 CONECT 3180 3159 3179 3182 CONECT 3181 3159 3177 CONECT 3182 3180 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 3187 CONECT 3186 3185 CONECT 3187 3185 MASTER 533 0 12 10 21 0 0 6 3238 2 166 39 END If you find results from this site helpful for your research, please cite one of our papers:
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