Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 01-SEP-11 3TN0 TITLE STRUCTURE OF MOUSE VA14VB8.2NKT TCR-MOUSE CD1D-A-C-GALACTOSYLCERAMIDE TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 19-297; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-2 MICROGLOBULIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: UNP RESIDUES 21-119; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MOUSE NKT VALPHA14 (MOUSE VARIABLE DOMAIN, HUMAN CONSTANT COMPND 13 DOMAIN); COMPND 14 CHAIN: C; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: FOR CHAIN C, RESIDUES 1 TO 116 IS MOUSE VARIABLE COMPND 17 DOMAIN AND 117-210 IS HUMAN CONSTANT DOMAIN; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: MOUSE NKT VBETA8.2 (MOUSE VARIABLE DOMAIN, HUMAN CONSTANT COMPND 20 DOMAIN); COMPND 21 CHAIN: D; COMPND 22 ENGINEERED: YES; COMPND 23 OTHER_DETAILS: FOR CHAIN D, RESIDUES 1 TO 117 IS MOUSE VARIABLE COMPND 24 DOMAIN AND 118-247 IS HUMAN CONSTANT DOMAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: CD1D1, CD1.1; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBACP10PH; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 GENE: B2M, RP23-34E24.5-001, MCG_11606; SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PBACP10PH; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS; SOURCE 19 ORGANISM_TAXID: 9606, 10090; SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET30B; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS, MUS MUSCULUS; SOURCE 25 ORGANISM_TAXID: 9606, 10090; SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET30B KEYWDS MOUSE CD1D, MOUSE NKT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR O.PATEL,J.ROSSJOHN REVDAT 2 29-JUL-20 3TN0 1 COMPND REMARK SEQADV HETNAM REVDAT 2 2 1 LINK SITE ATOM REVDAT 1 14-DEC-11 3TN0 0 JRNL AUTH O.PATEL,G.CAMERON,D.G.PELLICCI,Z.LIU,H.S.BYUN,T.BEDDOE, JRNL AUTH 2 J.MCCLUSKEY,R.W.FRANCK,A.R.CASTANO,Y.HARRAK,A.LLEBARIA, JRNL AUTH 3 R.BITTMAN,S.A.PORCELLI,D.I.GODFREY,J.ROSSJOHN JRNL TITL NKT TCR RECOGNITION OF CD1D-{ALPHA}-C-GALACTOSYLCERAMIDE. JRNL REF J.IMMUNOL. V. 187 4705 2011 JRNL REFN ISSN 0022-1767 JRNL PMID 21964029 JRNL DOI 10.4049/JIMMUNOL.1100794 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.77 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 19666 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.225 REMARK 3 FREE R VALUE : 0.289 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1056 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) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1360 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.15 REMARK 3 BIN R VALUE (WORKING SET) : 0.3350 REMARK 3 BIN FREE R VALUE SET COUNT : 57 REMARK 3 BIN FREE R VALUE : 0.3490 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6471 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 116 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 56.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.63000 REMARK 3 B22 (A**2) : 7.32000 REMARK 3 B33 (A**2) : -7.95000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.545 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.473 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 63.025 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6776 ; 0.006 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9236 ; 1.005 ; 1.939 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 823 ; 5.437 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 313 ;37.737 ;24.281 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1009 ;17.564 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;19.366 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1010 ; 0.065 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5210 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4137 ; 0.177 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6673 ; 0.344 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2639 ; 0.442 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2563 ; 0.761 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 5 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 7 A 186 REMARK 3 RESIDUE RANGE : A 1 A 1 REMARK 3 RESIDUE RANGE : A 303 A 303 REMARK 3 RESIDUE RANGE : A 304 A 304 REMARK 3 RESIDUE RANGE : A 305 A 306 REMARK 3 ORIGIN FOR THE GROUP (A): 14.8633 -47.3509 73.9446 REMARK 3 T TENSOR REMARK 3 T11: 0.2263 T22: 0.4439 REMARK 3 T33: 0.2889 T12: 0.0356 REMARK 3 T13: -0.0346 T23: 0.1518 REMARK 3 L TENSOR REMARK 3 L11: 2.0097 L22: 3.5327 REMARK 3 L33: 5.2889 L12: 0.4984 REMARK 3 L13: 1.3110 L23: 0.0280 REMARK 3 S TENSOR REMARK 3 S11: 0.0851 S12: 0.4400 S13: 0.0206 REMARK 3 S21: -0.0709 S22: -0.1237 S23: -0.2194 REMARK 3 S31: 0.0090 S32: 0.4705 S33: 0.0385 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 187 A 299 REMARK 3 ORIGIN FOR THE GROUP (A): 23.1904 -50.3904 112.4135 REMARK 3 T TENSOR REMARK 3 T11: 0.4820 T22: 0.1483 REMARK 3 T33: 0.2028 T12: -0.0221 REMARK 3 T13: -0.0912 T23: -0.1376 REMARK 3 L TENSOR REMARK 3 L11: 4.5803 L22: 4.1046 REMARK 3 L33: 3.7925 L12: 0.8507 REMARK 3 L13: -0.9585 L23: -2.2077 REMARK 3 S TENSOR REMARK 3 S11: -0.2828 S12: -0.1633 S13: 0.5116 REMARK 3 S21: 0.5159 S22: 0.1177 S23: -0.1257 REMARK 3 S31: -0.0346 S32: 0.0313 S33: 0.1651 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 2 B 99 REMARK 3 ORIGIN FOR THE GROUP (A): 6.0592 -45.9250 101.1338 REMARK 3 T TENSOR REMARK 3 T11: 0.3655 T22: 0.2109 REMARK 3 T33: 0.2937 T12: 0.0977 REMARK 3 T13: 0.0838 T23: 0.1661 REMARK 3 L TENSOR REMARK 3 L11: 4.8994 L22: 3.8325 REMARK 3 L33: 11.0721 L12: -0.1962 REMARK 3 L13: 0.5682 L23: 4.2839 REMARK 3 S TENSOR REMARK 3 S11: -0.0956 S12: 0.0407 S13: 0.4501 REMARK 3 S21: 0.4870 S22: 0.1438 S23: 0.2442 REMARK 3 S31: -0.1267 S32: -0.8361 S33: -0.0481 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 : C 4 C 116 REMARK 3 ORIGIN FOR THE GROUP (A): 3.8415 -37.1099 41.6244 REMARK 3 T TENSOR REMARK 3 T11: 0.0509 T22: 0.5677 REMARK 3 T33: 0.2945 T12: 0.0048 REMARK 3 T13: 0.0819 T23: 0.2064 REMARK 3 L TENSOR REMARK 3 L11: 4.5428 L22: 3.6906 REMARK 3 L33: 15.6962 L12: -1.0535 REMARK 3 L13: 7.1241 L23: -2.8976 REMARK 3 S TENSOR REMARK 3 S11: 0.2640 S12: 0.7415 S13: 0.3685 REMARK 3 S21: -0.1177 S22: -0.1163 S23: -0.1817 REMARK 3 S31: 0.0914 S32: 1.0081 S33: -0.1477 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 117 C 208 REMARK 3 ORIGIN FOR THE GROUP (A): -18.3431 -27.8377 15.8183 REMARK 3 T TENSOR REMARK 3 T11: 0.4252 T22: 0.1001 REMARK 3 T33: 0.0487 T12: -0.0066 REMARK 3 T13: -0.0375 T23: 0.0246 REMARK 3 L TENSOR REMARK 3 L11: 11.5038 L22: 7.8605 REMARK 3 L33: 9.8091 L12: -0.5652 REMARK 3 L13: -2.6785 L23: -0.6188 REMARK 3 S TENSOR REMARK 3 S11: 0.0889 S12: -0.4131 S13: 0.4844 REMARK 3 S21: 0.5835 S22: -0.1181 S23: -0.0301 REMARK 3 S31: -0.4176 S32: 0.0488 S33: 0.0292 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 5 D 117 REMARK 3 ORIGIN FOR THE GROUP (A): -13.0422 -52.1285 48.8918 REMARK 3 T TENSOR REMARK 3 T11: 0.3756 T22: 0.3166 REMARK 3 T33: 0.3107 T12: -0.0245 REMARK 3 T13: -0.0846 T23: 0.1322 REMARK 3 L TENSOR REMARK 3 L11: 10.1952 L22: 6.3189 REMARK 3 L33: 6.1778 L12: -1.0791 REMARK 3 L13: 2.9045 L23: -3.2958 REMARK 3 S TENSOR REMARK 3 S11: 0.7575 S12: 0.0595 S13: -0.9240 REMARK 3 S21: -0.5661 S22: -0.0808 S23: 0.0991 REMARK 3 S31: 1.0907 S32: -0.2987 S33: -0.6767 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 118 D 246 REMARK 3 ORIGIN FOR THE GROUP (A): -23.8334 -43.8866 20.9380 REMARK 3 T TENSOR REMARK 3 T11: 0.1867 T22: 0.2200 REMARK 3 T33: 0.4300 T12: -0.0760 REMARK 3 T13: -0.1726 T23: 0.1364 REMARK 3 L TENSOR REMARK 3 L11: 4.9749 L22: 4.1064 REMARK 3 L33: 10.1631 L12: 0.8507 REMARK 3 L13: -4.1892 L23: -2.5619 REMARK 3 S TENSOR REMARK 3 S11: 0.2372 S12: -0.4522 S13: -0.5235 REMARK 3 S21: -0.3189 S22: -0.0232 S23: 0.2048 REMARK 3 S31: 0.4331 S32: -0.6302 S33: -0.2141 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3TN0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-11. REMARK 100 THE DEPOSITION ID IS D_1000067673. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-FEB-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95453 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20725 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 8.100 REMARK 200 R MERGE (I) : 0.27200 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 8.40 REMARK 200 R MERGE FOR SHELL (I) : 1.08000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3HE6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15-17% PEG 10K, 0.1M AMMONIUM ACETAT, REMARK 280 0.1M BISTRIS PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.58550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 118.20150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.18400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 118.20150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.58550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.18400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 1 REMARK 465 GLU A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLN A 5 REMARK 465 LYS A 6 REMARK 465 HIS A 300 REMARK 465 HIS A 301 REMARK 465 HIS A 302 REMARK 465 ILE B 1 REMARK 465 SER C 134 REMARK 465 ASP C 135 REMARK 465 SER C 209 REMARK 465 SER C 210 REMARK 465 GLU D 1 REMARK 465 ALA D 2 REMARK 465 ASP D 98 REMARK 465 ALA D 99 REMARK 465 GLY D 100 REMARK 465 GLY D 101 REMARK 465 ASN D 102 REMARK 465 TYR D 103 REMARK 465 ALA D 104 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 51 CD CE NZ REMARK 470 LYS A 57 CG CD CE NZ REMARK 470 GLN A 61 CG CD OE1 NE2 REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 SER A 89 OG REMARK 470 LYS A 91 CG CD CE NZ REMARK 470 GLU A 92 CG CD OE1 OE2 REMARK 470 ASP A 93 CG OD1 OD2 REMARK 470 ASN A 110 CG OD1 ND2 REMARK 470 GLU A 113 CD OE1 OE2 REMARK 470 LYS A 123 CD CE NZ REMARK 470 LEU A 145 CG CD1 CD2 REMARK 470 LYS A 148 CD CE NZ REMARK 470 GLN A 154 CG CD OE1 NE2 REMARK 470 ARG A 173 NE CZ NH1 NH2 REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 LYS A 180 CG CD CE NZ REMARK 470 GLU A 257 CG CD OE1 OE2 REMARK 470 LEU A 282 CG CD1 CD2 REMARK 470 GLU B 16 CG CD OE1 OE2 REMARK 470 LYS B 19 CG CD CE NZ REMARK 470 LYS B 45 CD CE NZ REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 GLN C 14 CD OE1 NE2 REMARK 470 LYS C 41 CG CD CE NZ REMARK 470 LYS C 68 CE NZ REMARK 470 LEU C 99 CG CD1 CD2 REMARK 470 ARG C 103 CG CD NE CZ NH1 NH2 REMARK 470 ARG C 129 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 136 CG CD CE NZ REMARK 470 LYS C 154 CG CD CE NZ REMARK 470 LYS C 184 CD CE NZ REMARK 470 LYS D 18 NZ REMARK 470 GLU D 118 CG CD OE1 OE2 REMARK 470 ASP D 119 CG OD1 OD2 REMARK 470 LYS D 121 CG CD CE NZ REMARK 470 GLU D 225 CG CD OE1 OE2 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 LYS A 57 68.84 -103.46 REMARK 500 GLU A 92 87.48 54.53 REMARK 500 PRO A 217 105.85 -51.14 REMARK 500 THR A 244 -157.35 -93.22 REMARK 500 HIS A 295 -1.32 82.80 REMARK 500 HIS B 31 134.09 -177.06 REMARK 500 SER B 55 -162.06 -125.98 REMARK 500 TRP B 60 28.96 80.62 REMARK 500 GLN C 14 119.92 -38.74 REMARK 500 SER C 25 41.17 -140.19 REMARK 500 ASP C 29 71.26 -112.86 REMARK 500 LEU C 46 -61.31 -103.85 REMARK 500 VAL C 50 -55.64 -120.30 REMARK 500 ALA C 79 92.88 63.44 REMARK 500 SER C 97 -140.99 -146.00 REMARK 500 ASP C 122 56.28 -173.49 REMARK 500 ASN C 191 44.51 -97.22 REMARK 500 ASP C 201 27.62 -67.06 REMARK 500 ASN D 10 131.53 -171.51 REMARK 500 THR D 15 104.66 -55.29 REMARK 500 ASN D 28 70.13 64.28 REMARK 500 HIS D 41 -43.91 -149.61 REMARK 500 ILE D 46 -68.14 -103.35 REMARK 500 PRO D 70 -61.68 -94.70 REMARK 500 GLN D 142 37.01 71.75 REMARK 500 ASP D 188 28.86 -72.10 REMARK 500 CYS D 213 78.77 -114.16 REMARK 500 GLU D 222 40.18 -83.49 REMARK 500 THR D 227 -36.94 -136.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 QUX A 303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3QUX RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 SWISS-PROT ENTRY P11609 CONFLICTS WITH BRADBURY ET AL., 1988 WHICH REMARK 999 SUGGESTS A HISTIDINE IN PLACE OF ASPARTATE. SEQUENCE IN THIS PDB REMARK 999 AGREES WITH THE CITATION DBREF 3TN0 A 1 279 UNP P11609 CD1D1_MOUSE 19 297 DBREF 3TN0 B 1 99 UNP Q91XJ8 Q91XJ8_MOUSE 21 119 DBREF 3TN0 C 1 210 PDB 3TN0 3TN0 1 210 DBREF 3TN0 D 1 247 PDB 3TN0 3TN0 1 247 SEQADV 3TN0 HIS A 201 UNP P11609 ASP 219 SEE REMARK 999 SEQADV 3TN0 GLY A 280 UNP P11609 EXPRESSION TAG SEQADV 3TN0 SER A 281 UNP P11609 EXPRESSION TAG SEQADV 3TN0 LEU A 282 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 283 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 284 UNP P11609 EXPRESSION TAG SEQADV 3TN0 ILE A 285 UNP P11609 EXPRESSION TAG SEQADV 3TN0 LEU A 286 UNP P11609 EXPRESSION TAG SEQADV 3TN0 ASP A 287 UNP P11609 EXPRESSION TAG SEQADV 3TN0 ALA A 288 UNP P11609 EXPRESSION TAG SEQADV 3TN0 GLN A 289 UNP P11609 EXPRESSION TAG SEQADV 3TN0 LYS A 290 UNP P11609 EXPRESSION TAG SEQADV 3TN0 MET A 291 UNP P11609 EXPRESSION TAG SEQADV 3TN0 VAL A 292 UNP P11609 EXPRESSION TAG SEQADV 3TN0 TRP A 293 UNP P11609 EXPRESSION TAG SEQADV 3TN0 ASN A 294 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 295 UNP P11609 EXPRESSION TAG SEQADV 3TN0 ARG A 296 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 297 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 298 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 299 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 300 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 301 UNP P11609 EXPRESSION TAG SEQADV 3TN0 HIS A 302 UNP P11609 EXPRESSION TAG SEQRES 1 A 302 SER GLU ALA GLN GLN LYS ASN TYR THR PHE ARG CYS LEU SEQRES 2 A 302 GLN MET SER SER PHE ALA ASN ARG SER TRP SER ARG THR SEQRES 3 A 302 ASP SER VAL VAL TRP LEU GLY ASP LEU GLN THR HIS ARG SEQRES 4 A 302 TRP SER ASN ASP SER ALA THR ILE SER PHE THR LYS PRO SEQRES 5 A 302 TRP SER GLN GLY LYS LEU SER ASN GLN GLN TRP GLU LYS SEQRES 6 A 302 LEU GLN HIS MET PHE GLN VAL TYR ARG VAL SER PHE THR SEQRES 7 A 302 ARG ASP ILE GLN GLU LEU VAL LYS MET MET SER PRO LYS SEQRES 8 A 302 GLU ASP TYR PRO ILE GLU ILE GLN LEU SER ALA GLY CYS SEQRES 9 A 302 GLU MET TYR PRO GLY ASN ALA SER GLU SER PHE LEU HIS SEQRES 10 A 302 VAL ALA PHE GLN GLY LYS TYR VAL VAL ARG PHE TRP GLY SEQRES 11 A 302 THR SER TRP GLN THR VAL PRO GLY ALA PRO SER TRP LEU SEQRES 12 A 302 ASP LEU PRO ILE LYS VAL LEU ASN ALA ASP GLN GLY THR SEQRES 13 A 302 SER ALA THR VAL GLN MET LEU LEU ASN ASP THR CYS PRO SEQRES 14 A 302 LEU PHE VAL ARG GLY LEU LEU GLU ALA GLY LYS SER ASP SEQRES 15 A 302 LEU GLU LYS GLN GLU LYS PRO VAL ALA TRP LEU SER SER SEQRES 16 A 302 VAL PRO SER SER ALA HIS GLY HIS ARG GLN LEU VAL CYS SEQRES 17 A 302 HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL MET SEQRES 18 A 302 TRP MET ARG GLY ASP GLN GLU GLN GLN GLY THR HIS ARG SEQRES 19 A 302 GLY ASP PHE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU SEQRES 20 A 302 GLN ALA THR LEU ASP VAL GLU ALA GLY GLU GLU ALA GLY SEQRES 21 A 302 LEU ALA CYS ARG VAL LYS HIS SER SER LEU GLY GLY GLN SEQRES 22 A 302 ASP ILE ILE LEU TYR TRP GLY SER LEU HIS HIS ILE LEU SEQRES 23 A 302 ASP ALA GLN LYS MET VAL TRP ASN HIS ARG HIS HIS HIS SEQRES 24 A 302 HIS HIS HIS SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET SEQRES 1 C 207 THR GLN VAL GLU GLN SER PRO GLN SER LEU VAL VAL ARG SEQRES 2 C 207 GLN GLY GLU ASN SER VAL LEU GLN CYS ASN TYR SER VAL SEQRES 3 C 207 THR PRO ASP ASN HIS LEU ARG TRP PHE LYS GLN ASP THR SEQRES 4 C 207 GLY LYS GLY LEU VAL SER LEU THR VAL LEU VAL ASP GLN SEQRES 5 C 207 LYS ASP LYS THR SER ASN GLY ARG TYR SER ALA THR LEU SEQRES 6 C 207 ASP LYS ASP ALA LYS HIS SER THR LEU HIS ILE THR ALA SEQRES 7 C 207 THR LEU LEU ASP ASP THR ALA THR TYR ILE CYS VAL VAL SEQRES 8 C 207 GLY ASP ARG GLY SER ALA LEU GLY ARG LEU HIS PHE GLY SEQRES 9 C 207 ALA GLY THR GLN LEU ILE VAL ILE PRO ASP ILE GLN ASN SEQRES 10 C 207 PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS SER SEQRES 11 C 207 SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP SER SEQRES 12 C 207 GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL TYR SEQRES 13 C 207 ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET ASP SEQRES 14 C 207 PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS SER SEQRES 15 C 207 ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE ILE SEQRES 16 C 207 PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER SEQRES 1 D 244 GLU ALA ALA VAL THR GLN SER PRO ARG ASN LYS VAL ALA SEQRES 2 D 244 VAL THR GLY GLY LYS VAL THR LEU SER CYS ASN GLN THR SEQRES 3 D 244 ASN ASN HIS ASN ASN MET TYR TRP TYR ARG GLN ASP THR SEQRES 4 D 244 GLY HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY ALA SEQRES 5 D 244 GLY SER THR GLU LYS GLY ASP ILE PRO ASP GLY TYR LYS SEQRES 6 D 244 ALA SER ARG PRO SER GLN GLU ASN PHE SER LEU ILE LEU SEQRES 7 D 244 GLU LEU ALA THR PRO SER GLN THR SER VAL TYR PHE CYS SEQRES 8 D 244 ALA SER GLY ASP ALA GLY GLY ASN TYR ALA GLU GLN PHE SEQRES 9 D 244 PHE GLY PRO GLY THR ARG LEU THR VAL LEU GLU ASP LEU SEQRES 10 D 244 LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SEQRES 11 D 244 SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU SEQRES 12 D 244 VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU SEQRES 13 D 244 LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY SEQRES 14 D 244 VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA SEQRES 15 D 244 LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG SEQRES 16 D 244 VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE SEQRES 17 D 244 ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP SEQRES 18 D 244 GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE SEQRES 19 D 244 VAL SER ALA GLU ALA TRP GLY ARG ALA ASP MODRES 3TN0 ASN A 165 ASN GLYCOSYLATION SITE MODRES 3TN0 ASN A 42 ASN GLYCOSYLATION SITE MODRES 3TN0 ASN A 20 ASN GLYCOSYLATION SITE HET NAG E 1 14 HET NAG E 2 14 HET QUX A 303 60 HET NAG A 304 14 HET NAG A 307 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM QUX N-[(3S,4S,5R)-4,5-DIHYDROXY-1-[(2R,3R,4R,5R,6R)-3,4,5- HETNAM 2 QUX TRIHYDROXY-6-(HYDROXYMETHYL)OXAN-2-YL]NONADECAN-3- HETNAM 3 QUX YL]HEXACOSANAMIDE FORMUL 5 NAG 4(C8 H15 N O6) FORMUL 6 QUX C51 H101 N O8 HELIX 1 1 LYS A 51 GLY A 56 5 6 HELIX 2 2 SER A 59 MET A 88 1 30 HELIX 3 3 PRO A 140 TRP A 142 5 3 HELIX 4 4 LEU A 143 ALA A 152 1 10 HELIX 5 5 ASP A 153 ASP A 166 1 14 HELIX 6 6 ASP A 166 GLY A 179 1 14 HELIX 7 7 GLY A 179 GLU A 184 1 6 HELIX 8 8 HIS A 267 GLY A 271 5 5 HELIX 9 9 SER A 281 LYS A 290 1 10 HELIX 10 10 LEU C 81 THR C 85 5 5 HELIX 11 11 ALA C 188 PHE C 193 5 6 HELIX 12 12 THR D 83 THR D 87 5 5 HELIX 13 13 ASP D 119 VAL D 123 5 5 HELIX 14 14 SER D 134 GLN D 142 1 9 HELIX 15 15 ALA D 201 GLN D 205 1 5 SHEET 1 A 8 SER A 48 PHE A 49 0 SHEET 2 A 8 LEU A 35 TRP A 40 -1 N ARG A 39 O SER A 48 SHEET 3 A 8 SER A 24 LEU A 32 -1 N VAL A 30 O THR A 37 SHEET 4 A 8 TYR A 8 PHE A 18 -1 N LEU A 13 O VAL A 29 SHEET 5 A 8 ILE A 96 MET A 106 -1 O MET A 106 N TYR A 8 SHEET 6 A 8 SER A 112 PHE A 120 -1 O PHE A 115 N GLY A 103 SHEET 7 A 8 LYS A 123 TRP A 129 -1 O VAL A 126 N VAL A 118 SHEET 8 A 8 SER A 132 THR A 135 -1 O GLN A 134 N ARG A 127 SHEET 1 B 4 VAL A 190 PRO A 197 0 SHEET 2 B 4 HIS A 203 PHE A 213 -1 O GLN A 205 N VAL A 196 SHEET 3 B 4 TRP A 245 GLU A 254 -1 O LEU A 251 N LEU A 206 SHEET 4 B 4 HIS A 233 ARG A 234 -1 N HIS A 233 O THR A 250 SHEET 1 C 4 VAL A 190 PRO A 197 0 SHEET 2 C 4 HIS A 203 PHE A 213 -1 O GLN A 205 N VAL A 196 SHEET 3 C 4 TRP A 245 GLU A 254 -1 O LEU A 251 N LEU A 206 SHEET 4 C 4 LEU A 238 PRO A 239 -1 N LEU A 238 O TYR A 246 SHEET 1 D 4 GLN A 227 GLU A 228 0 SHEET 2 D 4 TRP A 219 ARG A 224 -1 N ARG A 224 O GLN A 227 SHEET 3 D 4 ALA A 262 LYS A 266 -1 O ALA A 262 N MET A 223 SHEET 4 D 4 ILE A 275 TYR A 278 -1 O LEU A 277 N CYS A 263 SHEET 1 E 4 GLN B 6 SER B 11 0 SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 E 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25 SHEET 4 E 4 GLU B 50 MET B 51 -1 N GLU B 50 O HIS B 67 SHEET 1 F 4 GLN B 6 SER B 11 0 SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 F 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25 SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 G 4 LYS B 44 LYS B 45 0 SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O LYS B 44 SHEET 3 G 4 TYR B 78 LYS B 83 -1 O ALA B 79 N LEU B 40 SHEET 4 G 4 LYS B 91 TYR B 94 -1 O VAL B 93 N CYS B 80 SHEET 1 H 5 VAL C 3 SER C 6 0 SHEET 2 H 5 SER C 18 TYR C 24 -1 O ASN C 23 N GLU C 4 SHEET 3 H 5 HIS C 72 ILE C 77 -1 O LEU C 75 N LEU C 20 SHEET 4 H 5 TYR C 62 ASP C 67 -1 N ASP C 67 O HIS C 72 SHEET 5 H 5 LYS C 53 ASN C 58 -1 N ASN C 58 O TYR C 62 SHEET 1 I 5 SER C 9 ARG C 13 0 SHEET 2 I 5 THR C 110 ILE C 115 1 O GLN C 111 N LEU C 10 SHEET 3 I 5 ALA C 86 GLY C 93 -1 N ALA C 86 O LEU C 112 SHEET 4 I 5 HIS C 31 GLN C 37 -1 N PHE C 35 O ILE C 89 SHEET 5 I 5 VAL C 44 LEU C 49 -1 O LEU C 49 N LEU C 32 SHEET 1 J 4 SER C 9 ARG C 13 0 SHEET 2 J 4 THR C 110 ILE C 115 1 O GLN C 111 N LEU C 10 SHEET 3 J 4 ALA C 86 GLY C 93 -1 N ALA C 86 O LEU C 112 SHEET 4 J 4 LEU C 104 PHE C 106 -1 O HIS C 105 N VAL C 92 SHEET 1 K 4 ALA C 124 ARG C 129 0 SHEET 2 K 4 SER C 137 THR C 142 -1 O THR C 142 N ALA C 124 SHEET 3 K 4 SER C 177 SER C 182 -1 O ALA C 180 N CYS C 139 SHEET 4 K 4 VAL C 158 ILE C 160 -1 N TYR C 159 O TRP C 181 SHEET 1 L 2 LEU C 166 MET C 168 0 SHEET 2 L 2 PHE C 173 SER C 175 -1 O PHE C 173 N MET C 168 SHEET 1 M 4 VAL D 4 SER D 7 0 SHEET 2 M 4 VAL D 19 GLN D 25 -1 O ASN D 24 N THR D 5 SHEET 3 M 4 ASN D 74 LEU D 79 -1 O LEU D 79 N VAL D 19 SHEET 4 M 4 LYS D 66 SER D 68 -1 N LYS D 66 O ILE D 78 SHEET 1 N 6 ASN D 10 VAL D 14 0 SHEET 2 N 6 THR D 112 LEU D 117 1 O ARG D 113 N LYS D 11 SHEET 3 N 6 SER D 88 SER D 94 -1 N TYR D 90 O THR D 112 SHEET 4 N 6 MET D 32 GLN D 37 -1 N TYR D 35 O PHE D 91 SHEET 5 N 6 ARG D 44 GLY D 51 -1 O SER D 49 N MET D 32 SHEET 6 N 6 SER D 54 LYS D 57 -1 O GLU D 56 N TYR D 48 SHEET 1 O 4 GLU D 127 PHE D 131 0 SHEET 2 O 4 VAL D 147 PHE D 153 -1 O VAL D 147 N PHE D 131 SHEET 3 O 4 TYR D 191 SER D 200 -1 O LEU D 193 N ALA D 150 SHEET 4 O 4 VAL D 173 THR D 175 -1 N CYS D 174 O ARG D 196 SHEET 1 P 3 LYS D 143 THR D 145 0 SHEET 2 P 3 TYR D 191 SER D 200 -1 O VAL D 199 N ALA D 144 SHEET 3 P 3 LEU D 180 LYS D 181 -1 N LEU D 180 O ALA D 192 SHEET 1 Q 4 LYS D 167 GLU D 168 0 SHEET 2 Q 4 VAL D 158 VAL D 164 -1 N VAL D 164 O LYS D 167 SHEET 3 Q 4 HIS D 210 PHE D 217 -1 O GLN D 214 N SER D 161 SHEET 4 Q 4 GLN D 236 TRP D 243 -1 O ALA D 240 N CYS D 213 SSBOND 1 CYS A 104 CYS A 168 1555 1555 2.05 SSBOND 2 CYS A 208 CYS A 263 1555 1555 2.03 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03 SSBOND 4 CYS C 22 CYS C 90 1555 1555 2.04 SSBOND 5 CYS C 139 CYS C 189 1555 1555 2.05 SSBOND 6 CYS C 164 CYS D 174 1555 1555 2.05 SSBOND 7 CYS D 23 CYS D 92 1555 1555 2.03 SSBOND 8 CYS D 148 CYS D 213 1555 1555 2.03 LINK ND2 ASN A 20 C1 NAG A 307 1555 1555 1.46 LINK ND2 ASN A 42 C1 NAG A 304 1555 1555 1.45 LINK ND2 ASN A 165 C1 NAG E 1 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45 CISPEP 1 TYR A 94 PRO A 95 0 0.23 CISPEP 2 TYR A 214 PRO A 215 0 -0.58 CISPEP 3 ARG A 296 HIS A 297 0 3.65 CISPEP 4 HIS B 31 PRO B 32 0 -2.76 CISPEP 5 SER C 6 PRO C 7 0 -3.46 CISPEP 6 THR C 27 PRO C 28 0 -0.29 CISPEP 7 SER D 7 PRO D 8 0 5.57 CISPEP 8 TYR D 154 PRO D 155 0 -2.07 CRYST1 59.171 86.368 236.403 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016900 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011578 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004230 0.00000 ATOM 1 N ASN A 7 34.373 -48.509 85.642 1.00102.28 N ANISOU 1 N ASN A 7 8756 16277 13830 177 -3046 2246 N ATOM 2 CA ASN A 7 33.304 -49.205 84.866 1.00 99.09 C ANISOU 2 CA ASN A 7 8623 15673 13355 445 -2766 2123 C ATOM 3 C ASN A 7 31.940 -48.542 85.070 1.00 94.85 C ANISOU 3 C ASN A 7 8622 14747 12671 178 -2642 2133 C ATOM 4 O ASN A 7 31.373 -48.596 86.163 1.00 93.53 O ANISOU 4 O ASN A 7 8872 14242 12423 100 -2821 2140 O ATOM 5 CB ASN A 7 33.242 -50.694 85.244 1.00 99.67 C ANISOU 5 CB ASN A 7 8843 15576 13451 911 -2920 2013 C ATOM 6 CG ASN A 7 34.506 -51.460 84.858 1.00104.07 C ANISOU 6 CG ASN A 7 8862 16518 14160 1285 -3003 1964 C ATOM 7 OD1 ASN A 7 34.913 -51.469 83.694 1.00105.45 O ANISOU 7 OD1 ASN A 7 8645 17040 14383 1413 -2744 1913 O ATOM 8 ND2 ASN A 7 35.120 -52.121 85.835 1.00106.55 N ANISOU 8 ND2 ASN A 7 9166 16778 14540 1482 -3367 1974 N ATOM 9 N TYR A 8 31.425 -47.914 84.013 1.00 93.08 N ANISOU 9 N TYR A 8 8379 14587 12402 49 -2336 2135 N ATOM 10 CA TYR A 8 30.153 -47.181 84.078 1.00 89.40 C ANISOU 10 CA TYR A 8 8360 13795 11813 -181 -2208 2143 C ATOM 11 C TYR A 8 29.097 -47.755 83.138 1.00 86.54 C ANISOU 11 C TYR A 8 8168 13319 11393 37 -1940 2038 C ATOM 12 O TYR A 8 29.379 -48.013 81.964 1.00 87.27 O ANISOU 12 O TYR A 8 7982 13666 11511 187 -1742 2002 O ATOM 13 CB TYR A 8 30.367 -45.689 83.792 1.00 89.90 C ANISOU 13 CB TYR A 8 8341 13962 11856 -599 -2145 2263 C ATOM 14 CG TYR A 8 30.928 -44.916 84.967 1.00 91.76 C ANISOU 14 CG TYR A 8 8641 14132 12092 -913 -2435 2359 C ATOM 15 CD1 TYR A 8 30.105 -44.524 86.027 1.00 89.91 C ANISOU 15 CD1 TYR A 8 8904 13507 11750 -1056 -2555 2346 C ATOM 16 CD2 TYR A 8 32.283 -44.579 85.024 1.00 95.80 C ANISOU 16 CD2 TYR A 8 8711 14989 12701 -1073 -2589 2456 C ATOM 17 CE1 TYR A 8 30.616 -43.815 87.114 1.00 91.86 C ANISOU 17 CE1 TYR A 8 9256 13676 11969 -1347 -2833 2419 C ATOM 18 CE2 TYR A 8 32.806 -43.865 86.108 1.00 97.66 C ANISOU 18 CE2 TYR A 8 9022 15157 12928 -1390 -2889 2544 C ATOM 19 CZ TYR A 8 31.966 -43.487 87.148 1.00 95.54 C ANISOU 19 CZ TYR A 8 9301 14465 12534 -1522 -3015 2521 C ATOM 20 OH TYR A 8 32.472 -42.786 88.219 1.00 96.97 O ANISOU 20 OH TYR A 8 9601 14563 12680 -1834 -3320 2593 O ATOM 21 N THR A 9 27.884 -47.945 83.662 1.00 83.43 N ANISOU 21 N THR A 9 8226 12563 10911 40 -1934 1988 N ATOM 22 CA THR A 9 26.791 -48.549 82.897 1.00 80.79 C ANISOU 22 CA THR A 9 8077 12098 10522 222 -1723 1890 C ATOM 23 C THR A 9 25.648 -47.570 82.660 1.00 78.09 C ANISOU 23 C THR A 9 7991 11584 10097 -4 -1563 1910 C ATOM 24 O THR A 9 24.850 -47.301 83.562 1.00 76.80 O ANISOU 24 O THR A 9 8162 11150 9868 -121 -1623 1906 O ATOM 25 CB THR A 9 26.255 -49.830 83.569 1.00 80.06 C ANISOU 25 CB THR A 9 8269 11751 10401 455 -1837 1804 C ATOM 26 OG1 THR A 9 27.344 -50.716 83.847 1.00 82.97 O ANISOU 26 OG1 THR A 9 8428 12247 10850 696 -2027 1788 O ATOM 27 CG2 THR A 9 25.269 -50.537 82.656 1.00 78.23 C ANISOU 27 CG2 THR A 9 8174 11427 10123 632 -1638 1702 C ATOM 28 N PHE A 10 25.582 -47.055 81.433 1.00 77.65 N ANISOU 28 N PHE A 10 7775 11697 10033 -45 -1358 1928 N ATOM 29 CA PHE A 10 24.573 -46.082 81.021 1.00 75.42 C ANISOU 29 CA PHE A 10 7699 11276 9681 -224 -1218 1955 C ATOM 30 C PHE A 10 23.392 -46.780 80.372 1.00 73.31 C ANISOU 30 C PHE A 10 7600 10888 9365 -34 -1067 1854 C ATOM 31 O PHE A 10 23.518 -47.346 79.286 1.00 73.62 O ANISOU 31 O PHE A 10 7479 11093 9399 135 -941 1808 O ATOM 32 CB PHE A 10 25.186 -45.079 80.042 1.00 76.76 C ANISOU 32 CB PHE A 10 7632 11685 9849 -410 -1108 2058 C ATOM 33 CG PHE A 10 24.188 -44.148 79.408 1.00 74.66 C ANISOU 33 CG PHE A 10 7576 11283 9509 -544 -974 2090 C ATOM 34 CD1 PHE A 10 23.841 -42.954 80.027 1.00 74.04 C ANISOU 34 CD1 PHE A 10 7732 10996 9402 -793 -1053 2158 C ATOM 35 CD2 PHE A 10 23.613 -44.452 78.180 1.00 73.54 C ANISOU 35 CD2 PHE A 10 7414 11211 9316 -406 -788 2049 C ATOM 36 CE1 PHE A 10 22.930 -42.085 79.440 1.00 72.65 C ANISOU 36 CE1 PHE A 10 7758 10680 9167 -875 -954 2185 C ATOM 37 CE2 PHE A 10 22.701 -43.591 77.589 1.00 72.22 C ANISOU 37 CE2 PHE A 10 7438 10919 9083 -511 -698 2087 C ATOM 38 CZ PHE A 10 22.358 -42.406 78.221 1.00 71.88 C ANISOU 38 CZ PHE A 10 7618 10663 9029 -732 -784 2157 C ATOM 39 N ARG A 11 22.242 -46.721 81.034 1.00 71.48 N ANISOU 39 N ARG A 11 7687 10384 9088 -71 -1078 1816 N ATOM 40 CA ARG A 11 21.047 -47.396 80.546 1.00 69.96 C ANISOU 40 CA ARG A 11 7649 10078 8855 69 -962 1725 C ATOM 41 C ARG A 11 19.859 -46.449 80.405 1.00 68.65 C ANISOU 41 C ARG A 11 7667 9772 8643 -56 -866 1735 C ATOM 42 O ARG A 11 19.654 -45.568 81.242 1.00 68.50 O ANISOU 42 O ARG A 11 7798 9621 8608 -212 -920 1770 O ATOM 43 CB ARG A 11 20.691 -48.588 81.439 1.00 69.56 C ANISOU 43 CB ARG A 11 7781 9856 8792 191 -1062 1652 C ATOM 44 CG ARG A 11 20.658 -48.279 82.926 1.00 70.02 C ANISOU 44 CG ARG A 11 8040 9743 8822 49 -1202 1684 C ATOM 45 CD ARG A 11 20.184 -49.481 83.728 1.00 70.97 C ANISOU 45 CD ARG A 11 8383 9685 8897 141 -1283 1629 C ATOM 46 NE ARG A 11 21.276 -50.217 84.374 1.00 73.23 N ANISOU 46 NE ARG A 11 8625 9988 9211 239 -1489 1650 N ATOM 47 CZ ARG A 11 21.897 -51.279 83.863 1.00 74.06 C ANISOU 47 CZ ARG A 11 8601 10170 9368 474 -1545 1610 C ATOM 48 NH1 ARG A 11 21.557 -51.755 82.671 1.00 73.50 N ANISOU 48 NH1 ARG A 11 8449 10169 9310 621 -1400 1540 N ATOM 49 NH2 ARG A 11 22.867 -51.867 84.553 1.00 76.04 N ANISOU 49 NH2 ARG A 11 8818 10423 9650 580 -1761 1632 N ATOM 50 N CYS A 12 19.104 -46.643 79.323 1.00 68.09 N ANISOU 50 N CYS A 12 7588 9736 8548 33 -735 1695 N ATOM 51 CA CYS A 12 17.871 -45.913 79.043 1.00 67.18 C ANISOU 51 CA CYS A 12 7618 9506 8400 -22 -654 1690 C ATOM 52 C CYS A 12 16.717 -46.867 79.227 1.00 66.04 C ANISOU 52 C CYS A 12 7604 9250 8240 81 -624 1591 C ATOM 53 O CYS A 12 16.657 -47.896 78.552 1.00 66.17 O ANISOU 53 O CYS A 12 7568 9326 8246 210 -599 1534 O ATOM 54 CB CYS A 12 17.848 -45.408 77.601 1.00 67.50 C ANISOU 54 CB CYS A 12 7549 9685 8412 -17 -554 1734 C ATOM 55 SG CYS A 12 19.324 -44.512 77.078 1.00 70.67 S ANISOU 55 SG CYS A 12 7745 10294 8811 -167 -556 1867 S ATOM 56 N LEU A 13 15.803 -46.517 80.130 1.00 65.56 N ANISOU 56 N LEU A 13 7714 9031 8163 14 -622 1567 N ATOM 57 CA LEU A 13 14.645 -47.360 80.458 1.00 64.87 C ANISOU 57 CA LEU A 13 7738 8855 8053 54 -583 1486 C ATOM 58 C LEU A 13 13.339 -46.823 79.884 1.00 64.44 C ANISOU 58 C LEU A 13 7691 8795 7998 65 -487 1458 C ATOM 59 O LEU A 13 13.011 -45.641 80.038 1.00 64.56 O ANISOU 59 O LEU A 13 7746 8766 8018 26 -463 1481 O ATOM 60 CB LEU A 13 14.513 -47.536 81.968 1.00 64.81 C ANISOU 60 CB LEU A 13 7904 8714 8008 -27 -631 1470 C ATOM 61 CG LEU A 13 15.777 -48.059 82.636 1.00 65.64 C ANISOU 61 CG LEU A 13 8017 8811 8113 -29 -770 1505 C ATOM 62 CD1 LEU A 13 15.681 -47.915 84.146 1.00 66.28 C ANISOU 62 CD1 LEU A 13 8304 8754 8124 -141 -831 1507 C ATOM 63 CD2 LEU A 13 16.040 -49.501 82.221 1.00 66.01 C ANISOU 63 CD2 LEU A 13 8033 8878 8168 99 -816 1470 C ATOM 64 N GLN A 14 12.598 -47.713 79.229 1.00 64.16 N ANISOU 64 N GLN A 14 7626 8795 7957 125 -454 1403 N ATOM 65 CA GLN A 14 11.338 -47.361 78.602 1.00 63.92 C ANISOU 65 CA GLN A 14 7562 8790 7934 146 -391 1375 C ATOM 66 C GLN A 14 10.252 -48.343 79.014 1.00 63.83 C ANISOU 66 C GLN A 14 7594 8749 7909 111 -365 1305 C ATOM 67 O GLN A 14 10.327 -49.531 78.708 1.00 63.78 O ANISOU 67 O GLN A 14 7610 8741 7882 117 -404 1274 O ATOM 68 CB GLN A 14 11.498 -47.351 77.085 1.00 64.10 C ANISOU 68 CB GLN A 14 7484 8924 7946 220 -394 1394 C ATOM 69 CG GLN A 14 10.292 -46.844 76.326 1.00 64.84 C ANISOU 69 CG GLN A 14 7539 9052 8047 253 -372 1384 C ATOM 70 CD GLN A 14 10.375 -47.150 74.842 1.00 66.21 C ANISOU 70 CD GLN A 14 7654 9330 8171 313 -391 1391 C ATOM 71 OE1 GLN A 14 11.402 -46.911 74.199 1.00 66.45 O ANISOU 71 OE1 GLN A 14 7657 9430 8160 330 -386 1444 O ATOM 72 NE2 GLN A 14 9.287 -47.678 74.288 1.00 66.83 N ANISOU 72 NE2 GLN A 14 7711 9440 8242 331 -411 1336 N ATOM 73 N MET A 15 9.255 -47.831 79.730 1.00 64.04 N ANISOU 73 N MET A 15 7639 8754 7941 68 -297 1277 N ATOM 74 CA MET A 15 8.061 -48.599 80.059 1.00 64.53 C ANISOU 74 CA MET A 15 7693 8838 7989 -3 -244 1221 C ATOM 75 C MET A 15 6.879 -48.056 79.278 1.00 64.90 C ANISOU 75 C MET A 15 7587 8989 8084 54 -204 1194 C ATOM 76 O MET A 15 6.614 -46.847 79.275 1.00 65.08 O ANISOU 76 O MET A 15 7570 9018 8138 138 -172 1198 O ATOM 77 CB MET A 15 7.774 -48.571 81.561 1.00 65.17 C ANISOU 77 CB MET A 15 7885 8858 8018 -102 -174 1201 C ATOM 78 CG MET A 15 7.451 -47.202 82.120 1.00 65.56 C ANISOU 78 CG MET A 15 7936 8900 8073 -50 -96 1182 C ATOM 79 SD MET A 15 8.233 -46.967 83.714 1.00 67.31 S ANISOU 79 SD MET A 15 8382 8993 8199 -136 -97 1189 S ATOM 80 CE MET A 15 9.957 -46.785 83.248 1.00 65.52 C ANISOU 80 CE MET A 15 8185 8705 8005 -107 -261 1274 C ATOM 81 N SER A 16 6.183 -48.959 78.602 1.00 65.19 N ANISOU 81 N SER A 16 7555 9093 8122 14 -230 1166 N ATOM 82 CA SER A 16 5.023 -48.587 77.821 1.00 65.88 C ANISOU 82 CA SER A 16 7474 9300 8256 60 -228 1142 C ATOM 83 C SER A 16 3.867 -49.504 78.176 1.00 67.09 C ANISOU 83 C SER A 16 7553 9532 8408 -88 -191 1096 C ATOM 84 O SER A 16 4.013 -50.730 78.170 1.00 67.18 O ANISOU 84 O SER A 16 7660 9493 8372 -216 -240 1090 O ATOM 85 CB SER A 16 5.335 -48.637 76.321 1.00 65.64 C ANISOU 85 CB SER A 16 7415 9306 8219 140 -332 1166 C ATOM 86 OG SER A 16 6.197 -47.577 75.933 1.00 64.41 O ANISOU 86 OG SER A 16 7294 9118 8062 248 -347 1226 O ATOM 87 N SER A 17 2.729 -48.891 78.498 1.00 68.29 N ANISOU 87 N SER A 17 7534 9804 8608 -68 -107 1061 N ATOM 88 CA SER A 17 1.528 -49.612 78.907 1.00 70.00 C ANISOU 88 CA SER A 17 7618 10153 8827 -234 -42 1022 C ATOM 89 C SER A 17 0.422 -49.456 77.873 1.00 71.28 C ANISOU 89 C SER A 17 7529 10489 9065 -188 -109 1002 C ATOM 90 O SER A 17 -0.103 -48.359 77.672 1.00 72.08 O ANISOU 90 O SER A 17 7471 10678 9237 -4 -90 983 O ATOM 91 CB SER A 17 1.030 -49.110 80.269 1.00 71.08 C ANISOU 91 CB SER A 17 7717 10345 8944 -256 141 985 C ATOM 92 OG SER A 17 2.073 -49.043 81.226 1.00 70.21 O ANISOU 92 OG SER A 17 7853 10070 8755 -277 177 1006 O ATOM 93 N PHE A 18 0.081 -50.558 77.215 1.00 71.84 N ANISOU 93 N PHE A 18 7586 10593 9116 -349 -213 1003 N ATOM 94 CA PHE A 18 -1.063 -50.596 76.316 1.00 73.44 C ANISOU 94 CA PHE A 18 7544 10979 9381 -364 -303 984 C ATOM 95 C PHE A 18 -2.220 -51.229 77.080 1.00 75.87 C ANISOU 95 C PHE A 18 7666 11459 9702 -602 -206 958 C ATOM 96 O PHE A 18 -2.157 -52.404 77.445 1.00 76.29 O ANISOU 96 O PHE A 18 7859 11444 9682 -863 -212 972 O ATOM 97 CB PHE A 18 -0.742 -51.410 75.055 1.00 73.04 C ANISOU 97 CB PHE A 18 7613 10860 9279 -417 -495 994 C ATOM 98 CG PHE A 18 0.438 -50.891 74.261 1.00 70.73 C ANISOU 98 CG PHE A 18 7494 10435 8944 -215 -564 1023 C ATOM 99 CD1 PHE A 18 1.708 -51.429 74.439 1.00 69.18 C ANISOU 99 CD1 PHE A 18 7552 10062 8671 -221 -556 1033 C ATOM 100 CD2 PHE A 18 0.275 -49.886 73.320 1.00 70.33 C ANISOU 100 CD2 PHE A 18 7347 10451 8924 -25 -641 1046 C ATOM 101 CE1 PHE A 18 2.797 -50.960 73.704 1.00 67.53 C ANISOU 101 CE1 PHE A 18 7457 9783 8419 -56 -594 1061 C ATOM 102 CE2 PHE A 18 1.357 -49.412 72.586 1.00 69.01 C ANISOU 102 CE2 PHE A 18 7342 10184 8695 115 -686 1089 C ATOM 103 CZ PHE A 18 2.619 -49.951 72.779 1.00 67.55 C ANISOU 103 CZ PHE A 18 7369 9862 8436 91 -647 1093 C ATOM 104 N ALA A 19 -3.262 -50.444 77.345 1.00 77.96 N ANISOU 104 N ALA A 19 7621 11948 10054 -510 -112 922 N ATOM 105 CA ALA A 19 -4.419 -50.928 78.106 1.00 81.03 C ANISOU 105 CA ALA A 19 7765 12569 10455 -736 23 896 C ATOM 106 C ALA A 19 -5.448 -51.619 77.216 1.00 83.52 C ANISOU 106 C ALA A 19 7837 13074 10821 -919 -129 899 C ATOM 107 O ALA A 19 -5.876 -52.738 77.504 1.00 85.12 O ANISOU 107 O ALA A 19 8042 13326 10972 -1266 -124 919 O ATOM 108 CB ALA A 19 -5.070 -49.793 78.885 1.00 82.45 C ANISOU 108 CB ALA A 19 7698 12933 10698 -533 220 833 C ATOM 109 N ASN A 20 -5.846 -50.934 76.148 1.00 84.27 N ANISOU 109 N ASN A 20 7744 13267 11009 -701 -282 887 N ATOM 110 CA ASN A 20 -6.783 -51.459 75.162 1.00 86.80 C ANISOU 110 CA ASN A 20 7835 13766 11378 -842 -478 891 C ATOM 111 C ASN A 20 -6.420 -50.906 73.779 1.00 85.78 C ANISOU 111 C ASN A 20 7788 13544 11261 -596 -713 908 C ATOM 112 O ASN A 20 -5.328 -50.352 73.607 1.00 83.21 O ANISOU 112 O ASN A 20 7734 12996 10886 -389 -710 929 O ATOM 113 CB ASN A 20 -8.239 -51.150 75.567 1.00 90.60 C ANISOU 113 CB ASN A 20 7816 14629 11977 -873 -381 852 C ATOM 114 CG ASN A 20 -8.438 -49.709 76.050 1.00 91.89 C ANISOU 114 CG ASN A 20 7791 14890 12232 -480 -231 799 C ATOM 115 OD1 ASN A 20 -7.874 -48.770 75.486 1.00 90.60 O ANISOU 115 OD1 ASN A 20 7764 14568 12091 -154 -329 805 O ATOM 116 ND2 ASN A 20 -9.256 -49.538 77.103 1.00 95.90 N ANISOU 116 ND2 ASN A 20 8001 15658 12779 -516 11 744 N ATOM 117 N ARG A 21 -7.313 -51.051 72.797 1.00 88.05 N ANISOU 117 N ARG A 21 7846 14010 11600 -638 -922 909 N ATOM 118 CA ARG A 21 -7.038 -50.574 71.430 1.00 87.44 C ANISOU 118 CA ARG A 21 7869 13854 11499 -432 -1163 935 C ATOM 119 C ARG A 21 -6.835 -49.060 71.310 1.00 86.57 C ANISOU 119 C ARG A 21 7722 13718 11454 -27 -1144 949 C ATOM 120 O ARG A 21 -6.200 -48.594 70.366 1.00 85.40 O ANISOU 120 O ARG A 21 7786 13422 11240 138 -1288 993 O ATOM 121 CB ARG A 21 -8.106 -51.049 70.439 1.00 90.47 C ANISOU 121 CB ARG A 21 8018 14444 11913 -577 -1420 933 C ATOM 122 CG ARG A 21 -7.634 -52.174 69.522 1.00 90.60 C ANISOU 122 CG ARG A 21 8357 14290 11778 -806 -1616 937 C ATOM 123 CD ARG A 21 -8.434 -52.237 68.218 1.00 94.39 C ANISOU 123 CD ARG A 21 8695 14914 12253 -831 -1934 943 C ATOM 124 NE ARG A 21 -9.781 -52.778 68.412 1.00 99.13 N ANISOU 124 NE ARG A 21 8900 15808 12957 -1105 -2011 929 N ATOM 125 CZ ARG A 21 -10.901 -52.055 68.411 1.00102.32 C ANISOU 125 CZ ARG A 21 8826 16530 13522 -979 -2064 932 C ATOM 126 NH1 ARG A 21 -10.858 -50.741 68.215 1.00102.20 N ANISOU 126 NH1 ARG A 21 8712 16538 13581 -562 -2067 947 N ATOM 127 NH2 ARG A 21 -12.072 -52.651 68.600 1.00105.81 N ANISOU 127 NH2 ARG A 21 8884 17267 14051 -1274 -2124 921 N ATOM 128 N SER A 22 -7.361 -48.305 72.269 1.00 87.42 N ANISOU 128 N SER A 22 7587 13958 11671 124 -965 911 N ATOM 129 CA SER A 22 -7.248 -46.850 72.257 1.00 87.16 C ANISOU 129 CA SER A 22 7545 13869 11702 516 -956 913 C ATOM 130 C SER A 22 -6.169 -46.323 73.210 1.00 84.53 C ANISOU 130 C SER A 22 7499 13302 11316 611 -743 908 C ATOM 131 O SER A 22 -5.260 -45.608 72.791 1.00 82.76 O ANISOU 131 O SER A 22 7547 12856 11041 780 -805 959 O ATOM 132 CB SER A 22 -8.602 -46.214 72.586 1.00 90.73 C ANISOU 132 CB SER A 22 7536 14623 12316 699 -928 850 C ATOM 133 OG SER A 22 -8.488 -44.810 72.706 1.00 90.88 O ANISOU 133 OG SER A 22 7593 14544 12393 1099 -914 836 O ATOM 134 N TRP A 23 -6.279 -46.694 74.483 1.00 84.48 N ANISOU 134 N TRP A 23 7435 13356 11307 473 -503 855 N ATOM 135 CA TRP A 23 -5.481 -46.111 75.562 1.00 82.70 C ANISOU 135 CA TRP A 23 7430 12955 11038 571 -301 833 C ATOM 136 C TRP A 23 -4.045 -46.643 75.597 1.00 79.29 C ANISOU 136 C TRP A 23 7399 12248 10479 421 -303 893 C ATOM 137 O TRP A 23 -3.820 -47.845 75.462 1.00 78.70 O ANISOU 137 O TRP A 23 7409 12155 10338 154 -336 914 O ATOM 138 CB TRP A 23 -6.179 -46.379 76.897 1.00 84.50 C ANISOU 138 CB TRP A 23 7456 13374 11278 458 -44 755 C ATOM 139 CG TRP A 23 -5.718 -45.533 78.032 1.00 84.13 C ANISOU 139 CG TRP A 23 7564 13206 11194 625 158 702 C ATOM 140 CD1 TRP A 23 -6.298 -44.382 78.482 1.00 86.26 C ANISOU 140 CD1 TRP A 23 7684 13555 11535 940 256 613 C ATOM 141 CD2 TRP A 23 -4.590 -45.777 78.882 1.00 82.22 C ANISOU 141 CD2 TRP A 23 7674 12736 10828 495 270 722 C ATOM 142 NE1 TRP A 23 -5.598 -43.888 79.557 1.00 85.80 N ANISOU 142 NE1 TRP A 23 7890 13320 11389 997 425 573 N ATOM 143 CE2 TRP A 23 -4.544 -44.723 79.824 1.00 83.32 C ANISOU 143 CE2 TRP A 23 7875 12825 10957 717 429 646 C ATOM 144 CE3 TRP A 23 -3.608 -46.781 78.937 1.00 79.76 C ANISOU 144 CE3 TRP A 23 7640 12254 10413 234 233 792 C ATOM 145 CZ2 TRP A 23 -3.550 -44.643 80.813 1.00 81.84 C ANISOU 145 CZ2 TRP A 23 8015 12429 10651 650 541 646 C ATOM 146 CZ3 TRP A 23 -2.623 -46.704 79.919 1.00 78.10 C ANISOU 146 CZ3 TRP A 23 7724 11849 10102 192 341 798 C ATOM 147 CH2 TRP A 23 -2.602 -45.640 80.844 1.00 79.24 C ANISOU 147 CH2 TRP A 23 7921 11955 10231 383 488 730 C ATOM 148 N SER A 24 -3.084 -45.735 75.780 1.00 77.44 N ANISOU 148 N SER A 24 7408 11801 10214 599 -279 916 N ATOM 149 CA SER A 24 -1.662 -46.084 75.876 1.00 74.51 C ANISOU 149 CA SER A 24 7371 11200 9738 494 -275 970 C ATOM 150 C SER A 24 -0.850 -45.036 76.627 1.00 73.43 C ANISOU 150 C SER A 24 7432 10885 9582 640 -186 973 C ATOM 151 O SER A 24 -1.220 -43.858 76.665 1.00 74.48 O ANISOU 151 O SER A 24 7522 11004 9773 873 -189 950 O ATOM 152 CB SER A 24 -1.053 -46.289 74.492 1.00 73.45 C ANISOU 152 CB SER A 24 7363 10989 9557 497 -467 1041 C ATOM 153 OG SER A 24 -1.556 -47.470 73.907 1.00 74.50 O ANISOU 153 OG SER A 24 7408 11230 9669 310 -555 1030 O ATOM 154 N ARG A 25 0.264 -45.483 77.210 1.00 71.41 N ANISOU 154 N ARG A 25 7408 10482 9244 504 -131 1000 N ATOM 155 CA ARG A 25 1.181 -44.616 77.951 1.00 70.43 C ANISOU 155 CA ARG A 25 7497 10179 9086 582 -73 1011 C ATOM 156 C ARG A 25 2.655 -45.004 77.736 1.00 68.40 C ANISOU 156 C ARG A 25 7463 9770 8755 477 -136 1087 C ATOM 157 O ARG A 25 2.991 -46.188 77.687 1.00 67.59 O ANISOU 157 O ARG A 25 7393 9680 8610 320 -149 1097 O ATOM 158 CB ARG A 25 0.828 -44.631 79.446 1.00 71.22 C ANISOU 158 CB ARG A 25 7601 10305 9155 532 113 932 C ATOM 159 CG ARG A 25 1.812 -43.868 80.319 1.00 70.22 C ANISOU 159 CG ARG A 25 7731 9982 8968 569 153 935 C ATOM 160 CD ARG A 25 1.285 -43.609 81.702 1.00 71.06 C ANISOU 160 CD ARG A 25 7852 10122 9024 579 337 837 C ATOM 161 NE ARG A 25 1.866 -42.374 82.212 1.00 71.56 N ANISOU 161 NE ARG A 25 8134 9996 9059 719 331 815 N ATOM 162 CZ ARG A 25 1.229 -41.207 82.255 1.00 73.79 C ANISOU 162 CZ ARG A 25 8392 10258 9386 966 356 739 C ATOM 163 NH1 ARG A 25 -0.030 -41.115 81.841 1.00 75.75 N ANISOU 163 NH1 ARG A 25 8360 10698 9723 1121 395 677 N ATOM 164 NH2 ARG A 25 1.845 -40.130 82.726 1.00 73.97 N ANISOU 164 NH2 ARG A 25 8677 10063 9367 1063 326 721 N ATOM 165 N THR A 26 3.523 -44.001 77.600 1.00 67.92 N ANISOU 165 N THR A 26 7554 9570 8682 567 -182 1141 N ATOM 166 CA THR A 26 4.971 -44.220 77.541 1.00 66.54 C ANISOU 166 CA THR A 26 7546 9288 8447 474 -223 1211 C ATOM 167 C THR A 26 5.738 -43.198 78.377 1.00 66.66 C ANISOU 167 C THR A 26 7733 9151 8443 490 -204 1230 C ATOM 168 O THR A 26 5.716 -41.992 78.094 1.00 67.39 O ANISOU 168 O THR A 26 7890 9159 8555 600 -251 1259 O ATOM 169 CB THR A 26 5.510 -44.220 76.091 1.00 66.11 C ANISOU 169 CB THR A 26 7491 9256 8371 496 -334 1290 C ATOM 170 OG1 THR A 26 5.000 -45.363 75.404 1.00 66.42 O ANISOU 170 OG1 THR A 26 7427 9411 8399 447 -366 1260 O ATOM 171 CG2 THR A 26 7.051 -44.268 76.061 1.00 64.75 C ANISOU 171 CG2 THR A 26 7443 9016 8143 419 -351 1360 C ATOM 172 N ASP A 27 6.409 -43.705 79.410 1.00 66.08 N ANISOU 172 N ASP A 27 7760 9026 8323 371 -159 1218 N ATOM 173 CA ASP A 27 7.303 -42.907 80.234 1.00 66.06 C ANISOU 173 CA ASP A 27 7936 8878 8284 339 -172 1240 C ATOM 174 C ASP A 27 8.703 -43.482 80.103 1.00 64.79 C ANISOU 174 C ASP A 27 7820 8704 8094 223 -244 1317 C ATOM 175 O ASP A 27 8.866 -44.691 79.956 1.00 64.09 O ANISOU 175 O ASP A 27 7672 8685 7994 172 -246 1312 O ATOM 176 CB ASP A 27 6.842 -42.915 81.694 1.00 67.03 C ANISOU 176 CB ASP A 27 8147 8964 8359 311 -66 1151 C ATOM 177 CG ASP A 27 5.415 -42.400 81.864 1.00 69.38 C ANISOU 177 CG ASP A 27 8349 9325 8688 455 37 1054 C ATOM 178 OD1 ASP A 27 5.159 -41.207 81.568 1.00 71.01 O ANISOU 178 OD1 ASP A 27 8596 9454 8931 611 3 1043 O ATOM 179 OD2 ASP A 27 4.548 -43.191 82.298 1.00 70.81 O ANISOU 179 OD2 ASP A 27 8412 9636 8855 411 148 991 O ATOM 180 N SER A 28 9.706 -42.609 80.147 1.00 64.91 N ANISOU 180 N SER A 28 7937 8630 8097 183 -312 1385 N ATOM 181 CA SER A 28 11.102 -43.009 79.971 1.00 64.52 C ANISOU 181 CA SER A 28 7873 8610 8032 84 -381 1462 C ATOM 182 C SER A 28 12.014 -42.375 81.025 1.00 65.02 C ANISOU 182 C SER A 28 8081 8559 8065 -24 -441 1490 C ATOM 183 O SER A 28 11.840 -41.210 81.381 1.00 65.99 O ANISOU 183 O SER A 28 8343 8555 8176 -28 -459 1489 O ATOM 184 CB SER A 28 11.594 -42.616 78.572 1.00 64.66 C ANISOU 184 CB SER A 28 7808 8702 8058 96 -420 1553 C ATOM 185 OG SER A 28 10.597 -42.820 77.580 1.00 65.09 O ANISOU 185 OG SER A 28 7779 8828 8125 201 -393 1529 O ATOM 186 N VAL A 29 12.983 -43.142 81.522 1.00 64.68 N ANISOU 186 N VAL A 29 8020 8548 8006 -102 -495 1512 N ATOM 187 CA VAL A 29 14.020 -42.596 82.405 1.00 65.48 C ANISOU 187 CA VAL A 29 8229 8570 8079 -228 -595 1556 C ATOM 188 C VAL A 29 15.413 -43.045 81.980 1.00 65.66 C ANISOU 188 C VAL A 29 8097 8719 8130 -287 -681 1640 C ATOM 189 O VAL A 29 15.571 -44.115 81.400 1.00 65.12 O ANISOU 189 O VAL A 29 7887 8772 8085 -205 -658 1629 O ATOM 190 CB VAL A 29 13.798 -42.970 83.882 1.00 65.77 C ANISOU 190 CB VAL A 29 8433 8510 8048 -269 -601 1487 C ATOM 191 CG1 VAL A 29 12.629 -42.188 84.462 1.00 66.33 C ANISOU 191 CG1 VAL A 29 8663 8468 8073 -222 -507 1399 C ATOM 192 CG2 VAL A 29 13.590 -44.462 84.030 1.00 65.50 C ANISOU 192 CG2 VAL A 29 8340 8544 8004 -231 -576 1455 C ATOM 193 N VAL A 30 16.417 -42.221 82.269 1.00 66.85 N ANISOU 193 N VAL A 30 8274 8847 8279 -428 -783 1716 N ATOM 194 CA VAL A 30 17.794 -42.507 81.860 1.00 67.68 C ANISOU 194 CA VAL A 30 8176 9120 8420 -494 -857 1801 C ATOM 195 C VAL A 30 18.808 -42.360 83.010 1.00 69.22 C ANISOU 195 C VAL A 30 8418 9280 8604 -636 -1018 1835 C ATOM 196 O VAL A 30 18.978 -41.278 83.589 1.00 70.00 O ANISOU 196 O VAL A 30 8679 9248 8669 -794 -1098 1866 O ATOM 197 CB VAL A 30 18.203 -41.679 80.616 1.00 68.21 C ANISOU 197 CB VAL A 30 8125 9292 8500 -567 -823 1901 C ATOM 198 CG1 VAL A 30 19.686 -41.774 80.360 1.00 69.66 C ANISOU 198 CG1 VAL A 30 8078 9679 8711 -678 -887 1993 C ATOM 199 CG2 VAL A 30 17.448 -42.153 79.398 1.00 66.94 C ANISOU 199 CG2 VAL A 30 7878 9219 8336 -413 -696 1872 C ATOM 200 N TRP A 31 19.469 -43.476 83.320 1.00 69.77 N ANISOU 200 N TRP A 31 8361 9452 8697 -569 -1084 1825 N ATOM 201 CA TRP A 31 20.431 -43.560 84.407 1.00 71.50 C ANISOU 201 CA TRP A 31 8601 9658 8907 -671 -1269 1856 C ATOM 202 C TRP A 31 21.837 -43.712 83.862 1.00 73.32 C ANISOU 202 C TRP A 31 8510 10133 9215 -701 -1350 1941 C ATOM 203 O TRP A 31 22.082 -44.520 82.960 1.00 73.37 O ANISOU 203 O TRP A 31 8290 10317 9270 -539 -1271 1927 O ATOM 204 CB TRP A 31 20.117 -44.757 85.313 1.00 71.15 C ANISOU 204 CB TRP A 31 8682 9529 8821 -556 -1319 1787 C ATOM 205 CG TRP A 31 18.782 -44.674 85.949 1.00 70.35 C ANISOU 205 CG TRP A 31 8863 9237 8630 -551 -1221 1707 C ATOM 206 CD1 TRP A 31 17.597 -45.091 85.418 1.00 69.49 C ANISOU 206 CD1 TRP A 31 8776 9111 8517 -437 -1051 1641 C ATOM 207 CD2 TRP A 31 18.477 -44.122 87.232 1.00 71.03 C ANISOU 207 CD2 TRP A 31 9233 9148 8606 -668 -1276 1676 C ATOM 208 NE1 TRP A 31 16.570 -44.836 86.293 1.00 69.56 N ANISOU 208 NE1 TRP A 31 9024 8972 8432 -473 -982 1574 N ATOM 209 CE2 TRP A 31 17.081 -44.240 87.415 1.00 70.32 C ANISOU 209 CE2 TRP A 31 9301 8966 8453 -604 -1105 1587 C ATOM 210 CE3 TRP A 31 19.246 -43.543 88.247 1.00 72.65 C ANISOU 210 CE3 TRP A 31 9576 9277 8750 -828 -1457 1710 C ATOM 211 CZ2 TRP A 31 16.435 -43.798 88.574 1.00 70.74 C ANISOU 211 CZ2 TRP A 31 9638 8868 8373 -672 -1076 1522 C ATOM 212 CZ3 TRP A 31 18.606 -43.098 89.395 1.00 73.52 C ANISOU 212 CZ3 TRP A 31 10014 9204 8717 -902 -1450 1643 C ATOM 213 CH2 TRP A 31 17.211 -43.232 89.549 1.00 72.67 C ANISOU 213 CH2 TRP A 31 10052 9020 8538 -813 -1245 1545 C ATOM 214 N LEU A 32 22.752 -42.920 84.409 1.00 75.33 N ANISOU 214 N LEU A 32 8742 10406 9474 -914 -1506 2020 N ATOM 215 CA LEU A 32 24.174 -43.113 84.191 1.00 77.62 C ANISOU 215 CA LEU A 32 8693 10957 9841 -964 -1618 2099 C ATOM 216 C LEU A 32 24.733 -43.653 85.495 1.00 78.90 C ANISOU 216 C LEU A 32 8917 11065 9996 -963 -1849 2089 C ATOM 217 O LEU A 32 24.724 -42.964 86.520 1.00 79.52 O ANISOU 217 O LEU A 32 9238 10969 10006 -1153 -1994 2104 O ATOM 218 CB LEU A 32 24.852 -41.797 83.786 1.00 79.40 C ANISOU 218 CB LEU A 32 8820 11271 10076 -1257 -1647 2220 C ATOM 219 CG LEU A 32 26.381 -41.720 83.650 1.00 82.46 C ANISOU 219 CG LEU A 32 8824 11965 10541 -1402 -1770 2324 C ATOM 220 CD1 LEU A 32 26.973 -42.885 82.849 1.00 83.12 C ANISOU 220 CD1 LEU A 32 8514 12365 10703 -1140 -1676 2296 C ATOM 221 CD2 LEU A 32 26.795 -40.381 83.045 1.00 83.70 C ANISOU 221 CD2 LEU A 32 8932 12188 10683 -1732 -1749 2455 C ATOM 222 N GLY A 33 25.205 -44.895 85.453 1.00 79.59 N ANISOU 222 N GLY A 33 8817 11283 10139 -736 -1898 2058 N ATOM 223 CA GLY A 33 25.598 -45.601 86.662 1.00 80.89 C ANISOU 223 CA GLY A 33 9087 11364 10284 -682 -2132 2047 C ATOM 224 C GLY A 33 24.344 -45.755 87.492 1.00 79.20 C ANISOU 224 C GLY A 33 9313 10839 9941 -679 -2093 1976 C ATOM 225 O GLY A 33 23.476 -46.561 87.157 1.00 77.78 O ANISOU 225 O GLY A 33 9226 10585 9741 -500 -1950 1905 O ATOM 226 N ASP A 34 24.240 -44.958 88.554 1.00 79.85 N ANISOU 226 N ASP A 34 9663 10751 9924 -892 -2212 1991 N ATOM 227 CA ASP A 34 23.020 -44.885 89.364 1.00 78.56 C ANISOU 227 CA ASP A 34 9913 10322 9613 -918 -2134 1916 C ATOM 228 C ASP A 34 22.647 -43.444 89.735 1.00 78.56 C ANISOU 228 C ASP A 34 10142 10177 9530 -1140 -2110 1907 C ATOM 229 O ASP A 34 22.269 -43.155 90.870 1.00 79.08 O ANISOU 229 O ASP A 34 10545 10052 9450 -1235 -2177 1864 O ATOM 230 CB ASP A 34 23.115 -45.791 90.604 1.00 79.63 C ANISOU 230 CB ASP A 34 10271 10338 9645 -879 -2318 1907 C ATOM 231 CG ASP A 34 24.401 -45.592 91.388 1.00 82.95 C ANISOU 231 CG ASP A 34 10634 10815 10068 -1005 -2636 1984 C ATOM 232 OD1 ASP A 34 24.893 -44.442 91.471 1.00 85.42 O ANISOU 232 OD1 ASP A 34 10916 11154 10386 -1224 -2715 2025 O ATOM 233 OD2 ASP A 34 24.919 -46.592 91.934 1.00 84.66 O ANISOU 233 OD2 ASP A 34 10850 11038 10278 -890 -2832 2009 O ATOM 234 N LEU A 35 22.777 -42.550 88.759 1.00 78.35 N ANISOU 234 N LEU A 35 9954 10232 9582 -1217 -2019 1946 N ATOM 235 CA LEU A 35 22.310 -41.173 88.871 1.00 78.61 C ANISOU 235 CA LEU A 35 10226 10094 9549 -1385 -1980 1933 C ATOM 236 C LEU A 35 21.331 -40.913 87.738 1.00 76.79 C ANISOU 236 C LEU A 35 9954 9861 9360 -1263 -1729 1900 C ATOM 237 O LEU A 35 21.642 -41.179 86.571 1.00 76.41 O ANISOU 237 O LEU A 35 9609 10008 9416 -1198 -1647 1955 O ATOM 238 CB LEU A 35 23.476 -40.190 88.756 1.00 80.92 C ANISOU 238 CB LEU A 35 10403 10458 9885 -1651 -2160 2043 C ATOM 239 CG LEU A 35 24.412 -39.953 89.942 1.00 83.63 C ANISOU 239 CG LEU A 35 10851 10757 10167 -1860 -2457 2081 C ATOM 240 CD1 LEU A 35 25.780 -39.534 89.440 1.00 86.03 C ANISOU 240 CD1 LEU A 35 10808 11296 10584 -2075 -2614 2218 C ATOM 241 CD2 LEU A 35 23.852 -38.901 90.888 1.00 84.85 C ANISOU 241 CD2 LEU A 35 11478 10602 10160 -2016 -2515 2012 C ATOM 242 N GLN A 36 20.149 -40.402 88.069 1.00 75.92 N ANISOU 242 N GLN A 36 10134 9548 9163 -1217 -1609 1807 N ATOM 243 CA GLN A 36 19.162 -40.096 87.039 1.00 74.39 C ANISOU 243 CA GLN A 36 9907 9346 9011 -1089 -1404 1777 C ATOM 244 C GLN A 36 19.565 -38.835 86.272 1.00 75.56 C ANISOU 244 C GLN A 36 10044 9468 9198 -1237 -1441 1864 C ATOM 245 O GLN A 36 19.898 -37.807 86.871 1.00 77.34 O ANISOU 245 O GLN A 36 10493 9528 9364 -1421 -1574 1880 O ATOM 246 CB GLN A 36 17.757 -39.959 87.632 1.00 73.66 C ANISOU 246 CB GLN A 36 10083 9080 8826 -967 -1263 1644 C ATOM 247 CG GLN A 36 16.657 -40.403 86.672 1.00 71.04 C ANISOU 247 CG GLN A 36 9616 8824 8553 -767 -1058 1599 C ATOM 248 CD GLN A 36 15.288 -39.874 87.035 1.00 69.56 C ANISOU 248 CD GLN A 36 9634 8496 8300 -654 -915 1479 C ATOM 249 OE1 GLN A 36 14.987 -39.635 88.201 1.00 69.99 O ANISOU 249 OE1 GLN A 36 9935 8422 8237 -681 -917 1396 O ATOM 250 NE2 GLN A 36 14.445 -39.693 86.028 1.00 68.71 N ANISOU 250 NE2 GLN A 36 9417 8429 8260 -515 -791 1464 N ATOM 251 N THR A 37 19.546 -38.927 84.946 1.00 74.83 N ANISOU 251 N THR A 37 9720 9527 9185 -1174 -1335 1924 N ATOM 252 CA THR A 37 19.973 -37.825 84.094 1.00 76.08 C ANISOU 252 CA THR A 37 9862 9682 9363 -1338 -1363 2037 C ATOM 253 C THR A 37 18.841 -37.311 83.222 1.00 75.37 C ANISOU 253 C THR A 37 9874 9493 9270 -1199 -1225 2012 C ATOM 254 O THR A 37 18.748 -36.109 82.969 1.00 76.78 O ANISOU 254 O THR A 37 10249 9503 9421 -1309 -1276 2064 O ATOM 255 CB THR A 37 21.139 -38.229 83.183 1.00 76.70 C ANISOU 255 CB THR A 37 9568 10063 9513 -1430 -1371 2160 C ATOM 256 OG1 THR A 37 20.809 -39.446 82.506 1.00 74.99 O ANISOU 256 OG1 THR A 37 9127 10029 9338 -1190 -1227 2110 O ATOM 257 CG2 THR A 37 22.413 -38.427 83.987 1.00 78.41 C ANISOU 257 CG2 THR A 37 9659 10386 9747 -1605 -1557 2212 C ATOM 258 N HIS A 38 17.984 -38.222 82.764 1.00 73.62 N ANISOU 258 N HIS A 38 9534 9363 9074 -963 -1075 1938 N ATOM 259 CA HIS A 38 16.921 -37.866 81.826 1.00 73.05 C ANISOU 259 CA HIS A 38 9502 9244 9011 -816 -964 1921 C ATOM 260 C HIS A 38 15.555 -38.417 82.226 1.00 71.82 C ANISOU 260 C HIS A 38 9409 9030 8849 -586 -849 1774 C ATOM 261 O HIS A 38 15.444 -39.472 82.857 1.00 70.67 O ANISOU 261 O HIS A 38 9199 8954 8698 -528 -813 1704 O ATOM 262 CB HIS A 38 17.286 -38.287 80.396 1.00 72.60 C ANISOU 262 CB HIS A 38 9182 9417 8985 -802 -895 2012 C ATOM 263 CG HIS A 38 18.551 -37.662 79.886 1.00 74.67 C ANISOU 263 CG HIS A 38 9353 9778 9239 -1048 -969 2168 C ATOM 264 ND1 HIS A 38 19.803 -38.149 80.199 1.00 75.33 N ANISOU 264 ND1 HIS A 38 9226 10047 9348 -1179 -1029 2216 N ATOM 265 CD2 HIS A 38 18.758 -36.588 79.085 1.00 76.39 C ANISOU 265 CD2 HIS A 38 9655 9947 9422 -1202 -998 2294 C ATOM 266 CE1 HIS A 38 20.724 -37.402 79.615 1.00 77.14 C ANISOU 266 CE1 HIS A 38 9377 10370 9563 -1419 -1072 2363 C ATOM 267 NE2 HIS A 38 20.117 -36.450 78.931 1.00 77.66 N ANISOU 267 NE2 HIS A 38 9639 10285 9582 -1454 -1052 2419 N ATOM 268 N ARG A 39 14.522 -37.667 81.852 1.00 72.38 N ANISOU 268 N ARG A 39 9608 8975 8918 -464 -804 1738 N ATOM 269 CA ARG A 39 13.138 -38.009 82.143 1.00 71.95 C ANISOU 269 CA ARG A 39 9574 8896 8866 -250 -687 1602 C ATOM 270 C ARG A 39 12.271 -37.636 80.947 1.00 71.95 C ANISOU 270 C ARG A 39 9516 8912 8908 -100 -648 1620 C ATOM 271 O ARG A 39 12.310 -36.497 80.484 1.00 73.41 O ANISOU 271 O ARG A 39 9852 8954 9085 -114 -725 1685 O ATOM 272 CB ARG A 39 12.669 -37.258 83.393 1.00 73.25 C ANISOU 272 CB ARG A 39 10015 8849 8968 -220 -694 1493 C ATOM 273 CG ARG A 39 11.157 -37.201 83.588 1.00 74.14 C ANISOU 273 CG ARG A 39 10148 8937 9083 18 -560 1353 C ATOM 274 CD ARG A 39 10.757 -35.978 84.399 1.00 77.36 C ANISOU 274 CD ARG A 39 10866 9100 9429 92 -583 1257 C ATOM 275 NE ARG A 39 11.346 -36.008 85.737 1.00 79.42 N ANISOU 275 NE ARG A 39 11322 9272 9583 -48 -617 1205 N ATOM 276 CZ ARG A 39 11.369 -34.979 86.580 1.00 82.24 C ANISOU 276 CZ ARG A 39 12007 9390 9849 -51 -675 1126 C ATOM 277 NH1 ARG A 39 10.837 -33.812 86.231 1.00 84.37 N ANISOU 277 NH1 ARG A 39 12459 9464 10133 99 -708 1087 N ATOM 278 NH2 ARG A 39 11.930 -35.119 87.778 1.00 83.00 N ANISOU 278 NH2 ARG A 39 12282 9426 9829 -197 -720 1083 N ATOM 279 N TRP A 40 11.502 -38.596 80.443 1.00 70.76 N ANISOU 279 N TRP A 40 9172 8922 8793 30 -552 1572 N ATOM 280 CA TRP A 40 10.550 -38.316 79.375 1.00 71.17 C ANISOU 280 CA TRP A 40 9161 9001 8879 186 -537 1577 C ATOM 281 C TRP A 40 9.165 -38.832 79.727 1.00 71.02 C ANISOU 281 C TRP A 40 9050 9042 8891 362 -433 1442 C ATOM 282 O TRP A 40 8.899 -40.032 79.664 1.00 69.98 O ANISOU 282 O TRP A 40 8749 9069 8770 355 -366 1405 O ATOM 283 CB TRP A 40 11.022 -38.884 78.031 1.00 70.56 C ANISOU 283 CB TRP A 40 8913 9094 8801 141 -549 1678 C ATOM 284 CG TRP A 40 10.359 -38.240 76.842 1.00 71.70 C ANISOU 284 CG TRP A 40 9072 9223 8947 248 -593 1733 C ATOM 285 CD1 TRP A 40 9.691 -37.047 76.821 1.00 73.94 C ANISOU 285 CD1 TRP A 40 9529 9323 9242 360 -660 1733 C ATOM 286 CD2 TRP A 40 10.339 -38.729 75.497 1.00 71.56 C ANISOU 286 CD2 TRP A 40 8923 9362 8903 262 -596 1796 C ATOM 287 NE1 TRP A 40 9.241 -36.771 75.551 1.00 74.48 N ANISOU 287 NE1 TRP A 40 9576 9424 9298 441 -720 1808 N ATOM 288 CE2 TRP A 40 9.627 -37.785 74.718 1.00 72.88 C ANISOU 288 CE2 TRP A 40 9192 9437 9063 369 -678 1848 C ATOM 289 CE3 TRP A 40 10.844 -39.873 74.875 1.00 70.73 C ANISOU 289 CE3 TRP A 40 8650 9456 8767 212 -546 1806 C ATOM 290 CZ2 TRP A 40 9.408 -37.952 73.353 1.00 72.98 C ANISOU 290 CZ2 TRP A 40 9145 9559 9024 401 -715 1919 C ATOM 291 CZ3 TRP A 40 10.626 -40.037 73.511 1.00 71.15 C ANISOU 291 CZ3 TRP A 40 8649 9619 8765 251 -563 1858 C ATOM 292 CH2 TRP A 40 9.914 -39.080 72.768 1.00 72.07 C ANISOU 292 CH2 TRP A 40 8871 9650 8863 331 -649 1920 C ATOM 293 N SER A 41 8.288 -37.911 80.108 1.00 72.40 N ANISOU 293 N SER A 41 9341 9091 9078 517 -423 1365 N ATOM 294 CA SER A 41 6.930 -38.267 80.475 1.00 72.74 C ANISOU 294 CA SER A 41 9257 9227 9153 688 -309 1233 C ATOM 295 C SER A 41 6.024 -38.311 79.248 1.00 72.96 C ANISOU 295 C SER A 41 9103 9367 9250 839 -341 1253 C ATOM 296 O SER A 41 6.269 -37.612 78.259 1.00 73.36 O ANISOU 296 O SER A 41 9224 9343 9308 870 -461 1353 O ATOM 297 CB SER A 41 6.385 -37.278 81.505 1.00 74.64 C ANISOU 297 CB SER A 41 9683 9307 9368 828 -266 1114 C ATOM 298 OG SER A 41 5.122 -37.707 81.984 1.00 75.65 O ANISOU 298 OG SER A 41 9643 9583 9516 974 -115 977 O ATOM 299 N ASN A 42 4.984 -39.144 79.321 1.00 72.77 N ANISOU 299 N ASN A 42 8856 9528 9264 905 -245 1166 N ATOM 300 CA ASN A 42 3.925 -39.163 78.318 1.00 73.36 C ANISOU 300 CA ASN A 42 8738 9727 9410 1060 -288 1162 C ATOM 301 C ASN A 42 3.222 -37.812 78.282 1.00 75.60 C ANISOU 301 C ASN A 42 9105 9881 9737 1318 -345 1120 C ATOM 302 O ASN A 42 2.731 -37.398 77.238 1.00 76.69 O ANISOU 302 O ASN A 42 9189 10030 9920 1456 -468 1171 O ATOM 303 CB ASN A 42 2.923 -40.289 78.605 1.00 73.42 C ANISOU 303 CB ASN A 42 8484 9963 9448 1040 -172 1071 C ATOM 304 CG ASN A 42 2.129 -40.699 77.373 1.00 73.76 C ANISOU 304 CG ASN A 42 8307 10168 9549 1099 -260 1098 C ATOM 305 OD1 ASN A 42 2.515 -41.628 76.665 1.00 72.12 O ANISOU 305 OD1 ASN A 42 8054 10035 9312 954 -308 1157 O ATOM 306 ND2 ASN A 42 1.013 -40.006 77.115 1.00 76.27 N ANISOU 306 ND2 ASN A 42 8495 10540 9944 1328 -295 1047 N ATOM 307 N ASP A 43 3.198 -37.132 79.431 1.00 76.64 N ANISOU 307 N ASP A 43 9400 9876 9843 1392 -271 1025 N ATOM 308 CA ASP A 43 2.647 -35.778 79.572 1.00 79.21 C ANISOU 308 CA ASP A 43 9879 10020 10196 1665 -327 960 C ATOM 309 C ASP A 43 3.221 -34.810 78.545 1.00 79.56 C ANISOU 309 C ASP A 43 10147 9847 10237 1686 -541 1106 C ATOM 310 O ASP A 43 2.474 -34.148 77.818 1.00 81.37 O ANISOU 310 O ASP A 43 10361 10031 10524 1924 -656 1115 O ATOM 311 CB ASP A 43 2.947 -35.207 80.968 1.00 80.24 C ANISOU 311 CB ASP A 43 10259 9977 10250 1674 -235 849 C ATOM 312 CG ASP A 43 2.428 -36.079 82.099 1.00 80.55 C ANISOU 312 CG ASP A 43 10138 10217 10250 1629 -9 713 C ATOM 313 OD1 ASP A 43 1.847 -37.155 81.832 1.00 80.92 O ANISOU 313 OD1 ASP A 43 9877 10531 10339 1567 74 712 O ATOM 314 OD2 ASP A 43 2.609 -35.679 83.269 1.00 81.40 O ANISOU 314 OD2 ASP A 43 10455 10206 10266 1636 79 610 O ATOM 315 N SER A 44 4.553 -34.743 78.503 1.00 78.00 N ANISOU 315 N SER A 44 10149 9524 9965 1427 -599 1227 N ATOM 316 CA SER A 44 5.274 -33.746 77.716 1.00 78.70 C ANISOU 316 CA SER A 44 10498 9387 10016 1368 -782 1380 C ATOM 317 C SER A 44 5.822 -34.315 76.414 1.00 77.21 C ANISOU 317 C SER A 44 10193 9342 9803 1198 -846 1546 C ATOM 318 O SER A 44 6.203 -35.487 76.349 1.00 75.11 O ANISOU 318 O SER A 44 9724 9291 9525 1039 -752 1552 O ATOM 319 CB SER A 44 6.408 -33.132 78.541 1.00 78.77 C ANISOU 319 CB SER A 44 10811 9169 9949 1170 -811 1409 C ATOM 320 OG SER A 44 7.390 -34.100 78.844 1.00 76.30 O ANISOU 320 OG SER A 44 10385 9007 9598 893 -735 1453 O ATOM 321 N ALA A 45 5.865 -33.465 75.388 1.00 78.54 N ANISOU 321 N ALA A 45 10523 9375 9945 1238 -1010 1676 N ATOM 322 CA ALA A 45 6.346 -33.850 74.061 1.00 77.67 C ANISOU 322 CA ALA A 45 10347 9392 9772 1088 -1071 1837 C ATOM 323 C ALA A 45 7.872 -33.752 73.924 1.00 76.80 C ANISOU 323 C ALA A 45 10368 9248 9566 760 -1070 1983 C ATOM 324 O ALA A 45 8.431 -34.066 72.868 1.00 76.38 O ANISOU 324 O ALA A 45 10264 9324 9434 613 -1085 2113 O ATOM 325 CB ALA A 45 5.645 -33.021 72.980 1.00 80.00 C ANISOU 325 CB ALA A 45 10762 9576 10058 1272 -1255 1924 C ATOM 326 N THR A 46 8.534 -33.321 74.998 1.00 76.66 N ANISOU 326 N THR A 46 10507 9076 9544 643 -1050 1954 N ATOM 327 CA THR A 46 9.985 -33.139 75.008 1.00 76.32 C ANISOU 327 CA THR A 46 10561 9012 9426 318 -1065 2088 C ATOM 328 C THR A 46 10.629 -33.872 76.180 1.00 74.54 C ANISOU 328 C THR A 46 10222 8877 9221 192 -957 1997 C ATOM 329 O THR A 46 10.030 -33.991 77.249 1.00 74.19 O ANISOU 329 O THR A 46 10191 8775 9221 330 -903 1841 O ATOM 330 CB THR A 46 10.374 -31.644 75.115 1.00 78.94 C ANISOU 330 CB THR A 46 11280 9006 9709 223 -1225 2189 C ATOM 331 OG1 THR A 46 9.947 -31.127 76.382 1.00 79.87 O ANISOU 331 OG1 THR A 46 11575 8904 9868 360 -1237 2035 O ATOM 332 CG2 THR A 46 9.746 -30.820 73.992 1.00 80.94 C ANISOU 332 CG2 THR A 46 11711 9114 9927 355 -1371 2297 C ATOM 333 N ILE A 47 11.851 -34.356 75.967 1.00 73.67 N ANISOU 333 N ILE A 47 10000 8921 9069 -61 -927 2096 N ATOM 334 CA ILE A 47 12.673 -34.933 77.034 1.00 72.69 C ANISOU 334 CA ILE A 47 9797 8863 8957 -203 -878 2044 C ATOM 335 C ILE A 47 13.111 -33.834 78.002 1.00 74.46 C ANISOU 335 C ILE A 47 10314 8818 9158 -330 -985 2051 C ATOM 336 O ILE A 47 13.329 -32.691 77.597 1.00 76.58 O ANISOU 336 O ILE A 47 10822 8889 9385 -428 -1104 2161 O ATOM 337 CB ILE A 47 13.918 -35.674 76.460 1.00 72.02 C ANISOU 337 CB ILE A 47 9489 9034 8843 -411 -834 2151 C ATOM 338 CG1 ILE A 47 13.492 -36.957 75.743 1.00 70.25 C ANISOU 338 CG1 ILE A 47 9005 9055 8631 -266 -725 2096 C ATOM 339 CG2 ILE A 47 14.934 -36.006 77.559 1.00 71.39 C ANISOU 339 CG2 ILE A 47 9360 8989 8777 -576 -846 2131 C ATOM 340 CD1 ILE A 47 14.364 -37.317 74.565 1.00 70.63 C ANISOU 340 CD1 ILE A 47 8897 9327 8613 -386 -684 2214 C ATOM 341 N SER A 48 13.228 -34.186 79.279 1.00 73.92 N ANISOU 341 N SER A 48 10262 8724 9100 -339 -957 1934 N ATOM 342 CA SER A 48 13.681 -33.249 80.296 1.00 75.66 C ANISOU 342 CA SER A 48 10778 8693 9277 -471 -1068 1918 C ATOM 343 C SER A 48 15.028 -33.661 80.876 1.00 75.59 C ANISOU 343 C SER A 48 10677 8795 9249 -751 -1115 1979 C ATOM 344 O SER A 48 15.339 -34.857 80.976 1.00 73.87 O ANISOU 344 O SER A 48 10186 8821 9059 -745 -1033 1957 O ATOM 345 CB SER A 48 12.651 -33.143 81.418 1.00 75.87 C ANISOU 345 CB SER A 48 10960 8572 9297 -242 -1014 1719 C ATOM 346 OG SER A 48 11.368 -32.848 80.903 1.00 76.45 O ANISOU 346 OG SER A 48 11047 8593 9408 50 -967 1650 O ATOM 347 N PHE A 49 15.822 -32.655 81.243 1.00 77.63 N ANISOU 347 N PHE A 49 11173 8863 9460 -994 -1268 2058 N ATOM 348 CA PHE A 49 17.047 -32.865 81.997 1.00 78.08 C ANISOU 348 CA PHE A 49 11176 8993 9499 -1264 -1357 2102 C ATOM 349 C PHE A 49 16.717 -32.896 83.479 1.00 78.07 C ANISOU 349 C PHE A 49 11383 8830 9450 -1193 -1384 1936 C ATOM 350 O PHE A 49 15.925 -32.086 83.954 1.00 79.25 O ANISOU 350 O PHE A 49 11856 8705 9552 -1063 -1404 1830 O ATOM 351 CB PHE A 49 18.043 -31.738 81.734 1.00 80.80 C ANISOU 351 CB PHE A 49 11688 9209 9803 -1609 -1529 2270 C ATOM 352 CG PHE A 49 18.396 -31.559 80.289 1.00 81.91 C ANISOU 352 CG PHE A 49 11675 9498 9950 -1724 -1497 2450 C ATOM 353 CD1 PHE A 49 18.205 -30.329 79.667 1.00 84.96 C ANISOU 353 CD1 PHE A 49 12366 9631 10283 -1821 -1595 2558 C ATOM 354 CD2 PHE A 49 18.924 -32.614 79.549 1.00 80.81 C ANISOU 354 CD2 PHE A 49 11118 9738 9848 -1732 -1372 2511 C ATOM 355 CE1 PHE A 49 18.534 -30.149 78.327 1.00 86.08 C ANISOU 355 CE1 PHE A 49 12399 9912 10396 -1955 -1563 2741 C ATOM 356 CE2 PHE A 49 19.255 -32.450 78.211 1.00 82.02 C ANISOU 356 CE2 PHE A 49 11144 10049 9972 -1843 -1320 2670 C ATOM 357 CZ PHE A 49 19.060 -31.215 77.595 1.00 84.74 C ANISOU 357 CZ PHE A 49 11795 10155 10249 -1970 -1412 2794 C ATOM 358 N THR A 50 17.319 -33.830 84.207 1.00 77.08 N ANISOU 358 N THR A 50 11088 8873 9324 -1263 -1386 1910 N ATOM 359 CA THR A 50 17.153 -33.884 85.659 1.00 77.43 C ANISOU 359 CA THR A 50 11355 8778 9286 -1246 -1427 1773 C ATOM 360 C THR A 50 18.384 -33.333 86.382 1.00 79.50 C ANISOU 360 C THR A 50 11760 8952 9494 -1573 -1652 1845 C ATOM 361 O THR A 50 18.319 -33.025 87.572 1.00 80.87 O ANISOU 361 O THR A 50 12225 8939 9564 -1608 -1734 1740 O ATOM 362 CB THR A 50 16.803 -35.314 86.170 1.00 75.46 C ANISOU 362 CB THR A 50 10901 8727 9042 -1088 -1301 1681 C ATOM 363 OG1 THR A 50 17.891 -36.211 85.919 1.00 74.50 O ANISOU 363 OG1 THR A 50 10473 8855 8979 -1216 -1357 1789 O ATOM 364 CG2 THR A 50 15.541 -35.847 85.493 1.00 73.67 C ANISOU 364 CG2 THR A 50 10536 8589 8866 -805 -1097 1609 C ATOM 365 N LYS A 51 19.492 -33.210 85.649 1.00 80.11 N ANISOU 365 N LYS A 51 11626 9182 9631 -1821 -1747 2022 N ATOM 366 CA LYS A 51 20.740 -32.620 86.149 1.00 82.39 C ANISOU 366 CA LYS A 51 11988 9430 9888 -2186 -1979 2123 C ATOM 367 C LYS A 51 21.158 -31.458 85.233 1.00 84.47 C ANISOU 367 C LYS A 51 12345 9592 10156 -2433 -2064 2282 C ATOM 368 O LYS A 51 20.682 -31.379 84.101 1.00 83.76 O ANISOU 368 O LYS A 51 12167 9553 10106 -2318 -1934 2338 O ATOM 369 CB LYS A 51 21.843 -33.686 86.209 1.00 81.96 C ANISOU 369 CB LYS A 51 11516 9725 9901 -2291 -2022 2202 C ATOM 370 CG LYS A 51 21.620 -34.786 87.253 1.00 80.45 C ANISOU 370 CG LYS A 51 11298 9589 9679 -2111 -2007 2074 C ATOM 371 N PRO A 52 22.034 -30.545 85.709 1.00 87.39 N ANISOU 371 N PRO A 52 12923 9809 10473 -2797 -2296 2364 N ATOM 372 CA PRO A 52 22.467 -29.463 84.812 1.00 89.72 C ANISOU 372 CA PRO A 52 13323 10006 10761 -3084 -2383 2542 C ATOM 373 C PRO A 52 23.325 -29.969 83.648 1.00 89.56 C ANISOU 373 C PRO A 52 12807 10399 10822 -3244 -2293 2731 C ATOM 374 O PRO A 52 23.218 -29.461 82.527 1.00 90.23 O ANISOU 374 O PRO A 52 12902 10481 10899 -3313 -2230 2857 O ATOM 375 CB PRO A 52 23.303 -28.552 85.726 1.00 93.04 C ANISOU 375 CB PRO A 52 14046 10203 11103 -3478 -2671 2581 C ATOM 376 CG PRO A 52 22.915 -28.918 87.114 1.00 92.39 C ANISOU 376 CG PRO A 52 14166 9986 10953 -3301 -2718 2376 C ATOM 377 CD PRO A 52 22.591 -30.379 87.063 1.00 89.15 C ANISOU 377 CD PRO A 52 13347 9907 10619 -2980 -2507 2303 C ATOM 378 N TRP A 53 24.146 -30.980 83.918 1.00 88.85 N ANISOU 378 N TRP A 53 12299 10663 10798 -3277 -2286 2743 N ATOM 379 CA TRP A 53 25.086 -31.523 82.935 1.00 89.19 C ANISOU 379 CA TRP A 53 11833 11143 10914 -3409 -2195 2896 C ATOM 380 C TRP A 53 24.498 -32.622 82.039 1.00 86.16 C ANISOU 380 C TRP A 53 11150 11005 10582 -3036 -1929 2840 C ATOM 381 O TRP A 53 25.237 -33.297 81.320 1.00 86.39 O ANISOU 381 O TRP A 53 10741 11420 10664 -3062 -1828 2919 O ATOM 382 CB TRP A 53 26.335 -32.041 83.649 1.00 90.62 C ANISOU 382 CB TRP A 53 11691 11592 11148 -3607 -2345 2933 C ATOM 383 CG TRP A 53 26.020 -32.909 84.828 1.00 88.89 C ANISOU 383 CG TRP A 53 11517 11322 10935 -3347 -2394 2759 C ATOM 384 CD1 TRP A 53 25.827 -32.503 86.118 1.00 89.79 C ANISOU 384 CD1 TRP A 53 12016 11133 10969 -3404 -2584 2661 C ATOM 385 CD2 TRP A 53 25.855 -34.329 84.826 1.00 86.46 C ANISOU 385 CD2 TRP A 53 10901 11255 10694 -3002 -2258 2666 C ATOM 386 NE1 TRP A 53 25.557 -33.584 86.921 1.00 87.86 N ANISOU 386 NE1 TRP A 53 11711 10945 10728 -3133 -2565 2527 N ATOM 387 CE2 TRP A 53 25.566 -34.717 86.152 1.00 85.82 C ANISOU 387 CE2 TRP A 53 11037 11004 10566 -2887 -2376 2532 C ATOM 388 CE3 TRP A 53 25.925 -35.313 83.833 1.00 85.08 C ANISOU 388 CE3 TRP A 53 10322 11408 10597 -2785 -2054 2679 C ATOM 389 CZ2 TRP A 53 25.347 -36.047 86.511 1.00 83.99 C ANISOU 389 CZ2 TRP A 53 10640 10906 10368 -2584 -2308 2432 C ATOM 390 CZ3 TRP A 53 25.704 -36.634 84.190 1.00 83.10 C ANISOU 390 CZ3 TRP A 53 9914 11272 10389 -2464 -1994 2561 C ATOM 391 CH2 TRP A 53 25.420 -36.989 85.518 1.00 82.60 C ANISOU 391 CH2 TRP A 53 10081 11021 10283 -2376 -2126 2450 C ATOM 392 N SER A 54 23.175 -32.786 82.075 1.00 83.68 N ANISOU 392 N SER A 54 11069 10478 10249 -2695 -1820 2698 N ATOM 393 CA SER A 54 22.486 -33.851 81.334 1.00 80.75 C ANISOU 393 CA SER A 54 10465 10297 9919 -2348 -1599 2625 C ATOM 394 C SER A 54 22.528 -33.669 79.815 1.00 81.17 C ANISOU 394 C SER A 54 10369 10516 9956 -2387 -1466 2755 C ATOM 395 O SER A 54 22.469 -34.648 79.066 1.00 79.52 O ANISOU 395 O SER A 54 9862 10578 9775 -2195 -1301 2732 O ATOM 396 CB SER A 54 21.038 -33.987 81.813 1.00 78.58 C ANISOU 396 CB SER A 54 10467 9765 9626 -2018 -1532 2447 C ATOM 397 OG SER A 54 20.976 -34.346 83.182 1.00 77.74 O ANISOU 397 OG SER A 54 10476 9557 9506 -1965 -1612 2321 O ATOM 398 N GLN A 55 22.633 -32.412 79.378 1.00 83.63 N ANISOU 398 N GLN A 55 10929 10645 10203 -2644 -1549 2891 N ATOM 399 CA GLN A 55 22.801 -32.049 77.962 1.00 84.95 C ANISOU 399 CA GLN A 55 11015 10948 10313 -2768 -1452 3055 C ATOM 400 C GLN A 55 24.000 -32.770 77.324 1.00 86.04 C ANISOU 400 C GLN A 55 10653 11569 10469 -2914 -1339 3154 C ATOM 401 O GLN A 55 24.092 -32.886 76.095 1.00 86.44 O ANISOU 401 O GLN A 55 10548 11835 10461 -2928 -1187 3248 O ATOM 402 CB GLN A 55 22.925 -30.520 77.835 1.00 87.85 C ANISOU 402 CB GLN A 55 11778 11003 10597 -3100 -1616 3208 C ATOM 403 CG GLN A 55 23.515 -29.991 76.525 1.00 90.11 C ANISOU 403 CG GLN A 55 11988 11456 10795 -3399 -1559 3440 C ATOM 404 CD GLN A 55 22.500 -29.844 75.407 1.00 88.91 C ANISOU 404 CD GLN A 55 12003 11207 10573 -3177 -1459 3463 C ATOM 405 OE1 GLN A 55 21.403 -29.326 75.606 1.00 88.27 O ANISOU 405 OE1 GLN A 55 12300 10753 10487 -2957 -1541 3382 O ATOM 406 NE2 GLN A 55 22.879 -30.276 74.212 1.00 89.18 N ANISOU 406 NE2 GLN A 55 11755 11588 10541 -3230 -1287 3572 N ATOM 407 N GLY A 56 24.894 -33.269 78.180 1.00 86.71 N ANISOU 407 N GLY A 56 10492 11828 10627 -3000 -1416 3123 N ATOM 408 CA GLY A 56 26.096 -33.982 77.761 1.00 88.17 C ANISOU 408 CA GLY A 56 10163 12486 10851 -3097 -1329 3191 C ATOM 409 C GLY A 56 27.122 -33.009 77.231 1.00 92.12 C ANISOU 409 C GLY A 56 10577 13131 11292 -3580 -1372 3417 C ATOM 410 O GLY A 56 27.143 -31.842 77.631 1.00 93.87 O ANISOU 410 O GLY A 56 11146 13052 11470 -3889 -1554 3510 O ATOM 411 N LYS A 57 27.980 -33.492 76.340 1.00 93.84 N ANISOU 411 N LYS A 57 10343 13813 11500 -3651 -1202 3501 N ATOM 412 CA LYS A 57 28.869 -32.617 75.589 1.00 97.91 C ANISOU 412 CA LYS A 57 10746 14527 11928 -4122 -1176 3734 C ATOM 413 C LYS A 57 28.305 -32.477 74.174 1.00 97.83 C ANISOU 413 C LYS A 57 10835 14558 11777 -4060 -962 3807 C ATOM 414 O LYS A 57 28.875 -32.990 73.211 1.00 99.26 O ANISOU 414 O LYS A 57 10639 15174 11902 -4060 -739 3856 O ATOM 415 CB LYS A 57 30.302 -33.163 75.583 1.00100.61 C ANISOU 415 CB LYS A 57 10478 15410 12338 -4283 -1124 3789 C ATOM 416 N LEU A 58 27.162 -31.796 74.069 1.00 96.45 N ANISOU 416 N LEU A 58 11176 13932 11538 -3981 -1035 3802 N ATOM 417 CA LEU A 58 26.470 -31.589 72.792 1.00 96.28 C ANISOU 417 CA LEU A 58 11331 13876 11375 -3901 -890 3871 C ATOM 418 C LEU A 58 25.920 -30.167 72.670 1.00 97.97 C ANISOU 418 C LEU A 58 12104 13628 11491 -4144 -1065 4016 C ATOM 419 O LEU A 58 25.493 -29.574 73.664 1.00 97.53 O ANISOU 419 O LEU A 58 12397 13163 11498 -4142 -1280 3956 O ATOM 420 CB LEU A 58 25.324 -32.599 72.621 1.00 92.21 C ANISOU 420 CB LEU A 58 10836 13303 10896 -3359 -782 3657 C ATOM 421 CG LEU A 58 25.587 -34.110 72.541 1.00 90.15 C ANISOU 421 CG LEU A 58 10126 13422 10706 -3030 -606 3492 C ATOM 422 CD1 LEU A 58 24.271 -34.858 72.464 1.00 86.34 C ANISOU 422 CD1 LEU A 58 9798 12759 10247 -2573 -563 3303 C ATOM 423 CD2 LEU A 58 26.461 -34.485 71.358 1.00 92.41 C ANISOU 423 CD2 LEU A 58 10035 14193 10882 -3138 -375 3586 C ATOM 424 N SER A 59 25.927 -29.630 71.449 1.00100.22 N ANISOU 424 N SER A 59 12502 13969 11607 -4338 -977 4202 N ATOM 425 CA SER A 59 25.403 -28.288 71.182 1.00102.28 C ANISOU 425 CA SER A 59 13330 13776 11756 -4554 -1155 4361 C ATOM 426 C SER A 59 23.889 -28.316 71.008 1.00 99.50 C ANISOU 426 C SER A 59 13332 13066 11407 -4093 -1199 4227 C ATOM 427 O SER A 59 23.320 -29.351 70.656 1.00 96.63 O ANISOU 427 O SER A 59 12751 12890 11074 -3697 -1040 4074 O ATOM 428 CB SER A 59 26.052 -27.696 69.932 1.00106.29 C ANISOU 428 CB SER A 59 13836 14492 12056 -4981 -1055 4641 C ATOM 429 OG SER A 59 25.438 -28.204 68.759 1.00105.44 O ANISOU 429 OG SER A 59 13701 14534 11827 -4715 -868 4630 O ATOM 430 N ASN A 60 23.250 -27.168 71.233 1.00100.81 N ANISOU 430 N ASN A 60 14045 12720 11540 -4148 -1425 4286 N ATOM 431 CA ASN A 60 21.785 -27.056 71.211 1.00 98.82 C ANISOU 431 CA ASN A 60 14131 12103 11314 -3698 -1504 4150 C ATOM 432 C ASN A 60 21.107 -27.718 70.012 1.00 97.44 C ANISOU 432 C ASN A 60 13832 12131 11059 -3412 -1340 4138 C ATOM 433 O ASN A 60 20.123 -28.442 70.174 1.00 94.17 O ANISOU 433 O ASN A 60 13347 11698 10737 -2962 -1297 3934 O ATOM 434 CB ASN A 60 21.352 -25.593 71.342 1.00101.55 C ANISOU 434 CB ASN A 60 15099 11890 11596 -3838 -1772 4263 C ATOM 435 CG ASN A 60 21.669 -25.008 72.711 1.00102.61 C ANISOU 435 CG ASN A 60 15443 11725 11820 -3986 -1965 4190 C ATOM 436 OD1 ASN A 60 22.226 -25.683 73.582 1.00101.06 O ANISOU 436 OD1 ASN A 60 14919 11748 11730 -4001 -1909 4068 O ATOM 437 ND2 ASN A 60 21.312 -23.742 72.907 1.00105.62 N ANISOU 437 ND2 ASN A 60 16404 11582 12144 -4088 -2213 4262 N ATOM 438 N GLN A 61 21.649 -27.474 68.820 1.00100.22 N ANISOU 438 N GLN A 61 14163 12691 11226 -3702 -1251 4361 N ATOM 439 CA GLN A 61 21.146 -28.078 67.584 1.00 99.68 C ANISOU 439 CA GLN A 61 13995 12845 11034 -3490 -1097 4369 C ATOM 440 C GLN A 61 21.477 -29.575 67.509 1.00 97.19 C ANISOU 440 C GLN A 61 13129 13019 10778 -3276 -841 4195 C ATOM 441 O GLN A 61 20.663 -30.382 67.047 1.00 94.91 O ANISOU 441 O GLN A 61 12759 12812 10489 -2906 -761 4056 O ATOM 442 CB GLN A 61 21.701 -27.340 66.358 1.00103.57 C ANISOU 442 CB GLN A 61 14660 13422 11271 -3903 -1068 4669 C ATOM 443 N GLN A 62 22.670 -29.935 67.977 1.00 97.97 N ANISOU 443 N GLN A 62 12863 13429 10931 -3508 -735 4201 N ATOM 444 CA GLN A 62 23.153 -31.315 67.940 1.00 96.29 C ANISOU 444 CA GLN A 62 12136 13675 10776 -3314 -509 4045 C ATOM 445 C GLN A 62 22.254 -32.231 68.761 1.00 92.35 C ANISOU 445 C GLN A 62 11579 13049 10462 -2843 -543 3770 C ATOM 446 O GLN A 62 22.060 -33.399 68.420 1.00 90.53 O ANISOU 446 O GLN A 62 11090 13065 10241 -2552 -390 3621 O ATOM 447 CB GLN A 62 24.581 -31.367 68.476 1.00 98.18 C ANISOU 447 CB GLN A 62 12015 14218 11071 -3644 -454 4107 C ATOM 448 CG GLN A 62 25.376 -32.585 68.069 1.00 97.76 C ANISOU 448 CG GLN A 62 11420 14712 11012 -3531 -195 4019 C ATOM 449 CD GLN A 62 26.853 -32.412 68.349 1.00100.50 C ANISOU 449 CD GLN A 62 11398 15408 11381 -3921 -143 4138 C ATOM 450 OE1 GLN A 62 27.247 -31.618 69.205 1.00101.26 O ANISOU 450 OE1 GLN A 62 11606 15311 11558 -4220 -337 4226 O ATOM 451 NE2 GLN A 62 27.682 -33.152 67.625 1.00102.16 N ANISOU 451 NE2 GLN A 62 11158 16144 11513 -3918 116 4133 N ATOM 452 N TRP A 63 21.714 -31.678 69.843 1.00 91.51 N ANISOU 452 N TRP A 63 11737 12550 10482 -2785 -744 3706 N ATOM 453 CA TRP A 63 20.798 -32.382 70.732 1.00 88.26 C ANISOU 453 CA TRP A 63 11320 11986 10228 -2387 -783 3464 C ATOM 454 C TRP A 63 19.379 -32.412 70.161 1.00 86.84 C ANISOU 454 C TRP A 63 11366 11611 10020 -2062 -811 3394 C ATOM 455 O TRP A 63 18.619 -33.344 70.424 1.00 84.10 O ANISOU 455 O TRP A 63 10899 11296 9761 -1725 -762 3203 O ATOM 456 CB TRP A 63 20.827 -31.719 72.114 1.00 88.45 C ANISOU 456 CB TRP A 63 11549 11692 10366 -2474 -969 3422 C ATOM 457 CG TRP A 63 19.712 -32.101 73.037 1.00 85.84 C ANISOU 457 CG TRP A 63 11330 11128 10157 -2104 -1023 3201 C ATOM 458 CD1 TRP A 63 18.646 -31.329 73.387 1.00 85.99 C ANISOU 458 CD1 TRP A 63 11726 10754 10194 -1946 -1158 3150 C ATOM 459 CD2 TRP A 63 19.558 -33.341 73.736 1.00 83.61 C ANISOU 459 CD2 TRP A 63 10783 11001 9984 -1851 -938 3005 C ATOM 460 NE1 TRP A 63 17.833 -32.010 74.260 1.00 83.82 N ANISOU 460 NE1 TRP A 63 11403 10418 10028 -1625 -1135 2932 N ATOM 461 CE2 TRP A 63 18.369 -33.249 74.490 1.00 82.32 C ANISOU 461 CE2 TRP A 63 10842 10547 9889 -1583 -1008 2850 C ATOM 462 CE3 TRP A 63 20.308 -34.524 73.795 1.00 83.21 C ANISOU 462 CE3 TRP A 63 10339 11302 9974 -1816 -814 2945 C ATOM 463 CZ2 TRP A 63 17.906 -34.298 75.296 1.00 80.36 C ANISOU 463 CZ2 TRP A 63 10446 10354 9733 -1332 -948 2658 C ATOM 464 CZ3 TRP A 63 19.847 -35.570 74.598 1.00 80.91 C ANISOU 464 CZ3 TRP A 63 9938 11023 9783 -1543 -786 2752 C ATOM 465 CH2 TRP A 63 18.658 -35.447 75.338 1.00 79.36 C ANISOU 465 CH2 TRP A 63 9979 10537 9637 -1330 -849 2620 C ATOM 466 N GLU A 64 19.034 -31.393 69.372 1.00 89.03 N ANISOU 466 N GLU A 64 11968 11689 10169 -2178 -906 3560 N ATOM 467 CA GLU A 64 17.706 -31.295 68.769 1.00 88.36 C ANISOU 467 CA GLU A 64 12101 11417 10053 -1879 -975 3518 C ATOM 468 C GLU A 64 17.391 -32.450 67.834 1.00 86.78 C ANISOU 468 C GLU A 64 11649 11534 9790 -1670 -815 3440 C ATOM 469 O GLU A 64 16.277 -32.969 67.850 1.00 84.81 O ANISOU 469 O GLU A 64 11398 11218 9609 -1336 -843 3289 O ATOM 470 CB GLU A 64 17.518 -29.959 68.042 1.00 91.64 C ANISOU 470 CB GLU A 64 12941 11554 10325 -2061 -1137 3739 C ATOM 471 CG GLU A 64 17.098 -28.815 68.954 1.00 93.42 C ANISOU 471 CG GLU A 64 13557 11304 10634 -2056 -1365 3737 C ATOM 472 CD GLU A 64 16.044 -29.231 69.968 1.00 91.86 C ANISOU 472 CD GLU A 64 13329 10953 10622 -1642 -1400 3477 C ATOM 473 OE1 GLU A 64 16.299 -29.066 71.183 1.00 91.97 O ANISOU 473 OE1 GLU A 64 13372 10831 10741 -1679 -1441 3381 O ATOM 474 OE2 GLU A 64 14.975 -29.741 69.556 1.00 90.65 O ANISOU 474 OE2 GLU A 64 13113 10834 10497 -1300 -1384 3370 O ATOM 475 N LYS A 65 18.377 -32.846 67.029 1.00 87.95 N ANISOU 475 N LYS A 65 11581 12035 9800 -1874 -646 3536 N ATOM 476 CA LYS A 65 18.240 -33.984 66.123 1.00 86.93 C ANISOU 476 CA LYS A 65 11227 12222 9581 -1691 -480 3448 C ATOM 477 C LYS A 65 17.900 -35.270 66.880 1.00 83.74 C ANISOU 477 C LYS A 65 10562 11907 9348 -1383 -418 3193 C ATOM 478 O LYS A 65 17.132 -36.095 66.387 1.00 82.47 O ANISOU 478 O LYS A 65 10355 11812 9167 -1129 -385 3070 O ATOM 479 CB LYS A 65 19.509 -34.167 65.286 1.00 89.26 C ANISOU 479 CB LYS A 65 11310 12907 9697 -1964 -279 3574 C ATOM 480 N LEU A 66 18.462 -35.425 68.079 1.00 82.74 N ANISOU 480 N LEU A 66 10293 11767 9379 -1429 -423 3123 N ATOM 481 CA LEU A 66 18.162 -36.569 68.939 1.00 79.90 C ANISOU 481 CA LEU A 66 9739 11445 9174 -1170 -391 2904 C ATOM 482 C LEU A 66 16.731 -36.499 69.456 1.00 78.12 C ANISOU 482 C LEU A 66 9706 10925 9050 -921 -515 2787 C ATOM 483 O LEU A 66 15.933 -37.400 69.195 1.00 76.68 O ANISOU 483 O LEU A 66 9452 10797 8885 -681 -482 2654 O ATOM 484 CB LEU A 66 19.146 -36.645 70.112 1.00 79.80 C ANISOU 484 CB LEU A 66 9563 11475 9281 -1303 -399 2883 C ATOM 485 CG LEU A 66 20.464 -37.428 70.001 1.00 80.93 C ANISOU 485 CG LEU A 66 9342 11994 9413 -1384 -255 2878 C ATOM 486 CD1 LEU A 66 20.214 -38.941 69.944 1.00 78.98 C ANISOU 486 CD1 LEU A 66 8896 11906 9207 -1066 -157 2680 C ATOM 487 CD2 LEU A 66 21.355 -36.960 68.834 1.00 84.02 C ANISOU 487 CD2 LEU A 66 9644 12651 9628 -1642 -134 3059 C ATOM 488 N GLN A 67 16.410 -35.419 70.172 1.00 78.68 N ANISOU 488 N GLN A 67 10021 10692 9182 -983 -658 2832 N ATOM 489 CA GLN A 67 15.077 -35.218 70.755 1.00 77.44 C ANISOU 489 CA GLN A 67 10029 10270 9123 -736 -762 2714 C ATOM 490 C GLN A 67 14.005 -35.377 69.692 1.00 77.58 C ANISOU 490 C GLN A 67 10097 10298 9080 -539 -786 2705 C ATOM 491 O GLN A 67 13.002 -36.050 69.915 1.00 76.14 O ANISOU 491 O GLN A 67 9836 10116 8979 -295 -784 2554 O ATOM 492 CB GLN A 67 14.964 -33.835 71.402 1.00 78.88 C ANISOU 492 CB GLN A 67 10526 10112 9333 -830 -916 2783 C ATOM 493 CG GLN A 67 13.913 -33.731 72.504 1.00 77.56 C ANISOU 493 CG GLN A 67 10463 9713 9292 -584 -978 2613 C ATOM 494 CD GLN A 67 13.910 -32.367 73.191 1.00 79.43 C ANISOU 494 CD GLN A 67 11046 9597 9538 -664 -1130 2658 C ATOM 495 OE1 GLN A 67 13.706 -31.338 72.546 1.00 81.26 O ANISOU 495 OE1 GLN A 67 11547 9628 9699 -704 -1254 2785 O ATOM 496 NE2 GLN A 67 14.134 -32.358 74.505 1.00 78.35 N ANISOU 496 NE2 GLN A 67 10940 9361 9470 -688 -1136 2551 N ATOM 497 N HIS A 68 14.240 -34.772 68.529 1.00 79.70 N ANISOU 497 N HIS A 68 10498 10591 9192 -671 -816 2877 N ATOM 498 CA HIS A 68 13.304 -34.840 67.411 1.00 80.16 C ANISOU 498 CA HIS A 68 10637 10662 9159 -512 -874 2896 C ATOM 499 C HIS A 68 13.137 -36.258 66.875 1.00 78.50 C ANISOU 499 C HIS A 68 10174 10735 8917 -380 -750 2768 C ATOM 500 O HIS A 68 12.017 -36.667 66.569 1.00 77.94 O ANISOU 500 O HIS A 68 10096 10646 8872 -163 -816 2677 O ATOM 501 CB HIS A 68 13.731 -33.908 66.276 1.00 83.05 C ANISOU 501 CB HIS A 68 11231 11001 9324 -725 -930 3129 C ATOM 502 CG HIS A 68 12.705 -33.768 65.196 1.00 84.31 C ANISOU 502 CG HIS A 68 11544 11111 9380 -561 -1050 3170 C ATOM 503 ND1 HIS A 68 12.406 -34.787 64.317 1.00 83.64 N ANISOU 503 ND1 HIS A 68 11307 11274 9200 -453 -977 3101 N ATOM 504 CD2 HIS A 68 11.907 -32.728 64.855 1.00 86.39 C ANISOU 504 CD2 HIS A 68 12113 11096 9616 -476 -1264 3271 C ATOM 505 CE1 HIS A 68 11.467 -34.380 63.481 1.00 85.55 C ANISOU 505 CE1 HIS A 68 11741 11408 9357 -329 -1146 3164 C ATOM 506 NE2 HIS A 68 11.149 -33.134 63.785 1.00 87.06 N ANISOU 506 NE2 HIS A 68 12203 11283 9594 -327 -1324 3271 N ATOM 507 N MET A 69 14.242 -36.994 66.752 1.00 77.98 N ANISOU 507 N MET A 69 9905 10928 8795 -505 -584 2759 N ATOM 508 CA MET A 69 14.185 -38.354 66.223 1.00 76.77 C ANISOU 508 CA MET A 69 9557 11018 8594 -372 -471 2626 C ATOM 509 C MET A 69 13.440 -39.239 67.207 1.00 73.99 C ANISOU 509 C MET A 69 9088 10600 8424 -167 -490 2428 C ATOM 510 O MET A 69 12.609 -40.051 66.811 1.00 73.15 O ANISOU 510 O MET A 69 8942 10540 8310 -6 -508 2318 O ATOM 511 CB MET A 69 15.589 -38.904 65.912 1.00 77.78 C ANISOU 511 CB MET A 69 9487 11439 8626 -512 -285 2647 C ATOM 512 CG MET A 69 16.204 -39.825 66.976 1.00 77.03 C ANISOU 512 CG MET A 69 9156 11431 8682 -453 -206 2506 C ATOM 513 SD MET A 69 16.131 -41.617 66.677 1.00 76.68 S ANISOU 513 SD MET A 69 8928 11584 8622 -213 -100 2290 S ATOM 514 CE MET A 69 14.889 -41.776 65.388 1.00 77.19 C ANISOU 514 CE MET A 69 9170 11623 8537 -94 -167 2270 C ATOM 515 N PHE A 70 13.739 -39.047 68.491 1.00 72.77 N ANISOU 515 N PHE A 70 8900 10334 8416 -204 -494 2393 N ATOM 516 CA PHE A 70 13.102 -39.779 69.570 1.00 70.51 C ANISOU 516 CA PHE A 70 8532 9977 8283 -55 -502 2226 C ATOM 517 C PHE A 70 11.619 -39.449 69.646 1.00 70.02 C ANISOU 517 C PHE A 70 8569 9752 8285 109 -610 2174 C ATOM 518 O PHE A 70 10.804 -40.332 69.894 1.00 68.90 O ANISOU 518 O PHE A 70 8329 9642 8207 243 -603 2041 O ATOM 519 CB PHE A 70 13.784 -39.466 70.900 1.00 70.16 C ANISOU 519 CB PHE A 70 8478 9837 8341 -155 -499 2222 C ATOM 520 CG PHE A 70 14.965 -40.360 71.214 1.00 70.41 C ANISOU 520 CG PHE A 70 8315 10059 8380 -217 -404 2187 C ATOM 521 CD1 PHE A 70 14.790 -41.733 71.418 1.00 69.49 C ANISOU 521 CD1 PHE A 70 8069 10034 8300 -73 -354 2042 C ATOM 522 CD2 PHE A 70 16.244 -39.825 71.347 1.00 71.71 C ANISOU 522 CD2 PHE A 70 8427 10300 8519 -421 -385 2300 C ATOM 523 CE1 PHE A 70 15.877 -42.563 71.725 1.00 69.00 C ANISOU 523 CE1 PHE A 70 7840 10124 8251 -83 -293 2003 C ATOM 524 CE2 PHE A 70 17.334 -40.645 71.656 1.00 71.68 C ANISOU 524 CE2 PHE A 70 8203 10493 8538 -444 -314 2262 C ATOM 525 CZ PHE A 70 17.148 -42.018 71.843 1.00 70.38 C ANISOU 525 CZ PHE A 70 7924 10405 8414 -250 -272 2109 C ATOM 526 N GLN A 71 11.278 -38.180 69.422 1.00 71.25 N ANISOU 526 N GLN A 71 8916 9735 8421 96 -719 2283 N ATOM 527 CA GLN A 71 9.884 -37.729 69.372 1.00 71.48 C ANISOU 527 CA GLN A 71 9025 9624 8511 291 -840 2243 C ATOM 528 C GLN A 71 9.107 -38.510 68.320 1.00 71.26 C ANISOU 528 C GLN A 71 8904 9748 8423 402 -870 2202 C ATOM 529 O GLN A 71 8.006 -38.996 68.587 1.00 70.68 O ANISOU 529 O GLN A 71 8723 9688 8444 558 -905 2082 O ATOM 530 CB GLN A 71 9.806 -36.226 69.093 1.00 73.57 C ANISOU 530 CB GLN A 71 9554 9663 8735 268 -977 2387 C ATOM 531 CG GLN A 71 10.028 -35.366 70.323 1.00 74.44 C ANISOU 531 CG GLN A 71 9803 9544 8937 238 -1003 2373 C ATOM 532 CD GLN A 71 10.234 -33.885 70.013 1.00 78.40 C ANISOU 532 CD GLN A 71 10627 9789 9373 157 -1149 2536 C ATOM 533 OE1 GLN A 71 10.328 -33.471 68.852 1.00 80.36 O ANISOU 533 OE1 GLN A 71 11000 10042 9493 89 -1225 2689 O ATOM 534 NE2 GLN A 71 10.311 -33.078 71.066 1.00 79.44 N ANISOU 534 NE2 GLN A 71 10931 9677 9574 153 -1199 2506 N ATOM 535 N VAL A 72 9.713 -38.630 67.136 1.00 71.90 N ANISOU 535 N VAL A 72 9027 9959 8333 299 -853 2302 N ATOM 536 CA VAL A 72 9.199 -39.428 66.020 1.00 71.89 C ANISOU 536 CA VAL A 72 8978 10114 8224 366 -881 2265 C ATOM 537 C VAL A 72 9.029 -40.883 66.443 1.00 69.87 C ANISOU 537 C VAL A 72 8526 9987 8036 422 -793 2086 C ATOM 538 O VAL A 72 8.079 -41.548 66.028 1.00 69.91 O ANISOU 538 O VAL A 72 8475 10046 8041 518 -865 2002 O ATOM 539 CB VAL A 72 10.153 -39.340 64.782 1.00 73.45 C ANISOU 539 CB VAL A 72 9268 10453 8185 216 -824 2395 C ATOM 540 CG1 VAL A 72 9.901 -40.465 63.781 1.00 73.63 C ANISOU 540 CG1 VAL A 72 9236 10667 8073 272 -803 2309 C ATOM 541 CG2 VAL A 72 10.036 -37.983 64.097 1.00 75.91 C ANISOU 541 CG2 VAL A 72 9828 10626 8389 155 -958 2591 C ATOM 542 N TYR A 73 9.947 -41.358 67.284 1.00 68.23 N ANISOU 542 N TYR A 73 8230 9812 7883 350 -662 2037 N ATOM 543 CA TYR A 73 9.961 -42.747 67.724 1.00 66.47 C ANISOU 543 CA TYR A 73 7870 9675 7709 390 -589 1885 C ATOM 544 C TYR A 73 8.811 -43.100 68.671 1.00 65.44 C ANISOU 544 C TYR A 73 7671 9457 7735 475 -636 1772 C ATOM 545 O TYR A 73 8.065 -44.045 68.413 1.00 65.42 O ANISOU 545 O TYR A 73 7608 9514 7735 521 -669 1675 O ATOM 546 CB TYR A 73 11.305 -43.106 68.355 1.00 65.66 C ANISOU 546 CB TYR A 73 7698 9629 7619 308 -465 1877 C ATOM 547 CG TYR A 73 11.249 -44.346 69.205 1.00 63.94 C ANISOU 547 CG TYR A 73 7390 9414 7492 362 -428 1732 C ATOM 548 CD1 TYR A 73 11.081 -45.604 68.624 1.00 64.01 C ANISOU 548 CD1 TYR A 73 7375 9509 7435 429 -418 1624 C ATOM 549 CD2 TYR A 73 11.350 -44.265 70.587 1.00 62.62 C ANISOU 549 CD2 TYR A 73 7200 9139 7453 337 -417 1705 C ATOM 550 CE1 TYR A 73 11.022 -46.752 69.398 1.00 63.15 C ANISOU 550 CE1 TYR A 73 7234 9363 7399 463 -408 1504 C ATOM 551 CE2 TYR A 73 11.296 -45.407 71.374 1.00 62.12 C ANISOU 551 CE2 TYR A 73 7093 9059 7450 367 -398 1591 C ATOM 552 CZ TYR A 73 11.133 -46.650 70.774 1.00 62.35 C ANISOU 552 CZ TYR A 73 7109 9158 7422 427 -398 1498 C ATOM 553 OH TYR A 73 11.076 -47.789 71.548 1.00 61.54 O ANISOU 553 OH TYR A 73 7011 9002 7369 443 -401 1399 O ATOM 554 N ARG A 74 8.678 -42.357 69.767 1.00 64.79 N ANISOU 554 N ARG A 74 7605 9242 7770 478 -634 1782 N ATOM 555 CA ARG A 74 7.592 -42.591 70.713 1.00 64.06 C ANISOU 555 CA ARG A 74 7436 9097 7807 554 -643 1676 C ATOM 556 C ARG A 74 6.286 -42.775 69.941 1.00 65.01 C ANISOU 556 C ARG A 74 7487 9281 7931 650 -746 1642 C ATOM 557 O ARG A 74 5.636 -43.814 70.042 1.00 64.73 O ANISOU 557 O ARG A 74 7342 9326 7925 644 -743 1544 O ATOM 558 CB ARG A 74 7.483 -41.434 71.709 1.00 64.26 C ANISOU 558 CB ARG A 74 7536 8963 7916 585 -645 1699 C ATOM 559 CG ARG A 74 6.578 -41.711 72.902 1.00 63.71 C ANISOU 559 CG ARG A 74 7382 8868 7956 646 -596 1577 C ATOM 560 CD ARG A 74 6.725 -40.661 73.990 1.00 63.81 C ANISOU 560 CD ARG A 74 7512 8716 8016 671 -573 1576 C ATOM 561 NE ARG A 74 6.148 -39.381 73.593 1.00 66.00 N ANISOU 561 NE ARG A 74 7888 8878 8312 809 -672 1623 N ATOM 562 CZ ARG A 74 6.073 -38.309 74.375 1.00 67.28 C ANISOU 562 CZ ARG A 74 8196 8859 8507 879 -684 1608 C ATOM 563 NH1 ARG A 74 6.536 -38.344 75.617 1.00 66.98 N ANISOU 563 NH1 ARG A 74 8219 8751 8478 805 -597 1549 N ATOM 564 NH2 ARG A 74 5.528 -37.194 73.911 1.00 69.60 N ANISOU 564 NH2 ARG A 74 8606 9024 8816 1035 -802 1650 N ATOM 565 N VAL A 75 5.945 -41.765 69.143 1.00 66.39 N ANISOU 565 N VAL A 75 7743 9415 8067 722 -857 1735 N ATOM 566 CA VAL A 75 4.756 -41.762 68.296 1.00 67.70 C ANISOU 566 CA VAL A 75 7850 9644 8230 827 -1001 1727 C ATOM 567 C VAL A 75 4.657 -43.004 67.413 1.00 67.69 C ANISOU 567 C VAL A 75 7798 9792 8129 763 -1027 1675 C ATOM 568 O VAL A 75 3.593 -43.617 67.312 1.00 68.26 O ANISOU 568 O VAL A 75 7738 9946 8253 792 -1102 1596 O ATOM 569 CB VAL A 75 4.713 -40.473 67.437 1.00 69.36 C ANISOU 569 CB VAL A 75 8225 9760 8369 900 -1140 1869 C ATOM 570 CG1 VAL A 75 4.004 -40.697 66.112 1.00 71.03 C ANISOU 570 CG1 VAL A 75 8435 10071 8481 948 -1304 1899 C ATOM 571 CG2 VAL A 75 4.055 -39.350 68.216 1.00 70.43 C ANISOU 571 CG2 VAL A 75 8381 9741 8639 1056 -1194 1866 C ATOM 572 N SER A 76 5.770 -43.376 66.790 1.00 67.45 N ANISOU 572 N SER A 76 7872 9805 7952 673 -962 1713 N ATOM 573 CA SER A 76 5.785 -44.494 65.859 1.00 68.01 C ANISOU 573 CA SER A 76 7955 9994 7892 634 -985 1652 C ATOM 574 C SER A 76 5.683 -45.823 66.583 1.00 67.04 C ANISOU 574 C SER A 76 7742 9890 7839 589 -920 1510 C ATOM 575 O SER A 76 4.967 -46.725 66.144 1.00 67.50 O ANISOU 575 O SER A 76 7774 10004 7869 568 -1005 1428 O ATOM 576 CB SER A 76 7.042 -44.457 64.998 1.00 68.38 C ANISOU 576 CB SER A 76 8133 10102 7746 578 -904 1720 C ATOM 577 OG SER A 76 7.086 -43.261 64.243 1.00 70.01 O ANISOU 577 OG SER A 76 8463 10283 7856 579 -979 1872 O ATOM 578 N PHE A 77 6.400 -45.924 67.698 1.00 66.04 N ANISOU 578 N PHE A 77 7593 9704 7796 557 -792 1491 N ATOM 579 CA PHE A 77 6.468 -47.146 68.493 1.00 65.48 C ANISOU 579 CA PHE A 77 7485 9617 7779 507 -734 1379 C ATOM 580 C PHE A 77 5.082 -47.626 68.902 1.00 66.03 C ANISOU 580 C PHE A 77 7448 9695 7945 475 -805 1307 C ATOM 581 O PHE A 77 4.745 -48.795 68.723 1.00 66.46 O ANISOU 581 O PHE A 77 7516 9767 7968 407 -847 1223 O ATOM 582 CB PHE A 77 7.337 -46.919 69.729 1.00 64.22 C ANISOU 582 CB PHE A 77 7323 9381 7698 483 -619 1395 C ATOM 583 CG PHE A 77 7.360 -48.080 70.678 1.00 63.79 C ANISOU 583 CG PHE A 77 7263 9279 7695 430 -581 1301 C ATOM 584 CD1 PHE A 77 6.523 -48.101 71.791 1.00 63.76 C ANISOU 584 CD1 PHE A 77 7199 9227 7799 383 -565 1268 C ATOM 585 CD2 PHE A 77 8.225 -49.148 70.467 1.00 63.76 C ANISOU 585 CD2 PHE A 77 7330 9276 7619 436 -560 1245 C ATOM 586 CE1 PHE A 77 6.542 -49.168 72.676 1.00 63.41 C ANISOU 586 CE1 PHE A 77 7189 9127 7777 302 -537 1204 C ATOM 587 CE2 PHE A 77 8.257 -50.217 71.348 1.00 63.53 C ANISOU 587 CE2 PHE A 77 7344 9164 7629 392 -556 1173 C ATOM 588 CZ PHE A 77 7.412 -50.228 72.455 1.00 63.39 C ANISOU 588 CZ PHE A 77 7291 9089 7706 304 -549 1163 C ATOM 589 N THR A 78 4.290 -46.707 69.450 1.00 66.49 N ANISOU 589 N THR A 78 7403 9744 8117 522 -818 1337 N ATOM 590 CA THR A 78 2.933 -46.997 69.881 1.00 67.44 C ANISOU 590 CA THR A 78 7359 9927 8340 498 -860 1275 C ATOM 591 C THR A 78 2.154 -47.584 68.718 1.00 68.95 C ANISOU 591 C THR A 78 7512 10218 8468 467 -1018 1251 C ATOM 592 O THR A 78 1.695 -48.727 68.785 1.00 69.30 O ANISOU 592 O THR A 78 7526 10298 8508 338 -1049 1175 O ATOM 593 CB THR A 78 2.228 -45.726 70.394 1.00 68.16 C ANISOU 593 CB THR A 78 7339 10014 8544 625 -857 1306 C ATOM 594 OG1 THR A 78 3.098 -45.025 71.288 1.00 67.28 O ANISOU 594 OG1 THR A 78 7329 9782 8454 651 -741 1337 O ATOM 595 CG2 THR A 78 0.954 -46.075 71.133 1.00 69.52 C ANISOU 595 CG2 THR A 78 7293 10291 8831 595 -834 1226 C ATOM 596 N ARG A 79 2.054 -46.811 67.638 1.00 70.10 N ANISOU 596 N ARG A 79 7696 10391 8546 566 -1135 1321 N ATOM 597 CA ARG A 79 1.252 -47.190 66.480 1.00 72.04 C ANISOU 597 CA ARG A 79 7919 10735 8719 548 -1323 1309 C ATOM 598 C ARG A 79 1.700 -48.508 65.852 1.00 72.14 C ANISOU 598 C ARG A 79 8078 10748 8585 427 -1345 1236 C ATOM 599 O ARG A 79 0.879 -49.235 65.302 1.00 73.54 O ANISOU 599 O ARG A 79 8220 10991 8729 341 -1491 1181 O ATOM 600 CB ARG A 79 1.237 -46.076 65.436 1.00 73.17 C ANISOU 600 CB ARG A 79 8141 10881 8780 677 -1451 1418 C ATOM 601 CG ARG A 79 -0.017 -46.075 64.586 1.00 75.69 C ANISOU 601 CG ARG A 79 8350 11312 9098 706 -1686 1418 C ATOM 602 CD ARG A 79 0.195 -45.376 63.258 1.00 77.71 C ANISOU 602 CD ARG A 79 8789 11557 9179 783 -1839 1526 C ATOM 603 NE ARG A 79 1.136 -46.101 62.402 1.00 77.90 N ANISOU 603 NE ARG A 79 9044 11582 8974 682 -1798 1511 N ATOM 604 CZ ARG A 79 1.230 -45.948 61.083 1.00 79.27 C ANISOU 604 CZ ARG A 79 9398 11789 8932 688 -1935 1570 C ATOM 605 NH1 ARG A 79 0.432 -45.103 60.442 1.00 80.75 N ANISOU 605 NH1 ARG A 79 9577 11996 9109 782 -2155 1665 N ATOM 606 NH2 ARG A 79 2.121 -46.653 60.401 1.00 79.03 N ANISOU 606 NH2 ARG A 79 9568 11776 8684 614 -1854 1530 N ATOM 607 N ASP A 80 2.994 -48.814 65.952 1.00 71.21 N ANISOU 607 N ASP A 80 8120 10555 8380 427 -1209 1228 N ATOM 608 CA ASP A 80 3.547 -50.070 65.423 1.00 71.70 C ANISOU 608 CA ASP A 80 8348 10595 8301 367 -1211 1136 C ATOM 609 C ASP A 80 3.133 -51.305 66.222 1.00 71.70 C ANISOU 609 C ASP A 80 8332 10534 8375 236 -1215 1034 C ATOM 610 O ASP A 80 2.715 -52.310 65.637 1.00 73.01 O ANISOU 610 O ASP A 80 8594 10691 8456 145 -1335 952 O ATOM 611 CB ASP A 80 5.073 -49.999 65.281 1.00 70.85 C ANISOU 611 CB ASP A 80 8374 10459 8087 441 -1061 1152 C ATOM 612 CG ASP A 80 5.521 -49.698 63.852 1.00 72.81 C ANISOU 612 CG ASP A 80 8757 10787 8119 497 -1093 1188 C ATOM 613 OD1 ASP A 80 4.675 -49.728 62.929 1.00 74.72 O ANISOU 613 OD1 ASP A 80 9038 11079 8272 476 -1258 1185 O ATOM 614 OD2 ASP A 80 6.730 -49.441 63.644 1.00 73.26 O ANISOU 614 OD2 ASP A 80 8878 10876 8083 548 -954 1222 O ATOM 615 N ILE A 81 3.246 -51.234 67.548 1.00 70.52 N ANISOU 615 N ILE A 81 8099 10331 8365 206 -1095 1043 N ATOM 616 CA ILE A 81 2.773 -52.324 68.399 1.00 70.90 C ANISOU 616 CA ILE A 81 8146 10318 8474 48 -1097 974 C ATOM 617 C ILE A 81 1.252 -52.460 68.262 1.00 72.80 C ANISOU 617 C ILE A 81 8211 10669 8780 -86 -1225 962 C ATOM 618 O ILE A 81 0.740 -53.568 68.074 1.00 74.23 O ANISOU 618 O ILE A 81 8457 10825 8921 -256 -1330 898 O ATOM 619 CB ILE A 81 3.215 -52.169 69.882 1.00 69.45 C ANISOU 619 CB ILE A 81 7930 10062 8397 34 -941 997 C ATOM 620 CG1 ILE A 81 4.658 -52.628 70.070 1.00 68.38 C ANISOU 620 CG1 ILE A 81 7979 9808 8194 109 -868 979 C ATOM 621 CG2 ILE A 81 2.388 -53.064 70.794 1.00 70.38 C ANISOU 621 CG2 ILE A 81 8013 10152 8575 -168 -946 958 C ATOM 622 CD1 ILE A 81 5.697 -51.674 69.580 1.00 68.41 C ANISOU 622 CD1 ILE A 81 7987 9854 8153 267 -801 1039 C ATOM 623 N GLN A 82 0.544 -51.331 68.320 1.00 73.18 N ANISOU 623 N GLN A 82 8040 10838 8927 -5 -1231 1023 N ATOM 624 CA GLN A 82 -0.906 -51.313 68.135 1.00 75.27 C ANISOU 624 CA GLN A 82 8068 11260 9272 -90 -1359 1015 C ATOM 625 C GLN A 82 -1.334 -52.061 66.873 1.00 77.19 C ANISOU 625 C GLN A 82 8396 11536 9395 -187 -1578 975 C ATOM 626 O GLN A 82 -2.378 -52.715 66.872 1.00 79.17 O ANISOU 626 O GLN A 82 8514 11879 9688 -377 -1694 940 O ATOM 627 CB GLN A 82 -1.435 -49.877 68.113 1.00 75.78 C ANISOU 627 CB GLN A 82 7925 11430 9438 102 -1367 1079 C ATOM 628 CG GLN A 82 -1.424 -49.190 69.478 1.00 74.97 C ANISOU 628 CG GLN A 82 7701 11318 9466 170 -1173 1089 C ATOM 629 CD GLN A 82 -1.787 -47.708 69.420 1.00 75.59 C ANISOU 629 CD GLN A 82 7650 11441 9629 410 -1190 1140 C ATOM 630 OE1 GLN A 82 -1.664 -47.055 68.379 1.00 75.86 O ANISOU 630 OE1 GLN A 82 7759 11459 9604 542 -1328 1200 O ATOM 631 NE2 GLN A 82 -2.230 -47.169 70.553 1.00 75.95 N ANISOU 631 NE2 GLN A 82 7533 11529 9797 473 -1051 1115 N ATOM 632 N GLU A 83 -0.524 -51.968 65.812 1.00 76.95 N ANISOU 632 N GLU A 83 8591 11444 9204 -77 -1631 981 N ATOM 633 CA GLU A 83 -0.744 -52.744 64.581 1.00 78.83 C ANISOU 633 CA GLU A 83 8991 11684 9275 -159 -1829 924 C ATOM 634 C GLU A 83 -0.333 -54.205 64.735 1.00 79.06 C ANISOU 634 C GLU A 83 9256 11565 9217 -312 -1826 817 C ATOM 635 O GLU A 83 -1.064 -55.106 64.330 1.00 80.94 O ANISOU 635 O GLU A 83 9546 11800 9406 -501 -2002 754 O ATOM 636 CB GLU A 83 -0.005 -52.135 63.386 1.00 78.74 C ANISOU 636 CB GLU A 83 9163 11673 9082 10 -1863 962 C ATOM 637 CG GLU A 83 -0.544 -50.796 62.900 1.00 79.91 C ANISOU 637 CG GLU A 83 9161 11934 9267 143 -1958 1074 C ATOM 638 CD GLU A 83 -2.052 -50.774 62.745 1.00 82.59 C ANISOU 638 CD GLU A 83 9253 12415 9714 65 -2177 1076 C ATOM 639 OE1 GLU A 83 -2.592 -51.602 61.977 1.00 84.82 O ANISOU 639 OE1 GLU A 83 9602 12733 9891 -78 -2375 1016 O ATOM 640 OE2 GLU A 83 -2.694 -49.918 63.392 1.00 82.77 O ANISOU 640 OE2 GLU A 83 9007 12519 9922 153 -2155 1131 O ATOM 641 N LEU A 84 0.842 -54.433 65.317 1.00 77.42 N ANISOU 641 N LEU A 84 9203 11223 8991 -228 -1648 798 N ATOM 642 CA LEU A 84 1.341 -55.784 65.540 1.00 77.97 C ANISOU 642 CA LEU A 84 9526 11114 8984 -318 -1650 696 C ATOM 643 C LEU A 84 0.363 -56.639 66.348 1.00 79.42 C ANISOU 643 C LEU A 84 9652 11258 9266 -593 -1721 677 C ATOM 644 O LEU A 84 0.284 -57.853 66.149 1.00 81.00 O ANISOU 644 O LEU A 84 10088 11313 9377 -743 -1839 591 O ATOM 645 CB LEU A 84 2.713 -55.745 66.216 1.00 75.88 C ANISOU 645 CB LEU A 84 9364 10741 8725 -159 -1453 697 C ATOM 646 CG LEU A 84 3.912 -55.419 65.319 1.00 75.43 C ANISOU 646 CG LEU A 84 9442 10701 8516 65 -1380 679 C ATOM 647 CD1 LEU A 84 5.124 -55.044 66.151 1.00 73.76 C ANISOU 647 CD1 LEU A 84 9201 10455 8368 203 -1186 719 C ATOM 648 CD2 LEU A 84 4.251 -56.568 64.377 1.00 76.93 C ANISOU 648 CD2 LEU A 84 9930 10792 8507 91 -1476 539 C ATOM 649 N VAL A 85 -0.375 -55.994 67.252 1.00 79.35 N ANISOU 649 N VAL A 85 9344 11378 9429 -664 -1645 754 N ATOM 650 CA VAL A 85 -1.429 -56.645 68.034 1.00 81.18 C ANISOU 650 CA VAL A 85 9449 11644 9752 -956 -1682 756 C ATOM 651 C VAL A 85 -2.548 -57.133 67.109 1.00 84.37 C ANISOU 651 C VAL A 85 9795 12148 10115 -1157 -1926 724 C ATOM 652 O VAL A 85 -3.013 -58.275 67.223 1.00 86.26 O ANISOU 652 O VAL A 85 10158 12299 10316 -1441 -2040 683 O ATOM 653 CB VAL A 85 -1.997 -55.689 69.117 1.00 80.44 C ANISOU 653 CB VAL A 85 9010 11721 9833 -942 -1518 832 C ATOM 654 CG1 VAL A 85 -3.345 -56.175 69.642 1.00 82.79 C ANISOU 654 CG1 VAL A 85 9073 12167 10216 -1249 -1561 840 C ATOM 655 CG2 VAL A 85 -1.013 -55.537 70.255 1.00 78.20 C ANISOU 655 CG2 VAL A 85 8833 11306 9574 -851 -1309 855 C ATOM 656 N LYS A 86 -2.957 -56.260 66.187 1.00 85.26 N ANISOU 656 N LYS A 86 9741 12428 10225 -1019 -2028 751 N ATOM 657 CA LYS A 86 -4.005 -56.566 65.216 1.00 88.44 C ANISOU 657 CA LYS A 86 10066 12951 10585 -1180 -2295 729 C ATOM 658 C LYS A 86 -3.573 -57.689 64.280 1.00 90.05 C ANISOU 658 C LYS A 86 10683 12959 10574 -1270 -2464 628 C ATOM 659 O LYS A 86 -4.412 -58.425 63.759 1.00 92.84 O ANISOU 659 O LYS A 86 11065 13333 10876 -1523 -2698 587 O ATOM 660 CB LYS A 86 -4.341 -55.330 64.378 1.00 88.63 C ANISOU 660 CB LYS A 86 9892 13159 10624 -957 -2385 788 C ATOM 661 CG LYS A 86 -4.693 -54.077 65.160 1.00 87.29 C ANISOU 661 CG LYS A 86 9365 13152 10650 -788 -2235 871 C ATOM 662 CD LYS A 86 -4.853 -52.895 64.216 1.00 86.83 C ANISOU 662 CD LYS A 86 9220 13199 10573 -538 -2358 933 C ATOM 663 CE LYS A 86 -5.423 -51.687 64.931 1.00 86.59 C ANISOU 663 CE LYS A 86 8834 13322 10744 -360 -2263 998 C ATOM 664 NZ LYS A 86 -5.869 -50.641 63.977 1.00 87.29 N ANISOU 664 NZ LYS A 86 8824 13514 10828 -144 -2459 1063 N ATOM 665 N MET A 87 -2.262 -57.808 64.071 1.00 88.86 N ANISOU 665 N MET A 87 10844 12625 10294 -1059 -2349 580 N ATOM 666 CA MET A 87 -1.698 -58.772 63.129 1.00 90.65 C ANISOU 666 CA MET A 87 11485 12664 10293 -1054 -2474 459 C ATOM 667 C MET A 87 -1.852 -60.196 63.641 1.00 92.45 C ANISOU 667 C MET A 87 11955 12670 10500 -1317 -2556 380 C ATOM 668 O MET A 87 -2.029 -61.125 62.855 1.00 94.91 O ANISOU 668 O MET A 87 12562 12849 10649 -1445 -2764 276 O ATOM 669 CB MET A 87 -0.224 -58.465 62.853 1.00 88.77 C ANISOU 669 CB MET A 87 11453 12336 9938 -732 -2291 427 C ATOM 670 CG MET A 87 0.186 -58.687 61.399 1.00 90.73 C ANISOU 670 CG MET A 87 11990 12560 9924 -615 -2404 332 C ATOM 671 SD MET A 87 1.949 -58.450 61.090 1.00 89.55 S ANISOU 671 SD MET A 87 12045 12355 9624 -261 -2153 283 S ATOM 672 CE MET A 87 2.596 -59.998 61.725 1.00 90.56 C ANISOU 672 CE MET A 87 12501 12181 9725 -276 -2137 132 C ATOM 673 N MET A 88 -1.781 -60.355 64.961 1.00 91.67 N ANISOU 673 N MET A 88 11767 12516 10548 -1405 -2402 433 N ATOM 674 CA MET A 88 -2.058 -61.635 65.603 1.00 93.70 C ANISOU 674 CA MET A 88 12241 12563 10797 -1705 -2484 398 C ATOM 675 C MET A 88 -3.492 -61.591 66.136 1.00 95.63 C ANISOU 675 C MET A 88 12137 13012 11186 -2066 -2551 485 C ATOM 676 O MET A 88 -3.741 -61.149 67.259 1.00 94.48 O ANISOU 676 O MET A 88 11721 12984 11193 -2121 -2369 575 O ATOM 677 CB MET A 88 -1.041 -61.917 66.715 1.00 91.91 C ANISOU 677 CB MET A 88 12175 12139 10608 -1591 -2289 409 C ATOM 678 CG MET A 88 0.407 -61.515 66.387 1.00 90.14 C ANISOU 678 CG MET A 88 12097 11844 10309 -1177 -2148 359 C ATOM 679 SD MET A 88 1.098 -62.283 64.899 1.00 93.00 S ANISOU 679 SD MET A 88 12889 12032 10413 -995 -2299 181 S ATOM 680 CE MET A 88 1.670 -63.858 65.540 1.00 94.25 C ANISOU 680 CE MET A 88 13518 11783 10509 -1055 -2374 81 C ATOM 681 N SER A 89 -4.429 -62.040 65.300 1.00 98.96 N ANISOU 681 N SER A 89 12557 13495 11547 -2311 -2813 451 N ATOM 682 CA SER A 89 -5.865 -61.854 65.533 1.00101.51 C ANISOU 682 CA SER A 89 12459 14103 12009 -2628 -2904 529 C ATOM 683 C SER A 89 -6.354 -62.391 66.888 1.00102.71 C ANISOU 683 C SER A 89 12501 14254 12270 -2965 -2787 601 C ATOM 684 O SER A 89 -6.792 -61.597 67.726 1.00101.97 O ANISOU 684 O SER A 89 11991 14413 12339 -2945 -2591 687 O ATOM 685 CB SER A 89 -6.692 -62.415 64.366 1.00105.00 C ANISOU 685 CB SER A 89 12976 14578 12343 -2868 -3250 473 C ATOM 686 N PRO A 90 -6.284 -63.728 67.110 1.00104.90 N ANISOU 686 N PRO A 90 13176 14240 12442 -3274 -2906 565 N ATOM 687 CA PRO A 90 -6.665 -64.262 68.427 1.00105.93 C ANISOU 687 CA PRO A 90 13262 14346 12642 -3617 -2786 653 C ATOM 688 C PRO A 90 -5.533 -64.206 69.460 1.00103.01 C ANISOU 688 C PRO A 90 13102 13767 12272 -3388 -2539 676 C ATOM 689 O PRO A 90 -5.775 -63.833 70.613 1.00102.43 O ANISOU 689 O PRO A 90 12780 13838 12299 -3473 -2320 770 O ATOM 690 CB PRO A 90 -7.045 -65.724 68.126 1.00109.65 C ANISOU 690 CB PRO A 90 14139 14546 12978 -4056 -3067 613 C ATOM 691 CG PRO A 90 -7.012 -65.863 66.612 1.00110.82 C ANISOU 691 CG PRO A 90 14479 14629 12998 -3941 -3341 492 C ATOM 692 CD PRO A 90 -6.059 -64.819 66.142 1.00107.11 C ANISOU 692 CD PRO A 90 13955 14218 12525 -3380 -3185 448 C ATOM 693 N LYS A 91 -4.317 -64.569 69.044 1.00101.51 N ANISOU 693 N LYS A 91 13352 13258 11960 -3094 -2575 584 N ATOM 694 CA LYS A 91 -3.152 -64.604 69.933 1.00 99.05 C ANISOU 694 CA LYS A 91 13259 12732 11642 -2859 -2391 597 C ATOM 695 C LYS A 91 -2.817 -63.214 70.472 1.00 95.72 C ANISOU 695 C LYS A 91 12451 12566 11351 -2554 -2119 661 C ATOM 696 O LYS A 91 -2.986 -62.216 69.770 1.00 94.68 O ANISOU 696 O LYS A 91 12030 12673 11271 -2346 -2095 652 O ATOM 697 CB LYS A 91 -1.942 -65.203 69.207 1.00 98.52 C ANISOU 697 CB LYS A 91 13673 12333 11428 -2555 -2493 465 C ATOM 698 N GLU A 92 -2.361 -63.167 71.725 1.00 94.40 N ANISOU 698 N GLU A 92 12316 12327 11224 -2544 -1937 729 N ATOM 699 CA GLU A 92 -1.948 -61.922 72.406 1.00 91.42 C ANISOU 699 CA GLU A 92 11648 12134 10953 -2276 -1685 785 C ATOM 700 C GLU A 92 -3.005 -60.793 72.428 1.00 91.39 C ANISOU 700 C GLU A 92 11120 12524 11081 -2302 -1580 834 C ATOM 701 O GLU A 92 -3.028 -59.927 71.543 1.00 90.52 O ANISOU 701 O GLU A 92 10817 12569 11008 -2061 -1607 806 O ATOM 702 CB GLU A 92 -0.605 -61.415 71.857 1.00 88.73 C ANISOU 702 CB GLU A 92 11439 11694 10580 -1829 -1646 725 C ATOM 703 N ASP A 93 -3.870 -60.821 73.447 1.00 92.53 N ANISOU 703 N ASP A 93 11048 12825 11284 -2587 -1462 906 N ATOM 704 CA ASP A 93 -4.854 -59.759 73.697 1.00 92.61 C ANISOU 704 CA ASP A 93 10542 13217 11427 -2576 -1323 940 C ATOM 705 C ASP A 93 -4.385 -58.840 74.836 1.00 90.20 C ANISOU 705 C ASP A 93 10131 12969 11173 -2370 -1051 976 C ATOM 706 O ASP A 93 -3.470 -59.188 75.586 1.00 88.89 O ANISOU 706 O ASP A 93 10270 12569 10936 -2341 -979 995 O ATOM 707 CB ASP A 93 -6.227 -60.358 74.017 1.00 96.22 C ANISOU 707 CB ASP A 93 10768 13882 11909 -3035 -1353 983 C ATOM 708 N TYR A 94 -5.012 -57.670 74.954 1.00 89.76 N ANISOU 708 N TYR A 94 9660 13212 11234 -2214 -922 978 N ATOM 709 CA TYR A 94 -4.661 -56.673 75.974 1.00 87.70 C ANISOU 709 CA TYR A 94 9296 13011 11015 -2001 -675 992 C ATOM 710 C TYR A 94 -4.988 -57.148 77.404 1.00 88.87 C ANISOU 710 C TYR A 94 9463 13192 11110 -2289 -483 1038 C ATOM 711 O TYR A 94 -5.791 -58.070 77.571 1.00 91.68 O ANISOU 711 O TYR A 94 9785 13620 11431 -2677 -521 1069 O ATOM 712 CB TYR A 94 -5.389 -55.361 75.679 1.00 88.12 C ANISOU 712 CB TYR A 94 8921 13360 11201 -1758 -614 968 C ATOM 713 CG TYR A 94 -4.982 -54.687 74.388 1.00 86.62 C ANISOU 713 CG TYR A 94 8744 13127 11041 -1448 -781 946 C ATOM 714 CD1 TYR A 94 -3.886 -53.829 74.343 1.00 83.80 C ANISOU 714 CD1 TYR A 94 8548 12619 10674 -1124 -727 948 C ATOM 715 CD2 TYR A 94 -5.702 -54.895 73.214 1.00 88.46 C ANISOU 715 CD2 TYR A 94 8835 13479 11296 -1507 -1001 932 C ATOM 716 CE1 TYR A 94 -3.511 -53.202 73.161 1.00 82.70 C ANISOU 716 CE1 TYR A 94 8438 12450 10536 -877 -867 946 C ATOM 717 CE2 TYR A 94 -5.334 -54.270 72.026 1.00 87.39 C ANISOU 717 CE2 TYR A 94 8744 13305 11154 -1238 -1155 923 C ATOM 718 CZ TYR A 94 -4.238 -53.425 72.008 1.00 84.51 C ANISOU 718 CZ TYR A 94 8549 12792 10769 -929 -1075 934 C ATOM 719 OH TYR A 94 -3.869 -52.800 70.840 1.00 84.17 O ANISOU 719 OH TYR A 94 8568 12719 10695 -699 -1213 943 O ATOM 720 N PRO A 95 -4.379 -56.523 78.443 1.00 86.91 N ANISOU 720 N PRO A 95 9288 12895 10840 -2131 -283 1047 N ATOM 721 CA PRO A 95 -3.415 -55.412 78.449 1.00 83.74 C ANISOU 721 CA PRO A 95 8942 12404 10471 -1731 -226 1023 C ATOM 722 C PRO A 95 -1.986 -55.863 78.159 1.00 81.10 C ANISOU 722 C PRO A 95 9014 11738 10064 -1612 -353 1033 C ATOM 723 O PRO A 95 -1.609 -56.977 78.516 1.00 81.67 O ANISOU 723 O PRO A 95 9382 11609 10040 -1814 -416 1061 O ATOM 724 CB PRO A 95 -3.505 -54.866 79.883 1.00 84.02 C ANISOU 724 CB PRO A 95 8926 12522 10475 -1737 30 1030 C ATOM 725 CG PRO A 95 -4.601 -55.646 80.557 1.00 87.31 C ANISOU 725 CG PRO A 95 9209 13121 10842 -2132 133 1059 C ATOM 726 CD PRO A 95 -4.718 -56.924 79.816 1.00 88.43 C ANISOU 726 CD PRO A 95 9514 13137 10948 -2409 -89 1093 C ATOM 727 N ILE A 96 -1.203 -54.992 77.526 1.00 78.56 N ANISOU 727 N ILE A 96 8700 11365 9784 -1284 -389 1012 N ATOM 728 CA ILE A 96 0.164 -55.317 77.120 1.00 76.23 C ANISOU 728 CA ILE A 96 8712 10820 9431 -1135 -494 1012 C ATOM 729 C ILE A 96 1.173 -54.441 77.852 1.00 74.06 C ANISOU 729 C ILE A 96 8508 10472 9160 -928 -382 1032 C ATOM 730 O ILE A 96 0.970 -53.234 77.987 1.00 73.47 O ANISOU 730 O ILE A 96 8245 10520 9149 -771 -284 1029 O ATOM 731 CB ILE A 96 0.355 -55.158 75.585 1.00 75.77 C ANISOU 731 CB ILE A 96 8630 10772 9386 -967 -649 978 C ATOM 732 CG1 ILE A 96 -0.661 -56.009 74.802 1.00 78.31 C ANISOU 732 CG1 ILE A 96 8898 11163 9694 -1186 -797 952 C ATOM 733 CG2 ILE A 96 1.792 -55.473 75.162 1.00 73.98 C ANISOU 733 CG2 ILE A 96 8681 10336 9092 -795 -719 966 C ATOM 734 CD1 ILE A 96 -0.557 -57.525 75.006 1.00 79.80 C ANISOU 734 CD1 ILE A 96 9386 11148 9787 -1445 -901 944 C ATOM 735 N GLU A 97 2.254 -55.058 78.324 1.00 73.09 N ANISOU 735 N GLU A 97 8667 10135 8967 -925 -418 1051 N ATOM 736 CA GLU A 97 3.342 -54.327 78.969 1.00 71.42 C ANISOU 736 CA GLU A 97 8537 9845 8753 -750 -356 1074 C ATOM 737 C GLU A 97 4.670 -54.582 78.272 1.00 70.17 C ANISOU 737 C GLU A 97 8535 9548 8577 -569 -472 1069 C ATOM 738 O GLU A 97 5.147 -55.714 78.216 1.00 70.69 O ANISOU 738 O GLU A 97 8817 9455 8586 -611 -578 1057 O ATOM 739 CB GLU A 97 3.438 -54.680 80.457 1.00 72.11 C ANISOU 739 CB GLU A 97 8783 9847 8769 -908 -276 1111 C ATOM 740 CG GLU A 97 2.262 -54.180 81.313 1.00 73.58 C ANISOU 740 CG GLU A 97 8791 10215 8952 -1049 -96 1108 C ATOM 741 CD GLU A 97 2.143 -52.657 81.347 1.00 72.80 C ANISOU 741 CD GLU A 97 8487 10248 8926 -833 17 1077 C ATOM 742 OE1 GLU A 97 3.185 -51.961 81.305 1.00 71.33 O ANISOU 742 OE1 GLU A 97 8385 9965 8754 -644 -17 1088 O ATOM 743 OE2 GLU A 97 1.001 -52.157 81.423 1.00 73.56 O ANISOU 743 OE2 GLU A 97 8339 10546 9066 -854 131 1042 O ATOM 744 N ILE A 98 5.255 -53.516 77.732 1.00 68.95 N ANISOU 744 N ILE A 98 8272 9458 8468 -363 -451 1075 N ATOM 745 CA ILE A 98 6.511 -53.605 76.987 1.00 68.19 C ANISOU 745 CA ILE A 98 8257 9300 8353 -188 -524 1071 C ATOM 746 C ILE A 98 7.593 -52.720 77.607 1.00 67.19 C ANISOU 746 C ILE A 98 8127 9155 8246 -78 -475 1118 C ATOM 747 O ILE A 98 7.359 -51.535 77.887 1.00 66.67 O ANISOU 747 O ILE A 98 7950 9159 8221 -54 -398 1147 O ATOM 748 CB ILE A 98 6.307 -53.260 75.495 1.00 68.20 C ANISOU 748 CB ILE A 98 8147 9410 8354 -85 -566 1048 C ATOM 749 CG1 ILE A 98 5.547 -54.391 74.799 1.00 69.75 C ANISOU 749 CG1 ILE A 98 8412 9585 8504 -194 -667 990 C ATOM 750 CG2 ILE A 98 7.642 -53.026 74.793 1.00 67.48 C ANISOU 750 CG2 ILE A 98 8089 9318 8231 99 -581 1054 C ATOM 751 CD1 ILE A 98 5.008 -54.031 73.429 1.00 70.67 C ANISOU 751 CD1 ILE A 98 8420 9827 8606 -139 -725 969 C ATOM 752 N GLN A 99 8.769 -53.313 77.815 1.00 67.11 N ANISOU 752 N GLN A 99 8246 9044 8208 -7 -538 1121 N ATOM 753 CA GLN A 99 9.897 -52.630 78.439 1.00 66.54 C ANISOU 753 CA GLN A 99 8167 8961 8155 68 -527 1170 C ATOM 754 C GLN A 99 11.140 -52.674 77.569 1.00 66.79 C ANISOU 754 C GLN A 99 8150 9041 8187 238 -570 1166 C ATOM 755 O GLN A 99 11.486 -53.713 77.014 1.00 67.59 O ANISOU 755 O GLN A 99 8328 9101 8254 322 -635 1111 O ATOM 756 CB GLN A 99 10.207 -53.250 79.797 1.00 66.93 C ANISOU 756 CB GLN A 99 8390 8870 8171 -15 -572 1190 C ATOM 757 CG GLN A 99 9.217 -52.892 80.880 1.00 66.59 C ANISOU 757 CG GLN A 99 8379 8818 8104 -184 -483 1206 C ATOM 758 CD GLN A 99 9.039 -54.010 81.866 1.00 66.75 C ANISOU 758 CD GLN A 99 8618 8697 8046 -330 -533 1218 C ATOM 759 OE1 GLN A 99 8.640 -55.117 81.500 1.00 67.50 O ANISOU 759 OE1 GLN A 99 8813 8722 8112 -395 -595 1196 O ATOM 760 NE2 GLN A 99 9.330 -53.734 83.127 1.00 66.69 N ANISOU 760 NE2 GLN A 99 8725 8630 7986 -399 -520 1258 N ATOM 761 N LEU A 100 11.809 -51.534 77.462 1.00 66.68 N ANISOU 761 N LEU A 100 8016 9118 8203 282 -528 1222 N ATOM 762 CA LEU A 100 13.044 -51.436 76.702 1.00 67.49 C ANISOU 762 CA LEU A 100 8024 9320 8299 411 -536 1234 C ATOM 763 C LEU A 100 14.172 -50.925 77.574 1.00 67.85 C ANISOU 763 C LEU A 100 8028 9371 8380 404 -566 1296 C ATOM 764 O LEU A 100 14.078 -49.837 78.148 1.00 67.32 O ANISOU 764 O LEU A 100 7946 9297 8337 305 -542 1356 O ATOM 765 CB LEU A 100 12.872 -50.500 75.503 1.00 67.44 C ANISOU 765 CB LEU A 100 7897 9453 8275 430 -469 1264 C ATOM 766 CG LEU A 100 12.495 -51.116 74.158 1.00 67.98 C ANISOU 766 CG LEU A 100 7971 9585 8273 507 -466 1200 C ATOM 767 CD1 LEU A 100 10.995 -51.323 74.056 1.00 67.48 C ANISOU 767 CD1 LEU A 100 7962 9466 8210 423 -488 1165 C ATOM 768 CD2 LEU A 100 12.998 -50.213 73.044 1.00 68.41 C ANISOU 768 CD2 LEU A 100 7915 9799 8277 544 -404 1256 C ATOM 769 N SER A 101 15.233 -51.718 77.672 1.00 69.08 N ANISOU 769 N SER A 101 8175 9534 8540 519 -636 1275 N ATOM 770 CA SER A 101 16.441 -51.289 78.352 1.00 70.10 C ANISOU 770 CA SER A 101 8215 9711 8709 523 -691 1336 C ATOM 771 C SER A 101 17.575 -51.318 77.361 1.00 71.51 C ANISOU 771 C SER A 101 8188 10091 8892 664 -660 1331 C ATOM 772 O SER A 101 18.020 -52.393 76.952 1.00 72.81 O ANISOU 772 O SER A 101 8350 10272 9042 848 -691 1252 O ATOM 773 CB SER A 101 16.758 -52.193 79.539 1.00 70.84 C ANISOU 773 CB SER A 101 8456 9653 8806 546 -826 1325 C ATOM 774 OG SER A 101 17.843 -51.673 80.287 1.00 71.95 O ANISOU 774 OG SER A 101 8509 9844 8986 523 -908 1392 O ATOM 775 N ALA A 102 18.031 -50.134 76.968 1.00 71.90 N ANISOU 775 N ALA A 102 8078 10292 8950 575 -593 1413 N ATOM 776 CA ALA A 102 19.080 -50.012 75.961 1.00 73.80 C ANISOU 776 CA ALA A 102 8091 10776 9172 662 -522 1425 C ATOM 777 C ALA A 102 20.142 -49.004 76.374 1.00 74.92 C ANISOU 777 C ALA A 102 8052 11052 9361 528 -543 1539 C ATOM 778 O ALA A 102 19.839 -48.021 77.047 1.00 74.32 O ANISOU 778 O ALA A 102 8060 10874 9305 338 -580 1617 O ATOM 779 CB ALA A 102 18.480 -49.628 74.622 1.00 73.60 C ANISOU 779 CB ALA A 102 8059 10840 9064 650 -396 1422 C ATOM 780 N GLY A 103 21.381 -49.252 75.962 1.00 77.09 N ANISOU 780 N GLY A 103 8079 11562 9649 628 -521 1540 N ATOM 781 CA GLY A 103 22.492 -48.368 76.295 1.00 78.77 C ANISOU 781 CA GLY A 103 8073 11947 9910 474 -551 1653 C ATOM 782 C GLY A 103 23.850 -48.999 76.064 1.00 81.60 C ANISOU 782 C GLY A 103 8120 12578 10308 648 -552 1622 C ATOM 783 O GLY A 103 23.983 -49.948 75.293 1.00 82.44 O ANISOU 783 O GLY A 103 8166 12782 10376 900 -472 1510 O ATOM 784 N CYS A 104 24.861 -48.470 76.740 1.00 83.37 N ANISOU 784 N CYS A 104 8143 12928 10605 520 -650 1713 N ATOM 785 CA CYS A 104 26.228 -48.922 76.536 1.00 86.89 C ANISOU 785 CA CYS A 104 8215 13693 11106 672 -652 1697 C ATOM 786 C CYS A 104 27.037 -48.884 77.824 1.00 88.49 C ANISOU 786 C CYS A 104 8315 13888 11419 618 -885 1752 C ATOM 787 O CYS A 104 26.881 -47.972 78.640 1.00 87.77 O ANISOU 787 O CYS A 104 8349 13659 11341 335 -996 1855 O ATOM 788 CB CYS A 104 26.905 -48.074 75.461 1.00 88.72 C ANISOU 788 CB CYS A 104 8149 14276 11284 513 -462 1785 C ATOM 789 SG CYS A 104 26.591 -46.291 75.603 1.00 88.02 S ANISOU 789 SG CYS A 104 8181 14103 11159 31 -466 1982 S ATOM 790 N GLU A 105 27.894 -49.886 78.001 1.00 91.13 N ANISOU 790 N GLU A 105 8441 14359 11824 907 -974 1674 N ATOM 791 CA GLU A 105 28.780 -49.952 79.157 1.00 93.26 C ANISOU 791 CA GLU A 105 8574 14660 12200 896 -1226 1726 C ATOM 792 C GLU A 105 30.135 -49.346 78.813 1.00 96.74 C ANISOU 792 C GLU A 105 8506 15545 12707 789 -1193 1810 C ATOM 793 O GLU A 105 30.562 -49.392 77.662 1.00 98.42 O ANISOU 793 O GLU A 105 8432 16073 12889 883 -970 1778 O ATOM 794 CB GLU A 105 28.944 -51.396 79.634 1.00 94.37 C ANISOU 794 CB GLU A 105 8795 14674 12389 1286 -1390 1604 C ATOM 795 CG GLU A 105 27.672 -52.015 80.203 1.00 92.11 C ANISOU 795 CG GLU A 105 9019 13944 12036 1324 -1464 1548 C ATOM 796 CD GLU A 105 27.946 -53.150 81.181 1.00 94.40 C ANISOU 796 CD GLU A 105 9457 14041 12370 1572 -1732 1500 C ATOM 797 OE1 GLU A 105 28.715 -52.949 82.149 1.00 96.32 O ANISOU 797 OE1 GLU A 105 9591 14326 12679 1512 -1959 1578 O ATOM 798 OE2 GLU A 105 27.377 -54.245 80.988 1.00 94.61 O ANISOU 798 OE2 GLU A 105 9738 13855 12356 1813 -1736 1391 O ATOM 799 N MET A 106 30.805 -48.784 79.816 1.00 98.21 N ANISOU 799 N MET A 106 8580 15766 12969 575 -1415 1919 N ATOM 800 CA MET A 106 32.076 -48.091 79.605 1.00101.84 C ANISOU 800 CA MET A 106 8545 16653 13498 386 -1414 2026 C ATOM 801 C MET A 106 33.252 -48.834 80.226 1.00105.33 C ANISOU 801 C MET A 106 8628 17315 14076 630 -1639 1997 C ATOM 802 O MET A 106 33.148 -49.365 81.334 1.00104.89 O ANISOU 802 O MET A 106 8793 17000 14061 743 -1915 1975 O ATOM 803 CB MET A 106 32.009 -46.662 80.149 1.00101.41 C ANISOU 803 CB MET A 106 8609 16505 13418 -122 -1505 2191 C ATOM 804 CG MET A 106 30.894 -45.797 79.554 1.00 98.91 C ANISOU 804 CG MET A 106 8638 15968 12975 -357 -1312 2232 C ATOM 805 SD MET A 106 30.840 -45.690 77.746 1.00100.36 S ANISOU 805 SD MET A 106 8618 16450 13063 -313 -933 2222 S ATOM 806 CE MET A 106 32.488 -45.091 77.370 1.00105.48 C ANISOU 806 CE MET A 106 8641 17665 13771 -550 -896 2355 C ATOM 807 N TYR A 107 34.370 -48.851 79.501 1.00109.09 N ANISOU 807 N TYR A 107 8545 18288 14615 708 -1520 2001 N ATOM 808 CA TYR A 107 35.548 -49.639 79.876 1.00113.16 C ANISOU 808 CA TYR A 107 8627 19093 15276 1026 -1702 1950 C ATOM 809 C TYR A 107 36.842 -48.817 79.788 1.00117.30 C ANISOU 809 C TYR A 107 8544 20135 15888 742 -1716 2084 C ATOM 810 O TYR A 107 36.805 -47.667 79.345 1.00117.07 O ANISOU 810 O TYR A 107 8467 20223 15791 290 -1562 2217 O ATOM 811 CB TYR A 107 35.631 -50.892 78.993 1.00114.50 C ANISOU 811 CB TYR A 107 8675 19388 15442 1579 -1523 1754 C ATOM 812 CG TYR A 107 34.578 -51.930 79.322 1.00111.82 C ANISOU 812 CG TYR A 107 8896 18542 15049 1888 -1615 1623 C ATOM 813 CD1 TYR A 107 34.879 -53.024 80.137 1.00113.60 C ANISOU 813 CD1 TYR A 107 9195 18605 15364 2269 -1907 1542 C ATOM 814 CD2 TYR A 107 33.275 -51.812 78.827 1.00107.85 C ANISOU 814 CD2 TYR A 107 8854 17720 14404 1781 -1428 1592 C ATOM 815 CE1 TYR A 107 33.909 -53.977 80.445 1.00111.33 C ANISOU 815 CE1 TYR A 107 9449 17839 15012 2501 -1997 1442 C ATOM 816 CE2 TYR A 107 32.302 -52.752 79.131 1.00105.37 C ANISOU 816 CE2 TYR A 107 9032 16965 14039 2010 -1513 1485 C ATOM 817 CZ TYR A 107 32.622 -53.830 79.937 1.00107.18 C ANISOU 817 CZ TYR A 107 9348 17030 14347 2351 -1790 1414 C ATOM 818 OH TYR A 107 31.650 -54.758 80.229 1.00105.07 O ANISOU 818 OH TYR A 107 9593 16315 14012 2528 -1875 1326 O ATOM 819 N PRO A 108 37.985 -49.391 80.235 1.00121.39 N ANISOU 819 N PRO A 108 8603 20959 16561 992 -1923 2059 N ATOM 820 CA PRO A 108 39.284 -48.727 80.057 1.00126.07 C ANISOU 820 CA PRO A 108 8522 22128 17252 748 -1918 2175 C ATOM 821 C PRO A 108 39.654 -48.504 78.581 1.00128.03 C ANISOU 821 C PRO A 108 8352 22860 17434 737 -1479 2155 C ATOM 822 O PRO A 108 39.753 -49.465 77.810 1.00129.24 O ANISOU 822 O PRO A 108 8351 23180 17576 1228 -1273 1979 O ATOM 823 CB PRO A 108 40.270 -49.701 80.714 1.00130.17 C ANISOU 823 CB PRO A 108 8659 22850 17951 1186 -2212 2097 C ATOM 824 CG PRO A 108 39.459 -50.449 81.704 1.00126.98 C ANISOU 824 CG PRO A 108 8864 21854 17527 1423 -2499 2029 C ATOM 825 CD PRO A 108 38.105 -50.596 81.080 1.00122.11 C ANISOU 825 CD PRO A 108 8810 20842 16744 1458 -2226 1947 C ATOM 826 N GLY A 109 39.849 -47.240 78.206 1.00128.49 N ANISOU 826 N GLY A 109 8269 23123 17429 170 -1344 2335 N ATOM 827 CA GLY A 109 40.202 -46.867 76.834 1.00130.49 C ANISOU 827 CA GLY A 109 8157 23842 17581 52 -925 2359 C ATOM 828 C GLY A 109 39.011 -46.376 76.031 1.00125.98 C ANISOU 828 C GLY A 109 8116 22950 16801 -136 -660 2377 C ATOM 829 O GLY A 109 38.048 -45.847 76.591 1.00121.82 O ANISOU 829 O GLY A 109 8158 21907 16222 -379 -808 2443 O ATOM 830 N ASN A 110 39.079 -46.545 74.713 1.00127.09 N ANISOU 830 N ASN A 110 8066 23409 16813 -11 -269 2315 N ATOM 831 CA ASN A 110 37.955 -46.215 73.840 1.00123.18 C ANISOU 831 CA ASN A 110 8060 22635 16109 -121 -24 2316 C ATOM 832 C ASN A 110 36.868 -47.299 73.877 1.00118.96 C ANISOU 832 C ASN A 110 8023 21635 15541 370 -54 2106 C ATOM 833 O ASN A 110 35.728 -47.062 73.458 1.00115.22 O ANISOU 833 O ASN A 110 8047 20806 14925 284 43 2105 O ATOM 834 CB ASN A 110 38.438 -45.984 72.405 1.00126.46 C ANISOU 834 CB ASN A 110 8117 23570 16363 -197 399 2335 C ATOM 835 N ALA A 111 37.229 -48.471 74.405 1.00119.79 N ANISOU 835 N ALA A 111 7996 21738 15779 868 -215 1940 N ATOM 836 CA ALA A 111 36.383 -49.672 74.385 1.00116.60 C ANISOU 836 CA ALA A 111 8006 20950 15346 1366 -245 1729 C ATOM 837 C ALA A 111 35.057 -49.520 75.119 1.00110.83 C ANISOU 837 C ALA A 111 7946 19579 14585 1218 -440 1761 C ATOM 838 O ALA A 111 35.006 -48.990 76.234 1.00109.62 O ANISOU 838 O ALA A 111 7925 19209 14516 952 -713 1881 O ATOM 839 CB ALA A 111 37.148 -50.874 74.933 1.00119.64 C ANISOU 839 CB ALA A 111 8123 21441 15892 1896 -435 1574 C ATOM 840 N SER A 112 33.996 -49.994 74.468 1.00107.43 N ANISOU 840 N SER A 112 7925 18872 14022 1394 -293 1645 N ATOM 841 CA SER A 112 32.651 -50.049 75.045 1.00102.11 C ANISOU 841 CA SER A 112 7860 17626 13312 1327 -438 1640 C ATOM 842 C SER A 112 31.825 -51.180 74.420 1.00100.15 C ANISOU 842 C SER A 112 7929 17151 12971 1719 -339 1442 C ATOM 843 O SER A 112 32.209 -51.744 73.396 1.00102.49 O ANISOU 843 O SER A 112 8026 17720 13195 2000 -123 1314 O ATOM 844 CB SER A 112 31.934 -48.701 74.892 1.00 99.55 C ANISOU 844 CB SER A 112 7772 17158 12893 825 -367 1810 C ATOM 845 OG SER A 112 31.983 -48.232 73.558 1.00100.78 O ANISOU 845 OG SER A 112 7795 17592 12904 713 -59 1839 O ATOM 846 N GLU A 113 30.706 -51.519 75.053 1.00 96.02 N ANISOU 846 N GLU A 113 7902 16142 12440 1728 -497 1412 N ATOM 847 CA GLU A 113 29.788 -52.521 74.523 1.00 93.93 C ANISOU 847 CA GLU A 113 7992 15616 12083 2014 -436 1246 C ATOM 848 C GLU A 113 28.347 -52.089 74.775 1.00 89.35 C ANISOU 848 C GLU A 113 7886 14629 11434 1749 -471 1303 C ATOM 849 O GLU A 113 27.956 -51.835 75.917 1.00 87.38 O ANISOU 849 O GLU A 113 7840 14111 11250 1580 -673 1381 O ATOM 850 CB GLU A 113 30.062 -53.898 75.139 1.00 95.34 C ANISOU 850 CB GLU A 113 8251 15628 12347 2445 -644 1100 C ATOM 851 CG GLU A 113 29.377 -55.056 74.427 1.00 94.69 C ANISOU 851 CG GLU A 113 8482 15335 12162 2781 -575 904 C ATOM 852 N SER A 114 27.573 -52.008 73.696 1.00 87.79 N ANISOU 852 N SER A 114 7850 14410 11097 1725 -273 1259 N ATOM 853 CA SER A 114 26.184 -51.558 73.749 1.00 83.92 C ANISOU 853 CA SER A 114 7749 13594 10541 1497 -282 1307 C ATOM 854 C SER A 114 25.182 -52.714 73.717 1.00 82.30 C ANISOU 854 C SER A 114 7912 13066 10293 1717 -346 1158 C ATOM 855 O SER A 114 25.526 -53.836 73.347 1.00 84.20 O ANISOU 855 O SER A 114 8145 13333 10516 2056 -343 1005 O ATOM 856 CB SER A 114 25.902 -50.587 72.605 1.00 83.63 C ANISOU 856 CB SER A 114 7672 13729 10374 1277 -64 1385 C ATOM 857 OG SER A 114 26.819 -49.510 72.628 1.00 85.46 O ANISOU 857 OG SER A 114 7595 14243 10633 1023 -12 1539 O ATOM 858 N PHE A 115 23.940 -52.420 74.101 1.00 79.09 N ANISOU 858 N PHE A 115 7825 12358 9867 1519 -404 1201 N ATOM 859 CA PHE A 115 22.871 -53.419 74.207 1.00 77.43 C ANISOU 859 CA PHE A 115 7969 11830 9621 1634 -482 1091 C ATOM 860 C PHE A 115 21.490 -52.805 73.946 1.00 74.66 C ANISOU 860 C PHE A 115 7843 11319 9206 1397 -430 1139 C ATOM 861 O PHE A 115 21.295 -51.595 74.104 1.00 73.49 O ANISOU 861 O PHE A 115 7643 11209 9069 1146 -393 1267 O ATOM 862 CB PHE A 115 22.889 -54.060 75.600 1.00 77.17 C ANISOU 862 CB PHE A 115 8094 11545 9682 1679 -709 1092 C ATOM 863 CG PHE A 115 22.777 -53.061 76.733 1.00 75.71 C ANISOU 863 CG PHE A 115 7920 11287 9561 1390 -797 1239 C ATOM 864 CD1 PHE A 115 23.918 -52.534 77.331 1.00 77.11 C ANISOU 864 CD1 PHE A 115 7840 11637 9820 1344 -874 1324 C ATOM 865 CD2 PHE A 115 21.530 -52.648 77.202 1.00 73.13 C ANISOU 865 CD2 PHE A 115 7854 10728 9205 1169 -806 1282 C ATOM 866 CE1 PHE A 115 23.820 -51.611 78.372 1.00 75.73 C ANISOU 866 CE1 PHE A 115 7720 11373 9682 1072 -970 1445 C ATOM 867 CE2 PHE A 115 21.425 -51.726 78.243 1.00 71.83 C ANISOU 867 CE2 PHE A 115 7729 10486 9076 931 -876 1392 C ATOM 868 CZ PHE A 115 22.572 -51.209 78.827 1.00 73.04 C ANISOU 868 CZ PHE A 115 7676 10780 9294 878 -965 1471 C ATOM 869 N LEU A 116 20.537 -53.647 73.548 1.00 73.80 N ANISOU 869 N LEU A 116 7987 11024 9031 1481 -445 1032 N ATOM 870 CA LEU A 116 19.133 -53.248 73.450 1.00 71.27 C ANISOU 870 CA LEU A 116 7868 10540 8671 1282 -436 1065 C ATOM 871 C LEU A 116 18.245 -54.451 73.743 1.00 70.74 C ANISOU 871 C LEU A 116 8089 10202 8588 1344 -548 963 C ATOM 872 O LEU A 116 18.036 -55.313 72.880 1.00 71.63 O ANISOU 872 O LEU A 116 8314 10287 8615 1492 -537 841 O ATOM 873 CB LEU A 116 18.815 -52.666 72.070 1.00 71.47 C ANISOU 873 CB LEU A 116 7842 10733 8582 1239 -288 1071 C ATOM 874 CG LEU A 116 17.692 -51.627 71.949 1.00 69.52 C ANISOU 874 CG LEU A 116 7673 10420 8321 1007 -270 1167 C ATOM 875 CD1 LEU A 116 17.743 -50.942 70.594 1.00 70.26 C ANISOU 875 CD1 LEU A 116 7692 10714 8291 974 -142 1205 C ATOM 876 CD2 LEU A 116 16.311 -52.214 72.180 1.00 68.64 C ANISOU 876 CD2 LEU A 116 7792 10078 8211 965 -355 1107 C ATOM 877 N HIS A 117 17.731 -54.496 74.970 1.00 69.31 N ANISOU 877 N HIS A 117 8045 9818 8470 1209 -656 1014 N ATOM 878 CA HIS A 117 16.906 -55.600 75.433 1.00 69.12 C ANISOU 878 CA HIS A 117 8304 9532 8428 1202 -769 949 C ATOM 879 C HIS A 117 15.429 -55.225 75.531 1.00 67.53 C ANISOU 879 C HIS A 117 8212 9237 8208 964 -740 984 C ATOM 880 O HIS A 117 15.077 -54.170 76.076 1.00 66.43 O ANISOU 880 O HIS A 117 7996 9135 8109 797 -693 1077 O ATOM 881 CB HIS A 117 17.403 -56.081 76.789 1.00 69.57 C ANISOU 881 CB HIS A 117 8457 9433 8542 1220 -916 983 C ATOM 882 CG HIS A 117 18.805 -56.596 76.768 1.00 71.67 C ANISOU 882 CG HIS A 117 8607 9781 8843 1490 -984 939 C ATOM 883 ND1 HIS A 117 19.229 -57.565 75.885 1.00 73.70 N ANISOU 883 ND1 HIS A 117 8898 10047 9056 1765 -991 805 N ATOM 884 CD2 HIS A 117 19.877 -56.290 77.535 1.00 72.76 C ANISOU 884 CD2 HIS A 117 8586 10003 9057 1543 -1059 1003 C ATOM 885 CE1 HIS A 117 20.505 -57.828 76.102 1.00 76.13 C ANISOU 885 CE1 HIS A 117 9046 10460 9421 2003 -1053 783 C ATOM 886 NE2 HIS A 117 20.922 -57.067 77.098 1.00 75.51 N ANISOU 886 NE2 HIS A 117 8834 10435 9420 1861 -1105 910 N ATOM 887 N VAL A 118 14.569 -56.098 75.007 1.00 67.73 N ANISOU 887 N VAL A 118 8417 9145 8172 955 -778 901 N ATOM 888 CA VAL A 118 13.126 -55.869 75.021 1.00 66.48 C ANISOU 888 CA VAL A 118 8322 8935 8003 737 -760 923 C ATOM 889 C VAL A 118 12.419 -57.002 75.758 1.00 67.16 C ANISOU 889 C VAL A 118 8662 8786 8070 623 -873 895 C ATOM 890 O VAL A 118 12.695 -58.178 75.507 1.00 68.81 O ANISOU 890 O VAL A 118 9065 8849 8231 735 -976 811 O ATOM 891 CB VAL A 118 12.553 -55.710 73.587 1.00 66.60 C ANISOU 891 CB VAL A 118 8294 9064 7948 753 -711 872 C ATOM 892 CG1 VAL A 118 11.044 -55.525 73.621 1.00 65.92 C ANISOU 892 CG1 VAL A 118 8232 8946 7867 541 -721 892 C ATOM 893 CG2 VAL A 118 13.199 -54.532 72.876 1.00 65.82 C ANISOU 893 CG2 VAL A 118 7977 9190 7842 819 -596 926 C ATOM 894 N ALA A 119 11.514 -56.632 76.666 1.00 66.29 N ANISOU 894 N ALA A 119 8564 8637 7987 400 -849 965 N ATOM 895 CA ALA A 119 10.735 -57.588 77.456 1.00 67.08 C ANISOU 895 CA ALA A 119 8891 8543 8052 218 -928 968 C ATOM 896 C ALA A 119 9.226 -57.412 77.273 1.00 67.01 C ANISOU 896 C ALA A 119 8830 8594 8037 -14 -873 974 C ATOM 897 O ALA A 119 8.680 -56.330 77.512 1.00 66.01 O ANISOU 897 O ALA A 119 8511 8613 7955 -90 -761 1022 O ATOM 898 CB ALA A 119 11.099 -57.476 78.921 1.00 66.97 C ANISOU 898 CB ALA A 119 8954 8442 8048 146 -947 1047 C ATOM 899 N PHE A 120 8.565 -58.489 76.856 1.00 68.43 N ANISOU 899 N PHE A 120 9183 8657 8162 -119 -967 921 N ATOM 900 CA PHE A 120 7.116 -58.508 76.650 1.00 68.86 C ANISOU 900 CA PHE A 120 9171 8781 8212 -364 -946 925 C ATOM 901 C PHE A 120 6.414 -59.159 77.844 1.00 70.14 C ANISOU 901 C PHE A 120 9486 8823 8341 -647 -960 982 C ATOM 902 O PHE A 120 6.547 -60.371 78.073 1.00 71.72 O ANISOU 902 O PHE A 120 9986 8793 8473 -726 -1093 971 O ATOM 903 CB PHE A 120 6.783 -59.244 75.343 1.00 70.02 C ANISOU 903 CB PHE A 120 9410 8893 8303 -350 -1057 834 C ATOM 904 CG PHE A 120 5.306 -59.392 75.062 1.00 70.85 C ANISOU 904 CG PHE A 120 9439 9076 8406 -621 -1080 837 C ATOM 905 CD1 PHE A 120 4.594 -58.370 74.435 1.00 70.07 C ANISOU 905 CD1 PHE A 120 9047 9219 8359 -619 -1011 848 C ATOM 906 CD2 PHE A 120 4.636 -60.568 75.389 1.00 72.65 C ANISOU 906 CD2 PHE A 120 9891 9136 8578 -886 -1191 834 C ATOM 907 CE1 PHE A 120 3.235 -58.509 74.160 1.00 70.90 C ANISOU 907 CE1 PHE A 120 9034 9429 8476 -854 -1052 849 C ATOM 908 CE2 PHE A 120 3.278 -60.714 75.119 1.00 73.82 C ANISOU 908 CE2 PHE A 120 9927 9392 8730 -1168 -1220 842 C ATOM 909 CZ PHE A 120 2.578 -59.682 74.504 1.00 73.11 C ANISOU 909 CZ PHE A 120 9495 9577 8708 -1140 -1151 845 C ATOM 910 N GLN A 121 5.683 -58.332 78.596 1.00 69.66 N ANISOU 910 N GLN A 121 9235 8917 8314 -791 -818 1041 N ATOM 911 CA GLN A 121 4.861 -58.753 79.743 1.00 71.03 C ANISOU 911 CA GLN A 121 9494 9058 8438 -1092 -770 1102 C ATOM 912 C GLN A 121 5.671 -59.258 80.943 1.00 71.53 C ANISOU 912 C GLN A 121 9836 8913 8428 -1112 -816 1161 C ATOM 913 O GLN A 121 5.182 -60.079 81.732 1.00 73.36 O ANISOU 913 O GLN A 121 10278 9025 8571 -1377 -843 1215 O ATOM 914 CB GLN A 121 3.811 -59.793 79.323 1.00 73.15 C ANISOU 914 CB GLN A 121 9850 9282 8662 -1367 -858 1088 C ATOM 915 CG GLN A 121 2.770 -59.276 78.347 1.00 73.38 C ANISOU 915 CG GLN A 121 9574 9550 8757 -1411 -824 1048 C ATOM 916 CD GLN A 121 1.579 -58.600 79.016 1.00 74.44 C ANISOU 916 CD GLN A 121 9417 9936 8930 -1606 -650 1089 C ATOM 917 OE1 GLN A 121 1.607 -58.253 80.199 1.00 74.63 O ANISOU 917 OE1 GLN A 121 9442 9986 8927 -1665 -512 1137 O ATOM 918 NE2 GLN A 121 0.516 -58.415 78.247 1.00 75.59 N ANISOU 918 NE2 GLN A 121 9308 10281 9130 -1696 -662 1061 N ATOM 919 N GLY A 122 6.901 -58.757 81.081 1.00 70.15 N ANISOU 919 N GLY A 122 9664 8706 8284 -850 -835 1160 N ATOM 920 CA GLY A 122 7.789 -59.166 82.175 1.00 70.50 C ANISOU 920 CA GLY A 122 9956 8564 8266 -827 -916 1217 C ATOM 921 C GLY A 122 9.004 -59.963 81.733 1.00 70.82 C ANISOU 921 C GLY A 122 10185 8413 8312 -580 -1106 1180 C ATOM 922 O GLY A 122 10.126 -59.655 82.127 1.00 70.31 O ANISOU 922 O GLY A 122 10118 8327 8271 -385 -1153 1198 O ATOM 923 N LYS A 123 8.776 -60.992 80.921 1.00 72.11 N ANISOU 923 N LYS A 123 10509 8440 8449 -583 -1223 1120 N ATOM 924 CA LYS A 123 9.851 -61.828 80.391 1.00 73.16 C ANISOU 924 CA LYS A 123 10833 8387 8579 -305 -1397 1051 C ATOM 925 C LYS A 123 10.598 -61.133 79.238 1.00 71.96 C ANISOU 925 C LYS A 123 10409 8430 8503 5 -1335 965 C ATOM 926 O LYS A 123 9.980 -60.531 78.355 1.00 71.12 O ANISOU 926 O LYS A 123 10089 8511 8421 -30 -1227 930 O ATOM 927 CB LYS A 123 9.292 -63.183 79.940 1.00 75.37 C ANISOU 927 CB LYS A 123 11436 8421 8780 -429 -1551 1003 C ATOM 928 CG LYS A 123 10.346 -64.234 79.622 1.00 76.95 C ANISOU 928 CG LYS A 123 11930 8355 8953 -134 -1758 924 C ATOM 929 N TYR A 124 11.927 -61.227 79.267 1.00 72.24 N ANISOU 929 N TYR A 124 10449 8431 8567 301 -1408 940 N ATOM 930 CA TYR A 124 12.813 -60.696 78.222 1.00 71.42 C ANISOU 930 CA TYR A 124 10100 8521 8514 596 -1345 865 C ATOM 931 C TYR A 124 12.813 -61.622 77.012 1.00 72.87 C ANISOU 931 C TYR A 124 10431 8616 8642 752 -1415 728 C ATOM 932 O TYR A 124 13.160 -62.799 77.127 1.00 74.96 O ANISOU 932 O TYR A 124 10996 8624 8861 870 -1582 670 O ATOM 933 CB TYR A 124 14.220 -60.524 78.808 1.00 71.94 C ANISOU 933 CB TYR A 124 10092 8610 8633 831 -1403 892 C ATOM 934 CG TYR A 124 15.394 -60.542 77.848 1.00 72.55 C ANISOU 934 CG TYR A 124 10000 8825 8741 1182 -1392 796 C ATOM 935 CD1 TYR A 124 15.547 -59.562 76.871 1.00 71.35 C ANISOU 935 CD1 TYR A 124 9542 8959 8610 1232 -1221 777 C ATOM 936 CD2 TYR A 124 16.387 -61.513 77.967 1.00 74.65 C ANISOU 936 CD2 TYR A 124 10409 8945 9008 1471 -1552 731 C ATOM 937 CE1 TYR A 124 16.639 -59.578 76.011 1.00 72.99 C ANISOU 937 CE1 TYR A 124 9579 9331 8822 1530 -1179 695 C ATOM 938 CE2 TYR A 124 17.481 -61.534 77.122 1.00 75.97 C ANISOU 938 CE2 TYR A 124 10382 9283 9202 1813 -1515 631 C ATOM 939 CZ TYR A 124 17.605 -60.565 76.147 1.00 75.39 C ANISOU 939 CZ TYR A 124 9989 9522 9132 1826 -1313 615 C ATOM 940 OH TYR A 124 18.692 -60.590 75.301 1.00 77.69 O ANISOU 940 OH TYR A 124 10072 10020 9426 2142 -1246 519 O ATOM 941 N VAL A 125 12.418 -61.085 75.857 1.00 71.95 N ANISOU 941 N VAL A 125 10134 8692 8513 758 -1301 674 N ATOM 942 CA VAL A 125 12.120 -61.922 74.679 1.00 73.42 C ANISOU 942 CA VAL A 125 10495 8792 8610 834 -1366 540 C ATOM 943 C VAL A 125 12.778 -61.516 73.356 1.00 73.32 C ANISOU 943 C VAL A 125 10304 8996 8560 1094 -1264 442 C ATOM 944 O VAL A 125 13.037 -62.364 72.501 1.00 75.24 O ANISOU 944 O VAL A 125 10733 9143 8710 1281 -1329 299 O ATOM 945 CB VAL A 125 10.593 -62.064 74.448 1.00 73.42 C ANISOU 945 CB VAL A 125 10571 8755 8569 497 -1385 557 C ATOM 946 CG1 VAL A 125 9.965 -62.972 75.514 1.00 74.84 C ANISOU 946 CG1 VAL A 125 11043 8664 8729 239 -1516 616 C ATOM 947 CG2 VAL A 125 9.921 -60.698 74.408 1.00 70.97 C ANISOU 947 CG2 VAL A 125 9921 8724 8322 340 -1224 647 C ATOM 948 N VAL A 126 13.032 -60.224 73.183 1.00 71.35 N ANISOU 948 N VAL A 126 9722 9027 8361 1097 -1104 516 N ATOM 949 CA VAL A 126 13.639 -59.732 71.950 1.00 71.50 C ANISOU 949 CA VAL A 126 9566 9280 8321 1292 -985 453 C ATOM 950 C VAL A 126 14.864 -58.860 72.237 1.00 70.82 C ANISOU 950 C VAL A 126 9193 9409 8307 1438 -873 520 C ATOM 951 O VAL A 126 14.865 -58.067 73.179 1.00 69.33 O ANISOU 951 O VAL A 126 8869 9259 8214 1296 -850 648 O ATOM 952 CB VAL A 126 12.615 -58.961 71.081 1.00 70.43 C ANISOU 952 CB VAL A 126 9328 9294 8138 1111 -913 483 C ATOM 953 CG1 VAL A 126 13.259 -58.466 69.802 1.00 71.09 C ANISOU 953 CG1 VAL A 126 9275 9613 8124 1288 -791 433 C ATOM 954 CG2 VAL A 126 11.408 -59.842 70.753 1.00 71.35 C ANISOU 954 CG2 VAL A 126 9697 9227 8186 942 -1046 416 C ATOM 955 N ARG A 127 15.905 -59.030 71.425 1.00 72.23 N ANISOU 955 N ARG A 127 9282 9734 8428 1712 -804 427 N ATOM 956 CA ARG A 127 17.101 -58.203 71.517 1.00 72.13 C ANISOU 956 CA ARG A 127 8954 9980 8471 1826 -687 490 C ATOM 957 C ARG A 127 17.521 -57.728 70.121 1.00 73.07 C ANISOU 957 C ARG A 127 8910 10382 8471 1931 -514 441 C ATOM 958 O ARG A 127 17.279 -58.415 69.119 1.00 74.41 O ANISOU 958 O ARG A 127 9247 10523 8504 2052 -506 302 O ATOM 959 CB ARG A 127 18.237 -58.972 72.214 1.00 73.97 C ANISOU 959 CB ARG A 127 9186 10147 8771 2086 -782 438 C ATOM 960 CG ARG A 127 19.391 -59.423 71.305 1.00 76.82 C ANISOU 960 CG ARG A 127 9424 10697 9068 2447 -697 295 C ATOM 961 CD ARG A 127 20.146 -60.612 71.875 1.00 79.36 C ANISOU 961 CD ARG A 127 9880 10837 9437 2760 -858 190 C ATOM 962 NE ARG A 127 21.582 -60.527 71.608 1.00 81.92 N ANISOU 962 NE ARG A 127 9879 11453 9792 3073 -766 135 N ATOM 963 CZ ARG A 127 22.405 -61.571 71.524 1.00 84.93 C ANISOU 963 CZ ARG A 127 10315 11781 10173 3479 -844 -23 C ATOM 964 NH1 ARG A 127 21.946 -62.809 71.665 1.00 86.17 N ANISOU 964 NH1 ARG A 127 10899 11553 10287 3615 -1033 -142 N ATOM 965 NH2 ARG A 127 23.693 -61.377 71.284 1.00 86.98 N ANISOU 965 NH2 ARG A 127 10201 12374 10472 3750 -736 -65 N ATOM 966 N PHE A 128 18.127 -56.544 70.058 1.00 72.38 N ANISOU 966 N PHE A 128 8526 10558 8416 1860 -381 560 N ATOM 967 CA PHE A 128 18.751 -56.085 68.825 1.00 73.71 C ANISOU 967 CA PHE A 128 8522 11028 8458 1950 -198 535 C ATOM 968 C PHE A 128 20.219 -56.485 68.840 1.00 76.45 C ANISOU 968 C PHE A 128 8657 11566 8824 2233 -131 462 C ATOM 969 O PHE A 128 20.929 -56.253 69.819 1.00 76.41 O ANISOU 969 O PHE A 128 8475 11594 8962 2236 -181 539 O ATOM 970 CB PHE A 128 18.597 -54.573 68.638 1.00 72.05 C ANISOU 970 CB PHE A 128 8129 10997 8249 1691 -94 715 C ATOM 971 CG PHE A 128 18.940 -54.097 67.248 1.00 73.05 C ANISOU 971 CG PHE A 128 8161 11400 8196 1714 84 710 C ATOM 972 CD1 PHE A 128 18.063 -54.304 66.187 1.00 73.06 C ANISOU 972 CD1 PHE A 128 8368 11361 8031 1695 88 645 C ATOM 973 CD2 PHE A 128 20.137 -53.449 66.997 1.00 74.09 C ANISOU 973 CD2 PHE A 128 8000 11843 8308 1729 243 778 C ATOM 974 CE1 PHE A 128 18.378 -53.877 64.902 1.00 74.02 C ANISOU 974 CE1 PHE A 128 8439 11735 7950 1705 250 647 C ATOM 975 CE2 PHE A 128 20.456 -53.014 65.712 1.00 75.79 C ANISOU 975 CE2 PHE A 128 8142 12328 8325 1719 428 787 C ATOM 976 CZ PHE A 128 19.573 -53.231 64.666 1.00 75.49 C ANISOU 976 CZ PHE A 128 8346 12232 8103 1714 432 720 C ATOM 977 N TRP A 129 20.664 -57.107 67.756 1.00 79.25 N ANISOU 977 N TRP A 129 9030 12054 9028 2483 -23 302 N ATOM 978 CA TRP A 129 22.035 -57.581 67.662 1.00 82.57 C ANISOU 978 CA TRP A 129 9227 12688 9458 2811 58 199 C ATOM 979 C TRP A 129 22.555 -57.460 66.238 1.00 85.15 C ANISOU 979 C TRP A 129 9430 13349 9576 2948 304 105 C ATOM 980 O TRP A 129 21.917 -57.928 65.292 1.00 85.82 O ANISOU 980 O TRP A 129 9780 13351 9477 3000 329 -19 O ATOM 981 CB TRP A 129 22.134 -59.028 68.160 1.00 84.20 C ANISOU 981 CB TRP A 129 9677 12603 9712 3120 -126 27 C ATOM 982 CG TRP A 129 23.531 -59.460 68.503 1.00 87.75 C ANISOU 982 CG TRP A 129 9865 13227 10250 3467 -116 -48 C ATOM 983 CD1 TRP A 129 24.193 -60.552 68.019 1.00 91.41 C ANISOU 983 CD1 TRP A 129 10384 13701 10647 3909 -104 -272 C ATOM 984 CD2 TRP A 129 24.439 -58.807 69.404 1.00 88.41 C ANISOU 984 CD2 TRP A 129 9582 13503 10506 3417 -133 95 C ATOM 985 NE1 TRP A 129 25.451 -60.623 68.564 1.00 93.89 N ANISOU 985 NE1 TRP A 129 10355 14223 11096 4159 -111 -277 N ATOM 986 CE2 TRP A 129 25.631 -59.564 69.415 1.00 92.18 C ANISOU 986 CE2 TRP A 129 9869 14127 11027 3845 -137 -47 C ATOM 987 CE3 TRP A 129 24.361 -57.653 70.205 1.00 86.16 C ANISOU 987 CE3 TRP A 129 9122 13276 10340 3059 -160 321 C ATOM 988 CZ2 TRP A 129 26.740 -59.207 70.196 1.00 93.90 C ANISOU 988 CZ2 TRP A 129 9694 14572 11412 3906 -179 43 C ATOM 989 CZ3 TRP A 129 25.465 -57.297 70.979 1.00 87.35 C ANISOU 989 CZ3 TRP A 129 8925 13625 10638 3098 -203 406 C ATOM 990 CH2 TRP A 129 26.637 -58.074 70.968 1.00 91.30 C ANISOU 990 CH2 TRP A 129 9208 14293 11188 3509 -218 274 C ATOM 991 N GLY A 130 23.714 -56.825 66.094 1.00 86.94 N ANISOU 991 N GLY A 130 9253 13963 9816 2983 482 167 N ATOM 992 CA GLY A 130 24.292 -56.564 64.783 1.00 89.71 C ANISOU 992 CA GLY A 130 9440 14696 9950 3063 758 108 C ATOM 993 C GLY A 130 23.410 -55.616 63.997 1.00 87.98 C ANISOU 993 C GLY A 130 9355 14501 9571 2720 834 240 C ATOM 994 O GLY A 130 23.406 -54.407 64.248 1.00 86.45 O ANISOU 994 O GLY A 130 8997 14414 9435 2397 865 461 O ATOM 995 N THR A 131 22.641 -56.174 63.065 1.00 88.40 N ANISOU 995 N THR A 131 9737 14429 9423 2791 835 104 N ATOM 996 CA THR A 131 21.805 -55.379 62.166 1.00 87.40 C ANISOU 996 CA THR A 131 9762 14334 9112 2513 887 211 C ATOM 997 C THR A 131 20.321 -55.757 62.208 1.00 85.03 C ANISOU 997 C THR A 131 9855 13644 8810 2401 656 182 C ATOM 998 O THR A 131 19.556 -55.343 61.336 1.00 84.88 O ANISOU 998 O THR A 131 10005 13629 8615 2239 661 224 O ATOM 999 CB THR A 131 22.276 -55.520 60.704 1.00 90.97 C ANISOU 999 CB THR A 131 10223 15096 9245 2654 1135 90 C ATOM 1000 OG1 THR A 131 22.227 -56.899 60.322 1.00 93.23 O ANISOU 1000 OG1 THR A 131 10760 15238 9426 3010 1096 -192 O ATOM 1001 CG2 THR A 131 23.695 -55.002 60.525 1.00 93.92 C ANISOU 1001 CG2 THR A 131 10160 15934 9591 2702 1407 144 C ATOM 1002 N SER A 132 19.909 -56.536 63.207 1.00 83.58 N ANISOU 1002 N SER A 132 9810 13135 8810 2470 445 121 N ATOM 1003 CA SER A 132 18.554 -57.096 63.219 1.00 82.05 C ANISOU 1003 CA SER A 132 9974 12597 8603 2372 234 68 C ATOM 1004 C SER A 132 18.044 -57.462 64.607 1.00 79.89 C ANISOU 1004 C SER A 132 9774 12008 8571 2292 21 113 C ATOM 1005 O SER A 132 18.826 -57.823 65.492 1.00 80.30 O ANISOU 1005 O SER A 132 9711 12031 8768 2441 -5 97 O ATOM 1006 CB SER A 132 18.495 -58.337 62.321 1.00 84.82 C ANISOU 1006 CB SER A 132 10621 12857 8750 2632 218 -187 C ATOM 1007 OG SER A 132 19.420 -59.321 62.749 1.00 86.55 O ANISOU 1007 OG SER A 132 10825 13029 9031 2973 217 -349 O ATOM 1008 N TRP A 133 16.726 -57.379 64.784 1.00 77.87 N ANISOU 1008 N TRP A 133 9706 11535 8347 2055 -134 170 N ATOM 1009 CA TRP A 133 16.077 -57.905 65.980 1.00 76.44 C ANISOU 1009 CA TRP A 133 9654 11049 8340 1960 -326 190 C ATOM 1010 C TRP A 133 16.079 -59.422 65.922 1.00 78.63 C ANISOU 1010 C TRP A 133 10236 11079 8561 2166 -453 -12 C ATOM 1011 O TRP A 133 15.943 -60.003 64.844 1.00 80.72 O ANISOU 1011 O TRP A 133 10698 11338 8634 2282 -447 -165 O ATOM 1012 CB TRP A 133 14.627 -57.452 66.068 1.00 74.42 C ANISOU 1012 CB TRP A 133 9486 10675 8115 1657 -436 289 C ATOM 1013 CG TRP A 133 14.419 -56.007 65.881 1.00 72.96 C ANISOU 1013 CG TRP A 133 9091 10684 7948 1478 -345 463 C ATOM 1014 CD1 TRP A 133 14.013 -55.387 64.742 1.00 73.82 C ANISOU 1014 CD1 TRP A 133 9210 10935 7903 1407 -299 496 C ATOM 1015 CD2 TRP A 133 14.585 -54.986 66.862 1.00 71.13 C ANISOU 1015 CD2 TRP A 133 8651 10493 7883 1346 -312 630 C ATOM 1016 NE1 TRP A 133 13.919 -54.035 64.948 1.00 72.62 N ANISOU 1016 NE1 TRP A 133 8876 10897 7821 1248 -246 680 N ATOM 1017 CE2 TRP A 133 14.267 -53.759 66.242 1.00 70.84 C ANISOU 1017 CE2 TRP A 133 8516 10607 7792 1208 -249 757 C ATOM 1018 CE3 TRP A 133 14.976 -54.985 68.205 1.00 70.42 C ANISOU 1018 CE3 TRP A 133 8480 10311 7967 1331 -346 683 C ATOM 1019 CZ2 TRP A 133 14.327 -52.538 66.915 1.00 69.53 C ANISOU 1019 CZ2 TRP A 133 8188 10484 7746 1063 -218 923 C ATOM 1020 CZ3 TRP A 133 15.035 -53.771 68.878 1.00 69.53 C ANISOU 1020 CZ3 TRP A 133 8194 10261 7963 1177 -308 843 C ATOM 1021 CH2 TRP A 133 14.709 -52.563 68.230 1.00 69.13 C ANISOU 1021 CH2 TRP A 133 8062 10342 7861 1049 -244 956 C ATOM 1022 N GLN A 134 16.215 -60.062 67.079 1.00 78.48 N ANISOU 1022 N GLN A 134 10295 10834 8689 2205 -584 -12 N ATOM 1023 CA GLN A 134 16.132 -61.518 67.146 1.00 80.79 C ANISOU 1023 CA GLN A 134 10941 10820 8936 2373 -749 -184 C ATOM 1024 C GLN A 134 15.476 -62.010 68.428 1.00 79.75 C ANISOU 1024 C GLN A 134 10987 10372 8943 2183 -946 -107 C ATOM 1025 O GLN A 134 15.669 -61.434 69.498 1.00 77.97 O ANISOU 1025 O GLN A 134 10578 10178 8868 2078 -940 41 O ATOM 1026 CB GLN A 134 17.509 -62.167 66.940 1.00 83.72 C ANISOU 1026 CB GLN A 134 11278 11259 9271 2802 -688 -340 C ATOM 1027 CG GLN A 134 18.555 -61.826 67.990 1.00 83.34 C ANISOU 1027 CG GLN A 134 10944 11318 9405 2917 -664 -243 C ATOM 1028 CD GLN A 134 19.962 -62.135 67.528 1.00 86.29 C ANISOU 1028 CD GLN A 134 11136 11913 9739 3340 -541 -384 C ATOM 1029 OE1 GLN A 134 20.668 -62.930 68.145 1.00 88.58 O ANISOU 1029 OE1 GLN A 134 11478 12067 10110 3620 -656 -462 O ATOM 1030 NE2 GLN A 134 20.376 -61.507 66.435 1.00 87.00 N ANISOU 1030 NE2 GLN A 134 11004 12357 9694 3394 -305 -414 N ATOM 1031 N THR A 135 14.687 -63.073 68.299 1.00 81.29 N ANISOU 1031 N THR A 135 11560 10263 9065 2114 -1123 -205 N ATOM 1032 CA THR A 135 14.061 -63.712 69.445 1.00 81.31 C ANISOU 1032 CA THR A 135 11787 9947 9159 1914 -1312 -138 C ATOM 1033 C THR A 135 15.133 -64.414 70.268 1.00 83.16 C ANISOU 1033 C THR A 135 12113 10020 9464 2196 -1398 -175 C ATOM 1034 O THR A 135 15.916 -65.210 69.743 1.00 86.12 O ANISOU 1034 O THR A 135 12639 10319 9763 2553 -1431 -350 O ATOM 1035 CB THR A 135 12.958 -64.723 69.029 1.00 82.89 C ANISOU 1035 CB THR A 135 12390 9856 9247 1731 -1496 -229 C ATOM 1036 OG1 THR A 135 13.500 -65.700 68.133 1.00 86.28 O ANISOU 1036 OG1 THR A 135 13104 10151 9528 2045 -1555 -450 O ATOM 1037 CG2 THR A 135 11.799 -64.015 68.347 1.00 81.57 C ANISOU 1037 CG2 THR A 135 12102 9855 9034 1427 -1453 -170 C ATOM 1038 N VAL A 136 15.171 -64.093 71.557 1.00 81.90 N ANISOU 1038 N VAL A 136 11862 9815 9441 2052 -1438 -17 N ATOM 1039 CA VAL A 136 16.119 -64.674 72.505 1.00 83.50 C ANISOU 1039 CA VAL A 136 12146 9860 9721 2280 -1559 -14 C ATOM 1040 C VAL A 136 16.001 -66.200 72.530 1.00 86.86 C ANISOU 1040 C VAL A 136 13072 9863 10068 2406 -1794 -144 C ATOM 1041 O VAL A 136 14.918 -66.733 72.296 1.00 87.24 O ANISOU 1041 O VAL A 136 13418 9696 10034 2148 -1891 -163 O ATOM 1042 CB VAL A 136 15.874 -64.087 73.916 1.00 81.21 C ANISOU 1042 CB VAL A 136 11754 9552 9549 2007 -1587 191 C ATOM 1043 CG1 VAL A 136 16.794 -64.703 74.963 1.00 82.90 C ANISOU 1043 CG1 VAL A 136 12089 9582 9829 2215 -1755 213 C ATOM 1044 CG2 VAL A 136 16.065 -62.591 73.882 1.00 78.67 C ANISOU 1044 CG2 VAL A 136 10989 9604 9299 1911 -1379 303 C ATOM 1045 N PRO A 137 17.124 -66.910 72.770 1.00 89.81 N ANISOU 1045 N PRO A 137 13541 10116 10466 2810 -1900 -238 N ATOM 1046 CA PRO A 137 17.043 -68.342 73.079 1.00 93.05 C ANISOU 1046 CA PRO A 137 14481 10053 10819 2923 -2172 -326 C ATOM 1047 C PRO A 137 16.133 -68.591 74.287 1.00 92.06 C ANISOU 1047 C PRO A 137 14616 9643 10719 2495 -2336 -141 C ATOM 1048 O PRO A 137 16.296 -67.950 75.331 1.00 90.15 O ANISOU 1048 O PRO A 137 14171 9506 10575 2358 -2311 31 O ATOM 1049 CB PRO A 137 18.501 -68.720 73.405 1.00 95.68 C ANISOU 1049 CB PRO A 137 14740 10388 11226 3434 -2246 -403 C ATOM 1050 CG PRO A 137 19.239 -67.398 73.568 1.00 93.31 C ANISOU 1050 CG PRO A 137 13841 10569 11043 3466 -2024 -297 C ATOM 1051 CD PRO A 137 18.525 -66.466 72.645 1.00 90.70 C ANISOU 1051 CD PRO A 137 13281 10530 10651 3203 -1783 -282 C ATOM 1052 N GLY A 138 15.176 -69.503 74.129 1.00 93.56 N ANISOU 1052 N GLY A 138 15258 9486 10803 2264 -2496 -178 N ATOM 1053 CA GLY A 138 14.167 -69.750 75.154 1.00 93.11 C ANISOU 1053 CA GLY A 138 15441 9197 10738 1789 -2617 1 C ATOM 1054 C GLY A 138 13.119 -68.656 75.144 1.00 89.81 C ANISOU 1054 C GLY A 138 14682 9093 10350 1356 -2413 130 C ATOM 1055 O GLY A 138 12.985 -67.897 76.106 1.00 87.63 O ANISOU 1055 O GLY A 138 14180 8964 10150 1155 -2325 299 O ATOM 1056 N ALA A 139 12.389 -68.567 74.038 1.00 89.77 N ANISOU 1056 N ALA A 139 14647 9186 10276 1237 -2346 39 N ATOM 1057 CA ALA A 139 11.344 -67.561 73.861 1.00 87.34 C ANISOU 1057 CA ALA A 139 14013 9175 9996 874 -2176 140 C ATOM 1058 C ALA A 139 10.238 -68.136 72.982 1.00 88.93 C ANISOU 1058 C ALA A 139 14439 9263 10089 621 -2270 61 C ATOM 1059 O ALA A 139 10.497 -69.049 72.191 1.00 91.71 O ANISOU 1059 O ALA A 139 15121 9391 10333 817 -2406 -110 O ATOM 1060 CB ALA A 139 11.918 -66.279 73.242 1.00 84.83 C ANISOU 1060 CB ALA A 139 13209 9283 9739 1086 -1938 127 C ATOM 1061 N PRO A 140 9.001 -67.616 73.124 1.00 87.65 N ANISOU 1061 N PRO A 140 14100 9254 9949 193 -2208 176 N ATOM 1062 CA PRO A 140 7.854 -68.133 72.362 1.00 89.40 C ANISOU 1062 CA PRO A 140 14493 9395 10079 -109 -2323 122 C ATOM 1063 C PRO A 140 7.985 -67.918 70.855 1.00 89.79 C ANISOU 1063 C PRO A 140 14473 9597 10046 109 -2289 -41 C ATOM 1064 O PRO A 140 8.448 -66.865 70.417 1.00 87.72 O ANISOU 1064 O PRO A 140 13844 9661 9826 318 -2098 -40 O ATOM 1065 CB PRO A 140 6.674 -67.340 72.923 1.00 87.63 C ANISOU 1065 CB PRO A 140 13942 9417 9935 -535 -2212 290 C ATOM 1066 CG PRO A 140 7.283 -66.134 73.565 1.00 84.53 C ANISOU 1066 CG PRO A 140 13158 9298 9661 -365 -1995 387 C ATOM 1067 CD PRO A 140 8.595 -66.582 74.092 1.00 84.87 C ANISOU 1067 CD PRO A 140 13396 9144 9708 -33 -2047 357 C ATOM 1068 N SER A 141 7.573 -68.914 70.077 1.00 92.88 N ANISOU 1068 N SER A 141 15248 9742 10301 36 -2484 -175 N ATOM 1069 CA SER A 141 7.802 -68.909 68.634 1.00 94.07 C ANISOU 1069 CA SER A 141 15442 9979 10321 274 -2478 -359 C ATOM 1070 C SER A 141 6.835 -68.016 67.858 1.00 92.85 C ANISOU 1070 C SER A 141 14964 10158 10158 40 -2406 -313 C ATOM 1071 O SER A 141 7.083 -67.712 66.691 1.00 93.21 O ANISOU 1071 O SER A 141 14964 10359 10092 243 -2355 -431 O ATOM 1072 CB SER A 141 7.777 -70.333 68.071 1.00 98.16 C ANISOU 1072 CB SER A 141 16549 10076 10671 313 -2734 -544 C ATOM 1073 OG SER A 141 6.481 -70.894 68.160 1.00 99.80 O ANISOU 1073 OG SER A 141 16962 10116 10843 -195 -2931 -485 O ATOM 1074 N TRP A 142 5.741 -67.600 68.494 1.00 91.90 N ANISOU 1074 N TRP A 142 14621 10156 10142 -373 -2404 -145 N ATOM 1075 CA TRP A 142 4.765 -66.727 67.833 1.00 91.10 C ANISOU 1075 CA TRP A 142 14183 10375 10055 -577 -2361 -92 C ATOM 1076 C TRP A 142 5.348 -65.351 67.530 1.00 88.12 C ANISOU 1076 C TRP A 142 13390 10353 9737 -303 -2125 -49 C ATOM 1077 O TRP A 142 4.860 -64.649 66.645 1.00 87.83 O ANISOU 1077 O TRP A 142 13153 10555 9664 -331 -2105 -47 O ATOM 1078 CB TRP A 142 3.480 -66.589 68.654 1.00 91.13 C ANISOU 1078 CB TRP A 142 13997 10457 10171 -1048 -2394 69 C ATOM 1079 CG TRP A 142 3.667 -65.890 69.969 1.00 89.42 C ANISOU 1079 CG TRP A 142 13503 10361 10110 -1064 -2205 226 C ATOM 1080 CD1 TRP A 142 3.964 -66.473 71.162 1.00 90.38 C ANISOU 1080 CD1 TRP A 142 13820 10258 10263 -1144 -2218 293 C ATOM 1081 CD2 TRP A 142 3.563 -64.480 70.226 1.00 87.01 C ANISOU 1081 CD2 TRP A 142 12721 10408 9930 -1001 -1993 332 C ATOM 1082 NE1 TRP A 142 4.056 -65.519 72.148 1.00 88.28 N ANISOU 1082 NE1 TRP A 142 13222 10197 10123 -1140 -2020 427 N ATOM 1083 CE2 TRP A 142 3.816 -64.287 71.601 1.00 85.87 C ANISOU 1083 CE2 TRP A 142 12508 10238 9882 -1047 -1879 446 C ATOM 1084 CE3 TRP A 142 3.285 -63.363 69.428 1.00 86.05 C ANISOU 1084 CE3 TRP A 142 12262 10597 9836 -907 -1908 342 C ATOM 1085 CZ2 TRP A 142 3.799 -63.025 72.200 1.00 83.34 C ANISOU 1085 CZ2 TRP A 142 11799 10184 9681 -998 -1676 551 C ATOM 1086 CZ3 TRP A 142 3.269 -62.105 70.025 1.00 83.81 C ANISOU 1086 CZ3 TRP A 142 11598 10563 9684 -852 -1715 457 C ATOM 1087 CH2 TRP A 142 3.525 -61.950 71.399 1.00 82.50 C ANISOU 1087 CH2 TRP A 142 11378 10357 9611 -896 -1599 551 C ATOM 1088 N LEU A 143 6.390 -64.977 68.269 1.00 86.29 N ANISOU 1088 N LEU A 143 13050 10145 9590 -54 -1970 -4 N ATOM 1089 CA LEU A 143 7.075 -63.701 68.082 1.00 83.79 C ANISOU 1089 CA LEU A 143 12372 10136 9330 183 -1753 49 C ATOM 1090 C LEU A 143 7.741 -63.560 66.715 1.00 84.64 C ANISOU 1090 C LEU A 143 12520 10358 9283 473 -1705 -85 C ATOM 1091 O LEU A 143 8.037 -62.443 66.282 1.00 83.11 O ANISOU 1091 O LEU A 143 12038 10443 9097 581 -1548 -28 O ATOM 1092 CB LEU A 143 8.123 -63.505 69.177 1.00 82.40 C ANISOU 1092 CB LEU A 143 12117 9928 9262 367 -1640 112 C ATOM 1093 CG LEU A 143 7.640 -63.012 70.540 1.00 80.99 C ANISOU 1093 CG LEU A 143 11755 9782 9234 130 -1586 281 C ATOM 1094 CD1 LEU A 143 8.689 -63.298 71.597 1.00 80.84 C ANISOU 1094 CD1 LEU A 143 11824 9621 9272 298 -1569 310 C ATOM 1095 CD2 LEU A 143 7.291 -61.519 70.513 1.00 79.07 C ANISOU 1095 CD2 LEU A 143 11098 9864 9081 83 -1422 393 C ATOM 1096 N ASP A 144 7.965 -64.693 66.048 1.00 87.42 N ANISOU 1096 N ASP A 144 13257 10483 9477 587 -1839 -263 N ATOM 1097 CA ASP A 144 8.670 -64.751 64.761 1.00 88.84 C ANISOU 1097 CA ASP A 144 13540 10749 9466 889 -1782 -425 C ATOM 1098 C ASP A 144 8.059 -63.884 63.657 1.00 88.26 C ANISOU 1098 C ASP A 144 13295 10948 9291 790 -1748 -397 C ATOM 1099 O ASP A 144 8.779 -63.131 63.000 1.00 87.76 O ANISOU 1099 O ASP A 144 13065 11129 9151 1008 -1571 -403 O ATOM 1100 CB ASP A 144 8.807 -66.204 64.287 1.00 92.49 C ANISOU 1100 CB ASP A 144 14509 10871 9762 998 -1967 -640 C ATOM 1101 CG ASP A 144 9.825 -66.999 65.099 1.00 93.92 C ANISOU 1101 CG ASP A 144 14879 10805 10001 1268 -1978 -705 C ATOM 1102 OD1 ASP A 144 10.506 -66.414 65.975 1.00 92.50 O ANISOU 1102 OD1 ASP A 144 14416 10749 9979 1380 -1837 -588 O ATOM 1103 OD2 ASP A 144 9.946 -68.220 64.854 1.00 97.31 O ANISOU 1103 OD2 ASP A 144 15762 10901 10312 1376 -2152 -877 O ATOM 1104 N LEU A 145 6.744 -63.994 63.455 1.00 88.55 N ANISOU 1104 N LEU A 145 13372 10952 9322 453 -1926 -358 N ATOM 1105 CA LEU A 145 6.047 -63.200 62.436 1.00 88.37 C ANISOU 1105 CA LEU A 145 13197 11170 9208 348 -1949 -319 C ATOM 1106 C LEU A 145 6.209 -61.683 62.637 1.00 85.46 C ANISOU 1106 C LEU A 145 12396 11113 8961 395 -1753 -142 C ATOM 1107 O LEU A 145 6.548 -60.979 61.682 1.00 85.53 O ANISOU 1107 O LEU A 145 12337 11323 8837 531 -1666 -142 O ATOM 1108 CB LEU A 145 4.569 -63.597 62.329 1.00 89.67 C ANISOU 1108 CB LEU A 145 13424 11262 9383 -38 -2201 -294 C ATOM 1109 N PRO A 146 5.972 -61.175 63.871 1.00 83.12 N ANISOU 1109 N PRO A 146 11842 10845 8896 274 -1688 8 N ATOM 1110 CA PRO A 146 6.242 -59.763 64.172 1.00 80.61 C ANISOU 1110 CA PRO A 146 11167 10768 8692 341 -1508 162 C ATOM 1111 C PRO A 146 7.708 -59.356 64.003 1.00 79.95 C ANISOU 1111 C PRO A 146 11040 10781 8555 642 -1304 145 C ATOM 1112 O PRO A 146 7.994 -58.221 63.612 1.00 79.01 O ANISOU 1112 O PRO A 146 10720 10878 8422 704 -1183 240 O ATOM 1113 CB PRO A 146 5.834 -59.641 65.641 1.00 79.04 C ANISOU 1113 CB PRO A 146 10807 10510 8716 175 -1485 274 C ATOM 1114 CG PRO A 146 4.767 -60.648 65.799 1.00 80.77 C ANISOU 1114 CG PRO A 146 11191 10564 8933 -95 -1682 230 C ATOM 1115 CD PRO A 146 5.216 -61.811 64.968 1.00 83.15 C ANISOU 1115 CD PRO A 146 11881 10671 9041 11 -1797 53 C ATOM 1116 N ILE A 147 8.620 -60.274 64.302 1.00 80.71 N ANISOU 1116 N ILE A 147 11321 10720 8624 821 -1278 31 N ATOM 1117 CA ILE A 147 10.044 -60.038 64.111 1.00 80.74 C ANISOU 1117 CA ILE A 147 11257 10843 8576 1119 -1090 -7 C ATOM 1118 C ILE A 147 10.367 -59.871 62.628 1.00 82.42 C ANISOU 1118 C ILE A 147 11546 11226 8545 1258 -1024 -97 C ATOM 1119 O ILE A 147 11.068 -58.931 62.243 1.00 81.95 O ANISOU 1119 O ILE A 147 11284 11412 8441 1356 -843 -25 O ATOM 1120 CB ILE A 147 10.888 -61.161 64.776 1.00 81.95 C ANISOU 1120 CB ILE A 147 11596 10779 8763 1315 -1113 -124 C ATOM 1121 CG1 ILE A 147 11.068 -60.873 66.273 1.00 79.91 C ANISOU 1121 CG1 ILE A 147 11167 10464 8730 1241 -1091 13 C ATOM 1122 CG2 ILE A 147 12.241 -61.368 64.078 1.00 83.94 C ANISOU 1122 CG2 ILE A 147 11866 11150 8878 1677 -965 -258 C ATOM 1123 CD1 ILE A 147 11.503 -59.444 66.607 1.00 77.44 C ANISOU 1123 CD1 ILE A 147 10488 10414 8523 1231 -916 176 C ATOM 1124 N LYS A 148 9.822 -60.771 61.808 1.00 84.59 N ANISOU 1124 N LYS A 148 12132 11365 8644 1235 -1177 -248 N ATOM 1125 CA LYS A 148 10.019 -60.744 60.357 1.00 86.64 C ANISOU 1125 CA LYS A 148 12535 11761 8624 1350 -1137 -356 C ATOM 1126 C LYS A 148 9.495 -59.439 59.759 1.00 85.49 C ANISOU 1126 C LYS A 148 12182 11864 8438 1198 -1105 -189 C ATOM 1127 O LYS A 148 10.106 -58.883 58.843 1.00 86.56 O ANISOU 1127 O LYS A 148 12291 12215 8384 1317 -955 -188 O ATOM 1128 CB LYS A 148 9.345 -61.958 59.693 1.00 89.42 C ANISOU 1128 CB LYS A 148 13299 11877 8800 1297 -1363 -544 C ATOM 1129 CG LYS A 148 9.816 -62.266 58.269 1.00 92.07 C ANISOU 1129 CG LYS A 148 13884 12298 8800 1499 -1308 -727 C ATOM 1130 N VAL A 149 8.371 -58.956 60.288 1.00 83.60 N ANISOU 1130 N VAL A 149 11799 11595 8369 940 -1243 -46 N ATOM 1131 CA VAL A 149 7.763 -57.710 59.823 1.00 82.57 C ANISOU 1131 CA VAL A 149 11481 11660 8233 815 -1256 118 C ATOM 1132 C VAL A 149 8.666 -56.518 60.129 1.00 80.89 C ANISOU 1132 C VAL A 149 11008 11634 8091 911 -1028 266 C ATOM 1133 O VAL A 149 8.842 -55.637 59.284 1.00 81.55 O ANISOU 1133 O VAL A 149 11054 11901 8031 924 -962 350 O ATOM 1134 CB VAL A 149 6.333 -57.506 60.409 1.00 81.52 C ANISOU 1134 CB VAL A 149 11217 11466 8291 555 -1454 219 C ATOM 1135 CG1 VAL A 149 5.829 -56.083 60.190 1.00 80.16 C ANISOU 1135 CG1 VAL A 149 10807 11480 8172 492 -1455 403 C ATOM 1136 CG2 VAL A 149 5.366 -58.497 59.793 1.00 83.70 C ANISOU 1136 CG2 VAL A 149 11737 11617 8450 404 -1706 98 C ATOM 1137 N LEU A 150 9.256 -56.510 61.320 1.00 79.07 N ANISOU 1137 N LEU A 150 10627 11350 8066 958 -923 303 N ATOM 1138 CA LEU A 150 10.057 -55.372 61.763 1.00 77.64 C ANISOU 1138 CA LEU A 150 10197 11324 7979 1000 -740 452 C ATOM 1139 C LEU A 150 11.416 -55.276 61.072 1.00 79.24 C ANISOU 1139 C LEU A 150 10392 11709 8005 1190 -531 409 C ATOM 1140 O LEU A 150 11.925 -54.175 60.863 1.00 78.90 O ANISOU 1140 O LEU A 150 10190 11851 7937 1165 -399 549 O ATOM 1141 CB LEU A 150 10.227 -55.394 63.283 1.00 75.59 C ANISOU 1141 CB LEU A 150 9792 10951 7979 971 -717 505 C ATOM 1142 CG LEU A 150 9.001 -55.004 64.112 1.00 73.87 C ANISOU 1142 CG LEU A 150 9474 10644 7949 769 -840 603 C ATOM 1143 CD1 LEU A 150 9.049 -55.634 65.492 1.00 72.63 C ANISOU 1143 CD1 LEU A 150 9308 10319 7969 735 -854 583 C ATOM 1144 CD2 LEU A 150 8.867 -53.491 64.216 1.00 72.80 C ANISOU 1144 CD2 LEU A 150 9135 10638 7888 712 -782 779 C ATOM 1145 N ASN A 151 11.992 -56.424 60.717 1.00 81.32 N ANISOU 1145 N ASN A 151 10832 11924 8142 1376 -502 214 N ATOM 1146 CA ASN A 151 13.313 -56.472 60.077 1.00 83.48 C ANISOU 1146 CA ASN A 151 11070 12406 8244 1595 -279 138 C ATOM 1147 C ASN A 151 13.355 -55.931 58.648 1.00 85.40 C ANISOU 1147 C ASN A 151 11392 12868 8190 1578 -191 154 C ATOM 1148 O ASN A 151 14.397 -55.460 58.192 1.00 86.77 O ANISOU 1148 O ASN A 151 11436 13296 8238 1668 38 183 O ATOM 1149 CB ASN A 151 13.873 -57.894 60.102 1.00 85.64 C ANISOU 1149 CB ASN A 151 11532 12547 8461 1850 -283 -101 C ATOM 1150 CG ASN A 151 14.423 -58.279 61.457 1.00 84.85 C ANISOU 1150 CG ASN A 151 11306 12319 8616 1939 -291 -97 C ATOM 1151 OD1 ASN A 151 15.313 -57.618 61.993 1.00 84.75 O ANISOU 1151 OD1 ASN A 151 11011 12475 8717 1983 -143 7 O ATOM 1152 ND2 ASN A 151 13.900 -59.361 62.016 1.00 85.50 N ANISOU 1152 ND2 ASN A 151 11616 12096 8776 1946 -480 -202 N ATOM 1153 N ALA A 152 12.225 -56.008 57.950 1.00 85.87 N ANISOU 1153 N ALA A 152 11660 12841 8126 1446 -378 143 N ATOM 1154 CA ALA A 152 12.105 -55.514 56.578 1.00 87.83 C ANISOU 1154 CA ALA A 152 12039 13265 8066 1405 -346 170 C ATOM 1155 C ALA A 152 12.433 -54.024 56.463 1.00 87.02 C ANISOU 1155 C ALA A 152 11725 13373 7964 1281 -217 414 C ATOM 1156 O ALA A 152 12.784 -53.541 55.389 1.00 89.08 O ANISOU 1156 O ALA A 152 12064 13836 7946 1269 -104 457 O ATOM 1157 CB ALA A 152 10.710 -55.794 56.040 1.00 88.31 C ANISOU 1157 CB ALA A 152 12328 13177 8049 1254 -633 142 C ATOM 1158 N ASP A 153 12.313 -53.309 57.577 1.00 84.35 N ANISOU 1158 N ASP A 153 11154 12975 7921 1179 -241 574 N ATOM 1159 CA ASP A 153 12.619 -51.886 57.631 1.00 83.76 C ANISOU 1159 CA ASP A 153 10908 13039 7878 1050 -149 808 C ATOM 1160 C ASP A 153 14.121 -51.682 57.821 1.00 84.73 C ANISOU 1160 C ASP A 153 10837 13372 7986 1132 130 826 C ATOM 1161 O ASP A 153 14.612 -51.633 58.954 1.00 83.19 O ANISOU 1161 O ASP A 153 10438 13135 8036 1152 174 853 O ATOM 1162 CB ASP A 153 11.823 -51.219 58.764 1.00 80.82 C ANISOU 1162 CB ASP A 153 10395 12496 7817 921 -300 946 C ATOM 1163 CG ASP A 153 11.982 -49.701 58.804 1.00 79.93 C ANISOU 1163 CG ASP A 153 10175 12460 7734 785 -258 1185 C ATOM 1164 OD1 ASP A 153 12.783 -49.131 58.037 1.00 81.19 O ANISOU 1164 OD1 ASP A 153 10348 12812 7688 751 -102 1271 O ATOM 1165 OD2 ASP A 153 11.290 -49.069 59.627 1.00 77.86 O ANISOU 1165 OD2 ASP A 153 9828 12059 7696 706 -380 1287 O ATOM 1166 N GLN A 154 14.839 -51.568 56.705 1.00 87.68 N ANISOU 1166 N GLN A 154 11267 13991 8057 1168 314 811 N ATOM 1167 CA GLN A 154 16.264 -51.246 56.717 1.00 89.28 C ANISOU 1167 CA GLN A 154 11241 14469 8212 1209 600 851 C ATOM 1168 C GLN A 154 16.516 -49.848 57.281 1.00 88.14 C ANISOU 1168 C GLN A 154 10902 14371 8215 980 627 1120 C ATOM 1169 O GLN A 154 17.531 -49.617 57.931 1.00 88.06 O ANISOU 1169 O GLN A 154 10633 14493 8334 979 776 1165 O ATOM 1170 CB GLN A 154 16.850 -51.350 55.308 1.00 93.08 C ANISOU 1170 CB GLN A 154 11838 15232 8295 1262 807 790 C ATOM 1171 N GLY A 155 15.579 -48.932 57.033 1.00 87.62 N ANISOU 1171 N GLY A 155 10975 14185 8132 793 458 1291 N ATOM 1172 CA GLY A 155 15.679 -47.535 57.471 1.00 87.09 C ANISOU 1172 CA GLY A 155 10811 14102 8177 574 443 1547 C ATOM 1173 C GLY A 155 15.751 -47.345 58.975 1.00 84.64 C ANISOU 1173 C GLY A 155 10304 13633 8224 561 381 1578 C ATOM 1174 O GLY A 155 16.493 -46.485 59.460 1.00 84.68 O ANISOU 1174 O GLY A 155 10153 13710 8311 422 468 1729 O ATOM 1175 N THR A 156 14.969 -48.133 59.711 1.00 82.85 N ANISOU 1175 N THR A 156 10100 13189 8190 677 225 1441 N ATOM 1176 CA THR A 156 15.027 -48.137 61.173 1.00 80.92 C ANISOU 1176 CA THR A 156 9698 12796 8253 681 174 1443 C ATOM 1177 C THR A 156 16.272 -48.893 61.609 1.00 81.78 C ANISOU 1177 C THR A 156 9622 13044 8405 813 338 1332 C ATOM 1178 O THR A 156 17.132 -48.344 62.305 1.00 81.73 O ANISOU 1178 O THR A 156 9419 13116 8517 740 417 1428 O ATOM 1179 CB THR A 156 13.779 -48.801 61.805 1.00 79.00 C ANISOU 1179 CB THR A 156 9543 12300 8175 738 -29 1338 C ATOM 1180 OG1 THR A 156 12.630 -47.978 61.582 1.00 78.91 O ANISOU 1180 OG1 THR A 156 9630 12176 8175 633 -192 1451 O ATOM 1181 CG2 THR A 156 13.956 -48.995 63.302 1.00 76.90 C ANISOU 1181 CG2 THR A 156 9140 11903 8177 752 -51 1318 C ATOM 1182 N SER A 157 16.362 -50.148 61.172 1.00 83.08 N ANISOU 1182 N SER A 157 9864 13235 8469 1014 368 1127 N ATOM 1183 CA SER A 157 17.490 -51.019 61.484 1.00 84.35 C ANISOU 1183 CA SER A 157 9872 13517 8659 1215 501 987 C ATOM 1184 C SER A 157 18.839 -50.367 61.196 1.00 86.40 C ANISOU 1184 C SER A 157 9881 14109 8838 1170 733 1083 C ATOM 1185 O SER A 157 19.856 -50.791 61.736 1.00 87.26 O ANISOU 1185 O SER A 157 9769 14341 9045 1304 826 1019 O ATOM 1186 CB SER A 157 17.376 -52.338 60.720 1.00 86.20 C ANISOU 1186 CB SER A 157 10294 13738 8721 1448 508 749 C ATOM 1187 OG SER A 157 18.530 -53.131 60.919 1.00 88.13 O ANISOU 1187 OG SER A 157 10391 14115 8978 1692 644 606 O ATOM 1188 N ALA A 158 18.838 -49.343 60.345 1.00 87.56 N ANISOU 1188 N ALA A 158 10061 14405 8803 972 814 1246 N ATOM 1189 CA ALA A 158 20.041 -48.564 60.078 1.00 89.78 C ANISOU 1189 CA ALA A 158 10106 15007 8999 839 1031 1382 C ATOM 1190 C ALA A 158 20.323 -47.606 61.229 1.00 88.08 C ANISOU 1190 C ALA A 158 9721 14715 9032 633 958 1565 C ATOM 1191 O ALA A 158 21.409 -47.625 61.808 1.00 89.09 O ANISOU 1191 O ALA A 158 9563 15018 9268 643 1057 1574 O ATOM 1192 CB ALA A 158 19.912 -47.804 58.765 1.00 91.88 C ANISOU 1192 CB ALA A 158 10522 15434 8955 662 1128 1511 C ATOM 1193 N THR A 159 19.337 -46.785 61.572 1.00 85.86 N ANISOU 1193 N THR A 159 9614 14169 8838 462 772 1700 N ATOM 1194 CA THR A 159 19.526 -45.757 62.591 1.00 84.63 C ANISOU 1194 CA THR A 159 9367 13908 8881 254 692 1871 C ATOM 1195 C THR A 159 19.696 -46.308 64.006 1.00 82.69 C ANISOU 1195 C THR A 159 8987 13523 8909 363 600 1779 C ATOM 1196 O THR A 159 20.242 -45.625 64.876 1.00 82.47 O ANISOU 1196 O THR A 159 8827 13484 9024 212 572 1892 O ATOM 1197 CB THR A 159 18.419 -44.677 62.550 1.00 83.32 C ANISOU 1197 CB THR A 159 9447 13488 8724 82 518 2027 C ATOM 1198 OG1 THR A 159 17.281 -45.178 61.839 1.00 82.83 O ANISOU 1198 OG1 THR A 159 9604 13311 8556 208 422 1934 O ATOM 1199 CG2 THR A 159 18.932 -43.428 61.841 1.00 85.53 C ANISOU 1199 CG2 THR A 159 9763 13903 8833 -192 598 2256 C ATOM 1200 N VAL A 160 19.248 -47.545 64.220 1.00 81.63 N ANISOU 1200 N VAL A 160 8915 13275 8826 607 541 1581 N ATOM 1201 CA VAL A 160 19.414 -48.229 65.510 1.00 80.11 C ANISOU 1201 CA VAL A 160 8638 12944 8857 725 447 1488 C ATOM 1202 C VAL A 160 20.872 -48.651 65.693 1.00 82.26 C ANISOU 1202 C VAL A 160 8621 13480 9154 834 576 1443 C ATOM 1203 O VAL A 160 21.415 -48.591 66.800 1.00 81.68 O ANISOU 1203 O VAL A 160 8400 13374 9262 813 509 1473 O ATOM 1204 CB VAL A 160 18.471 -49.450 65.644 1.00 78.83 C ANISOU 1204 CB VAL A 160 8667 12560 8723 921 330 1305 C ATOM 1205 CG1 VAL A 160 18.629 -50.120 66.997 1.00 77.38 C ANISOU 1205 CG1 VAL A 160 8441 12215 8746 1012 223 1237 C ATOM 1206 CG2 VAL A 160 17.033 -49.024 65.458 1.00 77.33 C ANISOU 1206 CG2 VAL A 160 8697 12163 8522 810 200 1352 C ATOM 1207 N GLN A 161 21.499 -49.065 64.597 1.00 84.97 N ANISOU 1207 N GLN A 161 8879 14099 9305 957 759 1366 N ATOM 1208 CA GLN A 161 22.929 -49.331 64.583 1.00 87.89 C ANISOU 1208 CA GLN A 161 8916 14801 9677 1064 920 1330 C ATOM 1209 C GLN A 161 23.704 -48.049 64.873 1.00 89.12 C ANISOU 1209 C GLN A 161 8838 15144 9880 751 975 1555 C ATOM 1210 O GLN A 161 24.715 -48.073 65.578 1.00 90.15 O ANISOU 1210 O GLN A 161 8673 15433 10147 761 984 1573 O ATOM 1211 CB GLN A 161 23.354 -49.891 63.230 1.00 90.87 C ANISOU 1211 CB GLN A 161 9265 15464 9796 1242 1141 1205 C ATOM 1212 CG GLN A 161 22.680 -51.187 62.851 1.00 90.09 C ANISOU 1212 CG GLN A 161 9427 15180 9622 1546 1081 967 C ATOM 1213 CD GLN A 161 22.975 -51.584 61.427 1.00 92.61 C ANISOU 1213 CD GLN A 161 9788 15760 9638 1691 1298 846 C ATOM 1214 OE1 GLN A 161 24.120 -51.863 61.075 1.00 95.89 O ANISOU 1214 OE1 GLN A 161 9935 16520 9977 1853 1510 769 O ATOM 1215 NE2 GLN A 161 21.943 -51.615 60.596 1.00 91.67 N ANISOU 1215 NE2 GLN A 161 9999 15497 9334 1639 1246 822 N ATOM 1216 N MET A 162 23.214 -46.933 64.329 1.00 89.31 N ANISOU 1216 N MET A 162 9013 15133 9787 466 987 1732 N ATOM 1217 CA MET A 162 23.846 -45.628 64.515 1.00 90.88 C ANISOU 1217 CA MET A 162 9071 15456 10002 116 1017 1964 C ATOM 1218 C MET A 162 23.904 -45.261 65.994 1.00 88.96 C ANISOU 1218 C MET A 162 8782 14998 10021 15 820 2024 C ATOM 1219 O MET A 162 24.961 -44.878 66.502 1.00 90.70 O ANISOU 1219 O MET A 162 8725 15411 10327 -126 843 2110 O ATOM 1220 CB MET A 162 23.123 -44.539 63.712 1.00 90.95 C ANISOU 1220 CB MET A 162 9351 15367 9838 -144 1007 2139 C ATOM 1221 CG MET A 162 23.959 -43.273 63.511 1.00 94.49 C ANISOU 1221 CG MET A 162 9675 16013 10214 -525 1093 2384 C ATOM 1222 SD MET A 162 23.221 -42.005 62.447 1.00 97.90 S ANISOU 1222 SD MET A 162 10469 16325 10404 -825 1072 2609 S ATOM 1223 CE MET A 162 23.434 -42.704 60.802 1.00100.33 C ANISOU 1223 CE MET A 162 10771 16987 10361 -691 1338 2520 C ATOM 1224 N LEU A 163 22.771 -45.406 66.677 1.00 85.78 N ANISOU 1224 N LEU A 163 8643 14218 9732 84 629 1973 N ATOM 1225 CA LEU A 163 22.670 -45.099 68.100 1.00 83.94 C ANISOU 1225 CA LEU A 163 8429 13751 9713 5 445 2009 C ATOM 1226 C LEU A 163 23.475 -46.056 68.973 1.00 84.42 C ANISOU 1226 C LEU A 163 8264 13893 9920 198 407 1892 C ATOM 1227 O LEU A 163 24.108 -45.633 69.941 1.00 84.70 O ANISOU 1227 O LEU A 163 8166 13931 10087 65 313 1968 O ATOM 1228 CB LEU A 163 21.210 -45.090 68.539 1.00 80.91 C ANISOU 1228 CB LEU A 163 8365 12990 9389 50 289 1967 C ATOM 1229 CG LEU A 163 20.323 -44.034 67.881 1.00 80.77 C ANISOU 1229 CG LEU A 163 8582 12840 9267 -118 264 2092 C ATOM 1230 CD1 LEU A 163 18.854 -44.358 68.094 1.00 78.51 C ANISOU 1230 CD1 LEU A 163 8535 12267 9027 13 142 2000 C ATOM 1231 CD2 LEU A 163 20.650 -42.640 68.401 1.00 81.82 C ANISOU 1231 CD2 LEU A 163 8747 12894 9448 -413 196 2281 C ATOM 1232 N LEU A 164 23.449 -47.341 68.624 1.00 84.77 N ANISOU 1232 N LEU A 164 8292 13985 9933 514 456 1706 N ATOM 1233 CA LEU A 164 24.160 -48.361 69.391 1.00 85.47 C ANISOU 1233 CA LEU A 164 8209 14115 10150 754 393 1583 C ATOM 1234 C LEU A 164 25.660 -48.350 69.146 1.00 88.90 C ANISOU 1234 C LEU A 164 8230 14964 10584 783 523 1603 C ATOM 1235 O LEU A 164 26.436 -48.359 70.093 1.00 89.76 O ANISOU 1235 O LEU A 164 8130 15129 10844 774 417 1633 O ATOM 1236 CB LEU A 164 23.612 -49.759 69.099 1.00 85.12 C ANISOU 1236 CB LEU A 164 8336 13938 10067 1091 377 1372 C ATOM 1237 CG LEU A 164 22.290 -50.218 69.716 1.00 82.24 C ANISOU 1237 CG LEU A 164 8315 13173 9761 1119 206 1312 C ATOM 1238 CD1 LEU A 164 22.125 -51.697 69.443 1.00 83.06 C ANISOU 1238 CD1 LEU A 164 8541 13191 9826 1441 184 1106 C ATOM 1239 CD2 LEU A 164 22.223 -49.953 71.213 1.00 80.86 C ANISOU 1239 CD2 LEU A 164 8172 12791 9761 1005 27 1381 C ATOM 1240 N ASN A 165 26.063 -48.345 67.879 1.00 91.26 N ANISOU 1240 N ASN A 165 8400 15572 10702 818 752 1585 N ATOM 1241 CA ASN A 165 27.478 -48.402 67.533 1.00 95.20 C ANISOU 1241 CA ASN A 165 8458 16531 11181 867 922 1587 C ATOM 1242 C ASN A 165 28.219 -47.097 67.810 1.00 96.58 C ANISOU 1242 C ASN A 165 8393 16906 11396 455 936 1821 C ATOM 1243 O ASN A 165 29.345 -47.118 68.311 1.00 98.88 O ANISOU 1243 O ASN A 165 8302 17465 11804 450 927 1846 O ATOM 1244 CB ASN A 165 27.670 -48.821 66.069 1.00 97.85 C ANISOU 1244 CB ASN A 165 8743 17160 11275 1031 1195 1483 C ATOM 1245 CG ASN A 165 27.385 -50.295 65.832 1.00 97.99 C ANISOU 1245 CG ASN A 165 8901 17066 11263 1494 1187 1215 C ATOM 1246 OD1 ASN A 165 27.124 -51.049 66.767 1.00 96.11 O ANISOU 1246 OD1 ASN A 165 8775 16548 11193 1691 979 1117 O ATOM 1247 ND2 ASN A 165 27.440 -50.709 64.568 1.00100.96 N ANISOU 1247 ND2 ASN A 165 9306 17651 11405 1656 1410 1096 N ATOM 1248 N ASP A 166 27.575 -45.970 67.502 1.00 95.34 N ANISOU 1248 N ASP A 166 8474 16605 11146 109 931 1994 N ATOM 1249 CA ASP A 166 28.249 -44.668 67.505 1.00 97.33 C ANISOU 1249 CA ASP A 166 8562 17039 11380 -327 964 2229 C ATOM 1250 C ASP A 166 27.738 -43.683 68.555 1.00 94.90 C ANISOU 1250 C ASP A 166 8495 16362 11202 -618 717 2374 C ATOM 1251 O ASP A 166 28.496 -43.230 69.413 1.00 96.02 O ANISOU 1251 O ASP A 166 8440 16568 11476 -812 603 2466 O ATOM 1252 CB ASP A 166 28.167 -44.021 66.114 1.00 99.25 C ANISOU 1252 CB ASP A 166 8877 17474 11358 -531 1187 2342 C ATOM 1253 CG ASP A 166 28.770 -44.889 65.020 1.00102.43 C ANISOU 1253 CG ASP A 166 9038 18292 11589 -270 1469 2199 C ATOM 1254 OD1 ASP A 166 29.717 -45.654 65.308 1.00104.53 O ANISOU 1254 OD1 ASP A 166 8922 18840 11954 -34 1531 2077 O ATOM 1255 OD2 ASP A 166 28.296 -44.796 63.866 1.00103.03 O ANISOU 1255 OD2 ASP A 166 9314 18410 11421 -287 1622 2204 O ATOM 1256 N THR A 167 26.453 -43.354 68.476 1.00 91.91 N ANISOU 1256 N THR A 167 8539 15606 10778 -639 628 2384 N ATOM 1257 CA THR A 167 25.867 -42.279 69.277 1.00 90.08 C ANISOU 1257 CA THR A 167 8581 15023 10624 -904 429 2515 C ATOM 1258 C THR A 167 25.920 -42.527 70.782 1.00 88.26 C ANISOU 1258 C THR A 167 8346 14586 10601 -846 216 2456 C ATOM 1259 O THR A 167 26.099 -41.585 71.554 1.00 88.44 O ANISOU 1259 O THR A 167 8440 14471 10692 -1123 72 2579 O ATOM 1260 CB THR A 167 24.417 -41.994 68.843 1.00 87.71 C ANISOU 1260 CB THR A 167 8697 14389 10239 -860 384 2508 C ATOM 1261 OG1 THR A 167 24.380 -41.804 67.422 1.00 89.92 O ANISOU 1261 OG1 THR A 167 9007 14859 10300 -912 561 2567 O ATOM 1262 CG2 THR A 167 23.866 -40.748 69.530 1.00 86.82 C ANISOU 1262 CG2 THR A 167 8867 13936 10183 -1118 203 2644 C ATOM 1263 N CYS A 168 25.772 -43.786 71.192 1.00 86.77 N ANISOU 1263 N CYS A 168 8112 14361 10495 -499 184 2270 N ATOM 1264 CA CYS A 168 25.784 -44.131 72.617 1.00 85.17 C ANISOU 1264 CA CYS A 168 7944 13956 10460 -430 -23 2214 C ATOM 1265 C CYS A 168 27.126 -43.801 73.285 1.00 87.04 C ANISOU 1265 C CYS A 168 7854 14422 10795 -604 -103 2303 C ATOM 1266 O CYS A 168 27.167 -42.934 74.157 1.00 86.73 O ANISOU 1266 O CYS A 168 7926 14213 10814 -867 -266 2407 O ATOM 1267 CB CYS A 168 25.379 -45.594 72.857 1.00 83.95 C ANISOU 1267 CB CYS A 168 7840 13706 10353 -40 -50 2013 C ATOM 1268 SG CYS A 168 24.854 -45.965 74.561 1.00 83.25 S ANISOU 1268 SG CYS A 168 7978 13246 10407 16 -306 1956 S ATOM 1269 N PRO A 169 28.226 -44.464 72.869 1.00 89.27 N ANISOU 1269 N PRO A 169 7729 15099 11090 -458 4 2258 N ATOM 1270 CA PRO A 169 29.495 -44.155 73.526 1.00 91.71 C ANISOU 1270 CA PRO A 169 7681 15657 11508 -628 -96 2347 C ATOM 1271 C PRO A 169 29.940 -42.706 73.315 1.00 93.15 C ANISOU 1271 C PRO A 169 7810 15946 11637 -1120 -80 2568 C ATOM 1272 O PRO A 169 30.557 -42.123 74.208 1.00 94.44 O ANISOU 1272 O PRO A 169 7879 16109 11895 -1374 -264 2667 O ATOM 1273 CB PRO A 169 30.482 -45.127 72.865 1.00 94.80 C ANISOU 1273 CB PRO A 169 7625 16492 11901 -335 68 2242 C ATOM 1274 CG PRO A 169 29.631 -46.219 72.314 1.00 92.97 C ANISOU 1274 CG PRO A 169 7618 16106 11601 63 161 2052 C ATOM 1275 CD PRO A 169 28.390 -45.530 71.865 1.00 90.37 C ANISOU 1275 CD PRO A 169 7708 15478 11152 -117 202 2111 C ATOM 1276 N LEU A 170 29.611 -42.127 72.161 1.00 92.91 N ANISOU 1276 N LEU A 170 7878 15981 11441 -1270 114 2649 N ATOM 1277 CA LEU A 170 30.021 -40.757 71.847 1.00 94.50 C ANISOU 1277 CA LEU A 170 8076 16265 11564 -1760 132 2877 C ATOM 1278 C LEU A 170 29.216 -39.716 72.617 1.00 91.74 C ANISOU 1278 C LEU A 170 8185 15436 11237 -2010 -89 2969 C ATOM 1279 O LEU A 170 29.549 -38.532 72.620 1.00 93.65 O ANISOU 1279 O LEU A 170 8497 15650 11436 -2434 -150 3157 O ATOM 1280 CB LEU A 170 29.987 -40.497 70.335 1.00 96.25 C ANISOU 1280 CB LEU A 170 8275 16722 11574 -1845 406 2949 C ATOM 1281 CG LEU A 170 31.308 -40.779 69.597 1.00101.04 C ANISOU 1281 CG LEU A 170 8335 17933 12123 -1890 640 2979 C ATOM 1282 CD1 LEU A 170 31.593 -42.281 69.418 1.00101.33 C ANISOU 1282 CD1 LEU A 170 8085 18209 12206 -1365 760 2738 C ATOM 1283 CD2 LEU A 170 31.355 -40.059 68.248 1.00103.58 C ANISOU 1283 CD2 LEU A 170 8699 18459 12197 -2170 881 3134 C ATOM 1284 N PHE A 171 28.160 -40.173 73.275 1.00 87.42 N ANISOU 1284 N PHE A 171 7955 14510 10749 -1747 -206 2830 N ATOM 1285 CA PHE A 171 27.408 -39.339 74.192 1.00 84.94 C ANISOU 1285 CA PHE A 171 8049 13755 10471 -1902 -413 2868 C ATOM 1286 C PHE A 171 27.969 -39.535 75.592 1.00 84.79 C ANISOU 1286 C PHE A 171 7941 13682 10592 -1926 -631 2832 C ATOM 1287 O PHE A 171 28.325 -38.565 76.260 1.00 86.15 O ANISOU 1287 O PHE A 171 8213 13735 10784 -2259 -799 2945 O ATOM 1288 CB PHE A 171 25.919 -39.702 74.149 1.00 81.28 C ANISOU 1288 CB PHE A 171 7951 12950 9982 -1618 -403 2739 C ATOM 1289 CG PHE A 171 25.050 -38.846 75.030 1.00 79.45 C ANISOU 1289 CG PHE A 171 8132 12282 9772 -1726 -579 2753 C ATOM 1290 CD1 PHE A 171 25.059 -37.458 74.911 1.00 80.81 C ANISOU 1290 CD1 PHE A 171 8524 12298 9883 -2063 -650 2913 C ATOM 1291 CD2 PHE A 171 24.206 -39.429 75.965 1.00 76.71 C ANISOU 1291 CD2 PHE A 171 7975 11678 9495 -1487 -666 2602 C ATOM 1292 CE1 PHE A 171 24.247 -36.663 75.720 1.00 79.51 C ANISOU 1292 CE1 PHE A 171 8762 11718 9732 -2115 -809 2900 C ATOM 1293 CE2 PHE A 171 23.388 -38.643 76.778 1.00 75.56 C ANISOU 1293 CE2 PHE A 171 8197 11159 9353 -1557 -797 2594 C ATOM 1294 CZ PHE A 171 23.411 -37.258 76.655 1.00 77.01 C ANISOU 1294 CZ PHE A 171 8598 11182 9482 -1848 -869 2731 C ATOM 1295 N VAL A 172 28.064 -40.802 76.002 1.00 83.21 N ANISOU 1295 N VAL A 172 7579 13561 10476 -1579 -644 2676 N ATOM 1296 CA VAL A 172 28.451 -41.212 77.361 1.00 82.45 C ANISOU 1296 CA VAL A 172 7448 13381 10498 -1525 -870 2621 C ATOM 1297 C VAL A 172 29.904 -40.879 77.728 1.00 85.70 C ANISOU 1297 C VAL A 172 7474 14106 10983 -1777 -986 2733 C ATOM 1298 O VAL A 172 30.190 -40.542 78.879 1.00 86.16 O ANISOU 1298 O VAL A 172 7615 14021 11099 -1937 -1229 2763 O ATOM 1299 CB VAL A 172 28.175 -42.722 77.582 1.00 80.89 C ANISOU 1299 CB VAL A 172 7204 13177 10354 -1077 -859 2439 C ATOM 1300 CG1 VAL A 172 28.382 -43.111 79.036 1.00 80.52 C ANISOU 1300 CG1 VAL A 172 7228 12970 10397 -1027 -1114 2394 C ATOM 1301 CG2 VAL A 172 26.765 -43.051 77.166 1.00 77.57 C ANISOU 1301 CG2 VAL A 172 7125 12487 9862 -877 -748 2339 C ATOM 1302 N ARG A 173 30.815 -40.977 76.761 1.00 87.93 N ANISOU 1302 N ARG A 173 7326 14832 11251 -1820 -814 2792 N ATOM 1303 CA ARG A 173 32.169 -40.450 76.939 1.00 91.41 C ANISOU 1303 CA ARG A 173 7361 15622 11750 -2143 -897 2931 C ATOM 1304 C ARG A 173 32.095 -38.945 77.216 1.00 91.68 C ANISOU 1304 C ARG A 173 7674 15435 11727 -2662 -1024 3110 C ATOM 1305 O ARG A 173 32.924 -38.400 77.946 1.00 94.17 O ANISOU 1305 O ARG A 173 7851 15825 12105 -2976 -1232 3211 O ATOM 1306 CB ARG A 173 33.040 -40.730 75.709 1.00 94.76 C ANISOU 1306 CB ARG A 173 7283 16586 12134 -2118 -627 2964 C ATOM 1307 CG ARG A 173 33.541 -42.169 75.582 1.00 95.57 C ANISOU 1307 CG ARG A 173 7005 16987 12321 -1627 -551 2790 C ATOM 1308 CD ARG A 173 34.806 -42.410 76.403 1.00 99.18 C ANISOU 1308 CD ARG A 173 6998 17746 12938 -1652 -751 2813 C ATOM 1309 N GLY A 174 31.089 -38.292 76.633 1.00 89.09 N ANISOU 1309 N GLY A 174 7755 14820 11277 -2739 -922 3145 N ATOM 1310 CA GLY A 174 30.782 -36.894 76.914 1.00 88.87 C ANISOU 1310 CA GLY A 174 8117 14465 11183 -3153 -1062 3286 C ATOM 1311 C GLY A 174 30.231 -36.689 78.314 1.00 86.57 C ANISOU 1311 C GLY A 174 8211 13738 10943 -3132 -1328 3207 C ATOM 1312 O GLY A 174 30.867 -36.029 79.135 1.00 88.73 O ANISOU 1312 O GLY A 174 8506 13960 11249 -3456 -1556 3290 O ATOM 1313 N LEU A 175 29.059 -37.266 78.590 1.00 82.51 N ANISOU 1313 N LEU A 175 7998 12928 10424 -2766 -1299 3046 N ATOM 1314 CA LEU A 175 28.389 -37.149 79.901 1.00 80.28 C ANISOU 1314 CA LEU A 175 8105 12240 10158 -2705 -1502 2949 C ATOM 1315 C LEU A 175 29.312 -37.337 81.104 1.00 81.99 C ANISOU 1315 C LEU A 175 8172 12527 10452 -2818 -1752 2949 C ATOM 1316 O LEU A 175 29.173 -36.636 82.104 1.00 82.32 O ANISOU 1316 O LEU A 175 8540 12272 10465 -3011 -1963 2954 O ATOM 1317 CB LEU A 175 27.217 -38.135 80.023 1.00 76.52 C ANISOU 1317 CB LEU A 175 7805 11585 9684 -2263 -1403 2766 C ATOM 1318 CG LEU A 175 25.763 -37.739 79.728 1.00 73.48 C ANISOU 1318 CG LEU A 175 7833 10861 9224 -2138 -1308 2708 C ATOM 1319 CD1 LEU A 175 24.841 -38.904 80.040 1.00 69.68 C ANISOU 1319 CD1 LEU A 175 7424 10286 8764 -1748 -1241 2532 C ATOM 1320 CD2 LEU A 175 25.325 -36.521 80.513 1.00 73.46 C ANISOU 1320 CD2 LEU A 175 8260 10479 9171 -2357 -1470 2734 C ATOM 1321 N LEU A 176 30.237 -38.290 81.000 1.00 83.32 N ANISOU 1321 N LEU A 176 7864 13083 10711 -2676 -1738 2933 N ATOM 1322 CA LEU A 176 31.197 -38.586 82.067 1.00 85.40 C ANISOU 1322 CA LEU A 176 7921 13468 11061 -2745 -1998 2939 C ATOM 1323 C LEU A 176 32.203 -37.468 82.273 1.00 89.27 C ANISOU 1323 C LEU A 176 8286 14077 11555 -3257 -2174 3112 C ATOM 1324 O LEU A 176 32.528 -37.121 83.409 1.00 90.45 O ANISOU 1324 O LEU A 176 8578 14075 11713 -3448 -2461 3126 O ATOM 1325 CB LEU A 176 31.935 -39.897 81.782 1.00 86.35 C ANISOU 1325 CB LEU A 176 7537 13987 11285 -2414 -1936 2874 C ATOM 1326 CG LEU A 176 31.241 -41.182 82.236 1.00 83.50 C ANISOU 1326 CG LEU A 176 7326 13457 10944 -1943 -1938 2699 C ATOM 1327 CD1 LEU A 176 31.746 -42.379 81.449 1.00 84.25 C ANISOU 1327 CD1 LEU A 176 6988 13913 11110 -1577 -1782 2626 C ATOM 1328 CD2 LEU A 176 31.425 -41.399 83.734 1.00 83.82 C ANISOU 1328 CD2 LEU A 176 7533 13305 11008 -1951 -2257 2668 C ATOM 1329 N GLU A 177 32.692 -36.913 81.166 1.00 91.59 N ANISOU 1329 N GLU A 177 8329 14645 11826 -3502 -2007 3248 N ATOM 1330 CA GLU A 177 33.649 -35.811 81.202 1.00 95.89 C ANISOU 1330 CA GLU A 177 8743 15327 12364 -4053 -2151 3440 C ATOM 1331 C GLU A 177 32.981 -34.489 81.587 1.00 95.58 C ANISOU 1331 C GLU A 177 9316 14787 12213 -4389 -2291 3502 C ATOM 1332 O GLU A 177 33.661 -33.544 82.001 1.00 99.04 O ANISOU 1332 O GLU A 177 9797 15196 12636 -4865 -2510 3637 O ATOM 1333 CB GLU A 177 34.370 -35.674 79.855 1.00 98.67 C ANISOU 1333 CB GLU A 177 8637 16154 12701 -4225 -1897 3575 C ATOM 1334 N ALA A 178 31.655 -34.436 81.458 1.00 91.82 N ANISOU 1334 N ALA A 178 9309 13918 11659 -4133 -2179 3398 N ATOM 1335 CA ALA A 178 30.885 -33.229 81.752 1.00 91.39 C ANISOU 1335 CA ALA A 178 9860 13366 11498 -4350 -2288 3425 C ATOM 1336 C ALA A 178 30.312 -33.223 83.165 1.00 89.90 C ANISOU 1336 C ALA A 178 10088 12778 11291 -4229 -2507 3277 C ATOM 1337 O ALA A 178 30.015 -32.163 83.713 1.00 90.80 O ANISOU 1337 O ALA A 178 10671 12507 11322 -4471 -2678 3294 O ATOM 1338 CB ALA A 178 29.778 -33.054 80.735 1.00 88.89 C ANISOU 1338 CB ALA A 178 9795 12875 11104 -4151 -2046 3406 C ATOM 1339 N GLY A 179 30.160 -34.408 83.750 1.00 87.99 N ANISOU 1339 N GLY A 179 9705 12619 11110 -3856 -2500 3131 N ATOM 1340 CA GLY A 179 29.566 -34.541 85.078 1.00 86.86 C ANISOU 1340 CA GLY A 179 9953 12131 10919 -3718 -2670 2987 C ATOM 1341 C GLY A 179 30.477 -35.132 86.139 1.00 88.78 C ANISOU 1341 C GLY A 179 9986 12531 11214 -3755 -2923 2973 C ATOM 1342 O GLY A 179 29.998 -35.649 87.148 1.00 87.28 O ANISOU 1342 O GLY A 179 10038 12142 10981 -3546 -3017 2843 O ATOM 1343 N LYS A 180 31.790 -35.047 85.917 1.00 92.47 N ANISOU 1343 N LYS A 180 9999 13370 11766 -4032 -3039 3112 N ATOM 1344 CA LYS A 180 32.790 -35.521 86.878 1.00 95.00 C ANISOU 1344 CA LYS A 180 10066 13878 12150 -4099 -3327 3122 C ATOM 1345 C LYS A 180 32.660 -34.823 88.230 1.00 96.18 C ANISOU 1345 C LYS A 180 10716 13641 12186 -4331 -3643 3086 C ATOM 1346 O LYS A 180 33.032 -35.382 89.259 1.00 97.10 O ANISOU 1346 O LYS A 180 10816 13772 12305 -4260 -3880 3037 O ATOM 1347 CB LYS A 180 34.205 -35.325 86.325 1.00 99.13 C ANISOU 1347 CB LYS A 180 9994 14888 12783 -4418 -3391 3294 C ATOM 1348 N SER A 181 32.120 -33.608 88.219 1.00 96.68 N ANISOU 1348 N SER A 181 11254 13345 12136 -4591 -3654 3105 N ATOM 1349 CA SER A 181 31.963 -32.804 89.430 1.00 98.34 C ANISOU 1349 CA SER A 181 12004 13152 12209 -4826 -3940 3055 C ATOM 1350 C SER A 181 30.958 -33.435 90.398 1.00 95.56 C ANISOU 1350 C SER A 181 12045 12510 11754 -4444 -3920 2856 C ATOM 1351 O SER A 181 31.271 -33.646 91.572 1.00 96.72 O ANISOU 1351 O SER A 181 12336 12580 11832 -4491 -4183 2807 O ATOM 1352 CB SER A 181 31.553 -31.370 89.066 1.00 99.51 C ANISOU 1352 CB SER A 181 12598 12955 12258 -5139 -3935 3109 C ATOM 1353 OG SER A 181 32.147 -30.423 89.940 1.00103.17 O ANISOU 1353 OG SER A 181 13356 13211 12634 -5587 -4290 3155 O ATOM 1354 N ASP A 182 29.764 -33.745 89.893 1.00 92.26 N ANISOU 1354 N ASP A 182 11788 11953 11315 -4085 -3612 2750 N ATOM 1355 CA ASP A 182 28.720 -34.407 90.682 1.00 89.81 C ANISOU 1355 CA ASP A 182 11801 11417 10907 -3725 -3531 2570 C ATOM 1356 C ASP A 182 29.016 -35.893 90.914 1.00 88.38 C ANISOU 1356 C ASP A 182 11268 11510 10803 -3434 -3527 2542 C ATOM 1357 O ASP A 182 28.641 -36.448 91.944 1.00 87.58 O ANISOU 1357 O ASP A 182 11414 11261 10600 -3281 -3609 2439 O ATOM 1358 CB ASP A 182 27.350 -34.244 90.010 1.00 87.09 C ANISOU 1358 CB ASP A 182 11691 10870 10530 -3457 -3211 2476 C ATOM 1359 CG ASP A 182 26.190 -34.353 91.000 1.00 86.64 C ANISOU 1359 CG ASP A 182 12116 10486 10319 -3227 -3158 2289 C ATOM 1360 OD1 ASP A 182 25.833 -35.483 91.421 1.00 85.64 O ANISOU 1360 OD1 ASP A 182 11919 10439 10181 -2955 -3082 2208 O ATOM 1361 OD2 ASP A 182 25.624 -33.295 91.349 1.00 89.01 O ANISOU 1361 OD2 ASP A 182 12876 10445 10498 -3319 -3185 2220 O ATOM 1362 N LEU A 183 29.686 -36.523 89.954 1.00 88.38 N ANISOU 1362 N LEU A 183 10718 11896 10965 -3356 -3433 2633 N ATOM 1363 CA LEU A 183 30.002 -37.949 90.027 1.00 87.64 C ANISOU 1363 CA LEU A 183 10285 12055 10960 -3040 -3429 2604 C ATOM 1364 C LEU A 183 31.019 -38.311 91.108 1.00 90.65 C ANISOU 1364 C LEU A 183 10558 12539 11345 -3143 -3792 2640 C ATOM 1365 O LEU A 183 30.976 -39.417 91.659 1.00 90.15 O ANISOU 1365 O LEU A 183 10475 12497 11280 -2866 -3859 2581 O ATOM 1366 CB LEU A 183 30.486 -38.463 88.669 1.00 87.50 C ANISOU 1366 CB LEU A 183 9717 12429 11101 -2910 -3225 2672 C ATOM 1367 CG LEU A 183 29.443 -39.106 87.752 1.00 83.54 C ANISOU 1367 CG LEU A 183 9229 11903 10610 -2556 -2882 2585 C ATOM 1368 CD1 LEU A 183 29.858 -38.989 86.297 1.00 83.66 C ANISOU 1368 CD1 LEU A 183 8835 12235 10717 -2581 -2670 2671 C ATOM 1369 CD2 LEU A 183 29.232 -40.561 88.129 1.00 81.71 C ANISOU 1369 CD2 LEU A 183 8937 11706 10402 -2171 -2879 2487 C ATOM 1370 N GLU A 184 31.927 -37.388 91.411 1.00 94.06 N ANISOU 1370 N GLU A 184 10938 13023 11778 -3554 -4048 2745 N ATOM 1371 CA GLU A 184 32.974 -37.647 92.398 1.00 97.35 C ANISOU 1371 CA GLU A 184 11215 13568 12207 -3690 -4435 2795 C ATOM 1372 C GLU A 184 32.748 -36.911 93.726 1.00 98.66 C ANISOU 1372 C GLU A 184 11964 13354 12169 -3941 -4710 2746 C ATOM 1373 O GLU A 184 33.686 -36.729 94.512 1.00102.12 O ANISOU 1373 O GLU A 184 12342 13866 12592 -4194 -5082 2811 O ATOM 1374 CB GLU A 184 34.354 -37.330 91.813 1.00101.13 C ANISOU 1374 CB GLU A 184 11099 14476 12851 -3974 -4568 2955 C ATOM 1375 CG GLU A 184 34.714 -38.164 90.584 1.00100.71 C ANISOU 1375 CG GLU A 184 10436 14850 12980 -3693 -4307 2986 C ATOM 1376 CD GLU A 184 36.122 -37.895 90.078 1.00105.34 C ANISOU 1376 CD GLU A 184 10383 15922 13720 -3970 -4423 3139 C ATOM 1377 OE1 GLU A 184 37.075 -37.971 90.889 1.00109.05 O ANISOU 1377 OE1 GLU A 184 10655 16545 14233 -4123 -4786 3195 O ATOM 1378 OE2 GLU A 184 36.277 -37.617 88.867 1.00105.36 O ANISOU 1378 OE2 GLU A 184 10070 16172 13789 -4042 -4152 3207 O ATOM 1379 N LYS A 185 31.501 -36.502 93.970 1.00 96.11 N ANISOU 1379 N LYS A 185 12197 12639 11682 -3859 -4529 2623 N ATOM 1380 CA LYS A 185 31.125 -35.844 95.224 1.00 97.29 C ANISOU 1380 CA LYS A 185 12959 12405 11600 -4034 -4731 2537 C ATOM 1381 C LYS A 185 31.137 -36.860 96.373 1.00 97.47 C ANISOU 1381 C LYS A 185 13121 12398 11516 -3841 -4914 2477 C ATOM 1382 O LYS A 185 30.999 -38.064 96.147 1.00 95.63 O ANISOU 1382 O LYS A 185 12642 12329 11365 -3499 -4795 2466 O ATOM 1383 CB LYS A 185 29.763 -35.134 95.092 1.00 94.86 C ANISOU 1383 CB LYS A 185 13163 11724 11156 -3948 -4451 2407 C ATOM 1384 CG LYS A 185 28.556 -35.952 95.527 1.00 92.01 C ANISOU 1384 CG LYS A 185 13076 11204 10678 -3559 -4223 2253 C ATOM 1385 CD LYS A 185 27.254 -35.506 94.867 1.00 90.08 C ANISOU 1385 CD LYS A 185 13056 10762 10408 -3377 -3859 2153 C ATOM 1386 CE LYS A 185 26.110 -36.496 95.172 1.00 87.46 C ANISOU 1386 CE LYS A 185 12866 10370 9995 -3002 -3611 2022 C ATOM 1387 NZ LYS A 185 25.008 -36.475 94.152 1.00 84.67 N ANISOU 1387 NZ LYS A 185 12463 9994 9713 -2760 -3241 1965 N ATOM 1388 N GLN A 186 31.325 -36.372 97.596 1.00100.08 N ANISOU 1388 N GLN A 186 13874 12505 11648 -4072 -5220 2442 N ATOM 1389 CA GLN A 186 31.424 -37.242 98.770 1.00100.94 C ANISOU 1389 CA GLN A 186 14169 12570 11615 -3948 -5447 2407 C ATOM 1390 C GLN A 186 30.430 -36.822 99.848 1.00100.80 C ANISOU 1390 C GLN A 186 14882 12141 11278 -3964 -5414 2251 C ATOM 1391 O GLN A 186 30.447 -35.675 100.295 1.00103.04 O ANISOU 1391 O GLN A 186 15544 12189 11416 -4261 -5548 2207 O ATOM 1392 CB GLN A 186 32.852 -37.221 99.340 1.00105.20 C ANISOU 1392 CB GLN A 186 14457 13311 12202 -4222 -5933 2533 C ATOM 1393 CG GLN A 186 33.938 -37.748 98.404 1.00105.90 C ANISOU 1393 CG GLN A 186 13768 13870 12600 -4176 -5985 2678 C ATOM 1394 CD GLN A 186 33.782 -39.227 98.085 1.00103.42 C ANISOU 1394 CD GLN A 186 13156 13740 12400 -3700 -5838 2667 C ATOM 1395 OE1 GLN A 186 34.122 -40.096 98.891 1.00104.14 O ANISOU 1395 OE1 GLN A 186 13273 13855 12442 -3551 -6097 2678 O ATOM 1396 NE2 GLN A 186 33.274 -39.519 96.897 1.00100.66 N ANISOU 1396 NE2 GLN A 186 12550 13501 12194 -3464 -5440 2646 N ATOM 1397 N GLU A 187 29.569 -37.748 100.264 1.00 71.70 N ANISOU 1397 N GLU A 187 8747 7274 11223 -1522 -1713 1382 N ATOM 1398 CA GLU A 187 28.601 -37.468 101.329 1.00 71.40 C ANISOU 1398 CA GLU A 187 8882 6976 11270 -1404 -1770 1126 C ATOM 1399 C GLU A 187 28.788 -38.355 102.558 1.00 69.63 C ANISOU 1399 C GLU A 187 8852 6747 10856 -1322 -1788 733 C ATOM 1400 O GLU A 187 28.723 -39.584 102.461 1.00 67.82 O ANISOU 1400 O GLU A 187 8692 6782 10295 -1272 -1688 639 O ATOM 1401 CB GLU A 187 27.166 -37.572 100.810 1.00 70.86 C ANISOU 1401 CB GLU A 187 8827 7017 11078 -1319 -1689 1241 C ATOM 1402 CG GLU A 187 26.801 -36.531 99.757 1.00 73.86 C ANISOU 1402 CG GLU A 187 9014 7363 11688 -1377 -1702 1659 C ATOM 1403 CD GLU A 187 26.975 -35.091 100.235 1.00 77.09 C ANISOU 1403 CD GLU A 187 9384 7316 12591 -1378 -1794 1714 C ATOM 1404 OE1 GLU A 187 27.383 -34.238 99.411 1.00 79.29 O ANISOU 1404 OE1 GLU A 187 9482 7536 13110 -1484 -1823 2069 O ATOM 1405 OE2 GLU A 187 26.704 -34.811 101.425 1.00 77.36 O ANISOU 1405 OE2 GLU A 187 9585 7041 12766 -1281 -1826 1402 O ATOM 1406 N LYS A 188 29.017 -37.719 103.708 1.00 70.65 N ANISOU 1406 N LYS A 188 9086 6566 11190 -1320 -1916 509 N ATOM 1407 CA LYS A 188 29.289 -38.415 104.973 1.00 69.42 C ANISOU 1407 CA LYS A 188 9114 6402 10861 -1265 -1970 160 C ATOM 1408 C LYS A 188 28.045 -39.105 105.555 1.00 67.53 C ANISOU 1408 C LYS A 188 9071 6211 10375 -1096 -1862 -53 C ATOM 1409 O LYS A 188 26.984 -38.494 105.649 1.00 68.22 O ANISOU 1409 O LYS A 188 9209 6133 10578 -1014 -1813 -59 O ATOM 1410 CB LYS A 188 29.907 -37.449 105.997 1.00 71.81 C ANISOU 1410 CB LYS A 188 9491 6372 11422 -1359 -2160 -20 C ATOM 1411 CG LYS A 188 31.346 -37.033 105.676 1.00 73.39 C ANISOU 1411 CG LYS A 188 9487 6570 11829 -1558 -2301 155 C ATOM 1412 CD LYS A 188 31.939 -36.077 106.709 1.00 76.00 C ANISOU 1412 CD LYS A 188 9908 6567 12401 -1708 -2525 -43 C ATOM 1413 CE LYS A 188 33.464 -36.054 106.598 1.00 78.06 C ANISOU 1413 CE LYS A 188 9944 6929 12786 -1912 -2690 108 C ATOM 1414 NZ LYS A 188 34.106 -34.809 107.130 1.00 81.93 N ANISOU 1414 NZ LYS A 188 10440 7067 13622 -2150 -2924 46 N ATOM 1415 N PRO A 189 28.171 -40.393 105.929 1.00 65.52 N ANISOU 1415 N PRO A 189 8909 6180 9806 -1037 -1807 -199 N ATOM 1416 CA PRO A 189 27.043 -41.115 106.529 1.00 63.98 C ANISOU 1416 CA PRO A 189 8892 6038 9380 -897 -1702 -385 C ATOM 1417 C PRO A 189 26.826 -40.859 108.031 1.00 64.81 C ANISOU 1417 C PRO A 189 9210 5937 9479 -822 -1765 -697 C ATOM 1418 O PRO A 189 27.780 -40.799 108.810 1.00 65.78 O ANISOU 1418 O PRO A 189 9390 5999 9604 -883 -1906 -837 O ATOM 1419 CB PRO A 189 27.401 -42.586 106.291 1.00 61.94 C ANISOU 1419 CB PRO A 189 8651 6067 8818 -881 -1612 -394 C ATOM 1420 CG PRO A 189 28.868 -42.612 106.178 1.00 62.77 C ANISOU 1420 CG PRO A 189 8639 6213 8999 -965 -1698 -321 C ATOM 1421 CD PRO A 189 29.305 -41.285 105.627 1.00 64.80 C ANISOU 1421 CD PRO A 189 8729 6314 9577 -1085 -1799 -136 C ATOM 1422 N VAL A 190 25.562 -40.699 108.411 1.00 64.88 N ANISOU 1422 N VAL A 190 9324 5858 9468 -698 -1658 -788 N ATOM 1423 CA VAL A 190 25.149 -40.670 109.811 1.00 65.51 C ANISOU 1423 CA VAL A 190 9639 5799 9451 -597 -1645 -1095 C ATOM 1424 C VAL A 190 24.776 -42.119 110.174 1.00 63.43 C ANISOU 1424 C VAL A 190 9466 5796 8838 -519 -1544 -1171 C ATOM 1425 O VAL A 190 24.333 -42.883 109.309 1.00 61.89 O ANISOU 1425 O VAL A 190 9170 5808 8538 -518 -1443 -1004 O ATOM 1426 CB VAL A 190 23.906 -39.754 110.029 1.00 67.16 C ANISOU 1426 CB VAL A 190 9899 5773 9847 -467 -1521 -1130 C ATOM 1427 CG1 VAL A 190 23.997 -39.039 111.365 1.00 69.52 C ANISOU 1427 CG1 VAL A 190 10446 5785 10184 -429 -1555 -1458 C ATOM 1428 CG2 VAL A 190 23.731 -38.736 108.885 1.00 68.23 C ANISOU 1428 CG2 VAL A 190 9822 5779 10324 -507 -1523 -836 C ATOM 1429 N ALA A 191 24.949 -42.503 111.436 1.00 63.70 N ANISOU 1429 N ALA A 191 9700 5820 8682 -472 -1576 -1416 N ATOM 1430 CA ALA A 191 24.603 -43.862 111.864 1.00 61.89 C ANISOU 1430 CA ALA A 191 9565 5807 8145 -395 -1475 -1467 C ATOM 1431 C ALA A 191 23.904 -43.896 113.221 1.00 62.95 C ANISOU 1431 C ALA A 191 9931 5877 8111 -279 -1403 -1709 C ATOM 1432 O ALA A 191 24.135 -43.038 114.068 1.00 65.25 O ANISOU 1432 O ALA A 191 10364 5981 8447 -285 -1485 -1905 O ATOM 1433 CB ALA A 191 25.842 -44.763 111.863 1.00 60.94 C ANISOU 1433 CB ALA A 191 9410 5851 7895 -461 -1576 -1422 C ATOM 1434 N TRP A 192 23.033 -44.884 113.410 1.00 61.88 N ANISOU 1434 N TRP A 192 9844 5893 7774 -188 -1240 -1698 N ATOM 1435 CA TRP A 192 22.347 -45.090 114.689 1.00 62.94 C ANISOU 1435 CA TRP A 192 10190 6017 7706 -70 -1133 -1893 C ATOM 1436 C TRP A 192 22.011 -46.557 114.925 1.00 61.50 C ANISOU 1436 C TRP A 192 10051 6054 7261 -32 -1025 -1839 C ATOM 1437 O TRP A 192 21.774 -47.312 113.982 1.00 59.78 O ANISOU 1437 O TRP A 192 9702 5958 7052 -75 -962 -1662 O ATOM 1438 CB TRP A 192 21.104 -44.186 114.832 1.00 64.39 C ANISOU 1438 CB TRP A 192 10388 6038 8041 51 -961 -1941 C ATOM 1439 CG TRP A 192 19.942 -44.458 113.886 1.00 63.13 C ANISOU 1439 CG TRP A 192 10027 5975 7986 93 -801 -1711 C ATOM 1440 CD1 TRP A 192 18.755 -45.057 114.201 1.00 63.06 C ANISOU 1440 CD1 TRP A 192 10018 6077 7866 192 -603 -1677 C ATOM 1441 CD2 TRP A 192 19.848 -44.100 112.500 1.00 62.03 C ANISOU 1441 CD2 TRP A 192 9646 5848 8075 14 -843 -1463 C ATOM 1442 NE1 TRP A 192 17.937 -45.110 113.098 1.00 61.87 N ANISOU 1442 NE1 TRP A 192 9629 6014 7864 163 -545 -1424 N ATOM 1443 CE2 TRP A 192 18.584 -44.527 112.042 1.00 61.54 C ANISOU 1443 CE2 TRP A 192 9448 5923 8012 55 -692 -1292 C ATOM 1444 CE3 TRP A 192 20.714 -43.473 111.599 1.00 61.78 C ANISOU 1444 CE3 TRP A 192 9490 5749 8235 -102 -997 -1346 C ATOM 1445 CZ2 TRP A 192 18.167 -44.346 110.724 1.00 61.35 C ANISOU 1445 CZ2 TRP A 192 9182 5986 8143 -26 -717 -1016 C ATOM 1446 CZ3 TRP A 192 20.297 -43.294 110.291 1.00 61.33 C ANISOU 1446 CZ3 TRP A 192 9204 5771 8327 -162 -990 -1070 C ATOM 1447 CH2 TRP A 192 19.037 -43.730 109.865 1.00 60.90 C ANISOU 1447 CH2 TRP A 192 9032 5869 8238 -129 -864 -912 C ATOM 1448 N LEU A 193 22.018 -46.952 116.194 1.00 62.63 N ANISOU 1448 N LEU A 193 10397 6240 7158 33 -1007 -1993 N ATOM 1449 CA LEU A 193 21.720 -48.322 116.591 1.00 61.73 C ANISOU 1449 CA LEU A 193 10348 6305 6802 75 -901 -1933 C ATOM 1450 C LEU A 193 20.286 -48.444 117.092 1.00 62.38 C ANISOU 1450 C LEU A 193 10492 6407 6801 186 -663 -1962 C ATOM 1451 O LEU A 193 19.673 -47.452 117.494 1.00 64.27 O ANISOU 1451 O LEU A 193 10782 6521 7115 268 -580 -2084 O ATOM 1452 CB LEU A 193 22.682 -48.771 117.695 1.00 62.99 C ANISOU 1452 CB LEU A 193 10670 6540 6724 73 -1040 -2020 C ATOM 1453 CG LEU A 193 24.188 -48.533 117.533 1.00 63.52 C ANISOU 1453 CG LEU A 193 10669 6602 6863 -31 -1301 -1996 C ATOM 1454 CD1 LEU A 193 24.913 -48.760 118.850 1.00 65.29 C ANISOU 1454 CD1 LEU A 193 11062 6919 6828 -35 -1458 -2089 C ATOM 1455 CD2 LEU A 193 24.768 -49.417 116.438 1.00 62.12 C ANISOU 1455 CD2 LEU A 193 10306 6505 6791 -68 -1295 -1776 C ATOM 1456 N SER A 194 19.757 -49.664 117.059 1.00 61.24 N ANISOU 1456 N SER A 194 10337 6405 6525 191 -535 -1842 N ATOM 1457 CA SER A 194 18.461 -49.990 117.658 1.00 62.13 C ANISOU 1457 CA SER A 194 10494 6578 6534 283 -304 -1832 C ATOM 1458 C SER A 194 18.312 -51.505 117.724 1.00 61.12 C ANISOU 1458 C SER A 194 10391 6590 6242 241 -226 -1699 C ATOM 1459 O SER A 194 19.238 -52.241 117.370 1.00 60.13 O ANISOU 1459 O SER A 194 10271 6488 6086 170 -338 -1638 O ATOM 1460 CB SER A 194 17.298 -49.374 116.868 1.00 62.32 C ANISOU 1460 CB SER A 194 10321 6563 6796 301 -175 -1732 C ATOM 1461 OG SER A 194 17.028 -50.103 115.678 1.00 60.99 O ANISOU 1461 OG SER A 194 9975 6488 6710 168 -185 -1531 O ATOM 1462 N SER A 195 17.146 -51.969 118.163 1.00 61.74 N ANISOU 1462 N SER A 195 10474 6743 6240 290 -16 -1640 N ATOM 1463 CA SER A 195 16.921 -53.395 118.338 1.00 61.12 C ANISOU 1463 CA SER A 195 10439 6764 6021 241 75 -1510 C ATOM 1464 C SER A 195 15.455 -53.784 118.283 1.00 61.68 C ANISOU 1464 C SER A 195 10401 6909 6125 226 294 -1381 C ATOM 1465 O SER A 195 14.569 -53.010 118.653 1.00 63.07 O ANISOU 1465 O SER A 195 10519 7093 6350 329 431 -1407 O ATOM 1466 CB SER A 195 17.524 -53.863 119.661 1.00 62.50 C ANISOU 1466 CB SER A 195 10834 6992 5920 325 62 -1568 C ATOM 1467 OG SER A 195 16.929 -53.176 120.747 1.00 64.87 O ANISOU 1467 OG SER A 195 11247 7321 6078 452 184 -1691 O ATOM 1468 N VAL A 196 15.224 -55.009 117.823 1.00 60.93 N ANISOU 1468 N VAL A 196 10278 6857 6017 92 337 -1237 N ATOM 1469 CA VAL A 196 13.892 -55.597 117.738 1.00 61.69 C ANISOU 1469 CA VAL A 196 10258 7037 6145 17 516 -1081 C ATOM 1470 C VAL A 196 13.956 -57.039 118.244 1.00 61.93 C ANISOU 1470 C VAL A 196 10427 7082 6023 -43 600 -988 C ATOM 1471 O VAL A 196 15.050 -57.592 118.358 1.00 61.21 O ANISOU 1471 O VAL A 196 10484 6924 5848 -35 505 -1022 O ATOM 1472 CB VAL A 196 13.348 -55.558 116.283 1.00 60.89 C ANISOU 1472 CB VAL A 196 9934 6955 6246 -175 454 -972 C ATOM 1473 CG1 VAL A 196 13.072 -54.117 115.841 1.00 60.97 C ANISOU 1473 CG1 VAL A 196 9771 6955 6440 -95 403 -993 C ATOM 1474 CG2 VAL A 196 14.307 -56.245 115.322 1.00 59.19 C ANISOU 1474 CG2 VAL A 196 9787 6672 6030 -331 311 -993 C ATOM 1475 N PRO A 197 12.796 -57.648 118.568 1.00 63.32 N ANISOU 1475 N PRO A 197 10536 7337 6184 -97 787 -841 N ATOM 1476 CA PRO A 197 12.778 -59.085 118.871 1.00 63.96 C ANISOU 1476 CA PRO A 197 10733 7394 6174 -197 871 -717 C ATOM 1477 C PRO A 197 13.141 -59.936 117.655 1.00 62.74 C ANISOU 1477 C PRO A 197 10583 7126 6130 -421 774 -694 C ATOM 1478 O PRO A 197 12.890 -59.539 116.516 1.00 61.68 O ANISOU 1478 O PRO A 197 10304 7001 6131 -560 682 -714 O ATOM 1479 CB PRO A 197 11.321 -59.349 119.266 1.00 65.90 C ANISOU 1479 CB PRO A 197 10839 7757 6442 -245 1084 -548 C ATOM 1480 CG PRO A 197 10.797 -58.032 119.688 1.00 66.80 C ANISOU 1480 CG PRO A 197 10840 7962 6578 -59 1159 -612 C ATOM 1481 CD PRO A 197 11.484 -57.026 118.821 1.00 64.87 C ANISOU 1481 CD PRO A 197 10548 7642 6458 -41 954 -762 C ATOM 1482 N SER A 198 13.737 -61.095 117.906 1.00 63.27 N ANISOU 1482 N SER A 198 10828 7081 6131 -448 806 -648 N ATOM 1483 CA SER A 198 14.079 -62.024 116.835 1.00 63.13 C ANISOU 1483 CA SER A 198 10870 6910 6206 -647 774 -652 C ATOM 1484 C SER A 198 12.937 -62.992 116.568 1.00 65.02 C ANISOU 1484 C SER A 198 11076 7128 6502 -898 897 -523 C ATOM 1485 O SER A 198 12.105 -63.229 117.442 1.00 66.64 O ANISOU 1485 O SER A 198 11242 7414 6666 -879 1033 -384 O ATOM 1486 CB SER A 198 15.339 -62.804 117.193 1.00 63.03 C ANISOU 1486 CB SER A 198 11061 6743 6144 -531 770 -653 C ATOM 1487 OG SER A 198 15.574 -63.833 116.255 1.00 62.70 O ANISOU 1487 OG SER A 198 11115 6512 6198 -706 811 -663 O ATOM 1488 N SER A 199 12.905 -63.554 115.361 1.00 65.38 N ANISOU 1488 N SER A 199 11144 7068 6628 -1150 852 -570 N ATOM 1489 CA SER A 199 11.942 -64.605 115.022 1.00 67.83 C ANISOU 1489 CA SER A 199 11463 7318 6992 -1452 940 -471 C ATOM 1490 C SER A 199 12.003 -65.712 116.059 1.00 69.55 C ANISOU 1490 C SER A 199 11850 7393 7184 -1392 1111 -343 C ATOM 1491 O SER A 199 10.988 -66.328 116.370 1.00 71.75 O ANISOU 1491 O SER A 199 12077 7686 7499 -1562 1220 -188 O ATOM 1492 CB SER A 199 12.229 -65.204 113.637 1.00 68.13 C ANISOU 1492 CB SER A 199 11615 7206 7067 -1725 876 -602 C ATOM 1493 OG SER A 199 12.405 -64.201 112.647 1.00 67.37 O ANISOU 1493 OG SER A 199 11390 7242 6966 -1759 712 -707 O ATOM 1494 N ALA A 200 13.205 -65.947 116.586 1.00 69.20 N ANISOU 1494 N ALA A 200 11982 7221 7088 -1154 1126 -373 N ATOM 1495 CA ALA A 200 13.461 -66.983 117.583 1.00 71.22 C ANISOU 1495 CA ALA A 200 12404 7336 7319 -1056 1273 -213 C ATOM 1496 C ALA A 200 13.164 -66.519 119.002 1.00 72.13 C ANISOU 1496 C ALA A 200 12461 7661 7286 -838 1330 -72 C ATOM 1497 O ALA A 200 13.407 -65.364 119.360 1.00 71.10 O ANISOU 1497 O ALA A 200 12247 7716 7052 -651 1237 -159 O ATOM 1498 CB ALA A 200 14.894 -67.459 117.485 1.00 70.73 C ANISOU 1498 CB ALA A 200 12526 7066 7283 -890 1258 -263 C ATOM 1499 N HIS A 201 12.639 -67.436 119.805 1.00 74.82 N ANISOU 1499 N HIS A 201 12864 7955 7608 -874 1496 142 N ATOM 1500 CA HIS A 201 12.360 -67.185 121.214 1.00 76.44 C ANISOU 1500 CA HIS A 201 13056 8361 7628 -678 1592 300 C ATOM 1501 C HIS A 201 13.647 -66.902 121.994 1.00 76.21 C ANISOU 1501 C HIS A 201 13159 8367 7430 -385 1497 283 C ATOM 1502 O HIS A 201 14.658 -67.585 121.807 1.00 76.25 O ANISOU 1502 O HIS A 201 13295 8174 7502 -332 1455 312 O ATOM 1503 CB HIS A 201 11.615 -68.384 121.807 1.00 79.34 C ANISOU 1503 CB HIS A 201 13472 8644 8028 -806 1797 572 C ATOM 1504 CG HIS A 201 11.636 -68.436 123.300 1.00 81.23 C ANISOU 1504 CG HIS A 201 13774 9049 8041 -588 1913 775 C ATOM 1505 ND1 HIS A 201 12.407 -69.338 123.999 1.00 82.93 N ANISOU 1505 ND1 HIS A 201 14175 9136 8199 -470 1953 965 N ATOM 1506 CD2 HIS A 201 10.985 -67.696 124.228 1.00 82.45 C ANISOU 1506 CD2 HIS A 201 13839 9495 7994 -462 2008 826 C ATOM 1507 CE1 HIS A 201 12.228 -69.156 125.294 1.00 85.07 C ANISOU 1507 CE1 HIS A 201 14471 9642 8211 -303 2043 1132 C ATOM 1508 NE2 HIS A 201 11.370 -68.165 125.460 1.00 84.98 N ANISOU 1508 NE2 HIS A 201 14310 9882 8098 -295 2092 1030 N ATOM 1509 N GLY A 202 13.604 -65.881 122.849 1.00 76.40 N ANISOU 1509 N GLY A 202 13144 8642 7241 -202 1467 235 N ATOM 1510 CA GLY A 202 14.737 -65.534 123.711 1.00 76.83 C ANISOU 1510 CA GLY A 202 13320 8787 7086 35 1345 223 C ATOM 1511 C GLY A 202 15.901 -64.868 122.998 1.00 74.74 C ANISOU 1511 C GLY A 202 13042 8462 6894 99 1114 19 C ATOM 1512 O GLY A 202 16.887 -64.487 123.634 1.00 75.00 O ANISOU 1512 O GLY A 202 13141 8584 6771 263 968 3 O ATOM 1513 N HIS A 203 15.793 -64.739 121.678 1.00 73.02 N ANISOU 1513 N HIS A 203 12732 8113 6901 -50 1072 -120 N ATOM 1514 CA HIS A 203 16.808 -64.065 120.870 1.00 71.11 C ANISOU 1514 CA HIS A 203 12450 7822 6745 -10 880 -301 C ATOM 1515 C HIS A 203 16.348 -62.665 120.491 1.00 69.76 C ANISOU 1515 C HIS A 203 12139 7787 6578 -26 796 -494 C ATOM 1516 O HIS A 203 15.154 -62.372 120.492 1.00 70.21 O ANISOU 1516 O HIS A 203 12100 7931 6645 -105 904 -487 O ATOM 1517 CB HIS A 203 17.133 -64.878 119.611 1.00 70.27 C ANISOU 1517 CB HIS A 203 12365 7472 6861 -152 906 -323 C ATOM 1518 CG HIS A 203 18.099 -65.999 119.840 1.00 71.51 C ANISOU 1518 CG HIS A 203 12657 7442 7072 -54 953 -175 C ATOM 1519 ND1 HIS A 203 18.192 -66.676 121.039 1.00 73.87 N ANISOU 1519 ND1 HIS A 203 13048 7761 7257 68 1024 55 N ATOM 1520 CD2 HIS A 203 18.998 -66.581 119.012 1.00 71.46 C ANISOU 1520 CD2 HIS A 203 12703 7217 7233 -45 964 -199 C ATOM 1521 CE1 HIS A 203 19.119 -67.612 120.944 1.00 75.04 C ANISOU 1521 CE1 HIS A 203 13281 7701 7528 158 1062 186 C ATOM 1522 NE2 HIS A 203 19.620 -67.579 119.722 1.00 73.73 N ANISOU 1522 NE2 HIS A 203 13096 7377 7541 100 1044 24 N ATOM 1523 N ARG A 204 17.305 -61.806 120.166 1.00 68.57 N ANISOU 1523 N ARG A 204 11959 7647 6448 52 610 -638 N ATOM 1524 CA ARG A 204 17.007 -60.448 119.748 1.00 67.61 C ANISOU 1524 CA ARG A 204 11713 7605 6372 47 523 -808 C ATOM 1525 C ARG A 204 17.808 -60.046 118.523 1.00 66.02 C ANISOU 1525 C ARG A 204 11431 7313 6339 -12 374 -910 C ATOM 1526 O ARG A 204 18.836 -60.649 118.217 1.00 65.94 O ANISOU 1526 O ARG A 204 11475 7205 6376 8 323 -876 O ATOM 1527 CB ARG A 204 17.285 -59.473 120.884 1.00 68.59 C ANISOU 1527 CB ARG A 204 11898 7860 6303 212 450 -901 C ATOM 1528 CG ARG A 204 16.099 -59.239 121.770 1.00 70.25 C ANISOU 1528 CG ARG A 204 12124 8195 6373 260 635 -880 C ATOM 1529 CD ARG A 204 16.047 -57.790 122.160 1.00 70.49 C ANISOU 1529 CD ARG A 204 12155 8288 6340 366 584 -1080 C ATOM 1530 NE ARG A 204 14.701 -57.257 121.989 1.00 70.97 N ANISOU 1530 NE ARG A 204 12081 8386 6499 365 771 -1084 N ATOM 1531 CZ ARG A 204 14.436 -56.011 121.618 1.00 70.66 C ANISOU 1531 CZ ARG A 204 11943 8314 6589 411 748 -1225 C ATOM 1532 NH1 ARG A 204 15.424 -55.166 121.375 1.00 69.33 N ANISOU 1532 NH1 ARG A 204 11815 8067 6461 435 540 -1390 N ATOM 1533 NH2 ARG A 204 13.181 -55.611 121.484 1.00 72.37 N ANISOU 1533 NH2 ARG A 204 12002 8571 6924 434 939 -1173 N ATOM 1534 N GLN A 205 17.335 -59.012 117.833 1.00 65.29 N ANISOU 1534 N GLN A 205 11201 7260 6347 -69 324 -1010 N ATOM 1535 CA GLN A 205 17.988 -58.527 116.621 1.00 63.91 C ANISOU 1535 CA GLN A 205 10935 7027 6319 -139 194 -1083 C ATOM 1536 C GLN A 205 18.502 -57.108 116.817 1.00 63.44 C ANISOU 1536 C GLN A 205 10817 7006 6283 -37 40 -1201 C ATOM 1537 O GLN A 205 17.744 -56.208 117.166 1.00 63.97 O ANISOU 1537 O GLN A 205 10830 7124 6352 6 67 -1254 O ATOM 1538 CB GLN A 205 17.022 -58.596 115.435 1.00 63.50 C ANISOU 1538 CB GLN A 205 10761 6983 6382 -338 244 -1057 C ATOM 1539 CG GLN A 205 17.661 -58.373 114.074 1.00 62.75 C ANISOU 1539 CG GLN A 205 10605 6845 6392 -444 143 -1105 C ATOM 1540 CD GLN A 205 16.740 -58.751 112.923 1.00 63.53 C ANISOU 1540 CD GLN A 205 10630 6973 6534 -690 183 -1063 C ATOM 1541 OE1 GLN A 205 16.902 -59.808 112.313 1.00 64.15 O ANISOU 1541 OE1 GLN A 205 10821 6964 6590 -830 248 -1069 O ATOM 1542 NE2 GLN A 205 15.763 -57.891 112.625 1.00 63.62 N ANISOU 1542 NE2 GLN A 205 10458 7104 6610 -749 144 -1016 N ATOM 1543 N LEU A 206 19.801 -56.934 116.598 1.00 62.98 N ANISOU 1543 N LEU A 206 10764 6903 6261 1 -105 -1233 N ATOM 1544 CA LEU A 206 20.457 -55.632 116.676 1.00 62.91 C ANISOU 1544 CA LEU A 206 10699 6898 6305 53 -278 -1340 C ATOM 1545 C LEU A 206 20.540 -55.017 115.283 1.00 61.61 C ANISOU 1545 C LEU A 206 10379 6696 6335 -52 -334 -1345 C ATOM 1546 O LEU A 206 20.870 -55.704 114.312 1.00 60.78 O ANISOU 1546 O LEU A 206 10244 6563 6285 -138 -301 -1284 O ATOM 1547 CB LEU A 206 21.866 -55.785 117.262 1.00 63.68 C ANISOU 1547 CB LEU A 206 10852 7002 6343 132 -428 -1327 C ATOM 1548 CG LEU A 206 22.106 -55.872 118.777 1.00 65.77 C ANISOU 1548 CG LEU A 206 11260 7348 6381 235 -482 -1338 C ATOM 1549 CD1 LEU A 206 21.217 -56.895 119.463 1.00 66.90 C ANISOU 1549 CD1 LEU A 206 11519 7535 6366 270 -288 -1244 C ATOM 1550 CD2 LEU A 206 23.574 -56.170 119.066 1.00 66.43 C ANISOU 1550 CD2 LEU A 206 11330 7460 6452 279 -660 -1252 C ATOM 1551 N VAL A 207 20.234 -53.725 115.183 1.00 61.71 N ANISOU 1551 N VAL A 207 10307 6697 6444 -43 -401 -1415 N ATOM 1552 CA VAL A 207 20.211 -53.051 113.887 1.00 60.88 C ANISOU 1552 CA VAL A 207 10039 6571 6520 -142 -456 -1377 C ATOM 1553 C VAL A 207 21.157 -51.869 113.853 1.00 61.16 C ANISOU 1553 C VAL A 207 10021 6539 6678 -114 -628 -1438 C ATOM 1554 O VAL A 207 21.090 -50.987 114.708 1.00 62.33 O ANISOU 1554 O VAL A 207 10222 6632 6827 -36 -677 -1549 O ATOM 1555 CB VAL A 207 18.798 -52.562 113.496 1.00 60.96 C ANISOU 1555 CB VAL A 207 9934 6616 6613 -181 -368 -1325 C ATOM 1556 CG1 VAL A 207 18.829 -51.932 112.126 1.00 60.57 C ANISOU 1556 CG1 VAL A 207 9712 6575 6725 -294 -445 -1237 C ATOM 1557 CG2 VAL A 207 17.813 -53.710 113.490 1.00 61.13 C ANISOU 1557 CG2 VAL A 207 9979 6714 6533 -255 -217 -1245 C ATOM 1558 N CYS A 208 22.033 -51.860 112.855 1.00 60.64 N ANISOU 1558 N CYS A 208 9860 6470 6712 -190 -703 -1371 N ATOM 1559 CA CYS A 208 22.881 -50.707 112.589 1.00 61.17 C ANISOU 1559 CA CYS A 208 9830 6472 6941 -206 -863 -1384 C ATOM 1560 C CYS A 208 22.415 -50.014 111.318 1.00 60.69 C ANISOU 1560 C CYS A 208 9608 6411 7042 -299 -857 -1283 C ATOM 1561 O CYS A 208 22.509 -50.570 110.224 1.00 59.93 O ANISOU 1561 O CYS A 208 9449 6391 6931 -394 -807 -1180 O ATOM 1562 CB CYS A 208 24.345 -51.118 112.463 1.00 61.42 C ANISOU 1562 CB CYS A 208 9832 6521 6984 -211 -954 -1338 C ATOM 1563 SG CYS A 208 25.511 -49.738 112.444 1.00 62.80 S ANISOU 1563 SG CYS A 208 9884 6619 7358 -254 -1182 -1346 S ATOM 1564 N HIS A 209 21.907 -48.796 111.482 1.00 61.47 N ANISOU 1564 N HIS A 209 9654 6416 7285 -269 -898 -1308 N ATOM 1565 CA HIS A 209 21.401 -48.005 110.373 1.00 61.44 C ANISOU 1565 CA HIS A 209 9477 6407 7460 -338 -906 -1165 C ATOM 1566 C HIS A 209 22.508 -47.121 109.825 1.00 61.83 C ANISOU 1566 C HIS A 209 9426 6377 7688 -394 -1047 -1111 C ATOM 1567 O HIS A 209 23.251 -46.509 110.586 1.00 62.69 O ANISOU 1567 O HIS A 209 9593 6360 7867 -360 -1155 -1225 O ATOM 1568 CB HIS A 209 20.252 -47.124 110.842 1.00 62.58 C ANISOU 1568 CB HIS A 209 9596 6457 7723 -243 -844 -1183 C ATOM 1569 CG HIS A 209 19.183 -47.859 111.591 1.00 62.82 C ANISOU 1569 CG HIS A 209 9709 6559 7599 -169 -691 -1233 C ATOM 1570 ND1 HIS A 209 18.011 -48.274 110.997 1.00 62.96 N ANISOU 1570 ND1 HIS A 209 9606 6705 7612 -219 -593 -1080 N ATOM 1571 CD2 HIS A 209 19.103 -48.240 112.888 1.00 63.48 C ANISOU 1571 CD2 HIS A 209 9974 6623 7524 -64 -623 -1395 C ATOM 1572 CE1 HIS A 209 17.255 -48.881 111.896 1.00 63.23 C ANISOU 1572 CE1 HIS A 209 9726 6779 7518 -145 -458 -1140 C ATOM 1573 NE2 HIS A 209 17.897 -48.878 113.050 1.00 63.49 N ANISOU 1573 NE2 HIS A 209 9952 6726 7444 -42 -462 -1330 N ATOM 1574 N VAL A 210 22.628 -47.080 108.504 1.00 61.54 N ANISOU 1574 N VAL A 210 9245 6429 7707 -504 -1051 -932 N ATOM 1575 CA VAL A 210 23.549 -46.166 107.839 1.00 62.35 C ANISOU 1575 CA VAL A 210 9217 6472 8003 -570 -1162 -823 C ATOM 1576 C VAL A 210 22.766 -45.400 106.779 1.00 63.16 C ANISOU 1576 C VAL A 210 9155 6599 8244 -631 -1156 -613 C ATOM 1577 O VAL A 210 22.117 -45.998 105.916 1.00 62.72 O ANISOU 1577 O VAL A 210 9051 6725 8054 -711 -1089 -492 O ATOM 1578 CB VAL A 210 24.747 -46.898 107.187 1.00 61.78 C ANISOU 1578 CB VAL A 210 9111 6517 7846 -640 -1157 -762 C ATOM 1579 CG1 VAL A 210 25.776 -45.900 106.711 1.00 63.41 C ANISOU 1579 CG1 VAL A 210 9167 6655 8272 -704 -1272 -643 C ATOM 1580 CG2 VAL A 210 25.400 -47.858 108.158 1.00 61.44 C ANISOU 1580 CG2 VAL A 210 9202 6481 7661 -562 -1145 -907 C ATOM 1581 N SER A 211 22.817 -44.073 106.854 1.00 64.82 N ANISOU 1581 N SER A 211 9284 6621 8725 -606 -1235 -560 N ATOM 1582 CA SER A 211 22.036 -43.234 105.955 1.00 66.13 C ANISOU 1582 CA SER A 211 9274 6783 9069 -632 -1234 -316 C ATOM 1583 C SER A 211 22.748 -41.957 105.563 1.00 67.83 C ANISOU 1583 C SER A 211 9373 6816 9582 -673 -1336 -182 C ATOM 1584 O SER A 211 23.435 -41.335 106.378 1.00 68.72 O ANISOU 1584 O SER A 211 9567 6699 9846 -644 -1408 -341 O ATOM 1585 CB SER A 211 20.684 -42.886 106.585 1.00 67.00 C ANISOU 1585 CB SER A 211 9393 6800 9264 -496 -1150 -345 C ATOM 1586 OG SER A 211 19.880 -42.143 105.681 1.00 68.52 O ANISOU 1586 OG SER A 211 9375 7014 9645 -506 -1151 -52 O ATOM 1587 N GLY A 212 22.560 -41.571 104.304 1.00 68.75 N ANISOU 1587 N GLY A 212 9304 7044 9773 -764 -1352 121 N ATOM 1588 CA GLY A 212 22.994 -40.266 103.807 1.00 70.95 C ANISOU 1588 CA GLY A 212 9439 7142 10376 -803 -1431 328 C ATOM 1589 C GLY A 212 24.374 -40.259 103.189 1.00 71.05 C ANISOU 1589 C GLY A 212 9386 7221 10388 -941 -1495 419 C ATOM 1590 O GLY A 212 24.998 -39.199 103.068 1.00 72.86 O ANISOU 1590 O GLY A 212 9525 7248 10910 -987 -1575 533 O ATOM 1591 N PHE A 213 24.847 -41.440 102.795 1.00 69.32 N ANISOU 1591 N PHE A 213 9208 7270 9862 -1005 -1439 376 N ATOM 1592 CA PHE A 213 26.177 -41.574 102.222 1.00 69.58 C ANISOU 1592 CA PHE A 213 9164 7394 9878 -1106 -1449 465 C ATOM 1593 C PHE A 213 26.144 -41.640 100.704 1.00 70.40 C ANISOU 1593 C PHE A 213 9134 7756 9860 -1227 -1388 768 C ATOM 1594 O PHE A 213 25.181 -42.137 100.114 1.00 70.25 O ANISOU 1594 O PHE A 213 9135 7934 9621 -1259 -1335 835 O ATOM 1595 CB PHE A 213 26.903 -42.789 102.800 1.00 68.01 C ANISOU 1595 CB PHE A 213 9096 7291 9455 -1069 -1394 234 C ATOM 1596 CG PHE A 213 26.288 -44.109 102.430 1.00 66.61 C ANISOU 1596 CG PHE A 213 9033 7345 8931 -1064 -1254 164 C ATOM 1597 CD1 PHE A 213 25.114 -44.544 103.034 1.00 65.78 C ANISOU 1597 CD1 PHE A 213 9051 7227 8714 -997 -1229 21 C ATOM 1598 CD2 PHE A 213 26.902 -44.933 101.499 1.00 66.52 C ANISOU 1598 CD2 PHE A 213 9015 7548 8710 -1132 -1130 233 C ATOM 1599 CE1 PHE A 213 24.554 -45.769 102.701 1.00 64.60 C ANISOU 1599 CE1 PHE A 213 9013 7268 8265 -1030 -1114 -43 C ATOM 1600 CE2 PHE A 213 26.344 -46.158 101.161 1.00 65.64 C ANISOU 1600 CE2 PHE A 213 9051 7607 8284 -1154 -997 135 C ATOM 1601 CZ PHE A 213 25.174 -46.577 101.764 1.00 64.73 C ANISOU 1601 CZ PHE A 213 9053 7467 8074 -1119 -1005 -1 C ATOM 1602 N TYR A 214 27.206 -41.124 100.087 1.00 71.72 N ANISOU 1602 N TYR A 214 9159 7933 10157 -1315 -1404 959 N ATOM 1603 CA TYR A 214 27.394 -41.190 98.640 1.00 72.73 C ANISOU 1603 CA TYR A 214 9171 8332 10132 -1438 -1325 1250 C ATOM 1604 C TYR A 214 28.885 -41.284 98.338 1.00 73.42 C ANISOU 1604 C TYR A 214 9166 8473 10257 -1488 -1264 1316 C ATOM 1605 O TYR A 214 29.679 -40.569 98.951 1.00 74.12 O ANISOU 1605 O TYR A 214 9165 8340 10657 -1487 -1366 1315 O ATOM 1606 CB TYR A 214 26.785 -39.959 97.955 1.00 74.80 C ANISOU 1606 CB TYR A 214 9265 8540 10614 -1495 -1409 1594 C ATOM 1607 CG TYR A 214 26.996 -39.908 96.456 1.00 76.52 C ANISOU 1607 CG TYR A 214 9358 9062 10655 -1641 -1346 1939 C ATOM 1608 CD1 TYR A 214 28.204 -39.468 95.921 1.00 78.38 C ANISOU 1608 CD1 TYR A 214 9454 9316 11009 -1719 -1308 2135 C ATOM 1609 CD2 TYR A 214 25.990 -40.297 95.573 1.00 77.19 C ANISOU 1609 CD2 TYR A 214 9456 9436 10437 -1718 -1327 2083 C ATOM 1610 CE1 TYR A 214 28.416 -39.422 94.545 1.00 80.45 C ANISOU 1610 CE1 TYR A 214 9614 9880 11072 -1851 -1223 2459 C ATOM 1611 CE2 TYR A 214 26.188 -40.253 94.189 1.00 79.44 C ANISOU 1611 CE2 TYR A 214 9654 10034 10497 -1873 -1275 2395 C ATOM 1612 CZ TYR A 214 27.406 -39.808 93.684 1.00 80.88 C ANISOU 1612 CZ TYR A 214 9717 10228 10784 -1928 -1207 2579 C ATOM 1613 OH TYR A 214 27.631 -39.748 92.326 1.00 82.84 O ANISOU 1613 OH TYR A 214 9888 10802 10784 -2078 -1129 2897 O ATOM 1614 N PRO A 215 29.274 -42.159 97.387 1.00 73.65 N ANISOU 1614 N PRO A 215 9215 8797 9973 -1541 -1090 1373 N ATOM 1615 CA PRO A 215 28.425 -43.061 96.596 1.00 73.33 C ANISOU 1615 CA PRO A 215 9313 9026 9523 -1595 -976 1346 C ATOM 1616 C PRO A 215 28.129 -44.401 97.279 1.00 71.37 C ANISOU 1616 C PRO A 215 9296 8785 9036 -1509 -887 994 C ATOM 1617 O PRO A 215 28.457 -44.585 98.452 1.00 70.20 O ANISOU 1617 O PRO A 215 9196 8439 9038 -1388 -932 786 O ATOM 1618 CB PRO A 215 29.253 -43.282 95.330 1.00 75.25 C ANISOU 1618 CB PRO A 215 9492 9531 9568 -1694 -801 1544 C ATOM 1619 CG PRO A 215 30.667 -43.177 95.793 1.00 75.54 C ANISOU 1619 CG PRO A 215 9411 9446 9844 -1620 -752 1533 C ATOM 1620 CD PRO A 215 30.675 -42.184 96.923 1.00 75.09 C ANISOU 1620 CD PRO A 215 9261 9063 10207 -1574 -984 1506 C ATOM 1621 N LYS A 216 27.521 -45.321 96.532 1.00 71.46 N ANISOU 1621 N LYS A 216 9456 9026 8670 -1595 -771 940 N ATOM 1622 CA LYS A 216 27.146 -46.639 97.041 1.00 69.98 C ANISOU 1622 CA LYS A 216 9502 8836 8250 -1546 -672 631 C ATOM 1623 C LYS A 216 28.212 -47.391 97.850 1.00 69.30 C ANISOU 1623 C LYS A 216 9486 8615 8230 -1390 -553 426 C ATOM 1624 O LYS A 216 28.000 -47.625 99.038 1.00 67.89 O ANISOU 1624 O LYS A 216 9373 8261 8160 -1277 -626 245 O ATOM 1625 CB LYS A 216 26.603 -47.533 95.921 1.00 71.09 C ANISOU 1625 CB LYS A 216 9808 9243 7959 -1711 -541 605 C ATOM 1626 CG LYS A 216 25.099 -47.708 95.941 1.00 70.50 C ANISOU 1626 CG LYS A 216 9801 9242 7743 -1820 -667 579 C ATOM 1627 CD LYS A 216 24.664 -48.710 94.893 1.00 71.82 C ANISOU 1627 CD LYS A 216 10169 9666 7455 -2028 -553 504 C ATOM 1628 CE LYS A 216 23.175 -48.982 94.966 1.00 71.52 C ANISOU 1628 CE LYS A 216 10172 9716 7285 -2167 -699 485 C ATOM 1629 NZ LYS A 216 22.680 -49.609 93.706 1.00 73.99 N ANISOU 1629 NZ LYS A 216 10632 10337 7144 -2454 -669 499 N ATOM 1630 N PRO A 217 29.357 -47.753 97.230 1.00 70.79 N ANISOU 1630 N PRO A 217 9643 8895 8359 -1373 -362 480 N ATOM 1631 CA PRO A 217 30.245 -48.762 97.846 1.00 70.64 C ANISOU 1631 CA PRO A 217 9703 8787 8350 -1213 -201 302 C ATOM 1632 C PRO A 217 30.613 -48.488 99.314 1.00 69.50 C ANISOU 1632 C PRO A 217 9479 8424 8503 -1073 -375 226 C ATOM 1633 O PRO A 217 31.420 -47.596 99.607 1.00 70.22 O ANISOU 1633 O PRO A 217 9357 8448 8874 -1058 -497 370 O ATOM 1634 CB PRO A 217 31.490 -48.734 96.950 1.00 72.87 C ANISOU 1634 CB PRO A 217 9854 9197 8638 -1202 4 474 C ATOM 1635 CG PRO A 217 31.437 -47.403 96.260 1.00 74.01 C ANISOU 1635 CG PRO A 217 9792 9429 8899 -1340 -133 763 C ATOM 1636 CD PRO A 217 29.986 -47.129 96.052 1.00 72.97 C ANISOU 1636 CD PRO A 217 9764 9343 8619 -1470 -286 750 C ATOM 1637 N VAL A 218 30.012 -49.258 100.221 1.00 68.09 N ANISOU 1637 N VAL A 218 9482 8144 8245 -995 -391 4 N ATOM 1638 CA VAL A 218 30.193 -49.055 101.657 1.00 67.33 C ANISOU 1638 CA VAL A 218 9360 7874 8350 -882 -564 -88 C ATOM 1639 C VAL A 218 30.437 -50.382 102.382 1.00 67.01 C ANISOU 1639 C VAL A 218 9474 7779 8207 -738 -437 -255 C ATOM 1640 O VAL A 218 30.228 -51.449 101.807 1.00 67.30 O ANISOU 1640 O VAL A 218 9674 7868 8028 -735 -214 -336 O ATOM 1641 CB VAL A 218 29.000 -48.257 102.269 1.00 66.28 C ANISOU 1641 CB VAL A 218 9261 7644 8279 -927 -769 -143 C ATOM 1642 CG1 VAL A 218 27.815 -49.163 102.580 1.00 65.18 C ANISOU 1642 CG1 VAL A 218 9336 7512 7917 -918 -705 -317 C ATOM 1643 CG2 VAL A 218 29.435 -47.476 103.510 1.00 66.50 C ANISOU 1643 CG2 VAL A 218 9214 7497 8556 -863 -976 -185 C ATOM 1644 N TRP A 219 30.879 -50.302 103.637 1.00 67.00 N ANISOU 1644 N TRP A 219 9432 7669 8355 -633 -581 -300 N ATOM 1645 CA TRP A 219 31.305 -51.468 104.406 1.00 67.37 C ANISOU 1645 CA TRP A 219 9574 7669 8354 -477 -486 -384 C ATOM 1646 C TRP A 219 30.828 -51.383 105.853 1.00 66.43 C ANISOU 1646 C TRP A 219 9541 7452 8246 -426 -681 -505 C ATOM 1647 O TRP A 219 31.384 -50.636 106.660 1.00 66.91 O ANISOU 1647 O TRP A 219 9483 7475 8463 -421 -898 -472 O ATOM 1648 CB TRP A 219 32.829 -51.595 104.353 1.00 69.27 C ANISOU 1648 CB TRP A 219 9605 7946 8769 -376 -430 -220 C ATOM 1649 CG TRP A 219 33.355 -52.909 104.830 1.00 71.24 C ANISOU 1649 CG TRP A 219 9923 8157 8987 -189 -260 -240 C ATOM 1650 CD1 TRP A 219 33.468 -54.063 104.101 1.00 73.10 C ANISOU 1650 CD1 TRP A 219 10286 8383 9104 -102 73 -271 C ATOM 1651 CD2 TRP A 219 33.853 -53.210 106.138 1.00 72.93 C ANISOU 1651 CD2 TRP A 219 10090 8326 9293 -65 -406 -215 C ATOM 1652 NE1 TRP A 219 34.002 -55.065 104.877 1.00 74.06 N ANISOU 1652 NE1 TRP A 219 10431 8426 9284 94 159 -249 N ATOM 1653 CE2 TRP A 219 34.248 -54.572 106.132 1.00 74.04 C ANISOU 1653 CE2 TRP A 219 10308 8424 9400 118 -144 -194 C ATOM 1654 CE3 TRP A 219 34.002 -52.466 107.320 1.00 73.37 C ANISOU 1654 CE3 TRP A 219 10064 8372 9440 -99 -732 -211 C ATOM 1655 CZ2 TRP A 219 34.784 -55.204 107.260 1.00 75.17 C ANISOU 1655 CZ2 TRP A 219 10412 8535 9615 280 -212 -117 C ATOM 1656 CZ3 TRP A 219 34.531 -53.097 108.444 1.00 74.52 C ANISOU 1656 CZ3 TRP A 219 10192 8516 9605 33 -816 -163 C ATOM 1657 CH2 TRP A 219 34.917 -54.455 108.403 1.00 75.32 C ANISOU 1657 CH2 TRP A 219 10335 8596 9689 228 -563 -90 C ATOM 1658 N VAL A 220 29.790 -52.155 106.169 1.00 65.61 N ANISOU 1658 N VAL A 220 9655 7315 7960 -409 -600 -647 N ATOM 1659 CA VAL A 220 29.227 -52.207 107.522 1.00 65.17 C ANISOU 1659 CA VAL A 220 9710 7188 7863 -352 -731 -761 C ATOM 1660 C VAL A 220 29.467 -53.589 108.143 1.00 65.75 C ANISOU 1660 C VAL A 220 9911 7230 7840 -215 -598 -788 C ATOM 1661 O VAL A 220 29.232 -54.613 107.494 1.00 65.98 O ANISOU 1661 O VAL A 220 10060 7243 7765 -207 -369 -813 O ATOM 1662 CB VAL A 220 27.712 -51.900 107.524 1.00 63.87 C ANISOU 1662 CB VAL A 220 9661 7010 7595 -438 -746 -862 C ATOM 1663 CG1 VAL A 220 27.221 -51.680 108.939 1.00 63.67 C ANISOU 1663 CG1 VAL A 220 9726 6920 7545 -371 -871 -970 C ATOM 1664 CG2 VAL A 220 27.412 -50.675 106.676 1.00 63.92 C ANISOU 1664 CG2 VAL A 220 9535 7043 7709 -559 -829 -783 C ATOM 1665 N MET A 221 29.936 -53.608 109.393 1.00 66.42 N ANISOU 1665 N MET A 221 9982 7299 7955 -119 -745 -778 N ATOM 1666 CA MET A 221 30.226 -54.854 110.107 1.00 67.15 C ANISOU 1666 CA MET A 221 10169 7362 7982 28 -647 -746 C ATOM 1667 C MET A 221 30.047 -54.769 111.620 1.00 67.56 C ANISOU 1667 C MET A 221 10293 7426 7951 78 -835 -782 C ATOM 1668 O MET A 221 30.453 -53.790 112.255 1.00 68.31 O ANISOU 1668 O MET A 221 10297 7562 8094 34 -1081 -789 O ATOM 1669 CB MET A 221 31.644 -55.320 109.800 1.00 68.88 C ANISOU 1669 CB MET A 221 10215 7604 8352 147 -570 -567 C ATOM 1670 CG MET A 221 31.741 -56.232 108.602 1.00 69.89 C ANISOU 1670 CG MET A 221 10402 7680 8473 187 -241 -556 C ATOM 1671 SD MET A 221 30.941 -57.822 108.872 1.00 70.56 S ANISOU 1671 SD MET A 221 10785 7618 8405 266 9 -650 S ATOM 1672 CE MET A 221 31.474 -58.708 107.406 1.00 72.40 C ANISOU 1672 CE MET A 221 11072 7770 8668 313 394 -649 C ATOM 1673 N TRP A 222 29.444 -55.807 112.195 1.00 67.50 N ANISOU 1673 N TRP A 222 10465 7378 7803 153 -713 -808 N ATOM 1674 CA TRP A 222 29.359 -55.934 113.649 1.00 68.22 C ANISOU 1674 CA TRP A 222 10640 7509 7773 218 -855 -806 C ATOM 1675 C TRP A 222 30.624 -56.582 114.207 1.00 70.21 C ANISOU 1675 C TRP A 222 10780 7805 8091 360 -911 -603 C ATOM 1676 O TRP A 222 31.059 -57.639 113.743 1.00 70.75 O ANISOU 1676 O TRP A 222 10833 7807 8243 476 -702 -478 O ATOM 1677 CB TRP A 222 28.109 -56.707 114.067 1.00 67.59 C ANISOU 1677 CB TRP A 222 10781 7381 7521 227 -701 -883 C ATOM 1678 CG TRP A 222 26.864 -55.885 113.992 1.00 66.20 C ANISOU 1678 CG TRP A 222 10671 7208 7273 110 -719 -1044 C ATOM 1679 CD1 TRP A 222 25.981 -55.836 112.956 1.00 64.99 C ANISOU 1679 CD1 TRP A 222 10532 7021 7142 3 -587 -1104 C ATOM 1680 CD2 TRP A 222 26.367 -54.979 114.990 1.00 66.28 C ANISOU 1680 CD2 TRP A 222 10737 7263 7184 96 -869 -1152 C ATOM 1681 NE1 TRP A 222 24.961 -54.960 113.245 1.00 65.05 N ANISOU 1681 NE1 TRP A 222 10559 7050 7108 -56 -645 -1204 N ATOM 1682 CE2 TRP A 222 25.174 -54.420 114.487 1.00 65.47 C ANISOU 1682 CE2 TRP A 222 10653 7131 7092 12 -793 -1253 C ATOM 1683 CE3 TRP A 222 26.812 -54.589 116.259 1.00 67.35 C ANISOU 1683 CE3 TRP A 222 10916 7464 7209 140 -1057 -1176 C ATOM 1684 CZ2 TRP A 222 24.417 -53.491 115.211 1.00 65.29 C ANISOU 1684 CZ2 TRP A 222 10687 7111 7009 10 -853 -1376 C ATOM 1685 CZ3 TRP A 222 26.062 -53.666 116.975 1.00 67.47 C ANISOU 1685 CZ3 TRP A 222 11032 7484 7118 109 -1123 -1341 C ATOM 1686 CH2 TRP A 222 24.879 -53.129 116.449 1.00 66.53 C ANISOU 1686 CH2 TRP A 222 10927 7303 7049 64 -999 -1440 C ATOM 1687 N MET A 223 31.205 -55.923 115.204 1.00 71.52 N ANISOU 1687 N MET A 223 10870 8082 8223 343 -1194 -566 N ATOM 1688 CA MET A 223 32.526 -56.263 115.709 1.00 73.88 C ANISOU 1688 CA MET A 223 10983 8477 8610 440 -1331 -330 C ATOM 1689 C MET A 223 32.498 -56.523 117.208 1.00 75.44 C ANISOU 1689 C MET A 223 11283 8788 8592 477 -1516 -277 C ATOM 1690 O MET A 223 31.816 -55.814 117.959 1.00 75.43 O ANISOU 1690 O MET A 223 11441 8829 8389 371 -1662 -465 O ATOM 1691 CB MET A 223 33.498 -55.100 115.448 1.00 74.99 C ANISOU 1691 CB MET A 223 10878 8696 8918 323 -1575 -291 C ATOM 1692 CG MET A 223 33.687 -54.707 113.990 1.00 74.22 C ANISOU 1692 CG MET A 223 10644 8529 9027 275 -1420 -296 C ATOM 1693 SD MET A 223 34.842 -55.787 113.128 1.00 77.10 S ANISOU 1693 SD MET A 223 10788 8889 9619 469 -1161 -18 S ATOM 1694 CE MET A 223 36.417 -55.045 113.557 1.00 79.80 C ANISOU 1694 CE MET A 223 10748 9403 10169 426 -1490 234 C ATOM 1695 N ARG A 224 33.239 -57.540 117.638 1.00 77.05 N ANISOU 1695 N ARG A 224 11399 9040 8836 638 -1493 -9 N ATOM 1696 CA ARG A 224 33.675 -57.626 119.025 1.00 79.31 C ANISOU 1696 CA ARG A 224 11681 9509 8944 654 -1763 135 C ATOM 1697 C ARG A 224 35.179 -57.419 119.072 1.00 81.52 C ANISOU 1697 C ARG A 224 11624 9933 9416 669 -1997 402 C ATOM 1698 O ARG A 224 35.952 -58.377 119.059 1.00 83.36 O ANISOU 1698 O ARG A 224 11685 10183 9805 858 -1909 717 O ATOM 1699 CB ARG A 224 33.273 -58.946 119.681 1.00 80.36 C ANISOU 1699 CB ARG A 224 11965 9617 8952 821 -1594 295 C ATOM 1700 CG ARG A 224 32.136 -58.784 120.668 1.00 80.73 C ANISOU 1700 CG ARG A 224 12300 9719 8656 744 -1635 116 C ATOM 1701 CD ARG A 224 32.009 -59.961 121.621 1.00 84.09 C ANISOU 1701 CD ARG A 224 12829 10193 8927 888 -1569 357 C ATOM 1702 NE ARG A 224 30.750 -59.888 122.359 1.00 84.52 N ANISOU 1702 NE ARG A 224 13167 10275 8672 824 -1507 176 N ATOM 1703 CZ ARG A 224 29.618 -60.487 121.990 1.00 83.70 C ANISOU 1703 CZ ARG A 224 13233 10002 8569 845 -1198 86 C ATOM 1704 NH1 ARG A 224 29.563 -61.230 120.888 1.00 82.33 N ANISOU 1704 NH1 ARG A 224 13018 9605 8660 909 -930 126 N ATOM 1705 NH2 ARG A 224 28.530 -60.347 122.732 1.00 84.37 N ANISOU 1705 NH2 ARG A 224 13532 10146 8379 790 -1149 -46 N ATOM 1706 N GLY A 225 35.580 -56.152 119.105 1.00 81.52 N ANISOU 1706 N GLY A 225 11519 10021 9434 467 -2284 287 N ATOM 1707 CA GLY A 225 36.989 -55.786 119.125 1.00 83.82 C ANISOU 1707 CA GLY A 225 11457 10467 9924 421 -2546 536 C ATOM 1708 C GLY A 225 37.596 -55.920 117.749 1.00 82.77 C ANISOU 1708 C GLY A 225 11069 10230 10149 511 -2306 664 C ATOM 1709 O GLY A 225 37.170 -55.250 116.810 1.00 80.40 O ANISOU 1709 O GLY A 225 10812 9805 9931 412 -2185 456 O ATOM 1710 N ASP A 226 38.587 -56.798 117.628 1.00 84.81 N ANISOU 1710 N ASP A 226 11058 10547 10619 712 -2219 1025 N ATOM 1711 CA ASP A 226 39.251 -57.023 116.349 1.00 84.62 C ANISOU 1711 CA ASP A 226 10787 10436 10927 835 -1939 1168 C ATOM 1712 C ASP A 226 38.556 -58.075 115.496 1.00 82.58 C ANISOU 1712 C ASP A 226 10742 9941 10695 1034 -1450 1081 C ATOM 1713 O ASP A 226 38.866 -58.222 114.318 1.00 82.30 O ANISOU 1713 O ASP A 226 10602 9807 10862 1112 -1160 1103 O ATOM 1714 CB ASP A 226 40.741 -57.359 116.542 1.00 88.60 C ANISOU 1714 CB ASP A 226 10850 11114 11700 965 -2054 1617 C ATOM 1715 CG ASP A 226 40.976 -58.672 117.288 1.00 90.85 C ANISOU 1715 CG ASP A 226 11118 11421 11979 1233 -1971 1917 C ATOM 1716 OD1 ASP A 226 42.154 -59.095 117.362 1.00 94.04 O ANISOU 1716 OD1 ASP A 226 11139 11947 12646 1396 -2001 2332 O ATOM 1717 OD2 ASP A 226 40.009 -59.277 117.802 1.00 89.37 O ANISOU 1717 OD2 ASP A 226 11272 11134 11550 1284 -1871 1777 O ATOM 1718 N GLN A 227 37.613 -58.799 116.092 1.00 81.67 N ANISOU 1718 N GLN A 227 10935 9736 10359 1095 -1356 977 N ATOM 1719 CA GLN A 227 36.937 -59.904 115.409 1.00 80.49 C ANISOU 1719 CA GLN A 227 11011 9344 10227 1251 -917 899 C ATOM 1720 C GLN A 227 35.563 -59.524 114.827 1.00 76.90 C ANISOU 1720 C GLN A 227 10868 8764 9587 1077 -792 516 C ATOM 1721 O GLN A 227 34.619 -59.234 115.571 1.00 75.71 O ANISOU 1721 O GLN A 227 10930 8642 9194 960 -935 345 O ATOM 1722 CB GLN A 227 36.837 -61.125 116.338 1.00 82.25 C ANISOU 1722 CB GLN A 227 11339 9520 10391 1445 -845 1099 C ATOM 1723 CG GLN A 227 36.396 -62.424 115.653 1.00 82.70 C ANISOU 1723 CG GLN A 227 11598 9283 10543 1626 -376 1079 C ATOM 1724 CD GLN A 227 37.110 -62.693 114.326 1.00 84.03 C ANISOU 1724 CD GLN A 227 11621 9316 10991 1754 -46 1119 C ATOM 1725 OE1 GLN A 227 38.338 -62.793 114.269 1.00 87.33 O ANISOU 1725 OE1 GLN A 227 11709 9811 11661 1925 -46 1423 O ATOM 1726 NE2 GLN A 227 36.334 -62.824 113.256 1.00 81.62 N ANISOU 1726 NE2 GLN A 227 11557 8826 10630 1669 243 826 N ATOM 1727 N GLU A 228 35.471 -59.530 113.496 1.00 75.56 N ANISOU 1727 N GLU A 228 10710 8474 9526 1064 -520 404 N ATOM 1728 CA GLU A 228 34.209 -59.301 112.789 1.00 72.60 C ANISOU 1728 CA GLU A 228 10595 7994 8996 903 -384 96 C ATOM 1729 C GLU A 228 33.218 -60.416 113.119 1.00 72.13 C ANISOU 1729 C GLU A 228 10834 7778 8794 956 -184 17 C ATOM 1730 O GLU A 228 33.574 -61.596 113.067 1.00 74.01 O ANISOU 1730 O GLU A 228 11109 7875 9135 1142 60 156 O ATOM 1731 CB GLU A 228 34.430 -59.276 111.274 1.00 72.26 C ANISOU 1731 CB GLU A 228 10508 7879 9069 887 -116 39 C ATOM 1732 CG GLU A 228 35.589 -58.422 110.774 1.00 73.61 C ANISOU 1732 CG GLU A 228 10347 8183 9440 875 -218 190 C ATOM 1733 CD GLU A 228 35.756 -58.476 109.255 1.00 73.97 C ANISOU 1733 CD GLU A 228 10380 8175 9551 867 95 140 C ATOM 1734 OE1 GLU A 228 36.495 -57.629 108.706 1.00 74.24 O ANISOU 1734 OE1 GLU A 228 10162 8324 9721 809 24 241 O ATOM 1735 OE2 GLU A 228 35.154 -59.364 108.607 1.00 73.87 O ANISOU 1735 OE2 GLU A 228 10618 8007 9441 899 411 0 O ATOM 1736 N GLN A 229 31.983 -60.051 113.454 1.00 69.99 N ANISOU 1736 N GLN A 229 10763 7516 8313 798 -268 -189 N ATOM 1737 CA GLN A 229 30.943 -61.048 113.723 1.00 69.56 C ANISOU 1737 CA GLN A 229 10976 7323 8132 805 -81 -258 C ATOM 1738 C GLN A 229 30.382 -61.604 112.416 1.00 68.76 C ANISOU 1738 C GLN A 229 11027 7049 8050 729 226 -413 C ATOM 1739 O GLN A 229 29.885 -60.854 111.583 1.00 67.19 O ANISOU 1739 O GLN A 229 10830 6899 7799 557 204 -578 O ATOM 1740 CB GLN A 229 29.831 -60.460 114.596 1.00 68.21 C ANISOU 1740 CB GLN A 229 10932 7246 7739 673 -263 -393 C ATOM 1741 CG GLN A 229 30.318 -59.909 115.926 1.00 69.31 C ANISOU 1741 CG GLN A 229 10984 7562 7787 715 -566 -288 C ATOM 1742 CD GLN A 229 31.155 -60.909 116.701 1.00 72.11 C ANISOU 1742 CD GLN A 229 11286 7922 8189 910 -558 -4 C ATOM 1743 OE1 GLN A 229 32.372 -60.757 116.824 1.00 73.88 O ANISOU 1743 OE1 GLN A 229 11282 8240 8549 999 -696 189 O ATOM 1744 NE2 GLN A 229 30.509 -61.945 117.220 1.00 72.84 N ANISOU 1744 NE2 GLN A 229 11566 7919 8192 977 -398 58 N ATOM 1745 N GLN A 230 30.470 -62.918 112.242 1.00 70.26 N ANISOU 1745 N GLN A 230 11354 7032 8309 847 508 -354 N ATOM 1746 CA GLN A 230 30.149 -63.545 110.959 1.00 70.56 C ANISOU 1746 CA GLN A 230 11563 6887 8360 772 819 -514 C ATOM 1747 C GLN A 230 28.652 -63.561 110.641 1.00 68.90 C ANISOU 1747 C GLN A 230 11574 6648 7957 514 836 -737 C ATOM 1748 O GLN A 230 28.261 -63.680 109.478 1.00 68.76 O ANISOU 1748 O GLN A 230 11674 6571 7882 358 991 -906 O ATOM 1749 CB GLN A 230 30.745 -64.957 110.872 1.00 73.54 C ANISOU 1749 CB GLN A 230 12045 6997 8898 983 1144 -399 C ATOM 1750 CG GLN A 230 32.278 -65.002 110.924 1.00 76.30 C ANISOU 1750 CG GLN A 230 12131 7372 9486 1256 1187 -147 C ATOM 1751 CD GLN A 230 32.948 -64.525 109.637 1.00 77.15 C ANISOU 1751 CD GLN A 230 12124 7523 9667 1244 1327 -219 C ATOM 1752 OE1 GLN A 230 33.464 -63.406 109.565 1.00 76.14 O ANISOU 1752 OE1 GLN A 230 11739 7627 9563 1201 1099 -158 O ATOM 1753 NE2 GLN A 230 32.943 -65.378 108.615 1.00 78.98 N ANISOU 1753 NE2 GLN A 230 12561 7522 9925 1271 1714 -353 N ATOM 1754 N GLY A 231 27.822 -63.441 111.673 1.00 67.97 N ANISOU 1754 N GLY A 231 11502 6595 7727 462 679 -722 N ATOM 1755 CA GLY A 231 26.373 -63.396 111.493 1.00 66.84 C ANISOU 1755 CA GLY A 231 11507 6461 7430 227 678 -882 C ATOM 1756 C GLY A 231 25.861 -62.027 111.065 1.00 64.91 C ANISOU 1756 C GLY A 231 11134 6421 7106 65 477 -991 C ATOM 1757 O GLY A 231 24.650 -61.813 110.952 1.00 63.84 O ANISOU 1757 O GLY A 231 11056 6336 6864 -117 445 -1083 O ATOM 1758 N THR A 232 26.788 -61.099 110.842 1.00 64.67 N ANISOU 1758 N THR A 232 10910 6504 7156 134 344 -951 N ATOM 1759 CA THR A 232 26.460 -59.759 110.389 1.00 63.39 C ANISOU 1759 CA THR A 232 10617 6500 6970 1 165 -1022 C ATOM 1760 C THR A 232 25.851 -59.843 109.008 1.00 63.42 C ANISOU 1760 C THR A 232 10690 6496 6910 -196 289 -1132 C ATOM 1761 O THR A 232 26.539 -60.141 108.039 1.00 64.46 O ANISOU 1761 O THR A 232 10831 6586 7075 -192 436 -1142 O ATOM 1762 CB THR A 232 27.708 -58.879 110.326 1.00 63.48 C ANISOU 1762 CB THR A 232 10410 6598 7113 96 23 -933 C ATOM 1763 OG1 THR A 232 28.370 -58.907 111.595 1.00 64.49 O ANISOU 1763 OG1 THR A 232 10475 6752 7275 253 -115 -816 O ATOM 1764 CG2 THR A 232 27.341 -57.445 109.977 1.00 62.38 C ANISOU 1764 CG2 THR A 232 10144 6580 6979 -37 -168 -988 C ATOM 1765 N HIS A 233 24.549 -59.600 108.930 1.00 63.05 N ANISOU 1765 N HIS A 233 10689 6507 6759 -371 236 -1202 N ATOM 1766 CA HIS A 233 23.839 -59.650 107.664 1.00 63.50 C ANISOU 1766 CA HIS A 233 10802 6606 6721 -603 301 -1284 C ATOM 1767 C HIS A 233 23.643 -58.245 107.135 1.00 62.85 C ANISOU 1767 C HIS A 233 10525 6696 6659 -686 118 -1250 C ATOM 1768 O HIS A 233 23.025 -57.404 107.786 1.00 62.27 O ANISOU 1768 O HIS A 233 10346 6692 6620 -674 -37 -1218 O ATOM 1769 CB HIS A 233 22.493 -60.351 107.822 1.00 63.77 C ANISOU 1769 CB HIS A 233 10973 6607 6648 -773 352 -1335 C ATOM 1770 CG HIS A 233 21.576 -60.170 106.653 1.00 63.99 C ANISOU 1770 CG HIS A 233 11006 6748 6559 -1056 327 -1387 C ATOM 1771 ND1 HIS A 233 20.424 -59.416 106.721 1.00 63.28 N ANISOU 1771 ND1 HIS A 233 10778 6815 6452 -1181 174 -1331 N ATOM 1772 CD2 HIS A 233 21.640 -60.646 105.386 1.00 65.01 C ANISOU 1772 CD2 HIS A 233 11259 6873 6570 -1242 434 -1477 C ATOM 1773 CE1 HIS A 233 19.815 -59.441 105.548 1.00 63.99 C ANISOU 1773 CE1 HIS A 233 10878 7011 6423 -1443 155 -1352 C ATOM 1774 NE2 HIS A 233 20.532 -60.182 104.722 1.00 64.89 N ANISOU 1774 NE2 HIS A 233 11171 7036 6448 -1500 306 -1458 N ATOM 1775 N ARG A 234 24.192 -58.007 105.952 1.00 63.64 N ANISOU 1775 N ARG A 234 10587 6851 6742 -757 164 -1248 N ATOM 1776 CA ARG A 234 24.066 -56.747 105.250 1.00 63.34 C ANISOU 1776 CA ARG A 234 10369 6968 6729 -852 15 -1178 C ATOM 1777 C ARG A 234 22.663 -56.682 104.670 1.00 63.37 C ANISOU 1777 C ARG A 234 10394 7082 6602 -1088 -34 -1187 C ATOM 1778 O ARG A 234 22.120 -57.695 104.255 1.00 64.44 O ANISOU 1778 O ARG A 234 10706 7192 6588 -1240 83 -1272 O ATOM 1779 CB ARG A 234 25.102 -56.727 104.132 1.00 64.56 C ANISOU 1779 CB ARG A 234 10500 7159 6870 -861 126 -1153 C ATOM 1780 CG ARG A 234 25.247 -55.433 103.390 1.00 65.81 C ANISOU 1780 CG ARG A 234 10458 7468 7080 -936 -11 -1034 C ATOM 1781 CD ARG A 234 25.524 -55.718 101.925 1.00 69.84 C ANISOU 1781 CD ARG A 234 11035 8079 7421 -1079 142 -1039 C ATOM 1782 NE ARG A 234 26.492 -54.776 101.370 1.00 72.38 N ANISOU 1782 NE ARG A 234 11161 8488 7854 -1034 111 -892 N ATOM 1783 CZ ARG A 234 26.746 -54.634 100.072 1.00 74.91 C ANISOU 1783 CZ ARG A 234 11480 8950 8031 -1160 209 -839 C ATOM 1784 NH1 ARG A 234 26.091 -55.366 99.174 1.00 76.69 N ANISOU 1784 NH1 ARG A 234 11916 9255 7969 -1358 327 -948 N ATOM 1785 NH2 ARG A 234 27.651 -53.748 99.672 1.00 75.92 N ANISOU 1785 NH2 ARG A 234 11404 9152 8291 -1110 184 -672 N ATOM 1786 N GLY A 235 22.070 -55.496 104.650 1.00 62.98 N ANISOU 1786 N GLY A 235 10159 7145 6627 -1125 -210 -1085 N ATOM 1787 CA GLY A 235 20.745 -55.310 104.061 1.00 63.75 C ANISOU 1787 CA GLY A 235 10203 7384 6634 -1340 -283 -1026 C ATOM 1788 C GLY A 235 20.827 -55.025 102.575 1.00 65.12 C ANISOU 1788 C GLY A 235 10338 7721 6683 -1536 -304 -955 C ATOM 1789 O GLY A 235 21.782 -55.435 101.909 1.00 66.04 O ANISOU 1789 O GLY A 235 10558 7822 6713 -1541 -181 -1014 O ATOM 1790 N ASP A 236 19.818 -54.332 102.052 1.00 65.86 N ANISOU 1790 N ASP A 236 10274 7985 6763 -1689 -448 -808 N ATOM 1791 CA ASP A 236 19.837 -53.851 100.668 1.00 67.43 C ANISOU 1791 CA ASP A 236 10399 8387 6836 -1878 -512 -680 C ATOM 1792 C ASP A 236 20.029 -52.341 100.644 1.00 66.82 C ANISOU 1792 C ASP A 236 10061 8342 6986 -1761 -653 -470 C ATOM 1793 O ASP A 236 19.813 -51.657 101.648 1.00 65.84 O ANISOU 1793 O ASP A 236 9820 8096 7099 -1580 -716 -439 O ATOM 1794 CB ASP A 236 18.539 -54.206 99.941 1.00 69.38 C ANISOU 1794 CB ASP A 236 10640 8839 6883 -2181 -600 -612 C ATOM 1795 CG ASP A 236 18.394 -55.695 99.681 1.00 71.90 C ANISOU 1795 CG ASP A 236 11253 9118 6948 -2375 -464 -831 C ATOM 1796 OD1 ASP A 236 18.975 -56.507 100.437 1.00 73.10 O ANISOU 1796 OD1 ASP A 236 11586 9041 7147 -2222 -297 -1014 O ATOM 1797 OD2 ASP A 236 17.680 -56.059 98.719 1.00 75.24 O ANISOU 1797 OD2 ASP A 236 11730 9734 7124 -2695 -531 -812 O ATOM 1798 N PHE A 237 20.435 -51.817 99.497 1.00 67.60 N ANISOU 1798 N PHE A 237 10086 8592 7007 -1870 -687 -330 N ATOM 1799 CA PHE A 237 20.576 -50.383 99.362 1.00 67.41 C ANISOU 1799 CA PHE A 237 9815 8582 7217 -1788 -818 -97 C ATOM 1800 C PHE A 237 19.211 -49.745 99.114 1.00 68.23 C ANISOU 1800 C PHE A 237 9721 8829 7373 -1890 -978 131 C ATOM 1801 O PHE A 237 18.606 -49.932 98.059 1.00 69.93 O ANISOU 1801 O PHE A 237 9911 9296 7365 -2132 -1045 264 O ATOM 1802 CB PHE A 237 21.573 -50.036 98.253 1.00 68.61 C ANISOU 1802 CB PHE A 237 9941 8845 7283 -1855 -778 13 C ATOM 1803 CG PHE A 237 23.006 -50.334 98.609 1.00 67.88 C ANISOU 1803 CG PHE A 237 9936 8597 7260 -1694 -631 -129 C ATOM 1804 CD1 PHE A 237 23.829 -49.336 99.126 1.00 67.33 C ANISOU 1804 CD1 PHE A 237 9705 8384 7495 -1527 -692 -40 C ATOM 1805 CD2 PHE A 237 23.536 -51.610 98.426 1.00 68.00 C ANISOU 1805 CD2 PHE A 237 10185 8598 7055 -1713 -429 -338 C ATOM 1806 CE1 PHE A 237 25.159 -49.609 99.459 1.00 67.12 C ANISOU 1806 CE1 PHE A 237 9709 8247 7546 -1394 -582 -129 C ATOM 1807 CE2 PHE A 237 24.862 -51.889 98.755 1.00 67.67 C ANISOU 1807 CE2 PHE A 237 10175 8423 7112 -1538 -284 -419 C ATOM 1808 CZ PHE A 237 25.676 -50.891 99.271 1.00 66.87 C ANISOU 1808 CZ PHE A 237 9873 8226 7310 -1385 -374 -299 C ATOM 1809 N LEU A 238 18.721 -49.020 100.113 1.00 67.27 N ANISOU 1809 N LEU A 238 9465 8553 7541 -1703 -1031 176 N ATOM 1810 CA LEU A 238 17.513 -48.227 99.963 1.00 68.47 C ANISOU 1810 CA LEU A 238 9376 8801 7839 -1725 -1154 439 C ATOM 1811 C LEU A 238 17.900 -46.819 99.529 1.00 69.37 C ANISOU 1811 C LEU A 238 9288 8869 8200 -1645 -1239 691 C ATOM 1812 O LEU A 238 18.888 -46.269 100.023 1.00 68.52 O ANISOU 1812 O LEU A 238 9212 8541 8280 -1486 -1205 604 O ATOM 1813 CB LEU A 238 16.709 -48.185 101.266 1.00 67.76 C ANISOU 1813 CB LEU A 238 9253 8552 7939 -1544 -1113 357 C ATOM 1814 CG LEU A 238 16.297 -49.508 101.925 1.00 67.03 C ANISOU 1814 CG LEU A 238 9346 8460 7664 -1591 -1015 132 C ATOM 1815 CD1 LEU A 238 15.302 -49.247 103.036 1.00 66.68 C ANISOU 1815 CD1 LEU A 238 9199 8324 7813 -1425 -974 149 C ATOM 1816 CD2 LEU A 238 15.725 -50.514 100.928 1.00 68.47 C ANISOU 1816 CD2 LEU A 238 9584 8896 7535 -1911 -1053 166 C ATOM 1817 N PRO A 239 17.130 -46.230 98.598 1.00 71.42 N ANISOU 1817 N PRO A 239 9329 9338 8469 -1771 -1364 1028 N ATOM 1818 CA PRO A 239 17.490 -44.915 98.083 1.00 72.69 C ANISOU 1818 CA PRO A 239 9295 9452 8872 -1710 -1440 1316 C ATOM 1819 C PRO A 239 16.888 -43.773 98.898 1.00 73.28 C ANISOU 1819 C PRO A 239 9181 9277 9385 -1467 -1454 1447 C ATOM 1820 O PRO A 239 15.787 -43.910 99.418 1.00 73.67 O ANISOU 1820 O PRO A 239 9148 9338 9506 -1405 -1443 1471 O ATOM 1821 CB PRO A 239 16.900 -44.931 96.672 1.00 75.15 C ANISOU 1821 CB PRO A 239 9468 10140 8946 -1974 -1570 1644 C ATOM 1822 CG PRO A 239 15.727 -45.863 96.757 1.00 75.49 C ANISOU 1822 CG PRO A 239 9523 10374 8786 -2119 -1608 1596 C ATOM 1823 CD PRO A 239 15.928 -46.774 97.935 1.00 73.03 C ANISOU 1823 CD PRO A 239 9446 9848 8455 -2003 -1459 1188 C ATOM 1824 N ASN A 240 17.616 -42.664 99.009 1.00 73.74 N ANISOU 1824 N ASN A 240 9178 9096 9743 -1335 -1459 1528 N ATOM 1825 CA ASN A 240 17.093 -41.443 99.631 1.00 75.12 C ANISOU 1825 CA ASN A 240 9193 8989 10360 -1110 -1452 1667 C ATOM 1826 C ASN A 240 16.674 -40.409 98.588 1.00 78.01 C ANISOU 1826 C ASN A 240 9274 9445 10921 -1149 -1558 2154 C ATOM 1827 O ASN A 240 17.086 -40.484 97.428 1.00 78.80 O ANISOU 1827 O ASN A 240 9325 9799 10817 -1351 -1643 2364 O ATOM 1828 CB ASN A 240 18.120 -40.828 100.585 1.00 74.29 C ANISOU 1828 CB ASN A 240 9231 8493 10502 -945 -1393 1413 C ATOM 1829 CG ASN A 240 18.398 -41.696 101.798 1.00 72.10 C ANISOU 1829 CG ASN A 240 9205 8111 10079 -865 -1302 980 C ATOM 1830 OD1 ASN A 240 19.180 -41.320 102.671 1.00 71.78 O ANISOU 1830 OD1 ASN A 240 9296 7794 10182 -758 -1279 751 O ATOM 1831 ND2 ASN A 240 17.763 -42.862 101.861 1.00 71.09 N ANISOU 1831 ND2 ASN A 240 9145 8206 9661 -937 -1262 881 N ATOM 1832 N ALA A 241 15.866 -39.439 99.014 1.00 79.93 N ANISOU 1832 N ALA A 241 9334 9475 11560 -943 -1532 2344 N ATOM 1833 CA ALA A 241 15.331 -38.404 98.123 1.00 83.08 C ANISOU 1833 CA ALA A 241 9426 9927 12214 -934 -1623 2865 C ATOM 1834 C ALA A 241 16.416 -37.633 97.393 1.00 83.87 C ANISOU 1834 C ALA A 241 9508 9940 12417 -1011 -1682 3044 C ATOM 1835 O ALA A 241 16.295 -37.370 96.197 1.00 85.83 O ANISOU 1835 O ALA A 241 9569 10460 12581 -1164 -1800 3461 O ATOM 1836 CB ALA A 241 14.443 -37.443 98.899 1.00 85.26 C ANISOU 1836 CB ALA A 241 9545 9875 12974 -633 -1520 2982 C ATOM 1837 N ASP A 242 17.475 -37.292 98.125 1.00 82.68 N ANISOU 1837 N ASP A 242 9548 9434 12432 -924 -1609 2740 N ATOM 1838 CA ASP A 242 18.566 -36.448 97.628 1.00 83.80 C ANISOU 1838 CA ASP A 242 9664 9418 12760 -982 -1649 2894 C ATOM 1839 C ASP A 242 19.681 -37.242 96.931 1.00 82.18 C ANISOU 1839 C ASP A 242 9575 9494 12155 -1213 -1676 2801 C ATOM 1840 O ASP A 242 20.814 -36.771 96.822 1.00 82.60 O ANISOU 1840 O ASP A 242 9656 9395 12335 -1256 -1675 2799 O ATOM 1841 CB ASP A 242 19.139 -35.604 98.777 1.00 83.97 C ANISOU 1841 CB ASP A 242 9814 8900 13189 -803 -1576 2628 C ATOM 1842 CG ASP A 242 19.590 -36.452 99.960 1.00 81.08 C ANISOU 1842 CG ASP A 242 9732 8446 12629 -763 -1510 2080 C ATOM 1843 OD1 ASP A 242 20.676 -37.060 99.884 1.00 78.80 O ANISOU 1843 OD1 ASP A 242 9570 8265 12106 -898 -1535 1894 O ATOM 1844 OD2 ASP A 242 18.857 -36.505 100.969 1.00 81.32 O ANISOU 1844 OD2 ASP A 242 9845 8307 12744 -584 -1420 1862 O ATOM 1845 N GLU A 243 19.341 -38.442 96.460 1.00 80.87 N ANISOU 1845 N GLU A 243 9474 9728 11524 -1363 -1685 2729 N ATOM 1846 CA GLU A 243 20.247 -39.322 95.699 1.00 79.66 C ANISOU 1846 CA GLU A 243 9450 9869 10948 -1570 -1663 2638 C ATOM 1847 C GLU A 243 21.448 -39.819 96.513 1.00 76.95 C ANISOU 1847 C GLU A 243 9325 9331 10581 -1518 -1564 2219 C ATOM 1848 O GLU A 243 22.520 -40.092 95.970 1.00 76.63 O ANISOU 1848 O GLU A 243 9333 9402 10380 -1623 -1516 2207 O ATOM 1849 CB GLU A 243 20.663 -38.702 94.343 1.00 82.31 C ANISOU 1849 CB GLU A 243 9621 10416 11237 -1728 -1722 3078 C ATOM 1850 CG GLU A 243 19.480 -38.322 93.432 1.00 85.31 C ANISOU 1850 CG GLU A 243 9769 11073 11572 -1812 -1853 3546 C ATOM 1851 CD GLU A 243 19.848 -38.207 91.954 1.00 87.86 C ANISOU 1851 CD GLU A 243 10004 11774 11604 -2044 -1908 3925 C ATOM 1852 OE1 GLU A 243 20.007 -37.062 91.466 1.00 90.03 O ANISOU 1852 OE1 GLU A 243 10072 11963 12173 -2019 -1961 4348 O ATOM 1853 OE2 GLU A 243 19.963 -39.258 91.281 1.00 87.41 O ANISOU 1853 OE2 GLU A 243 10100 12093 11020 -2253 -1887 3801 O ATOM 1854 N THR A 244 21.247 -39.927 97.823 1.00 75.23 N ANISOU 1854 N THR A 244 9223 8840 10522 -1348 -1529 1901 N ATOM 1855 CA THR A 244 22.169 -40.660 98.685 1.00 72.88 C ANISOU 1855 CA THR A 244 9137 8431 10124 -1305 -1458 1500 C ATOM 1856 C THR A 244 21.674 -42.091 98.821 1.00 70.95 C ANISOU 1856 C THR A 244 9055 8410 9492 -1350 -1390 1268 C ATOM 1857 O THR A 244 20.922 -42.583 97.970 1.00 71.58 O ANISOU 1857 O THR A 244 9097 8784 9317 -1487 -1406 1417 O ATOM 1858 CB THR A 244 22.319 -40.027 100.092 1.00 72.54 C ANISOU 1858 CB THR A 244 9167 7980 10414 -1122 -1464 1262 C ATOM 1859 OG1 THR A 244 21.055 -39.521 100.536 1.00 73.64 O ANISOU 1859 OG1 THR A 244 9245 7992 10742 -989 -1459 1322 O ATOM 1860 CG2 THR A 244 23.341 -38.901 100.076 1.00 74.08 C ANISOU 1860 CG2 THR A 244 9283 7919 10944 -1135 -1523 1367 C ATOM 1861 N TRP A 245 22.093 -42.751 99.895 1.00 68.86 N ANISOU 1861 N TRP A 245 8974 8006 9185 -1254 -1329 917 N ATOM 1862 CA TRP A 245 21.790 -44.156 100.101 1.00 67.37 C ANISOU 1862 CA TRP A 245 8961 7975 8663 -1291 -1245 688 C ATOM 1863 C TRP A 245 21.513 -44.500 101.561 1.00 66.14 C ANISOU 1863 C TRP A 245 8942 7619 8568 -1128 -1209 398 C ATOM 1864 O TRP A 245 21.735 -43.683 102.459 1.00 66.69 O ANISOU 1864 O TRP A 245 9006 7428 8904 -991 -1244 321 O ATOM 1865 CB TRP A 245 22.922 -45.023 99.546 1.00 66.76 C ANISOU 1865 CB TRP A 245 8995 8031 8338 -1382 -1153 595 C ATOM 1866 CG TRP A 245 22.980 -44.992 98.057 1.00 68.00 C ANISOU 1866 CG TRP A 245 9076 8461 8301 -1568 -1146 843 C ATOM 1867 CD1 TRP A 245 23.928 -44.387 97.288 1.00 68.86 C ANISOU 1867 CD1 TRP A 245 9077 8615 8472 -1619 -1136 1038 C ATOM 1868 CD2 TRP A 245 22.030 -45.565 97.149 1.00 68.64 C ANISOU 1868 CD2 TRP A 245 9181 8830 8069 -1750 -1156 939 C ATOM 1869 NE1 TRP A 245 23.636 -44.558 95.958 1.00 70.47 N ANISOU 1869 NE1 TRP A 245 9255 9128 8393 -1808 -1122 1244 N ATOM 1870 CE2 TRP A 245 22.475 -45.277 95.844 1.00 70.43 C ANISOU 1870 CE2 TRP A 245 9337 9281 8144 -1904 -1151 1179 C ATOM 1871 CE3 TRP A 245 20.846 -46.299 97.314 1.00 68.15 C ANISOU 1871 CE3 TRP A 245 9189 8873 7833 -1822 -1179 855 C ATOM 1872 CZ2 TRP A 245 21.780 -45.697 94.705 1.00 72.24 C ANISOU 1872 CZ2 TRP A 245 9588 9845 8014 -2137 -1182 1317 C ATOM 1873 CZ3 TRP A 245 20.156 -46.717 96.181 1.00 69.76 C ANISOU 1873 CZ3 TRP A 245 9392 9397 7715 -2069 -1226 997 C ATOM 1874 CH2 TRP A 245 20.626 -46.414 94.895 1.00 71.73 C ANISOU 1874 CH2 TRP A 245 9596 9876 7781 -2228 -1235 1216 C ATOM 1875 N TYR A 246 21.017 -45.712 101.783 1.00 64.98 N ANISOU 1875 N TYR A 246 8934 7594 8160 -1162 -1134 237 N ATOM 1876 CA TYR A 246 20.688 -46.200 103.107 1.00 63.79 C ANISOU 1876 CA TYR A 246 8921 7307 8009 -1025 -1081 -8 C ATOM 1877 C TYR A 246 20.965 -47.692 103.120 1.00 62.62 C ANISOU 1877 C TYR A 246 8962 7268 7563 -1092 -981 -187 C ATOM 1878 O TYR A 246 20.462 -48.426 102.269 1.00 63.20 O ANISOU 1878 O TYR A 246 9061 7539 7415 -1257 -948 -133 O ATOM 1879 CB TYR A 246 19.210 -45.934 103.415 1.00 64.63 C ANISOU 1879 CB TYR A 246 8935 7427 8195 -979 -1079 78 C ATOM 1880 CG TYR A 246 18.717 -46.476 104.745 1.00 64.39 C ANISOU 1880 CG TYR A 246 9041 7295 8131 -845 -991 -147 C ATOM 1881 CD1 TYR A 246 18.302 -45.616 105.758 1.00 65.59 C ANISOU 1881 CD1 TYR A 246 9174 7239 8509 -654 -965 -202 C ATOM 1882 CD2 TYR A 246 18.650 -47.851 104.985 1.00 63.99 C ANISOU 1882 CD2 TYR A 246 9152 7343 7818 -908 -913 -300 C ATOM 1883 CE1 TYR A 246 17.842 -46.114 106.984 1.00 65.85 C ANISOU 1883 CE1 TYR A 246 9343 7208 8470 -531 -862 -399 C ATOM 1884 CE2 TYR A 246 18.200 -48.359 106.202 1.00 63.73 C ANISOU 1884 CE2 TYR A 246 9237 7232 7744 -791 -825 -467 C ATOM 1885 CZ TYR A 246 17.794 -47.489 107.196 1.00 64.47 C ANISOU 1885 CZ TYR A 246 9305 7163 8028 -604 -800 -512 C ATOM 1886 OH TYR A 246 17.342 -47.996 108.396 1.00 63.84 O ANISOU 1886 OH TYR A 246 9353 7036 7868 -490 -692 -668 O ATOM 1887 N LEU A 247 21.769 -48.136 104.079 1.00 61.43 N ANISOU 1887 N LEU A 247 8949 6982 7409 -975 -938 -392 N ATOM 1888 CA LEU A 247 22.010 -49.557 104.279 1.00 60.43 C ANISOU 1888 CA LEU A 247 9007 6899 7055 -992 -821 -552 C ATOM 1889 C LEU A 247 21.990 -49.878 105.757 1.00 59.58 C ANISOU 1889 C LEU A 247 9017 6650 6970 -833 -802 -726 C ATOM 1890 O LEU A 247 22.751 -49.296 106.529 1.00 59.70 O ANISOU 1890 O LEU A 247 9028 6537 7120 -718 -871 -786 O ATOM 1891 CB LEU A 247 23.361 -49.976 103.693 1.00 60.50 C ANISOU 1891 CB LEU A 247 9051 6933 7004 -1011 -759 -561 C ATOM 1892 CG LEU A 247 23.724 -51.460 103.875 1.00 60.80 C ANISOU 1892 CG LEU A 247 9286 6964 6851 -994 -601 -714 C ATOM 1893 CD1 LEU A 247 22.924 -52.371 102.940 1.00 61.63 C ANISOU 1893 CD1 LEU A 247 9504 7202 6709 -1181 -500 -732 C ATOM 1894 CD2 LEU A 247 25.205 -51.686 103.664 1.00 61.86 C ANISOU 1894 CD2 LEU A 247 9410 7070 7025 -920 -528 -710 C ATOM 1895 N GLN A 248 21.126 -50.800 106.164 1.00 59.02 N ANISOU 1895 N GLN A 248 9055 6614 6756 -848 -717 -800 N ATOM 1896 CA GLN A 248 21.201 -51.282 107.534 1.00 58.26 C ANISOU 1896 CA GLN A 248 9092 6414 6629 -705 -676 -946 C ATOM 1897 C GLN A 248 21.895 -52.631 107.570 1.00 57.57 C ANISOU 1897 C GLN A 248 9162 6320 6391 -708 -569 -1023 C ATOM 1898 O GLN A 248 21.863 -53.368 106.590 1.00 57.66 O ANISOU 1898 O GLN A 248 9220 6400 6289 -840 -484 -1004 O ATOM 1899 CB GLN A 248 19.834 -51.293 108.229 1.00 58.59 C ANISOU 1899 CB GLN A 248 9137 6467 6659 -674 -631 -954 C ATOM 1900 CG GLN A 248 18.914 -52.455 107.902 1.00 59.20 C ANISOU 1900 CG GLN A 248 9271 6647 6574 -811 -531 -933 C ATOM 1901 CD GLN A 248 17.572 -52.340 108.612 1.00 60.48 C ANISOU 1901 CD GLN A 248 9377 6837 6765 -771 -481 -895 C ATOM 1902 OE1 GLN A 248 17.086 -51.238 108.869 1.00 61.37 O ANISOU 1902 OE1 GLN A 248 9356 6925 7036 -674 -514 -836 O ATOM 1903 NE2 GLN A 248 16.964 -53.480 108.923 1.00 61.37 N ANISOU 1903 NE2 GLN A 248 9586 6985 6745 -842 -379 -917 N ATOM 1904 N ALA A 249 22.560 -52.914 108.689 1.00 57.19 N ANISOU 1904 N ALA A 249 9201 6185 6344 -561 -573 -1104 N ATOM 1905 CA ALA A 249 23.218 -54.194 108.921 1.00 56.95 C ANISOU 1905 CA ALA A 249 9307 6117 6216 -513 -462 -1141 C ATOM 1906 C ALA A 249 22.772 -54.734 110.263 1.00 57.04 C ANISOU 1906 C ALA A 249 9439 6085 6147 -411 -432 -1196 C ATOM 1907 O ALA A 249 22.910 -54.068 111.292 1.00 56.95 O ANISOU 1907 O ALA A 249 9420 6055 6162 -307 -535 -1233 O ATOM 1908 CB ALA A 249 24.718 -54.047 108.879 1.00 57.19 C ANISOU 1908 CB ALA A 249 9275 6119 6337 -427 -509 -1106 C ATOM 1909 N THR A 250 22.225 -55.945 110.236 1.00 57.51 N ANISOU 1909 N THR A 250 9628 6126 6097 -461 -284 -1204 N ATOM 1910 CA THR A 250 21.617 -56.547 111.417 1.00 58.12 C ANISOU 1910 CA THR A 250 9817 6178 6087 -390 -225 -1218 C ATOM 1911 C THR A 250 22.484 -57.678 111.976 1.00 58.81 C ANISOU 1911 C THR A 250 10031 6180 6135 -279 -144 -1190 C ATOM 1912 O THR A 250 23.229 -58.325 111.237 1.00 58.88 O ANISOU 1912 O THR A 250 10069 6122 6179 -287 -59 -1174 O ATOM 1913 CB THR A 250 20.164 -57.055 111.137 1.00 58.37 C ANISOU 1913 CB THR A 250 9877 6247 6054 -544 -123 -1203 C ATOM 1914 OG1 THR A 250 20.188 -58.435 110.752 1.00 59.67 O ANISOU 1914 OG1 THR A 250 10188 6330 6153 -634 22 -1207 O ATOM 1915 CG2 THR A 250 19.473 -56.229 110.043 1.00 57.71 C ANISOU 1915 CG2 THR A 250 9640 6264 6025 -697 -190 -1169 C ATOM 1916 N LEU A 251 22.387 -57.887 113.286 1.00 59.63 N ANISOU 1916 N LEU A 251 10206 6286 6163 -162 -157 -1171 N ATOM 1917 CA LEU A 251 23.044 -59.006 113.958 1.00 61.08 C ANISOU 1917 CA LEU A 251 10499 6398 6309 -45 -83 -1088 C ATOM 1918 C LEU A 251 22.111 -59.648 114.981 1.00 62.18 C ANISOU 1918 C LEU A 251 10760 6544 6323 -29 9 -1047 C ATOM 1919 O LEU A 251 21.506 -58.960 115.804 1.00 62.29 O ANISOU 1919 O LEU A 251 10765 6655 6246 0 -51 -1081 O ATOM 1920 CB LEU A 251 24.352 -58.561 114.632 1.00 61.59 C ANISOU 1920 CB LEU A 251 10495 6506 6402 104 -247 -1035 C ATOM 1921 CG LEU A 251 25.150 -59.589 115.455 1.00 62.84 C ANISOU 1921 CG LEU A 251 10715 6628 6535 256 -215 -885 C ATOM 1922 CD1 LEU A 251 25.831 -60.631 114.586 1.00 63.08 C ANISOU 1922 CD1 LEU A 251 10755 6512 6702 297 -38 -805 C ATOM 1923 CD2 LEU A 251 26.179 -58.892 116.312 1.00 64.06 C ANISOU 1923 CD2 LEU A 251 10775 6897 6669 353 -452 -830 C ATOM 1924 N ASP A 252 22.001 -60.971 114.921 1.00 63.53 N ANISOU 1924 N ASP A 252 11052 6592 6493 -45 178 -973 N ATOM 1925 CA ASP A 252 21.196 -61.710 115.875 1.00 65.12 C ANISOU 1925 CA ASP A 252 11364 6786 6594 -36 284 -889 C ATOM 1926 C ASP A 252 22.036 -62.149 117.070 1.00 66.88 C ANISOU 1926 C ASP A 252 11645 7019 6749 159 247 -747 C ATOM 1927 O ASP A 252 23.135 -62.686 116.914 1.00 67.72 O ANISOU 1927 O ASP A 252 11750 7033 6949 264 252 -658 O ATOM 1928 CB ASP A 252 20.549 -62.914 115.208 1.00 65.97 C ANISOU 1928 CB ASP A 252 11582 6731 6751 -192 481 -871 C ATOM 1929 CG ASP A 252 19.472 -63.534 116.063 1.00 67.73 C ANISOU 1929 CG ASP A 252 11880 6961 6892 -239 591 -774 C ATOM 1930 OD1 ASP A 252 19.808 -64.308 116.990 1.00 69.80 O ANISOU 1930 OD1 ASP A 252 12241 7163 7118 -113 658 -628 O ATOM 1931 OD2 ASP A 252 18.287 -63.241 115.800 1.00 68.15 O ANISOU 1931 OD2 ASP A 252 11871 7094 6927 -403 613 -811 O ATOM 1932 N VAL A 253 21.503 -61.912 118.265 1.00 68.06 N ANISOU 1932 N VAL A 253 11834 7296 6728 211 218 -707 N ATOM 1933 CA VAL A 253 22.215 -62.176 119.511 1.00 69.92 C ANISOU 1933 CA VAL A 253 12125 7610 6831 373 139 -560 C ATOM 1934 C VAL A 253 21.363 -63.012 120.468 1.00 72.17 C ANISOU 1934 C VAL A 253 12536 7913 6972 383 293 -415 C ATOM 1935 O VAL A 253 20.127 -62.977 120.408 1.00 72.08 O ANISOU 1935 O VAL A 253 12540 7918 6930 273 421 -465 O ATOM 1936 CB VAL A 253 22.634 -60.861 120.227 1.00 69.73 C ANISOU 1936 CB VAL A 253 12055 7777 6661 428 -92 -664 C ATOM 1937 CG1 VAL A 253 23.585 -60.052 119.367 1.00 68.18 C ANISOU 1937 CG1 VAL A 253 11719 7560 6628 412 -255 -762 C ATOM 1938 CG2 VAL A 253 21.420 -60.036 120.599 1.00 68.81 C ANISOU 1938 CG2 VAL A 253 11969 7757 6417 372 -45 -811 C ATOM 1939 N GLU A 254 22.035 -63.775 121.330 1.00 74.59 N ANISOU 1939 N GLU A 254 12907 8227 7207 515 281 -198 N ATOM 1940 CA GLU A 254 21.407 -64.395 122.485 1.00 77.09 C ANISOU 1940 CA GLU A 254 13338 8621 7331 552 386 -21 C ATOM 1941 C GLU A 254 21.203 -63.258 123.491 1.00 77.89 C ANISOU 1941 C GLU A 254 13461 8993 7141 586 247 -131 C ATOM 1942 O GLU A 254 22.159 -62.547 123.822 1.00 78.22 O ANISOU 1942 O GLU A 254 13470 9154 7095 651 16 -182 O ATOM 1943 CB GLU A 254 22.327 -65.487 123.050 1.00 79.50 C ANISOU 1943 CB GLU A 254 13687 8859 7662 697 389 281 C ATOM 1944 CG GLU A 254 21.916 -66.072 124.417 1.00 82.65 C ANISOU 1944 CG GLU A 254 14198 9389 7815 760 452 528 C ATOM 1945 CD GLU A 254 23.115 -66.409 125.317 1.00 85.10 C ANISOU 1945 CD GLU A 254 14498 9817 8020 934 282 806 C ATOM 1946 OE1 GLU A 254 24.232 -66.626 124.791 1.00 85.35 O ANISOU 1946 OE1 GLU A 254 14424 9739 8267 1025 193 884 O ATOM 1947 OE2 GLU A 254 22.941 -66.455 126.556 1.00 86.75 O ANISOU 1947 OE2 GLU A 254 14791 10249 7921 979 238 967 O ATOM 1948 N ALA A 255 19.967 -63.070 123.956 1.00 78.69 N ANISOU 1948 N ALA A 255 13616 9183 7099 535 397 -176 N ATOM 1949 CA ALA A 255 19.664 -61.985 124.900 1.00 80.00 C ANISOU 1949 CA ALA A 255 13841 9576 6979 579 331 -319 C ATOM 1950 C ALA A 255 20.668 -62.000 126.047 1.00 82.58 C ANISOU 1950 C ALA A 255 14266 10078 7031 684 140 -207 C ATOM 1951 O ALA A 255 20.896 -63.042 126.667 1.00 84.56 O ANISOU 1951 O ALA A 255 14578 10355 7197 743 185 75 O ATOM 1952 CB ALA A 255 18.234 -62.091 125.425 1.00 81.10 C ANISOU 1952 CB ALA A 255 14028 9795 6993 552 585 -292 C ATOM 1953 N GLY A 256 21.285 -60.850 126.299 1.00 82.93 N ANISOU 1953 N GLY A 256 14321 10237 6951 690 -88 -409 N ATOM 1954 CA GLY A 256 22.357 -60.757 127.285 1.00 85.80 C ANISOU 1954 CA GLY A 256 14755 10792 7052 741 -342 -317 C ATOM 1955 C GLY A 256 23.718 -61.129 126.715 1.00 85.51 C ANISOU 1955 C GLY A 256 14563 10678 7248 767 -551 -162 C ATOM 1956 O GLY A 256 24.572 -61.679 127.417 1.00 88.00 O ANISOU 1956 O GLY A 256 14877 11120 7438 833 -704 93 O ATOM 1957 N GLU A 257 23.907 -60.845 125.430 1.00 82.81 N ANISOU 1957 N GLU A 257 14074 10143 7248 724 -545 -286 N ATOM 1958 CA GLU A 257 25.220 -60.916 124.789 1.00 82.39 C ANISOU 1958 CA GLU A 257 13849 10026 7429 751 -728 -191 C ATOM 1959 C GLU A 257 25.381 -59.663 123.930 1.00 80.16 C ANISOU 1959 C GLU A 257 13468 9687 7303 655 -842 -475 C ATOM 1960 O GLU A 257 26.166 -59.626 122.980 1.00 78.83 O ANISOU 1960 O GLU A 257 13133 9414 7405 652 -902 -449 O ATOM 1961 CB GLU A 257 25.358 -62.194 123.950 1.00 81.68 C ANISOU 1961 CB GLU A 257 13685 9710 7638 817 -524 19 C ATOM 1962 N GLU A 258 24.622 -58.635 124.293 1.00 79.99 N ANISOU 1962 N GLU A 258 13552 9728 7114 588 -846 -731 N ATOM 1963 CA GLU A 258 24.529 -57.410 123.515 1.00 78.21 C ANISOU 1963 CA GLU A 258 13254 9415 7049 502 -908 -991 C ATOM 1964 C GLU A 258 25.731 -56.509 123.782 1.00 79.21 C ANISOU 1964 C GLU A 258 13325 9624 7149 445 -1239 -1061 C ATOM 1965 O GLU A 258 26.201 -55.810 122.888 1.00 77.63 O ANISOU 1965 O GLU A 258 12980 9324 7192 380 -1335 -1149 O ATOM 1966 CB GLU A 258 23.211 -56.697 123.836 1.00 78.38 C ANISOU 1966 CB GLU A 258 13403 9437 6939 484 -744 -1210 C ATOM 1967 CG GLU A 258 22.001 -57.649 123.889 1.00 79.27 C ANISOU 1967 CG GLU A 258 13567 9532 7021 522 -439 -1092 C ATOM 1968 CD GLU A 258 20.682 -56.961 124.245 1.00 81.42 C ANISOU 1968 CD GLU A 258 13921 9829 7186 531 -247 -1264 C ATOM 1969 OE1 GLU A 258 20.581 -56.370 125.350 1.00 83.72 O ANISOU 1969 OE1 GLU A 258 14379 10245 7185 571 -272 -1390 O ATOM 1970 OE2 GLU A 258 19.735 -57.037 123.422 1.00 80.18 O ANISOU 1970 OE2 GLU A 258 13659 9575 7232 496 -62 -1262 O ATOM 1971 N ALA A 259 26.234 -56.559 125.013 1.00 82.06 N ANISOU 1971 N ALA A 259 13794 10181 7204 450 -1424 -999 N ATOM 1972 CA ALA A 259 27.361 -55.740 125.450 1.00 84.02 C ANISOU 1972 CA ALA A 259 14005 10546 7372 350 -1782 -1057 C ATOM 1973 C ALA A 259 28.668 -56.118 124.759 1.00 83.75 C ANISOU 1973 C ALA A 259 13694 10501 7628 359 -1950 -814 C ATOM 1974 O ALA A 259 28.814 -57.229 124.241 1.00 82.91 O ANISOU 1974 O ALA A 259 13472 10327 7704 480 -1789 -565 O ATOM 1975 CB ALA A 259 27.518 -55.834 126.955 1.00 87.75 C ANISOU 1975 CB ALA A 259 14674 11273 7394 331 -1942 -1021 C ATOM 1976 N GLY A 260 29.609 -55.177 124.750 1.00 84.90 N ANISOU 1976 N GLY A 260 13735 10696 7827 229 -2256 -892 N ATOM 1977 CA GLY A 260 30.929 -55.395 124.164 1.00 85.13 C ANISOU 1977 CA GLY A 260 13463 10749 8135 231 -2431 -646 C ATOM 1978 C GLY A 260 30.970 -55.259 122.653 1.00 82.00 C ANISOU 1978 C GLY A 260 12878 10138 8142 250 -2258 -667 C ATOM 1979 O GLY A 260 32.050 -55.134 122.073 1.00 82.50 O ANISOU 1979 O GLY A 260 12683 10209 8453 229 -2391 -518 O ATOM 1980 N LEU A 261 29.799 -55.287 122.017 1.00 79.14 N ANISOU 1980 N LEU A 261 12630 9607 7834 282 -1963 -830 N ATOM 1981 CA LEU A 261 29.686 -55.200 120.558 1.00 76.23 C ANISOU 1981 CA LEU A 261 12118 9060 7786 283 -1785 -854 C ATOM 1982 C LEU A 261 29.676 -53.757 120.065 1.00 75.63 C ANISOU 1982 C LEU A 261 11997 8906 7832 135 -1908 -1075 C ATOM 1983 O LEU A 261 29.315 -52.834 120.810 1.00 76.91 O ANISOU 1983 O LEU A 261 12313 9082 7826 47 -2035 -1290 O ATOM 1984 CB LEU A 261 28.419 -55.906 120.073 1.00 74.01 C ANISOU 1984 CB LEU A 261 11963 8658 7501 348 -1447 -898 C ATOM 1985 CG LEU A 261 28.335 -57.430 120.145 1.00 74.10 C ANISOU 1985 CG LEU A 261 12009 8646 7501 482 -1245 -677 C ATOM 1986 CD1 LEU A 261 26.901 -57.874 119.941 1.00 72.33 C ANISOU 1986 CD1 LEU A 261 11944 8327 7213 474 -971 -772 C ATOM 1987 CD2 LEU A 261 29.231 -58.069 119.109 1.00 73.76 C ANISOU 1987 CD2 LEU A 261 11779 8509 7736 550 -1157 -502 C ATOM 1988 N ALA A 262 30.069 -53.570 118.805 1.00 73.96 N ANISOU 1988 N ALA A 262 11590 8599 7911 112 -1849 -1020 N ATOM 1989 CA ALA A 262 30.086 -52.246 118.186 1.00 73.34 C ANISOU 1989 CA ALA A 262 11441 8426 8000 -24 -1944 -1172 C ATOM 1990 C ALA A 262 29.973 -52.323 116.672 1.00 71.11 C ANISOU 1990 C ALA A 262 11012 8042 7965 -19 -1749 -1108 C ATOM 1991 O ALA A 262 30.458 -53.273 116.050 1.00 70.68 O ANISOU 1991 O ALA A 262 10847 8005 8004 66 -1613 -927 O ATOM 1992 CB ALA A 262 31.337 -51.475 118.587 1.00 75.82 C ANISOU 1992 CB ALA A 262 11615 8813 8380 -148 -2280 -1133 C ATOM 1993 N CYS A 263 29.329 -51.311 116.094 1.00 70.06 N ANISOU 1993 N CYS A 263 10889 7800 7929 -108 -1724 -1252 N ATOM 1994 CA CYS A 263 29.124 -51.222 114.653 1.00 68.33 C ANISOU 1994 CA CYS A 263 10545 7516 7902 -136 -1566 -1192 C ATOM 1995 C CYS A 263 30.182 -50.312 114.026 1.00 69.12 C ANISOU 1995 C CYS A 263 10426 7598 8237 -240 -1727 -1110 C ATOM 1996 O CYS A 263 30.307 -49.151 114.410 1.00 70.37 O ANISOU 1996 O CYS A 263 10586 7689 8461 -346 -1920 -1214 O ATOM 1997 CB CYS A 263 27.713 -50.699 114.347 1.00 66.94 C ANISOU 1997 CB CYS A 263 10476 7253 7707 -162 -1439 -1330 C ATOM 1998 SG CYS A 263 27.307 -50.677 112.580 1.00 65.77 S ANISOU 1998 SG CYS A 263 10189 7080 7719 -224 -1264 -1229 S ATOM 1999 N ARG A 264 30.941 -50.852 113.073 1.00 68.80 N ANISOU 1999 N ARG A 264 10207 7605 8328 -212 -1628 -926 N ATOM 2000 CA ARG A 264 31.995 -50.109 112.382 1.00 69.82 C ANISOU 2000 CA ARG A 264 10091 7744 8695 -305 -1739 -795 C ATOM 2001 C ARG A 264 31.593 -49.841 110.931 1.00 68.64 C ANISOU 2001 C ARG A 264 9873 7557 8651 -351 -1556 -749 C ATOM 2002 O ARG A 264 31.161 -50.752 110.213 1.00 67.61 O ANISOU 2002 O ARG A 264 9801 7453 8434 -285 -1312 -724 O ATOM 2003 CB ARG A 264 33.307 -50.892 112.423 1.00 71.36 C ANISOU 2003 CB ARG A 264 10094 8052 8967 -221 -1750 -575 C ATOM 2004 CG ARG A 264 34.569 -50.054 112.263 1.00 73.81 C ANISOU 2004 CG ARG A 264 10122 8409 9512 -335 -1964 -422 C ATOM 2005 CD ARG A 264 35.789 -50.951 112.032 1.00 75.85 C ANISOU 2005 CD ARG A 264 10137 8791 9890 -208 -1885 -149 C ATOM 2006 NE ARG A 264 36.997 -50.433 112.679 1.00 79.06 N ANISOU 2006 NE ARG A 264 10296 9302 10441 -304 -2200 9 N ATOM 2007 CZ ARG A 264 37.432 -50.806 113.885 1.00 80.82 C ANISOU 2007 CZ ARG A 264 10514 9632 10561 -278 -2418 66 C ATOM 2008 NH1 ARG A 264 36.770 -51.706 114.600 1.00 80.11 N ANISOU 2008 NH1 ARG A 264 10660 9547 10232 -140 -2333 -12 N ATOM 2009 NH2 ARG A 264 38.538 -50.279 114.383 1.00 83.70 N ANISOU 2009 NH2 ARG A 264 10628 10115 11058 -410 -2735 226 N ATOM 2010 N VAL A 265 31.734 -48.586 110.506 1.00 69.21 N ANISOU 2010 N VAL A 265 9832 7563 8900 -484 -1680 -735 N ATOM 2011 CA VAL A 265 31.370 -48.174 109.148 1.00 68.28 C ANISOU 2011 CA VAL A 265 9634 7435 8876 -547 -1543 -651 C ATOM 2012 C VAL A 265 32.588 -47.641 108.402 1.00 69.77 C ANISOU 2012 C VAL A 265 9554 7664 9290 -628 -1594 -444 C ATOM 2013 O VAL A 265 33.222 -46.688 108.852 1.00 71.56 O ANISOU 2013 O VAL A 265 9670 7827 9693 -734 -1824 -421 O ATOM 2014 CB VAL A 265 30.266 -47.094 109.160 1.00 67.74 C ANISOU 2014 CB VAL A 265 9655 7234 8851 -620 -1601 -762 C ATOM 2015 CG1 VAL A 265 30.007 -46.568 107.754 1.00 67.62 C ANISOU 2015 CG1 VAL A 265 9514 7233 8946 -700 -1504 -610 C ATOM 2016 CG2 VAL A 265 28.986 -47.645 109.756 1.00 66.61 C ANISOU 2016 CG2 VAL A 265 9736 7075 8499 -534 -1502 -928 C ATOM 2017 N LYS A 266 32.910 -48.264 107.270 1.00 69.55 N ANISOU 2017 N LYS A 266 9433 7742 9249 -590 -1370 -299 N ATOM 2018 CA LYS A 266 34.006 -47.803 106.416 1.00 71.15 C ANISOU 2018 CA LYS A 266 9368 8013 9654 -655 -1354 -71 C ATOM 2019 C LYS A 266 33.475 -47.244 105.096 1.00 70.88 C ANISOU 2019 C LYS A 266 9306 7999 9626 -751 -1231 16 C ATOM 2020 O LYS A 266 32.848 -47.961 104.317 1.00 69.80 O ANISOU 2020 O LYS A 266 9291 7939 9289 -716 -1008 -12 O ATOM 2021 CB LYS A 266 35.021 -48.924 106.161 1.00 72.13 C ANISOU 2021 CB LYS A 266 9375 8259 9772 -515 -1164 65 C ATOM 2022 CG LYS A 266 35.881 -49.269 107.359 1.00 73.31 C ANISOU 2022 CG LYS A 266 9432 8427 9994 -440 -1336 103 C ATOM 2023 CD LYS A 266 37.100 -50.082 106.969 1.00 75.13 C ANISOU 2023 CD LYS A 266 9436 8775 10335 -299 -1155 332 C ATOM 2024 CE LYS A 266 37.880 -50.502 108.210 1.00 77.11 C ANISOU 2024 CE LYS A 266 9578 9072 10648 -216 -1349 413 C ATOM 2025 NZ LYS A 266 39.216 -51.077 107.897 1.00 79.91 N ANISOU 2025 NZ LYS A 266 9617 9547 11200 -78 -1214 708 N ATOM 2026 N HIS A 267 33.725 -45.957 104.858 1.00 72.25 N ANISOU 2026 N HIS A 267 9325 8103 10024 -891 -1390 130 N ATOM 2027 CA HIS A 267 33.300 -45.292 103.623 1.00 72.50 C ANISOU 2027 CA HIS A 267 9294 8164 10088 -992 -1304 279 C ATOM 2028 C HIS A 267 34.416 -44.436 103.029 1.00 74.73 C ANISOU 2028 C HIS A 267 9289 8468 10636 -1106 -1356 544 C ATOM 2029 O HIS A 267 35.285 -43.944 103.746 1.00 76.23 O ANISOU 2029 O HIS A 267 9337 8579 11047 -1162 -1552 578 O ATOM 2030 CB HIS A 267 32.040 -44.454 103.865 1.00 71.62 C ANISOU 2030 CB HIS A 267 9315 7899 9999 -1044 -1421 177 C ATOM 2031 CG HIS A 267 31.322 -44.056 102.611 1.00 72.16 C ANISOU 2031 CG HIS A 267 9350 8041 10025 -1117 -1318 340 C ATOM 2032 ND1 HIS A 267 30.981 -42.750 102.331 1.00 73.65 N ANISOU 2032 ND1 HIS A 267 9447 8095 10440 -1212 -1437 477 N ATOM 2033 CD2 HIS A 267 30.877 -44.792 101.563 1.00 72.18 C ANISOU 2033 CD2 HIS A 267 9408 8244 9775 -1120 -1116 400 C ATOM 2034 CE1 HIS A 267 30.359 -42.697 101.166 1.00 73.90 C ANISOU 2034 CE1 HIS A 267 9450 8269 10360 -1263 -1326 651 C ATOM 2035 NE2 HIS A 267 30.283 -43.923 100.679 1.00 73.17 N ANISOU 2035 NE2 HIS A 267 9454 8393 9954 -1225 -1141 594 N ATOM 2036 N SER A 268 34.386 -44.278 101.711 1.00 75.41 N ANISOU 2036 N SER A 268 9289 8680 10683 -1161 -1186 743 N ATOM 2037 CA SER A 268 35.324 -43.421 100.997 1.00 77.93 C ANISOU 2037 CA SER A 268 9329 9035 11245 -1281 -1200 1039 C ATOM 2038 C SER A 268 35.220 -41.964 101.448 1.00 79.20 C ANISOU 2038 C SER A 268 9414 8955 11722 -1432 -1478 1087 C ATOM 2039 O SER A 268 36.201 -41.222 101.418 1.00 81.52 O ANISOU 2039 O SER A 268 9472 9200 12301 -1553 -1588 1278 O ATOM 2040 CB SER A 268 35.057 -43.511 99.498 1.00 78.42 C ANISOU 2040 CB SER A 268 9372 9293 11132 -1318 -960 1230 C ATOM 2041 OG SER A 268 33.669 -43.407 99.230 1.00 76.91 O ANISOU 2041 OG SER A 268 9379 9084 10760 -1342 -973 1140 O ATOM 2042 N SER A 269 34.025 -41.572 101.880 1.00 78.11 N ANISOU 2042 N SER A 269 9478 8651 11548 -1423 -1575 914 N ATOM 2043 CA SER A 269 33.724 -40.194 102.252 1.00 79.46 C ANISOU 2043 CA SER A 269 9635 8540 12015 -1537 -1784 929 C ATOM 2044 C SER A 269 34.603 -39.644 103.375 1.00 81.22 C ANISOU 2044 C SER A 269 9805 8568 12485 -1632 -2031 825 C ATOM 2045 O SER A 269 35.042 -38.495 103.316 1.00 83.68 O ANISOU 2045 O SER A 269 9987 8689 13119 -1796 -2177 959 O ATOM 2046 CB SER A 269 32.248 -40.073 102.645 1.00 77.86 C ANISOU 2046 CB SER A 269 9670 8204 11711 -1452 -1792 733 C ATOM 2047 OG SER A 269 31.745 -38.779 102.376 1.00 79.55 O ANISOU 2047 OG SER A 269 9839 8191 12195 -1529 -1873 866 O ATOM 2048 N LEU A 270 34.866 -40.470 104.382 1.00 80.49 N ANISOU 2048 N LEU A 270 9814 8529 12238 -1549 -2088 602 N ATOM 2049 CA LEU A 270 35.467 -40.000 105.632 1.00 82.52 C ANISOU 2049 CA LEU A 270 10090 8619 12643 -1653 -2365 443 C ATOM 2050 C LEU A 270 37.007 -39.986 105.680 1.00 85.18 C ANISOU 2050 C LEU A 270 10130 9067 13166 -1780 -2491 643 C ATOM 2051 O LEU A 270 37.605 -39.341 106.551 1.00 87.35 O ANISOU 2051 O LEU A 270 10373 9200 13616 -1950 -2771 569 O ATOM 2052 CB LEU A 270 34.899 -40.806 106.800 1.00 80.78 C ANISOU 2052 CB LEU A 270 10135 8410 12146 -1515 -2397 124 C ATOM 2053 CG LEU A 270 34.757 -42.310 106.578 1.00 78.60 C ANISOU 2053 CG LEU A 270 9903 8394 11568 -1319 -2173 120 C ATOM 2054 CD1 LEU A 270 36.075 -43.050 106.824 1.00 79.83 C ANISOU 2054 CD1 LEU A 270 9859 8734 11737 -1299 -2208 247 C ATOM 2055 CD2 LEU A 270 33.651 -42.855 107.465 1.00 76.86 C ANISOU 2055 CD2 LEU A 270 9987 8126 11091 -1188 -2148 -171 C ATOM 2056 N GLY A 271 37.638 -40.684 104.740 1.00 85.39 N ANISOU 2056 N GLY A 271 9939 9350 13154 -1707 -2278 898 N ATOM 2057 CA GLY A 271 39.084 -40.865 104.759 1.00 88.06 C ANISOU 2057 CA GLY A 271 9953 9842 13663 -1774 -2341 1126 C ATOM 2058 C GLY A 271 39.393 -42.140 105.518 1.00 87.49 C ANISOU 2058 C GLY A 271 9922 9939 13380 -1596 -2315 1018 C ATOM 2059 O GLY A 271 39.017 -43.230 105.086 1.00 85.54 O ANISOU 2059 O GLY A 271 9776 9835 12892 -1383 -2034 990 O ATOM 2060 N GLY A 272 40.061 -42.004 106.660 1.00 89.46 N ANISOU 2060 N GLY A 272 10107 10167 13717 -1697 -2618 961 N ATOM 2061 CA GLY A 272 40.371 -43.151 107.512 1.00 89.15 C ANISOU 2061 CA GLY A 272 10094 10286 13493 -1536 -2640 896 C ATOM 2062 C GLY A 272 39.480 -43.271 108.738 1.00 87.89 C ANISOU 2062 C GLY A 272 10298 10007 13089 -1511 -2806 540 C ATOM 2063 O GLY A 272 39.409 -44.340 109.351 1.00 87.06 O ANISOU 2063 O GLY A 272 10289 10022 12768 -1336 -2758 471 O ATOM 2064 N GLN A 273 38.789 -42.184 109.087 1.00 87.98 N ANISOU 2064 N GLN A 273 10515 9772 13143 -1671 -2971 325 N ATOM 2065 CA GLN A 273 38.042 -42.095 110.350 1.00 87.59 C ANISOU 2065 CA GLN A 273 10806 9596 12880 -1678 -3141 -22 C ATOM 2066 C GLN A 273 36.700 -42.834 110.343 1.00 84.13 C ANISOU 2066 C GLN A 273 10670 9146 12148 -1445 -2884 -220 C ATOM 2067 O GLN A 273 35.650 -42.226 110.124 1.00 83.12 O ANISOU 2067 O GLN A 273 10732 8830 12018 -1443 -2803 -367 O ATOM 2068 CB GLN A 273 37.856 -40.629 110.764 1.00 89.68 C ANISOU 2068 CB GLN A 273 11190 9562 13322 -1929 -3383 -195 C ATOM 2069 CG GLN A 273 39.130 -39.977 111.304 1.00 94.16 C ANISOU 2069 CG GLN A 273 11545 10130 14103 -2220 -3746 -102 C ATOM 2070 CD GLN A 273 38.972 -38.495 111.639 1.00 97.09 C ANISOU 2070 CD GLN A 273 12063 10147 14681 -2497 -3966 -292 C ATOM 2071 OE1 GLN A 273 37.898 -37.910 111.473 1.00 96.14 O ANISOU 2071 OE1 GLN A 273 12195 9762 14570 -2439 -3829 -479 O ATOM 2072 NE2 GLN A 273 40.056 -37.882 112.112 1.00100.68 N ANISOU 2072 NE2 GLN A 273 12349 10582 15322 -2804 -4310 -230 N ATOM 2073 N ASP A 274 36.751 -44.142 110.607 1.00 82.69 N ANISOU 2073 N ASP A 274 10513 9158 11747 -1253 -2761 -197 N ATOM 2074 CA ASP A 274 35.565 -45.008 110.640 1.00 79.71 C ANISOU 2074 CA ASP A 274 10400 8791 11095 -1051 -2522 -357 C ATOM 2075 C ASP A 274 34.553 -44.609 111.706 1.00 79.15 C ANISOU 2075 C ASP A 274 10652 8571 10852 -1065 -2626 -671 C ATOM 2076 O ASP A 274 34.921 -44.145 112.787 1.00 81.35 O ANISOU 2076 O ASP A 274 11003 8806 11099 -1183 -2892 -800 O ATOM 2077 CB ASP A 274 35.962 -46.465 110.900 1.00 79.53 C ANISOU 2077 CB ASP A 274 10346 8964 10909 -863 -2402 -264 C ATOM 2078 CG ASP A 274 37.019 -46.977 109.940 1.00 81.13 C ANISOU 2078 CG ASP A 274 10237 9311 11277 -802 -2247 39 C ATOM 2079 OD1 ASP A 274 37.248 -46.343 108.881 1.00 82.20 O ANISOU 2079 OD1 ASP A 274 10209 9426 11596 -889 -2168 174 O ATOM 2080 OD2 ASP A 274 37.618 -48.031 110.254 1.00 82.49 O ANISOU 2080 OD2 ASP A 274 10326 9618 11398 -653 -2185 160 O ATOM 2081 N ILE A 275 33.276 -44.816 111.399 1.00 76.55 N ANISOU 2081 N ILE A 275 10514 8178 10393 -950 -2408 -789 N ATOM 2082 CA ILE A 275 32.204 -44.596 112.366 1.00 76.04 C ANISOU 2082 CA ILE A 275 10746 7995 10152 -910 -2424 -1066 C ATOM 2083 C ILE A 275 32.076 -45.858 113.225 1.00 75.06 C ANISOU 2083 C ILE A 275 10757 8031 9733 -769 -2376 -1123 C ATOM 2084 O ILE A 275 31.650 -46.904 112.731 1.00 73.25 O ANISOU 2084 O ILE A 275 10537 7899 9395 -631 -2147 -1047 O ATOM 2085 CB ILE A 275 30.823 -44.296 111.683 1.00 74.25 C ANISOU 2085 CB ILE A 275 10619 7654 9938 -840 -2206 -1118 C ATOM 2086 CG1 ILE A 275 30.982 -43.591 110.325 1.00 74.29 C ANISOU 2086 CG1 ILE A 275 10415 7608 10205 -924 -2154 -909 C ATOM 2087 CG2 ILE A 275 29.894 -43.531 112.635 1.00 74.99 C ANISOU 2087 CG2 ILE A 275 10961 7551 9981 -829 -2243 -1385 C ATOM 2088 CD1 ILE A 275 31.387 -42.120 110.394 1.00 77.76 C ANISOU 2088 CD1 ILE A 275 10796 7817 10931 -1090 -2345 -920 C ATOM 2089 N ILE A 276 32.457 -45.767 114.499 1.00 76.49 N ANISOU 2089 N ILE A 276 11050 8236 9778 -821 -2596 -1249 N ATOM 2090 CA ILE A 276 32.335 -46.910 115.397 1.00 75.80 C ANISOU 2090 CA ILE A 276 11093 8306 9403 -691 -2566 -1271 C ATOM 2091 C ILE A 276 31.336 -46.634 116.521 1.00 76.21 C ANISOU 2091 C ILE A 276 11467 8284 9204 -671 -2572 -1554 C ATOM 2092 O ILE A 276 31.662 -45.961 117.498 1.00 78.83 O ANISOU 2092 O ILE A 276 11921 8586 9446 -797 -2808 -1716 O ATOM 2093 CB ILE A 276 33.702 -47.363 115.980 1.00 78.10 C ANISOU 2093 CB ILE A 276 11215 8780 9680 -736 -2801 -1097 C ATOM 2094 CG1 ILE A 276 34.840 -47.118 114.981 1.00 78.67 C ANISOU 2094 CG1 ILE A 276 10936 8887 10068 -813 -2850 -840 C ATOM 2095 CG2 ILE A 276 33.636 -48.837 116.396 1.00 77.14 C ANISOU 2095 CG2 ILE A 276 11138 8822 9350 -541 -2668 -982 C ATOM 2096 CD1 ILE A 276 36.236 -47.224 115.576 1.00 81.65 C ANISOU 2096 CD1 ILE A 276 11086 9435 10502 -906 -3142 -650 C ATOM 2097 N LEU A 277 30.118 -47.155 116.369 1.00 73.91 N ANISOU 2097 N LEU A 277 11315 7972 8794 -525 -2305 -1614 N ATOM 2098 CA LEU A 277 29.063 -46.996 117.379 1.00 74.27 C ANISOU 2098 CA LEU A 277 11648 7967 8605 -467 -2236 -1853 C ATOM 2099 C LEU A 277 29.070 -48.138 118.381 1.00 74.58 C ANISOU 2099 C LEU A 277 11813 8195 8329 -372 -2227 -1827 C ATOM 2100 O LEU A 277 28.984 -49.305 118.002 1.00 73.03 O ANISOU 2100 O LEU A 277 11547 8099 8101 -260 -2069 -1651 O ATOM 2101 CB LEU A 277 27.680 -46.902 116.732 1.00 72.20 C ANISOU 2101 CB LEU A 277 11431 7599 8403 -369 -1957 -1894 C ATOM 2102 CG LEU A 277 27.370 -45.755 115.769 1.00 72.18 C ANISOU 2102 CG LEU A 277 11322 7404 8700 -430 -1927 -1893 C ATOM 2103 CD1 LEU A 277 25.895 -45.806 115.418 1.00 70.72 C ANISOU 2103 CD1 LEU A 277 11186 7170 8514 -314 -1668 -1911 C ATOM 2104 CD2 LEU A 277 27.749 -44.381 116.344 1.00 74.92 C ANISOU 2104 CD2 LEU A 277 11762 7550 9156 -553 -2120 -2084 C ATOM 2105 N TYR A 278 29.159 -47.792 119.661 1.00 77.00 N ANISOU 2105 N TYR A 278 12325 8539 8393 -426 -2388 -2004 N ATOM 2106 CA TYR A 278 29.264 -48.783 120.721 1.00 77.89 C ANISOU 2106 CA TYR A 278 12558 8857 8178 -356 -2421 -1949 C ATOM 2107 C TYR A 278 27.928 -49.025 121.402 1.00 77.51 C ANISOU 2107 C TYR A 278 12773 8803 7873 -235 -2181 -2107 C ATOM 2108 O TYR A 278 27.319 -48.091 121.925 1.00 78.93 O ANISOU 2108 O TYR A 278 13156 8868 7967 -266 -2155 -2373 O ATOM 2109 CB TYR A 278 30.298 -48.334 121.748 1.00 81.58 C ANISOU 2109 CB TYR A 278 13080 9437 8479 -520 -2783 -2008 C ATOM 2110 CG TYR A 278 31.727 -48.548 121.314 1.00 82.46 C ANISOU 2110 CG TYR A 278 12879 9659 8792 -606 -3023 -1740 C ATOM 2111 CD1 TYR A 278 32.398 -47.589 120.555 1.00 82.77 C ANISOU 2111 CD1 TYR A 278 12728 9571 9149 -763 -3168 -1736 C ATOM 2112 CD2 TYR A 278 32.414 -49.710 121.672 1.00 83.62 C ANISOU 2112 CD2 TYR A 278 12902 10034 8837 -521 -3091 -1458 C ATOM 2113 CE1 TYR A 278 33.719 -47.781 120.160 1.00 84.06 C ANISOU 2113 CE1 TYR A 278 12568 9855 9515 -838 -3366 -1460 C ATOM 2114 CE2 TYR A 278 33.734 -49.914 121.283 1.00 85.05 C ANISOU 2114 CE2 TYR A 278 12758 10324 9234 -570 -3285 -1178 C ATOM 2115 CZ TYR A 278 34.380 -48.945 120.527 1.00 85.21 C ANISOU 2115 CZ TYR A 278 12577 10237 9562 -732 -3418 -1183 C ATOM 2116 OH TYR A 278 35.684 -49.143 120.141 1.00 86.72 O ANISOU 2116 OH TYR A 278 12413 10552 9983 -775 -3587 -878 O ATOM 2117 N TRP A 279 27.483 -50.280 121.397 1.00 75.82 N ANISOU 2117 N TRP A 279 12553 8698 7556 -96 -1987 -1937 N ATOM 2118 CA TRP A 279 26.237 -50.648 122.054 1.00 75.89 C ANISOU 2118 CA TRP A 279 12774 8733 7328 14 -1746 -2029 C ATOM 2119 C TRP A 279 26.303 -50.351 123.541 1.00 79.74 C ANISOU 2119 C TRP A 279 13523 9338 7437 -19 -1872 -2196 C ATOM 2120 O TRP A 279 27.151 -50.891 124.251 1.00 81.83 O ANISOU 2120 O TRP A 279 13800 9790 7501 -53 -2077 -2070 O ATOM 2121 CB TRP A 279 25.918 -52.126 121.853 1.00 74.03 C ANISOU 2121 CB TRP A 279 12485 8588 7055 130 -1553 -1788 C ATOM 2122 CG TRP A 279 24.625 -52.525 122.505 1.00 73.82 C ANISOU 2122 CG TRP A 279 12642 8597 6809 224 -1299 -1843 C ATOM 2123 CD1 TRP A 279 24.458 -53.014 123.770 1.00 75.95 C ANISOU 2123 CD1 TRP A 279 13104 9025 6727 274 -1285 -1831 C ATOM 2124 CD2 TRP A 279 23.316 -52.448 121.932 1.00 71.80 C ANISOU 2124 CD2 TRP A 279 12370 8240 6669 272 -1023 -1889 C ATOM 2125 NE1 TRP A 279 23.128 -53.255 124.016 1.00 75.21 N ANISOU 2125 NE1 TRP A 279 13115 8927 6536 357 -991 -1869 N ATOM 2126 CE2 TRP A 279 22.405 -52.916 122.904 1.00 72.87 C ANISOU 2126 CE2 TRP A 279 12679 8474 6535 356 -834 -1900 C ATOM 2127 CE3 TRP A 279 22.823 -52.039 120.685 1.00 69.65 C ANISOU 2127 CE3 TRP A 279 11935 7831 6696 244 -925 -1889 C ATOM 2128 CZ2 TRP A 279 21.033 -52.983 122.671 1.00 72.34 C ANISOU 2128 CZ2 TRP A 279 12600 8365 6521 412 -550 -1907 C ATOM 2129 CZ3 TRP A 279 21.460 -52.105 120.454 1.00 68.94 C ANISOU 2129 CZ3 TRP A 279 11839 7712 6643 293 -672 -1892 C ATOM 2130 CH2 TRP A 279 20.579 -52.572 121.444 1.00 70.40 C ANISOU 2130 CH2 TRP A 279 12172 7990 6588 377 -485 -1899 C ATOM 2131 N GLY A 280 25.404 -49.493 124.008 1.00 81.32 N ANISOU 2131 N GLY A 280 13933 9434 7531 -3 -1741 -2470 N ATOM 2132 CA GLY A 280 25.302 -49.183 125.428 1.00 85.32 C ANISOU 2132 CA GLY A 280 14748 10047 7622 -30 -1798 -2680 C ATOM 2133 C GLY A 280 26.264 -48.114 125.898 1.00 88.65 C ANISOU 2133 C GLY A 280 15277 10428 7978 -230 -2133 -2897 C ATOM 2134 O GLY A 280 26.464 -47.949 127.101 1.00 92.30 O ANISOU 2134 O GLY A 280 16000 11028 8041 -307 -2265 -3057 O ATOM 2135 N SER A 281 26.866 -47.397 124.952 1.00 87.88 N ANISOU 2135 N SER A 281 14984 10152 8256 -337 -2279 -2896 N ATOM 2136 CA SER A 281 27.665 -46.213 125.262 1.00 91.40 C ANISOU 2136 CA SER A 281 15523 10486 8718 -560 -2578 -3125 C ATOM 2137 C SER A 281 26.743 -45.095 125.728 1.00 93.78 C ANISOU 2137 C SER A 281 16139 10545 8950 -541 -2391 -3518 C ATOM 2138 O SER A 281 25.562 -45.088 125.378 1.00 92.05 O ANISOU 2138 O SER A 281 15934 10201 8840 -346 -2033 -3543 O ATOM 2139 CB SER A 281 28.453 -45.756 124.032 1.00 89.74 C ANISOU 2139 CB SER A 281 14995 10130 8972 -666 -2729 -2980 C ATOM 2140 OG SER A 281 27.594 -45.464 122.938 1.00 87.15 O ANISOU 2140 OG SER A 281 14549 9583 8981 -540 -2445 -2956 O ATOM 2141 N LEU A 282 27.278 -44.156 126.510 1.00 98.34 N ANISOU 2141 N LEU A 282 16964 11048 9354 -748 -2627 -3817 N ATOM 2142 CA LEU A 282 26.502 -43.001 126.980 1.00101.65 C ANISOU 2142 CA LEU A 282 17723 11177 9724 -734 -2437 -4234 C ATOM 2143 C LEU A 282 25.844 -42.278 125.805 1.00 99.60 C ANISOU 2143 C LEU A 282 17291 10565 9986 -615 -2194 -4220 C ATOM 2144 O LEU A 282 24.805 -41.641 125.965 1.00100.90 O ANISOU 2144 O LEU A 282 17646 10498 10193 -464 -1877 -4443 O ATOM 2145 CB LEU A 282 27.373 -42.036 127.790 1.00106.57 C ANISOU 2145 CB LEU A 282 18619 11720 10153 -1041 -2782 -4563 C ATOM 2146 N HIS A 283 26.456 -42.408 124.627 1.00 96.89 N ANISOU 2146 N HIS A 283 16578 10202 10034 -671 -2333 -3928 N ATOM 2147 CA HIS A 283 25.916 -41.886 123.371 1.00 94.80 C ANISOU 2147 CA HIS A 283 16091 9677 10252 -570 -2139 -3815 C ATOM 2148 C HIS A 283 24.686 -42.679 122.898 1.00 91.63 C ANISOU 2148 C HIS A 283 15567 9365 9885 -299 -1770 -3626 C ATOM 2149 O HIS A 283 23.616 -42.098 122.699 1.00 91.96 O ANISOU 2149 O HIS A 283 15655 9196 10089 -143 -1481 -3715 O ATOM 2150 CB HIS A 283 27.013 -41.885 122.294 1.00 93.00 C ANISOU 2150 CB HIS A 283 15512 9463 10361 -728 -2400 -3540 C ATOM 2151 CG HIS A 283 26.641 -41.153 121.039 1.00 91.73 C ANISOU 2151 CG HIS A 283 15144 9033 10675 -683 -2265 -3428 C ATOM 2152 ND1 HIS A 283 26.534 -41.779 119.816 0.70 87.96 N ANISOU 2152 ND1 HIS A 283 14338 8662 10419 -598 -2170 -3089 N ATOM 2153 CD2 HIS A 283 26.361 -39.845 120.818 0.70 93.94 C ANISOU 2153 CD2 HIS A 283 15509 8942 11242 -718 -2210 -3598 C ATOM 2154 CE1 HIS A 283 26.200 -40.891 118.896 0.70 87.72 C ANISOU 2154 CE1 HIS A 283 14185 8377 10767 -588 -2081 -3032 C ATOM 2155 NE2 HIS A 283 26.088 -39.711 119.478 0.70 91.33 N ANISOU 2155 NE2 HIS A 283 14876 8528 11296 -648 -2098 -3321 N ATOM 2156 N HIS A 284 24.851 -43.995 122.726 1.00 89.07 N ANISOU 2156 N HIS A 284 15077 9338 9426 -251 -1783 -3354 N ATOM 2157 CA HIS A 284 23.772 -44.912 122.306 1.00 86.23 C ANISOU 2157 CA HIS A 284 14600 9090 9072 -50 -1475 -3159 C ATOM 2158 C HIS A 284 22.501 -44.773 123.157 1.00 88.29 C ANISOU 2158 C HIS A 284 15101 9320 9126 123 -1158 -3348 C ATOM 2159 O HIS A 284 21.390 -44.774 122.622 1.00 86.90 O ANISOU 2159 O HIS A 284 14811 9076 9131 276 -875 -3259 O ATOM 2160 CB HIS A 284 24.286 -46.367 122.295 1.00 84.09 C ANISOU 2160 CB HIS A 284 14207 9114 8628 -52 -1557 -2895 C ATOM 2161 CG HIS A 284 23.218 -47.407 122.102 1.00 81.55 C ANISOU 2161 CG HIS A 284 13829 8910 8248 109 -1263 -2729 C ATOM 2162 ND1 HIS A 284 22.293 -47.355 121.080 1.00 79.15 N ANISOU 2162 ND1 HIS A 284 13349 8511 8215 186 -1048 -2618 N ATOM 2163 CD2 HIS A 284 22.949 -48.544 122.788 1.00 80.90 C ANISOU 2163 CD2 HIS A 284 13830 9036 7874 183 -1168 -2629 C ATOM 2164 CE1 HIS A 284 21.491 -48.402 121.157 1.00 77.19 C ANISOU 2164 CE1 HIS A 284 13081 8403 7844 280 -841 -2479 C ATOM 2165 NE2 HIS A 284 21.870 -49.141 122.183 1.00 78.30 N ANISOU 2165 NE2 HIS A 284 13381 8713 7656 286 -897 -2482 N ATOM 2166 N ILE A 285 22.680 -44.643 124.472 1.00 92.04 N ANISOU 2166 N ILE A 285 15895 9863 9213 90 -1207 -3593 N ATOM 2167 CA ILE A 285 21.573 -44.426 125.409 1.00 95.02 C ANISOU 2167 CA ILE A 285 16542 10215 9346 253 -885 -3810 C ATOM 2168 C ILE A 285 20.914 -43.062 125.192 1.00 97.31 C ANISOU 2168 C ILE A 285 16914 10138 9920 338 -685 -4043 C ATOM 2169 O ILE A 285 19.686 -42.965 125.183 1.00 97.64 O ANISOU 2169 O ILE A 285 16945 10113 10042 554 -316 -4037 O ATOM 2170 CB ILE A 285 22.025 -44.581 126.890 1.00 98.81 C ANISOU 2170 CB ILE A 285 17382 10881 9281 169 -1006 -4032 C ATOM 2171 CG1 ILE A 285 22.537 -46.006 127.144 1.00 97.13 C ANISOU 2171 CG1 ILE A 285 17067 11029 8808 136 -1156 -3736 C ATOM 2172 CG2 ILE A 285 20.881 -44.234 127.854 1.00102.04 C ANISOU 2172 CG2 ILE A 285 18101 11246 9424 347 -626 -4291 C ATOM 2173 CD1 ILE A 285 23.290 -46.189 128.457 1.00100.75 C ANISOU 2173 CD1 ILE A 285 17811 11722 8749 -3 -1398 -3865 C ATOM 2174 N LEU A 286 21.732 -42.024 125.012 1.00 99.34 N ANISOU 2174 N LEU A 286 17234 10151 10358 168 -922 -4220 N ATOM 2175 CA LEU A 286 21.231 -40.674 124.729 1.00102.00 C ANISOU 2175 CA LEU A 286 17645 10077 11034 238 -750 -4420 C ATOM 2176 C LEU A 286 20.329 -40.640 123.495 1.00 99.26 C ANISOU 2176 C LEU A 286 16944 9630 11140 419 -518 -4120 C ATOM 2177 O LEU A 286 19.274 -40.007 123.506 1.00101.19 O ANISOU 2177 O LEU A 286 17224 9660 11565 628 -185 -4193 O ATOM 2178 CB LEU A 286 22.383 -39.670 124.571 1.00103.95 C ANISOU 2178 CB LEU A 286 17963 10075 11459 -23 -1090 -4588 C ATOM 2179 CG LEU A 286 22.960 -39.001 125.825 1.00109.36 C ANISOU 2179 CG LEU A 286 19096 10658 11797 -205 -1245 -5031 C ATOM 2180 CD1 LEU A 286 24.257 -38.277 125.482 1.00110.71 C ANISOU 2180 CD1 LEU A 286 19225 10662 12177 -528 -1664 -5082 C ATOM 2181 CD2 LEU A 286 21.961 -38.049 126.488 1.00113.52 C ANISOU 2181 CD2 LEU A 286 19978 10854 12302 -26 -862 -5409 C ATOM 2182 N ASP A 287 20.746 -41.329 122.440 1.00 95.42 N ANISOU 2182 N ASP A 287 16117 9310 10828 340 -690 -3776 N ATOM 2183 CA ASP A 287 19.936 -41.445 121.236 1.00 93.04 C ANISOU 2183 CA ASP A 287 15477 8992 10883 464 -519 -3465 C ATOM 2184 C ASP A 287 18.634 -42.205 121.508 1.00 92.53 C ANISOU 2184 C ASP A 287 15369 9107 10681 675 -184 -3357 C ATOM 2185 O ASP A 287 17.552 -41.689 121.240 1.00 93.59 O ANISOU 2185 O ASP A 287 15407 9099 11053 858 94 -3302 O ATOM 2186 CB ASP A 287 20.734 -42.116 120.106 1.00 89.48 C ANISOU 2186 CB ASP A 287 14723 8711 10565 309 -769 -3156 C ATOM 2187 CG ASP A 287 21.947 -41.294 119.668 1.00 90.67 C ANISOU 2187 CG ASP A 287 14837 8682 10930 106 -1069 -3194 C ATOM 2188 OD1 ASP A 287 22.463 -40.495 120.487 1.00 94.65 O ANISOU 2188 OD1 ASP A 287 15600 9002 11359 14 -1183 -3490 O ATOM 2189 OD2 ASP A 287 22.385 -41.451 118.504 1.00 88.37 O ANISOU 2189 OD2 ASP A 287 14266 8440 10872 22 -1188 -2928 O ATOM 2190 N ALA A 288 18.749 -43.413 122.063 1.00 91.32 N ANISOU 2190 N ALA A 288 15273 9260 10164 651 -208 -3301 N ATOM 2191 CA ALA A 288 17.600 -44.296 122.298 1.00 90.69 C ANISOU 2191 CA ALA A 288 15128 9380 9950 806 83 -3153 C ATOM 2192 C ALA A 288 16.503 -43.683 123.177 1.00 94.37 C ANISOU 2192 C ALA A 288 15776 9733 10348 1026 450 -3346 C ATOM 2193 O ALA A 288 15.318 -43.947 122.966 1.00 94.25 O ANISOU 2193 O ALA A 288 15582 9780 10447 1186 739 -3166 O ATOM 2194 CB ALA A 288 18.065 -45.625 122.872 1.00 89.55 C ANISOU 2194 CB ALA A 288 15061 9539 9425 729 -23 -3074 C ATOM 2195 N GLN A 289 16.900 -42.875 124.158 1.00 97.99 N ANISOU 2195 N GLN A 289 16586 10030 10617 1025 444 -3710 N ATOM 2196 CA GLN A 289 15.942 -42.144 124.991 1.00102.19 C ANISOU 2196 CA GLN A 289 17338 10397 11092 1248 829 -3950 C ATOM 2197 C GLN A 289 15.312 -41.002 124.202 1.00103.09 C ANISOU 2197 C GLN A 289 17280 10162 11727 1395 1008 -3913 C ATOM 2198 O GLN A 289 14.198 -40.570 124.498 1.00105.87 O ANISOU 2198 O GLN A 289 17638 10398 12188 1650 1406 -3945 O ATOM 2199 CB GLN A 289 16.608 -41.604 126.264 1.00106.41 C ANISOU 2199 CB GLN A 289 18351 10849 11230 1168 759 -4392 C ATOM 2200 CG GLN A 289 16.936 -42.671 127.319 1.00107.07 C ANISOU 2200 CG GLN A 289 18643 11303 10734 1089 683 -4422 C ATOM 2201 CD GLN A 289 17.477 -42.090 128.625 1.00112.11 C ANISOU 2201 CD GLN A 289 19779 11896 10922 998 625 -4867 C ATOM 2202 OE1 GLN A 289 18.045 -40.996 128.653 1.00114.61 O ANISOU 2202 OE1 GLN A 289 20286 11909 11352 885 483 -5162 O ATOM 2203 NE2 GLN A 289 17.304 -42.831 129.715 1.00113.83 N ANISOU 2203 NE2 GLN A 289 20220 12418 10612 1024 726 -4911 N ATOM 2204 N LYS A 290 16.032 -40.526 123.192 1.00101.08 N ANISOU 2204 N LYS A 290 16852 9747 11805 1245 724 -3812 N ATOM 2205 CA LYS A 290 15.571 -39.433 122.348 1.00102.05 C ANISOU 2205 CA LYS A 290 16791 9536 12448 1359 840 -3719 C ATOM 2206 C LYS A 290 14.612 -39.946 121.267 1.00 99.27 C ANISOU 2206 C LYS A 290 15984 9353 12382 1465 960 -3266 C ATOM 2207 O LYS A 290 14.023 -39.158 120.522 1.00100.35 O ANISOU 2207 O LYS A 290 15899 9277 12954 1593 1084 -3094 O ATOM 2208 CB LYS A 290 16.774 -38.733 121.710 1.00101.41 C ANISOU 2208 CB LYS A 290 16705 9238 12588 1129 477 -3763 C ATOM 2209 CG LYS A 290 16.643 -37.231 121.567 1.00104.92 C ANISOU 2209 CG LYS A 290 17239 9191 13433 1216 594 -3919 C ATOM 2210 CD LYS A 290 17.801 -36.684 120.743 1.00103.74 C ANISOU 2210 CD LYS A 290 16996 8878 13544 961 221 -3853 C ATOM 2211 CE LYS A 290 18.014 -35.202 120.990 1.00108.29 C ANISOU 2211 CE LYS A 290 17817 8924 14406 963 273 -4140 C ATOM 2212 NZ LYS A 290 18.624 -34.949 122.327 1.00111.88 N ANISOU 2212 NZ LYS A 290 18764 9276 14468 832 208 -4646 N ATOM 2213 N MET A 291 14.459 -41.265 121.184 1.00 96.05 N ANISOU 2213 N MET A 291 15440 9324 11732 1397 912 -3061 N ATOM 2214 CA MET A 291 13.529 -41.876 120.239 1.00 93.75 C ANISOU 2214 CA MET A 291 14746 9229 11644 1443 1003 -2655 C ATOM 2215 C MET A 291 12.773 -43.046 120.866 1.00 93.51 C ANISOU 2215 C MET A 291 14706 9511 11312 1502 1200 -2567 C ATOM 2216 O MET A 291 13.079 -44.213 120.609 1.00 90.75 O ANISOU 2216 O MET A 291 14284 9425 10773 1336 1034 -2419 O ATOM 2217 CB MET A 291 14.239 -42.302 118.943 1.00 89.82 C ANISOU 2217 CB MET A 291 14002 8846 11279 1210 664 -2402 C ATOM 2218 CG MET A 291 15.604 -42.972 119.115 1.00 87.51 C ANISOU 2218 CG MET A 291 13879 8674 10696 983 348 -2523 C ATOM 2219 SD MET A 291 16.227 -43.779 117.621 1.00 82.65 S ANISOU 2219 SD MET A 291 12968 8254 10181 754 64 -2201 S ATOM 2220 CE MET A 291 15.590 -45.446 117.829 1.00 80.72 C ANISOU 2220 CE MET A 291 12673 8353 9644 733 175 -2046 C ATOM 2221 N VAL A 292 11.786 -42.720 121.692 1.00 96.86 N ANISOU 2221 N VAL A 292 15209 9885 11710 1746 1579 -2655 N ATOM 2222 CA VAL A 292 10.952 -43.719 122.359 1.00 97.32 C ANISOU 2222 CA VAL A 292 15245 10225 11509 1823 1823 -2551 C ATOM 2223 C VAL A 292 9.516 -43.555 121.863 1.00 98.76 C ANISOU 2223 C VAL A 292 15045 10440 12039 2014 2126 -2233 C ATOM 2224 O VAL A 292 9.133 -42.460 121.465 1.00100.88 O ANISOU 2224 O VAL A 292 15191 10457 12682 2175 2245 -2204 O ATOM 2225 CB VAL A 292 11.066 -43.580 123.906 1.00100.76 C ANISOU 2225 CB VAL A 292 16116 10638 11530 1938 2031 -2920 C ATOM 2226 CG1 VAL A 292 9.918 -44.277 124.643 1.00102.69 C ANISOU 2226 CG1 VAL A 292 16312 11117 11590 2104 2415 -2794 C ATOM 2227 CG2 VAL A 292 12.408 -44.117 124.383 1.00 99.05 C ANISOU 2227 CG2 VAL A 292 16195 10524 10916 1705 1684 -3116 C ATOM 2228 N TRP A 293 8.737 -44.639 121.858 1.00 98.10 N ANISOU 2228 N TRP A 293 14753 10659 11860 1984 2236 -1967 N ATOM 2229 CA TRP A 293 7.334 -44.586 121.414 1.00 99.87 C ANISOU 2229 CA TRP A 293 14565 10973 12408 2133 2502 -1616 C ATOM 2230 C TRP A 293 6.434 -45.710 121.951 1.00100.67 C ANISOU 2230 C TRP A 293 14549 11387 12315 2136 2727 -1420 C ATOM 2231 O TRP A 293 6.893 -46.607 122.661 1.00 99.68 O ANISOU 2231 O TRP A 293 14673 11409 11790 2023 2680 -1541 O ATOM 2232 CB TRP A 293 7.254 -44.516 119.883 1.00 97.51 C ANISOU 2232 CB TRP A 293 13874 10703 12471 1975 2232 -1282 C ATOM 2233 CG TRP A 293 7.848 -45.690 119.159 1.00 93.27 C ANISOU 2233 CG TRP A 293 13285 10392 11762 1636 1880 -1156 C ATOM 2234 CD1 TRP A 293 9.111 -46.194 119.297 1.00 90.42 C ANISOU 2234 CD1 TRP A 293 13216 10028 11111 1449 1612 -1375 C ATOM 2235 CD2 TRP A 293 7.207 -46.484 118.160 1.00 91.72 C ANISOU 2235 CD2 TRP A 293 12723 10441 11685 1444 1767 -784 C ATOM 2236 NE1 TRP A 293 9.288 -47.260 118.457 1.00 87.25 N ANISOU 2236 NE1 TRP A 293 12670 9827 10655 1186 1383 -1175 N ATOM 2237 CE2 TRP A 293 8.134 -47.461 117.746 1.00 88.24 C ANISOU 2237 CE2 TRP A 293 12415 10104 11008 1157 1464 -833 C ATOM 2238 CE3 TRP A 293 5.932 -46.471 117.579 1.00 93.72 C ANISOU 2238 CE3 TRP A 293 12544 10844 12222 1476 1889 -405 C ATOM 2239 CZ2 TRP A 293 7.829 -48.420 116.777 1.00 86.98 C ANISOU 2239 CZ2 TRP A 293 12024 10160 10863 892 1297 -567 C ATOM 2240 CZ3 TRP A 293 5.629 -47.424 116.612 1.00 92.07 C ANISOU 2240 CZ3 TRP A 293 12080 10887 12014 1178 1675 -120 C ATOM 2241 CH2 TRP A 293 6.575 -48.384 116.221 1.00 88.69 C ANISOU 2241 CH2 TRP A 293 11847 10527 11325 885 1390 -227 C ATOM 2242 N ASN A 294 5.152 -45.644 121.595 1.00102.88 N ANISOU 2242 N ASN A 294 14421 11767 12900 2261 2965 -1079 N ATOM 2243 CA ASN A 294 4.135 -46.572 122.097 1.00104.70 C ANISOU 2243 CA ASN A 294 14477 12281 13023 2281 3228 -847 C ATOM 2244 C ASN A 294 4.191 -47.989 121.511 1.00101.67 C ANISOU 2244 C ASN A 294 13944 12171 12515 1928 2953 -606 C ATOM 2245 O ASN A 294 3.709 -48.939 122.135 1.00102.66 O ANISOU 2245 O ASN A 294 14067 12505 12436 1882 3116 -499 O ATOM 2246 CB ASN A 294 2.730 -45.973 121.937 1.00108.47 C ANISOU 2246 CB ASN A 294 14527 12780 13907 2541 3586 -534 C ATOM 2247 CG ASN A 294 2.386 -45.642 120.491 1.00107.39 C ANISOU 2247 CG ASN A 294 13935 12656 14212 2434 3344 -176 C ATOM 2248 OD1 ASN A 294 3.192 -45.835 119.576 1.00103.76 O ANISOU 2248 OD1 ASN A 294 13498 12186 13739 2163 2924 -182 O ATOM 2249 ND2 ASN A 294 1.174 -45.138 120.281 1.00110.76 N ANISOU 2249 ND2 ASN A 294 13932 13126 15027 2653 3618 161 N ATOM 2250 N HIS A 295 4.760 -48.114 120.313 1.00 98.60 N ANISOU 2250 N HIS A 295 13443 11767 12253 1680 2560 -520 N ATOM 2251 CA HIS A 295 5.034 -49.414 119.663 1.00 95.80 C ANISOU 2251 CA HIS A 295 13032 11602 11764 1323 2274 -373 C ATOM 2252 C HIS A 295 3.886 -50.090 118.902 1.00 96.54 C ANISOU 2252 C HIS A 295 12682 11939 12061 1142 2271 48 C ATOM 2253 O HIS A 295 4.083 -51.160 118.326 1.00 94.55 O ANISOU 2253 O HIS A 295 12412 11811 11703 824 2043 143 O ATOM 2254 CB HIS A 295 5.725 -50.399 120.618 1.00 94.76 C ANISOU 2254 CB HIS A 295 13274 11522 11209 1246 2272 -572 C ATOM 2255 CG HIS A 295 7.173 -50.096 120.840 1.00 93.27 C ANISOU 2255 CG HIS A 295 13467 11158 10814 1234 2048 -915 C ATOM 2256 ND1 HIS A 295 7.607 -48.930 121.435 1.00 95.24 N ANISOU 2256 ND1 HIS A 295 13938 11204 11045 1455 2130 -1201 N ATOM 2257 CD2 HIS A 295 8.288 -50.806 120.545 1.00 90.59 C ANISOU 2257 CD2 HIS A 295 13312 10813 10296 1022 1749 -1005 C ATOM 2258 CE1 HIS A 295 8.927 -48.934 121.496 1.00 93.50 C ANISOU 2258 CE1 HIS A 295 14002 10884 10638 1351 1859 -1438 C ATOM 2259 NE2 HIS A 295 9.364 -50.062 120.964 1.00 90.77 N ANISOU 2259 NE2 HIS A 295 13623 10664 10201 1108 1636 -1310 N ATOM 2260 N ARG A 296 2.703 -49.483 118.892 1.00 99.90 N ANISOU 2260 N ARG A 296 12749 12425 12784 1332 2522 301 N ATOM 2261 CA ARG A 296 1.666 -49.900 117.950 1.00100.99 C ANISOU 2261 CA ARG A 296 12398 12800 13174 1129 2435 737 C ATOM 2262 C ARG A 296 1.896 -49.139 116.643 1.00100.31 C ANISOU 2262 C ARG A 296 12111 12654 13347 1048 2138 854 C ATOM 2263 O ARG A 296 1.946 -47.909 116.660 1.00101.79 O ANISOU 2263 O ARG A 296 12270 12649 13758 1329 2242 806 O ATOM 2264 CB ARG A 296 0.255 -49.649 118.502 1.00105.39 C ANISOU 2264 CB ARG A 296 12590 13492 13960 1365 2835 1032 C ATOM 2265 CG ARG A 296 0.083 -48.384 119.349 1.00107.98 C ANISOU 2265 CG ARG A 296 13004 13605 14420 1840 3223 873 C ATOM 2266 CD ARG A 296 -1.387 -48.028 119.529 1.00111.81 C ANISOU 2266 CD ARG A 296 13001 14231 15250 2078 3597 1262 C ATOM 2267 NE ARG A 296 -1.860 -47.130 118.475 1.00112.78 N ANISOU 2267 NE ARG A 296 12697 14328 15827 2148 3486 1572 N ATOM 2268 CZ ARG A 296 -3.106 -47.092 118.004 1.00115.93 C ANISOU 2268 CZ ARG A 296 12507 14956 16586 2166 3576 2078 C ATOM 2269 NH1 ARG A 296 -4.033 -47.917 118.473 1.00118.10 N ANISOU 2269 NH1 ARG A 296 12533 15502 16836 2102 3785 2331 N ATOM 2270 NH2 ARG A 296 -3.422 -46.233 117.045 1.00117.12 N ANISOU 2270 NH2 ARG A 296 12291 15078 17132 2236 3443 2369 N ATOM 2271 N HIS A 297 2.059 -49.832 115.511 1.00 98.61 N ANISOU 2271 N HIS A 297 11780 12588 13098 667 1782 1000 N ATOM 2272 CA HIS A 297 1.966 -51.289 115.371 1.00 97.84 C ANISOU 2272 CA HIS A 297 11722 12676 12778 306 1657 1058 C ATOM 2273 C HIS A 297 3.278 -51.790 114.767 1.00 94.21 C ANISOU 2273 C HIS A 297 11606 12115 12076 60 1334 799 C ATOM 2274 O HIS A 297 3.721 -51.274 113.745 1.00 93.11 O ANISOU 2274 O HIS A 297 11410 11944 12022 -31 1089 817 O ATOM 2275 CB HIS A 297 0.806 -51.652 114.435 1.00 99.98 C ANISOU 2275 CB HIS A 297 11500 13231 13257 37 1532 1500 C ATOM 2276 CG HIS A 297 -0.262 -50.599 114.340 1.00103.69 C ANISOU 2276 CG HIS A 297 11506 13778 14113 295 1705 1837 C ATOM 2277 ND1 HIS A 297 -1.533 -50.778 114.841 1.00107.40 N ANISOU 2277 ND1 HIS A 297 11609 14438 14762 380 1975 2154 N ATOM 2278 CD2 HIS A 297 -0.248 -49.360 113.791 1.00104.37 C ANISOU 2278 CD2 HIS A 297 11415 13769 14471 498 1661 1939 C ATOM 2279 CE1 HIS A 297 -2.255 -49.695 114.608 1.00110.31 C ANISOU 2279 CE1 HIS A 297 11584 14825 15504 645 2099 2437 C ATOM 2280 NE2 HIS A 297 -1.497 -48.819 113.975 1.00108.50 N ANISOU 2280 NE2 HIS A 297 11473 14412 15341 723 1910 2313 N ATOM 2281 N HIS A 298 3.887 -52.806 115.367 1.00 93.05 N ANISOU 2281 N HIS A 298 11793 11923 11638 -42 1348 591 N ATOM 2282 CA HIS A 298 5.311 -53.069 115.118 1.00 90.30 C ANISOU 2282 CA HIS A 298 11815 11417 11077 -135 1133 297 C ATOM 2283 C HIS A 298 5.719 -54.381 114.404 1.00 89.06 C ANISOU 2283 C HIS A 298 11781 11308 10750 -513 921 285 C ATOM 2284 O HIS A 298 6.837 -54.871 114.607 1.00 87.17 O ANISOU 2284 O HIS A 298 11878 10933 10311 -533 852 49 O ATOM 2285 CB HIS A 298 6.084 -52.921 116.438 1.00 89.76 C ANISOU 2285 CB HIS A 298 12111 11187 10806 128 1300 0 C ATOM 2286 CG HIS A 298 5.760 -53.973 117.454 1.00 90.51 C ANISOU 2286 CG HIS A 298 12333 11356 10702 112 1496 17 C ATOM 2287 ND1 HIS A 298 4.520 -54.081 118.047 1.00 93.34 N ANISOU 2287 ND1 HIS A 298 12466 11857 11142 195 1772 232 N ATOM 2288 CD2 HIS A 298 6.519 -54.959 117.987 1.00 89.06 C ANISOU 2288 CD2 HIS A 298 12459 11124 10256 33 1469 -120 C ATOM 2289 CE1 HIS A 298 4.528 -55.091 118.898 1.00 93.94 C ANISOU 2289 CE1 HIS A 298 12722 11972 10998 151 1902 222 C ATOM 2290 NE2 HIS A 298 5.729 -55.640 118.881 1.00 91.59 N ANISOU 2290 NE2 HIS A 298 12753 11554 10492 56 1717 15 N ATOM 2291 N HIS A 299 4.849 -54.921 113.548 1.00 90.75 N ANISOU 2291 N HIS A 299 11727 11703 11049 -815 817 537 N ATOM 2292 CA HIS A 299 5.082 -56.222 112.877 1.00 90.28 C ANISOU 2292 CA HIS A 299 11805 11666 10832 -1204 651 512 C ATOM 2293 C HIS A 299 4.859 -57.398 113.838 1.00 90.92 C ANISOU 2293 C HIS A 299 12044 11715 10787 -1257 835 501 C ATOM 2294 O HIS A 299 5.341 -58.513 113.613 1.00 89.97 O ANISOU 2294 O HIS A 299 12160 11505 10520 -1491 764 400 O ATOM 2295 CB HIS A 299 6.486 -56.316 112.241 1.00 87.60 C ANISOU 2295 CB HIS A 299 11775 11169 10340 -1266 463 251 C ATOM 2296 CG HIS A 299 6.812 -55.199 111.296 1.00 87.63 C ANISOU 2296 CG HIS A 299 11649 11196 10452 -1226 286 272 C ATOM 2297 ND1 HIS A 299 6.323 -55.143 110.008 1.00 89.31 N ANISOU 2297 ND1 HIS A 299 11635 11585 10715 -1509 80 459 N ATOM 2298 CD2 HIS A 299 7.596 -54.104 111.448 1.00 86.86 C ANISOU 2298 CD2 HIS A 299 11620 10968 10413 -957 276 142 C ATOM 2299 CE1 HIS A 299 6.780 -54.055 109.411 1.00 88.78 C ANISOU 2299 CE1 HIS A 299 11494 11500 10739 -1393 -35 470 C ATOM 2300 NE2 HIS A 299 7.556 -53.408 110.263 1.00 87.40 N ANISOU 2300 NE2 HIS A 299 11495 11122 10590 -1062 85 275 N TER 2301 HIS A 299 ATOM 2302 N GLN B 2 2.000 -61.847 87.295 1.00 84.35 N ANISOU 2302 N GLN B 2 10591 11667 9792 -2786 342 -654 N ATOM 2303 CA GLN B 2 1.650 -60.572 87.989 1.00 81.69 C ANISOU 2303 CA GLN B 2 9968 11584 9485 -2597 454 -313 C ATOM 2304 C GLN B 2 2.236 -60.522 89.408 1.00 80.04 C ANISOU 2304 C GLN B 2 10308 10748 9354 -2477 518 -69 C ATOM 2305 O GLN B 2 1.694 -61.130 90.333 1.00 82.54 O ANISOU 2305 O GLN B 2 10991 10728 9643 -2866 692 -65 O ATOM 2306 CB GLN B 2 0.131 -60.402 88.022 1.00 84.51 C ANISOU 2306 CB GLN B 2 9870 12470 9771 -3001 639 -403 C ATOM 2307 CG GLN B 2 -0.323 -58.967 88.217 1.00 82.55 C ANISOU 2307 CG GLN B 2 9143 12706 9518 -2665 667 -154 C ATOM 2308 CD GLN B 2 -1.829 -58.828 88.288 1.00 85.89 C ANISOU 2308 CD GLN B 2 9049 13737 9848 -2993 826 -327 C ATOM 2309 OE1 GLN B 2 -2.488 -59.483 89.094 1.00 88.72 O ANISOU 2309 OE1 GLN B 2 9558 13963 10188 -3512 1059 -454 O ATOM 2310 NE2 GLN B 2 -2.382 -57.958 87.450 1.00 86.46 N ANISOU 2310 NE2 GLN B 2 8514 14511 9826 -2686 700 -347 N ATOM 2311 N LYS B 3 3.329 -59.778 89.573 1.00 76.43 N ANISOU 2311 N LYS B 3 9901 10178 8961 -1974 389 121 N ATOM 2312 CA LYS B 3 4.149 -59.845 90.792 1.00 75.31 C ANISOU 2312 CA LYS B 3 10296 9452 8867 -1770 370 277 C ATOM 2313 C LYS B 3 3.754 -58.874 91.919 1.00 73.67 C ANISOU 2313 C LYS B 3 10034 9272 8685 -1719 529 559 C ATOM 2314 O LYS B 3 3.320 -57.751 91.662 1.00 72.08 O ANISOU 2314 O LYS B 3 9348 9530 8511 -1590 576 684 O ATOM 2315 CB LYS B 3 5.638 -59.726 90.436 1.00 73.38 C ANISOU 2315 CB LYS B 3 10136 9085 8659 -1288 138 219 C ATOM 2316 CG LYS B 3 6.190 -60.930 89.642 1.00 76.12 C ANISOU 2316 CG LYS B 3 10710 9248 8963 -1272 -39 -123 C ATOM 2317 CD LYS B 3 7.719 -60.867 89.452 1.00 75.71 C ANISOU 2317 CD LYS B 3 10717 9128 8923 -761 -265 -255 C ATOM 2318 CE LYS B 3 8.129 -60.236 88.107 1.00 74.45 C ANISOU 2318 CE LYS B 3 9968 9598 8720 -630 -312 -360 C ATOM 2319 NZ LYS B 3 9.609 -60.021 88.000 1.00 72.74 N ANISOU 2319 NZ LYS B 3 9703 9441 8493 -204 -470 -513 N ATOM 2320 N THR B 4 3.931 -59.325 93.163 1.00 74.70 N ANISOU 2320 N THR B 4 10718 8886 8780 -1782 590 649 N ATOM 2321 CA THR B 4 3.416 -58.647 94.368 1.00 74.41 C ANISOU 2321 CA THR B 4 10706 8850 8717 -1828 778 862 C ATOM 2322 C THR B 4 4.380 -57.614 94.969 1.00 71.05 C ANISOU 2322 C THR B 4 10288 8340 8366 -1329 671 1034 C ATOM 2323 O THR B 4 5.520 -57.955 95.294 1.00 70.60 O ANISOU 2323 O THR B 4 10619 7900 8307 -1046 490 1009 O ATOM 2324 CB THR B 4 3.046 -59.686 95.466 1.00 78.07 C ANISOU 2324 CB THR B 4 11824 8811 9029 -2223 934 888 C ATOM 2325 OG1 THR B 4 1.861 -60.396 95.084 1.00 82.12 O ANISOU 2325 OG1 THR B 4 12229 9510 9462 -2839 1138 727 O ATOM 2326 CG2 THR B 4 2.809 -59.020 96.811 1.00 77.63 C ANISOU 2326 CG2 THR B 4 11877 8717 8902 -2186 1099 1099 C ATOM 2327 N PRO B 5 3.913 -56.359 95.143 1.00 69.38 N ANISOU 2327 N PRO B 5 9659 8491 8210 -1206 768 1167 N ATOM 2328 CA PRO B 5 4.724 -55.270 95.693 1.00 66.69 C ANISOU 2328 CA PRO B 5 9309 8081 7950 -805 694 1302 C ATOM 2329 C PRO B 5 5.208 -55.528 97.113 1.00 67.18 C ANISOU 2329 C PRO B 5 9879 7709 7936 -728 703 1364 C ATOM 2330 O PRO B 5 4.446 -56.003 97.946 1.00 69.61 O ANISOU 2330 O PRO B 5 10430 7904 8114 -1011 880 1405 O ATOM 2331 CB PRO B 5 3.764 -54.071 95.688 1.00 66.35 C ANISOU 2331 CB PRO B 5 8813 8451 7945 -761 825 1402 C ATOM 2332 CG PRO B 5 2.418 -54.652 95.640 1.00 69.43 C ANISOU 2332 CG PRO B 5 9035 9109 8236 -1155 1006 1307 C ATOM 2333 CD PRO B 5 2.556 -55.897 94.814 1.00 70.81 C ANISOU 2333 CD PRO B 5 9347 9186 8370 -1421 937 1150 C ATOM 2334 N GLN B 6 6.476 -55.213 97.365 1.00 65.68 N ANISOU 2334 N GLN B 6 9831 7330 7793 -366 516 1347 N ATOM 2335 CA GLN B 6 7.067 -55.280 98.699 1.00 66.34 C ANISOU 2335 CA GLN B 6 10349 7076 7783 -183 467 1384 C ATOM 2336 C GLN B 6 7.407 -53.851 99.151 1.00 64.19 C ANISOU 2336 C GLN B 6 9813 6964 7614 63 478 1440 C ATOM 2337 O GLN B 6 8.037 -53.098 98.408 1.00 62.67 O ANISOU 2337 O GLN B 6 9305 6951 7557 219 390 1394 O ATOM 2338 CB GLN B 6 8.316 -56.178 98.696 1.00 67.30 C ANISOU 2338 CB GLN B 6 10858 6872 7842 85 193 1228 C ATOM 2339 CG GLN B 6 8.175 -57.496 97.897 1.00 70.10 C ANISOU 2339 CG GLN B 6 11437 7052 8144 -86 122 1107 C ATOM 2340 CD GLN B 6 7.289 -58.560 98.573 1.00 74.72 C ANISOU 2340 CD GLN B 6 12590 7259 8542 -458 267 1204 C ATOM 2341 OE1 GLN B 6 6.594 -58.287 99.558 1.00 75.92 O ANISOU 2341 OE1 GLN B 6 12876 7386 8586 -657 475 1374 O ATOM 2342 NE2 GLN B 6 7.319 -59.782 98.037 1.00 77.18 N ANISOU 2342 NE2 GLN B 6 13260 7272 8792 -584 174 1075 N ATOM 2343 N ILE B 7 6.976 -53.477 100.357 1.00 64.80 N ANISOU 2343 N ILE B 7 10045 6971 7604 57 605 1528 N ATOM 2344 CA ILE B 7 7.089 -52.089 100.830 1.00 63.22 C ANISOU 2344 CA ILE B 7 9615 6902 7503 255 643 1554 C ATOM 2345 C ILE B 7 8.049 -51.976 102.006 1.00 63.24 C ANISOU 2345 C ILE B 7 9938 6675 7415 507 519 1488 C ATOM 2346 O ILE B 7 7.891 -52.672 103.003 1.00 65.33 O ANISOU 2346 O ILE B 7 10619 6741 7464 472 545 1526 O ATOM 2347 CB ILE B 7 5.707 -51.507 101.252 1.00 64.28 C ANISOU 2347 CB ILE B 7 9547 7265 7610 107 892 1636 C ATOM 2348 CG1 ILE B 7 4.646 -51.801 100.191 1.00 65.36 C ANISOU 2348 CG1 ILE B 7 9356 7702 7774 -141 996 1645 C ATOM 2349 CG2 ILE B 7 5.792 -49.995 101.497 1.00 63.17 C ANISOU 2349 CG2 ILE B 7 9172 7223 7607 364 897 1636 C ATOM 2350 CD1 ILE B 7 3.252 -51.952 100.752 1.00 68.58 C ANISOU 2350 CD1 ILE B 7 9653 8360 8046 -409 1254 1634 C ATOM 2351 N GLN B 8 9.043 -51.100 101.877 1.00 61.52 N ANISOU 2351 N GLN B 8 9539 6505 7331 730 387 1379 N ATOM 2352 CA GLN B 8 9.928 -50.753 102.987 1.00 61.79 C ANISOU 2352 CA GLN B 8 9759 6428 7292 974 266 1253 C ATOM 2353 C GLN B 8 9.686 -49.304 103.389 1.00 60.88 C ANISOU 2353 C GLN B 8 9427 6405 7301 1008 383 1254 C ATOM 2354 O GLN B 8 9.624 -48.426 102.525 1.00 60.13 O ANISOU 2354 O GLN B 8 9032 6416 7398 952 432 1282 O ATOM 2355 CB GLN B 8 11.386 -50.938 102.581 1.00 61.80 C ANISOU 2355 CB GLN B 8 9699 6454 7328 1178 11 1020 C ATOM 2356 CG GLN B 8 11.822 -52.390 102.433 1.00 64.30 C ANISOU 2356 CG GLN B 8 10327 6617 7486 1301 -184 943 C ATOM 2357 CD GLN B 8 12.699 -52.604 101.210 1.00 65.37 C ANISOU 2357 CD GLN B 8 10172 6937 7730 1360 -329 740 C ATOM 2358 OE1 GLN B 8 12.388 -52.108 100.120 1.00 64.64 O ANISOU 2358 OE1 GLN B 8 9725 7042 7795 1140 -198 805 O ATOM 2359 NE2 GLN B 8 13.795 -53.351 101.379 1.00 67.00 N ANISOU 2359 NE2 GLN B 8 10529 7113 7816 1692 -614 476 N ATOM 2360 N VAL B 9 9.533 -49.051 104.689 1.00 61.49 N ANISOU 2360 N VAL B 9 9706 6415 7241 1108 424 1225 N ATOM 2361 CA VAL B 9 9.312 -47.683 105.183 1.00 60.90 C ANISOU 2361 CA VAL B 9 9476 6387 7275 1180 519 1172 C ATOM 2362 C VAL B 9 10.409 -47.290 106.167 1.00 61.55 C ANISOU 2362 C VAL B 9 9687 6407 7292 1381 362 942 C ATOM 2363 O VAL B 9 10.710 -48.042 107.095 1.00 62.98 O ANISOU 2363 O VAL B 9 10174 6535 7219 1508 262 894 O ATOM 2364 CB VAL B 9 7.919 -47.506 105.836 1.00 62.10 C ANISOU 2364 CB VAL B 9 9639 6633 7322 1115 753 1274 C ATOM 2365 CG1 VAL B 9 7.758 -46.095 106.364 1.00 62.50 C ANISOU 2365 CG1 VAL B 9 9565 6699 7484 1274 811 1162 C ATOM 2366 CG2 VAL B 9 6.808 -47.820 104.842 1.00 61.47 C ANISOU 2366 CG2 VAL B 9 9334 6719 7301 919 895 1425 C ATOM 2367 N TYR B 10 10.995 -46.110 105.955 1.00 60.96 N ANISOU 2367 N TYR B 10 9410 6334 7419 1396 336 795 N ATOM 2368 CA TYR B 10 12.165 -45.656 106.716 1.00 61.77 C ANISOU 2368 CA TYR B 10 9535 6445 7489 1525 177 493 C ATOM 2369 C TYR B 10 12.366 -44.141 106.660 1.00 62.36 C ANISOU 2369 C TYR B 10 9461 6447 7786 1439 251 361 C ATOM 2370 O TYR B 10 11.669 -43.439 105.924 1.00 61.75 O ANISOU 2370 O TYR B 10 9304 6274 7885 1330 395 534 O ATOM 2371 CB TYR B 10 13.422 -46.351 106.206 1.00 61.59 C ANISOU 2371 CB TYR B 10 9426 6536 7439 1569 -44 310 C ATOM 2372 CG TYR B 10 13.686 -46.124 104.738 1.00 60.22 C ANISOU 2372 CG TYR B 10 8972 6434 7475 1346 5 354 C ATOM 2373 CD1 TYR B 10 12.875 -46.706 103.768 1.00 58.80 C ANISOU 2373 CD1 TYR B 10 8773 6240 7328 1237 99 625 C ATOM 2374 CD2 TYR B 10 14.753 -45.338 104.316 1.00 61.06 C ANISOU 2374 CD2 TYR B 10 8831 6659 7710 1202 -28 102 C ATOM 2375 CE1 TYR B 10 13.114 -46.510 102.419 1.00 57.91 C ANISOU 2375 CE1 TYR B 10 8423 6229 7350 1047 138 669 C ATOM 2376 CE2 TYR B 10 15.000 -45.136 102.965 1.00 60.39 C ANISOU 2376 CE2 TYR B 10 8526 6666 7752 951 49 161 C ATOM 2377 CZ TYR B 10 14.176 -45.728 102.025 1.00 58.63 C ANISOU 2377 CZ TYR B 10 8312 6427 7539 905 121 457 C ATOM 2378 OH TYR B 10 14.407 -45.546 100.685 1.00 58.76 O ANISOU 2378 OH TYR B 10 8131 6569 7628 673 191 520 O ATOM 2379 N SER B 11 13.341 -43.656 107.429 1.00 63.95 N ANISOU 2379 N SER B 11 9657 6684 7957 1499 132 35 N ATOM 2380 CA SER B 11 13.587 -42.225 107.584 1.00 65.59 C ANISOU 2380 CA SER B 11 9813 6758 8349 1380 201 -148 C ATOM 2381 C SER B 11 14.965 -41.806 107.098 1.00 66.75 C ANISOU 2381 C SER B 11 9754 7004 8605 1150 116 -446 C ATOM 2382 O SER B 11 15.897 -42.607 107.082 1.00 66.89 O ANISOU 2382 O SER B 11 9628 7289 8498 1210 -60 -648 O ATOM 2383 CB SER B 11 13.445 -41.834 109.050 1.00 67.64 C ANISOU 2383 CB SER B 11 10226 7007 8467 1579 177 -357 C ATOM 2384 OG SER B 11 14.502 -42.395 109.806 1.00 69.29 O ANISOU 2384 OG SER B 11 10425 7435 8466 1716 -45 -657 O ATOM 2385 N ARG B 12 15.088 -40.531 106.741 1.00 68.38 N ANISOU 2385 N ARG B 12 9965 6997 9018 888 241 -505 N ATOM 2386 CA ARG B 12 16.319 -39.987 106.169 1.00 70.47 C ANISOU 2386 CA ARG B 12 10039 7354 9384 513 244 -781 C ATOM 2387 C ARG B 12 17.416 -39.780 107.214 1.00 73.25 C ANISOU 2387 C ARG B 12 10251 7932 9648 511 98 -1315 C ATOM 2388 O ARG B 12 18.582 -40.081 106.958 1.00 74.70 O ANISOU 2388 O ARG B 12 10126 8478 9779 359 -3 -1646 O ATOM 2389 CB ARG B 12 16.022 -38.685 105.402 1.00 72.16 C ANISOU 2389 CB ARG B 12 10434 7173 9812 178 449 -614 C ATOM 2390 CG ARG B 12 17.238 -37.890 104.893 1.00 75.43 C ANISOU 2390 CG ARG B 12 10739 7609 10312 -361 533 -903 C ATOM 2391 CD ARG B 12 18.129 -38.686 103.936 1.00 74.37 C ANISOU 2391 CD ARG B 12 10242 7921 10093 -582 514 -985 C ATOM 2392 NE ARG B 12 19.307 -37.924 103.512 1.00 77.92 N ANISOU 2392 NE ARG B 12 10530 8492 10584 -1177 640 -1322 N ATOM 2393 CZ ARG B 12 20.425 -37.777 104.223 1.00 80.42 C ANISOU 2393 CZ ARG B 12 10557 9145 10855 -1342 561 -1898 C ATOM 2394 NH1 ARG B 12 20.553 -38.333 105.421 1.00 79.73 N ANISOU 2394 NH1 ARG B 12 10350 9284 10660 -890 317 -2181 N ATOM 2395 NH2 ARG B 12 21.425 -37.063 103.732 1.00 84.95 N ANISOU 2395 NH2 ARG B 12 10961 9859 11456 -1989 730 -2208 N ATOM 2396 N HIS B 13 17.043 -39.262 108.380 1.00 74.50 N ANISOU 2396 N HIS B 13 10595 7941 9769 694 78 -1445 N ATOM 2397 CA HIS B 13 18.011 -39.016 109.450 1.00 77.79 C ANISOU 2397 CA HIS B 13 10883 8600 10074 721 -80 -1982 C ATOM 2398 C HIS B 13 17.660 -39.849 110.687 1.00 77.34 C ANISOU 2398 C HIS B 13 10953 8715 9719 1230 -264 -2002 C ATOM 2399 O HIS B 13 16.522 -40.318 110.804 1.00 75.10 O ANISOU 2399 O HIS B 13 10901 8273 9361 1459 -188 -1606 O ATOM 2400 CB HIS B 13 18.080 -37.517 109.812 1.00 81.22 C ANISOU 2400 CB HIS B 13 11457 8710 10692 424 52 -2226 C ATOM 2401 CG HIS B 13 18.308 -36.612 108.639 1.00 82.38 C ANISOU 2401 CG HIS B 13 11652 8561 11089 -114 263 -2131 C ATOM 2402 ND1 HIS B 13 19.504 -36.560 107.957 1.00 84.15 N ANISOU 2402 ND1 HIS B 13 11568 9067 11337 -580 291 -2408 N ATOM 2403 CD2 HIS B 13 17.491 -35.716 108.034 1.00 82.44 C ANISOU 2403 CD2 HIS B 13 12013 8021 11288 -254 455 -1793 C ATOM 2404 CE1 HIS B 13 19.412 -35.679 106.977 1.00 85.75 C ANISOU 2404 CE1 HIS B 13 11978 8882 11720 -1051 524 -2203 C ATOM 2405 NE2 HIS B 13 18.200 -35.154 107.001 1.00 84.76 N ANISOU 2405 NE2 HIS B 13 12290 8217 11699 -826 603 -1813 N ATOM 2406 N PRO B 14 18.641 -40.059 111.600 1.00 80.10 N ANISOU 2406 N PRO B 14 11151 9427 9856 1393 -504 -2474 N ATOM 2407 CA PRO B 14 18.343 -40.627 112.915 1.00 80.69 C ANISOU 2407 CA PRO B 14 11440 9626 9591 1855 -674 -2513 C ATOM 2408 C PRO B 14 17.145 -39.910 113.527 1.00 80.35 C ANISOU 2408 C PRO B 14 11690 9254 9586 1892 -467 -2324 C ATOM 2409 O PRO B 14 17.152 -38.681 113.610 1.00 82.02 O ANISOU 2409 O PRO B 14 11893 9257 10014 1655 -345 -2537 O ATOM 2410 CB PRO B 14 19.602 -40.323 113.721 1.00 84.83 C ANISOU 2410 CB PRO B 14 11717 10544 9969 1903 -920 -3158 C ATOM 2411 CG PRO B 14 20.692 -40.293 112.719 1.00 86.01 C ANISOU 2411 CG PRO B 14 11445 10950 10284 1585 -956 -3426 C ATOM 2412 CD PRO B 14 20.096 -39.935 111.380 1.00 83.08 C ANISOU 2412 CD PRO B 14 11120 10205 10242 1179 -649 -2999 C ATOM 2413 N PRO B 15 16.119 -40.678 113.939 1.00 78.72 N ANISOU 2413 N PRO B 15 11751 9003 9157 2170 -418 -1954 N ATOM 2414 CA PRO B 15 14.810 -40.143 114.325 1.00 78.47 C ANISOU 2414 CA PRO B 15 11919 8745 9150 2214 -182 -1746 C ATOM 2415 C PRO B 15 14.725 -39.612 115.761 1.00 81.70 C ANISOU 2415 C PRO B 15 12454 9260 9328 2414 -218 -2073 C ATOM 2416 O PRO B 15 14.482 -40.382 116.689 1.00 82.64 O ANISOU 2416 O PRO B 15 12765 9590 9043 2678 -286 -2014 O ATOM 2417 CB PRO B 15 13.869 -41.347 114.146 1.00 76.12 C ANISOU 2417 CB PRO B 15 11794 8473 8654 2341 -101 -1274 C ATOM 2418 CG PRO B 15 14.757 -42.534 113.768 1.00 75.27 C ANISOU 2418 CG PRO B 15 11669 8528 8402 2416 -334 -1240 C ATOM 2419 CD PRO B 15 16.160 -42.145 114.065 1.00 77.69 C ANISOU 2419 CD PRO B 15 11765 9048 8706 2447 -581 -1739 C ATOM 2420 N GLU B 16 14.918 -38.305 115.928 1.00 83.93 N ANISOU 2420 N GLU B 16 12677 9372 9841 2271 -165 -2412 N ATOM 2421 CA GLU B 16 14.668 -37.635 117.206 1.00 87.13 C ANISOU 2421 CA GLU B 16 13200 9834 10072 2451 -160 -2746 C ATOM 2422 C GLU B 16 13.206 -37.185 117.272 1.00 86.80 C ANISOU 2422 C GLU B 16 13302 9585 10093 2567 98 -2516 C ATOM 2423 O GLU B 16 12.641 -36.751 116.266 1.00 85.33 O ANISOU 2423 O GLU B 16 13103 9088 10232 2443 244 -2275 O ATOM 2424 CB GLU B 16 15.611 -36.441 117.381 1.00 90.54 C ANISOU 2424 CB GLU B 16 13521 10161 10720 2223 -237 -3294 C ATOM 2425 N ASN B 17 12.596 -37.296 118.450 1.00 88.70 N ANISOU 2425 N ASN B 17 13665 10052 9985 2828 145 -2615 N ATOM 2426 CA ASN B 17 11.169 -37.005 118.614 1.00 89.24 C ANISOU 2426 CA ASN B 17 13787 10086 10034 2977 396 -2462 C ATOM 2427 C ASN B 17 10.809 -35.520 118.577 1.00 92.05 C ANISOU 2427 C ASN B 17 14158 10101 10717 3029 473 -2762 C ATOM 2428 O ASN B 17 11.295 -34.733 119.391 1.00 95.61 O ANISOU 2428 O ASN B 17 14667 10520 11139 3081 388 -3232 O ATOM 2429 CB ASN B 17 10.633 -37.637 119.901 1.00 91.15 C ANISOU 2429 CB ASN B 17 14153 10744 9736 3191 461 -2488 C ATOM 2430 CG ASN B 17 10.504 -39.140 119.804 1.00 88.77 C ANISOU 2430 CG ASN B 17 13971 10654 9104 3142 469 -2052 C ATOM 2431 OD1 ASN B 17 10.604 -39.715 118.723 1.00 85.59 O ANISOU 2431 OD1 ASN B 17 13513 10101 8907 2983 453 -1728 O ATOM 2432 ND2 ASN B 17 10.273 -39.786 120.938 1.00 90.77 N ANISOU 2432 ND2 ASN B 17 14441 11232 8814 3268 498 -2044 N ATOM 2433 N GLY B 18 9.949 -35.149 117.633 1.00 91.13 N ANISOU 2433 N GLY B 18 14020 9719 10887 3047 612 -2506 N ATOM 2434 CA GLY B 18 9.474 -33.773 117.508 1.00 94.41 C ANISOU 2434 CA GLY B 18 14544 9731 11595 3194 659 -2737 C ATOM 2435 C GLY B 18 10.343 -32.884 116.635 1.00 95.24 C ANISOU 2435 C GLY B 18 14799 9281 12107 2909 565 -2807 C ATOM 2436 O GLY B 18 10.019 -31.709 116.424 1.00 98.44 O ANISOU 2436 O GLY B 18 15423 9212 12767 3010 583 -2959 O ATOM 2437 N LYS B 19 11.448 -33.436 116.137 1.00 93.01 N ANISOU 2437 N LYS B 19 14428 9054 11859 2551 468 -2717 N ATOM 2438 CA LYS B 19 12.336 -32.710 115.231 1.00 94.16 C ANISOU 2438 CA LYS B 19 14679 8760 12339 2154 432 -2767 C ATOM 2439 C LYS B 19 12.005 -33.023 113.766 1.00 91.33 C ANISOU 2439 C LYS B 19 14313 8225 12163 2026 503 -2245 C ATOM 2440 O LYS B 19 11.765 -34.185 113.425 1.00 87.54 O ANISOU 2440 O LYS B 19 13630 8099 11533 2073 510 -1917 O ATOM 2441 CB LYS B 19 13.800 -33.033 115.532 1.00 94.44 C ANISOU 2441 CB LYS B 19 14538 9058 12286 1822 289 -3084 C ATOM 2442 N PRO B 20 11.968 -31.980 112.906 1.00 93.81 N ANISOU 2442 N PRO B 20 14906 7963 12773 1869 550 -2167 N ATOM 2443 CA PRO B 20 11.713 -32.104 111.461 1.00 92.00 C ANISOU 2443 CA PRO B 20 14734 7529 12693 1737 605 -1688 C ATOM 2444 C PRO B 20 12.606 -33.129 110.752 1.00 88.48 C ANISOU 2444 C PRO B 20 14002 7426 12189 1366 587 -1512 C ATOM 2445 O PRO B 20 13.833 -33.079 110.880 1.00 89.53 O ANISOU 2445 O PRO B 20 14039 7647 12332 981 544 -1803 O ATOM 2446 CB PRO B 20 11.988 -30.689 110.944 1.00 96.83 C ANISOU 2446 CB PRO B 20 15807 7418 13567 1508 635 -1768 C ATOM 2447 CG PRO B 20 11.603 -29.808 112.093 1.00100.80 C ANISOU 2447 CG PRO B 20 16525 7695 14080 1821 602 -2190 C ATOM 2448 CD PRO B 20 12.006 -30.563 113.331 1.00 99.16 C ANISOU 2448 CD PRO B 20 15952 8100 13626 1875 550 -2530 C ATOM 2449 N ASN B 21 11.977 -34.045 110.014 1.00 84.88 N ANISOU 2449 N ASN B 21 13385 7199 11665 1495 612 -1092 N ATOM 2450 CA ASN B 21 12.675 -35.151 109.346 1.00 81.55 C ANISOU 2450 CA ASN B 21 12692 7127 11165 1244 578 -930 C ATOM 2451 C ASN B 21 12.006 -35.570 108.033 1.00 79.03 C ANISOU 2451 C ASN B 21 12345 6788 10896 1255 637 -452 C ATOM 2452 O ASN B 21 10.973 -35.016 107.664 1.00 80.26 O ANISOU 2452 O ASN B 21 12673 6695 11128 1493 685 -244 O ATOM 2453 CB ASN B 21 12.782 -36.350 110.292 1.00 79.48 C ANISOU 2453 CB ASN B 21 12204 7366 10627 1442 488 -1039 C ATOM 2454 CG ASN B 21 14.009 -37.197 110.019 1.00 78.76 C ANISOU 2454 CG ASN B 21 11882 7591 10452 1209 371 -1145 C ATOM 2455 OD1 ASN B 21 13.908 -38.393 109.724 1.00 76.67 O ANISOU 2455 OD1 ASN B 21 11490 7598 10044 1303 322 -931 O ATOM 2456 ND2 ASN B 21 15.180 -36.576 110.103 1.00 82.02 N ANISOU 2456 ND2 ASN B 21 12232 7984 10947 899 324 -1521 N ATOM 2457 N ILE B 22 12.592 -36.542 107.331 1.00 76.21 N ANISOU 2457 N ILE B 22 11759 6722 10475 1045 609 -321 N ATOM 2458 CA ILE B 22 12.028 -37.049 106.066 1.00 73.92 C ANISOU 2458 CA ILE B 22 11406 6481 10199 1034 652 93 C ATOM 2459 C ILE B 22 11.747 -38.569 106.092 1.00 70.24 C ANISOU 2459 C ILE B 22 10691 6447 9551 1166 606 222 C ATOM 2460 O ILE B 22 12.633 -39.368 106.414 1.00 69.03 O ANISOU 2460 O ILE B 22 10394 6549 9284 1085 512 46 O ATOM 2461 CB ILE B 22 12.913 -36.656 104.835 1.00 74.96 C ANISOU 2461 CB ILE B 22 11574 6475 10433 589 700 176 C ATOM 2462 CG1 ILE B 22 12.740 -35.175 104.477 1.00 78.68 C ANISOU 2462 CG1 ILE B 22 12460 6377 11059 476 778 243 C ATOM 2463 CG2 ILE B 22 12.578 -37.508 103.617 1.00 72.40 C ANISOU 2463 CG2 ILE B 22 11092 6367 10049 565 712 526 C ATOM 2464 CD1 ILE B 22 13.765 -34.254 105.106 1.00 82.56 C ANISOU 2464 CD1 ILE B 22 13105 6626 11637 131 808 -156 C ATOM 2465 N LEU B 23 10.508 -38.944 105.754 1.00 68.98 N ANISOU 2465 N LEU B 23 10500 6360 9350 1380 661 500 N ATOM 2466 CA LEU B 23 10.062 -40.348 105.751 1.00 66.40 C ANISOU 2466 CA LEU B 23 10011 6368 8849 1441 655 638 C ATOM 2467 C LEU B 23 9.901 -40.915 104.343 1.00 64.64 C ANISOU 2467 C LEU B 23 9660 6242 8658 1303 661 909 C ATOM 2468 O LEU B 23 9.204 -40.336 103.509 1.00 65.49 O ANISOU 2468 O LEU B 23 9780 6251 8851 1353 706 1108 O ATOM 2469 CB LEU B 23 8.742 -40.512 106.512 1.00 66.96 C ANISOU 2469 CB LEU B 23 10074 6573 8796 1698 747 675 C ATOM 2470 CG LEU B 23 8.172 -41.932 106.617 1.00 65.21 C ANISOU 2470 CG LEU B 23 9761 6653 8364 1665 793 811 C ATOM 2471 CD1 LEU B 23 9.016 -42.782 107.540 1.00 65.47 C ANISOU 2471 CD1 LEU B 23 9926 6753 8195 1631 705 671 C ATOM 2472 CD2 LEU B 23 6.741 -41.912 107.107 1.00 66.74 C ANISOU 2472 CD2 LEU B 23 9868 7045 8445 1821 947 836 C ATOM 2473 N ASN B 24 10.529 -42.064 104.103 1.00 62.60 N ANISOU 2473 N ASN B 24 9300 6185 8302 1182 590 896 N ATOM 2474 CA ASN B 24 10.582 -42.664 102.776 1.00 60.96 C ANISOU 2474 CA ASN B 24 8957 6098 8107 1032 581 1078 C ATOM 2475 C ASN B 24 9.791 -43.965 102.705 1.00 59.49 C ANISOU 2475 C ASN B 24 8713 6110 7782 1083 590 1208 C ATOM 2476 O ASN B 24 9.969 -44.856 103.543 1.00 59.19 O ANISOU 2476 O ASN B 24 8772 6125 7594 1137 541 1112 O ATOM 2477 CB ASN B 24 12.038 -42.908 102.356 1.00 60.81 C ANISOU 2477 CB ASN B 24 8843 6168 8095 830 489 892 C ATOM 2478 CG ASN B 24 12.903 -41.648 102.436 1.00 63.00 C ANISOU 2478 CG ASN B 24 9168 6279 8492 644 519 711 C ATOM 2479 OD1 ASN B 24 12.417 -40.555 102.727 1.00 65.07 O ANISOU 2479 OD1 ASN B 24 9609 6264 8849 684 593 759 O ATOM 2480 ND2 ASN B 24 14.193 -41.803 102.175 1.00 63.33 N ANISOU 2480 ND2 ASN B 24 9047 6498 8517 430 464 462 N ATOM 2481 N CYS B 25 8.907 -44.046 101.708 1.00 59.05 N ANISOU 2481 N CYS B 25 8537 6149 7750 1055 649 1420 N ATOM 2482 CA CYS B 25 8.135 -45.246 101.413 1.00 58.08 C ANISOU 2482 CA CYS B 25 8329 6228 7510 1002 679 1517 C ATOM 2483 C CYS B 25 8.537 -45.767 100.048 1.00 56.90 C ANISOU 2483 C CYS B 25 8051 6190 7378 852 616 1589 C ATOM 2484 O CYS B 25 8.121 -45.229 99.021 1.00 57.24 O ANISOU 2484 O CYS B 25 7974 6303 7470 840 637 1734 O ATOM 2485 CB CYS B 25 6.634 -44.958 101.432 1.00 59.34 C ANISOU 2485 CB CYS B 25 8362 6537 7647 1102 797 1617 C ATOM 2486 SG CYS B 25 5.627 -46.383 100.926 1.00 60.51 S ANISOU 2486 SG CYS B 25 8349 6989 7652 906 871 1685 S ATOM 2487 N TYR B 26 9.332 -46.831 100.054 1.00 56.02 N ANISOU 2487 N TYR B 26 7990 6103 7192 784 522 1472 N ATOM 2488 CA TYR B 26 9.965 -47.357 98.849 1.00 55.49 C ANISOU 2488 CA TYR B 26 7791 6168 7124 667 446 1447 C ATOM 2489 C TYR B 26 9.386 -48.728 98.456 1.00 55.44 C ANISOU 2489 C TYR B 26 7796 6254 7015 598 429 1473 C ATOM 2490 O TYR B 26 9.618 -49.739 99.120 1.00 55.83 O ANISOU 2490 O TYR B 26 8060 6190 6962 638 358 1374 O ATOM 2491 CB TYR B 26 11.481 -47.386 99.078 1.00 55.44 C ANISOU 2491 CB TYR B 26 7791 6157 7118 687 323 1195 C ATOM 2492 CG TYR B 26 12.319 -48.164 98.085 1.00 55.38 C ANISOU 2492 CG TYR B 26 7632 6347 7062 625 222 1049 C ATOM 2493 CD1 TYR B 26 12.492 -47.721 96.768 1.00 55.20 C ANISOU 2493 CD1 TYR B 26 7400 6511 7064 438 287 1115 C ATOM 2494 CD2 TYR B 26 12.989 -49.321 98.483 1.00 55.13 C ANISOU 2494 CD2 TYR B 26 7699 6321 6926 791 46 822 C ATOM 2495 CE1 TYR B 26 13.287 -48.435 95.868 1.00 54.59 C ANISOU 2495 CE1 TYR B 26 7144 6686 6912 386 209 927 C ATOM 2496 CE2 TYR B 26 13.775 -50.034 97.597 1.00 55.05 C ANISOU 2496 CE2 TYR B 26 7531 6519 6865 805 -68 619 C ATOM 2497 CZ TYR B 26 13.922 -49.588 96.298 1.00 54.76 C ANISOU 2497 CZ TYR B 26 7215 6730 6860 586 28 653 C ATOM 2498 OH TYR B 26 14.705 -50.317 95.441 1.00 55.61 O ANISOU 2498 OH TYR B 26 7134 7106 6890 608 -72 402 O ATOM 2499 N VAL B 27 8.610 -48.740 97.377 1.00 55.77 N ANISOU 2499 N VAL B 27 7647 6480 7062 497 483 1601 N ATOM 2500 CA VAL B 27 7.946 -49.954 96.916 1.00 56.39 C ANISOU 2500 CA VAL B 27 7706 6666 7052 364 487 1592 C ATOM 2501 C VAL B 27 8.747 -50.607 95.803 1.00 56.38 C ANISOU 2501 C VAL B 27 7620 6776 7027 309 371 1476 C ATOM 2502 O VAL B 27 9.308 -49.926 94.949 1.00 56.17 O ANISOU 2502 O VAL B 27 7418 6896 7029 305 354 1492 O ATOM 2503 CB VAL B 27 6.524 -49.688 96.382 1.00 57.44 C ANISOU 2503 CB VAL B 27 7608 7046 7171 294 595 1721 C ATOM 2504 CG1 VAL B 27 5.662 -50.931 96.582 1.00 59.08 C ANISOU 2504 CG1 VAL B 27 7864 7309 7274 73 667 1657 C ATOM 2505 CG2 VAL B 27 5.878 -48.460 97.052 1.00 57.79 C ANISOU 2505 CG2 VAL B 27 7607 7083 7267 463 680 1815 C ATOM 2506 N THR B 28 8.776 -51.935 95.808 1.00 57.41 N ANISOU 2506 N THR B 28 7909 6826 7078 252 304 1352 N ATOM 2507 CA THR B 28 9.628 -52.691 94.906 1.00 58.21 C ANISOU 2507 CA THR B 28 7964 7011 7142 271 165 1159 C ATOM 2508 C THR B 28 8.904 -53.927 94.434 1.00 59.99 C ANISOU 2508 C THR B 28 8281 7217 7294 105 160 1101 C ATOM 2509 O THR B 28 7.848 -54.259 94.964 1.00 60.96 O ANISOU 2509 O THR B 28 8536 7242 7385 -66 275 1198 O ATOM 2510 CB THR B 28 10.885 -53.185 95.627 1.00 58.61 C ANISOU 2510 CB THR B 28 8244 6867 7160 503 -9 935 C ATOM 2511 OG1 THR B 28 10.943 -52.613 96.946 1.00 58.08 O ANISOU 2511 OG1 THR B 28 8356 6607 7104 612 18 1005 O ATOM 2512 CG2 THR B 28 12.148 -52.832 94.819 1.00 58.89 C ANISOU 2512 CG2 THR B 28 7991 7179 7206 587 -100 719 C ATOM 2513 N GLN B 29 9.475 -54.590 93.425 1.00 61.32 N ANISOU 2513 N GLN B 29 8363 7512 7425 121 42 906 N ATOM 2514 CA GLN B 29 9.120 -55.971 93.046 1.00 63.84 C ANISOU 2514 CA GLN B 29 8879 7705 7673 -1 -19 749 C ATOM 2515 C GLN B 29 7.737 -56.162 92.413 1.00 64.85 C ANISOU 2515 C GLN B 29 8826 8038 7776 -330 120 827 C ATOM 2516 O GLN B 29 7.311 -57.299 92.179 1.00 67.14 O ANISOU 2516 O GLN B 29 9306 8195 8011 -526 104 683 O ATOM 2517 CB GLN B 29 9.294 -56.927 94.244 1.00 65.59 C ANISOU 2517 CB GLN B 29 9671 7417 7834 81 -98 700 C ATOM 2518 CG GLN B 29 10.704 -56.963 94.847 1.00 66.60 C ANISOU 2518 CG GLN B 29 9981 7384 7939 493 -314 532 C ATOM 2519 CD GLN B 29 11.687 -57.752 93.995 1.00 69.38 C ANISOU 2519 CD GLN B 29 10301 7810 8251 726 -539 185 C ATOM 2520 OE1 GLN B 29 12.001 -58.911 94.298 1.00 72.72 O ANISOU 2520 OE1 GLN B 29 11191 7857 8583 919 -728 12 O ATOM 2521 NE2 GLN B 29 12.164 -57.136 92.915 1.00 68.19 N ANISOU 2521 NE2 GLN B 29 9637 8135 8137 716 -518 73 N ATOM 2522 N PHE B 30 7.051 -55.061 92.126 1.00 63.97 N ANISOU 2522 N PHE B 30 8362 8251 7691 -375 238 1019 N ATOM 2523 CA PHE B 30 5.692 -55.127 91.602 1.00 65.54 C ANISOU 2523 CA PHE B 30 8307 8752 7844 -618 343 1050 C ATOM 2524 C PHE B 30 5.657 -55.095 90.079 1.00 66.43 C ANISOU 2524 C PHE B 30 8075 9285 7879 -632 267 966 C ATOM 2525 O PHE B 30 6.657 -54.762 89.434 1.00 65.66 O ANISOU 2525 O PHE B 30 7908 9279 7760 -467 178 945 O ATOM 2526 CB PHE B 30 4.828 -54.012 92.196 1.00 65.14 C ANISOU 2526 CB PHE B 30 8078 8849 7825 -569 474 1259 C ATOM 2527 CG PHE B 30 5.321 -52.626 91.897 1.00 63.16 C ANISOU 2527 CG PHE B 30 7671 8711 7617 -290 433 1437 C ATOM 2528 CD1 PHE B 30 6.334 -52.059 92.645 1.00 61.52 C ANISOU 2528 CD1 PHE B 30 7671 8214 7489 -119 413 1495 C ATOM 2529 CD2 PHE B 30 4.751 -51.881 90.880 1.00 63.97 C ANISOU 2529 CD2 PHE B 30 7458 9197 7651 -211 409 1540 C ATOM 2530 CE1 PHE B 30 6.782 -50.780 92.370 1.00 61.17 C ANISOU 2530 CE1 PHE B 30 7543 8220 7478 42 405 1647 C ATOM 2531 CE2 PHE B 30 5.193 -50.602 90.603 1.00 63.33 C ANISOU 2531 CE2 PHE B 30 7366 9121 7577 8 381 1741 C ATOM 2532 CZ PHE B 30 6.210 -50.051 91.347 1.00 61.87 C ANISOU 2532 CZ PHE B 30 7411 8603 7493 92 398 1792 C ATOM 2533 N HIS B 31 4.491 -55.439 89.527 1.00 68.69 N ANISOU 2533 N HIS B 31 8124 9881 8093 -856 315 893 N ATOM 2534 CA HIS B 31 4.257 -55.534 88.084 1.00 70.32 C ANISOU 2534 CA HIS B 31 7998 10547 8175 -889 231 780 C ATOM 2535 C HIS B 31 2.786 -55.880 87.910 1.00 73.12 C ANISOU 2535 C HIS B 31 8081 11240 8461 -1158 305 665 C ATOM 2536 O HIS B 31 2.277 -56.750 88.622 1.00 74.59 O ANISOU 2536 O HIS B 31 8453 11204 8682 -1477 414 528 O ATOM 2537 CB HIS B 31 5.112 -56.654 87.479 1.00 71.20 C ANISOU 2537 CB HIS B 31 8274 10526 8251 -947 120 501 C ATOM 2538 CG HIS B 31 5.199 -56.630 85.982 1.00 72.87 C ANISOU 2538 CG HIS B 31 8161 11225 8302 -922 27 382 C ATOM 2539 ND1 HIS B 31 6.387 -56.416 85.311 1.00 72.16 N ANISOU 2539 ND1 HIS B 31 8042 11235 8139 -737 -51 337 N ATOM 2540 CD2 HIS B 31 4.257 -56.822 85.026 1.00 75.62 C ANISOU 2540 CD2 HIS B 31 8183 12041 8507 -1071 2 264 C ATOM 2541 CE1 HIS B 31 6.169 -56.465 84.008 1.00 74.01 C ANISOU 2541 CE1 HIS B 31 7988 11955 8179 -777 -107 233 C ATOM 2542 NE2 HIS B 31 4.885 -56.706 83.808 1.00 76.16 N ANISOU 2542 NE2 HIS B 31 8079 12451 8406 -953 -96 189 N ATOM 2543 N PRO B 32 2.079 -55.190 86.990 1.00 74.60 N ANISOU 2543 N PRO B 32 7840 11985 8520 -1041 247 707 N ATOM 2544 CA PRO B 32 2.464 -54.074 86.111 1.00 74.00 C ANISOU 2544 CA PRO B 32 7609 12178 8329 -697 135 926 C ATOM 2545 C PRO B 32 2.722 -52.740 86.843 1.00 72.33 C ANISOU 2545 C PRO B 32 7535 11746 8203 -395 170 1259 C ATOM 2546 O PRO B 32 2.512 -52.657 88.055 1.00 71.23 O ANISOU 2546 O PRO B 32 7536 11322 8208 -419 277 1295 O ATOM 2547 CB PRO B 32 1.257 -53.951 85.167 1.00 77.39 C ANISOU 2547 CB PRO B 32 7589 13254 8561 -680 52 827 C ATOM 2548 CG PRO B 32 0.115 -54.500 85.928 1.00 79.20 C ANISOU 2548 CG PRO B 32 7657 13580 8857 -954 171 621 C ATOM 2549 CD PRO B 32 0.694 -55.629 86.721 1.00 78.10 C ANISOU 2549 CD PRO B 32 7924 12881 8871 -1303 290 485 C ATOM 2550 N PRO B 33 3.171 -51.701 86.101 1.00 72.63 N ANISOU 2550 N PRO B 33 7573 11901 8123 -141 92 1496 N ATOM 2551 CA PRO B 33 3.589 -50.401 86.642 1.00 71.83 C ANISOU 2551 CA PRO B 33 7690 11514 8090 105 120 1800 C ATOM 2552 C PRO B 33 2.493 -49.506 87.223 1.00 73.62 C ANISOU 2552 C PRO B 33 7831 11801 8341 371 113 1931 C ATOM 2553 O PRO B 33 2.817 -48.573 87.958 1.00 72.97 O ANISOU 2553 O PRO B 33 7984 11373 8368 544 154 2117 O ATOM 2554 CB PRO B 33 4.205 -49.704 85.427 1.00 72.97 C ANISOU 2554 CB PRO B 33 7884 11824 8016 204 49 1994 C ATOM 2555 CG PRO B 33 3.529 -50.310 84.274 1.00 75.16 C ANISOU 2555 CG PRO B 33 7862 12627 8068 169 -60 1846 C ATOM 2556 CD PRO B 33 3.386 -51.750 84.643 1.00 74.34 C ANISOU 2556 CD PRO B 33 7643 12508 8095 -124 -17 1478 C ATOM 2557 N HIS B 34 1.226 -49.752 86.898 1.00 76.55 N ANISOU 2557 N HIS B 34 7845 12637 8602 420 54 1787 N ATOM 2558 CA HIS B 34 0.156 -48.948 87.487 1.00 78.87 C ANISOU 2558 CA HIS B 34 7984 13078 8906 728 35 1822 C ATOM 2559 C HIS B 34 -0.019 -49.287 88.967 1.00 77.49 C ANISOU 2559 C HIS B 34 7865 12640 8936 548 223 1695 C ATOM 2560 O HIS B 34 -0.358 -50.421 89.316 1.00 77.59 O ANISOU 2560 O HIS B 34 7757 12744 8978 161 341 1447 O ATOM 2561 CB HIS B 34 -1.159 -49.119 86.732 1.00 83.13 C ANISOU 2561 CB HIS B 34 8032 14315 9240 851 -94 1623 C ATOM 2562 CG HIS B 34 -2.259 -48.237 87.241 1.00 86.80 C ANISOU 2562 CG HIS B 34 8270 15032 9677 1273 -155 1597 C ATOM 2563 ND1 HIS B 34 -2.409 -46.927 86.838 1.00 89.69 N ANISOU 2563 ND1 HIS B 34 8778 15384 9915 1861 -356 1853 N ATOM 2564 CD2 HIS B 34 -3.253 -48.474 88.130 1.00 88.79 C ANISOU 2564 CD2 HIS B 34 8182 15563 9990 1206 -39 1319 C ATOM 2565 CE1 HIS B 34 -3.452 -46.397 87.451 1.00 92.89 C ANISOU 2565 CE1 HIS B 34 8916 16057 10321 2217 -398 1704 C ATOM 2566 NE2 HIS B 34 -3.981 -47.314 88.242 1.00 92.50 N ANISOU 2566 NE2 HIS B 34 8524 16239 10381 1807 -190 1364 N ATOM 2567 N ILE B 35 0.219 -48.296 89.825 1.00 76.81 N ANISOU 2567 N ILE B 35 8013 12207 8964 805 256 1867 N ATOM 2568 CA ILE B 35 0.210 -48.490 91.279 1.00 75.67 C ANISOU 2568 CA ILE B 35 7989 11787 8975 668 433 1781 C ATOM 2569 C ILE B 35 -0.089 -47.183 92.042 1.00 76.94 C ANISOU 2569 C ILE B 35 8232 11806 9196 1087 422 1888 C ATOM 2570 O ILE B 35 0.299 -46.098 91.600 1.00 77.59 O ANISOU 2570 O ILE B 35 8523 11689 9267 1421 294 2113 O ATOM 2571 CB ILE B 35 1.545 -49.136 91.751 1.00 72.11 C ANISOU 2571 CB ILE B 35 7924 10831 8643 385 507 1811 C ATOM 2572 CG1 ILE B 35 1.454 -49.609 93.203 1.00 71.30 C ANISOU 2572 CG1 ILE B 35 7974 10494 8622 202 676 1707 C ATOM 2573 CG2 ILE B 35 2.727 -48.194 91.521 1.00 70.37 C ANISOU 2573 CG2 ILE B 35 8002 10259 8478 574 433 2035 C ATOM 2574 CD1 ILE B 35 2.367 -50.773 93.517 1.00 69.58 C ANISOU 2574 CD1 ILE B 35 8066 9937 8436 -105 710 1634 C ATOM 2575 N GLU B 36 -0.782 -47.294 93.176 1.00 78.06 N ANISOU 2575 N GLU B 36 8245 12039 9376 1047 569 1716 N ATOM 2576 CA GLU B 36 -1.175 -46.124 93.978 1.00 79.84 C ANISOU 2576 CA GLU B 36 8504 12184 9647 1469 563 1731 C ATOM 2577 C GLU B 36 -0.526 -46.087 95.365 1.00 77.58 C ANISOU 2577 C GLU B 36 8540 11449 9489 1339 723 1733 C ATOM 2578 O GLU B 36 -0.982 -46.760 96.292 1.00 78.16 O ANISOU 2578 O GLU B 36 8511 11661 9527 1076 912 1554 O ATOM 2579 CB GLU B 36 -2.701 -46.046 94.129 1.00 84.25 C ANISOU 2579 CB GLU B 36 8532 13395 10084 1656 582 1455 C ATOM 2580 CG GLU B 36 -3.461 -45.723 92.847 1.00 88.22 C ANISOU 2580 CG GLU B 36 8691 14403 10426 2003 347 1424 C ATOM 2581 CD GLU B 36 -4.912 -45.340 93.105 1.00 94.06 C ANISOU 2581 CD GLU B 36 8879 15818 11043 2366 314 1099 C ATOM 2582 OE1 GLU B 36 -5.214 -44.819 94.204 1.00 95.17 O ANISOU 2582 OE1 GLU B 36 9009 15912 11240 2554 419 979 O ATOM 2583 OE2 GLU B 36 -5.752 -45.554 92.201 1.00 97.99 O ANISOU 2583 OE2 GLU B 36 8914 16952 11366 2486 171 919 O ATOM 2584 N ILE B 37 0.531 -45.289 95.500 1.00 75.70 N ANISOU 2584 N ILE B 37 8701 10697 9365 1494 654 1923 N ATOM 2585 CA ILE B 37 1.198 -45.092 96.785 1.00 73.94 C ANISOU 2585 CA ILE B 37 8772 10076 9244 1442 760 1897 C ATOM 2586 C ILE B 37 0.591 -43.907 97.530 1.00 76.53 C ANISOU 2586 C ILE B 37 9097 10377 9603 1866 756 1829 C ATOM 2587 O ILE B 37 0.440 -42.813 96.971 1.00 78.64 O ANISOU 2587 O ILE B 37 9445 10544 9890 2264 602 1935 O ATOM 2588 CB ILE B 37 2.711 -44.856 96.622 1.00 71.23 C ANISOU 2588 CB ILE B 37 8809 9251 9005 1340 699 2046 C ATOM 2589 CG1 ILE B 37 3.366 -46.008 95.861 1.00 69.58 C ANISOU 2589 CG1 ILE B 37 8585 9097 8755 999 680 2056 C ATOM 2590 CG2 ILE B 37 3.374 -44.686 97.971 1.00 70.09 C ANISOU 2590 CG2 ILE B 37 8917 8775 8938 1307 778 1962 C ATOM 2591 CD1 ILE B 37 3.604 -45.711 94.397 1.00 70.70 C ANISOU 2591 CD1 ILE B 37 8681 9338 8843 1039 559 2206 C ATOM 2592 N GLN B 38 0.249 -44.139 98.795 1.00 76.86 N ANISOU 2592 N GLN B 38 9095 10489 9620 1792 920 1648 N ATOM 2593 CA GLN B 38 -0.318 -43.114 99.663 1.00 79.37 C ANISOU 2593 CA GLN B 38 9386 10820 9951 2188 939 1505 C ATOM 2594 C GLN B 38 0.361 -43.191 101.025 1.00 77.78 C ANISOU 2594 C GLN B 38 9465 10314 9772 2030 1072 1433 C ATOM 2595 O GLN B 38 0.667 -44.281 101.519 1.00 76.10 O ANISOU 2595 O GLN B 38 9321 10118 9475 1625 1203 1420 O ATOM 2596 CB GLN B 38 -1.827 -43.316 99.801 1.00 83.07 C ANISOU 2596 CB GLN B 38 9331 11963 10268 2303 1029 1247 C ATOM 2597 CG GLN B 38 -2.613 -42.048 100.085 1.00 87.49 C ANISOU 2597 CG GLN B 38 9756 12658 10829 2937 930 1077 C ATOM 2598 CD GLN B 38 -4.087 -42.176 99.707 1.00 92.77 C ANISOU 2598 CD GLN B 38 9793 14120 11335 3153 922 802 C ATOM 2599 OE1 GLN B 38 -4.974 -41.999 100.545 1.00 96.68 O ANISOU 2599 OE1 GLN B 38 9947 15060 11728 3311 1052 472 O ATOM 2600 NE2 GLN B 38 -4.351 -42.487 98.441 1.00 93.20 N ANISOU 2600 NE2 GLN B 38 9648 14426 11337 3158 770 891 N ATOM 2601 N MET B 39 0.611 -42.030 101.619 1.00 78.83 N ANISOU 2601 N MET B 39 9812 10143 9998 2371 1016 1382 N ATOM 2602 CA MET B 39 1.242 -41.958 102.936 1.00 77.80 C ANISOU 2602 CA MET B 39 9932 9763 9867 2283 1112 1272 C ATOM 2603 C MET B 39 0.292 -41.412 104.001 1.00 81.08 C ANISOU 2603 C MET B 39 10176 10442 10188 2572 1223 999 C ATOM 2604 O MET B 39 -0.443 -40.441 103.768 1.00 84.28 O ANISOU 2604 O MET B 39 10446 10941 10635 3039 1131 892 O ATOM 2605 CB MET B 39 2.523 -41.137 102.872 1.00 76.49 C ANISOU 2605 CB MET B 39 10169 9020 9874 2334 979 1364 C ATOM 2606 CG MET B 39 3.704 -41.930 102.385 1.00 73.33 C ANISOU 2606 CG MET B 39 9915 8444 9502 1953 939 1508 C ATOM 2607 SD MET B 39 5.200 -40.946 102.422 1.00 73.79 S ANISOU 2607 SD MET B 39 10346 7959 9730 1918 835 1512 S ATOM 2608 CE MET B 39 6.329 -42.093 103.214 1.00 71.03 C ANISOU 2608 CE MET B 39 10072 7622 9293 1606 849 1397 C ATOM 2609 N LEU B 40 0.320 -42.040 105.172 1.00 80.53 N ANISOU 2609 N LEU B 40 10142 10499 9958 2326 1410 875 N ATOM 2610 CA LEU B 40 -0.702 -41.807 106.181 1.00 83.85 C ANISOU 2610 CA LEU B 40 10313 11342 10205 2483 1587 586 C ATOM 2611 C LEU B 40 -0.150 -41.364 107.533 1.00 84.11 C ANISOU 2611 C LEU B 40 10631 11148 10178 2559 1642 435 C ATOM 2612 O LEU B 40 0.682 -42.048 108.132 1.00 81.90 O ANISOU 2612 O LEU B 40 10645 10674 9800 2242 1686 523 O ATOM 2613 CB LEU B 40 -1.564 -43.063 106.341 1.00 85.04 C ANISOU 2613 CB LEU B 40 10160 12051 10100 2041 1840 533 C ATOM 2614 CG LEU B 40 -2.213 -43.607 105.065 1.00 85.05 C ANISOU 2614 CG LEU B 40 9811 12379 10124 1910 1804 603 C ATOM 2615 CD1 LEU B 40 -2.722 -45.016 105.272 1.00 85.69 C ANISOU 2615 CD1 LEU B 40 9763 12829 9966 1289 2070 582 C ATOM 2616 CD2 LEU B 40 -3.333 -42.691 104.592 1.00 89.37 C ANISOU 2616 CD2 LEU B 40 9889 13370 10698 2428 1715 376 C ATOM 2617 N LYS B 41 -0.619 -40.208 107.996 1.00 87.06 N ANISOU 2617 N LYS B 41 10931 11554 10595 3031 1607 180 N ATOM 2618 CA LYS B 41 -0.355 -39.754 109.355 1.00 88.34 C ANISOU 2618 CA LYS B 41 11273 11641 10652 3138 1685 -57 C ATOM 2619 C LYS B 41 -1.646 -39.876 110.151 1.00 92.53 C ANISOU 2619 C LYS B 41 11391 12862 10904 3215 1934 -374 C ATOM 2620 O LYS B 41 -2.610 -39.149 109.903 1.00 96.19 O ANISOU 2620 O LYS B 41 11512 13631 11404 3662 1898 -613 O ATOM 2621 CB LYS B 41 0.171 -38.315 109.371 1.00 89.51 C ANISOU 2621 CB LYS B 41 11701 11260 11050 3589 1470 -171 C ATOM 2622 CG LYS B 41 0.629 -37.811 110.745 1.00 90.73 C ANISOU 2622 CG LYS B 41 12079 11278 11116 3678 1516 -448 C ATOM 2623 CD LYS B 41 1.004 -36.333 110.685 1.00 92.99 C ANISOU 2623 CD LYS B 41 12655 11014 11663 4106 1312 -608 C ATOM 2624 CE LYS B 41 1.114 -35.711 112.070 1.00 95.86 C ANISOU 2624 CE LYS B 41 13138 11366 11918 4296 1365 -1001 C ATOM 2625 NZ LYS B 41 0.934 -34.226 112.030 1.00 99.72 N ANISOU 2625 NZ LYS B 41 13833 11434 12623 4838 1197 -1256 N ATOM 2626 N ASN B 42 -1.651 -40.822 111.089 1.00 92.50 N ANISOU 2626 N ASN B 42 11437 13122 10586 2781 2183 -383 N ATOM 2627 CA ASN B 42 -2.804 -41.118 111.942 1.00 96.91 C ANISOU 2627 CA ASN B 42 11626 14401 10793 2673 2503 -674 C ATOM 2628 C ASN B 42 -4.078 -41.514 111.187 1.00 99.50 C ANISOU 2628 C ASN B 42 11366 15380 11059 2580 2638 -777 C ATOM 2629 O ASN B 42 -5.197 -41.230 111.633 1.00104.70 O ANISOU 2629 O ASN B 42 11537 16718 11525 2741 2826 -1163 O ATOM 2630 CB ASN B 42 -3.057 -39.967 112.919 1.00100.61 C ANISOU 2630 CB ASN B 42 12036 14978 11213 3175 2508 -1079 C ATOM 2631 CG ASN B 42 -1.988 -39.871 113.979 1.00 99.32 C ANISOU 2631 CG ASN B 42 12372 14412 10952 3103 2480 -1064 C ATOM 2632 OD1 ASN B 42 -2.017 -40.594 114.974 1.00100.73 O ANISOU 2632 OD1 ASN B 42 12662 14864 10747 2747 2720 -1078 O ATOM 2633 ND2 ASN B 42 -1.030 -38.979 113.770 1.00 97.50 N ANISOU 2633 ND2 ASN B 42 12467 13542 11036 3415 2189 -1042 N ATOM 2634 N GLY B 43 -3.896 -42.187 110.053 1.00 96.34 N ANISOU 2634 N GLY B 43 10973 14831 10800 2317 2540 -482 N ATOM 2635 CA GLY B 43 -5.015 -42.672 109.251 1.00 98.57 C ANISOU 2635 CA GLY B 43 10696 15736 11019 2163 2643 -586 C ATOM 2636 C GLY B 43 -5.346 -41.812 108.047 1.00 98.93 C ANISOU 2636 C GLY B 43 10468 15782 11340 2749 2330 -627 C ATOM 2637 O GLY B 43 -5.759 -42.332 107.012 1.00 98.82 O ANISOU 2637 O GLY B 43 10176 16016 11356 2591 2285 -549 O ATOM 2638 N LYS B 44 -5.172 -40.499 108.182 1.00100.03 N ANISOU 2638 N LYS B 44 10734 15622 11652 3430 2103 -753 N ATOM 2639 CA LYS B 44 -5.482 -39.554 107.106 1.00101.53 C ANISOU 2639 CA LYS B 44 10805 15717 12056 4079 1773 -768 C ATOM 2640 C LYS B 44 -4.302 -39.430 106.138 1.00 96.62 C ANISOU 2640 C LYS B 44 10717 14293 11700 4027 1513 -310 C ATOM 2641 O LYS B 44 -3.150 -39.648 106.528 1.00 92.65 O ANISOU 2641 O LYS B 44 10689 13241 11272 3699 1536 -92 O ATOM 2642 CB LYS B 44 -5.841 -38.174 107.673 1.00106.00 C ANISOU 2642 CB LYS B 44 11373 16234 12670 4853 1634 -1117 C ATOM 2643 CG LYS B 44 -6.635 -38.186 108.981 1.00110.68 C ANISOU 2643 CG LYS B 44 11577 17492 12984 4870 1928 -1595 C ATOM 2644 CD LYS B 44 -7.181 -36.796 109.320 1.00116.71 C ANISOU 2644 CD LYS B 44 12247 18298 13799 5776 1736 -2021 C ATOM 2645 CE LYS B 44 -7.214 -36.534 110.828 1.00119.20 C ANISOU 2645 CE LYS B 44 12572 18793 13926 5785 1970 -2386 C ATOM 2646 NZ LYS B 44 -8.077 -37.481 111.591 1.00122.04 N ANISOU 2646 NZ LYS B 44 12348 20134 13888 5274 2407 -2671 N ATOM 2647 N LYS B 45 -4.596 -39.088 104.882 1.00 97.35 N ANISOU 2647 N LYS B 45 10708 14384 11897 4356 1266 -194 N ATOM 2648 CA LYS B 45 -3.560 -38.867 103.864 1.00 93.62 C ANISOU 2648 CA LYS B 45 10719 13223 11631 4319 1036 222 C ATOM 2649 C LYS B 45 -2.835 -37.544 104.105 1.00 94.35 C ANISOU 2649 C LYS B 45 11368 12569 11910 4738 850 268 C ATOM 2650 O LYS B 45 -3.361 -36.666 104.782 1.00 98.54 O ANISOU 2650 O LYS B 45 11872 13139 12428 5249 812 -37 O ATOM 2651 CB LYS B 45 -4.161 -38.904 102.452 1.00 95.06 C ANISOU 2651 CB LYS B 45 10644 13681 11793 4544 835 332 C ATOM 2652 CG LYS B 45 -5.232 -37.855 102.177 1.00101.25 C ANISOU 2652 CG LYS B 45 11188 14755 12528 5383 606 75 C ATOM 2653 N ILE B 46 -1.630 -37.407 103.560 1.00 91.02 N ANISOU 2653 N ILE B 46 11445 11489 11650 4496 749 606 N ATOM 2654 CA ILE B 46 -0.861 -36.168 103.697 1.00 92.39 C ANISOU 2654 CA ILE B 46 12198 10907 12000 4754 601 656 C ATOM 2655 C ILE B 46 -0.882 -35.381 102.383 1.00 94.95 C ANISOU 2655 C ILE B 46 12826 10864 12388 5100 340 924 C ATOM 2656 O ILE B 46 -0.381 -35.868 101.363 1.00 92.19 O ANISOU 2656 O ILE B 46 12545 10445 12037 4766 307 1243 O ATOM 2657 CB ILE B 46 0.590 -36.430 104.157 1.00 88.20 C ANISOU 2657 CB ILE B 46 12032 9909 11572 4201 695 775 C ATOM 2658 CG1 ILE B 46 0.593 -37.308 105.418 1.00 86.30 C ANISOU 2658 CG1 ILE B 46 11555 10042 11193 3892 922 560 C ATOM 2659 CG2 ILE B 46 1.334 -35.100 104.385 1.00 90.23 C ANISOU 2659 CG2 ILE B 46 12859 9421 12004 4389 576 745 C ATOM 2660 CD1 ILE B 46 1.845 -38.146 105.614 1.00 80.83 C ANISOU 2660 CD1 ILE B 46 11045 9158 10509 3324 990 708 C ATOM 2661 N PRO B 47 -1.449 -34.153 102.416 1.00100.74 N ANISOU 2661 N PRO B 47 13792 11340 13146 5797 143 787 N ATOM 2662 CA PRO B 47 -1.796 -33.329 101.246 1.00105.06 C ANISOU 2662 CA PRO B 47 14656 11595 13666 6322 -150 1008 C ATOM 2663 C PRO B 47 -0.702 -33.219 100.176 1.00103.11 C ANISOU 2663 C PRO B 47 14952 10753 13474 5902 -202 1486 C ATOM 2664 O PRO B 47 -1.024 -33.113 98.986 1.00105.15 O ANISOU 2664 O PRO B 47 15296 11046 13611 6128 -387 1748 O ATOM 2665 CB PRO B 47 -2.099 -31.951 101.857 1.00111.11 C ANISOU 2665 CB PRO B 47 15844 11872 14502 7013 -316 764 C ATOM 2666 CG PRO B 47 -1.548 -32.006 103.259 1.00108.92 C ANISOU 2666 CG PRO B 47 15564 11491 14329 6679 -86 478 C ATOM 2667 CD PRO B 47 -1.709 -33.423 103.671 1.00103.89 C ANISOU 2667 CD PRO B 47 14256 11637 13582 6156 176 394 C ATOM 2668 N LYS B 48 0.565 -33.232 100.591 1.00 99.78 N ANISOU 2668 N LYS B 48 14863 9854 13195 5307 -43 1564 N ATOM 2669 CA LYS B 48 1.681 -33.265 99.643 1.00 97.76 C ANISOU 2669 CA LYS B 48 15001 9180 12964 4782 -24 1946 C ATOM 2670 C LYS B 48 2.680 -34.381 99.942 1.00 91.55 C ANISOU 2670 C LYS B 48 13944 8615 12225 4032 200 1936 C ATOM 2671 O LYS B 48 3.397 -34.350 100.945 1.00 90.04 O ANISOU 2671 O LYS B 48 13827 8242 12143 3759 322 1734 O ATOM 2672 CB LYS B 48 2.376 -31.901 99.531 1.00102.00 C ANISOU 2672 CB LYS B 48 16364 8794 13598 4820 -103 2075 C ATOM 2673 CG LYS B 48 1.857 -31.050 98.378 1.00107.65 C ANISOU 2673 CG LYS B 48 17575 9152 14175 5318 -355 2390 C ATOM 2674 CD LYS B 48 2.614 -29.739 98.251 1.00112.53 C ANISOU 2674 CD LYS B 48 19140 8753 14863 5229 -395 2557 C ATOM 2675 CE LYS B 48 2.206 -28.989 96.989 1.00118.40 C ANISOU 2675 CE LYS B 48 20501 9089 15398 5658 -644 2967 C ATOM 2676 NZ LYS B 48 2.934 -27.695 96.840 1.00124.00 N ANISOU 2676 NZ LYS B 48 22266 8707 16141 5499 -659 3167 N ATOM 2677 N VAL B 49 2.692 -35.373 99.059 1.00 88.49 N ANISOU 2677 N VAL B 49 13246 8644 11734 3759 223 2125 N ATOM 2678 CA VAL B 49 3.645 -36.473 99.110 1.00 83.29 C ANISOU 2678 CA VAL B 49 12381 8174 11093 3128 381 2135 C ATOM 2679 C VAL B 49 4.321 -36.518 97.751 1.00 82.99 C ANISOU 2679 C VAL B 49 12535 8007 10990 2827 347 2456 C ATOM 2680 O VAL B 49 3.649 -36.588 96.722 1.00 84.66 O ANISOU 2680 O VAL B 49 12671 8435 11062 3046 233 2648 O ATOM 2681 CB VAL B 49 2.945 -37.829 99.386 1.00 80.33 C ANISOU 2681 CB VAL B 49 11418 8483 10622 3053 464 1998 C ATOM 2682 CG1 VAL B 49 3.901 -38.987 99.172 1.00 75.95 C ANISOU 2682 CG1 VAL B 49 10743 8058 10057 2494 560 2051 C ATOM 2683 CG2 VAL B 49 2.374 -37.872 100.794 1.00 80.93 C ANISOU 2683 CG2 VAL B 49 11309 8740 10702 3232 557 1680 C ATOM 2684 N GLU B 50 5.646 -36.472 97.744 1.00 81.51 N ANISOU 2684 N GLU B 50 12565 7534 10872 2325 447 2477 N ATOM 2685 CA GLU B 50 6.391 -36.471 96.492 1.00 81.84 C ANISOU 2685 CA GLU B 50 12782 7495 10819 1966 464 2742 C ATOM 2686 C GLU B 50 6.868 -37.861 96.086 1.00 77.31 C ANISOU 2686 C GLU B 50 11769 7423 10183 1596 532 2700 C ATOM 2687 O GLU B 50 7.311 -38.646 96.925 1.00 74.10 O ANISOU 2687 O GLU B 50 11111 7195 9850 1417 599 2457 O ATOM 2688 CB GLU B 50 7.565 -35.500 96.576 1.00 84.42 C ANISOU 2688 CB GLU B 50 13599 7254 11223 1586 555 2754 C ATOM 2689 CG GLU B 50 7.173 -34.054 96.308 1.00 90.87 C ANISOU 2689 CG GLU B 50 15062 7443 12023 1882 465 2952 C ATOM 2690 CD GLU B 50 8.102 -33.052 96.970 1.00 94.33 C ANISOU 2690 CD GLU B 50 15972 7266 12604 1556 568 2807 C ATOM 2691 OE1 GLU B 50 7.587 -32.042 97.492 1.00 98.64 O ANISOU 2691 OE1 GLU B 50 16934 7320 13226 1949 476 2759 O ATOM 2692 OE2 GLU B 50 9.336 -33.268 96.974 1.00 93.36 O ANISOU 2692 OE2 GLU B 50 15785 7177 12510 920 732 2694 O ATOM 2693 N MET B 51 6.766 -38.152 94.791 1.00 77.50 N ANISOU 2693 N MET B 51 11747 7657 10044 1525 492 2932 N ATOM 2694 CA MET B 51 7.203 -39.428 94.244 1.00 73.97 C ANISOU 2694 CA MET B 51 10924 7659 9521 1209 536 2879 C ATOM 2695 C MET B 51 8.245 -39.212 93.162 1.00 74.91 C ANISOU 2695 C MET B 51 11223 7722 9519 798 606 3034 C ATOM 2696 O MET B 51 8.178 -38.242 92.416 1.00 78.70 O ANISOU 2696 O MET B 51 12100 7925 9877 826 589 3310 O ATOM 2697 CB MET B 51 6.021 -40.203 93.665 1.00 73.56 C ANISOU 2697 CB MET B 51 10527 8076 9346 1471 438 2927 C ATOM 2698 CG MET B 51 4.963 -40.600 94.683 1.00 73.58 C ANISOU 2698 CG MET B 51 10256 8281 9420 1763 425 2725 C ATOM 2699 SD MET B 51 3.534 -41.448 93.959 1.00 76.83 S ANISOU 2699 SD MET B 51 10202 9322 9669 1979 335 2707 S ATOM 2700 CE MET B 51 2.908 -40.242 92.776 1.00 81.78 C ANISOU 2700 CE MET B 51 11075 9878 10120 2434 134 2996 C ATOM 2701 N SER B 52 9.208 -40.124 93.091 1.00 72.02 N ANISOU 2701 N SER B 52 10585 7625 9153 429 683 2842 N ATOM 2702 CA SER B 52 10.214 -40.129 92.037 1.00 72.93 C ANISOU 2702 CA SER B 52 10730 7864 9115 4 778 2904 C ATOM 2703 C SER B 52 9.668 -40.825 90.796 1.00 72.52 C ANISOU 2703 C SER B 52 10481 8223 8850 74 711 3060 C ATOM 2704 O SER B 52 8.682 -41.557 90.878 1.00 70.80 O ANISOU 2704 O SER B 52 10010 8249 8643 376 599 3025 O ATOM 2705 CB SER B 52 11.459 -40.874 92.517 1.00 70.89 C ANISOU 2705 CB SER B 52 10186 7817 8933 -323 851 2537 C ATOM 2706 OG SER B 52 11.183 -42.255 92.714 1.00 67.36 O ANISOU 2706 OG SER B 52 9369 7721 8502 -161 757 2354 O ATOM 2707 N ASP B 53 10.318 -40.599 89.654 1.00 74.52 N ANISOU 2707 N ASP B 53 10842 8589 8884 -250 797 3202 N ATOM 2708 CA ASP B 53 9.987 -41.299 88.414 1.00 74.26 C ANISOU 2708 CA ASP B 53 10601 9008 8607 -236 742 3300 C ATOM 2709 C ASP B 53 10.228 -42.791 88.604 1.00 70.30 C ANISOU 2709 C ASP B 53 9598 8926 8185 -278 710 2941 C ATOM 2710 O ASP B 53 11.229 -43.197 89.202 1.00 68.67 O ANISOU 2710 O ASP B 53 9245 8745 8100 -490 778 2643 O ATOM 2711 CB ASP B 53 10.846 -40.807 87.240 1.00 77.88 C ANISOU 2711 CB ASP B 53 11267 9548 8775 -664 890 3473 C ATOM 2712 CG ASP B 53 11.050 -39.297 87.228 1.00 82.12 C ANISOU 2712 CG ASP B 53 12435 9523 9245 -813 987 3783 C ATOM 2713 OD1 ASP B 53 10.347 -38.572 87.961 1.00 83.00 O ANISOU 2713 OD1 ASP B 53 12846 9178 9514 -460 886 3898 O ATOM 2714 OD2 ASP B 53 11.927 -38.833 86.470 1.00 84.75 O ANISOU 2714 OD2 ASP B 53 12989 9866 9346 -1309 1178 3893 O ATOM 2715 N MET B 54 9.306 -43.596 88.088 1.00 69.26 N ANISOU 2715 N MET B 54 9231 9117 7967 -59 589 2948 N ATOM 2716 CA MET B 54 9.362 -45.045 88.223 1.00 66.31 C ANISOU 2716 CA MET B 54 8487 9051 7655 -82 541 2629 C ATOM 2717 C MET B 54 10.355 -45.663 87.247 1.00 66.82 C ANISOU 2717 C MET B 54 8369 9474 7544 -368 592 2461 C ATOM 2718 O MET B 54 10.374 -45.311 86.070 1.00 69.43 O ANISOU 2718 O MET B 54 8745 10024 7612 -476 622 2643 O ATOM 2719 CB MET B 54 7.974 -45.633 87.975 1.00 66.12 C ANISOU 2719 CB MET B 54 8280 9256 7588 177 416 2658 C ATOM 2720 CG MET B 54 7.811 -47.102 88.369 1.00 63.87 C ANISOU 2720 CG MET B 54 7733 9135 7400 134 378 2342 C ATOM 2721 SD MET B 54 6.165 -47.735 87.986 1.00 64.49 S ANISOU 2721 SD MET B 54 7553 9555 7397 294 277 2323 S ATOM 2722 CE MET B 54 5.140 -46.648 88.975 1.00 65.63 C ANISOU 2722 CE MET B 54 7803 9479 7653 611 276 2494 C ATOM 2723 N SER B 55 11.169 -46.592 87.738 1.00 64.93 N ANISOU 2723 N SER B 55 7938 9317 7417 -449 587 2098 N ATOM 2724 CA SER B 55 12.043 -47.388 86.877 1.00 65.74 C ANISOU 2724 CA SER B 55 7792 9826 7361 -625 599 1827 C ATOM 2725 C SER B 55 11.830 -48.882 87.112 1.00 63.93 C ANISOU 2725 C SER B 55 7382 9695 7212 -459 456 1514 C ATOM 2726 O SER B 55 10.801 -49.286 87.656 1.00 62.46 O ANISOU 2726 O SER B 55 7259 9331 7141 -291 380 1578 O ATOM 2727 CB SER B 55 13.501 -47.014 87.114 1.00 66.87 C ANISOU 2727 CB SER B 55 7881 10020 7508 -877 718 1603 C ATOM 2728 OG SER B 55 13.696 -45.637 86.875 1.00 69.58 O ANISOU 2728 OG SER B 55 8472 10206 7760 -1126 881 1896 O ATOM 2729 N PHE B 56 12.795 -49.693 86.680 1.00 64.79 N ANISOU 2729 N PHE B 56 7286 10092 7240 -521 429 1153 N ATOM 2730 CA PHE B 56 12.821 -51.127 86.998 1.00 64.19 C ANISOU 2730 CA PHE B 56 7152 9996 7243 -337 270 810 C ATOM 2731 C PHE B 56 14.241 -51.692 87.059 1.00 65.51 C ANISOU 2731 C PHE B 56 7149 10360 7380 -286 213 354 C ATOM 2732 O PHE B 56 15.186 -51.083 86.558 1.00 67.46 O ANISOU 2732 O PHE B 56 7201 10930 7499 -478 332 253 O ATOM 2733 CB PHE B 56 11.950 -51.949 86.041 1.00 64.74 C ANISOU 2733 CB PHE B 56 7130 10278 7189 -333 202 788 C ATOM 2734 CG PHE B 56 12.154 -51.621 84.596 1.00 66.97 C ANISOU 2734 CG PHE B 56 7213 11041 7191 -498 274 825 C ATOM 2735 CD1 PHE B 56 13.231 -52.149 83.893 1.00 68.28 C ANISOU 2735 CD1 PHE B 56 7154 11589 7202 -555 275 455 C ATOM 2736 CD2 PHE B 56 11.256 -50.795 83.931 1.00 67.81 C ANISOU 2736 CD2 PHE B 56 7363 11254 7148 -559 326 1211 C ATOM 2737 CE1 PHE B 56 13.416 -51.859 82.555 1.00 70.52 C ANISOU 2737 CE1 PHE B 56 7262 12363 7170 -742 369 486 C ATOM 2738 CE2 PHE B 56 11.436 -50.497 82.591 1.00 70.50 C ANISOU 2738 CE2 PHE B 56 7588 12036 7162 -704 385 1280 C ATOM 2739 CZ PHE B 56 12.521 -51.032 81.902 1.00 71.85 C ANISOU 2739 CZ PHE B 56 7537 12598 7164 -832 428 926 C ATOM 2740 N SER B 57 14.369 -52.864 87.675 1.00 65.20 N ANISOU 2740 N SER B 57 7202 10135 7435 -26 30 63 N ATOM 2741 CA SER B 57 15.661 -53.480 87.937 1.00 66.96 C ANISOU 2741 CA SER B 57 7298 10506 7638 181 -104 -419 C ATOM 2742 C SER B 57 15.897 -54.668 87.012 1.00 69.15 C ANISOU 2742 C SER B 57 7442 11050 7783 314 -234 -793 C ATOM 2743 O SER B 57 15.003 -55.046 86.257 1.00 69.22 O ANISOU 2743 O SER B 57 7484 11085 7732 209 -217 -665 O ATOM 2744 CB SER B 57 15.715 -53.934 89.387 1.00 66.03 C ANISOU 2744 CB SER B 57 7490 9922 7676 477 -269 -483 C ATOM 2745 OG SER B 57 14.577 -54.720 89.687 1.00 65.15 O ANISOU 2745 OG SER B 57 7716 9411 7626 534 -334 -308 O ATOM 2746 N LYS B 58 17.093 -55.258 87.097 1.00 71.56 N ANISOU 2746 N LYS B 58 7580 11576 8034 581 -385 -1302 N ATOM 2747 CA LYS B 58 17.544 -56.337 86.200 1.00 74.38 C ANISOU 2747 CA LYS B 58 7767 12249 8246 777 -527 -1771 C ATOM 2748 C LYS B 58 16.489 -57.387 85.866 1.00 74.15 C ANISOU 2748 C LYS B 58 8044 11888 8241 832 -637 -1713 C ATOM 2749 O LYS B 58 16.439 -57.887 84.739 1.00 75.92 O ANISOU 2749 O LYS B 58 8083 12446 8317 784 -642 -1930 O ATOM 2750 CB LYS B 58 18.783 -57.028 86.775 1.00 77.18 C ANISOU 2750 CB LYS B 58 8046 12689 8588 1255 -783 -2343 C ATOM 2751 N ASP B 59 15.654 -57.709 86.847 1.00 72.38 N ANISOU 2751 N ASP B 59 8280 11040 8182 886 -705 -1450 N ATOM 2752 CA ASP B 59 14.625 -58.732 86.696 1.00 72.97 C ANISOU 2752 CA ASP B 59 8693 10747 8287 846 -781 -1416 C ATOM 2753 C ASP B 59 13.350 -58.236 86.001 1.00 71.41 C ANISOU 2753 C ASP B 59 8370 10698 8066 434 -582 -1045 C ATOM 2754 O ASP B 59 12.432 -59.024 85.753 1.00 72.46 O ANISOU 2754 O ASP B 59 8685 10641 8204 308 -613 -1060 O ATOM 2755 CB ASP B 59 14.270 -59.303 88.066 1.00 72.77 C ANISOU 2755 CB ASP B 59 9238 10022 8391 1006 -901 -1297 C ATOM 2756 CG ASP B 59 13.711 -58.254 89.002 1.00 70.22 C ANISOU 2756 CG ASP B 59 8976 9529 8175 819 -727 -834 C ATOM 2757 OD1 ASP B 59 13.621 -57.070 88.597 1.00 68.43 O ANISOU 2757 OD1 ASP B 59 8391 9665 7944 601 -538 -607 O ATOM 2758 OD2 ASP B 59 13.360 -58.618 90.145 1.00 71.04 O ANISOU 2758 OD2 ASP B 59 9534 9117 8342 896 -781 -700 O ATOM 2759 N TRP B 60 13.303 -56.937 85.703 1.00 69.66 N ANISOU 2759 N TRP B 60 7862 10807 7799 233 -392 -740 N ATOM 2760 CA TRP B 60 12.169 -56.284 85.032 1.00 68.71 C ANISOU 2760 CA TRP B 60 7612 10883 7610 -48 -245 -380 C ATOM 2761 C TRP B 60 11.021 -55.957 85.978 1.00 66.98 C ANISOU 2761 C TRP B 60 7624 10276 7549 -132 -183 -18 C ATOM 2762 O TRP B 60 9.865 -55.921 85.555 1.00 67.38 O ANISOU 2762 O TRP B 60 7605 10437 7558 -293 -137 143 O ATOM 2763 CB TRP B 60 11.640 -57.111 83.852 1.00 70.59 C ANISOU 2763 CB TRP B 60 7721 11404 7697 -141 -301 -590 C ATOM 2764 CG TRP B 60 12.666 -57.447 82.817 1.00 72.68 C ANISOU 2764 CG TRP B 60 7716 12137 7761 -62 -345 -982 C ATOM 2765 CD1 TRP B 60 13.333 -58.632 82.679 1.00 74.65 C ANISOU 2765 CD1 TRP B 60 8020 12343 8000 166 -520 -1493 C ATOM 2766 CD2 TRP B 60 13.139 -56.595 81.767 1.00 73.14 C ANISOU 2766 CD2 TRP B 60 7430 12795 7565 -205 -206 -918 C ATOM 2767 NE1 TRP B 60 14.194 -58.569 81.611 1.00 76.57 N ANISOU 2767 NE1 TRP B 60 7890 13196 8007 188 -493 -1798 N ATOM 2768 CE2 TRP B 60 14.095 -57.330 81.033 1.00 75.81 C ANISOU 2768 CE2 TRP B 60 7551 13513 7742 -83 -280 -1436 C ATOM 2769 CE3 TRP B 60 12.850 -55.282 81.377 1.00 72.32 C ANISOU 2769 CE3 TRP B 60 7235 12920 7324 -419 -29 -471 C ATOM 2770 CZ2 TRP B 60 14.765 -56.795 79.931 1.00 77.92 C ANISOU 2770 CZ2 TRP B 60 7462 14448 7696 -237 -138 -1524 C ATOM 2771 CZ3 TRP B 60 13.515 -54.752 80.283 1.00 74.70 C ANISOU 2771 CZ3 TRP B 60 7281 13792 7309 -578 100 -507 C ATOM 2772 CH2 TRP B 60 14.461 -55.508 79.572 1.00 77.41 C ANISOU 2772 CH2 TRP B 60 7361 14573 7477 -521 66 -1031 C ATOM 2773 N SER B 61 11.327 -55.718 87.251 1.00 65.76 N ANISOU 2773 N SER B 61 7701 9737 7546 -13 -187 69 N ATOM 2774 CA SER B 61 10.290 -55.336 88.215 1.00 64.45 C ANISOU 2774 CA SER B 61 7726 9262 7501 -90 -102 383 C ATOM 2775 C SER B 61 10.381 -53.860 88.611 1.00 63.03 C ANISOU 2775 C SER B 61 7466 9113 7368 -84 19 690 C ATOM 2776 O SER B 61 11.435 -53.365 89.020 1.00 62.66 O ANISOU 2776 O SER B 61 7423 9030 7354 9 15 627 O ATOM 2777 CB SER B 61 10.309 -56.241 89.451 1.00 64.66 C ANISOU 2777 CB SER B 61 8172 8774 7622 10 -184 283 C ATOM 2778 OG SER B 61 11.225 -55.779 90.431 1.00 63.98 O ANISOU 2778 OG SER B 61 8209 8504 7598 224 -225 281 O ATOM 2779 N PHE B 62 9.253 -53.171 88.492 1.00 62.82 N ANISOU 2779 N PHE B 62 7368 9162 7338 -172 112 979 N ATOM 2780 CA PHE B 62 9.183 -51.733 88.720 1.00 62.26 C ANISOU 2780 CA PHE B 62 7284 9078 7295 -136 206 1279 C ATOM 2781 C PHE B 62 9.456 -51.352 90.167 1.00 60.92 C ANISOU 2781 C PHE B 62 7334 8526 7286 -38 235 1322 C ATOM 2782 O PHE B 62 9.262 -52.157 91.074 1.00 60.70 O ANISOU 2782 O PHE B 62 7489 8250 7325 -2 200 1215 O ATOM 2783 CB PHE B 62 7.821 -51.201 88.267 1.00 63.17 C ANISOU 2783 CB PHE B 62 7280 9377 7344 -135 238 1519 C ATOM 2784 CG PHE B 62 7.540 -51.438 86.812 1.00 64.70 C ANISOU 2784 CG PHE B 62 7251 10004 7329 -201 189 1489 C ATOM 2785 CD1 PHE B 62 6.913 -52.606 86.393 1.00 65.25 C ANISOU 2785 CD1 PHE B 62 7193 10248 7350 -304 129 1261 C ATOM 2786 CD2 PHE B 62 7.924 -50.500 85.856 1.00 65.94 C ANISOU 2786 CD2 PHE B 62 7365 10384 7305 -194 210 1680 C ATOM 2787 CE1 PHE B 62 6.668 -52.833 85.048 1.00 67.33 C ANISOU 2787 CE1 PHE B 62 7231 10954 7397 -356 68 1191 C ATOM 2788 CE2 PHE B 62 7.680 -50.717 84.507 1.00 67.88 C ANISOU 2788 CE2 PHE B 62 7427 11067 7298 -239 157 1658 C ATOM 2789 CZ PHE B 62 7.048 -51.883 84.101 1.00 68.57 C ANISOU 2789 CZ PHE B 62 7328 11380 7347 -298 75 1396 C ATOM 2790 N TYR B 63 9.926 -50.127 90.369 1.00 60.75 N ANISOU 2790 N TYR B 63 7340 8444 7299 -19 302 1474 N ATOM 2791 CA TYR B 63 10.197 -49.615 91.708 1.00 59.82 C ANISOU 2791 CA TYR B 63 7407 8003 7319 72 327 1491 C ATOM 2792 C TYR B 63 10.115 -48.096 91.744 1.00 60.37 C ANISOU 2792 C TYR B 63 7537 7979 7420 66 420 1736 C ATOM 2793 O TYR B 63 10.454 -47.417 90.774 1.00 62.01 O ANISOU 2793 O TYR B 63 7701 8333 7527 -53 468 1850 O ATOM 2794 CB TYR B 63 11.560 -50.091 92.214 1.00 59.85 C ANISOU 2794 CB TYR B 63 7443 7953 7343 119 246 1188 C ATOM 2795 CG TYR B 63 12.748 -49.431 91.553 1.00 61.25 C ANISOU 2795 CG TYR B 63 7449 8362 7462 -15 291 1077 C ATOM 2796 CD1 TYR B 63 13.291 -48.255 92.070 1.00 62.24 C ANISOU 2796 CD1 TYR B 63 7628 8370 7651 -103 380 1127 C ATOM 2797 CD2 TYR B 63 13.336 -49.989 90.423 1.00 62.79 C ANISOU 2797 CD2 TYR B 63 7425 8916 7518 -100 266 885 C ATOM 2798 CE1 TYR B 63 14.386 -47.644 91.472 1.00 65.14 C ANISOU 2798 CE1 TYR B 63 7838 8972 7939 -344 470 1000 C ATOM 2799 CE2 TYR B 63 14.434 -49.388 89.811 1.00 65.42 C ANISOU 2799 CE2 TYR B 63 7564 9542 7751 -301 357 751 C ATOM 2800 CZ TYR B 63 14.956 -48.216 90.342 1.00 66.73 C ANISOU 2800 CZ TYR B 63 7791 9586 7977 -458 472 815 C ATOM 2801 OH TYR B 63 16.044 -47.613 89.745 1.00 69.45 O ANISOU 2801 OH TYR B 63 7946 10241 8200 -771 609 660 O ATOM 2802 N ILE B 64 9.685 -47.567 92.881 1.00 59.57 N ANISOU 2802 N ILE B 64 7589 7609 7434 187 451 1810 N ATOM 2803 CA ILE B 64 9.398 -46.149 92.996 1.00 60.35 C ANISOU 2803 CA ILE B 64 7817 7537 7575 244 515 2029 C ATOM 2804 C ILE B 64 9.581 -45.666 94.443 1.00 59.62 C ANISOU 2804 C ILE B 64 7894 7139 7619 343 539 1950 C ATOM 2805 O ILE B 64 9.175 -46.339 95.394 1.00 58.23 O ANISOU 2805 O ILE B 64 7740 6913 7471 442 522 1851 O ATOM 2806 CB ILE B 64 7.971 -45.843 92.431 1.00 61.67 C ANISOU 2806 CB ILE B 64 7927 7830 7674 405 501 2254 C ATOM 2807 CG1 ILE B 64 7.605 -44.356 92.582 1.00 63.93 C ANISOU 2807 CG1 ILE B 64 8430 7869 7992 581 519 2473 C ATOM 2808 CG2 ILE B 64 6.926 -46.796 93.037 1.00 60.59 C ANISOU 2808 CG2 ILE B 64 7657 7809 7556 478 493 2150 C ATOM 2809 CD1 ILE B 64 6.214 -43.988 92.092 1.00 65.49 C ANISOU 2809 CD1 ILE B 64 8554 8231 8098 869 448 2642 C ATOM 2810 N LEU B 65 10.220 -44.509 94.597 1.00 60.76 N ANISOU 2810 N LEU B 65 8189 7078 7819 274 590 1984 N ATOM 2811 CA LEU B 65 10.380 -43.891 95.908 1.00 60.77 C ANISOU 2811 CA LEU B 65 8353 6798 7939 367 609 1885 C ATOM 2812 C LEU B 65 9.369 -42.765 96.159 1.00 62.44 C ANISOU 2812 C LEU B 65 8748 6773 8204 577 639 2083 C ATOM 2813 O LEU B 65 9.251 -41.829 95.362 1.00 64.66 O ANISOU 2813 O LEU B 65 9188 6925 8454 561 658 2290 O ATOM 2814 CB LEU B 65 11.811 -43.377 96.100 1.00 61.69 C ANISOU 2814 CB LEU B 65 8506 6840 8092 132 639 1684 C ATOM 2815 CG LEU B 65 12.104 -42.728 97.460 1.00 62.22 C ANISOU 2815 CG LEU B 65 8723 6650 8268 202 642 1515 C ATOM 2816 CD1 LEU B 65 12.030 -43.746 98.603 1.00 59.78 C ANISOU 2816 CD1 LEU B 65 8363 6416 7936 415 546 1324 C ATOM 2817 CD2 LEU B 65 13.449 -42.011 97.454 1.00 64.21 C ANISOU 2817 CD2 LEU B 65 8980 6869 8549 -116 698 1299 C ATOM 2818 N ALA B 66 8.641 -42.877 97.269 1.00 61.94 N ANISOU 2818 N ALA B 66 8693 6657 8186 796 639 2008 N ATOM 2819 CA ALA B 66 7.760 -41.816 97.748 1.00 64.01 C ANISOU 2819 CA ALA B 66 9099 6720 8503 1069 653 2085 C ATOM 2820 C ALA B 66 8.305 -41.293 99.070 1.00 64.37 C ANISOU 2820 C ALA B 66 9308 6509 8641 1092 679 1878 C ATOM 2821 O ALA B 66 8.690 -42.076 99.936 1.00 62.81 O ANISOU 2821 O ALA B 66 9042 6408 8415 1041 677 1692 O ATOM 2822 CB ALA B 66 6.341 -42.328 97.912 1.00 64.02 C ANISOU 2822 CB ALA B 66 8890 6997 8437 1301 655 2104 C ATOM 2823 N HIS B 67 8.348 -39.973 99.217 1.00 67.07 N ANISOU 2823 N HIS B 67 9914 6501 9069 1181 687 1905 N ATOM 2824 CA HIS B 67 9.009 -39.355 100.362 1.00 68.23 C ANISOU 2824 CA HIS B 67 10229 6388 9306 1146 708 1667 C ATOM 2825 C HIS B 67 8.302 -38.084 100.818 1.00 71.48 C ANISOU 2825 C HIS B 67 10909 6454 9797 1452 702 1669 C ATOM 2826 O HIS B 67 8.039 -37.187 100.012 1.00 74.39 O ANISOU 2826 O HIS B 67 11535 6544 10185 1533 675 1871 O ATOM 2827 CB HIS B 67 10.470 -39.046 100.022 1.00 68.93 C ANISOU 2827 CB HIS B 67 10403 6352 9434 737 735 1565 C ATOM 2828 CG HIS B 67 10.629 -38.132 98.850 1.00 72.65 C ANISOU 2828 CG HIS B 67 11128 6569 9908 553 780 1804 C ATOM 2829 ND1 HIS B 67 10.622 -36.758 98.972 1.00 77.42 N ANISOU 2829 ND1 HIS B 67 12155 6670 10591 552 809 1846 N ATOM 2830 CD2 HIS B 67 10.772 -38.392 97.528 1.00 73.62 C ANISOU 2830 CD2 HIS B 67 11206 6843 9923 363 801 2027 C ATOM 2831 CE1 HIS B 67 10.769 -36.210 97.778 1.00 79.98 C ANISOU 2831 CE1 HIS B 67 12737 6810 10841 351 852 2122 C ATOM 2832 NE2 HIS B 67 10.860 -37.179 96.885 1.00 78.20 N ANISOU 2832 NE2 HIS B 67 12208 7014 10491 234 852 2235 N ATOM 2833 N THR B 68 8.006 -38.007 102.113 1.00 71.70 N ANISOU 2833 N THR B 68 10919 6487 9838 1649 714 1436 N ATOM 2834 CA THR B 68 7.341 -36.834 102.682 1.00 75.14 C ANISOU 2834 CA THR B 68 11589 6618 10343 1999 697 1349 C ATOM 2835 C THR B 68 8.108 -36.242 103.861 1.00 76.26 C ANISOU 2835 C THR B 68 11909 6508 10558 1913 715 1029 C ATOM 2836 O THR B 68 8.835 -36.950 104.565 1.00 74.01 O ANISOU 2836 O THR B 68 11469 6436 10216 1713 730 840 O ATOM 2837 CB THR B 68 5.861 -37.131 103.090 1.00 75.71 C ANISOU 2837 CB THR B 68 11413 7032 10321 2432 703 1316 C ATOM 2838 OG1 THR B 68 5.198 -35.907 103.441 1.00 79.83 O ANISOU 2838 OG1 THR B 68 12160 7264 10906 2863 650 1211 O ATOM 2839 CG2 THR B 68 5.788 -38.104 104.268 1.00 73.66 C ANISOU 2839 CG2 THR B 68 10912 7136 9941 2364 792 1110 C ATOM 2840 N GLU B 69 7.936 -34.936 104.051 1.00 80.18 N ANISOU 2840 N GLU B 69 12764 6538 11163 2097 689 955 N ATOM 2841 CA GLU B 69 8.465 -34.227 105.208 1.00 82.32 C ANISOU 2841 CA GLU B 69 13223 6550 11506 2072 698 600 C ATOM 2842 C GLU B 69 7.534 -34.460 106.410 1.00 82.21 C ANISOU 2842 C GLU B 69 13010 6836 11391 2490 709 372 C ATOM 2843 O GLU B 69 6.314 -34.539 106.240 1.00 82.85 O ANISOU 2843 O GLU B 69 12953 7116 11410 2882 703 468 O ATOM 2844 CB GLU B 69 8.588 -32.737 104.879 1.00 87.39 C ANISOU 2844 CB GLU B 69 14408 6502 12296 2095 667 607 C ATOM 2845 CG GLU B 69 9.476 -31.938 105.821 1.00 90.79 C ANISOU 2845 CG GLU B 69 15085 6582 12828 1862 690 220 C ATOM 2846 CD GLU B 69 9.550 -30.468 105.438 1.00 97.57 C ANISOU 2846 CD GLU B 69 16595 6651 13827 1838 672 248 C ATOM 2847 OE1 GLU B 69 10.247 -30.147 104.451 1.00 99.53 O ANISOU 2847 OE1 GLU B 69 17121 6593 14104 1375 731 468 O ATOM 2848 OE2 GLU B 69 8.917 -29.632 106.123 1.00101.25 O ANISOU 2848 OE2 GLU B 69 17331 6787 14351 2271 606 41 O ATOM 2849 N PHE B 70 8.109 -34.583 107.611 1.00 81.86 N ANISOU 2849 N PHE B 70 12920 6891 11292 2399 728 45 N ATOM 2850 CA PHE B 70 7.335 -34.851 108.841 1.00 82.08 C ANISOU 2850 CA PHE B 70 12777 7255 11155 2722 773 -185 C ATOM 2851 C PHE B 70 8.077 -34.522 110.146 1.00 83.45 C ANISOU 2851 C PHE B 70 13048 7384 11277 2661 758 -591 C ATOM 2852 O PHE B 70 9.202 -34.008 110.121 1.00 84.46 O ANISOU 2852 O PHE B 70 13354 7211 11527 2361 704 -745 O ATOM 2853 CB PHE B 70 6.825 -36.308 108.860 1.00 78.60 C ANISOU 2853 CB PHE B 70 11987 7382 10495 2679 845 -11 C ATOM 2854 CG PHE B 70 7.859 -37.337 109.271 1.00 75.46 C ANISOU 2854 CG PHE B 70 11526 7186 9961 2361 822 -45 C ATOM 2855 CD1 PHE B 70 9.154 -37.305 108.772 1.00 74.20 C ANISOU 2855 CD1 PHE B 70 11436 6842 9913 2043 733 -57 C ATOM 2856 CD2 PHE B 70 7.509 -38.370 110.130 1.00 74.59 C ANISOU 2856 CD2 PHE B 70 11296 7473 9571 2390 887 -71 C ATOM 2857 CE1 PHE B 70 10.089 -38.265 109.148 1.00 72.76 C ANISOU 2857 CE1 PHE B 70 11166 6897 9583 1865 661 -143 C ATOM 2858 CE2 PHE B 70 8.438 -39.342 110.506 1.00 73.00 C ANISOU 2858 CE2 PHE B 70 11121 7411 9205 2199 813 -89 C ATOM 2859 CZ PHE B 70 9.731 -39.287 110.014 1.00 71.82 C ANISOU 2859 CZ PHE B 70 11000 7103 9185 1988 675 -145 C ATOM 2860 N THR B 71 7.416 -34.791 111.274 1.00 83.91 N ANISOU 2860 N THR B 71 12972 7784 11126 2922 817 -793 N ATOM 2861 CA THR B 71 8.044 -34.783 112.597 1.00 84.81 C ANISOU 2861 CA THR B 71 13122 8020 11082 2889 797 -1160 C ATOM 2862 C THR B 71 7.559 -35.999 113.389 1.00 82.91 C ANISOU 2862 C THR B 71 12675 8347 10479 2942 887 -1111 C ATOM 2863 O THR B 71 6.376 -36.092 113.718 1.00 84.15 O ANISOU 2863 O THR B 71 12699 8781 10493 3186 1019 -1113 O ATOM 2864 CB THR B 71 7.750 -33.494 113.416 1.00 89.59 C ANISOU 2864 CB THR B 71 13925 8361 11755 3183 788 -1564 C ATOM 2865 OG1 THR B 71 6.337 -33.263 113.476 1.00 92.02 O ANISOU 2865 OG1 THR B 71 14129 8826 12009 3622 870 -1557 O ATOM 2866 CG2 THR B 71 8.436 -32.279 112.813 1.00 92.29 C ANISOU 2866 CG2 THR B 71 14613 8035 12418 3029 702 -1652 C ATOM 2867 N PRO B 72 8.472 -36.942 113.682 1.00 80.51 N ANISOU 2867 N PRO B 72 12363 8227 10000 2712 816 -1081 N ATOM 2868 CA PRO B 72 8.150 -38.120 114.488 1.00 79.63 C ANISOU 2868 CA PRO B 72 12214 8549 9493 2729 884 -1004 C ATOM 2869 C PRO B 72 7.908 -37.782 115.960 1.00 82.83 C ANISOU 2869 C PRO B 72 12693 9166 9613 2934 935 -1345 C ATOM 2870 O PRO B 72 8.530 -36.866 116.493 1.00 85.09 O ANISOU 2870 O PRO B 72 13070 9277 9985 3008 831 -1704 O ATOM 2871 CB PRO B 72 9.413 -38.975 114.363 1.00 77.62 C ANISOU 2871 CB PRO B 72 12019 8315 9159 2526 707 -946 C ATOM 2872 CG PRO B 72 10.505 -38.001 114.061 1.00 78.46 C ANISOU 2872 CG PRO B 72 12135 8126 9550 2414 564 -1207 C ATOM 2873 CD PRO B 72 9.867 -36.965 113.203 1.00 79.23 C ANISOU 2873 CD PRO B 72 12241 7882 9980 2428 660 -1123 C ATOM 2874 N THR B 73 7.004 -38.515 116.605 1.00 83.47 N ANISOU 2874 N THR B 73 12742 9640 9334 2980 1113 -1253 N ATOM 2875 CA THR B 73 6.817 -38.413 118.053 1.00 86.68 C ANISOU 2875 CA THR B 73 13238 10341 9355 3130 1183 -1542 C ATOM 2876 C THR B 73 6.623 -39.786 118.682 1.00 86.70 C ANISOU 2876 C THR B 73 13393 10696 8853 2976 1287 -1305 C ATOM 2877 O THR B 73 6.806 -40.817 118.029 1.00 83.92 O ANISOU 2877 O THR B 73 13117 10290 8480 2768 1258 -951 O ATOM 2878 CB THR B 73 5.609 -37.529 118.440 1.00 90.13 C ANISOU 2878 CB THR B 73 13501 10949 9795 3392 1377 -1797 C ATOM 2879 OG1 THR B 73 4.483 -37.865 117.621 1.00 89.24 O ANISOU 2879 OG1 THR B 73 13147 11002 9758 3359 1554 -1546 O ATOM 2880 CG2 THR B 73 5.938 -36.048 118.299 1.00 92.14 C ANISOU 2880 CG2 THR B 73 13793 10784 10432 3621 1236 -2145 C ATOM 2881 N GLU B 74 6.252 -39.785 119.959 1.00 90.22 N ANISOU 2881 N GLU B 74 13935 11479 8866 3075 1412 -1506 N ATOM 2882 CA GLU B 74 5.958 -41.014 120.678 1.00 91.65 C ANISOU 2882 CA GLU B 74 14367 11974 8482 2898 1556 -1268 C ATOM 2883 C GLU B 74 4.598 -41.584 120.256 1.00 91.91 C ANISOU 2883 C GLU B 74 14220 12274 8427 2653 1902 -1022 C ATOM 2884 O GLU B 74 4.465 -42.795 120.072 1.00 91.41 O ANISOU 2884 O GLU B 74 14372 12236 8123 2352 1990 -660 O ATOM 2885 CB GLU B 74 6.025 -40.794 122.199 1.00 96.15 C ANISOU 2885 CB GLU B 74 15123 12857 8551 3055 1592 -1569 C ATOM 2886 CG GLU B 74 7.342 -40.168 122.706 1.00 97.10 C ANISOU 2886 CG GLU B 74 15359 12806 8728 3295 1242 -1914 C ATOM 2887 CD GLU B 74 7.618 -40.411 124.198 1.00102.02 C ANISOU 2887 CD GLU B 74 16283 13770 8710 3428 1207 -2100 C ATOM 2888 OE1 GLU B 74 8.046 -39.459 124.891 1.00104.23 O ANISOU 2888 OE1 GLU B 74 16496 14111 8995 3655 1080 -2576 O ATOM 2889 OE2 GLU B 74 7.420 -41.551 124.676 1.00103.85 O ANISOU 2889 OE2 GLU B 74 16865 14186 8409 3296 1298 -1773 O ATOM 2890 N THR B 75 3.608 -40.708 120.069 1.00 93.15 N ANISOU 2890 N THR B 75 13986 12625 8782 2795 2079 -1254 N ATOM 2891 CA THR B 75 2.227 -41.134 119.796 1.00 94.66 C ANISOU 2891 CA THR B 75 13882 13239 8845 2590 2422 -1158 C ATOM 2892 C THR B 75 1.822 -41.249 118.318 1.00 91.51 C ANISOU 2892 C THR B 75 13200 12695 8874 2505 2397 -938 C ATOM 2893 O THR B 75 1.059 -42.146 117.962 1.00 91.95 O ANISOU 2893 O THR B 75 13143 13023 8772 2161 2622 -724 O ATOM 2894 CB THR B 75 1.202 -40.225 120.499 1.00 99.29 C ANISOU 2894 CB THR B 75 14122 14300 9304 2847 2644 -1604 C ATOM 2895 OG1 THR B 75 1.529 -38.856 120.243 1.00 99.26 O ANISOU 2895 OG1 THR B 75 14003 13966 9745 3310 2404 -1926 O ATOM 2896 CG2 THR B 75 1.194 -40.469 122.000 1.00103.54 C ANISOU 2896 CG2 THR B 75 14893 15214 9232 2780 2815 -1770 C ATOM 2897 N ASP B 76 2.317 -40.346 117.470 1.00 88.95 N ANISOU 2897 N ASP B 76 12786 11956 9056 2780 2139 -1000 N ATOM 2898 CA ASP B 76 1.852 -40.245 116.078 1.00 86.78 C ANISOU 2898 CA ASP B 76 12235 11581 9156 2789 2101 -833 C ATOM 2899 C ASP B 76 2.204 -41.455 115.220 1.00 83.33 C ANISOU 2899 C ASP B 76 11916 11006 8740 2403 2066 -416 C ATOM 2900 O ASP B 76 3.329 -41.951 115.272 1.00 81.03 O ANISOU 2900 O ASP B 76 11960 10399 8430 2287 1888 -261 O ATOM 2901 CB ASP B 76 2.372 -38.962 115.422 1.00 85.77 C ANISOU 2901 CB ASP B 76 12116 10972 9499 3144 1839 -964 C ATOM 2902 CG ASP B 76 1.697 -37.710 115.962 1.00 89.69 C ANISOU 2902 CG ASP B 76 12460 11575 10043 3599 1871 -1389 C ATOM 2903 OD1 ASP B 76 0.499 -37.766 116.308 1.00 92.68 O ANISOU 2903 OD1 ASP B 76 12510 12500 10205 3706 2093 -1566 O ATOM 2904 OD2 ASP B 76 2.365 -36.661 116.034 1.00 90.07 O ANISOU 2904 OD2 ASP B 76 12713 11171 10338 3841 1675 -1584 O ATOM 2905 N THR B 77 1.234 -41.915 114.429 1.00 83.63 N ANISOU 2905 N THR B 77 11650 11316 8810 2238 2218 -288 N ATOM 2906 CA THR B 77 1.394 -43.121 113.610 1.00 81.27 C ANISOU 2906 CA THR B 77 11445 10928 8507 1846 2217 63 C ATOM 2907 C THR B 77 1.529 -42.813 112.127 1.00 78.40 C ANISOU 2907 C THR B 77 10893 10330 8567 1948 2026 198 C ATOM 2908 O THR B 77 0.594 -42.317 111.492 1.00 79.73 O ANISOU 2908 O THR B 77 10675 10745 8873 2112 2073 108 O ATOM 2909 CB THR B 77 0.223 -44.118 113.777 1.00 84.18 C ANISOU 2909 CB THR B 77 11646 11805 8534 1426 2562 117 C ATOM 2910 OG1 THR B 77 -0.985 -43.537 113.270 1.00 86.43 O ANISOU 2910 OG1 THR B 77 11360 12541 8938 1578 2685 -98 O ATOM 2911 CG2 THR B 77 0.036 -44.520 115.240 1.00 88.31 C ANISOU 2911 CG2 THR B 77 12420 12587 8547 1235 2806 32 C ATOM 2912 N TYR B 78 2.697 -43.136 111.584 1.00 75.07 N ANISOU 2912 N TYR B 78 10738 9481 8305 1868 1803 395 N ATOM 2913 CA TYR B 78 2.972 -42.966 110.164 1.00 72.30 C ANISOU 2913 CA TYR B 78 10267 8913 8292 1894 1636 554 C ATOM 2914 C TYR B 78 2.930 -44.311 109.440 1.00 70.60 C ANISOU 2914 C TYR B 78 10077 8749 7999 1524 1670 804 C ATOM 2915 O TYR B 78 3.481 -45.306 109.923 1.00 70.03 O ANISOU 2915 O TYR B 78 10326 8569 7712 1305 1666 904 O ATOM 2916 CB TYR B 78 4.313 -42.260 109.965 1.00 70.26 C ANISOU 2916 CB TYR B 78 10222 8198 8275 2037 1386 527 C ATOM 2917 CG TYR B 78 4.281 -40.807 110.375 1.00 72.30 C ANISOU 2917 CG TYR B 78 10474 8310 8685 2375 1340 278 C ATOM 2918 CD1 TYR B 78 4.429 -40.431 111.713 1.00 74.48 C ANISOU 2918 CD1 TYR B 78 10881 8631 8787 2501 1379 16 C ATOM 2919 CD2 TYR B 78 4.096 -39.809 109.428 1.00 72.59 C ANISOU 2919 CD2 TYR B 78 10434 8135 9012 2581 1246 300 C ATOM 2920 CE1 TYR B 78 4.398 -39.095 112.092 1.00 77.10 C ANISOU 2920 CE1 TYR B 78 11242 8786 9266 2815 1329 -257 C ATOM 2921 CE2 TYR B 78 4.063 -38.475 109.791 1.00 75.91 C ANISOU 2921 CE2 TYR B 78 10955 8317 9570 2902 1188 71 C ATOM 2922 CZ TYR B 78 4.213 -38.118 111.124 1.00 78.31 C ANISOU 2922 CZ TYR B 78 11365 8655 9734 3015 1231 -229 C ATOM 2923 OH TYR B 78 4.177 -36.780 111.474 1.00 82.02 O ANISOU 2923 OH TYR B 78 11967 8843 10352 3339 1164 -499 O ATOM 2924 N ALA B 79 2.255 -44.331 108.292 1.00 70.25 N ANISOU 2924 N ALA B 79 9724 8861 8107 1492 1681 884 N ATOM 2925 CA ALA B 79 2.036 -45.556 107.528 1.00 69.22 C ANISOU 2925 CA ALA B 79 9565 8823 7913 1130 1729 1062 C ATOM 2926 C ALA B 79 2.077 -45.302 106.033 1.00 67.48 C ANISOU 2926 C ALA B 79 9125 8558 7958 1209 1573 1169 C ATOM 2927 O ALA B 79 1.852 -44.177 105.575 1.00 68.04 O ANISOU 2927 O ALA B 79 9015 8627 8211 1540 1483 1117 O ATOM 2928 CB ALA B 79 0.707 -46.183 107.906 1.00 72.57 C ANISOU 2928 CB ALA B 79 9763 9735 8074 846 2026 983 C ATOM 2929 N CYS B 80 2.356 -46.362 105.280 1.00 66.06 N ANISOU 2929 N CYS B 80 9012 8321 7766 921 1534 1316 N ATOM 2930 CA CYS B 80 2.306 -46.312 103.828 1.00 64.97 C ANISOU 2930 CA CYS B 80 8655 8226 7806 938 1412 1413 C ATOM 2931 C CYS B 80 1.358 -47.360 103.240 1.00 66.20 C ANISOU 2931 C CYS B 80 8582 8730 7842 600 1541 1417 C ATOM 2932 O CYS B 80 1.579 -48.569 103.380 1.00 65.95 O ANISOU 2932 O CYS B 80 8790 8592 7676 246 1600 1469 O ATOM 2933 CB CYS B 80 3.700 -46.459 103.236 1.00 62.15 C ANISOU 2933 CB CYS B 80 8536 7495 7582 933 1207 1520 C ATOM 2934 SG CYS B 80 3.752 -45.906 101.534 1.00 62.17 S ANISOU 2934 SG CYS B 80 8304 7540 7777 1037 1061 1638 S ATOM 2935 N ARG B 81 0.299 -46.874 102.591 1.00 68.10 N ANISOU 2935 N ARG B 81 8381 9378 8115 732 1566 1335 N ATOM 2936 CA ARG B 81 -0.695 -47.721 101.941 1.00 70.10 C ANISOU 2936 CA ARG B 81 8302 10071 8261 416 1679 1262 C ATOM 2937 C ARG B 81 -0.404 -47.785 100.449 1.00 68.39 C ANISOU 2937 C ARG B 81 7974 9834 8178 475 1472 1372 C ATOM 2938 O ARG B 81 -0.273 -46.753 99.793 1.00 67.94 O ANISOU 2938 O ARG B 81 7823 9743 8249 877 1293 1437 O ATOM 2939 CB ARG B 81 -2.104 -47.168 102.173 1.00 74.30 C ANISOU 2939 CB ARG B 81 8321 11215 8696 565 1816 1016 C ATOM 2940 CG ARG B 81 -3.240 -48.099 101.731 1.00 77.85 C ANISOU 2940 CG ARG B 81 8349 12247 8983 134 1993 839 C ATOM 2941 CD ARG B 81 -4.554 -47.342 101.465 1.00 82.75 C ANISOU 2941 CD ARG B 81 8302 13587 9554 465 2000 546 C ATOM 2942 NE ARG B 81 -5.003 -46.542 102.608 1.00 86.27 N ANISOU 2942 NE ARG B 81 8634 14226 9919 750 2125 350 N ATOM 2943 CZ ARG B 81 -5.687 -47.012 103.654 1.00 90.41 C ANISOU 2943 CZ ARG B 81 9009 15141 10200 366 2465 129 C ATOM 2944 NH1 ARG B 81 -6.018 -48.297 103.733 1.00 92.42 N ANISOU 2944 NH1 ARG B 81 9272 15576 10266 -376 2729 102 N ATOM 2945 NH2 ARG B 81 -6.041 -46.192 104.636 1.00 92.78 N ANISOU 2945 NH2 ARG B 81 9190 15640 10422 696 2555 -76 N ATOM 2946 N VAL B 82 -0.307 -49.001 99.921 1.00 68.05 N ANISOU 2946 N VAL B 82 7993 9788 8076 66 1500 1392 N ATOM 2947 CA VAL B 82 -0.007 -49.207 98.506 1.00 66.83 C ANISOU 2947 CA VAL B 82 7732 9656 8003 78 1319 1463 C ATOM 2948 C VAL B 82 -1.093 -50.037 97.833 1.00 69.52 C ANISOU 2948 C VAL B 82 7697 10491 8227 -257 1410 1297 C ATOM 2949 O VAL B 82 -1.307 -51.200 98.189 1.00 70.84 O ANISOU 2949 O VAL B 82 8003 10633 8279 -748 1579 1216 O ATOM 2950 CB VAL B 82 1.373 -49.876 98.312 1.00 63.87 C ANISOU 2950 CB VAL B 82 7790 8791 7688 -42 1202 1583 C ATOM 2951 CG1 VAL B 82 1.532 -50.392 96.898 1.00 63.82 C ANISOU 2951 CG1 VAL B 82 7645 8902 7701 -140 1073 1587 C ATOM 2952 CG2 VAL B 82 2.494 -48.901 98.637 1.00 61.76 C ANISOU 2952 CG2 VAL B 82 7759 8158 7549 292 1074 1692 C ATOM 2953 N LYS B 83 -1.771 -49.426 96.863 1.00 71.05 N ANISOU 2953 N LYS B 83 7451 11120 8426 9 1288 1238 N ATOM 2954 CA LYS B 83 -2.841 -50.084 96.113 1.00 74.25 C ANISOU 2954 CA LYS B 83 7391 12111 8710 -257 1334 1016 C ATOM 2955 C LYS B 83 -2.323 -50.641 94.787 1.00 72.70 C ANISOU 2955 C LYS B 83 7231 11856 8534 -354 1157 1080 C ATOM 2956 O LYS B 83 -1.679 -49.931 94.014 1.00 70.78 O ANISOU 2956 O LYS B 83 7070 11468 8357 19 942 1265 O ATOM 2957 CB LYS B 83 -4.012 -49.122 95.880 1.00 77.89 C ANISOU 2957 CB LYS B 83 7284 13208 9104 164 1271 838 C ATOM 2958 CG LYS B 83 -5.193 -49.720 95.120 1.00 82.38 C ANISOU 2958 CG LYS B 83 7252 14529 9519 -75 1298 524 C ATOM 2959 CD LYS B 83 -5.848 -50.860 95.892 1.00 85.66 C ANISOU 2959 CD LYS B 83 7557 15179 9810 -805 1648 265 C ATOM 2960 CE LYS B 83 -7.048 -51.427 95.150 1.00 90.66 C ANISOU 2960 CE LYS B 83 7529 16631 10288 -1116 1696 -124 C ATOM 2961 NZ LYS B 83 -7.507 -52.705 95.762 1.00 93.44 N ANISOU 2961 NZ LYS B 83 7919 17071 10513 -2008 2066 -340 N ATOM 2962 N HIS B 84 -2.609 -51.916 94.538 1.00 74.04 N ANISOU 2962 N HIS B 84 7372 12134 8626 -892 1268 912 N ATOM 2963 CA HIS B 84 -2.112 -52.604 93.355 1.00 73.18 C ANISOU 2963 CA HIS B 84 7319 11966 8521 -1027 1118 908 C ATOM 2964 C HIS B 84 -3.117 -53.629 92.845 1.00 77.36 C ANISOU 2964 C HIS B 84 7503 12967 8923 -1531 1222 590 C ATOM 2965 O HIS B 84 -4.086 -53.962 93.530 1.00 80.79 O ANISOU 2965 O HIS B 84 7726 13706 9263 -1892 1458 381 O ATOM 2966 CB HIS B 84 -0.763 -53.273 93.651 1.00 69.77 C ANISOU 2966 CB HIS B 84 7499 10836 8174 -1153 1092 1053 C ATOM 2967 CG HIS B 84 0.056 -53.561 92.430 1.00 68.07 C ANISOU 2967 CG HIS B 84 7343 10538 7983 -1072 888 1078 C ATOM 2968 ND1 HIS B 84 0.725 -54.750 92.247 1.00 67.81 N ANISOU 2968 ND1 HIS B 84 7652 10162 7952 -1350 865 986 N ATOM 2969 CD2 HIS B 84 0.311 -52.815 91.328 1.00 67.67 C ANISOU 2969 CD2 HIS B 84 7078 10714 7920 -737 702 1170 C ATOM 2970 CE1 HIS B 84 1.364 -54.723 91.090 1.00 67.03 C ANISOU 2970 CE1 HIS B 84 7475 10142 7851 -1187 684 982 C ATOM 2971 NE2 HIS B 84 1.127 -53.560 90.511 1.00 66.65 N ANISOU 2971 NE2 HIS B 84 7101 10445 7779 -850 598 1112 N ATOM 2972 N ALA B 85 -2.878 -54.114 91.630 1.00 77.68 N ANISOU 2972 N ALA B 85 7468 13106 8939 -1589 1061 521 N ATOM 2973 CA ALA B 85 -3.692 -55.158 91.023 1.00 81.81 C ANISOU 2973 CA ALA B 85 7702 14032 9349 -2104 1133 179 C ATOM 2974 C ALA B 85 -3.323 -56.553 91.544 1.00 82.63 C ANISOU 2974 C ALA B 85 8346 13582 9468 -2725 1309 102 C ATOM 2975 O ALA B 85 -4.090 -57.501 91.378 1.00 86.80 O ANISOU 2975 O ALA B 85 8742 14336 9901 -3313 1459 -200 O ATOM 2976 CB ALA B 85 -3.568 -55.099 89.504 1.00 81.99 C ANISOU 2976 CB ALA B 85 7455 14390 9309 -1887 873 116 C ATOM 2977 N SER B 86 -2.154 -56.672 92.171 1.00 79.46 N ANISOU 2977 N SER B 86 8575 12452 9165 -2586 1278 355 N ATOM 2978 CA SER B 86 -1.715 -57.930 92.770 1.00 80.89 C ANISOU 2978 CA SER B 86 9406 12001 9328 -3036 1391 329 C ATOM 2979 C SER B 86 -2.607 -58.349 93.930 1.00 84.91 C ANISOU 2979 C SER B 86 10037 12512 9713 -3576 1726 262 C ATOM 2980 O SER B 86 -2.797 -59.542 94.176 1.00 88.28 O ANISOU 2980 O SER B 86 10883 12614 10047 -4175 1884 142 O ATOM 2981 CB SER B 86 -0.282 -57.804 93.277 1.00 76.94 C ANISOU 2981 CB SER B 86 9486 10824 8925 -2636 1242 589 C ATOM 2982 OG SER B 86 0.594 -57.411 92.240 1.00 74.46 O ANISOU 2982 OG SER B 86 9045 10553 8693 -2209 981 626 O ATOM 2983 N MET B 87 -3.153 -57.357 94.630 1.00 85.19 N ANISOU 2983 N MET B 87 9737 12908 9725 -3375 1843 329 N ATOM 2984 CA MET B 87 -3.901 -57.579 95.868 1.00 89.13 C ANISOU 2984 CA MET B 87 10337 13459 10069 -3831 2187 285 C ATOM 2985 C MET B 87 -5.291 -56.928 95.879 1.00 92.98 C ANISOU 2985 C MET B 87 9996 14871 10460 -3914 2359 12 C ATOM 2986 O MET B 87 -5.439 -55.740 95.560 1.00 91.35 O ANISOU 2986 O MET B 87 9295 15083 10329 -3291 2184 30 O ATOM 2987 CB MET B 87 -3.079 -57.085 97.060 1.00 86.17 C ANISOU 2987 CB MET B 87 10469 12562 9711 -3485 2187 594 C ATOM 2988 CG MET B 87 -2.400 -55.738 96.823 1.00 81.38 C ANISOU 2988 CG MET B 87 9643 11997 9282 -2688 1920 770 C ATOM 2989 SD MET B 87 -0.906 -55.507 97.799 1.00 77.64 S ANISOU 2989 SD MET B 87 9887 10741 8872 -2292 1789 1080 S ATOM 2990 CE MET B 87 0.030 -56.967 97.356 1.00 77.38 C ANISOU 2990 CE MET B 87 10502 10070 8827 -2526 1648 1086 C ATOM 2991 N ALA B 88 -6.297 -57.716 96.259 1.00 98.85 N ANISOU 2991 N ALA B 88 10617 15925 11015 -4688 2701 -260 N ATOM 2992 CA ALA B 88 -7.676 -57.241 96.361 1.00103.78 C ANISOU 2992 CA ALA B 88 10393 17536 11504 -4850 2905 -622 C ATOM 2993 C ALA B 88 -7.818 -56.181 97.451 1.00103.21 C ANISOU 2993 C ALA B 88 10193 17629 11394 -4426 3001 -519 C ATOM 2994 O ALA B 88 -8.492 -55.170 97.258 1.00104.37 O ANISOU 2994 O ALA B 88 9620 18491 11543 -3942 2914 -711 O ATOM 2995 CB ALA B 88 -8.623 -58.403 96.616 1.00110.68 C ANISOU 2995 CB ALA B 88 11223 18673 12157 -5912 3310 -958 C ATOM 2996 N GLU B 89 -7.179 -56.414 98.591 1.00102.04 N ANISOU 2996 N GLU B 89 10765 16816 11188 -4561 3154 -235 N ATOM 2997 CA GLU B 89 -7.157 -55.429 99.660 1.00101.34 C ANISOU 2997 CA GLU B 89 10645 16798 11062 -4136 3224 -131 C ATOM 2998 C GLU B 89 -5.800 -54.726 99.651 1.00 94.77 C ANISOU 2998 C GLU B 89 10278 15274 10455 -3374 2871 252 C ATOM 2999 O GLU B 89 -4.769 -55.384 99.491 1.00 92.10 O ANISOU 2999 O GLU B 89 10590 14214 10189 -3426 2731 490 O ATOM 3000 CB GLU B 89 -7.423 -56.089 101.018 1.00105.31 C ANISOU 3000 CB GLU B 89 11602 17133 11279 -4812 3654 -104 C ATOM 3001 CG GLU B 89 -8.493 -57.191 101.008 1.00113.01 C ANISOU 3001 CG GLU B 89 12411 18526 12002 -5853 4060 -424 C ATOM 3002 CD GLU B 89 -9.925 -56.669 100.887 1.00118.90 C ANISOU 3002 CD GLU B 89 12065 20485 12625 -5984 4269 -939 C ATOM 3003 OE1 GLU B 89 -10.224 -55.911 99.937 1.00117.57 O ANISOU 3003 OE1 GLU B 89 11173 20870 12629 -5378 3968 -1139 O ATOM 3004 OE2 GLU B 89 -10.761 -57.044 101.741 1.00125.20 O ANISOU 3004 OE2 GLU B 89 12738 21714 13117 -6701 4735 -1164 O ATOM 3005 N PRO B 90 -5.795 -53.386 99.809 1.00 92.90 N ANISOU 3005 N PRO B 90 9708 15267 10321 -2665 2719 272 N ATOM 3006 CA PRO B 90 -4.552 -52.604 99.770 1.00 87.34 C ANISOU 3006 CA PRO B 90 9387 13971 9828 -2005 2410 585 C ATOM 3007 C PRO B 90 -3.604 -52.952 100.914 1.00 85.54 C ANISOU 3007 C PRO B 90 9909 13051 9541 -2104 2483 827 C ATOM 3008 O PRO B 90 -4.055 -53.234 102.024 1.00 88.58 O ANISOU 3008 O PRO B 90 10437 13515 9704 -2450 2777 773 O ATOM 3009 CB PRO B 90 -5.039 -51.158 99.922 1.00 87.89 C ANISOU 3009 CB PRO B 90 8969 14471 9953 -1363 2323 481 C ATOM 3010 CG PRO B 90 -6.501 -51.192 99.615 1.00 93.17 C ANISOU 3010 CG PRO B 90 8879 16046 10476 -1544 2472 89 C ATOM 3011 CD PRO B 90 -6.973 -52.532 100.038 1.00 96.61 C ANISOU 3011 CD PRO B 90 9428 16579 10702 -2449 2831 -47 C ATOM 3012 N LYS B 91 -2.302 -52.934 100.639 1.00 81.28 N ANISOU 3012 N LYS B 91 9824 11897 9162 -1798 2215 1065 N ATOM 3013 CA LYS B 91 -1.297 -53.219 101.662 1.00 79.86 C ANISOU 3013 CA LYS B 91 10328 11099 8916 -1769 2202 1261 C ATOM 3014 C LYS B 91 -0.919 -51.956 102.423 1.00 77.98 C ANISOU 3014 C LYS B 91 10057 10826 8746 -1244 2132 1309 C ATOM 3015 O LYS B 91 -0.378 -51.007 101.853 1.00 74.87 O ANISOU 3015 O LYS B 91 9501 10375 8572 -762 1896 1357 O ATOM 3016 CB LYS B 91 -0.054 -53.875 101.050 1.00 77.05 C ANISOU 3016 CB LYS B 91 10428 10177 8671 -1683 1938 1402 C ATOM 3017 CG LYS B 91 0.907 -54.494 102.074 1.00 77.26 C ANISOU 3017 CG LYS B 91 11203 9594 8558 -1686 1897 1552 C ATOM 3018 CD LYS B 91 1.976 -55.373 101.405 1.00 76.33 C ANISOU 3018 CD LYS B 91 11496 8998 8508 -1620 1638 1597 C ATOM 3019 CE LYS B 91 1.456 -56.792 101.127 1.00 80.14 C ANISOU 3019 CE LYS B 91 12300 9313 8837 -2194 1767 1547 C ATOM 3020 NZ LYS B 91 2.474 -57.696 100.508 1.00 78.97 N ANISOU 3020 NZ LYS B 91 12592 8674 8740 -2069 1494 1541 N ATOM 3021 N THR B 92 -1.222 -51.967 103.718 1.00 80.45 N ANISOU 3021 N THR B 92 10560 11167 8841 -1388 2357 1288 N ATOM 3022 CA THR B 92 -0.903 -50.870 104.626 1.00 79.59 C ANISOU 3022 CA THR B 92 10473 11018 8751 -946 2321 1284 C ATOM 3023 C THR B 92 0.285 -51.277 105.495 1.00 78.31 C ANISOU 3023 C THR B 92 10999 10270 8484 -894 2221 1456 C ATOM 3024 O THR B 92 0.199 -52.245 106.265 1.00 80.99 O ANISOU 3024 O THR B 92 11794 10447 8531 -1283 2392 1527 O ATOM 3025 CB THR B 92 -2.111 -50.517 105.535 1.00 83.84 C ANISOU 3025 CB THR B 92 10679 12110 9065 -1087 2643 1073 C ATOM 3026 OG1 THR B 92 -3.289 -50.342 104.737 1.00 86.18 O ANISOU 3026 OG1 THR B 92 10299 13045 9402 -1162 2731 848 O ATOM 3027 CG2 THR B 92 -1.849 -49.246 106.320 1.00 82.97 C ANISOU 3027 CG2 THR B 92 10522 11992 9012 -551 2571 1006 C ATOM 3028 N VAL B 93 1.393 -50.546 105.358 1.00 74.89 N ANISOU 3028 N VAL B 93 10660 9533 8261 -425 1939 1509 N ATOM 3029 CA VAL B 93 2.590 -50.792 106.170 1.00 74.01 C ANISOU 3029 CA VAL B 93 11102 8966 8053 -271 1786 1595 C ATOM 3030 C VAL B 93 2.939 -49.579 107.034 1.00 73.68 C ANISOU 3030 C VAL B 93 11008 8940 8048 118 1738 1502 C ATOM 3031 O VAL B 93 3.294 -48.516 106.519 1.00 71.70 O ANISOU 3031 O VAL B 93 10489 8686 8068 442 1588 1442 O ATOM 3032 CB VAL B 93 3.812 -51.226 105.315 1.00 71.01 C ANISOU 3032 CB VAL B 93 10915 8222 7842 -124 1481 1661 C ATOM 3033 CG1 VAL B 93 5.049 -51.398 106.186 1.00 70.46 C ANISOU 3033 CG1 VAL B 93 11327 7791 7654 126 1281 1671 C ATOM 3034 CG2 VAL B 93 3.517 -52.522 104.587 1.00 72.31 C ANISOU 3034 CG2 VAL B 93 11229 8306 7940 -498 1516 1718 C ATOM 3035 N TYR B 94 2.830 -49.762 108.349 1.00 76.30 N ANISOU 3035 N TYR B 94 11648 9267 8075 51 1877 1488 N ATOM 3036 CA TYR B 94 3.136 -48.725 109.329 1.00 76.65 C ANISOU 3036 CA TYR B 94 11692 9340 8093 387 1846 1355 C ATOM 3037 C TYR B 94 4.641 -48.604 109.562 1.00 74.91 C ANISOU 3037 C TYR B 94 11792 8735 7934 689 1530 1352 C ATOM 3038 O TYR B 94 5.374 -49.594 109.463 1.00 74.83 O ANISOU 3038 O TYR B 94 12160 8452 7819 634 1376 1461 O ATOM 3039 CB TYR B 94 2.408 -49.013 110.646 1.00 80.48 C ANISOU 3039 CB TYR B 94 12369 10048 8163 174 2133 1319 C ATOM 3040 CG TYR B 94 0.916 -48.764 110.593 1.00 82.82 C ANISOU 3040 CG TYR B 94 12176 10893 8398 -49 2462 1180 C ATOM 3041 CD1 TYR B 94 0.036 -49.754 110.158 1.00 84.84 C ANISOU 3041 CD1 TYR B 94 12361 11360 8513 -570 2697 1241 C ATOM 3042 CD2 TYR B 94 0.385 -47.539 110.986 1.00 83.91 C ANISOU 3042 CD2 TYR B 94 11909 11367 8607 271 2531 932 C ATOM 3043 CE1 TYR B 94 -1.339 -49.526 110.107 1.00 88.16 C ANISOU 3043 CE1 TYR B 94 12232 12408 8856 -783 2999 1032 C ATOM 3044 CE2 TYR B 94 -0.985 -47.300 110.942 1.00 87.43 C ANISOU 3044 CE2 TYR B 94 11835 12408 8975 148 2804 729 C ATOM 3045 CZ TYR B 94 -1.841 -48.296 110.502 1.00 89.59 C ANISOU 3045 CZ TYR B 94 11963 12979 9100 -386 3040 767 C ATOM 3046 OH TYR B 94 -3.196 -48.054 110.462 1.00 93.63 O ANISOU 3046 OH TYR B 94 11865 14196 9514 -513 3309 487 O ATOM 3047 N TRP B 95 5.092 -47.391 109.870 1.00 74.42 N ANISOU 3047 N TRP B 95 11575 8668 8035 1015 1426 1183 N ATOM 3048 CA TRP B 95 6.509 -47.125 110.121 1.00 73.60 C ANISOU 3048 CA TRP B 95 11662 8308 7993 1268 1142 1086 C ATOM 3049 C TRP B 95 6.961 -47.625 111.493 1.00 76.14 C ANISOU 3049 C TRP B 95 12431 8575 7924 1349 1093 1049 C ATOM 3050 O TRP B 95 6.746 -46.968 112.518 1.00 78.05 O ANISOU 3050 O TRP B 95 12686 8952 8018 1468 1178 901 O ATOM 3051 CB TRP B 95 6.818 -45.629 109.945 1.00 72.85 C ANISOU 3051 CB TRP B 95 11283 8194 8203 1502 1070 895 C ATOM 3052 CG TRP B 95 8.197 -45.184 110.397 1.00 73.02 C ANISOU 3052 CG TRP B 95 11432 8048 8263 1693 829 696 C ATOM 3053 CD1 TRP B 95 9.398 -45.722 110.033 1.00 72.47 C ANISOU 3053 CD1 TRP B 95 11456 7864 8216 1720 593 662 C ATOM 3054 CD2 TRP B 95 8.499 -44.087 111.268 1.00 75.37 C ANISOU 3054 CD2 TRP B 95 11722 8337 8579 1880 800 434 C ATOM 3055 NE1 TRP B 95 10.430 -45.040 110.634 1.00 73.39 N ANISOU 3055 NE1 TRP B 95 11578 7954 8351 1886 423 382 N ATOM 3056 CE2 TRP B 95 9.907 -44.031 111.396 1.00 75.29 C ANISOU 3056 CE2 TRP B 95 11781 8229 8597 1963 549 245 C ATOM 3057 CE3 TRP B 95 7.716 -43.143 111.955 1.00 78.14 C ANISOU 3057 CE3 TRP B 95 11991 8781 8917 1999 955 287 C ATOM 3058 CZ2 TRP B 95 10.553 -43.071 112.186 1.00 77.77 C ANISOU 3058 CZ2 TRP B 95 12092 8528 8930 2099 458 -79 C ATOM 3059 CZ3 TRP B 95 8.359 -42.184 112.746 1.00 79.93 C ANISOU 3059 CZ3 TRP B 95 12267 8931 9170 2171 857 -20 C ATOM 3060 CH2 TRP B 95 9.765 -42.158 112.852 1.00 79.77 C ANISOU 3060 CH2 TRP B 95 12323 8803 9182 2189 615 -197 C ATOM 3061 N ASP B 96 7.575 -48.805 111.497 1.00 76.74 N ANISOU 3061 N ASP B 96 12905 8448 7804 1321 938 1174 N ATOM 3062 CA ASP B 96 8.248 -49.315 112.681 1.00 79.57 C ANISOU 3062 CA ASP B 96 13765 8701 7767 1508 784 1150 C ATOM 3063 C ASP B 96 9.622 -48.648 112.729 1.00 78.50 C ANISOU 3063 C ASP B 96 13493 8539 7796 1877 449 876 C ATOM 3064 O ASP B 96 10.393 -48.707 111.769 1.00 76.40 O ANISOU 3064 O ASP B 96 13037 8198 7794 1944 255 809 O ATOM 3065 CB ASP B 96 8.354 -50.844 112.629 1.00 81.47 C ANISOU 3065 CB ASP B 96 14564 8673 7716 1395 710 1386 C ATOM 3066 CG ASP B 96 8.734 -51.466 113.971 1.00 85.75 C ANISOU 3066 CG ASP B 96 15769 9089 7724 1569 599 1446 C ATOM 3067 OD1 ASP B 96 8.748 -50.759 115.001 1.00 87.14 O ANISOU 3067 OD1 ASP B 96 15931 9462 7716 1715 635 1309 O ATOM 3068 OD2 ASP B 96 9.015 -52.684 113.993 1.00 88.39 O ANISOU 3068 OD2 ASP B 96 16690 9103 7791 1581 459 1630 O ATOM 3069 N ARG B 97 9.905 -47.990 113.844 1.00 80.49 N ANISOU 3069 N ARG B 97 13801 8909 7874 2079 404 675 N ATOM 3070 CA ARG B 97 11.086 -47.153 113.963 1.00 80.26 C ANISOU 3070 CA ARG B 97 13551 8931 8012 2344 141 332 C ATOM 3071 C ARG B 97 12.350 -47.965 114.229 1.00 81.99 C ANISOU 3071 C ARG B 97 14043 9109 8002 2651 -242 218 C ATOM 3072 O ARG B 97 13.369 -47.774 113.562 1.00 80.91 O ANISOU 3072 O ARG B 97 13625 9013 8103 2759 -467 -5 O ATOM 3073 CB ARG B 97 10.871 -46.115 115.061 1.00 82.15 C ANISOU 3073 CB ARG B 97 13731 9333 8149 2441 231 100 C ATOM 3074 CG ARG B 97 12.010 -45.141 115.227 1.00 82.24 C ANISOU 3074 CG ARG B 97 13499 9403 8344 2624 0 -309 C ATOM 3075 CD ARG B 97 11.465 -43.805 115.636 1.00 83.07 C ANISOU 3075 CD ARG B 97 13397 9557 8610 2588 187 -511 C ATOM 3076 NE ARG B 97 11.079 -43.758 117.042 1.00 85.72 N ANISOU 3076 NE ARG B 97 13970 10070 8528 2733 252 -614 N ATOM 3077 CZ ARG B 97 10.030 -43.089 117.507 1.00 86.57 C ANISOU 3077 CZ ARG B 97 14004 10276 8613 2696 521 -656 C ATOM 3078 NH1 ARG B 97 9.227 -42.427 116.682 1.00 84.59 N ANISOU 3078 NH1 ARG B 97 13470 9941 8731 2575 718 -595 N ATOM 3079 NH2 ARG B 97 9.777 -43.094 118.805 1.00 90.09 N ANISOU 3079 NH2 ARG B 97 14663 10941 8627 2822 578 -780 N ATOM 3080 N ASP B 98 12.275 -48.865 115.206 1.00 85.46 N ANISOU 3080 N ASP B 98 15039 9489 7942 2803 -316 356 N ATOM 3081 CA ASP B 98 13.408 -49.701 115.586 1.00 88.33 C ANISOU 3081 CA ASP B 98 15760 9801 7999 3220 -733 251 C ATOM 3082 C ASP B 98 13.737 -50.705 114.483 1.00 87.33 C ANISOU 3082 C ASP B 98 15717 9459 8005 3239 -883 379 C ATOM 3083 O ASP B 98 14.727 -51.433 114.566 1.00 89.50 O ANISOU 3083 O ASP B 98 16233 9690 8083 3652 -1271 248 O ATOM 3084 CB ASP B 98 13.114 -50.427 116.901 1.00 93.00 C ANISOU 3084 CB ASP B 98 17061 10316 7960 3371 -758 443 C ATOM 3085 CG ASP B 98 12.824 -49.470 118.052 1.00 95.03 C ANISOU 3085 CG ASP B 98 17236 10844 8027 3387 -622 268 C ATOM 3086 OD1 ASP B 98 13.717 -48.672 118.417 1.00 96.12 O ANISOU 3086 OD1 ASP B 98 17066 11219 8238 3662 -858 -145 O ATOM 3087 OD2 ASP B 98 11.703 -49.529 118.602 1.00 96.62 O ANISOU 3087 OD2 ASP B 98 17666 11058 7989 3102 -269 504 O ATOM 3088 N MET B 99 12.898 -50.722 113.451 1.00 84.53 N ANISOU 3088 N MET B 99 15143 9005 7968 2835 -595 595 N ATOM 3089 CA MET B 99 13.068 -51.604 112.307 1.00 83.68 C ANISOU 3089 CA MET B 99 15064 8714 8015 2789 -686 698 C ATOM 3090 C MET B 99 14.110 -51.041 111.347 1.00 81.43 C ANISOU 3090 C MET B 99 14194 8637 8110 2913 -880 366 C ATOM 3091 O MET B 99 14.098 -49.849 111.028 1.00 79.29 O ANISOU 3091 O MET B 99 13411 8560 8154 2733 -735 221 O ATOM 3092 CB MET B 99 11.732 -51.787 111.586 1.00 81.90 C ANISOU 3092 CB MET B 99 14777 8387 7953 2287 -299 1010 C ATOM 3093 CG MET B 99 11.565 -53.116 110.862 1.00 83.62 C ANISOU 3093 CG MET B 99 15357 8305 8108 2182 -345 1209 C ATOM 3094 SD MET B 99 11.528 -54.544 111.978 1.00 91.29 S ANISOU 3094 SD MET B 99 17374 8856 8457 2324 -473 1452 S ATOM 3095 CE MET B 99 13.247 -55.060 111.935 1.00 93.24 C ANISOU 3095 CE MET B 99 17791 9025 8612 3063 -1086 1145 C TER 3096 MET B 99 ATOM 3097 N THR C 1 -5.536 -34.175 53.138 1.00 86.86 N ANISOU 3097 N THR C 1 8034 15716 9252 2046 1634 1813 N ATOM 3098 CA THR C 1 -5.103 -32.874 53.735 1.00 89.06 C ANISOU 3098 CA THR C 1 8879 15542 9418 2708 1554 1404 C ATOM 3099 C THR C 1 -3.695 -32.966 54.339 1.00 86.09 C ANISOU 3099 C THR C 1 9011 14434 9264 2356 1370 1226 C ATOM 3100 O THR C 1 -3.085 -31.952 54.687 1.00 87.47 O ANISOU 3100 O THR C 1 9774 14028 9434 2680 1172 935 O ATOM 3101 CB THR C 1 -6.138 -32.333 54.771 1.00 95.82 C ANISOU 3101 CB THR C 1 9554 17205 9650 3531 1739 1288 C ATOM 3102 OG1 THR C 1 -5.835 -30.968 55.091 1.00 98.92 O ANISOU 3102 OG1 THR C 1 10655 17022 9908 4288 1540 856 O ATOM 3103 CG2 THR C 1 -6.168 -33.183 56.058 1.00 97.11 C ANISOU 3103 CG2 THR C 1 9457 17950 9489 3293 1893 1409 C ATOM 3104 N GLN C 2 -3.192 -34.193 54.453 1.00 82.63 N ANISOU 3104 N GLN C 2 8384 14019 8994 1689 1368 1418 N ATOM 3105 CA GLN C 2 -1.816 -34.451 54.873 1.00 79.68 C ANISOU 3105 CA GLN C 2 8381 13038 8857 1319 1183 1296 C ATOM 3106 C GLN C 2 -0.841 -34.129 53.745 1.00 76.37 C ANISOU 3106 C GLN C 2 8176 11983 8857 1068 1005 1269 C ATOM 3107 O GLN C 2 0.307 -33.759 53.994 1.00 75.64 O ANISOU 3107 O GLN C 2 8430 11391 8919 924 814 1141 O ATOM 3108 CB GLN C 2 -1.650 -35.921 55.270 1.00 78.08 C ANISOU 3108 CB GLN C 2 7944 13071 8653 769 1176 1511 C ATOM 3109 CG GLN C 2 -2.316 -36.319 56.586 1.00 81.79 C ANISOU 3109 CG GLN C 2 8239 14162 8674 839 1302 1599 C ATOM 3110 CD GLN C 2 -1.436 -36.063 57.797 1.00 82.29 C ANISOU 3110 CD GLN C 2 8715 13902 8650 931 1203 1354 C ATOM 3111 OE1 GLN C 2 -1.869 -35.444 58.771 1.00 86.18 O ANISOU 3111 OE1 GLN C 2 9294 14708 8742 1408 1311 1208 O ATOM 3112 NE2 GLN C 2 -0.196 -36.540 57.743 1.00 78.76 N ANISOU 3112 NE2 GLN C 2 8520 12877 8528 531 981 1299 N ATOM 3113 N VAL C 3 -1.314 -34.282 52.507 1.00 74.95 N ANISOU 3113 N VAL C 3 7748 11911 8817 986 1058 1431 N ATOM 3114 CA VAL C 3 -0.486 -34.150 51.302 1.00 72.00 C ANISOU 3114 CA VAL C 3 7462 11126 8768 720 938 1474 C ATOM 3115 C VAL C 3 -1.215 -33.358 50.209 1.00 72.91 C ANISOU 3115 C VAL C 3 7549 11245 8910 963 959 1533 C ATOM 3116 O VAL C 3 -2.136 -33.873 49.573 1.00 72.76 O ANISOU 3116 O VAL C 3 7189 11606 8850 961 1072 1696 O ATOM 3117 CB VAL C 3 -0.058 -35.542 50.763 1.00 69.01 C ANISOU 3117 CB VAL C 3 6857 10833 8529 289 917 1618 C ATOM 3118 CG1 VAL C 3 0.901 -36.213 51.717 1.00 68.01 C ANISOU 3118 CG1 VAL C 3 6851 10583 8408 85 813 1536 C ATOM 3119 CG2 VAL C 3 -1.261 -36.443 50.566 1.00 69.40 C ANISOU 3119 CG2 VAL C 3 6593 11346 8431 207 993 1823 C ATOM 3120 N GLU C 4 -0.807 -32.106 50.004 1.00 74.37 N ANISOU 3120 N GLU C 4 8140 10976 9142 1129 783 1429 N ATOM 3121 CA GLU C 4 -1.470 -31.209 49.046 1.00 76.14 C ANISOU 3121 CA GLU C 4 8467 11103 9359 1406 722 1469 C ATOM 3122 C GLU C 4 -0.699 -31.071 47.734 1.00 73.86 C ANISOU 3122 C GLU C 4 8208 10533 9322 984 610 1643 C ATOM 3123 O GLU C 4 0.529 -30.949 47.743 1.00 73.32 O ANISOU 3123 O GLU C 4 8296 10183 9378 598 463 1683 O ATOM 3124 CB GLU C 4 -1.697 -29.830 49.667 1.00 81.02 C ANISOU 3124 CB GLU C 4 9658 11359 9767 1944 492 1248 C ATOM 3125 CG GLU C 4 -2.994 -29.702 50.453 1.00 86.17 C ANISOU 3125 CG GLU C 4 10175 12530 10035 2673 656 1094 C ATOM 3126 CD GLU C 4 -3.142 -28.339 51.137 1.00 94.18 C ANISOU 3126 CD GLU C 4 11908 13126 10751 3378 354 785 C ATOM 3127 OE1 GLU C 4 -3.886 -27.475 50.610 1.00 98.54 O ANISOU 3127 OE1 GLU C 4 12688 13599 11153 3944 213 711 O ATOM 3128 OE2 GLU C 4 -2.511 -28.130 52.200 1.00 96.23 O ANISOU 3128 OE2 GLU C 4 12573 13093 10896 3405 202 600 O ATOM 3129 N GLN C 5 -1.428 -31.080 46.616 1.00 73.02 N ANISOU 3129 N GLN C 5 7909 10592 9245 1056 676 1776 N ATOM 3130 CA GLN C 5 -0.825 -31.009 45.280 1.00 71.25 C ANISOU 3130 CA GLN C 5 7660 10228 9183 696 609 1964 C ATOM 3131 C GLN C 5 -1.176 -29.732 44.515 1.00 73.94 C ANISOU 3131 C GLN C 5 8355 10239 9501 866 395 2031 C ATOM 3132 O GLN C 5 -2.319 -29.264 44.536 1.00 76.09 O ANISOU 3132 O GLN C 5 8691 10577 9642 1369 383 1953 O ATOM 3133 CB GLN C 5 -1.193 -32.240 44.444 1.00 68.53 C ANISOU 3133 CB GLN C 5 6875 10285 8879 545 793 2088 C ATOM 3134 CG GLN C 5 -0.445 -33.511 44.842 1.00 66.21 C ANISOU 3134 CG GLN C 5 6394 10148 8614 277 861 2058 C ATOM 3135 CD GLN C 5 -0.857 -34.729 44.028 1.00 65.12 C ANISOU 3135 CD GLN C 5 6016 10272 8453 172 902 2152 C ATOM 3136 OE1 GLN C 5 -1.593 -35.591 44.514 1.00 65.34 O ANISOU 3136 OE1 GLN C 5 5914 10516 8397 158 910 2176 O ATOM 3137 NE2 GLN C 5 -0.379 -34.810 42.790 1.00 64.17 N ANISOU 3137 NE2 GLN C 5 5876 10147 8357 69 878 2235 N ATOM 3138 N SER C 6 -0.178 -29.176 43.838 1.00 74.32 N ANISOU 3138 N SER C 6 8615 9991 9634 441 195 2206 N ATOM 3139 CA SER C 6 -0.370 -27.987 43.018 1.00 77.40 C ANISOU 3139 CA SER C 6 9421 9998 9990 454 -98 2344 C ATOM 3140 C SER C 6 0.277 -28.173 41.648 1.00 76.20 C ANISOU 3140 C SER C 6 9034 10016 9901 -54 -65 2657 C ATOM 3141 O SER C 6 1.341 -28.783 41.549 1.00 74.66 O ANISOU 3141 O SER C 6 8536 10092 9739 -471 47 2771 O ATOM 3142 CB SER C 6 0.201 -26.747 43.709 1.00 81.87 C ANISOU 3142 CB SER C 6 10701 9923 10483 382 -559 2315 C ATOM 3143 OG SER C 6 1.615 -26.808 43.786 1.00 82.03 O ANISOU 3143 OG SER C 6 10680 9913 10575 -306 -673 2524 O ATOM 3144 N PRO C 7 -0.375 -27.672 40.583 1.00 77.35 N ANISOU 3144 N PRO C 7 9293 10082 10013 44 -156 2791 N ATOM 3145 CA PRO C 7 -1.688 -27.022 40.597 1.00 79.52 C ANISOU 3145 CA PRO C 7 9850 10153 10211 649 -284 2650 C ATOM 3146 C PRO C 7 -2.846 -28.026 40.684 1.00 76.82 C ANISOU 3146 C PRO C 7 8975 10358 9857 1072 66 2511 C ATOM 3147 O PRO C 7 -2.614 -29.237 40.746 1.00 73.13 O ANISOU 3147 O PRO C 7 8046 10291 9450 851 342 2517 O ATOM 3148 CB PRO C 7 -1.718 -26.291 39.257 1.00 81.92 C ANISOU 3148 CB PRO C 7 10393 10242 10489 435 -518 2926 C ATOM 3149 CG PRO C 7 -0.861 -27.108 38.371 1.00 79.18 C ANISOU 3149 CG PRO C 7 9573 10326 10186 -129 -279 3169 C ATOM 3150 CD PRO C 7 0.217 -27.685 39.234 1.00 77.47 C ANISOU 3150 CD PRO C 7 9146 10277 10011 -423 -154 3116 C ATOM 3151 N GLN C 8 -4.077 -27.520 40.699 1.00 79.43 N ANISOU 3151 N GLN C 8 9392 10722 10067 1672 -5 2413 N ATOM 3152 CA GLN C 8 -5.258 -28.380 40.689 1.00 78.25 C ANISOU 3152 CA GLN C 8 8667 11208 9855 1978 267 2396 C ATOM 3153 C GLN C 8 -5.348 -29.104 39.354 1.00 75.57 C ANISOU 3153 C GLN C 8 8007 11093 9615 1599 360 2630 C ATOM 3154 O GLN C 8 -5.160 -30.319 39.288 1.00 72.38 O ANISOU 3154 O GLN C 8 7232 11008 9262 1275 549 2683 O ATOM 3155 CB GLN C 8 -6.528 -27.575 40.964 1.00 83.10 C ANISOU 3155 CB GLN C 8 9375 11952 10249 2781 155 2266 C ATOM 3156 CG GLN C 8 -6.668 -27.160 42.416 1.00 86.59 C ANISOU 3156 CG GLN C 8 10017 12404 10478 3324 136 1982 C ATOM 3157 CD GLN C 8 -8.102 -27.205 42.901 1.00 91.19 C ANISOU 3157 CD GLN C 8 10161 13737 10751 4101 291 1895 C ATOM 3158 OE1 GLN C 8 -8.437 -27.975 43.805 1.00 90.90 O ANISOU 3158 OE1 GLN C 8 9628 14334 10576 4147 570 1880 O ATOM 3159 NE2 GLN C 8 -8.963 -26.385 42.297 1.00 95.84 N ANISOU 3159 NE2 GLN C 8 10892 14337 11187 4713 95 1874 N ATOM 3160 N SER C 9 -5.626 -28.351 38.296 1.00 77.32 N ANISOU 3160 N SER C 9 8460 11094 9824 1667 166 2757 N ATOM 3161 CA SER C 9 -5.513 -28.872 36.943 1.00 75.33 C ANISOU 3161 CA SER C 9 8033 10967 9623 1292 206 2976 C ATOM 3162 C SER C 9 -4.498 -28.059 36.160 1.00 76.41 C ANISOU 3162 C SER C 9 8584 10677 9771 915 6 3146 C ATOM 3163 O SER C 9 -4.292 -26.875 36.435 1.00 79.63 O ANISOU 3163 O SER C 9 9510 10602 10145 1004 -291 3144 O ATOM 3164 CB SER C 9 -6.864 -28.883 36.238 1.00 76.98 C ANISOU 3164 CB SER C 9 8026 11461 9763 1621 164 3062 C ATOM 3165 OG SER C 9 -7.581 -27.703 36.527 1.00 81.90 O ANISOU 3165 OG SER C 9 8943 11896 10281 2216 -51 2968 O ATOM 3166 N LEU C 10 -3.856 -28.709 35.195 1.00 74.46 N ANISOU 3166 N LEU C 10 8139 10638 9513 490 125 3315 N ATOM 3167 CA LEU C 10 -2.813 -28.081 34.396 1.00 76.22 C ANISOU 3167 CA LEU C 10 8593 10701 9667 33 -10 3570 C ATOM 3168 C LEU C 10 -2.975 -28.389 32.910 1.00 76.27 C ANISOU 3168 C LEU C 10 8467 10957 9557 -104 32 3771 C ATOM 3169 O LEU C 10 -3.385 -29.492 32.532 1.00 73.90 O ANISOU 3169 O LEU C 10 7846 11002 9229 10 216 3688 O ATOM 3170 CB LEU C 10 -1.431 -28.517 34.891 1.00 74.98 C ANISOU 3170 CB LEU C 10 8270 10719 9499 -358 126 3587 C ATOM 3171 CG LEU C 10 -0.170 -27.914 34.259 1.00 78.11 C ANISOU 3171 CG LEU C 10 8744 11178 9756 -938 7 3934 C ATOM 3172 CD1 LEU C 10 -0.102 -26.389 34.407 1.00 82.93 C ANISOU 3172 CD1 LEU C 10 9971 11179 10360 -1164 -456 4136 C ATOM 3173 CD2 LEU C 10 1.066 -28.566 34.861 1.00 77.23 C ANISOU 3173 CD2 LEU C 10 8298 11436 9611 -1190 190 3913 C ATOM 3174 N VAL C 11 -2.645 -27.401 32.079 1.00 79.51 N ANISOU 3174 N VAL C 11 9193 11157 9862 -384 -202 4058 N ATOM 3175 CA VAL C 11 -2.734 -27.530 30.626 1.00 80.33 C ANISOU 3175 CA VAL C 11 9228 11497 9797 -537 -189 4288 C ATOM 3176 C VAL C 11 -1.403 -27.215 29.933 1.00 82.79 C ANISOU 3176 C VAL C 11 9512 12065 9878 -1132 -192 4646 C ATOM 3177 O VAL C 11 -0.836 -26.139 30.127 1.00 86.26 O ANISOU 3177 O VAL C 11 10292 12195 10289 -1528 -483 4901 O ATOM 3178 CB VAL C 11 -3.871 -26.651 30.043 1.00 83.09 C ANISOU 3178 CB VAL C 11 9941 11474 10156 -276 -498 4369 C ATOM 3179 CG1 VAL C 11 -5.211 -27.353 30.172 1.00 80.80 C ANISOU 3179 CG1 VAL C 11 9386 11354 9962 251 -396 4133 C ATOM 3180 CG2 VAL C 11 -3.909 -25.282 30.723 1.00 87.18 C ANISOU 3180 CG2 VAL C 11 11054 11346 10723 -212 -908 4392 C ATOM 3181 N VAL C 12 -0.908 -28.166 29.141 1.00 81.79 N ANISOU 3181 N VAL C 12 8993 12549 9533 -1188 91 4682 N ATOM 3182 CA VAL C 12 0.326 -27.989 28.357 1.00 85.32 C ANISOU 3182 CA VAL C 12 9243 13535 9639 -1672 164 5055 C ATOM 3183 C VAL C 12 0.141 -28.386 26.892 1.00 86.69 C ANISOU 3183 C VAL C 12 9307 14140 9493 -1598 270 5185 C ATOM 3184 O VAL C 12 -0.779 -29.136 26.557 1.00 84.23 O ANISOU 3184 O VAL C 12 9013 13760 9229 -1160 323 4918 O ATOM 3185 CB VAL C 12 1.539 -28.766 28.948 1.00 84.63 C ANISOU 3185 CB VAL C 12 8696 14022 9437 -1734 443 4971 C ATOM 3186 CG1 VAL C 12 2.130 -28.026 30.147 1.00 85.62 C ANISOU 3186 CG1 VAL C 12 8950 13829 9753 -2085 261 5055 C ATOM 3187 CG2 VAL C 12 1.161 -30.210 29.298 1.00 80.25 C ANISOU 3187 CG2 VAL C 12 7943 13600 8948 -1156 682 4497 C ATOM 3188 N ARG C 13 1.030 -27.892 26.032 1.00 91.29 N ANISOU 3188 N ARG C 13 9767 15216 9704 -2070 271 5631 N ATOM 3189 CA ARG C 13 0.923 -28.105 24.588 1.00 93.67 C ANISOU 3189 CA ARG C 13 10002 15973 9616 -2032 352 5809 C ATOM 3190 C ARG C 13 1.676 -29.357 24.133 1.00 93.92 C ANISOU 3190 C ARG C 13 9549 16905 9231 -1682 739 5636 C ATOM 3191 O ARG C 13 2.781 -29.625 24.607 1.00 95.15 O ANISOU 3191 O ARG C 13 9299 17630 9222 -1771 935 5675 O ATOM 3192 CB ARG C 13 1.432 -26.874 23.837 1.00 99.76 C ANISOU 3192 CB ARG C 13 10914 16876 10114 -2745 115 6444 C ATOM 3193 CG ARG C 13 0.966 -25.552 24.435 1.00101.21 C ANISOU 3193 CG ARG C 13 11708 16112 10637 -3101 -388 6623 C ATOM 3194 CD ARG C 13 1.239 -24.383 23.508 1.00108.14 C ANISOU 3194 CD ARG C 13 12906 16964 11217 -3813 -758 7271 C ATOM 3195 NE ARG C 13 0.931 -23.108 24.153 1.00110.92 N ANISOU 3195 NE ARG C 13 13991 16320 11832 -4132 -1362 7428 N ATOM 3196 CZ ARG C 13 0.694 -21.968 23.509 1.00116.66 C ANISOU 3196 CZ ARG C 13 15338 16556 12430 -4588 -1899 7872 C ATOM 3197 NH1 ARG C 13 0.717 -21.917 22.182 1.00120.05 N ANISOU 3197 NH1 ARG C 13 15677 17453 12483 -4848 -1862 8246 N ATOM 3198 NH2 ARG C 13 0.425 -20.869 24.199 1.00119.65 N ANISOU 3198 NH2 ARG C 13 16511 15935 13017 -4747 -2527 7929 N ATOM 3199 N GLN C 14 1.068 -30.109 23.211 1.00 93.47 N ANISOU 3199 N GLN C 14 9580 16968 8968 -1238 796 5436 N ATOM 3200 CA GLN C 14 1.632 -31.360 22.684 1.00 94.62 C ANISOU 3200 CA GLN C 14 9461 17848 8641 -716 1061 5178 C ATOM 3201 C GLN C 14 3.135 -31.233 22.504 1.00 99.85 C ANISOU 3201 C GLN C 14 9573 19562 8802 -914 1329 5484 C ATOM 3202 O GLN C 14 3.600 -30.366 21.776 1.00104.86 O ANISOU 3202 O GLN C 14 10050 20675 9117 -1430 1331 6017 O ATOM 3203 CB GLN C 14 0.963 -31.740 21.350 1.00 96.12 C ANISOU 3203 CB GLN C 14 9903 18117 8501 -417 993 5136 C ATOM 3204 CG GLN C 14 1.352 -33.111 20.792 1.00 97.39 C ANISOU 3204 CG GLN C 14 10018 18851 8136 290 1141 4760 C ATOM 3205 N GLY C 15 3.887 -32.080 23.194 1.00 99.57 N ANISOU 3205 N GLY C 15 9227 19929 8676 -538 1522 5190 N ATOM 3206 CA GLY C 15 5.344 -32.072 23.100 1.00105.51 C ANISOU 3206 CA GLY C 15 9326 21857 8906 -625 1794 5464 C ATOM 3207 C GLY C 15 6.029 -30.887 23.761 1.00107.92 C ANISOU 3207 C GLY C 15 9359 22248 9399 -1521 1713 6007 C ATOM 3208 O GLY C 15 6.986 -30.336 23.209 1.00114.55 O ANISOU 3208 O GLY C 15 9702 24076 9747 -1998 1822 6569 O ATOM 3209 N GLU C 16 5.537 -30.486 24.932 1.00103.45 N ANISOU 3209 N GLU C 16 9133 20686 9487 -1775 1481 5875 N ATOM 3210 CA GLU C 16 6.209 -29.469 25.745 1.00105.82 C ANISOU 3210 CA GLU C 16 9312 20919 9975 -2562 1305 6303 C ATOM 3211 C GLU C 16 6.298 -29.902 27.202 1.00101.50 C ANISOU 3211 C GLU C 16 8792 19911 9861 -2346 1293 5901 C ATOM 3212 O GLU C 16 5.547 -30.775 27.648 1.00 96.16 O ANISOU 3212 O GLU C 16 8369 18706 9461 -1712 1338 5335 O ATOM 3213 CB GLU C 16 5.528 -28.099 25.628 1.00106.70 C ANISOU 3213 CB GLU C 16 10002 20167 10373 -3244 878 6686 C ATOM 3214 CG GLU C 16 5.812 -27.374 24.311 1.00113.75 C ANISOU 3214 CG GLU C 16 10808 21637 10773 -3796 806 7319 C ATOM 3215 CD GLU C 16 5.923 -25.860 24.458 1.00118.56 C ANISOU 3215 CD GLU C 16 11835 21712 11499 -4808 283 7946 C ATOM 3216 OE1 GLU C 16 6.191 -25.383 25.583 1.00118.26 O ANISOU 3216 OE1 GLU C 16 11985 21159 11788 -5154 18 7971 O ATOM 3217 OE2 GLU C 16 5.757 -25.148 23.440 1.00122.86 O ANISOU 3217 OE2 GLU C 16 12591 22318 11771 -5266 77 8422 O ATOM 3218 N ASN C 17 7.225 -29.287 27.934 1.00104.58 N ANISOU 3218 N ASN C 17 8930 20528 10277 -2945 1187 6244 N ATOM 3219 CA ASN C 17 7.482 -29.621 29.336 1.00101.47 C ANISOU 3219 CA ASN C 17 8523 19797 10233 -2817 1162 5929 C ATOM 3220 C ASN C 17 6.360 -29.214 30.289 1.00 96.31 C ANISOU 3220 C ASN C 17 8577 17826 10191 -2777 877 5619 C ATOM 3221 O ASN C 17 5.642 -28.243 30.041 1.00 97.12 O ANISOU 3221 O ASN C 17 9187 17256 10457 -3092 577 5810 O ATOM 3222 CB ASN C 17 8.798 -28.990 29.794 1.00106.92 C ANISOU 3222 CB ASN C 17 8756 21129 10741 -3559 1061 6456 C ATOM 3223 CG ASN C 17 9.986 -29.486 28.998 1.00113.09 C ANISOU 3223 CG ASN C 17 8650 23479 10839 -3490 1400 6760 C ATOM 3224 OD1 ASN C 17 10.132 -30.686 28.766 1.00111.91 O ANISOU 3224 OD1 ASN C 17 8192 23895 10432 -2609 1740 6317 O ATOM 3225 ND2 ASN C 17 10.845 -28.562 28.576 1.00120.78 N ANISOU 3225 ND2 ASN C 17 9230 25204 11455 -4408 1262 7540 N ATOM 3226 N SER C 18 6.217 -29.964 31.376 1.00 91.88 N ANISOU 3226 N SER C 18 8044 16958 9907 -2340 957 5144 N ATOM 3227 CA SER C 18 5.249 -29.636 32.419 1.00 87.84 C ANISOU 3227 CA SER C 18 8083 15410 9884 -2243 738 4855 C ATOM 3228 C SER C 18 5.776 -30.003 33.807 1.00 86.18 C ANISOU 3228 C SER C 18 7774 15111 9861 -2186 748 4625 C ATOM 3229 O SER C 18 6.438 -31.035 33.990 1.00 85.71 O ANISOU 3229 O SER C 18 7297 15623 9646 -1871 982 4434 O ATOM 3230 CB SER C 18 3.910 -30.316 32.148 1.00 83.35 C ANISOU 3230 CB SER C 18 7768 14431 9472 -1643 817 4455 C ATOM 3231 OG SER C 18 4.110 -31.651 31.730 1.00 82.24 O ANISOU 3231 OG SER C 18 7327 14819 9101 -1156 1074 4194 O ATOM 3232 N VAL C 19 5.478 -29.145 34.779 1.00 85.89 N ANISOU 3232 N VAL C 19 8183 14336 10115 -2430 451 4623 N ATOM 3233 CA VAL C 19 5.938 -29.319 36.152 1.00 84.48 C ANISOU 3233 CA VAL C 19 8005 13986 10107 -2435 400 4433 C ATOM 3234 C VAL C 19 4.748 -29.615 37.090 1.00 79.84 C ANISOU 3234 C VAL C 19 7805 12703 9829 -1915 396 3959 C ATOM 3235 O VAL C 19 3.665 -29.042 36.933 1.00 79.48 O ANISOU 3235 O VAL C 19 8169 12132 9897 -1753 256 3901 O ATOM 3236 CB VAL C 19 6.767 -28.078 36.609 1.00 89.38 C ANISOU 3236 CB VAL C 19 8832 14420 10709 -3198 -6 4862 C ATOM 3237 CG1 VAL C 19 5.865 -26.880 36.930 1.00 90.46 C ANISOU 3237 CG1 VAL C 19 9798 13536 11035 -3285 -448 4859 C ATOM 3238 CG2 VAL C 19 7.668 -28.417 37.782 1.00 89.54 C ANISOU 3238 CG2 VAL C 19 8630 14611 10780 -3303 -17 4775 C ATOM 3239 N LEU C 20 4.948 -30.531 38.038 1.00 76.94 N ANISOU 3239 N LEU C 20 7266 12425 9543 -1638 545 3648 N ATOM 3240 CA LEU C 20 3.926 -30.865 39.036 1.00 73.39 C ANISOU 3240 CA LEU C 20 7084 11492 9310 -1230 555 3274 C ATOM 3241 C LEU C 20 4.513 -30.903 40.450 1.00 73.04 C ANISOU 3241 C LEU C 20 7095 11298 9357 -1301 475 3137 C ATOM 3242 O LEU C 20 5.613 -31.417 40.658 1.00 73.64 O ANISOU 3242 O LEU C 20 6838 11795 9346 -1445 540 3181 O ATOM 3243 CB LEU C 20 3.246 -32.198 38.696 1.00 70.23 C ANISOU 3243 CB LEU C 20 6493 11309 8882 -791 781 3024 C ATOM 3244 CG LEU C 20 2.446 -32.284 37.389 1.00 70.47 C ANISOU 3244 CG LEU C 20 6533 11416 8828 -658 825 3103 C ATOM 3245 CD1 LEU C 20 2.039 -33.709 37.090 1.00 68.67 C ANISOU 3245 CD1 LEU C 20 6188 11390 8514 -326 931 2888 C ATOM 3246 CD2 LEU C 20 1.220 -31.399 37.432 1.00 71.12 C ANISOU 3246 CD2 LEU C 20 6936 11037 9049 -565 686 3119 C ATOM 3247 N GLN C 21 3.774 -30.348 41.412 1.00 72.56 N ANISOU 3247 N GLN C 21 7450 10694 9427 -1138 326 2963 N ATOM 3248 CA GLN C 21 4.243 -30.223 42.798 1.00 72.66 C ANISOU 3248 CA GLN C 21 7629 10483 9494 -1192 200 2826 C ATOM 3249 C GLN C 21 3.412 -31.018 43.802 1.00 69.52 C ANISOU 3249 C GLN C 21 7237 10027 9150 -739 365 2479 C ATOM 3250 O GLN C 21 2.187 -31.099 43.681 1.00 68.72 O ANISOU 3250 O GLN C 21 7195 9868 9049 -385 454 2367 O ATOM 3251 CB GLN C 21 4.274 -28.751 43.226 1.00 76.60 C ANISOU 3251 CB GLN C 21 8733 10380 9991 -1402 -221 2933 C ATOM 3252 CG GLN C 21 5.642 -28.095 43.179 1.00 80.54 C ANISOU 3252 CG GLN C 21 9260 10917 10426 -2101 -529 3299 C ATOM 3253 CD GLN C 21 6.038 -27.619 41.792 1.00 83.82 C ANISOU 3253 CD GLN C 21 9518 11605 10723 -2563 -607 3741 C ATOM 3254 OE1 GLN C 21 5.441 -28.005 40.791 1.00 82.07 O ANISOU 3254 OE1 GLN C 21 9077 11631 10473 -2320 -356 3735 O ATOM 3255 NE2 GLN C 21 7.060 -26.774 41.731 1.00 89.53 N ANISOU 3255 NE2 GLN C 21 10358 12318 11343 -3296 -995 4174 N ATOM 3256 N CYS C 22 4.100 -31.589 44.791 1.00 68.39 N ANISOU 3256 N CYS C 22 6997 9970 9019 -793 381 2360 N ATOM 3257 CA CYS C 22 3.481 -32.286 45.914 1.00 66.23 C ANISOU 3257 CA CYS C 22 6756 9660 8747 -486 484 2096 C ATOM 3258 C CYS C 22 4.095 -31.764 47.205 1.00 67.50 C ANISOU 3258 C CYS C 22 7201 9543 8902 -589 288 2008 C ATOM 3259 O CYS C 22 5.319 -31.659 47.310 1.00 68.95 O ANISOU 3259 O CYS C 22 7308 9787 9102 -948 151 2134 O ATOM 3260 CB CYS C 22 3.716 -33.787 45.801 1.00 63.83 C ANISOU 3260 CB CYS C 22 6108 9724 8422 -434 648 2027 C ATOM 3261 SG CYS C 22 2.891 -34.761 47.078 1.00 63.34 S ANISOU 3261 SG CYS C 22 6089 9665 8314 -216 712 1821 S ATOM 3262 N ASN C 23 3.257 -31.449 48.189 1.00 67.63 N ANISOU 3262 N ASN C 23 7515 9335 8846 -256 263 1807 N ATOM 3263 CA ASN C 23 3.726 -30.744 49.385 1.00 69.66 C ANISOU 3263 CA ASN C 23 8201 9227 9039 -280 7 1693 C ATOM 3264 C ASN C 23 3.234 -31.286 50.720 1.00 68.86 C ANISOU 3264 C ASN C 23 8140 9215 8810 43 124 1447 C ATOM 3265 O ASN C 23 2.310 -30.734 51.322 1.00 71.13 O ANISOU 3265 O ASN C 23 8715 9402 8909 500 111 1275 O ATOM 3266 CB ASN C 23 3.396 -29.254 49.278 1.00 73.73 C ANISOU 3266 CB ASN C 23 9325 9217 9471 -159 -331 1695 C ATOM 3267 CG ASN C 23 4.619 -28.414 49.055 1.00 76.36 C ANISOU 3267 CG ASN C 23 9947 9212 9853 -757 -749 1946 C ATOM 3268 OD1 ASN C 23 5.132 -27.800 49.987 1.00 78.87 O ANISOU 3268 OD1 ASN C 23 10749 9121 10096 -880 -1109 1887 O ATOM 3269 ND2 ASN C 23 5.115 -28.398 47.825 1.00 75.84 N ANISOU 3269 ND2 ASN C 23 9575 9370 9870 -1180 -733 2268 N ATOM 3270 N TYR C 24 3.877 -32.343 51.203 1.00 66.32 N ANISOU 3270 N TYR C 24 7545 9122 8533 -152 214 1435 N ATOM 3271 CA TYR C 24 3.336 -33.074 52.343 1.00 65.38 C ANISOU 3271 CA TYR C 24 7393 9181 8266 71 345 1276 C ATOM 3272 C TYR C 24 3.751 -32.544 53.715 1.00 67.73 C ANISOU 3272 C TYR C 24 8099 9204 8430 137 148 1108 C ATOM 3273 O TYR C 24 4.621 -31.676 53.821 1.00 69.93 O ANISOU 3273 O TYR C 24 8714 9095 8761 -76 -159 1128 O ATOM 3274 CB TYR C 24 3.621 -34.574 52.212 1.00 62.36 C ANISOU 3274 CB TYR C 24 6636 9115 7944 -115 466 1337 C ATOM 3275 CG TYR C 24 5.071 -34.972 52.294 1.00 61.62 C ANISOU 3275 CG TYR C 24 6466 8988 7957 -398 316 1360 C ATOM 3276 CD1 TYR C 24 5.659 -35.267 53.524 1.00 62.35 C ANISOU 3276 CD1 TYR C 24 6693 9005 7993 -458 195 1256 C ATOM 3277 CD2 TYR C 24 5.847 -35.087 51.148 1.00 61.00 C ANISOU 3277 CD2 TYR C 24 6133 9060 7984 -561 302 1498 C ATOM 3278 CE1 TYR C 24 6.988 -35.645 53.614 1.00 62.51 C ANISOU 3278 CE1 TYR C 24 6580 9087 8085 -666 41 1288 C ATOM 3279 CE2 TYR C 24 7.183 -35.465 51.224 1.00 62.15 C ANISOU 3279 CE2 TYR C 24 6092 9371 8153 -733 183 1537 C ATOM 3280 CZ TYR C 24 7.744 -35.744 52.463 1.00 63.01 C ANISOU 3280 CZ TYR C 24 6321 9392 8229 -779 43 1432 C ATOM 3281 OH TYR C 24 9.061 -36.119 52.554 1.00 65.00 O ANISOU 3281 OH TYR C 24 6332 9887 8479 -901 -92 1480 O ATOM 3282 N SER C 25 3.085 -33.062 54.749 1.00 67.87 N ANISOU 3282 N SER C 25 8100 9457 8232 393 291 983 N ATOM 3283 CA SER C 25 3.383 -32.769 56.151 1.00 69.93 C ANISOU 3283 CA SER C 25 8731 9546 8295 513 142 801 C ATOM 3284 C SER C 25 3.245 -34.067 56.952 1.00 68.32 C ANISOU 3284 C SER C 25 8252 9727 7981 420 308 823 C ATOM 3285 O SER C 25 2.723 -34.088 58.064 1.00 70.53 O ANISOU 3285 O SER C 25 8656 10193 7949 677 371 713 O ATOM 3286 CB SER C 25 2.440 -31.688 56.685 1.00 74.21 C ANISOU 3286 CB SER C 25 9685 10006 8504 1122 107 595 C ATOM 3287 OG SER C 25 1.082 -32.068 56.528 1.00 74.47 O ANISOU 3287 OG SER C 25 9336 10632 8327 1500 444 630 O ATOM 3288 N VAL C 26 3.737 -35.148 56.361 1.00 65.24 N ANISOU 3288 N VAL C 26 7534 9456 7800 71 333 971 N ATOM 3289 CA VAL C 26 3.588 -36.495 56.889 1.00 64.12 C ANISOU 3289 CA VAL C 26 7216 9583 7564 -84 381 1043 C ATOM 3290 C VAL C 26 4.857 -36.933 57.631 1.00 63.83 C ANISOU 3290 C VAL C 26 7327 9330 7595 -298 151 973 C ATOM 3291 O VAL C 26 5.959 -36.828 57.094 1.00 63.11 O ANISOU 3291 O VAL C 26 7186 9073 7721 -450 3 981 O ATOM 3292 CB VAL C 26 3.266 -37.466 55.723 1.00 61.95 C ANISOU 3292 CB VAL C 26 6638 9488 7414 -243 437 1217 C ATOM 3293 CG1 VAL C 26 3.289 -38.919 56.169 1.00 62.09 C ANISOU 3293 CG1 VAL C 26 6643 9613 7336 -477 311 1312 C ATOM 3294 CG2 VAL C 26 1.927 -37.118 55.115 1.00 62.48 C ANISOU 3294 CG2 VAL C 26 6516 9843 7380 -68 642 1323 C ATOM 3295 N THR C 27 4.701 -37.405 58.867 1.00 65.08 N ANISOU 3295 N THR C 27 7623 9579 7525 -306 119 936 N ATOM 3296 CA THR C 27 5.825 -37.976 59.621 1.00 65.31 C ANISOU 3296 CA THR C 27 7790 9429 7594 -494 -126 882 C ATOM 3297 C THR C 27 5.525 -39.377 60.138 1.00 65.27 C ANISOU 3297 C THR C 27 7771 9596 7431 -659 -190 994 C ATOM 3298 O THR C 27 4.501 -39.593 60.784 1.00 67.01 O ANISOU 3298 O THR C 27 7992 10111 7356 -664 -62 1093 O ATOM 3299 CB THR C 27 6.279 -37.099 60.806 1.00 67.67 C ANISOU 3299 CB THR C 27 8449 9505 7757 -417 -265 718 C ATOM 3300 OG1 THR C 27 5.134 -36.566 61.479 1.00 70.20 O ANISOU 3300 OG1 THR C 27 8920 10022 7732 -105 -81 649 O ATOM 3301 CG2 THR C 27 7.180 -35.963 60.328 1.00 68.71 C ANISOU 3301 CG2 THR C 27 8705 9301 8099 -488 -456 675 C ATOM 3302 N PRO C 28 6.424 -40.335 59.857 1.00 64.37 N ANISOU 3302 N PRO C 28 7658 9341 7458 -780 -431 1001 N ATOM 3303 CA PRO C 28 7.667 -40.158 59.092 1.00 63.67 C ANISOU 3303 CA PRO C 28 7433 9134 7624 -723 -554 924 C ATOM 3304 C PRO C 28 7.478 -40.160 57.558 1.00 62.28 C ANISOU 3304 C PRO C 28 6999 9070 7596 -636 -430 987 C ATOM 3305 O PRO C 28 6.398 -40.496 57.061 1.00 61.63 O ANISOU 3305 O PRO C 28 6889 9080 7449 -644 -310 1085 O ATOM 3306 CB PRO C 28 8.528 -41.356 59.530 1.00 64.39 C ANISOU 3306 CB PRO C 28 7643 9146 7675 -729 -873 882 C ATOM 3307 CG PRO C 28 7.714 -42.108 60.555 1.00 65.50 C ANISOU 3307 CG PRO C 28 8068 9258 7562 -892 -953 965 C ATOM 3308 CD PRO C 28 6.296 -41.709 60.359 1.00 65.17 C ANISOU 3308 CD PRO C 28 7922 9441 7397 -957 -655 1103 C ATOM 3309 N ASP C 29 8.523 -39.764 56.831 1.00 62.30 N ANISOU 3309 N ASP C 29 6783 9136 7754 -588 -472 971 N ATOM 3310 CA ASP C 29 8.518 -39.805 55.371 1.00 61.61 C ANISOU 3310 CA ASP C 29 6437 9223 7749 -478 -365 1031 C ATOM 3311 C ASP C 29 9.510 -40.831 54.825 1.00 62.67 C ANISOU 3311 C ASP C 29 6430 9546 7834 -242 -548 968 C ATOM 3312 O ASP C 29 10.553 -40.477 54.260 1.00 64.17 O ANISOU 3312 O ASP C 29 6281 10048 8053 -170 -549 1003 O ATOM 3313 CB ASP C 29 8.757 -38.414 54.755 1.00 62.17 C ANISOU 3313 CB ASP C 29 6329 9348 7943 -597 -241 1128 C ATOM 3314 CG ASP C 29 9.775 -37.577 55.526 1.00 64.56 C ANISOU 3314 CG ASP C 29 6662 9585 8283 -814 -420 1153 C ATOM 3315 OD1 ASP C 29 9.594 -36.342 55.595 1.00 65.83 O ANISOU 3315 OD1 ASP C 29 6987 9545 8482 -984 -440 1215 O ATOM 3316 OD2 ASP C 29 10.753 -38.139 56.062 1.00 66.54 O ANISOU 3316 OD2 ASP C 29 6826 9955 8503 -813 -605 1117 O ATOM 3317 N ASN C 30 9.173 -42.105 55.006 1.00 62.82 N ANISOU 3317 N ASN C 30 6731 9416 7721 -109 -749 897 N ATOM 3318 CA ASN C 30 9.938 -43.204 54.431 1.00 64.70 C ANISOU 3318 CA ASN C 30 7005 9751 7827 287 -1005 770 C ATOM 3319 C ASN C 30 10.143 -42.986 52.932 1.00 65.20 C ANISOU 3319 C ASN C 30 6750 10145 7878 542 -843 780 C ATOM 3320 O ASN C 30 11.279 -42.964 52.453 1.00 67.54 O ANISOU 3320 O ASN C 30 6699 10873 8090 849 -854 731 O ATOM 3321 CB ASN C 30 9.233 -44.544 54.702 1.00 65.39 C ANISOU 3321 CB ASN C 30 7637 9465 7745 307 -1345 737 C ATOM 3322 CG ASN C 30 9.961 -45.736 54.089 1.00 67.97 C ANISOU 3322 CG ASN C 30 8204 9759 7861 852 -1732 541 C ATOM 3323 OD1 ASN C 30 9.490 -46.334 53.126 1.00 67.90 O ANISOU 3323 OD1 ASN C 30 8428 9639 7733 1037 -1869 510 O ATOM 3324 ND2 ASN C 30 11.111 -46.084 54.651 1.00 70.11 N ANISOU 3324 ND2 ASN C 30 8460 10133 8046 1169 -1951 390 N ATOM 3325 N HIS C 31 9.041 -42.798 52.206 1.00 63.62 N ANISOU 3325 N HIS C 31 6614 9837 7720 411 -685 872 N ATOM 3326 CA HIS C 31 9.093 -42.652 50.755 1.00 64.28 C ANISOU 3326 CA HIS C 31 6468 10197 7758 638 -547 889 C ATOM 3327 C HIS C 31 7.908 -41.905 50.146 1.00 62.34 C ANISOU 3327 C HIS C 31 6180 9867 7638 364 -298 1050 C ATOM 3328 O HIS C 31 6.815 -41.842 50.719 1.00 60.99 O ANISOU 3328 O HIS C 31 6207 9443 7524 90 -276 1132 O ATOM 3329 CB HIS C 31 9.229 -44.018 50.077 1.00 66.63 C ANISOU 3329 CB HIS C 31 7086 10434 7795 1128 -866 707 C ATOM 3330 CG HIS C 31 8.012 -44.876 50.196 1.00 66.03 C ANISOU 3330 CG HIS C 31 7571 9854 7664 936 -1136 742 C ATOM 3331 ND1 HIS C 31 7.587 -45.403 51.397 1.00 66.20 N ANISOU 3331 ND1 HIS C 31 7955 9521 7678 628 -1380 796 N ATOM 3332 CD2 HIS C 31 7.133 -45.308 49.264 1.00 66.45 C ANISOU 3332 CD2 HIS C 31 7873 9744 7630 932 -1247 790 C ATOM 3333 CE1 HIS C 31 6.497 -46.121 51.200 1.00 67.12 C ANISOU 3333 CE1 HIS C 31 8483 9325 7694 381 -1637 923 C ATOM 3334 NE2 HIS C 31 6.201 -46.081 49.913 1.00 67.49 N ANISOU 3334 NE2 HIS C 31 8485 9453 7704 560 -1581 913 N ATOM 3335 N LEU C 32 8.155 -41.354 48.961 1.00 62.92 N ANISOU 3335 N LEU C 32 5952 10249 7706 469 -115 1116 N ATOM 3336 CA LEU C 32 7.134 -40.711 48.162 1.00 61.44 C ANISOU 3336 CA LEU C 32 5730 10009 7606 303 77 1255 C ATOM 3337 C LEU C 32 7.069 -41.411 46.806 1.00 62.60 C ANISOU 3337 C LEU C 32 5914 10302 7568 631 17 1202 C ATOM 3338 O LEU C 32 8.095 -41.621 46.151 1.00 64.78 O ANISOU 3338 O LEU C 32 5974 10979 7661 979 15 1130 O ATOM 3339 CB LEU C 32 7.445 -39.219 48.012 1.00 61.38 C ANISOU 3339 CB LEU C 32 5426 10156 7739 51 294 1423 C ATOM 3340 CG LEU C 32 6.430 -38.334 47.281 1.00 60.59 C ANISOU 3340 CG LEU C 32 5331 9958 7734 -96 458 1567 C ATOM 3341 CD1 LEU C 32 6.330 -36.974 47.942 1.00 60.89 C ANISOU 3341 CD1 LEU C 32 5426 9800 7909 -364 497 1661 C ATOM 3342 CD2 LEU C 32 6.781 -38.191 45.800 1.00 61.82 C ANISOU 3342 CD2 LEU C 32 5247 10455 7788 9 548 1670 C ATOM 3343 N ARG C 33 5.857 -41.786 46.406 1.00 61.71 N ANISOU 3343 N ARG C 33 6062 9933 7452 539 -55 1250 N ATOM 3344 CA ARG C 33 5.632 -42.421 45.117 1.00 63.21 C ANISOU 3344 CA ARG C 33 6403 10164 7451 815 -176 1201 C ATOM 3345 C ARG C 33 4.658 -41.591 44.290 1.00 61.94 C ANISOU 3345 C ARG C 33 6096 10034 7406 592 40 1393 C ATOM 3346 O ARG C 33 3.708 -41.025 44.837 1.00 60.44 O ANISOU 3346 O ARG C 33 5871 9702 7390 260 141 1538 O ATOM 3347 CB ARG C 33 5.102 -43.846 45.302 1.00 64.59 C ANISOU 3347 CB ARG C 33 7158 9932 7451 880 -638 1107 C ATOM 3348 CG ARG C 33 5.326 -44.724 44.089 1.00 67.89 C ANISOU 3348 CG ARG C 33 7903 10335 7557 1368 -915 934 C ATOM 3349 CD ARG C 33 4.995 -46.176 44.339 1.00 71.22 C ANISOU 3349 CD ARG C 33 9081 10226 7754 1443 -1542 825 C ATOM 3350 NE ARG C 33 5.920 -46.817 45.274 1.00 73.35 N ANISOU 3350 NE ARG C 33 9563 10390 7916 1718 -1790 628 N ATOM 3351 CZ ARG C 33 6.368 -48.065 45.152 1.00 77.91 C ANISOU 3351 CZ ARG C 33 10810 10643 8151 2227 -2364 368 C ATOM 3352 NH1 ARG C 33 6.006 -48.814 44.116 1.00 81.61 N ANISOU 3352 NH1 ARG C 33 11848 10833 8326 2527 -2773 255 N ATOM 3353 NH2 ARG C 33 7.201 -48.563 46.056 1.00 79.63 N ANISOU 3353 NH2 ARG C 33 11191 10780 8283 2492 -2587 198 N ATOM 3354 N TRP C 34 4.911 -41.506 42.982 1.00 63.27 N ANISOU 3354 N TRP C 34 6163 10449 7428 837 107 1388 N ATOM 3355 CA TRP C 34 4.005 -40.832 42.051 1.00 62.64 C ANISOU 3355 CA TRP C 34 6001 10379 7419 672 250 1563 C ATOM 3356 C TRP C 34 3.196 -41.848 41.242 1.00 63.74 C ANISOU 3356 C TRP C 34 6532 10309 7379 788 -45 1523 C ATOM 3357 O TRP C 34 3.723 -42.883 40.818 1.00 66.25 O ANISOU 3357 O TRP C 34 7160 10600 7411 1185 -318 1320 O ATOM 3358 CB TRP C 34 4.774 -39.906 41.107 1.00 63.87 C ANISOU 3358 CB TRP C 34 5786 10970 7510 750 508 1663 C ATOM 3359 CG TRP C 34 5.150 -38.562 41.690 1.00 64.26 C ANISOU 3359 CG TRP C 34 5548 11095 7774 408 710 1840 C ATOM 3360 CD1 TRP C 34 6.330 -38.239 42.301 1.00 66.71 C ANISOU 3360 CD1 TRP C 34 5617 11654 8074 346 748 1860 C ATOM 3361 CD2 TRP C 34 4.360 -37.359 41.693 1.00 63.71 C ANISOU 3361 CD2 TRP C 34 5480 10816 7912 101 809 2024 C ATOM 3362 NE1 TRP C 34 6.321 -36.918 42.691 1.00 66.76 N ANISOU 3362 NE1 TRP C 34 5551 11542 8273 -55 814 2060 N ATOM 3363 CE2 TRP C 34 5.125 -36.356 42.331 1.00 64.92 C ANISOU 3363 CE2 TRP C 34 5505 10998 8162 -152 844 2134 C ATOM 3364 CE3 TRP C 34 3.083 -37.033 41.221 1.00 63.31 C ANISOU 3364 CE3 TRP C 34 5554 10560 7942 49 819 2107 C ATOM 3365 CZ2 TRP C 34 4.653 -35.051 42.512 1.00 65.18 C ANISOU 3365 CZ2 TRP C 34 5662 10755 8350 -404 835 2283 C ATOM 3366 CZ3 TRP C 34 2.616 -35.731 41.401 1.00 63.68 C ANISOU 3366 CZ3 TRP C 34 5625 10429 8142 -127 872 2243 C ATOM 3367 CH2 TRP C 34 3.402 -34.758 42.041 1.00 64.51 C ANISOU 3367 CH2 TRP C 34 5729 10462 8320 -328 854 2310 C ATOM 3368 N PHE C 35 1.916 -41.545 41.031 1.00 62.62 N ANISOU 3368 N PHE C 35 6406 10026 7362 477 -44 1717 N ATOM 3369 CA PHE C 35 1.014 -42.433 40.294 1.00 64.09 C ANISOU 3369 CA PHE C 35 6962 9999 7389 434 -392 1763 C ATOM 3370 C PHE C 35 0.330 -41.731 39.126 1.00 63.80 C ANISOU 3370 C PHE C 35 6767 10096 7379 388 -248 1919 C ATOM 3371 O PHE C 35 -0.010 -40.552 39.211 1.00 62.14 O ANISOU 3371 O PHE C 35 6199 10035 7376 235 64 2069 O ATOM 3372 CB PHE C 35 -0.053 -43.012 41.223 1.00 64.28 C ANISOU 3372 CB PHE C 35 7153 9800 7469 -10 -656 1942 C ATOM 3373 CG PHE C 35 0.421 -44.163 42.064 1.00 65.82 C ANISOU 3373 CG PHE C 35 7770 9715 7523 -2 -1038 1816 C ATOM 3374 CD1 PHE C 35 0.214 -45.471 41.647 1.00 69.24 C ANISOU 3374 CD1 PHE C 35 8853 9767 7689 6 -1640 1778 C ATOM 3375 CD2 PHE C 35 1.051 -43.942 43.286 1.00 64.64 C ANISOU 3375 CD2 PHE C 35 7460 9616 7484 -13 -875 1743 C ATOM 3376 CE1 PHE C 35 0.638 -46.547 42.432 1.00 71.81 C ANISOU 3376 CE1 PHE C 35 9693 9738 7855 17 -2096 1669 C ATOM 3377 CE2 PHE C 35 1.482 -45.009 44.075 1.00 66.39 C ANISOU 3377 CE2 PHE C 35 8109 9552 7564 -4 -1266 1637 C ATOM 3378 CZ PHE C 35 1.272 -46.315 43.647 1.00 69.98 C ANISOU 3378 CZ PHE C 35 9241 9600 7750 16 -1889 1603 C ATOM 3379 N LYS C 36 0.130 -42.472 38.041 1.00 65.91 N ANISOU 3379 N LYS C 36 7385 10257 7400 559 -540 1866 N ATOM 3380 CA LYS C 36 -0.597 -41.973 36.883 1.00 66.15 C ANISOU 3380 CA LYS C 36 7342 10374 7418 502 -486 2020 C ATOM 3381 C LYS C 36 -1.895 -42.749 36.743 1.00 68.04 C ANISOU 3381 C LYS C 36 7899 10345 7609 152 -928 2201 C ATOM 3382 O LYS C 36 -1.889 -43.981 36.656 1.00 70.81 O ANISOU 3382 O LYS C 36 8817 10369 7720 181 -1437 2106 O ATOM 3383 CB LYS C 36 0.240 -42.104 35.605 1.00 68.11 C ANISOU 3383 CB LYS C 36 7714 10816 7349 986 -463 1844 C ATOM 3384 CG LYS C 36 -0.414 -41.526 34.349 1.00 67.49 C ANISOU 3384 CG LYS C 36 7571 10845 7229 935 -395 2008 C ATOM 3385 CD LYS C 36 0.263 -42.041 33.090 1.00 69.31 C ANISOU 3385 CD LYS C 36 8073 11253 7009 1458 -500 1810 C ATOM 3386 CE LYS C 36 -0.421 -41.535 31.838 1.00 69.10 C ANISOU 3386 CE LYS C 36 8039 11303 6912 1385 -476 1981 C ATOM 3387 NZ LYS C 36 -0.022 -42.334 30.655 1.00 72.21 N ANISOU 3387 NZ LYS C 36 8876 11776 6784 1924 -719 1755 N ATOM 3388 N GLN C 37 -3.003 -42.011 36.724 1.00 67.45 N ANISOU 3388 N GLN C 37 7479 10423 7725 -175 -790 2484 N ATOM 3389 CA GLN C 37 -4.326 -42.591 36.587 1.00 69.81 C ANISOU 3389 CA GLN C 37 7896 10658 7971 -607 -1181 2770 C ATOM 3390 C GLN C 37 -5.002 -42.084 35.320 1.00 70.89 C ANISOU 3390 C GLN C 37 7947 10903 8085 -587 -1173 2906 C ATOM 3391 O GLN C 37 -5.353 -40.907 35.227 1.00 69.45 O ANISOU 3391 O GLN C 37 7309 10991 8086 -536 -800 3013 O ATOM 3392 CB GLN C 37 -5.178 -42.251 37.814 1.00 69.31 C ANISOU 3392 CB GLN C 37 7387 10873 8075 -987 -1047 3036 C ATOM 3393 CG GLN C 37 -6.608 -42.782 37.752 1.00 72.56 C ANISOU 3393 CG GLN C 37 7726 11457 8388 -1530 -1427 3453 C ATOM 3394 CD GLN C 37 -7.429 -42.440 38.978 1.00 72.57 C ANISOU 3394 CD GLN C 37 7166 11965 8444 -1825 -1239 3740 C ATOM 3395 OE1 GLN C 37 -7.270 -41.375 39.574 1.00 70.49 O ANISOU 3395 OE1 GLN C 37 6493 11963 8328 -1507 -748 3629 O ATOM 3396 NE2 GLN C 37 -8.322 -43.343 39.354 1.00 75.72 N ANISOU 3396 NE2 GLN C 37 7571 12537 8664 -2444 -1675 4137 N ATOM 3397 N ASP C 38 -5.164 -42.976 34.344 1.00 74.16 N ANISOU 3397 N ASP C 38 8885 11053 8241 -588 -1644 2883 N ATOM 3398 CA ASP C 38 -6.008 -42.703 33.177 1.00 76.05 C ANISOU 3398 CA ASP C 38 9113 11359 8425 -679 -1769 3069 C ATOM 3399 C ASP C 38 -7.463 -42.786 33.613 1.00 77.76 C ANISOU 3399 C ASP C 38 9027 11784 8736 -1277 -1997 3507 C ATOM 3400 O ASP C 38 -7.786 -43.476 34.582 1.00 79.20 O ANISOU 3400 O ASP C 38 9240 11957 8897 -1680 -2251 3673 O ATOM 3401 CB ASP C 38 -5.748 -43.716 32.054 1.00 79.68 C ANISOU 3401 CB ASP C 38 10324 11439 8510 -481 -2290 2894 C ATOM 3402 CG ASP C 38 -4.453 -43.441 31.290 1.00 79.99 C ANISOU 3402 CG ASP C 38 10486 11559 8349 210 -1986 2521 C ATOM 3403 OD1 ASP C 38 -4.319 -42.342 30.693 1.00 79.18 O ANISOU 3403 OD1 ASP C 38 9967 11781 8336 360 -1535 2571 O ATOM 3404 OD2 ASP C 38 -3.576 -44.339 31.270 1.00 82.39 O ANISOU 3404 OD2 ASP C 38 11309 11647 8350 615 -2236 2202 O ATOM 3405 N THR C 39 -8.341 -42.084 32.906 1.00 78.43 N ANISOU 3405 N THR C 39 8780 12136 8883 -1342 -1917 3732 N ATOM 3406 CA THR C 39 -9.750 -42.033 33.303 1.00 80.96 C ANISOU 3406 CA THR C 39 8625 12887 9249 -1837 -2070 4189 C ATOM 3407 C THR C 39 -10.443 -43.388 33.122 1.00 85.52 C ANISOU 3407 C THR C 39 9635 13274 9583 -2481 -2840 4496 C ATOM 3408 O THR C 39 -10.366 -44.003 32.059 1.00 87.54 O ANISOU 3408 O THR C 39 10517 13103 9643 -2489 -3300 4424 O ATOM 3409 CB THR C 39 -10.519 -40.891 32.593 1.00 81.11 C ANISOU 3409 CB THR C 39 8164 13281 9372 -1655 -1818 4344 C ATOM 3410 OG1 THR C 39 -10.287 -40.954 31.182 1.00 81.77 O ANISOU 3410 OG1 THR C 39 8688 13044 9338 -1486 -2004 4227 O ATOM 3411 CG2 THR C 39 -10.056 -39.533 33.118 1.00 77.82 C ANISOU 3411 CG2 THR C 39 7347 13047 9174 -1157 -1191 4145 C ATOM 3412 N GLY C 40 -11.091 -43.854 34.186 1.00 87.75 N ANISOU 3412 N GLY C 40 9632 13875 9834 -3039 -3022 4855 N ATOM 3413 CA GLY C 40 -11.684 -45.189 34.216 1.00 93.06 C ANISOU 3413 CA GLY C 40 10776 14334 10250 -3824 -3854 5232 C ATOM 3414 C GLY C 40 -10.729 -46.208 34.813 1.00 93.12 C ANISOU 3414 C GLY C 40 11551 13697 10133 -3852 -4199 4979 C ATOM 3415 O GLY C 40 -11.125 -47.044 35.634 1.00 96.70 O ANISOU 3415 O GLY C 40 12133 14165 10445 -4539 -4665 5338 O ATOM 3416 N LYS C 41 -9.466 -46.125 34.397 1.00 89.66 N ANISOU 3416 N LYS C 41 11597 12761 9707 -3102 -3986 4392 N ATOM 3417 CA LYS C 41 -8.417 -47.040 34.842 1.00 89.90 C ANISOU 3417 CA LYS C 41 12383 12190 9584 -2895 -4296 4052 C ATOM 3418 C LYS C 41 -8.000 -46.802 36.297 1.00 87.08 C ANISOU 3418 C LYS C 41 11598 12088 9400 -2915 -3878 4029 C ATOM 3419 O LYS C 41 -8.393 -45.807 36.912 1.00 84.35 O ANISOU 3419 O LYS C 41 10391 12375 9284 -2940 -3268 4187 O ATOM 3420 CB LYS C 41 -7.203 -46.939 33.910 1.00 88.12 C ANISOU 3420 CB LYS C 41 12628 11607 9247 -1993 -4125 3459 C ATOM 3421 N GLY C 42 -7.208 -47.730 36.836 1.00 88.27 N ANISOU 3421 N GLY C 42 12424 11719 9396 -2843 -4261 3809 N ATOM 3422 CA GLY C 42 -6.720 -47.657 38.212 1.00 86.20 C ANISOU 3422 CA GLY C 42 11897 11601 9254 -2864 -3966 3765 C ATOM 3423 C GLY C 42 -5.507 -46.757 38.382 1.00 80.93 C ANISOU 3423 C GLY C 42 10898 11063 8788 -2056 -3220 3274 C ATOM 3424 O GLY C 42 -5.422 -45.688 37.775 1.00 77.98 O ANISOU 3424 O GLY C 42 10041 11007 8580 -1685 -2671 3163 O ATOM 3425 N LEU C 43 -4.569 -47.191 39.216 1.00 80.33 N ANISOU 3425 N LEU C 43 11100 10742 8678 -1840 -3261 3024 N ATOM 3426 CA LEU C 43 -3.376 -46.409 39.508 1.00 76.22 C ANISOU 3426 CA LEU C 43 10244 10394 8323 -1193 -2634 2631 C ATOM 3427 C LEU C 43 -2.127 -47.169 39.112 1.00 77.96 C ANISOU 3427 C LEU C 43 11124 10202 8294 -545 -2922 2176 C ATOM 3428 O LEU C 43 -1.831 -48.227 39.667 1.00 80.91 O ANISOU 3428 O LEU C 43 12125 10142 8476 -586 -3468 2098 O ATOM 3429 CB LEU C 43 -3.307 -46.060 40.998 1.00 74.22 C ANISOU 3429 CB LEU C 43 9565 10390 8246 -1426 -2322 2733 C ATOM 3430 CG LEU C 43 -4.069 -44.849 41.538 1.00 71.82 C ANISOU 3430 CG LEU C 43 8436 10680 8174 -1630 -1747 2981 C ATOM 3431 CD1 LEU C 43 -5.559 -45.123 41.620 1.00 75.18 C ANISOU 3431 CD1 LEU C 43 8653 11412 8501 -2293 -2009 3493 C ATOM 3432 CD2 LEU C 43 -3.532 -44.459 42.907 1.00 69.43 C ANISOU 3432 CD2 LEU C 43 7869 10528 7983 -1569 -1415 2888 C ATOM 3433 N VAL C 44 -1.393 -46.630 38.150 1.00 77.07 N ANISOU 3433 N VAL C 44 10869 10283 8131 83 -2580 1891 N ATOM 3434 CA VAL C 44 -0.123 -47.224 37.766 1.00 79.64 C ANISOU 3434 CA VAL C 44 11639 10475 8144 862 -2738 1445 C ATOM 3435 C VAL C 44 1.017 -46.438 38.412 1.00 76.78 C ANISOU 3435 C VAL C 44 10662 10563 7947 1201 -2126 1277 C ATOM 3436 O VAL C 44 1.000 -45.207 38.431 1.00 73.34 O ANISOU 3436 O VAL C 44 9522 10555 7787 1053 -1531 1421 O ATOM 3437 CB VAL C 44 0.038 -47.304 36.230 1.00 82.18 C ANISOU 3437 CB VAL C 44 12229 10845 8149 1390 -2825 1255 C ATOM 3438 CG1 VAL C 44 1.368 -47.949 35.857 1.00 86.00 C ANISOU 3438 CG1 VAL C 44 13118 11365 8192 2354 -2975 771 C ATOM 3439 CG2 VAL C 44 -1.107 -48.102 35.616 1.00 85.81 C ANISOU 3439 CG2 VAL C 44 13377 10792 8435 987 -3530 1442 C ATOM 3440 N SER C 45 1.984 -47.166 38.966 1.00 78.99 N ANISOU 3440 N SER C 45 11271 10705 8037 1630 -2358 994 N ATOM 3441 CA SER C 45 3.177 -46.567 39.549 1.00 77.60 C ANISOU 3441 CA SER C 45 10549 10983 7952 1966 -1883 842 C ATOM 3442 C SER C 45 4.034 -45.927 38.460 1.00 78.63 C ANISOU 3442 C SER C 45 10248 11735 7894 2536 -1465 705 C ATOM 3443 O SER C 45 4.161 -46.472 37.362 1.00 82.32 O ANISOU 3443 O SER C 45 11092 12218 7966 3062 -1700 513 O ATOM 3444 CB SER C 45 3.994 -47.626 40.298 1.00 80.65 C ANISOU 3444 CB SER C 45 11439 11094 8109 2375 -2320 561 C ATOM 3445 OG SER C 45 3.408 -47.967 41.545 1.00 79.58 O ANISOU 3445 OG SER C 45 11506 10549 8181 1750 -2570 758 O ATOM 3446 N LEU C 46 4.612 -44.768 38.761 1.00 76.17 N ANISOU 3446 N LEU C 46 9178 11951 7813 2401 -891 834 N ATOM 3447 CA LEU C 46 5.547 -44.130 37.839 1.00 78.05 C ANISOU 3447 CA LEU C 46 8914 12913 7827 2813 -507 809 C ATOM 3448 C LEU C 46 6.997 -44.301 38.293 1.00 80.82 C ANISOU 3448 C LEU C 46 8954 13793 7960 3318 -408 628 C ATOM 3449 O LEU C 46 7.798 -44.902 37.576 1.00 85.75 O ANISOU 3449 O LEU C 46 9639 14858 8083 4103 -498 378 O ATOM 3450 CB LEU C 46 5.196 -42.655 37.621 1.00 74.88 C ANISOU 3450 CB LEU C 46 7929 12771 7752 2251 -36 1160 C ATOM 3451 CG LEU C 46 3.938 -42.343 36.806 1.00 73.40 C ANISOU 3451 CG LEU C 46 7905 12315 7669 1940 -68 1338 C ATOM 3452 CD1 LEU C 46 3.784 -40.841 36.637 1.00 71.31 C ANISOU 3452 CD1 LEU C 46 7124 12297 7673 1505 341 1649 C ATOM 3453 CD2 LEU C 46 3.978 -43.020 35.446 1.00 76.90 C ANISOU 3453 CD2 LEU C 46 8683 12877 7659 2461 -266 1176 C ATOM 3454 N THR C 47 7.321 -43.774 39.476 1.00 78.48 N ANISOU 3454 N THR C 47 8320 13507 7993 2918 -241 750 N ATOM 3455 CA THR C 47 8.657 -43.911 40.089 1.00 81.11 C ANISOU 3455 CA THR C 47 8315 14335 8170 3288 -187 629 C ATOM 3456 C THR C 47 8.621 -43.687 41.613 1.00 77.95 C ANISOU 3456 C THR C 47 7895 13562 8162 2787 -216 706 C ATOM 3457 O THR C 47 7.667 -43.103 42.132 1.00 74.10 O ANISOU 3457 O THR C 47 7469 12633 8054 2143 -138 902 O ATOM 3458 CB THR C 47 9.725 -42.987 39.410 1.00 83.90 C ANISOU 3458 CB THR C 47 7837 15721 8320 3389 248 830 C ATOM 3459 OG1 THR C 47 11.010 -43.215 40.004 1.00 87.23 O ANISOU 3459 OG1 THR C 47 7871 16730 8541 3762 255 743 O ATOM 3460 CG2 THR C 47 9.353 -41.503 39.523 1.00 80.36 C ANISOU 3460 CG2 THR C 47 6972 15277 8284 2523 579 1253 C ATOM 3461 N VAL C 48 9.655 -44.154 42.318 1.00 80.25 N ANISOU 3461 N VAL C 48 8094 14088 8309 3152 -335 540 N ATOM 3462 CA VAL C 48 9.714 -44.056 43.785 1.00 77.77 C ANISOU 3462 CA VAL C 48 7819 13429 8300 2748 -410 580 C ATOM 3463 C VAL C 48 10.910 -43.242 44.267 1.00 78.97 C ANISOU 3463 C VAL C 48 7271 14240 8493 2642 -152 726 C ATOM 3464 O VAL C 48 12.039 -43.460 43.819 1.00 83.70 O ANISOU 3464 O VAL C 48 7467 15601 8736 3193 -112 655 O ATOM 3465 CB VAL C 48 9.806 -45.437 44.467 1.00 79.61 C ANISOU 3465 CB VAL C 48 8711 13181 8358 3157 -928 280 C ATOM 3466 CG1 VAL C 48 9.270 -45.349 45.884 1.00 76.34 C ANISOU 3466 CG1 VAL C 48 8502 12216 8288 2532 -1022 395 C ATOM 3467 CG2 VAL C 48 9.048 -46.490 43.686 1.00 81.83 C ANISOU 3467 CG2 VAL C 48 9741 12968 8382 3479 -1350 102 C ATOM 3468 N LEU C 49 10.656 -42.327 45.201 1.00 75.58 N ANISOU 3468 N LEU C 49 6714 13558 8446 1958 -20 940 N ATOM 3469 CA LEU C 49 11.702 -41.511 45.821 1.00 76.82 C ANISOU 3469 CA LEU C 49 6332 14180 8675 1688 105 1126 C ATOM 3470 C LEU C 49 11.904 -41.908 47.298 1.00 75.85 C ANISOU 3470 C LEU C 49 6463 13665 8692 1602 -125 998 C ATOM 3471 O LEU C 49 10.929 -42.027 48.041 1.00 72.58 O ANISOU 3471 O LEU C 49 6520 12563 8493 1312 -219 954 O ATOM 3472 CB LEU C 49 11.341 -40.029 45.684 1.00 75.03 C ANISOU 3472 CB LEU C 49 5877 13919 8713 985 339 1472 C ATOM 3473 CG LEU C 49 11.317 -39.422 44.274 1.00 76.47 C ANISOU 3473 CG LEU C 49 5737 14567 8750 939 556 1693 C ATOM 3474 CD1 LEU C 49 10.265 -38.339 44.136 1.00 73.60 C ANISOU 3474 CD1 LEU C 49 5586 13699 8680 388 648 1892 C ATOM 3475 CD2 LEU C 49 12.676 -38.869 43.922 1.00 82.21 C ANISOU 3475 CD2 LEU C 49 5745 16252 9238 839 656 1983 C ATOM 3476 N VAL C 50 13.160 -42.110 47.717 1.00 79.23 N ANISOU 3476 N VAL C 50 6531 14618 8954 1856 -214 969 N ATOM 3477 CA VAL C 50 13.474 -42.700 49.042 1.00 78.97 C ANISOU 3477 CA VAL C 50 6774 14253 8977 1913 -493 806 C ATOM 3478 C VAL C 50 14.320 -41.824 50.004 1.00 79.75 C ANISOU 3478 C VAL C 50 6470 14605 9228 1443 -477 1020 C ATOM 3479 O VAL C 50 13.907 -41.561 51.140 1.00 77.06 O ANISOU 3479 O VAL C 50 6468 13686 9126 1028 -571 1022 O ATOM 3480 CB VAL C 50 14.150 -44.112 48.906 1.00 83.09 C ANISOU 3480 CB VAL C 50 7477 14980 9112 2813 -810 469 C ATOM 3481 CG1 VAL C 50 14.202 -44.815 50.251 1.00 82.88 C ANISOU 3481 CG1 VAL C 50 7932 14402 9156 2820 -1171 303 C ATOM 3482 CG2 VAL C 50 13.424 -44.991 47.900 1.00 83.15 C ANISOU 3482 CG2 VAL C 50 7994 14701 8898 3304 -948 251 C ATOM 3483 N ASP C 51 15.494 -41.386 49.550 1.00 84.10 N ANISOU 3483 N ASP C 51 6296 16072 9587 1493 -387 1227 N ATOM 3484 CA ASP C 51 16.471 -40.694 50.411 1.00 86.53 C ANISOU 3484 CA ASP C 51 6189 16725 9965 1046 -483 1471 C ATOM 3485 C ASP C 51 16.062 -39.260 50.761 1.00 84.40 C ANISOU 3485 C ASP C 51 6006 16053 10009 127 -435 1793 C ATOM 3486 O ASP C 51 15.098 -38.742 50.203 1.00 81.68 O ANISOU 3486 O ASP C 51 5924 15310 9800 -96 -275 1843 O ATOM 3487 CB ASP C 51 17.858 -40.699 49.754 1.00 93.33 C ANISOU 3487 CB ASP C 51 6142 18876 10445 1342 -432 1680 C ATOM 3488 CG ASP C 51 18.254 -42.067 49.208 1.00 96.91 C ANISOU 3488 CG ASP C 51 6548 19803 10472 2466 -492 1308 C ATOM 3489 OD1 ASP C 51 17.755 -43.097 49.714 1.00 95.03 O ANISOU 3489 OD1 ASP C 51 7027 18819 10260 2935 -735 903 O ATOM 3490 OD2 ASP C 51 19.074 -42.110 48.266 1.00102.57 O ANISOU 3490 OD2 ASP C 51 6536 21666 10769 2899 -339 1436 O ATOM 3491 N GLN C 52 16.801 -38.627 51.679 1.00 86.39 N ANISOU 3491 N GLN C 52 6098 16384 10342 -363 -635 1999 N ATOM 3492 CA GLN C 52 16.530 -37.238 52.101 1.00 85.70 C ANISOU 3492 CA GLN C 52 6247 15830 10486 -1195 -738 2282 C ATOM 3493 C GLN C 52 16.562 -36.235 50.947 1.00 87.79 C ANISOU 3493 C GLN C 52 6190 16466 10700 -1645 -627 2684 C ATOM 3494 O GLN C 52 15.692 -35.371 50.842 1.00 85.63 O ANISOU 3494 O GLN C 52 6389 15542 10605 -2010 -632 2746 O ATOM 3495 CB GLN C 52 17.482 -36.794 53.221 1.00 88.98 C ANISOU 3495 CB GLN C 52 6560 16322 10927 -1651 -1076 2462 C ATOM 3496 CG GLN C 52 16.937 -37.002 54.631 1.00 85.74 C ANISOU 3496 CG GLN C 52 6861 15028 10689 -1623 -1249 2148 C ATOM 3497 CD GLN C 52 16.739 -38.470 54.979 1.00 83.75 C ANISOU 3497 CD GLN C 52 6767 14694 10361 -897 -1201 1744 C ATOM 3498 OE1 GLN C 52 17.624 -39.298 54.755 1.00 87.15 O ANISOU 3498 OE1 GLN C 52 6741 15783 10588 -444 -1252 1700 O ATOM 3499 NE2 GLN C 52 15.575 -38.796 55.530 1.00 78.92 N ANISOU 3499 NE2 GLN C 52 6815 13311 9860 -774 -1148 1474 N ATOM 3500 N LYS C 53 17.581 -36.346 50.101 1.00 92.72 N ANISOU 3500 N LYS C 53 6002 18198 11028 -1589 -548 2973 N ATOM 3501 CA LYS C 53 17.605 -35.644 48.826 1.00 95.11 C ANISOU 3501 CA LYS C 53 5930 19020 11187 -1912 -394 3361 C ATOM 3502 C LYS C 53 17.724 -36.710 47.752 1.00 95.93 C ANISOU 3502 C LYS C 53 5595 19895 10959 -1050 -78 3160 C ATOM 3503 O LYS C 53 18.786 -37.316 47.590 1.00100.94 O ANISOU 3503 O LYS C 53 5535 21576 11241 -626 -50 3207 O ATOM 3504 CB LYS C 53 18.776 -34.654 48.741 1.00102.22 C ANISOU 3504 CB LYS C 53 6191 20728 11920 -2768 -629 4024 C ATOM 3505 CG LYS C 53 18.889 -33.658 49.895 1.00102.96 C ANISOU 3505 CG LYS C 53 6778 20078 12263 -3611 -1094 4227 C ATOM 3506 CD LYS C 53 17.637 -32.810 50.067 1.00 98.52 C ANISOU 3506 CD LYS C 53 7203 18228 12001 -3897 -1207 4093 C ATOM 3507 CE LYS C 53 17.807 -31.809 51.195 1.00100.54 C ANISOU 3507 CE LYS C 53 8053 17742 12406 -4621 -1745 4255 C ATOM 3508 NZ LYS C 53 18.552 -30.605 50.747 1.00107.53 N ANISOU 3508 NZ LYS C 53 8737 18969 13151 -5672 -2163 4973 N ATOM 3509 N ASP C 54 16.624 -36.956 47.046 1.00 91.58 N ANISOU 3509 N ASP C 54 5481 18835 10479 -728 121 2916 N ATOM 3510 CA ASP C 54 16.578 -37.996 46.022 1.00 92.26 C ANISOU 3510 CA ASP C 54 5376 19446 10234 138 343 2658 C ATOM 3511 C ASP C 54 16.163 -37.409 44.677 1.00 92.94 C ANISOU 3511 C ASP C 54 5311 19803 10198 -51 564 2913 C ATOM 3512 O ASP C 54 15.518 -36.362 44.628 1.00 90.85 O ANISOU 3512 O ASP C 54 5356 18956 10205 -746 527 3153 O ATOM 3513 CB ASP C 54 15.623 -39.120 46.444 1.00 87.12 C ANISOU 3513 CB ASP C 54 5484 17894 9723 765 278 2092 C ATOM 3514 CG ASP C 54 16.014 -40.477 45.871 1.00 89.91 C ANISOU 3514 CG ASP C 54 5746 18762 9655 1804 273 1739 C ATOM 3515 OD1 ASP C 54 17.133 -40.617 45.331 1.00 96.15 O ANISOU 3515 OD1 ASP C 54 5803 20714 10015 2187 355 1868 O ATOM 3516 OD2 ASP C 54 15.198 -41.416 45.968 1.00 86.62 O ANISOU 3516 OD2 ASP C 54 6015 17613 9282 2256 140 1343 O ATOM 3517 N LYS C 55 16.552 -38.080 43.594 1.00 96.52 N ANISOU 3517 N LYS C 55 5332 21148 10194 630 761 2847 N ATOM 3518 CA LYS C 55 16.221 -37.651 42.234 1.00 97.88 C ANISOU 3518 CA LYS C 55 5331 21697 10162 548 984 3074 C ATOM 3519 C LYS C 55 16.251 -38.826 41.258 1.00100.26 C ANISOU 3519 C LYS C 55 5570 22538 9985 1644 1135 2700 C ATOM 3520 O LYS C 55 17.289 -39.454 41.056 1.00106.23 O ANISOU 3520 O LYS C 55 5739 24379 10245 2317 1185 2642 O ATOM 3521 CB LYS C 55 17.146 -36.516 41.757 1.00104.03 C ANISOU 3521 CB LYS C 55 5304 23512 10712 -245 1033 3786 C ATOM 3522 CG LYS C 55 18.632 -36.757 41.983 1.00111.39 C ANISOU 3522 CG LYS C 55 5289 25815 11219 -95 1028 4031 C ATOM 3523 CD LYS C 55 19.496 -35.781 41.205 1.00118.66 C ANISOU 3523 CD LYS C 55 5296 28033 11757 -857 1103 4820 C ATOM 3524 CE LYS C 55 20.961 -36.187 41.279 1.00126.63 C ANISOU 3524 CE LYS C 55 5185 30715 12212 -528 1157 5065 C ATOM 3525 NZ LYS C 55 21.809 -35.351 40.394 1.00135.15 N ANISOU 3525 NZ LYS C 55 5231 33334 12787 -1251 1263 5908 N ATOM 3526 N THR C 56 15.105 -39.117 40.654 1.00 96.50 N ANISOU 3526 N THR C 56 5728 21321 9615 1868 1166 2442 N ATOM 3527 CA THR C 56 14.993 -40.227 39.705 1.00 99.05 C ANISOU 3527 CA THR C 56 6217 21941 9478 2894 1202 2052 C ATOM 3528 C THR C 56 14.407 -39.808 38.346 1.00 99.55 C ANISOU 3528 C THR C 56 6287 22164 9372 2804 1401 2223 C ATOM 3529 O THR C 56 13.762 -38.761 38.226 1.00 96.39 O ANISOU 3529 O THR C 56 5990 21305 9330 1962 1458 2558 O ATOM 3530 CB THR C 56 14.184 -41.409 40.306 1.00 94.94 C ANISOU 3530 CB THR C 56 6624 20307 9141 3431 891 1480 C ATOM 3531 OG1 THR C 56 13.934 -42.389 39.291 1.00 97.83 O ANISOU 3531 OG1 THR C 56 7349 20764 9059 4333 812 1124 O ATOM 3532 CG2 THR C 56 12.857 -40.929 40.882 1.00 87.65 C ANISOU 3532 CG2 THR C 56 6329 18139 8834 2681 807 1521 C ATOM 3533 N SER C 57 14.658 -40.631 37.329 1.00104.20 N ANISOU 3533 N SER C 57 6813 23408 9369 3743 1465 1971 N ATOM 3534 CA SER C 57 14.063 -40.445 36.012 1.00105.05 C ANISOU 3534 CA SER C 57 7040 23624 9251 3814 1612 2045 C ATOM 3535 C SER C 57 13.704 -41.786 35.377 1.00106.89 C ANISOU 3535 C SER C 57 7915 23629 9069 4951 1415 1458 C ATOM 3536 O SER C 57 14.399 -42.784 35.564 1.00111.27 O ANISOU 3536 O SER C 57 8500 24576 9200 5910 1259 1075 O ATOM 3537 CB SER C 57 14.987 -39.640 35.094 1.00111.73 C ANISOU 3537 CB SER C 57 6905 25947 9600 3590 1948 2585 C ATOM 3538 OG SER C 57 15.961 -40.466 34.486 1.00119.90 O ANISOU 3538 OG SER C 57 7449 28276 9833 4697 2063 2382 O ATOM 3539 N ASN C 58 12.611 -41.788 34.622 1.00104.37 N ANISOU 3539 N ASN C 58 8167 22641 8849 4847 1357 1393 N ATOM 3540 CA ASN C 58 12.085 -42.983 33.974 1.00106.18 C ANISOU 3540 CA ASN C 58 9190 22432 8722 5755 1052 881 C ATOM 3541 C ASN C 58 11.280 -42.585 32.735 1.00105.73 C ANISOU 3541 C ASN C 58 9313 22287 8572 5560 1156 1030 C ATOM 3542 O ASN C 58 10.196 -42.003 32.847 1.00 99.86 O ANISOU 3542 O ASN C 58 8875 20682 8384 4751 1120 1227 O ATOM 3543 CB ASN C 58 11.217 -43.774 34.964 1.00101.34 C ANISOU 3543 CB ASN C 58 9500 20441 8565 5669 583 546 C ATOM 3544 CG ASN C 58 10.582 -45.004 34.339 1.00103.81 C ANISOU 3544 CG ASN C 58 10795 20115 8532 6424 106 82 C ATOM 3545 OD1 ASN C 58 11.251 -45.786 33.657 1.00110.88 O ANISOU 3545 OD1 ASN C 58 11822 21587 8721 7520 -24 -265 O ATOM 3546 ND2 ASN C 58 9.284 -45.187 34.579 1.00 98.71 N ANISOU 3546 ND2 ASN C 58 10865 18309 8332 5858 -206 85 N ATOM 3547 N GLY C 59 11.816 -42.894 31.557 1.00112.51 N ANISOU 3547 N GLY C 59 9964 24106 8679 6364 1283 931 N ATOM 3548 CA GLY C 59 11.233 -42.422 30.304 1.00113.22 C ANISOU 3548 CA GLY C 59 10100 24330 8588 6184 1430 1131 C ATOM 3549 C GLY C 59 11.311 -40.908 30.262 1.00111.35 C ANISOU 3549 C GLY C 59 9117 24500 8692 5046 1813 1814 C ATOM 3550 O GLY C 59 12.354 -40.333 30.583 1.00114.48 O ANISOU 3550 O GLY C 59 8669 25868 8960 4788 2071 2164 O ATOM 3551 N ARG C 60 10.206 -40.263 29.890 1.00106.85 N ANISOU 3551 N ARG C 60 8897 23166 8537 4346 1777 2025 N ATOM 3552 CA ARG C 60 10.138 -38.797 29.893 1.00105.26 C ANISOU 3552 CA ARG C 60 8223 23080 8690 3255 1998 2648 C ATOM 3553 C ARG C 60 9.854 -38.251 31.291 1.00 99.51 C ANISOU 3553 C ARG C 60 7587 21515 8706 2505 1881 2754 C ATOM 3554 O ARG C 60 10.001 -37.048 31.537 1.00 99.00 O ANISOU 3554 O ARG C 60 7193 21512 8911 1648 1967 3238 O ATOM 3555 CB ARG C 60 9.094 -38.274 28.901 1.00103.61 C ANISOU 3555 CB ARG C 60 8367 22430 8570 2904 1975 2823 C ATOM 3556 CG ARG C 60 9.335 -38.660 27.440 1.00110.14 C ANISOU 3556 CG ARG C 60 9119 24103 8625 3567 2099 2773 C ATOM 3557 CD ARG C 60 8.375 -39.749 26.996 1.00109.23 C ANISOU 3557 CD ARG C 60 9902 23168 8431 4237 1762 2239 C ATOM 3558 NE ARG C 60 6.986 -39.335 27.187 1.00103.14 N ANISOU 3558 NE ARG C 60 9664 21190 8336 3549 1543 2324 N ATOM 3559 CZ ARG C 60 5.998 -40.153 27.538 1.00 99.93 C ANISOU 3559 CZ ARG C 60 10000 19753 8214 3701 1152 1967 C ATOM 3560 NH1 ARG C 60 6.232 -41.443 27.742 1.00102.40 N ANISOU 3560 NH1 ARG C 60 10769 19917 8223 4482 861 1483 N ATOM 3561 NH2 ARG C 60 4.773 -39.677 27.691 1.00 95.24 N ANISOU 3561 NH2 ARG C 60 9703 18312 8170 3067 1005 2125 N ATOM 3562 N TYR C 62 9.443 -39.143 32.194 1.00 95.92 N ANISOU 3562 N TYR C 62 7651 20265 8529 2833 1630 2311 N ATOM 3563 CA TYR C 62 9.189 -38.796 33.590 1.00 91.08 C ANISOU 3563 CA TYR C 62 7153 18922 8530 2274 1520 2340 C ATOM 3564 C TYR C 62 10.515 -38.636 34.316 1.00 94.30 C ANISOU 3564 C TYR C 62 6940 20075 8813 2239 1630 2474 C ATOM 3565 O TYR C 62 11.443 -39.410 34.083 1.00 99.35 O ANISOU 3565 O TYR C 62 7283 21533 8934 2975 1677 2284 O ATOM 3566 CB TYR C 62 8.357 -39.879 34.285 1.00 87.21 C ANISOU 3566 CB TYR C 62 7381 17474 8281 2598 1197 1887 C ATOM 3567 CG TYR C 62 7.092 -40.288 33.558 1.00 85.20 C ANISOU 3567 CG TYR C 62 7734 16577 8060 2685 998 1752 C ATOM 3568 CD1 TYR C 62 6.990 -41.536 32.939 1.00 87.96 C ANISOU 3568 CD1 TYR C 62 8586 16852 7984 3437 723 1373 C ATOM 3569 CD2 TYR C 62 5.993 -39.434 33.500 1.00 81.00 C ANISOU 3569 CD2 TYR C 62 7324 15503 7951 2045 1017 2001 C ATOM 3570 CE1 TYR C 62 5.820 -41.919 32.273 1.00 86.93 C ANISOU 3570 CE1 TYR C 62 9047 16111 7873 3421 456 1297 C ATOM 3571 CE2 TYR C 62 4.824 -39.802 32.837 1.00 79.89 C ANISOU 3571 CE2 TYR C 62 7663 14861 7830 2084 812 1927 C ATOM 3572 CZ TYR C 62 4.740 -41.043 32.228 1.00 82.70 C ANISOU 3572 CZ TYR C 62 8495 15142 7787 2707 525 1601 C ATOM 3573 OH TYR C 62 3.577 -41.397 31.575 1.00 81.80 O ANISOU 3573 OH TYR C 62 8879 14516 7685 2646 247 1578 O ATOM 3574 N SER C 63 10.598 -37.629 35.186 1.00 92.23 N ANISOU 3574 N SER C 63 6512 19548 8985 1432 1628 2794 N ATOM 3575 CA SER C 63 11.811 -37.340 35.966 1.00 95.19 C ANISOU 3575 CA SER C 63 6310 20558 9300 1208 1663 3002 C ATOM 3576 C SER C 63 11.481 -36.498 37.196 1.00 91.03 C ANISOU 3576 C SER C 63 6024 19203 9362 435 1500 3149 C ATOM 3577 O SER C 63 11.184 -35.304 37.088 1.00 90.81 O ANISOU 3577 O SER C 63 6048 18910 9547 -303 1456 3533 O ATOM 3578 CB SER C 63 12.887 -36.657 35.106 1.00102.35 C ANISOU 3578 CB SER C 63 6384 22792 9712 942 1876 3533 C ATOM 3579 OG SER C 63 12.316 -35.809 34.120 1.00102.99 O ANISOU 3579 OG SER C 63 6547 22803 9781 455 1937 3881 O ATOM 3580 N ALA C 64 11.533 -37.134 38.363 1.00 88.33 N ANISOU 3580 N ALA C 64 5902 18428 9231 657 1362 2826 N ATOM 3581 CA ALA C 64 11.100 -36.507 39.611 1.00 84.16 C ANISOU 3581 CA ALA C 64 5712 17059 9206 98 1197 2855 C ATOM 3582 C ALA C 64 12.237 -36.385 40.622 1.00 86.29 C ANISOU 3582 C ALA C 64 5613 17701 9472 -108 1107 2967 C ATOM 3583 O ALA C 64 13.189 -37.165 40.588 1.00 89.73 O ANISOU 3583 O ALA C 64 5624 18904 9567 390 1153 2863 O ATOM 3584 CB ALA C 64 9.931 -37.283 40.207 1.00 78.97 C ANISOU 3584 CB ALA C 64 5709 15469 8827 408 1081 2428 C ATOM 3585 N THR C 65 12.131 -35.395 41.509 1.00 84.75 N ANISOU 3585 N THR C 65 5616 16970 9615 -789 938 3169 N ATOM 3586 CA THR C 65 13.129 -35.149 42.557 1.00 86.81 C ANISOU 3586 CA THR C 65 5620 17450 9912 -1116 774 3310 C ATOM 3587 C THR C 65 12.432 -34.883 43.890 1.00 82.23 C ANISOU 3587 C THR C 65 5678 15817 9747 -1318 572 3094 C ATOM 3588 O THR C 65 11.377 -34.241 43.918 1.00 79.55 O ANISOU 3588 O THR C 65 5852 14732 9643 -1515 522 3070 O ATOM 3589 CB THR C 65 14.056 -33.943 42.225 1.00 92.79 C ANISOU 3589 CB THR C 65 5898 18840 10517 -1945 659 3956 C ATOM 3590 OG1 THR C 65 13.381 -32.714 42.513 1.00 92.01 O ANISOU 3590 OG1 THR C 65 6385 17848 10726 -2625 405 4155 O ATOM 3591 CG2 THR C 65 14.498 -33.945 40.753 1.00 97.61 C ANISOU 3591 CG2 THR C 65 5899 20511 10676 -1869 891 4273 C ATOM 3592 N LEU C 66 13.030 -35.364 44.984 1.00 81.95 N ANISOU 3592 N LEU C 66 5594 15796 9749 -1212 453 2937 N ATOM 3593 CA LEU C 66 12.455 -35.251 46.339 1.00 77.96 C ANISOU 3593 CA LEU C 66 5659 14413 9548 -1317 279 2705 C ATOM 3594 C LEU C 66 13.397 -34.579 47.345 1.00 80.77 C ANISOU 3594 C LEU C 66 5928 14809 9952 -1844 2 2926 C ATOM 3595 O LEU C 66 14.597 -34.861 47.375 1.00 84.69 O ANISOU 3595 O LEU C 66 5848 16082 10247 -1873 -41 3095 O ATOM 3596 CB LEU C 66 12.030 -36.637 46.860 1.00 74.46 C ANISOU 3596 CB LEU C 66 5447 13732 9112 -674 326 2248 C ATOM 3597 CG LEU C 66 12.025 -36.949 48.365 1.00 72.23 C ANISOU 3597 CG LEU C 66 5489 12979 8977 -678 149 2034 C ATOM 3598 CD1 LEU C 66 10.818 -36.357 49.073 1.00 68.80 C ANISOU 3598 CD1 LEU C 66 5628 11742 8772 -878 119 1943 C ATOM 3599 CD2 LEU C 66 12.074 -38.434 48.597 1.00 70.47 C ANISOU 3599 CD2 LEU C 66 5346 12804 8627 -80 114 1704 C ATOM 3600 N ASP C 67 12.832 -33.697 48.168 1.00 79.29 N ANISOU 3600 N ASP C 67 6327 13814 9984 -2208 -215 2917 N ATOM 3601 CA ASP C 67 13.543 -33.092 49.292 1.00 81.67 C ANISOU 3601 CA ASP C 67 6772 13920 10338 -2676 -566 3049 C ATOM 3602 C ASP C 67 12.803 -33.381 50.610 1.00 77.80 C ANISOU 3602 C ASP C 67 6888 12669 10005 -2384 -623 2631 C ATOM 3603 O ASP C 67 11.892 -32.640 50.991 1.00 76.92 O ANISOU 3603 O ASP C 67 7387 11849 9991 -2428 -725 2527 O ATOM 3604 CB ASP C 67 13.700 -31.582 49.062 1.00 85.87 C ANISOU 3604 CB ASP C 67 7568 14182 10878 -3444 -918 3483 C ATOM 3605 CG ASP C 67 14.438 -30.876 50.196 1.00 89.72 C ANISOU 3605 CG ASP C 67 8330 14374 11387 -4013 -1406 3655 C ATOM 3606 OD1 ASP C 67 14.701 -31.498 51.249 1.00 88.31 O ANISOU 3606 OD1 ASP C 67 8175 14130 11248 -3772 -1430 3392 O ATOM 3607 OD2 ASP C 67 14.748 -29.677 50.032 1.00 94.54 O ANISOU 3607 OD2 ASP C 67 9205 14763 11954 -4746 -1835 4075 O ATOM 3608 N LYS C 68 13.204 -34.452 51.301 1.00 76.17 N ANISOU 3608 N LYS C 68 6513 12663 9765 -2043 -579 2401 N ATOM 3609 CA LYS C 68 12.563 -34.879 52.554 1.00 72.58 C ANISOU 3609 CA LYS C 68 6558 11628 9392 -1790 -618 2052 C ATOM 3610 C LYS C 68 12.649 -33.831 53.654 1.00 74.37 C ANISOU 3610 C LYS C 68 7282 11309 9666 -2182 -952 2092 C ATOM 3611 O LYS C 68 11.869 -33.859 54.604 1.00 72.55 O ANISOU 3611 O LYS C 68 7552 10567 9446 -1968 -961 1823 O ATOM 3612 CB LYS C 68 13.148 -36.208 53.053 1.00 71.89 C ANISOU 3612 CB LYS C 68 6233 11858 9223 -1418 -608 1857 C ATOM 3613 CG LYS C 68 12.589 -37.444 52.356 1.00 68.95 C ANISOU 3613 CG LYS C 68 5791 11631 8776 -863 -386 1643 C ATOM 3614 CD LYS C 68 13.129 -38.741 52.949 1.00 68.33 C ANISOU 3614 CD LYS C 68 5687 11695 8581 -462 -514 1424 C ATOM 3615 N ASP C 69 13.593 -32.906 53.512 1.00 78.80 N ANISOU 3615 N ASP C 69 7721 12021 10200 -2770 -1265 2455 N ATOM 3616 CA ASP C 69 13.816 -31.859 54.506 1.00 82.02 C ANISOU 3616 CA ASP C 69 8709 11848 10608 -3210 -1730 2527 C ATOM 3617 C ASP C 69 12.977 -30.604 54.240 1.00 83.16 C ANISOU 3617 C ASP C 69 9535 11306 10756 -3355 -1928 2565 C ATOM 3618 O ASP C 69 12.922 -29.695 55.069 1.00 86.17 O ANISOU 3618 O ASP C 69 10630 11026 11083 -3557 -2368 2527 O ATOM 3619 CB ASP C 69 15.313 -31.520 54.609 1.00 87.65 C ANISOU 3619 CB ASP C 69 9004 13048 11250 -3879 -2107 2960 C ATOM 3620 CG ASP C 69 16.164 -32.703 55.098 1.00 87.52 C ANISOU 3620 CG ASP C 69 8404 13662 11188 -3616 -1996 2864 C ATOM 3621 OD1 ASP C 69 17.408 -32.591 55.046 1.00 92.74 O ANISOU 3621 OD1 ASP C 69 8504 14984 11749 -4066 -2229 3242 O ATOM 3622 OD2 ASP C 69 15.604 -33.740 55.531 1.00 83.08 O ANISOU 3622 OD2 ASP C 69 7939 12972 10656 -2982 -1724 2449 O ATOM 3623 N ALA C 70 12.331 -30.563 53.078 1.00 81.35 N ANISOU 3623 N ALA C 70 9146 11209 10554 -3196 -1654 2621 N ATOM 3624 CA ALA C 70 11.361 -29.517 52.752 1.00 82.18 C ANISOU 3624 CA ALA C 70 9899 10677 10648 -3144 -1801 2590 C ATOM 3625 C ALA C 70 10.002 -30.153 52.486 1.00 77.14 C ANISOU 3625 C ALA C 70 9254 10015 10041 -2420 -1322 2237 C ATOM 3626 O ALA C 70 9.053 -29.471 52.086 1.00 77.21 O ANISOU 3626 O ALA C 70 9665 9648 10025 -2206 -1344 2174 O ATOM 3627 CB ALA C 70 11.826 -28.707 51.545 1.00 86.07 C ANISOU 3627 CB ALA C 70 10243 11346 11112 -3744 -2010 3080 C ATOM 3628 N LYS C 71 9.942 -31.470 52.718 1.00 73.39 N ANISOU 3628 N LYS C 71 8338 9953 9592 -2073 -958 2039 N ATOM 3629 CA LYS C 71 8.759 -32.318 52.517 1.00 69.17 C ANISOU 3629 CA LYS C 71 7710 9509 9062 -1525 -557 1787 C ATOM 3630 C LYS C 71 8.009 -31.968 51.233 1.00 68.81 C ANISOU 3630 C LYS C 71 7599 9501 9044 -1437 -402 1895 C ATOM 3631 O LYS C 71 6.797 -31.738 51.235 1.00 67.87 O ANISOU 3631 O LYS C 71 7739 9159 8890 -1081 -290 1741 O ATOM 3632 CB LYS C 71 7.849 -32.260 53.742 1.00 68.58 C ANISOU 3632 CB LYS C 71 8100 9073 8884 -1157 -551 1485 C ATOM 3633 CG LYS C 71 8.506 -32.750 55.029 1.00 68.88 C ANISOU 3633 CG LYS C 71 8210 9092 8870 -1214 -679 1364 C ATOM 3634 CD LYS C 71 7.465 -32.920 56.128 1.00 68.53 C ANISOU 3634 CD LYS C 71 8498 8897 8643 -790 -566 1089 C ATOM 3635 CE LYS C 71 8.076 -33.122 57.506 1.00 69.02 C ANISOU 3635 CE LYS C 71 8790 8832 8603 -857 -765 968 C ATOM 3636 NZ LYS C 71 7.002 -33.128 58.539 1.00 68.79 N ANISOU 3636 NZ LYS C 71 9080 8757 8299 -418 -639 732 N ATOM 3637 N HIS C 72 8.761 -31.956 50.136 1.00 70.23 N ANISOU 3637 N HIS C 72 7374 10067 9242 -1743 -391 2179 N ATOM 3638 CA HIS C 72 8.339 -31.358 48.875 1.00 71.39 C ANISOU 3638 CA HIS C 72 7505 10230 9390 -1824 -352 2375 C ATOM 3639 C HIS C 72 8.929 -32.140 47.709 1.00 70.87 C ANISOU 3639 C HIS C 72 6797 10864 9268 -1856 -117 2547 C ATOM 3640 O HIS C 72 10.088 -32.557 47.749 1.00 72.51 O ANISOU 3640 O HIS C 72 6579 11576 9397 -2032 -140 2678 O ATOM 3641 CB HIS C 72 8.780 -29.881 48.854 1.00 76.54 C ANISOU 3641 CB HIS C 72 8588 10480 10012 -2345 -808 2660 C ATOM 3642 CG HIS C 72 8.820 -29.252 47.492 1.00 79.49 C ANISOU 3642 CG HIS C 72 8862 10995 10347 -2662 -862 3012 C ATOM 3643 ND1 HIS C 72 9.911 -28.537 47.040 1.00 84.91 N ANISOU 3643 ND1 HIS C 72 9422 11897 10943 -3399 -1185 3498 N ATOM 3644 CD2 HIS C 72 7.903 -29.207 46.495 1.00 78.65 C ANISOU 3644 CD2 HIS C 72 8762 10876 10247 -2399 -669 2997 C ATOM 3645 CE1 HIS C 72 9.668 -28.089 45.821 1.00 86.67 C ANISOU 3645 CE1 HIS C 72 9592 12232 11106 -3575 -1173 3767 C ATOM 3646 NE2 HIS C 72 8.458 -28.481 45.467 1.00 82.86 N ANISOU 3646 NE2 HIS C 72 9208 11580 10694 -2946 -861 3445 N ATOM 3647 N SER C 73 8.114 -32.349 46.682 1.00 69.26 N ANISOU 3647 N SER C 73 6523 10737 9055 -1616 97 2531 N ATOM 3648 CA SER C 73 8.537 -33.068 45.487 1.00 69.61 C ANISOU 3648 CA SER C 73 6060 11416 8972 -1525 307 2645 C ATOM 3649 C SER C 73 8.035 -32.361 44.234 1.00 70.90 C ANISOU 3649 C SER C 73 6263 11576 9099 -1652 336 2868 C ATOM 3650 O SER C 73 7.015 -31.670 44.273 1.00 70.41 O ANISOU 3650 O SER C 73 6634 10981 9139 -1599 256 2817 O ATOM 3651 CB SER C 73 8.017 -34.510 45.520 1.00 66.20 C ANISOU 3651 CB SER C 73 5550 11087 8515 -996 510 2324 C ATOM 3652 OG SER C 73 8.218 -35.167 44.277 1.00 66.67 O ANISOU 3652 OG SER C 73 5291 11642 8397 -775 660 2366 O ATOM 3653 N THR C 74 8.765 -32.517 43.131 1.00 73.34 N ANISOU 3653 N THR C 74 6111 12542 9212 -1771 439 3120 N ATOM 3654 CA THR C 74 8.282 -32.077 41.820 1.00 74.43 C ANISOU 3654 CA THR C 74 6245 12770 9266 -1834 506 3321 C ATOM 3655 C THR C 74 8.397 -33.227 40.825 1.00 73.80 C ANISOU 3655 C THR C 74 5763 13318 8961 -1388 784 3215 C ATOM 3656 O THR C 74 9.302 -34.055 40.926 1.00 75.04 O ANISOU 3656 O THR C 74 5529 14051 8930 -1165 873 3141 O ATOM 3657 CB THR C 74 9.012 -30.806 41.273 1.00 79.80 C ANISOU 3657 CB THR C 74 6867 13628 9826 -2545 267 3854 C ATOM 3658 OG1 THR C 74 10.408 -31.073 41.093 1.00 84.22 O ANISOU 3658 OG1 THR C 74 6777 15091 10131 -2807 313 4140 O ATOM 3659 CG2 THR C 74 8.854 -29.621 42.214 1.00 81.34 C ANISOU 3659 CG2 THR C 74 7678 13034 10194 -2953 -154 3933 C ATOM 3660 N LEU C 75 7.460 -33.287 39.885 1.00 72.48 N ANISOU 3660 N LEU C 75 5747 13014 8778 -1192 876 3179 N ATOM 3661 CA LEU C 75 7.495 -34.283 38.826 1.00 72.77 C ANISOU 3661 CA LEU C 75 5545 13558 8548 -755 1062 3074 C ATOM 3662 C LEU C 75 7.509 -33.575 37.483 1.00 76.05 C ANISOU 3662 C LEU C 75 5825 14305 8766 -989 1112 3419 C ATOM 3663 O LEU C 75 6.622 -32.769 37.187 1.00 75.45 O ANISOU 3663 O LEU C 75 6085 13730 8854 -1200 1014 3532 O ATOM 3664 CB LEU C 75 6.291 -35.227 38.911 1.00 68.67 C ANISOU 3664 CB LEU C 75 5377 12572 8143 -313 1064 2714 C ATOM 3665 CG LEU C 75 6.058 -36.143 37.703 1.00 68.73 C ANISOU 3665 CG LEU C 75 5368 12875 7870 115 1129 2599 C ATOM 3666 CD1 LEU C 75 7.162 -37.191 37.568 1.00 71.11 C ANISOU 3666 CD1 LEU C 75 5419 13784 7817 576 1163 2426 C ATOM 3667 CD2 LEU C 75 4.696 -36.795 37.769 1.00 64.47 C ANISOU 3667 CD2 LEU C 75 5234 11785 7477 300 1018 2388 C ATOM 3668 N HIS C 76 8.517 -33.883 36.675 1.00 80.29 N ANISOU 3668 N HIS C 76 5858 15748 8900 -902 1256 3590 N ATOM 3669 CA HIS C 76 8.651 -33.283 35.359 1.00 84.13 C ANISOU 3669 CA HIS C 76 6140 16725 9100 -1141 1327 3968 C ATOM 3670 C HIS C 76 8.300 -34.305 34.284 1.00 84.18 C ANISOU 3670 C HIS C 76 6133 17055 8795 -470 1498 3711 C ATOM 3671 O HIS C 76 8.688 -35.472 34.378 1.00 84.35 O ANISOU 3671 O HIS C 76 6043 17411 8595 159 1571 3372 O ATOM 3672 CB HIS C 76 10.081 -32.776 35.146 1.00 90.47 C ANISOU 3672 CB HIS C 76 6293 18528 9552 -1596 1362 4456 C ATOM 3673 CG HIS C 76 10.538 -31.778 36.168 1.00 91.97 C ANISOU 3673 CG HIS C 76 6554 18397 9992 -2342 1085 4759 C ATOM 3674 ND1 HIS C 76 10.875 -30.481 35.842 1.00 97.16 N ANISOU 3674 ND1 HIS C 76 7213 19118 10585 -3217 838 5364 N ATOM 3675 CD2 HIS C 76 10.730 -31.889 37.505 1.00 89.91 C ANISOU 3675 CD2 HIS C 76 6439 17714 10008 -2369 945 4555 C ATOM 3676 CE1 HIS C 76 11.248 -29.835 36.933 1.00 97.68 C ANISOU 3676 CE1 HIS C 76 7476 18763 10876 -3742 519 5504 C ATOM 3677 NE2 HIS C 76 11.166 -30.666 37.956 1.00 93.47 N ANISOU 3677 NE2 HIS C 76 7007 17954 10552 -3215 609 5005 N ATOM 3678 N ILE C 77 7.544 -33.868 33.280 1.00 84.53 N ANISOU 3678 N ILE C 77 6385 16928 8803 -574 1493 3855 N ATOM 3679 CA ILE C 77 7.407 -34.628 32.040 1.00 86.56 C ANISOU 3679 CA ILE C 77 6601 17644 8645 -39 1623 3725 C ATOM 3680 C ILE C 77 8.148 -33.881 30.942 1.00 92.70 C ANISOU 3680 C ILE C 77 6921 19323 8979 -384 1757 4236 C ATOM 3681 O ILE C 77 7.919 -32.686 30.730 1.00 93.73 O ANISOU 3681 O ILE C 77 7147 19209 9259 -1078 1636 4662 O ATOM 3682 CB ILE C 77 5.947 -34.810 31.581 1.00 82.84 C ANISOU 3682 CB ILE C 77 6686 16401 8387 121 1500 3528 C ATOM 3683 CG1 ILE C 77 4.976 -34.875 32.765 1.00 77.56 C ANISOU 3683 CG1 ILE C 77 6420 14800 8251 51 1330 3289 C ATOM 3684 CG2 ILE C 77 5.841 -36.025 30.646 1.00 84.37 C ANISOU 3684 CG2 ILE C 77 6996 16903 8156 836 1526 3217 C ATOM 3685 CD1 ILE C 77 4.927 -36.203 33.471 1.00 75.50 C ANISOU 3685 CD1 ILE C 77 6313 14371 8003 531 1262 2862 C ATOM 3686 N THR C 78 9.024 -34.593 30.243 1.00 97.66 N ANISOU 3686 N THR C 78 7084 21017 9005 134 1970 4199 N ATOM 3687 CA THR C 78 9.869 -33.984 29.225 1.00104.90 C ANISOU 3687 CA THR C 78 7404 23088 9367 -172 2147 4739 C ATOM 3688 C THR C 78 9.264 -34.187 27.828 1.00106.57 C ANISOU 3688 C THR C 78 7824 23447 9221 174 2223 4701 C ATOM 3689 O THR C 78 9.376 -35.273 27.249 1.00108.64 O ANISOU 3689 O THR C 78 8096 24159 9025 1073 2337 4308 O ATOM 3690 CB THR C 78 11.306 -34.545 29.304 1.00110.91 C ANISOU 3690 CB THR C 78 7366 25217 9558 231 2371 4787 C ATOM 3691 OG1 THR C 78 11.649 -34.783 30.677 1.00108.30 O ANISOU 3691 OG1 THR C 78 7025 24523 9600 207 2258 4585 O ATOM 3692 CG2 THR C 78 12.304 -33.569 28.693 1.00118.53 C ANISOU 3692 CG2 THR C 78 7545 27435 10055 -506 2498 5575 C ATOM 3693 N ALA C 79 8.632 -33.131 27.303 1.00106.39 N ANISOU 3693 N ALA C 79 8045 23000 9378 -509 2100 5099 N ATOM 3694 CA ALA C 79 7.866 -33.164 26.040 1.00107.02 C ANISOU 3694 CA ALA C 79 8432 23003 9226 -309 2104 5095 C ATOM 3695 C ALA C 79 6.653 -34.101 26.120 1.00101.36 C ANISOU 3695 C ALA C 79 8394 21307 8811 332 1953 4474 C ATOM 3696 O ALA C 79 6.753 -35.305 25.863 1.00102.11 O ANISOU 3696 O ALA C 79 8580 21649 8570 1157 1998 4025 O ATOM 3697 CB ALA C 79 8.764 -33.506 24.848 1.00114.47 C ANISOU 3697 CB ALA C 79 8807 25394 9293 78 2395 5283 C ATOM 3698 N THR C 80 5.508 -33.528 26.480 1.00 96.69 N ANISOU 3698 N THR C 80 8299 19633 8807 -54 1717 4478 N ATOM 3699 CA THR C 80 4.311 -34.303 26.811 1.00 91.64 C ANISOU 3699 CA THR C 80 8205 18092 8523 345 1529 4006 C ATOM 3700 C THR C 80 3.566 -34.820 25.588 1.00 92.76 C ANISOU 3700 C THR C 80 8676 18188 8379 725 1446 3874 C ATOM 3701 O THR C 80 3.450 -34.131 24.580 1.00 95.46 O ANISOU 3701 O THR C 80 8993 18773 8505 476 1471 4205 O ATOM 3702 CB THR C 80 3.337 -33.481 27.671 1.00 87.17 C ANISOU 3702 CB THR C 80 7946 16566 8608 -121 1326 4074 C ATOM 3703 OG1 THR C 80 3.182 -32.180 27.101 1.00 89.73 O ANISOU 3703 OG1 THR C 80 8314 16824 8954 -672 1244 4533 O ATOM 3704 CG2 THR C 80 3.867 -33.319 29.066 1.00 85.39 C ANISOU 3704 CG2 THR C 80 7576 16184 8686 -314 1334 4024 C ATOM 3705 N LEU C 81 3.056 -36.041 25.694 1.00 91.32 N ANISOU 3705 N LEU C 81 8866 17651 8179 1279 1281 3414 N ATOM 3706 CA LEU C 81 2.279 -36.652 24.622 1.00 92.86 C ANISOU 3706 CA LEU C 81 9497 17673 8112 1629 1087 3254 C ATOM 3707 C LEU C 81 0.784 -36.566 24.923 1.00 88.87 C ANISOU 3707 C LEU C 81 9389 16236 8141 1339 788 3234 C ATOM 3708 O LEU C 81 0.393 -36.153 26.016 1.00 85.37 O ANISOU 3708 O LEU C 81 8878 15346 8214 1001 764 3278 O ATOM 3709 CB LEU C 81 2.719 -38.105 24.417 1.00 95.53 C ANISOU 3709 CB LEU C 81 10105 18233 7960 2445 967 2785 C ATOM 3710 CG LEU C 81 4.076 -38.285 23.721 1.00102.13 C ANISOU 3710 CG LEU C 81 10537 20227 8041 2982 1259 2779 C ATOM 3711 CD1 LEU C 81 4.825 -39.512 24.237 1.00104.05 C ANISOU 3711 CD1 LEU C 81 10897 20680 7959 3781 1172 2300 C ATOM 3712 CD2 LEU C 81 3.924 -38.324 22.189 1.00106.90 C ANISOU 3712 CD2 LEU C 81 11310 21263 8045 3296 1261 2833 C ATOM 3713 N LEU C 82 -0.046 -36.933 23.946 1.00 90.33 N ANISOU 3713 N LEU C 82 9955 16215 8153 1489 555 3186 N ATOM 3714 CA LEU C 82 -1.504 -36.977 24.128 1.00 87.64 C ANISOU 3714 CA LEU C 82 9914 15156 8229 1241 235 3205 C ATOM 3715 C LEU C 82 -1.894 -38.148 25.022 1.00 85.93 C ANISOU 3715 C LEU C 82 9975 14506 8167 1374 -49 2904 C ATOM 3716 O LEU C 82 -2.893 -38.080 25.736 1.00 83.40 O ANISOU 3716 O LEU C 82 9663 13753 8274 1053 -216 2983 O ATOM 3717 CB LEU C 82 -2.225 -37.094 22.784 1.00 90.12 C ANISOU 3717 CB LEU C 82 10558 15419 8266 1327 10 3271 C ATOM 3718 CG LEU C 82 -2.006 -35.981 21.758 1.00 92.99 C ANISOU 3718 CG LEU C 82 10740 16164 8428 1145 207 3616 C ATOM 3719 CD1 LEU C 82 -1.994 -36.559 20.345 1.00 97.66 C ANISOU 3719 CD1 LEU C 82 11662 17033 8410 1527 77 3530 C ATOM 3720 CD2 LEU C 82 -3.043 -34.864 21.900 1.00 91.04 C ANISOU 3720 CD2 LEU C 82 10445 15480 8666 680 107 3921 C ATOM 3721 N ASP C 83 -1.094 -39.213 24.977 1.00 88.19 N ANISOU 3721 N ASP C 83 10491 14969 8050 1872 -129 2582 N ATOM 3722 CA ASP C 83 -1.279 -40.382 25.829 1.00 87.49 C ANISOU 3722 CA ASP C 83 10773 14440 8031 1997 -476 2305 C ATOM 3723 C ASP C 83 -1.076 -40.022 27.306 1.00 83.51 C ANISOU 3723 C ASP C 83 9891 13844 7994 1689 -273 2356 C ATOM 3724 O ASP C 83 -1.261 -40.864 28.189 1.00 82.69 O ANISOU 3724 O ASP C 83 10030 13382 8005 1672 -537 2198 O ATOM 3725 CB ASP C 83 -0.295 -41.482 25.407 1.00 92.22 C ANISOU 3725 CB ASP C 83 11752 15280 8009 2753 -622 1911 C ATOM 3726 CG ASP C 83 -0.851 -42.894 25.609 1.00 94.32 C ANISOU 3726 CG ASP C 83 12826 14867 8144 2926 -1293 1632 C ATOM 3727 OD1 ASP C 83 -1.146 -43.555 24.586 1.00 98.91 O ANISOU 3727 OD1 ASP C 83 14026 15273 8284 3261 -1699 1478 O ATOM 3728 OD2 ASP C 83 -0.986 -43.345 26.772 1.00 91.69 O ANISOU 3728 OD2 ASP C 83 12572 14157 8110 2699 -1470 1586 O ATOM 3729 N ASP C 84 -0.715 -38.767 27.569 1.00 81.58 N ANISOU 3729 N ASP C 84 9127 13882 7987 1413 131 2598 N ATOM 3730 CA ASP C 84 -0.401 -38.318 28.928 1.00 78.56 C ANISOU 3730 CA ASP C 84 8431 13433 7985 1165 316 2632 C ATOM 3731 C ASP C 84 -1.550 -37.643 29.686 1.00 75.36 C ANISOU 3731 C ASP C 84 7933 12627 8073 738 273 2817 C ATOM 3732 O ASP C 84 -1.446 -37.449 30.899 1.00 73.50 O ANISOU 3732 O ASP C 84 7540 12276 8110 597 359 2792 O ATOM 3733 CB ASP C 84 0.838 -37.411 28.934 1.00 79.73 C ANISOU 3733 CB ASP C 84 8134 14122 8036 1115 687 2782 C ATOM 3734 CG ASP C 84 2.112 -38.147 28.545 1.00 83.45 C ANISOU 3734 CG ASP C 84 8516 15205 7985 1629 787 2586 C ATOM 3735 OD1 ASP C 84 2.193 -39.379 28.746 1.00 84.34 O ANISOU 3735 OD1 ASP C 84 8970 15166 7908 2076 553 2240 O ATOM 3736 OD2 ASP C 84 3.044 -37.485 28.041 1.00 86.34 O ANISOU 3736 OD2 ASP C 84 8474 16249 8082 1595 1063 2800 O ATOM 3737 N THR C 85 -2.632 -37.285 28.998 1.00 75.34 N ANISOU 3737 N THR C 85 8012 12475 8137 597 137 2991 N ATOM 3738 CA THR C 85 -3.774 -36.663 29.676 1.00 73.39 C ANISOU 3738 CA THR C 85 7619 12002 8265 343 93 3152 C ATOM 3739 C THR C 85 -4.387 -37.615 30.700 1.00 72.09 C ANISOU 3739 C THR C 85 7499 11670 8223 241 -110 3069 C ATOM 3740 O THR C 85 -5.011 -38.620 30.348 1.00 73.30 O ANISOU 3740 O THR C 85 7909 11704 8237 178 -458 3068 O ATOM 3741 CB THR C 85 -4.835 -36.118 28.692 1.00 74.81 C ANISOU 3741 CB THR C 85 7834 12139 8451 273 -44 3367 C ATOM 3742 OG1 THR C 85 -4.307 -34.967 28.020 1.00 76.11 O ANISOU 3742 OG1 THR C 85 7944 12414 8560 262 139 3516 O ATOM 3743 CG2 THR C 85 -6.111 -35.709 29.432 1.00 74.33 C ANISOU 3743 CG2 THR C 85 7566 11994 8682 154 -127 3503 C ATOM 3744 N ALA C 86 -4.175 -37.280 31.971 1.00 70.09 N ANISOU 3744 N ALA C 86 7035 11404 8192 177 60 3033 N ATOM 3745 CA ALA C 86 -4.529 -38.138 33.100 1.00 69.35 C ANISOU 3745 CA ALA C 86 6947 11230 8173 43 -86 2980 C ATOM 3746 C ALA C 86 -4.445 -37.355 34.409 1.00 67.55 C ANISOU 3746 C ALA C 86 6440 11045 8182 18 163 2976 C ATOM 3747 O ALA C 86 -4.080 -36.176 34.409 1.00 67.15 O ANISOU 3747 O ALA C 86 6284 10997 8233 106 378 2996 O ATOM 3748 CB ALA C 86 -3.599 -39.344 33.151 1.00 69.99 C ANISOU 3748 CB ALA C 86 7357 11204 8032 175 -250 2746 C ATOM 3749 N THR C 87 -4.801 -38.007 35.515 1.00 67.09 N ANISOU 3749 N THR C 87 6327 10997 8166 -125 74 2971 N ATOM 3750 CA THR C 87 -4.571 -37.438 36.842 1.00 66.03 C ANISOU 3750 CA THR C 87 6002 10905 8181 -91 290 2909 C ATOM 3751 C THR C 87 -3.297 -38.008 37.457 1.00 64.66 C ANISOU 3751 C THR C 87 5985 10605 7978 -63 319 2697 C ATOM 3752 O THR C 87 -2.999 -39.197 37.320 1.00 65.06 O ANISOU 3752 O THR C 87 6285 10557 7878 -96 85 2612 O ATOM 3753 CB THR C 87 -5.767 -37.621 37.816 1.00 67.28 C ANISOU 3753 CB THR C 87 5898 11315 8350 -232 239 3073 C ATOM 3754 OG1 THR C 87 -6.280 -38.957 37.729 1.00 69.36 O ANISOU 3754 OG1 THR C 87 6275 11607 8471 -567 -103 3215 O ATOM 3755 CG2 THR C 87 -6.878 -36.640 37.492 1.00 69.22 C ANISOU 3755 CG2 THR C 87 5865 11816 8621 -69 312 3239 C ATOM 3756 N TYR C 88 -2.547 -37.138 38.123 1.00 63.62 N ANISOU 3756 N TYR C 88 5759 10451 7962 19 543 2612 N ATOM 3757 CA TYR C 88 -1.265 -37.503 38.708 1.00 62.76 C ANISOU 3757 CA TYR C 88 5714 10303 7828 54 586 2439 C ATOM 3758 C TYR C 88 -1.313 -37.384 40.237 1.00 62.12 C ANISOU 3758 C TYR C 88 5571 10174 7856 -10 642 2383 C ATOM 3759 O TYR C 88 -1.290 -36.287 40.812 1.00 62.15 O ANISOU 3759 O TYR C 88 5510 10135 7970 28 776 2388 O ATOM 3760 CB TYR C 88 -0.123 -36.686 38.081 1.00 63.07 C ANISOU 3760 CB TYR C 88 5687 10437 7839 109 738 2446 C ATOM 3761 CG TYR C 88 0.156 -37.049 36.632 1.00 64.00 C ANISOU 3761 CG TYR C 88 5851 10731 7734 232 702 2473 C ATOM 3762 CD1 TYR C 88 -0.533 -36.431 35.585 1.00 64.19 C ANISOU 3762 CD1 TYR C 88 5883 10761 7745 196 702 2641 C ATOM 3763 CD2 TYR C 88 1.103 -38.017 36.309 1.00 65.04 C ANISOU 3763 CD2 TYR C 88 6045 11054 7613 465 647 2310 C ATOM 3764 CE1 TYR C 88 -0.289 -36.770 34.257 1.00 65.28 C ANISOU 3764 CE1 TYR C 88 6088 11091 7626 330 668 2662 C ATOM 3765 CE2 TYR C 88 1.358 -38.360 34.986 1.00 66.93 C ANISOU 3765 CE2 TYR C 88 6353 11525 7553 696 615 2297 C ATOM 3766 CZ TYR C 88 0.659 -37.734 33.964 1.00 67.16 C ANISOU 3766 CZ TYR C 88 6386 11558 7575 597 636 2481 C ATOM 3767 OH TYR C 88 0.920 -38.082 32.655 1.00 69.77 O ANISOU 3767 OH TYR C 88 6806 12148 7556 848 605 2463 O ATOM 3768 N ILE C 89 -1.398 -38.545 40.875 1.00 62.00 N ANISOU 3768 N ILE C 89 5661 10129 7766 -102 473 2333 N ATOM 3769 CA ILE C 89 -1.570 -38.651 42.309 1.00 61.58 C ANISOU 3769 CA ILE C 89 5559 10092 7748 -200 495 2316 C ATOM 3770 C ILE C 89 -0.204 -38.812 42.973 1.00 60.84 C ANISOU 3770 C ILE C 89 5561 9883 7672 -132 516 2122 C ATOM 3771 O ILE C 89 0.641 -39.583 42.511 1.00 61.12 O ANISOU 3771 O ILE C 89 5743 9874 7604 -25 384 2006 O ATOM 3772 CB ILE C 89 -2.515 -39.830 42.646 1.00 62.85 C ANISOU 3772 CB ILE C 89 5786 10319 7775 -469 229 2472 C ATOM 3773 CG1 ILE C 89 -3.820 -39.688 41.855 1.00 64.26 C ANISOU 3773 CG1 ILE C 89 5795 10711 7911 -578 172 2718 C ATOM 3774 CG2 ILE C 89 -2.807 -39.897 44.143 1.00 63.57 C ANISOU 3774 CG2 ILE C 89 5759 10560 7834 -605 281 2521 C ATOM 3775 CD1 ILE C 89 -4.684 -40.933 41.822 1.00 66.53 C ANISOU 3775 CD1 ILE C 89 6194 11060 8026 -988 -221 2968 C ATOM 3776 N CYS C 90 0.011 -38.054 44.042 1.00 60.53 N ANISOU 3776 N CYS C 90 5448 9828 7722 -129 656 2077 N ATOM 3777 CA CYS C 90 1.227 -38.153 44.828 1.00 60.38 C ANISOU 3777 CA CYS C 90 5489 9730 7724 -119 646 1930 C ATOM 3778 C CYS C 90 0.911 -38.799 46.167 1.00 60.34 C ANISOU 3778 C CYS C 90 5564 9699 7664 -223 562 1901 C ATOM 3779 O CYS C 90 0.107 -38.276 46.936 1.00 60.67 O ANISOU 3779 O CYS C 90 5529 9834 7690 -236 665 1959 O ATOM 3780 CB CYS C 90 1.837 -36.765 45.037 1.00 60.82 C ANISOU 3780 CB CYS C 90 5499 9722 7888 -115 771 1926 C ATOM 3781 SG CYS C 90 3.043 -36.675 46.384 1.00 62.34 S ANISOU 3781 SG CYS C 90 5752 9825 8110 -189 718 1800 S ATOM 3782 N VAL C 91 1.537 -39.941 46.440 1.00 60.66 N ANISOU 3782 N VAL C 91 5778 9650 7621 -246 353 1813 N ATOM 3783 CA VAL C 91 1.353 -40.621 47.724 1.00 61.41 C ANISOU 3783 CA VAL C 91 6003 9695 7635 -408 217 1820 C ATOM 3784 C VAL C 91 2.641 -40.690 48.540 1.00 61.25 C ANISOU 3784 C VAL C 91 6064 9567 7641 -316 175 1638 C ATOM 3785 O VAL C 91 3.745 -40.773 47.985 1.00 61.41 O ANISOU 3785 O VAL C 91 6064 9598 7670 -119 139 1514 O ATOM 3786 CB VAL C 91 0.729 -42.044 47.584 1.00 63.03 C ANISOU 3786 CB VAL C 91 6475 9808 7666 -624 -149 1945 C ATOM 3787 CG1 VAL C 91 -0.475 -42.012 46.666 1.00 63.97 C ANISOU 3787 CG1 VAL C 91 6486 10070 7748 -768 -166 2165 C ATOM 3788 CG2 VAL C 91 1.747 -43.055 47.079 1.00 64.30 C ANISOU 3788 CG2 VAL C 91 6991 9710 7731 -404 -469 1750 C ATOM 3789 N VAL C 92 2.481 -40.642 49.860 1.00 61.54 N ANISOU 3789 N VAL C 92 6144 9595 7644 -443 182 1644 N ATOM 3790 CA VAL C 92 3.602 -40.700 50.787 1.00 61.73 C ANISOU 3790 CA VAL C 92 6258 9513 7684 -399 109 1493 C ATOM 3791 C VAL C 92 3.379 -41.870 51.738 1.00 63.08 C ANISOU 3791 C VAL C 92 6689 9585 7693 -574 -157 1531 C ATOM 3792 O VAL C 92 2.258 -42.089 52.209 1.00 64.23 O ANISOU 3792 O VAL C 92 6831 9862 7710 -817 -157 1724 O ATOM 3793 CB VAL C 92 3.757 -39.374 51.577 1.00 61.54 C ANISOU 3793 CB VAL C 92 6150 9496 7737 -388 308 1450 C ATOM 3794 CG1 VAL C 92 4.912 -39.455 52.561 1.00 61.98 C ANISOU 3794 CG1 VAL C 92 6306 9441 7801 -404 179 1324 C ATOM 3795 CG2 VAL C 92 3.978 -38.214 50.632 1.00 61.22 C ANISOU 3795 CG2 VAL C 92 5969 9464 7828 -313 450 1472 C ATOM 3796 N GLY C 93 4.444 -42.627 52.002 1.00 63.82 N ANISOU 3796 N GLY C 93 6986 9512 7750 -454 -412 1383 N ATOM 3797 CA GLY C 93 4.392 -43.766 52.919 1.00 65.61 C ANISOU 3797 CA GLY C 93 7573 9547 7807 -624 -764 1417 C ATOM 3798 C GLY C 93 5.159 -43.477 54.190 1.00 65.77 C ANISOU 3798 C GLY C 93 7604 9544 7843 -619 -745 1312 C ATOM 3799 O GLY C 93 6.325 -43.086 54.143 1.00 65.53 O ANISOU 3799 O GLY C 93 7447 9538 7915 -377 -710 1140 O ATOM 3800 N ASP C 94 4.506 -43.665 55.332 1.00 66.91 N ANISOU 3800 N ASP C 94 7863 9716 7842 -917 -781 1454 N ATOM 3801 CA ASP C 94 5.112 -43.316 56.617 1.00 67.26 C ANISOU 3801 CA ASP C 94 7953 9740 7863 -924 -758 1359 C ATOM 3802 C ASP C 94 6.065 -44.374 57.175 1.00 68.67 C ANISOU 3802 C ASP C 94 8480 9647 7964 -879 -1179 1257 C ATOM 3803 O ASP C 94 6.901 -44.068 58.025 1.00 68.92 O ANISOU 3803 O ASP C 94 8522 9641 8023 -806 -1199 1131 O ATOM 3804 CB ASP C 94 4.050 -42.897 57.653 1.00 68.41 C ANISOU 3804 CB ASP C 94 8028 10155 7811 -1155 -557 1530 C ATOM 3805 CG ASP C 94 2.955 -43.938 57.848 1.00 70.94 C ANISOU 3805 CG ASP C 94 8455 10633 7866 -1564 -752 1859 C ATOM 3806 OD1 ASP C 94 3.046 -45.050 57.282 1.00 72.24 O ANISOU 3806 OD1 ASP C 94 8912 10525 8010 -1710 -1149 1937 O ATOM 3807 OD2 ASP C 94 1.993 -43.635 58.583 1.00 72.84 O ANISOU 3807 OD2 ASP C 94 8505 11310 7862 -1738 -548 2063 O ATOM 3808 N ARG C 95 5.939 -45.612 56.701 1.00 70.21 N ANISOU 3808 N ARG C 95 9026 9613 8036 -902 -1582 1307 N ATOM 3809 CA ARG C 95 6.835 -46.690 57.128 1.00 72.43 C ANISOU 3809 CA ARG C 95 9755 9567 8198 -738 -2083 1174 C ATOM 3810 C ARG C 95 7.267 -47.588 55.973 1.00 74.31 C ANISOU 3810 C ARG C 95 10294 9576 8366 -326 -2454 1014 C ATOM 3811 O ARG C 95 6.507 -47.809 55.030 1.00 74.84 O ANISOU 3811 O ARG C 95 10440 9600 8397 -405 -2494 1117 O ATOM 3812 CB ARG C 95 6.196 -47.537 58.232 1.00 74.79 C ANISOU 3812 CB ARG C 95 10488 9678 8249 -1227 -2435 1421 C ATOM 3813 CG ARG C 95 5.897 -46.769 59.507 1.00 73.51 C ANISOU 3813 CG ARG C 95 10087 9801 8042 -1504 -2108 1531 C ATOM 3814 CD ARG C 95 6.095 -47.622 60.751 1.00 74.89 C ANISOU 3814 CD ARG C 95 10714 9763 7979 -1773 -2525 1636 C ATOM 3815 NE ARG C 95 5.287 -47.180 61.889 1.00 74.95 N ANISOU 3815 NE ARG C 95 10557 10148 7771 -2176 -2264 1882 N ATOM 3816 CZ ARG C 95 5.022 -45.915 62.217 1.00 72.96 C ANISOU 3816 CZ ARG C 95 9868 10293 7560 -2043 -1725 1812 C ATOM 3817 NH1 ARG C 95 4.263 -45.669 63.272 1.00 74.83 N ANISOU 3817 NH1 ARG C 95 10012 10939 7482 -2301 -1540 2020 N ATOM 3818 NH2 ARG C 95 5.510 -44.898 61.516 1.00 70.03 N ANISOU 3818 NH2 ARG C 95 9199 9929 7482 -1639 -1415 1548 N ATOM 3819 N GLY C 96 8.493 -48.096 56.054 1.00 76.12 N ANISOU 3819 N GLY C 96 10696 9698 8529 176 -2746 749 N ATOM 3820 CA GLY C 96 9.009 -49.035 55.065 1.00 78.95 C ANISOU 3820 CA GLY C 96 11428 9869 8701 771 -3167 522 C ATOM 3821 C GLY C 96 8.900 -50.466 55.549 1.00 83.15 C ANISOU 3821 C GLY C 96 12866 9780 8948 749 -3948 520 C ATOM 3822 O GLY C 96 9.898 -51.186 55.612 1.00 86.50 O ANISOU 3822 O GLY C 96 13643 10034 9188 1376 -4379 236 O ATOM 3823 N SER C 97 7.681 -50.866 55.899 1.00 83.70 N ANISOU 3823 N SER C 97 13308 9554 8939 16 -4170 870 N ATOM 3824 CA SER C 97 7.402 -52.214 56.383 1.00 88.72 C ANISOU 3824 CA SER C 97 14896 9540 9272 -249 -5013 1002 C ATOM 3825 C SER C 97 6.021 -52.634 55.914 1.00 90.18 C ANISOU 3825 C SER C 97 15399 9526 9338 -951 -5274 1402 C ATOM 3826 O SER C 97 5.628 -52.336 54.789 1.00 89.07 O ANISOU 3826 O SER C 97 15047 9527 9268 -820 -5068 1373 O ATOM 3827 CB SER C 97 7.458 -52.248 57.909 1.00 89.18 C ANISOU 3827 CB SER C 97 15012 9576 9297 -713 -5072 1188 C ATOM 3828 OG SER C 97 6.392 -51.495 58.463 1.00 87.04 O ANISOU 3828 OG SER C 97 14230 9735 9106 -1470 -4568 1581 O ATOM 3829 N ALA C 98 5.288 -53.327 56.779 1.00 93.44 N ANISOU 3829 N ALA C 98 16298 9667 9539 -1750 -5755 1823 N ATOM 3830 CA ALA C 98 3.886 -53.636 56.527 1.00 95.67 C ANISOU 3830 CA ALA C 98 16713 9961 9678 -2636 -5978 2357 C ATOM 3831 C ALA C 98 2.987 -52.724 57.359 1.00 93.22 C ANISOU 3831 C ALA C 98 15549 10434 9435 -3320 -5288 2775 C ATOM 3832 O ALA C 98 1.902 -52.334 56.922 1.00 92.82 O ANISOU 3832 O ALA C 98 15053 10826 9388 -3773 -5009 3113 O ATOM 3833 CB ALA C 98 3.598 -55.101 56.831 1.00102.73 C ANISOU 3833 CB ALA C 98 18767 10081 10186 -3172 -7104 2653 C ATOM 3834 N LEU C 99 3.470 -52.367 58.548 1.00 92.13 N ANISOU 3834 N LEU C 99 15187 10504 9313 -3297 -5024 2721 N ATOM 3835 CA LEU C 99 2.681 -51.650 59.552 1.00 91.43 C ANISOU 3835 CA LEU C 99 14453 11140 9147 -3851 -4485 3088 C ATOM 3836 C LEU C 99 2.518 -50.146 59.266 1.00 86.24 C ANISOU 3836 C LEU C 99 12860 11145 8761 -3462 -3544 2897 C ATOM 3837 O LEU C 99 2.175 -49.367 60.167 1.00 85.43 O ANISOU 3837 O LEU C 99 12260 11609 8589 -3586 -3048 3007 O ATOM 3838 CB LEU C 99 3.278 -51.887 60.947 1.00 92.80 C ANISOU 3838 CB LEU C 99 14869 11217 9172 -3944 -4641 3082 C ATOM 3839 N GLY C 100 2.749 -49.755 58.011 1.00 83.38 N ANISOU 3839 N GLY C 100 12335 10692 8654 -2970 -3357 2615 N ATOM 3840 CA GLY C 100 2.602 -48.364 57.577 1.00 79.23 C ANISOU 3840 CA GLY C 100 11060 10666 8378 -2623 -2594 2453 C ATOM 3841 C GLY C 100 1.413 -48.128 56.658 1.00 79.50 C ANISOU 3841 C GLY C 100 10772 11034 8400 -2877 -2428 2727 C ATOM 3842 O GLY C 100 1.009 -49.019 55.908 1.00 81.99 O ANISOU 3842 O GLY C 100 11483 11056 8612 -3143 -2923 2906 O ATOM 3843 N ARG C 103 0.854 -46.922 56.720 1.00 77.54 N ANISOU 3843 N ARG C 103 9865 11369 8227 -2762 -1792 2749 N ATOM 3844 CA ARG C 103 -0.286 -46.549 55.888 1.00 78.04 C ANISOU 3844 CA ARG C 103 9527 11850 8276 -2916 -1580 2996 C ATOM 3845 C ARG C 103 0.099 -45.468 54.871 1.00 74.18 C ANISOU 3845 C ARG C 103 8742 11334 8110 -2318 -1158 2645 C ATOM 3846 O ARG C 103 1.011 -44.671 55.121 1.00 71.58 O ANISOU 3846 O ARG C 103 8329 10903 7965 -1879 -883 2303 O ATOM 3847 CB ARG C 103 -1.457 -46.086 56.760 1.00 80.75 C ANISOU 3847 CB ARG C 103 9336 13022 8323 -3241 -1245 3375 C ATOM 3848 N LEU C 104 -0.598 -45.450 53.731 1.00 74.35 N ANISOU 3848 N LEU C 104 8630 11446 8173 -2376 -1163 2778 N ATOM 3849 CA LEU C 104 -0.308 -44.508 52.641 1.00 71.03 C ANISOU 3849 CA LEU C 104 7976 10993 8019 -1891 -830 2514 C ATOM 3850 C LEU C 104 -1.216 -43.272 52.641 1.00 70.84 C ANISOU 3850 C LEU C 104 7391 11523 8001 -1762 -332 2606 C ATOM 3851 O LEU C 104 -2.432 -43.374 52.845 1.00 73.62 O ANISOU 3851 O LEU C 104 7448 12395 8129 -2074 -297 2965 O ATOM 3852 CB LEU C 104 -0.396 -45.209 51.283 1.00 71.38 C ANISOU 3852 CB LEU C 104 8298 10735 8087 -1914 -1172 2535 C ATOM 3853 CG LEU C 104 0.581 -46.332 50.943 1.00 71.93 C ANISOU 3853 CG LEU C 104 9012 10213 8107 -1756 -1700 2322 C ATOM 3854 CD1 LEU C 104 0.295 -46.831 49.545 1.00 72.84 C ANISOU 3854 CD1 LEU C 104 9394 10104 8176 -1694 -1996 2331 C ATOM 3855 CD2 LEU C 104 2.019 -45.867 51.048 1.00 69.28 C ANISOU 3855 CD2 LEU C 104 8636 9757 7931 -1183 -1494 1907 C ATOM 3856 N HIS C 105 -0.605 -42.113 52.401 1.00 68.27 N ANISOU 3856 N HIS C 105 6935 11114 7889 -1296 -1 2305 N ATOM 3857 CA HIS C 105 -1.311 -40.835 52.370 1.00 68.64 C ANISOU 3857 CA HIS C 105 6619 11531 7930 -1019 385 2302 C ATOM 3858 C HIS C 105 -1.430 -40.347 50.941 1.00 67.10 C ANISOU 3858 C HIS C 105 6336 11235 7924 -843 454 2265 C ATOM 3859 O HIS C 105 -0.424 -40.077 50.296 1.00 65.28 O ANISOU 3859 O HIS C 105 6259 10647 7899 -669 439 2056 O ATOM 3860 CB HIS C 105 -0.566 -39.791 53.199 1.00 68.05 C ANISOU 3860 CB HIS C 105 6619 11325 7912 -677 582 2018 C ATOM 3861 CG HIS C 105 -0.370 -40.180 54.630 1.00 70.02 C ANISOU 3861 CG HIS C 105 6985 11660 7961 -801 525 2019 C ATOM 3862 ND1 HIS C 105 0.667 -40.989 55.046 1.00 69.30 N ANISOU 3862 ND1 HIS C 105 7197 11200 7935 -975 260 1930 N ATOM 3863 CD2 HIS C 105 -1.075 -39.867 55.742 1.00 73.02 C ANISOU 3863 CD2 HIS C 105 7217 12502 8025 -723 693 2095 C ATOM 3864 CE1 HIS C 105 0.587 -41.164 56.352 1.00 71.51 C ANISOU 3864 CE1 HIS C 105 7541 11646 7985 -1076 251 1970 C ATOM 3865 NE2 HIS C 105 -0.460 -40.493 56.799 1.00 74.17 N ANISOU 3865 NE2 HIS C 105 7597 12514 8071 -927 528 2073 N ATOM 3866 N PHE C 106 -2.661 -40.216 50.461 1.00 68.67 N ANISOU 3866 N PHE C 106 6240 11839 8012 -899 528 2505 N ATOM 3867 CA PHE C 106 -2.926 -39.917 49.059 1.00 67.59 C ANISOU 3867 CA PHE C 106 6038 11626 8016 -799 536 2527 C ATOM 3868 C PHE C 106 -3.243 -38.449 48.815 1.00 67.80 C ANISOU 3868 C PHE C 106 5881 11778 8102 -354 830 2413 C ATOM 3869 O PHE C 106 -4.073 -37.857 49.506 1.00 70.48 O ANISOU 3869 O PHE C 106 5976 12560 8243 -130 1009 2467 O ATOM 3870 CB PHE C 106 -4.094 -40.768 48.556 1.00 70.01 C ANISOU 3870 CB PHE C 106 6181 12262 8159 -1194 327 2902 C ATOM 3871 CG PHE C 106 -3.795 -42.232 48.495 1.00 70.06 C ANISOU 3871 CG PHE C 106 6576 11952 8093 -1648 -136 3020 C ATOM 3872 CD1 PHE C 106 -3.672 -42.978 49.658 1.00 71.13 C ANISOU 3872 CD1 PHE C 106 6854 12115 8056 -1964 -318 3130 C ATOM 3873 CD2 PHE C 106 -3.651 -42.868 47.271 1.00 69.46 C ANISOU 3873 CD2 PHE C 106 6805 11516 8071 -1726 -448 3014 C ATOM 3874 CE1 PHE C 106 -3.396 -44.324 49.600 1.00 72.74 C ANISOU 3874 CE1 PHE C 106 7559 11916 8162 -2359 -858 3234 C ATOM 3875 CE2 PHE C 106 -3.374 -44.220 47.202 1.00 70.69 C ANISOU 3875 CE2 PHE C 106 7486 11274 8100 -2045 -987 3076 C ATOM 3876 CZ PHE C 106 -3.248 -44.950 48.369 1.00 72.86 C ANISOU 3876 CZ PHE C 106 7959 11505 8219 -2371 -1221 3190 C ATOM 3877 N GLY C 107 -2.585 -37.867 47.818 1.00 65.86 N ANISOU 3877 N GLY C 107 5781 11173 8070 -192 843 2266 N ATOM 3878 CA GLY C 107 -2.927 -36.527 47.356 1.00 66.56 C ANISOU 3878 CA GLY C 107 5821 11263 8207 166 993 2205 C ATOM 3879 C GLY C 107 -4.239 -36.535 46.597 1.00 68.30 C ANISOU 3879 C GLY C 107 5747 11872 8332 206 1013 2428 C ATOM 3880 O GLY C 107 -4.720 -37.593 46.178 1.00 68.53 O ANISOU 3880 O GLY C 107 5654 12081 8305 -141 868 2648 O ATOM 3881 N ALA C 108 -4.823 -35.351 46.428 1.00 70.22 N ANISOU 3881 N ALA C 108 5931 12220 8530 635 1123 2379 N ATOM 3882 CA ALA C 108 -6.056 -35.199 45.658 1.00 72.37 C ANISOU 3882 CA ALA C 108 5888 12904 8705 762 1137 2582 C ATOM 3883 C ALA C 108 -5.783 -35.299 44.159 1.00 70.33 C ANISOU 3883 C ALA C 108 5761 12315 8647 577 1013 2642 C ATOM 3884 O ALA C 108 -6.715 -35.335 43.356 1.00 71.79 O ANISOU 3884 O ALA C 108 5720 12778 8780 586 967 2833 O ATOM 3885 CB ALA C 108 -6.739 -33.883 45.993 1.00 75.89 C ANISOU 3885 CB ALA C 108 6297 13556 8982 1429 1245 2459 C ATOM 3886 N GLY C 109 -4.500 -35.341 43.797 1.00 67.58 N ANISOU 3886 N GLY C 109 5738 11463 8478 424 960 2498 N ATOM 3887 CA GLY C 109 -4.064 -35.507 42.408 1.00 66.22 C ANISOU 3887 CA GLY C 109 5684 11065 8413 278 869 2544 C ATOM 3888 C GLY C 109 -4.101 -34.231 41.590 1.00 67.07 C ANISOU 3888 C GLY C 109 5908 10991 8584 506 883 2543 C ATOM 3889 O GLY C 109 -4.829 -33.294 41.923 1.00 69.31 O ANISOU 3889 O GLY C 109 6180 11345 8808 848 907 2524 O ATOM 3890 N THR C 110 -3.307 -34.189 40.523 1.00 66.03 N ANISOU 3890 N THR C 110 5917 10656 8517 356 838 2569 N ATOM 3891 CA THR C 110 -3.394 -33.101 39.549 1.00 67.58 C ANISOU 3891 CA THR C 110 6248 10691 8738 453 789 2655 C ATOM 3892 C THR C 110 -3.961 -33.628 38.236 1.00 67.57 C ANISOU 3892 C THR C 110 6147 10840 8685 382 734 2802 C ATOM 3893 O THR C 110 -3.548 -34.678 37.753 1.00 66.37 O ANISOU 3893 O THR C 110 5981 10761 8475 210 704 2799 O ATOM 3894 CB THR C 110 -2.029 -32.409 39.289 1.00 67.78 C ANISOU 3894 CB THR C 110 6491 10456 8805 260 755 2668 C ATOM 3895 OG1 THR C 110 -1.518 -31.865 40.510 1.00 68.77 O ANISOU 3895 OG1 THR C 110 6781 10378 8970 282 724 2549 O ATOM 3896 CG2 THR C 110 -2.183 -31.275 38.289 1.00 69.94 C ANISOU 3896 CG2 THR C 110 6970 10538 9067 264 628 2829 C ATOM 3897 N GLN C 111 -4.918 -32.898 37.677 1.00 69.50 N ANISOU 3897 N GLN C 111 6380 11113 8915 577 672 2907 N ATOM 3898 CA GLN C 111 -5.478 -33.231 36.377 1.00 70.08 C ANISOU 3898 CA GLN C 111 6399 11295 8934 509 581 3061 C ATOM 3899 C GLN C 111 -4.610 -32.567 35.312 1.00 70.38 C ANISOU 3899 C GLN C 111 6674 11110 8957 403 555 3127 C ATOM 3900 O GLN C 111 -4.504 -31.343 35.266 1.00 72.34 O ANISOU 3900 O GLN C 111 7129 11118 9238 489 488 3172 O ATOM 3901 CB GLN C 111 -6.938 -32.759 36.306 1.00 72.63 C ANISOU 3901 CB GLN C 111 6531 11848 9216 789 512 3172 C ATOM 3902 CG GLN C 111 -7.579 -32.733 34.918 1.00 74.23 C ANISOU 3902 CG GLN C 111 6726 12106 9372 762 370 3351 C ATOM 3903 CD GLN C 111 -8.934 -32.013 34.909 1.00 78.46 C ANISOU 3903 CD GLN C 111 7052 12909 9852 1151 292 3451 C ATOM 3904 OE1 GLN C 111 -9.239 -31.246 33.990 1.00 79.78 O ANISOU 3904 OE1 GLN C 111 7374 12933 10006 1316 166 3530 O ATOM 3905 NE2 GLN C 111 -9.748 -32.259 35.939 1.00 79.96 N ANISOU 3905 NE2 GLN C 111 6861 13562 9957 1330 360 3465 N ATOM 3906 N LEU C 112 -3.964 -33.376 34.479 1.00 69.39 N ANISOU 3906 N LEU C 112 6557 11083 8725 227 567 3145 N ATOM 3907 CA LEU C 112 -3.141 -32.840 33.397 1.00 70.55 C ANISOU 3907 CA LEU C 112 6822 11223 8759 105 578 3269 C ATOM 3908 C LEU C 112 -3.850 -32.982 32.055 1.00 71.77 C ANISOU 3908 C LEU C 112 7023 11454 8791 139 471 3399 C ATOM 3909 O LEU C 112 -4.334 -34.067 31.717 1.00 71.44 O ANISOU 3909 O LEU C 112 6956 11526 8661 175 389 3347 O ATOM 3910 CB LEU C 112 -1.770 -33.523 33.353 1.00 70.02 C ANISOU 3910 CB LEU C 112 6686 11372 8545 5 696 3194 C ATOM 3911 CG LEU C 112 -0.744 -32.937 32.377 1.00 72.03 C ANISOU 3911 CG LEU C 112 6918 11855 8595 -168 756 3392 C ATOM 3912 CD1 LEU C 112 -0.170 -31.631 32.902 1.00 73.37 C ANISOU 3912 CD1 LEU C 112 7160 11847 8871 -452 709 3570 C ATOM 3913 CD2 LEU C 112 0.365 -33.932 32.108 1.00 72.38 C ANISOU 3913 CD2 LEU C 112 6794 12340 8366 -64 881 3286 C ATOM 3914 N ILE C 113 -3.917 -31.878 31.309 1.00 73.69 N ANISOU 3914 N ILE C 113 7407 11583 9010 93 400 3587 N ATOM 3915 CA ILE C 113 -4.529 -31.866 29.979 1.00 75.14 C ANISOU 3915 CA ILE C 113 7665 11825 9059 113 284 3736 C ATOM 3916 C ILE C 113 -3.516 -31.418 28.932 1.00 77.11 C ANISOU 3916 C ILE C 113 8010 12214 9075 -101 328 3926 C ATOM 3917 O ILE C 113 -2.987 -30.305 29.003 1.00 79.06 O ANISOU 3917 O ILE C 113 8383 12318 9338 -312 280 4109 O ATOM 3918 CB ILE C 113 -5.754 -30.925 29.893 1.00 76.87 C ANISOU 3918 CB ILE C 113 7970 11839 9397 297 99 3839 C ATOM 3919 CG1 ILE C 113 -6.707 -31.140 31.074 1.00 76.67 C ANISOU 3919 CG1 ILE C 113 7738 11868 9526 549 99 3703 C ATOM 3920 CG2 ILE C 113 -6.480 -31.117 28.559 1.00 78.20 C ANISOU 3920 CG2 ILE C 113 8180 12101 9430 312 -46 3985 C ATOM 3921 CD1 ILE C 113 -7.743 -30.029 31.245 1.00 80.55 C ANISOU 3921 CD1 ILE C 113 8291 12246 10067 918 -61 3747 C ATOM 3922 N VAL C 114 -3.256 -32.287 27.960 1.00 77.38 N ANISOU 3922 N VAL C 114 8015 12550 8835 -57 372 3908 N ATOM 3923 CA VAL C 114 -2.346 -31.970 26.867 1.00 80.01 C ANISOU 3923 CA VAL C 114 8347 13223 8829 -208 453 4117 C ATOM 3924 C VAL C 114 -3.146 -31.557 25.626 1.00 82.06 C ANISOU 3924 C VAL C 114 8799 13410 8970 -217 283 4309 C ATOM 3925 O VAL C 114 -3.809 -32.387 24.998 1.00 82.03 O ANISOU 3925 O VAL C 114 8878 13439 8850 -14 185 4197 O ATOM 3926 CB VAL C 114 -1.394 -33.151 26.568 1.00 80.37 C ANISOU 3926 CB VAL C 114 8253 13764 8521 -4 621 3937 C ATOM 3927 CG1 VAL C 114 -0.623 -32.921 25.280 1.00 84.51 C ANISOU 3927 CG1 VAL C 114 8702 14840 8569 -54 730 4165 C ATOM 3928 CG2 VAL C 114 -0.434 -33.348 27.722 1.00 79.05 C ANISOU 3928 CG2 VAL C 114 7871 13724 8441 -30 777 3814 C ATOM 3929 N ILE C 115 -3.102 -30.267 25.296 1.00 84.34 N ANISOU 3929 N ILE C 115 9230 13539 9275 -481 173 4615 N ATOM 3930 CA ILE C 115 -3.774 -29.763 24.097 1.00 86.68 C ANISOU 3930 CA ILE C 115 9745 13753 9436 -514 -19 4835 C ATOM 3931 C ILE C 115 -2.913 -30.038 22.863 1.00 89.59 C ANISOU 3931 C ILE C 115 10043 14690 9307 -643 121 5018 C ATOM 3932 O ILE C 115 -1.689 -29.909 22.927 1.00 91.51 O ANISOU 3932 O ILE C 115 10074 15376 9320 -875 311 5166 O ATOM 3933 CB ILE C 115 -4.153 -28.250 24.193 1.00 89.12 C ANISOU 3933 CB ILE C 115 10373 13575 9915 -701 -305 5092 C ATOM 3934 CG1 ILE C 115 -2.965 -27.398 24.656 1.00 91.34 C ANISOU 3934 CG1 ILE C 115 10716 13843 10147 -1154 -318 5334 C ATOM 3935 CG2 ILE C 115 -5.360 -28.055 25.108 1.00 87.41 C ANISOU 3935 CG2 ILE C 115 10228 12923 10060 -323 -468 4870 C ATOM 3936 CD1 ILE C 115 -3.094 -25.916 24.334 1.00 95.54 C ANISOU 3936 CD1 ILE C 115 11743 13889 10667 -1472 -732 5696 C ATOM 3937 N PRO C 116 -3.545 -30.432 21.741 1.00 90.61 N ANISOU 3937 N PRO C 116 10313 14896 9217 -476 20 5025 N ATOM 3938 CA PRO C 116 -2.762 -30.764 20.560 1.00 93.95 C ANISOU 3938 CA PRO C 116 10678 15945 9073 -477 168 5155 C ATOM 3939 C PRO C 116 -2.258 -29.512 19.880 1.00 98.30 C ANISOU 3939 C PRO C 116 11270 16674 9406 -966 125 5662 C ATOM 3940 O PRO C 116 -2.959 -28.500 19.856 1.00 98.98 O ANISOU 3940 O PRO C 116 11646 16216 9746 -1184 -166 5872 O ATOM 3941 CB PRO C 116 -3.773 -31.472 19.662 1.00 93.87 C ANISOU 3941 CB PRO C 116 10923 15806 8939 -170 -29 5005 C ATOM 3942 CG PRO C 116 -5.063 -30.860 20.020 1.00 92.28 C ANISOU 3942 CG PRO C 116 10875 14983 9206 -229 -316 5054 C ATOM 3943 CD PRO C 116 -4.991 -30.571 21.491 1.00 89.55 C ANISOU 3943 CD PRO C 116 10370 14366 9289 -271 -249 4940 C ATOM 3944 N ASP C 117 -1.041 -29.576 19.354 1.00104.55 N ANISOU 3944 N ASP C 117 10054 17156 12514 -585 -3547 1437 N ATOM 3945 CA ASP C 117 -0.535 -28.516 18.497 1.00105.63 C ANISOU 3945 CA ASP C 117 9855 17174 13105 -1157 -3322 1204 C ATOM 3946 C ASP C 117 -1.122 -28.727 17.112 1.00 99.28 C ANISOU 3946 C ASP C 117 9418 15737 12566 -933 -2641 1329 C ATOM 3947 O ASP C 117 -0.975 -29.800 16.522 1.00 98.32 O ANISOU 3947 O ASP C 117 9205 15602 12552 -333 -2363 1648 O ATOM 3948 CB ASP C 117 0.996 -28.523 18.442 1.00113.85 C ANISOU 3948 CB ASP C 117 9840 18934 14482 -1238 -3549 1359 C ATOM 3949 CG ASP C 117 1.540 -27.700 17.286 1.00115.09 C ANISOU 3949 CG ASP C 117 9622 18914 15193 -1704 -3110 1288 C ATOM 3950 OD1 ASP C 117 1.219 -26.494 17.200 1.00114.86 O ANISOU 3950 OD1 ASP C 117 9867 18507 15267 -2402 -3046 930 O ATOM 3951 OD2 ASP C 117 2.283 -28.264 16.458 1.00117.17 O ANISOU 3951 OD2 ASP C 117 9336 19388 15796 -1348 -2781 1613 O ATOM 3952 N ILE C 118 -1.811 -27.709 16.611 1.00 95.77 N ANISOU 3952 N ILE C 118 9417 14768 12203 -1389 -2379 1066 N ATOM 3953 CA ILE C 118 -2.414 -27.776 15.290 1.00 90.78 C ANISOU 3953 CA ILE C 118 9140 13630 11724 -1221 -1794 1181 C ATOM 3954 C ILE C 118 -1.907 -26.610 14.454 1.00 93.51 C ANISOU 3954 C ILE C 118 9229 13848 12451 -1769 -1515 1137 C ATOM 3955 O ILE C 118 -2.353 -25.468 14.618 1.00 93.50 O ANISOU 3955 O ILE C 118 9544 13476 12504 -2279 -1534 893 O ATOM 3956 CB ILE C 118 -3.950 -27.775 15.367 1.00 84.18 C ANISOU 3956 CB ILE C 118 9149 12247 10587 -1114 -1684 1045 C ATOM 3957 CG1 ILE C 118 -4.427 -28.884 16.300 1.00 82.80 C ANISOU 3957 CG1 ILE C 118 9211 12189 10059 -662 -1929 1128 C ATOM 3958 CG2 ILE C 118 -4.559 -27.980 13.986 1.00 80.25 C ANISOU 3958 CG2 ILE C 118 8956 11370 10167 -894 -1163 1174 C ATOM 3959 CD1 ILE C 118 -5.671 -28.532 17.064 1.00 80.12 C ANISOU 3959 CD1 ILE C 118 9503 11556 9384 -786 -2035 894 C ATOM 3960 N GLN C 119 -0.958 -26.915 13.571 1.00 96.71 N ANISOU 3960 N GLN C 119 9063 14539 13143 -1640 -1208 1395 N ATOM 3961 CA GLN C 119 -0.316 -25.911 12.733 1.00100.69 C ANISOU 3961 CA GLN C 119 9222 15001 14035 -2153 -868 1464 C ATOM 3962 C GLN C 119 -1.250 -25.463 11.612 1.00 96.23 C ANISOU 3962 C GLN C 119 9297 13864 13403 -2146 -361 1563 C ATOM 3963 O GLN C 119 -1.212 -24.306 11.193 1.00 98.52 O ANISOU 3963 O GLN C 119 9647 13850 13936 -2666 -145 1591 O ATOM 3964 CB GLN C 119 0.995 -26.457 12.157 1.00106.39 C ANISOU 3964 CB GLN C 119 9076 16300 15046 -1955 -642 1739 C ATOM 3965 CG GLN C 119 2.013 -25.385 11.741 1.00113.81 C ANISOU 3965 CG GLN C 119 9364 17414 16465 -2649 -442 1804 C ATOM 3966 CD GLN C 119 2.911 -24.910 12.883 1.00121.00 C ANISOU 3966 CD GLN C 119 9580 18790 17605 -3191 -1032 1581 C ATOM 3967 OE1 GLN C 119 2.695 -25.241 14.053 1.00120.45 O ANISOU 3967 OE1 GLN C 119 9607 18910 17247 -3077 -1632 1362 O ATOM 3968 NE2 GLN C 119 3.929 -24.128 12.539 1.00128.48 N ANISOU 3968 NE2 GLN C 119 9802 19969 19047 -3816 -861 1641 N ATOM 3969 N ASN C 120 -2.090 -26.381 11.140 1.00 90.74 N ANISOU 3969 N ASN C 120 9072 13022 12384 -1565 -185 1628 N ATOM 3970 CA ASN C 120 -3.053 -26.075 10.091 1.00 87.03 C ANISOU 3970 CA ASN C 120 9182 12141 11744 -1490 205 1721 C ATOM 3971 C ASN C 120 -4.500 -26.115 10.568 1.00 81.10 C ANISOU 3971 C ASN C 120 9142 10979 10692 -1354 -4 1530 C ATOM 3972 O ASN C 120 -5.144 -27.169 10.522 1.00 77.45 O ANISOU 3972 O ASN C 120 8949 10516 9963 -897 -18 1485 O ATOM 3973 CB ASN C 120 -2.863 -27.012 8.902 1.00 87.06 C ANISOU 3973 CB ASN C 120 9114 12363 11602 -1003 648 1901 C ATOM 3974 CG ASN C 120 -1.857 -26.486 7.907 1.00 93.42 C ANISOU 3974 CG ASN C 120 9445 13421 12631 -1218 1116 2171 C ATOM 3975 OD1 ASN C 120 -1.965 -25.350 7.434 1.00 95.58 O ANISOU 3975 OD1 ASN C 120 9847 13459 13011 -1646 1325 2337 O ATOM 3976 ND2 ASN C 120 -0.870 -27.314 7.574 1.00 97.95 N ANISOU 3976 ND2 ASN C 120 9460 14455 13302 -896 1336 2254 N ATOM 3977 N PRO C 121 -5.024 -24.963 11.026 1.00 81.02 N ANISOU 3977 N PRO C 121 9427 10588 10770 -1760 -129 1401 N ATOM 3978 CA PRO C 121 -6.436 -24.893 11.401 1.00 76.28 C ANISOU 3978 CA PRO C 121 9448 9617 9918 -1608 -247 1241 C ATOM 3979 C PRO C 121 -7.347 -25.008 10.172 1.00 73.39 C ANISOU 3979 C PRO C 121 9448 9082 9355 -1315 85 1443 C ATOM 3980 O PRO C 121 -6.859 -25.064 9.048 1.00 75.32 O ANISOU 3980 O PRO C 121 9524 9489 9604 -1255 417 1694 O ATOM 3981 CB PRO C 121 -6.562 -23.502 12.047 1.00 78.95 C ANISOU 3981 CB PRO C 121 9943 9565 10488 -2110 -361 1049 C ATOM 3982 CG PRO C 121 -5.161 -23.061 12.331 1.00 84.89 C ANISOU 3982 CG PRO C 121 10117 10559 11579 -2580 -452 1012 C ATOM 3983 CD PRO C 121 -4.338 -23.680 11.255 1.00 86.24 C ANISOU 3983 CD PRO C 121 9847 11104 11815 -2386 -140 1361 C ATOM 3984 N ASP C 122 -8.656 -25.058 10.394 1.00 69.75 N ANISOU 3984 N ASP C 122 9444 8374 8682 -1132 -8 1329 N ATOM 3985 CA ASP C 122 -9.638 -25.136 9.308 1.00 67.92 C ANISOU 3985 CA ASP C 122 9520 8068 8220 -868 203 1490 C ATOM 3986 C ASP C 122 -11.064 -25.017 9.863 1.00 64.59 C ANISOU 3986 C ASP C 122 9482 7393 7667 -739 37 1329 C ATOM 3987 O ASP C 122 -11.907 -25.893 9.640 1.00 61.62 O ANISOU 3987 O ASP C 122 9245 7132 7037 -464 2 1259 O ATOM 3988 CB ASP C 122 -9.478 -26.451 8.546 1.00 67.21 C ANISOU 3988 CB ASP C 122 9332 8326 7880 -534 328 1501 C ATOM 3989 CG ASP C 122 -9.987 -26.363 7.130 1.00 68.75 C ANISOU 3989 CG ASP C 122 9704 8620 7797 -371 590 1694 C ATOM 3990 OD1 ASP C 122 -10.389 -25.249 6.715 1.00 71.01 O ANISOU 3990 OD1 ASP C 122 10152 8718 8110 -483 680 1935 O ATOM 3991 OD2 ASP C 122 -9.976 -27.411 6.437 1.00 69.52 O ANISOU 3991 OD2 ASP C 122 9796 8981 7637 -115 708 1602 O ATOM 3992 N PRO C 123 -11.338 -23.921 10.590 1.00 65.77 N ANISOU 3992 N PRO C 123 9785 7184 8021 -958 -34 1235 N ATOM 3993 CA PRO C 123 -12.553 -23.799 11.389 1.00 63.60 C ANISOU 3993 CA PRO C 123 9802 6705 7659 -833 -165 1021 C ATOM 3994 C PRO C 123 -13.807 -24.033 10.561 1.00 61.61 C ANISOU 3994 C PRO C 123 9722 6482 7205 -499 -79 1173 C ATOM 3995 O PRO C 123 -14.061 -23.306 9.606 1.00 63.70 O ANISOU 3995 O PRO C 123 10064 6629 7509 -426 85 1463 O ATOM 3996 CB PRO C 123 -12.491 -22.352 11.890 1.00 67.30 C ANISOU 3996 CB PRO C 123 10422 6706 8444 -1111 -121 930 C ATOM 3997 CG PRO C 123 -11.047 -21.969 11.789 1.00 70.92 C ANISOU 3997 CG PRO C 123 10589 7198 9159 -1505 -91 981 C ATOM 3998 CD PRO C 123 -10.565 -22.664 10.575 1.00 70.28 C ANISOU 3998 CD PRO C 123 10280 7469 8955 -1344 80 1323 C ATOM 3999 N ALA C 124 -14.572 -25.058 10.915 1.00 58.64 N ANISOU 3999 N ALA C 124 9380 6290 6610 -313 -195 1008 N ATOM 4000 CA ALA C 124 -15.774 -25.402 10.159 1.00 57.53 C ANISOU 4000 CA ALA C 124 9309 6273 6276 -62 -173 1084 C ATOM 4001 C ALA C 124 -16.871 -26.028 11.017 1.00 55.56 C ANISOU 4001 C ALA C 124 9115 6051 5944 29 -275 858 C ATOM 4002 O ALA C 124 -16.602 -26.880 11.866 1.00 54.42 O ANISOU 4002 O ALA C 124 8954 5966 5758 -37 -346 692 O ATOM 4003 CB ALA C 124 -15.424 -26.313 9.003 1.00 57.32 C ANISOU 4003 CB ALA C 124 9178 6575 6026 24 -116 1165 C ATOM 4004 N VAL C 125 -18.104 -25.583 10.784 1.00 56.11 N ANISOU 4004 N VAL C 125 9220 6098 6000 202 -261 911 N ATOM 4005 CA VAL C 125 -19.297 -26.119 11.441 1.00 54.82 C ANISOU 4005 CA VAL C 125 9027 6018 5785 283 -297 739 C ATOM 4006 C VAL C 125 -20.157 -26.811 10.384 1.00 54.88 C ANISOU 4006 C VAL C 125 8882 6350 5621 387 -365 785 C ATOM 4007 O VAL C 125 -20.707 -26.153 9.497 1.00 56.95 O ANISOU 4007 O VAL C 125 9079 6727 5834 567 -392 989 O ATOM 4008 CB VAL C 125 -20.127 -24.998 12.109 1.00 56.70 C ANISOU 4008 CB VAL C 125 9339 6019 6187 422 -209 714 C ATOM 4009 CG1 VAL C 125 -21.381 -25.563 12.738 1.00 56.70 C ANISOU 4009 CG1 VAL C 125 9227 6181 6134 510 -182 568 C ATOM 4010 CG2 VAL C 125 -19.302 -24.254 13.143 1.00 57.67 C ANISOU 4010 CG2 VAL C 125 9649 5819 6443 258 -160 550 C ATOM 4011 N TYR C 126 -20.262 -28.133 10.470 1.00 53.39 N ANISOU 4011 N TYR C 126 8641 6305 5338 270 -403 599 N ATOM 4012 CA TYR C 126 -21.035 -28.898 9.496 1.00 54.45 C ANISOU 4012 CA TYR C 126 8633 6746 5310 264 -494 514 C ATOM 4013 C TYR C 126 -22.384 -29.348 10.070 1.00 55.30 C ANISOU 4013 C TYR C 126 8570 6945 5498 209 -513 374 C ATOM 4014 O TYR C 126 -22.583 -29.317 11.280 1.00 54.65 O ANISOU 4014 O TYR C 126 8530 6681 5555 177 -401 342 O ATOM 4015 CB TYR C 126 -20.223 -30.095 8.993 1.00 54.03 C ANISOU 4015 CB TYR C 126 8650 6723 5155 140 -471 348 C ATOM 4016 CG TYR C 126 -18.860 -29.736 8.428 1.00 53.62 C ANISOU 4016 CG TYR C 126 8681 6654 5040 198 -391 489 C ATOM 4017 CD1 TYR C 126 -18.731 -29.160 7.165 1.00 55.41 C ANISOU 4017 CD1 TYR C 126 8889 7134 5030 300 -391 652 C ATOM 4018 CD2 TYR C 126 -17.698 -29.990 9.153 1.00 52.11 C ANISOU 4018 CD2 TYR C 126 8542 6255 5002 155 -309 498 C ATOM 4019 CE1 TYR C 126 -17.477 -28.831 6.645 1.00 56.12 C ANISOU 4019 CE1 TYR C 126 9015 7232 5075 322 -241 818 C ATOM 4020 CE2 TYR C 126 -16.442 -29.671 8.642 1.00 52.95 C ANISOU 4020 CE2 TYR C 126 8618 6400 5101 181 -212 631 C ATOM 4021 CZ TYR C 126 -16.337 -29.092 7.387 1.00 55.25 C ANISOU 4021 CZ TYR C 126 8893 6907 5191 246 -144 787 C ATOM 4022 OH TYR C 126 -15.090 -28.770 6.884 1.00 56.65 O ANISOU 4022 OH TYR C 126 9004 7146 5376 242 25 955 O ATOM 4023 N GLN C 127 -23.311 -29.741 9.198 1.00 57.75 N ANISOU 4023 N GLN C 127 8657 7597 5689 180 -652 287 N ATOM 4024 CA GLN C 127 -24.604 -30.288 9.620 1.00 59.49 C ANISOU 4024 CA GLN C 127 8607 7969 6027 46 -666 136 C ATOM 4025 C GLN C 127 -24.693 -31.756 9.222 1.00 60.67 C ANISOU 4025 C GLN C 127 8740 8160 6152 -290 -704 -182 C ATOM 4026 O GLN C 127 -24.525 -32.095 8.049 1.00 62.66 O ANISOU 4026 O GLN C 127 8990 8645 6172 -341 -858 -333 O ATOM 4027 CB GLN C 127 -25.770 -29.493 9.012 1.00 62.90 C ANISOU 4027 CB GLN C 127 8680 8811 6410 261 -831 272 C ATOM 4028 CG GLN C 127 -27.156 -29.921 9.513 1.00 65.99 C ANISOU 4028 CG GLN C 127 8662 9429 6984 130 -818 144 C ATOM 4029 CD GLN C 127 -28.257 -28.924 9.164 1.00 70.46 C ANISOU 4029 CD GLN C 127 8808 10384 7578 477 -944 363 C ATOM 4030 OE1 GLN C 127 -28.740 -28.875 8.031 1.00 73.92 O ANISOU 4030 OE1 GLN C 127 8967 11315 7804 546 -1250 405 O ATOM 4031 NE2 GLN C 127 -28.667 -28.133 10.149 1.00 71.17 N ANISOU 4031 NE2 GLN C 127 8847 10288 7908 734 -706 498 N ATOM 4032 N LEU C 128 -24.961 -32.619 10.198 1.00 60.45 N ANISOU 4032 N LEU C 128 8735 7884 6351 -520 -531 -285 N ATOM 4033 CA LEU C 128 -25.005 -34.064 9.970 1.00 62.33 C ANISOU 4033 CA LEU C 128 9029 7965 6689 -867 -488 -580 C ATOM 4034 C LEU C 128 -26.400 -34.634 10.196 1.00 66.02 C ANISOU 4034 C LEU C 128 9142 8584 7359 -1197 -473 -737 C ATOM 4035 O LEU C 128 -26.944 -34.537 11.294 1.00 66.26 O ANISOU 4035 O LEU C 128 9068 8533 7575 -1226 -272 -569 O ATOM 4036 CB LEU C 128 -23.998 -34.776 10.876 1.00 60.42 C ANISOU 4036 CB LEU C 128 9142 7215 6598 -879 -255 -491 C ATOM 4037 CG LEU C 128 -22.506 -34.577 10.601 1.00 58.15 C ANISOU 4037 CG LEU C 128 9127 6782 6185 -636 -257 -400 C ATOM 4038 CD1 LEU C 128 -21.999 -33.207 11.064 1.00 55.19 C ANISOU 4038 CD1 LEU C 128 8767 6495 5706 -371 -296 -118 C ATOM 4039 CD2 LEU C 128 -21.729 -35.691 11.270 1.00 58.46 C ANISOU 4039 CD2 LEU C 128 9421 6373 6418 -667 -65 -364 C ATOM 4040 N ARG C 129 -26.974 -35.227 9.155 1.00 69.82 N ANISOU 4040 N ARG C 129 9416 9331 7781 -1473 -675 -1084 N ATOM 4041 CA ARG C 129 -28.315 -35.796 9.243 1.00 74.61 C ANISOU 4041 CA ARG C 129 9585 10147 8618 -1881 -701 -1287 C ATOM 4042 C ARG C 129 -28.280 -37.178 9.900 1.00 76.64 C ANISOU 4042 C ARG C 129 10045 9822 9251 -2323 -396 -1445 C ATOM 4043 O ARG C 129 -27.291 -37.902 9.776 1.00 76.09 O ANISOU 4043 O ARG C 129 10426 9273 9210 -2336 -280 -1555 O ATOM 4044 CB ARG C 129 -28.952 -35.872 7.852 1.00 79.29 C ANISOU 4044 CB ARG C 129 9839 11329 8959 -2056 -1104 -1645 C ATOM 4045 N ASP C 130 -29.353 -37.529 10.610 1.00 79.84 N ANISOU 4045 N ASP C 130 10107 10253 9976 -2654 -222 -1407 N ATOM 4046 CA ASP C 130 -29.530 -38.870 11.185 1.00 83.44 C ANISOU 4046 CA ASP C 130 10707 10143 10854 -3155 105 -1506 C ATOM 4047 C ASP C 130 -29.760 -39.886 10.057 1.00 88.81 C ANISOU 4047 C ASP C 130 11353 10744 11648 -3666 -77 -2114 C ATOM 4048 O ASP C 130 -30.071 -39.501 8.930 1.00 90.52 O ANISOU 4048 O ASP C 130 11293 11539 11563 -3676 -487 -2443 O ATOM 4049 CB ASP C 130 -30.708 -38.839 12.182 1.00 86.65 C ANISOU 4049 CB ASP C 130 10669 10709 11544 -3393 374 -1272 C ATOM 4050 CG ASP C 130 -31.066 -40.218 12.769 1.00 92.50 C ANISOU 4050 CG ASP C 130 11500 10869 12778 -3995 767 -1300 C ATOM 4051 OD1 ASP C 130 -30.230 -41.150 12.764 1.00 93.20 O ANISOU 4051 OD1 ASP C 130 12128 10267 13016 -4088 921 -1353 O ATOM 4052 OD2 ASP C 130 -32.211 -40.360 13.255 1.00 97.26 O ANISOU 4052 OD2 ASP C 130 11606 11690 13660 -4362 966 -1231 O ATOM 4053 N SER C 131 -29.589 -41.174 10.349 1.00 92.31 N ANISOU 4053 N SER C 131 12110 10462 12501 -4076 230 -2266 N ATOM 4054 CA SER C 131 -29.946 -42.234 9.401 1.00 99.25 C ANISOU 4054 CA SER C 131 12968 11154 13587 -4680 124 -2946 C ATOM 4055 C SER C 131 -31.457 -42.352 9.198 1.00105.83 C ANISOU 4055 C SER C 131 13077 12498 14634 -5307 -40 -3230 C ATOM 4056 O SER C 131 -31.910 -42.900 8.193 1.00112.13 O ANISOU 4056 O SER C 131 13688 13477 15439 -5811 -319 -3895 O ATOM 4057 CB SER C 131 -29.372 -43.580 9.838 1.00102.47 C ANISOU 4057 CB SER C 131 13942 10502 14491 -4931 569 -2996 C ATOM 4058 OG SER C 131 -27.984 -43.640 9.571 1.00 98.73 O ANISOU 4058 OG SER C 131 14041 9661 13812 -4407 613 -2965 O ATOM 4059 N LYS C 132 -32.226 -41.836 10.154 1.00105.14 N ANISOU 4059 N LYS C 132 12557 12691 14702 -5277 136 -2759 N ATOM 4060 CA LYS C 132 -33.687 -41.867 10.088 1.00111.83 C ANISOU 4060 CA LYS C 132 12582 14106 15801 -5818 28 -2933 C ATOM 4061 C LYS C 132 -34.309 -40.472 10.294 1.00109.02 C ANISOU 4061 C LYS C 132 11629 14639 15156 -5306 -162 -2549 C ATOM 4062 O LYS C 132 -34.925 -40.194 11.329 1.00109.50 O ANISOU 4062 O LYS C 132 11371 14789 15444 -5270 190 -2135 O ATOM 4063 CB LYS C 132 -34.250 -42.879 11.100 1.00117.30 C ANISOU 4063 CB LYS C 132 13228 14185 17157 -6439 588 -2770 C ATOM 4064 CG LYS C 132 -34.145 -44.361 10.693 1.00124.12 C ANISOU 4064 CG LYS C 132 14434 14225 18501 -7188 739 -3302 C ATOM 4065 CD LYS C 132 -32.751 -44.975 10.912 1.00120.03 C ANISOU 4065 CD LYS C 132 14885 12710 18012 -6848 1033 -3165 C ATOM 4066 CE LYS C 132 -32.299 -44.941 12.370 1.00115.90 C ANISOU 4066 CE LYS C 132 14724 11708 17605 -6462 1569 -2318 C ATOM 4067 NZ LYS C 132 -33.084 -45.858 13.237 1.00123.09 N ANISOU 4067 NZ LYS C 132 15512 12099 19156 -7122 2109 -2068 N ATOM 4068 N SER C 133 -34.120 -39.602 9.299 1.00106.81 N ANISOU 4068 N SER C 133 11236 14982 14366 -4873 -672 -2670 N ATOM 4069 CA SER C 133 -34.742 -38.264 9.234 1.00105.60 C ANISOU 4069 CA SER C 133 10506 15658 13959 -4342 -918 -2346 C ATOM 4070 C SER C 133 -34.586 -37.412 10.499 1.00100.09 C ANISOU 4070 C SER C 133 9929 14790 13310 -3785 -494 -1736 C ATOM 4071 O SER C 133 -35.022 -36.259 10.543 1.00 99.06 O ANISOU 4071 O SER C 133 9415 15192 13030 -3265 -606 -1459 O ATOM 4072 CB SER C 133 -36.222 -38.383 8.847 1.00114.40 C ANISOU 4072 CB SER C 133 10629 17550 15287 -4806 -1187 -2590 C ATOM 4073 OG SER C 133 -36.376 -39.141 7.658 1.00120.26 O ANISOU 4073 OG SER C 133 11259 18525 15909 -5366 -1638 -3248 O ATOM 4074 N LYS C 136 -34.112 -34.688 12.245 1.00 90.57 N ANISOU 4074 N LYS C 136 8973 13661 11780 -2241 -34 -730 N ATOM 4075 CA LYS C 136 -33.076 -34.961 13.235 1.00 85.75 C ANISOU 4075 CA LYS C 136 9088 12374 11120 -2184 338 -558 C ATOM 4076 C LYS C 136 -31.688 -34.716 12.654 1.00 80.11 C ANISOU 4076 C LYS C 136 9006 11344 10088 -1903 93 -582 C ATOM 4077 O LYS C 136 -31.287 -35.347 11.678 1.00 80.49 O ANISOU 4077 O LYS C 136 9189 11327 10066 -2138 -173 -854 O ATOM 4078 CB LYS C 136 -33.194 -36.394 13.769 1.00 88.76 C ANISOU 4078 CB LYS C 136 9585 12329 11811 -2827 658 -633 C ATOM 4079 N SER C 137 -30.957 -33.792 13.262 1.00 75.89 N ANISOU 4079 N SER C 137 8840 10631 9362 -1421 210 -334 N ATOM 4080 CA SER C 137 -29.620 -33.431 12.797 1.00 71.36 C ANISOU 4080 CA SER C 137 8786 9797 8529 -1158 22 -311 C ATOM 4081 C SER C 137 -28.716 -32.996 13.952 1.00 67.83 C ANISOU 4081 C SER C 137 8812 8985 7976 -906 274 -95 C ATOM 4082 O SER C 137 -29.179 -32.844 15.084 1.00 69.26 O ANISOU 4082 O SER C 137 8947 9167 8202 -872 586 27 O ATOM 4083 CB SER C 137 -29.715 -32.311 11.757 1.00 71.28 C ANISOU 4083 CB SER C 137 8583 10167 8333 -779 -312 -268 C ATOM 4084 OG SER C 137 -30.488 -31.225 12.247 1.00 73.02 O ANISOU 4084 OG SER C 137 8497 10613 8634 -411 -198 -76 O ATOM 4085 N VAL C 138 -27.430 -32.805 13.663 1.00 64.28 N ANISOU 4085 N VAL C 138 8782 8289 7353 -748 139 -69 N ATOM 4086 CA VAL C 138 -26.487 -32.222 14.628 1.00 61.67 C ANISOU 4086 CA VAL C 138 8834 7716 6880 -517 263 88 C ATOM 4087 C VAL C 138 -25.604 -31.164 13.973 1.00 59.25 C ANISOU 4087 C VAL C 138 8686 7384 6441 -233 53 119 C ATOM 4088 O VAL C 138 -25.535 -31.085 12.748 1.00 59.36 O ANISOU 4088 O VAL C 138 8598 7538 6417 -208 -164 75 O ATOM 4089 CB VAL C 138 -25.578 -33.287 15.278 1.00 60.78 C ANISOU 4089 CB VAL C 138 9081 7266 6747 -682 377 166 C ATOM 4090 CG1 VAL C 138 -26.370 -34.162 16.236 1.00 64.14 C ANISOU 4090 CG1 VAL C 138 9443 7639 7290 -931 690 266 C ATOM 4091 CG2 VAL C 138 -24.883 -34.122 14.217 1.00 60.19 C ANISOU 4091 CG2 VAL C 138 9115 7023 6731 -803 211 41 C ATOM 4092 N CYS C 139 -24.937 -30.357 14.794 1.00 58.07 N ANISOU 4092 N CYS C 139 8788 7075 6200 -55 130 189 N ATOM 4093 CA CYS C 139 -23.949 -29.399 14.308 1.00 56.73 C ANISOU 4093 CA CYS C 139 8794 6786 5973 118 -16 233 C ATOM 4094 C CYS C 139 -22.591 -29.758 14.863 1.00 54.91 C ANISOU 4094 C CYS C 139 8853 6365 5644 30 -43 252 C ATOM 4095 O CYS C 139 -22.381 -29.719 16.076 1.00 55.69 O ANISOU 4095 O CYS C 139 9108 6414 5639 14 56 244 O ATOM 4096 CB CYS C 139 -24.301 -27.974 14.720 1.00 58.10 C ANISOU 4096 CB CYS C 139 8983 6895 6199 373 78 239 C ATOM 4097 SG CYS C 139 -25.957 -27.459 14.254 1.00 63.34 S ANISOU 4097 SG CYS C 139 9218 7827 7023 615 135 288 S ATOM 4098 N LEU C 140 -21.673 -30.115 13.974 1.00 53.57 N ANISOU 4098 N LEU C 140 8726 6158 5470 -4 -176 282 N ATOM 4099 CA LEU C 140 -20.330 -30.501 14.375 1.00 52.63 C ANISOU 4099 CA LEU C 140 8772 5922 5303 -38 -220 334 C ATOM 4100 C LEU C 140 -19.339 -29.388 14.076 1.00 52.11 C ANISOU 4100 C LEU C 140 8742 5814 5244 17 -310 371 C ATOM 4101 O LEU C 140 -19.038 -29.118 12.914 1.00 51.99 O ANISOU 4101 O LEU C 140 8661 5835 5257 54 -345 426 O ATOM 4102 CB LEU C 140 -19.918 -31.800 13.672 1.00 52.69 C ANISOU 4102 CB LEU C 140 8777 5883 5359 -94 -224 323 C ATOM 4103 CG LEU C 140 -18.437 -32.181 13.710 1.00 52.53 C ANISOU 4103 CG LEU C 140 8826 5786 5346 -26 -267 410 C ATOM 4104 CD1 LEU C 140 -18.021 -32.641 15.101 1.00 53.45 C ANISOU 4104 CD1 LEU C 140 9048 5848 5412 -3 -263 554 C ATOM 4105 CD2 LEU C 140 -18.145 -33.241 12.667 1.00 53.01 C ANISOU 4105 CD2 LEU C 140 8883 5775 5482 -9 -209 320 C ATOM 4106 N PHE C 141 -18.842 -28.744 15.128 1.00 52.85 N ANISOU 4106 N PHE C 141 8943 5848 5290 -15 -333 331 N ATOM 4107 CA PHE C 141 -17.837 -27.685 14.985 1.00 53.59 C ANISOU 4107 CA PHE C 141 9055 5848 5458 -73 -410 323 C ATOM 4108 C PHE C 141 -16.454 -28.273 15.162 1.00 53.81 C ANISOU 4108 C PHE C 141 9009 5977 5459 -151 -536 387 C ATOM 4109 O PHE C 141 -16.102 -28.703 16.259 1.00 54.91 O ANISOU 4109 O PHE C 141 9188 6223 5451 -178 -628 366 O ATOM 4110 CB PHE C 141 -18.073 -26.557 15.996 1.00 55.54 C ANISOU 4110 CB PHE C 141 9450 5960 5691 -115 -379 135 C ATOM 4111 CG PHE C 141 -16.941 -25.567 16.096 1.00 56.87 C ANISOU 4111 CG PHE C 141 9649 5984 5975 -298 -470 50 C ATOM 4112 CD1 PHE C 141 -16.363 -25.019 14.957 1.00 56.79 C ANISOU 4112 CD1 PHE C 141 9548 5840 6190 -346 -443 216 C ATOM 4113 CD2 PHE C 141 -16.471 -25.165 17.336 1.00 58.80 C ANISOU 4113 CD2 PHE C 141 10006 6255 6081 -464 -572 -208 C ATOM 4114 CE1 PHE C 141 -15.328 -24.104 15.057 1.00 59.44 C ANISOU 4114 CE1 PHE C 141 9871 6007 6705 -598 -487 147 C ATOM 4115 CE2 PHE C 141 -15.440 -24.250 17.443 1.00 61.50 C ANISOU 4115 CE2 PHE C 141 10333 6463 6570 -730 -679 -357 C ATOM 4116 CZ PHE C 141 -14.869 -23.716 16.303 1.00 61.82 C ANISOU 4116 CZ PHE C 141 10251 6305 6933 -819 -620 -170 C ATOM 4117 N THR C 142 -15.671 -28.264 14.088 1.00 53.61 N ANISOU 4117 N THR C 142 8849 5972 5548 -153 -529 497 N ATOM 4118 CA THR C 142 -14.434 -29.026 14.053 1.00 54.51 C ANISOU 4118 CA THR C 142 8802 6225 5685 -137 -594 586 C ATOM 4119 C THR C 142 -13.280 -28.342 13.328 1.00 56.14 C ANISOU 4119 C THR C 142 8807 6481 6044 -240 -576 670 C ATOM 4120 O THR C 142 -13.483 -27.373 12.601 1.00 56.54 O ANISOU 4120 O THR C 142 8893 6413 6178 -316 -474 715 O ATOM 4121 CB THR C 142 -14.671 -30.418 13.446 1.00 53.74 C ANISOU 4121 CB THR C 142 8708 6138 5571 33 -493 630 C ATOM 4122 OG1 THR C 142 -13.413 -31.075 13.258 1.00 55.71 O ANISOU 4122 OG1 THR C 142 8778 6484 5904 139 -494 730 O ATOM 4123 CG2 THR C 142 -15.393 -30.312 12.113 1.00 52.69 C ANISOU 4123 CG2 THR C 142 8602 5999 5417 61 -372 587 C ATOM 4124 N ASP C 143 -12.075 -28.877 13.546 1.00 58.06 N ANISOU 4124 N ASP C 143 8810 6910 6341 -221 -654 743 N ATOM 4125 CA ASP C 143 -10.822 -28.402 12.941 1.00 60.85 C ANISOU 4125 CA ASP C 143 8851 7395 6875 -337 -606 845 C ATOM 4126 C ASP C 143 -10.456 -26.959 13.313 1.00 63.25 C ANISOU 4126 C ASP C 143 9105 7600 7329 -699 -686 769 C ATOM 4127 O ASP C 143 -10.281 -26.112 12.436 1.00 64.59 O ANISOU 4127 O ASP C 143 9244 7637 7661 -843 -499 875 O ATOM 4128 CB ASP C 143 -10.827 -28.572 11.413 1.00 60.58 C ANISOU 4128 CB ASP C 143 8794 7375 6848 -214 -323 960 C ATOM 4129 CG ASP C 143 -11.125 -29.987 10.983 1.00 60.25 C ANISOU 4129 CG ASP C 143 8829 7371 6694 86 -222 916 C ATOM 4130 OD1 ASP C 143 -12.319 -30.348 10.916 1.00 58.74 O ANISOU 4130 OD1 ASP C 143 8903 7047 6369 142 -223 808 O ATOM 4131 OD2 ASP C 143 -10.166 -30.737 10.697 1.00 63.01 O ANISOU 4131 OD2 ASP C 143 8951 7865 7126 259 -121 969 O ATOM 4132 N PHE C 144 -10.332 -26.683 14.609 1.00 64.67 N ANISOU 4132 N PHE C 144 9301 7831 7439 -860 -945 582 N ATOM 4133 CA PHE C 144 -9.906 -25.362 15.080 1.00 67.96 C ANISOU 4133 CA PHE C 144 9686 8117 8020 -1272 -1042 385 C ATOM 4134 C PHE C 144 -8.693 -25.505 15.990 1.00 72.22 C ANISOU 4134 C PHE C 144 9848 9057 8537 -1474 -1373 286 C ATOM 4135 O PHE C 144 -8.434 -26.590 16.508 1.00 72.10 O ANISOU 4135 O PHE C 144 9694 9390 8309 -1212 -1551 394 O ATOM 4136 CB PHE C 144 -11.055 -24.620 15.776 1.00 67.26 C ANISOU 4136 CB PHE C 144 10024 7704 7826 -1322 -1036 119 C ATOM 4137 CG PHE C 144 -11.841 -25.473 16.728 1.00 64.83 C ANISOU 4137 CG PHE C 144 9913 7567 7152 -1080 -1146 34 C ATOM 4138 CD1 PHE C 144 -11.629 -25.384 18.095 1.00 67.31 C ANISOU 4138 CD1 PHE C 144 10277 8100 7198 -1216 -1403 -223 C ATOM 4139 CD2 PHE C 144 -12.789 -26.375 16.259 1.00 60.24 C ANISOU 4139 CD2 PHE C 144 9459 6961 6467 -752 -985 211 C ATOM 4140 CE1 PHE C 144 -12.347 -26.177 18.979 1.00 65.73 C ANISOU 4140 CE1 PHE C 144 10273 8086 6616 -990 -1444 -217 C ATOM 4141 CE2 PHE C 144 -13.506 -27.169 17.139 1.00 58.97 C ANISOU 4141 CE2 PHE C 144 9461 6922 6022 -585 -1025 186 C ATOM 4142 CZ PHE C 144 -13.286 -27.069 18.499 1.00 61.42 C ANISOU 4142 CZ PHE C 144 9841 7444 6050 -684 -1227 15 C ATOM 4143 N ASP C 145 -7.935 -24.427 16.160 1.00 77.05 N ANISOU 4143 N ASP C 145 10266 9619 9390 -1943 -1460 106 N ATOM 4144 CA ASP C 145 -6.731 -24.481 16.982 1.00 82.67 C ANISOU 4144 CA ASP C 145 10512 10813 10084 -2203 -1841 -20 C ATOM 4145 C ASP C 145 -7.113 -24.526 18.449 1.00 84.52 C ANISOU 4145 C ASP C 145 10982 11250 9882 -2234 -2201 -349 C ATOM 4146 O ASP C 145 -8.220 -24.136 18.821 1.00 82.69 O ANISOU 4146 O ASP C 145 11266 10676 9478 -2196 -2089 -569 O ATOM 4147 CB ASP C 145 -5.773 -23.316 16.682 1.00 88.31 C ANISOU 4147 CB ASP C 145 10891 11424 11239 -2801 -1820 -152 C ATOM 4148 CG ASP C 145 -6.330 -21.962 17.096 1.00 91.03 C ANISOU 4148 CG ASP C 145 11666 11208 11713 -3234 -1776 -571 C ATOM 4149 OD1 ASP C 145 -7.533 -21.701 16.873 1.00 88.07 O ANISOU 4149 OD1 ASP C 145 11833 10349 11280 -2999 -1519 -575 O ATOM 4150 OD2 ASP C 145 -5.553 -21.148 17.634 1.00 97.49 O ANISOU 4150 OD2 ASP C 145 12254 12058 12728 -3815 -1990 -917 O ATOM 4151 N SER C 146 -6.192 -25.007 19.275 1.00 89.19 N ANISOU 4151 N SER C 146 11167 12458 10264 -2267 -2623 -356 N ATOM 4152 CA SER C 146 -6.471 -25.246 20.684 1.00 91.96 C ANISOU 4152 CA SER C 146 11719 13171 10049 -2220 -2991 -574 C ATOM 4153 C SER C 146 -6.564 -23.959 21.502 1.00 97.09 C ANISOU 4153 C SER C 146 12596 13706 10588 -2779 -3168 -1211 C ATOM 4154 O SER C 146 -6.731 -23.999 22.720 1.00100.60 O ANISOU 4154 O SER C 146 13221 14523 10480 -2812 -3482 -1492 O ATOM 4155 CB SER C 146 -5.421 -26.192 21.270 1.00 96.19 C ANISOU 4155 CB SER C 146 11717 14476 10355 -2009 -3423 -296 C ATOM 4156 OG SER C 146 -5.344 -27.390 20.513 1.00 92.70 O ANISOU 4156 OG SER C 146 11121 14022 10078 -1455 -3193 243 O ATOM 4157 N GLN C 147 -6.475 -22.820 20.823 1.00 98.51 N ANISOU 4157 N GLN C 147 12810 13341 11280 -3208 -2930 -1437 N ATOM 4158 CA GLN C 147 -6.559 -21.523 21.485 1.00104.49 C ANISOU 4158 CA GLN C 147 13835 13796 12070 -3770 -3014 -2100 C ATOM 4159 C GLN C 147 -7.980 -20.950 21.455 1.00101.43 C ANISOU 4159 C GLN C 147 14164 12701 11675 -3589 -2601 -2302 C ATOM 4160 O GLN C 147 -8.180 -19.748 21.657 1.00105.78 O ANISOU 4160 O GLN C 147 15018 12713 12459 -3982 -2479 -2803 O ATOM 4161 CB GLN C 147 -5.545 -20.541 20.881 1.00109.81 C ANISOU 4161 CB GLN C 147 14113 14221 13387 -4414 -2985 -2239 C ATOM 4162 CG GLN C 147 -4.092 -21.036 20.904 1.00114.74 C ANISOU 4162 CG GLN C 147 13893 15616 14086 -4617 -3382 -2053 C ATOM 4163 CD GLN C 147 -3.528 -21.200 22.313 1.00122.04 C ANISOU 4163 CD GLN C 147 14578 17343 14449 -4836 -4053 -2466 C ATOM 4164 OE1 GLN C 147 -3.230 -20.216 23.000 1.00129.49 O ANISOU 4164 OE1 GLN C 147 15558 18252 15391 -5496 -4309 -3137 O ATOM 4165 NE2 GLN C 147 -3.366 -22.449 22.742 1.00120.29 N ANISOU 4165 NE2 GLN C 147 14120 17845 13738 -4283 -4343 -2065 N ATOM 4166 N THR C 148 -8.961 -21.817 21.204 1.00 95.00 N ANISOU 4166 N THR C 148 13588 11870 10637 -2993 -2372 -1921 N ATOM 4167 CA THR C 148 -10.376 -21.443 21.285 1.00 92.65 C ANISOU 4167 CA THR C 148 13859 11071 10272 -2737 -2014 -2069 C ATOM 4168 C THR C 148 -11.147 -22.390 22.207 1.00 90.88 C ANISOU 4168 C THR C 148 13848 11278 9404 -2340 -2077 -2023 C ATOM 4169 O THR C 148 -11.078 -23.616 22.061 1.00 87.25 O ANISOU 4169 O THR C 148 13193 11197 8760 -2007 -2147 -1552 O ATOM 4170 CB THR C 148 -11.069 -21.389 19.893 1.00 87.30 C ANISOU 4170 CB THR C 148 13264 9862 10043 -2442 -1574 -1632 C ATOM 4171 OG1 THR C 148 -10.902 -22.641 19.213 1.00 82.50 O ANISOU 4171 OG1 THR C 148 12370 9607 9369 -2102 -1584 -1097 O ATOM 4172 CG2 THR C 148 -10.510 -20.252 19.034 1.00 90.14 C ANISOU 4172 CG2 THR C 148 13548 9681 11019 -2822 -1398 -1639 C ATOM 4173 N ASN C 149 -11.877 -21.803 23.154 1.00 94.30 N ANISOU 4173 N ASN C 149 14702 11610 9519 -2378 -1997 -2516 N ATOM 4174 CA ASN C 149 -12.674 -22.557 24.120 1.00 94.18 C ANISOU 4174 CA ASN C 149 14927 12003 8854 -2046 -1972 -2492 C ATOM 4175 C ASN C 149 -14.153 -22.602 23.744 1.00 90.02 C ANISOU 4175 C ASN C 149 14688 11062 8452 -1651 -1473 -2351 C ATOM 4176 O ASN C 149 -14.763 -21.560 23.474 1.00 91.08 O ANISOU 4176 O ASN C 149 15060 10622 8923 -1671 -1174 -2653 O ATOM 4177 CB ASN C 149 -12.506 -21.972 25.527 1.00101.82 C ANISOU 4177 CB ASN C 149 16143 13305 9238 -2324 -2198 -3156 C ATOM 4178 CG ASN C 149 -11.105 -22.168 26.079 1.00107.35 C ANISOU 4178 CG ASN C 149 16471 14673 9646 -2672 -2800 -3247 C ATOM 4179 OD1 ASN C 149 -10.399 -23.104 25.699 1.00105.37 O ANISOU 4179 OD1 ASN C 149 15788 14799 9447 -2528 -3035 -2689 O ATOM 4180 ND2 ASN C 149 -10.697 -21.286 26.986 1.00115.71 N ANISOU 4180 ND2 ASN C 149 17672 15897 10397 -3123 -3059 -3984 N ATOM 4181 N VAL C 150 -14.716 -23.812 23.733 1.00 86.11 N ANISOU 4181 N VAL C 150 14143 10849 7727 -1293 -1381 -1881 N ATOM 4182 CA VAL C 150 -16.137 -24.017 23.432 1.00 82.87 C ANISOU 4182 CA VAL C 150 13891 10184 7410 -955 -949 -1725 C ATOM 4183 C VAL C 150 -16.994 -23.829 24.682 1.00 87.00 C ANISOU 4183 C VAL C 150 14740 10908 7408 -858 -744 -2064 C ATOM 4184 O VAL C 150 -16.995 -24.680 25.579 1.00 88.84 O ANISOU 4184 O VAL C 150 15022 11665 7069 -783 -825 -1906 O ATOM 4185 CB VAL C 150 -16.411 -25.421 22.840 1.00 77.86 C ANISOU 4185 CB VAL C 150 13053 9707 6825 -700 -899 -1121 C ATOM 4186 CG1 VAL C 150 -17.877 -25.562 22.473 1.00 75.28 C ANISOU 4186 CG1 VAL C 150 12794 9160 6650 -445 -494 -1013 C ATOM 4187 CG2 VAL C 150 -15.542 -25.676 21.622 1.00 74.81 C ANISOU 4187 CG2 VAL C 150 12364 9187 6875 -754 -1052 -831 C ATOM 4188 N SER C 151 -17.723 -22.715 24.730 1.00 89.31 N ANISOU 4188 N SER C 151 15265 10774 7893 -818 -434 -2496 N ATOM 4189 CA SER C 151 -18.589 -22.390 25.865 1.00 94.01 C ANISOU 4189 CA SER C 151 16179 11521 8019 -686 -136 -2905 C ATOM 4190 C SER C 151 -19.883 -23.206 25.849 1.00 91.40 C ANISOU 4190 C SER C 151 15772 11342 7615 -319 256 -2515 C ATOM 4191 O SER C 151 -20.309 -23.700 24.800 1.00 86.15 O ANISOU 4191 O SER C 151 14841 10490 7403 -170 335 -2061 O ATOM 4192 CB SER C 151 -18.906 -20.895 25.881 1.00 98.39 C ANISOU 4192 CB SER C 151 17007 11473 8903 -716 118 -3526 C ATOM 4193 OG SER C 151 -17.715 -20.130 25.876 1.00101.67 O ANISOU 4193 OG SER C 151 17477 11684 9468 -1156 -220 -3910 O ATOM 4194 N GLN C 152 -20.497 -23.347 27.023 1.00 95.89 N ANISOU 4194 N GLN C 152 16559 12296 7580 -212 506 -2715 N ATOM 4195 CA GLN C 152 -21.746 -24.093 27.163 1.00 94.86 C ANISOU 4195 CA GLN C 152 16322 12358 7362 69 941 -2367 C ATOM 4196 C GLN C 152 -22.921 -23.255 26.674 1.00 94.94 C ANISOU 4196 C GLN C 152 16265 11930 7876 354 1397 -2567 C ATOM 4197 O GLN C 152 -22.780 -22.052 26.445 1.00 97.17 O ANISOU 4197 O GLN C 152 16702 11740 8480 373 1426 -3011 O ATOM 4198 CB GLN C 152 -21.970 -24.538 28.620 1.00100.90 C ANISOU 4198 CB GLN C 152 17337 13752 7250 90 1112 -2445 C ATOM 4199 CG GLN C 152 -20.830 -25.368 29.256 1.00103.14 C ANISOU 4199 CG GLN C 152 17689 14572 6927 -105 638 -2176 C ATOM 4200 CD GLN C 152 -20.526 -26.692 28.536 1.00 98.75 C ANISOU 4200 CD GLN C 152 16837 14015 6670 -89 448 -1401 C ATOM 4201 OE1 GLN C 152 -19.524 -27.346 28.834 1.00100.16 O ANISOU 4201 OE1 GLN C 152 17000 14523 6535 -169 42 -1111 O ATOM 4202 NE2 GLN C 152 -21.385 -27.088 27.593 1.00 93.91 N ANISOU 4202 NE2 GLN C 152 15976 13044 6662 26 732 -1093 N ATOM 4203 N SER C 153 -24.076 -23.895 26.521 1.00 93.31 N ANISOU 4203 N SER C 153 15804 11873 7778 576 1760 -2217 N ATOM 4204 CA SER C 153 -25.271 -23.234 26.002 1.00 93.82 C ANISOU 4204 CA SER C 153 15662 11640 8346 914 2167 -2296 C ATOM 4205 C SER C 153 -25.888 -22.229 26.985 1.00100.86 C ANISOU 4205 C SER C 153 16827 12499 8997 1160 2639 -2894 C ATOM 4206 O SER C 153 -25.808 -22.408 28.204 1.00105.47 O ANISOU 4206 O SER C 153 17691 13509 8872 1085 2792 -3146 O ATOM 4207 CB SER C 153 -26.308 -24.280 25.600 1.00 91.58 C ANISOU 4207 CB SER C 153 14934 11623 8240 1005 2384 -1777 C ATOM 4208 OG SER C 153 -27.513 -23.661 25.191 1.00 94.18 O ANISOU 4208 OG SER C 153 14964 11807 9012 1366 2758 -1836 O ATOM 4209 N LYS C 154 -26.503 -21.178 26.438 1.00102.18 N ANISOU 4209 N LYS C 154 16923 12166 9734 1493 2887 -3102 N ATOM 4210 CA LYS C 154 -27.199 -20.165 27.238 1.00109.35 C ANISOU 4210 CA LYS C 154 18069 12920 10558 1832 3426 -3694 C ATOM 4211 C LYS C 154 -28.710 -20.413 27.275 1.00111.34 C ANISOU 4211 C LYS C 154 17880 13451 10975 2268 3991 -3470 C ATOM 4212 O LYS C 154 -29.467 -19.614 27.832 1.00118.22 O ANISOU 4212 O LYS C 154 18839 14210 11870 2669 4535 -3901 O ATOM 4213 CB LYS C 154 -26.899 -18.761 26.707 1.00111.86 C ANISOU 4213 CB LYS C 154 18628 12409 11466 1981 3413 -4080 C ATOM 4214 N ASP C 155 -29.133 -21.525 26.679 1.00105.86 N ANISOU 4214 N ASP C 155 16688 13113 10420 2174 3874 -2830 N ATOM 4215 CA ASP C 155 -30.531 -21.945 26.684 1.00107.86 C ANISOU 4215 CA ASP C 155 16395 13740 10847 2456 4350 -2561 C ATOM 4216 C ASP C 155 -30.627 -23.464 26.787 1.00104.26 C ANISOU 4216 C ASP C 155 15678 13820 10116 2071 4265 -2039 C ATOM 4217 O ASP C 155 -29.982 -24.181 26.019 1.00 97.91 O ANISOU 4217 O ASP C 155 14804 12940 9458 1753 3763 -1679 O ATOM 4218 CB ASP C 155 -31.239 -21.455 25.418 1.00106.83 C ANISOU 4218 CB ASP C 155 15759 13310 11523 2824 4301 -2306 C ATOM 4219 CG ASP C 155 -32.599 -22.102 25.221 1.00108.67 C ANISOU 4219 CG ASP C 155 15254 14045 11992 2993 4627 -1938 C ATOM 4220 OD1 ASP C 155 -33.324 -22.309 26.219 1.00113.80 O ANISOU 4220 OD1 ASP C 155 15803 15106 12331 3089 5191 -2065 O ATOM 4221 OD2 ASP C 155 -32.939 -22.405 24.060 1.00105.30 O ANISOU 4221 OD2 ASP C 155 14323 13647 12038 3002 4319 -1531 O ATOM 4222 N SER C 156 -31.456 -23.946 27.714 1.00108.88 N ANISOU 4222 N SER C 156 16120 14907 10342 2112 4814 -1991 N ATOM 4223 CA SER C 156 -31.539 -25.385 28.018 1.00107.19 C ANISOU 4223 CA SER C 156 15757 15134 9838 1717 4844 -1480 C ATOM 4224 C SER C 156 -32.237 -26.235 26.943 1.00103.49 C ANISOU 4224 C SER C 156 14614 14706 10002 1556 4732 -980 C ATOM 4225 O SER C 156 -32.469 -27.428 27.147 1.00103.59 O ANISOU 4225 O SER C 156 14458 14986 9915 1209 4845 -568 O ATOM 4226 CB SER C 156 -32.190 -25.617 29.387 1.00114.90 C ANISOU 4226 CB SER C 156 16821 16648 10187 1778 5532 -1537 C ATOM 4227 OG SER C 156 -33.587 -25.826 29.262 1.00118.84 O ANISOU 4227 OG SER C 156 16647 17426 11080 1935 6079 -1334 O ATOM 4228 N ASP C 157 -32.572 -25.616 25.813 1.00101.01 N ANISOU 4228 N ASP C 157 13931 14126 10321 1795 4512 -1019 N ATOM 4229 CA ASP C 157 -33.136 -26.329 24.665 1.00 97.79 C ANISOU 4229 CA ASP C 157 12896 13800 10459 1619 4272 -639 C ATOM 4230 C ASP C 157 -32.027 -26.740 23.700 1.00 90.02 C ANISOU 4230 C ASP C 157 12143 12486 9573 1326 3594 -493 C ATOM 4231 O ASP C 157 -32.220 -27.621 22.862 1.00 87.56 O ANISOU 4231 O ASP C 157 11479 12244 9546 1036 3347 -219 O ATOM 4232 CB ASP C 157 -34.170 -25.458 23.938 1.00101.08 C ANISOU 4232 CB ASP C 157 12721 14247 11437 2098 4380 -695 C ATOM 4233 CG ASP C 157 -35.350 -25.071 24.826 1.00109.44 C ANISOU 4233 CG ASP C 157 13430 15671 12483 2456 5115 -833 C ATOM 4234 OD1 ASP C 157 -36.128 -25.966 25.221 1.00113.15 O ANISOU 4234 OD1 ASP C 157 13459 16605 12929 2193 5472 -602 O ATOM 4235 OD2 ASP C 157 -35.510 -23.866 25.117 1.00113.37 O ANISOU 4235 OD2 ASP C 157 14085 15959 13031 3001 5382 -1175 O ATOM 4236 N VAL C 158 -30.869 -26.093 23.835 1.00 86.86 N ANISOU 4236 N VAL C 158 12321 11744 8937 1381 3323 -723 N ATOM 4237 CA VAL C 158 -29.689 -26.356 23.011 1.00 80.15 C ANISOU 4237 CA VAL C 158 11706 10601 8148 1147 2744 -614 C ATOM 4238 C VAL C 158 -28.633 -27.070 23.845 1.00 78.63 C ANISOU 4238 C VAL C 158 11982 10457 7437 840 2626 -562 C ATOM 4239 O VAL C 158 -28.412 -26.715 25.001 1.00 82.17 O ANISOU 4239 O VAL C 158 12784 11032 7406 900 2842 -789 O ATOM 4240 CB VAL C 158 -29.068 -25.040 22.509 1.00 79.12 C ANISOU 4240 CB VAL C 158 11823 10042 8197 1406 2518 -868 C ATOM 4241 CG1 VAL C 158 -27.993 -25.309 21.473 1.00 73.35 C ANISOU 4241 CG1 VAL C 158 11196 9077 7596 1182 1985 -695 C ATOM 4242 CG2 VAL C 158 -30.137 -24.110 21.950 1.00 82.59 C ANISOU 4242 CG2 VAL C 158 11879 10411 9092 1869 2721 -900 C ATOM 4243 N TYR C 159 -27.979 -28.070 23.263 1.00 74.18 N ANISOU 4243 N TYR C 159 11421 9821 6944 547 2282 -273 N ATOM 4244 CA TYR C 159 -26.923 -28.792 23.968 1.00 73.45 C ANISOU 4244 CA TYR C 159 11718 9773 6415 338 2126 -130 C ATOM 4245 C TYR C 159 -25.601 -28.753 23.210 1.00 68.82 C ANISOU 4245 C TYR C 159 11295 8920 5933 256 1606 -125 C ATOM 4246 O TYR C 159 -25.530 -29.149 22.047 1.00 65.43 O ANISOU 4246 O TYR C 159 10650 8320 5890 180 1393 13 O ATOM 4247 CB TYR C 159 -27.341 -30.235 24.251 1.00 74.80 C ANISOU 4247 CB TYR C 159 11773 10091 6556 92 2330 290 C ATOM 4248 CG TYR C 159 -28.709 -30.362 24.884 1.00 79.94 C ANISOU 4248 CG TYR C 159 12151 11037 7186 107 2899 348 C ATOM 4249 CD1 TYR C 159 -28.927 -29.972 26.205 1.00 84.75 C ANISOU 4249 CD1 TYR C 159 13000 11960 7242 247 3291 243 C ATOM 4250 CD2 TYR C 159 -29.787 -30.872 24.159 1.00 80.60 C ANISOU 4250 CD2 TYR C 159 11700 11148 7777 -39 3054 480 C ATOM 4251 CE1 TYR C 159 -30.185 -30.082 26.786 1.00 90.39 C ANISOU 4251 CE1 TYR C 159 13421 12991 7933 279 3893 310 C ATOM 4252 CE2 TYR C 159 -31.050 -30.990 24.730 1.00 85.97 C ANISOU 4252 CE2 TYR C 159 12021 12150 8493 -52 3605 550 C ATOM 4253 CZ TYR C 159 -31.242 -30.594 26.044 1.00 90.92 C ANISOU 4253 CZ TYR C 159 12888 13070 8588 125 4058 487 C ATOM 4254 OH TYR C 159 -32.489 -30.709 26.616 1.00 97.06 O ANISOU 4254 OH TYR C 159 13274 14210 9393 127 4680 572 O ATOM 4255 N ILE C 160 -24.561 -28.269 23.886 1.00 69.60 N ANISOU 4255 N ILE C 160 11748 9041 5655 254 1415 -306 N ATOM 4256 CA ILE C 160 -23.235 -28.081 23.295 1.00 66.18 C ANISOU 4256 CA ILE C 160 11415 8415 5315 167 959 -332 C ATOM 4257 C ILE C 160 -22.183 -28.801 24.145 1.00 67.72 C ANISOU 4257 C ILE C 160 11831 8851 5048 56 742 -154 C ATOM 4258 O ILE C 160 -21.951 -28.432 25.299 1.00 71.86 O ANISOU 4258 O ILE C 160 12604 9653 5046 61 764 -342 O ATOM 4259 CB ILE C 160 -22.882 -26.573 23.195 1.00 66.86 C ANISOU 4259 CB ILE C 160 11635 8274 5493 240 871 -769 C ATOM 4260 CG1 ILE C 160 -23.953 -25.809 22.418 1.00 66.43 C ANISOU 4260 CG1 ILE C 160 11369 7980 5890 463 1101 -856 C ATOM 4261 CG2 ILE C 160 -21.534 -26.378 22.547 1.00 64.14 C ANISOU 4261 CG2 ILE C 160 11316 7754 5299 89 453 -760 C ATOM 4262 CD1 ILE C 160 -23.855 -24.301 22.555 1.00 69.84 C ANISOU 4262 CD1 ILE C 160 12006 8087 6442 598 1175 -1275 C ATOM 4263 N THR C 161 -21.553 -29.828 23.581 1.00 65.34 N ANISOU 4263 N THR C 161 11438 8471 4917 -10 534 202 N ATOM 4264 CA THR C 161 -20.561 -30.600 24.332 1.00 67.89 C ANISOU 4264 CA THR C 161 11913 9024 4857 -19 321 484 C ATOM 4265 C THR C 161 -19.220 -29.880 24.362 1.00 68.24 C ANISOU 4265 C THR C 161 11984 9159 4785 -65 -112 259 C ATOM 4266 O THR C 161 -18.950 -29.036 23.511 1.00 65.71 O ANISOU 4266 O THR C 161 11552 8591 4822 -125 -228 -8 O ATOM 4267 CB THR C 161 -20.370 -32.056 23.791 1.00 66.50 C ANISOU 4267 CB THR C 161 11645 8660 4961 -12 319 968 C ATOM 4268 OG1 THR C 161 -19.478 -32.069 22.667 1.00 63.04 O ANISOU 4268 OG1 THR C 161 11051 7997 4906 -6 33 935 O ATOM 4269 CG2 THR C 161 -21.694 -32.676 23.397 1.00 66.47 C ANISOU 4269 CG2 THR C 161 11521 8464 5272 -93 708 1085 C ATOM 4270 N ASP C 162 -18.392 -30.218 25.349 1.00 72.47 N ANISOU 4270 N ASP C 162 12637 10082 4815 -48 -349 405 N ATOM 4271 CA ASP C 162 -17.037 -29.683 25.452 1.00 74.22 C ANISOU 4271 CA ASP C 162 12781 10500 4919 -140 -816 222 C ATOM 4272 C ASP C 162 -16.133 -30.239 24.343 1.00 70.98 C ANISOU 4272 C ASP C 162 12081 9876 5013 -99 -1029 492 C ATOM 4273 O ASP C 162 -16.325 -31.370 23.877 1.00 69.33 O ANISOU 4273 O ASP C 162 11819 9481 5041 52 -885 906 O ATOM 4274 CB ASP C 162 -16.450 -30.003 26.829 1.00 80.54 C ANISOU 4274 CB ASP C 162 13724 11908 4968 -97 -1060 359 C ATOM 4275 CG ASP C 162 -15.403 -28.990 27.276 1.00 84.49 C ANISOU 4275 CG ASP C 162 14177 12737 5190 -313 -1513 -116 C ATOM 4276 OD1 ASP C 162 -15.041 -28.095 26.477 1.00 82.60 O ANISOU 4276 OD1 ASP C 162 13788 12166 5429 -513 -1606 -489 O ATOM 4277 OD2 ASP C 162 -14.944 -29.089 28.436 1.00 90.20 O ANISOU 4277 OD2 ASP C 162 15006 14070 5195 -310 -1779 -107 O ATOM 4278 N LYS C 163 -15.155 -29.433 23.927 1.00 71.02 N ANISOU 4278 N LYS C 163 11903 9885 5196 -256 -1325 227 N ATOM 4279 CA LYS C 163 -14.227 -29.791 22.844 1.00 68.64 C ANISOU 4279 CA LYS C 163 11287 9437 5356 -221 -1474 427 C ATOM 4280 C LYS C 163 -13.407 -31.030 23.181 1.00 71.20 C ANISOU 4280 C LYS C 163 11467 10035 5552 23 -1667 916 C ATOM 4281 O LYS C 163 -13.073 -31.252 24.343 1.00 76.22 O ANISOU 4281 O LYS C 163 12164 11125 5672 86 -1889 1048 O ATOM 4282 CB LYS C 163 -13.304 -28.612 22.518 1.00 69.46 C ANISOU 4282 CB LYS C 163 11195 9553 5642 -496 -1719 68 C ATOM 4283 CG LYS C 163 -12.407 -28.171 23.668 1.00 75.49 C ANISOU 4283 CG LYS C 163 11894 10830 5957 -681 -2131 -147 C ATOM 4284 CD LYS C 163 -11.962 -26.727 23.514 1.00 77.41 C ANISOU 4284 CD LYS C 163 12084 10928 6400 -1091 -2248 -686 C ATOM 4285 CE LYS C 163 -10.862 -26.381 24.496 1.00 83.70 C ANISOU 4285 CE LYS C 163 12693 12297 6811 -1359 -2747 -939 C ATOM 4286 NZ LYS C 163 -9.583 -27.041 24.123 1.00 84.58 N ANISOU 4286 NZ LYS C 163 12268 12758 7110 -1292 -3064 -558 N ATOM 4287 N CYS C 164 -13.098 -31.845 22.175 1.00 68.95 N ANISOU 4287 N CYS C 164 11008 9483 5707 199 -1568 1191 N ATOM 4288 CA CYS C 164 -12.251 -33.016 22.398 1.00 72.50 C ANISOU 4288 CA CYS C 164 11304 10091 6152 516 -1707 1672 C ATOM 4289 C CYS C 164 -11.373 -33.396 21.197 1.00 70.78 C ANISOU 4289 C CYS C 164 10757 9689 6449 660 -1692 1762 C ATOM 4290 O CYS C 164 -11.759 -33.225 20.036 1.00 66.69 O ANISOU 4290 O CYS C 164 10245 8805 6290 571 -1446 1566 O ATOM 4291 CB CYS C 164 -13.065 -34.212 22.934 1.00 74.10 C ANISOU 4291 CB CYS C 164 11811 10120 6223 738 -1443 2091 C ATOM 4292 SG CYS C 164 -13.657 -35.415 21.707 1.00 73.60 S ANISOU 4292 SG CYS C 164 11831 9358 6777 877 -1011 2262 S ATOM 4293 N VAL C 165 -10.199 -33.937 21.513 1.00 74.92 N ANISOU 4293 N VAL C 165 10976 10532 6958 923 -1952 2081 N ATOM 4294 CA VAL C 165 -9.119 -34.170 20.559 1.00 75.29 C ANISOU 4294 CA VAL C 165 10600 10568 7437 1091 -1964 2152 C ATOM 4295 C VAL C 165 -9.123 -35.588 19.985 1.00 75.81 C ANISOU 4295 C VAL C 165 10741 10215 7849 1534 -1656 2498 C ATOM 4296 O VAL C 165 -9.062 -36.568 20.734 1.00 79.96 O ANISOU 4296 O VAL C 165 11379 10737 8266 1881 -1681 2947 O ATOM 4297 CB VAL C 165 -7.757 -33.949 21.251 1.00 81.09 C ANISOU 4297 CB VAL C 165 10840 11961 8009 1164 -2439 2303 C ATOM 4298 CG1 VAL C 165 -6.624 -33.984 20.245 1.00 82.24 C ANISOU 4298 CG1 VAL C 165 10448 12171 8630 1282 -2407 2327 C ATOM 4299 CG2 VAL C 165 -7.755 -32.643 22.021 1.00 82.52 C ANISOU 4299 CG2 VAL C 165 11010 12542 7800 685 -2773 1898 C ATOM 4300 N LEU C 166 -9.173 -35.705 18.661 1.00 72.64 N ANISOU 4300 N LEU C 166 10304 9449 7848 1533 -1351 2294 N ATOM 4301 CA LEU C 166 -8.999 -37.015 18.038 1.00 74.34 C ANISOU 4301 CA LEU C 166 10571 9247 8427 1949 -1047 2502 C ATOM 4302 C LEU C 166 -7.736 -37.089 17.195 1.00 76.67 C ANISOU 4302 C LEU C 166 10390 9699 9041 2202 -1004 2503 C ATOM 4303 O LEU C 166 -7.334 -36.101 16.577 1.00 74.88 O ANISOU 4303 O LEU C 166 9884 9728 8839 1929 -1047 2236 O ATOM 4304 CB LEU C 166 -10.233 -37.442 17.232 1.00 70.71 C ANISOU 4304 CB LEU C 166 10533 8206 8128 1794 -660 2243 C ATOM 4305 CG LEU C 166 -10.556 -36.972 15.812 1.00 66.48 C ANISOU 4305 CG LEU C 166 9995 7526 7737 1569 -448 1798 C ATOM 4306 CD1 LEU C 166 -9.619 -37.559 14.783 1.00 68.72 C ANISOU 4306 CD1 LEU C 166 10064 7718 8330 1889 -230 1757 C ATOM 4307 CD2 LEU C 166 -11.967 -37.401 15.497 1.00 64.31 C ANISOU 4307 CD2 LEU C 166 10120 6829 7486 1363 -218 1597 C ATOM 4308 N ASP C 167 -7.129 -38.274 17.177 1.00 81.38 N ANISOU 4308 N ASP C 167 10901 10107 9913 2743 -864 2834 N ATOM 4309 CA ASP C 167 -5.901 -38.522 16.437 1.00 85.00 C ANISOU 4309 CA ASP C 167 10866 10718 10711 3108 -748 2879 C ATOM 4310 C ASP C 167 -6.131 -39.611 15.389 1.00 85.92 C ANISOU 4310 C ASP C 167 11263 10174 11207 3425 -221 2731 C ATOM 4311 O ASP C 167 -6.407 -40.768 15.722 1.00 89.22 O ANISOU 4311 O ASP C 167 12001 10082 11818 3781 -45 2979 O ATOM 4312 CB ASP C 167 -4.775 -38.926 17.407 1.00 92.00 C ANISOU 4312 CB ASP C 167 11285 12060 11611 3585 -1080 3414 C ATOM 4313 CG ASP C 167 -3.376 -38.840 16.784 1.00 96.60 C ANISOU 4313 CG ASP C 167 11137 13050 12515 3883 -1049 3455 C ATOM 4314 OD1 ASP C 167 -3.251 -38.512 15.582 1.00 94.82 O ANISOU 4314 OD1 ASP C 167 10816 12727 12486 3733 -708 3085 O ATOM 4315 OD2 ASP C 167 -2.388 -39.101 17.511 1.00102.98 O ANISOU 4315 OD2 ASP C 167 11425 14347 13354 4285 -1366 3893 O ATOM 4316 N MET C 168 -6.044 -39.225 14.119 1.00 83.70 N ANISOU 4316 N MET C 168 10902 9885 11014 3267 52 2312 N ATOM 4317 CA MET C 168 -5.970 -40.187 13.030 1.00 86.21 C ANISOU 4317 CA MET C 168 11388 9725 11644 3601 550 2078 C ATOM 4318 C MET C 168 -4.500 -40.572 12.879 1.00 92.62 C ANISOU 4318 C MET C 168 11617 10804 12770 4193 663 2326 C ATOM 4319 O MET C 168 -3.794 -40.043 12.018 1.00 93.30 O ANISOU 4319 O MET C 168 11303 11262 12886 4171 830 2139 O ATOM 4320 CB MET C 168 -6.520 -39.575 11.737 1.00 82.13 C ANISOU 4320 CB MET C 168 11036 9217 10954 3195 778 1541 C ATOM 4321 CG MET C 168 -8.042 -39.602 11.627 1.00 77.70 C ANISOU 4321 CG MET C 168 11047 8275 10201 2765 782 1249 C ATOM 4322 SD MET C 168 -8.780 -38.432 10.449 1.00 72.20 S ANISOU 4322 SD MET C 168 10437 7859 9135 2231 807 804 S ATOM 4323 CE MET C 168 -8.212 -39.058 8.867 1.00 76.79 C ANISOU 4323 CE MET C 168 11016 8385 9776 2518 1306 412 C ATOM 4324 N ARG C 169 -4.041 -41.483 13.737 1.00 98.10 N ANISOU 4324 N ARG C 169 12232 11342 13699 4746 588 2807 N ATOM 4325 CA ARG C 169 -2.619 -41.870 13.793 1.00105.50 C ANISOU 4325 CA ARG C 169 12507 12613 14964 5409 624 3158 C ATOM 4326 C ARG C 169 -2.112 -42.562 12.523 1.00109.53 C ANISOU 4326 C ARG C 169 12965 12792 15860 5860 1252 2842 C ATOM 4327 O ARG C 169 -0.918 -42.842 12.388 1.00116.00 O ANISOU 4327 O ARG C 169 13169 13913 16992 6441 1384 3070 O ATOM 4328 CB ARG C 169 -2.304 -42.704 15.048 1.00111.52 C ANISOU 4328 CB ARG C 169 13219 13299 15855 5975 369 3845 C ATOM 4329 CG ARG C 169 -3.324 -43.780 15.403 1.00112.48 C ANISOU 4329 CG ARG C 169 14132 12507 16098 6102 594 3974 C ATOM 4330 CD ARG C 169 -2.781 -44.687 16.494 1.00121.21 C ANISOU 4330 CD ARG C 169 15130 13533 17391 6827 439 4780 C ATOM 4331 NE ARG C 169 -3.840 -45.364 17.243 1.00121.92 N ANISOU 4331 NE ARG C 169 15939 12966 17420 6738 491 5072 N ATOM 4332 CZ ARG C 169 -3.630 -46.305 18.165 1.00129.63 C ANISOU 4332 CZ ARG C 169 17039 13657 18559 7351 464 5841 C ATOM 4333 NH1 ARG C 169 -2.395 -46.699 18.460 1.00137.53 N ANISOU 4333 NH1 ARG C 169 17461 14997 19797 8164 337 6400 N ATOM 4334 NH2 ARG C 169 -4.661 -46.858 18.793 1.00129.81 N ANISOU 4334 NH2 ARG C 169 17733 13070 18517 7167 582 6106 N ATOM 4335 N SER C 170 -3.033 -42.824 11.600 1.00106.39 N ANISOU 4335 N SER C 170 13186 11830 15409 5590 1634 2286 N ATOM 4336 CA SER C 170 -2.702 -43.283 10.258 1.00109.71 C ANISOU 4336 CA SER C 170 13647 12027 16012 5861 2236 1804 C ATOM 4337 C SER C 170 -2.114 -42.134 9.437 1.00107.65 C ANISOU 4337 C SER C 170 12872 12543 15488 5557 2284 1604 C ATOM 4338 O SER C 170 -1.319 -42.358 8.526 1.00112.61 O ANISOU 4338 O SER C 170 13202 13317 16267 5928 2754 1413 O ATOM 4339 CB SER C 170 -3.953 -43.838 9.571 1.00107.58 C ANISOU 4339 CB SER C 170 14196 11022 15658 5548 2528 1219 C ATOM 4340 OG SER C 170 -3.652 -44.367 8.293 1.00111.91 O ANISOU 4340 OG SER C 170 14856 11354 16310 5823 3116 671 O ATOM 4341 N MET C 171 -2.506 -40.908 9.771 1.00101.17 N ANISOU 4341 N MET C 171 11964 12183 14293 4893 1848 1663 N ATOM 4342 CA MET C 171 -2.062 -39.724 9.043 1.00 99.48 C ANISOU 4342 CA MET C 171 11338 12605 13854 4506 1898 1541 C ATOM 4343 C MET C 171 -1.390 -38.676 9.927 1.00 98.78 C ANISOU 4343 C MET C 171 10609 13170 13753 4221 1402 1936 C ATOM 4344 O MET C 171 -1.247 -37.521 9.516 1.00 96.51 O ANISOU 4344 O MET C 171 10085 13296 13289 3718 1368 1865 O ATOM 4345 CB MET C 171 -3.237 -39.090 8.300 1.00 93.42 C ANISOU 4345 CB MET C 171 11130 11714 12652 3900 1936 1129 C ATOM 4346 CG MET C 171 -3.646 -39.821 7.041 1.00 96.23 C ANISOU 4346 CG MET C 171 11938 11723 12901 4062 2461 610 C ATOM 4347 SD MET C 171 -5.161 -39.132 6.350 1.00 91.70 S ANISOU 4347 SD MET C 171 11976 11095 11772 3377 2340 209 S ATOM 4348 CE MET C 171 -5.442 -40.271 4.993 1.00 96.95 C ANISOU 4348 CE MET C 171 13113 11406 12316 3650 2914 -464 C ATOM 4349 N ASP C 172 -0.984 -39.076 11.133 1.00101.58 N ANISOU 4349 N ASP C 172 10702 13611 14283 4524 1019 2353 N ATOM 4350 CA ASP C 172 -0.292 -38.183 12.072 1.00102.64 C ANISOU 4350 CA ASP C 172 10198 14429 14373 4257 476 2669 C ATOM 4351 C ASP C 172 -1.037 -36.844 12.190 1.00 95.91 C ANISOU 4351 C ASP C 172 9595 13691 13156 3412 190 2446 C ATOM 4352 O ASP C 172 -0.429 -35.769 12.215 1.00 96.72 O ANISOU 4352 O ASP C 172 9187 14304 13260 2982 14 2457 O ATOM 4353 CB ASP C 172 1.160 -37.973 11.616 1.00109.41 C ANISOU 4353 CB ASP C 172 10112 15915 15545 4494 655 2812 C ATOM 4354 CG ASP C 172 2.085 -37.580 12.751 1.00114.17 C ANISOU 4354 CG ASP C 172 9924 17226 16230 4476 57 3204 C ATOM 4355 OD1 ASP C 172 2.440 -38.454 13.570 1.00119.11 O ANISOU 4355 OD1 ASP C 172 10371 17897 16988 5085 -178 3594 O ATOM 4356 OD2 ASP C 172 2.478 -36.397 12.807 1.00114.04 O ANISOU 4356 OD2 ASP C 172 9452 17728 16150 3847 -179 3129 O ATOM 4357 N PHE C 173 -2.364 -36.934 12.262 1.00 90.07 N ANISOU 4357 N PHE C 173 9628 12435 12158 3183 175 2245 N ATOM 4358 CA PHE C 173 -3.246 -35.776 12.175 1.00 83.85 C ANISOU 4358 CA PHE C 173 9173 11621 11066 2504 31 2003 C ATOM 4359 C PHE C 173 -4.181 -35.685 13.378 1.00 80.50 C ANISOU 4359 C PHE C 173 9168 11030 10389 2297 -380 2055 C ATOM 4360 O PHE C 173 -4.868 -36.652 13.722 1.00 79.87 O ANISOU 4360 O PHE C 173 9525 10535 10288 2562 -326 2117 O ATOM 4361 CB PHE C 173 -4.049 -35.845 10.871 1.00 80.64 C ANISOU 4361 CB PHE C 173 9242 10854 10542 2411 476 1661 C ATOM 4362 CG PHE C 173 -5.139 -34.816 10.766 1.00 75.01 C ANISOU 4362 CG PHE C 173 8929 10037 9533 1849 342 1475 C ATOM 4363 CD1 PHE C 173 -4.879 -33.559 10.233 1.00 74.72 C ANISOU 4363 CD1 PHE C 173 8684 10266 9442 1440 381 1457 C ATOM 4364 CD2 PHE C 173 -6.432 -35.109 11.190 1.00 71.14 C ANISOU 4364 CD2 PHE C 173 9002 9160 8867 1749 217 1357 C ATOM 4365 CE1 PHE C 173 -5.888 -32.602 10.132 1.00 70.62 C ANISOU 4365 CE1 PHE C 173 8539 9591 8703 1013 283 1339 C ATOM 4366 CE2 PHE C 173 -7.443 -34.164 11.096 1.00 67.02 C ANISOU 4366 CE2 PHE C 173 8782 8569 8114 1316 111 1210 C ATOM 4367 CZ PHE C 173 -7.171 -32.904 10.565 1.00 66.67 C ANISOU 4367 CZ PHE C 173 8554 8755 8023 985 137 1208 C ATOM 4368 N LYS C 174 -4.208 -34.508 13.998 1.00 79.03 N ANISOU 4368 N LYS C 174 8861 11143 10024 1799 -739 2009 N ATOM 4369 CA LYS C 174 -5.043 -34.253 15.170 1.00 76.80 C ANISOU 4369 CA LYS C 174 8948 10801 9433 1575 -1097 2004 C ATOM 4370 C LYS C 174 -6.030 -33.108 14.913 1.00 71.92 C ANISOU 4370 C LYS C 174 8699 9989 8637 1037 -1072 1686 C ATOM 4371 O LYS C 174 -5.714 -32.164 14.180 1.00 71.61 O ANISOU 4371 O LYS C 174 8470 10034 8706 728 -959 1555 O ATOM 4372 CB LYS C 174 -4.165 -33.941 16.385 1.00 81.49 C ANISOU 4372 CB LYS C 174 9079 11967 9918 1531 -1605 2195 C ATOM 4373 CG LYS C 174 -3.367 -35.125 16.892 1.00 86.82 C ANISOU 4373 CG LYS C 174 9431 12853 10705 2162 -1715 2625 C ATOM 4374 CD LYS C 174 -1.886 -34.793 16.928 1.00 92.97 C ANISOU 4374 CD LYS C 174 9333 14298 11692 2204 -1943 2760 C ATOM 4375 CE LYS C 174 -1.044 -36.047 16.746 1.00 98.55 C ANISOU 4375 CE LYS C 174 9654 15067 12722 2986 -1781 3166 C ATOM 4376 NZ LYS C 174 0.073 -35.816 15.794 1.00101.89 N ANISOU 4376 NZ LYS C 174 9357 15809 13547 3050 -1527 3128 N ATOM 4377 N SER C 175 -7.214 -33.193 15.528 1.00 68.96 N ANISOU 4377 N SER C 175 8830 9353 8017 953 -1142 1613 N ATOM 4378 CA SER C 175 -8.293 -32.225 15.285 1.00 64.91 C ANISOU 4378 CA SER C 175 8674 8616 7372 567 -1077 1343 C ATOM 4379 C SER C 175 -9.313 -32.064 16.423 1.00 63.56 C ANISOU 4379 C SER C 175 8879 8368 6902 441 -1251 1277 C ATOM 4380 O SER C 175 -9.918 -33.042 16.883 1.00 63.45 O ANISOU 4380 O SER C 175 9121 8200 6788 666 -1195 1418 O ATOM 4381 CB SER C 175 -9.034 -32.590 13.998 1.00 62.04 C ANISOU 4381 CB SER C 175 8568 7918 7088 651 -705 1232 C ATOM 4382 OG SER C 175 -9.468 -33.939 14.040 1.00 62.54 O ANISOU 4382 OG SER C 175 8855 7728 7178 968 -568 1302 O ATOM 4383 N ASN C 176 -9.516 -30.815 16.842 1.00 63.26 N ANISOU 4383 N ASN C 176 8891 8397 6748 74 -1400 1053 N ATOM 4384 CA ASN C 176 -10.547 -30.455 17.816 1.00 62.44 C ANISOU 4384 CA ASN C 176 9153 8227 6346 -54 -1476 903 C ATOM 4385 C ASN C 176 -11.949 -30.468 17.212 1.00 58.60 C ANISOU 4385 C ASN C 176 9010 7364 5891 -41 -1180 809 C ATOM 4386 O ASN C 176 -12.113 -30.303 15.999 1.00 56.70 O ANISOU 4386 O ASN C 176 8742 6944 5857 -45 -984 781 O ATOM 4387 CB ASN C 176 -10.260 -29.078 18.406 1.00 64.57 C ANISOU 4387 CB ASN C 176 9377 8625 6531 -440 -1689 606 C ATOM 4388 CG ASN C 176 -8.910 -29.005 19.077 1.00 69.77 C ANISOU 4388 CG ASN C 176 9623 9760 7125 -541 -2063 635 C ATOM 4389 OD1 ASN C 176 -8.422 -29.995 19.623 1.00 72.65 O ANISOU 4389 OD1 ASN C 176 9827 10443 7332 -248 -2239 917 O ATOM 4390 ND2 ASN C 176 -8.296 -27.827 19.046 1.00 72.06 N ANISOU 4390 ND2 ASN C 176 9714 10101 7565 -962 -2192 363 N ATOM 4391 N SER C 177 -12.954 -30.648 18.067 1.00 58.31 N ANISOU 4391 N SER C 177 9258 7284 5612 -26 -1151 776 N ATOM 4392 CA SER C 177 -14.335 -30.834 17.629 1.00 55.69 C ANISOU 4392 CA SER C 177 9152 6686 5322 -3 -893 718 C ATOM 4393 C SER C 177 -15.286 -30.787 18.810 1.00 56.65 C ANISOU 4393 C SER C 177 9508 6862 5153 -32 -849 669 C ATOM 4394 O SER C 177 -14.912 -31.139 19.924 1.00 59.47 O ANISOU 4394 O SER C 177 9917 7456 5221 15 -984 790 O ATOM 4395 CB SER C 177 -14.491 -32.172 16.904 1.00 55.00 C ANISOU 4395 CB SER C 177 9065 6428 5403 182 -726 888 C ATOM 4396 OG SER C 177 -13.915 -33.230 17.665 1.00 58.56 O ANISOU 4396 OG SER C 177 9517 6944 5790 376 -788 1159 O ATOM 4397 N ALA C 178 -16.519 -30.356 18.552 1.00 55.27 N ANISOU 4397 N ALA C 178 9444 6529 5026 -79 -649 520 N ATOM 4398 CA ALA C 178 -17.563 -30.243 19.572 1.00 56.81 C ANISOU 4398 CA ALA C 178 9818 6791 4975 -90 -503 450 C ATOM 4399 C ALA C 178 -18.932 -30.317 18.914 1.00 55.26 C ANISOU 4399 C ALA C 178 9588 6436 4973 -75 -253 409 C ATOM 4400 O ALA C 178 -19.211 -29.561 17.981 1.00 54.04 O ANISOU 4400 O ALA C 178 9341 6167 5026 -69 -243 288 O ATOM 4401 CB ALA C 178 -17.421 -28.933 20.349 1.00 58.97 C ANISOU 4401 CB ALA C 178 10200 7159 5046 -189 -584 142 C ATOM 4402 N VAL C 179 -19.780 -31.218 19.406 1.00 56.33 N ANISOU 4402 N VAL C 179 9767 6596 5040 -76 -54 548 N ATOM 4403 CA VAL C 179 -21.105 -31.446 18.824 1.00 55.87 C ANISOU 4403 CA VAL C 179 9572 6466 5191 -121 158 508 C ATOM 4404 C VAL C 179 -22.169 -30.617 19.536 1.00 57.78 C ANISOU 4404 C VAL C 179 9804 6839 5312 -81 367 361 C ATOM 4405 O VAL C 179 -22.171 -30.523 20.766 1.00 60.29 O ANISOU 4405 O VAL C 179 10293 7309 5305 -64 477 365 O ATOM 4406 CB VAL C 179 -21.519 -32.939 18.881 1.00 57.17 C ANISOU 4406 CB VAL C 179 9738 6522 5462 -224 321 724 C ATOM 4407 CG1 VAL C 179 -22.520 -33.252 17.787 1.00 56.62 C ANISOU 4407 CG1 VAL C 179 9437 6381 5695 -353 395 599 C ATOM 4408 CG2 VAL C 179 -20.311 -33.847 18.742 1.00 57.23 C ANISOU 4408 CG2 VAL C 179 9855 6376 5515 -161 188 918 C ATOM 4409 N ALA C 180 -23.069 -30.021 18.754 1.00 57.46 N ANISOU 4409 N ALA C 180 9551 6782 5501 -24 431 240 N ATOM 4410 CA ALA C 180 -24.201 -29.258 19.290 1.00 60.25 C ANISOU 4410 CA ALA C 180 9812 7247 5835 98 685 109 C ATOM 4411 C ALA C 180 -25.505 -29.589 18.572 1.00 61.34 C ANISOU 4411 C ALA C 180 9562 7502 6244 86 804 153 C ATOM 4412 O ALA C 180 -25.540 -29.640 17.340 1.00 60.11 O ANISOU 4412 O ALA C 180 9223 7329 6286 78 600 169 O ATOM 4413 CB ALA C 180 -23.927 -27.771 19.209 1.00 60.57 C ANISOU 4413 CB ALA C 180 9955 7147 5912 283 630 -103 C ATOM 4414 N TRP C 181 -26.574 -29.801 19.340 1.00 64.62 N ANISOU 4414 N TRP C 181 9819 8104 6631 73 1131 166 N ATOM 4415 CA TRP C 181 -27.881 -30.139 18.769 1.00 66.87 C ANISOU 4415 CA TRP C 181 9620 8589 7198 10 1244 196 C ATOM 4416 C TRP C 181 -29.029 -29.570 19.598 1.00 71.39 C ANISOU 4416 C TRP C 181 9959 9400 7767 192 1643 140 C ATOM 4417 O TRP C 181 -28.880 -29.343 20.799 1.00 73.29 O ANISOU 4417 O TRP C 181 10474 9664 7708 264 1914 96 O ATOM 4418 CB TRP C 181 -28.028 -31.660 18.639 1.00 67.42 C ANISOU 4418 CB TRP C 181 9608 8631 7376 -382 1279 334 C ATOM 4419 CG TRP C 181 -28.321 -32.348 19.940 1.00 70.27 C ANISOU 4419 CG TRP C 181 10088 9033 7580 -535 1670 509 C ATOM 4420 CD1 TRP C 181 -29.539 -32.772 20.384 1.00 74.64 C ANISOU 4420 CD1 TRP C 181 10293 9799 8268 -707 2047 591 C ATOM 4421 CD2 TRP C 181 -27.383 -32.677 20.971 1.00 69.91 C ANISOU 4421 CD2 TRP C 181 10511 8876 7175 -522 1735 678 C ATOM 4422 NE1 TRP C 181 -29.419 -33.348 21.627 1.00 77.17 N ANISOU 4422 NE1 TRP C 181 10892 10114 8316 -805 2393 833 N ATOM 4423 CE2 TRP C 181 -28.106 -33.304 22.009 1.00 74.24 C ANISOU 4423 CE2 TRP C 181 11033 9566 7607 -670 2178 900 C ATOM 4424 CE3 TRP C 181 -26.001 -32.511 21.115 1.00 66.96 C ANISOU 4424 CE3 TRP C 181 10529 8356 6557 -402 1453 694 C ATOM 4425 CZ2 TRP C 181 -27.496 -33.761 23.174 1.00 76.21 C ANISOU 4425 CZ2 TRP C 181 11691 9831 7435 -659 2328 1174 C ATOM 4426 CZ3 TRP C 181 -25.397 -32.967 22.274 1.00 68.78 C ANISOU 4426 CZ3 TRP C 181 11098 8635 6402 -395 1550 926 C ATOM 4427 CH2 TRP C 181 -26.144 -33.585 23.287 1.00 73.48 C ANISOU 4427 CH2 TRP C 181 11714 9385 6820 -502 1974 1182 C ATOM 4428 N SER C 182 -30.173 -29.349 18.957 1.00 74.10 N ANISOU 4428 N SER C 182 9765 9981 8407 287 1680 134 N ATOM 4429 CA SER C 182 -31.371 -28.880 19.654 1.00 79.61 C ANISOU 4429 CA SER C 182 10108 10961 9180 500 2108 97 C ATOM 4430 C SER C 182 -32.642 -29.459 19.041 1.00 83.56 C ANISOU 4430 C SER C 182 9879 11842 10029 328 2138 182 C ATOM 4431 O SER C 182 -32.656 -29.829 17.870 1.00 82.56 O ANISOU 4431 O SER C 182 9517 11776 10075 164 1740 196 O ATOM 4432 CB SER C 182 -31.429 -27.352 19.647 1.00 80.73 C ANISOU 4432 CB SER C 182 10316 10991 9367 1040 2153 -53 C ATOM 4433 OG SER C 182 -32.688 -26.879 20.095 1.00 86.57 O ANISOU 4433 OG SER C 182 10602 12020 10269 1342 2569 -91 O ATOM 4434 N ASN C 183 -33.706 -29.540 19.834 1.00 89.24 N ANISOU 4434 N ASN C 183 10212 12872 10824 342 2614 212 N ATOM 4435 CA ASN C 183 -34.996 -30.008 19.333 1.00 94.50 C ANISOU 4435 CA ASN C 183 10053 13982 11869 153 2665 273 C ATOM 4436 C ASN C 183 -35.907 -28.865 18.886 1.00 98.51 C ANISOU 4436 C ASN C 183 9983 14823 12625 717 2657 247 C ATOM 4437 O ASN C 183 -36.967 -29.105 18.307 1.00103.15 O ANISOU 4437 O ASN C 183 9774 15883 13535 631 2579 300 O ATOM 4438 CB ASN C 183 -35.701 -30.898 20.367 1.00 99.49 C ANISOU 4438 CB ASN C 183 10467 14812 12524 -228 3228 394 C ATOM 4439 CG ASN C 183 -36.063 -30.151 21.650 1.00103.91 C ANISOU 4439 CG ASN C 183 11116 15518 12847 173 3839 373 C ATOM 4440 OD1 ASN C 183 -35.221 -29.480 22.259 1.00101.90 O ANISOU 4440 OD1 ASN C 183 11520 14995 12204 480 3884 255 O ATOM 4441 ND2 ASN C 183 -37.320 -30.280 22.074 1.00111.23 N ANISOU 4441 ND2 ASN C 183 11359 16905 13997 143 4330 446 N ATOM 4442 N LYS C 184 -35.483 -27.629 19.154 1.00 97.77 N ANISOU 4442 N LYS C 184 10274 14467 12408 1289 2730 166 N ATOM 4443 CA LYS C 184 -36.240 -26.426 18.793 1.00102.34 C ANISOU 4443 CA LYS C 184 10420 15206 13259 1955 2778 187 C ATOM 4444 C LYS C 184 -36.198 -26.172 17.278 1.00101.37 C ANISOU 4444 C LYS C 184 10032 15179 13306 2090 2152 347 C ATOM 4445 O LYS C 184 -35.280 -26.632 16.589 1.00 96.15 O ANISOU 4445 O LYS C 184 9753 14309 12469 1759 1720 356 O ATOM 4446 CB LYS C 184 -35.707 -25.211 19.566 1.00102.36 C ANISOU 4446 CB LYS C 184 11036 14744 13111 2471 3085 1 C ATOM 4447 CG LYS C 184 -36.701 -24.068 19.722 0.01109.45 C ANISOU 4447 CG LYS C 184 11508 15752 14327 3208 3451 -20 C ATOM 4448 N SER C 185 -37.197 -25.445 16.774 1.00107.43 N ANISOU 4448 N SER C 185 10128 16308 14381 2618 2124 497 N ATOM 4449 CA SER C 185 -37.338 -25.145 15.340 1.00108.54 C ANISOU 4449 CA SER C 185 9922 16703 14617 2835 1530 731 C ATOM 4450 C SER C 185 -36.337 -24.088 14.853 1.00105.39 C ANISOU 4450 C SER C 185 10205 15720 14119 3263 1334 853 C ATOM 4451 O SER C 185 -35.697 -24.253 13.808 1.00102.19 O ANISOU 4451 O SER C 185 9994 15300 13533 3100 840 979 O ATOM 4452 CB SER C 185 -38.763 -24.668 15.038 1.00117.17 C ANISOU 4452 CB SER C 185 10013 18433 16074 3349 1569 932 C ATOM 4453 OG SER C 185 -39.721 -25.382 15.799 1.00121.68 O ANISOU 4453 OG SER C 185 9952 19463 16817 3040 1966 812 O ATOM 4454 N ASP C 186 -36.217 -23.013 15.632 1.00107.18 N ANISOU 4454 N ASP C 186 10797 15458 14470 3780 1771 786 N ATOM 4455 CA ASP C 186 -35.367 -21.852 15.337 1.00105.92 C ANISOU 4455 CA ASP C 186 11273 14624 14346 4195 1717 882 C ATOM 4456 C ASP C 186 -33.868 -22.183 15.190 1.00 98.08 C ANISOU 4456 C ASP C 186 11059 13179 13028 3675 1467 771 C ATOM 4457 O ASP C 186 -33.087 -21.372 14.682 1.00 97.04 O ANISOU 4457 O ASP C 186 11378 12562 12930 3874 1332 913 O ATOM 4458 CB ASP C 186 -35.572 -20.807 16.447 1.00110.31 C ANISOU 4458 CB ASP C 186 12102 14699 15112 4712 2333 655 C ATOM 4459 CG ASP C 186 -35.091 -19.415 16.059 1.00112.80 C ANISOU 4459 CG ASP C 186 12885 14295 15679 5281 2355 804 C ATOM 4460 OD1 ASP C 186 -34.812 -18.620 16.982 1.00115.38 O ANISOU 4460 OD1 ASP C 186 13726 14009 16103 5501 2812 467 O ATOM 4461 OD2 ASP C 186 -34.995 -19.108 14.849 1.00113.24 O ANISOU 4461 OD2 ASP C 186 12819 14384 15822 5492 1941 1248 O ATOM 4462 N PHE C 187 -33.487 -23.383 15.619 1.00 93.37 N ANISOU 4462 N PHE C 187 10576 12742 12160 3025 1433 561 N ATOM 4463 CA PHE C 187 -32.088 -23.778 15.731 1.00 86.80 C ANISOU 4463 CA PHE C 187 10419 11521 11040 2572 1279 429 C ATOM 4464 C PHE C 187 -31.413 -24.075 14.391 1.00 83.51 C ANISOU 4464 C PHE C 187 10066 11157 10507 2388 774 639 C ATOM 4465 O PHE C 187 -31.700 -25.087 13.746 1.00 82.87 O ANISOU 4465 O PHE C 187 9645 11514 10329 2059 503 668 O ATOM 4466 CB PHE C 187 -31.981 -24.981 16.667 1.00 84.52 C ANISOU 4466 CB PHE C 187 10207 11380 10527 2041 1452 221 C ATOM 4467 CG PHE C 187 -30.587 -25.484 16.862 1.00 78.59 C ANISOU 4467 CG PHE C 187 10062 10305 9494 1636 1292 127 C ATOM 4468 CD1 PHE C 187 -30.200 -26.708 16.326 1.00 75.31 C ANISOU 4468 CD1 PHE C 187 9615 10032 8967 1178 1021 182 C ATOM 4469 CD2 PHE C 187 -29.664 -24.745 17.596 1.00 77.24 C ANISOU 4469 CD2 PHE C 187 10464 9693 9191 1713 1417 -49 C ATOM 4470 CE1 PHE C 187 -28.915 -27.189 16.515 1.00 71.14 C ANISOU 4470 CE1 PHE C 187 9583 9226 8222 890 897 132 C ATOM 4471 CE2 PHE C 187 -28.375 -25.213 17.789 1.00 73.05 C ANISOU 4471 CE2 PHE C 187 10381 8962 8413 1360 1234 -110 C ATOM 4472 CZ PHE C 187 -27.996 -26.439 17.248 1.00 70.09 C ANISOU 4472 CZ PHE C 187 9936 8747 7949 991 984 16 C ATOM 4473 N ALA C 188 -30.507 -23.183 13.992 1.00 82.22 N ANISOU 4473 N ALA C 188 10354 10531 10354 2572 688 753 N ATOM 4474 CA ALA C 188 -29.718 -23.345 12.774 1.00 79.53 C ANISOU 4474 CA ALA C 188 10152 10216 9848 2424 302 968 C ATOM 4475 C ALA C 188 -28.240 -23.507 13.108 1.00 74.62 C ANISOU 4475 C ALA C 188 10122 9162 9069 2055 304 808 C ATOM 4476 O ALA C 188 -27.715 -22.806 13.976 1.00 74.71 O ANISOU 4476 O ALA C 188 10515 8702 9169 2099 540 644 O ATOM 4477 CB ALA C 188 -29.925 -22.163 11.849 1.00 83.63 C ANISOU 4477 CB ALA C 188 10616 10632 10529 2961 209 1374 C ATOM 4478 N CYS C 189 -27.578 -24.421 12.397 1.00 71.27 N ANISOU 4478 N CYS C 189 9741 8927 8413 1700 38 825 N ATOM 4479 CA CYS C 189 -26.184 -24.798 12.659 1.00 67.10 C ANISOU 4479 CA CYS C 189 9640 8112 7742 1355 16 697 C ATOM 4480 C CYS C 189 -25.187 -23.664 12.663 1.00 66.99 C ANISOU 4480 C CYS C 189 10007 7610 7835 1449 84 782 C ATOM 4481 O CYS C 189 -24.164 -23.755 13.328 1.00 64.74 O ANISOU 4481 O CYS C 189 10019 7080 7501 1190 125 602 O ATOM 4482 CB CYS C 189 -25.714 -25.849 11.661 1.00 64.99 C ANISOU 4482 CB CYS C 189 9315 8124 7254 1082 -241 724 C ATOM 4483 SG CYS C 189 -25.976 -27.544 12.207 1.00 65.14 S ANISOU 4483 SG CYS C 189 9215 8343 7192 664 -229 452 S ATOM 4484 N ALA C 190 -25.480 -22.613 11.904 1.00 70.49 N ANISOU 4484 N ALA C 190 10418 7926 8440 1806 86 1086 N ATOM 4485 CA ALA C 190 -24.622 -21.430 11.836 1.00 72.03 C ANISOU 4485 CA ALA C 190 10977 7553 8840 1872 208 1213 C ATOM 4486 C ALA C 190 -24.543 -20.708 13.173 1.00 73.53 C ANISOU 4486 C ALA C 190 11440 7248 9250 1877 483 862 C ATOM 4487 O ALA C 190 -23.452 -20.473 13.687 1.00 72.66 O ANISOU 4487 O ALA C 190 11644 6806 9157 1560 513 651 O ATOM 4488 CB ALA C 190 -25.100 -20.481 10.745 1.00 76.81 C ANISOU 4488 CB ALA C 190 11498 8094 9593 2317 195 1711 C ATOM 4489 N ASN C 191 -25.695 -20.374 13.744 1.00 76.62 N ANISOU 4489 N ASN C 191 11682 7646 9784 2226 682 760 N ATOM 4490 CA ASN C 191 -25.717 -19.656 15.012 1.00 79.46 C ANISOU 4490 CA ASN C 191 12333 7565 10294 2277 995 350 C ATOM 4491 C ASN C 191 -25.913 -20.555 16.231 1.00 77.61 C ANISOU 4491 C ASN C 191 12068 7669 9750 2038 1076 -51 C ATOM 4492 O ASN C 191 -26.685 -20.241 17.142 1.00 81.12 O ANISOU 4492 O ASN C 191 12508 8085 10229 2265 1384 -313 O ATOM 4493 CB ASN C 191 -26.736 -18.517 14.962 1.00 85.74 C ANISOU 4493 CB ASN C 191 13066 8028 11483 2888 1280 469 C ATOM 4494 CG ASN C 191 -26.306 -17.394 14.031 1.00 88.89 C ANISOU 4494 CG ASN C 191 13685 7856 12233 3106 1292 867 C ATOM 4495 OD1 ASN C 191 -25.187 -17.390 13.510 1.00 85.64 O ANISOU 4495 OD1 ASN C 191 13490 7282 11769 2740 1132 1002 O ATOM 4496 ND2 ASN C 191 -27.195 -16.431 13.822 1.00 95.76 N ANISOU 4496 ND2 ASN C 191 14485 8410 13490 3731 1524 1104 N ATOM 4497 N ALA C 192 -25.183 -21.670 16.237 1.00 72.86 N ANISOU 4497 N ALA C 192 11463 7378 8842 1610 838 -63 N ATOM 4498 CA ALA C 192 -25.288 -22.682 17.286 1.00 71.31 C ANISOU 4498 CA ALA C 192 11252 7520 8324 1374 894 -293 C ATOM 4499 C ALA C 192 -24.198 -22.512 18.330 1.00 71.34 C ANISOU 4499 C ALA C 192 11660 7340 8105 1086 883 -625 C ATOM 4500 O ALA C 192 -24.391 -22.854 19.498 1.00 72.69 O ANISOU 4500 O ALA C 192 11935 7704 7980 1016 1034 -869 O ATOM 4501 CB ALA C 192 -25.224 -24.071 16.685 1.00 67.36 C ANISOU 4501 CB ALA C 192 10503 7424 7665 1133 662 -79 C ATOM 4502 N PHE C 193 -23.054 -21.992 17.898 1.00 70.57 N ANISOU 4502 N PHE C 193 11758 6935 8120 902 699 -615 N ATOM 4503 CA PHE C 193 -21.931 -21.763 18.791 1.00 71.52 C ANISOU 4503 CA PHE C 193 12178 6941 8055 576 605 -948 C ATOM 4504 C PHE C 193 -21.737 -20.270 18.998 1.00 76.69 C ANISOU 4504 C PHE C 193 13128 7005 9007 611 766 -1249 C ATOM 4505 O PHE C 193 -20.633 -19.803 19.281 1.00 78.29 O ANISOU 4505 O PHE C 193 13530 6989 9226 266 627 -1486 O ATOM 4506 CB PHE C 193 -20.667 -22.416 18.238 1.00 67.79 C ANISOU 4506 CB PHE C 193 11628 6609 7520 260 281 -746 C ATOM 4507 CG PHE C 193 -20.779 -23.900 18.074 1.00 63.46 C ANISOU 4507 CG PHE C 193 10864 6510 6739 230 163 -504 C ATOM 4508 CD1 PHE C 193 -21.270 -24.448 16.896 1.00 61.05 C ANISOU 4508 CD1 PHE C 193 10314 6315 6567 354 135 -190 C ATOM 4509 CD2 PHE C 193 -20.398 -24.755 19.097 1.00 63.18 C ANISOU 4509 CD2 PHE C 193 10891 6774 6341 77 83 -589 C ATOM 4510 CE1 PHE C 193 -21.382 -25.826 16.742 1.00 58.54 C ANISOU 4510 CE1 PHE C 193 9842 6302 6097 279 59 -48 C ATOM 4511 CE2 PHE C 193 -20.504 -26.140 18.953 1.00 60.41 C ANISOU 4511 CE2 PHE C 193 10390 6700 5862 60 30 -333 C ATOM 4512 CZ PHE C 193 -20.994 -26.673 17.777 1.00 58.31 C ANISOU 4512 CZ PHE C 193 9906 6443 5806 137 34 -104 C ATOM 4513 N ASN C 194 -22.833 -19.527 18.867 1.00 80.27 N ANISOU 4513 N ASN C 194 13581 7183 9734 1030 1071 -1248 N ATOM 4514 CA ASN C 194 -22.812 -18.082 19.067 1.00 86.56 C ANISOU 4514 CA ASN C 194 14706 7277 10907 1149 1317 -1539 C ATOM 4515 C ASN C 194 -22.777 -17.675 20.543 1.00 91.31 C ANISOU 4515 C ASN C 194 15654 7791 11250 1033 1504 -2242 C ATOM 4516 O ASN C 194 -23.038 -16.519 20.891 1.00 97.59 O ANISOU 4516 O ASN C 194 16753 7982 12343 1205 1812 -2616 O ATOM 4517 CB ASN C 194 -23.968 -17.412 18.315 1.00 89.62 C ANISOU 4517 CB ASN C 194 14950 7374 11729 1742 1583 -1211 C ATOM 4518 CG ASN C 194 -23.660 -17.196 16.833 1.00 88.51 C ANISOU 4518 CG ASN C 194 14672 7063 11894 1809 1414 -598 C ATOM 4519 OD1 ASN C 194 -22.873 -17.930 16.224 1.00 83.62 O ANISOU 4519 OD1 ASN C 194 13924 6764 11084 1477 1110 -352 O ATOM 4520 ND2 ASN C 194 -24.284 -16.181 16.249 1.00 94.01 N ANISOU 4520 ND2 ASN C 194 15407 7265 13048 2286 1641 -324 N ATOM 4521 N ASN C 195 -22.464 -18.647 21.400 1.00 89.13 N ANISOU 4521 N ASN C 195 15352 8119 10394 765 1334 -2412 N ATOM 4522 CA ASN C 195 -22.079 -18.399 22.789 1.00 93.67 C ANISOU 4522 CA ASN C 195 16272 8788 10530 524 1371 -3067 C ATOM 4523 C ASN C 195 -20.561 -18.355 22.880 1.00 93.26 C ANISOU 4523 C ASN C 195 16321 8735 10378 -43 946 -3231 C ATOM 4524 O ASN C 195 -19.983 -17.558 23.629 1.00 98.94 O ANISOU 4524 O ASN C 195 17364 9210 11019 -338 921 -3847 O ATOM 4525 CB ASN C 195 -22.613 -19.505 23.700 1.00 92.71 C ANISOU 4525 CB ASN C 195 16051 9406 9767 587 1432 -3050 C ATOM 4526 CG ASN C 195 -24.009 -19.224 24.199 1.00 97.16 C ANISOU 4526 CG ASN C 195 16615 9988 10314 1051 1958 -3219 C ATOM 4527 OD1 ASN C 195 -24.253 -18.207 24.854 1.00104.02 O ANISOU 4527 OD1 ASN C 195 17815 10500 11208 1188 2273 -3792 O ATOM 4528 ND2 ASN C 195 -24.939 -20.132 23.902 1.00 94.40 N ANISOU 4528 ND2 ASN C 195 15872 10051 9945 1281 2085 -2757 N ATOM 4529 N SER C 196 -19.941 -19.231 22.093 1.00 86.88 N ANISOU 4529 N SER C 196 15198 8225 9589 -193 622 -2704 N ATOM 4530 CA SER C 196 -18.502 -19.382 22.016 1.00 85.89 C ANISOU 4530 CA SER C 196 14999 8221 9414 -670 216 -2716 C ATOM 4531 C SER C 196 -17.892 -18.281 21.147 1.00 87.84 C ANISOU 4531 C SER C 196 15298 7784 10294 -873 243 -2706 C ATOM 4532 O SER C 196 -18.611 -17.575 20.440 1.00 88.81 O ANISOU 4532 O SER C 196 15501 7367 10876 -567 548 -2529 O ATOM 4533 CB SER C 196 -18.195 -20.755 21.421 1.00 79.38 C ANISOU 4533 CB SER C 196 13812 7912 8435 -642 -26 -2135 C ATOM 4534 OG SER C 196 -16.909 -21.202 21.794 1.00 79.94 O ANISOU 4534 OG SER C 196 13766 8349 8258 -1006 -415 -2179 O ATOM 4535 N ILE C 197 -16.571 -18.129 21.214 1.00 89.27 N ANISOU 4535 N ILE C 197 15403 8005 10510 -1382 -65 -2851 N ATOM 4536 CA ILE C 197 -15.844 -17.240 20.307 1.00 91.18 C ANISOU 4536 CA ILE C 197 15618 7655 11371 -1667 -26 -2724 C ATOM 4537 C ILE C 197 -15.299 -18.045 19.128 1.00 85.43 C ANISOU 4537 C ILE C 197 14484 7235 10740 -1646 -171 -2041 C ATOM 4538 O ILE C 197 -14.506 -18.976 19.311 1.00 83.14 O ANISOU 4538 O ILE C 197 13902 7548 10139 -1820 -489 -1947 O ATOM 4539 CB ILE C 197 -14.678 -16.509 21.019 1.00 97.89 C ANISOU 4539 CB ILE C 197 16550 8356 12286 -2328 -246 -3327 C ATOM 4540 CG1 ILE C 197 -15.189 -15.674 22.205 1.00104.90 C ANISOU 4540 CG1 ILE C 197 17909 8924 13025 -2378 -84 -4141 C ATOM 4541 CG2 ILE C 197 -13.857 -15.676 20.022 1.00100.28 C ANISOU 4541 CG2 ILE C 197 16760 8055 13287 -2701 -163 -3102 C ATOM 4542 CD1 ILE C 197 -16.160 -14.548 21.852 1.00108.59 C ANISOU 4542 CD1 ILE C 197 18765 8437 14056 -2040 443 -4227 C ATOM 4543 N ILE C 198 -15.725 -17.681 17.922 1.00 83.87 N ANISOU 4543 N ILE C 198 14275 6643 10947 -1391 76 -1559 N ATOM 4544 CA ILE C 198 -15.294 -18.375 16.707 1.00 79.19 C ANISOU 4544 CA ILE C 198 13352 6344 10392 -1335 5 -950 C ATOM 4545 C ILE C 198 -14.682 -17.405 15.698 1.00 82.42 C ANISOU 4545 C ILE C 198 13771 6215 11331 -1548 190 -644 C ATOM 4546 O ILE C 198 -15.183 -16.299 15.539 1.00 86.91 O ANISOU 4546 O ILE C 198 14637 6093 12293 -1446 469 -646 O ATOM 4547 CB ILE C 198 -16.451 -19.168 16.062 1.00 74.34 C ANISOU 4547 CB ILE C 198 12651 6015 9580 -795 89 -553 C ATOM 4548 CG1 ILE C 198 -17.743 -18.340 16.079 1.00 77.08 C ANISOU 4548 CG1 ILE C 198 13242 5910 10134 -391 379 -578 C ATOM 4549 CG2 ILE C 198 -16.621 -20.526 16.766 1.00 70.13 C ANISOU 4549 CG2 ILE C 198 11971 6129 8545 -722 -118 -660 C ATOM 4550 CD1 ILE C 198 -18.937 -19.022 15.446 1.00 74.21 C ANISOU 4550 CD1 ILE C 198 12701 5883 9612 99 424 -216 C ATOM 4551 N PRO C 199 -13.592 -17.818 15.018 1.00 81.10 N ANISOU 4551 N PRO C 199 13277 6343 11196 -1817 84 -345 N ATOM 4552 CA PRO C 199 -12.859 -16.931 14.097 1.00 85.13 C ANISOU 4552 CA PRO C 199 13754 6402 12191 -2108 306 -11 C ATOM 4553 C PRO C 199 -13.653 -16.472 12.865 1.00 85.12 C ANISOU 4553 C PRO C 199 13918 6060 12364 -1676 624 603 C ATOM 4554 O PRO C 199 -14.745 -16.973 12.607 1.00 81.28 O ANISOU 4554 O PRO C 199 13476 5811 11595 -1149 615 774 O ATOM 4555 CB PRO C 199 -11.655 -17.781 13.671 1.00 83.22 C ANISOU 4555 CB PRO C 199 13036 6773 11809 -2360 140 191 C ATOM 4556 CG PRO C 199 -12.051 -19.183 13.946 1.00 77.11 C ANISOU 4556 CG PRO C 199 12119 6677 10502 -1997 -97 160 C ATOM 4557 CD PRO C 199 -12.949 -19.142 15.130 1.00 76.80 C ANISOU 4557 CD PRO C 199 12365 6556 10259 -1853 -202 -296 C ATOM 4558 N GLU C 200 -13.099 -15.510 12.128 1.00 90.29 N ANISOU 4558 N GLU C 200 14639 6187 13479 -1921 899 956 N ATOM 4559 CA GLU C 200 -13.682 -15.049 10.867 1.00 91.71 C ANISOU 4559 CA GLU C 200 14960 6114 13772 -1515 1194 1675 C ATOM 4560 C GLU C 200 -13.715 -16.179 9.845 1.00 86.17 C ANISOU 4560 C GLU C 200 13963 6232 12544 -1217 1096 2117 C ATOM 4561 O GLU C 200 -14.783 -16.558 9.361 1.00 83.55 O ANISOU 4561 O GLU C 200 13678 6166 11903 -679 1052 2358 O ATOM 4562 CB GLU C 200 -12.894 -13.862 10.292 1.00 99.49 C ANISOU 4562 CB GLU C 200 16064 6387 15349 -1919 1549 2038 C ATOM 4563 CG GLU C 200 -13.194 -12.510 10.936 1.00107.16 C ANISOU 4563 CG GLU C 200 17481 6282 16952 -2055 1785 1757 C ATOM 4564 CD GLU C 200 -12.308 -12.196 12.137 1.00110.97 C ANISOU 4564 CD GLU C 200 17942 6515 17708 -2792 1642 939 C ATOM 4565 OE1 GLU C 200 -11.946 -11.006 12.310 1.00119.07 O ANISOU 4565 OE1 GLU C 200 19243 6606 19393 -3221 1915 800 O ATOM 4566 OE2 GLU C 200 -11.974 -13.132 12.903 1.00106.10 O ANISOU 4566 OE2 GLU C 200 17039 6629 16646 -2949 1252 442 O ATOM 4567 N ASP C 201 -12.535 -16.725 9.549 1.00 85.04 N ANISOU 4567 N ASP C 201 13489 6512 12310 -1581 1060 2165 N ATOM 4568 CA ASP C 201 -12.349 -17.764 8.524 1.00 81.10 C ANISOU 4568 CA ASP C 201 12730 6741 11344 -1356 1046 2516 C ATOM 4569 C ASP C 201 -12.996 -19.125 8.842 1.00 73.97 C ANISOU 4569 C ASP C 201 11720 6451 9936 -1020 737 2213 C ATOM 4570 O ASP C 201 -12.538 -20.173 8.374 1.00 71.06 O ANISOU 4570 O ASP C 201 11103 6652 9245 -973 681 2246 O ATOM 4571 CB ASP C 201 -10.853 -17.915 8.177 1.00 83.44 C ANISOU 4571 CB ASP C 201 12662 7281 11759 -1814 1170 2624 C ATOM 4572 CG ASP C 201 -9.964 -18.117 9.408 1.00 83.28 C ANISOU 4572 CG ASP C 201 12380 7325 11936 -2281 918 2046 C ATOM 4573 OD1 ASP C 201 -10.435 -17.950 10.557 1.00 82.18 O ANISOU 4573 OD1 ASP C 201 12424 6950 11849 -2322 687 1555 O ATOM 4574 OD2 ASP C 201 -8.772 -18.441 9.215 1.00 84.71 O ANISOU 4574 OD2 ASP C 201 12139 7859 12188 -2592 954 2095 O ATOM 4575 N THR C 202 -14.066 -19.097 9.631 1.00 71.76 N ANISOU 4575 N THR C 202 11632 6009 9625 -789 593 1919 N ATOM 4576 CA THR C 202 -14.839 -20.293 9.913 1.00 66.17 C ANISOU 4576 CA THR C 202 10846 5789 8508 -500 365 1696 C ATOM 4577 C THR C 202 -15.830 -20.533 8.773 1.00 65.69 C ANISOU 4577 C THR C 202 10801 5997 8163 -67 396 2076 C ATOM 4578 O THR C 202 -16.576 -19.636 8.369 1.00 68.65 O ANISOU 4578 O THR C 202 11335 6076 8671 190 512 2381 O ATOM 4579 CB THR C 202 -15.549 -20.236 11.294 1.00 65.02 C ANISOU 4579 CB THR C 202 10843 5458 8404 -466 237 1220 C ATOM 4580 OG1 THR C 202 -14.599 -19.898 12.310 1.00 66.06 O ANISOU 4580 OG1 THR C 202 10976 5402 8723 -895 166 849 O ATOM 4581 CG2 THR C 202 -16.170 -21.589 11.644 1.00 60.45 C ANISOU 4581 CG2 THR C 202 10144 5385 7440 -273 46 1032 C ATOM 4582 N PHE C 203 -15.802 -21.759 8.260 1.00 62.68 N ANISOU 4582 N PHE C 203 10243 6181 7390 18 281 2041 N ATOM 4583 CA PHE C 203 -16.605 -22.178 7.123 1.00 63.01 C ANISOU 4583 CA PHE C 203 10252 6634 7056 340 242 2294 C ATOM 4584 C PHE C 203 -17.969 -22.662 7.606 1.00 61.23 C ANISOU 4584 C PHE C 203 9995 6547 6721 570 46 2056 C ATOM 4585 O PHE C 203 -18.061 -23.625 8.379 1.00 57.89 O ANISOU 4585 O PHE C 203 9501 6253 6243 466 -74 1671 O ATOM 4586 CB PHE C 203 -15.853 -23.284 6.373 1.00 61.68 C ANISOU 4586 CB PHE C 203 9934 6957 6545 265 254 2247 C ATOM 4587 CG PHE C 203 -16.567 -23.823 5.166 1.00 62.38 C ANISOU 4587 CG PHE C 203 10002 7554 6147 522 187 2382 C ATOM 4588 CD1 PHE C 203 -16.903 -22.995 4.104 1.00 66.53 C ANISOU 4588 CD1 PHE C 203 10606 8193 6478 734 270 2888 C ATOM 4589 CD2 PHE C 203 -16.857 -25.179 5.071 1.00 60.29 C ANISOU 4589 CD2 PHE C 203 9650 7660 5597 535 40 2002 C ATOM 4590 CE1 PHE C 203 -17.548 -23.503 2.981 1.00 68.46 C ANISOU 4590 CE1 PHE C 203 10813 9037 6160 957 144 2980 C ATOM 4591 CE2 PHE C 203 -17.501 -25.700 3.946 1.00 62.04 C ANISOU 4591 CE2 PHE C 203 9851 8390 5330 698 -59 2011 C ATOM 4592 CZ PHE C 203 -17.844 -24.860 2.904 1.00 66.34 C ANISOU 4592 CZ PHE C 203 10445 9169 5593 907 -37 2483 C ATOM 4593 N PHE C 204 -19.018 -21.959 7.176 1.00 64.30 N ANISOU 4593 N PHE C 204 10412 6903 7116 896 38 2339 N ATOM 4594 CA PHE C 204 -20.400 -22.340 7.470 1.00 63.86 C ANISOU 4594 CA PHE C 204 10213 7072 6977 1139 -128 2182 C ATOM 4595 C PHE C 204 -21.122 -22.679 6.163 1.00 66.50 C ANISOU 4595 C PHE C 204 10376 7995 6897 1386 -300 2450 C ATOM 4596 O PHE C 204 -21.785 -21.812 5.577 1.00 70.87 O ANISOU 4596 O PHE C 204 10907 8569 7453 1741 -310 2882 O ATOM 4597 CB PHE C 204 -21.156 -21.210 8.179 1.00 66.54 C ANISOU 4597 CB PHE C 204 10639 6942 7701 1389 -13 2246 C ATOM 4598 CG PHE C 204 -20.607 -20.837 9.531 1.00 65.12 C ANISOU 4598 CG PHE C 204 10652 6241 7848 1140 126 1871 C ATOM 4599 CD1 PHE C 204 -19.670 -19.808 9.657 1.00 67.29 C ANISOU 4599 CD1 PHE C 204 11166 5955 8445 957 312 1964 C ATOM 4600 CD2 PHE C 204 -21.060 -21.476 10.680 1.00 62.00 C ANISOU 4600 CD2 PHE C 204 10200 5937 7419 1066 80 1428 C ATOM 4601 CE1 PHE C 204 -19.171 -19.443 10.900 1.00 66.73 C ANISOU 4601 CE1 PHE C 204 11263 5472 8619 679 384 1533 C ATOM 4602 CE2 PHE C 204 -20.569 -21.116 11.931 1.00 61.87 C ANISOU 4602 CE2 PHE C 204 10381 5549 7578 849 177 1065 C ATOM 4603 CZ PHE C 204 -19.622 -20.096 12.038 1.00 64.51 C ANISOU 4603 CZ PHE C 204 10942 5371 8197 648 298 1076 C ATOM 4604 N PRO C 205 -20.998 -23.936 5.696 1.00 64.84 N ANISOU 4604 N PRO C 205 10051 8268 6318 1218 -442 2188 N ATOM 4605 CA PRO C 205 -21.610 -24.306 4.425 1.00 68.38 C ANISOU 4605 CA PRO C 205 10351 9353 6279 1380 -644 2331 C ATOM 4606 C PRO C 205 -23.133 -24.164 4.476 1.00 71.30 C ANISOU 4606 C PRO C 205 10438 9998 6654 1647 -875 2370 C ATOM 4607 O PRO C 205 -23.755 -24.583 5.459 1.00 69.11 O ANISOU 4607 O PRO C 205 10017 9607 6634 1556 -900 2032 O ATOM 4608 CB PRO C 205 -21.204 -25.776 4.261 1.00 65.71 C ANISOU 4608 CB PRO C 205 9985 9301 5681 1081 -706 1843 C ATOM 4609 CG PRO C 205 -20.956 -26.252 5.631 1.00 61.12 C ANISOU 4609 CG PRO C 205 9436 8292 5494 863 -620 1493 C ATOM 4610 CD PRO C 205 -20.360 -25.092 6.350 1.00 60.54 C ANISOU 4610 CD PRO C 205 9517 7695 5792 896 -432 1728 C ATOM 4611 N SER C 206 -23.717 -23.558 3.441 1.00 77.16 N ANISOU 4611 N SER C 206 11069 11140 7107 1994 -1027 2830 N ATOM 4612 CA SER C 206 -25.173 -23.416 3.353 1.00 81.44 C ANISOU 4612 CA SER C 206 11226 12086 7632 2304 -1295 2925 C ATOM 4613 C SER C 206 -25.859 -24.781 3.368 1.00 80.87 C ANISOU 4613 C SER C 206 10832 12547 7349 1993 -1568 2352 C ATOM 4614 O SER C 206 -25.445 -25.685 2.640 1.00 81.04 O ANISOU 4614 O SER C 206 10913 12941 6936 1720 -1686 2075 O ATOM 4615 CB SER C 206 -25.583 -22.619 2.112 1.00 88.47 C ANISOU 4615 CB SER C 206 12033 13439 8143 2761 -1471 3585 C ATOM 4616 OG SER C 206 -25.806 -21.258 2.438 1.00 91.45 O ANISOU 4616 OG SER C 206 12500 13278 8969 3211 -1270 4130 O ATOM 4617 N PRO C 207 -26.903 -24.936 4.206 1.00 81.20 N ANISOU 4617 N PRO C 207 10537 12591 7725 2015 -1618 2149 N ATOM 4618 CA PRO C 207 -27.555 -26.238 4.384 1.00 81.06 C ANISOU 4618 CA PRO C 207 10208 12945 7646 1621 -1802 1601 C ATOM 4619 C PRO C 207 -28.525 -26.633 3.256 1.00 87.64 C ANISOU 4619 C PRO C 207 10587 14684 8028 1640 -2261 1565 C ATOM 4620 O PRO C 207 -28.821 -27.822 3.097 1.00 88.26 O ANISOU 4620 O PRO C 207 10496 15073 7966 1191 -2432 1037 O ATOM 4621 CB PRO C 207 -28.308 -26.067 5.703 1.00 79.85 C ANISOU 4621 CB PRO C 207 9837 12482 8020 1670 -1612 1503 C ATOM 4622 CG PRO C 207 -28.633 -24.611 5.758 1.00 82.78 C ANISOU 4622 CG PRO C 207 10179 12668 8604 2256 -1516 2029 C ATOM 4623 CD PRO C 207 -27.521 -23.890 5.044 1.00 82.45 C ANISOU 4623 CD PRO C 207 10593 12364 8371 2402 -1442 2411 C ATOM 4624 N GLU C 208 -29.003 -25.652 2.487 1.00 93.39 N ANISOU 4624 N GLU C 208 11126 15822 8535 2146 -2466 2122 N ATOM 4625 CA GLU C 208 -29.981 -25.900 1.419 1.00101.04 C ANISOU 4625 CA GLU C 208 11591 17791 9007 2229 -2985 2153 C ATOM 4626 C GLU C 208 -29.432 -25.493 0.050 1.00105.38 C ANISOU 4626 C GLU C 208 12388 18807 8843 2469 -3168 2564 C ATOM 4627 O GLU C 208 -30.090 -25.669 -0.981 1.00112.44 O ANISOU 4627 O GLU C 208 12938 20642 9142 2551 -3644 2613 O ATOM 4628 CB GLU C 208 -31.306 -25.171 1.702 1.00106.23 C ANISOU 4628 CB GLU C 208 11629 18756 9977 2704 -3146 2517 C ATOM 4629 CG GLU C 208 -32.000 -25.583 3.008 1.00103.94 C ANISOU 4629 CG GLU C 208 11006 18162 10325 2482 -2933 2129 C ATOM 4630 CD GLU C 208 -33.193 -24.701 3.350 1.00109.48 C ANISOU 4630 CD GLU C 208 11114 19083 11401 3070 -2962 2540 C ATOM 4631 OE1 GLU C 208 -34.145 -24.641 2.543 1.00116.94 O ANISOU 4631 OE1 GLU C 208 11429 20927 12074 3302 -3434 2741 O ATOM 4632 OE2 GLU C 208 -33.182 -24.076 4.434 1.00106.79 O ANISOU 4632 OE2 GLU C 208 10914 18051 11611 3317 -2515 2636 O TER 4633 GLU C 208 ATOM 4634 N ALA D 3 -1.822 -59.019 38.524 1.00129.13 N ANISOU 4634 N ALA D 3 18802 15954 14308 6657 719 -2845 N ATOM 4635 CA ALA D 3 -2.589 -57.798 38.915 1.00121.22 C ANISOU 4635 CA ALA D 3 17527 15261 13270 5899 727 -2274 C ATOM 4636 C ALA D 3 -3.779 -58.133 39.822 1.00116.69 C ANISOU 4636 C ALA D 3 17181 14035 13120 5175 87 -2212 C ATOM 4637 O ALA D 3 -3.914 -59.266 40.285 1.00119.12 O ANISOU 4637 O ALA D 3 17781 13640 13839 5182 -366 -2479 O ATOM 4638 CB ALA D 3 -3.049 -57.041 37.669 1.00122.63 C ANISOU 4638 CB ALA D 3 17808 16111 12673 5995 974 -2354 C ATOM 4639 N VAL D 4 -4.631 -57.139 40.070 1.00110.87 N ANISOU 4639 N VAL D 4 16275 13543 12306 4571 62 -1819 N ATOM 4640 CA VAL D 4 -5.805 -57.288 40.938 1.00106.72 C ANISOU 4640 CA VAL D 4 15855 12565 12130 3879 -448 -1657 C ATOM 4641 C VAL D 4 -7.095 -57.377 40.108 1.00108.24 C ANISOU 4641 C VAL D 4 16442 12737 11948 3672 -801 -1949 C ATOM 4642 O VAL D 4 -7.375 -56.497 39.292 1.00107.77 O ANISOU 4642 O VAL D 4 16320 13232 11397 3697 -557 -1881 O ATOM 4643 CB VAL D 4 -5.909 -56.116 41.954 1.00 99.50 C ANISOU 4643 CB VAL D 4 14444 11912 11450 3355 -253 -1018 C ATOM 4644 CG1 VAL D 4 -7.059 -56.340 42.923 1.00 96.22 C ANISOU 4644 CG1 VAL D 4 14092 11107 11361 2720 -712 -834 C ATOM 4645 CG2 VAL D 4 -4.601 -55.941 42.717 1.00 98.54 C ANISOU 4645 CG2 VAL D 4 13913 11866 11661 3529 47 -721 C ATOM 4646 N THR D 5 -7.874 -58.436 40.322 1.00110.62 N ANISOU 4646 N THR D 5 17120 12393 12519 3442 -1413 -2217 N ATOM 4647 CA THR D 5 -9.098 -58.658 39.549 1.00113.19 C ANISOU 4647 CA THR D 5 17821 12629 12556 3214 -1862 -2508 C ATOM 4648 C THR D 5 -10.352 -58.514 40.412 1.00108.96 C ANISOU 4648 C THR D 5 17134 11867 12399 2443 -2253 -2078 C ATOM 4649 O THR D 5 -10.846 -59.490 40.982 1.00110.93 O ANISOU 4649 O THR D 5 17554 11481 13114 2146 -2783 -2105 O ATOM 4650 CB THR D 5 -9.090 -60.037 38.843 1.00121.54 C ANISOU 4650 CB THR D 5 19488 13114 13577 3587 -2346 -3249 C ATOM 4651 OG1 THR D 5 -7.803 -60.271 38.261 1.00125.97 O ANISOU 4651 OG1 THR D 5 20129 13863 13870 4383 -1921 -3629 O ATOM 4652 CG2 THR D 5 -10.152 -60.094 37.749 1.00125.37 C ANISOU 4652 CG2 THR D 5 20371 13693 13570 3470 -2749 -3629 C ATOM 4653 N GLN D 6 -10.860 -57.289 40.498 1.00103.85 N ANISOU 4653 N GLN D 6 16139 11747 11573 2140 -1980 -1649 N ATOM 4654 CA GLN D 6 -12.075 -57.009 41.258 1.00100.27 C ANISOU 4654 CA GLN D 6 15475 11216 11408 1486 -2248 -1226 C ATOM 4655 C GLN D 6 -13.317 -56.963 40.361 1.00102.95 C ANISOU 4655 C GLN D 6 16006 11646 11466 1254 -2632 -1352 C ATOM 4656 O GLN D 6 -13.224 -56.643 39.171 1.00105.61 O ANISOU 4656 O GLN D 6 16529 12340 11258 1573 -2529 -1635 O ATOM 4657 CB GLN D 6 -11.928 -55.709 42.061 1.00 93.71 C ANISOU 4657 CB GLN D 6 14129 10828 10648 1301 -1758 -690 C ATOM 4658 CG GLN D 6 -11.539 -54.479 41.239 1.00 92.01 C ANISOU 4658 CG GLN D 6 13744 11221 9993 1572 -1270 -622 C ATOM 4659 CD GLN D 6 -11.479 -53.200 42.062 1.00 85.90 C ANISOU 4659 CD GLN D 6 12500 10748 9390 1353 -890 -136 C ATOM 4660 OE1 GLN D 6 -10.586 -52.371 41.878 1.00 84.30 O ANISOU 4660 OE1 GLN D 6 12082 10867 9080 1597 -454 -8 O ATOM 4661 NE2 GLN D 6 -12.434 -53.033 42.970 1.00 82.99 N ANISOU 4661 NE2 GLN D 6 11959 10276 9297 899 -1065 139 N ATOM 4662 N SER D 7 -14.468 -57.297 40.946 1.00102.85 N ANISOU 4662 N SER D 7 15911 11353 11815 695 -3082 -1092 N ATOM 4663 CA SER D 7 -15.763 -57.286 40.253 1.00105.67 C ANISOU 4663 CA SER D 7 16357 11769 12024 372 -3531 -1104 C ATOM 4664 C SER D 7 -16.921 -57.226 41.260 1.00103.49 C ANISOU 4664 C SER D 7 15702 11403 12218 -266 -3764 -538 C ATOM 4665 O SER D 7 -16.792 -57.741 42.373 1.00102.43 O ANISOU 4665 O SER D 7 15431 10949 12539 -476 -3815 -287 O ATOM 4666 CB SER D 7 -15.912 -58.506 39.329 1.00113.52 C ANISOU 4666 CB SER D 7 17934 12283 12915 496 -4164 -1728 C ATOM 4667 OG SER D 7 -16.147 -59.699 40.060 1.00116.59 O ANISOU 4667 OG SER D 7 18448 11933 13918 192 -4691 -1720 O ATOM 4668 N PRO D 8 -18.062 -56.617 40.875 1.00103.53 N ANISOU 4668 N PRO D 8 15504 11730 12104 -560 -3902 -293 N ATOM 4669 CA PRO D 8 -18.412 -56.079 39.558 1.00105.88 C ANISOU 4669 CA PRO D 8 15945 12410 11875 -397 -3964 -499 C ATOM 4670 C PRO D 8 -17.658 -54.795 39.227 1.00102.00 C ANISOU 4670 C PRO D 8 15272 12502 10980 7 -3267 -409 C ATOM 4671 O PRO D 8 -17.393 -53.987 40.117 1.00 96.69 O ANISOU 4671 O PRO D 8 14209 12010 10518 -24 -2793 -30 O ATOM 4672 CB PRO D 8 -19.910 -55.800 39.684 1.00106.38 C ANISOU 4672 CB PRO D 8 15666 12603 12149 -928 -4304 -48 C ATOM 4673 CG PRO D 8 -20.107 -55.502 41.117 1.00101.73 C ANISOU 4673 CG PRO D 8 14599 12026 12028 -1198 -4007 485 C ATOM 4674 CD PRO D 8 -19.117 -56.343 41.868 1.00101.35 C ANISOU 4674 CD PRO D 8 14746 11535 12226 -1080 -3956 315 C ATOM 4675 N ARG D 9 -17.318 -54.624 37.951 1.00105.39 N ANISOU 4675 N ARG D 9 15991 13226 10828 376 -3235 -748 N ATOM 4676 CA ARG D 9 -16.582 -53.449 37.486 1.00103.07 C ANISOU 4676 CA ARG D 9 15517 13498 10146 749 -2613 -596 C ATOM 4677 C ARG D 9 -17.488 -52.219 37.469 1.00100.30 C ANISOU 4677 C ARG D 9 14735 13547 9828 496 -2491 -56 C ATOM 4678 O ARG D 9 -17.027 -51.099 37.235 1.00 98.10 O ANISOU 4678 O ARG D 9 14218 13676 9380 707 -2007 210 O ATOM 4679 CB ARG D 9 -15.999 -53.697 36.088 1.00108.78 C ANISOU 4679 CB ARG D 9 16664 14502 10166 1233 -2616 -1071 C ATOM 4680 CG ARG D 9 -15.181 -54.987 35.943 1.00113.66 C ANISOU 4680 CG ARG D 9 17764 14698 10722 1579 -2786 -1714 C ATOM 4681 CD ARG D 9 -13.716 -54.813 36.353 1.00111.80 C ANISOU 4681 CD ARG D 9 17396 14541 10543 2017 -2157 -1711 C ATOM 4682 NE ARG D 9 -12.901 -54.230 35.285 1.00114.48 N ANISOU 4682 NE ARG D 9 17765 15517 10214 2550 -1687 -1793 N ATOM 4683 CZ ARG D 9 -12.531 -52.952 35.226 1.00111.02 C ANISOU 4683 CZ ARG D 9 16896 15617 9670 2600 -1143 -1271 C ATOM 4684 NH1 ARG D 9 -12.896 -52.099 36.177 1.00104.93 N ANISOU 4684 NH1 ARG D 9 15677 14784 9408 2191 -1007 -726 N ATOM 4685 NH2 ARG D 9 -11.791 -52.525 34.212 1.00114.40 N ANISOU 4685 NH2 ARG D 9 17336 16648 9484 3074 -738 -1289 N ATOM 4686 N ASN D 10 -18.777 -52.446 37.726 1.00100.99 N ANISOU 4686 N ASN D 10 14692 13489 10191 44 -2949 140 N ATOM 4687 CA ASN D 10 -19.789 -51.398 37.702 1.00 99.42 C ANISOU 4687 CA ASN D 10 14063 13629 10083 -180 -2905 646 C ATOM 4688 C ASN D 10 -21.126 -51.912 38.237 1.00100.53 C ANISOU 4688 C ASN D 10 14002 13545 10648 -693 -3408 876 C ATOM 4689 O ASN D 10 -21.587 -52.981 37.828 1.00105.24 O ANISOU 4689 O ASN D 10 14899 13862 11227 -898 -4026 611 O ATOM 4690 CB ASN D 10 -19.962 -50.878 36.272 1.00103.33 C ANISOU 4690 CB ASN D 10 14686 14585 9990 19 -2991 627 C ATOM 4691 CG ASN D 10 -20.400 -49.433 36.228 1.00101.46 C ANISOU 4691 CG ASN D 10 13972 14748 9830 11 -2664 1195 C ATOM 4692 OD1 ASN D 10 -21.501 -49.089 36.666 1.00101.50 O ANISOU 4692 OD1 ASN D 10 13611 14751 10205 -300 -2825 1567 O ATOM 4693 ND2 ASN D 10 -19.541 -48.572 35.688 1.00101.30 N ANISOU 4693 ND2 ASN D 10 13922 15068 9498 366 -2204 1301 N ATOM 4694 N LYS D 11 -21.737 -51.156 39.151 1.00 96.78 N ANISOU 4694 N LYS D 11 13011 13192 10570 -887 -3153 1365 N ATOM 4695 CA LYS D 11 -23.065 -51.491 39.691 1.00 98.26 C ANISOU 4695 CA LYS D 11 12865 13303 11166 -1353 -3531 1718 C ATOM 4696 C LYS D 11 -23.919 -50.293 40.101 1.00 96.06 C ANISOU 4696 C LYS D 11 11994 13390 11115 -1407 -3230 2252 C ATOM 4697 O LYS D 11 -23.404 -49.198 40.349 1.00 92.33 O ANISOU 4697 O LYS D 11 11356 13109 10618 -1114 -2677 2348 O ATOM 4698 CB LYS D 11 -22.961 -52.470 40.869 1.00 97.70 C ANISOU 4698 CB LYS D 11 12789 12830 11501 -1604 -3626 1727 C ATOM 4699 CG LYS D 11 -23.408 -53.899 40.538 1.00103.80 C ANISOU 4699 CG LYS D 11 13866 13163 12409 -1943 -4386 1532 C ATOM 4700 CD LYS D 11 -24.932 -54.028 40.374 1.00108.51 C ANISOU 4700 CD LYS D 11 14105 13857 13266 -2421 -4905 1949 C ATOM 4701 CE LYS D 11 -25.613 -54.577 41.630 1.00109.37 C ANISOU 4701 CE LYS D 11 13795 13811 13949 -2868 -5004 2439 C ATOM 4702 NZ LYS D 11 -25.689 -53.587 42.743 1.00104.70 N ANISOU 4702 NZ LYS D 11 12677 13623 13483 -2753 -4298 2865 N ATOM 4703 N VAL D 12 -25.232 -50.525 40.151 1.00 98.97 N ANISOU 4703 N VAL D 12 12033 13825 11745 -1778 -3632 2601 N ATOM 4704 CA VAL D 12 -26.200 -49.578 40.712 1.00 97.93 C ANISOU 4704 CA VAL D 12 11267 14014 11928 -1834 -3373 3133 C ATOM 4705 C VAL D 12 -27.205 -50.303 41.601 1.00100.10 C ANISOU 4705 C VAL D 12 11159 14231 12642 -2273 -3629 3497 C ATOM 4706 O VAL D 12 -27.766 -51.328 41.205 1.00104.64 O ANISOU 4706 O VAL D 12 11835 14612 13312 -2656 -4279 3513 O ATOM 4707 CB VAL D 12 -26.969 -48.769 39.627 1.00100.83 C ANISOU 4707 CB VAL D 12 11427 14722 12161 -1774 -3553 3387 C ATOM 4708 CG1 VAL D 12 -26.086 -47.688 39.025 1.00 98.36 C ANISOU 4708 CG1 VAL D 12 11274 14572 11526 -1323 -3120 3267 C ATOM 4709 CG2 VAL D 12 -27.525 -49.677 38.547 1.00106.34 C ANISOU 4709 CG2 VAL D 12 12382 15362 12659 -2069 -4340 3272 C ATOM 4710 N ALA D 13 -27.421 -49.773 42.802 1.00 97.44 N ANISOU 4710 N ALA D 13 10384 14075 12565 -2215 -3130 3794 N ATOM 4711 CA ALA D 13 -28.383 -50.348 43.741 1.00 99.89 C ANISOU 4711 CA ALA D 13 10226 14471 13256 -2592 -3250 4251 C ATOM 4712 C ALA D 13 -29.088 -49.264 44.549 1.00 99.19 C ANISOU 4712 C ALA D 13 9498 14834 13354 -2398 -2701 4656 C ATOM 4713 O ALA D 13 -28.570 -48.156 44.695 1.00 95.69 O ANISOU 4713 O ALA D 13 9071 14500 12785 -1963 -2179 4480 O ATOM 4714 CB ALA D 13 -27.702 -51.358 44.664 1.00 98.85 C ANISOU 4714 CB ALA D 13 10334 14031 13193 -2757 -3249 4128 C ATOM 4715 N VAL D 14 -30.264 -49.602 45.073 1.00103.09 N ANISOU 4715 N VAL D 14 9420 15576 14173 -2712 -2835 5200 N ATOM 4716 CA VAL D 14 -31.117 -48.659 45.798 1.00104.12 C ANISOU 4716 CA VAL D 14 8870 16199 14492 -2497 -2335 5614 C ATOM 4717 C VAL D 14 -30.748 -48.558 47.285 1.00102.10 C ANISOU 4717 C VAL D 14 8489 16122 14183 -2333 -1737 5614 C ATOM 4718 O VAL D 14 -30.129 -49.471 47.839 1.00101.11 O ANISOU 4718 O VAL D 14 8652 15782 13984 -2553 -1831 5514 O ATOM 4719 CB VAL D 14 -32.619 -49.031 45.625 1.00110.70 C ANISOU 4719 CB VAL D 14 9041 17323 15698 -2888 -2736 6279 C ATOM 4720 CG1 VAL D 14 -33.016 -50.213 46.527 1.00114.06 C ANISOU 4720 CG1 VAL D 14 9211 17774 16353 -3378 -2924 6690 C ATOM 4721 CG2 VAL D 14 -33.516 -47.816 45.860 1.00112.76 C ANISOU 4721 CG2 VAL D 14 8624 18085 16136 -2521 -2272 6637 C ATOM 4722 N THR D 15 -31.130 -47.444 47.914 1.00102.07 N ANISOU 4722 N THR D 15 8068 16508 14206 -1922 -1147 5713 N ATOM 4723 CA THR D 15 -30.903 -47.209 49.344 1.00101.28 C ANISOU 4723 CA THR D 15 7817 16691 13972 -1700 -556 5687 C ATOM 4724 C THR D 15 -31.498 -48.349 50.183 1.00105.23 C ANISOU 4724 C THR D 15 7963 17449 14570 -2150 -685 6218 C ATOM 4725 O THR D 15 -32.716 -48.440 50.346 1.00110.65 O ANISOU 4725 O THR D 15 7981 18555 15506 -2304 -700 6812 O ATOM 4726 CB THR D 15 -31.507 -45.847 49.802 1.00103.04 C ANISOU 4726 CB THR D 15 7570 17324 14257 -1161 38 5729 C ATOM 4727 OG1 THR D 15 -31.189 -44.824 48.853 1.00100.47 O ANISOU 4727 OG1 THR D 15 7463 16725 13985 -828 35 5419 O ATOM 4728 CG2 THR D 15 -30.968 -45.438 51.161 1.00102.09 C ANISOU 4728 CG2 THR D 15 7511 17419 13860 -824 638 5449 C ATOM 4729 N GLY D 16 -30.635 -49.224 50.695 1.00103.00 N ANISOU 4729 N GLY D 16 8088 16917 14130 -2370 -794 6070 N ATOM 4730 CA GLY D 16 -31.080 -50.326 51.546 1.00107.03 C ANISOU 4730 CA GLY D 16 8288 17630 14750 -2815 -928 6633 C ATOM 4731 C GLY D 16 -30.757 -51.733 51.064 1.00107.61 C ANISOU 4731 C GLY D 16 8723 17137 15028 -3373 -1653 6707 C ATOM 4732 O GLY D 16 -30.917 -52.696 51.817 1.00110.95 O ANISOU 4732 O GLY D 16 8970 17611 15574 -3758 -1797 7168 O ATOM 4733 N GLY D 17 -30.309 -51.860 49.817 1.00105.12 N ANISOU 4733 N GLY D 17 8911 16284 14745 -3401 -2117 6267 N ATOM 4734 CA GLY D 17 -29.941 -53.162 49.257 1.00106.12 C ANISOU 4734 CA GLY D 17 9475 15791 15053 -3839 -2833 6181 C ATOM 4735 C GLY D 17 -28.578 -53.630 49.732 1.00102.24 C ANISOU 4735 C GLY D 17 9556 14927 14362 -3721 -2741 5769 C ATOM 4736 O GLY D 17 -27.730 -52.814 50.098 1.00 97.45 O ANISOU 4736 O GLY D 17 9155 14447 13426 -3268 -2210 5376 O ATOM 4737 N LYS D 18 -28.370 -54.946 49.732 1.00104.87 N ANISOU 4737 N LYS D 18 10128 14768 14949 -4135 -3300 5879 N ATOM 4738 CA LYS D 18 -27.083 -55.527 50.125 1.00102.17 C ANISOU 4738 CA LYS D 18 10311 14010 14499 -4032 -3297 5534 C ATOM 4739 C LYS D 18 -26.108 -55.507 48.954 1.00 98.81 C ANISOU 4739 C LYS D 18 10564 13077 13903 -3742 -3510 4770 C ATOM 4740 O LYS D 18 -26.405 -56.024 47.876 1.00101.57 O ANISOU 4740 O LYS D 18 11144 13052 14396 -3921 -4090 4593 O ATOM 4741 CB LYS D 18 -27.258 -56.958 50.655 1.00107.41 C ANISOU 4741 CB LYS D 18 10928 14308 15576 -4567 -3814 6018 C ATOM 4742 CG LYS D 18 -25.975 -57.619 51.186 1.00105.64 C ANISOU 4742 CG LYS D 18 11168 13662 15307 -4462 -3826 5776 C ATOM 4743 CD LYS D 18 -26.246 -59.050 51.654 1.00112.10 C ANISOU 4743 CD LYS D 18 11908 14046 16639 -5021 -4412 6341 C ATOM 4744 CE LYS D 18 -24.967 -59.770 52.056 1.00110.77 C ANISOU 4744 CE LYS D 18 12217 13368 16504 -4894 -4508 6102 C ATOM 4745 N VAL D 19 -24.944 -54.903 49.173 1.00 93.45 N ANISOU 4745 N VAL D 19 10186 12426 12895 -3291 -3045 4326 N ATOM 4746 CA VAL D 19 -23.937 -54.793 48.126 1.00 90.57 C ANISOU 4746 CA VAL D 19 10389 11704 12321 -2956 -3124 3662 C ATOM 4747 C VAL D 19 -22.573 -55.305 48.587 1.00 88.32 C ANISOU 4747 C VAL D 19 10494 11084 11980 -2770 -3041 3371 C ATOM 4748 O VAL D 19 -22.030 -54.854 49.600 1.00 85.54 O ANISOU 4748 O VAL D 19 10017 10989 11496 -2614 -2587 3451 O ATOM 4749 CB VAL D 19 -23.819 -53.348 47.603 1.00 86.81 C ANISOU 4749 CB VAL D 19 9856 11597 11531 -2539 -2656 3410 C ATOM 4750 CG1 VAL D 19 -22.773 -53.260 46.498 1.00 85.14 C ANISOU 4750 CG1 VAL D 19 10175 11104 11069 -2205 -2711 2824 C ATOM 4751 CG2 VAL D 19 -25.162 -52.859 47.088 1.00 89.60 C ANISOU 4751 CG2 VAL D 19 9804 12260 11979 -2690 -2777 3724 C ATOM 4752 N THR D 20 -22.035 -56.254 47.827 1.00 90.16 N ANISOU 4752 N THR D 20 11200 10745 12310 -2768 -3508 3015 N ATOM 4753 CA THR D 20 -20.721 -56.828 48.088 1.00 88.94 C ANISOU 4753 CA THR D 20 11420 10216 12159 -2540 -3484 2716 C ATOM 4754 C THR D 20 -19.805 -56.546 46.903 1.00 87.24 C ANISOU 4754 C THR D 20 11648 9855 11645 -2078 -3415 2065 C ATOM 4755 O THR D 20 -20.241 -56.602 45.753 1.00 89.54 O ANISOU 4755 O THR D 20 12128 10064 11830 -2066 -3713 1813 O ATOM 4756 CB THR D 20 -20.801 -58.351 48.295 1.00 94.17 C ANISOU 4756 CB THR D 20 12259 10255 13267 -2880 -4109 2869 C ATOM 4757 OG1 THR D 20 -21.444 -58.948 47.164 1.00 98.74 O ANISOU 4757 OG1 THR D 20 13074 10453 13988 -3057 -4718 2648 O ATOM 4758 CG2 THR D 20 -21.593 -58.688 49.550 1.00 96.55 C ANISOU 4758 CG2 THR D 20 12077 10755 13853 -3347 -4143 3632 C ATOM 4759 N LEU D 21 -18.540 -56.247 47.187 1.00 83.83 N ANISOU 4759 N LEU D 21 11351 9442 11057 -1705 -3031 1831 N ATOM 4760 CA LEU D 21 -17.557 -55.971 46.139 1.00 82.57 C ANISOU 4760 CA LEU D 21 11536 9230 10605 -1235 -2881 1296 C ATOM 4761 C LEU D 21 -16.378 -56.943 46.198 1.00 84.15 C ANISOU 4761 C LEU D 21 12076 8964 10933 -991 -3009 1006 C ATOM 4762 O LEU D 21 -15.485 -56.794 47.032 1.00 81.67 O ANISOU 4762 O LEU D 21 11657 8705 10669 -853 -2711 1104 O ATOM 4763 CB LEU D 21 -17.070 -54.518 46.221 1.00 77.64 C ANISOU 4763 CB LEU D 21 10695 9106 9698 -955 -2264 1300 C ATOM 4764 CG LEU D 21 -18.092 -53.375 46.167 1.00 75.91 C ANISOU 4764 CG LEU D 21 10128 9334 9382 -1075 -2057 1556 C ATOM 4765 CD1 LEU D 21 -17.370 -52.042 46.070 1.00 71.96 C ANISOU 4765 CD1 LEU D 21 9518 9148 8676 -743 -1532 1470 C ATOM 4766 CD2 LEU D 21 -19.077 -53.527 45.008 1.00 79.13 C ANISOU 4766 CD2 LEU D 21 10617 9739 9709 -1195 -2431 1503 C ATOM 4767 N SER D 22 -16.385 -57.937 45.310 1.00 88.83 N ANISOU 4767 N SER D 22 13077 9087 11589 -920 -3485 630 N ATOM 4768 CA SER D 22 -15.331 -58.955 45.273 1.00 91.68 C ANISOU 4768 CA SER D 22 13782 8925 12126 -623 -3654 302 C ATOM 4769 C SER D 22 -13.983 -58.368 44.873 1.00 89.22 C ANISOU 4769 C SER D 22 13543 8869 11487 -35 -3129 -24 C ATOM 4770 O SER D 22 -13.916 -57.367 44.156 1.00 87.00 O ANISOU 4770 O SER D 22 13202 9062 10793 174 -2776 -141 O ATOM 4771 CB SER D 22 -15.697 -60.093 44.317 1.00 98.36 C ANISOU 4771 CB SER D 22 15098 9183 13090 -625 -4308 -136 C ATOM 4772 OG SER D 22 -16.870 -60.754 44.743 1.00101.62 O ANISOU 4772 OG SER D 22 15407 9277 13928 -1224 -4868 237 O ATOM 4773 N CYS D 23 -12.916 -59.000 45.351 1.00 90.10 N ANISOU 4773 N CYS D 23 13737 8670 11826 216 -3095 -95 N ATOM 4774 CA CYS D 23 -11.558 -58.612 45.001 1.00 88.86 C ANISOU 4774 CA CYS D 23 13597 8720 11446 781 -2637 -355 C ATOM 4775 C CYS D 23 -10.639 -59.821 44.987 1.00 93.44 C ANISOU 4775 C CYS D 23 14453 8731 12319 1141 -2858 -645 C ATOM 4776 O CYS D 23 -10.530 -60.542 45.978 1.00 94.32 O ANISOU 4776 O CYS D 23 14498 8451 12890 937 -3108 -358 O ATOM 4777 CB CYS D 23 -11.023 -57.571 45.978 1.00 83.41 C ANISOU 4777 CB CYS D 23 12467 8484 10742 716 -2150 56 C ATOM 4778 SG CYS D 23 -9.319 -57.116 45.643 1.00 82.94 S ANISOU 4778 SG CYS D 23 12317 8671 10527 1328 -1637 -130 S ATOM 4779 N ASN D 24 -9.972 -60.026 43.858 1.00 96.86 N ANISOU 4779 N ASN D 24 15181 9152 12471 1711 -2748 -1195 N ATOM 4780 CA ASN D 24 -9.103 -61.179 43.675 1.00102.38 C ANISOU 4780 CA ASN D 24 16177 9295 13429 2181 -2939 -1582 C ATOM 4781 C ASN D 24 -7.708 -60.787 43.199 1.00102.71 C ANISOU 4781 C ASN D 24 16111 9716 13197 2869 -2362 -1795 C ATOM 4782 O ASN D 24 -7.532 -59.753 42.548 1.00100.29 O ANISOU 4782 O ASN D 24 15653 10063 12390 3036 -1899 -1808 O ATOM 4783 CB ASN D 24 -9.739 -62.175 42.703 1.00109.27 C ANISOU 4783 CB ASN D 24 17610 9627 14280 2271 -3512 -2172 C ATOM 4784 CG ASN D 24 -9.071 -63.528 42.744 1.00116.04 C ANISOU 4784 CG ASN D 24 18801 9691 15598 2657 -3869 -2539 C ATOM 4785 OD1 ASN D 24 -8.464 -63.961 41.764 1.00121.87 O ANISOU 4785 OD1 ASN D 24 19903 10313 16088 3313 -3823 -3208 O ATOM 4786 ND2 ASN D 24 -9.160 -64.198 43.887 1.00116.11 N ANISOU 4786 ND2 ASN D 24 18676 9169 16271 2291 -4213 -2090 N ATOM 4787 N GLN D 25 -6.727 -61.625 43.534 1.00106.18 N ANISOU 4787 N GLN D 25 16587 9745 14011 3259 -2404 -1897 N ATOM 4788 CA GLN D 25 -5.327 -61.395 43.180 1.00107.52 C ANISOU 4788 CA GLN D 25 16576 10249 14028 3940 -1870 -2032 C ATOM 4789 C GLN D 25 -4.488 -62.671 43.325 1.00113.99 C ANISOU 4789 C GLN D 25 17578 10412 15320 4445 -2091 -2304 C ATOM 4790 O GLN D 25 -4.555 -63.354 44.344 1.00114.27 O ANISOU 4790 O GLN D 25 17567 9900 15951 4151 -2479 -1989 O ATOM 4791 CB GLN D 25 -4.765 -60.228 44.011 1.00100.91 C ANISOU 4791 CB GLN D 25 15142 9999 13200 3718 -1400 -1411 C ATOM 4792 CG GLN D 25 -3.325 -60.356 44.470 1.00102.05 C ANISOU 4792 CG GLN D 25 14951 10197 13627 4145 -1111 -1235 C ATOM 4793 CD GLN D 25 -3.203 -60.856 45.898 1.00100.39 C ANISOU 4793 CD GLN D 25 14558 9581 14003 3783 -1441 -777 C ATOM 4794 OE1 GLN D 25 -4.140 -61.419 46.465 1.00 99.88 O ANISOU 4794 OE1 GLN D 25 14691 9073 14186 3313 -1926 -657 O ATOM 4795 NE2 GLN D 25 -2.040 -60.644 46.487 1.00100.03 N ANISOU 4795 NE2 GLN D 25 14098 9731 14176 3986 -1191 -461 N ATOM 4796 N THR D 26 -3.713 -62.996 42.294 1.00119.90 N ANISOU 4796 N THR D 26 18526 11237 15794 5233 -1837 -2873 N ATOM 4797 CA THR D 26 -2.819 -64.153 42.355 1.00127.07 C ANISOU 4797 CA THR D 26 19580 11544 17158 5851 -1976 -3180 C ATOM 4798 C THR D 26 -1.383 -63.715 42.666 1.00126.57 C ANISOU 4798 C THR D 26 18955 11962 17174 6318 -1374 -2847 C ATOM 4799 O THR D 26 -0.451 -64.525 42.638 1.00132.76 O ANISOU 4799 O THR D 26 19743 12404 18297 6963 -1345 -3063 O ATOM 4800 CB THR D 26 -2.879 -65.028 41.063 1.00136.28 C ANISOU 4800 CB THR D 26 21384 12355 18041 6524 -2163 -4129 C ATOM 4801 OG1 THR D 26 -2.500 -64.252 39.921 1.00137.25 O ANISOU 4801 OG1 THR D 26 21467 13340 17340 7024 -1549 -4429 O ATOM 4802 CG2 THR D 26 -4.281 -65.595 40.848 1.00137.72 C ANISOU 4802 CG2 THR D 26 22113 11927 18288 5997 -2910 -4432 C ATOM 4803 N ASN D 27 -1.228 -62.430 42.986 1.00119.64 N ANISOU 4803 N ASN D 27 17575 11841 16043 5975 -934 -2302 N ATOM 4804 CA ASN D 27 0.077 -61.824 43.270 1.00118.97 C ANISOU 4804 CA ASN D 27 16883 12292 16029 6290 -388 -1898 C ATOM 4805 C ASN D 27 0.702 -62.227 44.610 1.00118.17 C ANISOU 4805 C ASN D 27 16436 11836 16628 6117 -608 -1384 C ATOM 4806 O ASN D 27 1.887 -61.968 44.842 1.00119.31 O ANISOU 4806 O ASN D 27 16084 12310 16939 6455 -253 -1087 O ATOM 4807 CB ASN D 27 -0.008 -60.294 43.181 1.00112.58 C ANISOU 4807 CB ASN D 27 15672 12312 14791 5916 57 -1479 C ATOM 4808 CG ASN D 27 -0.244 -59.790 41.763 1.00114.86 C ANISOU 4808 CG ASN D 27 16148 13141 14353 6247 419 -1858 C ATOM 4809 OD1 ASN D 27 -0.269 -60.565 40.803 1.00121.60 O ANISOU 4809 OD1 ASN D 27 17437 13834 14930 6814 381 -2494 O ATOM 4810 ND2 ASN D 27 -0.416 -58.477 41.628 1.00109.96 N ANISOU 4810 ND2 ASN D 27 15208 13161 13410 5901 749 -1468 N ATOM 4811 N ASN D 28 -0.099 -62.843 45.484 1.00116.70 N ANISOU 4811 N ASN D 28 16473 11028 16841 5573 -1203 -1219 N ATOM 4812 CA ASN D 28 0.368 -63.367 46.775 1.00116.93 C ANISOU 4812 CA ASN D 28 16239 10682 17506 5378 -1507 -704 C ATOM 4813 C ASN D 28 0.872 -62.281 47.746 1.00111.09 C ANISOU 4813 C ASN D 28 14899 10557 16752 4968 -1258 -31 C ATOM 4814 O ASN D 28 2.072 -62.173 48.011 1.00112.98 O ANISOU 4814 O ASN D 28 14699 11020 17210 5309 -1024 223 O ATOM 4815 CB ASN D 28 1.421 -64.472 46.547 1.00125.21 C ANISOU 4815 CB ASN D 28 17312 11252 19011 6182 -1546 -956 C ATOM 4816 CG ASN D 28 1.835 -65.175 47.827 1.00126.49 C ANISOU 4816 CG ASN D 28 17250 10929 19883 6001 -1958 -407 C ATOM 4817 OD1 ASN D 28 0.995 -65.585 48.626 1.00124.94 O ANISOU 4817 OD1 ASN D 28 17226 10297 19949 5389 -2478 -113 O ATOM 4818 ND2 ASN D 28 3.140 -65.328 48.019 1.00129.78 N ANISOU 4818 ND2 ASN D 28 17239 11458 20612 6541 -1730 -211 N ATOM 4819 N HIS D 29 -0.057 -61.473 48.259 1.00104.70 N ANISOU 4819 N HIS D 29 14070 10017 15693 4252 -1329 235 N ATOM 4820 CA HIS D 29 0.256 -60.420 49.237 1.00 99.57 C ANISOU 4820 CA HIS D 29 12947 9886 14999 3808 -1182 782 C ATOM 4821 C HIS D 29 -0.549 -60.618 50.509 1.00 96.91 C ANISOU 4821 C HIS D 29 12657 9348 14816 3134 -1625 1184 C ATOM 4822 O HIS D 29 -1.751 -60.880 50.455 1.00 95.77 O ANISOU 4822 O HIS D 29 12845 8971 14574 2789 -1874 1081 O ATOM 4823 CB HIS D 29 -0.025 -59.020 48.678 1.00 94.82 C ANISOU 4823 CB HIS D 29 12214 9920 13894 3634 -760 733 C ATOM 4824 CG HIS D 29 0.761 -58.683 47.450 1.00 97.61 C ANISOU 4824 CG HIS D 29 12442 10626 14018 4245 -268 470 C ATOM 4825 ND1 HIS D 29 2.135 -58.581 47.450 1.00100.85 N ANISOU 4825 ND1 HIS D 29 12396 11288 14634 4671 19 673 N ATOM 4826 CD2 HIS D 29 0.364 -58.409 46.185 1.00 98.47 C ANISOU 4826 CD2 HIS D 29 12784 10954 13677 4499 -2 77 C ATOM 4827 CE1 HIS D 29 2.552 -58.271 46.234 1.00103.59 C ANISOU 4827 CE1 HIS D 29 12684 12014 14662 5179 483 431 C ATOM 4828 NE2 HIS D 29 1.496 -58.159 45.449 1.00102.24 N ANISOU 4828 NE2 HIS D 29 12950 11840 14058 5087 475 58 N ATOM 4829 N ASN D 30 0.118 -60.479 51.649 1.00 96.53 N ANISOU 4829 N ASN D 30 12247 9449 14982 2947 -1725 1673 N ATOM 4830 CA ASN D 30 -0.510 -60.722 52.943 1.00 95.36 C ANISOU 4830 CA ASN D 30 12101 9209 14921 2363 -2124 2121 C ATOM 4831 C ASN D 30 -1.598 -59.715 53.268 1.00 89.78 C ANISOU 4831 C ASN D 30 11430 8920 13761 1798 -2031 2172 C ATOM 4832 O ASN D 30 -2.770 -60.071 53.399 1.00 89.08 O ANISOU 4832 O ASN D 30 11592 8642 13611 1458 -2254 2195 O ATOM 4833 CB ASN D 30 0.543 -60.760 54.053 1.00 97.02 C ANISOU 4833 CB ASN D 30 11910 9569 15384 2332 -2260 2620 C ATOM 4834 CG ASN D 30 1.304 -62.067 54.083 1.00103.40 C ANISOU 4834 CG ASN D 30 12712 9810 16764 2776 -2533 2726 C ATOM 4835 OD1 ASN D 30 0.814 -63.095 53.614 1.00106.74 O ANISOU 4835 OD1 ASN D 30 13497 9617 17442 2948 -2768 2505 O ATOM 4836 ND2 ASN D 30 2.508 -62.039 54.642 1.00105.99 N ANISOU 4836 ND2 ASN D 30 12620 10306 17344 2964 -2547 3069 N ATOM 4837 N ASN D 31 -1.193 -58.457 53.394 1.00 86.52 N ANISOU 4837 N ASN D 31 10738 9055 13082 1712 -1716 2206 N ATOM 4838 CA ASN D 31 -2.126 -57.375 53.646 1.00 81.94 C ANISOU 4838 CA ASN D 31 10173 8862 12100 1274 -1584 2193 C ATOM 4839 C ASN D 31 -2.666 -56.757 52.358 1.00 79.70 C ANISOU 4839 C ASN D 31 10045 8674 11562 1422 -1266 1790 C ATOM 4840 O ASN D 31 -1.944 -56.610 51.367 1.00 80.79 O ANISOU 4840 O ASN D 31 10125 8858 11715 1854 -999 1571 O ATOM 4841 CB ASN D 31 -1.536 -56.316 54.604 1.00 80.27 C ANISOU 4841 CB ASN D 31 9624 9114 11760 1034 -1517 2433 C ATOM 4842 CG ASN D 31 -0.039 -56.084 54.404 1.00 82.81 C ANISOU 4842 CG ASN D 31 9602 9540 12323 1373 -1386 2501 C ATOM 4843 OD1 ASN D 31 0.386 -55.522 53.394 1.00 83.29 O ANISOU 4843 OD1 ASN D 31 9558 9724 12365 1658 -1049 2299 O ATOM 4844 ND2 ASN D 31 0.760 -56.489 55.389 1.00 85.65 N ANISOU 4844 ND2 ASN D 31 9737 9904 12901 1325 -1658 2854 N ATOM 4845 N MET D 32 -3.957 -56.438 52.381 1.00 77.21 N ANISOU 4845 N MET D 32 9902 8429 11004 1075 -1299 1740 N ATOM 4846 CA MET D 32 -4.645 -55.810 51.253 1.00 75.37 C ANISOU 4846 CA MET D 32 9808 8320 10508 1140 -1060 1430 C ATOM 4847 C MET D 32 -5.748 -54.884 51.745 1.00 71.63 C ANISOU 4847 C MET D 32 9294 8142 9782 709 -1006 1527 C ATOM 4848 O MET D 32 -6.252 -55.044 52.854 1.00 71.36 O ANISOU 4848 O MET D 32 9217 8159 9738 368 -1193 1783 O ATOM 4849 CB MET D 32 -5.195 -56.856 50.289 1.00 78.48 C ANISOU 4849 CB MET D 32 10563 8301 10953 1334 -1245 1141 C ATOM 4850 CG MET D 32 -5.880 -58.038 50.945 1.00 81.39 C ANISOU 4850 CG MET D 32 11114 8232 11578 1065 -1709 1316 C ATOM 4851 SD MET D 32 -6.620 -59.111 49.702 1.00 87.08 S ANISOU 4851 SD MET D 32 12298 8411 12377 1239 -2008 888 S ATOM 4852 CE MET D 32 -5.163 -59.747 48.876 1.00 91.58 C ANISOU 4852 CE MET D 32 12965 8726 13105 1992 -1884 510 C ATOM 4853 N TYR D 33 -6.124 -53.925 50.908 1.00 69.52 N ANISOU 4853 N TYR D 33 9020 8094 9299 759 -738 1346 N ATOM 4854 CA TYR D 33 -6.835 -52.734 51.376 1.00 66.60 C ANISOU 4854 CA TYR D 33 8521 8040 8745 465 -599 1420 C ATOM 4855 C TYR D 33 -8.084 -52.406 50.558 1.00 65.68 C ANISOU 4855 C TYR D 33 8534 7973 8448 389 -541 1294 C ATOM 4856 O TYR D 33 -8.160 -52.721 49.368 1.00 67.07 O ANISOU 4856 O TYR D 33 8875 8044 8563 613 -522 1100 O ATOM 4857 CB TYR D 33 -5.873 -51.531 51.361 1.00 65.39 C ANISOU 4857 CB TYR D 33 8110 8126 8610 564 -337 1431 C ATOM 4858 CG TYR D 33 -4.510 -51.830 51.959 1.00 66.91 C ANISOU 4858 CG TYR D 33 8116 8290 9015 674 -408 1571 C ATOM 4859 CD1 TYR D 33 -3.476 -52.353 51.180 1.00 68.88 C ANISOU 4859 CD1 TYR D 33 8306 8444 9423 1063 -316 1537 C ATOM 4860 CD2 TYR D 33 -4.260 -51.607 53.309 1.00 66.91 C ANISOU 4860 CD2 TYR D 33 7986 8404 9033 417 -574 1742 C ATOM 4861 CE1 TYR D 33 -2.228 -52.650 51.736 1.00 70.66 C ANISOU 4861 CE1 TYR D 33 8295 8658 9895 1181 -392 1720 C ATOM 4862 CE2 TYR D 33 -3.015 -51.899 53.875 1.00 68.70 C ANISOU 4862 CE2 TYR D 33 8013 8623 9465 494 -701 1915 C ATOM 4863 CZ TYR D 33 -2.006 -52.418 53.085 1.00 70.25 C ANISOU 4863 CZ TYR D 33 8102 8696 9893 870 -611 1927 C ATOM 4864 OH TYR D 33 -0.782 -52.696 53.652 1.00 72.12 O ANISOU 4864 OH TYR D 33 8077 8945 10381 959 -742 2148 O ATOM 4865 N TRP D 34 -9.065 -51.783 51.204 1.00 64.19 N ANISOU 4865 N TRP D 34 8263 7978 8149 98 -521 1401 N ATOM 4866 CA TRP D 34 -10.181 -51.172 50.478 1.00 63.37 C ANISOU 4866 CA TRP D 34 8179 7991 7908 42 -424 1335 C ATOM 4867 C TRP D 34 -10.132 -49.649 50.579 1.00 61.42 C ANISOU 4867 C TRP D 34 7735 7990 7610 53 -144 1320 C ATOM 4868 O TRP D 34 -10.136 -49.085 51.674 1.00 61.12 O ANISOU 4868 O TRP D 34 7570 8091 7563 -87 -103 1374 O ATOM 4869 CB TRP D 34 -11.544 -51.716 50.935 1.00 64.10 C ANISOU 4869 CB TRP D 34 8296 8085 7975 -258 -629 1492 C ATOM 4870 CG TRP D 34 -12.004 -52.947 50.172 1.00 66.64 C ANISOU 4870 CG TRP D 34 8848 8089 8382 -279 -946 1443 C ATOM 4871 CD1 TRP D 34 -12.201 -54.199 50.681 1.00 69.16 C ANISOU 4871 CD1 TRP D 34 9262 8130 8884 -459 -1288 1603 C ATOM 4872 CD2 TRP D 34 -12.318 -53.033 48.772 1.00 67.32 C ANISOU 4872 CD2 TRP D 34 9117 8080 8380 -123 -1002 1214 C ATOM 4873 NE1 TRP D 34 -12.622 -55.054 49.691 1.00 71.60 N ANISOU 4873 NE1 TRP D 34 9821 8105 9280 -433 -1585 1439 N ATOM 4874 CE2 TRP D 34 -12.696 -54.366 48.510 1.00 70.54 C ANISOU 4874 CE2 TRP D 34 9760 8109 8932 -216 -1415 1169 C ATOM 4875 CE3 TRP D 34 -12.312 -52.113 47.715 1.00 66.54 C ANISOU 4875 CE3 TRP D 34 9011 8184 8089 80 -774 1065 C ATOM 4876 CZ2 TRP D 34 -13.063 -54.804 47.233 1.00 73.00 C ANISOU 4876 CZ2 TRP D 34 10338 8246 9152 -99 -1626 891 C ATOM 4877 CZ3 TRP D 34 -12.683 -52.549 46.446 1.00 68.54 C ANISOU 4877 CZ3 TRP D 34 9500 8344 8198 200 -945 857 C ATOM 4878 CH2 TRP D 34 -13.052 -53.884 46.219 1.00 71.70 C ANISOU 4878 CH2 TRP D 34 10172 8373 8699 117 -1376 728 C ATOM 4879 N TYR D 35 -10.066 -48.994 49.425 1.00 60.97 N ANISOU 4879 N TYR D 35 7669 7980 7518 231 25 1245 N ATOM 4880 CA TYR D 35 -10.051 -47.538 49.358 1.00 59.85 C ANISOU 4880 CA TYR D 35 7342 7977 7422 243 248 1274 C ATOM 4881 C TYR D 35 -11.277 -47.021 48.621 1.00 59.58 C ANISOU 4881 C TYR D 35 7304 8032 7303 220 295 1303 C ATOM 4882 O TYR D 35 -11.948 -47.775 47.913 1.00 60.56 O ANISOU 4882 O TYR D 35 7574 8136 7301 220 154 1286 O ATOM 4883 CB TYR D 35 -8.819 -47.057 48.598 1.00 60.51 C ANISOU 4883 CB TYR D 35 7323 8076 7592 463 422 1307 C ATOM 4884 CG TYR D 35 -7.490 -47.286 49.266 1.00 60.99 C ANISOU 4884 CG TYR D 35 7277 8085 7810 499 398 1339 C ATOM 4885 CD1 TYR D 35 -6.742 -48.427 48.995 1.00 62.79 C ANISOU 4885 CD1 TYR D 35 7587 8238 8033 690 336 1313 C ATOM 4886 CD2 TYR D 35 -6.960 -46.342 50.136 1.00 60.54 C ANISOU 4886 CD2 TYR D 35 7032 8037 7934 363 406 1384 C ATOM 4887 CE1 TYR D 35 -5.503 -48.627 49.587 1.00 63.89 C ANISOU 4887 CE1 TYR D 35 7567 8350 8358 745 305 1398 C ATOM 4888 CE2 TYR D 35 -5.728 -46.537 50.736 1.00 61.78 C ANISOU 4888 CE2 TYR D 35 7054 8169 8251 366 327 1451 C ATOM 4889 CZ TYR D 35 -5.002 -47.677 50.455 1.00 63.21 C ANISOU 4889 CZ TYR D 35 7263 8316 8439 559 290 1492 C ATOM 4890 OH TYR D 35 -3.778 -47.874 51.049 1.00 65.35 O ANISOU 4890 OH TYR D 35 7344 8580 8907 579 201 1610 O ATOM 4891 N ARG D 36 -11.559 -45.731 48.769 1.00 58.95 N ANISOU 4891 N ARG D 36 7057 8016 7325 205 448 1345 N ATOM 4892 CA ARG D 36 -12.541 -45.089 47.910 1.00 59.38 C ANISOU 4892 CA ARG D 36 7055 8150 7358 242 507 1435 C ATOM 4893 C ARG D 36 -12.157 -43.664 47.499 1.00 59.55 C ANISOU 4893 C ARG D 36 6902 8144 7580 342 689 1538 C ATOM 4894 O ARG D 36 -11.673 -42.867 48.306 1.00 59.27 O ANISOU 4894 O ARG D 36 6761 8000 7760 307 744 1483 O ATOM 4895 CB ARG D 36 -13.951 -45.163 48.507 1.00 59.76 C ANISOU 4895 CB ARG D 36 7045 8285 7376 94 437 1461 C ATOM 4896 CG ARG D 36 -14.259 -44.145 49.578 1.00 61.12 C ANISOU 4896 CG ARG D 36 7055 8492 7674 80 576 1404 C ATOM 4897 CD ARG D 36 -15.749 -43.962 49.698 1.00 64.20 C ANISOU 4897 CD ARG D 36 7302 9043 8048 46 597 1499 C ATOM 4898 NE ARG D 36 -16.098 -42.551 49.813 1.00 67.18 N ANISOU 4898 NE ARG D 36 7515 9385 8627 198 773 1458 N ATOM 4899 CZ ARG D 36 -17.321 -42.097 50.070 1.00 70.30 C ANISOU 4899 CZ ARG D 36 7718 9921 9071 258 861 1515 C ATOM 4900 NH1 ARG D 36 -18.336 -42.942 50.243 1.00 71.21 N ANISOU 4900 NH1 ARG D 36 7739 10276 9043 131 792 1675 N ATOM 4901 NH2 ARG D 36 -17.530 -40.790 50.154 1.00 72.66 N ANISOU 4901 NH2 ARG D 36 7891 10100 9615 453 1006 1436 N ATOM 4902 N GLN D 37 -12.382 -43.367 46.222 1.00 60.50 N ANISOU 4902 N GLN D 37 7002 8355 7630 453 740 1702 N ATOM 4903 CA GLN D 37 -11.987 -42.098 45.629 1.00 61.64 C ANISOU 4903 CA GLN D 37 6960 8473 7988 537 890 1923 C ATOM 4904 C GLN D 37 -13.194 -41.206 45.391 1.00 62.53 C ANISOU 4904 C GLN D 37 6951 8575 8232 536 889 2058 C ATOM 4905 O GLN D 37 -14.235 -41.668 44.918 1.00 62.82 O ANISOU 4905 O GLN D 37 7039 8758 8070 526 788 2093 O ATOM 4906 CB GLN D 37 -11.235 -42.338 44.313 1.00 63.14 C ANISOU 4906 CB GLN D 37 7166 8857 7968 702 985 2106 C ATOM 4907 CG GLN D 37 -10.599 -41.093 43.713 1.00 64.44 C ANISOU 4907 CG GLN D 37 7079 9029 8378 755 1151 2462 C ATOM 4908 CD GLN D 37 -9.796 -41.391 42.469 1.00 66.08 C ANISOU 4908 CD GLN D 37 7262 9555 8289 951 1309 2685 C ATOM 4909 OE1 GLN D 37 -10.275 -42.044 41.546 1.00 66.98 O ANISOU 4909 OE1 GLN D 37 7552 9929 7967 1083 1279 2645 O ATOM 4910 NE2 GLN D 37 -8.566 -40.902 42.434 1.00 67.78 N ANISOU 4910 NE2 GLN D 37 7243 9783 8727 977 1470 2924 N ATOM 4911 N ASP D 38 -13.039 -39.929 45.734 1.00 63.58 N ANISOU 4911 N ASP D 38 6910 8497 8750 545 963 2136 N ATOM 4912 CA ASP D 38 -14.061 -38.910 45.511 1.00 65.21 C ANISOU 4912 CA ASP D 38 6963 8617 9197 606 974 2288 C ATOM 4913 C ASP D 38 -13.361 -37.631 45.087 1.00 67.42 C ANISOU 4913 C ASP D 38 7065 8659 9891 641 1030 2561 C ATOM 4914 O ASP D 38 -12.213 -37.403 45.478 1.00 67.63 O ANISOU 4914 O ASP D 38 7068 8524 10105 572 1042 2524 O ATOM 4915 CB ASP D 38 -14.878 -38.675 46.784 1.00 65.30 C ANISOU 4915 CB ASP D 38 6956 8518 9338 605 969 1996 C ATOM 4916 CG ASP D 38 -15.744 -39.870 47.155 1.00 64.12 C ANISOU 4916 CG ASP D 38 6892 8633 8838 532 908 1876 C ATOM 4917 OD1 ASP D 38 -15.263 -40.787 47.869 1.00 61.85 O ANISOU 4917 OD1 ASP D 38 6748 8404 8350 425 865 1685 O ATOM 4918 OD2 ASP D 38 -16.919 -39.878 46.731 1.00 65.94 O ANISOU 4918 OD2 ASP D 38 7012 9005 9038 563 875 2029 O ATOM 4919 N THR D 39 -14.039 -36.802 44.291 1.00 69.57 N ANISOU 4919 N THR D 39 7181 8900 10351 725 1031 2892 N ATOM 4920 CA THR D 39 -13.388 -35.626 43.702 1.00 72.58 C ANISOU 4920 CA THR D 39 7362 9056 11158 729 1056 3297 C ATOM 4921 C THR D 39 -12.916 -34.644 44.762 1.00 73.81 C ANISOU 4921 C THR D 39 7463 8694 11888 676 992 3088 C ATOM 4922 O THR D 39 -13.669 -34.288 45.677 1.00 74.04 O ANISOU 4922 O THR D 39 7540 8495 12097 753 948 2734 O ATOM 4923 CB THR D 39 -14.273 -34.873 42.683 1.00 75.49 C ANISOU 4923 CB THR D 39 7554 9461 11667 830 1028 3757 C ATOM 4924 OG1 THR D 39 -15.453 -34.389 43.333 1.00 76.29 O ANISOU 4924 OG1 THR D 39 7608 9336 12043 934 971 3559 O ATOM 4925 CG2 THR D 39 -14.642 -35.766 41.497 1.00 75.37 C ANISOU 4925 CG2 THR D 39 7612 9987 11040 868 1028 3979 C ATOM 4926 N GLY D 40 -11.658 -34.228 44.620 1.00 75.23 N ANISOU 4926 N GLY D 40 7531 8718 12336 553 979 3308 N ATOM 4927 CA GLY D 40 -11.021 -33.272 45.523 1.00 77.34 C ANISOU 4927 CA GLY D 40 7746 8445 13196 442 827 3138 C ATOM 4928 C GLY D 40 -10.816 -33.831 46.915 1.00 75.02 C ANISOU 4928 C GLY D 40 7669 8107 12728 392 752 2510 C ATOM 4929 O GLY D 40 -11.166 -33.188 47.905 1.00 76.80 O ANISOU 4929 O GLY D 40 7985 7971 13226 432 630 2101 O ATOM 4930 N HIS D 41 -10.249 -35.032 46.987 1.00 71.70 N ANISOU 4930 N HIS D 41 7338 8067 11836 335 821 2432 N ATOM 4931 CA HIS D 41 -10.038 -35.705 48.261 1.00 69.64 C ANISOU 4931 CA HIS D 41 7268 7846 11345 276 740 1934 C ATOM 4932 C HIS D 41 -8.818 -36.615 48.266 1.00 68.20 C ANISOU 4932 C HIS D 41 7068 7887 10959 168 739 2012 C ATOM 4933 O HIS D 41 -8.044 -36.624 49.229 1.00 68.94 O ANISOU 4933 O HIS D 41 7186 7850 11157 37 580 1786 O ATOM 4934 CB HIS D 41 -11.280 -36.508 48.654 1.00 67.28 C ANISOU 4934 CB HIS D 41 7144 7825 10596 393 819 1654 C ATOM 4935 CG HIS D 41 -12.128 -35.835 49.684 1.00 68.85 C ANISOU 4935 CG HIS D 41 7410 7824 10925 491 782 1261 C ATOM 4936 ND1 HIS D 41 -11.862 -35.922 51.034 1.00 69.18 N ANISOU 4936 ND1 HIS D 41 7598 7830 10856 448 686 810 N ATOM 4937 CD2 HIS D 41 -13.234 -35.063 49.566 1.00 71.16 C ANISOU 4937 CD2 HIS D 41 7636 7979 11423 676 839 1242 C ATOM 4938 CE1 HIS D 41 -12.768 -35.231 51.703 1.00 72.25 C ANISOU 4938 CE1 HIS D 41 8028 8095 11329 628 716 486 C ATOM 4939 NE2 HIS D 41 -13.612 -34.700 50.835 1.00 73.23 N ANISOU 4939 NE2 HIS D 41 8009 8132 11683 781 816 743 N ATOM 4940 N GLY D 42 -8.652 -37.388 47.197 1.00 66.72 N ANISOU 4940 N GLY D 42 6840 8046 10464 252 901 2312 N ATOM 4941 CA GLY D 42 -7.634 -38.427 47.172 1.00 65.41 C ANISOU 4941 CA GLY D 42 6673 8122 10058 251 940 2336 C ATOM 4942 C GLY D 42 -8.126 -39.616 47.969 1.00 62.39 C ANISOU 4942 C GLY D 42 6550 7878 9277 267 878 1952 C ATOM 4943 O GLY D 42 -8.930 -39.463 48.889 1.00 61.41 O ANISOU 4943 O GLY D 42 6551 7654 9128 218 789 1657 O ATOM 4944 N LEU D 43 -7.634 -40.799 47.609 1.00 61.50 N ANISOU 4944 N LEU D 43 6500 8001 8866 356 933 1980 N ATOM 4945 CA LEU D 43 -8.118 -42.065 48.160 1.00 59.52 C ANISOU 4945 CA LEU D 43 6486 7853 8276 364 847 1719 C ATOM 4946 C LEU D 43 -8.112 -42.077 49.681 1.00 59.27 C ANISOU 4946 C LEU D 43 6514 7712 8294 203 678 1464 C ATOM 4947 O LEU D 43 -7.223 -41.501 50.308 1.00 60.91 O ANISOU 4947 O LEU D 43 6603 7790 8750 103 585 1448 O ATOM 4948 CB LEU D 43 -7.279 -43.227 47.637 1.00 59.68 C ANISOU 4948 CB LEU D 43 6544 8025 8105 513 890 1771 C ATOM 4949 CG LEU D 43 -7.619 -43.847 46.284 1.00 60.40 C ANISOU 4949 CG LEU D 43 6751 8314 7884 729 1003 1833 C ATOM 4950 CD1 LEU D 43 -7.334 -42.903 45.125 1.00 62.83 C ANISOU 4950 CD1 LEU D 43 6856 8775 8242 838 1208 2160 C ATOM 4951 CD2 LEU D 43 -6.827 -45.132 46.113 1.00 61.69 C ANISOU 4951 CD2 LEU D 43 7016 8543 7880 918 998 1733 C ATOM 4952 N ARG D 44 -9.116 -42.728 50.262 1.00 58.01 N ANISOU 4952 N ARG D 44 6522 7640 7881 164 620 1296 N ATOM 4953 CA ARG D 44 -9.237 -42.850 51.707 1.00 58.28 C ANISOU 4953 CA ARG D 44 6621 7697 7824 36 493 1088 C ATOM 4954 C ARG D 44 -9.416 -44.312 52.089 1.00 57.56 C ANISOU 4954 C ARG D 44 6661 7746 7462 -10 394 1110 C ATOM 4955 O ARG D 44 -10.140 -45.057 51.418 1.00 56.81 O ANISOU 4955 O ARG D 44 6649 7700 7238 26 406 1188 O ATOM 4956 CB ARG D 44 -10.417 -42.024 52.220 1.00 58.97 C ANISOU 4956 CB ARG D 44 6717 7798 7891 42 552 921 C ATOM 4957 CG ARG D 44 -10.157 -40.524 52.274 1.00 61.47 C ANISOU 4957 CG ARG D 44 6940 7862 8555 71 558 817 C ATOM 4958 CD ARG D 44 -11.378 -39.751 52.781 1.00 63.89 C ANISOU 4958 CD ARG D 44 7261 8165 8849 171 639 599 C ATOM 4959 NE ARG D 44 -12.373 -39.499 51.734 1.00 63.68 N ANISOU 4959 NE ARG D 44 7144 8143 8908 291 780 800 N ATOM 4960 CZ ARG D 44 -13.628 -39.112 51.962 1.00 65.10 C ANISOU 4960 CZ ARG D 44 7275 8403 9056 419 888 714 C ATOM 4961 NH1 ARG D 44 -14.066 -38.931 53.205 1.00 66.51 N ANISOU 4961 NH1 ARG D 44 7501 8702 9069 480 924 399 N ATOM 4962 NH2 ARG D 44 -14.455 -38.911 50.943 1.00 65.28 N ANISOU 4962 NH2 ARG D 44 7181 8440 9183 509 967 959 N ATOM 4963 N LEU D 45 -8.755 -44.721 53.169 1.00 58.39 N ANISOU 4963 N LEU D 45 6785 7893 7509 -110 244 1064 N ATOM 4964 CA LEU D 45 -8.860 -46.099 53.644 1.00 58.33 C ANISOU 4964 CA LEU D 45 6879 7973 7312 -176 107 1160 C ATOM 4965 C LEU D 45 -10.213 -46.368 54.312 1.00 58.67 C ANISOU 4965 C LEU D 45 6972 8213 7106 -287 114 1166 C ATOM 4966 O LEU D 45 -10.668 -45.584 55.149 1.00 59.85 O ANISOU 4966 O LEU D 45 7086 8524 7131 -318 179 1026 O ATOM 4967 CB LEU D 45 -7.705 -46.436 54.590 1.00 59.47 C ANISOU 4967 CB LEU D 45 6986 8134 7477 -249 -79 1192 C ATOM 4968 CG LEU D 45 -7.496 -47.929 54.854 1.00 59.74 C ANISOU 4968 CG LEU D 45 7093 8156 7448 -275 -252 1379 C ATOM 4969 CD1 LEU D 45 -6.995 -48.618 53.602 1.00 59.14 C ANISOU 4969 CD1 LEU D 45 7043 7874 7555 -66 -213 1437 C ATOM 4970 CD2 LEU D 45 -6.535 -48.161 56.015 1.00 61.56 C ANISOU 4970 CD2 LEU D 45 7259 8473 7657 -376 -470 1459 C ATOM 4971 N ILE D 46 -10.853 -47.469 53.929 1.00 58.36 N ANISOU 4971 N ILE D 46 7002 8163 7009 -334 40 1328 N ATOM 4972 CA ILE D 46 -12.122 -47.859 54.530 1.00 59.40 C ANISOU 4972 CA ILE D 46 7103 8512 6954 -481 31 1459 C ATOM 4973 C ILE D 46 -11.886 -48.995 55.510 1.00 61.16 C ANISOU 4973 C ILE D 46 7356 8815 7068 -647 -172 1678 C ATOM 4974 O ILE D 46 -12.049 -48.815 56.711 1.00 63.07 O ANISOU 4974 O ILE D 46 7534 9361 7067 -737 -148 1723 O ATOM 4975 CB ILE D 46 -13.162 -48.274 53.476 1.00 59.03 C ANISOU 4975 CB ILE D 46 7067 8391 6972 -498 12 1563 C ATOM 4976 CG1 ILE D 46 -13.443 -47.123 52.517 1.00 58.27 C ANISOU 4976 CG1 ILE D 46 6914 8261 6966 -335 197 1425 C ATOM 4977 CG2 ILE D 46 -14.452 -48.706 54.140 1.00 60.88 C ANISOU 4977 CG2 ILE D 46 7179 8880 7074 -688 -10 1794 C ATOM 4978 CD1 ILE D 46 -14.279 -47.520 51.311 1.00 59.41 C ANISOU 4978 CD1 ILE D 46 7090 8339 7145 -339 117 1517 C ATOM 4979 N HIS D 47 -11.519 -50.162 54.980 1.00 61.57 N ANISOU 4979 N HIS D 47 7513 8594 7287 -665 -380 1813 N ATOM 4980 CA HIS D 47 -11.133 -51.338 55.766 1.00 63.66 C ANISOU 4980 CA HIS D 47 7809 8810 7568 -803 -632 2078 C ATOM 4981 C HIS D 47 -9.855 -51.904 55.167 1.00 63.76 C ANISOU 4981 C HIS D 47 7924 8470 7833 -617 -764 2004 C ATOM 4982 O HIS D 47 -9.504 -51.577 54.032 1.00 62.62 O ANISOU 4982 O HIS D 47 7833 8156 7802 -402 -651 1784 O ATOM 4983 CB HIS D 47 -12.227 -52.404 55.740 1.00 65.30 C ANISOU 4983 CB HIS D 47 8023 8958 7831 -1021 -816 2384 C ATOM 4984 CG HIS D 47 -13.475 -52.015 56.469 1.00 66.60 C ANISOU 4984 CG HIS D 47 7998 9558 7749 -1200 -669 2576 C ATOM 4985 ND1 HIS D 47 -13.504 -51.782 57.828 1.00 68.86 N ANISOU 4985 ND1 HIS D 47 8160 10286 7718 -1288 -581 2733 N ATOM 4986 CD2 HIS D 47 -14.744 -51.839 56.032 1.00 66.99 C ANISOU 4986 CD2 HIS D 47 7933 9721 7801 -1281 -587 2654 C ATOM 4987 CE1 HIS D 47 -14.734 -51.468 58.193 1.00 70.42 C ANISOU 4987 CE1 HIS D 47 8167 10872 7718 -1376 -397 2885 C ATOM 4988 NE2 HIS D 47 -15.506 -51.494 57.122 1.00 69.40 N ANISOU 4988 NE2 HIS D 47 8013 10538 7816 -1383 -403 2864 N ATOM 4989 N TYR D 48 -9.161 -52.751 55.921 1.00 66.01 N ANISOU 4989 N TYR D 48 8206 8682 8191 -672 -987 2222 N ATOM 4990 CA TYR D 48 -7.893 -53.323 55.464 1.00 66.90 C ANISOU 4990 CA TYR D 48 8361 8482 8577 -440 -1099 2178 C ATOM 4991 C TYR D 48 -7.541 -54.609 56.207 1.00 70.09 C ANISOU 4991 C TYR D 48 8781 8704 9145 -529 -1429 2518 C ATOM 4992 O TYR D 48 -7.813 -54.741 57.404 1.00 71.64 O ANISOU 4992 O TYR D 48 8891 9167 9163 -780 -1543 2822 O ATOM 4993 CB TYR D 48 -6.759 -52.290 55.581 1.00 65.93 C ANISOU 4993 CB TYR D 48 8089 8514 8449 -301 -945 2028 C ATOM 4994 CG TYR D 48 -6.292 -51.998 56.995 1.00 67.77 C ANISOU 4994 CG TYR D 48 8198 9030 8523 -479 -1072 2181 C ATOM 4995 CD1 TYR D 48 -7.078 -51.245 57.876 1.00 68.20 C ANISOU 4995 CD1 TYR D 48 8238 9451 8225 -680 -998 2141 C ATOM 4996 CD2 TYR D 48 -5.059 -52.466 57.451 1.00 69.73 C ANISOU 4996 CD2 TYR D 48 8339 9212 8944 -415 -1273 2350 C ATOM 4997 CE1 TYR D 48 -6.649 -50.977 59.177 1.00 70.23 C ANISOU 4997 CE1 TYR D 48 8429 10021 8235 -819 -1138 2219 C ATOM 4998 CE2 TYR D 48 -4.623 -52.198 58.746 1.00 71.85 C ANISOU 4998 CE2 TYR D 48 8506 9780 9014 -596 -1450 2490 C ATOM 4999 CZ TYR D 48 -5.423 -51.456 59.602 1.00 72.03 C ANISOU 4999 CZ TYR D 48 8569 10184 8616 -801 -1389 2400 C ATOM 5000 OH TYR D 48 -4.998 -51.191 60.879 1.00 74.88 O ANISOU 5000 OH TYR D 48 8875 10889 8686 -957 -1586 2479 O ATOM 5001 N SER D 49 -6.933 -55.549 55.491 1.00 71.81 N ANISOU 5001 N SER D 49 9109 8483 9693 -294 -1580 2474 N ATOM 5002 CA SER D 49 -6.603 -56.857 56.057 1.00 75.75 C ANISOU 5002 CA SER D 49 9638 8672 10470 -335 -1938 2806 C ATOM 5003 C SER D 49 -5.102 -57.058 56.180 1.00 77.51 C ANISOU 5003 C SER D 49 9740 8787 10922 -44 -1987 2833 C ATOM 5004 O SER D 49 -4.332 -56.410 55.480 1.00 76.17 O ANISOU 5004 O SER D 49 9495 8677 10768 245 -1743 2553 O ATOM 5005 CB SER D 49 -7.210 -57.979 55.214 1.00 77.99 C ANISOU 5005 CB SER D 49 10167 8418 11048 -289 -2173 2741 C ATOM 5006 OG SER D 49 -6.759 -59.241 55.667 1.00 81.97 O ANISOU 5006 OG SER D 49 10709 8501 11936 -273 -2548 3045 O ATOM 5007 N TYR D 50 -4.704 -57.957 57.081 1.00 81.14 N ANISOU 5007 N TYR D 50 10135 9116 11579 -133 -2310 3241 N ATOM 5008 CA TYR D 50 -3.298 -58.298 57.286 1.00 83.62 C ANISOU 5008 CA TYR D 50 10284 9308 12180 144 -2420 3359 C ATOM 5009 C TYR D 50 -2.988 -59.692 56.775 1.00 88.03 C ANISOU 5009 C TYR D 50 10983 9213 13251 433 -2682 3402 C ATOM 5010 O TYR D 50 -1.837 -60.006 56.466 1.00 90.38 O ANISOU 5010 O TYR D 50 11167 9317 13858 839 -2680 3350 O ATOM 5011 CB TYR D 50 -2.916 -58.176 58.762 1.00 85.06 C ANISOU 5011 CB TYR D 50 10253 9872 12194 -136 -2625 3811 C ATOM 5012 CG TYR D 50 -2.488 -56.777 59.143 1.00 82.42 C ANISOU 5012 CG TYR D 50 9743 10068 11504 -217 -2414 3638 C ATOM 5013 CD1 TYR D 50 -1.255 -56.268 58.729 1.00 81.99 C ANISOU 5013 CD1 TYR D 50 9481 10026 11646 56 -2307 3486 C ATOM 5014 CD2 TYR D 50 -3.314 -55.956 59.908 1.00 80.70 C ANISOU 5014 CD2 TYR D 50 9551 10326 10786 -554 -2332 3625 C ATOM 5015 CE1 TYR D 50 -0.857 -54.979 59.068 1.00 80.08 C ANISOU 5015 CE1 TYR D 50 9077 10182 11169 -70 -2194 3343 C ATOM 5016 CE2 TYR D 50 -2.920 -54.662 60.258 1.00 78.72 C ANISOU 5016 CE2 TYR D 50 9188 10462 10261 -616 -2203 3394 C ATOM 5017 CZ TYR D 50 -1.693 -54.182 59.832 1.00 78.41 C ANISOU 5017 CZ TYR D 50 8959 10350 10485 -406 -2169 3261 C ATOM 5018 OH TYR D 50 -1.299 -52.907 60.168 1.00 77.21 O ANISOU 5018 OH TYR D 50 8693 10494 10151 -517 -2119 3052 O ATOM 5019 N GLY D 51 -4.029 -60.517 56.688 1.00 89.91 N ANISOU 5019 N GLY D 51 11450 9097 13613 231 -2922 3501 N ATOM 5020 CA GLY D 51 -3.914 -61.895 56.223 1.00 95.11 C ANISOU 5020 CA GLY D 51 12312 9009 14816 460 -3264 3505 C ATOM 5021 C GLY D 51 -5.256 -62.598 56.249 1.00 97.00 C ANISOU 5021 C GLY D 51 12763 8926 15167 70 -3571 3681 C ATOM 5022 O GLY D 51 -6.266 -62.009 56.638 1.00 94.21 O ANISOU 5022 O GLY D 51 12349 9004 14442 -350 -3466 3837 O ATOM 5023 N ALA D 52 -5.260 -63.864 55.839 1.00102.55 N ANISOU 5023 N ALA D 52 13692 8849 16423 221 -3969 3665 N ATOM 5024 CA ALA D 52 -6.478 -64.669 55.781 1.00105.90 C ANISOU 5024 CA ALA D 52 14311 8826 17100 -170 -4369 3859 C ATOM 5025 C ALA D 52 -7.223 -64.727 57.120 1.00106.93 C ANISOU 5025 C ALA D 52 14183 9328 17116 -794 -4532 4666 C ATOM 5026 O ALA D 52 -6.613 -64.918 58.174 1.00108.87 O ANISOU 5026 O ALA D 52 14203 9759 17404 -865 -4632 5196 O ATOM 5027 CB ALA D 52 -6.155 -66.068 55.287 1.00112.77 C ANISOU 5027 CB ALA D 52 15458 8702 18686 114 -4854 3743 C ATOM 5028 N GLY D 53 -8.541 -64.544 57.059 1.00106.38 N ANISOU 5028 N GLY D 53 14120 9431 16868 -1226 -4545 4779 N ATOM 5029 CA GLY D 53 -9.416 -64.636 58.230 1.00108.49 C ANISOU 5029 CA GLY D 53 14114 10114 16993 -1806 -4654 5568 C ATOM 5030 C GLY D 53 -9.273 -63.501 59.228 1.00105.08 C ANISOU 5030 C GLY D 53 13388 10668 15868 -1906 -4219 5765 C ATOM 5031 O GLY D 53 -9.530 -63.688 60.417 1.00107.83 O ANISOU 5031 O GLY D 53 13495 11421 16054 -2250 -4309 6464 O ATOM 5032 N SER D 54 -8.873 -62.321 58.750 1.00 99.90 N ANISOU 5032 N SER D 54 12758 10406 14793 -1608 -3768 5156 N ATOM 5033 CA SER D 54 -8.589 -61.191 59.640 1.00 97.37 C ANISOU 5033 CA SER D 54 12218 10914 13865 -1645 -3411 5208 C ATOM 5034 C SER D 54 -8.742 -59.837 58.957 1.00 91.83 C ANISOU 5034 C SER D 54 11551 10575 12767 -1465 -2948 4578 C ATOM 5035 O SER D 54 -8.138 -59.588 57.913 1.00 89.59 O ANISOU 5035 O SER D 54 11412 10000 12630 -1104 -2828 4052 O ATOM 5036 CB SER D 54 -7.171 -61.308 60.211 1.00 98.86 C ANISOU 5036 CB SER D 54 12320 11110 14131 -1413 -3510 5319 C ATOM 5037 OG SER D 54 -6.196 -61.065 59.205 1.00 97.15 O ANISOU 5037 OG SER D 54 12216 10569 14128 -940 -3377 4740 O ATOM 5038 N THR D 55 -9.533 -58.958 59.568 1.00 90.44 N ANISOU 5038 N THR D 55 11223 11056 12085 -1691 -2678 4661 N ATOM 5039 CA THR D 55 -9.770 -57.619 59.029 1.00 86.07 C ANISOU 5039 CA THR D 55 10679 10828 11197 -1541 -2264 4128 C ATOM 5040 C THR D 55 -9.753 -56.551 60.115 1.00 85.47 C ANISOU 5040 C THR D 55 10439 11473 10561 -1614 -2008 4144 C ATOM 5041 O THR D 55 -10.024 -56.837 61.285 1.00 88.74 O ANISOU 5041 O THR D 55 10719 12290 10709 -1849 -2094 4613 O ATOM 5042 CB THR D 55 -11.111 -57.540 58.298 1.00 85.25 C ANISOU 5042 CB THR D 55 10602 10678 11110 -1681 -2184 4048 C ATOM 5043 OG1 THR D 55 -12.120 -58.151 59.108 1.00 89.46 O ANISOU 5043 OG1 THR D 55 10963 11425 11601 -2070 -2330 4650 O ATOM 5044 CG2 THR D 55 -11.035 -58.260 56.954 1.00 85.73 C ANISOU 5044 CG2 THR D 55 10908 10042 11625 -1517 -2401 3763 C ATOM 5045 N GLU D 56 -9.432 -55.321 59.714 1.00 82.00 N ANISOU 5045 N GLU D 56 10023 11193 9941 -1404 -1714 3632 N ATOM 5046 CA GLU D 56 -9.330 -54.191 60.640 1.00 81.95 C ANISOU 5046 CA GLU D 56 9926 11765 9447 -1419 -1513 3489 C ATOM 5047 C GLU D 56 -9.919 -52.920 60.042 1.00 78.72 C ANISOU 5047 C GLU D 56 9530 11486 8894 -1296 -1165 3023 C ATOM 5048 O GLU D 56 -9.951 -52.754 58.822 1.00 76.02 O ANISOU 5048 O GLU D 56 9262 10786 8835 -1145 -1080 2766 O ATOM 5049 CB GLU D 56 -7.872 -53.952 61.052 1.00 82.44 C ANISOU 5049 CB GLU D 56 9972 11818 9533 -1299 -1653 3393 C ATOM 5050 CG GLU D 56 -7.310 -54.979 62.035 1.00 87.11 C ANISOU 5050 CG GLU D 56 10496 12471 10131 -1438 -2001 3917 C ATOM 5051 CD GLU D 56 -7.859 -54.832 63.451 1.00 91.55 C ANISOU 5051 CD GLU D 56 10975 13716 10092 -1675 -2006 4223 C ATOM 5052 OE1 GLU D 56 -8.394 -53.751 63.786 1.00 91.11 O ANISOU 5052 OE1 GLU D 56 10929 14107 9582 -1662 -1736 3897 O ATOM 5053 OE2 GLU D 56 -7.741 -55.800 64.237 1.00 96.26 O ANISOU 5053 OE2 GLU D 56 11497 14418 10661 -1847 -2280 4800 O ATOM 5054 N LYS D 57 -10.379 -52.026 60.915 1.00 79.70 N ANISOU 5054 N LYS D 57 9588 12134 8560 -1332 -973 2915 N ATOM 5055 CA LYS D 57 -11.030 -50.788 60.490 1.00 77.51 C ANISOU 5055 CA LYS D 57 9306 11973 8173 -1194 -654 2502 C ATOM 5056 C LYS D 57 -10.002 -49.759 60.056 1.00 75.15 C ANISOU 5056 C LYS D 57 9074 11452 8028 -1009 -622 2054 C ATOM 5057 O LYS D 57 -8.967 -49.597 60.706 1.00 76.48 O ANISOU 5057 O LYS D 57 9254 11680 8125 -1020 -791 2001 O ATOM 5058 CB LYS D 57 -11.903 -50.210 61.613 1.00 80.70 C ANISOU 5058 CB LYS D 57 9618 13009 8035 -1228 -447 2502 C ATOM 5059 CG LYS D 57 -12.965 -51.164 62.145 1.00 83.85 C ANISOU 5059 CG LYS D 57 9856 13750 8254 -1440 -438 3062 C ATOM 5060 CD LYS D 57 -13.970 -50.451 63.022 1.00 86.62 C ANISOU 5060 CD LYS D 57 10065 14786 8059 -1375 -108 3017 C ATOM 5061 CE LYS D 57 -14.995 -51.434 63.548 1.00 90.73 C ANISOU 5061 CE LYS D 57 10339 15710 8426 -1616 -85 3700 C ATOM 5062 NZ LYS D 57 -16.306 -50.781 63.803 1.00 93.34 N ANISOU 5062 NZ LYS D 57 10437 16587 8441 -1498 325 3684 N ATOM 5063 N GLY D 58 -10.302 -49.075 58.955 1.00 72.13 N ANISOU 5063 N GLY D 58 8704 10827 7874 -866 -435 1796 N ATOM 5064 CA GLY D 58 -9.448 -48.021 58.421 1.00 70.42 C ANISOU 5064 CA GLY D 58 8500 10390 7867 -718 -383 1460 C ATOM 5065 C GLY D 58 -9.876 -46.660 58.919 1.00 71.43 C ANISOU 5065 C GLY D 58 8626 10712 7804 -653 -221 1113 C ATOM 5066 O GLY D 58 -10.352 -46.535 60.044 1.00 74.13 O ANISOU 5066 O GLY D 58 8980 11444 7742 -697 -198 1069 O ATOM 5067 N ASP D 59 -9.710 -45.642 58.078 1.00 70.05 N ANISOU 5067 N ASP D 59 8435 10267 7913 -526 -109 876 N ATOM 5068 CA ASP D 59 -10.028 -44.263 58.451 1.00 71.99 C ANISOU 5068 CA ASP D 59 8698 10545 8111 -430 -1 503 C ATOM 5069 C ASP D 59 -11.513 -43.953 58.389 1.00 72.35 C ANISOU 5069 C ASP D 59 8703 10781 8004 -315 264 455 C ATOM 5070 O ASP D 59 -12.040 -43.284 59.278 1.00 75.39 O ANISOU 5070 O ASP D 59 9116 11417 8113 -217 363 186 O ATOM 5071 CB ASP D 59 -9.269 -43.271 57.572 1.00 71.33 C ANISOU 5071 CB ASP D 59 8570 10051 8481 -365 -19 365 C ATOM 5072 CG ASP D 59 -7.786 -43.218 57.893 1.00 73.76 C ANISOU 5072 CG ASP D 59 8846 10227 8953 -477 -288 365 C ATOM 5073 OD1 ASP D 59 -7.238 -42.092 57.935 1.00 77.13 O ANISOU 5073 OD1 ASP D 59 9246 10424 9634 -491 -389 143 O ATOM 5074 OD2 ASP D 59 -7.168 -44.291 58.102 1.00 74.32 O ANISOU 5074 OD2 ASP D 59 8893 10392 8953 -558 -429 612 O ATOM 5075 N ILE D 60 -12.178 -44.418 57.334 1.00 70.00 N ANISOU 5075 N ILE D 60 8334 10383 7879 -302 368 695 N ATOM 5076 CA ILE D 60 -13.622 -44.210 57.174 1.00 70.75 C ANISOU 5076 CA ILE D 60 8317 10671 7892 -214 590 742 C ATOM 5077 C ILE D 60 -14.374 -45.544 57.025 1.00 70.51 C ANISOU 5077 C ILE D 60 8212 10821 7758 -380 548 1153 C ATOM 5078 O ILE D 60 -14.737 -45.939 55.915 1.00 68.89 O ANISOU 5078 O ILE D 60 7982 10420 7772 -409 510 1320 O ATOM 5079 CB ILE D 60 -13.966 -43.213 56.016 1.00 69.45 C ANISOU 5079 CB ILE D 60 8091 10212 8083 -49 715 644 C ATOM 5080 CG1 ILE D 60 -13.238 -43.588 54.719 1.00 66.50 C ANISOU 5080 CG1 ILE D 60 7756 9518 7992 -95 603 815 C ATOM 5081 CG2 ILE D 60 -13.650 -41.771 56.432 1.00 71.30 C ANISOU 5081 CG2 ILE D 60 8362 10285 8443 118 763 247 C ATOM 5082 CD1 ILE D 60 -13.893 -43.050 53.449 1.00 65.64 C ANISOU 5082 CD1 ILE D 60 7561 9267 8111 18 708 907 C ATOM 5083 N PRO D 61 -14.616 -46.236 58.154 1.00 72.95 N ANISOU 5083 N PRO D 61 8483 11507 7726 -507 521 1337 N ATOM 5084 CA PRO D 61 -15.153 -47.593 58.136 1.00 73.58 C ANISOU 5084 CA PRO D 61 8484 11685 7787 -735 392 1802 C ATOM 5085 C PRO D 61 -16.679 -47.685 58.267 1.00 76.01 C ANISOU 5085 C PRO D 61 8537 12358 7987 -774 576 2067 C ATOM 5086 O PRO D 61 -17.250 -48.755 58.038 1.00 76.84 O ANISOU 5086 O PRO D 61 8540 12459 8198 -1007 422 2490 O ATOM 5087 CB PRO D 61 -14.496 -48.221 59.361 1.00 75.92 C ANISOU 5087 CB PRO D 61 8831 12226 7788 -868 250 1953 C ATOM 5088 CG PRO D 61 -14.310 -47.063 60.323 1.00 78.12 C ANISOU 5088 CG PRO D 61 9144 12820 7717 -687 420 1559 C ATOM 5089 CD PRO D 61 -14.361 -45.778 59.531 1.00 76.13 C ANISOU 5089 CD PRO D 61 8924 12273 7729 -453 573 1132 C ATOM 5090 N ASP D 62 -17.319 -46.576 58.635 1.00 77.80 N ANISOU 5090 N ASP D 62 8641 12870 8048 -539 880 1826 N ATOM 5091 CA ASP D 62 -18.756 -46.547 58.907 1.00 81.00 C ANISOU 5091 CA ASP D 62 8725 13729 8324 -508 1122 2087 C ATOM 5092 C ASP D 62 -19.582 -46.818 57.655 1.00 79.23 C ANISOU 5092 C ASP D 62 8345 13269 8490 -602 1038 2336 C ATOM 5093 O ASP D 62 -19.293 -46.281 56.585 1.00 76.48 O ANISOU 5093 O ASP D 62 8119 12505 8434 -493 975 2104 O ATOM 5094 CB ASP D 62 -19.157 -45.203 59.523 1.00 83.97 C ANISOU 5094 CB ASP D 62 9030 14402 8471 -131 1477 1672 C ATOM 5095 CG ASP D 62 -18.521 -44.970 60.887 1.00 87.87 C ANISOU 5095 CG ASP D 62 9679 15246 8460 -39 1535 1405 C ATOM 5096 OD1 ASP D 62 -18.763 -45.778 61.816 1.00 91.67 O ANISOU 5096 OD1 ASP D 62 10046 16245 8540 -193 1563 1769 O ATOM 5097 OD2 ASP D 62 -17.783 -43.969 61.031 1.00 88.49 O ANISOU 5097 OD2 ASP D 62 9990 15087 8546 168 1519 854 O ATOM 5098 N GLY D 63 -20.602 -47.660 57.800 1.00 81.52 N ANISOU 5098 N GLY D 63 8347 13851 8775 -830 1007 2851 N ATOM 5099 CA GLY D 63 -21.476 -48.028 56.693 1.00 80.66 C ANISOU 5099 CA GLY D 63 8066 13559 9023 -984 842 3131 C ATOM 5100 C GLY D 63 -21.002 -49.254 55.939 1.00 78.63 C ANISOU 5100 C GLY D 63 8031 12820 9024 -1305 379 3305 C ATOM 5101 O GLY D 63 -21.752 -49.832 55.154 1.00 79.70 O ANISOU 5101 O GLY D 63 8047 12815 9420 -1520 133 3579 O ATOM 5102 N TYR D 65 -19.759 -49.656 56.180 1.00 76.47 N ANISOU 5102 N TYR D 65 8078 12284 8695 -1323 231 3129 N ATOM 5103 CA TYR D 65 -19.155 -50.762 55.452 1.00 75.06 C ANISOU 5103 CA TYR D 65 8157 11590 8774 -1517 -185 3185 C ATOM 5104 C TYR D 65 -18.720 -51.876 56.387 1.00 76.96 C ANISOU 5104 C TYR D 65 8433 11840 8968 -1754 -388 3516 C ATOM 5105 O TYR D 65 -18.633 -51.689 57.601 1.00 78.89 O ANISOU 5105 O TYR D 65 8555 12521 8897 -1742 -190 3646 O ATOM 5106 CB TYR D 65 -17.919 -50.294 54.679 1.00 71.46 C ANISOU 5106 CB TYR D 65 8030 10737 8383 -1269 -200 2704 C ATOM 5107 CG TYR D 65 -18.069 -49.030 53.852 1.00 70.09 C ANISOU 5107 CG TYR D 65 7839 10548 8244 -1006 19 2398 C ATOM 5108 CD1 TYR D 65 -18.405 -49.089 52.497 1.00 69.55 C ANISOU 5108 CD1 TYR D 65 7835 10241 8350 -994 -135 2361 C ATOM 5109 CD2 TYR D 65 -17.831 -47.777 54.418 1.00 70.22 C ANISOU 5109 CD2 TYR D 65 7797 10761 8124 -767 338 2143 C ATOM 5110 CE1 TYR D 65 -18.520 -47.932 51.736 1.00 68.69 C ANISOU 5110 CE1 TYR D 65 7687 10133 8280 -764 48 2172 C ATOM 5111 CE2 TYR D 65 -17.946 -46.614 53.672 1.00 69.40 C ANISOU 5111 CE2 TYR D 65 7664 10566 8138 -538 499 1921 C ATOM 5112 CZ TYR D 65 -18.289 -46.695 52.333 1.00 68.96 C ANISOU 5112 CZ TYR D 65 7631 10312 8260 -542 366 1982 C ATOM 5113 OH TYR D 65 -18.389 -45.528 51.602 1.00 69.24 O ANISOU 5113 OH TYR D 65 7613 10275 8420 -323 514 1851 O ATOM 5114 N LYS D 66 -18.436 -53.035 55.800 1.00 77.06 N ANISOU 5114 N LYS D 66 8631 11360 9290 -1946 -805 3640 N ATOM 5115 CA LYS D 66 -17.767 -54.138 56.488 1.00 78.61 C ANISOU 5115 CA LYS D 66 8928 11376 9564 -2124 -1075 3918 C ATOM 5116 C LYS D 66 -16.662 -54.720 55.595 1.00 76.71 C ANISOU 5116 C LYS D 66 9067 10482 9597 -1989 -1366 3586 C ATOM 5117 O LYS D 66 -16.512 -54.327 54.436 1.00 74.39 O ANISOU 5117 O LYS D 66 8945 9943 9377 -1789 -1352 3184 O ATOM 5118 CB LYS D 66 -18.775 -55.229 56.870 1.00 83.40 C ANISOU 5118 CB LYS D 66 9290 12023 10374 -2550 -1353 4579 C ATOM 5119 CG LYS D 66 -19.673 -54.886 58.052 1.00 86.17 C ANISOU 5119 CG LYS D 66 9210 13139 10392 -2673 -1032 5048 C ATOM 5120 CD LYS D 66 -20.483 -56.092 58.496 1.00 90.97 C ANISOU 5120 CD LYS D 66 9536 13776 11253 -3145 -1342 5838 C ATOM 5121 CE LYS D 66 -21.277 -55.778 59.747 1.00 95.12 C ANISOU 5121 CE LYS D 66 9595 15188 11357 -3223 -954 6362 C ATOM 5122 NZ LYS D 66 -21.598 -57.008 60.524 1.00101.29 N ANISOU 5122 NZ LYS D 66 10128 16057 12300 -3674 -1239 7231 N ATOM 5123 N ALA D 67 -15.881 -55.648 56.141 1.00 78.23 N ANISOU 5123 N ALA D 67 9370 10433 9920 -2064 -1612 3779 N ATOM 5124 CA ALA D 67 -14.893 -56.391 55.355 1.00 77.54 C ANISOU 5124 CA ALA D 67 9608 9711 10141 -1900 -1903 3512 C ATOM 5125 C ALA D 67 -14.902 -57.887 55.697 1.00 81.86 C ANISOU 5125 C ALA D 67 10209 9822 11072 -2164 -2382 3941 C ATOM 5126 O ALA D 67 -15.334 -58.284 56.786 1.00 84.74 O ANISOU 5126 O ALA D 67 10338 10456 11404 -2466 -2446 4516 O ATOM 5127 CB ALA D 67 -13.513 -55.800 55.551 1.00 74.80 C ANISOU 5127 CB ALA D 67 9358 9418 9646 -1572 -1692 3194 C ATOM 5128 N SER D 68 -14.441 -58.711 54.758 1.00 82.76 N ANISOU 5128 N SER D 68 10631 9266 11548 -2032 -2722 3673 N ATOM 5129 CA SER D 68 -14.300 -60.147 54.992 1.00 87.46 C ANISOU 5129 CA SER D 68 11335 9279 12618 -2218 -3234 4003 C ATOM 5130 C SER D 68 -13.127 -60.737 54.214 1.00 88.02 C ANISOU 5130 C SER D 68 11767 8717 12958 -1810 -3421 3531 C ATOM 5131 O SER D 68 -13.010 -60.538 53.005 1.00 86.79 O ANISOU 5131 O SER D 68 11859 8352 12765 -1526 -3389 2966 O ATOM 5132 CB SER D 68 -15.594 -60.888 54.639 1.00 91.54 C ANISOU 5132 CB SER D 68 11811 9507 13462 -2639 -3647 4298 C ATOM 5133 OG SER D 68 -15.551 -62.230 55.098 1.00 96.91 O ANISOU 5133 OG SER D 68 12527 9637 14657 -2906 -4167 4765 O ATOM 5134 N ARG D 69 -12.261 -61.458 54.919 1.00 90.35 N ANISOU 5134 N ARG D 69 12069 8759 13500 -1753 -3603 3788 N ATOM 5135 CA ARG D 69 -11.169 -62.189 54.286 1.00 92.39 C ANISOU 5135 CA ARG D 69 12624 8377 14102 -1333 -3809 3413 C ATOM 5136 C ARG D 69 -11.375 -63.694 54.483 1.00 99.31 C ANISOU 5136 C ARG D 69 13630 8489 15616 -1549 -4437 3765 C ATOM 5137 O ARG D 69 -11.301 -64.180 55.610 1.00102.05 O ANISOU 5137 O ARG D 69 13767 8870 16139 -1815 -4608 4420 O ATOM 5138 CB ARG D 69 -9.827 -61.756 54.875 1.00 90.17 C ANISOU 5138 CB ARG D 69 12215 8371 13674 -1013 -3525 3408 C ATOM 5139 CG ARG D 69 -8.616 -62.205 54.082 1.00 91.21 C ANISOU 5139 CG ARG D 69 12570 8019 14066 -453 -3562 2945 C ATOM 5140 CD ARG D 69 -8.229 -61.189 53.022 1.00 86.64 C ANISOU 5140 CD ARG D 69 12060 7740 13120 -59 -3115 2337 C ATOM 5141 NE ARG D 69 -7.031 -61.587 52.281 1.00 88.51 N ANISOU 5141 NE ARG D 69 12444 7640 13545 530 -3069 1933 N ATOM 5142 CZ ARG D 69 -5.793 -61.179 52.560 1.00 87.56 C ANISOU 5142 CZ ARG D 69 12107 7766 13396 845 -2801 1956 C ATOM 5143 NH1 ARG D 69 -5.559 -60.353 53.571 1.00 84.65 N ANISOU 5143 NH1 ARG D 69 11419 7937 12809 604 -2613 2311 N ATOM 5144 NH2 ARG D 69 -4.776 -61.597 51.823 1.00 90.39 N ANISOU 5144 NH2 ARG D 69 12557 7847 13940 1418 -2731 1612 N ATOM 5145 N PRO D 70 -11.676 -64.432 53.397 1.00102.97 N ANISOU 5145 N PRO D 70 14445 8255 16424 -1455 -4820 3350 N ATOM 5146 CA PRO D 70 -11.699 -65.891 53.506 1.00110.39 C ANISOU 5146 CA PRO D 70 15567 8299 18079 -1588 -5479 3590 C ATOM 5147 C PRO D 70 -10.361 -66.518 53.087 1.00113.40 C ANISOU 5147 C PRO D 70 16231 8083 18773 -962 -5573 3139 C ATOM 5148 O PRO D 70 -9.697 -67.171 53.900 1.00116.50 O ANISOU 5148 O PRO D 70 16516 8200 19549 -931 -5766 3577 O ATOM 5149 CB PRO D 70 -12.833 -66.306 52.551 1.00113.56 C ANISOU 5149 CB PRO D 70 16213 8255 18681 -1847 -5904 3326 C ATOM 5150 CG PRO D 70 -13.292 -65.032 51.851 1.00107.42 C ANISOU 5150 CG PRO D 70 15389 8186 17241 -1761 -5415 2909 C ATOM 5151 CD PRO D 70 -12.271 -63.976 52.129 1.00101.43 C ANISOU 5151 CD PRO D 70 14471 8082 15984 -1348 -4752 2749 C ATOM 5152 N SER D 71 -9.980 -66.313 51.828 1.00113.08 N ANISOU 5152 N SER D 71 16519 7898 18547 -444 -5424 2303 N ATOM 5153 CA SER D 71 -8.704 -66.783 51.301 1.00116.18 C ANISOU 5153 CA SER D 71 17147 7856 19141 262 -5391 1796 C ATOM 5154 C SER D 71 -7.668 -65.683 51.462 1.00110.48 C ANISOU 5154 C SER D 71 16145 7907 17927 641 -4709 1719 C ATOM 5155 O SER D 71 -7.991 -64.580 51.899 1.00104.52 O ANISOU 5155 O SER D 71 15096 7922 16695 357 -4322 1965 O ATOM 5156 CB SER D 71 -8.844 -67.144 49.817 1.00119.86 C ANISOU 5156 CB SER D 71 18118 7846 19579 663 -5565 916 C ATOM 5157 OG SER D 71 -9.902 -68.062 49.596 1.00125.44 O ANISOU 5157 OG SER D 71 19095 7835 20733 241 -6262 941 O ATOM 5158 N GLN D 72 -6.421 -65.981 51.112 1.00113.15 N ANISOU 5158 N GLN D 72 16553 8020 18419 1291 -4580 1383 N ATOM 5159 CA GLN D 72 -5.408 -64.944 51.016 1.00108.94 C ANISOU 5159 CA GLN D 72 15752 8181 17461 1682 -3957 1249 C ATOM 5160 C GLN D 72 -5.643 -64.147 49.735 1.00106.63 C ANISOU 5160 C GLN D 72 15633 8258 16622 1937 -3581 621 C ATOM 5161 O GLN D 72 -5.386 -62.939 49.683 1.00101.26 O ANISOU 5161 O GLN D 72 14692 8303 15480 1956 -3074 643 O ATOM 5162 CB GLN D 72 -4.001 -65.543 51.016 1.00113.31 C ANISOU 5162 CB GLN D 72 16246 8419 18387 2318 -3925 1154 C ATOM 5163 CG GLN D 72 -2.895 -64.528 51.315 1.00109.29 C ANISOU 5163 CG GLN D 72 15300 8641 17584 2560 -3377 1301 C ATOM 5164 CD GLN D 72 -1.587 -64.853 50.617 1.00113.75 C ANISOU 5164 CD GLN D 72 15836 9061 18324 3380 -3147 921 C ATOM 5165 OE1 GLN D 72 -1.243 -66.021 50.425 1.00120.97 O ANISOU 5165 OE1 GLN D 72 16965 9249 19749 3775 -3471 747 O ATOM 5166 NE2 GLN D 72 -0.849 -63.818 50.233 1.00110.34 N ANISOU 5166 NE2 GLN D 72 15112 9310 17503 3656 -2586 813 N ATOM 5167 N GLU D 73 -6.146 -64.828 48.708 1.00111.33 N ANISOU 5167 N GLU D 73 16679 8338 17282 2114 -3878 77 N ATOM 5168 CA GLU D 73 -6.349 -64.205 47.403 1.00110.55 C ANISOU 5168 CA GLU D 73 16793 8584 16628 2405 -3580 -531 C ATOM 5169 C GLU D 73 -7.587 -63.299 47.294 1.00105.59 C ANISOU 5169 C GLU D 73 16096 8439 15584 1845 -3514 -385 C ATOM 5170 O GLU D 73 -7.608 -62.380 46.472 1.00102.94 O ANISOU 5170 O GLU D 73 15752 8645 14717 2028 -3116 -664 O ATOM 5171 CB GLU D 73 -6.305 -65.241 46.272 1.00118.22 C ANISOU 5171 CB GLU D 73 18310 8884 17723 2903 -3916 -1272 C ATOM 5172 CG GLU D 73 -6.954 -66.579 46.570 1.00124.50 C ANISOU 5172 CG GLU D 73 19427 8697 19181 2612 -4705 -1238 C ATOM 5173 CD GLU D 73 -6.572 -67.644 45.550 1.00133.92 C ANISOU 5173 CD GLU D 73 21173 9140 20572 3268 -5025 -2058 C ATOM 5174 OE1 GLU D 73 -5.903 -67.306 44.548 1.00135.35 O ANISOU 5174 OE1 GLU D 73 21490 9681 20254 3954 -4585 -2671 O ATOM 5175 OE2 GLU D 73 -6.937 -68.824 45.748 1.00140.42 O ANISOU 5175 OE2 GLU D 73 22291 9010 22053 3115 -5723 -2088 O ATOM 5176 N ASN D 74 -8.599 -63.544 48.126 1.00105.00 N ANISOU 5176 N ASN D 74 15928 8203 15764 1186 -3885 107 N ATOM 5177 CA ASN D 74 -9.853 -62.786 48.043 1.00101.39 C ANISOU 5177 CA ASN D 74 15368 8166 14988 680 -3855 272 C ATOM 5178 C ASN D 74 -10.080 -61.731 49.132 1.00 95.32 C ANISOU 5178 C ASN D 74 14125 8076 14018 291 -3489 859 C ATOM 5179 O ASN D 74 -9.487 -61.796 50.208 1.00 94.49 O ANISOU 5179 O ASN D 74 13777 8040 14086 228 -3422 1267 O ATOM 5180 CB ASN D 74 -11.055 -63.732 47.939 1.00106.03 C ANISOU 5180 CB ASN D 74 16185 8164 15937 221 -4531 340 C ATOM 5181 CG ASN D 74 -11.325 -64.184 46.509 1.00110.78 C ANISOU 5181 CG ASN D 74 17285 8388 16418 505 -4829 -398 C ATOM 5182 OD1 ASN D 74 -11.501 -63.364 45.600 1.00107.89 O ANISOU 5182 OD1 ASN D 74 16980 8513 15499 684 -4530 -747 O ATOM 5183 ND2 ASN D 74 -11.370 -65.498 46.305 1.00118.25 N ANISOU 5183 ND2 ASN D 74 18606 8443 17881 547 -5460 -638 N ATOM 5184 N PHE D 75 -10.936 -60.756 48.818 1.00 91.85 N ANISOU 5184 N PHE D 75 13570 8135 13195 66 -3274 866 N ATOM 5185 CA PHE D 75 -11.339 -59.680 49.736 1.00 87.00 C ANISOU 5185 CA PHE D 75 12552 8150 12355 -264 -2936 1311 C ATOM 5186 C PHE D 75 -12.714 -59.150 49.315 1.00 85.92 C ANISOU 5186 C PHE D 75 12358 8269 12020 -594 -2970 1356 C ATOM 5187 O PHE D 75 -13.081 -59.234 48.140 1.00 87.68 O ANISOU 5187 O PHE D 75 12833 8357 12125 -469 -3109 967 O ATOM 5188 CB PHE D 75 -10.321 -58.532 49.714 1.00 82.81 C ANISOU 5188 CB PHE D 75 11840 8115 11509 80 -2380 1181 C ATOM 5189 CG PHE D 75 -10.229 -57.751 51.009 1.00 79.44 C ANISOU 5189 CG PHE D 75 11053 8143 10986 -165 -2135 1602 C ATOM 5190 CD1 PHE D 75 -11.106 -57.984 52.066 1.00 79.92 C ANISOU 5190 CD1 PHE D 75 10950 8298 11117 -626 -2312 2066 C ATOM 5191 CD2 PHE D 75 -9.265 -56.758 51.157 1.00 76.64 C ANISOU 5191 CD2 PHE D 75 10516 8155 10449 69 -1737 1532 C ATOM 5192 CE1 PHE D 75 -11.015 -57.253 53.249 1.00 77.95 C ANISOU 5192 CE1 PHE D 75 10414 8531 10672 -792 -2078 2374 C ATOM 5193 CE2 PHE D 75 -9.169 -56.019 52.337 1.00 74.55 C ANISOU 5193 CE2 PHE D 75 9978 8283 10065 -145 -1573 1824 C ATOM 5194 CZ PHE D 75 -10.045 -56.268 53.386 1.00 75.04 C ANISOU 5194 CZ PHE D 75 9932 8468 10112 -548 -1734 2206 C ATOM 5195 N SER D 76 -13.464 -58.601 50.270 1.00 83.79 N ANISOU 5195 N SER D 76 11746 8406 11684 -983 -2842 1826 N ATOM 5196 CA SER D 76 -14.816 -58.098 50.017 1.00 83.26 C ANISOU 5196 CA SER D 76 11525 8620 11490 -1293 -2857 1966 C ATOM 5197 C SER D 76 -15.215 -56.946 50.936 1.00 79.71 C ANISOU 5197 C SER D 76 10678 8820 10789 -1435 -2424 2288 C ATOM 5198 O SER D 76 -15.060 -57.027 52.157 1.00 79.98 O ANISOU 5198 O SER D 76 10511 9032 10845 -1589 -2347 2654 O ATOM 5199 CB SER D 76 -15.842 -59.230 50.127 1.00 88.16 C ANISOU 5199 CB SER D 76 12167 8837 12491 -1741 -3430 2277 C ATOM 5200 OG SER D 76 -15.885 -59.993 48.935 1.00 92.01 O ANISOU 5200 OG SER D 76 13059 8776 13126 -1625 -3863 1833 O ATOM 5201 N LEU D 77 -15.736 -55.881 50.333 1.00 77.26 N ANISOU 5201 N LEU D 77 10269 8859 10227 -1357 -2160 2139 N ATOM 5202 CA LEU D 77 -16.252 -54.722 51.060 1.00 74.65 C ANISOU 5202 CA LEU D 77 9589 9089 9687 -1430 -1766 2353 C ATOM 5203 C LEU D 77 -17.784 -54.751 51.029 1.00 76.83 C ANISOU 5203 C LEU D 77 9620 9543 10028 -1764 -1906 2676 C ATOM 5204 O LEU D 77 -18.384 -54.738 49.953 1.00 77.85 O ANISOU 5204 O LEU D 77 9830 9568 10181 -1780 -2091 2536 O ATOM 5205 CB LEU D 77 -15.698 -53.441 50.429 1.00 71.03 C ANISOU 5205 CB LEU D 77 9148 8848 8993 -1079 -1376 2010 C ATOM 5206 CG LEU D 77 -16.069 -52.050 50.937 1.00 68.51 C ANISOU 5206 CG LEU D 77 8543 8988 8499 -1035 -969 2073 C ATOM 5207 CD1 LEU D 77 -15.598 -51.818 52.357 1.00 68.07 C ANISOU 5207 CD1 LEU D 77 8349 9154 8360 -1070 -787 2204 C ATOM 5208 CD2 LEU D 77 -15.450 -51.031 50.014 1.00 66.09 C ANISOU 5208 CD2 LEU D 77 8310 8712 8090 -719 -726 1770 C ATOM 5209 N ILE D 78 -18.410 -54.796 52.206 1.00 78.33 N ANISOU 5209 N ILE D 78 9485 10055 10223 -2024 -1822 3136 N ATOM 5210 CA ILE D 78 -19.851 -55.100 52.321 1.00 81.72 C ANISOU 5210 CA ILE D 78 9596 10653 10799 -2396 -2002 3590 C ATOM 5211 C ILE D 78 -20.723 -53.940 52.831 1.00 81.07 C ANISOU 5211 C ILE D 78 9091 11219 10493 -2348 -1553 3774 C ATOM 5212 O ILE D 78 -20.450 -53.345 53.881 1.00 80.14 O ANISOU 5212 O ILE D 78 8825 11501 10124 -2219 -1169 3825 O ATOM 5213 CB ILE D 78 -20.108 -56.345 53.230 1.00 86.01 C ANISOU 5213 CB ILE D 78 10016 11062 11603 -2798 -2331 4146 C ATOM 5214 CG1 ILE D 78 -18.991 -57.394 53.090 1.00 86.85 C ANISOU 5214 CG1 ILE D 78 10527 10533 11938 -2743 -2686 3964 C ATOM 5215 CG2 ILE D 78 -21.503 -56.924 52.985 1.00 90.47 C ANISOU 5215 CG2 ILE D 78 10298 11607 12469 -3239 -2691 4613 C ATOM 5216 CD1 ILE D 78 -18.931 -58.117 51.752 1.00 88.74 C ANISOU 5216 CD1 ILE D 78 11152 10118 12448 -2716 -3168 3581 C ATOM 5217 N LEU D 79 -21.785 -53.646 52.084 1.00 82.30 N ANISOU 5217 N LEU D 79 9057 11472 10741 -2434 -1635 3857 N ATOM 5218 CA LEU D 79 -22.780 -52.654 52.488 1.00 82.94 C ANISOU 5218 CA LEU D 79 8681 12132 10700 -2371 -1251 4080 C ATOM 5219 C LEU D 79 -24.108 -53.334 52.808 1.00 88.02 C ANISOU 5219 C LEU D 79 8876 12993 11575 -2795 -1471 4729 C ATOM 5220 O LEU D 79 -24.856 -53.706 51.900 1.00 90.24 O ANISOU 5220 O LEU D 79 9093 13077 12116 -3023 -1866 4850 O ATOM 5221 CB LEU D 79 -22.984 -51.618 51.382 1.00 80.79 C ANISOU 5221 CB LEU D 79 8443 11865 10387 -2100 -1137 3752 C ATOM 5222 CG LEU D 79 -21.900 -50.579 51.089 1.00 76.83 C ANISOU 5222 CG LEU D 79 8215 11291 9685 -1672 -816 3238 C ATOM 5223 CD1 LEU D 79 -20.637 -51.198 50.486 1.00 75.19 C ANISOU 5223 CD1 LEU D 79 8490 10611 9468 -1600 -1045 2889 C ATOM 5224 CD2 LEU D 79 -22.475 -49.545 50.143 1.00 76.69 C ANISOU 5224 CD2 LEU D 79 8072 11381 9686 -1478 -708 3148 C ATOM 5225 N GLU D 80 -24.390 -53.501 54.099 1.00 90.51 N ANISOU 5225 N GLU D 80 8861 13750 11780 -2913 -1233 5175 N ATOM 5226 CA GLU D 80 -25.628 -54.143 54.553 1.00 96.27 C ANISOU 5226 CA GLU D 80 9061 14790 12727 -3332 -1378 5926 C ATOM 5227 C GLU D 80 -26.845 -53.298 54.147 1.00 97.70 C ANISOU 5227 C GLU D 80 8772 15398 12953 -3242 -1170 6078 C ATOM 5228 O GLU D 80 -27.726 -53.773 53.427 1.00100.85 O ANISOU 5228 O GLU D 80 8957 15651 13712 -3574 -1590 6392 O ATOM 5229 CB GLU D 80 -25.601 -54.374 56.072 1.00 99.18 C ANISOU 5229 CB GLU D 80 9154 15689 12842 -3402 -1064 6393 C ATOM 5230 CG GLU D 80 -24.358 -55.116 56.602 1.00 98.29 C ANISOU 5230 CG GLU D 80 9457 15223 12664 -3452 -1242 6298 C ATOM 5231 CD GLU D 80 -24.545 -56.630 56.749 1.00103.44 C ANISOU 5231 CD GLU D 80 10058 15490 13755 -3996 -1817 6921 C ATOM 5232 OE1 GLU D 80 -25.388 -57.221 56.037 1.00107.00 O ANISOU 5232 OE1 GLU D 80 10350 15647 14657 -4358 -2260 7212 O ATOM 5233 OE2 GLU D 80 -23.833 -57.234 57.583 1.00104.24 O ANISOU 5233 OE2 GLU D 80 10277 15548 13781 -4077 -1873 7136 O ATOM 5234 N LEU D 81 -26.878 -52.049 54.612 1.00 95.87 N ANISOU 5234 N LEU D 81 8383 15657 12386 -2785 -562 5843 N ATOM 5235 CA LEU D 81 -27.845 -51.057 54.152 1.00 96.62 C ANISOU 5235 CA LEU D 81 8093 16078 12540 -2556 -320 5862 C ATOM 5236 C LEU D 81 -27.079 -50.017 53.347 1.00 91.09 C ANISOU 5236 C LEU D 81 7816 15057 11737 -2125 -197 5152 C ATOM 5237 O LEU D 81 -26.140 -49.396 53.859 1.00 88.11 O ANISOU 5237 O LEU D 81 7724 14676 11079 -1795 131 4712 O ATOM 5238 CB LEU D 81 -28.555 -50.367 55.327 1.00100.31 C ANISOU 5238 CB LEU D 81 8017 17352 12745 -2295 304 6142 C ATOM 5239 CG LEU D 81 -28.940 -51.118 56.609 1.00106.05 C ANISOU 5239 CG LEU D 81 8356 18628 13310 -2549 458 6787 C ATOM 5240 CD1 LEU D 81 -29.316 -50.126 57.712 1.00109.18 C ANISOU 5240 CD1 LEU D 81 8396 19838 13250 -2063 1196 6752 C ATOM 5241 CD2 LEU D 81 -30.064 -52.134 56.386 1.00112.16 C ANISOU 5241 CD2 LEU D 81 8605 19486 14523 -3119 55 7631 C ATOM 5242 N ALA D 82 -27.465 -49.838 52.087 1.00 90.20 N ANISOU 5242 N ALA D 82 7731 14686 11853 -2156 -494 5082 N ATOM 5243 CA ALA D 82 -26.809 -48.863 51.223 1.00 85.69 C ANISOU 5243 CA ALA D 82 7503 13849 11206 -1783 -399 4538 C ATOM 5244 C ALA D 82 -27.335 -47.465 51.515 1.00 86.24 C ANISOU 5244 C ALA D 82 7226 14299 11243 -1345 113 4485 C ATOM 5245 O ALA D 82 -28.408 -47.319 52.107 1.00 90.48 O ANISOU 5245 O ALA D 82 7214 15320 11845 -1332 333 4887 O ATOM 5246 CB ALA D 82 -27.020 -49.224 49.770 1.00 85.76 C ANISOU 5246 CB ALA D 82 7685 13507 11394 -1971 -924 4511 C ATOM 5247 N THR D 83 -26.564 -46.450 51.126 1.00 82.58 N ANISOU 5247 N THR D 83 7060 13609 10709 -973 303 4009 N ATOM 5248 CA THR D 83 -26.977 -45.043 51.219 1.00 83.45 C ANISOU 5248 CA THR D 83 6916 13904 10888 -522 708 3891 C ATOM 5249 C THR D 83 -26.469 -44.271 50.005 1.00 80.76 C ANISOU 5249 C THR D 83 6843 13175 10668 -337 585 3634 C ATOM 5250 O THR D 83 -25.480 -44.676 49.398 1.00 77.56 O ANISOU 5250 O THR D 83 6883 12421 10165 -457 347 3411 O ATOM 5251 CB THR D 83 -26.463 -44.348 52.505 1.00 83.37 C ANISOU 5251 CB THR D 83 6960 14069 10648 -180 1192 3552 C ATOM 5252 OG1 THR D 83 -25.147 -44.811 52.817 1.00 80.05 O ANISOU 5252 OG1 THR D 83 7026 13374 10017 -294 1093 3242 O ATOM 5253 CG2 THR D 83 -27.385 -44.621 53.684 1.00 88.30 C ANISOU 5253 CG2 THR D 83 7118 15305 11126 -175 1486 3886 C ATOM 5254 N PRO D 84 -27.148 -43.162 49.640 1.00 82.74 N ANISOU 5254 N PRO D 84 6792 13509 11138 -25 757 3708 N ATOM 5255 CA PRO D 84 -26.731 -42.320 48.524 1.00 81.08 C ANISOU 5255 CA PRO D 84 6768 12975 11062 159 662 3577 C ATOM 5256 C PRO D 84 -25.299 -41.838 48.668 1.00 77.63 C ANISOU 5256 C PRO D 84 6788 12187 10521 317 799 3122 C ATOM 5257 O PRO D 84 -24.547 -41.871 47.693 1.00 75.70 O ANISOU 5257 O PRO D 84 6847 11681 10235 253 593 3053 O ATOM 5258 CB PRO D 84 -27.676 -41.127 48.618 1.00 84.64 C ANISOU 5258 CB PRO D 84 6764 13583 11811 546 935 3720 C ATOM 5259 CG PRO D 84 -28.901 -41.685 49.207 1.00 88.92 C ANISOU 5259 CG PRO D 84 6799 14598 12388 431 990 4105 C ATOM 5260 CD PRO D 84 -28.433 -42.707 50.201 1.00 87.65 C ANISOU 5260 CD PRO D 84 6817 14567 11919 170 1032 4010 C ATOM 5261 N SER D 85 -24.921 -41.413 49.875 1.00 77.74 N ANISOU 5261 N SER D 85 6833 12236 10467 517 1132 2829 N ATOM 5262 CA SER D 85 -23.574 -40.883 50.142 1.00 74.91 C ANISOU 5262 CA SER D 85 6855 11543 10064 644 1227 2408 C ATOM 5263 C SER D 85 -22.441 -41.907 49.957 1.00 71.24 C ANISOU 5263 C SER D 85 6781 10919 9369 351 999 2309 C ATOM 5264 O SER D 85 -21.262 -41.562 50.068 1.00 69.29 O ANISOU 5264 O SER D 85 6806 10412 9108 415 1036 2032 O ATOM 5265 CB SER D 85 -23.511 -40.267 51.541 1.00 76.90 C ANISOU 5265 CB SER D 85 7066 11909 10242 909 1567 2078 C ATOM 5266 OG SER D 85 -23.725 -41.253 52.533 1.00 77.71 O ANISOU 5266 OG SER D 85 7115 12395 10018 726 1622 2149 O ATOM 5267 N GLN D 86 -22.804 -43.157 49.674 1.00 71.01 N ANISOU 5267 N GLN D 86 6755 11016 9211 39 740 2546 N ATOM 5268 CA GLN D 86 -21.833 -44.211 49.375 1.00 68.36 C ANISOU 5268 CA GLN D 86 6781 10483 8708 -189 489 2452 C ATOM 5269 C GLN D 86 -21.638 -44.379 47.864 1.00 67.51 C ANISOU 5269 C GLN D 86 6848 10199 8602 -229 220 2502 C ATOM 5270 O GLN D 86 -21.133 -45.405 47.402 1.00 66.77 O ANISOU 5270 O GLN D 86 7027 9973 8369 -395 -41 2440 O ATOM 5271 CB GLN D 86 -22.237 -45.531 50.046 1.00 69.57 C ANISOU 5271 CB GLN D 86 6887 10795 8751 -501 320 2644 C ATOM 5272 CG GLN D 86 -22.051 -45.524 51.564 1.00 70.62 C ANISOU 5272 CG GLN D 86 6948 11147 8736 -466 580 2578 C ATOM 5273 CD GLN D 86 -22.466 -46.828 52.232 1.00 73.27 C ANISOU 5273 CD GLN D 86 7187 11664 8987 -802 408 2899 C ATOM 5274 OE1 GLN D 86 -23.641 -47.206 52.218 1.00 76.75 O ANISOU 5274 OE1 GLN D 86 7288 12350 9524 -976 331 3286 O ATOM 5275 NE2 GLN D 86 -21.501 -47.515 52.837 1.00 72.14 N ANISOU 5275 NE2 GLN D 86 7300 11401 8708 -910 327 2804 N ATOM 5276 N THR D 87 -22.044 -43.359 47.108 1.00 68.26 N ANISOU 5276 N THR D 87 6788 10305 8843 -44 283 2610 N ATOM 5277 CA THR D 87 -21.760 -43.276 45.678 1.00 68.14 C ANISOU 5277 CA THR D 87 6932 10206 8752 -20 89 2674 C ATOM 5278 C THR D 87 -20.322 -42.814 45.485 1.00 65.91 C ANISOU 5278 C THR D 87 6903 9716 8425 138 247 2463 C ATOM 5279 O THR D 87 -19.992 -41.648 45.718 1.00 65.77 O ANISOU 5279 O THR D 87 6781 9583 8624 331 480 2443 O ATOM 5280 CB THR D 87 -22.706 -42.291 44.948 1.00 70.59 C ANISOU 5280 CB THR D 87 6939 10629 9254 119 85 2969 C ATOM 5281 OG1 THR D 87 -24.070 -42.704 45.111 1.00 73.25 O ANISOU 5281 OG1 THR D 87 6956 11199 9675 -31 -70 3228 O ATOM 5282 CG2 THR D 87 -22.375 -42.233 43.462 1.00 71.32 C ANISOU 5282 CG2 THR D 87 7208 10725 9164 139 -123 3079 C ATOM 5283 N SER D 88 -19.467 -43.744 45.075 1.00 64.86 N ANISOU 5283 N SER D 88 7080 9512 8050 60 104 2313 N ATOM 5284 CA SER D 88 -18.053 -43.459 44.851 1.00 63.40 C ANISOU 5284 CA SER D 88 7079 9194 7816 202 256 2171 C ATOM 5285 C SER D 88 -17.474 -44.415 43.825 1.00 64.14 C ANISOU 5285 C SER D 88 7465 9318 7589 211 72 2081 C ATOM 5286 O SER D 88 -18.203 -45.128 43.132 1.00 66.07 O ANISOU 5286 O SER D 88 7803 9652 7648 114 -214 2105 O ATOM 5287 CB SER D 88 -17.260 -43.589 46.155 1.00 61.45 C ANISOU 5287 CB SER D 88 6880 8813 7656 177 398 1956 C ATOM 5288 OG SER D 88 -17.561 -42.543 47.053 1.00 61.57 O ANISOU 5288 OG SER D 88 6688 8795 7911 250 595 1937 O ATOM 5289 N VAL D 89 -16.152 -44.407 43.730 1.00 63.41 N ANISOU 5289 N VAL D 89 7503 9155 7436 346 226 1963 N ATOM 5290 CA VAL D 89 -15.419 -45.419 42.994 1.00 64.57 C ANISOU 5290 CA VAL D 89 7936 9322 7274 439 119 1786 C ATOM 5291 C VAL D 89 -14.601 -46.205 44.020 1.00 63.09 C ANISOU 5291 C VAL D 89 7857 8934 7182 400 129 1574 C ATOM 5292 O VAL D 89 -14.042 -45.618 44.949 1.00 61.29 O ANISOU 5292 O VAL D 89 7482 8628 7179 388 315 1594 O ATOM 5293 CB VAL D 89 -14.489 -44.797 41.934 1.00 65.98 C ANISOU 5293 CB VAL D 89 8110 9677 7283 686 331 1905 C ATOM 5294 CG1 VAL D 89 -14.186 -45.815 40.854 1.00 69.04 C ANISOU 5294 CG1 VAL D 89 8806 10211 7216 849 192 1705 C ATOM 5295 CG2 VAL D 89 -15.109 -43.537 41.321 1.00 66.67 C ANISOU 5295 CG2 VAL D 89 7960 9915 7458 707 407 2260 C ATOM 5296 N TYR D 90 -14.540 -47.524 43.869 1.00 64.49 N ANISOU 5296 N TYR D 90 8296 8999 7210 377 -116 1371 N ATOM 5297 CA TYR D 90 -13.871 -48.368 44.873 1.00 63.88 C ANISOU 5297 CA TYR D 90 8304 8703 7266 326 -164 1237 C ATOM 5298 C TYR D 90 -12.657 -49.127 44.328 1.00 65.47 C ANISOU 5298 C TYR D 90 8726 8817 7331 596 -148 1020 C ATOM 5299 O TYR D 90 -12.761 -49.873 43.347 1.00 68.35 O ANISOU 5299 O TYR D 90 9353 9159 7457 732 -330 822 O ATOM 5300 CB TYR D 90 -14.871 -49.321 45.547 1.00 64.51 C ANISOU 5300 CB TYR D 90 8430 8635 7447 31 -487 1262 C ATOM 5301 CG TYR D 90 -15.963 -48.608 46.333 1.00 63.63 C ANISOU 5301 CG TYR D 90 8022 8677 7476 -183 -418 1500 C ATOM 5302 CD1 TYR D 90 -17.175 -48.266 45.725 1.00 64.82 C ANISOU 5302 CD1 TYR D 90 8051 8976 7603 -273 -526 1648 C ATOM 5303 CD2 TYR D 90 -15.783 -48.272 47.684 1.00 61.92 C ANISOU 5303 CD2 TYR D 90 7636 8500 7390 -260 -246 1568 C ATOM 5304 CE1 TYR D 90 -18.182 -47.606 46.436 1.00 64.68 C ANISOU 5304 CE1 TYR D 90 7713 9129 7732 -396 -418 1870 C ATOM 5305 CE2 TYR D 90 -16.787 -47.614 48.409 1.00 61.90 C ANISOU 5305 CE2 TYR D 90 7366 8694 7461 -370 -133 1733 C ATOM 5306 CZ TYR D 90 -17.986 -47.283 47.775 1.00 63.54 C ANISOU 5306 CZ TYR D 90 7420 9036 7688 -419 -197 1890 C ATOM 5307 OH TYR D 90 -18.992 -46.633 48.466 1.00 63.85 O ANISOU 5307 OH TYR D 90 7146 9296 7818 -459 -46 2060 O ATOM 5308 N PHE D 91 -11.511 -48.915 44.977 1.00 64.24 N ANISOU 5308 N PHE D 91 8455 8625 7327 693 58 1042 N ATOM 5309 CA PHE D 91 -10.243 -49.526 44.576 1.00 66.02 C ANISOU 5309 CA PHE D 91 8786 8811 7488 1001 144 893 C ATOM 5310 C PHE D 91 -9.746 -50.526 45.623 1.00 66.14 C ANISOU 5310 C PHE D 91 8865 8541 7724 942 -27 822 C ATOM 5311 O PHE D 91 -9.712 -50.224 46.816 1.00 64.09 O ANISOU 5311 O PHE D 91 8435 8248 7667 721 -26 974 O ATOM 5312 CB PHE D 91 -9.170 -48.453 44.330 1.00 65.67 C ANISOU 5312 CB PHE D 91 8473 8994 7486 1181 510 1077 C ATOM 5313 CG PHE D 91 -9.492 -47.505 43.205 1.00 66.04 C ANISOU 5313 CG PHE D 91 8436 9332 7326 1271 685 1238 C ATOM 5314 CD1 PHE D 91 -10.014 -46.244 43.469 1.00 64.05 C ANISOU 5314 CD1 PHE D 91 7950 9126 7259 1076 768 1488 C ATOM 5315 CD2 PHE D 91 -9.256 -47.864 41.883 1.00 69.14 C ANISOU 5315 CD2 PHE D 91 8984 9960 7326 1583 760 1144 C ATOM 5316 CE1 PHE D 91 -10.309 -45.357 42.433 1.00 65.09 C ANISOU 5316 CE1 PHE D 91 7978 9499 7253 1152 899 1721 C ATOM 5317 CE2 PHE D 91 -9.551 -46.986 40.839 1.00 70.25 C ANISOU 5317 CE2 PHE D 91 9029 10435 7227 1657 910 1373 C ATOM 5318 CZ PHE D 91 -10.078 -45.731 41.117 1.00 68.12 C ANISOU 5318 CZ PHE D 91 8497 10174 7211 1424 968 1703 C ATOM 5319 N CYS D 92 -9.361 -51.712 45.161 1.00 69.32 N ANISOU 5319 N CYS D 92 9526 8741 8073 1164 -190 585 N ATOM 5320 CA CYS D 92 -8.865 -52.770 46.032 1.00 70.58 C ANISOU 5320 CA CYS D 92 9756 8572 8489 1149 -396 553 C ATOM 5321 C CYS D 92 -7.361 -52.929 45.868 1.00 72.28 C ANISOU 5321 C CYS D 92 9880 8817 8765 1547 -175 500 C ATOM 5322 O CYS D 92 -6.890 -53.478 44.871 1.00 75.86 O ANISOU 5322 O CYS D 92 10514 9255 9055 1950 -120 239 O ATOM 5323 CB CYS D 92 -9.561 -54.090 45.707 1.00 73.87 C ANISOU 5323 CB CYS D 92 10528 8611 8930 1110 -821 330 C ATOM 5324 SG CYS D 92 -9.059 -55.453 46.777 1.00 77.33 S ANISOU 5324 SG CYS D 92 11049 8555 9777 1060 -1147 384 S ATOM 5325 N ALA D 93 -6.610 -52.452 46.853 1.00 70.56 N ANISOU 5325 N ALA D 93 9371 8671 8769 1451 -57 740 N ATOM 5326 CA ALA D 93 -5.150 -52.478 46.784 1.00 72.43 C ANISOU 5326 CA ALA D 93 9405 8988 9128 1788 154 790 C ATOM 5327 C ALA D 93 -4.568 -53.778 47.339 1.00 75.08 C ANISOU 5327 C ALA D 93 9838 8971 9719 1935 -87 734 C ATOM 5328 O ALA D 93 -5.242 -54.506 48.080 1.00 74.69 O ANISOU 5328 O ALA D 93 9953 8621 9803 1667 -433 763 O ATOM 5329 CB ALA D 93 -4.567 -51.278 47.511 1.00 70.17 C ANISOU 5329 CB ALA D 93 8735 8932 8995 1593 331 1086 C ATOM 5330 N SER D 94 -3.315 -54.056 46.976 1.00 78.18 N ANISOU 5330 N SER D 94 10084 9416 10206 2371 101 712 N ATOM 5331 CA SER D 94 -2.623 -55.262 47.428 1.00 81.67 C ANISOU 5331 CA SER D 94 10572 9505 10953 2604 -107 678 C ATOM 5332 C SER D 94 -1.126 -55.032 47.627 1.00 83.65 C ANISOU 5332 C SER D 94 10399 9963 11423 2897 133 903 C ATOM 5333 O SER D 94 -0.432 -54.575 46.713 1.00 85.71 O ANISOU 5333 O SER D 94 10466 10559 11541 3266 518 882 O ATOM 5334 CB SER D 94 -2.850 -56.408 46.448 1.00 86.05 C ANISOU 5334 CB SER D 94 11540 9737 11418 3013 -232 237 C ATOM 5335 OG SER D 94 -2.543 -57.639 47.065 1.00 89.29 O ANISOU 5335 OG SER D 94 12067 9641 12220 3115 -571 223 O ATOM 5336 N GLY D 95 -0.639 -55.359 48.824 1.00 83.69 N ANISOU 5336 N GLY D 95 10225 9808 11766 2722 -105 1173 N ATOM 5337 CA GLY D 95 0.759 -55.136 49.184 1.00 85.78 C ANISOU 5337 CA GLY D 95 10026 10265 12302 2916 32 1461 C ATOM 5338 C GLY D 95 1.273 -56.092 50.242 1.00 88.21 C ANISOU 5338 C GLY D 95 10264 10258 12992 2908 -324 1668 C ATOM 5339 O GLY D 95 2.229 -56.838 50.013 1.00 92.84 O ANISOU 5339 O GLY D 95 10708 10720 13847 3392 -283 1678 O ATOM 5340 N GLU D 105 5.346 -51.542 45.883 1.00104.61 N ANISOU 5340 N GLU D 105 10162 14824 14761 4093 2025 2657 N ATOM 5341 CA GLU D 105 5.016 -52.328 47.071 1.00102.35 C ANISOU 5341 CA GLU D 105 10158 14037 14695 3861 1524 2487 C ATOM 5342 C GLU D 105 3.507 -52.449 47.286 1.00 97.18 C ANISOU 5342 C GLU D 105 10128 13048 13748 3503 1243 2112 C ATOM 5343 O GLU D 105 3.029 -53.473 47.772 1.00 96.84 O ANISOU 5343 O GLU D 105 10449 12603 13742 3513 928 1870 O ATOM 5344 CB GLU D 105 5.702 -51.756 48.314 1.00101.69 C ANISOU 5344 CB GLU D 105 9639 13943 15057 3404 1227 2914 C ATOM 5345 CG GLU D 105 7.229 -51.786 48.234 1.00108.11 C ANISOU 5345 CG GLU D 105 9766 15053 16259 3731 1418 3349 C ATOM 5346 CD GLU D 105 7.908 -51.323 49.511 1.00109.23 C ANISOU 5346 CD GLU D 105 9501 15155 16846 3253 1010 3749 C ATOM 5347 OE1 GLU D 105 7.340 -50.457 50.218 1.00105.79 O ANISOU 5347 OE1 GLU D 105 9198 14617 16380 2641 715 3748 O ATOM 5348 OE2 GLU D 105 9.018 -51.827 49.803 1.00113.88 O ANISOU 5348 OE2 GLU D 105 9635 15825 17811 3515 970 4048 O ATOM 5349 N GLN D 106 2.765 -51.404 46.925 1.00 93.71 N ANISOU 5349 N GLN D 106 9766 12772 13069 3187 1347 2124 N ATOM 5350 CA GLN D 106 1.306 -51.466 46.916 1.00 89.54 C ANISOU 5350 CA GLN D 106 9760 12016 12244 2917 1154 1803 C ATOM 5351 C GLN D 106 0.776 -51.323 45.488 1.00 90.59 C ANISOU 5351 C GLN D 106 10102 12381 11937 3202 1459 1599 C ATOM 5352 O GLN D 106 1.002 -50.303 44.825 1.00 91.15 O ANISOU 5352 O GLN D 106 9901 12827 11905 3198 1765 1850 O ATOM 5353 CB GLN D 106 0.709 -50.400 47.836 1.00 85.07 C ANISOU 5353 CB GLN D 106 9151 11407 11766 2303 947 1953 C ATOM 5354 CG GLN D 106 -0.728 -50.682 48.267 1.00 81.23 C ANISOU 5354 CG GLN D 106 9122 10661 11079 2001 676 1689 C ATOM 5355 CD GLN D 106 -1.115 -49.971 49.558 1.00 77.91 C ANISOU 5355 CD GLN D 106 8650 10181 10773 1491 427 1796 C ATOM 5356 OE1 GLN D 106 -2.128 -49.279 49.618 1.00 75.19 O ANISOU 5356 OE1 GLN D 106 8448 9846 10276 1230 415 1714 O ATOM 5357 NE2 GLN D 106 -0.305 -50.139 50.596 1.00 79.10 N ANISOU 5357 NE2 GLN D 106 8593 10294 11169 1379 222 1969 N ATOM 5358 N PHE D 107 0.086 -52.362 45.020 1.00 91.50 N ANISOU 5358 N PHE D 107 10696 12264 11805 3434 1331 1172 N ATOM 5359 CA PHE D 107 -0.463 -52.392 43.664 1.00 93.28 C ANISOU 5359 CA PHE D 107 11198 12707 11537 3726 1534 900 C ATOM 5360 C PHE D 107 -1.993 -52.429 43.685 1.00 89.78 C ANISOU 5360 C PHE D 107 11197 12022 10895 3348 1215 667 C ATOM 5361 O PHE D 107 -2.595 -53.168 44.471 1.00 88.40 O ANISOU 5361 O PHE D 107 11276 11408 10905 3109 823 520 O ATOM 5362 CB PHE D 107 0.123 -53.564 42.875 1.00 99.36 C ANISOU 5362 CB PHE D 107 12152 13457 12142 4413 1659 532 C ATOM 5363 CG PHE D 107 1.630 -53.603 42.882 1.00103.57 C ANISOU 5363 CG PHE D 107 12185 14259 12909 4840 1997 796 C ATOM 5364 CD1 PHE D 107 2.374 -52.518 42.416 1.00105.14 C ANISOU 5364 CD1 PHE D 107 11855 15044 13049 4892 2440 1253 C ATOM 5365 CD2 PHE D 107 2.305 -54.722 43.351 1.00106.78 C ANISOU 5365 CD2 PHE D 107 12599 14325 13647 5183 1855 651 C ATOM 5366 CE1 PHE D 107 3.770 -52.547 42.422 1.00109.42 C ANISOU 5366 CE1 PHE D 107 11846 15879 13848 5266 2752 1574 C ATOM 5367 CE2 PHE D 107 3.699 -54.763 43.358 1.00111.30 C ANISOU 5367 CE2 PHE D 107 12641 15175 14473 5604 2170 936 C ATOM 5368 CZ PHE D 107 4.432 -53.672 42.893 1.00112.54 C ANISOU 5368 CZ PHE D 107 12234 15969 14556 5639 2627 1405 C ATOM 5369 N PHE D 108 -2.609 -51.634 42.810 1.00 88.89 N ANISOU 5369 N PHE D 108 11127 12225 10424 3292 1381 701 N ATOM 5370 CA PHE D 108 -4.028 -51.295 42.915 1.00 84.95 C ANISOU 5370 CA PHE D 108 10872 11593 9813 2862 1122 643 C ATOM 5371 C PHE D 108 -4.911 -51.965 41.875 1.00 87.65 C ANISOU 5371 C PHE D 108 11671 11912 9720 3038 965 245 C ATOM 5372 O PHE D 108 -4.436 -52.413 40.833 1.00 92.51 O ANISOU 5372 O PHE D 108 12424 12743 9982 3534 1145 3 O ATOM 5373 CB PHE D 108 -4.199 -49.782 42.809 1.00 82.34 C ANISOU 5373 CB PHE D 108 10224 11573 9487 2596 1335 1034 C ATOM 5374 CG PHE D 108 -3.647 -49.026 43.976 1.00 78.95 C ANISOU 5374 CG PHE D 108 9427 11058 9512 2284 1335 1354 C ATOM 5375 CD1 PHE D 108 -2.274 -48.896 44.154 1.00 80.92 C ANISOU 5375 CD1 PHE D 108 9304 11444 9998 2462 1536 1587 C ATOM 5376 CD2 PHE D 108 -4.497 -48.432 44.892 1.00 74.40 C ANISOU 5376 CD2 PHE D 108 8865 10291 9114 1830 1123 1411 C ATOM 5377 CE1 PHE D 108 -1.758 -48.198 45.234 1.00 78.89 C ANISOU 5377 CE1 PHE D 108 8727 11093 10156 2140 1449 1852 C ATOM 5378 CE2 PHE D 108 -3.994 -47.729 45.970 1.00 72.78 C ANISOU 5378 CE2 PHE D 108 8380 10008 9265 1565 1079 1616 C ATOM 5379 CZ PHE D 108 -2.621 -47.613 46.142 1.00 75.06 C ANISOU 5379 CZ PHE D 108 8332 10394 9794 1694 1206 1828 C ATOM 5380 N GLY D 109 -6.207 -52.012 42.167 1.00 85.15 N ANISOU 5380 N GLY D 109 11572 11367 9415 2634 621 179 N ATOM 5381 CA GLY D 109 -7.198 -52.586 41.260 1.00 87.75 C ANISOU 5381 CA GLY D 109 12318 11640 9383 2681 357 -164 C ATOM 5382 C GLY D 109 -7.741 -51.586 40.254 1.00 87.97 C ANISOU 5382 C GLY D 109 12288 12133 9002 2666 529 -13 C ATOM 5383 O GLY D 109 -7.547 -50.380 40.411 1.00 85.50 O ANISOU 5383 O GLY D 109 11606 12091 8788 2525 810 403 O ATOM 5384 N PRO D 110 -8.435 -52.084 39.215 1.00 91.63 N ANISOU 5384 N PRO D 110 13127 12665 9025 2798 310 -343 N ATOM 5385 CA PRO D 110 -8.957 -51.261 38.123 1.00 93.07 C ANISOU 5385 CA PRO D 110 13292 13337 8733 2827 424 -197 C ATOM 5386 C PRO D 110 -10.097 -50.323 38.532 1.00 88.77 C ANISOU 5386 C PRO D 110 12543 12786 8401 2319 284 179 C ATOM 5387 O PRO D 110 -10.376 -49.357 37.821 1.00 89.43 O ANISOU 5387 O PRO D 110 12469 13273 8238 2316 446 475 O ATOM 5388 CB PRO D 110 -9.463 -52.299 37.116 1.00 98.79 C ANISOU 5388 CB PRO D 110 14546 14019 8970 3059 72 -752 C ATOM 5389 CG PRO D 110 -9.777 -53.499 37.937 1.00 98.56 C ANISOU 5389 CG PRO D 110 14781 13305 9362 2879 -389 -1080 C ATOM 5390 CD PRO D 110 -8.744 -53.513 39.021 1.00 95.57 C ANISOU 5390 CD PRO D 110 14108 12735 9469 2924 -124 -884 C ATOM 5391 N GLY D 111 -10.756 -50.615 39.651 1.00 85.20 N ANISOU 5391 N GLY D 111 12073 11905 8396 1925 -4 196 N ATOM 5392 CA GLY D 111 -11.806 -49.742 40.176 1.00 81.49 C ANISOU 5392 CA GLY D 111 11363 11438 8161 1508 -82 535 C ATOM 5393 C GLY D 111 -13.228 -50.205 39.919 1.00 82.64 C ANISOU 5393 C GLY D 111 11697 11470 8233 1235 -543 442 C ATOM 5394 O GLY D 111 -13.505 -50.876 38.919 1.00 86.98 O ANISOU 5394 O GLY D 111 12578 12067 8403 1372 -807 144 O ATOM 5395 N THR D 112 -14.128 -49.828 40.829 1.00 79.34 N ANISOU 5395 N THR D 112 11048 10928 8169 857 -646 695 N ATOM 5396 CA THR D 112 -15.545 -50.175 40.742 1.00 80.31 C ANISOU 5396 CA THR D 112 11212 10975 8329 537 -1070 735 C ATOM 5397 C THR D 112 -16.435 -48.946 40.912 1.00 78.13 C ANISOU 5397 C THR D 112 10559 10932 8194 359 -942 1141 C ATOM 5398 O THR D 112 -16.324 -48.216 41.898 1.00 74.88 O ANISOU 5398 O THR D 112 9861 10501 8089 287 -670 1345 O ATOM 5399 CB THR D 112 -15.910 -51.216 41.800 1.00 79.98 C ANISOU 5399 CB THR D 112 11223 10528 8638 247 -1375 679 C ATOM 5400 OG1 THR D 112 -15.234 -52.441 41.498 1.00 83.34 O ANISOU 5400 OG1 THR D 112 12035 10648 8982 428 -1596 283 O ATOM 5401 CG2 THR D 112 -17.415 -51.456 41.835 1.00 81.59 C ANISOU 5401 CG2 THR D 112 11333 10695 8971 -143 -1785 858 C ATOM 5402 N ARG D 113 -17.323 -48.730 39.948 1.00 80.48 N ANISOU 5402 N ARG D 113 10869 11443 8268 309 -1166 1233 N ATOM 5403 CA ARG D 113 -18.195 -47.562 39.969 1.00 79.35 C ANISOU 5403 CA ARG D 113 10354 11514 8283 200 -1066 1639 C ATOM 5404 C ARG D 113 -19.576 -47.922 40.509 1.00 79.52 C ANISOU 5404 C ARG D 113 10196 11445 8574 -157 -1403 1794 C ATOM 5405 O ARG D 113 -20.375 -48.574 39.833 1.00 83.11 O ANISOU 5405 O ARG D 113 10777 11917 8883 -322 -1861 1751 O ATOM 5406 CB ARG D 113 -18.276 -46.903 38.578 1.00 82.47 C ANISOU 5406 CB ARG D 113 10772 12278 8286 386 -1063 1787 C ATOM 5407 CG ARG D 113 -16.916 -46.435 38.029 1.00 83.26 C ANISOU 5407 CG ARG D 113 10944 12567 8124 737 -664 1770 C ATOM 5408 CD ARG D 113 -17.037 -45.500 36.827 1.00 87.29 C ANISOU 5408 CD ARG D 113 11347 13508 8312 891 -578 2112 C ATOM 5409 NE ARG D 113 -17.642 -44.215 37.184 1.00 86.66 N ANISOU 5409 NE ARG D 113 10846 13423 8659 780 -443 2585 N ATOM 5410 CZ ARG D 113 -18.723 -43.694 36.602 1.00 89.29 C ANISOU 5410 CZ ARG D 113 11010 13948 8970 692 -660 2908 C ATOM 5411 NH1 ARG D 113 -19.327 -44.334 35.604 1.00 93.29 N ANISOU 5411 NH1 ARG D 113 11739 14709 8998 657 -1059 2819 N ATOM 5412 NH2 ARG D 113 -19.192 -42.519 37.012 1.00 87.84 N ANISOU 5412 NH2 ARG D 113 10436 13685 9256 656 -509 3307 N ATOM 5413 N LEU D 114 -19.843 -47.495 41.739 1.00 76.16 N ANISOU 5413 N LEU D 114 9458 10952 8527 -272 -1183 1979 N ATOM 5414 CA LEU D 114 -21.105 -47.790 42.400 1.00 76.73 C ANISOU 5414 CA LEU D 114 9262 11023 8868 -582 -1399 2204 C ATOM 5415 C LEU D 114 -21.954 -46.537 42.628 1.00 76.18 C ANISOU 5415 C LEU D 114 8740 11185 9019 -537 -1171 2557 C ATOM 5416 O LEU D 114 -21.645 -45.722 43.499 1.00 73.79 O ANISOU 5416 O LEU D 114 8251 10880 8905 -398 -775 2589 O ATOM 5417 CB LEU D 114 -20.833 -48.500 43.729 1.00 75.19 C ANISOU 5417 CB LEU D 114 9062 10627 8880 -734 -1342 2146 C ATOM 5418 CG LEU D 114 -22.014 -48.887 44.623 1.00 76.74 C ANISOU 5418 CG LEU D 114 8927 10883 9347 -1059 -1488 2455 C ATOM 5419 CD1 LEU D 114 -22.632 -50.216 44.189 1.00 80.76 C ANISOU 5419 CD1 LEU D 114 9587 11199 9901 -1397 -2083 2473 C ATOM 5420 CD2 LEU D 114 -21.561 -48.952 46.068 1.00 74.40 C ANISOU 5420 CD2 LEU D 114 8532 10564 9173 -1073 -1193 2474 C ATOM 5421 N THR D 115 -23.016 -46.386 41.839 1.00 78.87 N ANISOU 5421 N THR D 115 8912 11708 9346 -636 -1454 2800 N ATOM 5422 CA THR D 115 -23.996 -45.327 42.073 1.00 79.46 C ANISOU 5422 CA THR D 115 8503 11985 9703 -583 -1290 3172 C ATOM 5423 C THR D 115 -25.144 -45.895 42.895 1.00 81.17 C ANISOU 5423 C THR D 115 8379 12279 10183 -868 -1446 3404 C ATOM 5424 O THR D 115 -25.834 -46.817 42.461 1.00 84.28 O ANISOU 5424 O THR D 115 8785 12681 10555 -1176 -1930 3503 O ATOM 5425 CB THR D 115 -24.521 -44.685 40.755 1.00 82.45 C ANISOU 5425 CB THR D 115 8792 12576 9960 -500 -1489 3422 C ATOM 5426 OG1 THR D 115 -23.494 -43.879 40.165 1.00 81.14 O ANISOU 5426 OG1 THR D 115 8803 12406 9619 -208 -1220 3357 O ATOM 5427 CG2 THR D 115 -25.734 -43.795 41.009 1.00 84.36 C ANISOU 5427 CG2 THR D 115 8480 12999 10575 -464 -1413 3850 C ATOM 5428 N VAL D 116 -25.324 -45.349 44.093 1.00 79.78 N ANISOU 5428 N VAL D 116 7894 12173 10244 -765 -1044 3490 N ATOM 5429 CA VAL D 116 -26.414 -45.758 44.968 1.00 81.90 C ANISOU 5429 CA VAL D 116 7744 12636 10737 -979 -1072 3791 C ATOM 5430 C VAL D 116 -27.457 -44.655 44.982 1.00 84.20 C ANISOU 5430 C VAL D 116 7506 13202 11285 -774 -869 4123 C ATOM 5431 O VAL D 116 -27.154 -43.512 45.325 1.00 83.02 O ANISOU 5431 O VAL D 116 7279 13037 11229 -408 -449 4017 O ATOM 5432 CB VAL D 116 -25.927 -46.066 46.391 1.00 80.00 C ANISOU 5432 CB VAL D 116 7522 12382 10493 -983 -756 3662 C ATOM 5433 CG1 VAL D 116 -27.072 -46.576 47.241 1.00 83.52 C ANISOU 5433 CG1 VAL D 116 7497 13122 11116 -1224 -777 4068 C ATOM 5434 CG2 VAL D 116 -24.821 -47.100 46.350 1.00 77.95 C ANISOU 5434 CG2 VAL D 116 7769 11810 10040 -1131 -959 3357 C ATOM 5435 N LEU D 117 -28.684 -45.022 44.615 1.00 88.09 N ANISOU 5435 N LEU D 117 7622 13909 11938 -1015 -1205 4530 N ATOM 5436 CA LEU D 117 -29.766 -44.078 44.342 1.00 91.16 C ANISOU 5436 CA LEU D 117 7473 14564 12600 -830 -1128 4915 C ATOM 5437 C LEU D 117 -30.840 -44.050 45.423 1.00 94.29 C ANISOU 5437 C LEU D 117 7240 15314 13273 -827 -873 5273 C ATOM 5438 O LEU D 117 -30.978 -44.998 46.197 1.00 94.95 O ANISOU 5438 O LEU D 117 7257 15489 13330 -1118 -913 5363 O ATOM 5439 CB LEU D 117 -30.425 -44.443 43.010 1.00 94.58 C ANISOU 5439 CB LEU D 117 7869 15059 13008 -1092 -1742 5181 C ATOM 5440 CG LEU D 117 -29.566 -44.349 41.750 1.00 93.01 C ANISOU 5440 CG LEU D 117 8210 14670 12458 -1030 -1989 4911 C ATOM 5441 CD1 LEU D 117 -29.873 -45.497 40.806 1.00 95.94 C ANISOU 5441 CD1 LEU D 117 8817 15021 12614 -1446 -2701 4912 C ATOM 5442 CD2 LEU D 117 -29.768 -43.003 41.071 1.00 94.24 C ANISOU 5442 CD2 LEU D 117 8150 14934 12722 -680 -1838 5140 C ATOM 5443 N GLU D 118 -31.610 -42.963 45.447 1.00 96.86 N ANISOU 5443 N GLU D 118 7077 15853 13874 -478 -608 5519 N ATOM 5444 CA GLU D 118 -32.767 -42.836 46.335 1.00101.28 C ANISOU 5444 CA GLU D 118 6937 16848 14697 -387 -330 5914 C ATOM 5445 C GLU D 118 -33.920 -43.759 45.919 1.00105.92 C ANISOU 5445 C GLU D 118 7069 17707 15470 -874 -844 6500 C ATOM 5446 O GLU D 118 -34.451 -44.496 46.746 1.00108.47 O ANISOU 5446 O GLU D 118 7044 18312 15857 -1125 -793 6795 O ATOM 5447 CB GLU D 118 -33.240 -41.382 46.403 1.00103.61 C ANISOU 5447 CB GLU D 118 6845 17237 15285 198 83 5974 C ATOM 5448 N ASP D 119 -34.294 -43.716 44.641 1.00108.61 N ANISOU 5448 N ASP D 119 11215 18737 11316 -2126 1679 4038 N ATOM 5449 CA ASP D 119 -35.361 -44.565 44.098 1.00108.71 C ANISOU 5449 CA ASP D 119 10783 18733 11790 -2107 1651 4401 C ATOM 5450 C ASP D 119 -35.061 -45.017 42.660 1.00104.41 C ANISOU 5450 C ASP D 119 10087 17836 11749 -2119 1241 4374 C ATOM 5451 O ASP D 119 -34.554 -44.237 41.846 1.00101.36 O ANISOU 5451 O ASP D 119 9847 17217 11447 -1965 1154 4038 O ATOM 5452 CB ASP D 119 -36.712 -43.845 44.167 1.00111.67 C ANISOU 5452 CB ASP D 119 10947 19284 12198 -1844 2140 4423 C ATOM 5453 N LEU D 120 -35.388 -46.275 42.357 1.00104.63 N ANISOU 5453 N LEU D 120 9870 17801 12085 -2328 1029 4718 N ATOM 5454 CA LEU D 120 -35.059 -46.888 41.061 1.00101.32 C ANISOU 5454 CA LEU D 120 9385 17021 12092 -2412 653 4697 C ATOM 5455 C LEU D 120 -36.034 -46.576 39.916 1.00100.98 C ANISOU 5455 C LEU D 120 9018 16961 12389 -2331 662 4633 C ATOM 5456 O LEU D 120 -35.816 -47.011 38.781 1.00 98.66 O ANISOU 5456 O LEU D 120 8693 16391 12403 -2424 361 4574 O ATOM 5457 CB LEU D 120 -34.881 -48.408 41.200 1.00102.35 C ANISOU 5457 CB LEU D 120 9516 16998 12376 -2708 461 5063 C ATOM 5458 CG LEU D 120 -33.530 -48.978 41.646 1.00101.08 C ANISOU 5458 CG LEU D 120 9663 16697 12047 -2721 258 5162 C ATOM 5459 CD1 LEU D 120 -33.495 -50.472 41.397 1.00101.85 C ANISOU 5459 CD1 LEU D 120 9796 16479 12425 -2937 129 5521 C ATOM 5460 CD2 LEU D 120 -32.372 -48.315 40.928 1.00 96.73 C ANISOU 5460 CD2 LEU D 120 9300 15955 11497 -2545 25 4810 C ATOM 5461 N LYS D 121 -37.096 -45.829 40.208 1.00103.89 N ANISOU 5461 N LYS D 121 9141 17658 12675 -2140 1019 4669 N ATOM 5462 CA LYS D 121 -38.083 -45.453 39.191 1.00104.61 C ANISOU 5462 CA LYS D 121 8835 17879 13032 -1999 1047 4689 C ATOM 5463 C LYS D 121 -37.523 -44.447 38.174 1.00101.24 C ANISOU 5463 C LYS D 121 8593 17199 12675 -1682 955 4339 C ATOM 5464 O LYS D 121 -38.104 -44.231 37.111 1.00101.16 O ANISOU 5464 O LYS D 121 8291 17254 12891 -1569 867 4357 O ATOM 5465 CB LYS D 121 -39.344 -44.898 39.860 1.00109.25 C ANISOU 5465 CB LYS D 121 9080 18937 13492 -1782 1520 4896 C ATOM 5466 N ASN D 122 -36.379 -43.859 38.500 1.00 99.11 N ANISOU 5466 N ASN D 122 8795 16677 12184 -1579 966 4039 N ATOM 5467 CA ASN D 122 -35.813 -42.765 37.721 1.00 96.81 C ANISOU 5467 CA ASN D 122 8751 16131 11901 -1290 980 3693 C ATOM 5468 C ASN D 122 -34.781 -43.221 36.667 1.00 92.45 C ANISOU 5468 C ASN D 122 8347 15216 11564 -1434 523 3537 C ATOM 5469 O ASN D 122 -34.197 -42.396 35.947 1.00 89.94 O ANISOU 5469 O ASN D 122 8248 14659 11267 -1239 504 3256 O ATOM 5470 CB ASN D 122 -35.209 -41.732 38.683 1.00 97.87 C ANISOU 5470 CB ASN D 122 9338 16222 11628 -1159 1320 3414 C ATOM 5471 CG ASN D 122 -35.798 -40.344 38.493 1.00100.57 C ANISOU 5471 CG ASN D 122 9780 16534 11898 -713 1794 3258 C ATOM 5472 OD1 ASN D 122 -35.418 -39.613 37.575 1.00 99.93 O ANISOU 5472 OD1 ASN D 122 9873 16171 11926 -509 1775 3035 O ATOM 5473 ND2 ASN D 122 -36.735 -39.975 39.363 1.00105.25 N ANISOU 5473 ND2 ASN D 122 10289 17397 12303 -524 2272 3403 N ATOM 5474 N VAL D 123 -34.591 -44.538 36.569 1.00 91.90 N ANISOU 5474 N VAL D 123 8186 15077 11655 -1763 211 3734 N ATOM 5475 CA VAL D 123 -33.548 -45.133 35.726 1.00 88.53 C ANISOU 5475 CA VAL D 123 7947 14283 11406 -1889 -162 3626 C ATOM 5476 C VAL D 123 -34.014 -45.336 34.283 1.00 87.49 C ANISOU 5476 C VAL D 123 7632 14027 11585 -1907 -369 3598 C ATOM 5477 O VAL D 123 -35.067 -45.927 34.039 1.00 89.88 O ANISOU 5477 O VAL D 123 7604 14519 12027 -2094 -398 3812 O ATOM 5478 CB VAL D 123 -33.038 -46.479 36.321 1.00 89.33 C ANISOU 5478 CB VAL D 123 8135 14292 11513 -2178 -325 3875 C ATOM 5479 CG1 VAL D 123 -31.977 -47.116 35.433 1.00 86.50 C ANISOU 5479 CG1 VAL D 123 7988 13530 11349 -2230 -632 3800 C ATOM 5480 CG2 VAL D 123 -32.485 -46.270 37.720 1.00 90.67 C ANISOU 5480 CG2 VAL D 123 8472 14670 11308 -2163 -171 3925 C ATOM 5481 N PHE D 124 -33.211 -44.843 33.341 1.00 84.35 N ANISOU 5481 N PHE D 124 7443 13351 11257 -1755 -514 3335 N ATOM 5482 CA PHE D 124 -33.484 -44.977 31.912 1.00 83.41 C ANISOU 5482 CA PHE D 124 7216 13110 11367 -1767 -730 3274 C ATOM 5483 C PHE D 124 -32.266 -45.468 31.126 1.00 80.40 C ANISOU 5483 C PHE D 124 7148 12297 11102 -1840 -995 3107 C ATOM 5484 O PHE D 124 -31.137 -45.057 31.408 1.00 78.41 O ANISOU 5484 O PHE D 124 7164 11884 10743 -1712 -975 2951 O ATOM 5485 CB PHE D 124 -33.940 -43.641 31.334 1.00 83.35 C ANISOU 5485 CB PHE D 124 7116 13233 11319 -1385 -556 3149 C ATOM 5486 CG PHE D 124 -35.325 -43.248 31.737 1.00 87.63 C ANISOU 5486 CG PHE D 124 7257 14230 11810 -1244 -297 3381 C ATOM 5487 CD1 PHE D 124 -36.425 -43.674 30.997 1.00 90.66 C ANISOU 5487 CD1 PHE D 124 7184 14936 12328 -1364 -439 3597 C ATOM 5488 CD2 PHE D 124 -35.535 -42.443 32.853 1.00 89.65 C ANISOU 5488 CD2 PHE D 124 7578 14634 11852 -1003 109 3391 C ATOM 5489 CE1 PHE D 124 -37.717 -43.308 31.363 1.00 95.17 C ANISOU 5489 CE1 PHE D 124 7287 16025 12849 -1200 -187 3874 C ATOM 5490 CE2 PHE D 124 -36.820 -42.068 33.229 1.00 94.17 C ANISOU 5490 CE2 PHE D 124 7766 15636 12380 -800 415 3641 C ATOM 5491 CZ PHE D 124 -37.916 -42.506 32.483 1.00 96.96 C ANISOU 5491 CZ PHE D 124 7580 16363 12897 -875 263 3912 C ATOM 5492 N PRO D 125 -32.493 -46.352 30.137 1.00 80.74 N ANISOU 5492 N PRO D 125 7159 12179 11340 -2073 -1225 3138 N ATOM 5493 CA PRO D 125 -31.447 -46.750 29.198 1.00 78.42 C ANISOU 5493 CA PRO D 125 7176 11460 11161 -2085 -1420 2968 C ATOM 5494 C PRO D 125 -31.267 -45.666 28.130 1.00 76.37 C ANISOU 5494 C PRO D 125 6951 11171 10897 -1807 -1450 2727 C ATOM 5495 O PRO D 125 -32.129 -44.795 28.013 1.00 77.58 O ANISOU 5495 O PRO D 125 6862 11627 10987 -1631 -1337 2745 O ATOM 5496 CB PRO D 125 -32.015 -48.026 28.580 1.00 80.83 C ANISOU 5496 CB PRO D 125 7466 11625 11620 -2489 -1580 3069 C ATOM 5497 CG PRO D 125 -33.485 -47.842 28.631 1.00 83.84 C ANISOU 5497 CG PRO D 125 7410 12476 11969 -2642 -1548 3209 C ATOM 5498 CD PRO D 125 -33.761 -47.061 29.881 1.00 84.17 C ANISOU 5498 CD PRO D 125 7273 12845 11864 -2394 -1289 3330 C ATOM 5499 N PRO D 126 -30.163 -45.706 27.355 1.00 73.96 N ANISOU 5499 N PRO D 126 6939 10509 10653 -1727 -1562 2542 N ATOM 5500 CA PRO D 126 -29.944 -44.634 26.382 1.00 72.25 C ANISOU 5500 CA PRO D 126 6787 10249 10414 -1458 -1553 2333 C ATOM 5501 C PRO D 126 -30.545 -44.883 24.991 1.00 73.24 C ANISOU 5501 C PRO D 126 6845 10371 10611 -1547 -1743 2294 C ATOM 5502 O PRO D 126 -30.807 -46.025 24.615 1.00 74.83 O ANISOU 5502 O PRO D 126 7070 10472 10891 -1886 -1909 2343 O ATOM 5503 CB PRO D 126 -28.417 -44.554 26.298 1.00 69.60 C ANISOU 5503 CB PRO D 126 6769 9593 10083 -1355 -1562 2175 C ATOM 5504 CG PRO D 126 -27.941 -45.932 26.616 1.00 70.21 C ANISOU 5504 CG PRO D 126 6952 9472 10254 -1567 -1663 2321 C ATOM 5505 CD PRO D 126 -29.020 -46.637 27.404 1.00 73.16 C ANISOU 5505 CD PRO D 126 7120 10050 10628 -1810 -1642 2555 C ATOM 5506 N GLU D 127 -30.767 -43.805 24.246 1.00 73.01 N ANISOU 5506 N GLU D 127 6765 10453 10522 -1261 -1695 2210 N ATOM 5507 CA GLU D 127 -31.135 -43.898 22.840 1.00 74.28 C ANISOU 5507 CA GLU D 127 6893 10649 10682 -1303 -1892 2161 C ATOM 5508 C GLU D 127 -29.928 -43.478 21.996 1.00 71.61 C ANISOU 5508 C GLU D 127 6928 9924 10355 -1105 -1892 1930 C ATOM 5509 O GLU D 127 -29.478 -42.329 22.056 1.00 70.20 O ANISOU 5509 O GLU D 127 6853 9691 10128 -770 -1694 1849 O ATOM 5510 CB GLU D 127 -32.350 -43.019 22.533 1.00 76.89 C ANISOU 5510 CB GLU D 127 6838 11466 10910 -1070 -1834 2329 C ATOM 5511 CG GLU D 127 -33.637 -43.447 23.235 1.00 80.93 C ANISOU 5511 CG GLU D 127 6889 12456 11404 -1274 -1834 2597 C ATOM 5512 CD GLU D 127 -34.785 -42.475 23.000 1.00 84.77 C ANISOU 5512 CD GLU D 127 6935 13487 11787 -919 -1714 2837 C ATOM 5513 OE1 GLU D 127 -35.837 -42.910 22.484 1.00 88.80 O ANISOU 5513 OE1 GLU D 127 7012 14490 12239 -1148 -1922 3031 O ATOM 5514 OE2 GLU D 127 -34.635 -41.274 23.324 1.00 84.45 O ANISOU 5514 OE2 GLU D 127 6988 13395 11706 -417 -1390 2845 O ATOM 5515 N VAL D 128 -29.402 -44.426 21.226 1.00 71.51 N ANISOU 5515 N VAL D 128 7151 9618 10400 -1332 -2068 1820 N ATOM 5516 CA VAL D 128 -28.175 -44.227 20.457 1.00 69.13 C ANISOU 5516 CA VAL D 128 7202 8940 10123 -1168 -2047 1623 C ATOM 5517 C VAL D 128 -28.510 -43.892 19.015 1.00 70.02 C ANISOU 5517 C VAL D 128 7355 9115 10136 -1107 -2168 1538 C ATOM 5518 O VAL D 128 -29.215 -44.652 18.348 1.00 72.82 O ANISOU 5518 O VAL D 128 7657 9583 10428 -1412 -2372 1547 O ATOM 5519 CB VAL D 128 -27.293 -45.497 20.471 1.00 69.04 C ANISOU 5519 CB VAL D 128 7480 8526 10225 -1373 -2091 1579 C ATOM 5520 CG1 VAL D 128 -26.086 -45.329 19.557 1.00 67.36 C ANISOU 5520 CG1 VAL D 128 7587 7973 10032 -1181 -2047 1403 C ATOM 5521 CG2 VAL D 128 -26.855 -45.836 21.892 1.00 68.52 C ANISOU 5521 CG2 VAL D 128 7365 8447 10223 -1385 -1980 1722 C ATOM 5522 N ALA D 129 -27.997 -42.758 18.540 1.00 68.28 N ANISOU 5522 N ALA D 129 7247 8831 9866 -754 -2034 1457 N ATOM 5523 CA ALA D 129 -28.209 -42.318 17.160 1.00 68.94 C ANISOU 5523 CA ALA D 129 7394 8979 9820 -624 -2118 1411 C ATOM 5524 C ALA D 129 -26.890 -41.976 16.470 1.00 66.48 C ANISOU 5524 C ALA D 129 7463 8266 9530 -446 -2006 1219 C ATOM 5525 O ALA D 129 -26.064 -41.248 17.020 1.00 64.50 O ANISOU 5525 O ALA D 129 7317 7848 9342 -254 -1784 1165 O ATOM 5526 CB ALA D 129 -29.160 -41.131 17.122 1.00 70.40 C ANISOU 5526 CB ALA D 129 7298 9557 9893 -294 -2012 1596 C ATOM 5527 N VAL D 130 -26.696 -42.520 15.271 1.00 67.19 N ANISOU 5527 N VAL D 130 7764 8224 9540 -558 -2149 1107 N ATOM 5528 CA VAL D 130 -25.529 -42.205 14.446 1.00 65.43 C ANISOU 5528 CA VAL D 130 7885 7662 9313 -376 -2028 947 C ATOM 5529 C VAL D 130 -25.889 -41.137 13.414 1.00 66.35 C ANISOU 5529 C VAL D 130 8012 7952 9245 -99 -1999 987 C ATOM 5530 O VAL D 130 -26.893 -41.255 12.710 1.00 69.26 O ANISOU 5530 O VAL D 130 8233 8657 9426 -174 -2203 1076 O ATOM 5531 CB VAL D 130 -24.982 -43.466 13.726 1.00 66.27 C ANISOU 5531 CB VAL D 130 8309 7449 9421 -619 -2120 794 C ATOM 5532 CG1 VAL D 130 -23.904 -43.093 12.707 1.00 65.15 C ANISOU 5532 CG1 VAL D 130 8494 7024 9236 -399 -1977 653 C ATOM 5533 CG2 VAL D 130 -24.437 -44.455 14.728 1.00 65.32 C ANISOU 5533 CG2 VAL D 130 8234 7086 9497 -771 -2063 816 C ATOM 5534 N PHE D 131 -25.074 -40.094 13.324 1.00 64.56 N ANISOU 5534 N PHE D 131 7952 7530 9049 200 -1741 945 N ATOM 5535 CA PHE D 131 -25.283 -39.066 12.315 1.00 65.77 C ANISOU 5535 CA PHE D 131 8194 7764 9033 509 -1648 1012 C ATOM 5536 C PHE D 131 -24.235 -39.184 11.219 1.00 65.68 C ANISOU 5536 C PHE D 131 8543 7443 8969 535 -1596 846 C ATOM 5537 O PHE D 131 -23.082 -39.541 11.481 1.00 64.03 O ANISOU 5537 O PHE D 131 8505 6914 8909 452 -1482 699 O ATOM 5538 CB PHE D 131 -25.289 -37.685 12.954 1.00 65.08 C ANISOU 5538 CB PHE D 131 8093 7648 8987 831 -1316 1106 C ATOM 5539 CG PHE D 131 -26.396 -37.498 13.937 1.00 65.59 C ANISOU 5539 CG PHE D 131 7825 8029 9067 878 -1307 1290 C ATOM 5540 CD1 PHE D 131 -26.266 -37.944 15.243 1.00 63.65 C ANISOU 5540 CD1 PHE D 131 7465 7756 8963 656 -1294 1235 C ATOM 5541 CD2 PHE D 131 -27.583 -36.899 13.554 1.00 68.07 C ANISOU 5541 CD2 PHE D 131 7912 8719 9234 1173 -1301 1561 C ATOM 5542 CE1 PHE D 131 -27.300 -37.786 16.151 1.00 64.69 C ANISOU 5542 CE1 PHE D 131 7297 8187 9094 705 -1253 1410 C ATOM 5543 CE2 PHE D 131 -28.617 -36.736 14.457 1.00 69.23 C ANISOU 5543 CE2 PHE D 131 7717 9190 9398 1259 -1249 1765 C ATOM 5544 CZ PHE D 131 -28.475 -37.180 15.756 1.00 67.36 C ANISOU 5544 CZ PHE D 131 7405 8880 9308 1012 -1215 1670 C ATOM 5545 N GLU D 132 -24.645 -38.903 9.988 1.00 68.12 N ANISOU 5545 N GLU D 132 8938 7903 9042 666 -1674 904 N ATOM 5546 CA GLU D 132 -23.817 -39.189 8.826 1.00 68.77 C ANISOU 5546 CA GLU D 132 9375 7742 9014 654 -1652 747 C ATOM 5547 C GLU D 132 -23.062 -37.947 8.375 1.00 68.25 C ANISOU 5547 C GLU D 132 9528 7469 8936 1000 -1322 774 C ATOM 5548 O GLU D 132 -23.574 -36.840 8.512 1.00 69.06 O ANISOU 5548 O GLU D 132 9544 7699 8995 1285 -1168 960 O ATOM 5549 CB GLU D 132 -24.674 -39.776 7.700 1.00 72.41 C ANISOU 5549 CB GLU D 132 9845 8517 9152 491 -1960 761 C ATOM 5550 CG GLU D 132 -25.270 -41.148 8.050 1.00 74.72 C ANISOU 5550 CG GLU D 132 10028 8917 9444 16 -2248 667 C ATOM 5551 CD GLU D 132 -26.263 -41.652 7.020 1.00 80.39 C ANISOU 5551 CD GLU D 132 10708 10056 9780 -266 -2580 671 C ATOM 5552 OE1 GLU D 132 -25.824 -42.184 5.975 1.00 82.57 O ANISOU 5552 OE1 GLU D 132 11371 10155 9845 -426 -2613 466 O ATOM 5553 OE2 GLU D 132 -27.484 -41.528 7.264 1.00 83.18 O ANISOU 5553 OE2 GLU D 132 10631 10956 10016 -351 -2802 882 O ATOM 5554 N PRO D 133 -21.837 -38.128 7.837 1.00 67.58 N ANISOU 5554 N PRO D 133 9744 7043 8891 986 -1164 606 N ATOM 5555 CA PRO D 133 -20.969 -37.003 7.474 1.00 67.28 C ANISOU 5555 CA PRO D 133 9924 6772 8866 1229 -813 612 C ATOM 5556 C PRO D 133 -21.602 -36.128 6.406 1.00 70.11 C ANISOU 5556 C PRO D 133 10401 7286 8951 1531 -764 792 C ATOM 5557 O PRO D 133 -22.418 -36.610 5.621 1.00 72.49 O ANISOU 5557 O PRO D 133 10659 7887 8996 1508 -1044 860 O ATOM 5558 CB PRO D 133 -19.718 -37.684 6.908 1.00 66.83 C ANISOU 5558 CB PRO D 133 10105 6433 8854 1132 -721 431 C ATOM 5559 CG PRO D 133 -19.798 -39.115 7.340 1.00 66.34 C ANISOU 5559 CG PRO D 133 9958 6366 8883 869 -953 333 C ATOM 5560 CD PRO D 133 -21.243 -39.424 7.455 1.00 67.67 C ANISOU 5560 CD PRO D 133 9934 6862 8914 751 -1267 420 C ATOM 5561 N SER D 134 -21.231 -34.852 6.380 1.00 70.67 N ANISOU 5561 N SER D 134 10633 7171 9049 1789 -399 882 N ATOM 5562 CA SER D 134 -21.812 -33.915 5.422 1.00 73.84 C ANISOU 5562 CA SER D 134 11171 7690 9196 2166 -280 1130 C ATOM 5563 C SER D 134 -20.960 -33.813 4.170 1.00 74.82 C ANISOU 5563 C SER D 134 11647 7622 9159 2234 -138 1071 C ATOM 5564 O SER D 134 -19.726 -33.767 4.241 1.00 73.04 O ANISOU 5564 O SER D 134 11607 7048 9095 2105 105 887 O ATOM 5565 CB SER D 134 -21.975 -32.533 6.044 1.00 74.63 C ANISOU 5565 CB SER D 134 11348 7616 9393 2452 128 1294 C ATOM 5566 OG SER D 134 -20.710 -31.984 6.362 1.00 73.80 O ANISOU 5566 OG SER D 134 11514 7060 9466 2316 502 1102 O ATOM 5567 N GLU D 135 -21.637 -33.759 3.026 1.00 78.16 N ANISOU 5567 N GLU D 135 12128 8338 9233 2436 -289 1256 N ATOM 5568 CA GLU D 135 -20.972 -33.655 1.729 1.00 80.02 C ANISOU 5568 CA GLU D 135 12719 8452 9234 2529 -162 1232 C ATOM 5569 C GLU D 135 -19.958 -32.514 1.699 1.00 79.38 C ANISOU 5569 C GLU D 135 12943 7917 9299 2709 370 1257 C ATOM 5570 O GLU D 135 -18.997 -32.561 0.932 1.00 79.79 O ANISOU 5570 O GLU D 135 13275 7751 9290 2674 553 1148 O ATOM 5571 CB GLU D 135 -21.996 -33.514 0.587 1.00 84.55 C ANISOU 5571 CB GLU D 135 13277 9506 9343 2767 -389 1510 C ATOM 5572 CG GLU D 135 -22.887 -34.755 0.359 1.00 87.33 C ANISOU 5572 CG GLU D 135 13381 10350 9451 2436 -936 1426 C ATOM 5573 CD GLU D 135 -22.106 -36.084 0.301 1.00 87.11 C ANISOU 5573 CD GLU D 135 13541 10057 9498 1979 -1053 1004 C ATOM 5574 OE1 GLU D 135 -21.121 -36.184 -0.474 1.00 87.27 O ANISOU 5574 OE1 GLU D 135 13942 9776 9440 1989 -841 849 O ATOM 5575 OE2 GLU D 135 -22.491 -37.032 1.031 1.00 86.23 O ANISOU 5575 OE2 GLU D 135 13213 10026 9523 1638 -1315 855 O ATOM 5576 N ALA D 136 -20.184 -31.504 2.542 1.00 78.83 N ANISOU 5576 N ALA D 136 12844 7697 9409 2869 648 1390 N ATOM 5577 CA ALA D 136 -19.260 -30.388 2.719 1.00 78.39 C ANISOU 5577 CA ALA D 136 13108 7169 9509 2916 1189 1368 C ATOM 5578 C ALA D 136 -17.939 -30.850 3.337 1.00 75.11 C ANISOU 5578 C ALA D 136 12668 6505 9366 2476 1272 1030 C ATOM 5579 O ALA D 136 -16.867 -30.563 2.802 1.00 75.59 O ANISOU 5579 O ALA D 136 12963 6320 9436 2400 1558 952 O ATOM 5580 CB ALA D 136 -19.897 -29.309 3.568 1.00 79.58 C ANISOU 5580 CB ALA D 136 13287 7188 9761 3137 1484 1544 C ATOM 5581 N GLU D 137 -18.020 -31.575 4.451 1.00 72.13 N ANISOU 5581 N GLU D 137 11972 6245 9190 2201 1027 870 N ATOM 5582 CA GLU D 137 -16.829 -32.093 5.119 1.00 69.56 C ANISOU 5582 CA GLU D 137 11528 5804 9096 1825 1060 623 C ATOM 5583 C GLU D 137 -16.073 -33.042 4.191 1.00 69.04 C ANISOU 5583 C GLU D 137 11512 5753 8968 1780 961 531 C ATOM 5584 O GLU D 137 -14.843 -33.105 4.229 1.00 68.76 O ANISOU 5584 O GLU D 137 11479 5587 9060 1612 1166 422 O ATOM 5585 CB GLU D 137 -17.184 -32.802 6.438 1.00 67.47 C ANISOU 5585 CB GLU D 137 10907 5719 9008 1598 781 533 C ATOM 5586 CG GLU D 137 -16.004 -32.887 7.429 1.00 66.81 C ANISOU 5586 CG GLU D 137 10675 5567 9142 1238 903 358 C ATOM 5587 CD GLU D 137 -15.986 -34.147 8.311 1.00 65.68 C ANISOU 5587 CD GLU D 137 10178 5641 9137 1042 561 292 C ATOM 5588 OE1 GLU D 137 -17.040 -34.797 8.496 1.00 66.17 O ANISOU 5588 OE1 GLU D 137 10111 5863 9167 1109 260 351 O ATOM 5589 OE2 GLU D 137 -14.898 -34.484 8.829 1.00 64.65 O ANISOU 5589 OE2 GLU D 137 9879 5547 9138 816 610 214 O ATOM 5590 N ILE D 138 -16.812 -33.780 3.365 1.00 69.27 N ANISOU 5590 N ILE D 138 11576 5967 8776 1913 666 578 N ATOM 5591 CA ILE D 138 -16.198 -34.666 2.388 1.00 69.47 C ANISOU 5591 CA ILE D 138 11762 5954 8679 1891 626 469 C ATOM 5592 C ILE D 138 -15.461 -33.824 1.349 1.00 71.27 C ANISOU 5592 C ILE D 138 12315 5996 8768 2063 1008 535 C ATOM 5593 O ILE D 138 -14.239 -33.896 1.234 1.00 70.98 O ANISOU 5593 O ILE D 138 12324 5788 8856 1973 1271 444 O ATOM 5594 CB ILE D 138 -17.239 -35.608 1.735 1.00 70.75 C ANISOU 5594 CB ILE D 138 11953 6368 8562 1893 227 460 C ATOM 5595 CG1 ILE D 138 -17.535 -36.796 2.650 1.00 68.75 C ANISOU 5595 CG1 ILE D 138 11450 6187 8483 1632 -73 330 C ATOM 5596 CG2 ILE D 138 -16.742 -36.147 0.406 1.00 73.29 C ANISOU 5596 CG2 ILE D 138 12615 6614 8616 1933 290 364 C ATOM 5597 CD1 ILE D 138 -18.784 -36.657 3.465 1.00 67.79 C ANISOU 5597 CD1 ILE D 138 11030 6341 8385 1590 -342 448 C ATOM 5598 N SER D 139 -16.220 -33.000 0.635 1.00 73.55 N ANISOU 5598 N SER D 139 12795 6355 8796 2328 1056 740 N ATOM 5599 CA SER D 139 -15.709 -32.118 -0.415 1.00 76.00 C ANISOU 5599 CA SER D 139 13459 6493 8923 2538 1430 867 C ATOM 5600 C SER D 139 -14.467 -31.327 -0.008 1.00 75.56 C ANISOU 5600 C SER D 139 13478 6104 9126 2391 1903 809 C ATOM 5601 O SER D 139 -13.480 -31.295 -0.747 1.00 76.96 O ANISOU 5601 O SER D 139 13838 6146 9259 2375 2174 773 O ATOM 5602 CB SER D 139 -16.811 -31.150 -0.866 1.00 78.57 C ANISOU 5602 CB SER D 139 13914 6947 8993 2901 1456 1188 C ATOM 5603 OG SER D 139 -16.373 -30.335 -1.934 1.00 81.51 O ANISOU 5603 OG SER D 139 14664 7152 9153 3136 1825 1355 O ATOM 5604 N HIS D 140 -14.517 -30.709 1.168 1.00 74.11 N ANISOU 5604 N HIS D 140 13154 5819 9187 2241 2011 789 N ATOM 5605 CA HIS D 140 -13.506 -29.738 1.569 1.00 74.84 C ANISOU 5605 CA HIS D 140 13363 5619 9453 2020 2477 736 C ATOM 5606 C HIS D 140 -12.258 -30.317 2.242 1.00 73.39 C ANISOU 5606 C HIS D 140 12879 5493 9514 1615 2492 524 C ATOM 5607 O HIS D 140 -11.136 -29.959 1.896 1.00 74.98 O ANISOU 5607 O HIS D 140 13150 5584 9754 1454 2830 496 O ATOM 5608 CB HIS D 140 -14.142 -28.671 2.454 1.00 75.43 C ANISOU 5608 CB HIS D 140 13534 5522 9604 2023 2667 801 C ATOM 5609 CG HIS D 140 -13.184 -27.625 2.919 1.00 76.95 C ANISOU 5609 CG HIS D 140 13925 5383 9931 1687 3168 698 C ATOM 5610 ND1 HIS D 140 -12.974 -27.352 4.252 1.00 76.35 N ANISOU 5610 ND1 HIS D 140 13710 5267 10034 1292 3224 513 N ATOM 5611 CD2 HIS D 140 -12.370 -26.793 2.231 1.00 79.72 C ANISOU 5611 CD2 HIS D 140 14616 5442 10231 1618 3643 739 C ATOM 5612 CE1 HIS D 140 -12.081 -26.386 4.366 1.00 78.64 C ANISOU 5612 CE1 HIS D 140 14254 5264 10363 948 3702 421 C ATOM 5613 NE2 HIS D 140 -11.696 -26.032 3.155 1.00 81.11 N ANISOU 5613 NE2 HIS D 140 14855 5405 10558 1137 3974 562 N ATOM 5614 N THR D 141 -12.454 -31.210 3.201 1.00 71.12 N ANISOU 5614 N THR D 141 12225 5421 9376 1464 2139 418 N ATOM 5615 CA THR D 141 -11.344 -31.744 3.989 1.00 70.33 C ANISOU 5615 CA THR D 141 11769 5462 9493 1129 2132 293 C ATOM 5616 C THR D 141 -10.735 -33.017 3.408 1.00 70.19 C ANISOU 5616 C THR D 141 11613 5570 9486 1242 2008 283 C ATOM 5617 O THR D 141 -9.545 -33.271 3.592 1.00 71.05 O ANISOU 5617 O THR D 141 11483 5785 9726 1085 2163 271 O ATOM 5618 CB THR D 141 -11.779 -32.035 5.436 1.00 68.31 C ANISOU 5618 CB THR D 141 11193 5378 9384 917 1863 221 C ATOM 5619 OG1 THR D 141 -12.637 -33.185 5.459 1.00 66.14 O ANISOU 5619 OG1 THR D 141 10794 5247 9091 1103 1452 243 O ATOM 5620 CG2 THR D 141 -12.506 -30.824 6.033 1.00 69.09 C ANISOU 5620 CG2 THR D 141 11496 5307 9449 856 2031 220 C ATOM 5621 N GLN D 142 -11.555 -33.800 2.707 1.00 69.84 N ANISOU 5621 N GLN D 142 11725 5529 9281 1504 1756 296 N ATOM 5622 CA GLN D 142 -11.200 -35.160 2.271 1.00 70.29 C ANISOU 5622 CA GLN D 142 11749 5627 9331 1606 1636 245 C ATOM 5623 C GLN D 142 -11.176 -36.123 3.465 1.00 68.63 C ANISOU 5623 C GLN D 142 11168 5562 9347 1468 1383 212 C ATOM 5624 O GLN D 142 -10.350 -37.041 3.544 1.00 69.14 O ANISOU 5624 O GLN D 142 11085 5655 9530 1511 1445 223 O ATOM 5625 CB GLN D 142 -9.881 -35.192 1.481 1.00 72.60 C ANISOU 5625 CB GLN D 142 12110 5851 9622 1676 2015 267 C ATOM 5626 CG GLN D 142 -9.873 -34.318 0.230 1.00 74.72 C ANISOU 5626 CG GLN D 142 12784 5966 9639 1827 2293 322 C ATOM 5627 CD GLN D 142 -10.989 -34.668 -0.735 1.00 75.49 C ANISOU 5627 CD GLN D 142 13240 6041 9401 2049 2065 311 C ATOM 5628 OE1 GLN D 142 -11.116 -35.816 -1.177 1.00 75.69 O ANISOU 5628 OE1 GLN D 142 13375 6070 9312 2122 1913 211 O ATOM 5629 NE2 GLN D 142 -11.810 -33.677 -1.065 1.00 76.25 N ANISOU 5629 NE2 GLN D 142 13535 6127 9311 2148 2060 428 N ATOM 5630 N LYS D 143 -12.116 -35.895 4.380 1.00 67.04 N ANISOU 5630 N LYS D 143 10832 5451 9191 1351 1132 209 N ATOM 5631 CA LYS D 143 -12.284 -36.687 5.594 1.00 65.65 C ANISOU 5631 CA LYS D 143 10325 5425 9195 1211 878 204 C ATOM 5632 C LYS D 143 -13.774 -36.777 5.950 1.00 64.49 C ANISOU 5632 C LYS D 143 10198 5336 8968 1204 555 199 C ATOM 5633 O LYS D 143 -14.555 -35.877 5.621 1.00 64.68 O ANISOU 5633 O LYS D 143 10380 5347 8850 1284 572 238 O ATOM 5634 CB LYS D 143 -11.519 -36.036 6.750 1.00 65.43 C ANISOU 5634 CB LYS D 143 9968 5558 9335 949 1000 223 C ATOM 5635 CG LYS D 143 -10.011 -36.072 6.615 1.00 67.43 C ANISOU 5635 CG LYS D 143 10031 5910 9680 893 1270 274 C ATOM 5636 CD LYS D 143 -9.368 -34.842 7.227 1.00 68.83 C ANISOU 5636 CD LYS D 143 10063 6207 9881 544 1484 244 C ATOM 5637 CE LYS D 143 -7.878 -35.058 7.455 1.00 72.04 C ANISOU 5637 CE LYS D 143 10069 6914 10388 396 1653 339 C ATOM 5638 NZ LYS D 143 -7.127 -35.451 6.216 1.00 74.82 N ANISOU 5638 NZ LYS D 143 10530 7172 10726 679 1905 421 N ATOM 5639 N ALA D 144 -14.160 -37.855 6.631 1.00 63.74 N ANISOU 5639 N ALA D 144 9930 5322 8968 1129 293 193 N ATOM 5640 CA ALA D 144 -15.551 -38.054 7.051 1.00 63.07 C ANISOU 5640 CA ALA D 144 9788 5353 8821 1075 -16 207 C ATOM 5641 C ALA D 144 -15.669 -38.293 8.554 1.00 61.61 C ANISOU 5641 C ALA D 144 9267 5317 8826 897 -146 244 C ATOM 5642 O ALA D 144 -15.076 -39.240 9.078 1.00 61.58 O ANISOU 5642 O ALA D 144 9115 5319 8963 842 -182 267 O ATOM 5643 CB ALA D 144 -16.170 -39.214 6.284 1.00 64.23 C ANISOU 5643 CB ALA D 144 10130 5452 8823 1084 -229 149 C ATOM 5644 N THR D 145 -16.429 -37.434 9.237 1.00 60.94 N ANISOU 5644 N THR D 145 9081 5349 8724 847 -177 277 N ATOM 5645 CA THR D 145 -16.711 -37.600 10.671 1.00 60.02 C ANISOU 5645 CA THR D 145 8678 5398 8727 671 -299 306 C ATOM 5646 C THR D 145 -18.128 -38.139 10.879 1.00 59.76 C ANISOU 5646 C THR D 145 8567 5497 8643 669 -582 364 C ATOM 5647 O THR D 145 -19.070 -37.649 10.263 1.00 60.89 O ANISOU 5647 O THR D 145 8801 5697 8637 803 -623 413 O ATOM 5648 CB THR D 145 -16.559 -36.273 11.469 1.00 60.12 C ANISOU 5648 CB THR D 145 8660 5443 8741 568 -78 276 C ATOM 5649 OG1 THR D 145 -15.322 -35.626 11.137 1.00 61.39 O ANISOU 5649 OG1 THR D 145 8913 5503 8911 496 204 212 O ATOM 5650 CG2 THR D 145 -16.604 -36.533 12.974 1.00 59.37 C ANISOU 5650 CG2 THR D 145 8283 5550 8725 344 -185 283 C ATOM 5651 N LEU D 146 -18.272 -39.138 11.746 1.00 58.91 N ANISOU 5651 N LEU D 146 8264 5477 8644 520 -763 397 N ATOM 5652 CA LEU D 146 -19.576 -39.712 12.063 1.00 59.02 C ANISOU 5652 CA LEU D 146 8160 5643 8622 438 -1017 460 C ATOM 5653 C LEU D 146 -19.901 -39.466 13.527 1.00 58.24 C ANISOU 5653 C LEU D 146 7798 5726 8604 325 -1030 527 C ATOM 5654 O LEU D 146 -19.251 -40.025 14.407 1.00 58.08 O ANISOU 5654 O LEU D 146 7645 5727 8697 205 -1039 553 O ATOM 5655 CB LEU D 146 -19.575 -41.218 11.814 1.00 59.87 C ANISOU 5655 CB LEU D 146 8343 5637 8766 316 -1180 443 C ATOM 5656 CG LEU D 146 -19.515 -41.784 10.403 1.00 61.49 C ANISOU 5656 CG LEU D 146 8874 5658 8833 345 -1199 339 C ATOM 5657 CD1 LEU D 146 -18.162 -41.551 9.781 1.00 61.97 C ANISOU 5657 CD1 LEU D 146 9118 5502 8927 526 -935 284 C ATOM 5658 CD2 LEU D 146 -19.796 -43.267 10.470 1.00 62.78 C ANISOU 5658 CD2 LEU D 146 9150 5677 9025 140 -1329 308 C ATOM 5659 N VAL D 147 -20.903 -38.635 13.794 1.00 58.45 N ANISOU 5659 N VAL D 147 7750 5908 8551 397 -1008 584 N ATOM 5660 CA VAL D 147 -21.277 -38.316 15.171 1.00 57.95 C ANISOU 5660 CA VAL D 147 7489 6004 8525 306 -965 630 C ATOM 5661 C VAL D 147 -22.143 -39.423 15.764 1.00 58.36 C ANISOU 5661 C VAL D 147 7317 6240 8619 154 -1220 736 C ATOM 5662 O VAL D 147 -22.988 -39.996 15.076 1.00 59.53 O ANISOU 5662 O VAL D 147 7437 6469 8713 137 -1412 790 O ATOM 5663 CB VAL D 147 -22.011 -36.957 15.257 1.00 58.83 C ANISOU 5663 CB VAL D 147 7657 6159 8537 507 -740 672 C ATOM 5664 CG1 VAL D 147 -22.742 -36.809 16.575 1.00 59.10 C ANISOU 5664 CG1 VAL D 147 7499 6384 8572 442 -705 737 C ATOM 5665 CG2 VAL D 147 -21.032 -35.816 15.075 1.00 58.95 C ANISOU 5665 CG2 VAL D 147 7939 5935 8525 549 -406 545 C ATOM 5666 N CYS D 148 -21.906 -39.732 17.035 1.00 57.93 N ANISOU 5666 N CYS D 148 7106 6275 8630 -2 -1221 768 N ATOM 5667 CA CYS D 148 -22.822 -40.561 17.806 1.00 58.71 C ANISOU 5667 CA CYS D 148 6990 6558 8758 -147 -1392 896 C ATOM 5668 C CYS D 148 -23.440 -39.767 18.950 1.00 59.03 C ANISOU 5668 C CYS D 148 6880 6812 8737 -137 -1258 947 C ATOM 5669 O CYS D 148 -22.786 -38.915 19.556 1.00 58.90 O ANISOU 5669 O CYS D 148 6942 6769 8669 -138 -1050 853 O ATOM 5670 CB CYS D 148 -22.121 -41.786 18.366 1.00 58.61 C ANISOU 5670 CB CYS D 148 6946 6471 8853 -308 -1488 954 C ATOM 5671 SG CYS D 148 -23.286 -43.066 18.888 1.00 60.95 S ANISOU 5671 SG CYS D 148 7091 6873 9195 -530 -1689 1113 S ATOM 5672 N LEU D 149 -24.698 -40.057 19.254 1.00 60.01 N ANISOU 5672 N LEU D 149 6797 7161 8844 -161 -1355 1086 N ATOM 5673 CA LEU D 149 -25.394 -39.324 20.288 1.00 60.73 C ANISOU 5673 CA LEU D 149 6757 7452 8865 -97 -1176 1154 C ATOM 5674 C LEU D 149 -26.270 -40.247 21.136 1.00 61.95 C ANISOU 5674 C LEU D 149 6634 7857 9048 -284 -1322 1323 C ATOM 5675 O LEU D 149 -27.412 -40.545 20.779 1.00 63.76 O ANISOU 5675 O LEU D 149 6650 8307 9270 -283 -1440 1467 O ATOM 5676 CB LEU D 149 -26.212 -38.198 19.654 1.00 62.10 C ANISOU 5676 CB LEU D 149 6951 7691 8954 228 -995 1212 C ATOM 5677 CG LEU D 149 -26.282 -36.857 20.386 1.00 63.03 C ANISOU 5677 CG LEU D 149 7215 7752 8980 424 -590 1169 C ATOM 5678 CD1 LEU D 149 -24.965 -36.100 20.275 1.00 61.75 C ANISOU 5678 CD1 LEU D 149 7415 7259 8788 373 -380 929 C ATOM 5679 CD2 LEU D 149 -27.419 -36.027 19.831 1.00 65.02 C ANISOU 5679 CD2 LEU D 149 7399 8137 9168 833 -410 1364 C ATOM 5680 N ALA D 150 -25.712 -40.715 22.251 1.00 61.50 N ANISOU 5680 N ALA D 150 6557 7811 9000 -467 -1317 1330 N ATOM 5681 CA ALA D 150 -26.454 -41.502 23.231 1.00 62.65 C ANISOU 5681 CA ALA D 150 6476 8175 9154 -643 -1391 1508 C ATOM 5682 C ALA D 150 -27.149 -40.521 24.164 1.00 63.87 C ANISOU 5682 C ALA D 150 6538 8553 9178 -524 -1136 1540 C ATOM 5683 O ALA D 150 -26.497 -39.634 24.716 1.00 63.62 O ANISOU 5683 O ALA D 150 6687 8455 9029 -478 -917 1393 O ATOM 5684 CB ALA D 150 -25.512 -42.409 24.002 1.00 62.15 C ANISOU 5684 CB ALA D 150 6450 8043 9122 -829 -1470 1555 C ATOM 5685 N THR D 151 -28.464 -40.673 24.327 1.00 65.86 N ANISOU 5685 N THR D 151 6521 9075 9429 -496 -1137 1726 N ATOM 5686 CA THR D 151 -29.283 -39.668 25.025 1.00 67.82 C ANISOU 5686 CA THR D 151 6682 9527 9558 -271 -821 1792 C ATOM 5687 C THR D 151 -30.359 -40.229 25.962 1.00 70.20 C ANISOU 5687 C THR D 151 6655 10177 9841 -384 -807 2025 C ATOM 5688 O THR D 151 -30.918 -41.300 25.721 1.00 71.05 O ANISOU 5688 O THR D 151 6516 10436 10044 -614 -1061 2183 O ATOM 5689 CB THR D 151 -30.004 -38.727 24.027 1.00 69.13 C ANISOU 5689 CB THR D 151 6804 9751 9712 107 -685 1857 C ATOM 5690 OG1 THR D 151 -30.706 -39.512 23.056 1.00 69.96 O ANISOU 5690 OG1 THR D 151 6625 10067 9891 20 -1003 2015 O ATOM 5691 CG2 THR D 151 -29.018 -37.798 23.324 1.00 67.23 C ANISOU 5691 CG2 THR D 151 6953 9147 9446 283 -538 1635 C ATOM 5692 N GLY D 152 -30.644 -39.473 27.022 1.00 71.81 N ANISOU 5692 N GLY D 152 6897 10487 9900 -250 -469 2030 N ATOM 5693 CA GLY D 152 -31.771 -39.737 27.914 1.00 74.66 C ANISOU 5693 CA GLY D 152 6943 11209 10215 -264 -347 2268 C ATOM 5694 C GLY D 152 -31.552 -40.823 28.949 1.00 74.65 C ANISOU 5694 C GLY D 152 6879 11292 10192 -635 -486 2346 C ATOM 5695 O GLY D 152 -32.514 -41.424 29.426 1.00 77.08 O ANISOU 5695 O GLY D 152 6869 11898 10520 -748 -492 2588 O ATOM 5696 N PHE D 153 -30.297 -41.070 29.309 1.00 72.44 N ANISOU 5696 N PHE D 153 6873 10791 9858 -816 -583 2183 N ATOM 5697 CA PHE D 153 -29.980 -42.145 30.239 1.00 72.79 C ANISOU 5697 CA PHE D 153 6871 10916 9869 -1109 -719 2319 C ATOM 5698 C PHE D 153 -29.697 -41.650 31.658 1.00 74.42 C ANISOU 5698 C PHE D 153 7204 11285 9786 -1152 -478 2272 C ATOM 5699 O PHE D 153 -29.245 -40.521 31.853 1.00 74.44 O ANISOU 5699 O PHE D 153 7459 11219 9606 -1048 -251 2027 O ATOM 5700 CB PHE D 153 -28.822 -43.003 29.710 1.00 70.49 C ANISOU 5700 CB PHE D 153 6723 10360 9700 -1259 -1009 2282 C ATOM 5701 CG PHE D 153 -27.526 -42.252 29.535 1.00 68.52 C ANISOU 5701 CG PHE D 153 6735 9947 9353 -1186 -981 2032 C ATOM 5702 CD1 PHE D 153 -26.638 -42.102 30.592 1.00 68.80 C ANISOU 5702 CD1 PHE D 153 6866 10116 9157 -1310 -933 1993 C ATOM 5703 CD2 PHE D 153 -27.182 -41.708 28.307 1.00 66.78 C ANISOU 5703 CD2 PHE D 153 6644 9490 9241 -1036 -1010 1850 C ATOM 5704 CE1 PHE D 153 -25.442 -41.414 30.430 1.00 67.17 C ANISOU 5704 CE1 PHE D 153 6847 9836 8837 -1332 -921 1765 C ATOM 5705 CE2 PHE D 153 -25.982 -41.021 28.145 1.00 64.91 C ANISOU 5705 CE2 PHE D 153 6630 9117 8916 -1021 -962 1629 C ATOM 5706 CZ PHE D 153 -25.118 -40.877 29.210 1.00 65.12 C ANISOU 5706 CZ PHE D 153 6717 9306 8721 -1194 -921 1582 C ATOM 5707 N TYR D 154 -29.976 -42.511 32.636 1.00 76.38 N ANISOU 5707 N TYR D 154 7313 11740 9967 -1342 -511 2501 N ATOM 5708 CA TYR D 154 -29.727 -42.237 34.051 1.00 78.46 C ANISOU 5708 CA TYR D 154 7684 12229 9899 -1437 -322 2495 C ATOM 5709 C TYR D 154 -29.561 -43.557 34.809 1.00 79.75 C ANISOU 5709 C TYR D 154 7728 12527 10045 -1666 -501 2801 C ATOM 5710 O TYR D 154 -30.374 -44.464 34.648 1.00 80.58 O ANISOU 5710 O TYR D 154 7622 12643 10350 -1744 -569 3053 O ATOM 5711 CB TYR D 154 -30.872 -41.421 34.657 1.00 81.30 C ANISOU 5711 CB TYR D 154 7992 12790 10109 -1273 76 2503 C ATOM 5712 CG TYR D 154 -30.606 -40.912 36.060 1.00 83.94 C ANISOU 5712 CG TYR D 154 8544 13322 10027 -1376 340 2404 C ATOM 5713 CD1 TYR D 154 -29.722 -39.857 36.285 1.00 84.38 C ANISOU 5713 CD1 TYR D 154 8982 13272 9805 -1419 495 2046 C ATOM 5714 CD2 TYR D 154 -31.247 -41.474 37.160 1.00 86.83 C ANISOU 5714 CD2 TYR D 154 8761 13993 10239 -1481 451 2655 C ATOM 5715 CE1 TYR D 154 -29.475 -39.381 37.566 1.00 87.24 C ANISOU 5715 CE1 TYR D 154 9589 13845 9715 -1600 734 1910 C ATOM 5716 CE2 TYR D 154 -31.009 -41.002 38.447 1.00 89.61 C ANISOU 5716 CE2 TYR D 154 9344 14557 10145 -1598 698 2550 C ATOM 5717 CZ TYR D 154 -30.122 -39.956 38.640 1.00 89.89 C ANISOU 5717 CZ TYR D 154 9777 14500 9878 -1673 829 2162 C ATOM 5718 OH TYR D 154 -29.878 -39.480 39.907 1.00 93.61 O ANISOU 5718 OH TYR D 154 10520 15206 9841 -1874 1069 2012 O ATOM 5719 N PRO D 155 -28.494 -43.677 35.623 1.00 80.44 N ANISOU 5719 N PRO D 155 7949 12739 9874 -1790 -572 2802 N ATOM 5720 CA PRO D 155 -27.439 -42.685 35.833 1.00 80.35 C ANISOU 5720 CA PRO D 155 8166 12778 9585 -1827 -529 2496 C ATOM 5721 C PRO D 155 -26.393 -42.736 34.716 1.00 77.78 C ANISOU 5721 C PRO D 155 7897 12192 9465 -1781 -763 2374 C ATOM 5722 O PRO D 155 -26.624 -43.382 33.693 1.00 75.94 O ANISOU 5722 O PRO D 155 7580 11691 9582 -1677 -909 2471 O ATOM 5723 CB PRO D 155 -26.835 -43.104 37.171 1.00 82.97 C ANISOU 5723 CB PRO D 155 8492 13488 9543 -2031 -582 2667 C ATOM 5724 CG PRO D 155 -27.039 -44.574 37.221 1.00 83.22 C ANISOU 5724 CG PRO D 155 8330 13495 9794 -2023 -764 3099 C ATOM 5725 CD PRO D 155 -28.233 -44.916 36.376 1.00 82.03 C ANISOU 5725 CD PRO D 155 8063 13075 10030 -1932 -713 3160 C ATOM 5726 N ASP D 156 -25.258 -42.069 34.909 1.00 78.25 N ANISOU 5726 N ASP D 156 8099 12353 9280 -1897 -785 2157 N ATOM 5727 CA ASP D 156 -24.261 -41.963 33.843 1.00 76.45 C ANISOU 5727 CA ASP D 156 7913 11907 9229 -1847 -950 2027 C ATOM 5728 C ASP D 156 -23.231 -43.093 33.834 1.00 76.75 C ANISOU 5728 C ASP D 156 7783 12045 9335 -1850 -1235 2321 C ATOM 5729 O ASP D 156 -22.025 -42.850 33.821 1.00 77.22 O ANISOU 5729 O ASP D 156 7817 12270 9252 -1935 -1341 2258 O ATOM 5730 CB ASP D 156 -23.584 -40.585 33.852 1.00 76.99 C ANISOU 5730 CB ASP D 156 8219 11994 9040 -1992 -787 1627 C ATOM 5731 CG ASP D 156 -22.899 -40.275 35.165 1.00 80.76 C ANISOU 5731 CG ASP D 156 8732 12931 9022 -2327 -774 1567 C ATOM 5732 OD1 ASP D 156 -23.268 -40.881 36.202 1.00 83.20 O ANISOU 5732 OD1 ASP D 156 8924 13546 9143 -2390 -799 1810 O ATOM 5733 OD2 ASP D 156 -21.990 -39.415 35.150 1.00 81.89 O ANISOU 5733 OD2 ASP D 156 9027 13153 8934 -2569 -735 1274 O ATOM 5734 N HIS D 157 -23.721 -44.329 33.820 1.00 77.38 N ANISOU 5734 N HIS D 157 7750 12018 9633 -1753 -1324 2663 N ATOM 5735 CA HIS D 157 -22.861 -45.503 33.706 1.00 78.48 C ANISOU 5735 CA HIS D 157 7797 12127 9895 -1652 -1506 2998 C ATOM 5736 C HIS D 157 -22.899 -46.075 32.296 1.00 76.37 C ANISOU 5736 C HIS D 157 7622 11354 10041 -1483 -1560 2980 C ATOM 5737 O HIS D 157 -23.703 -46.961 32.001 1.00 76.75 O ANISOU 5737 O HIS D 157 7714 11130 10319 -1473 -1548 3137 O ATOM 5738 CB HIS D 157 -23.267 -46.572 34.719 1.00 81.42 C ANISOU 5738 CB HIS D 157 8082 12660 10193 -1673 -1503 3419 C ATOM 5739 CG HIS D 157 -22.918 -46.226 36.129 1.00 85.03 C ANISOU 5739 CG HIS D 157 8443 13686 10178 -1825 -1496 3514 C ATOM 5740 ND1 HIS D 157 -21.638 -46.344 36.627 1.00 88.08 N ANISOU 5740 ND1 HIS D 157 8686 14481 10301 -1825 -1648 3698 N ATOM 5741 CD2 HIS D 157 -23.677 -45.759 37.147 1.00 87.32 C ANISOU 5741 CD2 HIS D 157 8751 14255 10170 -1995 -1349 3458 C ATOM 5742 CE1 HIS D 157 -21.625 -45.969 37.893 1.00 91.37 C ANISOU 5742 CE1 HIS D 157 9045 15425 10245 -2037 -1630 3733 C ATOM 5743 NE2 HIS D 157 -22.850 -45.610 38.233 1.00 91.02 N ANISOU 5743 NE2 HIS D 157 9134 15274 10174 -2136 -1428 3572 N ATOM 5744 N VAL D 158 -22.027 -45.558 31.430 1.00 74.79 N ANISOU 5744 N VAL D 158 7471 11041 9904 -1400 -1605 2773 N ATOM 5745 CA VAL D 158 -21.962 -45.986 30.027 1.00 72.91 C ANISOU 5745 CA VAL D 158 7365 10338 10001 -1244 -1638 2708 C ATOM 5746 C VAL D 158 -20.546 -45.932 29.448 1.00 72.54 C ANISOU 5746 C VAL D 158 7303 10277 9983 -1099 -1689 2700 C ATOM 5747 O VAL D 158 -19.824 -44.946 29.635 1.00 72.23 O ANISOU 5747 O VAL D 158 7189 10517 9740 -1188 -1688 2518 O ATOM 5748 CB VAL D 158 -22.901 -45.147 29.112 1.00 70.72 C ANISOU 5748 CB VAL D 158 7196 9844 9829 -1264 -1574 2377 C ATOM 5749 CG1 VAL D 158 -24.342 -45.621 29.217 1.00 71.17 C ANISOU 5749 CG1 VAL D 158 7218 9842 9981 -1354 -1548 2472 C ATOM 5750 CG2 VAL D 158 -22.785 -43.653 29.426 1.00 70.45 C ANISOU 5750 CG2 VAL D 158 7184 10026 9559 -1330 -1453 2085 C ATOM 5751 N GLU D 159 -20.160 -47.002 28.754 1.00 73.01 N ANISOU 5751 N GLU D 159 7454 10004 10283 -898 -1697 2896 N ATOM 5752 CA GLU D 159 -18.955 -46.994 27.926 1.00 72.83 C ANISOU 5752 CA GLU D 159 7438 9885 10349 -697 -1691 2882 C ATOM 5753 C GLU D 159 -19.340 -47.101 26.454 1.00 70.70 C ANISOU 5753 C GLU D 159 7445 9084 10333 -624 -1643 2647 C ATOM 5754 O GLU D 159 -20.066 -48.013 26.048 1.00 71.16 O ANISOU 5754 O GLU D 159 7709 8767 10563 -629 -1616 2709 O ATOM 5755 CB GLU D 159 -17.969 -48.102 28.310 1.00 76.16 C ANISOU 5755 CB GLU D 159 7750 10387 10800 -432 -1670 3342 C ATOM 5756 CG GLU D 159 -17.144 -47.825 29.571 1.00 79.45 C ANISOU 5756 CG GLU D 159 7800 11497 10890 -474 -1762 3591 C ATOM 5757 CD GLU D 159 -17.388 -48.841 30.690 1.00 83.96 C ANISOU 5757 CD GLU D 159 8300 12227 11375 -393 -1758 4058 C ATOM 5758 OE1 GLU D 159 -17.680 -50.022 30.381 1.00 85.62 O ANISOU 5758 OE1 GLU D 159 8735 11959 11837 -175 -1631 4312 O ATOM 5759 OE2 GLU D 159 -17.271 -48.467 31.881 1.00 85.79 O ANISOU 5759 OE2 GLU D 159 8288 13046 11262 -566 -1856 4172 O ATOM 5760 N LEU D 160 -18.845 -46.149 25.669 1.00 68.74 N ANISOU 5760 N LEU D 160 7220 8827 10070 -603 -1627 2370 N ATOM 5761 CA LEU D 160 -19.190 -46.028 24.258 1.00 66.81 C ANISOU 5761 CA LEU D 160 7228 8169 9988 -546 -1593 2124 C ATOM 5762 C LEU D 160 -18.102 -46.630 23.374 1.00 67.67 C ANISOU 5762 C LEU D 160 7452 8025 10236 -292 -1509 2206 C ATOM 5763 O LEU D 160 -16.935 -46.251 23.474 1.00 68.30 O ANISOU 5763 O LEU D 160 7350 8348 10252 -186 -1473 2268 O ATOM 5764 CB LEU D 160 -19.391 -44.552 23.902 1.00 64.44 C ANISOU 5764 CB LEU D 160 6933 7974 9576 -641 -1566 1795 C ATOM 5765 CG LEU D 160 -20.076 -44.222 22.578 1.00 62.47 C ANISOU 5765 CG LEU D 160 6906 7409 9419 -596 -1552 1566 C ATOM 5766 CD1 LEU D 160 -20.632 -42.825 22.651 1.00 61.80 C ANISOU 5766 CD1 LEU D 160 6814 7466 9203 -658 -1479 1353 C ATOM 5767 CD2 LEU D 160 -19.141 -44.372 21.387 1.00 61.65 C ANISOU 5767 CD2 LEU D 160 6965 7046 9413 -423 -1493 1497 C ATOM 5768 N SER D 161 -18.491 -47.552 22.499 1.00 68.21 N ANISOU 5768 N SER D 161 7824 7624 10469 -223 -1456 2199 N ATOM 5769 CA SER D 161 -17.548 -48.169 21.578 1.00 69.52 C ANISOU 5769 CA SER D 161 8189 7466 10760 51 -1304 2255 C ATOM 5770 C SER D 161 -17.944 -47.976 20.119 1.00 68.23 C ANISOU 5770 C SER D 161 8354 6935 10637 11 -1279 1930 C ATOM 5771 O SER D 161 -19.123 -48.063 19.774 1.00 67.84 O ANISOU 5771 O SER D 161 8460 6747 10569 -224 -1377 1767 O ATOM 5772 CB SER D 161 -17.413 -49.657 21.887 1.00 73.13 C ANISOU 5772 CB SER D 161 8826 7618 11343 214 -1166 2585 C ATOM 5773 OG SER D 161 -16.604 -50.300 20.920 1.00 75.57 O ANISOU 5773 OG SER D 161 9415 7523 11774 517 -941 2625 O ATOM 5774 N TRP D 162 -16.953 -47.709 19.269 1.00 68.09 N ANISOU 5774 N TRP D 162 8404 6824 10643 231 -1152 1862 N ATOM 5775 CA TRP D 162 -17.156 -47.690 17.819 1.00 67.67 C ANISOU 5775 CA TRP D 162 8712 6404 10595 240 -1091 1595 C ATOM 5776 C TRP D 162 -16.723 -49.030 17.226 1.00 70.75 C ANISOU 5776 C TRP D 162 9490 6294 11098 439 -866 1697 C ATOM 5777 O TRP D 162 -15.642 -49.539 17.545 1.00 72.69 O ANISOU 5777 O TRP D 162 9656 6529 11435 767 -670 1979 O ATOM 5778 CB TRP D 162 -16.363 -46.564 17.158 1.00 66.01 C ANISOU 5778 CB TRP D 162 8411 6343 10325 355 -1029 1445 C ATOM 5779 CG TRP D 162 -16.906 -45.175 17.346 1.00 63.90 C ANISOU 5779 CG TRP D 162 7968 6377 9934 163 -1156 1260 C ATOM 5780 CD1 TRP D 162 -16.447 -44.226 18.217 1.00 63.45 C ANISOU 5780 CD1 TRP D 162 7603 6705 9802 88 -1164 1288 C ATOM 5781 CD2 TRP D 162 -17.978 -44.560 16.618 1.00 63.14 C ANISOU 5781 CD2 TRP D 162 8029 6215 9747 39 -1247 1036 C ATOM 5782 NE1 TRP D 162 -17.168 -43.062 18.085 1.00 61.64 N ANISOU 5782 NE1 TRP D 162 7402 6553 9466 -49 -1194 1079 N ATOM 5783 CE2 TRP D 162 -18.116 -43.239 17.112 1.00 61.53 C ANISOU 5783 CE2 TRP D 162 7634 6295 9450 -33 -1250 961 C ATOM 5784 CE3 TRP D 162 -18.843 -44.997 15.606 1.00 64.04 C ANISOU 5784 CE3 TRP D 162 8424 6093 9814 -33 -1319 905 C ATOM 5785 CZ2 TRP D 162 -19.086 -42.356 16.629 1.00 60.61 C ANISOU 5785 CZ2 TRP D 162 7590 6205 9233 -66 -1283 821 C ATOM 5786 CZ3 TRP D 162 -19.811 -44.112 15.125 1.00 62.89 C ANISOU 5786 CZ3 TRP D 162 8269 6090 9538 -110 -1424 774 C ATOM 5787 CH2 TRP D 162 -19.921 -42.810 15.639 1.00 61.21 C ANISOU 5787 CH2 TRP D 162 7852 6133 9271 -74 -1386 763 C ATOM 5788 N TRP D 163 -17.571 -49.592 16.366 1.00 71.68 N ANISOU 5788 N TRP D 163 10034 6020 11183 236 -870 1480 N ATOM 5789 CA TRP D 163 -17.306 -50.879 15.721 1.00 75.39 C ANISOU 5789 CA TRP D 163 11026 5901 11719 344 -599 1496 C ATOM 5790 C TRP D 163 -17.398 -50.760 14.202 1.00 75.69 C ANISOU 5790 C TRP D 163 11477 5653 11628 276 -540 1150 C ATOM 5791 O TRP D 163 -18.489 -50.608 13.643 1.00 75.43 O ANISOU 5791 O TRP D 163 11589 5633 11439 -111 -747 887 O ATOM 5792 CB TRP D 163 -18.267 -51.958 16.240 1.00 78.04 C ANISOU 5792 CB TRP D 163 11599 5964 12089 40 -613 1559 C ATOM 5793 CG TRP D 163 -18.046 -52.316 17.684 1.00 78.97 C ANISOU 5793 CG TRP D 163 11409 6276 12321 178 -590 1958 C ATOM 5794 CD1 TRP D 163 -18.555 -51.672 18.772 1.00 76.47 C ANISOU 5794 CD1 TRP D 163 10619 6475 11961 15 -842 2061 C ATOM 5795 CD2 TRP D 163 -17.255 -53.399 18.195 1.00 83.29 C ANISOU 5795 CD2 TRP D 163 12118 6518 13010 541 -271 2339 C ATOM 5796 NE1 TRP D 163 -18.137 -52.283 19.929 1.00 78.51 N ANISOU 5796 NE1 TRP D 163 10724 6809 12297 208 -740 2465 N ATOM 5797 CE2 TRP D 163 -17.334 -53.345 19.604 1.00 82.96 C ANISOU 5797 CE2 TRP D 163 11649 6889 12982 557 -395 2672 C ATOM 5798 CE3 TRP D 163 -16.492 -54.411 17.599 1.00 87.83 C ANISOU 5798 CE3 TRP D 163 13181 6504 13686 895 148 2455 C ATOM 5799 CZ2 TRP D 163 -16.676 -54.265 20.430 1.00 87.12 C ANISOU 5799 CZ2 TRP D 163 12181 7311 13611 922 -150 3156 C ATOM 5800 CZ3 TRP D 163 -15.833 -55.323 18.418 1.00 92.17 C ANISOU 5800 CZ3 TRP D 163 13750 6901 14370 1307 438 2948 C ATOM 5801 CH2 TRP D 163 -15.932 -55.243 19.819 1.00 91.82 C ANISOU 5801 CH2 TRP D 163 13232 7328 14327 1320 269 3311 C ATOM 5802 N VAL D 164 -16.244 -50.828 13.545 1.00 76.66 N ANISOU 5802 N VAL D 164 11755 5582 11789 658 -254 1182 N ATOM 5803 CA VAL D 164 -16.164 -50.707 12.090 1.00 77.35 C ANISOU 5803 CA VAL D 164 12259 5407 11725 648 -146 874 C ATOM 5804 C VAL D 164 -15.967 -52.077 11.436 1.00 82.46 C ANISOU 5804 C VAL D 164 13598 5360 12373 716 222 812 C ATOM 5805 O VAL D 164 -14.965 -52.761 11.681 1.00 85.22 O ANISOU 5805 O VAL D 164 14048 5443 12889 1162 596 1083 O ATOM 5806 CB VAL D 164 -15.050 -49.727 11.667 1.00 75.47 C ANISOU 5806 CB VAL D 164 11762 5421 11491 993 -34 910 C ATOM 5807 CG1 VAL D 164 -14.888 -49.705 10.151 1.00 77.02 C ANISOU 5807 CG1 VAL D 164 12437 5314 11514 1028 136 627 C ATOM 5808 CG2 VAL D 164 -15.357 -48.334 12.185 1.00 71.16 C ANISOU 5808 CG2 VAL D 164 10692 5446 10901 840 -342 892 C ATOM 5809 N ASN D 165 -16.935 -52.457 10.600 1.00 84.27 N ANISOU 5809 N ASN D 165 14307 5324 12388 268 134 464 N ATOM 5810 CA ASN D 165 -16.978 -53.773 9.963 1.00 89.84 C ANISOU 5810 CA ASN D 165 15799 5310 13027 158 483 305 C ATOM 5811 C ASN D 165 -16.964 -54.900 10.993 1.00 92.90 C ANISOU 5811 C ASN D 165 16334 5329 13636 221 710 592 C ATOM 5812 O ASN D 165 -16.372 -55.957 10.762 1.00 98.02 O ANISOU 5812 O ASN D 165 17562 5323 14358 484 1205 664 O ATOM 5813 CB ASN D 165 -15.838 -53.941 8.940 1.00 92.31 C ANISOU 5813 CB ASN D 165 16524 5248 13302 609 928 243 C ATOM 5814 CG ASN D 165 -16.012 -53.063 7.700 1.00 90.76 C ANISOU 5814 CG ASN D 165 16401 5276 12809 449 758 -98 C ATOM 5815 OD1 ASN D 165 -17.130 -52.777 7.271 1.00 90.22 O ANISOU 5815 OD1 ASN D 165 16379 5419 12481 -85 393 -374 O ATOM 5816 ND2 ASN D 165 -14.894 -52.646 7.113 1.00 90.23 N ANISOU 5816 ND2 ASN D 165 16319 5201 12763 928 1037 -38 N ATOM 5817 N GLY D 166 -17.618 -54.664 12.129 1.00 90.32 N ANISOU 5817 N GLY D 166 15512 5404 13403 13 392 778 N ATOM 5818 CA GLY D 166 -17.684 -55.645 13.218 1.00 93.08 C ANISOU 5818 CA GLY D 166 15939 5484 13944 58 572 1101 C ATOM 5819 C GLY D 166 -16.388 -55.815 13.995 1.00 93.58 C ANISOU 5819 C GLY D 166 15731 5581 14245 777 871 1600 C ATOM 5820 O GLY D 166 -16.169 -56.847 14.637 1.00 97.59 O ANISOU 5820 O GLY D 166 16485 5693 14902 987 1189 1919 O ATOM 5821 N LYS D 167 -15.529 -54.798 13.928 1.00 90.08 N ANISOU 5821 N LYS D 167 14771 5641 13816 1142 779 1692 N ATOM 5822 CA LYS D 167 -14.278 -54.762 14.683 1.00 90.50 C ANISOU 5822 CA LYS D 167 14381 5966 14038 1764 970 2185 C ATOM 5823 C LYS D 167 -14.104 -53.377 15.314 1.00 85.12 C ANISOU 5823 C LYS D 167 12893 6134 13314 1710 560 2241 C ATOM 5824 O LYS D 167 -14.347 -52.354 14.672 1.00 81.53 O ANISOU 5824 O LYS D 167 12320 5925 12734 1482 334 1913 O ATOM 5825 CB LYS D 167 -13.084 -55.134 13.790 1.00 93.99 C ANISOU 5825 CB LYS D 167 15129 6053 14531 2324 1458 2267 C ATOM 5826 CG LYS D 167 -11.801 -55.449 14.553 1.00 96.62 C ANISOU 5826 CG LYS D 167 15056 6614 15040 3027 1749 2879 C ATOM 5827 CD LYS D 167 -10.969 -56.510 13.850 1.00102.79 C ANISOU 5827 CD LYS D 167 16426 6713 15917 3613 2415 3055 C ATOM 5828 CE LYS D 167 -10.101 -57.268 14.858 1.00107.72 C ANISOU 5828 CE LYS D 167 16779 7424 16725 4289 2741 3774 C ATOM 5829 NZ LYS D 167 -9.573 -58.568 14.346 1.00114.47 N ANISOU 5829 NZ LYS D 167 18384 7414 17695 4870 3487 3994 N ATOM 5830 N GLU D 168 -13.694 -53.358 16.578 1.00 85.13 N ANISOU 5830 N GLU D 168 12387 6567 13392 1904 491 2663 N ATOM 5831 CA GLU D 168 -13.621 -52.121 17.347 1.00 81.01 C ANISOU 5831 CA GLU D 168 11177 6818 12786 1748 122 2689 C ATOM 5832 C GLU D 168 -12.441 -51.253 16.930 1.00 80.13 C ANISOU 5832 C GLU D 168 10704 7093 12648 2009 179 2717 C ATOM 5833 O GLU D 168 -11.303 -51.724 16.880 1.00 83.59 O ANISOU 5833 O GLU D 168 11040 7549 13173 2498 478 3059 O ATOM 5834 CB GLU D 168 -13.543 -52.428 18.846 1.00 82.28 C ANISOU 5834 CB GLU D 168 10939 7357 12966 1823 32 3125 C ATOM 5835 CG GLU D 168 -13.728 -51.211 19.747 1.00 78.49 C ANISOU 5835 CG GLU D 168 9870 7613 12338 1523 -348 3074 C ATOM 5836 CD GLU D 168 -13.577 -51.543 21.217 1.00 80.05 C ANISOU 5836 CD GLU D 168 9690 8233 12491 1596 -429 3515 C ATOM 5837 OE1 GLU D 168 -12.427 -51.706 21.671 1.00 83.04 O ANISOU 5837 OE1 GLU D 168 9707 8985 12859 1976 -324 3930 O ATOM 5838 OE2 GLU D 168 -14.605 -51.633 21.921 1.00 78.90 O ANISOU 5838 OE2 GLU D 168 9576 8104 12297 1278 -597 3473 O ATOM 5839 N VAL D 169 -12.718 -49.984 16.643 1.00 75.94 N ANISOU 5839 N VAL D 169 9975 6881 11997 1693 -73 2391 N ATOM 5840 CA VAL D 169 -11.658 -49.033 16.317 1.00 75.23 C ANISOU 5840 CA VAL D 169 9533 7184 11866 1824 -27 2392 C ATOM 5841 C VAL D 169 -11.290 -48.132 17.494 1.00 73.98 C ANISOU 5841 C VAL D 169 8741 7759 11610 1646 -262 2540 C ATOM 5842 O VAL D 169 -12.089 -47.928 18.411 1.00 72.12 O ANISOU 5842 O VAL D 169 8389 7712 11302 1352 -505 2511 O ATOM 5843 CB VAL D 169 -11.999 -48.169 15.092 1.00 72.60 C ANISOU 5843 CB VAL D 169 9465 6676 11443 1630 -54 1954 C ATOM 5844 CG1 VAL D 169 -11.811 -48.962 13.810 1.00 75.25 C ANISOU 5844 CG1 VAL D 169 10357 6419 11814 1879 259 1849 C ATOM 5845 CG2 VAL D 169 -13.409 -47.607 15.202 1.00 69.44 C ANISOU 5845 CG2 VAL D 169 9174 6271 10938 1189 -361 1651 C ATOM 5846 N HIS D 170 -10.061 -47.618 17.452 1.00 75.54 N ANISOU 5846 N HIS D 170 8538 8384 11780 1797 -165 2695 N ATOM 5847 CA HIS D 170 -9.542 -46.686 18.450 1.00 75.60 C ANISOU 5847 CA HIS D 170 7957 9134 11632 1536 -365 2788 C ATOM 5848 C HIS D 170 -9.006 -45.425 17.775 1.00 74.21 C ANISOU 5848 C HIS D 170 7674 9148 11373 1319 -328 2514 C ATOM 5849 O HIS D 170 -9.175 -44.319 18.289 1.00 72.48 O ANISOU 5849 O HIS D 170 7279 9265 10995 887 -498 2307 O ATOM 5850 CB HIS D 170 -8.431 -47.337 19.283 1.00 80.39 C ANISOU 5850 CB HIS D 170 8045 10266 12232 1864 -299 3349 C ATOM 5851 CG HIS D 170 -8.883 -48.516 20.086 1.00 82.78 C ANISOU 5851 CG HIS D 170 8435 10421 12596 2089 -306 3688 C ATOM 5852 ND1 HIS D 170 -9.877 -48.433 21.038 1.00 81.29 N ANISOU 5852 ND1 HIS D 170 8272 10308 12308 1749 -564 3607 N ATOM 5853 CD2 HIS D 170 -8.468 -49.806 20.087 1.00 87.56 C ANISOU 5853 CD2 HIS D 170 9138 10781 13348 2641 -34 4134 C ATOM 5854 CE1 HIS D 170 -10.059 -49.621 21.586 1.00 84.43 C ANISOU 5854 CE1 HIS D 170 8770 10523 12787 2043 -473 3985 C ATOM 5855 NE2 HIS D 170 -9.216 -50.472 21.027 1.00 88.23 N ANISOU 5855 NE2 HIS D 170 9320 10781 13421 2594 -141 4313 N ATOM 5856 N SER D 171 -8.353 -45.613 16.627 1.00 75.45 N ANISOU 5856 N SER D 171 7988 9051 11629 1621 -54 2516 N ATOM 5857 CA SER D 171 -7.810 -44.520 15.821 1.00 74.62 C ANISOU 5857 CA SER D 171 7846 9043 11463 1459 51 2284 C ATOM 5858 C SER D 171 -8.926 -43.676 15.204 1.00 70.33 C ANISOU 5858 C SER D 171 7761 8106 10854 1151 -43 1818 C ATOM 5859 O SER D 171 -9.879 -44.206 14.629 1.00 68.68 O ANISOU 5859 O SER D 171 8018 7387 10689 1242 -58 1666 O ATOM 5860 CB SER D 171 -6.885 -45.077 14.731 1.00 77.56 C ANISOU 5860 CB SER D 171 8307 9211 11953 1924 412 2441 C ATOM 5861 OG SER D 171 -6.490 -44.071 13.811 1.00 77.37 O ANISOU 5861 OG SER D 171 8343 9184 11871 1770 545 2197 O ATOM 5862 N GLY D 172 -8.794 -42.359 15.342 1.00 69.17 N ANISOU 5862 N GLY D 172 7477 8224 10579 773 -88 1614 N ATOM 5863 CA GLY D 172 -9.781 -41.409 14.831 1.00 66.08 C ANISOU 5863 CA GLY D 172 7479 7519 10111 540 -126 1246 C ATOM 5864 C GLY D 172 -11.062 -41.314 15.643 1.00 63.81 C ANISOU 5864 C GLY D 172 7292 7184 9768 341 -363 1136 C ATOM 5865 O GLY D 172 -12.092 -40.884 15.132 1.00 61.62 O ANISOU 5865 O GLY D 172 7353 6604 9455 297 -396 919 O ATOM 5866 N VAL D 173 -10.993 -41.708 16.911 1.00 64.86 N ANISOU 5866 N VAL D 173 7099 7670 9873 241 -517 1325 N ATOM 5867 CA VAL D 173 -12.160 -41.729 17.790 1.00 63.44 C ANISOU 5867 CA VAL D 173 6976 7489 9639 71 -714 1267 C ATOM 5868 C VAL D 173 -11.961 -40.772 18.954 1.00 64.25 C ANISOU 5868 C VAL D 173 6818 8045 9549 -322 -777 1202 C ATOM 5869 O VAL D 173 -10.870 -40.693 19.519 1.00 66.74 O ANISOU 5869 O VAL D 173 6754 8830 9774 -450 -778 1354 O ATOM 5870 CB VAL D 173 -12.415 -43.143 18.359 1.00 64.42 C ANISOU 5870 CB VAL D 173 7030 7584 9861 276 -820 1551 C ATOM 5871 CG1 VAL D 173 -13.651 -43.149 19.241 1.00 63.00 C ANISOU 5871 CG1 VAL D 173 6896 7422 9621 79 -1001 1499 C ATOM 5872 CG2 VAL D 173 -12.554 -44.162 17.240 1.00 64.81 C ANISOU 5872 CG2 VAL D 173 7425 7132 10068 604 -703 1581 C ATOM 5873 N CYS D 174 -13.018 -40.046 19.305 1.00 62.95 N ANISOU 5873 N CYS D 174 6857 7770 9293 -521 -811 983 N ATOM 5874 CA CYS D 174 -12.989 -39.160 20.462 1.00 64.39 C ANISOU 5874 CA CYS D 174 6913 8300 9253 -917 -823 870 C ATOM 5875 C CYS D 174 -14.342 -39.086 21.146 1.00 63.22 C ANISOU 5875 C CYS D 174 6916 8053 9053 -963 -896 799 C ATOM 5876 O CYS D 174 -15.286 -38.492 20.615 1.00 61.78 O ANISOU 5876 O CYS D 174 7040 7539 8896 -890 -795 625 O ATOM 5877 CB CYS D 174 -12.528 -37.751 20.078 1.00 65.10 C ANISOU 5877 CB CYS D 174 7171 8340 9224 -1198 -597 591 C ATOM 5878 SG CYS D 174 -12.110 -36.743 21.522 1.00 68.70 S ANISOU 5878 SG CYS D 174 7494 9271 9338 -1815 -567 421 S ATOM 5879 N THR D 175 -14.419 -39.690 22.327 1.00 64.52 N ANISOU 5879 N THR D 175 6835 8551 9127 -1055 -1054 979 N ATOM 5880 CA THR D 175 -15.618 -39.650 23.151 1.00 64.21 C ANISOU 5880 CA THR D 175 6880 8507 9011 -1125 -1102 946 C ATOM 5881 C THR D 175 -15.485 -38.514 24.158 1.00 66.33 C ANISOU 5881 C THR D 175 7170 9053 8978 -1530 -996 735 C ATOM 5882 O THR D 175 -14.370 -38.127 24.504 1.00 68.61 O ANISOU 5882 O THR D 175 7287 9689 9093 -1819 -989 699 O ATOM 5883 CB THR D 175 -15.813 -40.981 23.898 1.00 64.75 C ANISOU 5883 CB THR D 175 6723 8752 9127 -1008 -1294 1274 C ATOM 5884 OG1 THR D 175 -15.615 -42.070 22.993 1.00 64.00 O ANISOU 5884 OG1 THR D 175 6657 8382 9278 -685 -1328 1458 O ATOM 5885 CG2 THR D 175 -17.207 -41.076 24.469 1.00 64.19 C ANISOU 5885 CG2 THR D 175 6757 8597 9037 -1029 -1321 1259 C ATOM 5886 N ASP D 176 -16.616 -37.977 24.616 1.00 66.42 N ANISOU 5886 N ASP D 176 7397 8931 8907 -1572 -890 595 N ATOM 5887 CA ASP D 176 -16.614 -36.963 25.666 1.00 69.33 C ANISOU 5887 CA ASP D 176 7887 9500 8956 -1957 -730 370 C ATOM 5888 C ASP D 176 -16.084 -37.536 26.967 1.00 71.79 C ANISOU 5888 C ASP D 176 7870 10382 9026 -2221 -933 537 C ATOM 5889 O ASP D 176 -16.460 -38.644 27.355 1.00 71.23 O ANISOU 5889 O ASP D 176 7583 10437 9043 -2020 -1129 835 O ATOM 5890 CB ASP D 176 -18.016 -36.415 25.915 1.00 69.25 C ANISOU 5890 CB ASP D 176 8162 9228 8923 -1835 -528 256 C ATOM 5891 CG ASP D 176 -18.515 -35.536 24.790 1.00 69.42 C ANISOU 5891 CG ASP D 176 8529 8768 9081 -1598 -264 99 C ATOM 5892 OD1 ASP D 176 -17.716 -34.762 24.210 1.00 71.33 O ANISOU 5892 OD1 ASP D 176 8955 8856 9290 -1736 -96 -82 O ATOM 5893 OD2 ASP D 176 -19.727 -35.616 24.499 1.00 69.64 O ANISOU 5893 OD2 ASP D 176 8620 8610 9230 -1276 -217 190 O ATOM 5894 N PRO D 177 -15.208 -36.780 27.646 1.00 75.24 N ANISOU 5894 N PRO D 177 8279 11185 9125 -2705 -880 354 N ATOM 5895 CA PRO D 177 -14.709 -37.172 28.953 1.00 78.64 C ANISOU 5895 CA PRO D 177 8392 12268 9221 -3017 -1081 504 C ATOM 5896 C PRO D 177 -15.858 -37.430 29.925 1.00 78.81 C ANISOU 5896 C PRO D 177 8514 12303 9127 -2959 -1068 555 C ATOM 5897 O PRO D 177 -15.905 -38.487 30.558 1.00 79.38 O ANISOU 5897 O PRO D 177 8280 12699 9182 -2827 -1297 907 O ATOM 5898 CB PRO D 177 -13.887 -35.951 29.400 1.00 82.67 C ANISOU 5898 CB PRO D 177 9028 13053 9331 -3663 -936 145 C ATOM 5899 CG PRO D 177 -14.273 -34.835 28.473 1.00 81.16 C ANISOU 5899 CG PRO D 177 9355 12199 9283 -3643 -566 -219 C ATOM 5900 CD PRO D 177 -14.614 -35.511 27.195 1.00 76.88 C ANISOU 5900 CD PRO D 177 8762 11234 9214 -3037 -623 1 C ATOM 5901 N GLN D 178 -16.780 -36.475 30.016 1.00 78.79 N ANISOU 5901 N GLN D 178 8947 11934 9055 -3014 -759 241 N ATOM 5902 CA GLN D 178 -17.943 -36.589 30.891 1.00 79.25 C ANISOU 5902 CA GLN D 178 9118 11988 9005 -2936 -668 274 C ATOM 5903 C GLN D 178 -19.226 -36.189 30.149 1.00 76.70 C ANISOU 5903 C GLN D 178 9097 11083 8961 -2537 -402 193 C ATOM 5904 O GLN D 178 -19.182 -35.321 29.272 1.00 76.39 O ANISOU 5904 O GLN D 178 9346 10651 9026 -2472 -169 -27 O ATOM 5905 CB GLN D 178 -17.741 -35.747 32.156 1.00 83.68 C ANISOU 5905 CB GLN D 178 9884 12877 9034 -3474 -504 -6 C ATOM 5906 CG GLN D 178 -17.459 -34.274 31.900 1.00 86.38 C ANISOU 5906 CG GLN D 178 10719 12907 9196 -3817 -122 -486 C ATOM 5907 CD GLN D 178 -16.915 -33.575 33.128 1.00 92.89 C ANISOU 5907 CD GLN D 178 11724 14148 9422 -4513 -22 -790 C ATOM 5908 OE1 GLN D 178 -15.714 -33.624 33.405 1.00 96.02 O ANISOU 5908 OE1 GLN D 178 11849 15081 9553 -4989 -261 -803 O ATOM 5909 NE2 GLN D 178 -17.797 -32.914 33.872 1.00 95.28 N ANISOU 5909 NE2 GLN D 178 12480 14246 9477 -4589 347 -1031 N ATOM 5910 N PRO D 179 -20.366 -36.833 30.481 1.00 75.47 N ANISOU 5910 N PRO D 179 8844 10915 8916 -2266 -432 411 N ATOM 5911 CA PRO D 179 -21.649 -36.497 29.862 1.00 73.88 C ANISOU 5911 CA PRO D 179 8813 10321 8938 -1887 -205 406 C ATOM 5912 C PRO D 179 -22.230 -35.195 30.399 1.00 76.44 C ANISOU 5912 C PRO D 179 9554 10476 9014 -1944 265 124 C ATOM 5913 O PRO D 179 -21.774 -34.695 31.430 1.00 79.45 O ANISOU 5913 O PRO D 179 10113 11059 9014 -2341 398 -85 O ATOM 5914 CB PRO D 179 -22.543 -37.668 30.267 1.00 73.14 C ANISOU 5914 CB PRO D 179 8416 10402 8973 -1711 -400 745 C ATOM 5915 CG PRO D 179 -21.974 -38.138 31.541 1.00 75.53 C ANISOU 5915 CG PRO D 179 8570 11150 8977 -2023 -541 835 C ATOM 5916 CD PRO D 179 -20.492 -37.983 31.393 1.00 76.14 C ANISOU 5916 CD PRO D 179 8604 11393 8932 -2287 -687 732 C ATOM 5917 N LEU D 180 -23.229 -34.659 29.700 1.00 75.82 N ANISOU 5917 N LEU D 180 9640 10045 9122 -1542 534 136 N ATOM 5918 CA LEU D 180 -23.907 -33.440 30.140 1.00 78.94 C ANISOU 5918 CA LEU D 180 10469 10202 9322 -1452 1078 -66 C ATOM 5919 C LEU D 180 -25.347 -33.679 30.579 1.00 79.80 C ANISOU 5919 C LEU D 180 10426 10413 9482 -1094 1226 176 C ATOM 5920 O LEU D 180 -26.047 -34.535 30.027 1.00 77.52 O ANISOU 5920 O LEU D 180 9739 10241 9473 -813 962 492 O ATOM 5921 CB LEU D 180 -23.844 -32.339 29.074 1.00 79.33 C ANISOU 5921 CB LEU D 180 10906 9755 9480 -1226 1421 -226 C ATOM 5922 CG LEU D 180 -23.896 -32.669 27.577 1.00 76.42 C ANISOU 5922 CG LEU D 180 10345 9222 9468 -872 1201 -33 C ATOM 5923 CD1 LEU D 180 -25.204 -33.335 27.179 1.00 75.50 C ANISOU 5923 CD1 LEU D 180 9864 9241 9580 -413 1063 326 C ATOM 5924 CD2 LEU D 180 -23.665 -31.406 26.745 1.00 77.92 C ANISOU 5924 CD2 LEU D 180 11017 8924 9665 -723 1621 -218 C ATOM 5925 N LYS D 181 -25.765 -32.921 31.592 1.00 83.53 N ANISOU 5925 N LYS D 181 11229 10857 9653 -1153 1671 12 N ATOM 5926 CA LYS D 181 -27.138 -32.928 32.076 1.00 85.51 C ANISOU 5926 CA LYS D 181 11380 11198 9913 -781 1943 229 C ATOM 5927 C LYS D 181 -28.073 -32.397 30.995 1.00 85.68 C ANISOU 5927 C LYS D 181 11395 10949 10210 -169 2200 418 C ATOM 5928 O LYS D 181 -27.833 -31.323 30.441 1.00 87.16 O ANISOU 5928 O LYS D 181 12027 10711 10380 -17 2572 232 O ATOM 5929 CB LYS D 181 -27.269 -32.051 33.325 1.00 90.30 C ANISOU 5929 CB LYS D 181 12472 11744 10092 -958 2475 -45 C ATOM 5930 CG LYS D 181 -26.825 -32.698 34.631 1.00 91.41 C ANISOU 5930 CG LYS D 181 12505 12333 9893 -1463 2247 -99 C ATOM 5931 CD LYS D 181 -27.509 -32.015 35.820 1.00 96.39 C ANISOU 5931 CD LYS D 181 13525 12954 10143 -1459 2818 -248 C ATOM 5932 CE LYS D 181 -27.068 -32.585 37.159 1.00 97.50 C ANISOU 5932 CE LYS D 181 13599 13584 9862 -1979 2611 -304 C ATOM 5933 NZ LYS D 181 -25.820 -31.940 37.639 1.00 99.97 N ANISOU 5933 NZ LYS D 181 14354 13906 9725 -2630 2640 -763 N ATOM 5934 N GLU D 182 -29.132 -33.145 30.695 1.00 84.80 N ANISOU 5934 N GLU D 182 10774 11116 10329 159 2009 807 N ATOM 5935 CA GLU D 182 -30.139 -32.694 29.732 1.00 85.85 C ANISOU 5935 CA GLU D 182 10782 11167 10671 756 2217 1070 C ATOM 5936 C GLU D 182 -31.017 -31.571 30.307 1.00 91.26 C ANISOU 5936 C GLU D 182 11784 11696 11193 1190 2946 1096 C ATOM 5937 O GLU D 182 -31.617 -30.796 29.556 1.00 93.51 O ANISOU 5937 O GLU D 182 12156 11794 11579 1746 3294 1267 O ATOM 5938 CB GLU D 182 -30.988 -33.866 29.227 1.00 84.14 C ANISOU 5938 CB GLU D 182 9883 11384 10703 869 1760 1471 C ATOM 5939 CG GLU D 182 -30.222 -34.866 28.358 1.00 79.31 C ANISOU 5939 CG GLU D 182 9059 10794 10280 569 1149 1460 C ATOM 5940 CD GLU D 182 -31.127 -35.873 27.664 1.00 78.50 C ANISOU 5940 CD GLU D 182 8395 11039 10391 652 769 1806 C ATOM 5941 OE1 GLU D 182 -32.160 -36.263 28.243 1.00 80.98 O ANISOU 5941 OE1 GLU D 182 8359 11709 10701 708 815 2057 O ATOM 5942 OE2 GLU D 182 -30.807 -36.285 26.533 1.00 76.26 O ANISOU 5942 OE2 GLU D 182 8028 10690 10257 617 434 1818 O ATOM 5943 N GLN D 183 -31.077 -31.490 31.638 1.00 93.82 N ANISOU 5943 N GLN D 183 12302 12103 11243 965 3205 949 N ATOM 5944 CA GLN D 183 -31.746 -30.393 32.345 1.00 99.47 C ANISOU 5944 CA GLN D 183 13467 12590 11738 1316 3989 890 C ATOM 5945 C GLN D 183 -30.959 -30.023 33.607 1.00101.55 C ANISOU 5945 C GLN D 183 14300 12707 11576 756 4230 426 C ATOM 5946 O GLN D 183 -31.180 -30.599 34.672 1.00102.39 O ANISOU 5946 O GLN D 183 14239 13174 11490 514 4153 455 O ATOM 5947 CB GLN D 183 -33.193 -30.762 32.676 1.00102.13 C ANISOU 5947 CB GLN D 183 13286 13356 12162 1780 4137 1344 C ATOM 5948 CG GLN D 183 -34.158 -30.554 31.518 1.00103.49 C ANISOU 5948 CG GLN D 183 13062 13633 12625 2469 4203 1790 C ATOM 5949 CD GLN D 183 -35.207 -31.644 31.421 1.00103.48 C ANISOU 5949 CD GLN D 183 12194 14311 12814 2569 3804 2267 C ATOM 5950 OE1 GLN D 183 -35.149 -32.495 30.533 1.00100.07 O ANISOU 5950 OE1 GLN D 183 11290 14131 12602 2406 3188 2425 O ATOM 5951 NE2 GLN D 183 -36.170 -31.628 32.337 1.00107.86 N ANISOU 5951 NE2 GLN D 183 12559 15160 13262 2797 4180 2485 N ATOM 5952 N PRO D 184 -30.035 -29.054 33.483 1.00102.95 N ANISOU 5952 N PRO D 184 15161 12383 11573 505 4527 -1 N ATOM 5953 CA PRO D 184 -29.050 -28.725 34.519 1.00105.11 C ANISOU 5953 CA PRO D 184 15961 12581 11396 -208 4634 -500 C ATOM 5954 C PRO D 184 -29.629 -28.205 35.835 1.00110.93 C ANISOU 5954 C PRO D 184 17135 13287 11728 -219 5252 -661 C ATOM 5955 O PRO D 184 -29.114 -28.550 36.902 1.00111.83 O ANISOU 5955 O PRO D 184 17318 13710 11463 -817 5082 -890 O ATOM 5956 CB PRO D 184 -28.191 -27.635 33.857 1.00106.38 C ANISOU 5956 CB PRO D 184 16774 12138 11509 -369 4945 -869 C ATOM 5957 CG PRO D 184 -28.421 -27.797 32.397 1.00102.80 C ANISOU 5957 CG PRO D 184 15958 11581 11521 145 4711 -530 C ATOM 5958 CD PRO D 184 -29.849 -28.219 32.284 1.00103.06 C ANISOU 5958 CD PRO D 184 15476 11900 11784 842 4762 -21 C ATOM 5959 N ALA D 185 -30.683 -27.392 35.755 1.00115.35 N ANISOU 5959 N ALA D 185 17979 13506 12343 465 5978 -515 N ATOM 5960 CA ALA D 185 -31.244 -26.704 36.927 1.00122.04 C ANISOU 5960 CA ALA D 185 19395 14183 12790 542 6742 -701 C ATOM 5961 C ALA D 185 -31.823 -27.637 38.000 1.00122.22 C ANISOU 5961 C ALA D 185 18938 14842 12658 439 6526 -493 C ATOM 5962 O ALA D 185 -31.942 -27.253 39.170 1.00127.22 O ANISOU 5962 O ALA D 185 20060 15442 12835 226 7003 -757 O ATOM 5963 CB ALA D 185 -32.282 -25.670 36.492 1.00127.02 C ANISOU 5963 CB ALA D 185 20380 14312 13571 1446 7609 -484 C ATOM 5964 N LEU D 186 -32.176 -28.856 37.595 1.00117.17 N ANISOU 5964 N LEU D 186 17392 14756 12373 558 5838 -33 N ATOM 5965 CA LEU D 186 -32.661 -29.881 38.520 1.00116.86 C ANISOU 5965 CA LEU D 186 16847 15324 12231 410 5562 211 C ATOM 5966 C LEU D 186 -31.657 -31.035 38.656 1.00111.77 C ANISOU 5966 C LEU D 186 15809 15095 11563 -268 4701 180 C ATOM 5967 O LEU D 186 -30.889 -31.316 37.730 1.00107.31 O ANISOU 5967 O LEU D 186 15073 14454 11246 -428 4210 156 O ATOM 5968 CB LEU D 186 -34.048 -30.382 38.092 1.00116.86 C ANISOU 5968 CB LEU D 186 16134 15647 12622 1093 5579 816 C ATOM 5969 CG LEU D 186 -34.206 -31.218 36.818 1.00111.61 C ANISOU 5969 CG LEU D 186 14726 15216 12465 1261 4918 1202 C ATOM 5970 CD1 LEU D 186 -34.282 -32.708 37.156 1.00108.29 C ANISOU 5970 CD1 LEU D 186 13633 15372 12142 886 4249 1468 C ATOM 5971 CD2 LEU D 186 -35.446 -30.785 36.056 1.00114.16 C ANISOU 5971 CD2 LEU D 186 14733 15564 13078 2077 5287 1636 C ATOM 5972 N ASN D 187 -31.685 -31.702 39.808 1.00112.87 N ANISOU 5972 N ASN D 187 15811 15676 11399 -609 4562 222 N ATOM 5973 CA ASN D 187 -30.688 -32.719 40.156 1.00109.52 C ANISOU 5973 CA ASN D 187 15100 15660 10853 -1221 3852 217 C ATOM 5974 C ASN D 187 -30.783 -34.032 39.369 1.00103.95 C ANISOU 5974 C ASN D 187 13631 15226 10641 -1117 3169 668 C ATOM 5975 O ASN D 187 -29.837 -34.402 38.666 1.00100.15 O ANISOU 5975 O ASN D 187 13022 14703 10327 -1343 2680 619 O ATOM 5976 CB ASN D 187 -30.706 -32.995 41.668 1.00113.35 C ANISOU 5976 CB ASN D 187 15712 16549 10805 -1589 3956 160 C ATOM 5977 CG ASN D 187 -30.403 -31.753 42.496 1.00119.20 C ANISOU 5977 CG ASN D 187 17305 17031 10955 -1871 4585 -382 C ATOM 5978 OD1 ASN D 187 -31.145 -31.415 43.419 1.00123.83 O ANISOU 5978 OD1 ASN D 187 18173 17656 11222 -1744 5132 -417 O ATOM 5979 ND2 ASN D 187 -29.312 -31.066 42.164 1.00119.13 N ANISOU 5979 ND2 ASN D 187 17738 16745 10780 -2287 4543 -821 N ATOM 5980 N ASP D 188 -31.927 -34.710 39.475 1.00104.00 N ANISOU 5980 N ASP D 188 13158 15494 10864 -796 3181 1095 N ATOM 5981 CA ASP D 188 -32.122 -36.069 38.939 1.00 99.85 C ANISOU 5981 CA ASP D 188 11968 15239 10730 -810 2589 1512 C ATOM 5982 C ASP D 188 -32.212 -36.128 37.407 1.00 95.97 C ANISOU 5982 C ASP D 188 11225 14518 10722 -532 2340 1619 C ATOM 5983 O ASP D 188 -32.860 -37.024 36.852 1.00 94.33 O ANISOU 5983 O ASP D 188 10494 14497 10851 -422 2045 1976 O ATOM 5984 CB ASP D 188 -33.388 -36.692 39.540 1.00102.38 C ANISOU 5984 CB ASP D 188 11878 15922 11101 -626 2741 1915 C ATOM 5985 CG ASP D 188 -34.090 -35.766 40.519 1.00108.27 C ANISOU 5985 CG ASP D 188 12971 16680 11488 -409 3459 1808 C ATOM 5986 OD1 ASP D 188 -34.459 -34.640 40.107 1.00110.43 O ANISOU 5986 OD1 ASP D 188 13544 16628 11786 0 3961 1661 O ATOM 5987 OD2 ASP D 188 -34.280 -36.164 41.692 1.00111.23 O ANISOU 5987 OD2 ASP D 188 13347 17369 11545 -615 3561 1889 O ATOM 5988 N SER D 189 -31.551 -35.183 36.740 1.00 94.75 N ANISOU 5988 N SER D 189 11469 13969 10564 -475 2468 1300 N ATOM 5989 CA SER D 189 -31.614 -35.026 35.289 1.00 91.58 C ANISOU 5989 CA SER D 189 10926 13326 10546 -176 2318 1371 C ATOM 5990 C SER D 189 -31.058 -36.229 34.538 1.00 86.75 C ANISOU 5990 C SER D 189 9922 12820 10218 -411 1640 1523 C ATOM 5991 O SER D 189 -30.133 -36.891 35.009 1.00 85.20 O ANISOU 5991 O SER D 189 9735 12737 9902 -819 1310 1458 O ATOM 5992 CB SER D 189 -30.859 -33.759 34.871 1.00 92.23 C ANISOU 5992 CB SER D 189 11605 12931 10506 -147 2633 973 C ATOM 5993 OG SER D 189 -30.795 -33.610 33.459 1.00 89.30 O ANISOU 5993 OG SER D 189 11130 12331 10468 122 2474 1044 O ATOM 5994 N ARG D 190 -31.637 -36.496 33.370 1.00 84.90 N ANISOU 5994 N ARG D 190 9360 12566 10331 -132 1465 1744 N ATOM 5995 CA ARG D 190 -31.123 -37.489 32.434 1.00 80.87 C ANISOU 5995 CA ARG D 190 8599 12038 10089 -313 908 1830 C ATOM 5996 C ARG D 190 -29.803 -36.991 31.859 1.00 78.43 C ANISOU 5996 C ARG D 190 8655 11390 9753 -436 814 1510 C ATOM 5997 O ARG D 190 -29.514 -35.797 31.909 1.00 79.82 O ANISOU 5997 O ARG D 190 9244 11318 9765 -334 1191 1249 O ATOM 5998 CB ARG D 190 -32.109 -37.695 31.282 1.00 80.86 C ANISOU 5998 CB ARG D 190 8220 12126 10379 -15 797 2092 C ATOM 5999 CG ARG D 190 -33.566 -37.892 31.669 1.00 84.13 C ANISOU 5999 CG ARG D 190 8211 12935 10820 178 975 2434 C ATOM 6000 CD ARG D 190 -33.914 -39.361 31.763 1.00 83.64 C ANISOU 6000 CD ARG D 190 7730 13151 10899 -181 566 2682 C ATOM 6001 NE ARG D 190 -35.327 -39.608 31.480 1.00 86.89 N ANISOU 6001 NE ARG D 190 7610 13977 11427 -33 598 3033 N ATOM 6002 CZ ARG D 190 -35.798 -40.021 30.306 1.00 86.83 C ANISOU 6002 CZ ARG D 190 7268 14115 11609 -48 295 3182 C ATOM 6003 NH1 ARG D 190 -34.976 -40.238 29.288 1.00 83.52 N ANISOU 6003 NH1 ARG D 190 7045 13394 11294 -165 -30 2995 N ATOM 6004 NH2 ARG D 190 -37.096 -40.220 30.149 1.00 90.59 N ANISOU 6004 NH2 ARG D 190 7195 15088 12137 30 321 3523 N ATOM 6005 N TYR D 191 -29.013 -37.900 31.298 1.00 75.44 N ANISOU 6005 N TYR D 191 8148 10982 9535 -655 359 1537 N ATOM 6006 CA TYR D 191 -27.722 -37.535 30.714 1.00 73.58 C ANISOU 6006 CA TYR D 191 8177 10489 9290 -778 251 1279 C ATOM 6007 C TYR D 191 -27.650 -37.817 29.213 1.00 71.01 C ANISOU 6007 C TYR D 191 7749 9968 9264 -612 12 1334 C ATOM 6008 O TYR D 191 -28.398 -38.648 28.694 1.00 70.68 O ANISOU 6008 O TYR D 191 7400 10034 9422 -539 -205 1572 O ATOM 6009 CB TYR D 191 -26.578 -38.249 31.447 1.00 73.00 C ANISOU 6009 CB TYR D 191 8083 10582 9070 -1163 -18 1254 C ATOM 6010 CG TYR D 191 -26.397 -37.797 32.880 1.00 76.40 C ANISOU 6010 CG TYR D 191 8689 11238 9101 -1402 204 1129 C ATOM 6011 CD1 TYR D 191 -25.692 -36.630 33.183 1.00 78.47 C ANISOU 6011 CD1 TYR D 191 9352 11392 9070 -1586 472 765 C ATOM 6012 CD2 TYR D 191 -26.936 -38.531 33.934 1.00 78.54 C ANISOU 6012 CD2 TYR D 191 8764 11828 9250 -1493 168 1360 C ATOM 6013 CE1 TYR D 191 -25.529 -36.207 34.500 1.00 82.17 C ANISOU 6013 CE1 TYR D 191 10034 12088 9100 -1883 681 604 C ATOM 6014 CE2 TYR D 191 -26.779 -38.117 35.257 1.00 82.15 C ANISOU 6014 CE2 TYR D 191 9406 12528 9278 -1729 376 1238 C ATOM 6015 CZ TYR D 191 -26.076 -36.955 35.531 1.00 83.99 C ANISOU 6015 CZ TYR D 191 10050 12670 9191 -1936 623 845 C ATOM 6016 OH TYR D 191 -25.920 -36.547 36.835 1.00 88.08 O ANISOU 6016 OH TYR D 191 10799 13447 9219 -2244 829 682 O ATOM 6017 N ALA D 192 -26.753 -37.108 28.527 1.00 69.68 N ANISOU 6017 N ALA D 192 7858 9526 9090 -600 68 1102 N ATOM 6018 CA ALA D 192 -26.432 -37.384 27.126 1.00 67.15 C ANISOU 6018 CA ALA D 192 7500 9016 8999 -486 -160 1120 C ATOM 6019 C ALA D 192 -24.915 -37.413 26.914 1.00 65.48 C ANISOU 6019 C ALA D 192 7449 8671 8758 -720 -292 931 C ATOM 6020 O ALA D 192 -24.186 -36.673 27.577 1.00 66.83 O ANISOU 6020 O ALA D 192 7846 8836 8709 -923 -103 715 O ATOM 6021 CB ALA D 192 -27.081 -36.359 26.221 1.00 67.97 C ANISOU 6021 CB ALA D 192 7741 8936 9150 -107 107 1108 C ATOM 6022 N LEU D 193 -24.447 -38.269 26.003 1.00 63.20 N ANISOU 6022 N LEU D 193 7044 8304 8666 -717 -594 1012 N ATOM 6023 CA LEU D 193 -23.016 -38.394 25.705 1.00 61.92 C ANISOU 6023 CA LEU D 193 6958 8063 8506 -873 -708 900 C ATOM 6024 C LEU D 193 -22.753 -38.459 24.200 1.00 60.54 C ANISOU 6024 C LEU D 193 6862 7622 8519 -692 -790 873 C ATOM 6025 O LEU D 193 -23.488 -39.130 23.470 1.00 59.90 O ANISOU 6025 O LEU D 193 6680 7493 8588 -554 -945 1008 O ATOM 6026 CB LEU D 193 -22.432 -39.631 26.385 1.00 61.66 C ANISOU 6026 CB LEU D 193 6701 8247 8480 -1050 -969 1087 C ATOM 6027 CG LEU D 193 -20.918 -39.822 26.291 1.00 60.80 C ANISOU 6027 CG LEU D 193 6564 8197 8342 -1176 -1073 1061 C ATOM 6028 CD1 LEU D 193 -20.224 -39.126 27.440 1.00 62.86 C ANISOU 6028 CD1 LEU D 193 6831 8769 8283 -1479 -976 936 C ATOM 6029 CD2 LEU D 193 -20.572 -41.289 26.283 1.00 59.93 C ANISOU 6029 CD2 LEU D 193 6260 8131 8381 -1120 -1311 1348 C ATOM 6030 N SER D 194 -21.697 -37.775 23.751 1.00 60.49 N ANISOU 6030 N SER D 194 7039 7474 8471 -745 -681 691 N ATOM 6031 CA SER D 194 -21.380 -37.668 22.321 1.00 59.58 C ANISOU 6031 CA SER D 194 7048 7100 8490 -567 -696 649 C ATOM 6032 C SER D 194 -19.976 -38.153 21.961 1.00 58.99 C ANISOU 6032 C SER D 194 6932 7013 8469 -677 -810 632 C ATOM 6033 O SER D 194 -19.007 -37.825 22.648 1.00 59.94 O ANISOU 6033 O SER D 194 7013 7301 8460 -916 -755 554 O ATOM 6034 CB SER D 194 -21.552 -36.223 21.847 1.00 60.60 C ANISOU 6034 CB SER D 194 7482 7005 8538 -434 -358 484 C ATOM 6035 OG SER D 194 -20.390 -35.449 22.108 1.00 61.90 O ANISOU 6035 OG SER D 194 7829 7110 8581 -685 -171 273 O ATOM 6036 N SER D 195 -19.875 -38.915 20.873 1.00 58.08 N ANISOU 6036 N SER D 195 6820 6734 8514 -514 -952 709 N ATOM 6037 CA SER D 195 -18.581 -39.404 20.386 1.00 58.15 C ANISOU 6037 CA SER D 195 6799 6703 8594 -520 -998 730 C ATOM 6038 C SER D 195 -18.406 -39.251 18.878 1.00 57.57 C ANISOU 6038 C SER D 195 6935 6342 8598 -327 -939 654 C ATOM 6039 O SER D 195 -19.366 -39.366 18.115 1.00 57.60 O ANISOU 6039 O SER D 195 7050 6208 8628 -181 -994 659 O ATOM 6040 CB SER D 195 -18.361 -40.866 20.778 1.00 58.55 C ANISOU 6040 CB SER D 195 6664 6837 8745 -506 -1192 956 C ATOM 6041 OG SER D 195 -17.119 -41.356 20.282 1.00 58.98 O ANISOU 6041 OG SER D 195 6680 6854 8875 -416 -1176 1029 O ATOM 6042 N ARG D 196 -17.164 -39.018 18.464 1.00 57.76 N ANISOU 6042 N ARG D 196 6977 6339 8629 -347 -835 604 N ATOM 6043 CA ARG D 196 -16.820 -38.851 17.057 1.00 57.25 C ANISOU 6043 CA ARG D 196 7123 6017 8612 -170 -740 537 C ATOM 6044 C ARG D 196 -16.085 -40.056 16.475 1.00 57.57 C ANISOU 6044 C ARG D 196 7128 5975 8772 -33 -809 655 C ATOM 6045 O ARG D 196 -15.577 -40.913 17.206 1.00 58.70 O ANISOU 6045 O ARG D 196 7055 6277 8973 -53 -888 820 O ATOM 6046 CB ARG D 196 -15.960 -37.604 16.897 1.00 57.98 C ANISOU 6046 CB ARG D 196 7311 6099 8620 -292 -487 391 C ATOM 6047 CG ARG D 196 -16.758 -36.334 16.763 1.00 58.13 C ANISOU 6047 CG ARG D 196 7592 5955 8538 -271 -288 261 C ATOM 6048 CD ARG D 196 -16.327 -35.326 17.802 1.00 60.08 C ANISOU 6048 CD ARG D 196 7863 6315 8650 -597 -87 117 C ATOM 6049 NE ARG D 196 -17.069 -35.487 19.050 1.00 60.84 N ANISOU 6049 NE ARG D 196 7836 6606 8676 -705 -180 142 N ATOM 6050 CZ ARG D 196 -16.872 -34.755 20.142 1.00 62.88 C ANISOU 6050 CZ ARG D 196 8136 6996 8759 -1027 -29 1 C ATOM 6051 NH1 ARG D 196 -17.603 -34.973 21.229 1.00 63.02 N ANISOU 6051 NH1 ARG D 196 8057 7193 8696 -1089 -102 39 N ATOM 6052 NH2 ARG D 196 -15.945 -33.806 20.148 1.00 65.45 N ANISOU 6052 NH2 ARG D 196 8624 7280 8964 -1332 212 -191 N ATOM 6053 N LEU D 197 -16.051 -40.118 15.148 1.00 57.18 N ANISOU 6053 N LEU D 197 7321 5668 8737 141 -744 590 N ATOM 6054 CA LEU D 197 -15.205 -41.056 14.418 1.00 57.89 C ANISOU 6054 CA LEU D 197 7477 5606 8912 308 -688 661 C ATOM 6055 C LEU D 197 -14.856 -40.438 13.076 1.00 57.97 C ANISOU 6055 C LEU D 197 7744 5420 8861 433 -513 536 C ATOM 6056 O LEU D 197 -15.744 -40.096 12.296 1.00 57.44 O ANISOU 6056 O LEU D 197 7912 5218 8695 482 -552 440 O ATOM 6057 CB LEU D 197 -15.892 -42.414 14.227 1.00 58.35 C ANISOU 6057 CB LEU D 197 7671 5472 9028 370 -830 725 C ATOM 6058 CG LEU D 197 -15.252 -43.365 13.211 1.00 59.54 C ANISOU 6058 CG LEU D 197 8075 5319 9227 573 -696 738 C ATOM 6059 CD1 LEU D 197 -13.885 -43.860 13.680 1.00 61.04 C ANISOU 6059 CD1 LEU D 197 8047 5606 9541 746 -529 952 C ATOM 6060 CD2 LEU D 197 -16.178 -44.528 12.934 1.00 60.28 C ANISOU 6060 CD2 LEU D 197 8431 5156 9317 510 -813 712 C ATOM 6061 N ARG D 198 -13.562 -40.288 12.813 1.00 59.04 N ANISOU 6061 N ARG D 198 7800 5597 9035 490 -316 574 N ATOM 6062 CA ARG D 198 -13.123 -39.601 11.602 1.00 59.53 C ANISOU 6062 CA ARG D 198 8095 5493 9029 589 -103 473 C ATOM 6063 C ARG D 198 -12.260 -40.468 10.681 1.00 61.37 C ANISOU 6063 C ARG D 198 8440 5564 9313 833 55 536 C ATOM 6064 O ARG D 198 -11.080 -40.704 10.949 1.00 62.81 O ANISOU 6064 O ARG D 198 8365 5915 9586 893 201 678 O ATOM 6065 CB ARG D 198 -12.430 -38.271 11.931 1.00 59.72 C ANISOU 6065 CB ARG D 198 8000 5681 9008 383 85 416 C ATOM 6066 CG ARG D 198 -12.339 -37.345 10.743 1.00 59.28 C ANISOU 6066 CG ARG D 198 8262 5401 8859 460 317 312 C ATOM 6067 CD ARG D 198 -11.849 -35.977 11.121 1.00 58.95 C ANISOU 6067 CD ARG D 198 8206 5430 8763 187 542 226 C ATOM 6068 NE ARG D 198 -12.182 -35.018 10.071 1.00 58.88 N ANISOU 6068 NE ARG D 198 8592 5130 8649 303 764 156 N ATOM 6069 CZ ARG D 198 -12.068 -33.698 10.179 1.00 59.52 C ANISOU 6069 CZ ARG D 198 8854 5101 8659 115 1035 69 C ATOM 6070 NH1 ARG D 198 -12.403 -32.927 9.159 1.00 59.81 N ANISOU 6070 NH1 ARG D 198 9274 4851 8599 305 1257 70 N ATOM 6071 NH2 ARG D 198 -11.621 -33.145 11.299 1.00 60.47 N ANISOU 6071 NH2 ARG D 198 8812 5390 8775 -279 1108 -17 N ATOM 6072 N VAL D 199 -12.877 -40.919 9.590 1.00 61.76 N ANISOU 6072 N VAL D 199 8870 5324 9271 970 39 438 N ATOM 6073 CA VAL D 199 -12.199 -41.700 8.554 1.00 63.93 C ANISOU 6073 CA VAL D 199 9394 5359 9538 1208 246 441 C ATOM 6074 C VAL D 199 -11.931 -40.867 7.292 1.00 64.59 C ANISOU 6074 C VAL D 199 9742 5335 9466 1290 447 333 C ATOM 6075 O VAL D 199 -12.483 -39.768 7.139 1.00 63.53 O ANISOU 6075 O VAL D 199 9659 5260 9220 1185 400 264 O ATOM 6076 CB VAL D 199 -13.005 -42.961 8.191 1.00 64.94 C ANISOU 6076 CB VAL D 199 9853 5207 9616 1236 123 374 C ATOM 6077 CG1 VAL D 199 -12.843 -44.007 9.279 1.00 65.77 C ANISOU 6077 CG1 VAL D 199 9759 5324 9907 1258 76 548 C ATOM 6078 CG2 VAL D 199 -14.481 -42.621 7.962 1.00 63.30 C ANISOU 6078 CG2 VAL D 199 9792 5029 9229 1030 -166 233 C ATOM 6079 N SER D 200 -11.080 -41.385 6.402 1.00 66.67 N ANISOU 6079 N SER D 200 10194 5424 9713 1515 717 346 N ATOM 6080 CA SER D 200 -10.790 -40.716 5.127 1.00 67.57 C ANISOU 6080 CA SER D 200 10600 5423 9650 1614 940 260 C ATOM 6081 C SER D 200 -12.022 -40.728 4.222 1.00 67.21 C ANISOU 6081 C SER D 200 10980 5227 9331 1575 752 95 C ATOM 6082 O SER D 200 -12.843 -41.644 4.298 1.00 67.55 O ANISOU 6082 O SER D 200 11171 5178 9318 1496 530 20 O ATOM 6083 CB SER D 200 -9.584 -41.357 4.420 1.00 70.71 C ANISOU 6083 CB SER D 200 11097 5687 10084 1893 1312 328 C ATOM 6084 OG SER D 200 -9.827 -42.708 4.047 1.00 72.98 O ANISOU 6084 OG SER D 200 11728 5670 10331 2046 1339 270 O ATOM 6085 N ALA D 201 -12.152 -39.707 3.379 1.00 66.99 N ANISOU 6085 N ALA D 201 11132 5210 9110 1607 843 63 N ATOM 6086 CA ALA D 201 -13.311 -39.584 2.496 1.00 67.22 C ANISOU 6086 CA ALA D 201 11487 5233 8821 1591 644 -25 C ATOM 6087 C ALA D 201 -13.466 -40.799 1.588 1.00 69.52 C ANISOU 6087 C ALA D 201 12184 5330 8901 1609 629 -177 C ATOM 6088 O ALA D 201 -14.580 -41.279 1.386 1.00 70.19 O ANISOU 6088 O ALA D 201 12415 5474 8781 1440 325 -272 O ATOM 6089 CB ALA D 201 -13.247 -38.297 1.678 1.00 67.86 C ANISOU 6089 CB ALA D 201 11720 5345 8717 1702 823 33 C ATOM 6090 N THR D 202 -12.350 -41.300 1.064 1.00 71.17 N ANISOU 6090 N THR D 202 12575 5322 9145 1790 982 -201 N ATOM 6091 CA THR D 202 -12.363 -42.508 0.233 1.00 74.44 C ANISOU 6091 CA THR D 202 13474 5452 9356 1817 1078 -377 C ATOM 6092 C THR D 202 -12.887 -43.729 1.000 1.00 74.39 C ANISOU 6092 C THR D 202 13483 5305 9475 1651 892 -440 C ATOM 6093 O THR D 202 -13.541 -44.597 0.419 1.00 76.89 O ANISOU 6093 O THR D 202 14240 5439 9537 1470 800 -646 O ATOM 6094 CB THR D 202 -10.972 -42.821 -0.371 1.00 77.02 C ANISOU 6094 CB THR D 202 13975 5551 9738 2125 1589 -346 C ATOM 6095 OG1 THR D 202 -9.993 -42.853 0.672 1.00 76.38 O ANISOU 6095 OG1 THR D 202 13410 5552 10060 2270 1758 -127 O ATOM 6096 CG2 THR D 202 -10.574 -41.765 -1.398 1.00 77.93 C ANISOU 6096 CG2 THR D 202 14222 5752 9635 2243 1800 -322 C ATOM 6097 N PHE D 203 -12.613 -43.770 2.304 1.00 71.88 N ANISOU 6097 N PHE D 203 12707 5087 9518 1667 841 -265 N ATOM 6098 CA PHE D 203 -13.058 -44.865 3.171 1.00 72.09 C ANISOU 6098 CA PHE D 203 12709 4984 9697 1535 696 -260 C ATOM 6099 C PHE D 203 -14.576 -44.881 3.379 1.00 70.99 C ANISOU 6099 C PHE D 203 12571 5008 9394 1160 246 -370 C ATOM 6100 O PHE D 203 -15.198 -45.952 3.344 1.00 73.20 O ANISOU 6100 O PHE D 203 13145 5082 9586 937 151 -503 O ATOM 6101 CB PHE D 203 -12.333 -44.813 4.522 1.00 70.28 C ANISOU 6101 CB PHE D 203 11945 4915 9845 1664 749 2 C ATOM 6102 CG PHE D 203 -12.289 -46.136 5.244 1.00 72.55 C ANISOU 6102 CG PHE D 203 12289 4964 10311 1707 803 90 C ATOM 6103 CD1 PHE D 203 -13.111 -46.373 6.344 1.00 71.21 C ANISOU 6103 CD1 PHE D 203 11882 4923 10250 1472 492 152 C ATOM 6104 CD2 PHE D 203 -11.417 -47.146 4.829 1.00 76.98 C ANISOU 6104 CD2 PHE D 203 13170 5149 10930 2023 1222 141 C ATOM 6105 CE1 PHE D 203 -13.070 -47.602 7.024 1.00 73.38 C ANISOU 6105 CE1 PHE D 203 12246 4947 10688 1523 578 270 C ATOM 6106 CE2 PHE D 203 -11.368 -48.376 5.501 1.00 79.22 C ANISOU 6106 CE2 PHE D 203 13567 5148 11385 2122 1343 270 C ATOM 6107 CZ PHE D 203 -12.198 -48.602 6.601 1.00 77.27 C ANISOU 6107 CZ PHE D 203 13090 5026 11244 1857 1011 338 C ATOM 6108 N TRP D 204 -15.159 -43.698 3.589 1.00 68.05 N ANISOU 6108 N TRP D 204 11881 4999 8975 1090 13 -299 N ATOM 6109 CA TRP D 204 -16.607 -43.543 3.770 1.00 67.30 C ANISOU 6109 CA TRP D 204 11680 5173 8718 807 -392 -329 C ATOM 6110 C TRP D 204 -17.399 -43.824 2.488 1.00 70.61 C ANISOU 6110 C TRP D 204 12502 5633 8695 618 -544 -513 C ATOM 6111 O TRP D 204 -18.549 -44.272 2.542 1.00 71.92 O ANISOU 6111 O TRP D 204 12657 5981 8690 287 -868 -578 O ATOM 6112 CB TRP D 204 -16.929 -42.143 4.299 1.00 64.42 C ANISOU 6112 CB TRP D 204 10912 5146 8419 887 -493 -164 C ATOM 6113 CG TRP D 204 -18.387 -41.751 4.202 1.00 64.99 C ANISOU 6113 CG TRP D 204 10861 5564 8267 729 -838 -127 C ATOM 6114 CD1 TRP D 204 -18.934 -40.835 3.344 1.00 66.12 C ANISOU 6114 CD1 TRP D 204 11053 5946 8123 838 -901 -61 C ATOM 6115 CD2 TRP D 204 -19.479 -42.267 4.983 1.00 64.98 C ANISOU 6115 CD2 TRP D 204 10627 5762 8300 466 -1146 -97 C ATOM 6116 NE1 TRP D 204 -20.293 -40.749 3.541 1.00 67.08 N ANISOU 6116 NE1 TRP D 204 10941 6451 8095 692 -1236 33 N ATOM 6117 CE2 TRP D 204 -20.654 -41.614 4.542 1.00 66.38 C ANISOU 6117 CE2 TRP D 204 10669 6349 8204 437 -1391 -3 C ATOM 6118 CE3 TRP D 204 -19.579 -43.215 6.013 1.00 63.89 C ANISOU 6118 CE3 TRP D 204 10367 5520 8388 272 -1218 -102 C ATOM 6119 CZ2 TRP D 204 -21.916 -41.884 5.093 1.00 67.00 C ANISOU 6119 CZ2 TRP D 204 10449 6772 8236 198 -1709 76 C ATOM 6120 CZ3 TRP D 204 -20.834 -43.478 6.561 1.00 64.23 C ANISOU 6120 CZ3 TRP D 204 10171 5848 8386 3 -1524 -50 C ATOM 6121 CH2 TRP D 204 -21.983 -42.813 6.099 1.00 65.63 C ANISOU 6121 CH2 TRP D 204 10172 6467 8296 -42 -1768 34 C ATOM 6122 N GLN D 205 -16.771 -43.575 1.341 1.00 72.33 N ANISOU 6122 N GLN D 205 13057 5729 8696 793 -309 -591 N ATOM 6123 CA GLN D 205 -17.432 -43.699 0.041 1.00 75.79 C ANISOU 6123 CA GLN D 205 13883 6282 8631 619 -448 -756 C ATOM 6124 C GLN D 205 -17.563 -45.140 -0.467 1.00 80.01 C ANISOU 6124 C GLN D 205 14954 6493 8953 310 -411 -1049 C ATOM 6125 O GLN D 205 -18.122 -45.371 -1.533 1.00 84.06 O ANISOU 6125 O GLN D 205 15834 7120 8985 60 -542 -1238 O ATOM 6126 CB GLN D 205 -16.757 -42.786 -0.990 1.00 76.34 C ANISOU 6126 CB GLN D 205 14128 6370 8508 924 -196 -707 C ATOM 6127 CG GLN D 205 -17.072 -41.296 -0.769 1.00 73.92 C ANISOU 6127 CG GLN D 205 13432 6413 8242 1122 -282 -444 C ATOM 6128 CD GLN D 205 -16.024 -40.341 -1.341 1.00 73.57 C ANISOU 6128 CD GLN D 205 13488 6248 8216 1455 107 -343 C ATOM 6129 OE1 GLN D 205 -14.864 -40.709 -1.548 1.00 74.17 O ANISOU 6129 OE1 GLN D 205 13744 6016 8422 1583 464 -416 O ATOM 6130 NE2 GLN D 205 -16.433 -39.097 -1.583 1.00 72.69 N ANISOU 6130 NE2 GLN D 205 13256 6381 7980 1615 79 -140 N ATOM 6131 N ASN D 206 -17.064 -46.104 0.301 1.00 79.87 N ANISOU 6131 N ASN D 206 15008 6076 9262 313 -216 -1078 N ATOM 6132 CA ASN D 206 -17.265 -47.518 -0.011 1.00 84.34 C ANISOU 6132 CA ASN D 206 16144 6234 9668 -7 -123 -1351 C ATOM 6133 C ASN D 206 -18.488 -48.084 0.722 1.00 85.02 C ANISOU 6133 C ASN D 206 16064 6483 9756 -503 -510 -1387 C ATOM 6134 O ASN D 206 -18.507 -48.126 1.955 1.00 82.03 O ANISOU 6134 O ASN D 206 15274 6123 9771 -434 -563 -1185 O ATOM 6135 CB ASN D 206 -16.001 -48.329 0.315 1.00 85.16 C ANISOU 6135 CB ASN D 206 16501 5750 10105 347 404 -1315 C ATOM 6136 CG ASN D 206 -16.140 -49.819 -0.009 1.00 90.19 C ANISOU 6136 CG ASN D 206 17860 5817 10591 69 629 -1594 C ATOM 6137 OD1 ASN D 206 -16.943 -50.226 -0.849 1.00 93.88 O ANISOU 6137 OD1 ASN D 206 18791 6281 10598 -415 469 -1910 O ATOM 6138 ND2 ASN D 206 -15.337 -50.636 0.659 1.00 90.64 N ANISOU 6138 ND2 ASN D 206 18031 5396 11012 369 1029 -1465 N ATOM 6139 N PRO D 207 -19.518 -48.508 -0.038 1.00 89.45 N ANISOU 6139 N PRO D 207 16925 7221 9842 -1042 -788 -1635 N ATOM 6140 CA PRO D 207 -20.743 -49.123 0.492 1.00 91.46 C ANISOU 6140 CA PRO D 207 17050 7678 10022 -1629 -1153 -1699 C ATOM 6141 C PRO D 207 -20.546 -50.458 1.216 1.00 93.54 C ANISOU 6141 C PRO D 207 17665 7323 10552 -1825 -899 -1801 C ATOM 6142 O PRO D 207 -21.414 -50.858 1.994 1.00 93.95 O ANISOU 6142 O PRO D 207 17479 7523 10693 -2218 -1150 -1756 O ATOM 6143 CB PRO D 207 -21.600 -49.343 -0.764 1.00 97.24 C ANISOU 6143 CB PRO D 207 18143 8713 10089 -2181 -1419 -1988 C ATOM 6144 CG PRO D 207 -20.643 -49.292 -1.906 1.00 99.10 C ANISOU 6144 CG PRO D 207 18951 8620 10083 -1901 -1052 -2163 C ATOM 6145 CD PRO D 207 -19.621 -48.284 -1.490 1.00 93.20 C ANISOU 6145 CD PRO D 207 17807 7844 9762 -1157 -811 -1843 C ATOM 6146 N ARG D 208 -19.433 -51.142 0.953 1.00 95.47 N ANISOU 6146 N ARG D 208 18476 6884 10915 -1528 -370 -1903 N ATOM 6147 CA ARG D 208 -19.125 -52.416 1.614 1.00 98.15 C ANISOU 6147 CA ARG D 208 19217 6551 11524 -1582 -20 -1933 C ATOM 6148 C ARG D 208 -18.755 -52.223 3.091 1.00 93.41 C ANISOU 6148 C ARG D 208 18000 6007 11484 -1188 -2 -1526 C ATOM 6149 O ARG D 208 -18.780 -53.183 3.873 1.00 95.04 O ANISOU 6149 O ARG D 208 18379 5810 11922 -1277 172 -1459 O ATOM 6150 CB ARG D 208 -18.000 -53.155 0.875 1.00102.22 C ANISOU 6150 CB ARG D 208 20512 6330 11998 -1256 615 -2098 C ATOM 6151 CG ARG D 208 -18.399 -53.761 -0.466 1.00108.77 C ANISOU 6151 CG ARG D 208 22184 6908 12234 -1778 699 -2582 C ATOM 6152 CD ARG D 208 -17.177 -54.245 -1.230 1.00112.05 C ANISOU 6152 CD ARG D 208 23312 6649 12614 -1306 1384 -2702 C ATOM 6153 NE ARG D 208 -17.517 -55.168 -2.316 1.00120.23 N ANISOU 6153 NE ARG D 208 25358 7220 13105 -1863 1603 -3216 N ATOM 6154 CZ ARG D 208 -17.469 -56.499 -2.228 1.00126.15 C ANISOU 6154 CZ ARG D 208 26927 7144 13860 -2097 2064 -3439 C ATOM 6155 NH1 ARG D 208 -17.099 -57.090 -1.098 1.00125.17 N ANISOU 6155 NH1 ARG D 208 26699 6586 14272 -1762 2350 -3137 N ATOM 6156 NH2 ARG D 208 -17.793 -57.248 -3.276 1.00133.17 N ANISOU 6156 NH2 ARG D 208 28787 7626 14184 -2681 2268 -3962 N ATOM 6157 N ASN D 209 -18.416 -50.981 3.451 1.00 88.08 N ANISOU 6157 N ASN D 209 16656 5824 10988 -783 -160 -1260 N ATOM 6158 CA ASN D 209 -18.032 -50.607 4.816 1.00 83.80 C ANISOU 6158 CA ASN D 209 15494 5449 10896 -447 -178 -896 C ATOM 6159 C ASN D 209 -19.225 -50.430 5.742 1.00 82.17 C ANISOU 6159 C ASN D 209 14817 5661 10741 -828 -613 -799 C ATOM 6160 O ASN D 209 -20.308 -50.029 5.317 1.00 82.68 O ANISOU 6160 O ASN D 209 14758 6142 10516 -1216 -984 -919 O ATOM 6161 CB ASN D 209 -17.181 -49.336 4.816 1.00 79.55 C ANISOU 6161 CB ASN D 209 14502 5238 10486 41 -130 -702 C ATOM 6162 CG ASN D 209 -15.747 -49.586 4.374 1.00 81.04 C ANISOU 6162 CG ASN D 209 14958 5045 10787 533 377 -648 C ATOM 6163 OD1 ASN D 209 -15.260 -50.719 4.394 1.00 84.33 O ANISOU 6163 OD1 ASN D 209 15806 4938 11297 657 741 -653 O ATOM 6164 ND2 ASN D 209 -15.059 -48.519 3.979 1.00 78.80 N ANISOU 6164 ND2 ASN D 209 14424 5018 10499 836 447 -569 N ATOM 6165 N HIS D 210 -19.003 -50.717 7.018 1.00 80.84 N ANISOU 6165 N HIS D 210 14354 5436 10926 -683 -553 -542 N ATOM 6166 CA HIS D 210 -20.083 -50.854 7.988 1.00 80.64 C ANISOU 6166 CA HIS D 210 13987 5685 10968 -1052 -864 -444 C ATOM 6167 C HIS D 210 -19.711 -50.150 9.287 1.00 76.26 C ANISOU 6167 C HIS D 210 12799 5448 10727 -717 -914 -112 C ATOM 6168 O HIS D 210 -18.584 -50.276 9.775 1.00 75.52 O ANISOU 6168 O HIS D 210 12653 5171 10871 -296 -636 84 O ATOM 6169 CB HIS D 210 -20.365 -52.349 8.221 1.00 85.54 C ANISOU 6169 CB HIS D 210 15117 5763 11622 -1390 -681 -522 C ATOM 6170 CG HIS D 210 -21.405 -52.629 9.263 1.00 85.86 C ANISOU 6170 CG HIS D 210 14837 6033 11751 -1785 -937 -397 C ATOM 6171 ND1 HIS D 210 -22.751 -52.430 9.045 1.00 87.29 N ANISOU 6171 ND1 HIS D 210 14824 6663 11679 -2354 -1336 -530 N ATOM 6172 CD2 HIS D 210 -21.295 -53.121 10.521 1.00 85.62 C ANISOU 6172 CD2 HIS D 210 14636 5882 12015 -1687 -833 -120 C ATOM 6173 CE1 HIS D 210 -23.425 -52.772 10.129 1.00 87.41 C ANISOU 6173 CE1 HIS D 210 14556 6805 11850 -2597 -1450 -355 C ATOM 6174 NE2 HIS D 210 -22.565 -53.194 11.039 1.00 86.44 N ANISOU 6174 NE2 HIS D 210 14469 6321 12052 -2204 -1149 -114 N ATOM 6175 N PHE D 211 -20.656 -49.402 9.842 1.00 74.13 N ANISOU 6175 N PHE D 211 12041 5697 10427 -905 -1256 -37 N ATOM 6176 CA PHE D 211 -20.382 -48.617 11.038 1.00 70.60 C ANISOU 6176 CA PHE D 211 11048 5574 10204 -649 -1299 221 C ATOM 6177 C PHE D 211 -21.432 -48.872 12.093 1.00 70.89 C ANISOU 6177 C PHE D 211 10790 5846 10298 -954 -1511 344 C ATOM 6178 O PHE D 211 -22.604 -49.031 11.775 1.00 72.75 O ANISOU 6178 O PHE D 211 11020 6266 10355 -1352 -1740 241 O ATOM 6179 CB PHE D 211 -20.298 -47.125 10.700 1.00 67.41 C ANISOU 6179 CB PHE D 211 10347 5555 9711 -441 -1389 214 C ATOM 6180 CG PHE D 211 -19.237 -46.796 9.684 1.00 67.61 C ANISOU 6180 CG PHE D 211 10631 5380 9679 -149 -1157 118 C ATOM 6181 CD1 PHE D 211 -19.554 -46.709 8.329 1.00 69.78 C ANISOU 6181 CD1 PHE D 211 11234 5613 9668 -245 -1198 -90 C ATOM 6182 CD2 PHE D 211 -17.918 -46.590 10.075 1.00 66.45 C ANISOU 6182 CD2 PHE D 211 10373 5144 9730 199 -900 253 C ATOM 6183 CE1 PHE D 211 -18.574 -46.415 7.380 1.00 70.09 C ANISOU 6183 CE1 PHE D 211 11530 5464 9637 30 -951 -169 C ATOM 6184 CE2 PHE D 211 -16.929 -46.290 9.133 1.00 66.90 C ANISOU 6184 CE2 PHE D 211 10632 5048 9738 461 -657 188 C ATOM 6185 CZ PHE D 211 -17.259 -46.204 7.785 1.00 68.59 C ANISOU 6185 CZ PHE D 211 11217 5160 9683 389 -665 -28 C ATOM 6186 N ARG D 212 -20.991 -48.931 13.346 1.00 69.83 N ANISOU 6186 N ARG D 212 10389 5757 10387 -781 -1431 583 N ATOM 6187 CA ARG D 212 -21.869 -49.168 14.490 1.00 70.26 C ANISOU 6187 CA ARG D 212 10155 6034 10506 -1022 -1580 740 C ATOM 6188 C ARG D 212 -21.334 -48.440 15.720 1.00 67.48 C ANISOU 6188 C ARG D 212 9372 5982 10287 -754 -1554 963 C ATOM 6189 O ARG D 212 -20.123 -48.401 15.962 1.00 66.84 O ANISOU 6189 O ARG D 212 9277 5811 10310 -438 -1373 1075 O ATOM 6190 CB ARG D 212 -22.013 -50.671 14.760 1.00 74.18 C ANISOU 6190 CB ARG D 212 11009 6091 11085 -1252 -1447 793 C ATOM 6191 CG ARG D 212 -23.074 -51.038 15.786 1.00 75.28 C ANISOU 6191 CG ARG D 212 10908 6436 11259 -1595 -1592 938 C ATOM 6192 CD ARG D 212 -23.589 -52.457 15.586 1.00 81.17 C ANISOU 6192 CD ARG D 212 12126 6723 11992 -2026 -1490 872 C ATOM 6193 NE ARG D 212 -22.544 -53.473 15.727 1.00 84.91 N ANISOU 6193 NE ARG D 212 13053 6578 12630 -1753 -1113 998 N ATOM 6194 CZ ARG D 212 -22.145 -54.011 16.881 1.00 86.24 C ANISOU 6194 CZ ARG D 212 13149 6631 12987 -1546 -941 1336 C ATOM 6195 NH1 ARG D 212 -21.188 -54.931 16.879 1.00 89.63 N ANISOU 6195 NH1 ARG D 212 14004 6503 13550 -1217 -559 1497 N ATOM 6196 NH2 ARG D 212 -22.688 -53.637 18.038 1.00 84.37 N ANISOU 6196 NH2 ARG D 212 12425 6845 12786 -1625 -1119 1546 N ATOM 6197 N CYS D 213 -22.243 -47.852 16.486 1.00 66.54 N ANISOU 6197 N CYS D 213 8890 6263 10131 -900 -1725 1032 N ATOM 6198 CA CYS D 213 -21.858 -47.095 17.660 1.00 64.76 C ANISOU 6198 CA CYS D 213 8308 6340 9956 -730 -1697 1187 C ATOM 6199 C CYS D 213 -22.378 -47.800 18.899 1.00 66.06 C ANISOU 6199 C CYS D 213 8320 6595 10183 -901 -1729 1399 C ATOM 6200 O CYS D 213 -23.393 -47.399 19.462 1.00 66.17 O ANISOU 6200 O CYS D 213 8082 6922 10137 -1065 -1840 1433 O ATOM 6201 CB CYS D 213 -22.403 -45.667 17.579 1.00 62.77 C ANISOU 6201 CB CYS D 213 7819 6443 9586 -684 -1771 1095 C ATOM 6202 SG CYS D 213 -22.082 -44.696 19.061 1.00 62.02 S ANISOU 6202 SG CYS D 213 7392 6688 9484 -590 -1695 1208 S ATOM 6203 N GLN D 214 -21.679 -48.851 19.315 1.00 67.82 N ANISOU 6203 N GLN D 214 8701 6546 10521 -821 -1593 1577 N ATOM 6204 CA GLN D 214 -22.098 -49.688 20.441 1.00 69.66 C ANISOU 6204 CA GLN D 214 8865 6791 10812 -963 -1578 1825 C ATOM 6205 C GLN D 214 -21.988 -48.953 21.781 1.00 68.04 C ANISOU 6205 C GLN D 214 8249 7057 10547 -886 -1622 1994 C ATOM 6206 O GLN D 214 -20.958 -48.340 22.084 1.00 66.82 O ANISOU 6206 O GLN D 214 7943 7088 10358 -652 -1577 2038 O ATOM 6207 CB GLN D 214 -21.268 -50.968 20.466 1.00 72.70 C ANISOU 6207 CB GLN D 214 9577 6717 11327 -795 -1352 2024 C ATOM 6208 CG GLN D 214 -21.742 -52.007 21.443 1.00 76.02 C ANISOU 6208 CG GLN D 214 10053 7020 11811 -949 -1281 2297 C ATOM 6209 CD GLN D 214 -20.626 -52.518 22.332 1.00 78.40 C ANISOU 6209 CD GLN D 214 10294 7311 12183 -560 -1098 2693 C ATOM 6210 OE1 GLN D 214 -20.428 -53.728 22.463 1.00 82.85 O ANISOU 6210 OE1 GLN D 214 11192 7433 12855 -472 -864 2926 O ATOM 6211 NE2 GLN D 214 -19.893 -51.598 22.956 1.00 75.87 N ANISOU 6211 NE2 GLN D 214 9555 7495 11778 -335 -1186 2791 N ATOM 6212 N VAL D 215 -23.058 -49.019 22.577 1.00 68.55 N ANISOU 6212 N VAL D 215 8138 7340 10569 -1127 -1699 2079 N ATOM 6213 CA VAL D 215 -23.095 -48.373 23.900 1.00 67.46 C ANISOU 6213 CA VAL D 215 7669 7639 10324 -1100 -1712 2218 C ATOM 6214 C VAL D 215 -23.599 -49.322 25.001 1.00 69.89 C ANISOU 6214 C VAL D 215 7928 7981 10647 -1254 -1678 2510 C ATOM 6215 O VAL D 215 -24.767 -49.719 25.013 1.00 71.10 O ANISOU 6215 O VAL D 215 8075 8120 10821 -1536 -1714 2515 O ATOM 6216 CB VAL D 215 -23.915 -47.043 23.885 1.00 65.47 C ANISOU 6216 CB VAL D 215 7203 7724 9948 -1157 -1770 2022 C ATOM 6217 CG1 VAL D 215 -24.135 -46.507 25.299 1.00 65.30 C ANISOU 6217 CG1 VAL D 215 6932 8095 9784 -1187 -1725 2140 C ATOM 6218 CG2 VAL D 215 -23.224 -45.996 23.029 1.00 63.04 C ANISOU 6218 CG2 VAL D 215 6959 7389 9603 -966 -1744 1791 C ATOM 6219 N GLN D 216 -22.692 -49.681 25.908 1.00 70.95 N ANISOU 6219 N GLN D 216 8001 8206 10749 -1073 -1607 2783 N ATOM 6220 CA GLN D 216 -23.005 -50.506 27.073 1.00 73.54 C ANISOU 6220 CA GLN D 216 8279 8609 11053 -1154 -1549 3123 C ATOM 6221 C GLN D 216 -23.530 -49.627 28.209 1.00 72.71 C ANISOU 6221 C GLN D 216 7853 9039 10734 -1267 -1603 3132 C ATOM 6222 O GLN D 216 -22.825 -48.727 28.677 1.00 71.57 O ANISOU 6222 O GLN D 216 7535 9246 10413 -1155 -1632 3078 O ATOM 6223 CB GLN D 216 -21.755 -51.272 27.528 1.00 75.79 C ANISOU 6223 CB GLN D 216 8618 8821 11357 -838 -1438 3482 C ATOM 6224 CG GLN D 216 -21.944 -52.125 28.784 1.00 78.87 C ANISOU 6224 CG GLN D 216 8967 9311 11690 -849 -1355 3912 C ATOM 6225 CD GLN D 216 -22.627 -53.455 28.508 1.00 81.79 C ANISOU 6225 CD GLN D 216 9718 9103 12254 -1004 -1186 4051 C ATOM 6226 OE1 GLN D 216 -23.783 -53.664 28.879 1.00 82.65 O ANISOU 6226 OE1 GLN D 216 9819 9230 12356 -1353 -1192 4043 O ATOM 6227 NE2 GLN D 216 -21.910 -54.362 27.855 1.00 83.84 N ANISOU 6227 NE2 GLN D 216 10336 8839 12681 -761 -994 4177 N ATOM 6228 N PHE D 217 -24.763 -49.892 28.637 1.00 73.77 N ANISOU 6228 N PHE D 217 7928 9236 10866 -1521 -1589 3190 N ATOM 6229 CA PHE D 217 -25.383 -49.168 29.745 1.00 73.73 C ANISOU 6229 CA PHE D 217 7660 9700 10653 -1613 -1571 3221 C ATOM 6230 C PHE D 217 -25.482 -50.075 30.949 1.00 76.92 C ANISOU 6230 C PHE D 217 8038 10202 10987 -1677 -1492 3609 C ATOM 6231 O PHE D 217 -25.827 -51.247 30.811 1.00 79.50 O ANISOU 6231 O PHE D 217 8539 10191 11478 -1795 -1429 3807 O ATOM 6232 CB PHE D 217 -26.775 -48.656 29.354 1.00 73.27 C ANISOU 6232 CB PHE D 217 7474 9745 10622 -1802 -1578 3040 C ATOM 6233 CG PHE D 217 -27.622 -48.205 30.522 1.00 74.45 C ANISOU 6233 CG PHE D 217 7387 10309 10591 -1890 -1477 3143 C ATOM 6234 CD1 PHE D 217 -27.364 -47.001 31.170 1.00 73.62 C ANISOU 6234 CD1 PHE D 217 7195 10526 10251 -1758 -1395 3009 C ATOM 6235 CD2 PHE D 217 -28.691 -48.979 30.962 1.00 77.42 C ANISOU 6235 CD2 PHE D 217 7661 10739 11015 -2138 -1424 3359 C ATOM 6236 CE1 PHE D 217 -28.147 -46.581 32.247 1.00 75.11 C ANISOU 6236 CE1 PHE D 217 7227 11065 10245 -1818 -1241 3086 C ATOM 6237 CE2 PHE D 217 -29.476 -48.569 32.036 1.00 78.82 C ANISOU 6237 CE2 PHE D 217 7615 11314 11020 -2191 -1290 3472 C ATOM 6238 CZ PHE D 217 -29.202 -47.366 32.678 1.00 77.77 C ANISOU 6238 CZ PHE D 217 7423 11483 10643 -2004 -1188 3332 C ATOM 6239 N TYR D 218 -25.179 -49.528 32.125 1.00 77.51 N ANISOU 6239 N TYR D 218 7936 10727 10789 -1627 -1474 3711 N ATOM 6240 CA TYR D 218 -25.299 -50.265 33.384 1.00 80.84 C ANISOU 6240 CA TYR D 218 8308 11339 11069 -1673 -1396 4107 C ATOM 6241 C TYR D 218 -26.506 -49.763 34.154 1.00 81.66 C ANISOU 6241 C TYR D 218 8248 11762 11018 -1881 -1307 4065 C ATOM 6242 O TYR D 218 -26.620 -48.569 34.451 1.00 80.39 O ANISOU 6242 O TYR D 218 7976 11923 10647 -1876 -1282 3816 O ATOM 6243 CB TYR D 218 -24.022 -50.157 34.225 1.00 81.91 C ANISOU 6243 CB TYR D 218 8347 11838 10936 -1479 -1448 4320 C ATOM 6244 CG TYR D 218 -22.801 -50.714 33.526 1.00 82.09 C ANISOU 6244 CG TYR D 218 8465 11610 11114 -1202 -1492 4453 C ATOM 6245 CD1 TYR D 218 -21.996 -49.897 32.727 1.00 79.03 C ANISOU 6245 CD1 TYR D 218 8041 11247 10740 -1101 -1583 4151 C ATOM 6246 CD2 TYR D 218 -22.460 -52.062 33.646 1.00 85.42 C ANISOU 6246 CD2 TYR D 218 9041 11740 11675 -1014 -1386 4902 C ATOM 6247 CE1 TYR D 218 -20.885 -50.406 32.072 1.00 79.54 C ANISOU 6247 CE1 TYR D 218 8163 11111 10949 -816 -1584 4296 C ATOM 6248 CE2 TYR D 218 -21.346 -52.582 32.994 1.00 86.28 C ANISOU 6248 CE2 TYR D 218 9248 11602 11932 -680 -1355 5059 C ATOM 6249 CZ TYR D 218 -20.564 -51.746 32.211 1.00 83.48 C ANISOU 6249 CZ TYR D 218 8798 11336 11584 -581 -1462 4755 C ATOM 6250 OH TYR D 218 -19.461 -52.253 31.567 1.00 85.30 O ANISOU 6250 OH TYR D 218 9094 11359 11959 -221 -1395 4934 O ATOM 6251 N GLY D 219 -27.417 -50.687 34.440 1.00 84.37 N ANISOU 6251 N GLY D 219 8607 11981 11470 -2070 -1211 4309 N ATOM 6252 CA GLY D 219 -28.642 -50.386 35.165 1.00 85.96 C ANISOU 6252 CA GLY D 219 8615 12494 11552 -2263 -1086 4343 C ATOM 6253 C GLY D 219 -29.031 -51.537 36.068 1.00 90.01 C ANISOU 6253 C GLY D 219 9166 12988 12047 -2415 -957 4777 C ATOM 6254 O GLY D 219 -28.167 -52.210 36.630 1.00 91.83 O ANISOU 6254 O GLY D 219 9528 13171 12192 -2274 -947 5088 O ATOM 6255 N LEU D 220 -30.334 -51.761 36.202 1.00 92.07 N ANISOU 6255 N LEU D 220 9287 13317 12378 -2692 -841 4838 N ATOM 6256 CA LEU D 220 -30.860 -52.856 37.006 1.00 96.64 C ANISOU 6256 CA LEU D 220 9911 13848 12958 -2908 -676 5247 C ATOM 6257 C LEU D 220 -30.297 -54.201 36.556 1.00 98.90 C ANISOU 6257 C LEU D 220 10559 13541 13477 -2946 -657 5475 C ATOM 6258 O LEU D 220 -29.989 -54.392 35.375 1.00 97.44 O ANISOU 6258 O LEU D 220 10554 12946 13521 -2950 -758 5256 O ATOM 6259 CB LEU D 220 -32.388 -52.886 36.927 1.00 98.55 C ANISOU 6259 CB LEU D 220 9901 14249 13294 -3265 -569 5235 C ATOM 6260 CG LEU D 220 -33.219 -51.964 37.826 1.00 99.28 C ANISOU 6260 CG LEU D 220 9659 14927 13137 -3234 -411 5234 C ATOM 6261 CD1 LEU D 220 -32.925 -50.482 37.594 1.00 95.42 C ANISOU 6261 CD1 LEU D 220 9072 14687 12497 -2921 -459 4861 C ATOM 6262 CD2 LEU D 220 -34.700 -52.251 37.619 1.00102.09 C ANISOU 6262 CD2 LEU D 220 9712 15438 13640 -3599 -304 5317 C ATOM 6263 N SER D 221 -30.133 -55.116 37.508 1.00103.00 N ANISOU 6263 N SER D 221 11224 13997 13913 -2937 -488 5930 N ATOM 6264 CA SER D 221 -29.835 -56.506 37.188 1.00106.64 C ANISOU 6264 CA SER D 221 12098 13813 14607 -2991 -344 6214 C ATOM 6265 C SER D 221 -31.122 -57.312 37.357 1.00110.98 C ANISOU 6265 C SER D 221 12698 14189 15281 -3515 -140 6363 C ATOM 6266 O SER D 221 -32.161 -56.758 37.721 1.00111.15 O ANISOU 6266 O SER D 221 12361 14665 15206 -3769 -137 6276 O ATOM 6267 CB SER D 221 -28.709 -57.049 38.073 1.00109.02 C ANISOU 6267 CB SER D 221 12559 14124 14738 -2573 -251 6699 C ATOM 6268 OG SER D 221 -29.184 -57.399 39.359 1.00113.06 O ANISOU 6268 OG SER D 221 13001 14927 15031 -2660 -76 7109 O ATOM 6269 N GLU D 222 -31.060 -58.613 37.095 1.00115.26 N ANISOU 6269 N GLU D 222 13695 14067 16030 -3684 70 6596 N ATOM 6270 CA GLU D 222 -32.242 -59.465 37.190 1.00120.17 C ANISOU 6270 CA GLU D 222 14422 14462 16774 -4290 288 6721 C ATOM 6271 C GLU D 222 -32.484 -59.922 38.634 1.00124.40 C ANISOU 6271 C GLU D 222 14931 15213 17123 -4272 540 7252 C ATOM 6272 O GLU D 222 -32.856 -61.073 38.887 1.00129.93 O ANISOU 6272 O GLU D 222 15986 15447 17936 -4583 845 7573 O ATOM 6273 CB GLU D 222 -32.119 -60.641 36.217 1.00123.59 C ANISOU 6273 CB GLU D 222 15457 14010 17490 -4572 458 6674 C ATOM 6274 CG GLU D 222 -32.154 -60.210 34.745 1.00120.19 C ANISOU 6274 CG GLU D 222 15035 13432 17199 -4738 212 6116 C ATOM 6275 CD GLU D 222 -31.251 -61.045 33.849 1.00121.47 C ANISOU 6275 CD GLU D 222 15858 12748 17548 -4593 359 6059 C ATOM 6276 OE1 GLU D 222 -31.091 -62.258 34.108 1.00127.07 O ANISOU 6276 OE1 GLU D 222 17123 12798 18361 -4672 729 6387 O ATOM 6277 OE2 GLU D 222 -30.704 -60.483 32.875 1.00117.02 O ANISOU 6277 OE2 GLU D 222 15290 12149 17023 -4379 148 5696 O ATOM 6278 N ASN D 223 -32.272 -58.992 39.567 1.00122.25 N ANISOU 6278 N ASN D 223 14276 15635 16538 -3934 435 7325 N ATOM 6279 CA ASN D 223 -32.443 -59.213 41.008 1.00125.98 C ANISOU 6279 CA ASN D 223 14671 16463 16731 -3864 637 7802 C ATOM 6280 C ASN D 223 -33.391 -58.181 41.618 1.00124.71 C ANISOU 6280 C ASN D 223 14000 17044 16339 -4018 603 7637 C ATOM 6281 O ASN D 223 -34.024 -58.439 42.643 1.00128.44 O ANISOU 6281 O ASN D 223 14379 17786 16637 -4173 830 7967 O ATOM 6282 CB ASN D 223 -31.092 -59.123 41.736 1.00125.79 C ANISOU 6282 CB ASN D 223 14730 16636 16430 -3253 580 8119 C ATOM 6283 CG ASN D 223 -30.119 -60.224 41.330 1.00128.60 C ANISOU 6283 CG ASN D 223 15576 16300 16986 -2964 711 8440 C ATOM 6284 OD1 ASN D 223 -30.379 -61.414 41.538 1.00134.15 O ANISOU 6284 OD1 ASN D 223 16670 16471 17831 -3111 1041 8840 O ATOM 6285 ND2 ASN D 223 -28.979 -59.826 40.770 1.00124.92 N ANISOU 6285 ND2 ASN D 223 15110 15828 16527 -2532 500 8291 N ATOM 6286 N ASP D 224 -33.459 -57.010 40.985 1.00119.91 N ANISOU 6286 N ASP D 224 13096 16740 15725 -3931 365 7150 N ATOM 6287 CA ASP D 224 -34.278 -55.896 41.456 1.00118.86 C ANISOU 6287 CA ASP D 224 12521 17261 15378 -3960 384 6964 C ATOM 6288 C ASP D 224 -35.666 -56.000 40.841 1.00120.69 C ANISOU 6288 C ASP D 224 12476 17530 15850 -4441 448 6840 C ATOM 6289 O ASP D 224 -35.798 -56.102 39.618 1.00119.21 O ANISOU 6289 O ASP D 224 12310 17050 15935 -4630 282 6564 O ATOM 6290 CB ASP D 224 -33.647 -54.546 41.072 1.00113.56 C ANISOU 6290 CB ASP D 224 11715 16859 14573 -3598 157 6529 C ATOM 6291 CG ASP D 224 -32.116 -54.573 41.072 1.00111.41 C ANISOU 6291 CG ASP D 224 11708 16430 14194 -3220 -14 6557 C ATOM 6292 OD1 ASP D 224 -31.506 -54.098 42.052 1.00111.52 O ANISOU 6292 OD1 ASP D 224 11694 16858 13819 -2988 -16 6662 O ATOM 6293 OD2 ASP D 224 -31.520 -55.059 40.086 1.00109.77 O ANISOU 6293 OD2 ASP D 224 11720 15726 14260 -3170 -140 6477 O ATOM 6294 N GLU D 225 -36.695 -55.971 41.687 1.00124.48 N ANISOU 6294 N GLU D 225 12668 18431 16196 -4649 687 7058 N ATOM 6295 CA GLU D 225 -38.086 -56.109 41.234 1.00127.59 C ANISOU 6295 CA GLU D 225 12687 19013 16780 -5142 766 7030 C ATOM 6296 C GLU D 225 -38.602 -54.849 40.521 1.00124.63 C ANISOU 6296 C GLU D 225 11861 19073 16419 -4982 620 6650 C ATOM 6297 O GLU D 225 -38.352 -53.727 40.967 1.00122.01 O ANISOU 6297 O GLU D 225 11416 19090 15851 -4528 654 6509 O ATOM 6298 CB GLU D 225 -39.000 -56.480 42.408 1.00132.87 C ANISOU 6298 CB GLU D 225 13153 20039 17293 -5383 1111 7436 C ATOM 6299 N TRP D 226 -39.319 -55.049 39.415 1.00125.84 N ANISOU 6299 N TRP D 226 11789 19201 16822 -5369 479 6499 N ATOM 6300 CA TRP D 226 -39.880 -53.949 38.619 1.00124.01 C ANISOU 6300 CA TRP D 226 11100 19401 16616 -5208 340 6218 C ATOM 6301 C TRP D 226 -41.409 -54.021 38.535 1.00129.14 C ANISOU 6301 C TRP D 226 11125 20622 17321 -5630 454 6396 C ATOM 6302 O TRP D 226 -41.999 -55.098 38.688 1.00134.12 O ANISOU 6302 O TRP D 226 11734 21181 18046 -6239 547 6632 O ATOM 6303 CB TRP D 226 -39.276 -53.958 37.214 1.00120.72 C ANISOU 6303 CB TRP D 226 10903 18579 16388 -5223 3 5870 C ATOM 6304 CG TRP D 226 -39.579 -52.723 36.402 1.00118.72 C ANISOU 6304 CG TRP D 226 10277 18709 16123 -4908 -143 5598 C ATOM 6305 CD1 TRP D 226 -40.395 -52.639 35.306 1.00120.80 C ANISOU 6305 CD1 TRP D 226 10159 19236 16502 -5188 -327 5499 C ATOM 6306 CD2 TRP D 226 -39.065 -51.401 36.622 1.00114.95 C ANISOU 6306 CD2 TRP D 226 9798 18395 15482 -4263 -95 5415 C ATOM 6307 NE1 TRP D 226 -40.418 -51.348 34.830 1.00118.01 N ANISOU 6307 NE1 TRP D 226 9560 19193 16084 -4676 -382 5316 N ATOM 6308 CE2 TRP D 226 -39.613 -50.568 35.619 1.00114.31 C ANISOU 6308 CE2 TRP D 226 9356 18618 15460 -4118 -215 5242 C ATOM 6309 CE3 TRP D 226 -38.198 -50.839 37.569 1.00112.26 C ANISOU 6309 CE3 TRP D 226 9743 17992 14918 -3835 48 5380 C ATOM 6310 CZ2 TRP D 226 -39.323 -49.204 35.539 1.00111.09 C ANISOU 6310 CZ2 TRP D 226 8927 18350 14933 -3526 -139 5046 C ATOM 6311 CZ3 TRP D 226 -37.911 -49.484 37.487 1.00109.28 C ANISOU 6311 CZ3 TRP D 226 9347 17775 14400 -3341 100 5128 C ATOM 6312 CH2 TRP D 226 -38.473 -48.682 36.479 1.00108.71 C ANISOU 6312 CH2 TRP D 226 8973 17903 14429 -3173 35 4967 C ATOM 6313 N THR D 227 -42.044 -52.873 38.292 1.00128.52 N ANISOU 6313 N THR D 227 10535 21119 17176 -5304 475 6310 N ATOM 6314 CA THR D 227 -43.507 -52.797 38.237 1.00133.83 C ANISOU 6314 CA THR D 227 10485 22492 17873 -5593 598 6541 C ATOM 6315 C THR D 227 -44.058 -51.961 37.079 1.00133.34 C ANISOU 6315 C THR D 227 9925 22869 17871 -5430 393 6387 C ATOM 6316 O THR D 227 -45.086 -52.312 36.499 1.00138.08 O ANISOU 6316 O THR D 227 9980 23936 18548 -5917 289 6529 O ATOM 6317 CB THR D 227 -44.113 -52.264 39.564 1.00136.64 C ANISOU 6317 CB THR D 227 10544 23358 18015 -5280 1042 6830 C ATOM 6318 OG1 THR D 227 -43.319 -51.178 40.058 1.00132.14 O ANISOU 6318 OG1 THR D 227 10280 22688 17241 -4563 1167 6633 O ATOM 6319 CG2 THR D 227 -44.188 -53.370 40.621 1.00140.40 C ANISOU 6319 CG2 THR D 227 11236 23667 18442 -5707 1267 7150 C ATOM 6320 N GLN D 228 -43.377 -50.867 36.745 1.00128.23 N ANISOU 6320 N GLN D 228 9456 22103 17163 -4775 337 6122 N ATOM 6321 CA GLN D 228 -43.928 -49.870 35.817 1.00128.21 C ANISOU 6321 CA GLN D 228 8975 22566 17172 -4440 244 6057 C ATOM 6322 C GLN D 228 -44.129 -50.355 34.376 1.00128.93 C ANISOU 6322 C GLN D 228 8909 22677 17402 -4911 -189 5928 C ATOM 6323 O GLN D 228 -43.555 -51.364 33.962 1.00127.98 O ANISOU 6323 O GLN D 228 9238 22008 17382 -5423 -424 5765 O ATOM 6324 CB GLN D 228 -43.126 -48.563 35.869 1.00123.17 C ANISOU 6324 CB GLN D 228 8656 21720 16422 -3643 363 5805 C ATOM 6325 CG GLN D 228 -43.292 -47.787 37.183 1.00124.34 C ANISOU 6325 CG GLN D 228 8810 22078 16356 -3156 856 5932 C ATOM 6326 CD GLN D 228 -44.757 -47.579 37.588 1.00130.88 C ANISOU 6326 CD GLN D 228 8895 23688 17146 -3111 1183 6333 C ATOM 6327 OE1 GLN D 228 -45.590 -47.154 36.782 1.00133.56 O ANISOU 6327 OE1 GLN D 228 8650 24538 17557 -2984 1131 6473 O ATOM 6328 NE2 GLN D 228 -45.067 -47.875 38.847 1.00133.46 N ANISOU 6328 NE2 GLN D 228 9213 24159 17336 -3191 1532 6558 N ATOM 6329 N ASP D 229 -44.953 -49.614 33.634 1.00131.25 N ANISOU 6329 N ASP D 229 8579 23621 17669 -4705 -258 6024 N ATOM 6330 CA ASP D 229 -45.463 -50.027 32.318 1.00134.04 C ANISOU 6330 CA ASP D 229 8585 24279 18064 -5222 -664 5986 C ATOM 6331 C ASP D 229 -44.409 -50.198 31.231 1.00129.18 C ANISOU 6331 C ASP D 229 8571 23009 17502 -5290 -1025 5571 C ATOM 6332 O ASP D 229 -44.471 -51.143 30.444 1.00131.29 O ANISOU 6332 O ASP D 229 8942 23141 17803 -6009 -1328 5443 O ATOM 6333 CB ASP D 229 -46.556 -49.067 31.840 1.00138.08 C ANISOU 6333 CB ASP D 229 8234 25744 18487 -4841 -633 6267 C ATOM 6334 CG ASP D 229 -47.903 -49.342 32.489 1.00145.65 C ANISOU 6334 CG ASP D 229 8384 27552 19406 -5141 -413 6732 C ATOM 6335 OD1 ASP D 229 -48.931 -49.013 31.863 1.00151.13 O ANISOU 6335 OD1 ASP D 229 8247 29146 20031 -5155 -520 7015 O ATOM 6336 OD2 ASP D 229 -47.941 -49.884 33.617 1.00146.70 O ANISOU 6336 OD2 ASP D 229 8674 27506 19559 -5355 -130 6850 O ATOM 6337 N ARG D 230 -43.462 -49.268 31.179 1.00123.25 N ANISOU 6337 N ARG D 230 8230 21863 16738 -4571 -959 5352 N ATOM 6338 CA ARG D 230 -42.323 -49.382 30.271 1.00118.31 C ANISOU 6338 CA ARG D 230 8215 20573 16166 -4556 -1236 4968 C ATOM 6339 C ARG D 230 -41.390 -50.513 30.713 1.00116.26 C ANISOU 6339 C ARG D 230 8640 19532 16000 -4943 -1244 4823 C ATOM 6340 O ARG D 230 -41.397 -50.919 31.880 1.00117.18 O ANISOU 6340 O ARG D 230 8848 19559 16117 -5011 -995 5003 O ATOM 6341 CB ARG D 230 -41.564 -48.047 30.149 1.00113.25 C ANISOU 6341 CB ARG D 230 7808 19743 15479 -3716 -1122 4794 C ATOM 6342 CG ARG D 230 -41.464 -47.235 31.445 1.00112.16 C ANISOU 6342 CG ARG D 230 7717 19640 15259 -3157 -687 4901 C ATOM 6343 CD ARG D 230 -40.507 -46.060 31.315 1.00106.84 C ANISOU 6343 CD ARG D 230 7459 18607 14528 -2494 -571 4640 C ATOM 6344 NE ARG D 230 -39.117 -46.479 31.483 1.00101.94 N ANISOU 6344 NE ARG D 230 7511 17284 13938 -2588 -682 4355 N ATOM 6345 CZ ARG D 230 -38.424 -46.372 32.613 1.00 99.86 C ANISOU 6345 CZ ARG D 230 7596 16771 13575 -2443 -465 4310 C ATOM 6346 NH1 ARG D 230 -38.976 -45.847 33.700 1.00101.88 N ANISOU 6346 NH1 ARG D 230 7677 17349 13682 -2214 -97 4478 N ATOM 6347 NH2 ARG D 230 -37.165 -46.786 32.650 1.00 96.22 N ANISOU 6347 NH2 ARG D 230 7648 15778 13134 -2519 -607 4111 N ATOM 6348 N ALA D 231 -40.605 -51.021 29.765 1.00113.92 N ANISOU 6348 N ALA D 231 8827 18690 15769 -5161 -1502 4531 N ATOM 6349 CA ALA D 231 -39.667 -52.116 30.010 1.00112.50 C ANISOU 6349 CA ALA D 231 9329 17725 15690 -5448 -1481 4423 C ATOM 6350 C ALA D 231 -38.665 -51.773 31.110 1.00108.13 C ANISOU 6350 C ALA D 231 9129 16831 15124 -4899 -1249 4459 C ATOM 6351 O ALA D 231 -38.226 -50.624 31.222 1.00104.32 O ANISOU 6351 O ALA D 231 8616 16456 14565 -4293 -1196 4361 O ATOM 6352 CB ALA D 231 -38.937 -52.481 28.720 1.00110.79 C ANISOU 6352 CB ALA D 231 9571 17003 15522 -5605 -1739 4089 C ATOM 6353 N LYS D 232 -38.318 -52.772 31.920 1.00109.22 N ANISOU 6353 N LYS D 232 9613 16579 15308 -5142 -1100 4613 N ATOM 6354 CA LYS D 232 -37.328 -52.592 32.979 1.00106.04 C ANISOU 6354 CA LYS D 232 9531 15922 14838 -4692 -921 4690 C ATOM 6355 C LYS D 232 -35.957 -52.235 32.398 1.00100.92 C ANISOU 6355 C LYS D 232 9311 14822 14213 -4284 -1059 4419 C ATOM 6356 O LYS D 232 -35.474 -52.904 31.479 1.00100.68 O ANISOU 6356 O LYS D 232 9626 14318 14309 -4478 -1200 4267 O ATOM 6357 CB LYS D 232 -37.251 -53.818 33.905 1.00109.41 C ANISOU 6357 CB LYS D 232 10235 16043 15294 -5016 -730 4985 C ATOM 6358 CG LYS D 232 -36.676 -55.103 33.294 1.00110.72 C ANISOU 6358 CG LYS D 232 10963 15480 15625 -5374 -776 4944 C ATOM 6359 CD LYS D 232 -36.658 -56.263 34.304 1.00114.49 C ANISOU 6359 CD LYS D 232 11734 15644 16123 -5626 -505 5310 C ATOM 6360 CE LYS D 232 -35.741 -55.990 35.503 1.00111.83 C ANISOU 6360 CE LYS D 232 11537 15321 15634 -5062 -364 5536 C ATOM 6361 NZ LYS D 232 -35.613 -57.159 36.420 1.00115.53 N ANISOU 6361 NZ LYS D 232 12338 15452 16106 -5230 -97 5948 N ATOM 6362 N PRO D 233 -35.344 -51.156 32.918 1.00 97.25 N ANISOU 6362 N PRO D 233 8835 14511 13606 -3749 -990 4344 N ATOM 6363 CA PRO D 233 -34.055 -50.679 32.429 1.00 92.74 C ANISOU 6363 CA PRO D 233 8591 13615 13032 -3381 -1105 4098 C ATOM 6364 C PRO D 233 -32.884 -51.509 32.961 1.00 92.32 C ANISOU 6364 C PRO D 233 8955 13136 12985 -3321 -1074 4231 C ATOM 6365 O PRO D 233 -32.237 -51.125 33.936 1.00 91.32 O ANISOU 6365 O PRO D 233 8871 13149 12676 -3050 -983 4320 O ATOM 6366 CB PRO D 233 -34.000 -49.237 32.940 1.00 90.59 C ANISOU 6366 CB PRO D 233 8141 13715 12565 -2948 -984 3991 C ATOM 6367 CG PRO D 233 -34.867 -49.218 34.141 1.00 93.76 C ANISOU 6367 CG PRO D 233 8279 14518 12826 -3018 -745 4247 C ATOM 6368 CD PRO D 233 -35.885 -50.302 33.993 1.00 97.97 C ANISOU 6368 CD PRO D 233 8613 15107 13504 -3509 -763 4473 C ATOM 6369 N VAL D 234 -32.624 -52.645 32.319 1.00 93.79 N ANISOU 6369 N VAL D 234 9457 12826 13353 -3572 -1127 4260 N ATOM 6370 CA VAL D 234 -31.521 -53.521 32.717 1.00 94.41 C ANISOU 6370 CA VAL D 234 9943 12464 13465 -3434 -1047 4458 C ATOM 6371 C VAL D 234 -30.210 -53.091 32.076 1.00 90.77 C ANISOU 6371 C VAL D 234 9687 11781 13020 -3037 -1162 4258 C ATOM 6372 O VAL D 234 -30.200 -52.253 31.170 1.00 87.89 O ANISOU 6372 O VAL D 234 9230 11491 12672 -2946 -1303 3936 O ATOM 6373 CB VAL D 234 -31.778 -55.012 32.360 1.00 98.68 C ANISOU 6373 CB VAL D 234 10845 12453 14196 -3848 -941 4606 C ATOM 6374 CG1 VAL D 234 -32.873 -55.601 33.235 1.00102.99 C ANISOU 6374 CG1 VAL D 234 11233 13186 14712 -4255 -770 4895 C ATOM 6375 CG2 VAL D 234 -32.095 -55.178 30.873 1.00 98.83 C ANISOU 6375 CG2 VAL D 234 10998 12199 14355 -4150 -1085 4268 C ATOM 6376 N THR D 235 -29.110 -53.664 32.563 1.00 91.42 N ANISOU 6376 N THR D 235 10018 11632 13085 -2781 -1084 4496 N ATOM 6377 CA THR D 235 -27.822 -53.551 31.895 1.00 89.15 C ANISOU 6377 CA THR D 235 9934 11089 12851 -2435 -1154 4384 C ATOM 6378 C THR D 235 -27.957 -54.210 30.528 1.00 89.84 C ANISOU 6378 C THR D 235 10348 10616 13172 -2627 -1160 4180 C ATOM 6379 O THR D 235 -28.368 -55.373 30.421 1.00 93.82 O ANISOU 6379 O THR D 235 11152 10692 13805 -2917 -1011 4323 O ATOM 6380 CB THR D 235 -26.701 -54.218 32.705 1.00 91.22 C ANISOU 6380 CB THR D 235 10345 11268 13047 -2109 -1041 4791 C ATOM 6381 OG1 THR D 235 -26.555 -53.538 33.956 1.00 91.29 O ANISOU 6381 OG1 THR D 235 10050 11878 12757 -1992 -1071 4941 O ATOM 6382 CG2 THR D 235 -25.376 -54.173 31.947 1.00 89.48 C ANISOU 6382 CG2 THR D 235 10282 10815 12902 -1736 -1083 4721 C ATOM 6383 N GLN D 236 -27.628 -53.445 29.491 1.00 86.37 N ANISOU 6383 N GLN D 236 9888 10172 12755 -2503 -1307 3831 N ATOM 6384 CA GLN D 236 -27.876 -53.843 28.111 1.00 86.64 C ANISOU 6384 CA GLN D 236 10196 9792 12931 -2729 -1350 3561 C ATOM 6385 C GLN D 236 -27.014 -53.030 27.155 1.00 82.82 C ANISOU 6385 C GLN D 236 9744 9278 12444 -2410 -1461 3278 C ATOM 6386 O GLN D 236 -26.423 -52.021 27.541 1.00 79.70 O ANISOU 6386 O GLN D 236 9108 9235 11940 -2097 -1520 3249 O ATOM 6387 CB GLN D 236 -29.352 -53.632 27.766 1.00 87.76 C ANISOU 6387 CB GLN D 236 10093 10208 13045 -3202 -1466 3403 C ATOM 6388 CG GLN D 236 -29.808 -52.176 27.877 1.00 84.31 C ANISOU 6388 CG GLN D 236 9178 10385 12472 -3039 -1604 3262 C ATOM 6389 CD GLN D 236 -31.205 -51.948 27.336 1.00 85.51 C ANISOU 6389 CD GLN D 236 9029 10868 12593 -3414 -1721 3156 C ATOM 6390 OE1 GLN D 236 -31.985 -51.198 27.916 1.00 85.17 O ANISOU 6390 OE1 GLN D 236 8566 11341 12454 -3374 -1710 3234 O ATOM 6391 NE2 GLN D 236 -31.525 -52.592 26.218 1.00 87.17 N ANISOU 6391 NE2 GLN D 236 9447 10818 12857 -3781 -1818 2988 N ATOM 6392 N ILE D 237 -26.951 -53.480 25.906 1.00 83.45 N ANISOU 6392 N ILE D 237 10159 8931 12618 -2538 -1466 3055 N ATOM 6393 CA ILE D 237 -26.231 -52.761 24.870 1.00 80.29 C ANISOU 6393 CA ILE D 237 9817 8480 12208 -2276 -1552 2781 C ATOM 6394 C ILE D 237 -27.193 -52.205 23.827 1.00 79.75 C ANISOU 6394 C ILE D 237 9640 8589 12071 -2565 -1741 2467 C ATOM 6395 O ILE D 237 -27.906 -52.952 23.153 1.00 82.91 O ANISOU 6395 O ILE D 237 10251 8772 12478 -2995 -1766 2357 O ATOM 6396 CB ILE D 237 -25.142 -53.631 24.205 1.00 81.77 C ANISOU 6396 CB ILE D 237 10499 8056 12515 -2062 -1367 2797 C ATOM 6397 CG1 ILE D 237 -23.955 -53.801 25.153 1.00 81.58 C ANISOU 6397 CG1 ILE D 237 10421 8060 12515 -1597 -1220 3152 C ATOM 6398 CG2 ILE D 237 -24.677 -53.000 22.898 1.00 79.57 C ANISOU 6398 CG2 ILE D 237 10326 7693 12213 -1922 -1447 2464 C ATOM 6399 CD1 ILE D 237 -22.811 -54.617 24.587 1.00 83.58 C ANISOU 6399 CD1 ILE D 237 11093 7770 12892 -1253 -977 3261 C ATOM 6400 N VAL D 238 -27.209 -50.882 23.721 1.00 76.40 N ANISOU 6400 N VAL D 238 8894 8583 11552 -2340 -1858 2341 N ATOM 6401 CA VAL D 238 -27.950 -50.186 22.686 1.00 76.00 C ANISOU 6401 CA VAL D 238 8707 8756 11412 -2458 -2023 2108 C ATOM 6402 C VAL D 238 -26.923 -49.654 21.699 1.00 73.72 C ANISOU 6402 C VAL D 238 8635 8257 11119 -2141 -2022 1899 C ATOM 6403 O VAL D 238 -25.865 -49.186 22.115 1.00 71.50 O ANISOU 6403 O VAL D 238 8354 7949 10863 -1789 -1926 1941 O ATOM 6404 CB VAL D 238 -28.734 -49.001 23.271 1.00 74.55 C ANISOU 6404 CB VAL D 238 8046 9154 11125 -2348 -2068 2163 C ATOM 6405 CG1 VAL D 238 -29.816 -48.549 22.310 1.00 76.00 C ANISOU 6405 CG1 VAL D 238 8012 9656 11209 -2510 -2231 2056 C ATOM 6406 CG2 VAL D 238 -29.346 -49.374 24.608 1.00 76.41 C ANISOU 6406 CG2 VAL D 238 8061 9607 11363 -2504 -1985 2420 C ATOM 6407 N SER D 239 -27.214 -49.747 20.402 1.00 75.01 N ANISOU 6407 N SER D 239 8973 8308 11218 -2304 -2126 1684 N ATOM 6408 CA SER D 239 -26.321 -49.202 19.371 1.00 73.31 C ANISOU 6408 CA SER D 239 8967 7915 10972 -2014 -2109 1487 C ATOM 6409 C SER D 239 -27.025 -48.876 18.051 1.00 74.84 C ANISOU 6409 C SER D 239 9178 8259 10998 -2189 -2284 1282 C ATOM 6410 O SER D 239 -28.012 -49.517 17.684 1.00 78.34 O ANISOU 6410 O SER D 239 9622 8796 11346 -2643 -2420 1244 O ATOM 6411 CB SER D 239 -25.135 -50.138 19.118 1.00 73.97 C ANISOU 6411 CB SER D 239 9508 7427 11171 -1887 -1921 1478 C ATOM 6412 OG SER D 239 -25.395 -51.037 18.065 1.00 77.38 O ANISOU 6412 OG SER D 239 10359 7490 11551 -2198 -1916 1295 O ATOM 6413 N ALA D 240 -26.500 -47.878 17.344 1.00 73.00 N ANISOU 6413 N ALA D 240 8953 8084 10699 -1858 -2280 1167 N ATOM 6414 CA ALA D 240 -26.996 -47.505 16.017 1.00 74.68 C ANISOU 6414 CA ALA D 240 9209 8454 10713 -1939 -2434 1008 C ATOM 6415 C ALA D 240 -25.929 -47.767 14.955 1.00 74.78 C ANISOU 6415 C ALA D 240 9696 8016 10700 -1812 -2330 805 C ATOM 6416 O ALA D 240 -24.765 -48.009 15.285 1.00 73.30 O ANISOU 6416 O ALA D 240 9714 7464 10674 -1567 -2123 822 O ATOM 6417 CB ALA D 240 -27.431 -46.043 15.999 1.00 72.88 C ANISOU 6417 CB ALA D 240 8609 8687 10394 -1623 -2469 1089 C ATOM 6418 N GLU D 241 -26.327 -47.722 13.686 1.00 77.27 N ANISOU 6418 N GLU D 241 10159 8412 10788 -1969 -2467 639 N ATOM 6419 CA GLU D 241 -25.405 -47.993 12.586 1.00 78.29 C ANISOU 6419 CA GLU D 241 10777 8126 10845 -1872 -2346 429 C ATOM 6420 C GLU D 241 -25.712 -47.204 11.309 1.00 79.22 C ANISOU 6420 C GLU D 241 10897 8527 10676 -1811 -2488 319 C ATOM 6421 O GLU D 241 -26.869 -46.881 11.031 1.00 81.37 O ANISOU 6421 O GLU D 241 10862 9316 10740 -2018 -2741 381 O ATOM 6422 CB GLU D 241 -25.351 -49.499 12.290 1.00 82.33 C ANISOU 6422 CB GLU D 241 11790 8152 11339 -2278 -2265 275 C ATOM 6423 CG GLU D 241 -26.657 -50.125 11.809 1.00 87.94 C ANISOU 6423 CG GLU D 241 12517 9103 11795 -2934 -2517 158 C ATOM 6424 CD GLU D 241 -26.755 -51.600 12.156 1.00 92.91 C ANISOU 6424 CD GLU D 241 13565 9235 12500 -3392 -2372 87 C ATOM 6425 OE1 GLU D 241 -25.701 -52.238 12.374 1.00 93.34 O ANISOU 6425 OE1 GLU D 241 14050 8661 12753 -3141 -2040 89 O ATOM 6426 OE2 GLU D 241 -27.888 -52.124 12.217 1.00 97.07 O ANISOU 6426 OE2 GLU D 241 13986 10009 12886 -4000 -2563 57 O ATOM 6427 N ALA D 242 -24.660 -46.902 10.547 1.00 78.30 N ANISOU 6427 N ALA D 242 11097 8115 10540 -1506 -2311 201 N ATOM 6428 CA ALA D 242 -24.785 -46.331 9.201 1.00 79.95 C ANISOU 6428 CA ALA D 242 11437 8496 10443 -1450 -2398 88 C ATOM 6429 C ALA D 242 -23.892 -47.080 8.210 1.00 82.04 C ANISOU 6429 C ALA D 242 12313 8248 10611 -1487 -2211 -161 C ATOM 6430 O ALA D 242 -22.900 -47.700 8.601 1.00 81.45 O ANISOU 6430 O ALA D 242 12497 7679 10771 -1343 -1936 -184 O ATOM 6431 CB ALA D 242 -24.449 -44.844 9.210 1.00 76.75 C ANISOU 6431 CB ALA D 242 10781 8305 10074 -953 -2309 233 C ATOM 6432 N TRP D 243 -24.252 -47.025 6.930 1.00 85.27 N ANISOU 6432 N TRP D 243 12944 8808 10646 -1656 -2341 -321 N ATOM 6433 CA TRP D 243 -23.481 -47.684 5.879 1.00 87.98 C ANISOU 6433 CA TRP D 243 13922 8680 10825 -1701 -2135 -586 C ATOM 6434 C TRP D 243 -22.816 -46.666 4.960 1.00 86.86 C ANISOU 6434 C TRP D 243 13855 8604 10544 -1277 -2020 -581 C ATOM 6435 O TRP D 243 -23.317 -45.550 4.795 1.00 85.92 O ANISOU 6435 O TRP D 243 13368 8971 10305 -1097 -2190 -412 O ATOM 6436 CB TRP D 243 -24.384 -48.605 5.063 1.00 93.76 C ANISOU 6436 CB TRP D 243 14981 9490 11153 -2357 -2347 -839 C ATOM 6437 CG TRP D 243 -24.859 -49.807 5.816 1.00 96.31 C ANISOU 6437 CG TRP D 243 15423 9567 11603 -2846 -2352 -902 C ATOM 6438 CD1 TRP D 243 -25.813 -49.839 6.796 1.00 95.98 C ANISOU 6438 CD1 TRP D 243 14883 9900 11684 -3097 -2583 -715 C ATOM 6439 CD2 TRP D 243 -24.413 -51.157 5.645 1.00100.09 C ANISOU 6439 CD2 TRP D 243 16604 9333 12092 -3133 -2059 -1153 C ATOM 6440 NE1 TRP D 243 -25.984 -51.125 7.248 1.00 99.31 N ANISOU 6440 NE1 TRP D 243 15645 9895 12195 -3558 -2470 -832 N ATOM 6441 CE2 TRP D 243 -25.140 -51.955 6.558 1.00101.96 C ANISOU 6441 CE2 TRP D 243 16745 9529 12466 -3582 -2134 -1100 C ATOM 6442 CE3 TRP D 243 -23.469 -51.771 4.809 1.00102.43 C ANISOU 6442 CE3 TRP D 243 17637 8990 12293 -3029 -1685 -1404 C ATOM 6443 CZ2 TRP D 243 -24.951 -53.337 6.660 1.00106.23 C ANISOU 6443 CZ2 TRP D 243 17942 9364 13057 -3937 -1836 -1286 C ATOM 6444 CZ3 TRP D 243 -23.282 -53.144 4.911 1.00106.90 C ANISOU 6444 CZ3 TRP D 243 18858 8851 12907 -3340 -1369 -1592 C ATOM 6445 CH2 TRP D 243 -24.020 -53.912 5.832 1.00108.94 C ANISOU 6445 CH2 TRP D 243 19045 9039 13310 -3794 -1441 -1530 C ATOM 6446 N GLY D 244 -21.689 -47.057 4.365 1.00 87.70 N ANISOU 6446 N GLY D 244 14452 8204 10665 -1088 -1687 -737 N ATOM 6447 CA GLY D 244 -20.973 -46.221 3.397 1.00 87.33 C ANISOU 6447 CA GLY D 244 14554 8162 10466 -725 -1522 -751 C ATOM 6448 C GLY D 244 -21.792 -45.875 2.162 1.00 90.96 C ANISOU 6448 C GLY D 244 15125 9033 10403 -936 -1782 -843 C ATOM 6449 O GLY D 244 -22.587 -46.688 1.682 1.00 95.31 O ANISOU 6449 O GLY D 244 15903 9687 10625 -1453 -1998 -1039 O ATOM 6450 N ARG D 245 -21.593 -44.663 1.650 1.00 89.74 N ANISOU 6450 N ARG D 245 14819 9135 10144 -563 -1751 -689 N ATOM 6451 CA ARG D 245 -22.384 -44.141 0.534 1.00 93.34 C ANISOU 6451 CA ARG D 245 15282 10095 10087 -654 -2008 -663 C ATOM 6452 C ARG D 245 -21.540 -43.823 -0.695 1.00 94.92 C ANISOU 6452 C ARG D 245 15934 10106 10026 -409 -1751 -762 C ATOM 6453 O ARG D 245 -20.457 -43.243 -0.588 1.00 91.93 O ANISOU 6453 O ARG D 245 15596 9417 9916 20 -1395 -683 O ATOM 6454 CB ARG D 245 -23.149 -42.884 0.968 1.00 91.61 C ANISOU 6454 CB ARG D 245 14469 10430 9909 -383 -2196 -300 C ATOM 6455 CG ARG D 245 -24.607 -43.118 1.363 1.00 93.97 C ANISOU 6455 CG ARG D 245 14330 11316 10058 -745 -2625 -180 C ATOM 6456 CD ARG D 245 -25.056 -42.174 2.479 1.00 90.72 C ANISOU 6456 CD ARG D 245 13341 11160 9967 -416 -2629 159 C ATOM 6457 NE ARG D 245 -24.584 -40.802 2.294 1.00 88.63 N ANISOU 6457 NE ARG D 245 13033 10877 9765 166 -2376 384 N ATOM 6458 CZ ARG D 245 -24.732 -39.823 3.185 1.00 86.22 C ANISOU 6458 CZ ARG D 245 12389 10636 9733 518 -2238 639 C ATOM 6459 NH1 ARG D 245 -25.350 -40.046 4.339 1.00 84.71 N ANISOU 6459 NH1 ARG D 245 11826 10587 9773 386 -2348 719 N ATOM 6460 NH2 ARG D 245 -24.262 -38.609 2.920 1.00 85.48 N ANISOU 6460 NH2 ARG D 245 12377 10436 9665 989 -1948 807 N ATOM 6461 N ALA D 246 -22.051 -44.199 -1.863 1.00100.22 N ANISOU 6461 N ALA D 246 16932 11011 10136 -727 -1934 -935 N ATOM 6462 CA ALA D 246 -21.432 -43.826 -3.127 1.00102.62 C ANISOU 6462 CA ALA D 246 17655 11250 10086 -514 -1730 -1004 C ATOM 6463 C ALA D 246 -21.846 -42.411 -3.538 1.00102.58 C ANISOU 6463 C ALA D 246 17297 11790 9887 -138 -1854 -640 C ATOM 6464 O ALA D 246 -21.058 -41.695 -4.159 1.00102.09 O ANISOU 6464 O ALA D 246 17438 11574 9779 256 -1554 -559 O ATOM 6465 CB ALA D 246 -21.792 -44.829 -4.214 1.00108.91 C ANISOU 6465 CB ALA D 246 19010 12077 10292 -1048 -1856 -1363 C ATOM 6466 N ASP D 247 -23.071 -42.025 -3.158 1.00103.60 N ANISOU 6466 N ASP D 247 16902 12541 9922 -235 -2252 -391 N ATOM 6467 CA ASP D 247 -23.743 -40.764 -3.550 1.00105.10 C ANISOU 6467 CA ASP D 247 16726 13342 9865 134 -2399 27 C ATOM 6468 C ASP D 247 -24.687 -40.985 -4.746 1.00111.99 C ANISOU 6468 C ASP D 247 17643 14920 9987 -191 -2804 40 C ATOM 6469 O ASP D 247 -24.383 -40.693 -5.907 1.00114.99 O ANISOU 6469 O ASP D 247 18369 15395 9928 -64 -2728 40 O ATOM 6470 CB ASP D 247 -22.751 -39.610 -3.814 1.00102.61 C ANISOU 6470 CB ASP D 247 16564 12703 9720 746 -1956 214 C ATOM 6471 CG ASP D 247 -23.438 -38.247 -3.930 1.00103.85 C ANISOU 6471 CG ASP D 247 16353 13352 9752 1215 -2001 706 C ATOM 6472 OD1 ASP D 247 -23.520 -37.705 -5.058 1.00107.11 O ANISOU 6472 OD1 ASP D 247 16941 14051 9705 1428 -1993 881 O ATOM 6473 OD2 ASP D 247 -23.890 -37.715 -2.890 1.00101.81 O ANISOU 6473 OD2 ASP D 247 15661 13179 9844 1403 -2004 938 O ATOM 6474 OXT ASP D 247 -25.804 -41.474 -4.575 1.00115.26 O ANISOU 6474 OXT ASP D 247 17722 15893 10180 -630 -3235 62 O TER 6475 ASP D 247 HETATM 6476 C1 NAG E 1 27.203 -52.071 64.142 1.00102.95 C ANISOU 6476 C1 NAG E 1 9733 17806 11579 2087 1422 828 C HETATM 6477 C2 NAG E 1 27.501 -52.231 62.651 1.00106.89 C ANISOU 6477 C2 NAG E 1 10202 18640 11771 2196 1722 728 C HETATM 6478 C3 NAG E 1 27.261 -53.673 62.184 1.00108.51 C ANISOU 6478 C3 NAG E 1 10639 18714 11875 2660 1722 423 C HETATM 6479 C4 NAG E 1 27.849 -54.750 63.116 1.00109.76 C ANISOU 6479 C4 NAG E 1 10669 18777 12256 3057 1577 254 C HETATM 6480 C5 NAG E 1 27.673 -54.362 64.594 1.00106.08 C ANISOU 6480 C5 NAG E 1 10169 18046 12090 2858 1298 420 C HETATM 6481 C6 NAG E 1 28.518 -55.228 65.524 1.00107.68 C ANISOU 6481 C6 NAG E 1 10162 18246 12506 3212 1163 304 C HETATM 6482 C7 NAG E 1 27.104 -50.049 61.572 1.00106.37 C ANISOU 6482 C7 NAG E 1 10204 18779 11432 1468 1906 1123 C HETATM 6483 C8 NAG E 1 26.176 -49.228 60.726 1.00105.02 C ANISOU 6483 C8 NAG E 1 10368 18492 11044 1173 1916 1267 C HETATM 6484 N2 NAG E 1 26.717 -51.300 61.848 1.00105.54 N ANISOU 6484 N2 NAG E 1 10273 18429 11399 1850 1781 885 N HETATM 6485 O3 NAG E 1 27.793 -53.826 60.884 1.00112.60 O ANISOU 6485 O3 NAG E 1 11064 19615 12103 2797 2033 311 O HETATM 6486 O4 NAG E 1 27.208 -56.004 62.895 1.00110.71 O ANISOU 6486 O4 NAG E 1 11182 18571 12310 3394 1465 11 O HETATM 6487 O5 NAG E 1 28.010 -53.005 64.835 1.00105.18 O ANISOU 6487 O5 NAG E 1 9797 18139 12028 2440 1353 680 O HETATM 6488 O6 NAG E 1 28.442 -54.705 66.834 1.00104.94 O ANISOU 6488 O6 NAG E 1 9768 17712 12394 2973 929 482 O HETATM 6489 O7 NAG E 1 28.156 -49.553 61.979 1.00108.21 O ANISOU 6489 O7 NAG E 1 10037 19310 11768 1340 1989 1233 O HETATM 6490 C1 NAG E 2 27.868 -56.859 61.924 1.00115.99 C ANISOU 6490 C1 NAG E 2 11797 19494 12780 3811 1682 -246 C HETATM 6491 C2 NAG E 2 27.577 -58.338 62.198 1.00117.00 C ANISOU 6491 C2 NAG E 2 12263 19240 12953 4250 1481 -512 C HETATM 6492 C3 NAG E 2 28.393 -59.211 61.247 1.00122.35 C ANISOU 6492 C3 NAG E 2 12863 20193 13431 4741 1713 -803 C HETATM 6493 C4 NAG E 2 28.048 -58.860 59.801 1.00123.79 C ANISOU 6493 C4 NAG E 2 13200 20584 13250 4612 1977 -842 C HETATM 6494 C5 NAG E 2 28.094 -57.341 59.561 1.00122.44 C ANISOU 6494 C5 NAG E 2 12762 20730 13029 4094 2144 -534 C HETATM 6495 C6 NAG E 2 27.432 -56.984 58.231 1.00123.01 C ANISOU 6495 C6 NAG E 2 13129 20871 12738 3903 2307 -533 C HETATM 6496 C7 NAG E 2 26.851 -59.241 64.348 1.00114.11 C ANISOU 6496 C7 NAG E 2 12229 18121 13008 4303 908 -476 C HETATM 6497 C8 NAG E 2 27.246 -59.568 65.757 1.00113.80 C ANISOU 6497 C8 NAG E 2 12090 17898 13250 4403 655 -424 C HETATM 6498 N2 NAG E 2 27.809 -58.707 63.583 1.00116.49 N ANISOU 6498 N2 NAG E 2 12125 18942 13195 4350 1213 -476 N HETATM 6499 O3 NAG E 2 28.139 -60.579 61.480 1.00123.17 O ANISOU 6499 O3 NAG E 2 13331 19902 13567 5155 1505 -1054 O HETATM 6500 O4 NAG E 2 28.940 -59.531 58.932 1.00128.95 O ANISOU 6500 O4 NAG E 2 13718 21578 13701 5058 2249 -1107 O HETATM 6501 O5 NAG E 2 27.456 -56.589 60.591 1.00117.26 O ANISOU 6501 O5 NAG E 2 12142 19794 12616 3703 1892 -276 O HETATM 6502 O6 NAG E 2 27.577 -55.603 57.980 1.00122.55 O ANISOU 6502 O6 NAG E 2 12842 21105 12618 3448 2459 -246 O HETATM 6503 O7 NAG E 2 25.698 -59.469 63.970 1.00112.39 O ANISOU 6503 O7 NAG E 2 12441 17591 12670 4169 820 -508 O HETATM 6504 C1A QUX A 303 10.191 -44.924 59.929 1.00 79.10 C ANISOU 6504 C1A QUX A 303 9993 12032 8030 414 -628 1883 C HETATM 6505 C2A QUX A 303 10.532 -45.640 58.616 1.00 80.65 C ANISOU 6505 C2A QUX A 303 10325 12400 7920 431 -565 1812 C HETATM 6506 O2A QUX A 303 10.059 -46.987 58.637 1.00 79.27 O ANISOU 6506 O2A QUX A 303 10151 12205 7763 533 -617 1602 O HETATM 6507 C3A QUX A 303 12.029 -45.659 58.312 1.00 82.14 C ANISOU 6507 C3A QUX A 303 10471 12792 7948 387 -297 1833 C HETATM 6508 O3A QUX A 303 12.221 -46.117 56.970 1.00 85.46 O ANISOU 6508 O3A QUX A 303 11055 13378 8037 404 -239 1782 O HETATM 6509 C4A QUX A 303 12.668 -44.283 58.478 1.00 82.77 C ANISOU 6509 C4A QUX A 303 10530 12885 8033 223 -231 2062 C HETATM 6510 O4A QUX A 303 12.245 -43.428 57.406 1.00 84.59 O ANISOU 6510 O4A QUX A 303 10987 13113 8040 127 -340 2226 O HETATM 6511 C5M QUX A 303 12.290 -43.713 59.846 1.00 80.58 C ANISOU 6511 C5M QUX A 303 10142 12396 8079 214 -330 2106 C HETATM 6512 O5M QUX A 303 11.894 -41.313 59.939 1.00 82.12 O ANISOU 6512 O5M QUX A 303 10539 12349 8313 23 -520 2457 O HETATM 6513 C6A QUX A 303 12.892 -42.332 60.107 1.00 81.86 C ANISOU 6513 C6A QUX A 303 10327 12516 8259 39 -300 2324 C HETATM 6514 O6A QUX A 303 10.863 -43.657 59.983 1.00 79.63 O ANISOU 6514 O6A QUX A 303 10087 12095 8073 296 -566 2079 O HETATM 6515 CAG QUX A 303 10.489 -45.782 61.162 1.00 77.85 C ANISOU 6515 CAG QUX A 303 9660 11830 8091 473 -540 1739 C HETATM 6516 CAL QUX A 303 10.047 -45.134 62.474 1.00 77.19 C ANISOU 6516 CAL QUX A 303 9470 11579 8279 460 -602 1788 C HETATM 6517 CAM QUX A 303 10.313 -46.009 63.708 1.00 76.28 C ANISOU 6517 CAM QUX A 303 9219 11414 8350 500 -529 1658 C HETATM 6518 CAN QUX A 303 9.710 -47.410 63.522 1.00 76.73 C ANISOU 6518 CAN QUX A 303 9300 11467 8388 570 -588 1482 C HETATM 6519 CAO QUX A 303 10.120 -48.503 64.519 1.00 76.39 C ANISOU 6519 CAO QUX A 303 9189 11370 8464 611 -523 1350 C HETATM 6520 CAP QUX A 303 10.047 -48.102 66.000 1.00 74.77 C ANISOU 6520 CAP QUX A 303 8877 11050 8484 573 -512 1387 C HETATM 6521 CAQ QUX A 303 9.826 -49.291 66.942 1.00 74.02 C ANISOU 6521 CAQ QUX A 303 8770 10856 8497 588 -529 1259 C HETATM 6522 CAR QUX A 303 11.109 -50.061 67.257 0.00 74.09 C ANISOU 6522 CAR QUX A 303 8773 10890 8488 659 -430 1194 C HETATM 6523 CAS QUX A 303 11.060 -50.676 68.656 0.00 72.64 C ANISOU 6523 CAS QUX A 303 8577 10567 8456 642 -450 1146 C HETATM 6524 CAT QUX A 303 11.060 -52.202 68.610 1.00 72.84 C ANISOU 6524 CAT QUX A 303 8725 10512 8440 707 -500 1002 C HETATM 6525 CAU QUX A 303 9.751 -52.779 69.143 1.00 72.09 C ANISOU 6525 CAU QUX A 303 8695 10281 8414 593 -609 960 C HETATM 6526 CAV QUX A 303 9.983 -54.008 70.014 1.00 71.89 C ANISOU 6526 CAV QUX A 303 8789 10098 8428 598 -651 879 C HETATM 6527 CAW QUX A 303 9.742 -55.294 69.230 1.00 73.76 C ANISOU 6527 CAW QUX A 303 9220 10254 8551 635 -745 748 C HETATM 6528 CAX QUX A 303 8.871 -56.279 70.003 0.00 74.57 C ANISOU 6528 CAX QUX A 303 9460 10171 8704 480 -856 708 C HETATM 6529 CAY QUX A 303 7.461 -56.357 69.417 0.00 76.02 C ANISOU 6529 CAY QUX A 303 9643 10379 8861 310 -954 696 C HETATM 6530 CAZ QUX A 303 6.580 -57.346 70.180 0.00 77.24 C ANISOU 6530 CAZ QUX A 303 9917 10374 9055 99 -1056 671 C HETATM 6531 CBA QUX A 303 5.101 -56.991 70.046 0.00 77.69 C ANISOU 6531 CBA QUX A 303 9822 10537 9159 -111 -1112 711 C HETATM 6532 CBB QUX A 303 4.255 -58.226 69.748 0.00 79.90 C ANISOU 6532 CBB QUX A 303 10281 10700 9376 -314 -1277 637 C HETATM 6533 CBC QUX A 303 2.855 -58.098 70.311 0.00 79.95 C ANISOU 6533 CBC QUX A 303 10101 10799 9477 -587 -1303 696 C HETATM 6534 OBD QUX A 303 8.285 -47.285 63.547 1.00 76.81 O ANISOU 6534 OBD QUX A 303 9310 11394 8479 565 -766 1477 O HETATM 6535 OBE QUX A 303 9.281 -49.646 64.274 1.00 76.86 O ANISOU 6535 OBE QUX A 303 9324 11378 8501 633 -631 1213 O HETATM 6536 NBF QUX A 303 11.768 -46.132 63.838 1.00 77.09 N ANISOU 6536 NBF QUX A 303 9254 11632 8404 479 -349 1667 N HETATM 6537 CBG QUX A 303 12.547 -45.192 64.397 1.00 77.58 C ANISOU 6537 CBG QUX A 303 9253 11694 8529 385 -280 1792 C HETATM 6538 OBH QUX A 303 12.136 -44.128 64.852 1.00 77.18 O ANISOU 6538 OBH QUX A 303 9238 11514 8572 320 -359 1902 O HETATM 6539 CBI QUX A 303 14.028 -45.508 64.437 1.00 78.60 C ANISOU 6539 CBI QUX A 303 9259 11999 8607 368 -103 1783 C HETATM 6540 CBK QUX A 303 14.563 -45.455 65.867 1.00 77.42 C ANISOU 6540 CBK QUX A 303 8980 11772 8664 343 -89 1779 C HETATM 6541 CBL QUX A 303 14.286 -46.748 66.626 1.00 76.40 C ANISOU 6541 CBL QUX A 303 8818 11561 8649 479 -122 1606 C HETATM 6542 CBM QUX A 303 15.200 -46.845 67.836 1.00 76.04 C ANISOU 6542 CBM QUX A 303 8644 11504 8745 466 -87 1605 C HETATM 6543 CBN QUX A 303 14.558 -47.646 68.962 1.00 75.08 C ANISOU 6543 CBN QUX A 303 8559 11199 8768 528 -176 1498 C HETATM 6544 CBO QUX A 303 14.572 -46.852 70.267 0.00 74.16 C ANISOU 6544 CBO QUX A 303 8426 10955 8797 423 -220 1574 C HETATM 6545 CBP QUX A 303 15.783 -47.186 71.139 0.00 74.68 C ANISOU 6545 CBP QUX A 303 8379 11065 8931 430 -199 1566 C HETATM 6546 CBQ QUX A 303 15.423 -47.233 72.625 0.00 73.56 C ANISOU 6546 CBQ QUX A 303 8296 10737 8918 391 -280 1548 C HETATM 6547 CBR QUX A 303 15.474 -45.850 73.277 0.00 72.90 C ANISOU 6547 CBR QUX A 303 8238 10576 8884 239 -307 1662 C HETATM 6548 CBS QUX A 303 14.676 -45.809 74.581 0.00 70.86 C ANISOU 6548 CBS QUX A 303 8092 10122 8709 214 -367 1621 C HETATM 6549 CBT QUX A 303 14.079 -44.428 74.839 1.00 69.96 C ANISOU 6549 CBT QUX A 303 8076 9891 8614 128 -389 1691 C HETATM 6550 CBU QUX A 303 14.960 -43.586 75.758 1.00 69.62 C ANISOU 6550 CBU QUX A 303 8062 9788 8602 -3 -432 1763 C HETATM 6551 CBV QUX A 303 14.370 -42.193 75.947 1.00 69.12 C ANISOU 6551 CBV QUX A 303 8150 9570 8544 -65 -467 1818 C HETATM 6552 CBW QUX A 303 15.167 -41.153 75.170 1.00 70.29 C ANISOU 6552 CBW QUX A 303 8302 9763 8642 -199 -484 1960 C HETATM 6553 CBX QUX A 303 16.097 -40.361 76.087 1.00 70.75 C ANISOU 6553 CBX QUX A 303 8419 9741 8720 -380 -556 2029 C HETATM 6554 CBY QUX A 303 17.187 -39.643 75.299 1.00 71.80 C ANISOU 6554 CBY QUX A 303 8488 9994 8798 -572 -560 2183 C HETATM 6555 CBZ QUX A 303 18.497 -39.635 76.078 1.00 72.45 C ANISOU 6555 CBZ QUX A 303 8460 10156 8913 -742 -614 2228 C HETATM 6556 CCA QUX A 303 19.700 -39.490 75.153 1.00 73.99 C ANISOU 6556 CCA QUX A 303 8444 10613 9056 -902 -560 2355 C HETATM 6557 CCB QUX A 303 20.476 -40.797 75.062 1.00 73.69 C ANISOU 6557 CCB QUX A 303 8109 10845 9046 -779 -491 2285 C HETATM 6558 CCC QUX A 303 20.844 -41.115 73.618 1.00 74.91 C ANISOU 6558 CCC QUX A 303 8085 11269 9107 -744 -343 2323 C HETATM 6559 CCD QUX A 303 21.622 -42.423 73.538 1.00 75.41 C ANISOU 6559 CCD QUX A 303 7868 11587 9198 -568 -274 2226 C HETATM 6560 CCE QUX A 303 20.768 -43.539 72.952 1.00 74.02 C ANISOU 6560 CCE QUX A 303 7742 11397 8985 -291 -203 2083 C HETATM 6561 CCF QUX A 303 21.505 -44.870 73.030 1.00 74.84 C ANISOU 6561 CCF QUX A 303 7632 11681 9124 -80 -170 1967 C HETATM 6562 CCG QUX A 303 20.525 -46.027 73.188 1.00 72.82 C ANISOU 6562 CCG QUX A 303 7529 11256 8882 158 -198 1810 C HETATM 6563 CCH QUX A 303 20.343 -46.755 71.875 1.00 73.41 C ANISOU 6563 CCH QUX A 303 7579 11472 8843 326 -75 1727 C HETATM 6564 C1 NAG A 304 0.145 -40.249 75.979 1.00 77.21 C ANISOU 6564 C1 NAG A 304 8397 10816 10122 1408 -415 1070 C HETATM 6565 C2 NAG A 304 -1.371 -40.167 76.184 1.00 79.74 C ANISOU 6565 C2 NAG A 304 8411 11339 10547 1591 -375 960 C HETATM 6566 C3 NAG A 304 -2.117 -40.448 74.875 1.00 80.67 C ANISOU 6566 C3 NAG A 304 8322 11612 10717 1640 -556 1008 C HETATM 6567 C4 NAG A 304 -1.670 -39.473 73.796 1.00 81.01 C ANISOU 6567 C4 NAG A 304 8579 11468 10733 1782 -768 1123 C HETATM 6568 C5 NAG A 304 -0.147 -39.524 73.658 1.00 78.44 C ANISOU 6568 C5 NAG A 304 8568 10948 10287 1584 -762 1227 C HETATM 6569 C6 NAG A 304 0.325 -38.369 72.792 1.00 79.34 C ANISOU 6569 C6 NAG A 304 8930 10859 10356 1699 -938 1350 C HETATM 6570 C7 NAG A 304 -2.191 -40.692 78.455 1.00 81.94 C ANISOU 6570 C7 NAG A 304 8501 11812 10819 1530 11 751 C HETATM 6571 C8 NAG A 304 -2.123 -39.231 78.814 1.00 83.16 C ANISOU 6571 C8 NAG A 304 8841 11769 10987 1822 -2 700 C HETATM 6572 N2 NAG A 304 -1.823 -41.073 77.226 1.00 80.12 N ANISOU 6572 N2 NAG A 304 8288 11562 10591 1444 -173 865 N HETATM 6573 O3 NAG A 304 -3.505 -40.300 75.048 1.00 83.68 O ANISOU 6573 O3 NAG A 304 8376 12207 11211 1822 -538 911 O HETATM 6574 O4 NAG A 304 -2.327 -39.758 72.572 1.00 81.81 O ANISOU 6574 O4 NAG A 304 8522 11708 10854 1816 -956 1173 O HETATM 6575 O5 NAG A 304 0.512 -39.387 74.911 1.00 77.28 O ANISOU 6575 O5 NAG A 304 8561 10685 10116 1514 -598 1178 O HETATM 6576 O6 NAG A 304 0.594 -37.277 73.642 1.00 80.25 O ANISOU 6576 O6 NAG A 304 9245 10758 10487 1821 -898 1323 O HETATM 6577 O7 NAG A 304 -2.578 -41.504 79.298 1.00 82.72 O ANISOU 6577 O7 NAG A 304 8466 12075 10888 1370 188 687 O HETATM 6578 C1 NAG A 307 -9.588 -48.255 77.705 1.00 99.07 C ANISOU 6578 C1 NAG A 307 8213 16173 13256 -144 183 661 C HETATM 6579 C2 NAG A 307 -11.103 -48.160 77.975 1.00104.98 C ANISOU 6579 C2 NAG A 307 8383 17384 14122 -150 292 594 C HETATM 6580 C3 NAG A 307 -11.497 -46.850 78.679 1.00106.88 C ANISOU 6580 C3 NAG A 307 8428 17750 14432 279 495 477 C HETATM 6581 C4 NAG A 307 -10.570 -46.515 79.852 1.00104.67 C ANISOU 6581 C4 NAG A 307 8534 17223 14011 329 739 443 C HETATM 6582 C5 NAG A 307 -9.097 -46.679 79.451 1.00 99.39 C ANISOU 6582 C5 NAG A 307 8414 16103 13245 279 574 535 C HETATM 6583 C6 NAG A 307 -8.165 -46.436 80.637 1.00 97.20 C ANISOU 6583 C6 NAG A 307 8509 15597 12827 284 783 511 C HETATM 6584 C7 NAG A 307 -12.755 -49.334 76.577 1.00110.44 C ANISOU 6584 C7 NAG A 307 8470 18538 14953 -540 -41 650 C HETATM 6585 C8 NAG A 307 -13.487 -49.364 75.267 1.00112.47 C ANISOU 6585 C8 NAG A 307 8445 18962 15327 -507 -376 675 C HETATM 6586 N2 NAG A 307 -11.885 -48.332 76.753 1.00107.31 N ANISOU 6586 N2 NAG A 307 8373 17865 14534 -160 10 622 N HETATM 6587 O3 NAG A 307 -12.827 -46.921 79.156 1.00111.08 O ANISOU 6587 O3 NAG A 307 8413 18748 15045 235 670 403 O HETATM 6588 O4 NAG A 307 -10.840 -45.205 80.319 1.00106.79 O ANISOU 6588 O4 NAG A 307 8703 17535 14337 775 870 323 O HETATM 6589 O5 NAG A 307 -8.865 -47.974 78.902 1.00 97.82 O ANISOU 6589 O5 NAG A 307 8323 15851 12993 -109 426 632 O HETATM 6590 O6 NAG A 307 -8.395 -47.399 81.638 1.00 98.16 O ANISOU 6590 O6 NAG A 307 8615 15850 12831 -82 996 517 O HETATM 6591 O7 NAG A 307 -12.980 -50.210 77.415 1.00111.89 O ANISOU 6591 O7 NAG A 307 8618 18838 15056 -928 152 664 O CONECT 116 6578 CONECT 306 6564 CONECT 789 1268 CONECT 1247 6476 CONECT 1268 789 CONECT 1563 1998 CONECT 1998 1563 CONECT 2486 2934 CONECT 2934 2486 CONECT 3261 3781 CONECT 3781 3261 CONECT 4097 4483 CONECT 4292 5878 CONECT 4483 4097 CONECT 4778 5324 CONECT 5324 4778 CONECT 5671 6202 CONECT 5878 4292 CONECT 6202 5671 CONECT 6476 1247 6477 6487 CONECT 6477 6476 6478 6484 CONECT 6478 6477 6479 6485 CONECT 6479 6478 6480 6486 CONECT 6480 6479 6481 6487 CONECT 6481 6480 6488 CONECT 6482 6483 6484 6489 CONECT 6483 6482 CONECT 6484 6477 6482 CONECT 6485 6478 CONECT 6486 6479 6490 CONECT 6487 6476 6480 CONECT 6488 6481 CONECT 6489 6482 CONECT 6490 6486 6491 6501 CONECT 6491 6490 6492 6498 CONECT 6492 6491 6493 6499 CONECT 6493 6492 6494 6500 CONECT 6494 6493 6495 6501 CONECT 6495 6494 6502 CONECT 6496 6497 6498 6503 CONECT 6497 6496 CONECT 6498 6491 6496 CONECT 6499 6492 CONECT 6500 6493 CONECT 6501 6490 6494 CONECT 6502 6495 CONECT 6503 6496 CONECT 6504 6505 6514 6515 CONECT 6505 6504 6506 6507 CONECT 6506 6505 CONECT 6507 6505 6508 6509 CONECT 6508 6507 CONECT 6509 6507 6510 6511 CONECT 6510 6509 CONECT 6511 6509 6513 6514 CONECT 6512 6513 CONECT 6513 6511 6512 CONECT 6514 6504 6511 CONECT 6515 6504 6516 CONECT 6516 6515 6517 CONECT 6517 6516 6518 6536 CONECT 6518 6517 6519 6534 CONECT 6519 6518 6520 6535 CONECT 6520 6519 6521 CONECT 6521 6520 6522 CONECT 6522 6521 6523 CONECT 6523 6522 6524 CONECT 6524 6523 6525 CONECT 6525 6524 6526 CONECT 6526 6525 6527 CONECT 6527 6526 6528 CONECT 6528 6527 6529 CONECT 6529 6528 6530 CONECT 6530 6529 6531 CONECT 6531 6530 6532 CONECT 6532 6531 6533 CONECT 6533 6532 CONECT 6534 6518 CONECT 6535 6519 CONECT 6536 6517 6537 CONECT 6537 6536 6538 6539 CONECT 6538 6537 CONECT 6539 6537 6540 CONECT 6540 6539 6541 CONECT 6541 6540 6542 CONECT 6542 6541 6543 CONECT 6543 6542 6544 CONECT 6544 6543 6545 CONECT 6545 6544 6546 CONECT 6546 6545 6547 CONECT 6547 6546 6548 CONECT 6548 6547 6549 CONECT 6549 6548 6550 CONECT 6550 6549 6551 CONECT 6551 6550 6552 CONECT 6552 6551 6553 CONECT 6553 6552 6554 CONECT 6554 6553 6555 CONECT 6555 6554 6556 CONECT 6556 6555 6557 CONECT 6557 6556 6558 CONECT 6558 6557 6559 CONECT 6559 6558 6560 CONECT 6560 6559 6561 CONECT 6561 6560 6562 CONECT 6562 6561 6563 CONECT 6563 6562 CONECT 6564 306 6565 6575 CONECT 6565 6564 6566 6572 CONECT 6566 6565 6567 6573 CONECT 6567 6566 6568 6574 CONECT 6568 6567 6569 6575 CONECT 6569 6568 6576 CONECT 6570 6571 6572 6577 CONECT 6571 6570 CONECT 6572 6565 6570 CONECT 6573 6566 CONECT 6574 6567 CONECT 6575 6564 6568 CONECT 6576 6569 CONECT 6577 6570 CONECT 6578 116 6579 6589 CONECT 6579 6578 6580 6586 CONECT 6580 6579 6581 6587 CONECT 6581 6580 6582 6588 CONECT 6582 6581 6583 6589 CONECT 6583 6582 6590 CONECT 6584 6585 6586 6591 CONECT 6585 6584 CONECT 6586 6579 6584 CONECT 6587 6580 CONECT 6588 6581 CONECT 6589 6578 6582 CONECT 6590 6583 CONECT 6591 6584 MASTER 500 0 5 15 73 0 0 6 6587 4 135 67 END
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3qux
RCSB PDB
PDBbind
QUX
Entry Information
PDB ID
3tn0
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Va14Vb8.2 NKT TCR
Ligand Name
QUX
EC.Number
E.C.-.-.-.-
Resolution
3.2(Å)
Affinity (Kd/Ki/IC50)
Kd=2.20uM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) J.Immunol. Vol. 187: pp. 4705-4713
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P01850
P01848
P01887
P11609
Entrez Gene ID
NCBI Entrez Gene ID:
12010
12479
ASD
Information of known allosteric effects of PDB entries
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