Browse entries in the PDBbind-CN Database
HEADER PROTEIN BINDING 04-APR-11 3REA TITLE HIV-1 NEF PROTEIN IN COMPLEX WITH ENGINEERED HCK-SH3 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN NEF; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: 3'ORF, NEGATIVE FACTOR, F-PROTEIN, C-TERMINAL CORE PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: TYROSINE-PROTEIN KINASE HCK; COMPND 9 CHAIN: B, D; COMPND 10 SYNONYM: HEMOPOIETIC CELL KINASE, P59-HCK/P60-HCK; COMPND 11 EC: 2.7.10.2; COMPND 12 ENGINEERED: YES; COMPND 13 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HIV-1 M:B_ARV2/SF2; SOURCE 3 ORGANISM_COMMON: HIV-1; SOURCE 4 ORGANISM_TAXID: 11685; SOURCE 5 STRAIN: SF2; SOURCE 6 GENE: HIV-1 NEF, NEF; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1 TEV; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: HCK; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PET-28B KEYWDS HIV-1 NEF, SH3 DOMAIN BINDING, SIGNALING, HCK SH3 DOMAIN, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR A.SCHULTE,W.BLANKENFELDT,M.GEYER REVDAT 2 10-OCT-18 3REA 1 COMPND JRNL REVDAT 1 01-JUN-11 3REA 0 JRNL AUTH S.BREUER,S.I.SCHIEVINK,A.SCHULTE,W.BLANKENFELDT,O.T.FACKLER, JRNL AUTH 2 M.GEYER JRNL TITL MOLECULAR DESIGN, FUNCTIONAL CHARACTERIZATION AND STRUCTURAL JRNL TITL 2 BASIS OF A PROTEIN INHIBITOR AGAINST THE HIV-1 PATHOGENICITY JRNL TITL 3 FACTOR NEF. JRNL REF PLOS ONE V. 6 20033 2011 JRNL REFN ESSN 1932-6203 JRNL PMID 21625496 JRNL DOI 10.1371/JOURNAL.PONE.0020033 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 40486 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.170 REMARK 3 R VALUE (WORKING SET) : 0.168 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2148 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2934 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.2000 REMARK 3 BIN FREE R VALUE SET COUNT : 161 REMARK 3 BIN FREE R VALUE : 0.2170 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3046 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 331 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.24000 REMARK 3 B22 (A**2) : -0.24000 REMARK 3 B33 (A**2) : 0.49000 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): 0.121 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.889 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3188 ; 0.026 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 2193 ; 0.003 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4345 ; 1.823 ; 1.940 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5288 ; 1.021 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 7.236 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 160 ;35.172 ;23.125 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 503 ;15.000 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;15.987 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.139 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3542 ; 0.011 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 708 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1873 ; 1.466 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 742 ; 0.432 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3015 ; 2.472 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1315 ; 3.320 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1325 ; 5.127 ; 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 : 5 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 56 A 205 REMARK 3 ORIGIN FOR THE GROUP (A): -14.9761 8.7210 -4.0375 REMARK 3 T TENSOR REMARK 3 T11: 0.0750 T22: 0.0945 REMARK 3 T33: 0.0842 T12: -0.0669 REMARK 3 T13: -0.0581 T23: 0.0737 REMARK 3 L TENSOR REMARK 3 L11: 1.8825 L22: 1.5921 REMARK 3 L33: 2.4022 L12: -0.2781 REMARK 3 L13: 0.5611 L23: 0.0780 REMARK 3 S TENSOR REMARK 3 S11: -0.0617 S12: 0.0069 S13: 0.1544 REMARK 3 S21: 0.2249 S22: -0.0286 S23: -0.0525 REMARK 3 S31: 0.0245 S32: -0.0902 S33: 0.0903 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 : B 79 B 138 REMARK 3 ORIGIN FOR THE GROUP (A): -0.4689 6.2628 -26.4239 REMARK 3 T TENSOR REMARK 3 T11: 0.0263 T22: 0.1908 REMARK 3 T33: 0.1420 T12: 0.0104 REMARK 3 T13: 0.0149 T23: 0.1349 REMARK 3 L TENSOR REMARK 3 L11: 3.8331 L22: 3.8339 REMARK 3 L33: 6.3246 L12: -0.1603 REMARK 3 L13: -0.4775 L23: -1.3377 REMARK 3 S TENSOR REMARK 3 S11: 0.0958 S12: 0.1291 S13: -0.1362 REMARK 3 S21: -0.2691 S22: -0.2544 S23: -0.4135 REMARK 3 S31: 0.1890 S32: 0.4486 S33: 0.1586 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 : C 59 C 210 REMARK 3 ORIGIN FOR THE GROUP (A): -32.3749 -8.2622 -13.9319 REMARK 3 T TENSOR REMARK 3 T11: 0.0843 T22: 0.1280 REMARK 3 T33: 0.1880 T12: -0.0501 REMARK 3 T13: -0.0249 T23: 0.0409 REMARK 3 L TENSOR REMARK 3 L11: 2.2022 L22: 2.2470 REMARK 3 L33: 1.8992 L12: 1.1514 REMARK 3 L13: -0.9096 L23: -1.8665 REMARK 3 S TENSOR REMARK 3 S11: -0.1238 S12: 0.0990 S13: -0.5134 REMARK 3 S21: -0.1619 S22: -0.0084 S23: -0.2588 REMARK 3 S31: 0.2579 S32: 0.0308 S33: 0.1323 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 : D 78 D 137 REMARK 3 ORIGIN FOR THE GROUP (A): -40.6034 16.1208 -23.6222 REMARK 3 T TENSOR REMARK 3 T11: 0.0216 T22: 0.1813 REMARK 3 T33: 0.0807 T12: -0.0033 REMARK 3 T13: -0.0125 T23: 0.0792 REMARK 3 L TENSOR REMARK 3 L11: 3.2174 L22: 4.1512 REMARK 3 L33: 4.3204 L12: -0.8350 REMARK 3 L13: 0.9223 L23: -2.2831 REMARK 3 S TENSOR REMARK 3 S11: -0.0652 S12: -0.1271 S13: 0.1704 REMARK 3 S21: 0.1876 S22: 0.1607 S23: 0.2086 REMARK 3 S31: -0.2300 S32: -0.5372 S33: -0.0955 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 4 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 301 A 429 REMARK 3 RESIDUE RANGE : B 301 B 352 REMARK 3 RESIDUE RANGE : C 301 C 389 REMARK 3 RESIDUE RANGE : D 301 D 361 REMARK 3 ORIGIN FOR THE GROUP (A): -23.2261 5.9786 -14.0988 REMARK 3 T TENSOR REMARK 3 T11: 0.0745 T22: 0.1240 REMARK 3 T33: 0.0874 T12: -0.0485 REMARK 3 T13: -0.0241 T23: 0.0481 REMARK 3 L TENSOR REMARK 3 L11: 1.0221 L22: 0.6440 REMARK 3 L33: 0.6625 L12: -0.1221 REMARK 3 L13: 0.0733 L23: -0.3243 REMARK 3 S TENSOR REMARK 3 S11: 0.0253 S12: 0.0437 S13: -0.0265 REMARK 3 S21: 0.0538 S22: -0.0203 S23: -0.0556 REMARK 3 S31: 0.0082 S32: -0.0530 S33: -0.0050 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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 3REA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-11. REMARK 100 THE DEPOSITION ID IS D_1000064824. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-MAY-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : DIAMOND(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40486 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 69.770 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: REFMAC 5.5.0102 REMARK 200 STARTING MODEL: PDB ENTRY 1EFN REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS BUFFER, 5% ETHYLNE GLYCOL, REMARK 280 10% PEG 8000, 0.2 M MGCL2, 15 MM MNCL2, PH 7.0, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 285K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.53400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 32.84600 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 32.84600 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.76700 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 32.84600 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 32.84600 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 209.30100 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 32.84600 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 32.84600 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.76700 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 32.84600 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 32.84600 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 209.30100 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 139.53400 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 GLY A 45 REMARK 465 ALA A 46 REMARK 465 MET A 47 REMARK 465 ALA A 48 REMARK 465 SER A 49 REMARK 465 SER A 50 REMARK 465 ASN A 51 REMARK 465 THR A 52 REMARK 465 ALA A 53 REMARK 465 ALA A 54 REMARK 465 THR A 55 REMARK 465 LYS A 156 REMARK 465 VAL A 157 REMARK 465 GLU A 158 REMARK 465 GLU A 159 REMARK 465 ALA A 160 REMARK 465 ASN A 161 REMARK 465 GLU A 162 REMARK 465 GLY A 163 REMARK 465 GLU A 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 SER A 167 REMARK 465 LEU A 168 REMARK 465 LEU A 169 REMARK 465 HIS A 170 REMARK 465 PRO A 171 REMARK 465 MET A 172 REMARK 465 SER A 173 REMARK 465 LEU A 174 REMARK 465 HIS A 175 REMARK 465 GLY A 176 REMARK 465 MET A 177 REMARK 465 GLU A 178 REMARK 465 TYR A 206 REMARK 465 TYR A 207 REMARK 465 LYS A 208 REMARK 465 ASP A 209 REMARK 465 ALA A 210 REMARK 465 MET B 78 REMARK 465 GLY C 45 REMARK 465 ALA C 46 REMARK 465 MET C 47 REMARK 465 ALA C 48 REMARK 465 SER C 49 REMARK 465 SER C 50 REMARK 465 ASN C 51 REMARK 465 THR C 52 REMARK 465 ALA C 53 REMARK 465 ALA C 54 REMARK 465 THR C 55 REMARK 465 ASN C 56 REMARK 465 ALA C 57 REMARK 465 ASP C 58 REMARK 465 PRO C 154 REMARK 465 GLU C 155 REMARK 465 LYS C 156 REMARK 465 VAL C 157 REMARK 465 GLU C 158 REMARK 465 GLU C 159 REMARK 465 ALA C 160 REMARK 465 ASN C 161 REMARK 465 GLU C 162 REMARK 465 GLY C 163 REMARK 465 GLU C 164 REMARK 465 ASN C 165 REMARK 465 ASN C 166 REMARK 465 SER C 167 REMARK 465 LEU C 168 REMARK 465 LEU C 169 REMARK 465 HIS C 170 REMARK 465 PRO C 171 REMARK 465 MET C 172 REMARK 465 SER C 173 REMARK 465 LEU C 174 REMARK 465 HIS C 175 REMARK 465 GLY C 176 REMARK 465 MET C 177 REMARK 465 GLU C 178 REMARK 465 ASP C 179 REMARK 465 ALA C 180 REMARK 465 SER D 138 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 GLU A 153 CG CD OE1 OE2 REMARK 470 GLU A 155 CG CD OE1 OE2 REMARK 470 ASP A 179 CG OD1 OD2 REMARK 470 GLU A 181 CG CD OE1 OE2 REMARK 470 PRO A 204 CG CD REMARK 470 SER C 59 OG REMARK 470 TRP C 61 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 61 CZ3 CH2 REMARK 470 LEU C 62 CG CD1 CD2 REMARK 470 GLN C 65 CG CD OE1 NE2 REMARK 470 GLU C 66 CG CD OE1 OE2 REMARK 470 GLU C 67 CG CD OE1 OE2 REMARK 470 GLU C 68 CG CD OE1 OE2 REMARK 470 GLU C 181 CG CD OE1 OE2 REMARK 470 LYS C 182 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 302 O HOH A 403 2.13 REMARK 500 NH1 ARG A 75 O HOH A 364 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 395 O HOH A 395 7555 1.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ALA A 194 CA ALA A 194 CB 0.132 REMARK 500 ARG B 123 CZ ARG B 123 NH1 0.119 REMARK 500 GLU C 112 CB GLU C 112 CG 0.117 REMARK 500 VAL D 90 CB VAL D 90 CG1 0.133 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET A 83 CG - SD - CE ANGL. DEV. = 12.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 ALA A 57 -171.05 -46.84 REMARK 500 ALA A 180 -87.21 -163.03 REMARK 500 HIS A 203 -132.28 -127.42 REMARK 500 PRO A 204 34.51 170.60 REMARK 500 SER B 111 -75.70 -70.11 REMARK 500 ASP B 137 161.84 94.23 REMARK 500 GLU C 69 -30.16 -165.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASP A 58 SER A 59 -138.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3REB RELATED DB: PDB REMARK 900 RELATED ID: 3RBB RELATED DB: PDB REMARK 900 RELATED ID: 1EFN RELATED DB: PDB REMARK 900 RELATED ID: 1AVZ RELATED DB: PDB REMARK 900 RELATED ID: 2NEF RELATED DB: PDB REMARK 900 RELATED ID: 1QA5 RELATED DB: PDB DBREF 3REA A 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3REA B 79 138 UNP P08631 HCK_HUMAN 79 138 DBREF 3REA C 45 210 UNP P03407 NEF_HV1A2 45 210 DBREF 3REA D 79 138 UNP P08631 HCK_HUMAN 79 138 SEQADV 3REA MET A 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3REA ALA A 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3REA SER A 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3REA ALA A 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3REA MET B 78 UNP P08631 INITIATING METHIONINE SEQADV 3REA VAL B 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3REA SER B 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3REA TRP B 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3REA SER B 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3REA PRO B 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3REA ASP B 95 UNP P08631 GLU 95 ENGINEERED MUTATION SEQADV 3REA MET C 47 UNP P03407 ILE 47 ENGINEERED MUTATION SEQADV 3REA ALA C 48 UNP P03407 THR 48 ENGINEERED MUTATION SEQADV 3REA SER C 59 UNP P03407 CYS 59 ENGINEERED MUTATION SEQADV 3REA ALA C 210 UNP P03407 CYS 210 ENGINEERED MUTATION SEQADV 3REA MET D 78 UNP P08631 INITIATING METHIONINE SEQADV 3REA VAL D 90 UNP P08631 GLU 90 ENGINEERED MUTATION SEQADV 3REA SER D 91 UNP P08631 ALA 91 ENGINEERED MUTATION SEQADV 3REA TRP D 92 UNP P08631 ILE 92 ENGINEERED MUTATION SEQADV 3REA SER D 93 UNP P08631 HIS 93 ENGINEERED MUTATION SEQADV 3REA PRO D 94 UNP P08631 HIS 94 ENGINEERED MUTATION SEQADV 3REA ASP D 95 UNP P08631 GLU 95 ENGINEERED MUTATION SEQRES 1 A 166 GLY ALA MET ALA SER SER ASN THR ALA ALA THR ASN ALA SEQRES 2 A 166 ASP SER ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL SEQRES 3 A 166 GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET SEQRES 4 A 166 THR TYR LYS ALA ALA LEU ASP ILE SER HIS PHE LEU LYS SEQRES 5 A 166 GLU LYS GLY GLY LEU GLU GLY LEU ILE TRP SER GLN ARG SEQRES 6 A 166 ARG GLN GLU ILE LEU ASP LEU TRP ILE TYR HIS THR GLN SEQRES 7 A 166 GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO SEQRES 8 A 166 GLY ILE ARG TYR PRO LEU THR PHE GLY TRP CYS PHE LYS SEQRES 9 A 166 LEU VAL PRO VAL GLU PRO GLU LYS VAL GLU GLU ALA ASN SEQRES 10 A 166 GLU GLY GLU ASN ASN SER LEU LEU HIS PRO MET SER LEU SEQRES 11 A 166 HIS GLY MET GLU ASP ALA GLU LYS GLU VAL LEU VAL TRP SEQRES 12 A 166 ARG PHE ASP SER LYS LEU ALA PHE HIS HIS MET ALA ARG SEQRES 13 A 166 GLU LEU HIS PRO GLU TYR TYR LYS ASP ALA SEQRES 1 B 61 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR VAL SEQRES 2 B 61 SER TRP SER PRO ASP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 B 61 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 B 61 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 B 61 SER ASN TYR VAL ALA ARG VAL ASP SER SEQRES 1 C 166 GLY ALA MET ALA SER SER ASN THR ALA ALA THR ASN ALA SEQRES 2 C 166 ASP SER ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU VAL SEQRES 3 C 166 GLY PHE PRO VAL ARG PRO GLN VAL PRO LEU ARG PRO MET SEQRES 4 C 166 THR TYR LYS ALA ALA LEU ASP ILE SER HIS PHE LEU LYS SEQRES 5 C 166 GLU LYS GLY GLY LEU GLU GLY LEU ILE TRP SER GLN ARG SEQRES 6 C 166 ARG GLN GLU ILE LEU ASP LEU TRP ILE TYR HIS THR GLN SEQRES 7 C 166 GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY PRO SEQRES 8 C 166 GLY ILE ARG TYR PRO LEU THR PHE GLY TRP CYS PHE LYS SEQRES 9 C 166 LEU VAL PRO VAL GLU PRO GLU LYS VAL GLU GLU ALA ASN SEQRES 10 C 166 GLU GLY GLU ASN ASN SER LEU LEU HIS PRO MET SER LEU SEQRES 11 C 166 HIS GLY MET GLU ASP ALA GLU LYS GLU VAL LEU VAL TRP SEQRES 12 C 166 ARG PHE ASP SER LYS LEU ALA PHE HIS HIS MET ALA ARG SEQRES 13 C 166 GLU LEU HIS PRO GLU TYR TYR LYS ASP ALA SEQRES 1 D 61 MET GLU ASP ILE ILE VAL VAL ALA LEU TYR ASP TYR VAL SEQRES 2 D 61 SER TRP SER PRO ASP ASP LEU SER PHE GLN LYS GLY ASP SEQRES 3 D 61 GLN MET VAL VAL LEU GLU GLU SER GLY GLU TRP TRP LYS SEQRES 4 D 61 ALA ARG SER LEU ALA THR ARG LYS GLU GLY TYR ILE PRO SEQRES 5 D 61 SER ASN TYR VAL ALA ARG VAL ASP SER FORMUL 5 HOH *331(H2 O) HELIX 1 1 SER A 59 GLY A 71 1 13 HELIX 2 2 THR A 84 GLY A 99 1 16 HELIX 3 3 SER A 107 GLY A 123 1 17 HELIX 4 4 SER A 191 PHE A 195 5 5 HELIX 5 5 HIS A 197 LEU A 202 1 6 HELIX 6 6 GLU C 63 GLU C 68 1 6 HELIX 7 7 THR C 84 GLY C 99 1 16 HELIX 8 8 SER C 107 GLY C 123 1 17 HELIX 9 9 SER C 191 PHE C 195 5 5 HELIX 10 10 HIS C 197 GLU C 201 5 5 HELIX 11 11 HIS C 203 LYS C 208 5 6 SHEET 1 A 2 PHE A 147 VAL A 152 0 SHEET 2 A 2 VAL A 184 PHE A 189 -1 O VAL A 184 N VAL A 152 SHEET 1 B 5 GLU B 125 PRO B 129 0 SHEET 2 B 5 TRP B 114 SER B 119 -1 N ALA B 117 O GLY B 126 SHEET 3 B 5 GLN B 104 GLU B 109 -1 N VAL B 106 O ARG B 118 SHEET 4 B 5 ILE B 81 ALA B 85 -1 N VAL B 83 O MET B 105 SHEET 5 B 5 VAL B 133 ARG B 135 -1 O ALA B 134 N VAL B 84 SHEET 1 C 2 PHE C 147 PRO C 151 0 SHEET 2 C 2 LEU C 185 PHE C 189 -1 O ARG C 188 N LYS C 148 SHEET 1 D 5 GLU D 125 PRO D 129 0 SHEET 2 D 5 TRP D 114 SER D 119 -1 N ALA D 117 O GLY D 126 SHEET 3 D 5 GLN D 104 GLU D 109 -1 N LEU D 108 O LYS D 116 SHEET 4 D 5 ILE D 82 ALA D 85 -1 N VAL D 83 O MET D 105 SHEET 5 D 5 VAL D 133 ARG D 135 -1 O ALA D 134 N VAL D 84 CISPEP 1 GLY A 134 PRO A 135 0 3.70 CISPEP 2 ALA A 180 GLU A 181 0 3.56 CISPEP 3 GLY C 134 PRO C 135 0 -2.12 CRYST1 65.692 65.692 279.068 90.00 90.00 90.00 P 41 21 2 16 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 0.015223 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015223 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003583 0.00000 ATOM 1 N ASN A 56 -9.472 30.624 -6.694 1.00 96.73 N ANISOU 1 N ASN A 56 12763 9927 14062 -1295 -2025 1494 N ATOM 2 CA ASN A 56 -10.316 29.440 -6.337 1.00 94.81 C ANISOU 2 CA ASN A 56 12461 9909 13654 -1122 -1911 1363 C ATOM 3 C ASN A 56 -10.021 28.181 -7.208 1.00 92.67 C ANISOU 3 C ASN A 56 12018 9922 13270 -1166 -1759 1475 C ATOM 4 O ASN A 56 -9.932 28.272 -8.455 1.00 93.54 O ANISOU 4 O ASN A 56 12079 10081 13380 -1223 -1706 1661 O ATOM 5 CB ASN A 56 -11.811 29.775 -6.455 1.00 95.37 C ANISOU 5 CB ASN A 56 12622 9930 13684 -909 -1903 1303 C ATOM 6 CG ASN A 56 -12.215 31.021 -5.682 1.00 98.66 C ANISOU 6 CG ASN A 56 13216 10065 14204 -828 -2048 1183 C ATOM 7 OD1 ASN A 56 -11.425 31.609 -4.931 1.00103.75 O ANISOU 7 OD1 ASN A 56 13933 10544 14945 -928 -2163 1118 O ATOM 8 ND2 ASN A 56 -13.457 31.439 -5.879 1.00 98.87 N ANISOU 8 ND2 ASN A 56 13314 10037 14213 -637 -2051 1146 N ATOM 9 N ALA A 57 -9.927 27.017 -6.554 1.00 89.44 N ANISOU 9 N ALA A 57 11533 9693 12755 -1126 -1691 1358 N ATOM 10 CA ALA A 57 -9.483 25.745 -7.187 1.00 86.75 C ANISOU 10 CA ALA A 57 11040 9605 12315 -1167 -1563 1431 C ATOM 11 C ALA A 57 -10.150 25.444 -8.533 1.00 84.03 C ANISOU 11 C ALA A 57 10649 9379 11900 -1118 -1463 1560 C ATOM 12 O ALA A 57 -10.851 26.343 -9.101 1.00 86.22 O ANISOU 12 O ALA A 57 11006 9536 12219 -1071 -1501 1630 O ATOM 13 CB ALA A 57 -9.700 24.561 -6.209 1.00 85.62 C ANISOU 13 CB ALA A 57 10870 9604 12058 -1079 -1513 1267 C ATOM 14 N ASP A 58 -9.945 24.230 -9.084 1.00 78.59 N ANISOU 14 N ASP A 58 9841 8916 11103 -1122 -1347 1594 N ATOM 15 CA ASP A 58 -10.943 23.756 -10.101 1.00 74.77 C ANISOU 15 CA ASP A 58 9334 8559 10517 -1024 -1259 1645 C ATOM 16 C ASP A 58 -11.496 22.347 -10.101 1.00 67.11 C ANISOU 16 C ASP A 58 8301 7788 9411 -937 -1157 1559 C ATOM 17 O ASP A 58 -10.978 21.358 -10.624 1.00 67.52 O ANISOU 17 O ASP A 58 8258 8006 9390 -972 -1076 1595 O ATOM 18 CB ASP A 58 -10.765 24.294 -11.502 1.00 75.84 C ANISOU 18 CB ASP A 58 9448 8704 10663 -1088 -1239 1845 C ATOM 19 CG ASP A 58 -11.943 25.186 -11.894 1.00 81.50 C ANISOU 19 CG ASP A 58 10267 9301 11398 -982 -1291 1877 C ATOM 20 OD1 ASP A 58 -13.092 24.641 -11.954 1.00 87.36 O ANISOU 20 OD1 ASP A 58 11005 10136 12051 -841 -1252 1794 O ATOM 21 OD2 ASP A 58 -11.744 26.428 -12.108 1.00 87.04 O ANISOU 21 OD2 ASP A 58 11051 9810 12210 -1037 -1378 1980 O ATOM 22 N SER A 59 -12.698 22.374 -9.639 1.00 60.07 N ANISOU 22 N SER A 59 7467 6869 8487 -811 -1166 1453 N ATOM 23 CA SER A 59 -13.199 21.419 -8.756 1.00 54.08 C ANISOU 23 CA SER A 59 6701 6194 7651 -739 -1123 1305 C ATOM 24 C SER A 59 -13.599 20.114 -9.447 1.00 51.12 C ANISOU 24 C SER A 59 6247 6019 7159 -712 -1018 1311 C ATOM 25 O SER A 59 -14.292 20.126 -10.474 1.00 48.26 O ANISOU 25 O SER A 59 5860 5720 6756 -672 -988 1376 O ATOM 26 CB SER A 59 -14.379 22.089 -8.050 1.00 53.87 C ANISOU 26 CB SER A 59 6760 6067 7641 -616 -1169 1197 C ATOM 27 OG SER A 59 -15.224 21.135 -7.455 1.00 51.44 O ANISOU 27 OG SER A 59 6431 5876 7236 -534 -1102 1076 O ATOM 28 N ALA A 60 -13.167 19.010 -8.844 1.00 47.02 N ANISOU 28 N ALA A 60 5695 5586 6584 -730 -973 1238 N ATOM 29 CA ALA A 60 -13.633 17.694 -9.179 1.00 45.00 C ANISOU 29 CA ALA A 60 5390 5484 6222 -698 -887 1205 C ATOM 30 C ALA A 60 -15.166 17.648 -9.133 1.00 42.55 C ANISOU 30 C ALA A 60 5098 5202 5867 -602 -866 1138 C ATOM 31 O ALA A 60 -15.748 17.050 -10.026 1.00 41.77 O ANISOU 31 O ALA A 60 4952 5216 5704 -583 -817 1163 O ATOM 32 CB ALA A 60 -13.107 16.631 -8.220 1.00 42.54 C ANISOU 32 CB ALA A 60 5079 5216 5870 -712 -863 1119 C ATOM 33 N TRP A 61 -15.800 18.233 -8.098 1.00 41.89 N ANISOU 33 N TRP A 61 5073 5032 5811 -540 -904 1046 N ATOM 34 CA TRP A 61 -17.262 18.177 -7.970 1.00 42.33 C ANISOU 34 CA TRP A 61 5121 5136 5825 -443 -876 974 C ATOM 35 C TRP A 61 -17.862 18.955 -9.154 1.00 43.00 C ANISOU 35 C TRP A 61 5185 5215 5938 -397 -906 1063 C ATOM 36 O TRP A 61 -18.746 18.460 -9.848 1.00 40.93 O ANISOU 36 O TRP A 61 4864 5070 5618 -360 -867 1067 O ATOM 37 CB TRP A 61 -17.771 18.721 -6.591 1.00 42.39 C ANISOU 37 CB TRP A 61 5194 5063 5848 -370 -904 851 C ATOM 38 CG TRP A 61 -19.228 18.960 -6.569 1.00 44.25 C ANISOU 38 CG TRP A 61 5404 5347 6061 -258 -882 790 C ATOM 39 CD1 TRP A 61 -19.886 20.175 -6.456 1.00 45.63 C ANISOU 39 CD1 TRP A 61 5615 5426 6295 -152 -942 761 C ATOM 40 CD2 TRP A 61 -20.249 17.992 -6.913 1.00 41.38 C ANISOU 40 CD2 TRP A 61 4957 5147 5620 -239 -803 766 C ATOM 41 NE1 TRP A 61 -21.239 19.984 -6.631 1.00 45.88 N ANISOU 41 NE1 TRP A 61 5576 5570 6284 -58 -898 714 N ATOM 42 CE2 TRP A 61 -21.477 18.650 -6.877 1.00 44.85 C ANISOU 42 CE2 TRP A 61 5369 5602 6072 -122 -813 716 C ATOM 43 CE3 TRP A 61 -20.230 16.607 -7.145 1.00 43.25 C ANISOU 43 CE3 TRP A 61 5142 5509 5781 -312 -730 771 C ATOM 44 CZ2 TRP A 61 -22.701 17.983 -7.121 1.00 48.03 C ANISOU 44 CZ2 TRP A 61 5672 6161 6415 -86 -750 678 C ATOM 45 CZ3 TRP A 61 -21.491 15.934 -7.345 1.00 44.13 C ANISOU 45 CZ3 TRP A 61 5174 5758 5836 -285 -671 728 C ATOM 46 CH2 TRP A 61 -22.648 16.628 -7.397 1.00 42.37 C ANISOU 46 CH2 TRP A 61 4905 5564 5630 -183 -683 691 C ATOM 47 N LEU A 62 -17.381 20.181 -9.414 1.00 43.45 N ANISOU 47 N LEU A 62 5294 5131 6084 -406 -983 1140 N ATOM 48 CA LEU A 62 -18.031 21.018 -10.459 1.00 45.07 C ANISOU 48 CA LEU A 62 5501 5310 6314 -346 -1024 1231 C ATOM 49 C LEU A 62 -17.888 20.399 -11.870 1.00 44.02 C ANISOU 49 C LEU A 62 5299 5316 6109 -393 -979 1347 C ATOM 50 O LEU A 62 -18.847 20.409 -12.650 1.00 42.92 O ANISOU 50 O LEU A 62 5127 5255 5927 -322 -981 1371 O ATOM 51 CB LEU A 62 -17.468 22.448 -10.463 1.00 47.87 C ANISOU 51 CB LEU A 62 5944 5461 6784 -362 -1122 1307 C ATOM 52 CG LEU A 62 -17.681 23.196 -9.149 1.00 49.88 C ANISOU 52 CG LEU A 62 6283 5562 7106 -297 -1184 1180 C ATOM 53 CD1 LEU A 62 -16.887 24.568 -9.259 1.00 52.14 C ANISOU 53 CD1 LEU A 62 6668 5621 7522 -352 -1293 1271 C ATOM 54 CD2 LEU A 62 -19.209 23.400 -8.815 1.00 50.89 C ANISOU 54 CD2 LEU A 62 6407 5719 7209 -125 -1182 1070 C ATOM 55 N GLU A 63 -16.772 19.733 -12.125 1.00 42.52 N ANISOU 55 N GLU A 63 5080 5182 5892 -499 -935 1395 N ATOM 56 CA GLU A 63 -16.583 19.023 -13.395 1.00 43.81 C ANISOU 56 CA GLU A 63 5182 5495 5968 -534 -882 1479 C ATOM 57 C GLU A 63 -17.526 17.789 -13.534 1.00 43.77 C ANISOU 57 C GLU A 63 5122 5645 5863 -488 -825 1383 C ATOM 58 O GLU A 63 -18.178 17.601 -14.547 1.00 42.63 O ANISOU 58 O GLU A 63 4944 5602 5653 -453 -820 1420 O ATOM 59 CB GLU A 63 -15.147 18.590 -13.530 1.00 45.43 C ANISOU 59 CB GLU A 63 5360 5730 6172 -640 -845 1534 C ATOM 60 CG GLU A 63 -14.220 19.811 -13.692 1.00 54.45 C ANISOU 60 CG GLU A 63 6535 6743 7410 -714 -899 1661 C ATOM 61 CD GLU A 63 -12.786 19.446 -14.089 1.00 62.08 C ANISOU 61 CD GLU A 63 7439 7777 8370 -825 -852 1742 C ATOM 62 OE1 GLU A 63 -12.496 18.249 -14.271 1.00 65.65 O ANISOU 62 OE1 GLU A 63 7832 8372 8739 -824 -781 1695 O ATOM 63 OE2 GLU A 63 -11.970 20.375 -14.274 1.00 70.11 O ANISOU 63 OE2 GLU A 63 8465 8707 9467 -911 -888 1857 O ATOM 64 N ALA A 64 -17.622 16.997 -12.476 1.00 40.20 N ANISOU 64 N ALA A 64 4668 5204 5401 -492 -791 1262 N ATOM 65 CA ALA A 64 -18.499 15.876 -12.498 1.00 39.71 C ANISOU 65 CA ALA A 64 4563 5264 5262 -472 -742 1176 C ATOM 66 C ALA A 64 -19.970 16.272 -12.696 1.00 39.40 C ANISOU 66 C ALA A 64 4492 5262 5216 -384 -767 1144 C ATOM 67 O ALA A 64 -20.750 15.605 -13.421 1.00 41.09 O ANISOU 67 O ALA A 64 4648 5603 5363 -372 -749 1127 O ATOM 68 CB ALA A 64 -18.302 15.006 -11.198 1.00 36.35 C ANISOU 68 CB ALA A 64 4157 4824 4828 -501 -701 1068 C ATOM 69 N GLN A 65 -20.387 17.295 -11.972 1.00 40.81 N ANISOU 69 N GLN A 65 4704 5337 5464 -316 -811 1116 N ATOM 70 CA GLN A 65 -21.701 17.802 -12.007 1.00 41.50 C ANISOU 70 CA GLN A 65 4757 5452 5561 -211 -839 1078 C ATOM 71 C GLN A 65 -22.023 18.364 -13.375 1.00 43.51 C ANISOU 71 C GLN A 65 4992 5739 5803 -168 -893 1187 C ATOM 72 O GLN A 65 -23.108 18.110 -13.934 1.00 42.12 O ANISOU 72 O GLN A 65 4743 5681 5581 -111 -901 1165 O ATOM 73 CB GLN A 65 -21.910 18.839 -10.950 1.00 43.91 C ANISOU 73 CB GLN A 65 5117 5624 5944 -134 -879 1021 C ATOM 74 CG GLN A 65 -23.332 19.362 -10.881 1.00 48.21 C ANISOU 74 CG GLN A 65 5611 6207 6498 3 -903 961 C ATOM 75 CD GLN A 65 -23.488 20.565 -9.975 1.00 53.37 C ANISOU 75 CD GLN A 65 6336 6710 7232 106 -956 906 C ATOM 76 OE1 GLN A 65 -22.720 21.553 -10.053 1.00 55.04 O ANISOU 76 OE1 GLN A 65 6645 6750 7518 102 -1028 973 O ATOM 77 NE2 GLN A 65 -24.504 20.517 -9.145 1.00 55.26 N ANISOU 77 NE2 GLN A 65 6528 7011 7458 200 -923 782 N ATOM 78 N GLU A 66 -21.085 19.100 -13.951 1.00 42.68 N ANISOU 78 N GLU A 66 4946 5540 5730 -203 -931 1311 N ATOM 79 CA GLU A 66 -21.347 19.700 -15.273 1.00 45.80 C ANISOU 79 CA GLU A 66 5341 5962 6100 -163 -985 1438 C ATOM 80 C GLU A 66 -21.424 18.592 -16.353 1.00 45.84 C ANISOU 80 C GLU A 66 5279 6155 5983 -207 -941 1458 C ATOM 81 O GLU A 66 -22.285 18.613 -17.209 1.00 45.11 O ANISOU 81 O GLU A 66 5147 6159 5835 -144 -977 1482 O ATOM 82 CB GLU A 66 -20.361 20.806 -15.640 1.00 46.50 C ANISOU 82 CB GLU A 66 5514 5903 6252 -203 -1033 1585 C ATOM 83 CG GLU A 66 -20.745 21.539 -16.975 1.00 57.05 C ANISOU 83 CG GLU A 66 6867 7256 7555 -149 -1096 1735 C ATOM 84 CD GLU A 66 -19.856 22.776 -17.243 1.00 66.09 C ANISOU 84 CD GLU A 66 8110 8222 8780 -197 -1151 1895 C ATOM 85 OE1 GLU A 66 -18.700 22.740 -16.785 1.00 71.37 O ANISOU 85 OE1 GLU A 66 8800 8823 9495 -312 -1117 1912 O ATOM 86 OE2 GLU A 66 -20.305 23.769 -17.930 1.00 80.71 O ANISOU 86 OE2 GLU A 66 10016 10001 10649 -125 -1232 2011 O ATOM 87 N GLU A 67 -20.577 17.572 -16.265 1.00 45.50 N ANISOU 87 N GLU A 67 5226 6165 5896 -304 -870 1431 N ATOM 88 CA GLU A 67 -20.656 16.472 -17.241 1.00 46.80 C ANISOU 88 CA GLU A 67 5343 6497 5944 -335 -833 1425 C ATOM 89 C GLU A 67 -22.009 15.750 -17.203 1.00 46.17 C ANISOU 89 C GLU A 67 5193 6528 5822 -292 -838 1310 C ATOM 90 O GLU A 67 -22.578 15.473 -18.252 1.00 46.88 O ANISOU 90 O GLU A 67 5244 6739 5830 -269 -864 1328 O ATOM 91 CB GLU A 67 -19.544 15.488 -17.006 1.00 49.57 C ANISOU 91 CB GLU A 67 5699 6868 6267 -424 -761 1395 C ATOM 92 CG GLU A 67 -19.328 14.397 -18.073 1.00 58.57 C ANISOU 92 CG GLU A 67 6812 8158 7286 -453 -722 1390 C ATOM 93 CD GLU A 67 -17.854 13.879 -18.038 1.00 68.08 C ANISOU 93 CD GLU A 67 8030 9359 8478 -520 -660 1413 C ATOM 94 OE1 GLU A 67 -17.652 12.636 -18.063 1.00 77.09 O ANISOU 94 OE1 GLU A 67 9160 10568 9562 -541 -615 1328 O ATOM 95 OE2 GLU A 67 -16.910 14.723 -17.998 1.00 73.06 O ANISOU 95 OE2 GLU A 67 8678 9919 9162 -550 -661 1517 O ATOM 96 N GLU A 68 -22.545 15.494 -16.003 1.00 42.10 N ANISOU 96 N GLU A 68 4658 5979 5359 -284 -815 1197 N ATOM 97 CA GLU A 68 -23.834 14.825 -15.877 1.00 42.50 C ANISOU 97 CA GLU A 68 4626 6142 5382 -263 -811 1094 C ATOM 98 C GLU A 68 -24.954 15.692 -16.445 1.00 44.33 C ANISOU 98 C GLU A 68 4802 6420 5621 -153 -887 1121 C ATOM 99 O GLU A 68 -25.915 15.183 -17.087 1.00 45.46 O ANISOU 99 O GLU A 68 4860 6704 5708 -138 -913 1083 O ATOM 100 CB GLU A 68 -24.162 14.491 -14.404 1.00 41.29 C ANISOU 100 CB GLU A 68 4462 5949 5277 -278 -759 984 C ATOM 101 CG GLU A 68 -25.415 13.453 -14.318 1.00 44.11 C ANISOU 101 CG GLU A 68 4717 6450 5594 -305 -732 881 C ATOM 102 CD GLU A 68 -26.678 14.189 -14.351 1.00 51.55 C ANISOU 102 CD GLU A 68 5570 7453 6565 -202 -776 858 C ATOM 103 OE1 GLU A 68 -26.684 15.461 -14.072 1.00 52.13 O ANISOU 103 OE1 GLU A 68 5674 7433 6699 -96 -817 893 O ATOM 104 OE2 GLU A 68 -27.670 13.553 -14.736 1.00 46.22 O ANISOU 104 OE2 GLU A 68 4792 6915 5854 -219 -782 806 O ATOM 105 N GLU A 69 -24.846 17.013 -16.249 1.00 45.16 N ANISOU 105 N GLU A 69 4957 6403 5798 -70 -937 1187 N ATOM 106 CA AGLU A 69 -25.897 17.941 -16.723 0.30 46.12 C ANISOU 106 CA AGLU A 69 5038 6546 5939 62 -1023 1216 C ATOM 107 CA BGLU A 69 -25.934 17.884 -16.734 0.70 46.78 C ANISOU 107 CA BGLU A 69 5117 6639 6020 61 -1021 1212 C ATOM 108 C GLU A 69 -25.940 17.977 -18.266 1.00 47.22 C ANISOU 108 C GLU A 69 5173 6779 5990 74 -1081 1325 C ATOM 109 O GLU A 69 -26.995 17.850 -18.886 1.00 47.62 O ANISOU 109 O GLU A 69 5139 6960 5996 138 -1135 1303 O ATOM 110 CB AGLU A 69 -25.708 19.347 -16.116 0.30 47.06 C ANISOU 110 CB AGLU A 69 5238 6481 6163 152 -1071 1256 C ATOM 111 CB BGLU A 69 -25.893 19.248 -16.119 0.70 48.72 C ANISOU 111 CB BGLU A 69 5430 6715 6367 159 -1070 1242 C ATOM 112 CG AGLU A 69 -26.473 19.549 -14.793 0.30 47.72 C ANISOU 112 CG AGLU A 69 5283 6537 6313 229 -1049 1120 C ATOM 113 CG BGLU A 69 -27.028 20.119 -16.649 0.70 55.22 C ANISOU 113 CG BGLU A 69 6209 7566 7208 316 -1165 1267 C ATOM 114 CD AGLU A 69 -25.928 20.645 -13.878 0.30 46.79 C ANISOU 114 CD AGLU A 69 5274 6211 6292 278 -1075 1119 C ATOM 115 CD BGLU A 69 -27.086 21.451 -16.016 0.70 63.04 C ANISOU 115 CD BGLU A 69 7274 8375 8305 434 -1222 1277 C ATOM 116 OE1AGLU A 69 -25.104 21.466 -14.314 0.30 47.69 O ANISOU 116 OE1AGLU A 69 5491 6182 6447 264 -1130 1237 O ATOM 117 OE1BGLU A 69 -26.363 21.633 -15.000 0.70 67.33 O ANISOU 117 OE1BGLU A 69 7892 8784 8908 388 -1182 1236 O ATOM 118 OE2AGLU A 69 -26.335 20.663 -12.694 0.30 45.39 O ANISOU 118 OE2AGLU A 69 5081 6018 6148 323 -1038 996 O ATOM 119 OE2BGLU A 69 -27.870 22.299 -16.552 0.70 70.77 O ANISOU 119 OE2BGLU A 69 8240 9344 9304 579 -1316 1322 O ATOM 120 N VAL A 70 -24.791 18.145 -18.875 1.00 46.36 N ANISOU 120 N VAL A 70 5148 6618 5849 11 -1071 1442 N ATOM 121 CA VAL A 70 -24.741 18.282 -20.325 1.00 48.47 C ANISOU 121 CA VAL A 70 5426 6974 6014 25 -1120 1561 C ATOM 122 C VAL A 70 -24.896 16.884 -20.973 1.00 46.39 C ANISOU 122 C VAL A 70 5102 6896 5629 -42 -1084 1486 C ATOM 123 O VAL A 70 -25.628 16.699 -21.930 1.00 47.69 O ANISOU 123 O VAL A 70 5220 7195 5705 2 -1143 1493 O ATOM 124 CB VAL A 70 -23.363 18.964 -20.791 1.00 48.02 C ANISOU 124 CB VAL A 70 5476 6812 5956 -34 -1106 1728 C ATOM 125 CG1 VAL A 70 -23.414 19.168 -22.385 1.00 53.74 C ANISOU 125 CG1 VAL A 70 6218 7653 6548 -7 -1155 1869 C ATOM 126 CG2 VAL A 70 -23.270 20.426 -20.159 1.00 55.28 C ANISOU 126 CG2 VAL A 70 6474 7518 7012 26 -1164 1800 C ATOM 127 N GLY A 71 -24.125 15.954 -20.470 1.00 47.31 N ANISOU 127 N GLY A 71 5230 7003 5741 -144 -997 1420 N ATOM 128 CA GLY A 71 -24.140 14.551 -20.900 1.00 47.89 C ANISOU 128 CA GLY A 71 5268 7208 5717 -213 -958 1330 C ATOM 129 C GLY A 71 -23.676 14.311 -22.311 1.00 48.60 C ANISOU 129 C GLY A 71 5386 7409 5669 -222 -970 1406 C ATOM 130 O GLY A 71 -24.158 13.379 -22.951 1.00 49.47 O ANISOU 130 O GLY A 71 5459 7653 5684 -238 -986 1327 O ATOM 131 N PHE A 72 -22.862 15.191 -22.902 1.00 47.76 N ANISOU 131 N PHE A 72 5343 7265 5540 -208 -972 1561 N ATOM 132 CA PHE A 72 -22.558 14.958 -24.328 1.00 49.68 C ANISOU 132 CA PHE A 72 5606 7649 5621 -205 -980 1635 C ATOM 133 C PHE A 72 -21.013 15.115 -24.519 1.00 51.53 C ANISOU 133 C PHE A 72 5897 7848 5836 -269 -894 1743 C ATOM 134 O PHE A 72 -20.612 16.132 -25.021 1.00 53.96 O ANISOU 134 O PHE A 72 6247 8122 6133 -257 -910 1907 O ATOM 135 CB PHE A 72 -23.355 15.957 -25.220 1.00 50.53 C ANISOU 135 CB PHE A 72 5719 7802 5678 -109 -1085 1751 C ATOM 136 CG PHE A 72 -23.611 15.498 -26.639 1.00 55.58 C ANISOU 136 CG PHE A 72 6357 8632 6128 -84 -1124 1770 C ATOM 137 CD1 PHE A 72 -24.322 16.275 -27.496 1.00 63.63 C ANISOU 137 CD1 PHE A 72 7384 9711 7079 6 -1227 1873 C ATOM 138 CD2 PHE A 72 -23.230 14.248 -27.090 1.00 60.39 C ANISOU 138 CD2 PHE A 72 6961 9363 6624 -139 -1070 1669 C ATOM 139 CE1 PHE A 72 -24.556 15.884 -28.838 1.00 67.24 C ANISOU 139 CE1 PHE A 72 7850 10358 7341 36 -1274 1893 C ATOM 140 CE2 PHE A 72 -23.474 13.845 -28.390 1.00 61.67 C ANISOU 140 CE2 PHE A 72 7131 9702 6599 -108 -1113 1672 C ATOM 141 CZ PHE A 72 -24.131 14.684 -29.282 1.00 65.59 C ANISOU 141 CZ PHE A 72 7639 10271 7013 -23 -1216 1789 C ATOM 142 N PRO A 73 -20.175 14.102 -24.210 1.00 52.38 N ANISOU 142 N PRO A 73 6000 7973 5930 -334 -808 1659 N ATOM 143 CA PRO A 73 -18.720 14.301 -24.409 1.00 53.15 C ANISOU 143 CA PRO A 73 6124 8060 6012 -387 -727 1763 C ATOM 144 C PRO A 73 -18.289 14.561 -25.842 1.00 56.15 C ANISOU 144 C PRO A 73 6523 8581 6231 -373 -711 1896 C ATOM 145 O PRO A 73 -18.987 14.187 -26.801 1.00 55.54 O ANISOU 145 O PRO A 73 6446 8642 6015 -323 -754 1869 O ATOM 146 CB PRO A 73 -18.124 12.944 -23.891 1.00 53.32 C ANISOU 146 CB PRO A 73 6127 8101 6030 -428 -653 1615 C ATOM 147 CG PRO A 73 -19.094 12.355 -23.113 1.00 53.54 C ANISOU 147 CG PRO A 73 6139 8086 6118 -422 -689 1471 C ATOM 148 CD PRO A 73 -20.437 12.752 -23.653 1.00 51.45 C ANISOU 148 CD PRO A 73 5854 7878 5815 -365 -779 1475 C ATOM 149 N VAL A 74 -17.164 15.239 -25.987 1.00 60.00 N ANISOU 149 N VAL A 74 7025 9039 6734 -423 -655 2045 N ATOM 150 CA VAL A 74 -16.562 15.487 -27.293 1.00 62.78 C ANISOU 150 CA VAL A 74 7391 9536 6926 -427 -612 2191 C ATOM 151 C VAL A 74 -15.550 14.397 -27.736 1.00 61.68 C ANISOU 151 C VAL A 74 7217 9549 6671 -446 -500 2125 C ATOM 152 O VAL A 74 -14.909 14.526 -28.820 1.00 60.64 O ANISOU 152 O VAL A 74 7085 9567 6387 -449 -438 2240 O ATOM 153 CB VAL A 74 -15.858 16.909 -27.304 1.00 65.02 C ANISOU 153 CB VAL A 74 7705 9713 7288 -488 -605 2418 C ATOM 154 CG1 VAL A 74 -16.900 17.995 -26.862 1.00 68.18 C ANISOU 154 CG1 VAL A 74 8155 9945 7807 -443 -727 2469 C ATOM 155 CG2 VAL A 74 -14.637 16.923 -26.412 1.00 67.11 C ANISOU 155 CG2 VAL A 74 7931 9886 7682 -579 -529 2420 C ATOM 156 N ARG A 75 -15.460 13.331 -26.931 1.00 58.74 N ANISOU 156 N ARG A 75 6818 9142 6358 -448 -476 1941 N ATOM 157 CA AARG A 75 -14.521 12.251 -27.168 0.70 59.85 C ANISOU 157 CA AARG A 75 6930 9394 6417 -446 -381 1854 C ATOM 158 CA BARG A 75 -14.505 12.250 -27.143 0.30 58.51 C ANISOU 158 CA BARG A 75 6759 9221 6251 -447 -380 1853 C ATOM 159 C ARG A 75 -15.048 10.893 -26.688 1.00 58.60 C ANISOU 159 C ARG A 75 6781 9220 6266 -414 -403 1629 C ATOM 160 O ARG A 75 -15.947 10.832 -25.841 1.00 56.57 O ANISOU 160 O ARG A 75 6534 8842 6118 -422 -471 1549 O ATOM 161 CB AARG A 75 -13.246 12.539 -26.394 0.70 59.55 C ANISOU 161 CB AARG A 75 6847 9278 6502 -511 -309 1913 C ATOM 162 CB BARG A 75 -13.210 12.541 -26.380 0.30 57.45 C ANISOU 162 CB BARG A 75 6579 9011 6238 -512 -307 1914 C ATOM 163 CG AARG A 75 -13.514 12.398 -24.970 0.70 58.95 C ANISOU 163 CG AARG A 75 6774 9021 6602 -533 -352 1812 C ATOM 164 CG BARG A 75 -13.389 12.657 -24.884 0.30 52.26 C ANISOU 164 CG BARG A 75 5925 8154 5780 -546 -352 1845 C ATOM 165 CD AARG A 75 -12.763 13.347 -24.150 0.70 60.30 C ANISOU 165 CD AARG A 75 6924 9061 6925 -605 -346 1918 C ATOM 166 CD BARG A 75 -12.084 13.057 -24.252 0.30 47.44 C ANISOU 166 CD BARG A 75 5265 7485 5276 -614 -296 1919 C ATOM 167 NE AARG A 75 -13.036 12.927 -22.796 0.70 61.50 N ANISOU 167 NE AARG A 75 7087 9071 7209 -608 -382 1784 N ATOM 168 NE BARG A 75 -11.762 14.432 -24.540 0.30 39.15 N ANISOU 168 NE BARG A 75 4215 6395 4267 -678 -303 2119 N ATOM 169 CZ AARG A 75 -12.452 13.411 -21.713 0.70 57.68 C ANISOU 169 CZ AARG A 75 6591 8452 6872 -661 -391 1803 C ATOM 170 CZ BARG A 75 -12.085 15.444 -23.744 0.30 38.14 C ANISOU 170 CZ BARG A 75 4120 6082 4288 -718 -376 2175 C ATOM 171 NH1AARG A 75 -11.568 14.404 -21.800 0.70 62.92 N ANISOU 171 NH1AARG A 75 7227 9088 7591 -729 -374 1954 N ATOM 172 NH1BARG A 75 -12.744 15.227 -22.638 0.30 32.54 N ANISOU 172 NH1BARG A 75 3439 5241 3684 -694 -436 2045 N ATOM 173 NH2AARG A 75 -12.810 12.936 -20.569 0.70 49.24 N ANISOU 173 NH2AARG A 75 5543 7278 5887 -652 -422 1677 N ATOM 174 NH2BARG A 75 -11.782 16.688 -24.073 0.30 44.81 N ANISOU 174 NH2BARG A 75 4982 6873 5172 -780 -391 2363 N ATOM 175 N PRO A 76 -14.461 9.803 -27.212 1.00 57.88 N ANISOU 175 N PRO A 76 6686 9247 6058 -378 -340 1528 N ATOM 176 CA PRO A 76 -15.103 8.553 -26.849 1.00 55.27 C ANISOU 176 CA PRO A 76 6385 8881 5734 -356 -380 1324 C ATOM 177 C PRO A 76 -14.958 8.179 -25.421 1.00 50.69 C ANISOU 177 C PRO A 76 5801 8131 5326 -394 -380 1247 C ATOM 178 O PRO A 76 -14.124 8.715 -24.667 1.00 52.34 O ANISOU 178 O PRO A 76 5981 8260 5647 -428 -340 1325 O ATOM 179 CB PRO A 76 -14.504 7.510 -27.823 1.00 56.37 C ANISOU 179 CB PRO A 76 6540 9178 5700 -293 -322 1230 C ATOM 180 CG PRO A 76 -13.480 8.248 -28.692 1.00 59.94 C ANISOU 180 CG PRO A 76 6953 9776 6045 -281 -233 1394 C ATOM 181 CD PRO A 76 -13.314 9.633 -28.127 1.00 58.68 C ANISOU 181 CD PRO A 76 6761 9514 6021 -353 -238 1584 C ATOM 182 N GLN A 77 -15.870 7.297 -24.995 1.00 48.47 N ANISOU 182 N GLN A 77 5554 7790 5073 -398 -435 1096 N ATOM 183 CA GLN A 77 -15.827 6.672 -23.681 1.00 44.14 C ANISOU 183 CA GLN A 77 5021 7092 4659 -431 -435 1004 C ATOM 184 C GLN A 77 -14.521 5.835 -23.649 1.00 40.76 C ANISOU 184 C GLN A 77 4600 6681 4207 -396 -362 952 C ATOM 185 O GLN A 77 -14.335 5.012 -24.509 1.00 41.40 O ANISOU 185 O GLN A 77 4706 6860 4165 -344 -345 869 O ATOM 186 CB GLN A 77 -17.068 5.707 -23.571 1.00 44.16 C ANISOU 186 CB GLN A 77 5059 7066 4653 -451 -502 854 C ATOM 187 CG GLN A 77 -16.964 4.741 -22.455 1.00 43.07 C ANISOU 187 CG GLN A 77 4959 6795 4609 -483 -493 748 C ATOM 188 CD GLN A 77 -16.848 5.385 -21.060 1.00 46.29 C ANISOU 188 CD GLN A 77 5350 7071 5167 -523 -483 810 C ATOM 189 OE1 GLN A 77 -17.667 6.257 -20.692 1.00 42.11 O ANISOU 189 OE1 GLN A 77 4789 6516 4696 -548 -518 863 O ATOM 190 NE2 GLN A 77 -15.824 4.995 -20.298 1.00 41.19 N ANISOU 190 NE2 GLN A 77 4725 6349 4578 -518 -441 799 N ATOM 191 N VAL A 78 -13.642 6.012 -22.692 1.00 40.47 N ANISOU 191 N VAL A 78 4541 6556 4280 -412 -326 989 N ATOM 192 CA VAL A 78 -12.452 5.141 -22.570 1.00 39.32 C ANISOU 192 CA VAL A 78 4392 6425 4123 -362 -269 927 C ATOM 193 C VAL A 78 -12.802 3.690 -22.313 1.00 40.61 C ANISOU 193 C VAL A 78 4634 6521 4275 -334 -296 755 C ATOM 194 O VAL A 78 -13.836 3.434 -21.747 1.00 39.74 O ANISOU 194 O VAL A 78 4569 6312 4217 -385 -354 701 O ATOM 195 CB VAL A 78 -11.437 5.635 -21.515 1.00 42.07 C ANISOU 195 CB VAL A 78 4693 6693 4600 -387 -242 999 C ATOM 196 CG1 VAL A 78 -10.889 6.991 -21.911 1.00 38.06 C ANISOU 196 CG1 VAL A 78 4109 6254 4100 -424 -210 1170 C ATOM 197 CG2 VAL A 78 -12.018 5.627 -20.054 1.00 37.14 C ANISOU 197 CG2 VAL A 78 4110 5888 4112 -440 -299 965 C ATOM 198 N PRO A 79 -11.925 2.723 -22.694 1.00 41.65 N ANISOU 198 N PRO A 79 4782 6700 4343 -252 -255 669 N ATOM 199 CA PRO A 79 -12.339 1.295 -22.449 1.00 42.14 C ANISOU 199 CA PRO A 79 4946 6663 4403 -228 -298 501 C ATOM 200 C PRO A 79 -12.438 0.961 -20.967 1.00 40.17 C ANISOU 200 C PRO A 79 4738 6226 4296 -277 -330 484 C ATOM 201 O PRO A 79 -11.668 1.488 -20.091 1.00 38.26 O ANISOU 201 O PRO A 79 4450 5940 4146 -282 -308 565 O ATOM 202 CB PRO A 79 -11.181 0.461 -23.095 1.00 42.33 C ANISOU 202 CB PRO A 79 4974 6771 4338 -104 -243 421 C ATOM 203 CG PRO A 79 -10.598 1.466 -24.175 1.00 45.05 C ANISOU 203 CG PRO A 79 5217 7326 4575 -76 -170 540 C ATOM 204 CD PRO A 79 -10.665 2.788 -23.435 1.00 41.89 C ANISOU 204 CD PRO A 79 4747 6877 4291 -173 -173 705 C ATOM 205 N LEU A 80 -13.340 0.028 -20.642 1.00 39.38 N ANISOU 205 N LEU A 80 4732 6016 4215 -317 -386 378 N ATOM 206 CA LEU A 80 -13.415 -0.499 -19.274 1.00 40.26 C ANISOU 206 CA LEU A 80 4904 5954 4439 -359 -410 358 C ATOM 207 C LEU A 80 -12.087 -1.137 -18.822 1.00 39.71 C ANISOU 207 C LEU A 80 4859 5833 4396 -265 -387 333 C ATOM 208 O LEU A 80 -11.412 -1.778 -19.613 1.00 41.70 O ANISOU 208 O LEU A 80 5124 6146 4574 -163 -366 260 O ATOM 209 CB LEU A 80 -14.506 -1.564 -19.204 1.00 42.36 C ANISOU 209 CB LEU A 80 5271 6120 4704 -421 -467 246 C ATOM 210 CG LEU A 80 -15.939 -0.936 -19.143 1.00 47.33 C ANISOU 210 CG LEU A 80 5860 6771 5353 -534 -500 279 C ATOM 211 CD1 LEU A 80 -17.029 -2.091 -19.386 1.00 54.06 C ANISOU 211 CD1 LEU A 80 6795 7559 6188 -608 -561 154 C ATOM 212 CD2 LEU A 80 -16.221 -0.185 -17.799 1.00 44.62 C ANISOU 212 CD2 LEU A 80 5484 6353 5118 -601 -490 373 C ATOM 213 N ARG A 81 -11.738 -0.995 -17.538 1.00 39.52 N ANISOU 213 N ARG A 81 4841 5702 4472 -288 -395 385 N ATOM 214 CA ARG A 81 -10.668 -1.747 -16.987 1.00 41.03 C ANISOU 214 CA ARG A 81 5069 5824 4694 -200 -396 351 C ATOM 215 C ARG A 81 -10.934 -1.958 -15.492 1.00 41.77 C ANISOU 215 C ARG A 81 5234 5755 4880 -261 -436 377 C ATOM 216 O ARG A 81 -11.664 -1.185 -14.908 1.00 41.38 O ANISOU 216 O ARG A 81 5163 5689 4871 -358 -441 441 O ATOM 217 CB ARG A 81 -9.349 -1.007 -17.176 1.00 41.15 C ANISOU 217 CB ARG A 81 4960 5963 4714 -126 -348 425 C ATOM 218 CG ARG A 81 -9.477 0.493 -16.822 1.00 37.56 C ANISOU 218 CG ARG A 81 4407 5554 4310 -216 -336 558 C ATOM 219 CD ARG A 81 -8.059 1.186 -16.909 1.00 38.71 C ANISOU 219 CD ARG A 81 4422 5808 4477 -166 -294 637 C ATOM 220 NE ARG A 81 -8.118 2.619 -16.687 1.00 38.68 N ANISOU 220 NE ARG A 81 4337 5834 4525 -256 -291 761 N ATOM 221 CZ ARG A 81 -7.045 3.438 -16.629 1.00 38.55 C ANISOU 221 CZ ARG A 81 4203 5891 4552 -260 -266 851 C ATOM 222 NH1 ARG A 81 -5.823 2.975 -16.657 1.00 36.97 N ANISOU 222 NH1 ARG A 81 3936 5757 4355 -177 -242 832 N ATOM 223 NH2 ARG A 81 -7.268 4.738 -16.410 1.00 36.99 N ANISOU 223 NH2 ARG A 81 3961 5684 4409 -354 -278 957 N ATOM 224 N PRO A 82 -10.351 -2.991 -14.904 1.00 45.33 N ANISOU 224 N PRO A 82 5775 6093 5356 -194 -464 327 N ATOM 225 CA PRO A 82 -10.760 -3.265 -13.493 1.00 47.20 C ANISOU 225 CA PRO A 82 6102 6175 5658 -265 -502 358 C ATOM 226 C PRO A 82 -10.153 -2.291 -12.429 1.00 44.23 C ANISOU 226 C PRO A 82 5655 5810 5340 -274 -503 458 C ATOM 227 O PRO A 82 -9.039 -1.808 -12.582 1.00 43.06 O ANISOU 227 O PRO A 82 5411 5747 5203 -198 -491 490 O ATOM 228 CB PRO A 82 -10.192 -4.655 -13.226 1.00 49.13 C ANISOU 228 CB PRO A 82 6473 6288 5907 -173 -542 285 C ATOM 229 CG PRO A 82 -9.113 -4.900 -14.230 1.00 51.89 C ANISOU 229 CG PRO A 82 6764 6739 6213 -22 -520 227 C ATOM 230 CD PRO A 82 -9.605 -4.124 -15.484 1.00 48.34 C ANISOU 230 CD PRO A 82 6214 6456 5697 -62 -471 226 C ATOM 231 N MET A 83 -10.882 -2.031 -11.384 1.00 44.28 N ANISOU 231 N MET A 83 5706 5739 5378 -368 -518 500 N ATOM 232 CA MET A 83 -10.298 -1.274 -10.251 1.00 46.16 C ANISOU 232 CA MET A 83 5910 5967 5662 -368 -536 573 C ATOM 233 C MET A 83 -9.188 -2.131 -9.547 1.00 44.76 C ANISOU 233 C MET A 83 5797 5710 5501 -267 -582 561 C ATOM 234 O MET A 83 -9.268 -3.326 -9.525 1.00 47.08 O ANISOU 234 O MET A 83 6206 5904 5779 -232 -604 511 O ATOM 235 CB MET A 83 -11.381 -0.820 -9.273 1.00 46.60 C ANISOU 235 CB MET A 83 6006 5971 5730 -479 -536 609 C ATOM 236 CG MET A 83 -10.846 -0.064 -8.029 1.00 49.65 C ANISOU 236 CG MET A 83 6378 6338 6149 -478 -564 667 C ATOM 237 SD MET A 83 -9.983 1.389 -8.478 1.00 48.01 S ANISOU 237 SD MET A 83 6014 6246 5982 -454 -562 715 S ATOM 238 CE MET A 83 -11.036 2.622 -9.238 1.00 46.86 C ANISOU 238 CE MET A 83 5787 6177 5839 -530 -523 742 C ATOM 239 N THR A 84 -8.106 -1.496 -9.077 1.00 40.96 N ANISOU 239 N THR A 84 5232 5278 5053 -215 -604 606 N ATOM 240 CA THR A 84 -7.019 -2.166 -8.388 1.00 39.44 C ANISOU 240 CA THR A 84 5076 5033 4878 -109 -660 601 C ATOM 241 C THR A 84 -6.623 -1.234 -7.274 1.00 38.44 C ANISOU 241 C THR A 84 4904 4916 4787 -143 -700 665 C ATOM 242 O THR A 84 -7.053 -0.056 -7.220 1.00 37.27 O ANISOU 242 O THR A 84 4687 4819 4655 -232 -680 704 O ATOM 243 CB THR A 84 -5.819 -2.325 -9.298 1.00 42.59 C ANISOU 243 CB THR A 84 5362 5538 5281 17 -647 570 C ATOM 244 OG1 THR A 84 -5.345 -0.992 -9.653 1.00 39.53 O ANISOU 244 OG1 THR A 84 4804 5294 4922 -22 -617 628 O ATOM 245 CG2 THR A 84 -6.187 -3.119 -10.613 1.00 42.90 C ANISOU 245 CG2 THR A 84 5434 5596 5268 62 -602 489 C ATOM 246 N TYR A 85 -5.824 -1.751 -6.353 1.00 38.54 N ANISOU 246 N TYR A 85 4965 4869 4809 -66 -769 672 N ATOM 247 CA TYR A 85 -5.382 -0.963 -5.237 1.00 36.60 C ANISOU 247 CA TYR A 85 4690 4631 4586 -89 -826 719 C ATOM 248 C TYR A 85 -4.629 0.293 -5.785 1.00 36.40 C ANISOU 248 C TYR A 85 4471 4745 4615 -106 -814 745 C ATOM 249 O TYR A 85 -4.849 1.400 -5.330 1.00 36.53 O ANISOU 249 O TYR A 85 4449 4776 4654 -191 -826 779 O ATOM 250 CB TYR A 85 -4.460 -1.852 -4.368 1.00 37.63 C ANISOU 250 CB TYR A 85 4890 4695 4713 26 -914 718 C ATOM 251 CG TYR A 85 -3.651 -1.041 -3.330 1.00 37.95 C ANISOU 251 CG TYR A 85 4866 4775 4779 29 -995 755 C ATOM 252 CD1 TYR A 85 -4.128 -0.816 -2.040 1.00 38.58 C ANISOU 252 CD1 TYR A 85 5058 4784 4819 -28 -1041 783 C ATOM 253 CD2 TYR A 85 -2.419 -0.467 -3.688 1.00 39.05 C ANISOU 253 CD2 TYR A 85 4823 5036 4978 82 -1024 757 C ATOM 254 CE1 TYR A 85 -3.375 -0.040 -1.127 1.00 39.94 C ANISOU 254 CE1 TYR A 85 5173 4995 5008 -25 -1128 801 C ATOM 255 CE2 TYR A 85 -1.684 0.328 -2.811 1.00 41.72 C ANISOU 255 CE2 TYR A 85 5089 5413 5349 67 -1109 782 C ATOM 256 CZ TYR A 85 -2.145 0.529 -1.521 1.00 42.72 C ANISOU 256 CZ TYR A 85 5341 5458 5433 18 -1169 798 C ATOM 257 OH TYR A 85 -1.413 1.332 -0.660 1.00 39.94 O ANISOU 257 OH TYR A 85 4924 5144 5107 3 -1266 808 O ATOM 258 N LYS A 86 -3.728 0.080 -6.731 1.00 37.88 N ANISOU 258 N LYS A 86 4543 5028 4820 -23 -792 729 N ATOM 259 CA LYS A 86 -2.820 1.188 -7.237 1.00 39.04 C ANISOU 259 CA LYS A 86 4493 5320 5022 -43 -780 770 C ATOM 260 C LYS A 86 -3.669 2.285 -7.951 1.00 38.47 C ANISOU 260 C LYS A 86 4378 5288 4951 -167 -713 808 C ATOM 261 O LYS A 86 -3.435 3.471 -7.818 1.00 38.98 O ANISOU 261 O LYS A 86 4354 5391 5066 -245 -727 860 O ATOM 262 CB LYS A 86 -1.789 0.586 -8.183 1.00 41.29 C ANISOU 262 CB LYS A 86 4665 5717 5306 80 -747 741 C ATOM 263 CG LYS A 86 -0.699 1.619 -8.691 1.00 43.12 C ANISOU 263 CG LYS A 86 4672 6117 5595 54 -726 795 C ATOM 264 CD LYS A 86 -0.150 2.509 -7.614 1.00 44.73 C ANISOU 264 CD LYS A 86 4815 6309 5869 -14 -815 841 C ATOM 265 CE LYS A 86 1.314 3.099 -8.042 1.00 48.66 C ANISOU 265 CE LYS A 86 5068 6984 6436 -4 -813 883 C ATOM 266 NZ LYS A 86 1.091 3.795 -9.338 1.00 46.06 N ANISOU 266 NZ LYS A 86 4645 6761 6096 -81 -702 933 N ATOM 267 N ALA A 87 -4.671 1.884 -8.700 1.00 38.47 N ANISOU 267 N ALA A 87 4448 5271 4899 -182 -652 781 N ATOM 268 CA ALA A 87 -5.581 2.871 -9.372 1.00 39.35 C ANISOU 268 CA ALA A 87 4529 5417 5004 -284 -601 817 C ATOM 269 C ALA A 87 -6.367 3.635 -8.389 1.00 39.31 C ANISOU 269 C ALA A 87 4587 5328 5023 -372 -636 839 C ATOM 270 O ALA A 87 -6.491 4.851 -8.529 1.00 37.83 O ANISOU 270 O ALA A 87 4334 5166 4873 -442 -634 889 O ATOM 271 CB ALA A 87 -6.553 2.177 -10.374 1.00 40.98 C ANISOU 271 CB ALA A 87 4799 5629 5142 -277 -543 771 C ATOM 272 N ALA A 88 -6.895 2.962 -7.362 1.00 37.73 N ANISOU 272 N ALA A 88 4516 5022 4798 -368 -669 805 N ATOM 273 CA ALA A 88 -7.673 3.676 -6.345 1.00 37.80 C ANISOU 273 CA ALA A 88 4585 4966 4813 -441 -693 817 C ATOM 274 C ALA A 88 -6.747 4.684 -5.596 1.00 37.40 C ANISOU 274 C ALA A 88 4469 4922 4820 -454 -762 847 C ATOM 275 O ALA A 88 -7.177 5.790 -5.225 1.00 35.88 O ANISOU 275 O ALA A 88 4271 4708 4653 -516 -777 862 O ATOM 276 CB ALA A 88 -8.359 2.683 -5.280 1.00 36.58 C ANISOU 276 CB ALA A 88 4587 4709 4604 -438 -707 786 C ATOM 277 N LEU A 89 -5.531 4.262 -5.333 1.00 36.20 N ANISOU 277 N LEU A 89 4275 4792 4687 -390 -811 847 N ATOM 278 CA LEU A 89 -4.536 5.107 -4.626 1.00 38.61 C ANISOU 278 CA LEU A 89 4505 5112 5052 -406 -893 868 C ATOM 279 C LEU A 89 -4.231 6.320 -5.497 1.00 38.12 C ANISOU 279 C LEU A 89 4306 5120 5058 -476 -869 918 C ATOM 280 O LEU A 89 -4.238 7.482 -5.000 1.00 37.66 O ANISOU 280 O LEU A 89 4233 5026 5050 -550 -917 936 O ATOM 281 CB LEU A 89 -3.260 4.305 -4.378 1.00 39.35 C ANISOU 281 CB LEU A 89 4551 5243 5156 -310 -948 858 C ATOM 282 CG LEU A 89 -2.173 5.025 -3.520 1.00 43.16 C ANISOU 282 CG LEU A 89 4953 5748 5699 -325 -1055 870 C ATOM 283 CD1 LEU A 89 -2.596 5.318 -2.069 1.00 42.17 C ANISOU 283 CD1 LEU A 89 4956 5527 5540 -352 -1137 846 C ATOM 284 CD2 LEU A 89 -0.847 4.172 -3.515 1.00 42.60 C ANISOU 284 CD2 LEU A 89 4795 5747 5645 -209 -1104 861 C ATOM 285 N ASP A 90 -3.940 6.041 -6.773 1.00 37.54 N ANISOU 285 N ASP A 90 4143 5141 4981 -452 -797 941 N ATOM 286 CA ASP A 90 -3.567 7.131 -7.732 1.00 39.47 C ANISOU 286 CA ASP A 90 4252 5466 5277 -522 -762 1011 C ATOM 287 C ASP A 90 -4.724 8.129 -7.904 1.00 38.39 C ANISOU 287 C ASP A 90 4172 5268 5146 -605 -744 1038 C ATOM 288 O ASP A 90 -4.547 9.353 -7.874 1.00 37.07 O ANISOU 288 O ASP A 90 3957 5082 5047 -686 -775 1091 O ATOM 289 CB ASP A 90 -3.103 6.558 -9.078 1.00 38.31 C ANISOU 289 CB ASP A 90 4011 5451 5095 -468 -677 1027 C ATOM 290 CG ASP A 90 -1.730 5.904 -9.018 1.00 43.11 C ANISOU 290 CG ASP A 90 4510 6147 5721 -383 -695 1013 C ATOM 291 OD1 ASP A 90 -0.991 6.066 -8.020 1.00 43.55 O ANISOU 291 OD1 ASP A 90 4535 6178 5833 -384 -783 1008 O ATOM 292 OD2 ASP A 90 -1.390 5.147 -9.940 1.00 49.21 O ANISOU 292 OD2 ASP A 90 5232 7018 6447 -299 -628 994 O ATOM 293 N ILE A 91 -5.955 7.616 -8.022 1.00 38.54 N ANISOU 293 N ILE A 91 4297 5247 5099 -585 -703 999 N ATOM 294 CA ILE A 91 -7.125 8.485 -8.126 1.00 38.62 C ANISOU 294 CA ILE A 91 4355 5207 5112 -641 -691 1014 C ATOM 295 C ILE A 91 -7.388 9.294 -6.877 1.00 38.12 C ANISOU 295 C ILE A 91 4353 5042 5089 -677 -762 993 C ATOM 296 O ILE A 91 -7.658 10.511 -6.977 1.00 38.35 O ANISOU 296 O ILE A 91 4369 5034 5170 -729 -782 1028 O ATOM 297 CB ILE A 91 -8.388 7.709 -8.515 1.00 40.58 C ANISOU 297 CB ILE A 91 4682 5454 5285 -616 -636 970 C ATOM 298 CG1 ILE A 91 -8.185 7.075 -9.901 1.00 41.97 C ANISOU 298 CG1 ILE A 91 4801 5731 5413 -582 -573 982 C ATOM 299 CG2 ILE A 91 -9.667 8.645 -8.397 1.00 41.38 C ANISOU 299 CG2 ILE A 91 4823 5505 5394 -659 -636 975 C ATOM 300 CD1 ILE A 91 -9.258 5.905 -10.025 1.00 45.45 C ANISOU 300 CD1 ILE A 91 5337 6150 5781 -555 -541 911 C ATOM 301 N SER A 92 -7.202 8.673 -5.713 1.00 37.96 N ANISOU 301 N SER A 92 4402 4976 5044 -644 -807 939 N ATOM 302 CA SER A 92 -7.253 9.402 -4.434 1.00 38.27 C ANISOU 302 CA SER A 92 4502 4935 5105 -667 -883 908 C ATOM 303 C SER A 92 -6.294 10.594 -4.430 1.00 38.29 C ANISOU 303 C SER A 92 4419 4926 5205 -726 -953 947 C ATOM 304 O SER A 92 -6.713 11.690 -4.098 1.00 39.64 O ANISOU 304 O SER A 92 4622 5024 5414 -767 -990 941 O ATOM 305 CB SER A 92 -6.896 8.504 -3.223 1.00 40.46 C ANISOU 305 CB SER A 92 4857 5185 5330 -619 -932 859 C ATOM 306 OG SER A 92 -7.677 7.359 -3.152 1.00 38.81 O ANISOU 306 OG SER A 92 4735 4971 5040 -581 -875 835 O ATOM 307 N HIS A 93 -5.025 10.382 -4.800 1.00 39.91 N ANISOU 307 N HIS A 93 4513 5201 5451 -729 -972 984 N ATOM 308 CA HIS A 93 -4.061 11.468 -4.783 1.00 42.90 C ANISOU 308 CA HIS A 93 4795 5574 5930 -808 -1040 1028 C ATOM 309 C HIS A 93 -4.417 12.593 -5.837 1.00 42.19 C ANISOU 309 C HIS A 93 4661 5473 5897 -886 -1000 1109 C ATOM 310 O HIS A 93 -4.268 13.833 -5.563 1.00 43.13 O ANISOU 310 O HIS A 93 4780 5507 6099 -967 -1069 1131 O ATOM 311 CB HIS A 93 -2.620 10.960 -4.991 1.00 44.96 C ANISOU 311 CB HIS A 93 4918 5941 6225 -795 -1060 1055 C ATOM 312 CG HIS A 93 -2.107 10.153 -3.820 1.00 50.14 C ANISOU 312 CG HIS A 93 5616 6588 6847 -724 -1139 988 C ATOM 313 ND1 HIS A 93 -1.330 9.032 -3.978 1.00 58.25 N ANISOU 313 ND1 HIS A 93 6581 7704 7848 -636 -1129 981 N ATOM 314 CD2 HIS A 93 -2.211 10.348 -2.479 1.00 57.66 C ANISOU 314 CD2 HIS A 93 6667 7457 7783 -721 -1238 927 C ATOM 315 CE1 HIS A 93 -0.980 8.560 -2.781 1.00 57.89 C ANISOU 315 CE1 HIS A 93 6598 7624 7776 -583 -1223 929 C ATOM 316 NE2 HIS A 93 -1.513 9.333 -1.855 1.00 55.65 N ANISOU 316 NE2 HIS A 93 6414 7242 7489 -636 -1288 897 N ATOM 317 N PHE A 94 -4.854 12.158 -7.004 1.00 40.03 N ANISOU 317 N PHE A 94 4360 5275 5575 -860 -900 1150 N ATOM 318 CA PHE A 94 -5.241 13.079 -8.082 1.00 40.37 C ANISOU 318 CA PHE A 94 4372 5320 5646 -918 -858 1238 C ATOM 319 C PHE A 94 -6.380 13.947 -7.620 1.00 41.72 C ANISOU 319 C PHE A 94 4655 5363 5833 -928 -895 1211 C ATOM 320 O PHE A 94 -6.367 15.180 -7.864 1.00 40.02 O ANISOU 320 O PHE A 94 4436 5076 5695 -997 -933 1274 O ATOM 321 CB PHE A 94 -5.606 12.326 -9.367 1.00 40.27 C ANISOU 321 CB PHE A 94 4327 5423 5550 -871 -751 1269 C ATOM 322 CG PHE A 94 -6.009 13.255 -10.528 1.00 43.80 C ANISOU 322 CG PHE A 94 4750 5887 6007 -923 -712 1372 C ATOM 323 CD1 PHE A 94 -5.019 13.856 -11.329 1.00 48.34 C ANISOU 323 CD1 PHE A 94 5209 6534 6626 -998 -690 1486 C ATOM 324 CD2 PHE A 94 -7.333 13.581 -10.718 1.00 46.04 C ANISOU 324 CD2 PHE A 94 5122 6111 6259 -900 -705 1361 C ATOM 325 CE1 PHE A 94 -5.417 14.746 -12.385 1.00 50.41 C ANISOU 325 CE1 PHE A 94 5466 6800 6886 -1049 -658 1600 C ATOM 326 CE2 PHE A 94 -7.700 14.482 -11.743 1.00 47.26 C ANISOU 326 CE2 PHE A 94 5264 6270 6420 -937 -686 1464 C ATOM 327 CZ PHE A 94 -6.730 15.050 -12.549 1.00 46.08 C ANISOU 327 CZ PHE A 94 5020 6181 6305 -1013 -665 1587 C ATOM 328 N LEU A 95 -7.397 13.357 -6.986 1.00 38.66 N ANISOU 328 N LEU A 95 4369 4944 5376 -859 -883 1123 N ATOM 329 CA LEU A 95 -8.538 14.181 -6.582 1.00 38.41 C ANISOU 329 CA LEU A 95 4428 4813 5354 -850 -907 1090 C ATOM 330 C LEU A 95 -8.259 15.062 -5.370 1.00 39.06 C ANISOU 330 C LEU A 95 4567 4777 5498 -875 -1009 1038 C ATOM 331 O LEU A 95 -8.860 16.159 -5.232 1.00 39.24 O ANISOU 331 O LEU A 95 4645 4698 5567 -881 -1048 1031 O ATOM 332 CB LEU A 95 -9.772 13.295 -6.336 1.00 37.99 C ANISOU 332 CB LEU A 95 4444 4786 5205 -779 -849 1017 C ATOM 333 CG LEU A 95 -10.252 12.561 -7.594 1.00 38.48 C ANISOU 333 CG LEU A 95 4464 4948 5209 -758 -764 1054 C ATOM 334 CD1 LEU A 95 -11.386 11.491 -7.234 1.00 40.99 C ANISOU 334 CD1 LEU A 95 4845 5291 5440 -710 -714 975 C ATOM 335 CD2 LEU A 95 -10.683 13.596 -8.727 1.00 37.70 C ANISOU 335 CD2 LEU A 95 4331 4850 5144 -779 -755 1138 C ATOM 336 N LYS A 96 -7.410 14.595 -4.477 1.00 38.58 N ANISOU 336 N LYS A 96 4504 4723 5432 -877 -1060 993 N ATOM 337 CA LYS A 96 -6.928 15.406 -3.386 1.00 40.65 C ANISOU 337 CA LYS A 96 4808 4886 5749 -910 -1173 942 C ATOM 338 C LYS A 96 -6.246 16.677 -3.932 1.00 44.17 C ANISOU 338 C LYS A 96 5195 5266 6323 -1012 -1233 1020 C ATOM 339 O LYS A 96 -6.514 17.801 -3.484 1.00 43.82 O ANISOU 339 O LYS A 96 5220 5089 6339 -1039 -1309 990 O ATOM 340 CB LYS A 96 -5.926 14.658 -2.483 1.00 41.71 C ANISOU 340 CB LYS A 96 4927 5061 5858 -900 -1232 898 C ATOM 341 CG LYS A 96 -5.323 15.568 -1.322 1.00 46.93 C ANISOU 341 CG LYS A 96 5630 5625 6576 -944 -1374 834 C ATOM 342 CD LYS A 96 -4.327 14.871 -0.393 1.00 54.53 C ANISOU 342 CD LYS A 96 6575 6635 7508 -926 -1452 791 C ATOM 343 CE LYS A 96 -3.731 15.881 0.692 1.00 57.62 C ANISOU 343 CE LYS A 96 7007 6930 7957 -981 -1611 720 C ATOM 344 NZ LYS A 96 -3.110 17.135 0.210 1.00 65.82 N ANISOU 344 NZ LYS A 96 7972 7894 9143 -1104 -1681 768 N ATOM 345 N GLU A 97 -5.346 16.476 -4.877 1.00 45.29 N ANISOU 345 N GLU A 97 5208 5498 6502 -1070 -1197 1119 N ATOM 346 CA GLU A 97 -4.595 17.593 -5.408 1.00 47.36 C ANISOU 346 CA GLU A 97 5400 5712 6883 -1189 -1245 1214 C ATOM 347 C GLU A 97 -5.520 18.471 -6.282 1.00 48.37 C ANISOU 347 C GLU A 97 5579 5767 7034 -1201 -1209 1285 C ATOM 348 O GLU A 97 -5.376 19.687 -6.242 1.00 45.58 O ANISOU 348 O GLU A 97 5256 5280 6782 -1281 -1286 1323 O ATOM 349 CB GLU A 97 -3.474 17.077 -6.237 1.00 50.14 C ANISOU 349 CB GLU A 97 5591 6212 7250 -1238 -1192 1305 C ATOM 350 CG GLU A 97 -2.494 18.122 -6.549 1.00 63.11 C ANISOU 350 CG GLU A 97 7140 7821 9018 -1383 -1248 1401 C ATOM 351 CD GLU A 97 -1.623 18.396 -5.300 1.00 71.20 C ANISOU 351 CD GLU A 97 8153 8785 10115 -1436 -1387 1323 C ATOM 352 OE1 GLU A 97 -1.743 17.622 -4.261 1.00 76.19 O ANISOU 352 OE1 GLU A 97 8845 9429 10675 -1340 -1426 1202 O ATOM 353 OE2 GLU A 97 -0.840 19.347 -5.413 1.00 79.89 O ANISOU 353 OE2 GLU A 97 9185 9834 11336 -1576 -1456 1390 O ATOM 354 N LYS A 98 -6.468 17.872 -7.021 1.00 42.99 N ANISOU 354 N LYS A 98 4914 5159 6261 -1121 -1109 1299 N ATOM 355 CA LYS A 98 -7.387 18.677 -7.854 1.00 45.70 C ANISOU 355 CA LYS A 98 5303 5443 6617 -1114 -1087 1367 C ATOM 356 C LYS A 98 -8.273 19.616 -7.053 1.00 45.27 C ANISOU 356 C LYS A 98 5377 5220 6603 -1074 -1165 1290 C ATOM 357 O LYS A 98 -8.446 20.793 -7.423 1.00 45.23 O ANISOU 357 O LYS A 98 5413 5092 6679 -1113 -1215 1356 O ATOM 358 CB LYS A 98 -8.308 17.812 -8.716 1.00 43.23 C ANISOU 358 CB LYS A 98 4983 5250 6193 -1030 -981 1376 C ATOM 359 CG LYS A 98 -9.120 18.604 -9.719 1.00 48.84 C ANISOU 359 CG LYS A 98 5720 5927 6909 -1021 -965 1464 C ATOM 360 CD LYS A 98 -9.825 17.644 -10.720 1.00 47.75 C ANISOU 360 CD LYS A 98 5550 5940 6654 -954 -866 1478 C ATOM 361 CE LYS A 98 -10.556 18.305 -11.792 1.00 56.39 C ANISOU 361 CE LYS A 98 6660 7031 7735 -938 -855 1572 C ATOM 362 NZ LYS A 98 -9.717 19.185 -12.714 1.00 53.18 N ANISOU 362 NZ LYS A 98 6212 6613 7381 -1037 -861 1739 N ATOM 363 N GLY A 99 -8.757 19.141 -5.921 1.00 42.51 N ANISOU 363 N GLY A 99 5096 4859 6199 -997 -1181 1153 N ATOM 364 CA GLY A 99 -9.621 19.933 -5.105 1.00 44.18 C ANISOU 364 CA GLY A 99 5423 4936 6427 -936 -1242 1060 C ATOM 365 C GLY A 99 -11.093 19.608 -5.435 1.00 44.05 C ANISOU 365 C GLY A 99 5436 4971 6329 -824 -1163 1029 C ATOM 366 O GLY A 99 -11.395 19.135 -6.506 1.00 44.79 O ANISOU 366 O GLY A 99 5469 5164 6383 -818 -1087 1106 O ATOM 367 N GLY A 100 -11.975 19.916 -4.505 1.00 43.67 N ANISOU 367 N GLY A 100 5476 4861 6257 -738 -1187 912 N ATOM 368 CA GLY A 100 -13.389 19.844 -4.737 1.00 44.54 C ANISOU 368 CA GLY A 100 5601 5011 6312 -633 -1127 877 C ATOM 369 C GLY A 100 -14.083 18.634 -4.105 1.00 40.41 C ANISOU 369 C GLY A 100 5071 4615 5667 -575 -1043 788 C ATOM 370 O GLY A 100 -15.283 18.712 -3.854 1.00 42.58 O ANISOU 370 O GLY A 100 5367 4913 5900 -486 -1008 722 O ATOM 371 N LEU A 101 -13.368 17.549 -3.810 1.00 40.48 N ANISOU 371 N LEU A 101 5054 4704 5623 -622 -1014 787 N ATOM 372 CA LEU A 101 -14.008 16.391 -3.163 1.00 38.35 C ANISOU 372 CA LEU A 101 4797 4534 5241 -581 -939 716 C ATOM 373 C LEU A 101 -13.892 16.500 -1.613 1.00 39.69 C ANISOU 373 C LEU A 101 5056 4658 5368 -552 -982 607 C ATOM 374 O LEU A 101 -14.841 16.330 -0.854 1.00 39.29 O ANISOU 374 O LEU A 101 5048 4641 5240 -488 -939 526 O ATOM 375 CB LEU A 101 -13.432 15.113 -3.713 1.00 37.58 C ANISOU 375 CB LEU A 101 4643 4535 5101 -628 -886 772 C ATOM 376 CG LEU A 101 -13.980 13.827 -3.047 1.00 38.67 C ANISOU 376 CG LEU A 101 4810 4753 5131 -606 -817 716 C ATOM 377 CD1 LEU A 101 -15.502 13.838 -3.318 1.00 35.92 C ANISOU 377 CD1 LEU A 101 4446 4457 4746 -560 -749 687 C ATOM 378 CD2 LEU A 101 -13.427 12.600 -3.672 1.00 38.41 C ANISOU 378 CD2 LEU A 101 4735 4791 5067 -640 -776 765 C ATOM 379 N GLU A 102 -12.707 16.902 -1.144 1.00 39.52 N ANISOU 379 N GLU A 102 5057 4561 5396 -601 -1075 605 N ATOM 380 CA GLU A 102 -12.501 17.141 0.279 1.00 39.83 C ANISOU 380 CA GLU A 102 5189 4552 5393 -573 -1140 499 C ATOM 381 C GLU A 102 -13.566 18.092 0.805 1.00 41.49 C ANISOU 381 C GLU A 102 5470 4700 5594 -485 -1148 403 C ATOM 382 O GLU A 102 -13.775 19.202 0.231 1.00 42.39 O ANISOU 382 O GLU A 102 5586 4714 5807 -473 -1193 420 O ATOM 383 CB GLU A 102 -11.073 17.657 0.518 1.00 41.84 C ANISOU 383 CB GLU A 102 5442 4726 5731 -649 -1262 513 C ATOM 384 CG GLU A 102 -10.740 17.946 1.921 1.00 43.28 C ANISOU 384 CG GLU A 102 5719 4857 5869 -627 -1352 401 C ATOM 385 CD GLU A 102 -10.456 16.629 2.698 1.00 47.90 C ANISOU 385 CD GLU A 102 6322 5550 6327 -611 -1321 384 C ATOM 386 OE1 GLU A 102 -9.910 15.698 2.137 1.00 53.46 O ANISOU 386 OE1 GLU A 102 6953 6327 7032 -647 -1285 465 O ATOM 387 OE2 GLU A 102 -10.822 16.526 3.850 1.00 50.44 O ANISOU 387 OE2 GLU A 102 6737 5883 6543 -554 -1331 291 O ATOM 388 N GLY A 103 -14.233 17.704 1.891 1.00 39.80 N ANISOU 388 N GLY A 103 5319 4543 5261 -417 -1106 306 N ATOM 389 CA GLY A 103 -15.256 18.515 2.547 1.00 41.14 C ANISOU 389 CA GLY A 103 5553 4681 5399 -311 -1100 193 C ATOM 390 C GLY A 103 -16.637 18.556 1.910 1.00 40.71 C ANISOU 390 C GLY A 103 5438 4694 5336 -240 -1002 198 C ATOM 391 O GLY A 103 -17.588 19.108 2.486 1.00 43.50 O ANISOU 391 O GLY A 103 5826 5053 5649 -133 -979 97 O ATOM 392 N LEU A 104 -16.786 17.983 0.730 1.00 39.97 N ANISOU 392 N LEU A 104 5250 4662 5275 -288 -946 307 N ATOM 393 CA LEU A 104 -18.098 17.942 0.088 1.00 39.91 C ANISOU 393 CA LEU A 104 5171 4736 5257 -226 -863 313 C ATOM 394 C LEU A 104 -19.078 17.157 0.947 1.00 40.71 C ANISOU 394 C LEU A 104 5266 4973 5228 -184 -756 241 C ATOM 395 O LEU A 104 -18.745 16.102 1.395 1.00 39.11 O ANISOU 395 O LEU A 104 5078 4836 4947 -245 -713 258 O ATOM 396 CB LEU A 104 -17.994 17.292 -1.283 1.00 38.39 C ANISOU 396 CB LEU A 104 4886 4602 5100 -297 -827 436 C ATOM 397 CG LEU A 104 -19.217 17.264 -2.211 1.00 40.73 C ANISOU 397 CG LEU A 104 5094 4982 5400 -249 -767 461 C ATOM 398 CD1 LEU A 104 -19.561 18.666 -2.621 1.00 42.27 C ANISOU 398 CD1 LEU A 104 5302 5073 5685 -166 -838 457 C ATOM 399 CD2 LEU A 104 -18.892 16.319 -3.425 1.00 38.63 C ANISOU 399 CD2 LEU A 104 4755 4789 5134 -337 -733 569 C ATOM 400 N ILE A 105 -20.294 17.681 1.107 1.00 42.25 N ANISOU 400 N ILE A 105 5433 5214 5406 -78 -712 169 N ATOM 401 CA ILE A 105 -21.363 17.049 1.827 1.00 43.37 C ANISOU 401 CA ILE A 105 5542 5507 5431 -38 -596 108 C ATOM 402 C ILE A 105 -21.908 15.846 0.979 1.00 42.81 C ANISOU 402 C ILE A 105 5360 5567 5340 -122 -504 195 C ATOM 403 O ILE A 105 -22.164 15.968 -0.236 1.00 41.03 O ANISOU 403 O ILE A 105 5055 5344 5192 -130 -519 258 O ATOM 404 CB ILE A 105 -22.529 18.007 2.112 1.00 46.38 C ANISOU 404 CB ILE A 105 5896 5916 5812 112 -574 4 C ATOM 405 CG1 ILE A 105 -22.094 19.218 2.984 1.00 50.13 C ANISOU 405 CG1 ILE A 105 6495 6250 6302 209 -671 -107 C ATOM 406 CG2 ILE A 105 -23.765 17.230 2.791 1.00 47.23 C ANISOU 406 CG2 ILE A 105 5927 6229 5788 139 -424 -48 C ATOM 407 CD1 ILE A 105 -21.974 18.927 4.466 1.00 52.44 C ANISOU 407 CD1 ILE A 105 6877 6596 6452 229 -635 -206 C ATOM 408 N TRP A 106 -21.935 14.691 1.611 1.00 42.50 N ANISOU 408 N TRP A 106 5335 5615 5198 -193 -427 205 N ATOM 409 CA TRP A 106 -22.261 13.430 0.966 1.00 41.97 C ANISOU 409 CA TRP A 106 5196 5640 5110 -293 -355 281 C ATOM 410 C TRP A 106 -23.758 13.350 0.745 1.00 43.35 C ANISOU 410 C TRP A 106 5250 5956 5266 -261 -264 252 C ATOM 411 O TRP A 106 -24.557 13.695 1.629 1.00 43.37 O ANISOU 411 O TRP A 106 5238 6037 5204 -188 -203 173 O ATOM 412 CB TRP A 106 -21.879 12.254 1.859 1.00 42.95 C ANISOU 412 CB TRP A 106 5394 5797 5129 -375 -305 301 C ATOM 413 CG TRP A 106 -22.143 10.947 1.161 1.00 40.31 C ANISOU 413 CG TRP A 106 5007 5522 4787 -484 -248 377 C ATOM 414 CD1 TRP A 106 -21.311 10.329 0.317 1.00 40.11 C ANISOU 414 CD1 TRP A 106 4992 5437 4811 -550 -294 446 C ATOM 415 CD2 TRP A 106 -23.294 10.137 1.270 1.00 42.66 C ANISOU 415 CD2 TRP A 106 5236 5947 5027 -539 -139 381 C ATOM 416 NE1 TRP A 106 -21.889 9.191 -0.174 1.00 38.81 N ANISOU 416 NE1 TRP A 106 4781 5339 4627 -636 -231 485 N ATOM 417 CE2 TRP A 106 -23.103 9.032 0.413 1.00 40.77 C ANISOU 417 CE2 TRP A 106 4980 5698 4813 -644 -138 451 C ATOM 418 CE3 TRP A 106 -24.467 10.232 1.990 1.00 45.40 C ANISOU 418 CE3 TRP A 106 5526 6420 5303 -513 -41 330 C ATOM 419 CZ2 TRP A 106 -24.037 8.039 0.257 1.00 43.44 C ANISOU 419 CZ2 TRP A 106 5257 6129 5120 -738 -55 473 C ATOM 420 CZ3 TRP A 106 -25.445 9.203 1.848 1.00 49.90 C ANISOU 420 CZ3 TRP A 106 6013 7108 5837 -616 58 363 C ATOM 421 CH2 TRP A 106 -25.211 8.128 0.986 1.00 45.86 C ANISOU 421 CH2 TRP A 106 5497 6563 5364 -733 43 435 C ATOM 422 N SER A 107 -24.097 12.851 -0.432 1.00 42.97 N ANISOU 422 N SER A 107 5110 5950 5266 -318 -257 314 N ATOM 423 CA SER A 107 -25.417 12.290 -0.718 1.00 43.12 C ANISOU 423 CA SER A 107 4999 6123 5260 -344 -169 307 C ATOM 424 C SER A 107 -25.226 11.129 -1.669 1.00 41.57 C ANISOU 424 C SER A 107 4777 5940 5079 -472 -167 384 C ATOM 425 O SER A 107 -24.221 11.004 -2.360 1.00 36.46 O ANISOU 425 O SER A 107 4182 5197 4474 -503 -236 437 O ATOM 426 CB SER A 107 -26.368 13.316 -1.297 1.00 43.59 C ANISOU 426 CB SER A 107 4948 6234 5380 -226 -189 266 C ATOM 427 OG SER A 107 -26.060 13.440 -2.686 1.00 41.37 O ANISOU 427 OG SER A 107 4636 5903 5179 -243 -267 334 O ATOM 428 N GLN A 108 -26.243 10.270 -1.736 1.00 40.79 N ANISOU 428 N GLN A 108 4585 5968 4945 -547 -86 385 N ATOM 429 CA GLN A 108 -26.175 9.136 -2.644 1.00 41.18 C ANISOU 429 CA GLN A 108 4614 6024 5008 -669 -91 440 C ATOM 430 C GLN A 108 -26.082 9.627 -4.125 1.00 40.18 C ANISOU 430 C GLN A 108 4427 5880 4959 -629 -177 463 C ATOM 431 O GLN A 108 -25.250 9.153 -4.908 1.00 37.22 O ANISOU 431 O GLN A 108 4103 5436 4602 -677 -226 510 O ATOM 432 CB GLN A 108 -27.444 8.239 -2.443 1.00 45.31 C ANISOU 432 CB GLN A 108 5033 6693 5492 -769 5 429 C ATOM 433 CG GLN A 108 -27.452 7.062 -3.361 1.00 50.05 C ANISOU 433 CG GLN A 108 5620 7286 6109 -900 -11 470 C ATOM 434 CD GLN A 108 -26.429 6.071 -3.018 1.00 55.57 C ANISOU 434 CD GLN A 108 6469 7868 6776 -982 -16 515 C ATOM 435 OE1 GLN A 108 -26.090 5.893 -1.852 1.00 63.97 O ANISOU 435 OE1 GLN A 108 7626 8900 7780 -991 27 524 O ATOM 436 NE2 GLN A 108 -25.872 5.423 -4.054 1.00 61.53 N ANISOU 436 NE2 GLN A 108 7257 8557 7565 -1030 -77 540 N ATOM 437 N ARG A 109 -26.838 10.662 -4.469 1.00 39.31 N ANISOU 437 N ARG A 109 4221 5826 4887 -523 -199 432 N ATOM 438 CA ARG A 109 -26.763 11.191 -5.800 1.00 41.03 C ANISOU 438 CA ARG A 109 4397 6029 5164 -478 -282 467 C ATOM 439 C ARG A 109 -25.410 11.807 -6.138 1.00 38.98 C ANISOU 439 C ARG A 109 4249 5621 4941 -444 -359 519 C ATOM 440 O ARG A 109 -24.848 11.560 -7.194 1.00 37.36 O ANISOU 440 O ARG A 109 4053 5391 4749 -479 -404 575 O ATOM 441 CB ARG A 109 -27.814 12.302 -5.928 1.00 44.13 C ANISOU 441 CB ARG A 109 4682 6494 5592 -345 -300 426 C ATOM 442 CG ARG A 109 -27.717 13.072 -7.227 1.00 45.45 C ANISOU 442 CG ARG A 109 4825 6629 5813 -273 -398 476 C ATOM 443 CD ARG A 109 -28.894 14.101 -7.442 1.00 50.75 C ANISOU 443 CD ARG A 109 5381 7380 6523 -126 -428 437 C ATOM 444 NE ARG A 109 -28.479 15.117 -8.464 1.00 54.00 N ANISOU 444 NE ARG A 109 5832 7699 6988 -37 -536 505 N ATOM 445 CZ ARG A 109 -28.752 15.004 -9.764 1.00 54.20 C ANISOU 445 CZ ARG A 109 5797 7785 7013 -44 -595 559 C ATOM 446 NH1 ARG A 109 -29.324 13.933 -10.229 1.00 50.92 N ANISOU 446 NH1 ARG A 109 5288 7503 6556 -138 -567 545 N ATOM 447 NH2 ARG A 109 -28.363 15.909 -10.619 1.00 56.77 N ANISOU 447 NH2 ARG A 109 6169 8027 7373 30 -684 635 N ATOM 448 N ARG A 110 -24.846 12.566 -5.186 1.00 38.38 N ANISOU 448 N ARG A 110 4256 5452 4873 -383 -371 495 N ATOM 449 CA ARG A 110 -23.489 13.087 -5.411 1.00 39.23 C ANISOU 449 CA ARG A 110 4461 5422 5024 -379 -443 546 C ATOM 450 C ARG A 110 -22.438 12.043 -5.618 1.00 37.13 C ANISOU 450 C ARG A 110 4251 5123 4733 -480 -439 593 C ATOM 451 O ARG A 110 -21.576 12.154 -6.498 1.00 38.81 O ANISOU 451 O ARG A 110 4480 5289 4979 -497 -488 656 O ATOM 452 CB ARG A 110 -23.101 14.040 -4.258 1.00 39.66 C ANISOU 452 CB ARG A 110 4597 5381 5091 -307 -467 496 C ATOM 453 CG ARG A 110 -23.913 15.315 -4.284 1.00 44.14 C ANISOU 453 CG ARG A 110 5127 5938 5704 -176 -501 454 C ATOM 454 CD ARG A 110 -23.348 16.261 -3.243 1.00 46.14 C ANISOU 454 CD ARG A 110 5487 6069 5977 -110 -545 398 C ATOM 455 NE ARG A 110 -24.199 17.451 -3.216 1.00 47.52 N ANISOU 455 NE ARG A 110 5636 6225 6196 34 -577 341 N ATOM 456 CZ ARG A 110 -24.083 18.410 -2.340 1.00 50.13 C ANISOU 456 CZ ARG A 110 6048 6458 6543 127 -617 262 C ATOM 457 NH1 ARG A 110 -23.174 18.330 -1.361 1.00 48.64 N ANISOU 457 NH1 ARG A 110 5966 6194 6321 84 -631 227 N ATOM 458 NH2 ARG A 110 -24.867 19.465 -2.416 1.00 52.53 N ANISOU 458 NH2 ARG A 110 6331 6735 6892 273 -652 210 N ATOM 459 N GLN A 111 -22.473 11.018 -4.816 1.00 35.72 N ANISOU 459 N GLN A 111 4105 4971 4495 -545 -380 568 N ATOM 460 CA GLN A 111 -21.564 9.876 -4.947 1.00 35.94 C ANISOU 460 CA GLN A 111 4193 4966 4498 -628 -377 604 C ATOM 461 C GLN A 111 -21.725 9.240 -6.325 1.00 35.66 C ANISOU 461 C GLN A 111 4100 4979 4469 -671 -384 636 C ATOM 462 O GLN A 111 -20.741 8.990 -7.020 1.00 37.36 O ANISOU 462 O GLN A 111 4343 5155 4695 -685 -418 678 O ATOM 463 CB GLN A 111 -21.773 8.827 -3.840 1.00 36.99 C ANISOU 463 CB GLN A 111 4379 5116 4561 -690 -313 580 C ATOM 464 CG GLN A 111 -20.664 7.716 -3.878 1.00 42.03 C ANISOU 464 CG GLN A 111 5103 5688 5180 -751 -328 617 C ATOM 465 CD GLN A 111 -20.968 6.681 -2.846 1.00 49.27 C ANISOU 465 CD GLN A 111 6085 6611 6026 -814 -270 610 C ATOM 466 OE1 GLN A 111 -21.011 6.979 -1.644 1.00 49.28 O ANISOU 466 OE1 GLN A 111 6135 6609 5980 -791 -249 591 O ATOM 467 NE2 GLN A 111 -21.414 5.510 -3.304 1.00 56.86 N ANISOU 467 NE2 GLN A 111 7039 7593 6971 -899 -238 623 N ATOM 468 N GLU A 112 -22.957 8.998 -6.776 1.00 35.84 N ANISOU 468 N GLU A 112 4035 5102 4481 -688 -356 612 N ATOM 469 CA GLU A 112 -23.156 8.489 -8.134 1.00 35.17 C ANISOU 469 CA GLU A 112 3898 5070 4394 -721 -379 631 C ATOM 470 C GLU A 112 -22.653 9.415 -9.229 1.00 36.93 C ANISOU 470 C GLU A 112 4104 5280 4649 -656 -443 682 C ATOM 471 O GLU A 112 -22.089 8.948 -10.224 1.00 36.76 O ANISOU 471 O GLU A 112 4092 5266 4609 -679 -464 712 O ATOM 472 CB GLU A 112 -24.672 8.222 -8.373 1.00 36.97 C ANISOU 472 CB GLU A 112 4014 5421 4611 -749 -352 590 C ATOM 473 CG GLU A 112 -25.149 7.054 -7.456 1.00 38.13 C ANISOU 473 CG GLU A 112 4178 5587 4721 -855 -280 558 C ATOM 474 CD GLU A 112 -26.635 6.777 -7.543 1.00 46.86 C ANISOU 474 CD GLU A 112 5155 6826 5823 -904 -245 520 C ATOM 475 OE1 GLU A 112 -27.307 7.467 -8.252 1.00 45.60 O ANISOU 475 OE1 GLU A 112 4892 6747 5688 -843 -281 509 O ATOM 476 OE2 GLU A 112 -27.089 5.898 -6.810 1.00 48.63 O ANISOU 476 OE2 GLU A 112 5385 7073 6020 -1004 -180 507 O ATOM 477 N ILE A 113 -22.876 10.733 -9.075 1.00 37.09 N ANISOU 477 N ILE A 113 4102 5279 4712 -570 -473 694 N ATOM 478 CA ILE A 113 -22.348 11.701 -10.060 1.00 36.42 C ANISOU 478 CA ILE A 113 4017 5161 4661 -517 -536 765 C ATOM 479 C ILE A 113 -20.801 11.560 -10.193 1.00 36.52 C ANISOU 479 C ILE A 113 4102 5095 4679 -553 -548 819 C ATOM 480 O ILE A 113 -20.210 11.522 -11.328 1.00 36.71 O ANISOU 480 O ILE A 113 4117 5141 4689 -563 -568 881 O ATOM 481 CB ILE A 113 -22.836 13.101 -9.839 1.00 35.77 C ANISOU 481 CB ILE A 113 3919 5042 4631 -419 -576 769 C ATOM 482 CG1 ILE A 113 -24.354 13.201 -10.191 1.00 40.96 C ANISOU 482 CG1 ILE A 113 4469 5816 5279 -368 -576 730 C ATOM 483 CG2 ILE A 113 -21.944 14.213 -10.582 1.00 39.00 C ANISOU 483 CG2 ILE A 113 4370 5360 5089 -384 -645 866 C ATOM 484 CD1 ILE A 113 -25.001 14.562 -9.793 1.00 41.09 C ANISOU 484 CD1 ILE A 113 4468 5796 5350 -240 -613 711 C ATOM 485 N LEU A 114 -20.124 11.498 -9.065 1.00 36.69 N ANISOU 485 N LEU A 114 4186 5039 4715 -568 -537 796 N ATOM 486 CA LEU A 114 -18.682 11.357 -9.048 1.00 36.88 C ANISOU 486 CA LEU A 114 4259 5001 4752 -598 -553 838 C ATOM 487 C LEU A 114 -18.237 10.000 -9.610 1.00 36.15 C ANISOU 487 C LEU A 114 4170 4957 4607 -646 -522 837 C ATOM 488 O LEU A 114 -17.319 9.959 -10.393 1.00 35.57 O ANISOU 488 O LEU A 114 4089 4892 4534 -651 -533 887 O ATOM 489 CB LEU A 114 -18.142 11.493 -7.611 1.00 36.57 C ANISOU 489 CB LEU A 114 4287 4880 4730 -599 -559 801 C ATOM 490 CG LEU A 114 -18.210 12.943 -7.128 1.00 40.42 C ANISOU 490 CG LEU A 114 4792 5289 5278 -546 -609 799 C ATOM 491 CD1 LEU A 114 -18.404 13.072 -5.514 1.00 40.82 C ANISOU 491 CD1 LEU A 114 4906 5294 5311 -522 -603 715 C ATOM 492 CD2 LEU A 114 -16.961 13.771 -7.708 1.00 40.54 C ANISOU 492 CD2 LEU A 114 4813 5231 5360 -564 -669 883 C ATOM 493 N ASP A 115 -18.928 8.917 -9.279 1.00 35.14 N ANISOU 493 N ASP A 115 4051 4864 4435 -681 -483 780 N ATOM 494 CA ASP A 115 -18.617 7.617 -9.822 1.00 35.74 C ANISOU 494 CA ASP A 115 4148 4965 4468 -721 -464 765 C ATOM 495 C ASP A 115 -18.800 7.537 -11.313 1.00 34.07 C ANISOU 495 C ASP A 115 3885 4832 4228 -713 -476 784 C ATOM 496 O ASP A 115 -18.027 6.891 -12.047 1.00 34.25 O ANISOU 496 O ASP A 115 3923 4870 4219 -713 -475 790 O ATOM 497 CB ASP A 115 -19.432 6.536 -9.173 1.00 37.59 C ANISOU 497 CB ASP A 115 4410 5203 4670 -776 -427 708 C ATOM 498 CG ASP A 115 -18.910 6.097 -7.773 1.00 46.68 C ANISOU 498 CG ASP A 115 5647 6276 5815 -792 -412 698 C ATOM 499 OD1 ASP A 115 -17.758 6.313 -7.436 1.00 52.91 O ANISOU 499 OD1 ASP A 115 6475 7008 6620 -761 -438 723 O ATOM 500 OD2 ASP A 115 -19.747 5.579 -7.028 1.00 53.99 O ANISOU 500 OD2 ASP A 115 6591 7209 6715 -839 -373 669 O ATOM 501 N LEU A 116 -19.821 8.193 -11.821 1.00 35.27 N ANISOU 501 N LEU A 116 3975 5044 4382 -694 -492 789 N ATOM 502 CA LEU A 116 -20.043 8.182 -13.259 1.00 35.76 C ANISOU 502 CA LEU A 116 3993 5193 4401 -681 -514 810 C ATOM 503 C LEU A 116 -18.974 9.001 -13.980 1.00 36.80 C ANISOU 503 C LEU A 116 4125 5319 4537 -643 -531 899 C ATOM 504 O LEU A 116 -18.583 8.642 -15.093 1.00 36.81 O ANISOU 504 O LEU A 116 4119 5389 4479 -637 -530 919 O ATOM 505 CB LEU A 116 -21.433 8.697 -13.604 1.00 36.11 C ANISOU 505 CB LEU A 116 3964 5311 4446 -661 -539 797 C ATOM 506 CG LEU A 116 -22.635 7.738 -13.285 1.00 36.65 C ANISOU 506 CG LEU A 116 3996 5432 4498 -721 -521 713 C ATOM 507 CD1 LEU A 116 -23.913 8.559 -13.436 1.00 39.23 C ANISOU 507 CD1 LEU A 116 4226 5837 4844 -677 -548 708 C ATOM 508 CD2 LEU A 116 -22.621 6.573 -14.196 1.00 39.02 C ANISOU 508 CD2 LEU A 116 4309 5779 4739 -771 -530 673 C ATOM 509 N TRP A 117 -18.570 10.102 -13.359 1.00 36.98 N ANISOU 509 N TRP A 117 4158 5268 4625 -621 -547 949 N ATOM 510 CA TRP A 117 -17.479 10.921 -13.928 1.00 36.94 C ANISOU 510 CA TRP A 117 4150 5245 4639 -610 -562 1047 C ATOM 511 C TRP A 117 -16.110 10.133 -14.024 1.00 37.28 C ANISOU 511 C TRP A 117 4208 5296 4661 -635 -529 1053 C ATOM 512 O TRP A 117 -15.420 10.149 -15.036 1.00 38.40 O ANISOU 512 O TRP A 117 4323 5504 4762 -631 -515 1111 O ATOM 513 CB TRP A 117 -17.390 12.169 -13.115 1.00 37.71 C ANISOU 513 CB TRP A 117 4266 5240 4822 -595 -597 1081 C ATOM 514 CG TRP A 117 -16.238 13.081 -13.489 1.00 36.11 C ANISOU 514 CG TRP A 117 4065 4993 4663 -612 -617 1187 C ATOM 515 CD1 TRP A 117 -16.043 13.711 -14.686 1.00 40.09 C ANISOU 515 CD1 TRP A 117 4545 5540 5147 -610 -628 1294 C ATOM 516 CD2 TRP A 117 -15.165 13.463 -12.630 1.00 35.79 C ANISOU 516 CD2 TRP A 117 4047 4860 4692 -645 -633 1201 C ATOM 517 NE1 TRP A 117 -14.853 14.488 -14.608 1.00 39.24 N ANISOU 517 NE1 TRP A 117 4440 5367 5102 -654 -641 1383 N ATOM 518 CE2 TRP A 117 -14.341 14.358 -13.336 1.00 37.81 C ANISOU 518 CE2 TRP A 117 4283 5101 4983 -675 -651 1319 C ATOM 519 CE3 TRP A 117 -14.865 13.192 -11.299 1.00 37.39 C ANISOU 519 CE3 TRP A 117 4286 4992 4928 -655 -640 1128 C ATOM 520 CZ2 TRP A 117 -13.204 14.902 -12.770 1.00 42.28 C ANISOU 520 CZ2 TRP A 117 4851 5588 5625 -726 -676 1357 C ATOM 521 CZ3 TRP A 117 -13.756 13.751 -10.737 1.00 37.76 C ANISOU 521 CZ3 TRP A 117 4344 4963 5042 -690 -675 1159 C ATOM 522 CH2 TRP A 117 -12.935 14.587 -11.457 1.00 41.20 C ANISOU 522 CH2 TRP A 117 4746 5386 5523 -730 -694 1268 C ATOM 523 N ILE A 118 -15.789 9.387 -13.012 1.00 36.15 N ANISOU 523 N ILE A 118 4102 5099 4533 -650 -516 990 N ATOM 524 CA ILE A 118 -14.611 8.525 -12.962 1.00 37.03 C ANISOU 524 CA ILE A 118 4227 5215 4630 -652 -494 977 C ATOM 525 C ILE A 118 -14.679 7.401 -13.993 1.00 36.30 C ANISOU 525 C ILE A 118 4133 5205 4453 -637 -466 936 C ATOM 526 O ILE A 118 -13.706 7.159 -14.737 1.00 35.79 O ANISOU 526 O ILE A 118 4044 5201 4355 -613 -444 962 O ATOM 527 CB ILE A 118 -14.340 8.024 -11.531 1.00 35.92 C ANISOU 527 CB ILE A 118 4142 4985 4521 -662 -501 925 C ATOM 528 CG1 ILE A 118 -14.106 9.262 -10.604 1.00 36.03 C ANISOU 528 CG1 ILE A 118 4159 4922 4609 -669 -539 958 C ATOM 529 CG2 ILE A 118 -13.230 6.997 -11.523 1.00 37.17 C ANISOU 529 CG2 ILE A 118 4316 5148 4659 -643 -489 904 C ATOM 530 CD1 ILE A 118 -14.065 8.901 -9.083 1.00 34.37 C ANISOU 530 CD1 ILE A 118 4014 4634 4410 -674 -552 901 C ATOM 531 N TYR A 119 -15.857 6.813 -14.120 1.00 36.74 N ANISOU 531 N TYR A 119 4208 5278 4473 -652 -469 873 N ATOM 532 CA TYR A 119 -16.146 5.875 -15.159 1.00 35.68 C ANISOU 532 CA TYR A 119 4079 5217 4259 -645 -461 822 C ATOM 533 C TYR A 119 -15.986 6.523 -16.572 1.00 37.42 C ANISOU 533 C TYR A 119 4247 5550 4419 -613 -461 886 C ATOM 534 O TYR A 119 -15.340 5.963 -17.403 1.00 36.74 O ANISOU 534 O TYR A 119 4162 5531 4266 -583 -439 872 O ATOM 535 CB TYR A 119 -17.590 5.238 -14.987 1.00 37.56 C ANISOU 535 CB TYR A 119 4333 5454 4485 -691 -475 745 C ATOM 536 CG TYR A 119 -18.145 4.651 -16.278 1.00 36.47 C ANISOU 536 CG TYR A 119 4183 5409 4265 -690 -492 697 C ATOM 537 CD1 TYR A 119 -17.514 3.583 -16.913 1.00 37.87 C ANISOU 537 CD1 TYR A 119 4407 5600 4381 -669 -484 639 C ATOM 538 CD2 TYR A 119 -19.305 5.135 -16.842 1.00 40.96 C ANISOU 538 CD2 TYR A 119 4696 6053 4813 -701 -525 700 C ATOM 539 CE1 TYR A 119 -18.047 3.046 -18.112 1.00 42.15 C ANISOU 539 CE1 TYR A 119 4949 6230 4837 -666 -509 579 C ATOM 540 CE2 TYR A 119 -19.813 4.619 -17.978 1.00 42.73 C ANISOU 540 CE2 TYR A 119 4911 6368 4958 -702 -554 651 C ATOM 541 CZ TYR A 119 -19.162 3.571 -18.633 1.00 42.87 C ANISOU 541 CZ TYR A 119 4985 6398 4907 -687 -547 587 C ATOM 542 OH TYR A 119 -19.678 3.082 -19.831 1.00 49.09 O ANISOU 542 OH TYR A 119 5771 7282 5599 -682 -586 525 O ATOM 543 N HIS A 120 -16.621 7.643 -16.814 1.00 38.71 N ANISOU 543 N HIS A 120 4373 5735 4600 -613 -486 951 N ATOM 544 CA HIS A 120 -16.594 8.299 -18.127 1.00 40.56 C ANISOU 544 CA HIS A 120 4572 6072 4767 -585 -493 1030 C ATOM 545 C HIS A 120 -15.136 8.668 -18.487 1.00 41.32 C ANISOU 545 C HIS A 120 4648 6194 4856 -575 -453 1117 C ATOM 546 O HIS A 120 -14.713 8.461 -19.608 1.00 43.27 O ANISOU 546 O HIS A 120 4879 6553 5008 -550 -425 1142 O ATOM 547 CB HIS A 120 -17.524 9.544 -18.117 1.00 41.55 C ANISOU 547 CB HIS A 120 4671 6182 4933 -576 -540 1095 C ATOM 548 CG HIS A 120 -19.010 9.215 -18.183 1.00 45.27 C ANISOU 548 CG HIS A 120 5125 6691 5385 -574 -578 1020 C ATOM 549 ND1 HIS A 120 -19.981 9.971 -17.546 1.00 45.88 N ANISOU 549 ND1 HIS A 120 5176 6726 5530 -561 -612 1022 N ATOM 550 CD2 HIS A 120 -19.679 8.210 -18.799 1.00 50.00 C ANISOU 550 CD2 HIS A 120 5718 7370 5908 -586 -591 933 C ATOM 551 CE1 HIS A 120 -21.173 9.425 -17.754 1.00 54.18 C ANISOU 551 CE1 HIS A 120 6191 7846 6551 -569 -637 946 C ATOM 552 NE2 HIS A 120 -21.018 8.347 -18.496 1.00 49.92 N ANISOU 552 NE2 HIS A 120 5666 7373 5928 -594 -629 891 N ATOM 553 N THR A 121 -14.376 9.120 -17.493 1.00 39.30 N ANISOU 553 N THR A 121 4391 5846 4696 -597 -448 1150 N ATOM 554 CA THR A 121 -13.005 9.722 -17.776 1.00 38.37 C ANISOU 554 CA THR A 121 4228 5756 4596 -609 -417 1254 C ATOM 555 C THR A 121 -11.941 8.622 -17.799 1.00 38.22 C ANISOU 555 C THR A 121 4194 5785 4542 -582 -370 1196 C ATOM 556 O THR A 121 -11.069 8.656 -18.628 1.00 40.33 O ANISOU 556 O THR A 121 4410 6157 4757 -567 -323 1250 O ATOM 557 CB THR A 121 -12.657 10.785 -16.734 1.00 38.01 C ANISOU 557 CB THR A 121 4181 5587 4674 -650 -452 1312 C ATOM 558 OG1 THR A 121 -13.779 11.654 -16.649 1.00 37.64 O ANISOU 558 OG1 THR A 121 4160 5485 4657 -648 -500 1336 O ATOM 559 CG2 THR A 121 -11.340 11.693 -17.177 1.00 39.43 C ANISOU 559 CG2 THR A 121 4298 5797 4886 -693 -430 1450 C ATOM 560 N GLN A 122 -12.003 7.632 -16.896 1.00 36.47 N ANISOU 560 N GLN A 122 4019 5491 4347 -569 -380 1088 N ATOM 561 CA GLN A 122 -10.917 6.633 -16.704 1.00 37.55 C ANISOU 561 CA GLN A 122 4150 5643 4474 -527 -351 1034 C ATOM 562 C GLN A 122 -11.257 5.186 -16.861 1.00 39.69 C ANISOU 562 C GLN A 122 4487 5912 4683 -481 -347 910 C ATOM 563 O GLN A 122 -10.377 4.356 -16.816 1.00 38.66 O ANISOU 563 O GLN A 122 4358 5792 4538 -425 -328 862 O ATOM 564 CB GLN A 122 -10.232 6.918 -15.367 1.00 37.69 C ANISOU 564 CB GLN A 122 4164 5559 4596 -549 -380 1047 C ATOM 565 CG GLN A 122 -9.674 8.349 -15.275 1.00 37.22 C ANISOU 565 CG GLN A 122 4039 5495 4609 -603 -392 1166 C ATOM 566 CD GLN A 122 -8.495 8.592 -16.198 1.00 39.93 C ANISOU 566 CD GLN A 122 4282 5964 4925 -598 -340 1245 C ATOM 567 OE1 GLN A 122 -8.010 7.663 -16.865 1.00 39.01 O ANISOU 567 OE1 GLN A 122 4141 5950 4731 -535 -291 1200 O ATOM 568 NE2 GLN A 122 -8.177 9.885 -16.419 1.00 39.89 N ANISOU 568 NE2 GLN A 122 4224 5962 4970 -666 -345 1370 N ATOM 569 N GLY A 123 -12.561 4.874 -17.093 1.00 39.79 N ANISOU 569 N GLY A 123 4551 5910 4658 -504 -371 856 N ATOM 570 CA GLY A 123 -12.988 3.547 -17.468 1.00 39.97 C ANISOU 570 CA GLY A 123 4639 5931 4616 -479 -376 740 C ATOM 571 C GLY A 123 -13.251 2.582 -16.343 1.00 39.89 C ANISOU 571 C GLY A 123 4713 5785 4657 -500 -401 663 C ATOM 572 O GLY A 123 -13.379 1.396 -16.552 1.00 39.86 O ANISOU 572 O GLY A 123 4779 5750 4617 -480 -410 569 O ATOM 573 N TYR A 124 -13.284 3.051 -15.120 1.00 39.11 N ANISOU 573 N TYR A 124 4620 5599 4640 -538 -415 702 N ATOM 574 CA TYR A 124 -13.510 2.135 -14.011 1.00 38.69 C ANISOU 574 CA TYR A 124 4656 5423 4621 -560 -434 647 C ATOM 575 C TYR A 124 -15.006 1.957 -13.813 1.00 37.93 C ANISOU 575 C TYR A 124 4590 5300 4523 -640 -446 613 C ATOM 576 O TYR A 124 -15.736 2.906 -13.518 1.00 37.96 O ANISOU 576 O TYR A 124 4548 5322 4554 -679 -448 655 O ATOM 577 CB TYR A 124 -12.815 2.613 -12.696 1.00 37.53 C ANISOU 577 CB TYR A 124 4512 5204 4545 -560 -445 697 C ATOM 578 CG TYR A 124 -11.318 2.656 -12.857 1.00 37.54 C ANISOU 578 CG TYR A 124 4467 5242 4557 -488 -440 723 C ATOM 579 CD1 TYR A 124 -10.596 1.498 -12.960 1.00 34.24 C ANISOU 579 CD1 TYR A 124 4092 4803 4115 -416 -441 665 C ATOM 580 CD2 TYR A 124 -10.622 3.850 -12.936 1.00 40.21 C ANISOU 580 CD2 TYR A 124 4711 5635 4932 -491 -436 805 C ATOM 581 CE1 TYR A 124 -9.233 1.513 -13.173 1.00 39.09 C ANISOU 581 CE1 TYR A 124 4639 5476 4737 -337 -431 682 C ATOM 582 CE2 TYR A 124 -9.252 3.863 -13.173 1.00 39.94 C ANISOU 582 CE2 TYR A 124 4606 5659 4908 -436 -424 831 C ATOM 583 CZ TYR A 124 -8.576 2.709 -13.295 1.00 38.95 C ANISOU 583 CZ TYR A 124 4506 5538 4754 -355 -419 768 C ATOM 584 OH TYR A 124 -7.210 2.638 -13.511 1.00 43.08 O ANISOU 584 OH TYR A 124 4943 6137 5287 -284 -404 783 O ATOM 585 N PHE A 125 -15.473 0.734 -13.950 1.00 39.22 N ANISOU 585 N PHE A 125 4828 5415 4658 -663 -458 533 N ATOM 586 CA PHE A 125 -16.901 0.450 -13.761 1.00 39.10 C ANISOU 586 CA PHE A 125 4827 5383 4647 -758 -469 498 C ATOM 587 C PHE A 125 -17.296 0.948 -12.325 1.00 37.51 C ANISOU 587 C PHE A 125 4628 5123 4501 -808 -455 547 C ATOM 588 O PHE A 125 -16.560 0.674 -11.397 1.00 35.57 O ANISOU 588 O PHE A 125 4442 4795 4277 -788 -452 564 O ATOM 589 CB PHE A 125 -17.184 -1.058 -13.948 1.00 39.96 C ANISOU 589 CB PHE A 125 5036 5413 4733 -794 -491 408 C ATOM 590 CG PHE A 125 -18.643 -1.411 -13.842 1.00 39.84 C ANISOU 590 CG PHE A 125 5019 5393 4727 -913 -504 373 C ATOM 591 CD1 PHE A 125 -19.434 -1.534 -14.986 1.00 40.02 C ANISOU 591 CD1 PHE A 125 4998 5500 4707 -942 -534 315 C ATOM 592 CD2 PHE A 125 -19.267 -1.570 -12.593 1.00 40.85 C ANISOU 592 CD2 PHE A 125 5173 5448 4899 -1001 -484 401 C ATOM 593 CE1 PHE A 125 -20.761 -1.829 -14.891 1.00 41.67 C ANISOU 593 CE1 PHE A 125 5180 5719 4932 -1059 -552 283 C ATOM 594 CE2 PHE A 125 -20.675 -1.896 -12.533 1.00 46.95 C ANISOU 594 CE2 PHE A 125 5916 6241 5682 -1126 -487 372 C ATOM 595 CZ PHE A 125 -21.399 -1.978 -13.694 1.00 44.24 C ANISOU 595 CZ PHE A 125 5514 5985 5310 -1153 -524 314 C ATOM 596 N PRO A 126 -18.456 1.659 -12.162 1.00 36.84 N ANISOU 596 N PRO A 126 4477 5091 4430 -861 -448 561 N ATOM 597 CA PRO A 126 -18.816 2.349 -10.966 1.00 37.46 C ANISOU 597 CA PRO A 126 4541 5146 4546 -882 -428 599 C ATOM 598 C PRO A 126 -19.420 1.462 -9.845 1.00 40.16 C ANISOU 598 C PRO A 126 4953 5417 4890 -965 -404 579 C ATOM 599 O PRO A 126 -20.564 1.657 -9.440 1.00 42.77 O ANISOU 599 O PRO A 126 5237 5788 5225 -1027 -379 574 O ATOM 600 CB PRO A 126 -19.753 3.438 -11.478 1.00 38.46 C ANISOU 600 CB PRO A 126 4561 5372 4679 -878 -433 614 C ATOM 601 CG PRO A 126 -20.470 2.787 -12.577 1.00 38.06 C ANISOU 601 CG PRO A 126 4484 5384 4592 -914 -453 564 C ATOM 602 CD PRO A 126 -19.403 2.002 -13.263 1.00 39.94 C ANISOU 602 CD PRO A 126 4789 5591 4795 -877 -465 542 C ATOM 603 N ASP A 127 -18.668 0.465 -9.383 1.00 39.65 N ANISOU 603 N ASP A 127 4997 5250 4817 -964 -410 574 N ATOM 604 CA ASP A 127 -19.084 -0.323 -8.228 1.00 41.70 C ANISOU 604 CA ASP A 127 5344 5429 5073 -1041 -388 581 C ATOM 605 C ASP A 127 -17.997 -0.518 -7.199 1.00 42.07 C ANISOU 605 C ASP A 127 5485 5385 5115 -989 -399 618 C ATOM 606 O ASP A 127 -18.062 -1.461 -6.398 1.00 39.92 O ANISOU 606 O ASP A 127 5322 5020 4826 -1039 -394 632 O ATOM 607 CB ASP A 127 -19.687 -1.663 -8.673 1.00 44.07 C ANISOU 607 CB ASP A 127 5705 5675 5364 -1132 -397 535 C ATOM 608 CG ASP A 127 -18.654 -2.626 -9.289 1.00 46.68 C ANISOU 608 CG ASP A 127 6133 5915 5688 -1069 -442 499 C ATOM 609 OD1 ASP A 127 -17.469 -2.297 -9.505 1.00 48.58 O ANISOU 609 OD1 ASP A 127 6372 6159 5927 -954 -459 508 O ATOM 610 OD2 ASP A 127 -19.035 -3.776 -9.483 1.00 53.46 O ANISOU 610 OD2 ASP A 127 7074 6691 6546 -1139 -460 458 O ATOM 611 N TRP A 128 -16.997 0.395 -7.199 1.00 38.45 N ANISOU 611 N TRP A 128 4985 4951 4671 -895 -420 642 N ATOM 612 CA TRP A 128 -15.825 0.225 -6.321 1.00 41.30 C ANISOU 612 CA TRP A 128 5422 5240 5032 -834 -449 670 C ATOM 613 C TRP A 128 -15.934 1.190 -5.103 1.00 41.68 C ANISOU 613 C TRP A 128 5461 5301 5074 -836 -441 702 C ATOM 614 O TRP A 128 -15.222 0.991 -4.083 1.00 42.43 O ANISOU 614 O TRP A 128 5633 5337 5150 -805 -468 725 O ATOM 615 CB TRP A 128 -14.522 0.506 -7.080 1.00 39.10 C ANISOU 615 CB TRP A 128 5095 4984 4776 -736 -484 670 C ATOM 616 CG TRP A 128 -14.577 1.864 -7.721 1.00 39.32 C ANISOU 616 CG TRP A 128 5002 5110 4830 -722 -476 688 C ATOM 617 CD1 TRP A 128 -15.052 2.195 -8.956 1.00 38.43 C ANISOU 617 CD1 TRP A 128 4813 5076 4713 -729 -462 677 C ATOM 618 CD2 TRP A 128 -14.234 3.095 -7.084 1.00 39.41 C ANISOU 618 CD2 TRP A 128 4969 5135 4871 -705 -492 724 C ATOM 619 NE1 TRP A 128 -15.052 3.570 -9.125 1.00 38.09 N ANISOU 619 NE1 TRP A 128 4685 5090 4699 -716 -464 716 N ATOM 620 CE2 TRP A 128 -14.542 4.140 -7.986 1.00 42.53 C ANISOU 620 CE2 TRP A 128 5267 5605 5288 -704 -484 741 C ATOM 621 CE3 TRP A 128 -13.661 3.408 -5.848 1.00 42.49 C ANISOU 621 CE3 TRP A 128 5400 5477 5267 -688 -522 741 C ATOM 622 CZ2 TRP A 128 -14.294 5.491 -7.681 1.00 42.55 C ANISOU 622 CZ2 TRP A 128 5220 5614 5332 -691 -505 776 C ATOM 623 CZ3 TRP A 128 -13.452 4.715 -5.534 1.00 39.84 C ANISOU 623 CZ3 TRP A 128 5012 5158 4967 -678 -544 761 C ATOM 624 CH2 TRP A 128 -13.738 5.753 -6.462 1.00 43.97 C ANISOU 624 CH2 TRP A 128 5444 5737 5526 -681 -536 779 C ATOM 625 N GLN A 129 -16.775 2.222 -5.189 1.00 39.98 N ANISOU 625 N GLN A 129 5160 5161 4869 -857 -413 697 N ATOM 626 CA GLN A 129 -16.804 3.255 -4.150 1.00 42.52 C ANISOU 626 CA GLN A 129 5475 5495 5187 -836 -413 708 C ATOM 627 C GLN A 129 -17.820 2.996 -3.024 1.00 44.29 C ANISOU 627 C GLN A 129 5746 5727 5356 -894 -360 705 C ATOM 628 O GLN A 129 -18.859 3.687 -2.932 1.00 50.06 O ANISOU 628 O GLN A 129 6407 6530 6084 -911 -318 686 O ATOM 629 CB GLN A 129 -17.049 4.658 -4.765 1.00 42.22 C ANISOU 629 CB GLN A 129 5328 5520 5193 -802 -421 704 C ATOM 630 CG GLN A 129 -16.629 5.662 -3.713 1.00 45.23 C ANISOU 630 CG GLN A 129 5729 5877 5581 -761 -449 704 C ATOM 631 CD GLN A 129 -17.023 7.132 -3.951 1.00 42.77 C ANISOU 631 CD GLN A 129 5343 5595 5314 -726 -462 696 C ATOM 632 OE1 GLN A 129 -16.919 7.927 -3.021 1.00 44.85 O ANISOU 632 OE1 GLN A 129 5634 5831 5576 -696 -483 676 O ATOM 633 NE2 GLN A 129 -17.342 7.491 -5.147 1.00 46.05 N ANISOU 633 NE2 GLN A 129 5681 6053 5764 -722 -461 710 N ATOM 634 N ASN A 130 -17.656 1.927 -2.284 1.00 43.01 N ANISOU 634 N ASN A 130 5694 5501 5147 -929 -353 728 N ATOM 635 CA ASN A 130 -18.608 1.543 -1.225 1.00 42.34 C ANISOU 635 CA ASN A 130 5659 5432 4994 -1002 -289 743 C ATOM 636 C ASN A 130 -17.894 1.780 0.110 1.00 41.55 C ANISOU 636 C ASN A 130 5654 5299 4836 -952 -315 764 C ATOM 637 O ASN A 130 -16.645 1.671 0.182 1.00 41.44 O ANISOU 637 O ASN A 130 5692 5220 4836 -886 -390 776 O ATOM 638 CB ASN A 130 -18.867 0.051 -1.319 1.00 44.58 C ANISOU 638 CB ASN A 130 6031 5646 5261 -1090 -272 771 C ATOM 639 CG ASN A 130 -19.243 -0.388 -2.734 1.00 51.79 C ANISOU 639 CG ASN A 130 6880 6566 6231 -1128 -279 737 C ATOM 640 OD1 ASN A 130 -20.319 -0.064 -3.126 1.00 50.44 O ANISOU 640 OD1 ASN A 130 6610 6482 6072 -1182 -237 714 O ATOM 641 ND2 ASN A 130 -18.311 -1.117 -3.504 1.00 53.20 N ANISOU 641 ND2 ASN A 130 7113 6662 6440 -1084 -339 727 N ATOM 642 N TYR A 131 -18.687 2.051 1.138 1.00 41.15 N ANISOU 642 N TYR A 131 5619 5303 4712 -982 -254 766 N ATOM 643 CA TYR A 131 -18.249 2.282 2.495 1.00 39.50 C ANISOU 643 CA TYR A 131 5505 5085 4417 -942 -268 778 C ATOM 644 C TYR A 131 -18.938 1.421 3.490 1.00 43.67 C ANISOU 644 C TYR A 131 6127 5626 4839 -1022 -194 829 C ATOM 645 O TYR A 131 -20.003 0.854 3.203 1.00 41.95 O ANISOU 645 O TYR A 131 5871 5447 4622 -1123 -113 847 O ATOM 646 CB TYR A 131 -18.465 3.763 2.861 1.00 39.83 C ANISOU 646 CB TYR A 131 5478 5200 4457 -873 -268 716 C ATOM 647 CG TYR A 131 -17.778 4.735 1.915 1.00 39.34 C ANISOU 647 CG TYR A 131 5330 5116 4503 -806 -343 681 C ATOM 648 CD1 TYR A 131 -16.466 5.148 2.122 1.00 40.21 C ANISOU 648 CD1 TYR A 131 5474 5165 4638 -743 -442 678 C ATOM 649 CD2 TYR A 131 -18.467 5.252 0.812 1.00 40.19 C ANISOU 649 CD2 TYR A 131 5316 5270 4685 -812 -318 658 C ATOM 650 CE1 TYR A 131 -15.867 6.046 1.257 1.00 37.75 C ANISOU 650 CE1 TYR A 131 5079 4839 4426 -703 -500 662 C ATOM 651 CE2 TYR A 131 -17.835 6.166 -0.080 1.00 38.52 C ANISOU 651 CE2 TYR A 131 5035 5037 4565 -759 -383 646 C ATOM 652 CZ TYR A 131 -16.531 6.490 0.130 1.00 39.24 C ANISOU 652 CZ TYR A 131 5163 5065 4681 -715 -467 654 C ATOM 653 OH TYR A 131 -15.957 7.426 -0.746 1.00 40.55 O ANISOU 653 OH TYR A 131 5253 5215 4937 -683 -522 656 O ATOM 654 N THR A 132 -18.309 1.260 4.649 1.00 42.72 N ANISOU 654 N THR A 132 6132 5474 4626 -986 -226 861 N ATOM 655 CA THR A 132 -18.899 0.513 5.735 1.00 43.31 C ANISOU 655 CA THR A 132 6313 5567 4574 -1059 -152 926 C ATOM 656 C THR A 132 -20.173 1.239 6.198 1.00 45.43 C ANISOU 656 C THR A 132 6493 5985 4783 -1089 -36 889 C ATOM 657 O THR A 132 -20.333 2.477 6.023 1.00 44.40 O ANISOU 657 O THR A 132 6260 5924 4687 -1011 -41 803 O ATOM 658 CB THR A 132 -17.927 0.360 6.931 1.00 43.50 C ANISOU 658 CB THR A 132 6490 5545 4491 -993 -223 964 C ATOM 659 OG1 THR A 132 -17.496 1.647 7.358 1.00 44.36 O ANISOU 659 OG1 THR A 132 6562 5709 4585 -890 -273 885 O ATOM 660 CG2 THR A 132 -16.727 -0.484 6.565 1.00 47.62 C ANISOU 660 CG2 THR A 132 7098 5930 5067 -954 -334 1006 C ATOM 661 N PRO A 133 -21.122 0.466 6.781 1.00 49.34 N ANISOU 661 N PRO A 133 7024 6533 5190 -1203 74 954 N ATOM 662 CA PRO A 133 -22.364 1.075 7.173 1.00 51.28 C ANISOU 662 CA PRO A 133 7162 6942 5379 -1229 197 918 C ATOM 663 C PRO A 133 -22.159 1.949 8.449 1.00 53.30 C ANISOU 663 C PRO A 133 7477 7276 5498 -1124 206 875 C ATOM 664 O PRO A 133 -21.213 1.768 9.236 1.00 53.09 O ANISOU 664 O PRO A 133 7600 7183 5388 -1074 134 906 O ATOM 665 CB PRO A 133 -23.325 -0.148 7.410 1.00 54.40 C ANISOU 665 CB PRO A 133 7581 7366 5723 -1405 310 1018 C ATOM 666 CG PRO A 133 -22.484 -1.275 7.720 1.00 55.12 C ANISOU 666 CG PRO A 133 7859 7303 5782 -1444 246 1116 C ATOM 667 CD PRO A 133 -21.149 -1.005 6.866 1.00 49.74 C ANISOU 667 CD PRO A 133 7193 6488 5218 -1321 88 1062 C ATOM 668 N GLY A 134 -23.050 2.895 8.635 1.00 54.50 N ANISOU 668 N GLY A 134 7511 7571 5625 -1081 286 796 N ATOM 669 CA GLY A 134 -23.053 3.678 9.856 1.00 56.92 C ANISOU 669 CA GLY A 134 7872 7967 5786 -984 312 740 C ATOM 670 C GLY A 134 -23.457 2.858 11.080 1.00 60.55 C ANISOU 670 C GLY A 134 8444 8505 6055 -1062 419 831 C ATOM 671 O GLY A 134 -23.802 1.683 10.959 1.00 61.23 O ANISOU 671 O GLY A 134 8559 8567 6137 -1207 476 946 O ATOM 672 N PRO A 135 -23.432 3.472 12.270 1.00 61.68 N ANISOU 672 N PRO A 135 8658 8742 6035 -972 445 782 N ATOM 673 CA PRO A 135 -23.126 4.883 12.510 1.00 61.24 C ANISOU 673 CA PRO A 135 8580 8711 5977 -806 379 633 C ATOM 674 C PRO A 135 -21.622 5.226 12.624 1.00 58.93 C ANISOU 674 C PRO A 135 8410 8266 5714 -717 191 603 C ATOM 675 O PRO A 135 -20.726 4.354 12.638 1.00 58.02 O ANISOU 675 O PRO A 135 8407 8038 5601 -761 108 697 O ATOM 676 CB PRO A 135 -23.900 5.181 13.835 1.00 64.09 C ANISOU 676 CB PRO A 135 8972 9261 6117 -766 513 599 C ATOM 677 CG PRO A 135 -23.910 3.885 14.538 1.00 65.81 C ANISOU 677 CG PRO A 135 9318 9493 6193 -893 579 756 C ATOM 678 CD PRO A 135 -24.153 2.874 13.414 1.00 63.79 C ANISOU 678 CD PRO A 135 8990 9147 6099 -1047 592 862 C ATOM 679 N GLY A 136 -21.349 6.525 12.599 1.00 57.02 N ANISOU 679 N GLY A 136 8132 8014 5517 -590 115 467 N ATOM 680 CA GLY A 136 -19.987 7.000 12.746 1.00 54.97 C ANISOU 680 CA GLY A 136 7965 7630 5292 -514 -63 424 C ATOM 681 C GLY A 136 -19.258 7.081 11.428 1.00 50.67 C ANISOU 681 C GLY A 136 7342 6947 4963 -532 -171 439 C ATOM 682 O GLY A 136 -19.869 7.259 10.421 1.00 47.35 O ANISOU 682 O GLY A 136 6790 6533 4667 -558 -124 432 O ATOM 683 N ILE A 137 -17.927 6.886 11.477 1.00 49.44 N ANISOU 683 N ILE A 137 7267 6679 4838 -516 -317 465 N ATOM 684 CA ILE A 137 -17.103 7.086 10.320 1.00 47.53 C ANISOU 684 CA ILE A 137 6949 6324 4786 -519 -421 469 C ATOM 685 C ILE A 137 -17.417 5.922 9.383 1.00 45.16 C ANISOU 685 C ILE A 137 6601 6003 4557 -615 -355 575 C ATOM 686 O ILE A 137 -17.565 4.801 9.814 1.00 44.25 O ANISOU 686 O ILE A 137 6568 5894 4350 -675 -306 663 O ATOM 687 CB ILE A 137 -15.557 7.228 10.667 1.00 46.48 C ANISOU 687 CB ILE A 137 6893 6100 4668 -473 -597 461 C ATOM 688 CG1 ILE A 137 -15.268 8.598 11.331 1.00 48.14 C ANISOU 688 CG1 ILE A 137 7126 6310 4853 -388 -684 331 C ATOM 689 CG2 ILE A 137 -14.798 7.238 9.419 1.00 40.93 C ANISOU 689 CG2 ILE A 137 6094 5309 4149 -492 -670 488 C ATOM 690 CD1 ILE A 137 -13.958 8.701 12.061 1.00 49.68 C ANISOU 690 CD1 ILE A 137 7414 6455 5007 -349 -847 312 C ATOM 691 N ARG A 138 -17.495 6.218 8.097 1.00 42.43 N ANISOU 691 N ARG A 138 6130 5621 4369 -630 -362 564 N ATOM 692 CA ARG A 138 -17.663 5.139 7.117 1.00 42.24 C ANISOU 692 CA ARG A 138 6066 5565 4418 -713 -323 646 C ATOM 693 C ARG A 138 -16.384 4.949 6.332 1.00 41.68 C ANISOU 693 C ARG A 138 5987 5392 4459 -693 -440 669 C ATOM 694 O ARG A 138 -15.900 5.933 5.628 1.00 41.68 O ANISOU 694 O ARG A 138 5899 5367 4572 -649 -506 620 O ATOM 695 CB ARG A 138 -18.806 5.490 6.157 1.00 42.49 C ANISOU 695 CB ARG A 138 5955 5658 4530 -745 -236 619 C ATOM 696 CG ARG A 138 -19.996 6.228 6.747 1.00 46.02 C ANISOU 696 CG ARG A 138 6353 6226 4907 -719 -139 555 C ATOM 697 CD ARG A 138 -20.728 5.408 7.801 1.00 51.57 C ANISOU 697 CD ARG A 138 7126 7015 5453 -781 -27 602 C ATOM 698 NE ARG A 138 -21.688 6.240 8.569 1.00 57.61 N ANISOU 698 NE ARG A 138 7850 7915 6126 -725 63 524 N ATOM 699 CZ ARG A 138 -22.924 6.553 8.208 1.00 55.63 C ANISOU 699 CZ ARG A 138 7461 7778 5899 -734 167 489 C ATOM 700 NH1 ARG A 138 -23.436 6.122 7.076 1.00 56.30 N ANISOU 700 NH1 ARG A 138 7432 7864 6096 -810 192 525 N ATOM 701 NH2 ARG A 138 -23.663 7.298 9.008 1.00 60.74 N ANISOU 701 NH2 ARG A 138 8080 8547 6449 -658 243 409 N ATOM 702 N TYR A 139 -15.832 3.745 6.398 1.00 41.11 N ANISOU 702 N TYR A 139 5998 5260 4364 -720 -465 744 N ATOM 703 CA TYR A 139 -14.503 3.438 5.824 1.00 41.67 C ANISOU 703 CA TYR A 139 6067 5247 4520 -680 -577 765 C ATOM 704 C TYR A 139 -14.676 2.740 4.475 1.00 40.71 C ANISOU 704 C TYR A 139 5877 5093 4498 -725 -543 793 C ATOM 705 O TYR A 139 -15.682 2.057 4.261 1.00 39.75 O ANISOU 705 O TYR A 139 5763 4986 4355 -801 -452 821 O ATOM 706 CB TYR A 139 -13.709 2.565 6.785 1.00 42.73 C ANISOU 706 CB TYR A 139 6344 5330 4560 -652 -643 821 C ATOM 707 CG TYR A 139 -13.330 3.291 8.059 1.00 44.43 C ANISOU 707 CG TYR A 139 6629 5581 4673 -596 -706 783 C ATOM 708 CD1 TYR A 139 -12.268 4.210 8.058 1.00 44.80 C ANISOU 708 CD1 TYR A 139 6625 5613 4782 -531 -829 724 C ATOM 709 CD2 TYR A 139 -14.014 3.097 9.246 1.00 45.83 C ANISOU 709 CD2 TYR A 139 6916 5810 4686 -612 -645 800 C ATOM 710 CE1 TYR A 139 -11.921 4.870 9.148 1.00 45.80 C ANISOU 710 CE1 TYR A 139 6815 5766 4822 -484 -900 675 C ATOM 711 CE2 TYR A 139 -13.617 3.763 10.398 1.00 52.66 C ANISOU 711 CE2 TYR A 139 7854 6713 5442 -550 -713 752 C ATOM 712 CZ TYR A 139 -12.568 4.653 10.325 1.00 50.52 C ANISOU 712 CZ TYR A 139 7535 6415 5247 -485 -848 683 C ATOM 713 OH TYR A 139 -12.200 5.390 11.396 1.00 52.28 O ANISOU 713 OH TYR A 139 7823 6668 5371 -429 -928 616 O ATOM 714 N PRO A 140 -13.743 2.973 3.533 1.00 39.26 N ANISOU 714 N PRO A 140 5617 4879 4423 -682 -613 781 N ATOM 715 CA PRO A 140 -13.842 2.490 2.195 1.00 38.52 C ANISOU 715 CA PRO A 140 5453 4771 4413 -706 -587 789 C ATOM 716 C PRO A 140 -13.619 1.010 2.126 1.00 40.26 C ANISOU 716 C PRO A 140 5769 4918 4611 -719 -591 837 C ATOM 717 O PRO A 140 -12.698 0.486 2.762 1.00 41.99 O ANISOU 717 O PRO A 140 6076 5081 4797 -665 -662 866 O ATOM 718 CB PRO A 140 -12.676 3.208 1.453 1.00 40.10 C ANISOU 718 CB PRO A 140 5555 4972 4709 -645 -666 770 C ATOM 719 CG PRO A 140 -11.685 3.436 2.479 1.00 40.27 C ANISOU 719 CG PRO A 140 5631 4972 4698 -591 -756 770 C ATOM 720 CD PRO A 140 -12.492 3.760 3.721 1.00 39.14 C ANISOU 720 CD PRO A 140 5571 4852 4450 -612 -724 755 C ATOM 721 N LEU A 141 -14.482 0.323 1.380 1.00 39.74 N ANISOU 721 N LEU A 141 5693 4843 4562 -790 -523 843 N ATOM 722 CA LEU A 141 -14.319 -1.100 1.232 1.00 41.42 C ANISOU 722 CA LEU A 141 6011 4961 4767 -807 -534 880 C ATOM 723 C LEU A 141 -13.251 -1.433 0.248 1.00 40.26 C ANISOU 723 C LEU A 141 5829 4774 4694 -726 -598 858 C ATOM 724 O LEU A 141 -12.693 -2.519 0.335 1.00 41.18 O ANISOU 724 O LEU A 141 6048 4795 4803 -689 -641 881 O ATOM 725 CB LEU A 141 -15.638 -1.754 0.741 1.00 42.04 C ANISOU 725 CB LEU A 141 6090 5037 4846 -927 -449 883 C ATOM 726 CG LEU A 141 -16.818 -1.560 1.728 1.00 48.04 C ANISOU 726 CG LEU A 141 6870 5857 5525 -1020 -363 911 C ATOM 727 CD1 LEU A 141 -18.016 -2.428 1.192 1.00 56.36 C ANISOU 727 CD1 LEU A 141 7920 6901 6595 -1156 -292 923 C ATOM 728 CD2 LEU A 141 -16.519 -1.926 3.034 1.00 50.06 C ANISOU 728 CD2 LEU A 141 7260 6074 5685 -1011 -376 970 C ATOM 729 N THR A 142 -12.988 -0.565 -0.729 1.00 38.43 N ANISOU 729 N THR A 142 5458 4614 4531 -694 -601 816 N ATOM 730 CA THR A 142 -11.897 -0.820 -1.672 1.00 38.95 C ANISOU 730 CA THR A 142 5474 4672 4655 -610 -649 796 C ATOM 731 C THR A 142 -10.576 -0.279 -1.109 1.00 38.28 C ANISOU 731 C THR A 142 5359 4601 4584 -520 -730 806 C ATOM 732 O THR A 142 -10.369 0.929 -1.048 1.00 36.57 O ANISOU 732 O THR A 142 5048 4450 4395 -521 -742 798 O ATOM 733 CB THR A 142 -12.205 -0.171 -3.056 1.00 40.14 C ANISOU 733 CB THR A 142 5488 4905 4860 -625 -610 761 C ATOM 734 OG1 THR A 142 -13.415 -0.724 -3.547 1.00 39.51 O ANISOU 734 OG1 THR A 142 5430 4816 4765 -708 -552 745 O ATOM 735 CG2 THR A 142 -11.048 -0.386 -4.118 1.00 39.72 C ANISOU 735 CG2 THR A 142 5367 4874 4852 -533 -642 741 C ATOM 736 N PHE A 143 -9.668 -1.182 -0.795 1.00 38.20 N ANISOU 736 N PHE A 143 5422 4526 4564 -441 -793 821 N ATOM 737 CA PHE A 143 -8.389 -0.817 -0.209 1.00 38.61 C ANISOU 737 CA PHE A 143 5441 4599 4629 -353 -883 829 C ATOM 738 C PHE A 143 -7.616 -0.114 -1.321 1.00 38.40 C ANISOU 738 C PHE A 143 5243 4663 4686 -315 -886 803 C ATOM 739 O PHE A 143 -7.527 -0.569 -2.459 1.00 37.75 O ANISOU 739 O PHE A 143 5113 4596 4634 -288 -850 781 O ATOM 740 CB PHE A 143 -7.658 -2.046 0.268 1.00 39.58 C ANISOU 740 CB PHE A 143 5679 4633 4725 -262 -952 852 C ATOM 741 CG PHE A 143 -6.325 -1.782 1.024 1.00 39.16 C ANISOU 741 CG PHE A 143 5596 4607 4678 -162 -1066 862 C ATOM 742 CD1 PHE A 143 -6.195 -0.750 1.945 1.00 40.50 C ANISOU 742 CD1 PHE A 143 5739 4826 4822 -191 -1109 867 C ATOM 743 CD2 PHE A 143 -5.326 -2.688 0.933 1.00 41.78 C ANISOU 743 CD2 PHE A 143 5948 4899 5026 -38 -1136 864 C ATOM 744 CE1 PHE A 143 -5.040 -0.590 2.667 1.00 41.75 C ANISOU 744 CE1 PHE A 143 5877 5007 4980 -110 -1226 871 C ATOM 745 CE2 PHE A 143 -4.173 -2.545 1.666 1.00 40.85 C ANISOU 745 CE2 PHE A 143 5800 4810 4910 56 -1249 874 C ATOM 746 CZ PHE A 143 -4.014 -1.535 2.502 1.00 40.48 C ANISOU 746 CZ PHE A 143 5718 4821 4843 16 -1296 879 C ATOM 747 N GLY A 144 -7.061 1.032 -0.955 1.00 38.12 N ANISOU 747 N GLY A 144 5117 4687 4681 -320 -930 805 N ATOM 748 CA GLY A 144 -6.415 1.896 -1.888 1.00 36.41 C ANISOU 748 CA GLY A 144 4735 4558 4543 -317 -926 800 C ATOM 749 C GLY A 144 -7.100 3.225 -1.979 1.00 38.15 C ANISOU 749 C GLY A 144 4900 4809 4785 -405 -894 801 C ATOM 750 O GLY A 144 -6.426 4.216 -2.306 1.00 36.61 O ANISOU 750 O GLY A 144 4586 4667 4656 -419 -922 811 O ATOM 751 N TRP A 145 -8.431 3.242 -1.845 1.00 35.68 N ANISOU 751 N TRP A 145 4660 4468 4428 -465 -832 792 N ATOM 752 CA TRP A 145 -9.225 4.489 -1.885 1.00 34.59 C ANISOU 752 CA TRP A 145 4481 4353 4309 -529 -803 786 C ATOM 753 C TRP A 145 -9.061 5.200 -0.561 1.00 37.49 C ANISOU 753 C TRP A 145 4896 4694 4654 -532 -867 771 C ATOM 754 O TRP A 145 -9.342 4.647 0.503 1.00 38.68 O ANISOU 754 O TRP A 145 5161 4809 4725 -523 -878 764 O ATOM 755 CB TRP A 145 -10.694 4.198 -2.181 1.00 36.15 C ANISOU 755 CB TRP A 145 4721 4548 4466 -579 -717 774 C ATOM 756 CG TRP A 145 -11.651 5.355 -2.232 1.00 35.95 C ANISOU 756 CG TRP A 145 4656 4549 4455 -622 -685 761 C ATOM 757 CD1 TRP A 145 -12.730 5.501 -1.417 1.00 37.20 C ANISOU 757 CD1 TRP A 145 4874 4702 4559 -649 -649 739 C ATOM 758 CD2 TRP A 145 -11.606 6.534 -3.081 1.00 33.96 C ANISOU 758 CD2 TRP A 145 4300 4330 4272 -632 -688 772 C ATOM 759 NE1 TRP A 145 -13.432 6.672 -1.738 1.00 37.79 N ANISOU 759 NE1 TRP A 145 4885 4805 4668 -661 -629 723 N ATOM 760 CE2 TRP A 145 -12.744 7.329 -2.748 1.00 36.47 C ANISOU 760 CE2 TRP A 145 4628 4649 4579 -652 -660 748 C ATOM 761 CE3 TRP A 145 -10.755 6.963 -4.128 1.00 37.84 C ANISOU 761 CE3 TRP A 145 4693 4856 4828 -625 -705 807 C ATOM 762 CZ2 TRP A 145 -13.038 8.494 -3.383 1.00 38.32 C ANISOU 762 CZ2 TRP A 145 4794 4896 4871 -657 -663 757 C ATOM 763 CZ3 TRP A 145 -11.024 8.160 -4.755 1.00 38.25 C ANISOU 763 CZ3 TRP A 145 4677 4924 4932 -648 -702 830 C ATOM 764 CH2 TRP A 145 -12.198 8.914 -4.398 1.00 40.22 C ANISOU 764 CH2 TRP A 145 4954 5152 5175 -660 -687 805 C ATOM 765 N CYS A 146 -8.502 6.411 -0.596 1.00 36.81 N ANISOU 765 N CYS A 146 4731 4622 4635 -547 -919 767 N ATOM 766 CA CYS A 146 -8.069 7.049 0.627 1.00 37.30 C ANISOU 766 CA CYS A 146 4836 4655 4682 -542 -1008 739 C ATOM 767 C CYS A 146 -9.044 8.127 1.075 1.00 38.30 C ANISOU 767 C CYS A 146 4997 4759 4795 -574 -991 699 C ATOM 768 O CYS A 146 -8.642 9.082 1.740 1.00 41.06 O ANISOU 768 O CYS A 146 5352 5081 5166 -579 -1071 665 O ATOM 769 CB CYS A 146 -6.655 7.660 0.435 1.00 38.87 C ANISOU 769 CB CYS A 146 4925 4873 4972 -542 -1101 752 C ATOM 770 SG CYS A 146 -5.454 6.339 0.253 1.00 42.15 S ANISOU 770 SG CYS A 146 5305 5326 5384 -467 -1135 780 S ATOM 771 N PHE A 147 -10.311 8.031 0.690 1.00 37.77 N ANISOU 771 N PHE A 147 4946 4705 4699 -590 -895 695 N ATOM 772 CA PHE A 147 -11.344 8.907 1.266 1.00 37.42 C ANISOU 772 CA PHE A 147 4942 4651 4625 -595 -871 646 C ATOM 773 C PHE A 147 -12.266 8.072 2.176 1.00 36.68 C ANISOU 773 C PHE A 147 4951 4578 4408 -589 -806 629 C ATOM 774 O PHE A 147 -12.554 6.902 1.848 1.00 36.74 O ANISOU 774 O PHE A 147 4977 4600 4381 -607 -749 667 O ATOM 775 CB PHE A 147 -12.166 9.639 0.245 1.00 38.16 C ANISOU 775 CB PHE A 147 4961 4757 4780 -612 -817 651 C ATOM 776 CG PHE A 147 -11.443 10.780 -0.471 1.00 35.95 C ANISOU 776 CG PHE A 147 4601 4446 4614 -628 -880 673 C ATOM 777 CD1 PHE A 147 -11.635 12.093 -0.072 1.00 37.28 C ANISOU 777 CD1 PHE A 147 4785 4556 4823 -622 -930 632 C ATOM 778 CD2 PHE A 147 -10.578 10.509 -1.523 1.00 38.77 C ANISOU 778 CD2 PHE A 147 4871 4827 5031 -649 -885 736 C ATOM 779 CE1 PHE A 147 -10.997 13.150 -0.705 1.00 41.21 C ANISOU 779 CE1 PHE A 147 5222 5004 5431 -654 -991 666 C ATOM 780 CE2 PHE A 147 -9.854 11.587 -2.168 1.00 37.99 C ANISOU 780 CE2 PHE A 147 4693 4705 5036 -684 -937 776 C ATOM 781 CZ PHE A 147 -10.088 12.888 -1.757 1.00 41.14 C ANISOU 781 CZ PHE A 147 5118 5029 5483 -695 -991 747 C ATOM 782 N LYS A 148 -12.720 8.692 3.275 1.00 36.96 N ANISOU 782 N LYS A 148 5054 4614 4377 -568 -816 573 N ATOM 783 CA LYS A 148 -13.717 8.150 4.226 1.00 37.52 C ANISOU 783 CA LYS A 148 5213 4727 4317 -567 -738 556 C ATOM 784 C LYS A 148 -14.806 9.190 4.383 1.00 38.40 C ANISOU 784 C LYS A 148 5299 4870 4421 -546 -688 490 C ATOM 785 O LYS A 148 -14.623 10.325 3.947 1.00 37.24 O ANISOU 785 O LYS A 148 5100 4686 4366 -524 -739 456 O ATOM 786 CB LYS A 148 -13.099 7.818 5.585 1.00 39.35 C ANISOU 786 CB LYS A 148 5564 4950 4438 -539 -801 546 C ATOM 787 CG LYS A 148 -12.439 9.008 6.299 1.00 40.69 C ANISOU 787 CG LYS A 148 5756 5090 4616 -497 -913 472 C ATOM 788 CD LYS A 148 -11.612 8.662 7.535 1.00 41.22 C ANISOU 788 CD LYS A 148 5932 5152 4579 -466 -1006 463 C ATOM 789 CE LYS A 148 -11.082 9.877 8.303 1.00 41.51 C ANISOU 789 CE LYS A 148 5998 5160 4612 -431 -1124 368 C ATOM 790 NZ LYS A 148 -9.967 9.473 9.263 1.00 40.40 N ANISOU 790 NZ LYS A 148 5937 5017 4397 -404 -1251 370 N ATOM 791 N LEU A 149 -15.961 8.795 4.943 1.00 37.52 N ANISOU 791 N LEU A 149 5221 4829 4208 -552 -584 478 N ATOM 792 CA LEU A 149 -17.070 9.672 5.149 1.00 37.63 C ANISOU 792 CA LEU A 149 5199 4895 4203 -513 -524 409 C ATOM 793 C LEU A 149 -17.190 9.965 6.634 1.00 40.14 C ANISOU 793 C LEU A 149 5621 5245 4383 -464 -525 343 C ATOM 794 O LEU A 149 -17.258 9.034 7.447 1.00 40.55 O ANISOU 794 O LEU A 149 5755 5341 4309 -491 -481 380 O ATOM 795 CB LEU A 149 -18.377 9.083 4.548 1.00 37.54 C ANISOU 795 CB LEU A 149 5109 4969 4185 -558 -397 438 C ATOM 796 CG LEU A 149 -18.363 8.590 3.119 1.00 38.84 C ANISOU 796 CG LEU A 149 5185 5118 4453 -611 -392 498 C ATOM 797 CD1 LEU A 149 -19.812 8.072 2.831 1.00 36.66 C ANISOU 797 CD1 LEU A 149 4837 4944 4148 -659 -272 504 C ATOM 798 CD2 LEU A 149 -17.948 9.704 2.141 1.00 36.42 C ANISOU 798 CD2 LEU A 149 4805 4759 4273 -571 -465 484 C ATOM 799 N VAL A 150 -17.199 11.223 7.010 1.00 40.12 N ANISOU 799 N VAL A 150 5630 5218 4396 -390 -578 248 N ATOM 800 CA VAL A 150 -17.079 11.587 8.442 1.00 42.80 C ANISOU 800 CA VAL A 150 6085 5578 4598 -330 -607 166 C ATOM 801 C VAL A 150 -18.293 12.354 8.870 1.00 44.88 C ANISOU 801 C VAL A 150 6332 5918 4803 -252 -523 69 C ATOM 802 O VAL A 150 -18.697 13.307 8.185 1.00 42.55 O ANISOU 802 O VAL A 150 5962 5586 4620 -206 -536 21 O ATOM 803 CB VAL A 150 -15.807 12.410 8.737 1.00 43.95 C ANISOU 803 CB VAL A 150 6287 5614 4799 -302 -776 113 C ATOM 804 CG1 VAL A 150 -15.671 12.721 10.266 1.00 49.31 C ANISOU 804 CG1 VAL A 150 7100 6323 5314 -237 -819 17 C ATOM 805 CG2 VAL A 150 -14.523 11.576 8.382 1.00 46.21 C ANISOU 805 CG2 VAL A 150 6573 5850 5136 -367 -859 209 C ATOM 806 N PRO A 151 -18.914 11.964 9.984 1.00 48.59 N ANISOU 806 N PRO A 151 6867 6500 5094 -229 -433 42 N ATOM 807 CA PRO A 151 -20.041 12.727 10.473 1.00 51.38 C ANISOU 807 CA PRO A 151 7197 6947 5379 -135 -346 -66 C ATOM 808 C PRO A 151 -19.645 14.139 10.855 1.00 54.80 C ANISOU 808 C PRO A 151 7689 7290 5844 -23 -465 -207 C ATOM 809 O PRO A 151 -18.587 14.354 11.451 1.00 53.76 O ANISOU 809 O PRO A 151 7665 7077 5684 -18 -592 -239 O ATOM 810 CB PRO A 151 -20.483 11.969 11.732 1.00 53.96 C ANISOU 810 CB PRO A 151 7608 7414 5482 -142 -240 -56 C ATOM 811 CG PRO A 151 -20.110 10.551 11.466 1.00 53.99 C ANISOU 811 CG PRO A 151 7627 7411 5476 -271 -216 97 C ATOM 812 CD PRO A 151 -18.739 10.716 10.750 1.00 51.66 C ANISOU 812 CD PRO A 151 7344 6950 5334 -291 -385 125 C ATOM 813 N VAL A 152 -20.462 15.110 10.527 1.00 57.28 N ANISOU 813 N VAL A 152 7936 7606 6220 68 -438 -295 N ATOM 814 CA VAL A 152 -20.210 16.400 11.129 1.00 63.15 C ANISOU 814 CA VAL A 152 8767 8265 6963 186 -542 -447 C ATOM 815 C VAL A 152 -21.361 16.892 12.017 1.00 68.22 C ANISOU 815 C VAL A 152 9421 9039 7462 325 -435 -583 C ATOM 816 O VAL A 152 -22.476 16.356 11.933 1.00 68.23 O ANISOU 816 O VAL A 152 9319 9202 7401 326 -271 -549 O ATOM 817 CB VAL A 152 -19.778 17.368 10.050 1.00 62.97 C ANISOU 817 CB VAL A 152 8701 8068 7158 192 -664 -450 C ATOM 818 CG1 VAL A 152 -18.311 16.909 9.616 1.00 60.09 C ANISOU 818 CG1 VAL A 152 8361 7591 6882 63 -787 -342 C ATOM 819 CG2 VAL A 152 -20.810 17.393 8.862 1.00 57.96 C ANISOU 819 CG2 VAL A 152 7912 7477 6632 202 -571 -394 C ATOM 820 N GLU A 153 -21.066 17.874 12.870 1.00 73.23 N ANISOU 820 N GLU A 153 10175 9609 8040 437 -528 -738 N ATOM 821 CA GLU A 153 -22.117 18.618 13.639 1.00 79.29 C ANISOU 821 CA GLU A 153 10958 10479 8689 609 -445 -905 C ATOM 822 C GLU A 153 -22.969 19.387 12.630 1.00 82.53 C ANISOU 822 C GLU A 153 11241 10851 9267 692 -422 -933 C ATOM 823 O GLU A 153 -22.429 20.076 11.754 1.00 82.72 O ANISOU 823 O GLU A 153 11263 10683 9486 678 -556 -916 O ATOM 824 CB GLU A 153 -21.489 19.566 14.661 1.00 80.60 C ANISOU 824 CB GLU A 153 11296 10548 8779 713 -583 -1079 C ATOM 825 N PRO A 154 -24.309 19.264 12.712 1.00 87.13 N ANISOU 825 N PRO A 154 11708 11622 9776 776 -253 -964 N ATOM 826 CA PRO A 154 -25.097 19.672 11.508 1.00 88.13 C ANISOU 826 CA PRO A 154 11678 11732 10076 819 -229 -935 C ATOM 827 C PRO A 154 -25.031 21.194 11.089 1.00 90.27 C ANISOU 827 C PRO A 154 11994 11801 10504 970 -374 -1056 C ATOM 828 O PRO A 154 -25.409 21.527 9.969 1.00 91.03 O ANISOU 828 O PRO A 154 11985 11840 10762 985 -395 -1001 O ATOM 829 CB PRO A 154 -26.527 19.169 11.825 1.00 89.30 C ANISOU 829 CB PRO A 154 11681 12151 10097 874 -17 -951 C ATOM 830 CG PRO A 154 -26.587 19.113 13.403 1.00 91.34 C ANISOU 830 CG PRO A 154 12058 12540 10107 948 55 -1067 C ATOM 831 CD PRO A 154 -25.145 18.949 13.898 1.00 89.48 C ANISOU 831 CD PRO A 154 12012 12150 9835 856 -92 -1045 C ATOM 832 N GLU A 155 -24.541 22.086 11.952 1.00 92.91 N ANISOU 832 N GLU A 155 12490 12020 10792 1074 -482 -1212 N ATOM 833 CA GLU A 155 -24.209 23.490 11.563 1.00 94.53 C ANISOU 833 CA GLU A 155 12778 11973 11165 1178 -655 -1310 C ATOM 834 C GLU A 155 -25.406 24.308 11.058 1.00 96.07 C ANISOU 834 C GLU A 155 12877 12183 11441 1366 -613 -1387 C ATOM 835 O GLU A 155 -25.851 25.245 11.734 1.00 99.26 O ANISOU 835 O GLU A 155 13357 12557 11798 1566 -635 -1578 O ATOM 836 CB GLU A 155 -23.067 23.531 10.526 1.00 92.62 C ANISOU 836 CB GLU A 155 12553 11518 11119 1011 -804 -1163 C ATOM 837 N ASP A 179 -29.727 19.332 15.249 1.00111.81 N ANISOU 837 N ASP A 179 14417 15774 12292 1289 517 -1328 N ATOM 838 CA ASP A 179 -30.940 19.471 14.456 1.00112.21 C ANISOU 838 CA ASP A 179 14233 15951 12450 1354 616 -1324 C ATOM 839 C ASP A 179 -30.911 18.576 13.192 1.00109.72 C ANISOU 839 C ASP A 179 13786 15602 12301 1143 610 -1116 C ATOM 840 O ASP A 179 -30.181 18.867 12.233 1.00107.93 O ANISOU 840 O ASP A 179 13602 15143 12263 1096 445 -1060 O ATOM 841 CB ASP A 179 -31.150 20.949 14.078 1.00113.04 C ANISOU 841 CB ASP A 179 14347 15907 12695 1593 494 -1494 C ATOM 842 N ALA A 180 -31.660 17.465 13.235 1.00109.46 N ANISOU 842 N ALA A 180 13604 15800 12187 1007 788 -1002 N ATOM 843 CA ALA A 180 -32.079 16.709 12.021 1.00107.48 C ANISOU 843 CA ALA A 180 13174 15578 12087 849 813 -847 C ATOM 844 C ALA A 180 -33.269 15.722 12.288 1.00108.15 C ANISOU 844 C ALA A 180 13060 15971 12062 745 1039 -775 C ATOM 845 O ALA A 180 -34.428 16.138 12.117 1.00109.72 O ANISOU 845 O ALA A 180 13057 16349 12283 865 1132 -850 O ATOM 846 CB ALA A 180 -30.871 16.027 11.289 1.00104.92 C ANISOU 846 CB ALA A 180 12961 15031 11873 649 676 -691 C ATOM 847 N GLU A 181 -33.057 14.461 12.722 1.00106.71 N ANISOU 847 N GLU A 181 12921 15860 11765 531 1130 -633 N ATOM 848 CA GLU A 181 -31.756 13.844 13.076 1.00103.70 C ANISOU 848 CA GLU A 181 12770 15303 11330 398 1038 -540 C ATOM 849 C GLU A 181 -31.442 12.635 12.165 1.00100.11 C ANISOU 849 C GLU A 181 12285 14767 10986 155 1012 -349 C ATOM 850 O GLU A 181 -31.807 11.489 12.467 1.00100.89 O ANISOU 850 O GLU A 181 12349 14992 10994 -18 1139 -227 O ATOM 851 CB GLU A 181 -31.738 13.411 14.562 1.00105.44 C ANISOU 851 CB GLU A 181 13106 15673 11282 384 1164 -544 C ATOM 852 N LYS A 182 -30.819 12.912 11.021 1.00 95.49 N ANISOU 852 N LYS A 182 11709 13975 10598 145 849 -325 N ATOM 853 CA LYS A 182 -30.040 11.905 10.284 1.00 91.15 C ANISOU 853 CA LYS A 182 11215 13280 10136 -49 774 -172 C ATOM 854 C LYS A 182 -28.618 12.491 10.163 1.00 86.14 C ANISOU 854 C LYS A 182 10764 12396 9567 7 582 -199 C ATOM 855 O LYS A 182 -28.439 13.725 10.264 1.00 86.59 O ANISOU 855 O LYS A 182 10859 12380 9661 178 498 -327 O ATOM 856 CB LYS A 182 -30.636 11.589 8.899 1.00 90.75 C ANISOU 856 CB LYS A 182 10982 13240 10257 -130 765 -109 C ATOM 857 CG LYS A 182 -30.176 10.231 8.315 1.00 90.52 C ANISOU 857 CG LYS A 182 10987 13134 10272 -354 748 48 C ATOM 858 CD LYS A 182 -29.901 10.342 6.820 1.00 90.71 C ANISOU 858 CD LYS A 182 10949 13027 10488 -376 623 79 C ATOM 859 CE LYS A 182 -29.873 8.987 6.117 1.00 91.12 C ANISOU 859 CE LYS A 182 10978 13056 10587 -585 634 208 C ATOM 860 NZ LYS A 182 -29.215 9.078 4.744 1.00 90.82 N ANISOU 860 NZ LYS A 182 10941 12857 10707 -595 490 236 N ATOM 861 N GLU A 183 -27.631 11.603 9.984 1.00 79.64 N ANISOU 861 N GLU A 183 10053 11447 8760 -136 514 -82 N ATOM 862 CA GLU A 183 -26.235 11.960 10.040 1.00 74.27 C ANISOU 862 CA GLU A 183 9537 10565 8117 -110 349 -92 C ATOM 863 C GLU A 183 -25.878 12.754 8.753 1.00 68.07 C ANISOU 863 C GLU A 183 8694 9629 7542 -63 217 -110 C ATOM 864 O GLU A 183 -26.116 12.255 7.666 1.00 68.74 O ANISOU 864 O GLU A 183 8675 9708 7736 -150 222 -29 O ATOM 865 CB GLU A 183 -25.402 10.663 10.142 1.00 73.99 C ANISOU 865 CB GLU A 183 9607 10464 8041 -271 329 48 C ATOM 866 CG GLU A 183 -24.034 10.827 10.800 1.00 75.05 C ANISOU 866 CG GLU A 183 9928 10462 8126 -241 196 34 C ATOM 867 CD GLU A 183 -23.598 9.660 11.739 1.00 77.18 C ANISOU 867 CD GLU A 183 10333 10760 8232 -337 232 133 C ATOM 868 OE1 GLU A 183 -23.400 8.524 11.257 1.00 76.28 O ANISOU 868 OE1 GLU A 183 10220 10606 8156 -470 242 262 O ATOM 869 OE2 GLU A 183 -23.415 9.910 12.963 1.00 78.50 O ANISOU 869 OE2 GLU A 183 10617 10979 8229 -269 237 77 O ATOM 870 N VAL A 184 -25.352 13.969 8.880 1.00 61.01 N ANISOU 870 N VAL A 184 7870 8616 6695 68 101 -214 N ATOM 871 CA VAL A 184 -24.669 14.659 7.775 1.00 55.61 C ANISOU 871 CA VAL A 184 7180 7753 6197 83 -44 -201 C ATOM 872 C VAL A 184 -23.197 14.200 7.706 1.00 50.23 C ANISOU 872 C VAL A 184 6617 6925 5544 -17 -160 -124 C ATOM 873 O VAL A 184 -22.487 14.204 8.716 1.00 49.89 O ANISOU 873 O VAL A 184 6705 6849 5401 -5 -204 -160 O ATOM 874 CB VAL A 184 -24.728 16.203 7.940 1.00 57.17 C ANISOU 874 CB VAL A 184 7412 7864 6448 257 -129 -341 C ATOM 875 CG1 VAL A 184 -24.086 16.897 6.778 1.00 55.87 C ANISOU 875 CG1 VAL A 184 7240 7517 6472 255 -268 -304 C ATOM 876 CG2 VAL A 184 -26.227 16.701 8.154 1.00 61.99 C ANISOU 876 CG2 VAL A 184 7901 8639 7015 396 -10 -441 C ATOM 877 N LEU A 185 -22.739 13.787 6.540 1.00 46.95 N ANISOU 877 N LEU A 185 6150 6436 5254 -107 -208 -22 N ATOM 878 CA LEU A 185 -21.393 13.299 6.292 1.00 42.86 C ANISOU 878 CA LEU A 185 5707 5799 4779 -194 -307 56 C ATOM 879 C LEU A 185 -20.650 14.150 5.256 1.00 43.46 C ANISOU 879 C LEU A 185 5761 5730 5021 -182 -432 70 C ATOM 880 O LEU A 185 -21.298 14.714 4.381 1.00 42.67 O ANISOU 880 O LEU A 185 5569 5632 5012 -142 -424 68 O ATOM 881 CB LEU A 185 -21.410 11.882 5.756 1.00 43.29 C ANISOU 881 CB LEU A 185 5722 5899 4825 -322 -245 175 C ATOM 882 CG LEU A 185 -22.199 10.842 6.585 1.00 45.85 C ANISOU 882 CG LEU A 185 6059 6362 5000 -377 -109 201 C ATOM 883 CD1 LEU A 185 -22.646 9.573 5.739 1.00 47.99 C ANISOU 883 CD1 LEU A 185 6253 6676 5304 -507 -38 306 C ATOM 884 CD2 LEU A 185 -21.305 10.405 7.724 1.00 46.74 C ANISOU 884 CD2 LEU A 185 6326 6441 4994 -390 -148 212 C ATOM 885 N VAL A 186 -19.307 14.240 5.415 1.00 40.42 N ANISOU 885 N VAL A 186 5459 5231 4668 -216 -547 89 N ATOM 886 CA VAL A 186 -18.429 14.853 4.417 1.00 40.50 C ANISOU 886 CA VAL A 186 5443 5114 4831 -241 -657 133 C ATOM 887 C VAL A 186 -17.393 13.851 3.992 1.00 37.66 C ANISOU 887 C VAL A 186 5080 4738 4490 -341 -685 234 C ATOM 888 O VAL A 186 -16.971 13.016 4.748 1.00 38.69 O ANISOU 888 O VAL A 186 5275 4899 4528 -371 -678 247 O ATOM 889 CB VAL A 186 -17.756 16.187 4.909 1.00 42.64 C ANISOU 889 CB VAL A 186 5793 5251 5155 -184 -788 48 C ATOM 890 CG1 VAL A 186 -18.858 17.226 5.253 1.00 45.79 C ANISOU 890 CG1 VAL A 186 6199 5655 5543 -57 -763 -66 C ATOM 891 CG2 VAL A 186 -16.764 15.919 6.149 1.00 40.92 C ANISOU 891 CG2 VAL A 186 5691 5012 4843 -201 -861 6 C ATOM 892 N TRP A 187 -16.985 13.942 2.744 1.00 37.23 N ANISOU 892 N TRP A 187 4952 4640 4553 -383 -716 308 N ATOM 893 CA TRP A 187 -15.820 13.280 2.302 1.00 36.40 C ANISOU 893 CA TRP A 187 4839 4507 4485 -454 -762 386 C ATOM 894 C TRP A 187 -14.544 13.852 2.937 1.00 37.14 C ANISOU 894 C TRP A 187 4992 4512 4609 -459 -887 360 C ATOM 895 O TRP A 187 -14.380 15.057 3.076 1.00 37.66 O ANISOU 895 O TRP A 187 5078 4493 4738 -432 -964 310 O ATOM 896 CB TRP A 187 -15.703 13.414 0.788 1.00 38.26 C ANISOU 896 CB TRP A 187 4977 4730 4829 -488 -762 465 C ATOM 897 CG TRP A 187 -16.410 12.397 -0.059 1.00 37.79 C ANISOU 897 CG TRP A 187 4853 4760 4746 -519 -668 516 C ATOM 898 CD1 TRP A 187 -15.903 11.195 -0.466 1.00 37.39 C ANISOU 898 CD1 TRP A 187 4793 4738 4675 -571 -645 573 C ATOM 899 CD2 TRP A 187 -17.650 12.553 -0.747 1.00 34.55 C ANISOU 899 CD2 TRP A 187 4373 4409 4345 -497 -603 513 C ATOM 900 NE1 TRP A 187 -16.731 10.618 -1.381 1.00 38.97 N ANISOU 900 NE1 TRP A 187 4930 5003 4872 -593 -575 600 N ATOM 901 CE2 TRP A 187 -17.839 11.396 -1.531 1.00 37.24 C ANISOU 901 CE2 TRP A 187 4669 4815 4667 -554 -547 566 C ATOM 902 CE3 TRP A 187 -18.611 13.556 -0.801 1.00 39.37 C ANISOU 902 CE3 TRP A 187 4954 5025 4981 -428 -597 467 C ATOM 903 CZ2 TRP A 187 -18.946 11.214 -2.332 1.00 42.27 C ANISOU 903 CZ2 TRP A 187 5228 5528 5306 -556 -491 572 C ATOM 904 CZ3 TRP A 187 -19.694 13.382 -1.599 1.00 38.11 C ANISOU 904 CZ3 TRP A 187 4707 4947 4826 -419 -538 481 C ATOM 905 CH2 TRP A 187 -19.876 12.219 -2.349 1.00 39.48 C ANISOU 905 CH2 TRP A 187 4831 5194 4976 -489 -487 532 C ATOM 906 N ARG A 188 -13.645 12.963 3.326 1.00 39.00 N ANISOU 906 N ARG A 188 5256 4760 4801 -494 -917 393 N ATOM 907 CA ARG A 188 -12.399 13.365 4.027 1.00 40.05 C ANISOU 907 CA ARG A 188 5435 4831 4952 -502 -1046 365 C ATOM 908 C ARG A 188 -11.266 12.490 3.529 1.00 40.95 C ANISOU 908 C ARG A 188 5497 4960 5102 -548 -1077 448 C ATOM 909 O ARG A 188 -11.336 11.249 3.631 1.00 39.74 O ANISOU 909 O ARG A 188 5364 4862 4872 -547 -1022 487 O ATOM 910 CB ARG A 188 -12.515 13.245 5.548 1.00 42.48 C ANISOU 910 CB ARG A 188 5862 5159 5120 -456 -1069 284 C ATOM 911 CG ARG A 188 -11.172 13.752 6.210 1.00 46.01 C ANISOU 911 CG ARG A 188 6346 5540 5595 -468 -1229 246 C ATOM 912 CD ARG A 188 -11.362 14.416 7.479 1.00 51.46 C ANISOU 912 CD ARG A 188 7148 6211 6193 -414 -1287 129 C ATOM 913 NE ARG A 188 -12.312 15.493 7.479 1.00 50.91 N ANISOU 913 NE ARG A 188 7099 6102 6144 -364 -1260 46 N ATOM 914 CZ ARG A 188 -12.935 15.833 8.585 1.00 52.31 C ANISOU 914 CZ ARG A 188 7378 6304 6195 -287 -1249 -65 C ATOM 915 NH1 ARG A 188 -12.670 15.141 9.685 1.00 52.08 N ANISOU 915 NH1 ARG A 188 7438 6342 6010 -270 -1263 -85 N ATOM 916 NH2 ARG A 188 -13.847 16.822 8.618 1.00 50.34 N ANISOU 916 NH2 ARG A 188 7146 6021 5960 -216 -1222 -156 N ATOM 917 N PHE A 189 -10.175 13.122 3.073 1.00 40.03 N ANISOU 917 N PHE A 189 5317 4793 5100 -588 -1172 473 N ATOM 918 CA PHE A 189 -8.965 12.377 2.704 1.00 38.29 C ANISOU 918 CA PHE A 189 5031 4603 4915 -617 -1211 538 C ATOM 919 C PHE A 189 -8.217 11.910 3.920 1.00 39.09 C ANISOU 919 C PHE A 189 5202 4712 4940 -592 -1298 502 C ATOM 920 O PHE A 189 -8.203 12.626 4.940 1.00 42.35 O ANISOU 920 O PHE A 189 5692 5084 5316 -578 -1377 422 O ATOM 921 CB PHE A 189 -8.039 13.255 1.787 1.00 39.32 C ANISOU 921 CB PHE A 189 5048 4698 5195 -681 -1273 586 C ATOM 922 CG PHE A 189 -6.805 12.535 1.351 1.00 38.35 C ANISOU 922 CG PHE A 189 4830 4632 5110 -701 -1301 648 C ATOM 923 CD1 PHE A 189 -5.657 12.576 2.114 1.00 44.93 C ANISOU 923 CD1 PHE A 189 5650 5463 5957 -710 -1420 625 C ATOM 924 CD2 PHE A 189 -6.777 11.820 0.204 1.00 40.88 C ANISOU 924 CD2 PHE A 189 5071 5016 5446 -701 -1214 719 C ATOM 925 CE1 PHE A 189 -4.459 11.982 1.683 1.00 45.53 C ANISOU 925 CE1 PHE A 189 5614 5606 6081 -717 -1450 679 C ATOM 926 CE2 PHE A 189 -5.598 11.149 -0.223 1.00 44.33 C ANISOU 926 CE2 PHE A 189 5410 5517 5916 -699 -1234 766 C ATOM 927 CZ PHE A 189 -4.456 11.232 0.533 1.00 46.45 C ANISOU 927 CZ PHE A 189 5651 5789 6209 -703 -1350 747 C ATOM 928 N ASP A 190 -7.670 10.684 3.887 1.00 39.37 N ANISOU 928 N ASP A 190 5228 4796 4934 -572 -1290 551 N ATOM 929 CA ASP A 190 -6.889 10.210 4.998 1.00 42.09 C ANISOU 929 CA ASP A 190 5637 5150 5205 -537 -1387 529 C ATOM 930 C ASP A 190 -5.735 9.338 4.498 1.00 42.12 C ANISOU 930 C ASP A 190 5554 5192 5256 -523 -1425 592 C ATOM 931 O ASP A 190 -5.969 8.230 3.960 1.00 41.11 O ANISOU 931 O ASP A 190 5430 5090 5102 -495 -1342 642 O ATOM 932 CB ASP A 190 -7.760 9.391 5.964 1.00 42.61 C ANISOU 932 CB ASP A 190 5848 5235 5107 -492 -1329 514 C ATOM 933 CG ASP A 190 -7.026 8.982 7.222 1.00 48.58 C ANISOU 933 CG ASP A 190 6695 6000 5761 -447 -1439 495 C ATOM 934 OD1 ASP A 190 -5.746 9.067 7.275 1.00 47.08 O ANISOU 934 OD1 ASP A 190 6441 5813 5635 -442 -1565 498 O ATOM 935 OD2 ASP A 190 -7.743 8.466 8.137 1.00 48.11 O ANISOU 935 OD2 ASP A 190 6769 5960 5552 -417 -1395 486 O ATOM 936 N SER A 191 -4.515 9.853 4.643 1.00 41.45 N ANISOU 936 N SER A 191 5388 5113 5249 -541 -1549 582 N ATOM 937 CA SER A 191 -3.344 9.184 4.070 1.00 43.78 C ANISOU 937 CA SER A 191 5561 5464 5607 -520 -1584 636 C ATOM 938 C SER A 191 -3.091 7.771 4.737 1.00 42.50 C ANISOU 938 C SER A 191 5487 5325 5336 -424 -1606 653 C ATOM 939 O SER A 191 -2.588 6.848 4.091 1.00 44.13 O ANISOU 939 O SER A 191 5632 5567 5567 -375 -1579 699 O ATOM 940 CB SER A 191 -2.080 10.060 4.154 1.00 44.74 C ANISOU 940 CB SER A 191 5558 5602 5839 -571 -1718 623 C ATOM 941 OG SER A 191 -1.778 10.227 5.485 1.00 49.32 O ANISOU 941 OG SER A 191 6226 6164 6349 -548 -1847 560 O ATOM 942 N LYS A 192 -3.567 7.567 5.939 1.00 42.69 N ANISOU 942 N LYS A 192 5667 5322 5232 -393 -1637 620 N ATOM 943 CA LYS A 192 -3.354 6.300 6.649 1.00 43.02 C ANISOU 943 CA LYS A 192 5816 5369 5162 -308 -1668 650 C ATOM 944 C LYS A 192 -4.174 5.181 5.974 1.00 42.77 C ANISOU 944 C LYS A 192 5836 5315 5098 -291 -1528 706 C ATOM 945 O LYS A 192 -3.894 4.021 6.189 1.00 40.88 O ANISOU 945 O LYS A 192 5665 5063 4806 -222 -1544 747 O ATOM 946 CB LYS A 192 -3.810 6.401 8.101 1.00 43.43 C ANISOU 946 CB LYS A 192 6036 5404 5059 -289 -1718 612 C ATOM 947 CG LYS A 192 -2.982 7.360 8.963 1.00 52.09 C ANISOU 947 CG LYS A 192 7115 6516 6160 -295 -1883 541 C ATOM 948 CD LYS A 192 -3.478 7.424 10.440 1.00 58.15 C ANISOU 948 CD LYS A 192 8070 7283 6743 -262 -1928 494 C ATOM 949 CE LYS A 192 -5.014 7.704 10.657 1.00 60.74 C ANISOU 949 CE LYS A 192 8509 7595 6975 -291 -1781 467 C ATOM 950 NZ LYS A 192 -5.487 9.061 10.192 1.00 60.80 N ANISOU 950 NZ LYS A 192 8448 7573 7080 -353 -1751 393 N ATOM 951 N LEU A 193 -5.199 5.543 5.189 1.00 42.38 N ANISOU 951 N LEU A 193 5765 5257 5082 -353 -1402 703 N ATOM 952 CA LEU A 193 -5.972 4.524 4.457 1.00 42.52 C ANISOU 952 CA LEU A 193 5819 5257 5081 -353 -1281 746 C ATOM 953 C LEU A 193 -5.187 3.812 3.326 1.00 42.55 C ANISOU 953 C LEU A 193 5719 5277 5170 -309 -1274 777 C ATOM 954 O LEU A 193 -5.638 2.797 2.820 1.00 41.39 O ANISOU 954 O LEU A 193 5621 5101 5002 -292 -1202 802 O ATOM 955 CB LEU A 193 -7.270 5.116 3.923 1.00 41.74 C ANISOU 955 CB LEU A 193 5709 5158 4991 -424 -1163 729 C ATOM 956 CG LEU A 193 -8.217 5.687 4.991 1.00 42.50 C ANISOU 956 CG LEU A 193 5908 5251 4990 -449 -1142 690 C ATOM 957 CD1 LEU A 193 -9.400 6.442 4.379 1.00 43.64 C ANISOU 957 CD1 LEU A 193 6007 5408 5166 -501 -1040 664 C ATOM 958 CD2 LEU A 193 -8.738 4.545 5.829 1.00 38.93 C ANISOU 958 CD2 LEU A 193 5606 4783 4402 -434 -1105 726 C ATOM 959 N ALA A 194 -3.996 4.289 2.985 1.00 40.51 N ANISOU 959 N ALA A 194 5321 5068 5003 -288 -1351 772 N ATOM 960 CA ALA A 194 -3.153 3.626 1.977 1.00 40.17 C ANISOU 960 CA ALA A 194 5167 5066 5030 -228 -1343 793 C ATOM 961 C ALA A 194 -2.535 2.362 2.579 1.00 41.41 C ANISOU 961 C ALA A 194 5407 5195 5131 -114 -1413 809 C ATOM 962 O ALA A 194 -2.143 1.480 1.844 1.00 41.32 O ANISOU 962 O ALA A 194 5364 5191 5147 -40 -1388 818 O ATOM 963 CB ALA A 194 -1.922 4.624 1.510 1.00 40.43 C ANISOU 963 CB ALA A 194 4993 5186 5182 -250 -1409 791 C ATOM 964 N PHE A 195 -2.487 2.304 3.905 1.00 42.04 N ANISOU 964 N PHE A 195 5605 5242 5127 -94 -1501 809 N ATOM 965 CA APHE A 195 -1.692 1.318 4.684 0.50 44.71 C ANISOU 965 CA APHE A 195 6020 5558 5411 23 -1610 831 C ATOM 966 CA BPHE A 195 -1.752 1.226 4.578 0.50 44.70 C ANISOU 966 CA BPHE A 195 6021 5552 5411 24 -1598 833 C ATOM 967 C PHE A 195 -2.547 0.485 5.667 1.00 44.80 C ANISOU 967 C PHE A 195 6263 5478 5280 31 -1597 868 C ATOM 968 O PHE A 195 -2.109 -0.545 6.102 1.00 45.07 O ANISOU 968 O PHE A 195 6392 5466 5267 129 -1661 905 O ATOM 969 CB APHE A 195 -0.588 2.027 5.497 0.50 46.37 C ANISOU 969 CB APHE A 195 6149 5831 5637 48 -1766 807 C ATOM 970 CB BPHE A 195 -0.323 1.637 5.028 0.50 46.51 C ANISOU 970 CB BPHE A 195 6126 5857 5689 86 -1752 816 C ATOM 971 CG APHE A 195 0.320 2.899 4.666 0.50 48.23 C ANISOU 971 CG APHE A 195 6150 6161 6014 16 -1789 783 C ATOM 972 CG BPHE A 195 -0.221 2.878 5.921 0.50 48.11 C ANISOU 972 CG BPHE A 195 6313 6089 5876 10 -1839 778 C ATOM 973 CD1APHE A 195 1.291 2.350 3.850 0.50 49.97 C ANISOU 973 CD1APHE A 195 6225 6447 6315 101 -1796 794 C ATOM 974 CD1BPHE A 195 -0.283 2.785 7.300 0.50 49.84 C ANISOU 974 CD1BPHE A 195 6683 6282 5972 38 -1936 774 C ATOM 975 CD2APHE A 195 0.228 4.280 4.743 0.50 49.76 C ANISOU 975 CD2APHE A 195 6271 6379 6258 -99 -1805 751 C ATOM 976 CD2BPHE A 195 0.052 4.126 5.372 0.50 47.44 C ANISOU 976 CD2BPHE A 195 6065 6059 5902 -83 -1837 746 C ATOM 977 CE1APHE A 195 2.107 3.154 3.075 0.50 52.18 C ANISOU 977 CE1APHE A 195 6277 6830 6717 57 -1800 785 C ATOM 978 CE1BPHE A 195 -0.112 3.952 8.133 0.50 50.77 C ANISOU 978 CE1BPHE A 195 6791 6428 6072 -22 -2033 718 C ATOM 979 CE2APHE A 195 1.026 5.068 3.973 0.50 51.81 C ANISOU 979 CE2APHE A 195 6323 6715 6648 -149 -1819 747 C ATOM 980 CE2BPHE A 195 0.176 5.227 6.157 0.50 48.23 C ANISOU 980 CE2BPHE A 195 6164 6164 5998 -149 -1929 701 C ATOM 981 CZ APHE A 195 1.965 4.509 3.123 0.50 51.61 C ANISOU 981 CZ APHE A 195 6140 6772 6697 -79 -1810 771 C ATOM 982 CZ BPHE A 195 0.091 5.144 7.575 0.50 49.27 C ANISOU 982 CZ BPHE A 195 6450 6270 5999 -115 -2032 676 C ATOM 983 N HIS A 196 -3.738 0.990 6.015 1.00 44.12 N ANISOU 983 N HIS A 196 6260 5375 5130 -69 -1514 861 N ATOM 984 CA HIS A 196 -4.626 0.330 6.939 1.00 46.22 C ANISOU 984 CA HIS A 196 6726 5579 5255 -86 -1479 904 C ATOM 985 C HIS A 196 -5.957 0.116 6.245 1.00 46.92 C ANISOU 985 C HIS A 196 6844 5637 5347 -178 -1321 914 C ATOM 986 O HIS A 196 -6.658 1.063 5.872 1.00 42.90 O ANISOU 986 O HIS A 196 6260 5172 4870 -258 -1246 873 O ATOM 987 CB HIS A 196 -4.824 1.158 8.223 1.00 46.78 C ANISOU 987 CB HIS A 196 6870 5687 5219 -114 -1532 879 C ATOM 988 CG HIS A 196 -3.596 1.282 9.063 1.00 51.68 C ANISOU 988 CG HIS A 196 7486 6338 5812 -28 -1706 868 C ATOM 989 ND1 HIS A 196 -3.140 0.268 9.907 1.00 53.75 N ANISOU 989 ND1 HIS A 196 7888 6564 5972 64 -1796 928 N ATOM 990 CD2 HIS A 196 -2.667 2.279 9.132 1.00 52.43 C ANISOU 990 CD2 HIS A 196 7445 6496 5980 -21 -1818 807 C ATOM 991 CE1 HIS A 196 -1.993 0.637 10.460 1.00 51.81 C ANISOU 991 CE1 HIS A 196 7584 6370 5732 133 -1959 899 C ATOM 992 NE2 HIS A 196 -1.684 1.854 10.008 1.00 56.63 N ANISOU 992 NE2 HIS A 196 8022 7042 6451 75 -1975 823 N ATOM 993 N HIS A 197 -6.262 -1.147 5.961 1.00 47.60 N ANISOU 993 N HIS A 197 7028 5642 5415 -163 -1279 963 N ATOM 994 CA HIS A 197 -7.550 -1.454 5.348 1.00 47.75 C ANISOU 994 CA HIS A 197 7076 5631 5435 -262 -1141 972 C ATOM 995 C HIS A 197 -8.520 -1.534 6.537 1.00 48.81 C ANISOU 995 C HIS A 197 7359 5757 5428 -332 -1094 1015 C ATOM 996 O HIS A 197 -8.823 -2.625 7.006 1.00 46.74 O ANISOU 996 O HIS A 197 7252 5414 5092 -341 -1083 1086 O ATOM 997 CB HIS A 197 -7.514 -2.843 4.653 1.00 47.98 C ANISOU 997 CB HIS A 197 7174 5558 5497 -230 -1125 1004 C ATOM 998 CG HIS A 197 -8.651 -3.081 3.736 1.00 47.43 C ANISOU 998 CG HIS A 197 7089 5470 5460 -331 -1004 992 C ATOM 999 ND1 HIS A 197 -8.778 -4.238 3.009 1.00 48.56 N ANISOU 999 ND1 HIS A 197 7295 5518 5639 -322 -986 1000 N ATOM 1000 CD2 HIS A 197 -9.704 -2.295 3.378 1.00 46.91 C ANISOU 1000 CD2 HIS A 197 6946 5473 5404 -436 -905 963 C ATOM 1001 CE1 HIS A 197 -9.854 -4.163 2.242 1.00 49.41 C ANISOU 1001 CE1 HIS A 197 7361 5640 5772 -428 -885 976 C ATOM 1002 NE2 HIS A 197 -10.430 -2.995 2.451 1.00 49.64 N ANISOU 1002 NE2 HIS A 197 7301 5774 5787 -494 -834 957 N ATOM 1003 N MET A 198 -9.007 -0.389 6.971 1.00 48.08 N ANISOU 1003 N MET A 198 7219 5746 5302 -379 -1063 971 N ATOM 1004 CA MET A 198 -9.859 -0.266 8.175 1.00 50.36 C ANISOU 1004 CA MET A 198 7629 6065 5441 -428 -1014 995 C ATOM 1005 C MET A 198 -11.208 -1.021 8.081 1.00 53.13 C ANISOU 1005 C MET A 198 8053 6392 5742 -534 -874 1049 C ATOM 1006 O MET A 198 -11.684 -1.588 9.127 1.00 53.50 O ANISOU 1006 O MET A 198 8251 6431 5647 -568 -842 1119 O ATOM 1007 CB MET A 198 -10.139 1.184 8.498 1.00 49.18 C ANISOU 1007 CB MET A 198 7400 6006 5280 -442 -1006 913 C ATOM 1008 CG MET A 198 -8.877 2.019 8.753 1.00 54.82 C ANISOU 1008 CG MET A 198 8050 6742 6037 -365 -1152 858 C ATOM 1009 SD MET A 198 -8.224 1.763 10.414 1.00 63.76 S ANISOU 1009 SD MET A 198 9346 7882 6997 -294 -1276 882 S ATOM 1010 CE MET A 198 -6.717 0.853 10.241 1.00 67.93 C ANISOU 1010 CE MET A 198 9872 8355 7584 -191 -1425 931 C ATOM 1011 N ALA A 199 -11.793 -1.063 6.886 1.00 50.68 N ANISOU 1011 N ALA A 199 7640 6077 5537 -592 -796 1025 N ATOM 1012 CA ALA A 199 -13.000 -1.857 6.615 1.00 55.43 C ANISOU 1012 CA ALA A 199 8287 6652 6121 -704 -678 1070 C ATOM 1013 C ALA A 199 -12.799 -3.340 6.978 1.00 59.63 C ANISOU 1013 C ALA A 199 8994 7058 6605 -712 -706 1166 C ATOM 1014 O ALA A 199 -13.694 -3.959 7.508 1.00 62.12 O ANISOU 1014 O ALA A 199 9410 7355 6837 -811 -627 1236 O ATOM 1015 CB ALA A 199 -13.428 -1.728 5.159 1.00 51.54 C ANISOU 1015 CB ALA A 199 7657 6169 5758 -745 -627 1019 C ATOM 1016 N ARG A 200 -11.616 -3.871 6.712 1.00 63.81 N ANISOU 1016 N ARG A 200 9556 7504 7186 -606 -819 1172 N ATOM 1017 CA ARG A 200 -11.268 -5.247 6.988 1.00 68.21 C ANISOU 1017 CA ARG A 200 10285 7919 7714 -581 -871 1257 C ATOM 1018 C ARG A 200 -10.679 -5.429 8.409 1.00 72.15 C ANISOU 1018 C ARG A 200 10933 8405 8078 -514 -955 1330 C ATOM 1019 O ARG A 200 -11.040 -6.385 9.097 1.00 74.71 O ANISOU 1019 O ARG A 200 11436 8641 8308 -560 -942 1435 O ATOM 1020 CB ARG A 200 -10.334 -5.765 5.896 1.00 68.40 C ANISOU 1020 CB ARG A 200 10260 7865 7864 -479 -946 1214 C ATOM 1021 CG ARG A 200 -9.695 -7.110 6.109 1.00 72.44 C ANISOU 1021 CG ARG A 200 10942 8216 8367 -400 -1033 1280 C ATOM 1022 CD ARG A 200 -9.160 -7.659 4.774 1.00 77.08 C ANISOU 1022 CD ARG A 200 11468 8736 9084 -323 -1063 1214 C ATOM 1023 NE ARG A 200 -8.418 -8.905 4.954 1.00 82.35 N ANISOU 1023 NE ARG A 200 12295 9241 9754 -209 -1163 1261 N ATOM 1024 CZ ARG A 200 -7.728 -9.556 4.008 1.00 87.43 C ANISOU 1024 CZ ARG A 200 12920 9808 10490 -93 -1215 1204 C ATOM 1025 NH1 ARG A 200 -7.622 -9.083 2.762 1.00 89.06 N ANISOU 1025 NH1 ARG A 200 12950 10099 10788 -76 -1173 1100 N ATOM 1026 NH2 ARG A 200 -7.115 -10.701 4.322 1.00 89.27 N ANISOU 1026 NH2 ARG A 200 13322 9879 10716 22 -1313 1251 N ATOM 1027 N GLU A 201 -9.810 -4.509 8.846 1.00 74.25 N ANISOU 1027 N GLU A 201 11128 8757 8327 -416 -1045 1279 N ATOM 1028 CA GLU A 201 -9.224 -4.504 10.207 1.00 78.33 C ANISOU 1028 CA GLU A 201 11769 9290 8704 -344 -1141 1330 C ATOM 1029 C GLU A 201 -10.293 -4.154 11.257 1.00 81.72 C ANISOU 1029 C GLU A 201 12282 9798 8969 -443 -1042 1367 C ATOM 1030 O GLU A 201 -10.059 -4.330 12.454 1.00 84.10 O ANISOU 1030 O GLU A 201 12726 10112 9116 -407 -1096 1429 O ATOM 1031 CB GLU A 201 -7.954 -3.571 10.284 1.00 77.88 C ANISOU 1031 CB GLU A 201 11589 9308 8693 -221 -1279 1247 C ATOM 1032 CG GLU A 201 -6.705 -4.104 9.411 1.00 76.82 C ANISOU 1032 CG GLU A 201 11380 9111 8699 -97 -1388 1228 C ATOM 1033 CD GLU A 201 -5.707 -3.002 8.847 1.00 74.96 C ANISOU 1033 CD GLU A 201 10925 8976 8582 -34 -1464 1127 C ATOM 1034 OE1 GLU A 201 -5.460 -2.002 9.605 1.00 74.24 O ANISOU 1034 OE1 GLU A 201 10800 8972 8438 -33 -1522 1087 O ATOM 1035 OE2 GLU A 201 -5.148 -3.194 7.680 1.00 60.79 O ANISOU 1035 OE2 GLU A 201 9004 7169 6925 15 -1469 1091 O ATOM 1036 N LEU A 202 -11.483 -3.751 10.807 1.00 84.48 N ANISOU 1036 N LEU A 202 12549 10207 9344 -563 -894 1335 N ATOM 1037 CA LEU A 202 -12.642 -3.531 11.687 1.00 88.61 C ANISOU 1037 CA LEU A 202 13131 10819 9716 -663 -770 1370 C ATOM 1038 C LEU A 202 -13.911 -4.403 11.430 1.00 91.76 C ANISOU 1038 C LEU A 202 13577 11182 10107 -820 -622 1452 C ATOM 1039 O LEU A 202 -14.861 -4.344 12.224 1.00 93.41 O ANISOU 1039 O LEU A 202 13835 11477 10181 -908 -509 1500 O ATOM 1040 CB LEU A 202 -13.032 -2.041 11.699 1.00 87.58 C ANISOU 1040 CB LEU A 202 12852 10834 9590 -659 -724 1249 C ATOM 1041 CG LEU A 202 -11.970 -1.027 12.162 1.00 87.50 C ANISOU 1041 CG LEU A 202 12805 10872 9567 -538 -861 1163 C ATOM 1042 CD1 LEU A 202 -12.516 0.363 11.976 1.00 85.97 C ANISOU 1042 CD1 LEU A 202 12473 10785 9407 -549 -805 1044 C ATOM 1043 CD2 LEU A 202 -11.510 -1.236 13.627 1.00 90.89 C ANISOU 1043 CD2 LEU A 202 13409 11326 9802 -478 -940 1216 C ATOM 1044 N HIS A 203 -13.932 -5.205 10.359 1.00 94.15 N ANISOU 1044 N HIS A 203 13862 11366 10546 -858 -622 1466 N ATOM 1045 CA HIS A 203 -15.027 -6.168 10.086 1.00 96.98 C ANISOU 1045 CA HIS A 203 14276 11659 10911 -1018 -511 1545 C ATOM 1046 C HIS A 203 -14.480 -7.618 9.836 1.00 99.01 C ANISOU 1046 C HIS A 203 14700 11705 11216 -1007 -594 1634 C ATOM 1047 O HIS A 203 -13.648 -8.124 10.616 1.00100.22 O ANISOU 1047 O HIS A 203 15013 11779 11289 -916 -696 1710 O ATOM 1048 CB HIS A 203 -15.909 -5.694 8.915 1.00 95.95 C ANISOU 1048 CB HIS A 203 13955 11595 10909 -1103 -416 1455 C ATOM 1049 CG HIS A 203 -16.810 -4.527 9.236 1.00 99.92 C ANISOU 1049 CG HIS A 203 14324 12286 11355 -1144 -306 1395 C ATOM 1050 ND1 HIS A 203 -16.462 -3.514 10.115 1.00103.43 N ANISOU 1050 ND1 HIS A 203 14760 12839 11700 -1051 -331 1351 N ATOM 1051 CD2 HIS A 203 -18.044 -4.199 8.761 1.00101.97 C ANISOU 1051 CD2 HIS A 203 14450 12644 11650 -1255 -180 1360 C ATOM 1052 CE1 HIS A 203 -17.448 -2.633 10.189 1.00102.41 C ANISOU 1052 CE1 HIS A 203 14509 12858 11545 -1094 -219 1291 C ATOM 1053 NE2 HIS A 203 -18.423 -3.030 9.384 1.00102.49 N ANISOU 1053 NE2 HIS A 203 14435 12871 11635 -1216 -125 1300 N ATOM 1054 N PRO A 204 -14.949 -8.296 8.759 1.00100.12 N ANISOU 1054 N PRO A 204 14813 11748 11482 -1093 -560 1620 N ATOM 1055 CA PRO A 204 -14.730 -9.749 8.523 1.00102.49 C ANISOU 1055 CA PRO A 204 15290 11826 11824 -1115 -618 1701 C ATOM 1056 C PRO A 204 -15.546 -10.335 7.357 1.00102.85 C ANISOU 1056 C PRO A 204 15288 11795 11997 -1248 -560 1664 C ATOM 1057 O PRO A 204 -15.960 -11.484 7.425 1.00104.79 O ANISOU 1057 O PRO A 204 15689 11880 12247 -1358 -554 1755 O ATOM 1058 CB PRO A 204 -15.169 -10.395 9.857 1.00104.29 C ANISOU 1058 CB PRO A 204 15721 12014 11890 -1209 -579 1867 C ATOM 1059 N GLU A 205 -15.757 -9.536 6.308 1.00102.39 N ANISOU 1059 N GLU A 205 15021 11845 12037 -1238 -528 1534 N ATOM 1060 CA GLU A 205 -16.516 -9.917 5.097 1.00102.66 C ANISOU 1060 CA GLU A 205 14979 11840 12186 -1350 -484 1473 C ATOM 1061 C GLU A 205 -15.628 -9.936 3.837 1.00101.46 C ANISOU 1061 C GLU A 205 14759 11636 12156 -1209 -575 1356 C ATOM 1062 O GLU A 205 -15.076 -10.975 3.471 1.00102.74 O ANISOU 1062 O GLU A 205 15052 11617 12368 -1156 -657 1361 O ATOM 1063 CB GLU A 205 -17.691 -8.940 4.882 1.00101.99 C ANISOU 1063 CB GLU A 205 14697 11954 12098 -1466 -358 1423 C ATOM 1064 CG GLU A 205 -17.313 -7.529 4.307 1.00100.61 C ANISOU 1064 CG GLU A 205 14317 11943 11967 -1342 -368 1302 C ATOM 1065 CD GLU A 205 -18.261 -6.396 4.777 1.00100.84 C ANISOU 1065 CD GLU A 205 14206 12173 11936 -1402 -257 1284 C ATOM 1066 OE1 GLU A 205 -19.309 -6.719 5.394 1.00102.18 O ANISOU 1066 OE1 GLU A 205 14404 12382 12038 -1549 -158 1354 O ATOM 1067 OE2 GLU A 205 -17.959 -5.188 4.552 1.00 95.38 O ANISOU 1067 OE2 GLU A 205 13378 11598 11265 -1302 -269 1202 O TER 1068 GLU A 205 ATOM 1069 N GLU B 79 9.257 -3.561 -36.825 1.00100.72 N ANISOU 1069 N GLU B 79 12612 13459 12197 3987 3125 962 N ATOM 1070 CA GLU B 79 9.418 -2.080 -36.665 1.00 98.51 C ANISOU 1070 CA GLU B 79 11886 13579 11965 3638 3022 1200 C ATOM 1071 C GLU B 79 8.338 -1.374 -35.815 1.00 92.57 C ANISOU 1071 C GLU B 79 11126 12733 11314 3138 2614 1205 C ATOM 1072 O GLU B 79 7.279 -1.953 -35.524 1.00 91.35 O ANISOU 1072 O GLU B 79 11325 12238 11144 3004 2404 1005 O ATOM 1073 CB GLU B 79 9.444 -1.414 -38.036 1.00 99.96 C ANISOU 1073 CB GLU B 79 12160 13980 11840 3613 3233 1141 C ATOM 1074 CG GLU B 79 10.259 -0.152 -38.069 1.00101.49 C ANISOU 1074 CG GLU B 79 11838 14622 12103 3464 3326 1459 C ATOM 1075 CD GLU B 79 11.049 -0.088 -39.323 1.00109.38 C ANISOU 1075 CD GLU B 79 12810 15887 12861 3746 3742 1493 C ATOM 1076 OE1 GLU B 79 10.413 0.135 -40.366 1.00112.48 O ANISOU 1076 OE1 GLU B 79 13561 16244 12932 3668 3790 1320 O ATOM 1077 OE2 GLU B 79 12.287 -0.296 -39.287 1.00114.98 O ANISOU 1077 OE2 GLU B 79 13142 16864 13683 4063 4027 1695 O ATOM 1078 N ASP B 80 8.621 -0.110 -35.467 1.00 89.39 N ANISOU 1078 N ASP B 80 10327 12634 11005 2863 2525 1434 N ATOM 1079 CA ASP B 80 7.770 0.715 -34.584 1.00 83.98 C ANISOU 1079 CA ASP B 80 9580 11901 10426 2430 2180 1471 C ATOM 1080 C ASP B 80 6.310 0.790 -35.050 1.00 79.35 C ANISOU 1080 C ASP B 80 9409 11086 9653 2204 2005 1228 C ATOM 1081 O ASP B 80 6.040 1.096 -36.219 1.00 79.52 O ANISOU 1081 O ASP B 80 9619 11167 9426 2203 2114 1131 O ATOM 1082 CB ASP B 80 8.308 2.165 -34.533 1.00 84.31 C ANISOU 1082 CB ASP B 80 9238 12274 10523 2177 2177 1710 C ATOM 1083 CG ASP B 80 9.582 2.335 -33.652 1.00 88.14 C ANISOU 1083 CG ASP B 80 9212 13025 11251 2226 2204 1986 C ATOM 1084 OD1 ASP B 80 10.039 1.387 -32.992 1.00 90.68 O ANISOU 1084 OD1 ASP B 80 9446 13301 11707 2477 2204 2025 O ATOM 1085 OD2 ASP B 80 10.107 3.470 -33.610 1.00 92.07 O ANISOU 1085 OD2 ASP B 80 9396 13782 11805 1986 2204 2179 O ATOM 1086 N ILE B 81 5.385 0.540 -34.127 1.00 73.38 N ANISOU 1086 N ILE B 81 8766 10112 9005 2010 1732 1155 N ATOM 1087 CA ILE B 81 3.971 0.830 -34.339 1.00 68.76 C ANISOU 1087 CA ILE B 81 8439 9392 8294 1736 1519 989 C ATOM 1088 C ILE B 81 3.703 2.287 -33.939 1.00 63.50 C ANISOU 1088 C ILE B 81 7539 8904 7683 1444 1373 1143 C ATOM 1089 O ILE B 81 3.834 2.650 -32.771 1.00 59.81 O ANISOU 1089 O ILE B 81 6852 8461 7412 1314 1239 1271 O ATOM 1090 CB ILE B 81 3.077 -0.138 -33.525 1.00 67.81 C ANISOU 1090 CB ILE B 81 8529 8969 8267 1655 1322 857 C ATOM 1091 CG1 ILE B 81 3.307 -1.588 -34.004 1.00 73.22 C ANISOU 1091 CG1 ILE B 81 9532 9399 8891 1936 1475 684 C ATOM 1092 CG2 ILE B 81 1.625 0.253 -33.664 1.00 65.14 C ANISOU 1092 CG2 ILE B 81 8357 8569 7823 1353 1095 728 C ATOM 1093 CD1 ILE B 81 2.510 -2.669 -33.204 1.00 75.60 C ANISOU 1093 CD1 ILE B 81 10075 9347 9302 1845 1307 579 C ATOM 1094 N ILE B 82 3.350 3.123 -34.916 1.00 60.92 N ANISOU 1094 N ILE B 82 7290 8690 7166 1354 1405 1133 N ATOM 1095 CA ILE B 82 3.149 4.556 -34.668 1.00 58.06 C ANISOU 1095 CA ILE B 82 6760 8451 6850 1114 1303 1288 C ATOM 1096 C ILE B 82 1.674 4.866 -34.701 1.00 53.67 C ANISOU 1096 C ILE B 82 6400 7789 6204 937 1079 1172 C ATOM 1097 O ILE B 82 0.996 4.511 -35.662 1.00 54.53 O ANISOU 1097 O ILE B 82 6754 7872 6093 977 1069 1026 O ATOM 1098 CB ILE B 82 3.839 5.500 -35.711 1.00 60.49 C ANISOU 1098 CB ILE B 82 6986 8973 7022 1132 1508 1439 C ATOM 1099 CG1 ILE B 82 5.334 5.190 -35.830 1.00 67.79 C ANISOU 1099 CG1 ILE B 82 7664 10073 8018 1325 1772 1575 C ATOM 1100 CG2 ILE B 82 3.528 6.978 -35.384 1.00 56.34 C ANISOU 1100 CG2 ILE B 82 6359 8485 6564 867 1386 1593 C ATOM 1101 CD1 ILE B 82 6.129 5.260 -34.529 1.00 66.52 C ANISOU 1101 CD1 ILE B 82 7158 9971 8148 1261 1704 1728 C ATOM 1102 N VAL B 83 1.202 5.563 -33.663 1.00 49.19 N ANISOU 1102 N VAL B 83 5712 7187 5792 746 902 1241 N ATOM 1103 CA VAL B 83 -0.157 6.057 -33.570 1.00 45.95 C ANISOU 1103 CA VAL B 83 5409 6722 5328 600 707 1181 C ATOM 1104 C VAL B 83 -0.211 7.566 -33.356 1.00 45.78 C ANISOU 1104 C VAL B 83 5286 6756 5354 472 674 1338 C ATOM 1105 O VAL B 83 0.772 8.200 -32.861 1.00 44.32 O ANISOU 1105 O VAL B 83 4924 6613 5301 411 746 1481 O ATOM 1106 CB VAL B 83 -1.007 5.320 -32.452 1.00 45.16 C ANISOU 1106 CB VAL B 83 5327 6482 5349 515 528 1078 C ATOM 1107 CG1 VAL B 83 -1.076 3.802 -32.704 1.00 42.24 C ANISOU 1107 CG1 VAL B 83 5129 5985 4937 613 551 918 C ATOM 1108 CG2 VAL B 83 -0.493 5.588 -31.087 1.00 42.84 C ANISOU 1108 CG2 VAL B 83 4841 6176 5261 446 490 1184 C ATOM 1109 N VAL B 84 -1.333 8.153 -33.824 1.00 43.84 N ANISOU 1109 N VAL B 84 5160 6511 4987 432 566 1319 N ATOM 1110 CA VAL B 84 -1.595 9.586 -33.733 1.00 44.26 C ANISOU 1110 CA VAL B 84 5194 6558 5064 353 534 1459 C ATOM 1111 C VAL B 84 -2.826 9.727 -32.845 1.00 42.71 C ANISOU 1111 C VAL B 84 4998 6289 4941 296 349 1391 C ATOM 1112 O VAL B 84 -3.807 9.008 -33.099 1.00 42.21 O ANISOU 1112 O VAL B 84 4996 6256 4787 321 241 1273 O ATOM 1113 CB VAL B 84 -1.906 10.261 -35.122 1.00 44.98 C ANISOU 1113 CB VAL B 84 5425 6735 4928 422 583 1545 C ATOM 1114 CG1 VAL B 84 -2.067 11.796 -34.962 1.00 43.07 C ANISOU 1114 CG1 VAL B 84 5196 6422 4745 359 574 1724 C ATOM 1115 CG2 VAL B 84 -0.762 9.985 -36.092 1.00 48.84 C ANISOU 1115 CG2 VAL B 84 5926 7334 5298 501 801 1603 C ATOM 1116 N ALA B 85 -2.771 10.632 -31.857 1.00 41.23 N ANISOU 1116 N ALA B 85 4748 6019 4899 210 319 1460 N ATOM 1117 CA ALA B 85 -3.894 10.916 -30.997 1.00 40.83 C ANISOU 1117 CA ALA B 85 4696 5916 4901 191 191 1410 C ATOM 1118 C ALA B 85 -4.982 11.688 -31.735 1.00 42.12 C ANISOU 1118 C ALA B 85 4945 6111 4948 285 138 1463 C ATOM 1119 O ALA B 85 -4.728 12.749 -32.357 1.00 41.42 O ANISOU 1119 O ALA B 85 4942 5984 4814 321 203 1598 O ATOM 1120 CB ALA B 85 -3.479 11.732 -29.759 1.00 39.49 C ANISOU 1120 CB ALA B 85 4489 5637 4880 89 191 1445 C ATOM 1121 N LEU B 86 -6.215 11.165 -31.628 1.00 40.48 N ANISOU 1121 N LEU B 86 4701 5983 4697 320 14 1380 N ATOM 1122 CA LEU B 86 -7.431 11.792 -32.191 1.00 41.77 C ANISOU 1122 CA LEU B 86 4877 6236 4757 435 -74 1441 C ATOM 1123 C LEU B 86 -8.162 12.747 -31.230 1.00 41.58 C ANISOU 1123 C LEU B 86 4817 6142 4839 503 -89 1486 C ATOM 1124 O LEU B 86 -8.969 13.549 -31.651 1.00 42.54 O ANISOU 1124 O LEU B 86 4956 6304 4901 654 -124 1584 O ATOM 1125 CB LEU B 86 -8.378 10.693 -32.672 1.00 42.29 C ANISOU 1125 CB LEU B 86 4883 6473 4711 411 -212 1335 C ATOM 1126 CG LEU B 86 -7.772 9.671 -33.619 1.00 45.44 C ANISOU 1126 CG LEU B 86 5379 6910 4974 362 -195 1243 C ATOM 1127 CD1 LEU B 86 -8.706 8.386 -33.783 1.00 46.61 C ANISOU 1127 CD1 LEU B 86 5500 7159 5051 255 -353 1083 C ATOM 1128 CD2 LEU B 86 -7.396 10.271 -34.989 1.00 43.58 C ANISOU 1128 CD2 LEU B 86 5275 6748 4536 464 -142 1344 C ATOM 1129 N TYR B 87 -7.838 12.658 -29.943 1.00 40.64 N ANISOU 1129 N TYR B 87 4662 5920 4859 416 -54 1418 N ATOM 1130 CA TYR B 87 -8.453 13.438 -28.842 1.00 42.01 C ANISOU 1130 CA TYR B 87 4833 6016 5113 480 -39 1414 C ATOM 1131 C TYR B 87 -7.396 13.653 -27.772 1.00 43.04 C ANISOU 1131 C TYR B 87 5023 5986 5346 343 24 1366 C ATOM 1132 O TYR B 87 -6.436 12.911 -27.712 1.00 41.02 O ANISOU 1132 O TYR B 87 4728 5741 5118 212 29 1337 O ATOM 1133 CB TYR B 87 -9.623 12.634 -28.198 1.00 42.15 C ANISOU 1133 CB TYR B 87 4681 6198 5137 487 -110 1341 C ATOM 1134 CG TYR B 87 -10.579 12.112 -29.229 1.00 44.08 C ANISOU 1134 CG TYR B 87 4817 6654 5277 535 -220 1366 C ATOM 1135 CD1 TYR B 87 -11.611 12.903 -29.731 1.00 47.56 C ANISOU 1135 CD1 TYR B 87 5203 7208 5658 731 -262 1469 C ATOM 1136 CD2 TYR B 87 -10.450 10.852 -29.726 1.00 43.48 C ANISOU 1136 CD2 TYR B 87 4706 6663 5152 393 -292 1288 C ATOM 1137 CE1 TYR B 87 -12.463 12.418 -30.770 1.00 53.18 C ANISOU 1137 CE1 TYR B 87 5795 8167 6244 750 -408 1500 C ATOM 1138 CE2 TYR B 87 -11.330 10.355 -30.766 1.00 48.58 C ANISOU 1138 CE2 TYR B 87 5279 7513 5667 390 -429 1285 C ATOM 1139 CZ TYR B 87 -12.285 11.134 -31.258 1.00 52.42 C ANISOU 1139 CZ TYR B 87 5682 8153 6082 550 -497 1392 C ATOM 1140 OH TYR B 87 -13.138 10.658 -32.256 1.00 60.50 O ANISOU 1140 OH TYR B 87 6610 9420 6956 524 -669 1394 O ATOM 1141 N ASP B 88 -7.556 14.677 -26.950 1.00 44.10 N ANISOU 1141 N ASP B 88 5259 5974 5523 384 66 1357 N ATOM 1142 CA ASP B 88 -6.750 14.827 -25.743 1.00 42.26 C ANISOU 1142 CA ASP B 88 5079 5626 5350 230 84 1278 C ATOM 1143 C ASP B 88 -7.157 13.737 -24.705 1.00 39.96 C ANISOU 1143 C ASP B 88 4653 5475 5054 186 42 1187 C ATOM 1144 O ASP B 88 -8.335 13.346 -24.606 1.00 39.87 O ANISOU 1144 O ASP B 88 4545 5593 5012 293 31 1175 O ATOM 1145 CB ASP B 88 -7.013 16.180 -25.110 1.00 44.20 C ANISOU 1145 CB ASP B 88 5525 5663 5608 299 140 1253 C ATOM 1146 CG ASP B 88 -6.627 17.367 -26.015 1.00 49.28 C ANISOU 1146 CG ASP B 88 6356 6100 6268 328 194 1367 C ATOM 1147 OD1 ASP B 88 -5.899 17.242 -27.012 1.00 47.39 O ANISOU 1147 OD1 ASP B 88 6089 5887 6029 246 200 1472 O ATOM 1148 OD2 ASP B 88 -7.108 18.441 -25.721 1.00 52.27 O ANISOU 1148 OD2 ASP B 88 6928 6279 6651 453 248 1361 O ATOM 1149 N TYR B 89 -6.194 13.304 -23.904 1.00 39.29 N ANISOU 1149 N TYR B 89 4552 5378 4997 23 17 1147 N ATOM 1150 CA TYR B 89 -6.408 12.368 -22.798 1.00 38.66 C ANISOU 1150 CA TYR B 89 4388 5401 4900 -31 -16 1093 C ATOM 1151 C TYR B 89 -5.596 12.869 -21.620 1.00 40.85 C ANISOU 1151 C TYR B 89 4756 5604 5160 -158 -37 1040 C ATOM 1152 O TYR B 89 -4.363 13.201 -21.804 1.00 38.75 O ANISOU 1152 O TYR B 89 4507 5277 4939 -292 -69 1070 O ATOM 1153 CB TYR B 89 -5.970 10.979 -23.150 1.00 37.51 C ANISOU 1153 CB TYR B 89 4118 5349 4784 -91 -56 1126 C ATOM 1154 CG TYR B 89 -6.000 10.089 -21.947 1.00 37.74 C ANISOU 1154 CG TYR B 89 4097 5443 4799 -158 -87 1110 C ATOM 1155 CD1 TYR B 89 -7.176 9.808 -21.288 1.00 36.52 C ANISOU 1155 CD1 TYR B 89 3911 5366 4598 -124 -67 1090 C ATOM 1156 CD2 TYR B 89 -4.854 9.606 -21.422 1.00 36.96 C ANISOU 1156 CD2 TYR B 89 3970 5349 4723 -248 -131 1142 C ATOM 1157 CE1 TYR B 89 -7.196 8.964 -20.150 1.00 36.78 C ANISOU 1157 CE1 TYR B 89 3916 5462 4598 -196 -80 1108 C ATOM 1158 CE2 TYR B 89 -4.831 8.875 -20.301 1.00 37.47 C ANISOU 1158 CE2 TYR B 89 4011 5471 4753 -295 -166 1159 C ATOM 1159 CZ TYR B 89 -5.989 8.540 -19.649 1.00 38.96 C ANISOU 1159 CZ TYR B 89 4202 5717 4883 -276 -136 1144 C ATOM 1160 OH TYR B 89 -5.976 7.737 -18.513 1.00 37.98 O ANISOU 1160 OH TYR B 89 4070 5657 4706 -329 -157 1194 O ATOM 1161 N VAL B 90 -6.260 13.003 -20.480 1.00 39.51 N ANISOU 1161 N VAL B 90 4641 5458 4914 -127 -18 967 N ATOM 1162 CA VAL B 90 -5.633 13.431 -19.221 1.00 40.81 C ANISOU 1162 CA VAL B 90 4923 5579 5002 -253 -57 887 C ATOM 1163 C VAL B 90 -5.468 12.245 -18.320 1.00 40.75 C ANISOU 1163 C VAL B 90 4805 5737 4941 -322 -113 915 C ATOM 1164 O VAL B 90 -6.429 11.677 -17.856 1.00 37.88 O ANISOU 1164 O VAL B 90 4395 5476 4522 -242 -61 920 O ATOM 1165 CB VAL B 90 -6.348 14.609 -18.520 1.00 43.39 C ANISOU 1165 CB VAL B 90 5470 5782 5234 -157 23 766 C ATOM 1166 CG1 VAL B 90 -5.554 15.111 -17.270 1.00 46.24 C ANISOU 1166 CG1 VAL B 90 6008 6082 5479 -336 -46 647 C ATOM 1167 CG2 VAL B 90 -6.544 15.875 -19.521 1.00 43.14 C ANISOU 1167 CG2 VAL B 90 5593 5526 5274 -48 90 773 C ATOM 1168 N SER B 91 -4.219 11.893 -18.003 1.00 39.14 N ANISOU 1168 N SER B 91 4551 5573 4750 -474 -219 956 N ATOM 1169 CA SER B 91 -3.924 10.837 -17.075 1.00 38.96 C ANISOU 1169 CA SER B 91 4446 5693 4663 -523 -287 1013 C ATOM 1170 C SER B 91 -4.107 11.261 -15.632 1.00 42.20 C ANISOU 1170 C SER B 91 4999 6151 4884 -578 -313 926 C ATOM 1171 O SER B 91 -3.778 12.381 -15.259 1.00 41.49 O ANISOU 1171 O SER B 91 5070 5972 4723 -664 -344 808 O ATOM 1172 CB SER B 91 -2.462 10.381 -17.189 1.00 41.23 C ANISOU 1172 CB SER B 91 4603 6045 5019 -629 -402 1111 C ATOM 1173 OG SER B 91 -2.089 9.551 -16.078 1.00 41.74 O ANISOU 1173 OG SER B 91 4620 6249 4991 -666 -493 1182 O ATOM 1174 N TRP B 92 -4.595 10.342 -14.770 1.00 42.14 N ANISOU 1174 N TRP B 92 4960 6277 4774 -546 -299 983 N ATOM 1175 CA TRP B 92 -4.724 10.656 -13.340 1.00 42.98 C ANISOU 1175 CA TRP B 92 5215 6469 4647 -593 -317 909 C ATOM 1176 C TRP B 92 -3.714 9.867 -12.513 1.00 45.24 C ANISOU 1176 C TRP B 92 5438 6905 4844 -705 -478 1024 C ATOM 1177 O TRP B 92 -3.836 9.820 -11.260 1.00 48.27 O ANISOU 1177 O TRP B 92 5933 7413 4994 -740 -505 1006 O ATOM 1178 CB TRP B 92 -6.142 10.347 -12.791 1.00 42.06 C ANISOU 1178 CB TRP B 92 5124 6436 4420 -465 -151 909 C ATOM 1179 CG TRP B 92 -7.276 11.234 -13.317 1.00 40.48 C ANISOU 1179 CG TRP B 92 4976 6149 4257 -306 13 803 C ATOM 1180 CD1 TRP B 92 -7.215 12.170 -14.312 1.00 39.76 C ANISOU 1180 CD1 TRP B 92 4931 5885 4293 -253 26 732 C ATOM 1181 CD2 TRP B 92 -8.646 11.145 -12.930 1.00 42.59 C ANISOU 1181 CD2 TRP B 92 5212 6529 4444 -161 191 806 C ATOM 1182 NE1 TRP B 92 -8.441 12.744 -14.501 1.00 40.25 N ANISOU 1182 NE1 TRP B 92 5016 5932 4345 -55 187 682 N ATOM 1183 CE2 TRP B 92 -9.348 12.130 -13.655 1.00 40.54 C ANISOU 1183 CE2 TRP B 92 4981 6162 4258 8 296 722 C ATOM 1184 CE3 TRP B 92 -9.334 10.343 -12.001 1.00 39.86 C ANISOU 1184 CE3 TRP B 92 4806 6378 3960 -156 283 893 C ATOM 1185 CZ2 TRP B 92 -10.688 12.326 -13.522 1.00 44.81 C ANISOU 1185 CZ2 TRP B 92 5454 6812 4758 202 479 722 C ATOM 1186 CZ3 TRP B 92 -10.703 10.569 -11.844 1.00 41.39 C ANISOU 1186 CZ3 TRP B 92 4933 6687 4107 8 487 886 C ATOM 1187 CH2 TRP B 92 -11.372 11.569 -12.614 1.00 41.85 C ANISOU 1187 CH2 TRP B 92 4984 6659 4256 200 581 797 C ATOM 1188 N SER B 93 -2.768 9.228 -13.200 1.00 45.13 N ANISOU 1188 N SER B 93 5250 6901 4998 -729 -569 1153 N ATOM 1189 CA SER B 93 -1.842 8.266 -12.612 1.00 47.13 C ANISOU 1189 CA SER B 93 5388 7303 5216 -759 -709 1321 C ATOM 1190 C SER B 93 -0.448 8.325 -13.256 1.00 47.31 C ANISOU 1190 C SER B 93 5232 7357 5388 -818 -833 1393 C ATOM 1191 O SER B 93 -0.375 8.416 -14.495 1.00 44.49 O ANISOU 1191 O SER B 93 4797 6886 5222 -767 -751 1387 O ATOM 1192 CB SER B 93 -2.408 6.819 -12.791 1.00 46.83 C ANISOU 1192 CB SER B 93 5282 7254 5259 -629 -622 1487 C ATOM 1193 OG SER B 93 -1.440 5.791 -12.401 1.00 45.92 O ANISOU 1193 OG SER B 93 5060 7235 5153 -596 -743 1689 O ATOM 1194 N PRO B 94 0.623 8.084 -12.463 1.00 49.38 N ANISOU 1194 N PRO B 94 5394 7808 5560 -898 -1021 1498 N ATOM 1195 CA PRO B 94 1.943 8.000 -13.114 1.00 49.79 C ANISOU 1195 CA PRO B 94 5198 7944 5777 -925 -1116 1610 C ATOM 1196 C PRO B 94 2.007 6.824 -14.059 1.00 49.23 C ANISOU 1196 C PRO B 94 4991 7809 5905 -701 -999 1761 C ATOM 1197 O PRO B 94 2.944 6.752 -14.874 1.00 47.67 O ANISOU 1197 O PRO B 94 4591 7655 5866 -664 -999 1840 O ATOM 1198 CB PRO B 94 2.950 7.826 -11.969 1.00 54.45 C ANISOU 1198 CB PRO B 94 5675 8802 6210 -1024 -1357 1726 C ATOM 1199 CG PRO B 94 2.173 7.983 -10.701 1.00 55.78 C ANISOU 1199 CG PRO B 94 6091 9009 6094 -1080 -1393 1638 C ATOM 1200 CD PRO B 94 0.698 7.934 -11.011 1.00 50.97 C ANISOU 1200 CD PRO B 94 5682 8187 5498 -963 -1153 1530 C ATOM 1201 N ASP B 95 1.064 5.874 -13.940 1.00 45.00 N ANISOU 1201 N ASP B 95 4567 7174 5356 -561 -894 1805 N ATOM 1202 CA ASP B 95 1.111 4.659 -14.757 1.00 45.97 C ANISOU 1202 CA ASP B 95 4628 7189 5649 -364 -793 1927 C ATOM 1203 C ASP B 95 0.485 4.901 -16.123 1.00 42.84 C ANISOU 1203 C ASP B 95 4280 6612 5387 -330 -635 1797 C ATOM 1204 O ASP B 95 0.677 4.100 -17.081 1.00 43.41 O ANISOU 1204 O ASP B 95 4314 6583 5597 -184 -546 1845 O ATOM 1205 CB ASP B 95 0.379 3.444 -14.045 1.00 45.50 C ANISOU 1205 CB ASP B 95 4695 7067 5525 -275 -758 2050 C ATOM 1206 CG ASP B 95 1.105 2.952 -12.831 1.00 52.11 C ANISOU 1206 CG ASP B 95 5483 8085 6232 -247 -912 2244 C ATOM 1207 OD1 ASP B 95 2.349 3.047 -12.757 1.00 56.33 O ANISOU 1207 OD1 ASP B 95 5823 8788 6793 -214 -1046 2344 O ATOM 1208 OD2 ASP B 95 0.485 2.625 -11.857 1.00 55.91 O ANISOU 1208 OD2 ASP B 95 6095 8596 6552 -279 -921 2303 O ATOM 1209 N ASP B 96 -0.305 5.968 -16.261 1.00 43.26 N ANISOU 1209 N ASP B 96 4437 6613 5385 -440 -591 1630 N ATOM 1210 CA ASP B 96 -1.029 6.250 -17.497 1.00 40.94 C ANISOU 1210 CA ASP B 96 4194 6179 5182 -400 -463 1526 C ATOM 1211 C ASP B 96 -0.417 7.492 -18.158 1.00 41.32 C ANISOU 1211 C ASP B 96 4200 6227 5271 -480 -467 1458 C ATOM 1212 O ASP B 96 0.040 8.354 -17.444 1.00 42.20 O ANISOU 1212 O ASP B 96 4321 6403 5309 -619 -559 1424 O ATOM 1213 CB ASP B 96 -2.507 6.523 -17.231 1.00 40.83 C ANISOU 1213 CB ASP B 96 4315 6112 5087 -421 -393 1425 C ATOM 1214 CG ASP B 96 -3.247 5.307 -16.527 1.00 45.36 C ANISOU 1214 CG ASP B 96 4930 6689 5617 -395 -369 1514 C ATOM 1215 OD1 ASP B 96 -2.731 4.200 -16.687 1.00 43.75 O ANISOU 1215 OD1 ASP B 96 4693 6440 5489 -329 -383 1630 O ATOM 1216 OD2 ASP B 96 -4.274 5.494 -15.826 1.00 44.42 O ANISOU 1216 OD2 ASP B 96 4877 6610 5389 -434 -322 1479 O ATOM 1217 N LEU B 97 -0.468 7.578 -19.473 1.00 40.46 N ANISOU 1217 N LEU B 97 4076 6040 5258 -414 -369 1437 N ATOM 1218 CA LEU B 97 0.227 8.643 -20.258 1.00 40.25 C ANISOU 1218 CA LEU B 97 4002 6007 5283 -488 -345 1425 C ATOM 1219 C LEU B 97 -0.751 9.673 -20.825 1.00 40.26 C ANISOU 1219 C LEU B 97 4161 5878 5256 -502 -276 1318 C ATOM 1220 O LEU B 97 -1.616 9.337 -21.607 1.00 39.45 O ANISOU 1220 O LEU B 97 4110 5720 5159 -389 -201 1290 O ATOM 1221 CB LEU B 97 1.020 7.979 -21.365 1.00 41.35 C ANISOU 1221 CB LEU B 97 4007 6183 5522 -371 -263 1516 C ATOM 1222 CG LEU B 97 1.813 8.925 -22.360 1.00 43.44 C ANISOU 1222 CG LEU B 97 4193 6472 5842 -440 -194 1552 C ATOM 1223 CD1 LEU B 97 2.952 9.520 -21.594 1.00 46.01 C ANISOU 1223 CD1 LEU B 97 4360 6932 6191 -627 -305 1624 C ATOM 1224 CD2 LEU B 97 2.228 8.078 -23.525 1.00 46.68 C ANISOU 1224 CD2 LEU B 97 4525 6910 6300 -256 -62 1610 C ATOM 1225 N SER B 98 -0.582 10.941 -20.437 1.00 41.59 N ANISOU 1225 N SER B 98 4417 5994 5393 -642 -311 1263 N ATOM 1226 CA SER B 98 -1.403 11.999 -20.949 1.00 41.66 C ANISOU 1226 CA SER B 98 4593 5850 5385 -618 -239 1188 C ATOM 1227 C SER B 98 -0.928 12.305 -22.360 1.00 42.51 C ANISOU 1227 C SER B 98 4657 5923 5571 -599 -158 1268 C ATOM 1228 O SER B 98 0.267 12.085 -22.639 1.00 41.05 O ANISOU 1228 O SER B 98 4317 5832 5449 -678 -165 1361 O ATOM 1229 CB SER B 98 -1.230 13.246 -20.131 1.00 44.17 C ANISOU 1229 CB SER B 98 5071 6065 5649 -775 -290 1100 C ATOM 1230 OG SER B 98 -1.836 13.039 -18.910 1.00 41.46 O ANISOU 1230 OG SER B 98 4807 5758 5187 -757 -332 1013 O ATOM 1231 N PHE B 99 -1.812 12.855 -23.188 1.00 40.97 N ANISOU 1231 N PHE B 99 4584 5622 5359 -492 -80 1251 N ATOM 1232 CA PHE B 99 -1.414 13.248 -24.540 1.00 42.38 C ANISOU 1232 CA PHE B 99 4759 5774 5570 -472 4 1344 C ATOM 1233 C PHE B 99 -2.427 14.242 -25.079 1.00 41.99 C ANISOU 1233 C PHE B 99 4896 5578 5481 -371 54 1334 C ATOM 1234 O PHE B 99 -3.602 14.311 -24.633 1.00 41.47 O ANISOU 1234 O PHE B 99 4904 5485 5369 -250 40 1258 O ATOM 1235 CB PHE B 99 -1.218 12.029 -25.497 1.00 41.37 C ANISOU 1235 CB PHE B 99 4501 5779 5439 -350 55 1393 C ATOM 1236 CG PHE B 99 -2.425 11.121 -25.602 1.00 38.40 C ANISOU 1236 CG PHE B 99 4151 5432 5008 -207 34 1321 C ATOM 1237 CD1 PHE B 99 -3.467 11.373 -26.440 1.00 37.72 C ANISOU 1237 CD1 PHE B 99 4147 5330 4856 -99 53 1308 C ATOM 1238 CD2 PHE B 99 -2.439 9.922 -24.870 1.00 37.58 C ANISOU 1238 CD2 PHE B 99 3972 5388 4920 -198 -14 1288 C ATOM 1239 CE1 PHE B 99 -4.560 10.503 -26.497 1.00 38.83 C ANISOU 1239 CE1 PHE B 99 4270 5530 4953 -25 9 1245 C ATOM 1240 CE2 PHE B 99 -3.495 9.056 -24.965 1.00 39.86 C ANISOU 1240 CE2 PHE B 99 4283 5689 5173 -128 -34 1233 C ATOM 1241 CZ PHE B 99 -4.518 9.306 -25.774 1.00 38.21 C ANISOU 1241 CZ PHE B 99 4128 5485 4906 -62 -28 1204 C ATOM 1242 N GLN B 100 -1.971 15.048 -26.022 1.00 42.64 N ANISOU 1242 N GLN B 100 5043 5578 5579 -406 125 1436 N ATOM 1243 CA GLN B 100 -2.878 15.934 -26.741 1.00 45.79 C ANISOU 1243 CA GLN B 100 5617 5845 5934 -263 176 1479 C ATOM 1244 C GLN B 100 -3.160 15.424 -28.122 1.00 44.23 C ANISOU 1244 C GLN B 100 5368 5776 5663 -118 222 1566 C ATOM 1245 O GLN B 100 -2.333 14.738 -28.727 1.00 43.97 O ANISOU 1245 O GLN B 100 5215 5870 5620 -162 263 1614 O ATOM 1246 CB GLN B 100 -2.238 17.264 -27.005 1.00 50.20 C ANISOU 1246 CB GLN B 100 6342 6191 6539 -400 234 1571 C ATOM 1247 CG GLN B 100 -1.481 17.750 -25.923 1.00 58.31 C ANISOU 1247 CG GLN B 100 7413 7111 7632 -642 182 1501 C ATOM 1248 CD GLN B 100 -2.245 18.672 -25.150 1.00 65.57 C ANISOU 1248 CD GLN B 100 8587 7793 8535 -592 170 1392 C ATOM 1249 OE1 GLN B 100 -3.133 18.266 -24.399 1.00 71.53 O ANISOU 1249 OE1 GLN B 100 9338 8604 9234 -443 137 1270 O ATOM 1250 NE2 GLN B 100 -1.932 19.972 -25.311 1.00 73.81 N ANISOU 1250 NE2 GLN B 100 9878 8544 9621 -714 216 1439 N ATOM 1251 N LYS B 101 -4.319 15.779 -28.617 1.00 42.67 N ANISOU 1251 N LYS B 101 5260 5558 5395 70 215 1587 N ATOM 1252 CA LYS B 101 -4.704 15.528 -29.981 1.00 42.94 C ANISOU 1252 CA LYS B 101 5289 5713 5312 205 230 1676 C ATOM 1253 C LYS B 101 -3.561 15.917 -30.924 1.00 43.26 C ANISOU 1253 C LYS B 101 5372 5733 5331 113 339 1820 C ATOM 1254 O LYS B 101 -2.997 17.043 -30.856 1.00 43.84 O ANISOU 1254 O LYS B 101 5569 5619 5470 6 405 1922 O ATOM 1255 CB LYS B 101 -5.953 16.391 -30.293 1.00 44.34 C ANISOU 1255 CB LYS B 101 5582 5831 5434 415 207 1740 C ATOM 1256 CG LYS B 101 -6.562 16.281 -31.679 1.00 45.98 C ANISOU 1256 CG LYS B 101 5794 6193 5482 575 179 1850 C ATOM 1257 CD LYS B 101 -7.892 17.043 -31.780 1.00 49.96 C ANISOU 1257 CD LYS B 101 6347 6688 5947 820 128 1925 C ATOM 1258 CE LYS B 101 -8.300 16.922 -33.220 1.00 55.26 C ANISOU 1258 CE LYS B 101 7020 7547 6428 946 74 2054 C ATOM 1259 NZ LYS B 101 -9.488 17.576 -33.539 1.00 62.23 N ANISOU 1259 NZ LYS B 101 7910 8486 7250 1202 7 2173 N ATOM 1260 N GLY B 102 -3.267 14.988 -31.805 1.00 41.28 N ANISOU 1260 N GLY B 102 5037 5667 4980 149 368 1824 N ATOM 1261 CA GLY B 102 -2.237 15.143 -32.777 1.00 45.71 C ANISOU 1261 CA GLY B 102 5604 6281 5484 97 502 1959 C ATOM 1262 C GLY B 102 -0.848 14.664 -32.337 1.00 45.12 C ANISOU 1262 C GLY B 102 5359 6264 5520 -63 580 1955 C ATOM 1263 O GLY B 102 0.064 14.605 -33.199 1.00 45.39 O ANISOU 1263 O GLY B 102 5343 6406 5498 -84 724 2071 O ATOM 1264 N ASP B 103 -0.675 14.346 -31.070 1.00 43.79 N ANISOU 1264 N ASP B 103 5091 6061 5487 -158 495 1846 N ATOM 1265 CA ASP B 103 0.628 13.788 -30.620 1.00 44.51 C ANISOU 1265 CA ASP B 103 4974 6258 5678 -278 539 1862 C ATOM 1266 C ASP B 103 0.842 12.404 -31.238 1.00 45.81 C ANISOU 1266 C ASP B 103 5046 6595 5765 -114 601 1811 C ATOM 1267 O ASP B 103 -0.117 11.533 -31.335 1.00 42.94 O ANISOU 1267 O ASP B 103 4757 6238 5322 24 528 1677 O ATOM 1268 CB ASP B 103 0.707 13.621 -29.097 1.00 44.32 C ANISOU 1268 CB ASP B 103 4873 6192 5775 -392 406 1760 C ATOM 1269 CG ASP B 103 0.784 14.939 -28.304 1.00 48.26 C ANISOU 1269 CG ASP B 103 5480 6508 6350 -593 349 1772 C ATOM 1270 OD1 ASP B 103 0.967 16.015 -28.856 1.00 47.89 O ANISOU 1270 OD1 ASP B 103 5552 6337 6308 -682 419 1881 O ATOM 1271 OD2 ASP B 103 0.728 14.859 -27.044 1.00 48.27 O ANISOU 1271 OD2 ASP B 103 5464 6478 6399 -679 233 1668 O ATOM 1272 N GLN B 104 2.102 12.140 -31.588 1.00 46.59 N ANISOU 1272 N GLN B 104 4977 6830 5894 -136 737 1910 N ATOM 1273 CA GLN B 104 2.471 10.823 -32.073 1.00 47.58 C ANISOU 1273 CA GLN B 104 5031 7088 5959 52 827 1854 C ATOM 1274 C GLN B 104 3.127 9.997 -30.959 1.00 46.96 C ANISOU 1274 C GLN B 104 4755 7059 6030 50 769 1823 C ATOM 1275 O GLN B 104 3.929 10.499 -30.154 1.00 49.73 O ANISOU 1275 O GLN B 104 4921 7459 6514 -117 728 1917 O ATOM 1276 CB GLN B 104 3.394 10.941 -33.288 1.00 52.05 C ANISOU 1276 CB GLN B 104 5537 7810 6430 114 1058 1992 C ATOM 1277 CG GLN B 104 2.720 11.608 -34.468 1.00 51.78 C ANISOU 1277 CG GLN B 104 5725 7750 6199 153 1113 2039 C ATOM 1278 CD GLN B 104 3.615 11.710 -35.666 1.00 58.33 C ANISOU 1278 CD GLN B 104 6513 8755 6896 217 1366 2188 C ATOM 1279 OE1 GLN B 104 3.525 12.670 -36.449 1.00 55.78 O ANISOU 1279 OE1 GLN B 104 6303 8429 6462 159 1444 2340 O ATOM 1280 NE2 GLN B 104 4.435 10.686 -35.870 1.00 53.96 N ANISOU 1280 NE2 GLN B 104 5819 8354 6330 372 1514 2155 N ATOM 1281 N MET B 105 2.775 8.744 -30.911 1.00 45.58 N ANISOU 1281 N MET B 105 4633 6863 5822 221 750 1700 N ATOM 1282 CA MET B 105 3.271 7.839 -29.882 1.00 46.23 C ANISOU 1282 CA MET B 105 4572 6966 6028 268 690 1690 C ATOM 1283 C MET B 105 3.719 6.500 -30.457 1.00 47.33 C ANISOU 1283 C MET B 105 4719 7134 6129 529 828 1650 C ATOM 1284 O MET B 105 3.197 6.032 -31.449 1.00 47.71 O ANISOU 1284 O MET B 105 4972 7125 6033 652 904 1540 O ATOM 1285 CB MET B 105 2.176 7.589 -28.806 1.00 44.03 C ANISOU 1285 CB MET B 105 4406 6545 5777 198 494 1576 C ATOM 1286 CG MET B 105 1.872 8.786 -27.957 1.00 44.43 C ANISOU 1286 CG MET B 105 4450 6557 5873 -15 371 1599 C ATOM 1287 SD MET B 105 0.399 8.617 -26.931 1.00 45.11 S ANISOU 1287 SD MET B 105 4686 6513 5939 -56 206 1467 S ATOM 1288 CE MET B 105 -0.838 8.827 -28.231 1.00 43.28 C ANISOU 1288 CE MET B 105 4644 6227 5575 25 242 1393 C ATOM 1289 N VAL B 106 4.664 5.839 -29.789 1.00 48.48 N ANISOU 1289 N VAL B 106 4663 7361 6397 628 848 1732 N ATOM 1290 CA VAL B 106 5.067 4.526 -30.230 1.00 51.55 C ANISOU 1290 CA VAL B 106 5097 7725 6766 924 989 1690 C ATOM 1291 C VAL B 106 4.339 3.547 -29.326 1.00 49.76 C ANISOU 1291 C VAL B 106 5022 7297 6589 954 837 1593 C ATOM 1292 O VAL B 106 4.329 3.769 -28.113 1.00 46.92 O ANISOU 1292 O VAL B 106 4542 6957 6329 820 674 1664 O ATOM 1293 CB VAL B 106 6.626 4.274 -30.114 1.00 55.78 C ANISOU 1293 CB VAL B 106 5290 8492 7413 1094 1136 1881 C ATOM 1294 CG1 VAL B 106 6.939 2.836 -30.495 1.00 57.74 C ANISOU 1294 CG1 VAL B 106 5643 8652 7643 1465 1294 1821 C ATOM 1295 CG2 VAL B 106 7.435 5.208 -31.054 1.00 60.50 C ANISOU 1295 CG2 VAL B 106 5699 9322 7966 1043 1327 2012 C ATOM 1296 N VAL B 107 3.776 2.477 -29.896 1.00 50.45 N ANISOU 1296 N VAL B 107 5382 7193 6593 1109 892 1438 N ATOM 1297 CA VAL B 107 3.030 1.480 -29.115 1.00 50.24 C ANISOU 1297 CA VAL B 107 5532 6941 6617 1104 765 1358 C ATOM 1298 C VAL B 107 3.980 0.353 -28.682 1.00 52.72 C ANISOU 1298 C VAL B 107 5789 7201 7040 1382 854 1451 C ATOM 1299 O VAL B 107 4.590 -0.313 -29.510 1.00 56.36 O ANISOU 1299 O VAL B 107 6325 7627 7463 1654 1052 1415 O ATOM 1300 CB VAL B 107 1.813 0.872 -29.904 1.00 51.00 C ANISOU 1300 CB VAL B 107 5981 6822 6575 1062 742 1133 C ATOM 1301 CG1 VAL B 107 1.039 -0.223 -29.069 1.00 47.58 C ANISOU 1301 CG1 VAL B 107 5730 6136 6213 1006 621 1074 C ATOM 1302 CG2 VAL B 107 0.808 1.996 -30.271 1.00 50.50 C ANISOU 1302 CG2 VAL B 107 5937 6845 6407 824 631 1079 C ATOM 1303 N LEU B 108 4.101 0.148 -27.383 1.00 51.86 N ANISOU 1303 N LEU B 108 5562 7093 7050 1340 716 1577 N ATOM 1304 CA LEU B 108 5.032 -0.848 -26.818 1.00 55.88 C ANISOU 1304 CA LEU B 108 5982 7579 7671 1625 771 1724 C ATOM 1305 C LEU B 108 4.313 -2.169 -26.498 1.00 58.26 C ANISOU 1305 C LEU B 108 6624 7522 7992 1704 743 1647 C ATOM 1306 O LEU B 108 4.907 -3.244 -26.569 1.00 59.69 O ANISOU 1306 O LEU B 108 6897 7551 8231 2020 864 1695 O ATOM 1307 CB LEU B 108 5.615 -0.258 -25.552 1.00 55.16 C ANISOU 1307 CB LEU B 108 5562 7728 7668 1513 608 1934 C ATOM 1308 CG LEU B 108 6.281 1.128 -25.780 1.00 58.23 C ANISOU 1308 CG LEU B 108 5635 8439 8052 1344 606 2008 C ATOM 1309 CD1 LEU B 108 6.764 1.687 -24.429 1.00 60.14 C ANISOU 1309 CD1 LEU B 108 5601 8895 8353 1173 396 2176 C ATOM 1310 CD2 LEU B 108 7.408 1.003 -26.801 1.00 62.82 C ANISOU 1310 CD2 LEU B 108 6033 9184 8651 1606 847 2081 C ATOM 1311 N GLU B 109 3.031 -2.095 -26.129 1.00 56.30 N ANISOU 1311 N GLU B 109 6561 7131 7701 1419 594 1541 N ATOM 1312 CA GLU B 109 2.288 -3.314 -25.815 1.00 60.65 C ANISOU 1312 CA GLU B 109 7431 7338 8277 1418 564 1483 C ATOM 1313 C GLU B 109 0.829 -3.094 -26.094 1.00 58.10 C ANISOU 1313 C GLU B 109 7296 6915 7866 1096 462 1300 C ATOM 1314 O GLU B 109 0.321 -1.990 -25.891 1.00 52.66 O ANISOU 1314 O GLU B 109 6446 6433 7131 874 361 1296 O ATOM 1315 CB GLU B 109 2.573 -3.780 -24.364 1.00 61.51 C ANISOU 1315 CB GLU B 109 7451 7433 8487 1460 461 1712 C ATOM 1316 CG GLU B 109 1.585 -4.791 -23.750 1.00 69.67 C ANISOU 1316 CG GLU B 109 8786 8139 9545 1335 394 1704 C ATOM 1317 CD GLU B 109 1.575 -4.714 -22.203 1.00 75.06 C ANISOU 1317 CD GLU B 109 9327 8936 10255 1246 249 1936 C ATOM 1318 OE1 GLU B 109 0.497 -4.495 -21.602 1.00 77.35 O ANISOU 1318 OE1 GLU B 109 9673 9220 10498 951 146 1913 O ATOM 1319 OE2 GLU B 109 2.667 -4.850 -21.605 1.00 82.17 O ANISOU 1319 OE2 GLU B 109 10042 9971 11209 1482 242 2148 O ATOM 1320 N GLU B 110 0.205 -4.154 -26.608 1.00 61.23 N ANISOU 1320 N GLU B 110 8035 6992 8239 1086 495 1148 N ATOM 1321 CA GLU B 110 -1.184 -4.148 -27.030 1.00 63.45 C ANISOU 1321 CA GLU B 110 8493 7181 8433 778 392 966 C ATOM 1322 C GLU B 110 -1.869 -5.365 -26.464 1.00 66.23 C ANISOU 1322 C GLU B 110 9111 7197 8857 656 343 964 C ATOM 1323 O GLU B 110 -2.435 -6.102 -27.209 1.00 69.84 O ANISOU 1323 O GLU B 110 9868 7406 9262 567 349 776 O ATOM 1324 CB GLU B 110 -1.298 -4.258 -28.554 1.00 65.15 C ANISOU 1324 CB GLU B 110 8917 7337 8501 825 473 729 C ATOM 1325 CG GLU B 110 -0.999 -3.041 -29.255 1.00 64.85 C ANISOU 1325 CG GLU B 110 8672 7610 8358 852 506 720 C ATOM 1326 CD GLU B 110 -1.371 -3.031 -30.751 1.00 70.49 C ANISOU 1326 CD GLU B 110 9601 8316 8866 840 547 491 C ATOM 1327 OE1 GLU B 110 -0.944 -2.041 -31.423 1.00 70.40 O ANISOU 1327 OE1 GLU B 110 9436 8559 8755 910 615 518 O ATOM 1328 OE2 GLU B 110 -2.079 -3.951 -31.243 1.00 72.15 O ANISOU 1328 OE2 GLU B 110 10135 8280 9000 736 503 296 O ATOM 1329 N SER B 111 -1.866 -5.594 -25.165 1.00 67.85 N ANISOU 1329 N SER B 111 9233 7384 9163 620 287 1170 N ATOM 1330 CA SER B 111 -2.627 -6.760 -24.679 1.00 71.40 C ANISOU 1330 CA SER B 111 9961 7491 9675 454 252 1187 C ATOM 1331 C SER B 111 -4.136 -6.491 -24.832 1.00 69.24 C ANISOU 1331 C SER B 111 9694 7275 9340 38 126 1062 C ATOM 1332 O SER B 111 -4.797 -7.052 -25.730 1.00 73.04 O ANISOU 1332 O SER B 111 10422 7556 9773 -123 104 855 O ATOM 1333 CB SER B 111 -2.266 -7.135 -23.247 1.00 72.42 C ANISOU 1333 CB SER B 111 10024 7593 9901 526 233 1471 C ATOM 1334 OG SER B 111 -0.886 -7.357 -23.181 1.00 77.21 O ANISOU 1334 OG SER B 111 10574 8199 10562 924 329 1598 O ATOM 1335 N GLY B 112 -4.693 -5.681 -23.970 1.00 64.58 N ANISOU 1335 N GLY B 112 8839 6958 8740 -134 42 1180 N ATOM 1336 CA GLY B 112 -6.135 -5.457 -24.013 1.00 61.70 C ANISOU 1336 CA GLY B 112 8423 6688 8332 -492 -60 1105 C ATOM 1337 C GLY B 112 -6.346 -4.114 -24.689 1.00 56.89 C ANISOU 1337 C GLY B 112 7582 6415 7620 -489 -103 1000 C ATOM 1338 O GLY B 112 -5.585 -3.751 -25.590 1.00 57.17 O ANISOU 1338 O GLY B 112 7634 6486 7601 -289 -51 906 O ATOM 1339 N GLU B 113 -7.333 -3.360 -24.195 1.00 51.88 N ANISOU 1339 N GLU B 113 6729 6027 6956 -682 -174 1044 N ATOM 1340 CA GLU B 113 -7.771 -2.114 -24.779 1.00 50.65 C ANISOU 1340 CA GLU B 113 6377 6159 6710 -690 -221 968 C ATOM 1341 C GLU B 113 -7.016 -0.897 -24.266 1.00 45.28 C ANISOU 1341 C GLU B 113 5505 5681 6017 -504 -180 1061 C ATOM 1342 O GLU B 113 -7.153 0.154 -24.844 1.00 43.39 O ANISOU 1342 O GLU B 113 5156 5619 5712 -463 -196 1008 O ATOM 1343 CB GLU B 113 -9.272 -1.871 -24.568 1.00 51.76 C ANISOU 1343 CB GLU B 113 6361 6476 6828 -952 -307 971 C ATOM 1344 CG GLU B 113 -10.160 -3.077 -24.666 1.00 63.47 C ANISOU 1344 CG GLU B 113 7977 7787 8349 -1241 -366 933 C ATOM 1345 CD GLU B 113 -10.493 -3.482 -26.034 1.00 73.84 C ANISOU 1345 CD GLU B 113 9444 9022 9589 -1348 -456 730 C ATOM 1346 OE1 GLU B 113 -11.686 -3.859 -26.258 1.00 80.56 O ANISOU 1346 OE1 GLU B 113 10247 9934 10430 -1661 -570 684 O ATOM 1347 OE2 GLU B 113 -9.579 -3.447 -26.885 1.00 77.97 O ANISOU 1347 OE2 GLU B 113 10130 9444 10051 -1136 -414 618 O ATOM 1348 N TRP B 114 -6.264 -1.066 -23.169 1.00 43.00 N ANISOU 1348 N TRP B 114 5196 5360 5783 -414 -141 1206 N ATOM 1349 CA TRP B 114 -5.358 -0.043 -22.676 1.00 41.34 C ANISOU 1349 CA TRP B 114 4835 5315 5558 -271 -124 1281 C ATOM 1350 C TRP B 114 -3.930 -0.500 -23.119 1.00 43.05 C ANISOU 1350 C TRP B 114 5108 5425 5822 -49 -62 1307 C ATOM 1351 O TRP B 114 -3.479 -1.535 -22.729 1.00 43.02 O ANISOU 1351 O TRP B 114 5211 5256 5879 31 -37 1389 O ATOM 1352 CB TRP B 114 -5.472 0.102 -21.177 1.00 40.61 C ANISOU 1352 CB TRP B 114 4663 5312 5453 -326 -145 1422 C ATOM 1353 CG TRP B 114 -6.723 0.894 -20.815 1.00 40.22 C ANISOU 1353 CG TRP B 114 4508 5435 5339 -470 -161 1390 C ATOM 1354 CD1 TRP B 114 -7.990 0.383 -20.710 1.00 41.57 C ANISOU 1354 CD1 TRP B 114 4677 5608 5511 -645 -164 1390 C ATOM 1355 CD2 TRP B 114 -6.808 2.285 -20.515 1.00 36.58 C ANISOU 1355 CD2 TRP B 114 3929 5159 4810 -437 -162 1363 C ATOM 1356 NE1 TRP B 114 -8.872 1.425 -20.412 1.00 42.59 N ANISOU 1356 NE1 TRP B 114 4653 5956 5574 -679 -154 1370 N ATOM 1357 CE2 TRP B 114 -8.145 2.569 -20.232 1.00 38.60 C ANISOU 1357 CE2 TRP B 114 4111 5533 5024 -539 -147 1349 C ATOM 1358 CE3 TRP B 114 -5.846 3.322 -20.429 1.00 38.21 C ANISOU 1358 CE3 TRP B 114 4092 5434 4993 -340 -171 1354 C ATOM 1359 CZ2 TRP B 114 -8.584 3.813 -19.888 1.00 37.04 C ANISOU 1359 CZ2 TRP B 114 3828 5490 4757 -494 -122 1317 C ATOM 1360 CZ3 TRP B 114 -6.285 4.576 -20.046 1.00 36.88 C ANISOU 1360 CZ3 TRP B 114 3874 5385 4755 -348 -163 1311 C ATOM 1361 CH2 TRP B 114 -7.669 4.818 -19.853 1.00 36.33 C ANISOU 1361 CH2 TRP B 114 3761 5402 4642 -395 -130 1284 C ATOM 1362 N TRP B 115 -3.301 0.288 -23.974 1.00 42.57 N ANISOU 1362 N TRP B 115 4975 5468 5732 55 -24 1251 N ATOM 1363 CA TRP B 115 -2.001 -0.102 -24.622 1.00 44.92 C ANISOU 1363 CA TRP B 115 5290 5714 6063 283 74 1269 C ATOM 1364 C TRP B 115 -0.909 0.618 -23.909 1.00 44.90 C ANISOU 1364 C TRP B 115 5067 5896 6097 358 65 1413 C ATOM 1365 O TRP B 115 -1.135 1.767 -23.465 1.00 44.08 O ANISOU 1365 O TRP B 115 4841 5951 5957 227 0 1424 O ATOM 1366 CB TRP B 115 -2.001 0.318 -26.109 1.00 44.70 C ANISOU 1366 CB TRP B 115 5314 5720 5952 329 140 1131 C ATOM 1367 CG TRP B 115 -2.953 -0.387 -26.996 1.00 45.93 C ANISOU 1367 CG TRP B 115 5694 5723 6034 248 125 963 C ATOM 1368 CD1 TRP B 115 -3.645 -1.500 -26.677 1.00 49.11 C ANISOU 1368 CD1 TRP B 115 6273 5916 6472 141 80 921 C ATOM 1369 CD2 TRP B 115 -3.243 -0.132 -28.387 1.00 47.51 C ANISOU 1369 CD2 TRP B 115 5994 5961 6098 253 148 815 C ATOM 1370 NE1 TRP B 115 -4.406 -1.918 -27.716 1.00 44.13 N ANISOU 1370 NE1 TRP B 115 5830 5193 5745 38 49 741 N ATOM 1371 CE2 TRP B 115 -4.198 -1.100 -28.787 1.00 49.47 C ANISOU 1371 CE2 TRP B 115 6466 6033 6298 114 81 667 C ATOM 1372 CE3 TRP B 115 -2.901 0.876 -29.287 1.00 48.65 C ANISOU 1372 CE3 TRP B 115 6063 6281 6141 321 200 806 C ATOM 1373 CZ2 TRP B 115 -4.734 -1.154 -30.084 1.00 50.48 C ANISOU 1373 CZ2 TRP B 115 6749 6172 6258 62 50 491 C ATOM 1374 CZ3 TRP B 115 -3.447 0.850 -30.575 1.00 47.33 C ANISOU 1374 CZ3 TRP B 115 6052 6130 5802 298 190 658 C ATOM 1375 CH2 TRP B 115 -4.336 -0.153 -30.976 1.00 51.26 C ANISOU 1375 CH2 TRP B 115 6772 6474 6231 175 105 493 C ATOM 1376 N LYS B 116 0.280 0.009 -23.807 1.00 46.92 N ANISOU 1376 N LYS B 116 5266 6140 6420 568 125 1524 N ATOM 1377 CA LYS B 116 1.411 0.742 -23.296 1.00 48.81 C ANISOU 1377 CA LYS B 116 5245 6611 6691 613 98 1663 C ATOM 1378 C LYS B 116 2.014 1.480 -24.470 1.00 48.72 C ANISOU 1378 C LYS B 116 5133 6715 6662 665 207 1616 C ATOM 1379 O LYS B 116 2.160 0.892 -25.532 1.00 48.61 O ANISOU 1379 O LYS B 116 5234 6603 6633 827 341 1542 O ATOM 1380 CB LYS B 116 2.478 -0.131 -22.631 1.00 52.61 C ANISOU 1380 CB LYS B 116 5628 7108 7251 830 101 1848 C ATOM 1381 CG LYS B 116 3.476 0.659 -21.758 1.00 58.38 C ANISOU 1381 CG LYS B 116 6052 8135 7994 787 -7 2010 C ATOM 1382 CD LYS B 116 4.244 -0.282 -20.758 1.00 66.69 C ANISOU 1382 CD LYS B 116 7016 9226 9096 981 -73 2231 C ATOM 1383 CE LYS B 116 5.759 -0.029 -20.680 1.00 73.94 C ANISOU 1383 CE LYS B 116 7574 10443 10077 1129 -87 2412 C ATOM 1384 NZ LYS B 116 6.598 -1.190 -20.082 1.00 78.26 N ANISOU 1384 NZ LYS B 116 8032 11010 10694 1453 -100 2651 N ATOM 1385 N ALA B 117 2.321 2.764 -24.248 1.00 46.53 N ANISOU 1385 N ALA B 117 4678 6629 6373 514 152 1655 N ATOM 1386 CA ALA B 117 2.892 3.646 -25.263 1.00 48.06 C ANISOU 1386 CA ALA B 117 4767 6944 6550 507 253 1652 C ATOM 1387 C ALA B 117 3.976 4.570 -24.724 1.00 48.68 C ANISOU 1387 C ALA B 117 4565 7248 6684 399 202 1793 C ATOM 1388 O ALA B 117 4.065 4.842 -23.501 1.00 48.25 O ANISOU 1388 O ALA B 117 4429 7262 6641 266 43 1848 O ATOM 1389 CB ALA B 117 1.775 4.521 -25.859 1.00 44.75 C ANISOU 1389 CB ALA B 117 4502 6461 6040 352 239 1522 C ATOM 1390 N ARG B 118 4.765 5.113 -25.664 1.00 49.98 N ANISOU 1390 N ARG B 118 4592 7539 6859 422 333 1847 N ATOM 1391 CA ARG B 118 5.751 6.110 -25.345 1.00 50.50 C ANISOU 1391 CA ARG B 118 4389 7817 6981 247 291 1977 C ATOM 1392 C ARG B 118 5.507 7.375 -26.170 1.00 49.79 C ANISOU 1392 C ARG B 118 4370 7702 6845 64 356 1943 C ATOM 1393 O ARG B 118 5.235 7.312 -27.379 1.00 48.65 O ANISOU 1393 O ARG B 118 4347 7506 6632 177 516 1899 O ATOM 1394 CB ARG B 118 7.231 5.539 -25.597 1.00 53.84 C ANISOU 1394 CB ARG B 118 4482 8480 7494 447 408 2161 C ATOM 1395 CG ARG B 118 8.223 6.587 -25.528 1.00 55.78 C ANISOU 1395 CG ARG B 118 4425 8970 7800 225 387 2301 C ATOM 1396 CD ARG B 118 9.756 5.984 -25.479 1.00 69.51 C ANISOU 1396 CD ARG B 118 5723 11040 9649 422 463 2531 C ATOM 1397 NE ARG B 118 10.024 5.196 -26.673 1.00 69.86 N ANISOU 1397 NE ARG B 118 5786 11081 9678 775 749 2538 N ATOM 1398 CZ ARG B 118 10.306 3.894 -26.670 1.00 71.41 C ANISOU 1398 CZ ARG B 118 5974 11254 9902 1162 842 2571 C ATOM 1399 NH1 ARG B 118 10.394 3.212 -25.538 1.00 74.63 N ANISOU 1399 NH1 ARG B 118 6328 11660 10368 1251 666 2640 N ATOM 1400 NH2 ARG B 118 10.521 3.270 -27.823 1.00 73.09 N ANISOU 1400 NH2 ARG B 118 6261 11437 10071 1478 1124 2539 N ATOM 1401 N SER B 119 5.583 8.527 -25.519 1.00 50.17 N ANISOU 1401 N SER B 119 4379 7771 6912 -218 230 1960 N ATOM 1402 CA SER B 119 5.407 9.798 -26.204 1.00 51.85 C ANISOU 1402 CA SER B 119 4686 7917 7098 -399 288 1958 C ATOM 1403 C SER B 119 6.721 10.150 -26.910 1.00 55.12 C ANISOU 1403 C SER B 119 4827 8540 7577 -455 429 2137 C ATOM 1404 O SER B 119 7.796 10.168 -26.316 1.00 56.12 O ANISOU 1404 O SER B 119 4652 8875 7794 -562 367 2261 O ATOM 1405 CB SER B 119 5.000 10.937 -25.241 1.00 50.83 C ANISOU 1405 CB SER B 119 4675 7672 6966 -680 119 1894 C ATOM 1406 OG SER B 119 5.171 12.206 -25.839 1.00 55.93 O ANISOU 1406 OG SER B 119 5383 8246 7623 -875 181 1942 O ATOM 1407 N LEU B 120 6.600 10.413 -28.200 1.00 57.29 N ANISOU 1407 N LEU B 120 5194 8787 7786 -381 619 2163 N ATOM 1408 CA LEU B 120 7.713 10.992 -28.978 1.00 61.77 C ANISOU 1408 CA LEU B 120 5534 9544 8391 -480 791 2352 C ATOM 1409 C LEU B 120 8.075 12.403 -28.529 1.00 65.71 C ANISOU 1409 C LEU B 120 5991 10009 8968 -883 692 2434 C ATOM 1410 O LEU B 120 9.197 12.900 -28.789 1.00 66.70 O ANISOU 1410 O LEU B 120 5839 10332 9173 -1070 778 2621 O ATOM 1411 CB LEU B 120 7.367 11.000 -30.458 1.00 61.70 C ANISOU 1411 CB LEU B 120 5699 9501 8244 -312 1016 2359 C ATOM 1412 CG LEU B 120 7.593 9.705 -31.255 1.00 65.61 C ANISOU 1412 CG LEU B 120 6166 10110 8655 55 1206 2331 C ATOM 1413 CD1 LEU B 120 6.824 8.566 -30.859 1.00 71.35 C ANISOU 1413 CD1 LEU B 120 7063 10697 9350 268 1108 2149 C ATOM 1414 CD2 LEU B 120 7.226 9.931 -32.693 1.00 71.19 C ANISOU 1414 CD2 LEU B 120 7081 10795 9172 159 1402 2330 C ATOM 1415 N ALA B 121 7.138 13.088 -27.877 1.00 67.18 N ANISOU 1415 N ALA B 121 6457 9938 9130 -1030 526 2298 N ATOM 1416 CA ALA B 121 7.406 14.467 -27.428 1.00 70.05 C ANISOU 1416 CA ALA B 121 6873 10186 9556 -1417 432 2336 C ATOM 1417 C ALA B 121 8.245 14.469 -26.195 1.00 72.11 C ANISOU 1417 C ALA B 121 6888 10606 9905 -1654 234 2350 C ATOM 1418 O ALA B 121 9.394 15.031 -26.203 1.00 77.57 O ANISOU 1418 O ALA B 121 7309 11471 10693 -1948 233 2510 O ATOM 1419 CB ALA B 121 6.119 15.199 -27.157 1.00 70.11 C ANISOU 1419 CB ALA B 121 7288 9855 9497 -1438 349 2178 C ATOM 1420 N THR B 122 7.704 13.852 -25.145 1.00 71.04 N ANISOU 1420 N THR B 122 6824 10441 9726 -1550 62 2203 N ATOM 1421 CA THR B 122 8.257 13.904 -23.798 1.00 71.54 C ANISOU 1421 CA THR B 122 6740 10629 9811 -1771 -179 2180 C ATOM 1422 C THR B 122 9.040 12.653 -23.412 1.00 70.15 C ANISOU 1422 C THR B 122 6198 10783 9671 -1578 -224 2291 C ATOM 1423 O THR B 122 9.714 12.669 -22.394 1.00 70.95 O ANISOU 1423 O THR B 122 6099 11074 9785 -1762 -432 2329 O ATOM 1424 CB THR B 122 7.145 14.107 -22.723 1.00 70.91 C ANISOU 1424 CB THR B 122 7003 10316 9623 -1786 -344 1959 C ATOM 1425 OG1 THR B 122 6.268 12.971 -22.669 1.00 72.05 O ANISOU 1425 OG1 THR B 122 7235 10436 9703 -1432 -306 1888 O ATOM 1426 CG2 THR B 122 6.308 15.343 -23.036 1.00 72.27 C ANISOU 1426 CG2 THR B 122 7557 10140 9763 -1909 -291 1850 C ATOM 1427 N ARG B 123 8.987 11.588 -24.222 1.00 66.66 N ANISOU 1427 N ARG B 123 5683 10409 9236 -1205 -37 2347 N ATOM 1428 CA ARG B 123 9.651 10.332 -23.888 1.00 66.24 C ANISOU 1428 CA ARG B 123 5340 10607 9222 -946 -52 2455 C ATOM 1429 C ARG B 123 9.062 9.614 -22.699 1.00 64.37 C ANISOU 1429 C ARG B 123 5232 10308 8919 -843 -243 2361 C ATOM 1430 O ARG B 123 9.574 8.606 -22.333 1.00 63.06 O ANISOU 1430 O ARG B 123 4863 10314 8783 -625 -273 2468 O ATOM 1431 CB ARG B 123 11.093 10.574 -23.540 1.00 71.24 C ANISOU 1431 CB ARG B 123 5509 11603 9955 -1139 -135 2659 C ATOM 1432 CG ARG B 123 11.774 11.240 -24.633 1.00 73.33 C ANISOU 1432 CG ARG B 123 5596 11975 10292 -1266 68 2794 C ATOM 1433 CD ARG B 123 11.664 10.397 -25.854 1.00 74.72 C ANISOU 1433 CD ARG B 123 5795 12148 10448 -852 371 2826 C ATOM 1434 NE ARG B 123 12.352 9.027 -25.728 1.00 79.00 N ANISOU 1434 NE ARG B 123 6040 12939 11039 -454 432 2943 N ATOM 1435 CZ ARG B 123 12.425 8.266 -26.805 1.00 84.56 C ANISOU 1435 CZ ARG B 123 6758 13653 11718 -81 718 2966 C ATOM 1436 NH1 ARG B 123 11.826 8.743 -28.030 1.00 84.09 N ANISOU 1436 NH1 ARG B 123 6983 13407 11560 -86 932 2881 N ATOM 1437 NH2 ARG B 123 12.916 7.053 -26.713 1.00 86.62 N ANISOU 1437 NH2 ARG B 123 6843 14052 12018 314 793 3044 N ATOM 1438 N LYS B 124 7.985 10.120 -22.119 1.00 61.98 N ANISOU 1438 N LYS B 124 5267 9761 8521 -974 -351 2180 N ATOM 1439 CA LYS B 124 7.404 9.434 -20.994 1.00 60.60 C ANISOU 1439 CA LYS B 124 5213 9550 8263 -882 -503 2111 C ATOM 1440 C LYS B 124 6.553 8.267 -21.536 1.00 56.09 C ANISOU 1440 C LYS B 124 4812 8820 7679 -534 -353 2066 C ATOM 1441 O LYS B 124 6.211 8.211 -22.694 1.00 50.38 O ANISOU 1441 O LYS B 124 4184 7985 6974 -412 -170 2029 O ATOM 1442 CB LYS B 124 6.579 10.385 -20.115 1.00 61.52 C ANISOU 1442 CB LYS B 124 5618 9494 8264 -1131 -646 1935 C ATOM 1443 CG LYS B 124 7.408 11.437 -19.302 1.00 67.28 C ANISOU 1443 CG LYS B 124 6243 10353 8969 -1519 -852 1939 C ATOM 1444 CD LYS B 124 8.709 10.851 -18.673 1.00 76.73 C ANISOU 1444 CD LYS B 124 7029 11927 10197 -1550 -1019 2130 C ATOM 1445 CE LYS B 124 9.546 11.914 -17.943 1.00 84.26 C ANISOU 1445 CE LYS B 124 7861 13035 11118 -1998 -1254 2125 C ATOM 1446 NZ LYS B 124 8.716 12.598 -16.877 1.00 85.44 N ANISOU 1446 NZ LYS B 124 8402 12984 11078 -2194 -1410 1891 N ATOM 1447 N GLU B 125 6.299 7.287 -20.675 1.00 55.27 N ANISOU 1447 N GLU B 125 4743 8723 7535 -389 -443 2085 N ATOM 1448 CA GLU B 125 5.720 6.028 -21.090 1.00 53.66 C ANISOU 1448 CA GLU B 125 4671 8374 7342 -90 -322 2073 C ATOM 1449 C GLU B 125 4.550 5.737 -20.166 1.00 51.05 C ANISOU 1449 C GLU B 125 4592 7893 6911 -125 -415 1977 C ATOM 1450 O GLU B 125 4.557 6.167 -19.010 1.00 50.84 O ANISOU 1450 O GLU B 125 4565 7953 6800 -291 -582 1979 O ATOM 1451 CB GLU B 125 6.701 4.867 -20.991 1.00 56.42 C ANISOU 1451 CB GLU B 125 4799 8868 7769 177 -299 2257 C ATOM 1452 CG GLU B 125 7.968 5.074 -21.702 1.00 61.73 C ANISOU 1452 CG GLU B 125 5146 9770 8539 237 -202 2393 C ATOM 1453 CD GLU B 125 8.860 3.825 -21.846 1.00 69.26 C ANISOU 1453 CD GLU B 125 5896 10842 9579 613 -109 2573 C ATOM 1454 OE1 GLU B 125 8.544 2.735 -21.310 1.00 71.01 O ANISOU 1454 OE1 GLU B 125 6255 10935 9793 829 -140 2606 O ATOM 1455 OE2 GLU B 125 9.897 3.968 -22.531 1.00 74.24 O ANISOU 1455 OE2 GLU B 125 6226 11692 10290 702 18 2694 O ATOM 1456 N GLY B 126 3.563 5.009 -20.676 1.00 48.06 N ANISOU 1456 N GLY B 126 4425 7309 6527 13 -307 1894 N ATOM 1457 CA GLY B 126 2.508 4.501 -19.795 1.00 46.76 C ANISOU 1457 CA GLY B 126 4451 7033 6284 -6 -369 1852 C ATOM 1458 C GLY B 126 1.283 4.137 -20.649 1.00 44.95 C ANISOU 1458 C GLY B 126 4432 6595 6054 40 -253 1721 C ATOM 1459 O GLY B 126 1.373 4.107 -21.910 1.00 43.43 O ANISOU 1459 O GLY B 126 4254 6345 5903 124 -136 1670 O ATOM 1460 N TYR B 127 0.192 3.785 -19.948 1.00 44.07 N ANISOU 1460 N TYR B 127 4466 6401 5879 -18 -287 1684 N ATOM 1461 CA TYR B 127 -0.979 3.231 -20.562 1.00 42.13 C ANISOU 1461 CA TYR B 127 4379 5994 5635 -9 -214 1591 C ATOM 1462 C TYR B 127 -1.851 4.330 -21.204 1.00 40.12 C ANISOU 1462 C TYR B 127 4163 5746 5336 -103 -188 1455 C ATOM 1463 O TYR B 127 -2.016 5.409 -20.633 1.00 41.60 O ANISOU 1463 O TYR B 127 4332 6007 5466 -200 -230 1426 O ATOM 1464 CB TYR B 127 -1.821 2.377 -19.564 1.00 43.59 C ANISOU 1464 CB TYR B 127 4668 6114 5782 -57 -245 1643 C ATOM 1465 CG TYR B 127 -1.153 1.033 -19.293 1.00 47.84 C ANISOU 1465 CG TYR B 127 5240 6553 6383 85 -240 1786 C ATOM 1466 CD1 TYR B 127 -0.402 0.838 -18.147 1.00 54.91 C ANISOU 1466 CD1 TYR B 127 6058 7560 7244 129 -326 1953 C ATOM 1467 CD2 TYR B 127 -1.151 0.038 -20.256 1.00 45.76 C ANISOU 1467 CD2 TYR B 127 5096 6088 6203 202 -153 1752 C ATOM 1468 CE1 TYR B 127 0.308 -0.352 -17.944 1.00 61.93 C ANISOU 1468 CE1 TYR B 127 6970 8359 8201 318 -319 2119 C ATOM 1469 CE2 TYR B 127 -0.495 -1.148 -20.066 1.00 56.67 C ANISOU 1469 CE2 TYR B 127 6546 7334 7655 380 -126 1881 C ATOM 1470 CZ TYR B 127 0.253 -1.337 -18.922 1.00 62.61 C ANISOU 1470 CZ TYR B 127 7197 8198 8393 458 -204 2081 C ATOM 1471 OH TYR B 127 0.951 -2.509 -18.777 1.00 70.25 O ANISOU 1471 OH TYR B 127 8228 9025 9438 692 -171 2240 O ATOM 1472 N ILE B 128 -2.446 3.995 -22.344 1.00 38.57 N ANISOU 1472 N ILE B 128 4046 5459 5151 -65 -126 1374 N ATOM 1473 CA ILE B 128 -3.323 4.864 -23.064 1.00 38.20 C ANISOU 1473 CA ILE B 128 4030 5430 5055 -111 -111 1279 C ATOM 1474 C ILE B 128 -4.589 4.130 -23.552 1.00 38.20 C ANISOU 1474 C ILE B 128 4113 5367 5032 -149 -116 1206 C ATOM 1475 O ILE B 128 -4.550 2.931 -23.799 1.00 38.14 O ANISOU 1475 O ILE B 128 4188 5249 5055 -132 -105 1198 O ATOM 1476 CB ILE B 128 -2.625 5.426 -24.333 1.00 38.72 C ANISOU 1476 CB ILE B 128 4079 5511 5120 -41 -47 1263 C ATOM 1477 CG1 ILE B 128 -2.232 4.292 -25.307 1.00 41.65 C ANISOU 1477 CG1 ILE B 128 4516 5807 5501 77 23 1238 C ATOM 1478 CG2 ILE B 128 -1.377 6.250 -23.902 1.00 37.12 C ANISOU 1478 CG2 ILE B 128 3757 5392 4956 -67 -49 1348 C ATOM 1479 CD1 ILE B 128 -1.979 4.836 -26.764 1.00 39.37 C ANISOU 1479 CD1 ILE B 128 4257 5557 5146 142 106 1200 C ATOM 1480 N PRO B 129 -5.713 4.862 -23.713 1.00 37.11 N ANISOU 1480 N PRO B 129 3956 5302 4844 -199 -137 1157 N ATOM 1481 CA PRO B 129 -6.946 4.284 -24.167 1.00 36.30 C ANISOU 1481 CA PRO B 129 3869 5207 4717 -271 -170 1103 C ATOM 1482 C PRO B 129 -6.856 4.095 -25.675 1.00 38.33 C ANISOU 1482 C PRO B 129 4201 5434 4928 -227 -174 1025 C ATOM 1483 O PRO B 129 -6.631 5.065 -26.392 1.00 40.07 O ANISOU 1483 O PRO B 129 4410 5717 5099 -149 -155 1023 O ATOM 1484 CB PRO B 129 -7.958 5.320 -23.760 1.00 36.57 C ANISOU 1484 CB PRO B 129 3810 5376 4711 -280 -178 1109 C ATOM 1485 CG PRO B 129 -7.274 6.587 -23.712 1.00 34.93 C ANISOU 1485 CG PRO B 129 3609 5172 4489 -192 -146 1121 C ATOM 1486 CD PRO B 129 -5.922 6.240 -23.234 1.00 38.15 C ANISOU 1486 CD PRO B 129 4044 5512 4942 -196 -134 1162 C ATOM 1487 N SER B 130 -6.925 2.880 -26.143 1.00 40.13 N ANISOU 1487 N SER B 130 4540 5550 5157 -273 -188 964 N ATOM 1488 CA SER B 130 -6.599 2.622 -27.521 1.00 42.78 C ANISOU 1488 CA SER B 130 4998 5845 5413 -209 -172 870 C ATOM 1489 C SER B 130 -7.584 3.227 -28.474 1.00 44.54 C ANISOU 1489 C SER B 130 5193 6212 5517 -250 -252 814 C ATOM 1490 O SER B 130 -7.206 3.422 -29.640 1.00 45.69 O ANISOU 1490 O SER B 130 5428 6381 5551 -164 -228 763 O ATOM 1491 CB SER B 130 -6.513 1.150 -27.830 1.00 44.55 C ANISOU 1491 CB SER B 130 5411 5870 5646 -249 -168 781 C ATOM 1492 OG SER B 130 -7.673 0.454 -27.479 1.00 44.15 O ANISOU 1492 OG SER B 130 5377 5781 5616 -460 -263 749 O ATOM 1493 N ASN B 131 -8.834 3.435 -28.057 1.00 43.55 N ANISOU 1493 N ASN B 131 4942 6207 5397 -368 -342 834 N ATOM 1494 CA ASN B 131 -9.785 4.054 -28.958 1.00 44.25 C ANISOU 1494 CA ASN B 131 4962 6480 5372 -373 -437 814 C ATOM 1495 C ASN B 131 -9.580 5.609 -29.163 1.00 42.79 C ANISOU 1495 C ASN B 131 4709 6399 5151 -193 -390 909 C ATOM 1496 O ASN B 131 -10.309 6.235 -29.869 1.00 41.63 O ANISOU 1496 O ASN B 131 4506 6403 4910 -146 -461 934 O ATOM 1497 CB ASN B 131 -11.255 3.703 -28.565 1.00 45.34 C ANISOU 1497 CB ASN B 131 4939 6760 5529 -552 -550 822 C ATOM 1498 CG ASN B 131 -11.615 4.215 -27.181 1.00 45.33 C ANISOU 1498 CG ASN B 131 4770 6823 5632 -533 -484 932 C ATOM 1499 OD1 ASN B 131 -10.729 4.416 -26.346 1.00 40.07 O ANISOU 1499 OD1 ASN B 131 4157 6038 5029 -456 -381 973 O ATOM 1500 ND2 ASN B 131 -12.881 4.400 -26.918 1.00 45.01 N ANISOU 1500 ND2 ASN B 131 4522 6988 5592 -601 -539 981 N ATOM 1501 N TYR B 132 -8.594 6.213 -28.537 1.00 41.56 N ANISOU 1501 N TYR B 132 4567 6154 5070 -107 -282 971 N ATOM 1502 CA TYR B 132 -8.291 7.626 -28.749 1.00 41.28 C ANISOU 1502 CA TYR B 132 4526 6144 5014 20 -230 1054 C ATOM 1503 C TYR B 132 -7.234 7.850 -29.809 1.00 42.21 C ANISOU 1503 C TYR B 132 4754 6222 5060 90 -159 1070 C ATOM 1504 O TYR B 132 -6.855 9.002 -30.014 1.00 42.30 O ANISOU 1504 O TYR B 132 4785 6223 5065 162 -103 1160 O ATOM 1505 CB TYR B 132 -7.729 8.240 -27.450 1.00 41.05 C ANISOU 1505 CB TYR B 132 4468 6035 5093 22 -161 1102 C ATOM 1506 CG TYR B 132 -8.782 8.653 -26.427 1.00 37.70 C ANISOU 1506 CG TYR B 132 3952 5674 4697 26 -178 1114 C ATOM 1507 CD1 TYR B 132 -9.947 7.865 -26.200 1.00 38.24 C ANISOU 1507 CD1 TYR B 132 3910 5860 4761 -47 -240 1092 C ATOM 1508 CD2 TYR B 132 -8.679 9.849 -25.761 1.00 37.91 C ANISOU 1508 CD2 TYR B 132 4008 5652 4745 98 -123 1146 C ATOM 1509 CE1 TYR B 132 -10.909 8.271 -25.261 1.00 38.75 C ANISOU 1509 CE1 TYR B 132 3857 6025 4841 -18 -215 1123 C ATOM 1510 CE2 TYR B 132 -9.604 10.212 -24.767 1.00 37.76 C ANISOU 1510 CE2 TYR B 132 3926 5692 4728 141 -100 1142 C ATOM 1511 CZ TYR B 132 -10.690 9.426 -24.505 1.00 42.43 C ANISOU 1511 CZ TYR B 132 4373 6433 5313 98 -132 1141 C ATOM 1512 OH TYR B 132 -11.596 9.897 -23.581 1.00 40.36 O ANISOU 1512 OH TYR B 132 4029 6265 5042 176 -70 1155 O ATOM 1513 N VAL B 133 -6.738 6.781 -30.418 1.00 42.24 N ANISOU 1513 N VAL B 133 4845 6189 5016 72 -141 991 N ATOM 1514 CA VAL B 133 -5.587 6.861 -31.347 1.00 42.98 C ANISOU 1514 CA VAL B 133 5029 6266 5037 162 -22 1010 C ATOM 1515 C VAL B 133 -5.872 6.136 -32.632 1.00 45.50 C ANISOU 1515 C VAL B 133 5491 6631 5167 183 -50 901 C ATOM 1516 O VAL B 133 -6.699 5.195 -32.669 1.00 45.90 O ANISOU 1516 O VAL B 133 5590 6668 5182 86 -164 779 O ATOM 1517 CB VAL B 133 -4.252 6.407 -30.709 1.00 42.83 C ANISOU 1517 CB VAL B 133 4976 6156 5144 184 92 1036 C ATOM 1518 CG1 VAL B 133 -4.004 7.149 -29.374 1.00 38.46 C ANISOU 1518 CG1 VAL B 133 4296 5579 4738 124 80 1125 C ATOM 1519 CG2 VAL B 133 -4.177 4.870 -30.507 1.00 41.47 C ANISOU 1519 CG2 VAL B 133 4878 5877 5001 179 87 928 C ATOM 1520 N ALA B 134 -5.116 6.548 -33.683 1.00 47.03 N ANISOU 1520 N ALA B 134 5765 6876 5227 289 64 946 N ATOM 1521 CA ALA B 134 -5.189 5.931 -34.992 1.00 48.18 C ANISOU 1521 CA ALA B 134 6091 7078 5136 335 69 833 C ATOM 1522 C ALA B 134 -3.815 5.476 -35.369 1.00 49.12 C ANISOU 1522 C ALA B 134 6280 7145 5236 458 283 822 C ATOM 1523 O ALA B 134 -2.806 6.232 -35.283 1.00 47.42 O ANISOU 1523 O ALA B 134 5960 6967 5092 523 437 978 O ATOM 1524 CB ALA B 134 -5.756 6.925 -36.013 1.00 47.40 C ANISOU 1524 CB ALA B 134 6029 7150 4832 379 11 923 C ATOM 1525 N ARG B 135 -3.758 4.234 -35.837 1.00 50.99 N ANISOU 1525 N ARG B 135 6701 7301 5373 490 304 639 N ATOM 1526 CA ARG B 135 -2.521 3.712 -36.356 1.00 53.21 C ANISOU 1526 CA ARG B 135 7071 7549 5598 671 535 611 C ATOM 1527 C ARG B 135 -2.264 4.228 -37.777 1.00 55.19 C ANISOU 1527 C ARG B 135 7444 7972 5555 774 648 632 C ATOM 1528 O ARG B 135 -3.129 4.091 -38.616 1.00 55.37 O ANISOU 1528 O ARG B 135 7646 8059 5334 722 519 514 O ATOM 1529 CB ARG B 135 -2.572 2.176 -36.365 1.00 55.81 C ANISOU 1529 CB ARG B 135 7620 7673 5912 701 538 390 C ATOM 1530 CG ARG B 135 -1.231 1.603 -36.682 1.00 62.81 C ANISOU 1530 CG ARG B 135 8566 8509 6790 952 807 380 C ATOM 1531 CD ARG B 135 -1.083 0.095 -36.551 1.00 72.45 C ANISOU 1531 CD ARG B 135 10027 9458 8043 1047 855 189 C ATOM 1532 NE ARG B 135 0.091 -0.280 -37.359 1.00 79.84 N ANISOU 1532 NE ARG B 135 11068 10414 8853 1353 1150 156 N ATOM 1533 CZ ARG B 135 0.807 -1.398 -37.254 1.00 84.68 C ANISOU 1533 CZ ARG B 135 11827 10821 9528 1589 1321 70 C ATOM 1534 NH1 ARG B 135 0.502 -2.350 -36.373 1.00 84.33 N ANISOU 1534 NH1 ARG B 135 11882 10487 9671 1543 1220 9 N ATOM 1535 NH2 ARG B 135 1.854 -1.547 -38.066 1.00 88.31 N ANISOU 1535 NH2 ARG B 135 12335 11369 9849 1897 1618 64 N ATOM 1536 N VAL B 136 -1.052 4.723 -38.036 1.00 57.61 N ANISOU 1536 N VAL B 136 7651 8370 5871 910 889 784 N ATOM 1537 CA VAL B 136 -0.632 5.192 -39.363 1.00 63.83 C ANISOU 1537 CA VAL B 136 8547 9335 6369 1023 1056 843 C ATOM 1538 C VAL B 136 0.531 4.345 -39.933 1.00 71.16 C ANISOU 1538 C VAL B 136 9563 10276 7200 1256 1350 768 C ATOM 1539 O VAL B 136 1.157 3.554 -39.192 1.00 71.89 O ANISOU 1539 O VAL B 136 9575 10239 7503 1349 1431 725 O ATOM 1540 CB VAL B 136 -0.248 6.690 -39.258 1.00 63.08 C ANISOU 1540 CB VAL B 136 8247 9361 6359 960 1117 1135 C ATOM 1541 CG1 VAL B 136 -1.531 7.537 -38.791 1.00 56.45 C ANISOU 1541 CG1 VAL B 136 7375 8490 5582 795 840 1191 C ATOM 1542 CG2 VAL B 136 0.862 6.901 -38.244 1.00 60.52 C ANISOU 1542 CG2 VAL B 136 7646 9006 6345 947 1242 1280 C ATOM 1543 N ASP B 137 0.805 4.519 -41.239 1.00 79.17 N ANISOU 1543 N ASP B 137 10743 11456 7880 1377 1518 767 N ATOM 1544 CA ASP B 137 1.985 3.952 -42.010 1.00 85.73 C ANISOU 1544 CA ASP B 137 11651 12374 8549 1650 1874 734 C ATOM 1545 C ASP B 137 1.725 2.625 -42.736 1.00 90.66 C ANISOU 1545 C ASP B 137 12671 12872 8902 1801 1910 393 C ATOM 1546 O ASP B 137 0.760 1.908 -42.426 1.00 91.67 O ANISOU 1546 O ASP B 137 12987 12794 9048 1670 1654 169 O ATOM 1547 CB ASP B 137 3.252 3.683 -41.158 1.00 86.67 C ANISOU 1547 CB ASP B 137 11469 12475 8988 1788 2086 862 C ATOM 1548 CG ASP B 137 3.972 4.935 -40.713 1.00 88.21 C ANISOU 1548 CG ASP B 137 11284 12844 9387 1672 2162 1198 C ATOM 1549 OD1 ASP B 137 4.624 4.855 -39.638 1.00 88.15 O ANISOU 1549 OD1 ASP B 137 10987 12805 9702 1660 2166 1302 O ATOM 1550 OD2 ASP B 137 3.897 5.967 -41.418 1.00 91.54 O ANISOU 1550 OD2 ASP B 137 11712 13426 9644 1583 2207 1360 O ATOM 1551 N SER B 138 2.617 2.340 -43.699 1.00 96.02 N ANISOU 1551 N SER B 138 13476 13680 9328 2066 2245 364 N ATOM 1552 CA SER B 138 2.997 0.982 -44.192 1.00100.37 C ANISOU 1552 CA SER B 138 14356 14076 9706 2339 2441 68 C ATOM 1553 C SER B 138 1.932 0.176 -44.969 1.00103.05 C ANISOU 1553 C SER B 138 15204 14264 9689 2260 2245 -307 C ATOM 1554 O SER B 138 2.171 -0.184 -46.131 1.00106.64 O ANISOU 1554 O SER B 138 15986 14802 9732 2445 2441 -479 O ATOM 1555 CB SER B 138 3.591 0.143 -43.041 1.00 99.91 C ANISOU 1555 CB SER B 138 14142 13777 10042 2473 2500 58 C ATOM 1556 OG SER B 138 2.825 0.266 -41.849 1.00 95.59 O ANISOU 1556 OG SER B 138 13439 13065 9814 2194 2164 102 O ATOM 1557 OXT SER B 138 0.836 -0.145 -44.470 1.00101.34 O ANISOU 1557 OXT SER B 138 15081 13856 9568 2000 1895 -450 O TER 1558 SER B 138 ATOM 1559 N SER C 59 -33.548 -9.510 -29.415 1.00138.14 N ANISOU 1559 N SER C 59 18120 17940 16428 -1865 412 -1091 N ATOM 1560 CA SER C 59 -32.487 -10.297 -28.721 1.00138.39 C ANISOU 1560 CA SER C 59 18169 17710 16704 -1654 611 -1151 C ATOM 1561 C SER C 59 -31.728 -9.454 -27.671 1.00136.22 C ANISOU 1561 C SER C 59 17678 17446 16635 -1395 570 -963 C ATOM 1562 O SER C 59 -31.946 -8.241 -27.546 1.00134.61 O ANISOU 1562 O SER C 59 17338 17429 16378 -1372 416 -818 O ATOM 1563 CB SER C 59 -31.515 -10.902 -29.746 1.00140.57 C ANISOU 1563 CB SER C 59 18624 17865 16922 -1669 879 -1350 C ATOM 1564 N ALA C 60 -30.877 -10.138 -26.895 1.00136.42 N ANISOU 1564 N ALA C 60 17677 17262 16895 -1215 707 -959 N ATOM 1565 CA ALA C 60 -29.934 -9.524 -25.937 1.00134.70 C ANISOU 1565 CA ALA C 60 17275 17032 16872 -989 694 -791 C ATOM 1566 C ALA C 60 -28.523 -10.182 -25.995 1.00136.22 C ANISOU 1566 C ALA C 60 17474 17038 17245 -828 942 -824 C ATOM 1567 O ALA C 60 -27.584 -9.700 -25.338 1.00135.43 O ANISOU 1567 O ALA C 60 17216 16939 17300 -659 942 -672 O ATOM 1568 CB ALA C 60 -30.498 -9.564 -24.523 1.00132.72 C ANISOU 1568 CB ALA C 60 16916 16752 16759 -927 544 -652 C ATOM 1569 N TRP C 61 -28.387 -11.285 -26.751 1.00138.64 N ANISOU 1569 N TRP C 61 17959 17179 17538 -887 1158 -1009 N ATOM 1570 CA TRP C 61 -27.089 -11.725 -27.308 1.00140.44 C ANISOU 1570 CA TRP C 61 18225 17263 17872 -762 1443 -1069 C ATOM 1571 C TRP C 61 -26.785 -10.884 -28.556 1.00140.83 C ANISOU 1571 C TRP C 61 18325 17488 17698 -837 1483 -1135 C ATOM 1572 O TRP C 61 -25.615 -10.734 -28.937 1.00141.57 O ANISOU 1572 O TRP C 61 18375 17547 17868 -705 1667 -1111 O ATOM 1573 CB TRP C 61 -27.101 -13.222 -27.669 1.00143.04 C ANISOU 1573 CB TRP C 61 18758 17321 18268 -801 1694 -1259 C ATOM 1574 N LEU C 62 -27.859 -10.348 -29.168 1.00140.31 N ANISOU 1574 N LEU C 62 18333 17615 17363 -1050 1308 -1194 N ATOM 1575 CA LEU C 62 -27.811 -9.392 -30.303 1.00140.32 C ANISOU 1575 CA LEU C 62 18359 17836 17119 -1156 1279 -1219 C ATOM 1576 C LEU C 62 -27.845 -7.898 -29.877 1.00137.42 C ANISOU 1576 C LEU C 62 17776 17694 16744 -1095 1048 -1005 C ATOM 1577 O LEU C 62 -27.725 -7.011 -30.724 1.00137.41 O ANISOU 1577 O LEU C 62 17761 17876 16575 -1157 1017 -986 O ATOM 1578 CB LEU C 62 -28.952 -9.682 -31.301 1.00141.62 C ANISOU 1578 CB LEU C 62 18726 18096 16988 -1449 1222 -1382 C ATOM 1579 N GLU C 63 -28.032 -7.629 -28.582 1.00135.03 N ANISOU 1579 N GLU C 63 17322 17371 16613 -985 896 -847 N ATOM 1580 CA GLU C 63 -27.675 -6.326 -27.983 1.00132.65 C ANISOU 1580 CA GLU C 63 16827 17203 16370 -877 747 -650 C ATOM 1581 C GLU C 63 -26.473 -6.422 -27.006 1.00131.83 C ANISOU 1581 C GLU C 63 16589 16973 16525 -666 817 -527 C ATOM 1582 O GLU C 63 -26.037 -5.394 -26.455 1.00130.48 O ANISOU 1582 O GLU C 63 16274 16894 16410 -588 704 -367 O ATOM 1583 CB GLU C 63 -28.886 -5.669 -27.302 1.00130.79 C ANISOU 1583 CB GLU C 63 16525 17082 16087 -945 502 -545 C ATOM 1584 CG GLU C 63 -29.708 -4.777 -28.227 1.00130.49 C ANISOU 1584 CG GLU C 63 16498 17262 15820 -1103 383 -531 C ATOM 1585 CD GLU C 63 -29.085 -3.400 -28.454 1.00129.92 C ANISOU 1585 CD GLU C 63 16305 17331 15728 -1036 337 -404 C ATOM 1586 OE1 GLU C 63 -27.843 -3.238 -28.325 1.00128.82 O ANISOU 1586 OE1 GLU C 63 16108 17135 15701 -901 438 -373 O ATOM 1587 OE2 GLU C 63 -29.856 -2.471 -28.772 1.00129.68 O ANISOU 1587 OE2 GLU C 63 16226 17469 15578 -1124 198 -318 O ATOM 1588 N ALA C 64 -25.957 -7.648 -26.801 1.00132.57 N ANISOU 1588 N ALA C 64 16733 16858 16779 -587 1002 -589 N ATOM 1589 CA ALA C 64 -24.674 -7.897 -26.107 1.00132.14 C ANISOU 1589 CA ALA C 64 16545 16684 16980 -392 1113 -456 C ATOM 1590 C ALA C 64 -23.508 -7.571 -27.047 1.00132.75 C ANISOU 1590 C ALA C 64 16596 16790 17053 -322 1294 -454 C ATOM 1591 O ALA C 64 -22.574 -6.846 -26.688 1.00132.30 O ANISOU 1591 O ALA C 64 16372 16796 17100 -215 1260 -278 O ATOM 1592 CB ALA C 64 -24.586 -9.355 -25.634 1.00133.41 C ANISOU 1592 CB ALA C 64 16760 16600 17330 -328 1269 -504 C ATOM 1593 N GLN C 65 -23.572 -8.109 -28.259 1.00133.79 N ANISOU 1593 N GLN C 65 16903 16880 17052 -399 1488 -647 N ATOM 1594 CA GLN C 65 -22.630 -7.736 -29.300 1.00134.46 C ANISOU 1594 CA GLN C 65 16989 17018 17081 -359 1665 -665 C ATOM 1595 C GLN C 65 -22.826 -6.265 -29.733 1.00132.29 C ANISOU 1595 C GLN C 65 16642 17008 16614 -441 1470 -590 C ATOM 1596 O GLN C 65 -21.851 -5.606 -30.104 1.00132.65 O ANISOU 1596 O GLN C 65 16584 17128 16688 -360 1535 -492 O ATOM 1597 CB GLN C 65 -22.762 -8.683 -30.502 1.00137.06 C ANISOU 1597 CB GLN C 65 17566 17238 17274 -453 1928 -916 C ATOM 1598 N GLU C 66 -24.068 -5.756 -29.660 1.00129.82 N ANISOU 1598 N GLU C 66 16368 16828 16131 -593 1239 -612 N ATOM 1599 CA GLU C 66 -24.430 -4.401 -30.177 1.00127.75 C ANISOU 1599 CA GLU C 66 16052 16806 15682 -687 1067 -543 C ATOM 1600 C GLU C 66 -24.249 -3.217 -29.181 1.00124.45 C ANISOU 1600 C GLU C 66 15440 16475 15370 -605 860 -327 C ATOM 1601 O GLU C 66 -24.153 -2.053 -29.604 1.00123.46 O ANISOU 1601 O GLU C 66 15246 16513 15151 -634 771 -242 O ATOM 1602 CB GLU C 66 -25.867 -4.407 -30.733 1.00127.65 C ANISOU 1602 CB GLU C 66 16167 16904 15431 -901 941 -648 C ATOM 1603 N GLU C 67 -24.224 -3.516 -27.876 1.00121.99 N ANISOU 1603 N GLU C 67 15055 16051 15243 -517 787 -242 N ATOM 1604 CA GLU C 67 -23.833 -2.538 -26.839 1.00118.92 C ANISOU 1604 CA GLU C 67 14510 15709 14965 -443 628 -51 C ATOM 1605 C GLU C 67 -22.297 -2.369 -26.805 1.00118.12 C ANISOU 1605 C GLU C 67 14282 15583 15015 -315 734 72 C ATOM 1606 O GLU C 67 -21.802 -1.271 -26.519 1.00117.24 O ANISOU 1606 O GLU C 67 14057 15566 14922 -299 623 216 O ATOM 1607 CB GLU C 67 -24.362 -2.956 -25.453 1.00117.55 C ANISOU 1607 CB GLU C 67 14317 15439 14908 -418 514 -1 C ATOM 1608 N GLU C 68 -21.566 -3.458 -27.092 1.00117.77 N ANISOU 1608 N GLU C 68 14256 15402 15088 -229 957 24 N ATOM 1609 CA GLU C 68 -20.094 -3.431 -27.237 1.00117.20 C ANISOU 1609 CA GLU C 68 14053 15304 15174 -99 1103 153 C ATOM 1610 C GLU C 68 -19.646 -3.260 -28.713 1.00116.69 C ANISOU 1610 C GLU C 68 14047 15307 14983 -113 1291 64 C ATOM 1611 O GLU C 68 -19.231 -4.235 -29.354 1.00118.70 O ANISOU 1611 O GLU C 68 14382 15440 15280 -57 1553 -39 O ATOM 1612 CB GLU C 68 -19.476 -4.705 -26.632 1.00118.47 C ANISOU 1612 CB GLU C 68 14173 15263 15578 30 1267 197 C ATOM 1613 N GLU C 69 -19.739 -2.022 -29.233 1.00113.18 N ANISOU 1613 N GLU C 69 13569 15049 14385 -187 1168 108 N ATOM 1614 CA GLU C 69 -19.255 -1.660 -30.602 1.00112.26 C ANISOU 1614 CA GLU C 69 13483 15035 14135 -209 1319 61 C ATOM 1615 C GLU C 69 -19.119 -0.132 -30.921 1.00108.61 C ANISOU 1615 C GLU C 69 12919 14775 13571 -263 1157 190 C ATOM 1616 O GLU C 69 -18.273 0.258 -31.746 1.00109.45 O ANISOU 1616 O GLU C 69 12973 14958 13656 -230 1278 241 O ATOM 1617 CB GLU C 69 -20.099 -2.348 -31.707 1.00113.83 C ANISOU 1617 CB GLU C 69 13909 15232 14110 -335 1445 -185 C ATOM 1618 CG GLU C 69 -21.600 -1.967 -31.779 1.00112.91 C ANISOU 1618 CG GLU C 69 13890 15229 13783 -514 1227 -265 C ATOM 1619 CD GLU C 69 -22.277 -2.442 -33.076 1.00115.89 C ANISOU 1619 CD GLU C 69 14474 15663 13898 -681 1333 -472 C ATOM 1620 OE1 GLU C 69 -23.359 -3.072 -32.989 1.00115.96 O ANISOU 1620 OE1 GLU C 69 14611 15632 13815 -800 1272 -594 O ATOM 1621 OE2 GLU C 69 -21.726 -2.193 -34.183 1.00117.69 O ANISOU 1621 OE2 GLU C 69 14738 15981 13999 -708 1475 -505 O ATOM 1622 N VAL C 70 -19.954 0.712 -30.299 1.00103.13 N ANISOU 1622 N VAL C 70 12204 14157 12823 -341 906 243 N ATOM 1623 CA VAL C 70 -19.903 2.182 -30.497 1.00 99.27 C ANISOU 1623 CA VAL C 70 11627 13828 12264 -391 754 371 C ATOM 1624 C VAL C 70 -19.669 2.918 -29.137 1.00 94.33 C ANISOU 1624 C VAL C 70 10884 13172 11787 -359 562 539 C ATOM 1625 O VAL C 70 -20.605 3.093 -28.335 1.00 93.14 O ANISOU 1625 O VAL C 70 10777 12994 11620 -406 411 524 O ATOM 1626 CB VAL C 70 -21.187 2.692 -31.290 1.00 98.87 C ANISOU 1626 CB VAL C 70 11677 13914 11974 -541 660 284 C ATOM 1627 CG1 VAL C 70 -21.576 4.131 -30.928 1.00 96.72 C ANISOU 1627 CG1 VAL C 70 11321 13741 11687 -584 452 427 C ATOM 1628 CG2 VAL C 70 -20.972 2.540 -32.804 1.00100.64 C ANISOU 1628 CG2 VAL C 70 11972 14243 12023 -599 824 195 C ATOM 1629 N GLY C 71 -18.410 3.318 -28.900 1.00 90.17 N ANISOU 1629 N GLY C 71 10215 12651 11397 -289 579 701 N ATOM 1630 CA GLY C 71 -17.994 4.093 -27.695 1.00 85.26 C ANISOU 1630 CA GLY C 71 9488 12014 10892 -293 398 872 C ATOM 1631 C GLY C 71 -18.114 5.617 -27.837 1.00 80.59 C ANISOU 1631 C GLY C 71 8866 11532 10221 -375 250 960 C ATOM 1632 O GLY C 71 -17.686 6.381 -26.956 1.00 76.43 O ANISOU 1632 O GLY C 71 8275 10995 9771 -404 112 1095 O ATOM 1633 N PHE C 72 -18.738 6.051 -28.948 1.00 77.07 N ANISOU 1633 N PHE C 72 8478 11190 9615 -427 280 886 N ATOM 1634 CA PHE C 72 -18.922 7.470 -29.254 1.00 73.85 C ANISOU 1634 CA PHE C 72 8039 10882 9139 -497 168 975 C ATOM 1635 C PHE C 72 -20.371 7.776 -29.805 1.00 70.66 C ANISOU 1635 C PHE C 72 7733 10545 8571 -575 120 884 C ATOM 1636 O PHE C 72 -20.564 7.885 -31.001 1.00 68.33 O ANISOU 1636 O PHE C 72 7449 10368 8146 -615 185 855 O ATOM 1637 CB PHE C 72 -17.816 7.904 -30.252 1.00 74.76 C ANISOU 1637 CB PHE C 72 8049 11101 9255 -475 264 1073 C ATOM 1638 CG PHE C 72 -17.490 9.363 -30.222 1.00 74.64 C ANISOU 1638 CG PHE C 72 7955 11151 9256 -528 141 1228 C ATOM 1639 CD1 PHE C 72 -18.194 10.255 -29.418 1.00 75.79 C ANISOU 1639 CD1 PHE C 72 8143 11250 9404 -591 -22 1259 C ATOM 1640 CD2 PHE C 72 -16.486 9.859 -31.037 1.00 76.85 C ANISOU 1640 CD2 PHE C 72 8125 11528 9548 -516 209 1343 C ATOM 1641 CE1 PHE C 72 -17.895 11.593 -29.413 1.00 77.03 C ANISOU 1641 CE1 PHE C 72 8247 11440 9583 -645 -114 1392 C ATOM 1642 CE2 PHE C 72 -16.161 11.212 -31.032 1.00 78.12 C ANISOU 1642 CE2 PHE C 72 8212 11739 9731 -573 96 1493 C ATOM 1643 CZ PHE C 72 -16.856 12.082 -30.221 1.00 79.10 C ANISOU 1643 CZ PHE C 72 8391 11799 9863 -642 -64 1513 C ATOM 1644 N PRO C 73 -21.372 7.903 -28.902 1.00 66.63 N ANISOU 1644 N PRO C 73 7285 9963 8068 -602 7 858 N ATOM 1645 CA PRO C 73 -22.773 8.099 -29.327 1.00 64.40 C ANISOU 1645 CA PRO C 73 7068 9741 7661 -669 -37 808 C ATOM 1646 C PRO C 73 -23.053 9.456 -29.973 1.00 62.75 C ANISOU 1646 C PRO C 73 6806 9641 7395 -720 -96 925 C ATOM 1647 O PRO C 73 -22.349 10.443 -29.768 1.00 62.01 O ANISOU 1647 O PRO C 73 6647 9540 7374 -710 -135 1042 O ATOM 1648 CB PRO C 73 -23.595 7.933 -28.035 1.00 63.23 C ANISOU 1648 CB PRO C 73 6979 9471 7575 -660 -123 783 C ATOM 1649 CG PRO C 73 -22.652 7.427 -26.998 1.00 64.64 C ANISOU 1649 CG PRO C 73 7141 9534 7885 -602 -120 792 C ATOM 1650 CD PRO C 73 -21.251 7.841 -27.436 1.00 65.57 C ANISOU 1650 CD PRO C 73 7159 9699 8055 -578 -79 889 C ATOM 1651 N VAL C 74 -24.073 9.440 -30.803 1.00 61.73 N ANISOU 1651 N VAL C 74 6702 9618 7134 -787 -100 904 N ATOM 1652 CA VAL C 74 -24.503 10.595 -31.574 1.00 60.58 C ANISOU 1652 CA VAL C 74 6493 9597 6926 -842 -148 1033 C ATOM 1653 C VAL C 74 -25.545 11.413 -30.791 1.00 56.63 C ANISOU 1653 C VAL C 74 5991 9028 6498 -839 -241 1120 C ATOM 1654 O VAL C 74 -26.084 12.364 -31.340 1.00 53.64 O ANISOU 1654 O VAL C 74 5552 8734 6096 -875 -276 1250 O ATOM 1655 CB VAL C 74 -25.144 10.128 -32.956 1.00 62.85 C ANISOU 1655 CB VAL C 74 6801 10066 7014 -945 -112 993 C ATOM 1656 CG1 VAL C 74 -24.016 9.693 -33.910 1.00 66.95 C ANISOU 1656 CG1 VAL C 74 7321 10664 7453 -948 12 936 C ATOM 1657 CG2 VAL C 74 -26.198 9.008 -32.773 1.00 64.81 C ANISOU 1657 CG2 VAL C 74 7143 10290 7192 -994 -120 867 C ATOM 1658 N ARG C 75 -25.862 11.018 -29.542 1.00 50.77 N ANISOU 1658 N ARG C 75 5314 8134 5844 -795 -265 1059 N ATOM 1659 CA ARG C 75 -26.833 11.780 -28.742 1.00 48.90 C ANISOU 1659 CA ARG C 75 5090 7810 5679 -780 -317 1135 C ATOM 1660 C ARG C 75 -26.376 11.787 -27.296 1.00 48.51 C ANISOU 1660 C ARG C 75 5109 7582 5742 -732 -333 1093 C ATOM 1661 O ARG C 75 -25.513 10.962 -26.946 1.00 45.17 O ANISOU 1661 O ARG C 75 4705 7122 5336 -714 -319 1011 O ATOM 1662 CB ARG C 75 -28.245 11.226 -28.879 1.00 51.16 C ANISOU 1662 CB ARG C 75 5392 8141 5905 -812 -333 1119 C ATOM 1663 CG ARG C 75 -28.348 9.845 -28.278 1.00 54.21 C ANISOU 1663 CG ARG C 75 5859 8457 6282 -801 -318 965 C ATOM 1664 CD ARG C 75 -29.661 9.250 -28.635 1.00 58.90 C ANISOU 1664 CD ARG C 75 6458 9124 6796 -862 -341 958 C ATOM 1665 NE ARG C 75 -29.731 8.946 -30.045 1.00 64.52 N ANISOU 1665 NE ARG C 75 7145 10015 7354 -962 -335 952 N ATOM 1666 CZ ARG C 75 -29.472 7.753 -30.597 1.00 73.49 C ANISOU 1666 CZ ARG C 75 8352 11189 8383 -1021 -289 804 C ATOM 1667 NH1 ARG C 75 -29.056 6.729 -29.839 1.00 75.83 N ANISOU 1667 NH1 ARG C 75 8726 11347 8740 -967 -242 663 N ATOM 1668 NH2 ARG C 75 -29.608 7.581 -31.929 1.00 74.60 N ANISOU 1668 NH2 ARG C 75 8491 11504 8350 -1141 -279 798 N ATOM 1669 N PRO C 76 -26.887 12.732 -26.504 1.00 45.69 N ANISOU 1669 N PRO C 76 4785 7117 5459 -717 -352 1161 N ATOM 1670 CA PRO C 76 -26.491 12.803 -25.158 1.00 44.61 C ANISOU 1670 CA PRO C 76 4734 6823 5393 -704 -370 1120 C ATOM 1671 C PRO C 76 -26.758 11.550 -24.340 1.00 41.31 C ANISOU 1671 C PRO C 76 4378 6348 4968 -684 -374 1006 C ATOM 1672 O PRO C 76 -27.677 10.721 -24.608 1.00 39.66 O ANISOU 1672 O PRO C 76 4168 6184 4716 -676 -359 958 O ATOM 1673 CB PRO C 76 -27.257 14.028 -24.599 1.00 44.56 C ANISOU 1673 CB PRO C 76 4777 6704 5448 -695 -351 1200 C ATOM 1674 CG PRO C 76 -27.681 14.771 -25.773 1.00 47.00 C ANISOU 1674 CG PRO C 76 4988 7121 5749 -698 -332 1322 C ATOM 1675 CD PRO C 76 -27.851 13.801 -26.860 1.00 47.83 C ANISOU 1675 CD PRO C 76 5017 7404 5753 -717 -342 1291 C ATOM 1676 N GLN C 77 -25.982 11.458 -23.278 1.00 40.71 N ANISOU 1676 N GLN C 77 4358 6173 4937 -693 -404 979 N ATOM 1677 CA GLN C 77 -26.292 10.470 -22.211 1.00 39.77 C ANISOU 1677 CA GLN C 77 4308 5974 4828 -678 -415 899 C ATOM 1678 C GLN C 77 -27.481 11.026 -21.418 1.00 38.38 C ANISOU 1678 C GLN C 77 4222 5701 4661 -669 -396 906 C ATOM 1679 O GLN C 77 -27.381 12.136 -20.870 1.00 38.52 O ANISOU 1679 O GLN C 77 4305 5628 4702 -695 -392 950 O ATOM 1680 CB GLN C 77 -25.037 10.343 -21.299 1.00 39.09 C ANISOU 1680 CB GLN C 77 4240 5830 4782 -712 -468 908 C ATOM 1681 CG GLN C 77 -25.349 9.612 -19.980 1.00 37.98 C ANISOU 1681 CG GLN C 77 4183 5598 4649 -716 -493 857 C ATOM 1682 CD GLN C 77 -25.849 8.197 -20.144 1.00 37.45 C ANISOU 1682 CD GLN C 77 4091 5555 4585 -664 -461 785 C ATOM 1683 OE1 GLN C 77 -26.979 7.896 -19.669 1.00 39.12 O ANISOU 1683 OE1 GLN C 77 4362 5722 4779 -648 -445 744 O ATOM 1684 NE2 GLN C 77 -25.045 7.309 -20.761 1.00 30.31 N ANISOU 1684 NE2 GLN C 77 3103 4705 3709 -637 -437 773 N ATOM 1685 N VAL C 78 -28.591 10.270 -21.299 1.00 37.39 N ANISOU 1685 N VAL C 78 4108 5579 4522 -638 -373 867 N ATOM 1686 CA VAL C 78 -29.759 10.791 -20.566 1.00 35.30 C ANISOU 1686 CA VAL C 78 3912 5221 4279 -613 -329 896 C ATOM 1687 C VAL C 78 -29.373 10.995 -19.088 1.00 36.84 C ANISOU 1687 C VAL C 78 4239 5275 4484 -638 -336 856 C ATOM 1688 O VAL C 78 -28.454 10.250 -18.577 1.00 35.17 O ANISOU 1688 O VAL C 78 4040 5064 4260 -671 -396 808 O ATOM 1689 CB VAL C 78 -30.991 9.844 -20.648 1.00 36.05 C ANISOU 1689 CB VAL C 78 3980 5354 4362 -585 -313 879 C ATOM 1690 CG1 VAL C 78 -31.532 9.711 -22.094 1.00 35.12 C ANISOU 1690 CG1 VAL C 78 3749 5390 4206 -600 -318 931 C ATOM 1691 CG2 VAL C 78 -30.624 8.411 -20.110 1.00 32.52 C ANISOU 1691 CG2 VAL C 78 3559 4896 3901 -592 -349 776 C ATOM 1692 N PRO C 79 -30.026 11.962 -18.411 1.00 37.27 N ANISOU 1692 N PRO C 79 4391 5211 4559 -629 -267 885 N ATOM 1693 CA PRO C 79 -29.716 12.229 -17.003 1.00 37.81 C ANISOU 1693 CA PRO C 79 4620 5144 4601 -681 -262 836 C ATOM 1694 C PRO C 79 -29.868 11.021 -16.115 1.00 37.84 C ANISOU 1694 C PRO C 79 4659 5144 4573 -684 -296 773 C ATOM 1695 O PRO C 79 -30.805 10.184 -16.255 1.00 36.32 O ANISOU 1695 O PRO C 79 4415 4990 4395 -623 -271 767 O ATOM 1696 CB PRO C 79 -30.716 13.323 -16.600 1.00 37.60 C ANISOU 1696 CB PRO C 79 4694 4983 4609 -643 -131 871 C ATOM 1697 CG PRO C 79 -31.015 14.015 -17.936 1.00 37.52 C ANISOU 1697 CG PRO C 79 4552 5043 4662 -594 -98 974 C ATOM 1698 CD PRO C 79 -31.110 12.854 -18.856 1.00 37.94 C ANISOU 1698 CD PRO C 79 4453 5270 4694 -573 -173 974 C ATOM 1699 N LEU C 80 -29.050 11.072 -15.071 1.00 36.40 N ANISOU 1699 N LEU C 80 4583 4902 4343 -772 -349 742 N ATOM 1700 CA LEU C 80 -29.140 10.142 -13.995 1.00 38.17 C ANISOU 1700 CA LEU C 80 4866 5106 4530 -796 -380 702 C ATOM 1701 C LEU C 80 -30.507 10.186 -13.298 1.00 38.55 C ANISOU 1701 C LEU C 80 5011 5068 4568 -743 -269 680 C ATOM 1702 O LEU C 80 -31.076 11.281 -13.020 1.00 38.80 O ANISOU 1702 O LEU C 80 5156 4990 4596 -735 -159 684 O ATOM 1703 CB LEU C 80 -28.039 10.474 -12.925 1.00 39.91 C ANISOU 1703 CB LEU C 80 5203 5283 4679 -937 -462 700 C ATOM 1704 CG LEU C 80 -28.019 9.723 -11.613 1.00 38.79 C ANISOU 1704 CG LEU C 80 5147 5120 4472 -1000 -507 681 C ATOM 1705 CD1 LEU C 80 -27.727 8.255 -11.804 1.00 37.69 C ANISOU 1705 CD1 LEU C 80 4854 5076 4389 -951 -577 708 C ATOM 1706 CD2 LEU C 80 -26.925 10.489 -10.721 1.00 40.49 C ANISOU 1706 CD2 LEU C 80 5495 5298 4589 -1186 -594 698 C ATOM 1707 N ARG C 81 -30.999 8.994 -12.997 1.00 37.98 N ANISOU 1707 N ARG C 81 4895 5033 4502 -705 -286 666 N ATOM 1708 CA ARG C 81 -32.179 8.880 -12.144 1.00 40.39 C ANISOU 1708 CA ARG C 81 5289 5264 4794 -666 -190 657 C ATOM 1709 C ARG C 81 -32.151 7.595 -11.341 1.00 41.25 C ANISOU 1709 C ARG C 81 5395 5399 4879 -685 -252 638 C ATOM 1710 O ARG C 81 -31.545 6.597 -11.768 1.00 41.19 O ANISOU 1710 O ARG C 81 5272 5473 4905 -687 -345 640 O ATOM 1711 CB ARG C 81 -33.436 9.058 -13.019 1.00 41.43 C ANISOU 1711 CB ARG C 81 5325 5416 5001 -558 -97 712 C ATOM 1712 CG ARG C 81 -33.586 8.026 -14.171 1.00 36.76 C ANISOU 1712 CG ARG C 81 4554 4959 4453 -525 -169 729 C ATOM 1713 CD ARG C 81 -34.966 8.158 -14.883 1.00 38.58 C ANISOU 1713 CD ARG C 81 4691 5228 4741 -453 -96 813 C ATOM 1714 NE ARG C 81 -34.982 7.393 -16.122 1.00 37.50 N ANISOU 1714 NE ARG C 81 4413 5225 4610 -465 -172 821 N ATOM 1715 CZ ARG C 81 -36.062 7.216 -16.893 1.00 37.78 C ANISOU 1715 CZ ARG C 81 4341 5340 4673 -445 -158 902 C ATOM 1716 NH1 ARG C 81 -37.249 7.770 -16.559 1.00 37.22 N ANISOU 1716 NH1 ARG C 81 4259 5228 4657 -388 -64 1010 N ATOM 1717 NH2 ARG C 81 -35.949 6.493 -17.974 1.00 37.83 N ANISOU 1717 NH2 ARG C 81 4257 5466 4652 -492 -232 884 N ATOM 1718 N PRO C 82 -32.730 7.605 -10.133 1.00 44.89 N ANISOU 1718 N PRO C 82 5990 5784 5283 -703 -190 622 N ATOM 1719 CA PRO C 82 -32.544 6.416 -9.292 1.00 44.14 C ANISOU 1719 CA PRO C 82 5891 5721 5160 -739 -264 622 C ATOM 1720 C PRO C 82 -33.614 5.317 -9.630 1.00 42.21 C ANISOU 1720 C PRO C 82 5529 5515 4994 -642 -237 643 C ATOM 1721 O PRO C 82 -34.694 5.686 -10.056 1.00 41.58 O ANISOU 1721 O PRO C 82 5426 5418 4955 -567 -139 666 O ATOM 1722 CB PRO C 82 -32.866 6.926 -7.897 1.00 46.58 C ANISOU 1722 CB PRO C 82 6403 5937 5357 -805 -191 597 C ATOM 1723 CG PRO C 82 -33.857 7.988 -8.108 1.00 46.28 C ANISOU 1723 CG PRO C 82 6438 5806 5340 -731 -21 589 C ATOM 1724 CD PRO C 82 -33.455 8.689 -9.433 1.00 45.91 C ANISOU 1724 CD PRO C 82 6289 5787 5367 -699 -39 607 C ATOM 1725 N MET C 83 -33.246 4.055 -9.529 1.00 43.18 N ANISOU 1725 N MET C 83 5569 5689 5149 -652 -325 652 N ATOM 1726 CA MET C 83 -34.182 2.943 -9.657 1.00 45.76 C ANISOU 1726 CA MET C 83 5813 6036 5539 -592 -310 668 C ATOM 1727 C MET C 83 -35.378 3.072 -8.697 1.00 46.56 C ANISOU 1727 C MET C 83 6000 6083 5607 -566 -212 693 C ATOM 1728 O MET C 83 -35.238 3.543 -7.577 1.00 48.28 O ANISOU 1728 O MET C 83 6360 6250 5737 -616 -179 685 O ATOM 1729 CB MET C 83 -33.505 1.625 -9.489 1.00 45.85 C ANISOU 1729 CB MET C 83 5750 6075 5597 -613 -401 676 C ATOM 1730 CG MET C 83 -34.396 0.327 -9.949 1.00 45.03 C ANISOU 1730 CG MET C 83 5546 5983 5580 -562 -392 678 C ATOM 1731 SD MET C 83 -35.099 0.408 -11.513 1.00 46.72 S ANISOU 1731 SD MET C 83 5672 6246 5834 -526 -362 652 S ATOM 1732 CE MET C 83 -33.577 0.551 -12.548 1.00 43.88 C ANISOU 1732 CE MET C 83 5262 5921 5487 -544 -410 606 C ATOM 1733 N THR C 84 -36.546 2.727 -9.231 1.00 45.15 N ANISOU 1733 N THR C 84 5736 5923 5495 -497 -160 728 N ATOM 1734 CA THR C 84 -37.817 2.567 -8.499 1.00 44.13 C ANISOU 1734 CA THR C 84 5633 5762 5373 -452 -63 783 C ATOM 1735 C THR C 84 -38.437 1.203 -8.829 1.00 43.63 C ANISOU 1735 C THR C 84 5443 5749 5386 -439 -118 816 C ATOM 1736 O THR C 84 -38.068 0.531 -9.810 1.00 40.22 O ANISOU 1736 O THR C 84 4914 5368 5002 -458 -202 788 O ATOM 1737 CB THR C 84 -38.858 3.636 -8.895 1.00 45.85 C ANISOU 1737 CB THR C 84 5845 5952 5624 -378 73 843 C ATOM 1738 OG1 THR C 84 -39.222 3.444 -10.265 1.00 43.51 O ANISOU 1738 OG1 THR C 84 5391 5739 5403 -358 26 884 O ATOM 1739 CG2 THR C 84 -38.330 5.138 -8.641 1.00 46.83 C ANISOU 1739 CG2 THR C 84 6115 5992 5688 -388 160 805 C ATOM 1740 N TYR C 85 -39.418 0.793 -7.982 1.00 44.00 N ANISOU 1740 N TYR C 85 5503 5773 5440 -413 -56 876 N ATOM 1741 CA TYR C 85 -40.227 -0.405 -8.256 1.00 41.62 C ANISOU 1741 CA TYR C 85 5086 5511 5217 -409 -95 927 C ATOM 1742 C TYR C 85 -40.777 -0.352 -9.670 1.00 40.39 C ANISOU 1742 C TYR C 85 4806 5421 5119 -405 -118 955 C ATOM 1743 O TYR C 85 -40.648 -1.267 -10.422 1.00 38.42 O ANISOU 1743 O TYR C 85 4484 5210 4904 -452 -204 924 O ATOM 1744 CB TYR C 85 -41.384 -0.533 -7.213 1.00 44.74 C ANISOU 1744 CB TYR C 85 5504 5879 5617 -368 5 1017 C ATOM 1745 CG TYR C 85 -42.352 -1.555 -7.614 1.00 41.91 C ANISOU 1745 CG TYR C 85 5014 5565 5345 -371 -31 1092 C ATOM 1746 CD1 TYR C 85 -42.182 -2.891 -7.287 1.00 44.92 C ANISOU 1746 CD1 TYR C 85 5365 5943 5759 -416 -116 1081 C ATOM 1747 CD2 TYR C 85 -43.460 -1.182 -8.367 1.00 44.81 C ANISOU 1747 CD2 TYR C 85 5275 5979 5772 -339 16 1193 C ATOM 1748 CE1 TYR C 85 -43.125 -3.868 -7.701 1.00 45.64 C ANISOU 1748 CE1 TYR C 85 5344 6066 5933 -441 -154 1149 C ATOM 1749 CE2 TYR C 85 -44.399 -2.151 -8.793 1.00 47.59 C ANISOU 1749 CE2 TYR C 85 5498 6386 6196 -375 -40 1278 C ATOM 1750 CZ TYR C 85 -44.215 -3.495 -8.461 1.00 46.66 C ANISOU 1750 CZ TYR C 85 5374 6253 6101 -432 -125 1242 C ATOM 1751 OH TYR C 85 -45.143 -4.459 -8.913 1.00 45.09 O ANISOU 1751 OH TYR C 85 5062 6098 5971 -491 -185 1320 O ATOM 1752 N LYS C 86 -41.407 0.738 -9.998 1.00 39.53 N ANISOU 1752 N LYS C 86 4682 5320 5018 -357 -30 1022 N ATOM 1753 CA LYS C 86 -42.150 0.892 -11.232 1.00 42.75 C ANISOU 1753 CA LYS C 86 4957 5812 5475 -362 -48 1102 C ATOM 1754 C LYS C 86 -41.243 0.870 -12.470 1.00 41.87 C ANISOU 1754 C LYS C 86 4815 5759 5336 -422 -147 1017 C ATOM 1755 O LYS C 86 -41.588 0.262 -13.484 1.00 40.33 O ANISOU 1755 O LYS C 86 4527 5646 5150 -486 -221 1030 O ATOM 1756 CB LYS C 86 -42.963 2.186 -11.210 1.00 44.15 C ANISOU 1756 CB LYS C 86 5115 5971 5687 -280 90 1225 C ATOM 1757 CG LYS C 86 -43.801 2.437 -12.427 1.00 49.13 C ANISOU 1757 CG LYS C 86 5582 6707 6376 -290 68 1361 C ATOM 1758 CD LYS C 86 -44.712 1.218 -12.810 1.00 55.38 C ANISOU 1758 CD LYS C 86 6247 7592 7203 -363 -26 1440 C ATOM 1759 CE LYS C 86 -45.890 1.673 -13.681 1.00 59.81 C ANISOU 1759 CE LYS C 86 6633 8263 7831 -369 -17 1653 C ATOM 1760 NZ LYS C 86 -45.489 2.174 -14.981 1.00 57.66 N ANISOU 1760 NZ LYS C 86 6304 8082 7521 -428 -91 1652 N ATOM 1761 N ALA C 87 -40.066 1.473 -12.365 1.00 40.17 N ANISOU 1761 N ALA C 87 4685 5503 5074 -417 -148 928 N ATOM 1762 CA ALA C 87 -39.103 1.470 -13.512 1.00 39.77 C ANISOU 1762 CA ALA C 87 4606 5507 4999 -465 -225 851 C ATOM 1763 C ALA C 87 -38.541 0.058 -13.634 1.00 38.56 C ANISOU 1763 C ALA C 87 4444 5351 4854 -517 -304 763 C ATOM 1764 O ALA C 87 -38.401 -0.460 -14.715 1.00 37.41 O ANISOU 1764 O ALA C 87 4250 5261 4702 -570 -350 720 O ATOM 1765 CB ALA C 87 -38.001 2.541 -13.225 1.00 38.51 C ANISOU 1765 CB ALA C 87 4535 5298 4800 -447 -200 804 C ATOM 1766 N ALA C 88 -38.279 -0.604 -12.508 1.00 38.23 N ANISOU 1766 N ALA C 88 4456 5242 4829 -507 -307 745 N ATOM 1767 CA ALA C 88 -37.780 -1.965 -12.580 1.00 39.69 C ANISOU 1767 CA ALA C 88 4624 5402 5054 -542 -361 684 C ATOM 1768 C ALA C 88 -38.792 -2.949 -13.241 1.00 40.64 C ANISOU 1768 C ALA C 88 4682 5552 5206 -594 -384 694 C ATOM 1769 O ALA C 88 -38.425 -3.896 -13.999 1.00 40.00 O ANISOU 1769 O ALA C 88 4591 5461 5145 -647 -413 615 O ATOM 1770 CB ALA C 88 -37.413 -2.492 -11.189 1.00 40.05 C ANISOU 1770 CB ALA C 88 4720 5379 5119 -527 -366 701 C ATOM 1771 N LEU C 89 -40.038 -2.746 -12.915 1.00 40.49 N ANISOU 1771 N LEU C 89 4629 5559 5195 -585 -360 793 N ATOM 1772 CA LEU C 89 -41.122 -3.591 -13.444 1.00 42.01 C ANISOU 1772 CA LEU C 89 4754 5795 5414 -657 -397 837 C ATOM 1773 C LEU C 89 -41.263 -3.329 -14.969 1.00 42.61 C ANISOU 1773 C LEU C 89 4781 5970 5438 -737 -438 820 C ATOM 1774 O LEU C 89 -41.364 -4.262 -15.773 1.00 43.58 O ANISOU 1774 O LEU C 89 4901 6111 5546 -842 -489 759 O ATOM 1775 CB LEU C 89 -42.434 -3.242 -12.711 1.00 41.77 C ANISOU 1775 CB LEU C 89 4674 5783 5414 -616 -350 989 C ATOM 1776 CG LEU C 89 -43.759 -3.930 -13.180 1.00 48.19 C ANISOU 1776 CG LEU C 89 5385 6663 6260 -699 -396 1093 C ATOM 1777 CD1 LEU C 89 -43.680 -5.455 -13.002 1.00 44.30 C ANISOU 1777 CD1 LEU C 89 4917 6112 5804 -773 -453 1023 C ATOM 1778 CD2 LEU C 89 -45.104 -3.317 -12.540 1.00 47.15 C ANISOU 1778 CD2 LEU C 89 5171 6566 6177 -633 -322 1294 C ATOM 1779 N ASP C 90 -41.294 -2.054 -15.358 1.00 41.70 N ANISOU 1779 N ASP C 90 4639 5915 5291 -699 -411 879 N ATOM 1780 CA ASP C 90 -41.396 -1.675 -16.773 1.00 43.72 C ANISOU 1780 CA ASP C 90 4841 6285 5486 -778 -453 890 C ATOM 1781 C ASP C 90 -40.178 -2.163 -17.586 1.00 42.75 C ANISOU 1781 C ASP C 90 4782 6151 5311 -830 -477 723 C ATOM 1782 O ASP C 90 -40.354 -2.664 -18.652 1.00 42.75 O ANISOU 1782 O ASP C 90 4774 6219 5250 -946 -521 682 O ATOM 1783 CB ASP C 90 -41.464 -0.153 -16.907 1.00 42.80 C ANISOU 1783 CB ASP C 90 4686 6210 5367 -705 -402 990 C ATOM 1784 CG ASP C 90 -42.752 0.443 -16.358 1.00 50.93 C ANISOU 1784 CG ASP C 90 5635 7255 6462 -646 -345 1180 C ATOM 1785 OD1 ASP C 90 -43.763 -0.295 -16.171 1.00 50.48 O ANISOU 1785 OD1 ASP C 90 5516 7225 6438 -690 -371 1264 O ATOM 1786 OD2 ASP C 90 -42.748 1.708 -16.169 1.00 55.03 O ANISOU 1786 OD2 ASP C 90 6150 7753 7007 -556 -260 1255 O ATOM 1787 N ILE C 91 -38.962 -2.103 -17.015 1.00 42.09 N ANISOU 1787 N ILE C 91 4765 5977 5251 -754 -441 635 N ATOM 1788 CA ILE C 91 -37.780 -2.620 -17.669 1.00 41.92 C ANISOU 1788 CA ILE C 91 4789 5928 5210 -779 -436 502 C ATOM 1789 C ILE C 91 -37.873 -4.142 -17.801 1.00 43.56 C ANISOU 1789 C ILE C 91 5033 6070 5447 -847 -439 415 C ATOM 1790 O ILE C 91 -37.642 -4.678 -18.901 1.00 42.61 O ANISOU 1790 O ILE C 91 4945 5970 5274 -934 -432 318 O ATOM 1791 CB ILE C 91 -36.500 -2.201 -16.975 1.00 41.61 C ANISOU 1791 CB ILE C 91 4783 5819 5207 -689 -406 474 C ATOM 1792 CG1 ILE C 91 -36.271 -0.696 -17.142 1.00 40.18 C ANISOU 1792 CG1 ILE C 91 4588 5694 4986 -651 -397 531 C ATOM 1793 CG2 ILE C 91 -35.243 -3.002 -17.581 1.00 40.01 C ANISOU 1793 CG2 ILE C 91 4608 5570 5026 -698 -377 357 C ATOM 1794 CD1 ILE C 91 -35.280 -0.145 -16.078 1.00 39.62 C ANISOU 1794 CD1 ILE C 91 4562 5551 4942 -586 -384 538 C ATOM 1795 N SER C 92 -38.397 -4.817 -16.752 1.00 43.33 N ANISOU 1795 N SER C 92 5003 5969 5490 -825 -445 456 N ATOM 1796 CA SER C 92 -38.620 -6.290 -16.828 1.00 42.47 C ANISOU 1796 CA SER C 92 4930 5781 5428 -896 -446 388 C ATOM 1797 C SER C 92 -39.514 -6.628 -17.977 1.00 43.15 C ANISOU 1797 C SER C 92 5017 5948 5431 -1048 -488 367 C ATOM 1798 O SER C 92 -39.213 -7.518 -18.736 1.00 44.96 O ANISOU 1798 O SER C 92 5317 6129 5637 -1138 -465 243 O ATOM 1799 CB SER C 92 -39.293 -6.837 -15.543 1.00 42.54 C ANISOU 1799 CB SER C 92 4918 5726 5519 -862 -458 473 C ATOM 1800 OG SER C 92 -38.548 -6.610 -14.379 1.00 41.88 O ANISOU 1800 OG SER C 92 4842 5580 5491 -752 -433 505 O ATOM 1801 N HIS C 93 -40.638 -5.952 -18.075 1.00 43.24 N ANISOU 1801 N HIS C 93 4951 6077 5399 -1087 -543 500 N ATOM 1802 CA HIS C 93 -41.558 -6.149 -19.180 1.00 45.92 C ANISOU 1802 CA HIS C 93 5269 6534 5646 -1259 -612 526 C ATOM 1803 C HIS C 93 -41.003 -5.836 -20.552 1.00 46.77 C ANISOU 1803 C HIS C 93 5417 6724 5629 -1349 -614 435 C ATOM 1804 O HIS C 93 -41.250 -6.568 -21.511 1.00 46.46 O ANISOU 1804 O HIS C 93 5439 6717 5495 -1524 -645 353 O ATOM 1805 CB HIS C 93 -42.875 -5.415 -18.938 1.00 47.35 C ANISOU 1805 CB HIS C 93 5322 6833 5836 -1264 -664 741 C ATOM 1806 CG HIS C 93 -43.709 -6.017 -17.824 1.00 52.50 C ANISOU 1806 CG HIS C 93 5936 7424 6587 -1234 -668 835 C ATOM 1807 ND1 HIS C 93 -44.430 -5.253 -16.938 1.00 58.08 N ANISOU 1807 ND1 HIS C 93 6553 8156 7361 -1123 -637 1010 N ATOM 1808 CD2 HIS C 93 -43.961 -7.314 -17.494 1.00 58.25 C ANISOU 1808 CD2 HIS C 93 6708 8064 7361 -1306 -687 783 C ATOM 1809 CE1 HIS C 93 -45.097 -6.051 -16.109 1.00 59.71 C ANISOU 1809 CE1 HIS C 93 6741 8308 7640 -1127 -642 1067 C ATOM 1810 NE2 HIS C 93 -44.812 -7.305 -16.415 1.00 57.92 N ANISOU 1810 NE2 HIS C 93 6590 8012 7406 -1238 -681 934 N ATOM 1811 N PHE C 94 -40.288 -4.729 -20.670 1.00 46.30 N ANISOU 1811 N PHE C 94 5333 6705 5555 -1247 -581 452 N ATOM 1812 CA PHE C 94 -39.640 -4.384 -21.945 1.00 47.16 C ANISOU 1812 CA PHE C 94 5478 6896 5547 -1317 -571 370 C ATOM 1813 C PHE C 94 -38.708 -5.519 -22.371 1.00 48.99 C ANISOU 1813 C PHE C 94 5841 7009 5763 -1360 -497 164 C ATOM 1814 O PHE C 94 -38.760 -5.978 -23.517 1.00 49.24 O ANISOU 1814 O PHE C 94 5947 7092 5668 -1519 -497 67 O ATOM 1815 CB PHE C 94 -38.830 -3.124 -21.812 1.00 47.55 C ANISOU 1815 CB PHE C 94 5486 6965 5614 -1181 -534 412 C ATOM 1816 CG PHE C 94 -38.125 -2.728 -23.095 1.00 49.69 C ANISOU 1816 CG PHE C 94 5784 7327 5769 -1244 -518 343 C ATOM 1817 CD1 PHE C 94 -38.810 -2.144 -24.096 1.00 55.12 C ANISOU 1817 CD1 PHE C 94 6413 8187 6342 -1362 -583 437 C ATOM 1818 CD2 PHE C 94 -36.786 -2.944 -23.258 1.00 49.21 C ANISOU 1818 CD2 PHE C 94 5791 7184 5721 -1182 -434 210 C ATOM 1819 CE1 PHE C 94 -38.160 -1.791 -25.276 1.00 58.97 C ANISOU 1819 CE1 PHE C 94 6928 8769 6709 -1429 -567 379 C ATOM 1820 CE2 PHE C 94 -36.189 -2.596 -24.454 1.00 52.99 C ANISOU 1820 CE2 PHE C 94 6293 7752 6087 -1241 -407 154 C ATOM 1821 CZ PHE C 94 -36.881 -2.046 -25.422 1.00 52.23 C ANISOU 1821 CZ PHE C 94 6155 7826 5861 -1366 -474 230 C ATOM 1822 N LEU C 95 -37.902 -6.018 -21.460 1.00 46.75 N ANISOU 1822 N LEU C 95 5590 6567 5607 -1230 -425 105 N ATOM 1823 CA LEU C 95 -36.968 -7.062 -21.786 1.00 49.05 C ANISOU 1823 CA LEU C 95 5987 6723 5927 -1236 -322 -62 C ATOM 1824 C LEU C 95 -37.589 -8.427 -22.037 1.00 52.08 C ANISOU 1824 C LEU C 95 6464 7020 6302 -1377 -312 -157 C ATOM 1825 O LEU C 95 -37.136 -9.153 -22.952 1.00 53.75 O ANISOU 1825 O LEU C 95 6800 7169 6454 -1469 -224 -318 O ATOM 1826 CB LEU C 95 -35.860 -7.152 -20.766 1.00 48.64 C ANISOU 1826 CB LEU C 95 5914 6539 6029 -1057 -253 -56 C ATOM 1827 CG LEU C 95 -35.033 -5.914 -20.595 1.00 47.76 C ANISOU 1827 CG LEU C 95 5737 6489 5919 -944 -253 12 C ATOM 1828 CD1 LEU C 95 -34.068 -6.091 -19.351 1.00 47.22 C ANISOU 1828 CD1 LEU C 95 5637 6302 6004 -799 -219 57 C ATOM 1829 CD2 LEU C 95 -34.294 -5.573 -21.948 1.00 50.99 C ANISOU 1829 CD2 LEU C 95 6182 6965 6226 -987 -193 -76 C ATOM 1830 N LYS C 96 -38.681 -8.749 -21.313 1.00 52.28 N ANISOU 1830 N LYS C 96 6444 7046 6375 -1414 -395 -59 N ATOM 1831 CA LYS C 96 -39.408 -9.998 -21.547 1.00 53.68 C ANISOU 1831 CA LYS C 96 6706 7151 6540 -1577 -407 -129 C ATOM 1832 C LYS C 96 -39.936 -9.919 -22.973 1.00 56.50 C ANISOU 1832 C LYS C 96 7126 7646 6693 -1804 -459 -186 C ATOM 1833 O LYS C 96 -39.766 -10.837 -23.737 1.00 57.88 O ANISOU 1833 O LYS C 96 7452 7741 6798 -1947 -397 -353 O ATOM 1834 CB LYS C 96 -40.601 -10.150 -20.578 1.00 53.17 C ANISOU 1834 CB LYS C 96 6548 7106 6547 -1585 -505 28 C ATOM 1835 CG LYS C 96 -41.488 -11.451 -20.818 1.00 57.31 C ANISOU 1835 CG LYS C 96 7151 7565 7060 -1785 -543 -22 C ATOM 1836 CD LYS C 96 -42.756 -11.381 -19.945 1.00 57.87 C ANISOU 1836 CD LYS C 96 7095 7702 7191 -1794 -650 178 C ATOM 1837 CE LYS C 96 -43.883 -12.363 -20.364 1.00 63.27 C ANISOU 1837 CE LYS C 96 7819 8395 7826 -2039 -736 184 C ATOM 1838 NZ LYS C 96 -43.432 -13.559 -21.011 1.00 67.98 N ANISOU 1838 NZ LYS C 96 8602 8833 8395 -2176 -664 -33 N ATOM 1839 N GLU C 97 -40.573 -8.809 -23.323 1.00 57.57 N ANISOU 1839 N GLU C 97 7152 7988 6733 -1843 -566 -38 N ATOM 1840 CA GLU C 97 -41.198 -8.693 -24.650 1.00 61.87 C ANISOU 1840 CA GLU C 97 7732 8705 7072 -2087 -647 -43 C ATOM 1841 C GLU C 97 -40.217 -8.621 -25.797 1.00 62.97 C ANISOU 1841 C GLU C 97 7994 8857 7074 -2142 -556 -213 C ATOM 1842 O GLU C 97 -40.465 -9.196 -26.832 1.00 64.36 O ANISOU 1842 O GLU C 97 8300 9075 7080 -2374 -566 -325 O ATOM 1843 CB GLU C 97 -42.191 -7.542 -24.676 1.00 62.15 C ANISOU 1843 CB GLU C 97 7586 8957 7072 -2105 -781 207 C ATOM 1844 CG GLU C 97 -43.311 -7.810 -23.631 1.00 67.67 C ANISOU 1844 CG GLU C 97 8176 9638 7896 -2083 -853 374 C ATOM 1845 CD GLU C 97 -44.324 -8.976 -24.065 1.00 75.59 C ANISOU 1845 CD GLU C 97 9240 10660 8822 -2357 -948 360 C ATOM 1846 OE1 GLU C 97 -44.924 -8.854 -25.152 1.00 84.21 O ANISOU 1846 OE1 GLU C 97 10328 11927 9739 -2592 -1052 409 O ATOM 1847 OE2 GLU C 97 -44.532 -9.985 -23.323 1.00 75.55 O ANISOU 1847 OE2 GLU C 97 9282 10501 8923 -2353 -927 313 O ATOM 1848 N LYS C 98 -39.092 -7.929 -25.616 1.00 62.30 N ANISOU 1848 N LYS C 98 7879 8738 7053 -1942 -464 -233 N ATOM 1849 CA LYS C 98 -38.040 -7.922 -26.625 1.00 65.61 C ANISOU 1849 CA LYS C 98 8411 9150 7368 -1964 -347 -393 C ATOM 1850 C LYS C 98 -37.399 -9.304 -26.897 1.00 67.38 C ANISOU 1850 C LYS C 98 8832 9161 7609 -2010 -184 -627 C ATOM 1851 O LYS C 98 -36.941 -9.574 -28.003 1.00 70.08 O ANISOU 1851 O LYS C 98 9318 9509 7802 -2128 -88 -783 O ATOM 1852 CB LYS C 98 -36.932 -6.940 -26.241 1.00 65.05 C ANISOU 1852 CB LYS C 98 8250 9072 7395 -1732 -283 -342 C ATOM 1853 CG LYS C 98 -35.695 -7.053 -27.148 1.00 70.44 C ANISOU 1853 CG LYS C 98 9039 9715 8012 -1718 -129 -501 C ATOM 1854 CD LYS C 98 -34.657 -5.986 -26.845 1.00 76.27 C ANISOU 1854 CD LYS C 98 9667 10476 8835 -1517 -93 -420 C ATOM 1855 CE LYS C 98 -34.444 -5.058 -28.035 1.00 79.09 C ANISOU 1855 CE LYS C 98 10012 11019 9017 -1595 -106 -402 C ATOM 1856 NZ LYS C 98 -33.063 -4.640 -28.040 1.00 79.98 N ANISOU 1856 NZ LYS C 98 10101 11082 9207 -1433 12 -423 N ATOM 1857 N GLY C 99 -37.313 -10.153 -25.879 1.00 67.04 N ANISOU 1857 N GLY C 99 8798 8920 7753 -1906 -132 -647 N ATOM 1858 CA GLY C 99 -36.638 -11.429 -26.009 1.00 68.15 C ANISOU 1858 CA GLY C 99 9106 8825 7964 -1907 50 -843 C ATOM 1859 C GLY C 99 -35.126 -11.282 -25.886 1.00 67.49 C ANISOU 1859 C GLY C 99 9011 8627 8006 -1686 228 -889 C ATOM 1860 O GLY C 99 -34.547 -10.195 -26.026 1.00 67.02 O ANISOU 1860 O GLY C 99 8852 8691 7921 -1583 211 -811 O ATOM 1861 N GLY C 100 -34.462 -12.384 -25.614 1.00 68.31 N ANISOU 1861 N GLY C 100 9204 8487 8264 -1609 404 -997 N ATOM 1862 CA GLY C 100 -33.009 -12.366 -25.537 1.00 68.22 C ANISOU 1862 CA GLY C 100 9168 8359 8394 -1402 589 -1016 C ATOM 1863 C GLY C 100 -32.394 -12.533 -24.154 1.00 65.72 C ANISOU 1863 C GLY C 100 8705 7918 8348 -1174 605 -874 C ATOM 1864 O GLY C 100 -31.327 -13.140 -24.053 1.00 67.93 O ANISOU 1864 O GLY C 100 8997 8018 8794 -1038 797 -904 O ATOM 1865 N LEU C 101 -33.042 -12.013 -23.100 1.00 61.08 N ANISOU 1865 N LEU C 101 7980 7423 7805 -1135 417 -707 N ATOM 1866 CA LEU C 101 -32.599 -12.266 -21.749 1.00 57.56 C ANISOU 1866 CA LEU C 101 7416 6872 7583 -963 414 -572 C ATOM 1867 C LEU C 101 -33.117 -13.599 -21.242 1.00 59.85 C ANISOU 1867 C LEU C 101 7769 6975 7995 -1002 455 -607 C ATOM 1868 O LEU C 101 -32.381 -14.347 -20.598 1.00 58.06 O ANISOU 1868 O LEU C 101 7509 6571 7980 -872 568 -566 O ATOM 1869 CB LEU C 101 -33.024 -11.121 -20.839 1.00 55.45 C ANISOU 1869 CB LEU C 101 7003 6773 7292 -912 223 -395 C ATOM 1870 CG LEU C 101 -32.330 -11.025 -19.488 1.00 54.05 C ANISOU 1870 CG LEU C 101 6699 6542 7295 -745 204 -239 C ATOM 1871 CD1 LEU C 101 -30.813 -10.838 -19.677 1.00 48.42 C ANISOU 1871 CD1 LEU C 101 5936 5785 6676 -615 324 -218 C ATOM 1872 CD2 LEU C 101 -32.889 -9.908 -18.618 1.00 49.92 C ANISOU 1872 CD2 LEU C 101 6082 6171 6715 -727 35 -96 C ATOM 1873 N GLU C 102 -34.386 -13.923 -21.527 1.00 61.65 N ANISOU 1873 N GLU C 102 8078 7243 8102 -1188 361 -662 N ATOM 1874 CA GLU C 102 -34.948 -15.188 -21.088 1.00 62.83 C ANISOU 1874 CA GLU C 102 8294 7215 8363 -1248 390 -695 C ATOM 1875 C GLU C 102 -34.113 -16.294 -21.658 1.00 64.75 C ANISOU 1875 C GLU C 102 8682 7212 8709 -1230 635 -855 C ATOM 1876 O GLU C 102 -33.892 -16.341 -22.864 1.00 66.14 O ANISOU 1876 O GLU C 102 9004 7381 8743 -1333 744 -1026 O ATOM 1877 CB GLU C 102 -36.391 -15.361 -21.580 1.00 65.02 C ANISOU 1877 CB GLU C 102 8652 7585 8466 -1493 258 -741 C ATOM 1878 CG GLU C 102 -37.059 -16.662 -21.142 1.00 66.68 C ANISOU 1878 CG GLU C 102 8935 7617 8785 -1582 273 -769 C ATOM 1879 CD GLU C 102 -37.464 -16.681 -19.662 1.00 68.36 C ANISOU 1879 CD GLU C 102 8985 7832 9158 -1463 165 -568 C ATOM 1880 OE1 GLU C 102 -37.576 -15.600 -19.032 1.00 65.55 O ANISOU 1880 OE1 GLU C 102 8480 7651 8777 -1365 44 -412 O ATOM 1881 OE2 GLU C 102 -37.740 -17.779 -19.141 1.00 69.68 O ANISOU 1881 OE2 GLU C 102 9186 7824 9466 -1483 203 -566 O ATOM 1882 N GLY C 103 -33.642 -17.183 -20.803 1.00 63.69 N ANISOU 1882 N GLY C 103 8508 6871 8822 -1099 736 -795 N ATOM 1883 CA GLY C 103 -32.832 -18.286 -21.293 1.00 66.64 C ANISOU 1883 CA GLY C 103 9011 6971 9337 -1056 1007 -930 C ATOM 1884 C GLY C 103 -31.324 -18.095 -21.248 1.00 66.74 C ANISOU 1884 C GLY C 103 8932 6914 9513 -832 1182 -865 C ATOM 1885 O GLY C 103 -30.613 -19.081 -21.120 1.00 68.04 O ANISOU 1885 O GLY C 103 9123 6827 9903 -723 1401 -874 O ATOM 1886 N LEU C 104 -30.847 -16.838 -21.265 1.00 63.90 N ANISOU 1886 N LEU C 104 8446 6770 9064 -757 1084 -770 N ATOM 1887 CA LEU C 104 -29.422 -16.543 -21.370 1.00 63.31 C ANISOU 1887 CA LEU C 104 8278 6662 9116 -572 1236 -701 C ATOM 1888 C LEU C 104 -28.640 -17.051 -20.157 1.00 63.26 C ANISOU 1888 C LEU C 104 8098 6524 9414 -376 1282 -487 C ATOM 1889 O LEU C 104 -29.053 -16.875 -19.016 1.00 61.65 O ANISOU 1889 O LEU C 104 7771 6396 9258 -358 1097 -325 O ATOM 1890 CB LEU C 104 -29.267 -15.019 -21.500 1.00 61.72 C ANISOU 1890 CB LEU C 104 7970 6738 8745 -565 1069 -622 C ATOM 1891 CG LEU C 104 -27.919 -14.468 -21.935 1.00 62.87 C ANISOU 1891 CG LEU C 104 8038 6910 8941 -428 1198 -575 C ATOM 1892 CD1 LEU C 104 -27.564 -15.047 -23.362 1.00 66.93 C ANISOU 1892 CD1 LEU C 104 8749 7296 9386 -480 1464 -801 C ATOM 1893 CD2 LEU C 104 -27.898 -12.937 -21.889 1.00 59.02 C ANISOU 1893 CD2 LEU C 104 7439 6689 8296 -436 1000 -477 C ATOM 1894 N ILE C 105 -27.509 -17.698 -20.392 1.00 64.75 N ANISOU 1894 N ILE C 105 8272 6519 9812 -232 1539 -471 N ATOM 1895 CA ILE C 105 -26.623 -18.130 -19.308 1.00 65.33 C ANISOU 1895 CA ILE C 105 8145 6487 10191 -42 1588 -221 C ATOM 1896 C ILE C 105 -25.997 -16.868 -18.661 1.00 63.14 C ANISOU 1896 C ILE C 105 7653 6454 9883 35 1396 -2 C ATOM 1897 O ILE C 105 -25.506 -16.006 -19.350 1.00 62.41 O ANISOU 1897 O ILE C 105 7555 6488 9670 41 1406 -38 O ATOM 1898 CB ILE C 105 -25.483 -19.080 -19.837 1.00 68.23 C ANISOU 1898 CB ILE C 105 8531 6579 10812 112 1947 -232 C ATOM 1899 CG1 ILE C 105 -26.049 -20.438 -20.263 1.00 70.83 C ANISOU 1899 CG1 ILE C 105 9079 6619 11216 41 2153 -430 C ATOM 1900 CG2 ILE C 105 -24.393 -19.270 -18.798 1.00 69.12 C ANISOU 1900 CG2 ILE C 105 8380 6645 11238 317 1977 89 C ATOM 1901 CD1 ILE C 105 -24.964 -21.510 -20.580 1.00 72.01 C ANISOU 1901 CD1 ILE C 105 9242 6442 11677 219 2543 -413 C ATOM 1902 N TRP C 106 -26.032 -16.798 -17.338 1.00 62.55 N ANISOU 1902 N TRP C 106 7418 6439 9909 77 1225 220 N ATOM 1903 CA TRP C 106 -25.565 -15.687 -16.591 1.00 61.94 C ANISOU 1903 CA TRP C 106 7171 6578 9786 108 1029 417 C ATOM 1904 C TRP C 106 -24.038 -15.673 -16.483 1.00 64.38 C ANISOU 1904 C TRP C 106 7300 6854 10307 266 1148 622 C ATOM 1905 O TRP C 106 -23.395 -16.767 -16.400 1.00 66.15 O ANISOU 1905 O TRP C 106 7465 6864 10806 388 1356 713 O ATOM 1906 CB TRP C 106 -26.143 -15.781 -15.195 1.00 61.51 C ANISOU 1906 CB TRP C 106 7032 6578 9759 78 830 578 C ATOM 1907 CG TRP C 106 -25.692 -14.694 -14.329 1.00 62.44 C ANISOU 1907 CG TRP C 106 7007 6903 9814 83 631 773 C ATOM 1908 CD1 TRP C 106 -26.246 -13.481 -14.209 1.00 59.62 C ANISOU 1908 CD1 TRP C 106 6687 6748 9217 -12 444 731 C ATOM 1909 CD2 TRP C 106 -24.571 -14.736 -13.441 1.00 66.38 C ANISOU 1909 CD2 TRP C 106 7304 7420 10496 173 605 1054 C ATOM 1910 NE1 TRP C 106 -25.539 -12.720 -13.291 1.00 60.97 N ANISOU 1910 NE1 TRP C 106 6720 7056 9390 1 303 942 N ATOM 1911 CE2 TRP C 106 -24.490 -13.475 -12.819 1.00 64.72 C ANISOU 1911 CE2 TRP C 106 7041 7435 10114 104 385 1149 C ATOM 1912 CE3 TRP C 106 -23.617 -15.730 -13.122 1.00 73.69 C ANISOU 1912 CE3 TRP C 106 8084 8190 11724 302 752 1250 C ATOM 1913 CZ2 TRP C 106 -23.493 -13.151 -11.892 1.00 67.21 C ANISOU 1913 CZ2 TRP C 106 7175 7844 10517 127 282 1425 C ATOM 1914 CZ3 TRP C 106 -22.599 -15.413 -12.200 1.00 75.53 C ANISOU 1914 CZ3 TRP C 106 8101 8529 12069 344 648 1560 C ATOM 1915 CH2 TRP C 106 -22.566 -14.132 -11.580 1.00 74.70 C ANISOU 1915 CH2 TRP C 106 7960 8667 11753 240 401 1639 C ATOM 1916 N SER C 107 -23.454 -14.477 -16.496 1.00 61.78 N ANISOU 1916 N SER C 107 6878 6723 9874 266 1031 710 N ATOM 1917 CA SER C 107 -22.084 -14.330 -15.995 1.00 63.24 C ANISOU 1917 CA SER C 107 6839 6934 10255 386 1052 989 C ATOM 1918 C SER C 107 -21.954 -12.946 -15.404 1.00 61.88 C ANISOU 1918 C SER C 107 6585 7017 9910 306 789 1105 C ATOM 1919 O SER C 107 -22.827 -12.113 -15.648 1.00 57.92 O ANISOU 1919 O SER C 107 6210 6640 9156 192 656 942 O ATOM 1920 CB SER C 107 -21.095 -14.494 -17.122 1.00 65.03 C ANISOU 1920 CB SER C 107 7054 7066 10590 496 1316 951 C ATOM 1921 OG SER C 107 -21.125 -13.341 -17.960 1.00 62.97 O ANISOU 1921 OG SER C 107 6864 6973 10090 426 1256 818 O ATOM 1922 N GLN C 108 -20.839 -12.653 -14.707 1.00 62.85 N ANISOU 1922 N GLN C 108 6497 7216 10166 359 723 1390 N ATOM 1923 CA GLN C 108 -20.619 -11.311 -14.091 1.00 61.60 C ANISOU 1923 CA GLN C 108 6276 7291 9838 258 471 1506 C ATOM 1924 C GLN C 108 -20.530 -10.310 -15.190 1.00 60.10 C ANISOU 1924 C GLN C 108 6164 7192 9477 230 495 1347 C ATOM 1925 O GLN C 108 -21.055 -9.176 -15.126 1.00 57.12 O ANISOU 1925 O GLN C 108 5867 6966 8869 118 323 1267 O ATOM 1926 CB GLN C 108 -19.312 -11.206 -13.269 1.00 64.07 C ANISOU 1926 CB GLN C 108 6342 7677 10324 293 398 1859 C ATOM 1927 CG GLN C 108 -19.234 -9.865 -12.436 1.00 66.01 C ANISOU 1927 CG GLN C 108 6566 8153 10361 138 110 1963 C ATOM 1928 CD GLN C 108 -20.426 -9.728 -11.480 1.00 68.16 C ANISOU 1928 CD GLN C 108 6969 8472 10456 18 -64 1884 C ATOM 1929 OE1 GLN C 108 -20.915 -10.724 -10.966 1.00 76.55 O ANISOU 1929 OE1 GLN C 108 8035 9433 11619 47 -30 1907 O ATOM 1930 NE2 GLN C 108 -20.909 -8.506 -11.266 1.00 74.06 N ANISOU 1930 NE2 GLN C 108 7828 9361 10952 -111 -230 1792 N ATOM 1931 N ARG C 109 -19.801 -10.750 -16.199 1.00 62.22 N ANISOU 1931 N ARG C 109 6404 7358 9879 342 730 1319 N ATOM 1932 CA ARG C 109 -19.500 -9.943 -17.348 1.00 61.58 C ANISOU 1932 CA ARG C 109 6372 7353 9673 337 796 1200 C ATOM 1933 C ARG C 109 -20.789 -9.540 -18.070 1.00 57.10 C ANISOU 1933 C ARG C 109 6031 6825 8841 228 758 901 C ATOM 1934 O ARG C 109 -21.013 -8.398 -18.335 1.00 53.74 O ANISOU 1934 O ARG C 109 5642 6553 8224 146 630 850 O ATOM 1935 CB ARG C 109 -18.588 -10.738 -18.278 1.00 64.98 C ANISOU 1935 CB ARG C 109 6755 7629 10307 487 1106 1208 C ATOM 1936 CG ARG C 109 -18.115 -9.960 -19.497 1.00 71.83 C ANISOU 1936 CG ARG C 109 7654 8577 11061 494 1203 1113 C ATOM 1937 CD ARG C 109 -17.727 -8.480 -19.148 1.00 77.94 C ANISOU 1937 CD ARG C 109 8325 9587 11702 409 955 1251 C ATOM 1938 NE ARG C 109 -17.540 -7.649 -20.348 1.00 83.37 N ANISOU 1938 NE ARG C 109 9072 10366 12238 389 1020 1128 N ATOM 1939 CZ ARG C 109 -17.925 -6.369 -20.469 1.00 88.51 C ANISOU 1939 CZ ARG C 109 9772 11190 12665 271 828 1074 C ATOM 1940 NH1 ARG C 109 -18.547 -5.707 -19.459 1.00 88.65 N ANISOU 1940 NH1 ARG C 109 9808 11303 12572 158 568 1113 N ATOM 1941 NH2 ARG C 109 -17.714 -5.742 -21.626 1.00 89.05 N ANISOU 1941 NH2 ARG C 109 9885 11331 12620 264 912 977 N ATOM 1942 N ARG C 110 -21.662 -10.502 -18.321 1.00 55.66 N ANISOU 1942 N ARG C 110 5988 6502 8659 216 859 728 N ATOM 1943 CA ARG C 110 -22.897 -10.228 -19.020 1.00 54.38 C ANISOU 1943 CA ARG C 110 6019 6382 8259 97 818 478 C ATOM 1944 C ARG C 110 -23.806 -9.341 -18.181 1.00 50.64 C ANISOU 1944 C ARG C 110 5560 6060 7620 -11 554 505 C ATOM 1945 O ARG C 110 -24.490 -8.492 -18.743 1.00 50.55 O ANISOU 1945 O ARG C 110 5637 6166 7402 -100 475 386 O ATOM 1946 CB ARG C 110 -23.615 -11.540 -19.380 1.00 55.24 C ANISOU 1946 CB ARG C 110 6272 6299 8416 85 973 308 C ATOM 1947 CG ARG C 110 -23.219 -12.127 -20.688 1.00 61.66 C ANISOU 1947 CG ARG C 110 7194 6986 9247 120 1245 144 C ATOM 1948 CD ARG C 110 -23.530 -13.644 -20.713 1.00 68.24 C ANISOU 1948 CD ARG C 110 8133 7563 10232 143 1437 47 C ATOM 1949 NE ARG C 110 -23.152 -14.188 -22.001 1.00 74.20 N ANISOU 1949 NE ARG C 110 9031 8180 10982 162 1726 -137 N ATOM 1950 CZ ARG C 110 -23.543 -15.358 -22.485 1.00 80.43 C ANISOU 1950 CZ ARG C 110 10000 8747 11814 130 1930 -318 C ATOM 1951 NH1 ARG C 110 -24.338 -16.168 -21.794 1.00 79.09 N ANISOU 1951 NH1 ARG C 110 9875 8461 11714 83 1872 -330 N ATOM 1952 NH2 ARG C 110 -23.118 -15.714 -23.693 1.00 85.18 N ANISOU 1952 NH2 ARG C 110 10751 9236 12379 136 2206 -494 N ATOM 1953 N GLN C 111 -23.870 -9.572 -16.864 1.00 49.01 N ANISOU 1953 N GLN C 111 5274 5846 7503 -5 435 661 N ATOM 1954 CA GLN C 111 -24.707 -8.745 -15.953 1.00 48.44 C ANISOU 1954 CA GLN C 111 5228 5901 7276 -101 212 692 C ATOM 1955 C GLN C 111 -24.261 -7.291 -16.052 1.00 46.84 C ANISOU 1955 C GLN C 111 4992 5860 6944 -142 101 741 C ATOM 1956 O GLN C 111 -25.077 -6.362 -16.181 1.00 45.14 O ANISOU 1956 O GLN C 111 4861 5743 6546 -221 2 655 O ATOM 1957 CB GLN C 111 -24.615 -9.295 -14.485 1.00 49.49 C ANISOU 1957 CB GLN C 111 5273 6000 7533 -89 121 878 C ATOM 1958 CG GLN C 111 -25.352 -8.513 -13.360 1.00 52.99 C ANISOU 1958 CG GLN C 111 5750 6561 7825 -185 -83 929 C ATOM 1959 CD GLN C 111 -25.298 -9.292 -12.000 1.00 61.02 C ANISOU 1959 CD GLN C 111 6691 7535 8960 -181 -146 1104 C ATOM 1960 OE1 GLN C 111 -25.628 -10.480 -11.948 1.00 67.54 O ANISOU 1960 OE1 GLN C 111 7517 8229 9917 -137 -57 1091 O ATOM 1961 NE2 GLN C 111 -24.826 -8.646 -10.935 1.00 63.69 N ANISOU 1961 NE2 GLN C 111 6966 7981 9251 -239 -296 1275 N ATOM 1962 N GLU C 112 -22.935 -7.066 -16.055 1.00 47.85 N ANISOU 1962 N GLU C 112 4988 6012 7181 -85 128 893 N ATOM 1963 CA GLU C 112 -22.402 -5.706 -16.162 1.00 45.89 C ANISOU 1963 CA GLU C 112 4704 5908 6826 -133 25 953 C ATOM 1964 C GLU C 112 -22.703 -5.062 -17.524 1.00 46.40 C ANISOU 1964 C GLU C 112 4854 6023 6752 -150 93 781 C ATOM 1965 O GLU C 112 -22.983 -3.858 -17.619 1.00 41.97 O ANISOU 1965 O GLU C 112 4332 5574 6039 -221 -15 760 O ATOM 1966 CB GLU C 112 -20.879 -5.661 -15.736 1.00 49.31 C ANISOU 1966 CB GLU C 112 4948 6366 7421 -87 15 1202 C ATOM 1967 CG GLU C 112 -20.861 -5.854 -14.114 1.00 52.90 C ANISOU 1967 CG GLU C 112 5341 6842 7916 -147 -152 1390 C ATOM 1968 CD GLU C 112 -19.512 -5.601 -13.370 1.00 64.16 C ANISOU 1968 CD GLU C 112 6579 8346 9453 -169 -249 1682 C ATOM 1969 OE1 GLU C 112 -18.536 -5.113 -14.009 1.00 63.17 O ANISOU 1969 OE1 GLU C 112 6356 8271 9375 -142 -209 1762 O ATOM 1970 OE2 GLU C 112 -19.449 -5.953 -12.120 1.00 71.18 O ANISOU 1970 OE2 GLU C 112 7411 9252 10381 -224 -369 1850 O ATOM 1971 N ILE C 113 -22.694 -5.852 -18.605 1.00 47.56 N ANISOU 1971 N ILE C 113 5046 6085 6940 -95 281 655 N ATOM 1972 CA ILE C 113 -23.077 -5.312 -19.921 1.00 47.74 C ANISOU 1972 CA ILE C 113 5164 6172 6802 -138 340 490 C ATOM 1973 C ILE C 113 -24.557 -4.873 -19.927 1.00 44.98 C ANISOU 1973 C ILE C 113 4937 5886 6268 -245 222 368 C ATOM 1974 O ILE C 113 -24.932 -3.768 -20.364 1.00 41.63 O ANISOU 1974 O ILE C 113 4541 5583 5695 -306 143 341 O ATOM 1975 CB ILE C 113 -22.868 -6.404 -21.040 1.00 50.95 C ANISOU 1975 CB ILE C 113 5636 6458 7267 -85 583 354 C ATOM 1976 CG1 ILE C 113 -21.358 -6.532 -21.345 1.00 52.87 C ANISOU 1976 CG1 ILE C 113 5747 6666 7676 33 734 482 C ATOM 1977 CG2 ILE C 113 -23.719 -6.034 -22.318 1.00 50.81 C ANISOU 1977 CG2 ILE C 113 5764 6516 7024 -186 610 152 C ATOM 1978 CD1 ILE C 113 -20.834 -7.994 -21.746 1.00 55.33 C ANISOU 1978 CD1 ILE C 113 6071 6771 8181 146 1011 443 C ATOM 1979 N LEU C 114 -25.393 -5.698 -19.352 1.00 44.86 N ANISOU 1979 N LEU C 114 4976 5789 6280 -263 205 327 N ATOM 1980 CA LEU C 114 -26.819 -5.366 -19.252 1.00 42.68 C ANISOU 1980 CA LEU C 114 4790 5568 5858 -355 99 249 C ATOM 1981 C LEU C 114 -27.003 -4.126 -18.383 1.00 41.69 C ANISOU 1981 C LEU C 114 4632 5543 5665 -382 -61 356 C ATOM 1982 O LEU C 114 -27.717 -3.224 -18.771 1.00 42.76 O ANISOU 1982 O LEU C 114 4809 5771 5668 -438 -118 320 O ATOM 1983 CB LEU C 114 -27.586 -6.517 -18.631 1.00 43.24 C ANISOU 1983 CB LEU C 114 4905 5528 5997 -365 107 219 C ATOM 1984 CG LEU C 114 -29.075 -6.345 -18.366 1.00 43.15 C ANISOU 1984 CG LEU C 114 4961 5563 5870 -451 3 176 C ATOM 1985 CD1 LEU C 114 -29.753 -6.160 -19.757 1.00 44.83 C ANISOU 1985 CD1 LEU C 114 5256 5846 5932 -542 37 40 C ATOM 1986 CD2 LEU C 114 -29.668 -7.576 -17.616 1.00 45.89 C ANISOU 1986 CD2 LEU C 114 5331 5789 6316 -452 13 176 C ATOM 1987 N ASP C 115 -26.352 -4.040 -17.218 1.00 40.29 N ANISOU 1987 N ASP C 115 4385 5348 5574 -353 -127 495 N ATOM 1988 CA ASP C 115 -26.495 -2.873 -16.350 1.00 40.70 C ANISOU 1988 CA ASP C 115 4444 5477 5544 -401 -263 576 C ATOM 1989 C ASP C 115 -26.056 -1.553 -17.055 1.00 39.29 C ANISOU 1989 C ASP C 115 4256 5394 5278 -425 -284 581 C ATOM 1990 O ASP C 115 -26.719 -0.554 -16.940 1.00 38.26 O ANISOU 1990 O ASP C 115 4181 5316 5041 -471 -346 568 O ATOM 1991 CB ASP C 115 -25.567 -3.027 -15.152 1.00 44.48 C ANISOU 1991 CB ASP C 115 4847 5937 6118 -394 -328 736 C ATOM 1992 CG ASP C 115 -26.141 -3.929 -14.054 1.00 49.72 C ANISOU 1992 CG ASP C 115 5525 6534 6831 -397 -359 773 C ATOM 1993 OD1 ASP C 115 -27.332 -4.150 -13.998 1.00 64.92 O ANISOU 1993 OD1 ASP C 115 7530 8440 8699 -415 -357 686 O ATOM 1994 OD2 ASP C 115 -25.307 -4.448 -13.293 1.00 66.10 O ANISOU 1994 OD2 ASP C 115 7512 8585 9020 -380 -384 915 O ATOM 1995 N LEU C 116 -24.942 -1.592 -17.760 1.00 40.88 N ANISOU 1995 N LEU C 116 4383 5609 5541 -385 -218 612 N ATOM 1996 CA LEU C 116 -24.429 -0.390 -18.486 1.00 42.08 C ANISOU 1996 CA LEU C 116 4512 5854 5624 -407 -233 631 C ATOM 1997 C LEU C 116 -25.283 -0.038 -19.658 1.00 42.22 C ANISOU 1997 C LEU C 116 4593 5927 5523 -432 -189 510 C ATOM 1998 O LEU C 116 -25.504 1.120 -19.928 1.00 40.16 O ANISOU 1998 O LEU C 116 4346 5740 5174 -472 -241 525 O ATOM 1999 CB LEU C 116 -22.987 -0.646 -18.987 1.00 44.45 C ANISOU 1999 CB LEU C 116 4698 6156 6036 -348 -152 713 C ATOM 2000 CG LEU C 116 -21.918 -0.298 -18.024 1.00 48.27 C ANISOU 2000 CG LEU C 116 5082 6656 6601 -362 -244 896 C ATOM 2001 CD1 LEU C 116 -20.495 -0.594 -18.732 1.00 49.78 C ANISOU 2001 CD1 LEU C 116 5131 6856 6928 -286 -133 1000 C ATOM 2002 CD2 LEU C 116 -22.078 1.143 -17.474 1.00 43.80 C ANISOU 2002 CD2 LEU C 116 4567 6160 5916 -464 -391 937 C ATOM 2003 N TRP C 117 -25.867 -1.060 -20.331 1.00 42.44 N ANISOU 2003 N TRP C 117 4668 5915 5542 -426 -97 394 N ATOM 2004 CA TRP C 117 -26.774 -0.758 -21.441 1.00 42.84 C ANISOU 2004 CA TRP C 117 4779 6043 5455 -486 -80 296 C ATOM 2005 C TRP C 117 -28.041 -0.023 -20.950 1.00 40.12 C ANISOU 2005 C TRP C 117 4472 5742 5031 -538 -187 318 C ATOM 2006 O TRP C 117 -28.476 1.003 -21.490 1.00 38.55 O ANISOU 2006 O TRP C 117 4271 5635 4742 -575 -223 340 O ATOM 2007 CB TRP C 117 -27.136 -2.064 -22.182 1.00 46.61 C ANISOU 2007 CB TRP C 117 5322 6462 5925 -504 33 163 C ATOM 2008 CG TRP C 117 -28.272 -1.913 -23.199 1.00 46.63 C ANISOU 2008 CG TRP C 117 5396 6556 5765 -610 19 74 C ATOM 2009 CD1 TRP C 117 -28.369 -0.947 -24.187 1.00 52.50 C ANISOU 2009 CD1 TRP C 117 6129 7437 6383 -664 0 84 C ATOM 2010 CD2 TRP C 117 -29.368 -2.767 -23.375 1.00 49.17 C ANISOU 2010 CD2 TRP C 117 5796 6851 6034 -689 19 -14 C ATOM 2011 NE1 TRP C 117 -29.506 -1.135 -24.918 1.00 51.40 N ANISOU 2011 NE1 TRP C 117 6048 7370 6112 -777 -25 23 N ATOM 2012 CE2 TRP C 117 -30.130 -2.260 -24.475 1.00 52.58 C ANISOU 2012 CE2 TRP C 117 6257 7421 6298 -802 -14 -44 C ATOM 2013 CE3 TRP C 117 -29.787 -3.950 -22.760 1.00 54.97 C ANISOU 2013 CE3 TRP C 117 6576 7462 6848 -688 41 -62 C ATOM 2014 CZ2 TRP C 117 -31.303 -2.866 -24.918 1.00 53.18 C ANISOU 2014 CZ2 TRP C 117 6403 7526 6276 -929 -43 -109 C ATOM 2015 CZ3 TRP C 117 -30.999 -4.553 -23.195 1.00 56.83 C ANISOU 2015 CZ3 TRP C 117 6890 7712 6991 -808 18 -141 C ATOM 2016 CH2 TRP C 117 -31.728 -4.009 -24.269 1.00 57.40 C ANISOU 2016 CH2 TRP C 117 6987 7933 6888 -934 -28 -162 C ATOM 2017 N ILE C 118 -28.571 -0.468 -19.809 1.00 38.00 N ANISOU 2017 N ILE C 118 4226 5401 4811 -529 -232 339 N ATOM 2018 CA ILE C 118 -29.684 0.191 -19.190 1.00 36.09 C ANISOU 2018 CA ILE C 118 4016 5179 4517 -556 -304 377 C ATOM 2019 C ILE C 118 -29.346 1.578 -18.657 1.00 35.88 C ANISOU 2019 C ILE C 118 3985 5176 4470 -553 -356 461 C ATOM 2020 O ILE C 118 -30.164 2.503 -18.830 1.00 36.97 O ANISOU 2020 O ILE C 118 4141 5357 4550 -572 -371 488 O ATOM 2021 CB ILE C 118 -30.288 -0.690 -18.040 1.00 37.02 C ANISOU 2021 CB ILE C 118 4164 5212 4692 -546 -324 383 C ATOM 2022 CG1 ILE C 118 -30.909 -1.996 -18.653 1.00 39.73 C ANISOU 2022 CG1 ILE C 118 4529 5523 5043 -574 -274 291 C ATOM 2023 CG2 ILE C 118 -31.373 0.161 -17.212 1.00 37.04 C ANISOU 2023 CG2 ILE C 118 4202 5225 4646 -559 -375 441 C ATOM 2024 CD1 ILE C 118 -31.228 -3.027 -17.615 1.00 42.02 C ANISOU 2024 CD1 ILE C 118 4833 5716 5417 -557 -281 303 C ATOM 2025 N TYR C 119 -28.141 1.792 -18.091 1.00 36.03 N ANISOU 2025 N TYR C 119 3979 5169 4541 -539 -379 517 N ATOM 2026 CA TYR C 119 -27.702 3.121 -17.703 1.00 36.01 C ANISOU 2026 CA TYR C 119 3990 5184 4507 -566 -429 585 C ATOM 2027 C TYR C 119 -27.511 4.028 -18.984 1.00 35.79 C ANISOU 2027 C TYR C 119 3926 5240 4434 -573 -404 587 C ATOM 2028 O TYR C 119 -28.032 5.163 -19.030 1.00 36.76 O ANISOU 2028 O TYR C 119 4080 5378 4510 -593 -417 618 O ATOM 2029 CB TYR C 119 -26.371 3.120 -16.885 1.00 36.81 C ANISOU 2029 CB TYR C 119 4058 5262 4665 -583 -481 667 C ATOM 2030 CG TYR C 119 -25.800 4.492 -16.847 1.00 34.61 C ANISOU 2030 CG TYR C 119 3795 5011 4346 -635 -527 725 C ATOM 2031 CD1 TYR C 119 -26.466 5.541 -16.174 1.00 38.31 C ANISOU 2031 CD1 TYR C 119 4371 5442 4744 -683 -551 725 C ATOM 2032 CD2 TYR C 119 -24.602 4.816 -17.564 1.00 36.75 C ANISOU 2032 CD2 TYR C 119 3976 5336 4652 -637 -527 782 C ATOM 2033 CE1 TYR C 119 -26.003 6.792 -16.197 1.00 34.29 C ANISOU 2033 CE1 TYR C 119 3893 4934 4201 -737 -578 766 C ATOM 2034 CE2 TYR C 119 -24.125 6.088 -17.560 1.00 37.47 C ANISOU 2034 CE2 TYR C 119 4083 5448 4708 -697 -574 838 C ATOM 2035 CZ TYR C 119 -24.849 7.085 -16.922 1.00 36.49 C ANISOU 2035 CZ TYR C 119 4079 5273 4513 -749 -598 822 C ATOM 2036 OH TYR C 119 -24.446 8.429 -16.969 1.00 38.51 O ANISOU 2036 OH TYR C 119 4372 5524 4737 -816 -627 866 O ATOM 2037 N HIS C 120 -26.821 3.499 -20.010 1.00 36.81 N ANISOU 2037 N HIS C 120 3993 5414 4580 -554 -351 560 N ATOM 2038 CA HIS C 120 -26.564 4.300 -21.249 1.00 38.80 C ANISOU 2038 CA HIS C 120 4205 5759 4777 -568 -325 570 C ATOM 2039 C HIS C 120 -27.894 4.756 -21.874 1.00 41.59 C ANISOU 2039 C HIS C 120 4584 6172 5045 -599 -327 554 C ATOM 2040 O HIS C 120 -27.983 5.844 -22.387 1.00 41.02 O ANISOU 2040 O HIS C 120 4491 6160 4937 -617 -339 611 O ATOM 2041 CB HIS C 120 -25.749 3.492 -22.254 1.00 39.43 C ANISOU 2041 CB HIS C 120 4236 5872 4873 -542 -237 526 C ATOM 2042 CG HIS C 120 -24.284 3.367 -21.872 1.00 37.68 C ANISOU 2042 CG HIS C 120 3941 5619 4754 -504 -226 603 C ATOM 2043 ND1 HIS C 120 -23.513 2.269 -22.214 1.00 42.29 N ANISOU 2043 ND1 HIS C 120 4481 6168 5419 -447 -122 582 N ATOM 2044 CD2 HIS C 120 -23.479 4.186 -21.150 1.00 39.31 C ANISOU 2044 CD2 HIS C 120 4108 5823 5004 -522 -304 716 C ATOM 2045 CE1 HIS C 120 -22.289 2.422 -21.703 1.00 44.04 C ANISOU 2045 CE1 HIS C 120 4612 6378 5744 -421 -142 707 C ATOM 2046 NE2 HIS C 120 -22.237 3.581 -21.048 1.00 42.08 N ANISOU 2046 NE2 HIS C 120 4367 6158 5464 -480 -266 789 N ATOM 2047 N THR C 121 -28.898 3.862 -21.886 1.00 38.72 N ANISOU 2047 N THR C 121 4253 5799 4660 -611 -315 493 N ATOM 2048 CA THR C 121 -30.123 4.183 -22.616 1.00 39.95 C ANISOU 2048 CA THR C 121 4404 6038 4737 -657 -325 509 C ATOM 2049 C THR C 121 -31.156 4.958 -21.781 1.00 38.70 C ANISOU 2049 C THR C 121 4260 5844 4601 -643 -357 590 C ATOM 2050 O THR C 121 -31.842 5.888 -22.292 1.00 38.07 O ANISOU 2050 O THR C 121 4142 5829 4493 -657 -361 676 O ATOM 2051 CB THR C 121 -30.800 2.892 -23.166 1.00 42.62 C ANISOU 2051 CB THR C 121 4769 6398 5027 -709 -303 418 C ATOM 2052 OG1 THR C 121 -29.799 2.029 -23.776 1.00 43.85 O ANISOU 2052 OG1 THR C 121 4940 6539 5181 -707 -231 323 O ATOM 2053 CG2 THR C 121 -31.833 3.274 -24.192 1.00 41.24 C ANISOU 2053 CG2 THR C 121 4565 6354 4749 -791 -330 461 C ATOM 2054 N GLN C 122 -31.298 4.611 -20.490 1.00 37.40 N ANISOU 2054 N GLN C 122 4146 5573 4491 -611 -365 580 N ATOM 2055 CA GLN C 122 -32.360 5.096 -19.655 1.00 34.09 C ANISOU 2055 CA GLN C 122 3758 5104 4090 -591 -361 639 C ATOM 2056 C GLN C 122 -31.934 5.819 -18.419 1.00 35.85 C ANISOU 2056 C GLN C 122 4054 5224 4343 -567 -357 662 C ATOM 2057 O GLN C 122 -32.793 6.358 -17.752 1.00 35.20 O ANISOU 2057 O GLN C 122 4016 5087 4272 -546 -322 707 O ATOM 2058 CB GLN C 122 -33.321 3.930 -19.275 1.00 35.67 C ANISOU 2058 CB GLN C 122 3968 5285 4300 -598 -365 609 C ATOM 2059 CG GLN C 122 -34.014 3.356 -20.543 1.00 35.89 C ANISOU 2059 CG GLN C 122 3941 5424 4271 -662 -377 598 C ATOM 2060 CD GLN C 122 -34.864 4.351 -21.287 1.00 38.30 C ANISOU 2060 CD GLN C 122 4179 5827 4544 -684 -382 716 C ATOM 2061 OE1 GLN C 122 -35.257 5.425 -20.772 1.00 37.20 O ANISOU 2061 OE1 GLN C 122 4031 5651 4451 -631 -353 816 O ATOM 2062 NE2 GLN C 122 -35.124 4.005 -22.566 1.00 36.68 N ANISOU 2062 NE2 GLN C 122 3929 5750 4257 -772 -410 710 N ATOM 2063 N GLY C 123 -30.631 5.896 -18.094 1.00 36.86 N ANISOU 2063 N GLY C 123 4200 5324 4481 -581 -387 642 N ATOM 2064 CA GLY C 123 -30.173 6.738 -17.015 1.00 35.87 C ANISOU 2064 CA GLY C 123 4159 5116 4353 -602 -398 668 C ATOM 2065 C GLY C 123 -30.147 6.145 -15.622 1.00 36.68 C ANISOU 2065 C GLY C 123 4339 5143 4455 -619 -421 651 C ATOM 2066 O GLY C 123 -29.783 6.840 -14.697 1.00 37.77 O ANISOU 2066 O GLY C 123 4572 5219 4562 -666 -434 665 O ATOM 2067 N TYR C 124 -30.526 4.860 -15.439 1.00 36.30 N ANISOU 2067 N TYR C 124 4261 5099 4431 -596 -426 621 N ATOM 2068 CA TYR C 124 -30.516 4.243 -14.165 1.00 36.16 C ANISOU 2068 CA TYR C 124 4301 5024 4415 -613 -451 623 C ATOM 2069 C TYR C 124 -29.074 3.829 -13.740 1.00 36.49 C ANISOU 2069 C TYR C 124 4312 5071 4482 -655 -523 654 C ATOM 2070 O TYR C 124 -28.459 3.017 -14.399 1.00 37.16 O ANISOU 2070 O TYR C 124 4301 5187 4630 -626 -526 652 O ATOM 2071 CB TYR C 124 -31.477 3.010 -14.112 1.00 35.57 C ANISOU 2071 CB TYR C 124 4196 4945 4373 -577 -431 599 C ATOM 2072 CG TYR C 124 -32.895 3.502 -14.262 1.00 38.42 C ANISOU 2072 CG TYR C 124 4577 5306 4715 -549 -371 615 C ATOM 2073 CD1 TYR C 124 -33.521 4.192 -13.210 1.00 37.72 C ANISOU 2073 CD1 TYR C 124 4585 5150 4595 -544 -323 645 C ATOM 2074 CD2 TYR C 124 -33.612 3.348 -15.457 1.00 35.31 C ANISOU 2074 CD2 TYR C 124 4106 4982 4330 -537 -354 616 C ATOM 2075 CE1 TYR C 124 -34.826 4.674 -13.313 1.00 37.62 C ANISOU 2075 CE1 TYR C 124 4572 5128 4593 -500 -242 691 C ATOM 2076 CE2 TYR C 124 -34.961 3.878 -15.596 1.00 37.76 C ANISOU 2076 CE2 TYR C 124 4401 5306 4640 -513 -303 682 C ATOM 2077 CZ TYR C 124 -35.542 4.508 -14.540 1.00 38.48 C ANISOU 2077 CZ TYR C 124 4567 5320 4734 -481 -240 725 C ATOM 2078 OH TYR C 124 -36.813 5.048 -14.720 1.00 38.62 O ANISOU 2078 OH TYR C 124 4548 5346 4780 -439 -168 818 O ATOM 2079 N PHE C 125 -28.631 4.308 -12.587 1.00 35.87 N ANISOU 2079 N PHE C 125 4317 4958 4354 -727 -571 692 N ATOM 2080 CA PHE C 125 -27.303 3.990 -12.048 1.00 37.13 C ANISOU 2080 CA PHE C 125 4434 5140 4535 -791 -660 767 C ATOM 2081 C PHE C 125 -27.228 2.524 -11.860 1.00 38.52 C ANISOU 2081 C PHE C 125 4524 5317 4797 -744 -667 792 C ATOM 2082 O PHE C 125 -28.153 1.950 -11.268 1.00 39.78 O ANISOU 2082 O PHE C 125 4729 5441 4945 -726 -644 767 O ATOM 2083 CB PHE C 125 -27.017 4.721 -10.751 1.00 37.34 C ANISOU 2083 CB PHE C 125 4590 5138 4458 -915 -722 803 C ATOM 2084 CG PHE C 125 -25.594 4.555 -10.272 1.00 35.77 C ANISOU 2084 CG PHE C 125 4328 4990 4273 -1012 -840 918 C ATOM 2085 CD1 PHE C 125 -24.583 5.362 -10.800 1.00 38.51 C ANISOU 2085 CD1 PHE C 125 4632 5374 4625 -1066 -886 967 C ATOM 2086 CD2 PHE C 125 -25.303 3.646 -9.316 1.00 42.13 C ANISOU 2086 CD2 PHE C 125 5105 5813 5091 -1054 -906 999 C ATOM 2087 CE1 PHE C 125 -23.276 5.247 -10.382 1.00 39.61 C ANISOU 2087 CE1 PHE C 125 4690 5574 4786 -1164 -1002 1106 C ATOM 2088 CE2 PHE C 125 -23.963 3.471 -8.878 1.00 43.79 C ANISOU 2088 CE2 PHE C 125 5222 6088 5328 -1150 -1027 1151 C ATOM 2089 CZ PHE C 125 -22.956 4.237 -9.453 1.00 38.04 C ANISOU 2089 CZ PHE C 125 4437 5402 4615 -1200 -1073 1208 C ATOM 2090 N PRO C 126 -26.110 1.888 -12.245 1.00 39.08 N ANISOU 2090 N PRO C 126 4468 5417 4964 -725 -690 859 N ATOM 2091 CA PRO C 126 -26.121 0.431 -12.254 1.00 39.93 C ANISOU 2091 CA PRO C 126 4491 5496 5184 -657 -657 874 C ATOM 2092 C PRO C 126 -25.759 -0.196 -10.903 1.00 43.98 C ANISOU 2092 C PRO C 126 4990 6000 5722 -708 -734 990 C ATOM 2093 O PRO C 126 -24.701 -0.790 -10.789 1.00 44.58 O ANISOU 2093 O PRO C 126 4945 6089 5904 -701 -762 1111 O ATOM 2094 CB PRO C 126 -25.115 0.111 -13.318 1.00 43.15 C ANISOU 2094 CB PRO C 126 4777 5924 5695 -599 -610 899 C ATOM 2095 CG PRO C 126 -24.079 1.268 -13.246 1.00 38.46 C ANISOU 2095 CG PRO C 126 4161 5390 5059 -675 -685 987 C ATOM 2096 CD PRO C 126 -24.920 2.447 -12.908 1.00 38.92 C ANISOU 2096 CD PRO C 126 4367 5446 4974 -742 -713 917 C ATOM 2097 N ASP C 127 -26.621 -0.047 -9.888 1.00 42.82 N ANISOU 2097 N ASP C 127 4957 5835 5478 -760 -761 971 N ATOM 2098 CA ASP C 127 -26.393 -0.651 -8.542 1.00 46.79 C ANISOU 2098 CA ASP C 127 5459 6344 5976 -826 -839 1086 C ATOM 2099 C ASP C 127 -27.623 -1.415 -8.064 1.00 45.38 C ANISOU 2099 C ASP C 127 5331 6117 5795 -785 -791 1036 C ATOM 2100 O ASP C 127 -27.687 -1.758 -6.904 1.00 45.93 O ANISOU 2100 O ASP C 127 5430 6196 5825 -847 -846 1116 O ATOM 2101 CB ASP C 127 -26.047 0.406 -7.441 1.00 46.54 C ANISOU 2101 CB ASP C 127 5547 6354 5780 -987 -938 1138 C ATOM 2102 CG ASP C 127 -27.231 1.391 -7.219 1.00 51.32 C ANISOU 2102 CG ASP C 127 6345 6916 6239 -1007 -872 1003 C ATOM 2103 OD1 ASP C 127 -28.274 1.321 -7.933 1.00 51.90 O ANISOU 2103 OD1 ASP C 127 6429 6948 6345 -900 -768 900 O ATOM 2104 OD2 ASP C 127 -27.111 2.243 -6.330 1.00 58.75 O ANISOU 2104 OD2 ASP C 127 7428 7862 7033 -1139 -916 1010 O ATOM 2105 N TRP C 128 -28.559 -1.685 -8.961 1.00 43.43 N ANISOU 2105 N TRP C 128 5086 5830 5585 -695 -698 922 N ATOM 2106 CA TRP C 128 -29.907 -2.191 -8.646 1.00 43.69 C ANISOU 2106 CA TRP C 128 5172 5824 5604 -664 -649 872 C ATOM 2107 C TRP C 128 -30.074 -3.692 -8.953 1.00 45.19 C ANISOU 2107 C TRP C 128 5268 5961 5940 -598 -614 879 C ATOM 2108 O TRP C 128 -30.986 -4.329 -8.370 1.00 45.44 O ANISOU 2108 O TRP C 128 5323 5963 5978 -592 -601 886 O ATOM 2109 CB TRP C 128 -31.014 -1.441 -9.406 1.00 42.20 C ANISOU 2109 CB TRP C 128 5047 5634 5354 -631 -578 765 C ATOM 2110 CG TRP C 128 -30.817 -1.525 -10.913 1.00 41.87 C ANISOU 2110 CG TRP C 128 4933 5605 5372 -582 -537 699 C ATOM 2111 CD1 TRP C 128 -30.099 -0.641 -11.723 1.00 43.27 C ANISOU 2111 CD1 TRP C 128 5095 5821 5526 -588 -538 681 C ATOM 2112 CD2 TRP C 128 -31.272 -2.551 -11.787 1.00 43.76 C ANISOU 2112 CD2 TRP C 128 5118 5819 5690 -539 -489 643 C ATOM 2113 NE1 TRP C 128 -30.121 -1.065 -13.024 1.00 40.96 N ANISOU 2113 NE1 TRP C 128 4742 5538 5281 -546 -488 617 N ATOM 2114 CE2 TRP C 128 -30.822 -2.231 -13.091 1.00 43.21 C ANISOU 2114 CE2 TRP C 128 5014 5782 5623 -525 -456 585 C ATOM 2115 CE3 TRP C 128 -32.082 -3.670 -11.620 1.00 47.68 C ANISOU 2115 CE3 TRP C 128 5605 6270 6243 -526 -467 631 C ATOM 2116 CZ2 TRP C 128 -31.085 -3.039 -14.182 1.00 46.61 C ANISOU 2116 CZ2 TRP C 128 5418 6198 6095 -510 -400 507 C ATOM 2117 CZ3 TRP C 128 -32.293 -4.500 -12.687 1.00 49.58 C ANISOU 2117 CZ3 TRP C 128 5814 6483 6541 -513 -418 556 C ATOM 2118 CH2 TRP C 128 -31.812 -4.169 -13.963 1.00 49.26 C ANISOU 2118 CH2 TRP C 128 5758 6475 6482 -511 -382 487 C ATOM 2119 N GLN C 129 -29.216 -4.254 -9.778 1.00 44.70 N ANISOU 2119 N GLN C 129 5110 5879 5996 -551 -585 884 N ATOM 2120 CA GLN C 129 -29.414 -5.598 -10.256 1.00 48.10 C ANISOU 2120 CA GLN C 129 5482 6228 6564 -490 -516 858 C ATOM 2121 C GLN C 129 -28.637 -6.602 -9.409 1.00 48.73 C ANISOU 2121 C GLN C 129 5469 6266 6781 -475 -539 1006 C ATOM 2122 O GLN C 129 -27.658 -7.142 -9.831 1.00 51.50 O ANISOU 2122 O GLN C 129 5723 6576 7267 -424 -494 1061 O ATOM 2123 CB GLN C 129 -29.014 -5.682 -11.735 1.00 49.39 C ANISOU 2123 CB GLN C 129 5616 6373 6776 -444 -430 761 C ATOM 2124 CG GLN C 129 -29.602 -6.933 -12.430 1.00 51.95 C ANISOU 2124 CG GLN C 129 5947 6600 7191 -412 -335 669 C ATOM 2125 CD GLN C 129 -28.846 -7.401 -13.673 1.00 55.09 C ANISOU 2125 CD GLN C 129 6316 6944 7671 -365 -220 598 C ATOM 2126 OE1 GLN C 129 -28.962 -8.570 -14.048 1.00 59.99 O ANISOU 2126 OE1 GLN C 129 6945 7453 8398 -340 -124 545 O ATOM 2127 NE2 GLN C 129 -28.042 -6.538 -14.275 1.00 59.30 N ANISOU 2127 NE2 GLN C 129 6823 7544 8163 -356 -214 599 N ATOM 2128 N ASN C 130 -29.046 -6.732 -8.169 1.00 46.99 N ANISOU 2128 N ASN C 130 5274 6063 6515 -523 -606 1091 N ATOM 2129 CA ASN C 130 -28.372 -7.586 -7.185 1.00 48.72 C ANISOU 2129 CA ASN C 130 5397 6268 6845 -530 -654 1271 C ATOM 2130 C ASN C 130 -29.279 -8.765 -6.913 1.00 47.86 C ANISOU 2130 C ASN C 130 5286 6073 6824 -495 -608 1264 C ATOM 2131 O ASN C 130 -30.508 -8.603 -6.998 1.00 44.67 O ANISOU 2131 O ASN C 130 4976 5666 6330 -507 -587 1153 O ATOM 2132 CB ASN C 130 -28.177 -6.798 -5.932 1.00 49.92 C ANISOU 2132 CB ASN C 130 5600 6523 6846 -642 -775 1377 C ATOM 2133 CG ASN C 130 -27.362 -5.556 -6.215 1.00 52.65 C ANISOU 2133 CG ASN C 130 5969 6944 7092 -700 -825 1371 C ATOM 2134 OD1 ASN C 130 -26.254 -5.691 -6.684 1.00 53.79 O ANISOU 2134 OD1 ASN C 130 5995 7094 7346 -672 -828 1453 O ATOM 2135 ND2 ASN C 130 -27.980 -4.377 -6.092 1.00 48.32 N ANISOU 2135 ND2 ASN C 130 5568 6435 6358 -761 -837 1266 N ATOM 2136 N TYR C 131 -28.690 -9.927 -6.704 1.00 47.09 N ANISOU 2136 N TYR C 131 5074 5899 6919 -446 -579 1387 N ATOM 2137 CA TYR C 131 -29.500 -11.169 -6.445 1.00 48.28 C ANISOU 2137 CA TYR C 131 5217 5946 7183 -416 -529 1392 C ATOM 2138 C TYR C 131 -29.142 -11.812 -5.110 1.00 51.85 C ANISOU 2138 C TYR C 131 5578 6415 7709 -441 -602 1619 C ATOM 2139 O TYR C 131 -28.063 -11.554 -4.592 1.00 53.49 O ANISOU 2139 O TYR C 131 5696 6694 7934 -469 -675 1787 O ATOM 2140 CB TYR C 131 -29.317 -12.178 -7.556 1.00 48.34 C ANISOU 2140 CB TYR C 131 5189 5798 7380 -329 -386 1310 C ATOM 2141 CG TYR C 131 -29.714 -11.664 -8.912 1.00 48.33 C ANISOU 2141 CG TYR C 131 5282 5790 7290 -326 -316 1092 C ATOM 2142 CD1 TYR C 131 -31.037 -11.696 -9.348 1.00 50.42 C ANISOU 2142 CD1 TYR C 131 5649 6044 7463 -368 -303 943 C ATOM 2143 CD2 TYR C 131 -28.765 -11.073 -9.746 1.00 48.74 C ANISOU 2143 CD2 TYR C 131 5309 5868 7341 -295 -276 1058 C ATOM 2144 CE1 TYR C 131 -31.374 -11.211 -10.591 1.00 53.10 C ANISOU 2144 CE1 TYR C 131 6061 6401 7712 -387 -256 774 C ATOM 2145 CE2 TYR C 131 -29.107 -10.605 -10.978 1.00 52.57 C ANISOU 2145 CE2 TYR C 131 5876 6363 7735 -304 -217 876 C ATOM 2146 CZ TYR C 131 -30.444 -10.663 -11.395 1.00 51.65 C ANISOU 2146 CZ TYR C 131 5862 6243 7520 -357 -214 734 C ATOM 2147 OH TYR C 131 -30.783 -10.129 -12.618 1.00 52.17 O ANISOU 2147 OH TYR C 131 5998 6347 7477 -387 -176 580 O ATOM 2148 N THR C 132 -30.027 -12.627 -4.512 1.00 53.42 N ANISOU 2148 N THR C 132 5788 6564 7946 -446 -598 1648 N ATOM 2149 CA THR C 132 -29.690 -13.266 -3.244 1.00 55.50 C ANISOU 2149 CA THR C 132 5955 6854 8278 -476 -670 1884 C ATOM 2150 C THR C 132 -28.459 -14.225 -3.485 1.00 59.64 C ANISOU 2150 C THR C 132 6304 7279 9080 -390 -611 2051 C ATOM 2151 O THR C 132 -28.232 -14.706 -4.606 1.00 59.88 O ANISOU 2151 O THR C 132 6319 7170 9264 -296 -474 1945 O ATOM 2152 CB THR C 132 -30.844 -14.079 -2.689 1.00 55.59 C ANISOU 2152 CB THR C 132 5996 6812 8313 -483 -656 1891 C ATOM 2153 OG1 THR C 132 -31.244 -15.012 -3.708 1.00 53.84 O ANISOU 2153 OG1 THR C 132 5774 6418 8266 -405 -529 1768 O ATOM 2154 CG2 THR C 132 -32.084 -13.168 -2.291 1.00 55.58 C ANISOU 2154 CG2 THR C 132 6147 6912 8060 -555 -696 1774 C ATOM 2155 N PRO C 133 -27.671 -14.503 -2.440 1.00 62.17 N ANISOU 2155 N PRO C 133 6490 7668 9463 -426 -703 2324 N ATOM 2156 CA PRO C 133 -26.485 -15.338 -2.680 1.00 65.70 C ANISOU 2156 CA PRO C 133 6745 8022 10196 -330 -632 2519 C ATOM 2157 C PRO C 133 -26.829 -16.821 -2.901 1.00 68.59 C ANISOU 2157 C PRO C 133 7055 8173 10831 -222 -485 2540 C ATOM 2158 O PRO C 133 -27.891 -17.306 -2.475 1.00 69.44 O ANISOU 2158 O PRO C 133 7233 8244 10906 -251 -493 2491 O ATOM 2159 CB PRO C 133 -25.675 -15.135 -1.394 1.00 66.92 C ANISOU 2159 CB PRO C 133 6770 8346 10311 -434 -803 2834 C ATOM 2160 CG PRO C 133 -26.731 -15.135 -0.313 1.00 66.68 C ANISOU 2160 CG PRO C 133 6841 8395 10099 -540 -900 2835 C ATOM 2161 CD PRO C 133 -27.863 -14.240 -1.006 1.00 62.96 C ANISOU 2161 CD PRO C 133 6599 7920 9404 -553 -856 2488 C ATOM 2162 N GLY C 134 -25.971 -17.569 -3.584 1.00 71.77 N ANISOU 2162 N GLY C 134 7340 8419 11511 -95 -332 2609 N ATOM 2163 CA GLY C 134 -26.330 -18.979 -3.807 1.00 74.60 C ANISOU 2163 CA GLY C 134 7675 8541 12129 1 -169 2609 C ATOM 2164 C GLY C 134 -26.436 -19.825 -2.533 1.00 76.61 C ANISOU 2164 C GLY C 134 7802 8799 12507 -20 -244 2889 C ATOM 2165 O GLY C 134 -26.392 -19.309 -1.414 1.00 77.27 O ANISOU 2165 O GLY C 134 7840 9089 12431 -130 -435 3064 O ATOM 2166 N PRO C 135 -26.606 -21.146 -2.690 1.00 78.37 N ANISOU 2166 N PRO C 135 7981 8788 13008 74 -87 2930 N ATOM 2167 CA PRO C 135 -26.740 -21.822 -3.974 1.00 77.58 C ANISOU 2167 CA PRO C 135 7977 8426 13075 175 153 2700 C ATOM 2168 C PRO C 135 -28.188 -22.040 -4.273 1.00 74.09 C ANISOU 2168 C PRO C 135 7735 7917 12500 101 159 2433 C ATOM 2169 O PRO C 135 -29.053 -21.808 -3.410 1.00 73.24 O ANISOU 2169 O PRO C 135 7660 7945 12223 1 0 2465 O ATOM 2170 CB PRO C 135 -26.016 -23.147 -3.732 1.00 81.29 C ANISOU 2170 CB PRO C 135 8266 8679 13941 305 311 2960 C ATOM 2171 CG PRO C 135 -26.355 -23.465 -2.263 1.00 82.85 C ANISOU 2171 CG PRO C 135 8348 8998 14133 231 131 3236 C ATOM 2172 CD PRO C 135 -26.382 -22.099 -1.576 1.00 80.56 C ANISOU 2172 CD PRO C 135 8078 9039 13492 89 -124 3265 C ATOM 2173 N GLY C 136 -28.466 -22.514 -5.476 1.00 71.40 N ANISOU 2173 N GLY C 136 7529 7368 12232 139 347 2182 N ATOM 2174 CA GLY C 136 -29.843 -22.674 -5.894 1.00 68.98 C ANISOU 2174 CA GLY C 136 7412 7012 11784 42 341 1928 C ATOM 2175 C GLY C 136 -30.285 -21.344 -6.514 1.00 64.52 C ANISOU 2175 C GLY C 136 6979 6641 10897 -41 243 1705 C ATOM 2176 O GLY C 136 -29.486 -20.586 -7.016 1.00 62.73 O ANISOU 2176 O GLY C 136 6735 6489 10612 -5 259 1675 O ATOM 2177 N ILE C 137 -31.575 -21.081 -6.459 1.00 62.57 N ANISOU 2177 N ILE C 137 6846 6470 10456 -151 146 1572 N ATOM 2178 CA ILE C 137 -32.152 -19.974 -7.172 1.00 58.94 C ANISOU 2178 CA ILE C 137 6511 6154 9728 -226 82 1362 C ATOM 2179 C ILE C 137 -31.727 -18.658 -6.527 1.00 56.57 C ANISOU 2179 C ILE C 137 6154 6096 9245 -234 -66 1463 C ATOM 2180 O ILE C 137 -31.654 -18.504 -5.311 1.00 57.26 O ANISOU 2180 O ILE C 137 6156 6293 9307 -249 -180 1660 O ATOM 2181 CB ILE C 137 -33.684 -20.166 -7.272 1.00 58.97 C ANISOU 2181 CB ILE C 137 6627 6162 9615 -338 31 1236 C ATOM 2182 CG1 ILE C 137 -33.972 -21.467 -8.028 1.00 61.50 C ANISOU 2182 CG1 ILE C 137 7030 6226 10112 -358 184 1117 C ATOM 2183 CG2 ILE C 137 -34.314 -18.998 -7.986 1.00 56.40 C ANISOU 2183 CG2 ILE C 137 6405 5997 9030 -413 -36 1060 C ATOM 2184 CD1 ILE C 137 -35.504 -21.767 -8.316 1.00 62.09 C ANISOU 2184 CD1 ILE C 137 7219 6292 10080 -501 132 988 C ATOM 2185 N ARG C 138 -31.342 -17.702 -7.356 1.00 55.31 N ANISOU 2185 N ARG C 138 6045 6015 8956 -233 -57 1334 N ATOM 2186 CA AARG C 138 -30.946 -16.398 -6.835 0.60 53.75 C ANISOU 2186 CA AARG C 138 5816 6027 8578 -257 -188 1406 C ATOM 2187 CA BARG C 138 -30.939 -16.387 -6.861 0.40 53.24 C ANISOU 2187 CA BARG C 138 5753 5962 8512 -257 -186 1403 C ATOM 2188 C ARG C 138 -32.067 -15.407 -7.196 1.00 51.54 C ANISOU 2188 C ARG C 138 5665 5868 8048 -338 -254 1233 C ATOM 2189 O ARG C 138 -32.363 -15.231 -8.351 1.00 49.79 O ANISOU 2189 O ARG C 138 5526 5615 7775 -352 -191 1050 O ATOM 2190 CB AARG C 138 -29.576 -15.998 -7.381 0.60 54.34 C ANISOU 2190 CB AARG C 138 5823 6108 8716 -191 -134 1440 C ATOM 2191 CB BARG C 138 -29.626 -15.955 -7.510 0.40 53.46 C ANISOU 2191 CB BARG C 138 5724 5994 8593 -192 -127 1414 C ATOM 2192 CG AARG C 138 -28.418 -16.944 -6.949 0.60 58.05 C ANISOU 2192 CG AARG C 138 6126 6467 9462 -97 -62 1670 C ATOM 2193 CG BARG C 138 -28.603 -17.082 -7.726 0.40 54.97 C ANISOU 2193 CG BARG C 138 5804 6003 9080 -83 24 1528 C ATOM 2194 CD AARG C 138 -27.024 -16.404 -7.383 0.60 60.86 C ANISOU 2194 CD AARG C 138 6383 6865 9875 -34 -25 1751 C ATOM 2195 CD BARG C 138 -28.259 -17.826 -6.444 0.40 55.53 C ANISOU 2195 CD BARG C 138 5725 6056 9317 -59 -28 1810 C ATOM 2196 NE AARG C 138 -26.638 -15.182 -6.656 0.60 58.67 N ANISOU 2196 NE AARG C 138 6069 6814 9410 -113 -210 1864 N ATOM 2197 NE BARG C 138 -27.406 -18.972 -6.735 0.40 57.55 N ANISOU 2197 NE BARG C 138 5872 6103 9890 62 150 1921 N ATOM 2198 CZ AARG C 138 -25.821 -14.242 -7.134 0.60 61.79 C ANISOU 2198 CZ AARG C 138 6440 7302 9734 -113 -229 1858 C ATOM 2199 CZ BARG C 138 -26.100 -18.861 -6.874 0.40 59.74 C ANISOU 2199 CZ BARG C 138 6009 6382 10307 146 207 2078 C ATOM 2200 NH1AARG C 138 -25.293 -14.364 -8.359 0.60 62.17 N ANISOU 2200 NH1AARG C 138 6490 7252 9881 -26 -68 1748 N ATOM 2201 NH1BARG C 138 -25.534 -17.694 -6.692 0.40 60.36 N ANISOU 2201 NH1BARG C 138 6046 6666 10224 100 74 2139 N ATOM 2202 NH2AARG C 138 -25.555 -13.151 -6.399 0.60 58.85 N ANISOU 2202 NH2AARG C 138 6059 7121 9179 -212 -403 1951 N ATOM 2203 NH2BARG C 138 -25.360 -19.907 -7.139 0.40 64.29 N ANISOU 2203 NH2BARG C 138 6482 6752 11194 273 399 2193 N ATOM 2204 N TYR C 139 -32.669 -14.812 -6.161 1.00 49.53 N ANISOU 2204 N TYR C 139 5423 5748 7649 -391 -371 1313 N ATOM 2205 CA TYR C 139 -33.798 -13.934 -6.277 1.00 50.02 C ANISOU 2205 CA TYR C 139 5583 5913 7509 -450 -416 1204 C ATOM 2206 C TYR C 139 -33.376 -12.451 -6.324 1.00 48.69 C ANISOU 2206 C TYR C 139 5452 5885 7162 -466 -469 1175 C ATOM 2207 O TYR C 139 -32.397 -12.073 -5.699 1.00 48.47 O ANISOU 2207 O TYR C 139 5378 5915 7124 -466 -520 1290 O ATOM 2208 CB TYR C 139 -34.736 -14.170 -5.116 1.00 50.45 C ANISOU 2208 CB TYR C 139 5639 6008 7520 -489 -473 1308 C ATOM 2209 CG TYR C 139 -35.345 -15.584 -5.168 1.00 52.23 C ANISOU 2209 CG TYR C 139 5837 6091 7915 -488 -424 1324 C ATOM 2210 CD1 TYR C 139 -36.325 -15.903 -6.091 1.00 55.19 C ANISOU 2210 CD1 TYR C 139 6274 6407 8288 -528 -381 1181 C ATOM 2211 CD2 TYR C 139 -34.941 -16.562 -4.279 1.00 57.49 C ANISOU 2211 CD2 TYR C 139 6415 6689 8738 -465 -428 1497 C ATOM 2212 CE1 TYR C 139 -36.869 -17.217 -6.158 1.00 58.45 C ANISOU 2212 CE1 TYR C 139 6678 6674 8855 -552 -339 1188 C ATOM 2213 CE2 TYR C 139 -35.497 -17.880 -4.326 1.00 60.20 C ANISOU 2213 CE2 TYR C 139 6738 6880 9254 -467 -374 1514 C ATOM 2214 CZ TYR C 139 -36.441 -18.182 -5.276 1.00 58.05 C ANISOU 2214 CZ TYR C 139 6547 6534 8975 -514 -328 1348 C ATOM 2215 OH TYR C 139 -37.010 -19.437 -5.341 1.00 63.02 O ANISOU 2215 OH TYR C 139 7176 7009 9762 -543 -281 1355 O ATOM 2216 N PRO C 140 -34.127 -11.630 -7.032 1.00 47.81 N ANISOU 2216 N PRO C 140 5420 5830 6918 -491 -461 1041 N ATOM 2217 CA PRO C 140 -33.706 -10.216 -7.132 1.00 46.56 C ANISOU 2217 CA PRO C 140 5302 5781 6609 -502 -495 1012 C ATOM 2218 C PRO C 140 -33.913 -9.480 -5.832 1.00 46.22 C ANISOU 2218 C PRO C 140 5301 5829 6433 -543 -560 1107 C ATOM 2219 O PRO C 140 -34.977 -9.610 -5.218 1.00 48.72 O ANISOU 2219 O PRO C 140 5651 6156 6703 -561 -557 1131 O ATOM 2220 CB PRO C 140 -34.628 -9.664 -8.245 1.00 46.30 C ANISOU 2220 CB PRO C 140 5328 5772 6491 -517 -460 868 C ATOM 2221 CG PRO C 140 -35.902 -10.574 -8.205 1.00 47.58 C ANISOU 2221 CG PRO C 140 5493 5885 6700 -543 -444 862 C ATOM 2222 CD PRO C 140 -35.297 -11.936 -7.884 1.00 47.95 C ANISOU 2222 CD PRO C 140 5484 5812 6924 -519 -421 922 C ATOM 2223 N LEU C 141 -32.945 -8.645 -5.441 1.00 45.79 N ANISOU 2223 N LEU C 141 5256 5840 6300 -571 -611 1155 N ATOM 2224 CA LEU C 141 -33.033 -7.833 -4.248 1.00 45.62 C ANISOU 2224 CA LEU C 141 5314 5901 6117 -640 -664 1221 C ATOM 2225 C LEU C 141 -33.873 -6.592 -4.513 1.00 46.07 C ANISOU 2225 C LEU C 141 5488 5994 6022 -648 -618 1110 C ATOM 2226 O LEU C 141 -34.505 -6.051 -3.601 1.00 46.52 O ANISOU 2226 O LEU C 141 5642 6084 5951 -686 -604 1129 O ATOM 2227 CB LEU C 141 -31.595 -7.420 -3.757 1.00 49.52 C ANISOU 2227 CB LEU C 141 5780 6456 6581 -701 -750 1326 C ATOM 2228 CG LEU C 141 -30.772 -8.644 -3.275 1.00 53.75 C ANISOU 2228 CG LEU C 141 6173 6966 7282 -693 -795 1500 C ATOM 2229 CD1 LEU C 141 -29.397 -8.252 -2.747 1.00 58.66 C ANISOU 2229 CD1 LEU C 141 6738 7671 7878 -770 -898 1651 C ATOM 2230 CD2 LEU C 141 -31.554 -9.385 -2.232 1.00 52.63 C ANISOU 2230 CD2 LEU C 141 6039 6821 7136 -715 -807 1586 C ATOM 2231 N THR C 142 -33.888 -6.098 -5.764 1.00 42.61 N ANISOU 2231 N THR C 142 5044 5547 5599 -610 -579 1001 N ATOM 2232 CA THR C 142 -34.666 -4.890 -6.061 1.00 41.65 C ANISOU 2232 CA THR C 142 5011 5454 5360 -607 -528 926 C ATOM 2233 C THR C 142 -36.116 -5.359 -6.450 1.00 42.05 C ANISOU 2233 C THR C 142 5040 5485 5453 -569 -470 903 C ATOM 2234 O THR C 142 -36.353 -5.977 -7.476 1.00 41.89 O ANISOU 2234 O THR C 142 4955 5443 5518 -551 -461 855 O ATOM 2235 CB THR C 142 -34.071 -4.083 -7.253 1.00 40.87 C ANISOU 2235 CB THR C 142 4903 5374 5254 -594 -521 847 C ATOM 2236 OG1 THR C 142 -32.796 -3.574 -6.832 1.00 40.89 O ANISOU 2236 OG1 THR C 142 4919 5402 5213 -643 -582 889 O ATOM 2237 CG2 THR C 142 -35.048 -2.899 -7.664 1.00 38.74 C ANISOU 2237 CG2 THR C 142 4700 5123 4897 -577 -454 794 C ATOM 2238 N PHE C 143 -37.067 -5.040 -5.593 1.00 43.88 N ANISOU 2238 N PHE C 143 5332 5727 5614 -570 -425 946 N ATOM 2239 CA PHE C 143 -38.515 -5.392 -5.839 1.00 44.16 C ANISOU 2239 CA PHE C 143 5330 5759 5691 -539 -372 966 C ATOM 2240 C PHE C 143 -38.951 -4.651 -7.072 1.00 42.98 C ANISOU 2240 C PHE C 143 5157 5636 5537 -518 -339 912 C ATOM 2241 O PHE C 143 -38.749 -3.433 -7.178 1.00 41.97 O ANISOU 2241 O PHE C 143 5089 5525 5333 -505 -301 888 O ATOM 2242 CB PHE C 143 -39.336 -5.023 -4.570 1.00 44.26 C ANISOU 2242 CB PHE C 143 5418 5779 5621 -534 -304 1039 C ATOM 2243 CG PHE C 143 -40.798 -5.508 -4.567 1.00 45.52 C ANISOU 2243 CG PHE C 143 5517 5941 5839 -503 -250 1107 C ATOM 2244 CD1 PHE C 143 -41.159 -6.699 -5.124 1.00 45.49 C ANISOU 2244 CD1 PHE C 143 5410 5923 5951 -518 -302 1123 C ATOM 2245 CD2 PHE C 143 -41.810 -4.681 -4.021 1.00 48.65 C ANISOU 2245 CD2 PHE C 143 5965 6346 6173 -461 -131 1161 C ATOM 2246 CE1 PHE C 143 -42.505 -7.118 -5.152 1.00 45.47 C ANISOU 2246 CE1 PHE C 143 5341 5934 6000 -512 -269 1203 C ATOM 2247 CE2 PHE C 143 -43.169 -5.111 -4.038 1.00 52.43 C ANISOU 2247 CE2 PHE C 143 6361 6840 6722 -430 -81 1258 C ATOM 2248 CZ PHE C 143 -43.487 -6.306 -4.629 1.00 47.49 C ANISOU 2248 CZ PHE C 143 5620 6218 6206 -465 -165 1281 C ATOM 2249 N GLY C 144 -39.562 -5.378 -7.994 1.00 42.14 N ANISOU 2249 N GLY C 144 4970 5534 5506 -529 -356 901 N ATOM 2250 CA GLY C 144 -39.966 -4.850 -9.218 1.00 42.30 C ANISOU 2250 CA GLY C 144 4953 5600 5518 -535 -348 870 C ATOM 2251 C GLY C 144 -39.183 -5.479 -10.370 1.00 43.05 C ANISOU 2251 C GLY C 144 5019 5686 5652 -575 -397 774 C ATOM 2252 O GLY C 144 -39.713 -5.562 -11.471 1.00 43.82 O ANISOU 2252 O GLY C 144 5077 5825 5747 -619 -408 749 O ATOM 2253 N TRP C 145 -37.929 -5.897 -10.130 1.00 42.17 N ANISOU 2253 N TRP C 145 4926 5524 5572 -567 -417 732 N ATOM 2254 CA TRP C 145 -37.158 -6.622 -11.174 1.00 41.23 C ANISOU 2254 CA TRP C 145 4785 5370 5510 -588 -424 642 C ATOM 2255 C TRP C 145 -37.673 -8.054 -11.161 1.00 42.15 C ANISOU 2255 C TRP C 145 4881 5414 5718 -623 -424 638 C ATOM 2256 O TRP C 145 -37.613 -8.677 -10.092 1.00 42.55 O ANISOU 2256 O TRP C 145 4923 5413 5831 -603 -432 707 O ATOM 2257 CB TRP C 145 -35.713 -6.539 -10.860 1.00 39.78 C ANISOU 2257 CB TRP C 145 4604 5157 5354 -555 -429 640 C ATOM 2258 CG TRP C 145 -34.763 -7.258 -11.831 1.00 42.33 C ANISOU 2258 CG TRP C 145 4903 5425 5756 -551 -398 563 C ATOM 2259 CD1 TRP C 145 -33.835 -8.155 -11.474 1.00 46.24 C ANISOU 2259 CD1 TRP C 145 5363 5836 6369 -518 -380 593 C ATOM 2260 CD2 TRP C 145 -34.593 -7.073 -13.268 1.00 39.81 C ANISOU 2260 CD2 TRP C 145 4593 5131 5402 -574 -363 459 C ATOM 2261 NE1 TRP C 145 -33.070 -8.531 -12.548 1.00 45.89 N ANISOU 2261 NE1 TRP C 145 5310 5746 6379 -504 -315 513 N ATOM 2262 CE2 TRP C 145 -33.542 -7.934 -13.675 1.00 45.30 C ANISOU 2262 CE2 TRP C 145 5273 5737 6201 -547 -303 416 C ATOM 2263 CE3 TRP C 145 -35.191 -6.285 -14.210 1.00 46.78 C ANISOU 2263 CE3 TRP C 145 5490 6103 6183 -615 -369 416 C ATOM 2264 CZ2 TRP C 145 -33.079 -8.015 -15.000 1.00 45.84 C ANISOU 2264 CZ2 TRP C 145 5363 5801 6254 -562 -237 308 C ATOM 2265 CZ3 TRP C 145 -34.767 -6.376 -15.542 1.00 45.81 C ANISOU 2265 CZ3 TRP C 145 5379 5993 6032 -648 -330 317 C ATOM 2266 CH2 TRP C 145 -33.708 -7.242 -15.922 1.00 43.76 C ANISOU 2266 CH2 TRP C 145 5128 5640 5860 -622 -257 252 C ATOM 2267 N CYS C 146 -38.192 -8.559 -12.291 1.00 42.86 N ANISOU 2267 N CYS C 146 4972 5504 5810 -692 -420 565 N ATOM 2268 CA CYS C 146 -38.921 -9.855 -12.295 1.00 44.93 C ANISOU 2268 CA CYS C 146 5231 5694 6145 -756 -425 562 C ATOM 2269 C CYS C 146 -38.100 -10.952 -12.919 1.00 45.15 C ANISOU 2269 C CYS C 146 5296 5598 6260 -776 -374 454 C ATOM 2270 O CYS C 146 -38.660 -11.913 -13.424 1.00 48.53 O ANISOU 2270 O CYS C 146 5756 5963 6721 -864 -365 399 O ATOM 2271 CB CYS C 146 -40.293 -9.757 -12.995 1.00 43.77 C ANISOU 2271 CB CYS C 146 5068 5630 5934 -856 -463 580 C ATOM 2272 SG CYS C 146 -41.325 -8.488 -12.208 1.00 46.21 S ANISOU 2272 SG CYS C 146 5318 6057 6182 -801 -477 738 S ATOM 2273 N PHE C 147 -36.786 -10.822 -12.946 1.00 45.78 N ANISOU 2273 N PHE C 147 5376 5636 6381 -703 -329 426 N ATOM 2274 CA PHE C 147 -35.941 -11.929 -13.404 1.00 46.56 C ANISOU 2274 CA PHE C 147 5501 5588 6600 -692 -241 348 C ATOM 2275 C PHE C 147 -35.194 -12.487 -12.206 1.00 47.60 C ANISOU 2275 C PHE C 147 5573 5635 6879 -602 -228 465 C ATOM 2276 O PHE C 147 -34.740 -11.750 -11.319 1.00 46.63 O ANISOU 2276 O PHE C 147 5400 5585 6730 -547 -281 573 O ATOM 2277 CB PHE C 147 -34.937 -11.465 -14.436 1.00 48.06 C ANISOU 2277 CB PHE C 147 5715 5793 6755 -669 -177 254 C ATOM 2278 CG PHE C 147 -35.506 -11.262 -15.811 1.00 49.32 C ANISOU 2278 CG PHE C 147 5946 6010 6782 -779 -167 124 C ATOM 2279 CD1 PHE C 147 -35.516 -12.310 -16.753 1.00 50.30 C ANISOU 2279 CD1 PHE C 147 6164 6021 6928 -861 -77 -16 C ATOM 2280 CD2 PHE C 147 -36.048 -10.060 -16.170 1.00 46.52 C ANISOU 2280 CD2 PHE C 147 5574 5819 6282 -815 -242 147 C ATOM 2281 CE1 PHE C 147 -36.009 -12.113 -18.054 1.00 51.49 C ANISOU 2281 CE1 PHE C 147 6395 6247 6923 -997 -79 -134 C ATOM 2282 CE2 PHE C 147 -36.568 -9.892 -17.449 1.00 50.26 C ANISOU 2282 CE2 PHE C 147 6099 6369 6629 -934 -248 57 C ATOM 2283 CZ PHE C 147 -36.510 -10.927 -18.403 1.00 49.42 C ANISOU 2283 CZ PHE C 147 6093 6170 6516 -1035 -173 -88 C ATOM 2284 N LYS C 148 -35.054 -13.801 -12.181 1.00 49.83 N ANISOU 2284 N LYS C 148 5862 5758 7313 -600 -157 453 N ATOM 2285 CA LYS C 148 -34.292 -14.518 -11.158 1.00 49.57 C ANISOU 2285 CA LYS C 148 5753 5628 7453 -516 -133 588 C ATOM 2286 C LYS C 148 -33.287 -15.373 -11.897 1.00 50.96 C ANISOU 2286 C LYS C 148 5940 5637 7786 -464 16 523 C ATOM 2287 O LYS C 148 -33.390 -15.523 -13.102 1.00 51.48 O ANISOU 2287 O LYS C 148 6098 5654 7806 -515 98 356 O ATOM 2288 CB LYS C 148 -35.264 -15.379 -10.296 1.00 51.23 C ANISOU 2288 CB LYS C 148 5950 5784 7729 -553 -172 668 C ATOM 2289 CG LYS C 148 -35.998 -16.491 -11.048 1.00 50.58 C ANISOU 2289 CG LYS C 148 5946 5562 7709 -638 -107 551 C ATOM 2290 CD LYS C 148 -37.095 -17.106 -10.171 1.00 53.40 C ANISOU 2290 CD LYS C 148 6279 5906 8104 -688 -173 649 C ATOM 2291 CE LYS C 148 -37.818 -18.331 -10.869 1.00 57.37 C ANISOU 2291 CE LYS C 148 6868 6249 8682 -800 -116 541 C ATOM 2292 NZ LYS C 148 -39.008 -18.709 -10.029 1.00 51.78 N ANISOU 2292 NZ LYS C 148 6118 5570 7983 -859 -203 656 N ATOM 2293 N LEU C 149 -32.296 -15.938 -11.184 1.00 52.60 N ANISOU 2293 N LEU C 149 6049 5755 8180 -367 63 669 N ATOM 2294 CA LEU C 149 -31.248 -16.714 -11.809 1.00 54.18 C ANISOU 2294 CA LEU C 149 6238 5783 8565 -287 238 643 C ATOM 2295 C LEU C 149 -31.450 -18.165 -11.328 1.00 57.20 C ANISOU 2295 C LEU C 149 6607 5963 9165 -267 319 706 C ATOM 2296 O LEU C 149 -31.510 -18.404 -10.128 1.00 57.72 O ANISOU 2296 O LEU C 149 6571 6052 9307 -243 234 895 O ATOM 2297 CB LEU C 149 -29.852 -16.227 -11.346 1.00 54.25 C ANISOU 2297 CB LEU C 149 6105 5848 8658 -180 235 818 C ATOM 2298 CG LEU C 149 -29.474 -14.775 -11.687 1.00 55.18 C ANISOU 2298 CG LEU C 149 6221 6157 8589 -195 152 790 C ATOM 2299 CD1 LEU C 149 -27.938 -14.482 -11.273 1.00 51.47 C ANISOU 2299 CD1 LEU C 149 5595 5721 8241 -101 160 989 C ATOM 2300 CD2 LEU C 149 -29.673 -14.474 -13.120 1.00 50.36 C ANISOU 2300 CD2 LEU C 149 5728 5541 7865 -233 238 570 C ATOM 2301 N VAL C 150 -31.555 -19.089 -12.267 1.00 59.87 N ANISOU 2301 N VAL C 150 7056 6102 9588 -289 486 545 N ATOM 2302 CA VAL C 150 -31.995 -20.468 -11.990 1.00 62.44 C ANISOU 2302 CA VAL C 150 7414 6211 10098 -304 571 557 C ATOM 2303 C VAL C 150 -30.935 -21.446 -12.471 1.00 65.18 C ANISOU 2303 C VAL C 150 7764 6298 10701 -192 823 548 C ATOM 2304 O VAL C 150 -30.576 -21.443 -13.650 1.00 64.82 O ANISOU 2304 O VAL C 150 7838 6173 10619 -199 978 361 O ATOM 2305 CB VAL C 150 -33.327 -20.816 -12.664 1.00 61.29 C ANISOU 2305 CB VAL C 150 7438 6030 9818 -475 549 357 C ATOM 2306 CG1 VAL C 150 -33.788 -22.239 -12.260 1.00 66.12 C ANISOU 2306 CG1 VAL C 150 8079 6413 10632 -502 623 388 C ATOM 2307 CG2 VAL C 150 -34.383 -19.891 -12.198 1.00 60.16 C ANISOU 2307 CG2 VAL C 150 7271 6128 9459 -564 331 395 C ATOM 2308 N PRO C 151 -30.484 -22.326 -11.567 1.00 68.61 N ANISOU 2308 N PRO C 151 8073 6594 11402 -92 878 757 N ATOM 2309 CA PRO C 151 -29.497 -23.335 -11.955 1.00 72.66 C ANISOU 2309 CA PRO C 151 8571 6828 12206 37 1149 783 C ATOM 2310 C PRO C 151 -30.034 -24.274 -13.014 1.00 75.40 C ANISOU 2310 C PRO C 151 9151 6919 12578 -49 1349 513 C ATOM 2311 O PRO C 151 -31.178 -24.683 -12.902 1.00 76.22 O ANISOU 2311 O PRO C 151 9356 6998 12606 -188 1263 427 O ATOM 2312 CB PRO C 151 -29.207 -24.090 -10.651 1.00 73.82 C ANISOU 2312 CB PRO C 151 8528 6902 12617 130 1126 1088 C ATOM 2313 CG PRO C 151 -30.016 -23.453 -9.588 1.00 72.56 C ANISOU 2313 CG PRO C 151 8301 6993 12275 40 842 1203 C ATOM 2314 CD PRO C 151 -31.073 -22.603 -10.245 1.00 68.00 C ANISOU 2314 CD PRO C 151 7889 6576 11371 -112 720 956 C ATOM 2315 N VAL C 152 -29.247 -24.551 -14.052 1.00 78.72 N ANISOU 2315 N VAL C 152 9667 7165 13079 16 1607 376 N ATOM 2316 CA VAL C 152 -29.606 -25.537 -15.067 1.00 83.49 C ANISOU 2316 CA VAL C 152 10521 7485 13717 -71 1842 110 C ATOM 2317 C VAL C 152 -29.111 -26.940 -14.615 1.00 88.33 C ANISOU 2317 C VAL C 152 11089 7750 14722 61 2082 241 C ATOM 2318 O VAL C 152 -27.990 -27.066 -14.104 1.00 89.90 O ANISOU 2318 O VAL C 152 11082 7895 15182 266 2188 490 O ATOM 2319 CB VAL C 152 -28.981 -25.203 -16.447 1.00 84.10 C ANISOU 2319 CB VAL C 152 10752 7519 13684 -67 2048 -117 C ATOM 2320 CG1 VAL C 152 -29.438 -26.202 -17.505 1.00 88.52 C ANISOU 2320 CG1 VAL C 152 11616 7791 14226 -202 2285 -421 C ATOM 2321 CG2 VAL C 152 -29.339 -23.826 -16.862 1.00 82.60 C ANISOU 2321 CG2 VAL C 152 10574 7661 13149 -172 1825 -202 C ATOM 2322 N GLU C 153 -29.952 -27.965 -14.758 1.00 92.05 N ANISOU 2322 N GLU C 153 11734 7997 15244 -63 2155 103 N ATOM 2323 CA GLU C 153 -29.472 -29.370 -14.785 1.00 97.14 C ANISOU 2323 CA GLU C 153 12428 8230 16251 42 2478 127 C ATOM 2324 C GLU C 153 -30.487 -30.275 -15.479 1.00 99.24 C ANISOU 2324 C GLU C 153 13003 8258 16445 -175 2577 -167 C ATOM 2325 O GLU C 153 -30.113 -31.092 -16.323 1.00103.22 O ANISOU 2325 O GLU C 153 13714 8430 17074 -166 2910 -357 O ATOM 2326 CB GLU C 153 -29.162 -29.913 -13.382 1.00 98.05 C ANISOU 2326 CB GLU C 153 12271 8299 16685 195 2425 501 C ATOM 2327 CG GLU C 153 -28.178 -31.112 -13.383 1.00103.71 C ANISOU 2327 CG GLU C 153 12944 8618 17845 397 2798 625 C ATOM 2328 CD GLU C 153 -26.708 -30.703 -13.565 1.00106.09 C ANISOU 2328 CD GLU C 153 13068 8932 18309 628 2973 791 C ATOM 2329 OE1 GLU C 153 -26.406 -29.505 -13.421 1.00106.50 O ANISOU 2329 OE1 GLU C 153 12986 9321 18157 638 2758 872 O ATOM 2330 OE2 GLU C 153 -25.851 -31.575 -13.844 1.00111.71 O ANISOU 2330 OE2 GLU C 153 13771 9310 19364 802 3333 853 O ATOM 2331 N GLU C 181 -18.991 -30.430 -13.227 1.00119.31 N ANISOU 2331 N GLU C 181 13371 10395 21569 1939 4017 2396 N ATOM 2332 CA GLU C 181 -18.156 -29.251 -12.969 1.00117.95 C ANISOU 2332 CA GLU C 181 12938 10586 21293 1973 3800 2642 C ATOM 2333 C GLU C 181 -18.936 -28.180 -12.170 1.00113.58 C ANISOU 2333 C GLU C 181 12354 10461 20339 1747 3277 2640 C ATOM 2334 O GLU C 181 -19.842 -28.523 -11.407 1.00113.00 O ANISOU 2334 O GLU C 181 12316 10409 20208 1631 3082 2644 O ATOM 2335 CB GLU C 181 -17.583 -28.691 -14.286 1.00118.13 C ANISOU 2335 CB GLU C 181 13100 10589 21195 2025 4034 2402 C ATOM 2336 N LYS C 182 -18.579 -26.901 -12.339 1.00110.91 N ANISOU 2336 N LYS C 182 11955 10448 19738 1688 3072 2639 N ATOM 2337 CA LYS C 182 -19.132 -25.800 -11.529 1.00106.72 C ANISOU 2337 CA LYS C 182 11373 10316 18859 1497 2608 2681 C ATOM 2338 C LYS C 182 -20.564 -25.373 -11.955 1.00103.11 C ANISOU 2338 C LYS C 182 11247 9941 17990 1279 2442 2242 C ATOM 2339 O LYS C 182 -21.027 -25.757 -13.031 1.00104.16 O ANISOU 2339 O LYS C 182 11653 9867 18057 1253 2665 1890 O ATOM 2340 CB LYS C 182 -18.165 -24.604 -11.568 1.00106.16 C ANISOU 2340 CB LYS C 182 11116 10534 18686 1514 2471 2856 C ATOM 2341 N GLU C 183 -21.250 -24.579 -11.121 1.00 98.67 N ANISOU 2341 N GLU C 183 10660 9679 17150 1116 2063 2276 N ATOM 2342 CA GLU C 183 -22.724 -24.352 -11.251 1.00 95.07 C ANISOU 2342 CA GLU C 183 10465 9290 16367 919 1894 1948 C ATOM 2343 C GLU C 183 -23.141 -23.365 -12.354 1.00 90.68 C ANISOU 2343 C GLU C 183 10128 8865 15462 809 1857 1598 C ATOM 2344 O GLU C 183 -22.532 -22.306 -12.496 1.00 89.28 O ANISOU 2344 O GLU C 183 9865 8901 15154 814 1757 1655 O ATOM 2345 CB GLU C 183 -23.326 -23.857 -9.916 1.00 93.96 C ANISOU 2345 CB GLU C 183 10218 9414 16067 798 1530 2126 C ATOM 2346 CG GLU C 183 -24.879 -23.747 -9.914 1.00 94.65 C ANISOU 2346 CG GLU C 183 10533 9555 15873 617 1373 1850 C ATOM 2347 CD GLU C 183 -25.460 -23.060 -8.670 1.00 95.65 C ANISOU 2347 CD GLU C 183 10577 9965 15799 500 1037 2000 C ATOM 2348 OE1 GLU C 183 -25.084 -21.900 -8.429 1.00 97.70 O ANISOU 2348 OE1 GLU C 183 10769 10481 15871 460 861 2067 O ATOM 2349 OE2 GLU C 183 -26.297 -23.660 -7.950 1.00 96.97 O ANISOU 2349 OE2 GLU C 183 10761 10095 15989 440 958 2043 O ATOM 2350 N VAL C 184 -24.195 -23.690 -13.108 1.00 86.82 N ANISOU 2350 N VAL C 184 9913 8259 14815 691 1921 1256 N ATOM 2351 CA VAL C 184 -24.593 -22.846 -14.228 1.00 82.79 C ANISOU 2351 CA VAL C 184 9606 7865 13987 579 1902 943 C ATOM 2352 C VAL C 184 -25.975 -22.227 -13.961 1.00 78.41 C ANISOU 2352 C VAL C 184 9167 7518 13109 379 1609 799 C ATOM 2353 O VAL C 184 -26.935 -22.956 -13.687 1.00 77.46 O ANISOU 2353 O VAL C 184 9142 7291 12998 292 1581 729 O ATOM 2354 CB VAL C 184 -24.590 -23.610 -15.571 1.00 84.89 C ANISOU 2354 CB VAL C 184 10113 7847 14296 584 2239 650 C ATOM 2355 CG1 VAL C 184 -24.933 -22.656 -16.710 1.00 81.21 C ANISOU 2355 CG1 VAL C 184 9832 7543 13482 455 2195 365 C ATOM 2356 CG2 VAL C 184 -23.211 -24.282 -15.831 1.00 88.52 C ANISOU 2356 CG2 VAL C 184 10455 8065 15112 811 2583 806 C ATOM 2357 N LEU C 185 -26.062 -20.893 -14.042 1.00 73.31 N ANISOU 2357 N LEU C 185 8503 7156 12194 310 1404 772 N ATOM 2358 CA LEU C 185 -27.314 -20.188 -13.830 1.00 68.97 C ANISOU 2358 CA LEU C 185 8046 6808 11353 143 1152 659 C ATOM 2359 C LEU C 185 -27.824 -19.569 -15.147 1.00 67.14 C ANISOU 2359 C LEU C 185 8012 6646 10854 26 1173 365 C ATOM 2360 O LEU C 185 -27.017 -19.094 -15.943 1.00 66.16 O ANISOU 2360 O LEU C 185 7891 6546 10701 80 1283 313 O ATOM 2361 CB LEU C 185 -27.111 -19.101 -12.772 1.00 66.98 C ANISOU 2361 CB LEU C 185 7624 6824 11000 143 896 876 C ATOM 2362 CG LEU C 185 -26.677 -19.424 -11.340 1.00 69.00 C ANISOU 2362 CG LEU C 185 7676 7104 11436 208 798 1195 C ATOM 2363 CD1 LEU C 185 -26.026 -18.198 -10.643 1.00 69.57 C ANISOU 2363 CD1 LEU C 185 7604 7435 11394 203 601 1384 C ATOM 2364 CD2 LEU C 185 -27.821 -19.976 -10.525 1.00 69.00 C ANISOU 2364 CD2 LEU C 185 7715 7085 11418 126 687 1212 C ATOM 2365 N VAL C 186 -29.157 -19.542 -15.361 1.00 63.86 N ANISOU 2365 N VAL C 186 7742 6282 10241 -140 1058 200 N ATOM 2366 CA VAL C 186 -29.753 -18.765 -16.469 1.00 62.18 C ANISOU 2366 CA VAL C 186 7679 6204 9741 -277 1010 -22 C ATOM 2367 C VAL C 186 -30.795 -17.750 -15.949 1.00 59.26 C ANISOU 2367 C VAL C 186 7277 6091 9149 -382 734 19 C ATOM 2368 O VAL C 186 -31.466 -17.982 -14.916 1.00 58.52 O ANISOU 2368 O VAL C 186 7123 6017 9093 -401 607 137 O ATOM 2369 CB VAL C 186 -30.334 -19.591 -17.606 1.00 63.78 C ANISOU 2369 CB VAL C 186 8114 6238 9882 -409 1165 -284 C ATOM 2370 CG1 VAL C 186 -29.222 -20.432 -18.256 1.00 68.10 C ANISOU 2370 CG1 VAL C 186 8719 6524 10630 -293 1486 -349 C ATOM 2371 CG2 VAL C 186 -31.512 -20.481 -17.126 1.00 64.28 C ANISOU 2371 CG2 VAL C 186 8247 6203 9974 -528 1095 -305 C ATOM 2372 N TRP C 187 -30.897 -16.620 -16.638 1.00 56.14 N ANISOU 2372 N TRP C 187 6913 5882 8535 -438 659 -61 N ATOM 2373 CA TRP C 187 -31.940 -15.650 -16.329 1.00 53.31 C ANISOU 2373 CA TRP C 187 6540 5742 7974 -535 441 -35 C ATOM 2374 C TRP C 187 -33.324 -16.231 -16.658 1.00 54.68 C ANISOU 2374 C TRP C 187 6834 5888 8056 -701 395 -149 C ATOM 2375 O TRP C 187 -33.525 -16.710 -17.751 1.00 53.80 O ANISOU 2375 O TRP C 187 6867 5698 7878 -806 494 -328 O ATOM 2376 CB TRP C 187 -31.802 -14.382 -17.150 1.00 52.36 C ANISOU 2376 CB TRP C 187 6435 5806 7655 -567 391 -98 C ATOM 2377 CG TRP C 187 -30.941 -13.273 -16.563 1.00 48.12 C ANISOU 2377 CG TRP C 187 5763 5402 7119 -460 317 52 C ATOM 2378 CD1 TRP C 187 -31.259 -12.434 -15.525 1.00 48.44 C ANISOU 2378 CD1 TRP C 187 5721 5580 7105 -451 151 191 C ATOM 2379 CD2 TRP C 187 -29.629 -12.913 -16.973 1.00 49.75 C ANISOU 2379 CD2 TRP C 187 5915 5607 7380 -364 413 78 C ATOM 2380 NE1 TRP C 187 -30.275 -11.498 -15.364 1.00 48.05 N ANISOU 2380 NE1 TRP C 187 5590 5623 7046 -382 124 279 N ATOM 2381 CE2 TRP C 187 -29.241 -11.797 -16.212 1.00 48.24 C ANISOU 2381 CE2 TRP C 187 5613 5568 7149 -323 275 228 C ATOM 2382 CE3 TRP C 187 -28.738 -13.418 -17.926 1.00 50.16 C ANISOU 2382 CE3 TRP C 187 6008 5538 7511 -312 617 -11 C ATOM 2383 CZ2 TRP C 187 -27.979 -11.195 -16.357 1.00 49.73 C ANISOU 2383 CZ2 TRP C 187 5714 5802 7382 -241 311 309 C ATOM 2384 CZ3 TRP C 187 -27.533 -12.800 -18.102 1.00 53.93 C ANISOU 2384 CZ3 TRP C 187 6391 6067 8034 -214 666 72 C ATOM 2385 CH2 TRP C 187 -27.168 -11.669 -17.339 1.00 48.66 C ANISOU 2385 CH2 TRP C 187 5598 5567 7326 -186 499 236 C ATOM 2386 N ARG C 188 -34.265 -16.075 -15.749 1.00 54.22 N ANISOU 2386 N ARG C 188 6717 5915 7970 -737 240 -39 N ATOM 2387 CA ARG C 188 -35.641 -16.510 -15.995 1.00 56.62 C ANISOU 2387 CA ARG C 188 7101 6226 8186 -901 169 -103 C ATOM 2388 C ARG C 188 -36.598 -15.467 -15.498 1.00 54.34 C ANISOU 2388 C ARG C 188 6736 6155 7757 -937 -10 5 C ATOM 2389 O ARG C 188 -36.482 -15.049 -14.340 1.00 53.87 O ANISOU 2389 O ARG C 188 6570 6152 7748 -837 -76 160 O ATOM 2390 CB ARG C 188 -35.899 -17.848 -15.267 1.00 58.63 C ANISOU 2390 CB ARG C 188 7358 6286 8631 -899 215 -55 C ATOM 2391 CG ARG C 188 -35.179 -19.060 -15.873 1.00 65.32 C ANISOU 2391 CG ARG C 188 8314 6869 9636 -886 429 -181 C ATOM 2392 CD ARG C 188 -36.001 -19.993 -16.760 1.00 72.54 C ANISOU 2392 CD ARG C 188 9413 7651 10496 -1082 486 -366 C ATOM 2393 NE ARG C 188 -35.700 -19.931 -18.199 1.00 76.65 N ANISOU 2393 NE ARG C 188 10102 8145 10876 -1181 606 -586 N ATOM 2394 CZ ARG C 188 -34.969 -20.792 -18.910 1.00 80.43 C ANISOU 2394 CZ ARG C 188 10725 8387 11448 -1172 843 -742 C ATOM 2395 NH1 ARG C 188 -34.371 -21.842 -18.362 1.00 84.70 N ANISOU 2395 NH1 ARG C 188 11254 8669 12261 -1050 1009 -697 N ATOM 2396 NH2 ARG C 188 -34.823 -20.587 -20.214 1.00 82.05 N ANISOU 2396 NH2 ARG C 188 11092 8611 11472 -1286 932 -942 N ATOM 2397 N PHE C 189 -37.572 -15.101 -16.343 1.00 54.28 N ANISOU 2397 N PHE C 189 6784 6263 7577 -1090 -82 -64 N ATOM 2398 CA PHE C 189 -38.665 -14.231 -15.964 1.00 51.27 C ANISOU 2398 CA PHE C 189 6326 6068 7086 -1131 -228 54 C ATOM 2399 C PHE C 189 -39.624 -14.941 -15.013 1.00 53.01 C ANISOU 2399 C PHE C 189 6504 6245 7392 -1162 -286 162 C ATOM 2400 O PHE C 189 -39.884 -16.117 -15.188 1.00 54.92 O ANISOU 2400 O PHE C 189 6814 6344 7708 -1250 -248 100 O ATOM 2401 CB PHE C 189 -39.424 -13.754 -17.185 1.00 51.72 C ANISOU 2401 CB PHE C 189 6431 6262 6958 -1295 -287 -15 C ATOM 2402 CG PHE C 189 -40.492 -12.720 -16.872 1.00 51.55 C ANISOU 2402 CG PHE C 189 6304 6437 6847 -1313 -414 139 C ATOM 2403 CD1 PHE C 189 -41.831 -13.104 -16.632 1.00 53.03 C ANISOU 2403 CD1 PHE C 189 6453 6667 7029 -1427 -502 235 C ATOM 2404 CD2 PHE C 189 -40.176 -11.389 -16.832 1.00 50.42 C ANISOU 2404 CD2 PHE C 189 6097 6421 6638 -1218 -433 200 C ATOM 2405 CE1 PHE C 189 -42.799 -12.154 -16.329 1.00 53.89 C ANISOU 2405 CE1 PHE C 189 6449 6944 7084 -1420 -588 401 C ATOM 2406 CE2 PHE C 189 -41.141 -10.420 -16.544 1.00 49.90 C ANISOU 2406 CE2 PHE C 189 5938 6508 6514 -1216 -514 349 C ATOM 2407 CZ PHE C 189 -42.427 -10.784 -16.263 1.00 51.60 C ANISOU 2407 CZ PHE C 189 6102 6763 6740 -1302 -581 457 C ATOM 2408 N ASP C 190 -40.113 -14.238 -14.000 1.00 50.85 N ANISOU 2408 N ASP C 190 6129 6081 7110 -1090 -364 321 N ATOM 2409 CA ASP C 190 -41.098 -14.843 -13.059 1.00 52.32 C ANISOU 2409 CA ASP C 190 6264 6247 7367 -1116 -415 445 C ATOM 2410 C ASP C 190 -42.123 -13.769 -12.722 1.00 50.28 C ANISOU 2410 C ASP C 190 5924 6172 7008 -1116 -497 578 C ATOM 2411 O ASP C 190 -41.851 -12.841 -11.944 1.00 50.50 O ANISOU 2411 O ASP C 190 5905 6269 7013 -995 -493 661 O ATOM 2412 CB ASP C 190 -40.430 -15.363 -11.791 1.00 51.13 C ANISOU 2412 CB ASP C 190 6071 5989 7365 -989 -377 532 C ATOM 2413 CG ASP C 190 -41.419 -16.090 -10.823 1.00 54.80 C ANISOU 2413 CG ASP C 190 6486 6427 7910 -1020 -421 664 C ATOM 2414 OD1 ASP C 190 -42.665 -15.964 -10.956 1.00 57.12 O ANISOU 2414 OD1 ASP C 190 6753 6811 8140 -1115 -487 719 O ATOM 2415 OD2 ASP C 190 -40.921 -16.749 -9.889 1.00 56.51 O ANISOU 2415 OD2 ASP C 190 6670 6543 8257 -944 -390 738 O ATOM 2416 N SER C 191 -43.295 -13.899 -13.313 1.00 49.68 N ANISOU 2416 N SER C 191 5834 6168 6873 -1259 -561 606 N ATOM 2417 CA SER C 191 -44.398 -12.970 -13.145 1.00 50.44 C ANISOU 2417 CA SER C 191 5833 6432 6899 -1267 -622 760 C ATOM 2418 C SER C 191 -44.819 -12.742 -11.679 1.00 49.15 C ANISOU 2418 C SER C 191 5593 6281 6800 -1145 -607 923 C ATOM 2419 O SER C 191 -45.328 -11.659 -11.316 1.00 48.11 O ANISOU 2419 O SER C 191 5397 6263 6619 -1074 -599 1039 O ATOM 2420 CB SER C 191 -45.597 -13.441 -14.034 1.00 53.39 C ANISOU 2420 CB SER C 191 6189 6873 7223 -1476 -709 791 C ATOM 2421 OG SER C 191 -46.107 -14.657 -13.571 1.00 56.37 O ANISOU 2421 OG SER C 191 6573 7148 7698 -1551 -728 821 O ATOM 2422 N LYS C 192 -44.556 -13.719 -10.816 1.00 49.67 N ANISOU 2422 N LYS C 192 5673 6224 6976 -1113 -585 935 N ATOM 2423 CA LYS C 192 -44.953 -13.655 -9.389 1.00 48.99 C ANISOU 2423 CA LYS C 192 5528 6150 6938 -1019 -568 1090 C ATOM 2424 C LYS C 192 -44.155 -12.603 -8.666 1.00 47.93 C ANISOU 2424 C LYS C 192 5412 6053 6748 -879 -520 1100 C ATOM 2425 O LYS C 192 -44.584 -12.001 -7.701 1.00 49.38 O ANISOU 2425 O LYS C 192 5569 6294 6900 -808 -490 1213 O ATOM 2426 CB LYS C 192 -44.692 -15.002 -8.714 1.00 48.75 C ANISOU 2426 CB LYS C 192 5508 5975 7040 -1027 -561 1101 C ATOM 2427 CG LYS C 192 -45.661 -16.058 -9.245 1.00 55.92 C ANISOU 2427 CG LYS C 192 6405 6837 8004 -1184 -610 1111 C ATOM 2428 CD LYS C 192 -45.445 -17.382 -8.537 1.00 63.17 C ANISOU 2428 CD LYS C 192 7330 7596 9075 -1186 -592 1138 C ATOM 2429 CE LYS C 192 -44.301 -18.126 -9.190 1.00 61.05 C ANISOU 2429 CE LYS C 192 7157 7158 8881 -1198 -536 969 C ATOM 2430 NZ LYS C 192 -43.346 -18.173 -8.176 1.00 69.22 N ANISOU 2430 NZ LYS C 192 8165 8140 9994 -1054 -490 1028 N ATOM 2431 N LEU C 193 -42.968 -12.364 -9.162 1.00 46.26 N ANISOU 2431 N LEU C 193 5255 5805 6516 -849 -504 977 N ATOM 2432 CA LEU C 193 -42.071 -11.412 -8.528 1.00 44.17 C ANISOU 2432 CA LEU C 193 5016 5570 6196 -746 -473 981 C ATOM 2433 C LEU C 193 -42.510 -9.997 -8.739 1.00 43.47 C ANISOU 2433 C LEU C 193 4925 5595 5995 -715 -455 1007 C ATOM 2434 O LEU C 193 -41.975 -9.110 -8.115 1.00 47.48 O ANISOU 2434 O LEU C 193 5470 6127 6443 -646 -424 1019 O ATOM 2435 CB LEU C 193 -40.661 -11.612 -9.085 1.00 43.94 C ANISOU 2435 CB LEU C 193 5027 5471 6197 -728 -461 863 C ATOM 2436 CG LEU C 193 -40.005 -12.981 -8.885 1.00 44.49 C ANISOU 2436 CG LEU C 193 5094 5397 6411 -730 -445 848 C ATOM 2437 CD1 LEU C 193 -38.594 -13.001 -9.515 1.00 48.41 C ANISOU 2437 CD1 LEU C 193 5615 5832 6946 -691 -403 752 C ATOM 2438 CD2 LEU C 193 -39.846 -13.427 -7.411 1.00 46.68 C ANISOU 2438 CD2 LEU C 193 5336 5647 6755 -680 -454 986 C ATOM 2439 N ALA C 194 -43.487 -9.695 -9.566 1.00 43.86 N ANISOU 2439 N ALA C 194 4932 5718 6015 -771 -471 1032 N ATOM 2440 CA ALA C 194 -44.084 -8.325 -9.561 1.00 44.00 C ANISOU 2440 CA ALA C 194 4923 5834 5960 -719 -429 1112 C ATOM 2441 C ALA C 194 -44.893 -8.005 -8.312 1.00 45.87 C ANISOU 2441 C ALA C 194 5140 6085 6204 -649 -363 1253 C ATOM 2442 O ALA C 194 -45.067 -6.823 -7.934 1.00 44.19 O ANISOU 2442 O ALA C 194 4948 5905 5938 -571 -282 1301 O ATOM 2443 CB ALA C 194 -44.986 -8.131 -10.828 1.00 45.15 C ANISOU 2443 CB ALA C 194 4995 6073 6086 -810 -473 1149 C ATOM 2444 N PHE C 195 -45.360 -9.083 -7.645 1.00 46.32 N ANISOU 2444 N PHE C 195 5168 6102 6329 -676 -381 1317 N ATOM 2445 CA PHE C 195 -46.327 -9.001 -6.540 1.00 47.80 C ANISOU 2445 CA PHE C 195 5322 6311 6531 -626 -314 1469 C ATOM 2446 C PHE C 195 -45.680 -9.403 -5.216 1.00 48.47 C ANISOU 2446 C PHE C 195 5476 6336 6605 -586 -291 1468 C ATOM 2447 O PHE C 195 -46.070 -8.919 -4.162 1.00 50.89 O ANISOU 2447 O PHE C 195 5813 6659 6864 -525 -205 1552 O ATOM 2448 CB PHE C 195 -47.530 -9.957 -6.871 1.00 48.46 C ANISOU 2448 CB PHE C 195 5293 6418 6700 -714 -368 1580 C ATOM 2449 CG PHE C 195 -48.219 -9.575 -8.177 1.00 49.09 C ANISOU 2449 CG PHE C 195 5293 6586 6774 -788 -414 1613 C ATOM 2450 CD1 PHE C 195 -48.864 -8.346 -8.279 1.00 53.56 C ANISOU 2450 CD1 PHE C 195 5802 7235 7314 -718 -338 1727 C ATOM 2451 CD2 PHE C 195 -48.117 -10.354 -9.311 1.00 46.14 C ANISOU 2451 CD2 PHE C 195 4914 6207 6409 -930 -520 1528 C ATOM 2452 CE1 PHE C 195 -49.496 -7.959 -9.489 1.00 57.19 C ANISOU 2452 CE1 PHE C 195 6163 7796 7770 -794 -392 1797 C ATOM 2453 CE2 PHE C 195 -48.735 -9.968 -10.507 1.00 49.80 C ANISOU 2453 CE2 PHE C 195 5308 6777 6838 -1027 -577 1572 C ATOM 2454 CZ PHE C 195 -49.454 -8.810 -10.581 1.00 53.54 C ANISOU 2454 CZ PHE C 195 5690 7356 7298 -962 -526 1725 C ATOM 2455 N HIS C 196 -44.731 -10.309 -5.285 1.00 47.23 N ANISOU 2455 N HIS C 196 5342 6109 6495 -624 -360 1387 N ATOM 2456 CA HIS C 196 -44.146 -10.893 -4.075 1.00 46.50 C ANISOU 2456 CA HIS C 196 5282 5972 6415 -607 -363 1427 C ATOM 2457 C HIS C 196 -42.622 -10.670 -4.065 1.00 46.53 C ANISOU 2457 C HIS C 196 5348 5945 6387 -594 -392 1333 C ATOM 2458 O HIS C 196 -41.907 -11.117 -4.959 1.00 46.45 O ANISOU 2458 O HIS C 196 5324 5883 6440 -617 -433 1243 O ATOM 2459 CB HIS C 196 -44.401 -12.364 -4.010 1.00 46.53 C ANISOU 2459 CB HIS C 196 5223 5907 6549 -660 -414 1472 C ATOM 2460 CG HIS C 196 -43.782 -13.076 -2.823 1.00 44.67 C ANISOU 2460 CG HIS C 196 4995 5627 6349 -647 -426 1543 C ATOM 2461 ND1 HIS C 196 -43.084 -14.229 -2.955 1.00 41.95 N ANISOU 2461 ND1 HIS C 196 4622 5183 6134 -672 -470 1529 N ATOM 2462 CD2 HIS C 196 -43.760 -12.771 -1.505 1.00 45.44 C ANISOU 2462 CD2 HIS C 196 5127 5773 6366 -618 -394 1639 C ATOM 2463 CE1 HIS C 196 -42.634 -14.616 -1.771 1.00 46.21 C ANISOU 2463 CE1 HIS C 196 5154 5718 6685 -656 -480 1636 C ATOM 2464 NE2 HIS C 196 -43.059 -13.753 -0.859 1.00 42.94 N ANISOU 2464 NE2 HIS C 196 4784 5404 6129 -635 -442 1701 N ATOM 2465 N HIS C 197 -42.158 -10.072 -2.989 1.00 48.51 N ANISOU 2465 N HIS C 197 5667 6226 6539 -570 -367 1371 N ATOM 2466 CA HIS C 197 -40.689 -9.805 -2.820 1.00 48.54 C ANISOU 2466 CA HIS C 197 5717 6222 6503 -578 -411 1322 C ATOM 2467 C HIS C 197 -40.021 -10.985 -2.193 1.00 49.03 C ANISOU 2467 C HIS C 197 5728 6238 6662 -599 -469 1400 C ATOM 2468 O HIS C 197 -39.703 -11.002 -0.988 1.00 50.87 O ANISOU 2468 O HIS C 197 5990 6507 6830 -622 -487 1496 O ATOM 2469 CB HIS C 197 -40.464 -8.543 -2.013 1.00 49.71 C ANISOU 2469 CB HIS C 197 5979 6428 6482 -577 -368 1324 C ATOM 2470 CG HIS C 197 -39.072 -7.945 -2.178 1.00 48.26 C ANISOU 2470 CG HIS C 197 5840 6253 6242 -602 -419 1263 C ATOM 2471 ND1 HIS C 197 -38.617 -6.921 -1.385 1.00 51.12 N ANISOU 2471 ND1 HIS C 197 6323 6657 6444 -642 -404 1260 N ATOM 2472 CD2 HIS C 197 -38.045 -8.265 -3.014 1.00 51.87 C ANISOU 2472 CD2 HIS C 197 6240 6682 6786 -602 -479 1214 C ATOM 2473 CE1 HIS C 197 -37.354 -6.630 -1.721 1.00 55.68 C ANISOU 2473 CE1 HIS C 197 6900 7242 7013 -673 -475 1226 C ATOM 2474 NE2 HIS C 197 -36.987 -7.433 -2.711 1.00 54.95 N ANISOU 2474 NE2 HIS C 197 6691 7109 7077 -638 -513 1203 N ATOM 2475 N MET C 198 -39.787 -11.983 -3.010 1.00 49.59 N ANISOU 2475 N MET C 198 5729 6227 6887 -600 -492 1366 N ATOM 2476 CA MET C 198 -39.283 -13.251 -2.546 1.00 50.03 C ANISOU 2476 CA MET C 198 5718 6206 7085 -605 -523 1454 C ATOM 2477 C MET C 198 -38.010 -13.113 -1.698 1.00 51.65 C ANISOU 2477 C MET C 198 5916 6444 7266 -609 -570 1544 C ATOM 2478 O MET C 198 -37.862 -13.794 -0.662 1.00 49.53 O ANISOU 2478 O MET C 198 5603 6179 7039 -627 -603 1692 O ATOM 2479 CB MET C 198 -39.028 -14.185 -3.716 1.00 49.60 C ANISOU 2479 CB MET C 198 5622 6029 7196 -603 -508 1369 C ATOM 2480 CG MET C 198 -38.458 -15.523 -3.303 1.00 54.47 C ANISOU 2480 CG MET C 198 6167 6531 7999 -592 -510 1466 C ATOM 2481 SD MET C 198 -39.614 -16.597 -2.359 1.00 54.37 S ANISOU 2481 SD MET C 198 6107 6485 8067 -624 -519 1608 S ATOM 2482 CE MET C 198 -39.758 -17.998 -3.418 1.00 58.95 C ANISOU 2482 CE MET C 198 6668 6866 8864 -648 -471 1527 C ATOM 2483 N ALA C 199 -37.128 -12.239 -2.119 1.00 50.69 N ANISOU 2483 N ALA C 199 5828 6359 7074 -605 -583 1476 N ATOM 2484 CA ALA C 199 -35.810 -12.125 -1.465 1.00 52.46 C ANISOU 2484 CA ALA C 199 6024 6621 7285 -629 -646 1578 C ATOM 2485 C ALA C 199 -35.939 -11.844 0.024 1.00 55.06 C ANISOU 2485 C ALA C 199 6402 7050 7470 -697 -692 1708 C ATOM 2486 O ALA C 199 -35.010 -12.099 0.755 1.00 54.35 O ANISOU 2486 O ALA C 199 6263 7001 7389 -742 -765 1848 O ATOM 2487 CB ALA C 199 -34.933 -11.044 -2.121 1.00 49.50 C ANISOU 2487 CB ALA C 199 5689 6287 6831 -631 -658 1488 C ATOM 2488 N ARG C 200 -37.085 -11.306 0.478 1.00 55.48 N ANISOU 2488 N ARG C 200 6549 7147 7383 -710 -642 1675 N ATOM 2489 CA ARG C 200 -37.261 -10.990 1.905 1.00 57.77 C ANISOU 2489 CA ARG C 200 6918 7528 7503 -784 -658 1778 C ATOM 2490 C ARG C 200 -37.773 -12.097 2.762 1.00 56.77 C ANISOU 2490 C ARG C 200 6724 7398 7447 -795 -669 1928 C ATOM 2491 O ARG C 200 -37.854 -11.929 4.008 1.00 57.30 O ANISOU 2491 O ARG C 200 6857 7554 7362 -870 -685 2030 O ATOM 2492 CB ARG C 200 -38.209 -9.795 2.068 1.00 60.02 C ANISOU 2492 CB ARG C 200 7353 7851 7603 -784 -559 1679 C ATOM 2493 CG ARG C 200 -37.684 -8.541 1.407 1.00 67.38 C ANISOU 2493 CG ARG C 200 8371 8790 8441 -788 -545 1547 C ATOM 2494 CD ARG C 200 -38.397 -7.281 1.960 1.00 77.01 C ANISOU 2494 CD ARG C 200 9767 10039 9456 -808 -435 1484 C ATOM 2495 NE ARG C 200 -37.562 -6.570 2.938 1.00 82.70 N ANISOU 2495 NE ARG C 200 10627 10822 9974 -933 -476 1501 N ATOM 2496 CZ ARG C 200 -36.812 -5.490 2.675 1.00 88.38 C ANISOU 2496 CZ ARG C 200 11445 11548 10589 -986 -491 1415 C ATOM 2497 NH1 ARG C 200 -36.764 -4.951 1.452 1.00 89.39 N ANISOU 2497 NH1 ARG C 200 11540 11628 10799 -910 -462 1308 N ATOM 2498 NH2 ARG C 200 -36.095 -4.928 3.647 1.00 90.12 N ANISOU 2498 NH2 ARG C 200 11802 11830 10609 -1135 -543 1441 N ATOM 2499 N GLU C 201 -38.079 -13.259 2.176 1.00 54.13 N ANISOU 2499 N GLU C 201 6270 6964 7333 -736 -661 1950 N ATOM 2500 CA GLU C 201 -38.653 -14.310 2.963 1.00 53.63 C ANISOU 2500 CA GLU C 201 6140 6888 7349 -745 -666 2097 C ATOM 2501 C GLU C 201 -37.525 -15.040 3.744 1.00 55.75 C ANISOU 2501 C GLU C 201 6314 7177 7692 -789 -758 2288 C ATOM 2502 O GLU C 201 -36.526 -15.465 3.183 1.00 53.32 O ANISOU 2502 O GLU C 201 5916 6803 7541 -759 -790 2309 O ATOM 2503 CB GLU C 201 -39.423 -15.341 2.139 1.00 51.98 C ANISOU 2503 CB GLU C 201 5847 6552 7349 -692 -626 2064 C ATOM 2504 CG GLU C 201 -40.623 -14.793 1.371 1.00 54.22 C ANISOU 2504 CG GLU C 201 6185 6833 7584 -667 -556 1930 C ATOM 2505 CD GLU C 201 -41.728 -14.222 2.234 1.00 54.74 C ANISOU 2505 CD GLU C 201 6312 6989 7496 -677 -499 1984 C ATOM 2506 OE1 GLU C 201 -41.742 -14.539 3.435 1.00 52.55 O ANISOU 2506 OE1 GLU C 201 6035 6764 7167 -710 -512 2123 O ATOM 2507 OE2 GLU C 201 -42.555 -13.431 1.710 1.00 50.08 O ANISOU 2507 OE2 GLU C 201 5767 6421 6839 -650 -431 1899 O ATOM 2508 N LEU C 202 -37.723 -15.227 5.033 1.00 56.63 N ANISOU 2508 N LEU C 202 6435 7380 7701 -857 -792 2446 N ATOM 2509 CA LEU C 202 -36.766 -16.012 5.809 1.00 58.39 C ANISOU 2509 CA LEU C 202 6541 7637 8009 -906 -889 2674 C ATOM 2510 C LEU C 202 -36.859 -17.492 5.384 1.00 58.96 C ANISOU 2510 C LEU C 202 6451 7553 8397 -826 -867 2762 C ATOM 2511 O LEU C 202 -35.844 -18.202 5.339 1.00 58.39 O ANISOU 2511 O LEU C 202 6245 7428 8512 -807 -910 2902 O ATOM 2512 CB LEU C 202 -37.076 -15.822 7.293 1.00 60.84 C ANISOU 2512 CB LEU C 202 6919 8098 8101 -1018 -926 2818 C ATOM 2513 CG LEU C 202 -36.334 -16.617 8.363 1.00 65.67 C ANISOU 2513 CG LEU C 202 7411 8791 8751 -1102 -1038 3103 C ATOM 2514 CD1 LEU C 202 -34.821 -16.233 8.395 1.00 73.88 C ANISOU 2514 CD1 LEU C 202 8401 9905 9764 -1176 -1156 3194 C ATOM 2515 CD2 LEU C 202 -37.019 -16.490 9.798 1.00 72.33 C ANISOU 2515 CD2 LEU C 202 8349 9782 9349 -1216 -1044 3219 C ATOM 2516 N HIS C 203 -38.077 -17.957 5.067 1.00 57.76 N ANISOU 2516 N HIS C 203 6310 7319 8316 -782 -793 2691 N ATOM 2517 CA HIS C 203 -38.348 -19.357 4.652 1.00 58.62 C ANISOU 2517 CA HIS C 203 6302 7260 8712 -728 -760 2749 C ATOM 2518 C HIS C 203 -38.958 -19.426 3.228 1.00 57.42 C ANISOU 2518 C HIS C 203 6190 6969 8656 -677 -682 2524 C ATOM 2519 O HIS C 203 -40.200 -19.583 3.068 1.00 55.46 O ANISOU 2519 O HIS C 203 5972 6703 8399 -686 -645 2472 O ATOM 2520 CB HIS C 203 -39.346 -19.987 5.628 1.00 60.40 C ANISOU 2520 CB HIS C 203 6498 7520 8932 -762 -760 2898 C ATOM 2521 CG HIS C 203 -38.733 -20.320 6.947 1.00 65.40 C ANISOU 2521 CG HIS C 203 7059 8261 9529 -822 -840 3156 C ATOM 2522 ND1 HIS C 203 -38.317 -21.588 7.269 1.00 72.09 N ANISOU 2522 ND1 HIS C 203 7749 9018 10622 -805 -866 3367 N ATOM 2523 CD2 HIS C 203 -38.310 -19.515 7.952 1.00 71.31 C ANISOU 2523 CD2 HIS C 203 7872 9199 10025 -912 -906 3241 C ATOM 2524 CE1 HIS C 203 -37.721 -21.559 8.454 1.00 78.19 C ANISOU 2524 CE1 HIS C 203 8473 9943 11293 -883 -956 3596 C ATOM 2525 NE2 HIS C 203 -37.679 -20.306 8.875 1.00 72.42 N ANISOU 2525 NE2 HIS C 203 7883 9386 10246 -961 -987 3516 N ATOM 2526 N PRO C 204 -38.126 -19.341 2.205 1.00 56.83 N ANISOU 2526 N PRO C 204 6112 6809 8673 -634 -659 2408 N ATOM 2527 CA PRO C 204 -38.637 -19.331 0.815 1.00 56.55 C ANISOU 2527 CA PRO C 204 6133 6663 8688 -613 -592 2187 C ATOM 2528 C PRO C 204 -39.383 -20.586 0.421 1.00 56.17 C ANISOU 2528 C PRO C 204 6053 6452 8839 -621 -547 2184 C ATOM 2529 O PRO C 204 -40.248 -20.562 -0.466 1.00 52.62 O ANISOU 2529 O PRO C 204 5663 5958 8373 -653 -517 2033 O ATOM 2530 CB PRO C 204 -37.385 -19.107 -0.054 1.00 58.04 C ANISOU 2530 CB PRO C 204 6316 6792 8944 -566 -568 2100 C ATOM 2531 CG PRO C 204 -36.198 -19.263 0.851 1.00 60.00 C ANISOU 2531 CG PRO C 204 6466 7087 9245 -554 -620 2309 C ATOM 2532 CD PRO C 204 -36.667 -19.084 2.276 1.00 60.01 C ANISOU 2532 CD PRO C 204 6464 7238 9099 -618 -697 2478 C ATOM 2533 N GLU C 205 -39.157 -21.669 1.148 1.00 56.75 N ANISOU 2533 N GLU C 205 6029 6445 9087 -612 -551 2369 N ATOM 2534 CA GLU C 205 -39.777 -22.892 0.752 1.00 57.33 C ANISOU 2534 CA GLU C 205 6082 6335 9365 -629 -500 2362 C ATOM 2535 C GLU C 205 -41.322 -22.876 0.807 1.00 55.86 C ANISOU 2535 C GLU C 205 5934 6199 9089 -700 -519 2333 C ATOM 2536 O GLU C 205 -41.965 -23.631 0.116 1.00 58.66 O ANISOU 2536 O GLU C 205 6310 6416 9563 -748 -486 2257 O ATOM 2537 CB GLU C 205 -39.164 -24.060 1.518 1.00 61.48 C ANISOU 2537 CB GLU C 205 6484 6750 10125 -596 -489 2588 C ATOM 2538 CG GLU C 205 -39.498 -24.172 3.051 1.00 63.45 C ANISOU 2538 CG GLU C 205 6653 7146 10309 -625 -569 2844 C ATOM 2539 CD GLU C 205 -38.547 -23.337 3.920 1.00 67.21 C ANISOU 2539 CD GLU C 205 7097 7814 10627 -622 -645 2974 C ATOM 2540 OE1 GLU C 205 -37.820 -22.434 3.377 1.00 64.11 O ANISOU 2540 OE1 GLU C 205 6755 7474 10128 -603 -649 2851 O ATOM 2541 OE2 GLU C 205 -38.551 -23.586 5.148 1.00 69.26 O ANISOU 2541 OE2 GLU C 205 7283 8177 10854 -657 -707 3205 O ATOM 2542 N TYR C 206 -41.931 -21.996 1.592 1.00 53.43 N ANISOU 2542 N TYR C 206 5642 6087 8571 -715 -562 2394 N ATOM 2543 CA TYR C 206 -43.402 -21.947 1.666 1.00 53.01 C ANISOU 2543 CA TYR C 206 5599 6089 8451 -767 -564 2401 C ATOM 2544 C TYR C 206 -43.981 -21.190 0.451 1.00 49.63 C ANISOU 2544 C TYR C 206 5248 5686 7925 -794 -548 2201 C ATOM 2545 O TYR C 206 -45.225 -21.182 0.241 1.00 52.00 O ANISOU 2545 O TYR C 206 5539 6021 8196 -847 -552 2209 O ATOM 2546 CB TYR C 206 -43.889 -21.353 2.986 1.00 51.92 C ANISOU 2546 CB TYR C 206 5453 6134 8141 -763 -579 2555 C ATOM 2547 CG TYR C 206 -43.390 -22.079 4.236 1.00 54.90 C ANISOU 2547 CG TYR C 206 5751 6523 8587 -761 -610 2778 C ATOM 2548 CD1 TYR C 206 -42.613 -21.421 5.170 1.00 57.20 C ANISOU 2548 CD1 TYR C 206 6061 6952 8719 -757 -642 2865 C ATOM 2549 CD2 TYR C 206 -43.698 -23.406 4.459 1.00 60.93 C ANISOU 2549 CD2 TYR C 206 6424 7162 9567 -781 -614 2909 C ATOM 2550 CE1 TYR C 206 -42.157 -22.080 6.351 1.00 57.95 C ANISOU 2550 CE1 TYR C 206 6073 7086 8859 -779 -688 3101 C ATOM 2551 CE2 TYR C 206 -43.215 -24.111 5.617 1.00 62.97 C ANISOU 2551 CE2 TYR C 206 6588 7434 9903 -781 -647 3148 C ATOM 2552 CZ TYR C 206 -42.427 -23.435 6.530 1.00 60.67 C ANISOU 2552 CZ TYR C 206 6306 7304 9443 -781 -689 3247 C ATOM 2553 OH TYR C 206 -42.029 -24.074 7.670 1.00 60.46 O ANISOU 2553 OH TYR C 206 6182 7323 9465 -803 -736 3501 O ATOM 2554 N TYR C 207 -43.115 -20.603 -0.351 1.00 49.10 N ANISOU 2554 N TYR C 207 5236 5604 7815 -765 -535 2050 N ATOM 2555 CA TYR C 207 -43.505 -19.755 -1.511 1.00 49.67 C ANISOU 2555 CA TYR C 207 5377 5721 7776 -790 -527 1873 C ATOM 2556 C TYR C 207 -43.121 -20.373 -2.867 1.00 51.41 C ANISOU 2556 C TYR C 207 5640 5782 8110 -832 -501 1705 C ATOM 2557 O TYR C 207 -43.158 -19.679 -3.892 1.00 51.02 O ANISOU 2557 O TYR C 207 5650 5772 7965 -855 -497 1556 O ATOM 2558 CB TYR C 207 -42.870 -18.321 -1.346 1.00 48.67 C ANISOU 2558 CB TYR C 207 5300 5733 7459 -730 -524 1825 C ATOM 2559 CG TYR C 207 -43.278 -17.762 0.025 1.00 47.64 C ANISOU 2559 CG TYR C 207 5164 5739 7197 -709 -525 1972 C ATOM 2560 CD1 TYR C 207 -42.625 -18.110 1.157 1.00 46.64 C ANISOU 2560 CD1 TYR C 207 5009 5628 7083 -697 -548 2111 C ATOM 2561 CD2 TYR C 207 -44.346 -16.923 0.145 1.00 49.32 C ANISOU 2561 CD2 TYR C 207 5402 6060 7278 -709 -492 1981 C ATOM 2562 CE1 TYR C 207 -43.051 -17.648 2.389 1.00 51.51 C ANISOU 2562 CE1 TYR C 207 5646 6372 7555 -701 -539 2234 C ATOM 2563 CE2 TYR C 207 -44.792 -16.474 1.341 1.00 46.24 C ANISOU 2563 CE2 TYR C 207 5027 5772 6770 -690 -457 2101 C ATOM 2564 CZ TYR C 207 -44.143 -16.820 2.476 1.00 47.73 C ANISOU 2564 CZ TYR C 207 5214 5981 6941 -694 -481 2215 C ATOM 2565 OH TYR C 207 -44.699 -16.403 3.666 1.00 47.21 O ANISOU 2565 OH TYR C 207 5183 6021 6733 -694 -433 2328 O ATOM 2566 N LYS C 208 -42.623 -21.593 -2.856 1.00 56.17 N ANISOU 2566 N LYS C 208 6224 6206 8914 -834 -468 1730 N ATOM 2567 CA LYS C 208 -42.390 -22.338 -4.082 1.00 60.66 C ANISOU 2567 CA LYS C 208 6861 6590 9598 -889 -411 1566 C ATOM 2568 C LYS C 208 -43.000 -23.698 -3.932 1.00 63.84 C ANISOU 2568 C LYS C 208 7248 6828 10180 -963 -397 1628 C ATOM 2569 O LYS C 208 -43.127 -24.210 -2.819 1.00 65.25 O ANISOU 2569 O LYS C 208 7340 7003 10449 -930 -416 1817 O ATOM 2570 CB LYS C 208 -40.906 -22.352 -4.560 1.00 61.94 C ANISOU 2570 CB LYS C 208 7047 6648 9838 -803 -333 1482 C ATOM 2571 CG LYS C 208 -39.784 -23.044 -3.795 1.00 66.66 C ANISOU 2571 CG LYS C 208 7561 7138 10630 -703 -284 1630 C ATOM 2572 CD LYS C 208 -38.432 -22.280 -4.191 1.00 71.24 C ANISOU 2572 CD LYS C 208 8142 7754 11173 -612 -247 1573 C ATOM 2573 CE LYS C 208 -37.205 -22.440 -3.272 1.00 74.77 C ANISOU 2573 CE LYS C 208 8468 8201 11741 -511 -243 1777 C ATOM 2574 NZ LYS C 208 -36.038 -21.401 -3.554 1.00 68.36 N ANISOU 2574 NZ LYS C 208 7646 7492 10837 -448 -247 1746 N ATOM 2575 N ASP C 209 -43.453 -24.286 -5.020 1.00 68.58 N ANISOU 2575 N ASP C 209 7938 7300 10819 -1083 -371 1476 N ATOM 2576 CA ASP C 209 -44.096 -25.615 -4.893 1.00 73.70 C ANISOU 2576 CA ASP C 209 8589 7774 11641 -1180 -360 1529 C ATOM 2577 C ASP C 209 -43.027 -26.702 -5.008 1.00 76.71 C ANISOU 2577 C ASP C 209 9001 7883 12264 -1121 -230 1500 C ATOM 2578 O ASP C 209 -42.088 -26.562 -5.770 1.00 77.37 O ANISOU 2578 O ASP C 209 9157 7880 12360 -1073 -138 1353 O ATOM 2579 CB ASP C 209 -45.257 -25.800 -5.900 1.00 75.42 C ANISOU 2579 CB ASP C 209 8891 7987 11777 -1380 -410 1409 C ATOM 2580 CG ASP C 209 -46.253 -26.948 -5.489 1.00 80.25 C ANISOU 2580 CG ASP C 209 9472 8492 12526 -1502 -446 1526 C ATOM 2581 OD1 ASP C 209 -47.006 -26.868 -4.446 1.00 80.38 O ANISOU 2581 OD1 ASP C 209 9363 8637 12540 -1481 -517 1738 O ATOM 2582 OD2 ASP C 209 -46.301 -27.961 -6.236 1.00 88.03 O ANISOU 2582 OD2 ASP C 209 10571 9253 13622 -1632 -392 1400 O ATOM 2583 N ALA C 210 -43.155 -27.738 -4.182 1.00 81.12 N ANISOU 2583 N ALA C 210 9489 8313 13022 -1109 -213 1666 N ATOM 2584 CA ALA C 210 -42.308 -28.974 -4.253 1.00 84.74 C ANISOU 2584 CA ALA C 210 9965 8466 13765 -1059 -67 1673 C ATOM 2585 C ALA C 210 -43.210 -30.218 -4.319 1.00 87.64 C ANISOU 2585 C ALA C 210 10379 8634 14286 -1200 -52 1684 C ATOM 2586 O ALA C 210 -42.765 -31.392 -4.287 1.00 90.90 O ANISOU 2586 O ALA C 210 10811 8764 14964 -1179 75 1711 O ATOM 2587 CB ALA C 210 -41.344 -29.072 -3.048 1.00 84.88 C ANISOU 2587 CB ALA C 210 9820 8505 13924 -886 -51 1922 C ATOM 2588 OXT ALA C 210 -44.442 -30.074 -4.411 1.00 88.30 O ANISOU 2588 OXT ALA C 210 10478 8833 14238 -1347 -165 1678 O TER 2589 ALA C 210 ATOM 2590 N MET D 78 -48.292 31.078 -15.304 1.00112.10 N ANISOU 2590 N MET D 78 15855 13783 12955 4490 1172 -412 N ATOM 2591 CA MET D 78 -47.138 31.176 -16.248 1.00108.79 C ANISOU 2591 CA MET D 78 15470 13079 12787 4012 811 -414 C ATOM 2592 C MET D 78 -47.649 31.144 -17.719 1.00106.05 C ANISOU 2592 C MET D 78 14687 12858 12748 3911 802 -117 C ATOM 2593 O MET D 78 -48.838 31.385 -17.964 1.00108.57 O ANISOU 2593 O MET D 78 14776 13368 13108 4254 1020 44 O ATOM 2594 CB MET D 78 -46.111 30.057 -15.939 1.00105.73 C ANISOU 2594 CB MET D 78 15032 12804 12336 3553 660 -446 C ATOM 2595 CG MET D 78 -45.721 29.873 -14.418 1.00109.29 C ANISOU 2595 CG MET D 78 15856 13233 12437 3650 682 -694 C ATOM 2596 SD MET D 78 -45.326 31.376 -13.403 1.00118.22 S ANISOU 2596 SD MET D 78 17749 13827 13342 3977 543 -1092 S ATOM 2597 CE MET D 78 -44.255 30.686 -12.112 1.00116.08 C ANISOU 2597 CE MET D 78 17782 13563 12761 3733 370 -1303 C ATOM 2598 N GLU D 79 -46.748 30.911 -18.683 1.00101.29 N ANISOU 2598 N GLU D 79 13988 12148 12351 3470 550 -40 N ATOM 2599 CA GLU D 79 -47.086 30.702 -20.120 1.00 97.94 C ANISOU 2599 CA GLU D 79 13169 11874 12170 3309 509 238 C ATOM 2600 C GLU D 79 -46.587 29.309 -20.560 1.00 91.61 C ANISOU 2600 C GLU D 79 12059 11351 11397 2868 441 354 C ATOM 2601 O GLU D 79 -45.903 28.631 -19.786 1.00 89.50 O ANISOU 2601 O GLU D 79 11894 11114 10998 2690 411 228 O ATOM 2602 CB GLU D 79 -46.457 31.788 -21.023 1.00 98.80 C ANISOU 2602 CB GLU D 79 13475 11577 12486 3218 281 249 C ATOM 2603 CG GLU D 79 -47.442 32.832 -21.614 1.00103.25 C ANISOU 2603 CG GLU D 79 14011 12045 13174 3592 359 378 C ATOM 2604 CD GLU D 79 -48.406 32.260 -22.676 1.00103.35 C ANISOU 2604 CD GLU D 79 13511 12455 13303 3585 449 693 C ATOM 2605 OE1 GLU D 79 -48.395 31.024 -22.918 1.00100.68 O ANISOU 2605 OE1 GLU D 79 12856 12462 12937 3302 461 796 O ATOM 2606 OE2 GLU D 79 -49.188 33.057 -23.259 1.00106.03 O ANISOU 2606 OE2 GLU D 79 13780 12746 13761 3867 488 841 O ATOM 2607 N ASP D 80 -46.943 28.884 -21.778 1.00 87.23 N ANISOU 2607 N ASP D 80 11154 10990 11000 2712 410 589 N ATOM 2608 CA ASP D 80 -46.605 27.532 -22.228 1.00 82.52 C ANISOU 2608 CA ASP D 80 10291 10648 10414 2342 358 689 C ATOM 2609 C ASP D 80 -45.115 27.463 -22.533 1.00 77.13 C ANISOU 2609 C ASP D 80 9793 9730 9783 2000 148 599 C ATOM 2610 O ASP D 80 -44.623 28.226 -23.353 1.00 77.44 O ANISOU 2610 O ASP D 80 9924 9542 9957 1931 13 642 O ATOM 2611 CB ASP D 80 -47.391 27.126 -23.484 1.00 82.57 C ANISOU 2611 CB ASP D 80 9924 10904 10546 2271 348 945 C ATOM 2612 CG ASP D 80 -48.746 26.448 -23.171 1.00 86.14 C ANISOU 2612 CG ASP D 80 10032 11741 10956 2426 532 1102 C ATOM 2613 OD1 ASP D 80 -49.192 26.373 -21.998 1.00 88.31 O ANISOU 2613 OD1 ASP D 80 10338 12115 11102 2646 721 1038 O ATOM 2614 OD2 ASP D 80 -49.365 25.964 -24.140 1.00 90.25 O ANISOU 2614 OD2 ASP D 80 10240 12481 11572 2311 478 1311 O ATOM 2615 N ILE D 81 -44.388 26.577 -21.862 1.00 71.87 N ANISOU 2615 N ILE D 81 9168 9120 9019 1795 124 502 N ATOM 2616 CA ILE D 81 -42.986 26.306 -22.269 1.00 66.35 C ANISOU 2616 CA ILE D 81 8545 8273 8394 1456 -61 477 C ATOM 2617 C ILE D 81 -43.005 25.225 -23.355 1.00 60.73 C ANISOU 2617 C ILE D 81 7533 7799 7741 1227 -67 646 C ATOM 2618 O ILE D 81 -43.355 24.077 -23.124 1.00 58.12 O ANISOU 2618 O ILE D 81 7031 7713 7338 1152 7 680 O ATOM 2619 CB ILE D 81 -42.100 25.922 -21.062 1.00 66.01 C ANISOU 2619 CB ILE D 81 8699 8155 8226 1354 -114 304 C ATOM 2620 CG1 ILE D 81 -42.115 27.047 -20.017 1.00 71.64 C ANISOU 2620 CG1 ILE D 81 9773 8605 8842 1593 -138 107 C ATOM 2621 CG2 ILE D 81 -40.637 25.600 -21.479 1.00 60.63 C ANISOU 2621 CG2 ILE D 81 8035 7354 7646 1015 -297 320 C ATOM 2622 CD1 ILE D 81 -41.827 26.565 -18.565 1.00 73.31 C ANISOU 2622 CD1 ILE D 81 10166 8859 8827 1619 -119 -63 C ATOM 2623 N ILE D 82 -42.619 25.612 -24.553 1.00 57.96 N ANISOU 2623 N ILE D 82 7149 7360 7514 1117 -164 756 N ATOM 2624 CA ILE D 82 -42.547 24.699 -25.692 1.00 53.46 C ANISOU 2624 CA ILE D 82 6368 6978 6966 920 -188 893 C ATOM 2625 C ILE D 82 -41.056 24.399 -25.959 1.00 49.48 C ANISOU 2625 C ILE D 82 5942 6357 6500 671 -282 876 C ATOM 2626 O ILE D 82 -40.205 25.302 -25.961 1.00 49.16 O ANISOU 2626 O ILE D 82 6057 6073 6548 632 -371 864 O ATOM 2627 CB ILE D 82 -43.218 25.341 -26.934 1.00 55.08 C ANISOU 2627 CB ILE D 82 6475 7208 7245 1005 -214 1060 C ATOM 2628 CG1 ILE D 82 -44.697 25.723 -26.634 1.00 60.74 C ANISOU 2628 CG1 ILE D 82 7077 8048 7953 1286 -118 1110 C ATOM 2629 CG2 ILE D 82 -43.064 24.419 -28.160 1.00 50.22 C ANISOU 2629 CG2 ILE D 82 5706 6770 6606 803 -263 1178 C ATOM 2630 CD1 ILE D 82 -45.649 24.555 -26.327 1.00 60.83 C ANISOU 2630 CD1 ILE D 82 6839 8381 7891 1273 -32 1157 C ATOM 2631 N VAL D 83 -40.750 23.127 -26.134 1.00 46.58 N ANISOU 2631 N VAL D 83 5463 6157 6079 508 -265 887 N ATOM 2632 CA VAL D 83 -39.403 22.655 -26.463 1.00 44.53 C ANISOU 2632 CA VAL D 83 5226 5845 5850 308 -317 901 C ATOM 2633 C VAL D 83 -39.480 21.800 -27.763 1.00 43.94 C ANISOU 2633 C VAL D 83 5022 5937 5735 217 -299 1008 C ATOM 2634 O VAL D 83 -40.556 21.250 -28.113 1.00 41.46 O ANISOU 2634 O VAL D 83 4604 5793 5357 254 -277 1037 O ATOM 2635 CB VAL D 83 -38.790 21.808 -25.295 1.00 42.39 C ANISOU 2635 CB VAL D 83 4993 5587 5525 227 -315 787 C ATOM 2636 CG1 VAL D 83 -38.664 22.707 -24.022 1.00 41.23 C ANISOU 2636 CG1 VAL D 83 5032 5264 5372 321 -362 661 C ATOM 2637 CG2 VAL D 83 -39.669 20.551 -25.037 1.00 43.67 C ANISOU 2637 CG2 VAL D 83 5035 5973 5586 231 -235 777 C ATOM 2638 N VAL D 84 -38.350 21.741 -28.473 1.00 41.66 N ANISOU 2638 N VAL D 84 4749 5600 5481 105 -315 1077 N ATOM 2639 CA VAL D 84 -38.222 20.954 -29.671 1.00 40.35 C ANISOU 2639 CA VAL D 84 4527 5568 5236 46 -287 1153 C ATOM 2640 C VAL D 84 -37.120 19.939 -29.387 1.00 41.49 C ANISOU 2640 C VAL D 84 4674 5725 5367 -55 -252 1112 C ATOM 2641 O VAL D 84 -36.061 20.243 -28.806 1.00 40.09 O ANISOU 2641 O VAL D 84 4513 5437 5283 -108 -267 1117 O ATOM 2642 CB VAL D 84 -37.928 21.852 -30.898 1.00 43.26 C ANISOU 2642 CB VAL D 84 4908 5898 5631 61 -294 1313 C ATOM 2643 CG1 VAL D 84 -36.599 22.675 -30.717 1.00 42.18 C ANISOU 2643 CG1 VAL D 84 4806 5584 5636 -9 -305 1392 C ATOM 2644 CG2 VAL D 84 -37.927 21.055 -32.244 1.00 41.71 C ANISOU 2644 CG2 VAL D 84 4699 5864 5285 38 -261 1382 C ATOM 2645 N ALA D 85 -37.371 18.738 -29.800 1.00 40.30 N ANISOU 2645 N ALA D 85 4508 5696 5109 -82 -226 1079 N ATOM 2646 CA ALA D 85 -36.381 17.709 -29.726 1.00 40.77 C ANISOU 2646 CA ALA D 85 4581 5763 5146 -136 -180 1053 C ATOM 2647 C ALA D 85 -35.244 17.868 -30.693 1.00 40.12 C ANISOU 2647 C ALA D 85 4499 5680 5066 -130 -112 1167 C ATOM 2648 O ALA D 85 -35.447 18.003 -31.882 1.00 40.93 O ANISOU 2648 O ALA D 85 4629 5847 5074 -91 -84 1238 O ATOM 2649 CB ALA D 85 -37.058 16.294 -29.894 1.00 40.74 C ANISOU 2649 CB ALA D 85 4606 5849 5025 -163 -189 973 C ATOM 2650 N LEU D 86 -34.015 17.715 -30.181 1.00 38.84 N ANISOU 2650 N LEU D 86 4293 5469 4996 -164 -78 1201 N ATOM 2651 CA LEU D 86 -32.828 17.700 -30.993 1.00 39.65 C ANISOU 2651 CA LEU D 86 4345 5606 5114 -145 22 1343 C ATOM 2652 C LEU D 86 -32.319 16.357 -31.346 1.00 40.46 C ANISOU 2652 C LEU D 86 4476 5782 5114 -82 124 1309 C ATOM 2653 O LEU D 86 -31.515 16.233 -32.267 1.00 40.15 O ANISOU 2653 O LEU D 86 4417 5812 5028 -8 252 1427 O ATOM 2654 CB LEU D 86 -31.709 18.466 -30.256 1.00 41.47 C ANISOU 2654 CB LEU D 86 4469 5742 5546 -228 -20 1451 C ATOM 2655 CG LEU D 86 -32.010 19.898 -29.840 1.00 45.79 C ANISOU 2655 CG LEU D 86 5034 6149 6217 -292 -143 1480 C ATOM 2656 CD1 LEU D 86 -30.790 20.535 -29.079 1.00 48.07 C ANISOU 2656 CD1 LEU D 86 5238 6317 6711 -418 -239 1581 C ATOM 2657 CD2 LEU D 86 -32.383 20.735 -31.017 1.00 48.21 C ANISOU 2657 CD2 LEU D 86 5355 6466 6495 -255 -107 1608 C ATOM 2658 N TYR D 87 -32.755 15.318 -30.635 1.00 38.27 N ANISOU 2658 N TYR D 87 4256 5487 4796 -93 82 1163 N ATOM 2659 CA TYR D 87 -32.274 13.929 -30.852 1.00 38.42 C ANISOU 2659 CA TYR D 87 4341 5524 4732 -21 162 1112 C ATOM 2660 C TYR D 87 -33.490 13.002 -30.675 1.00 39.73 C ANISOU 2660 C TYR D 87 4634 5668 4793 -60 74 954 C ATOM 2661 O TYR D 87 -34.485 13.402 -30.021 1.00 38.29 O ANISOU 2661 O TYR D 87 4421 5481 4647 -142 -27 912 O ATOM 2662 CB TYR D 87 -31.202 13.587 -29.748 1.00 39.68 C ANISOU 2662 CB TYR D 87 4395 5641 5040 -36 167 1152 C ATOM 2663 CG TYR D 87 -30.127 14.563 -29.673 1.00 39.94 C ANISOU 2663 CG TYR D 87 4266 5685 5225 -63 188 1324 C ATOM 2664 CD1 TYR D 87 -29.052 14.497 -30.555 1.00 46.17 C ANISOU 2664 CD1 TYR D 87 4967 6553 6024 35 343 1486 C ATOM 2665 CD2 TYR D 87 -30.137 15.588 -28.763 1.00 43.24 C ANISOU 2665 CD2 TYR D 87 4619 6032 5779 -183 54 1345 C ATOM 2666 CE1 TYR D 87 -27.988 15.447 -30.528 1.00 50.07 C ANISOU 2666 CE1 TYR D 87 5260 7069 6698 -23 355 1707 C ATOM 2667 CE2 TYR D 87 -29.076 16.529 -28.723 1.00 44.36 C ANISOU 2667 CE2 TYR D 87 4611 6153 6091 -251 30 1527 C ATOM 2668 CZ TYR D 87 -28.044 16.452 -29.609 1.00 49.67 C ANISOU 2668 CZ TYR D 87 5152 6917 6804 -188 174 1721 C ATOM 2669 OH TYR D 87 -27.070 17.376 -29.556 1.00 57.13 O ANISOU 2669 OH TYR D 87 5919 7847 7942 -289 134 1934 O ATOM 2670 N ASP D 88 -33.457 11.799 -31.216 1.00 40.56 N ANISOU 2670 N ASP D 88 4879 5754 4777 -2 107 879 N ATOM 2671 CA ASP D 88 -34.513 10.810 -30.967 1.00 39.33 C ANISOU 2671 CA ASP D 88 4837 5546 4561 -81 -8 754 C ATOM 2672 C ASP D 88 -34.348 10.225 -29.526 1.00 39.28 C ANISOU 2672 C ASP D 88 4770 5473 4680 -141 -39 740 C ATOM 2673 O ASP D 88 -33.215 9.912 -29.112 1.00 37.92 O ANISOU 2673 O ASP D 88 4563 5268 4577 -70 37 783 O ATOM 2674 CB ASP D 88 -34.374 9.660 -31.952 1.00 41.51 C ANISOU 2674 CB ASP D 88 5334 5765 4671 1 16 666 C ATOM 2675 CG ASP D 88 -34.646 10.055 -33.392 1.00 46.51 C ANISOU 2675 CG ASP D 88 6083 6470 5116 64 25 663 C ATOM 2676 OD1 ASP D 88 -35.232 11.136 -33.651 1.00 44.34 O ANISOU 2676 OD1 ASP D 88 5711 6287 4850 12 -22 733 O ATOM 2677 OD2 ASP D 88 -34.319 9.249 -34.241 1.00 45.01 O ANISOU 2677 OD2 ASP D 88 6106 6238 4758 176 72 587 O ATOM 2678 N TYR D 89 -35.465 9.957 -28.836 1.00 37.36 N ANISOU 2678 N TYR D 89 4514 5226 4455 -260 -145 702 N ATOM 2679 CA TYR D 89 -35.479 9.262 -27.524 1.00 36.92 C ANISOU 2679 CA TYR D 89 4430 5122 4476 -320 -174 704 C ATOM 2680 C TYR D 89 -36.521 8.112 -27.566 1.00 39.30 C ANISOU 2680 C TYR D 89 4827 5367 4739 -433 -274 660 C ATOM 2681 O TYR D 89 -37.673 8.367 -27.930 1.00 37.61 O ANISOU 2681 O TYR D 89 4580 5216 4493 -520 -355 662 O ATOM 2682 CB TYR D 89 -35.770 10.236 -26.378 1.00 36.57 C ANISOU 2682 CB TYR D 89 4246 5147 4501 -356 -187 746 C ATOM 2683 CG TYR D 89 -36.030 9.518 -25.101 1.00 36.21 C ANISOU 2683 CG TYR D 89 4189 5087 4482 -417 -215 760 C ATOM 2684 CD1 TYR D 89 -35.040 8.769 -24.487 1.00 34.70 C ANISOU 2684 CD1 TYR D 89 4030 4824 4329 -388 -200 782 C ATOM 2685 CD2 TYR D 89 -37.303 9.463 -24.557 1.00 34.84 C ANISOU 2685 CD2 TYR D 89 3963 4983 4293 -496 -251 781 C ATOM 2686 CE1 TYR D 89 -35.333 8.024 -23.269 1.00 36.16 C ANISOU 2686 CE1 TYR D 89 4217 5000 4522 -449 -231 822 C ATOM 2687 CE2 TYR D 89 -37.594 8.704 -23.421 1.00 40.21 C ANISOU 2687 CE2 TYR D 89 4631 5667 4980 -556 -259 829 C ATOM 2688 CZ TYR D 89 -36.622 7.986 -22.780 1.00 36.49 C ANISOU 2688 CZ TYR D 89 4217 5115 4532 -537 -253 847 C ATOM 2689 OH TYR D 89 -36.939 7.273 -21.648 1.00 33.90 O ANISOU 2689 OH TYR D 89 3884 4800 4198 -595 -261 921 O ATOM 2690 N VAL D 90 -36.089 6.891 -27.251 1.00 38.83 N ANISOU 2690 N VAL D 90 4877 5180 4696 -433 -281 641 N ATOM 2691 CA VAL D 90 -36.975 5.728 -27.233 1.00 40.39 C ANISOU 2691 CA VAL D 90 5182 5276 4887 -569 -401 619 C ATOM 2692 C VAL D 90 -37.296 5.369 -25.766 1.00 40.33 C ANISOU 2692 C VAL D 90 5068 5282 4972 -665 -415 715 C ATOM 2693 O VAL D 90 -36.449 4.989 -24.990 1.00 39.63 O ANISOU 2693 O VAL D 90 4988 5140 4929 -602 -363 749 O ATOM 2694 CB VAL D 90 -36.434 4.544 -28.020 1.00 41.85 C ANISOU 2694 CB VAL D 90 5624 5266 5011 -504 -421 526 C ATOM 2695 CG1 VAL D 90 -37.443 3.230 -27.974 1.00 45.14 C ANISOU 2695 CG1 VAL D 90 6192 5511 5447 -702 -607 506 C ATOM 2696 CG2 VAL D 90 -36.158 4.907 -29.490 1.00 41.42 C ANISOU 2696 CG2 VAL D 90 5701 5227 4809 -384 -388 435 C ATOM 2697 N SER D 91 -38.545 5.556 -25.364 1.00 40.80 N ANISOU 2697 N SER D 91 5005 5444 5054 -804 -475 783 N ATOM 2698 CA SER D 91 -39.027 5.115 -24.047 1.00 41.59 C ANISOU 2698 CA SER D 91 5010 5581 5212 -898 -473 903 C ATOM 2699 C SER D 91 -39.167 3.599 -23.911 1.00 43.80 C ANISOU 2699 C SER D 91 5422 5676 5544 -1026 -568 944 C ATOM 2700 O SER D 91 -39.638 2.905 -24.835 1.00 42.19 O ANISOU 2700 O SER D 91 5347 5343 5340 -1134 -699 895 O ATOM 2701 CB SER D 91 -40.396 5.688 -23.773 1.00 44.36 C ANISOU 2701 CB SER D 91 5169 6114 5573 -992 -487 998 C ATOM 2702 OG SER D 91 -40.945 5.033 -22.644 1.00 47.67 O ANISOU 2702 OG SER D 91 5507 6571 6036 -1096 -477 1143 O ATOM 2703 N TRP D 92 -38.859 3.071 -22.731 1.00 42.02 N ANISOU 2703 N TRP D 92 5179 5427 5358 -1033 -529 1044 N ATOM 2704 CA TRP D 92 -39.116 1.676 -22.431 1.00 44.82 C ANISOU 2704 CA TRP D 92 5641 5602 5785 -1174 -622 1130 C ATOM 2705 C TRP D 92 -40.345 1.470 -21.514 1.00 46.65 C ANISOU 2705 C TRP D 92 5694 5964 6066 -1363 -639 1334 C ATOM 2706 O TRP D 92 -40.580 0.339 -21.106 1.00 49.90 O ANISOU 2706 O TRP D 92 6170 6232 6556 -1505 -715 1454 O ATOM 2707 CB TRP D 92 -37.949 1.020 -21.754 1.00 44.06 C ANISOU 2707 CB TRP D 92 5656 5374 5712 -1059 -577 1153 C ATOM 2708 CG TRP D 92 -36.710 0.859 -22.631 1.00 43.88 C ANISOU 2708 CG TRP D 92 5805 5196 5670 -866 -549 1004 C ATOM 2709 CD1 TRP D 92 -36.501 1.339 -23.906 1.00 44.57 C ANISOU 2709 CD1 TRP D 92 5964 5279 5694 -777 -536 853 C ATOM 2710 CD2 TRP D 92 -35.467 0.273 -22.221 1.00 45.12 C ANISOU 2710 CD2 TRP D 92 6049 5230 5863 -706 -500 1026 C ATOM 2711 NE1 TRP D 92 -35.228 0.985 -24.331 1.00 44.03 N ANISOU 2711 NE1 TRP D 92 6030 5085 5617 -567 -464 785 N ATOM 2712 CE2 TRP D 92 -34.583 0.331 -23.319 1.00 45.33 C ANISOU 2712 CE2 TRP D 92 6192 5174 5856 -518 -445 891 C ATOM 2713 CE3 TRP D 92 -35.041 -0.337 -21.057 1.00 46.23 C ANISOU 2713 CE3 TRP D 92 6177 5329 6057 -695 -498 1168 C ATOM 2714 CZ2 TRP D 92 -33.263 -0.195 -23.258 1.00 45.04 C ANISOU 2714 CZ2 TRP D 92 6229 5025 5860 -302 -372 905 C ATOM 2715 CZ3 TRP D 92 -33.733 -0.867 -21.000 1.00 49.11 C ANISOU 2715 CZ3 TRP D 92 6627 5566 6466 -495 -458 1175 C ATOM 2716 CH2 TRP D 92 -32.858 -0.775 -22.089 1.00 45.01 C ANISOU 2716 CH2 TRP D 92 6191 4979 5933 -295 -388 1048 C ATOM 2717 N SER D 93 -41.051 2.538 -21.164 1.00 44.23 N ANISOU 2717 N SER D 93 5170 5918 5717 -1342 -554 1389 N ATOM 2718 CA SER D 93 -42.012 2.512 -20.079 1.00 46.78 C ANISOU 2718 CA SER D 93 5296 6426 6053 -1434 -490 1604 C ATOM 2719 C SER D 93 -43.216 3.348 -20.480 1.00 46.46 C ANISOU 2719 C SER D 93 5035 6600 6017 -1472 -477 1654 C ATOM 2720 O SER D 93 -43.021 4.437 -21.060 1.00 44.56 O ANISOU 2720 O SER D 93 4783 6430 5718 -1326 -440 1512 O ATOM 2721 CB SER D 93 -41.405 3.154 -18.822 1.00 46.00 C ANISOU 2721 CB SER D 93 5167 6471 5842 -1254 -330 1626 C ATOM 2722 OG SER D 93 -42.422 3.526 -17.894 1.00 47.50 O ANISOU 2722 OG SER D 93 5157 6910 5981 -1263 -213 1803 O ATOM 2723 N PRO D 94 -44.410 2.935 -20.063 1.00 49.85 N ANISOU 2723 N PRO D 94 5265 7155 6522 -1642 -487 1885 N ATOM 2724 CA PRO D 94 -45.546 3.827 -20.262 1.00 50.67 C ANISOU 2724 CA PRO D 94 5105 7513 6633 -1626 -438 1974 C ATOM 2725 C PRO D 94 -45.475 5.183 -19.542 1.00 49.42 C ANISOU 2725 C PRO D 94 4855 7581 6341 -1348 -217 1934 C ATOM 2726 O PRO D 94 -46.226 6.103 -19.946 1.00 50.89 O ANISOU 2726 O PRO D 94 4871 7934 6529 -1268 -179 1948 O ATOM 2727 CB PRO D 94 -46.778 3.034 -19.747 1.00 53.93 C ANISOU 2727 CB PRO D 94 5276 8045 7169 -1861 -463 2293 C ATOM 2728 CG PRO D 94 -46.309 1.803 -19.225 1.00 57.35 C ANISOU 2728 CG PRO D 94 5863 8279 7649 -2001 -521 2371 C ATOM 2729 CD PRO D 94 -44.784 1.693 -19.381 1.00 51.84 C ANISOU 2729 CD PRO D 94 5495 7335 6865 -1847 -534 2109 C ATOM 2730 N ASP D 95 -44.554 5.347 -18.573 1.00 46.42 N ANISOU 2730 N ASP D 95 4613 7183 5843 -1195 -100 1869 N ATOM 2731 CA ASP D 95 -44.349 6.612 -17.868 1.00 46.16 C ANISOU 2731 CA ASP D 95 4578 7302 5660 -936 67 1788 C ATOM 2732 C ASP D 95 -43.412 7.627 -18.557 1.00 43.38 C ANISOU 2732 C ASP D 95 4378 6836 5271 -788 27 1535 C ATOM 2733 O ASP D 95 -43.411 8.820 -18.164 1.00 42.84 O ANISOU 2733 O ASP D 95 4311 6863 5103 -589 130 1459 O ATOM 2734 CB ASP D 95 -43.890 6.383 -16.391 1.00 47.33 C ANISOU 2734 CB ASP D 95 4808 7509 5666 -850 185 1856 C ATOM 2735 CG ASP D 95 -44.885 5.577 -15.582 1.00 55.00 C ANISOU 2735 CG ASP D 95 5602 8646 6648 -961 277 2151 C ATOM 2736 OD1 ASP D 95 -46.093 5.628 -15.919 1.00 56.47 O ANISOU 2736 OD1 ASP D 95 5542 8989 6924 -1033 310 2312 O ATOM 2737 OD2 ASP D 95 -44.457 4.835 -14.661 1.00 60.15 O ANISOU 2737 OD2 ASP D 95 6345 9273 7237 -995 301 2253 O ATOM 2738 N ASP D 96 -42.622 7.184 -19.544 1.00 42.15 N ANISOU 2738 N ASP D 96 4358 6473 5186 -869 -111 1416 N ATOM 2739 CA ASP D 96 -41.652 8.027 -20.229 1.00 42.59 C ANISOU 2739 CA ASP D 96 4534 6427 5221 -751 -138 1227 C ATOM 2740 C ASP D 96 -42.222 8.221 -21.669 1.00 42.26 C ANISOU 2740 C ASP D 96 4443 6371 5243 -812 -228 1195 C ATOM 2741 O ASP D 96 -42.849 7.290 -22.249 1.00 41.68 O ANISOU 2741 O ASP D 96 4340 6259 5236 -985 -335 1265 O ATOM 2742 CB ASP D 96 -40.287 7.337 -20.289 1.00 39.20 C ANISOU 2742 CB ASP D 96 4280 5808 4807 -763 -197 1151 C ATOM 2743 CG ASP D 96 -39.653 7.113 -18.872 1.00 43.31 C ANISOU 2743 CG ASP D 96 4854 6345 5257 -710 -147 1198 C ATOM 2744 OD1 ASP D 96 -40.035 7.860 -17.939 1.00 43.05 O ANISOU 2744 OD1 ASP D 96 4777 6460 5122 -617 -61 1222 O ATOM 2745 OD2 ASP D 96 -38.859 6.122 -18.696 1.00 45.96 O ANISOU 2745 OD2 ASP D 96 5287 6548 5629 -753 -199 1222 O ATOM 2746 N LEU D 97 -41.969 9.384 -22.220 1.00 41.72 N ANISOU 2746 N LEU D 97 4387 6315 5150 -684 -208 1097 N ATOM 2747 CA LEU D 97 -42.454 9.799 -23.525 1.00 40.88 C ANISOU 2747 CA LEU D 97 4242 6220 5070 -702 -284 1075 C ATOM 2748 C LEU D 97 -41.421 9.677 -24.642 1.00 40.14 C ANISOU 2748 C LEU D 97 4319 5972 4962 -699 -350 955 C ATOM 2749 O LEU D 97 -40.452 10.421 -24.638 1.00 39.62 O ANISOU 2749 O LEU D 97 4319 5857 4877 -582 -295 883 O ATOM 2750 CB LEU D 97 -42.984 11.251 -23.401 1.00 40.30 C ANISOU 2750 CB LEU D 97 4062 6272 4979 -537 -203 1084 C ATOM 2751 CG LEU D 97 -43.583 11.851 -24.666 1.00 42.41 C ANISOU 2751 CG LEU D 97 4265 6579 5270 -529 -278 1097 C ATOM 2752 CD1 LEU D 97 -44.922 11.198 -25.077 1.00 45.14 C ANISOU 2752 CD1 LEU D 97 4431 7050 5671 -677 -376 1241 C ATOM 2753 CD2 LEU D 97 -43.853 13.354 -24.482 1.00 43.02 C ANISOU 2753 CD2 LEU D 97 4287 6721 5339 -325 -190 1093 C ATOM 2754 N SER D 98 -41.616 8.743 -25.594 1.00 40.16 N ANISOU 2754 N SER D 98 4400 5893 4964 -823 -470 940 N ATOM 2755 CA SER D 98 -40.820 8.688 -26.807 1.00 40.76 C ANISOU 2755 CA SER D 98 4646 5859 4981 -780 -509 832 C ATOM 2756 C SER D 98 -41.007 9.934 -27.692 1.00 42.07 C ANISOU 2756 C SER D 98 4765 6113 5107 -689 -502 826 C ATOM 2757 O SER D 98 -42.100 10.560 -27.770 1.00 41.51 O ANISOU 2757 O SER D 98 4542 6171 5057 -702 -538 903 O ATOM 2758 CB SER D 98 -41.187 7.458 -27.645 1.00 41.10 C ANISOU 2758 CB SER D 98 4830 5790 4996 -924 -662 799 C ATOM 2759 OG SER D 98 -40.828 6.277 -26.967 1.00 41.42 O ANISOU 2759 OG SER D 98 4963 5695 5081 -992 -672 802 O ATOM 2760 N PHE D 99 -39.974 10.280 -28.400 1.00 39.88 N ANISOU 2760 N PHE D 99 4603 5772 4777 -589 -454 762 N ATOM 2761 CA PHE D 99 -40.071 11.360 -29.408 1.00 40.19 C ANISOU 2761 CA PHE D 99 4629 5875 4767 -512 -455 779 C ATOM 2762 C PHE D 99 -38.954 11.202 -30.424 1.00 40.51 C ANISOU 2762 C PHE D 99 4834 5844 4714 -432 -407 726 C ATOM 2763 O PHE D 99 -37.939 10.535 -30.205 1.00 39.60 O ANISOU 2763 O PHE D 99 4807 5639 4602 -392 -337 684 O ATOM 2764 CB PHE D 99 -40.070 12.782 -28.763 1.00 38.65 C ANISOU 2764 CB PHE D 99 4304 5736 4646 -412 -375 831 C ATOM 2765 CG PHE D 99 -38.912 13.023 -27.846 1.00 38.34 C ANISOU 2765 CG PHE D 99 4284 5620 4662 -357 -284 806 C ATOM 2766 CD1 PHE D 99 -37.695 13.409 -28.331 1.00 37.79 C ANISOU 2766 CD1 PHE D 99 4270 5489 4598 -298 -231 809 C ATOM 2767 CD2 PHE D 99 -39.054 12.843 -26.455 1.00 36.38 C ANISOU 2767 CD2 PHE D 99 3987 5379 4457 -370 -259 802 C ATOM 2768 CE1 PHE D 99 -36.632 13.599 -27.477 1.00 39.30 C ANISOU 2768 CE1 PHE D 99 4451 5620 4862 -277 -188 810 C ATOM 2769 CE2 PHE D 99 -38.001 13.047 -25.586 1.00 37.05 C ANISOU 2769 CE2 PHE D 99 4102 5398 4577 -336 -220 781 C ATOM 2770 CZ PHE D 99 -36.804 13.431 -26.070 1.00 38.69 C ANISOU 2770 CZ PHE D 99 4346 5537 4816 -301 -201 785 C ATOM 2771 N GLN D 100 -39.162 11.875 -31.541 1.00 42.47 N ANISOU 2771 N GLN D 100 5109 6152 4876 -387 -432 754 N ATOM 2772 CA GLN D 100 -38.196 11.970 -32.577 1.00 43.21 C ANISOU 2772 CA GLN D 100 5334 6227 4856 -282 -353 746 C ATOM 2773 C GLN D 100 -37.718 13.373 -32.736 1.00 41.60 C ANISOU 2773 C GLN D 100 5029 6072 4705 -197 -263 852 C ATOM 2774 O GLN D 100 -38.451 14.329 -32.469 1.00 40.70 O ANISOU 2774 O GLN D 100 4797 6003 4666 -209 -309 913 O ATOM 2775 CB GLN D 100 -38.840 11.510 -33.902 1.00 45.00 C ANISOU 2775 CB GLN D 100 5726 6483 4889 -306 -476 702 C ATOM 2776 CG GLN D 100 -39.373 10.140 -33.848 1.00 53.37 C ANISOU 2776 CG GLN D 100 6920 7454 5904 -424 -615 596 C ATOM 2777 CD GLN D 100 -38.338 9.126 -34.117 1.00 59.69 C ANISOU 2777 CD GLN D 100 7946 8124 6611 -333 -532 490 C ATOM 2778 OE1 GLN D 100 -37.578 8.755 -33.224 1.00 69.75 O ANISOU 2778 OE1 GLN D 100 9177 9325 8001 -295 -423 487 O ATOM 2779 NE2 GLN D 100 -38.294 8.631 -35.354 1.00 68.99 N ANISOU 2779 NE2 GLN D 100 9385 9269 7560 -277 -586 400 N ATOM 2780 N LYS D 101 -36.504 13.536 -33.274 1.00 41.45 N ANISOU 2780 N LYS D 101 5059 6042 4648 -99 -132 896 N ATOM 2781 CA LYS D 101 -35.997 14.879 -33.464 1.00 41.32 C ANISOU 2781 CA LYS D 101 4942 6051 4707 -51 -63 1033 C ATOM 2782 C LYS D 101 -36.958 15.757 -34.317 1.00 40.54 C ANISOU 2782 C LYS D 101 4843 6024 4537 -45 -144 1105 C ATOM 2783 O LYS D 101 -37.484 15.297 -35.311 1.00 39.78 O ANISOU 2783 O LYS D 101 4866 5992 4258 -34 -205 1077 O ATOM 2784 CB LYS D 101 -34.627 14.917 -34.115 1.00 44.17 C ANISOU 2784 CB LYS D 101 5322 6431 5032 47 98 1127 C ATOM 2785 CG LYS D 101 -34.452 14.186 -35.347 1.00 51.33 C ANISOU 2785 CG LYS D 101 6403 7396 5705 148 163 1099 C ATOM 2786 CD LYS D 101 -32.884 14.217 -35.714 1.00 61.50 C ANISOU 2786 CD LYS D 101 7642 8725 7000 281 386 1234 C ATOM 2787 CE LYS D 101 -32.448 12.776 -36.030 1.00 68.62 C ANISOU 2787 CE LYS D 101 8724 9604 7744 408 471 1107 C ATOM 2788 NZ LYS D 101 -33.319 12.373 -37.247 1.00 71.40 N ANISOU 2788 NZ LYS D 101 9339 9991 7797 451 396 999 N ATOM 2789 N GLY D 102 -37.096 17.011 -33.916 1.00 39.56 N ANISOU 2789 N GLY D 102 4605 5871 4553 -42 -154 1198 N ATOM 2790 CA GLY D 102 -38.046 17.959 -34.533 1.00 40.87 C ANISOU 2790 CA GLY D 102 4746 6085 4696 -15 -235 1288 C ATOM 2791 C GLY D 102 -39.428 17.935 -33.932 1.00 41.59 C ANISOU 2791 C GLY D 102 4759 6208 4835 -43 -353 1236 C ATOM 2792 O GLY D 102 -40.186 18.845 -34.223 1.00 42.50 O ANISOU 2792 O GLY D 102 4817 6352 4978 8 -410 1327 O ATOM 2793 N ASP D 103 -39.757 16.936 -33.090 1.00 41.56 N ANISOU 2793 N ASP D 103 4734 6205 4851 -111 -379 1121 N ATOM 2794 CA ASP D 103 -41.044 16.927 -32.378 1.00 44.04 C ANISOU 2794 CA ASP D 103 4925 6577 5232 -132 -455 1114 C ATOM 2795 C ASP D 103 -41.110 18.071 -31.394 1.00 43.25 C ANISOU 2795 C ASP D 103 4745 6415 5274 -40 -396 1140 C ATOM 2796 O ASP D 103 -40.111 18.359 -30.663 1.00 41.47 O ANISOU 2796 O ASP D 103 4565 6074 5119 -29 -323 1098 O ATOM 2797 CB ASP D 103 -41.264 15.647 -31.588 1.00 43.32 C ANISOU 2797 CB ASP D 103 4823 6490 5145 -234 -475 1022 C ATOM 2798 CG ASP D 103 -41.644 14.444 -32.471 1.00 45.56 C ANISOU 2798 CG ASP D 103 5201 6811 5299 -343 -596 982 C ATOM 2799 OD1 ASP D 103 -41.966 14.543 -33.650 1.00 48.20 O ANISOU 2799 OD1 ASP D 103 5600 7200 5514 -345 -689 1015 O ATOM 2800 OD2 ASP D 103 -41.656 13.372 -31.884 1.00 45.58 O ANISOU 2800 OD2 ASP D 103 5228 6773 5318 -435 -615 917 O ATOM 2801 N GLN D 104 -42.297 18.657 -31.316 1.00 42.63 N ANISOU 2801 N GLN D 104 4553 6410 5234 31 -440 1206 N ATOM 2802 CA GLN D 104 -42.564 19.685 -30.317 1.00 44.17 C ANISOU 2802 CA GLN D 104 4705 6539 5538 164 -378 1207 C ATOM 2803 C GLN D 104 -43.309 19.198 -29.096 1.00 43.50 C ANISOU 2803 C GLN D 104 4520 6531 5477 184 -333 1162 C ATOM 2804 O GLN D 104 -44.247 18.405 -29.233 1.00 44.52 O ANISOU 2804 O GLN D 104 4519 6814 5583 118 -381 1214 O ATOM 2805 CB GLN D 104 -43.318 20.855 -30.941 1.00 46.53 C ANISOU 2805 CB GLN D 104 4951 6852 5878 301 -414 1330 C ATOM 2806 CG GLN D 104 -42.320 21.718 -31.732 1.00 51.20 C ANISOU 2806 CG GLN D 104 5669 7302 6482 310 -416 1389 C ATOM 2807 CD GLN D 104 -42.857 23.037 -32.131 1.00 57.26 C ANISOU 2807 CD GLN D 104 6425 8011 7320 461 -443 1512 C ATOM 2808 OE1 GLN D 104 -42.235 24.090 -31.819 1.00 63.29 O ANISOU 2808 OE1 GLN D 104 7292 8569 8186 522 -419 1520 O ATOM 2809 NE2 GLN D 104 -43.960 23.031 -32.873 1.00 50.36 N ANISOU 2809 NE2 GLN D 104 5436 7294 6404 512 -518 1625 N ATOM 2810 N MET D 105 -42.941 19.691 -27.916 1.00 42.97 N ANISOU 2810 N MET D 105 4515 6363 5447 270 -252 1084 N ATOM 2811 CA MET D 105 -43.576 19.221 -26.647 1.00 43.96 C ANISOU 2811 CA MET D 105 4567 6580 5555 313 -174 1051 C ATOM 2812 C MET D 105 -43.827 20.424 -25.746 1.00 46.43 C ANISOU 2812 C MET D 105 4943 6812 5887 537 -93 1009 C ATOM 2813 O MET D 105 -43.052 21.391 -25.798 1.00 47.72 O ANISOU 2813 O MET D 105 5268 6776 6086 586 -123 954 O ATOM 2814 CB MET D 105 -42.705 18.175 -25.931 1.00 42.09 C ANISOU 2814 CB MET D 105 4407 6308 5277 176 -161 962 C ATOM 2815 CG MET D 105 -42.676 16.831 -26.629 1.00 41.74 C ANISOU 2815 CG MET D 105 4322 6333 5206 -9 -227 989 C ATOM 2816 SD MET D 105 -41.374 15.686 -26.128 1.00 44.62 S ANISOU 2816 SD MET D 105 4809 6600 5543 -140 -223 900 S ATOM 2817 CE MET D 105 -39.893 16.495 -26.882 1.00 43.35 C ANISOU 2817 CE MET D 105 4776 6283 5411 -119 -235 871 C ATOM 2818 N VAL D 106 -44.878 20.377 -24.917 1.00 47.25 N ANISOU 2818 N VAL D 106 4932 7059 5963 676 10 1043 N ATOM 2819 CA VAL D 106 -45.060 21.378 -23.851 1.00 49.65 C ANISOU 2819 CA VAL D 106 5355 7279 6232 928 116 963 C ATOM 2820 C VAL D 106 -44.554 20.794 -22.522 1.00 50.58 C ANISOU 2820 C VAL D 106 5587 7394 6239 898 178 850 C ATOM 2821 O VAL D 106 -44.829 19.599 -22.222 1.00 48.41 O ANISOU 2821 O VAL D 106 5175 7291 5928 771 213 912 O ATOM 2822 CB VAL D 106 -46.548 21.844 -23.727 1.00 53.59 C ANISOU 2822 CB VAL D 106 5661 7954 6745 1180 234 1088 C ATOM 2823 CG1 VAL D 106 -47.513 20.681 -23.558 1.00 55.65 C ANISOU 2823 CG1 VAL D 106 5634 8512 6998 1093 293 1240 C ATOM 2824 CG2 VAL D 106 -46.720 22.839 -22.602 1.00 55.83 C ANISOU 2824 CG2 VAL D 106 6121 8139 6955 1489 368 980 C ATOM 2825 N VAL D 107 -43.794 21.609 -21.763 1.00 49.70 N ANISOU 2825 N VAL D 107 5736 7071 6076 992 162 694 N ATOM 2826 CA VAL D 107 -43.165 21.165 -20.547 1.00 50.12 C ANISOU 2826 CA VAL D 107 5938 7099 6006 956 176 581 C ATOM 2827 C VAL D 107 -44.177 21.432 -19.393 1.00 53.32 C ANISOU 2827 C VAL D 107 6365 7634 6260 1239 361 562 C ATOM 2828 O VAL D 107 -44.607 22.545 -19.199 1.00 55.99 O ANISOU 2828 O VAL D 107 6822 7877 6572 1496 416 503 O ATOM 2829 CB VAL D 107 -41.842 21.894 -20.271 1.00 49.77 C ANISOU 2829 CB VAL D 107 6170 6769 5972 896 27 431 C ATOM 2830 CG1 VAL D 107 -41.255 21.461 -18.911 1.00 50.71 C ANISOU 2830 CG1 VAL D 107 6454 6879 5934 874 15 317 C ATOM 2831 CG2 VAL D 107 -40.839 21.583 -21.347 1.00 48.40 C ANISOU 2831 CG2 VAL D 107 5937 6515 5938 647 -105 490 C ATOM 2832 N LEU D 108 -44.584 20.374 -18.709 1.00 54.42 N ANISOU 2832 N LEU D 108 6377 7996 6305 1198 468 637 N ATOM 2833 CA LEU D 108 -45.602 20.411 -17.641 1.00 56.57 C ANISOU 2833 CA LEU D 108 6609 8468 6418 1459 689 681 C ATOM 2834 C LEU D 108 -44.965 20.501 -16.258 1.00 58.82 C ANISOU 2834 C LEU D 108 7195 8678 6475 1546 712 515 C ATOM 2835 O LEU D 108 -45.570 21.089 -15.330 1.00 59.16 O ANISOU 2835 O LEU D 108 7364 8781 6332 1861 884 460 O ATOM 2836 CB LEU D 108 -46.422 19.142 -17.752 1.00 57.13 C ANISOU 2836 CB LEU D 108 6339 8833 6532 1322 779 910 C ATOM 2837 CG LEU D 108 -47.192 19.001 -19.076 1.00 56.23 C ANISOU 2837 CG LEU D 108 5925 8820 6620 1228 726 1084 C ATOM 2838 CD1 LEU D 108 -47.903 17.640 -19.035 1.00 60.45 C ANISOU 2838 CD1 LEU D 108 6161 9610 7198 1035 765 1305 C ATOM 2839 CD2 LEU D 108 -48.165 20.198 -19.250 1.00 57.36 C ANISOU 2839 CD2 LEU D 108 5998 9010 6789 1560 844 1130 C ATOM 2840 N GLU D 109 -43.760 19.911 -16.102 1.00 56.05 N ANISOU 2840 N GLU D 109 6965 8209 6120 1292 543 442 N ATOM 2841 CA GLU D 109 -42.996 20.098 -14.859 1.00 59.96 C ANISOU 2841 CA GLU D 109 7778 8601 6402 1346 492 275 C ATOM 2842 C GLU D 109 -41.497 19.913 -15.046 1.00 58.30 C ANISOU 2842 C GLU D 109 7697 8179 6275 1073 234 190 C ATOM 2843 O GLU D 109 -41.083 19.128 -15.887 1.00 53.88 O ANISOU 2843 O GLU D 109 6946 7639 5887 836 161 296 O ATOM 2844 CB GLU D 109 -43.513 19.214 -13.717 1.00 63.42 C ANISOU 2844 CB GLU D 109 8172 9299 6624 1419 669 366 C ATOM 2845 CG GLU D 109 -43.128 17.734 -13.798 1.00 67.16 C ANISOU 2845 CG GLU D 109 8461 9888 7169 1123 618 518 C ATOM 2846 CD GLU D 109 -42.909 17.068 -12.407 1.00 73.47 C ANISOU 2846 CD GLU D 109 9394 10808 7714 1149 676 533 C ATOM 2847 OE1 GLU D 109 -42.119 16.078 -12.268 1.00 70.00 O ANISOU 2847 OE1 GLU D 109 8940 10352 7305 917 556 588 O ATOM 2848 OE2 GLU D 109 -43.561 17.537 -11.466 1.00 81.50 O ANISOU 2848 OE2 GLU D 109 10533 11945 8488 1427 856 503 O ATOM 2849 N GLU D 110 -40.718 20.682 -14.305 1.00 60.79 N ANISOU 2849 N GLU D 110 8338 8287 6471 1121 93 4 N ATOM 2850 CA GLU D 110 -39.272 20.627 -14.342 1.00 62.85 C ANISOU 2850 CA GLU D 110 8708 8357 6814 874 -168 -56 C ATOM 2851 C GLU D 110 -38.687 20.483 -12.969 1.00 65.95 C ANISOU 2851 C GLU D 110 9358 8735 6965 886 -265 -166 C ATOM 2852 O GLU D 110 -37.979 21.326 -12.527 1.00 69.27 O ANISOU 2852 O GLU D 110 10060 8930 7331 880 -466 -325 O ATOM 2853 CB GLU D 110 -38.628 21.859 -14.988 1.00 64.20 C ANISOU 2853 CB GLU D 110 9021 8225 7147 827 -358 -150 C ATOM 2854 CG GLU D 110 -39.432 22.526 -16.013 1.00 66.53 C ANISOU 2854 CG GLU D 110 9203 8491 7585 944 -257 -98 C ATOM 2855 CD GLU D 110 -38.652 23.607 -16.756 1.00 70.80 C ANISOU 2855 CD GLU D 110 9853 8726 8320 840 -459 -136 C ATOM 2856 OE1 GLU D 110 -38.947 23.835 -17.955 1.00 71.55 O ANISOU 2856 OE1 GLU D 110 9771 8819 8595 818 -418 -19 O ATOM 2857 OE2 GLU D 110 -37.735 24.198 -16.164 1.00 71.99 O ANISOU 2857 OE2 GLU D 110 10260 8647 8447 760 -673 -260 O ATOM 2858 N SER D 111 -38.953 19.378 -12.297 1.00 68.06 N ANISOU 2858 N SER D 111 9536 9236 7089 882 -147 -66 N ATOM 2859 CA SER D 111 -38.239 19.040 -11.082 1.00 70.09 C ANISOU 2859 CA SER D 111 10008 9500 7124 846 -270 -127 C ATOM 2860 C SER D 111 -37.178 18.107 -11.553 1.00 66.17 C ANISOU 2860 C SER D 111 9326 8988 6830 552 -429 -4 C ATOM 2861 O SER D 111 -37.462 17.087 -12.126 1.00 68.29 O ANISOU 2861 O SER D 111 9325 9396 7225 461 -313 165 O ATOM 2862 CB SER D 111 -39.143 18.290 -10.114 1.00 72.10 C ANISOU 2862 CB SER D 111 10245 10037 7112 1012 -29 -37 C ATOM 2863 OG SER D 111 -40.336 19.014 -9.984 1.00 79.12 O ANISOU 2863 OG SER D 111 11183 11002 7877 1314 203 -83 O ATOM 2864 N GLY D 112 -35.947 18.434 -11.335 1.00 64.31 N ANISOU 2864 N GLY D 112 9227 8575 6633 406 -704 -76 N ATOM 2865 CA GLY D 112 -34.886 17.547 -11.778 1.00 59.78 C ANISOU 2865 CA GLY D 112 8452 8001 6261 164 -835 65 C ATOM 2866 C GLY D 112 -34.695 17.565 -13.287 1.00 52.63 C ANISOU 2866 C GLY D 112 7297 7029 5671 49 -810 154 C ATOM 2867 O GLY D 112 -35.246 18.364 -13.992 1.00 53.07 O ANISOU 2867 O GLY D 112 7347 7014 5805 122 -743 107 O ATOM 2868 N GLU D 113 -33.897 16.645 -13.767 1.00 46.71 N ANISOU 2868 N GLU D 113 6352 6310 5084 -109 -857 291 N ATOM 2869 CA GLU D 113 -33.430 16.718 -15.124 1.00 44.10 C ANISOU 2869 CA GLU D 113 5830 5909 5017 -212 -862 370 C ATOM 2870 C GLU D 113 -34.313 15.901 -16.042 1.00 40.79 C ANISOU 2870 C GLU D 113 5227 5614 4658 -179 -645 457 C ATOM 2871 O GLU D 113 -34.147 15.957 -17.239 1.00 39.53 O ANISOU 2871 O GLU D 113 4938 5418 4665 -228 -616 509 O ATOM 2872 CB GLU D 113 -31.939 16.355 -15.166 1.00 41.25 C ANISOU 2872 CB GLU D 113 5375 5494 4804 -374 -1045 470 C ATOM 2873 CG GLU D 113 -31.016 17.396 -14.433 1.00 49.94 C ANISOU 2873 CG GLU D 113 6643 6436 5896 -462 -1331 396 C ATOM 2874 CD GLU D 113 -29.574 16.849 -14.176 1.00 56.41 C ANISOU 2874 CD GLU D 113 7332 7262 6839 -619 -1531 538 C ATOM 2875 OE1 GLU D 113 -29.001 16.116 -15.043 1.00 59.13 O ANISOU 2875 OE1 GLU D 113 7422 7666 7378 -665 -1451 701 O ATOM 2876 OE2 GLU D 113 -29.003 17.176 -13.126 1.00 63.24 O ANISOU 2876 OE2 GLU D 113 8353 8073 7603 -682 -1773 490 O ATOM 2877 N TRP D 114 -35.217 15.068 -15.480 1.00 41.44 N ANISOU 2877 N TRP D 114 5297 5848 4599 -113 -507 491 N ATOM 2878 CA TRP D 114 -36.263 14.463 -16.271 1.00 40.52 C ANISOU 2878 CA TRP D 114 5027 5836 4533 -97 -338 565 C ATOM 2879 C TRP D 114 -37.530 15.324 -16.122 1.00 42.32 C ANISOU 2879 C TRP D 114 5292 6128 4661 63 -218 508 C ATOM 2880 O TRP D 114 -38.047 15.493 -15.041 1.00 43.74 O ANISOU 2880 O TRP D 114 5578 6388 4651 185 -153 474 O ATOM 2881 CB TRP D 114 -36.496 13.025 -15.778 1.00 41.84 C ANISOU 2881 CB TRP D 114 5131 6118 4650 -147 -274 681 C ATOM 2882 CG TRP D 114 -35.403 12.056 -16.268 1.00 39.41 C ANISOU 2882 CG TRP D 114 4756 5735 4483 -267 -356 755 C ATOM 2883 CD1 TRP D 114 -34.158 11.847 -15.688 1.00 40.61 C ANISOU 2883 CD1 TRP D 114 4954 5830 4645 -308 -490 776 C ATOM 2884 CD2 TRP D 114 -35.436 11.211 -17.420 1.00 37.67 C ANISOU 2884 CD2 TRP D 114 4425 5485 4401 -333 -313 817 C ATOM 2885 NE1 TRP D 114 -33.445 10.934 -16.428 1.00 39.15 N ANISOU 2885 NE1 TRP D 114 4671 5593 4611 -366 -499 860 N ATOM 2886 CE2 TRP D 114 -34.218 10.507 -17.468 1.00 39.72 C ANISOU 2886 CE2 TRP D 114 4676 5670 4745 -375 -388 869 C ATOM 2887 CE3 TRP D 114 -36.368 10.966 -18.396 1.00 37.47 C ANISOU 2887 CE3 TRP D 114 4323 5488 4426 -353 -235 833 C ATOM 2888 CZ2 TRP D 114 -33.940 9.614 -18.465 1.00 37.79 C ANISOU 2888 CZ2 TRP D 114 4380 5367 4613 -402 -356 913 C ATOM 2889 CZ3 TRP D 114 -36.095 10.088 -19.342 1.00 37.69 C ANISOU 2889 CZ3 TRP D 114 4319 5451 4551 -413 -240 866 C ATOM 2890 CH2 TRP D 114 -34.877 9.400 -19.371 1.00 36.79 C ANISOU 2890 CH2 TRP D 114 4229 5249 4501 -423 -288 897 C ATOM 2891 N TRP D 115 -38.022 15.842 -17.205 1.00 41.55 N ANISOU 2891 N TRP D 115 5104 6005 4677 84 -177 512 N ATOM 2892 CA TRP D 115 -39.167 16.772 -17.181 1.00 43.95 C ANISOU 2892 CA TRP D 115 5423 6355 4920 265 -69 474 C ATOM 2893 C TRP D 115 -40.413 16.045 -17.642 1.00 44.26 C ANISOU 2893 C TRP D 115 5245 6584 4986 270 73 609 C ATOM 2894 O TRP D 115 -40.351 15.129 -18.494 1.00 42.55 O ANISOU 2894 O TRP D 115 4892 6390 4884 113 44 696 O ATOM 2895 CB TRP D 115 -38.894 17.899 -18.132 1.00 43.36 C ANISOU 2895 CB TRP D 115 5380 6121 4975 280 -145 422 C ATOM 2896 CG TRP D 115 -37.736 18.843 -17.744 1.00 44.29 C ANISOU 2896 CG TRP D 115 5705 6017 5105 252 -319 308 C ATOM 2897 CD1 TRP D 115 -37.074 18.901 -16.576 1.00 49.27 C ANISOU 2897 CD1 TRP D 115 6518 6590 5614 243 -424 222 C ATOM 2898 CD2 TRP D 115 -37.187 19.889 -18.560 1.00 46.50 C ANISOU 2898 CD2 TRP D 115 6027 6106 5536 212 -429 291 C ATOM 2899 NE1 TRP D 115 -36.140 19.936 -16.587 1.00 46.10 N ANISOU 2899 NE1 TRP D 115 6271 5956 5287 182 -620 142 N ATOM 2900 CE2 TRP D 115 -36.184 20.543 -17.801 1.00 48.29 C ANISOU 2900 CE2 TRP D 115 6456 6147 5746 156 -616 196 C ATOM 2901 CE3 TRP D 115 -37.481 20.361 -19.839 1.00 50.17 C ANISOU 2901 CE3 TRP D 115 6386 6538 6139 213 -400 364 C ATOM 2902 CZ2 TRP D 115 -35.401 21.589 -18.312 1.00 49.74 C ANISOU 2902 CZ2 TRP D 115 6710 6103 6087 67 -778 193 C ATOM 2903 CZ3 TRP D 115 -36.706 21.398 -20.355 1.00 49.07 C ANISOU 2903 CZ3 TRP D 115 6323 6188 6135 151 -532 366 C ATOM 2904 CH2 TRP D 115 -35.707 22.030 -19.577 1.00 52.64 C ANISOU 2904 CH2 TRP D 115 6958 6443 6599 74 -717 285 C ATOM 2905 N LYS D 116 -41.542 16.436 -17.103 1.00 46.38 N ANISOU 2905 N LYS D 116 5482 6987 5151 452 219 634 N ATOM 2906 CA LYS D 116 -42.792 15.877 -17.567 1.00 48.19 C ANISOU 2906 CA LYS D 116 5460 7412 5438 445 333 798 C ATOM 2907 C LYS D 116 -43.293 16.715 -18.732 1.00 46.33 C ANISOU 2907 C LYS D 116 5135 7141 5329 505 313 804 C ATOM 2908 O LYS D 116 -43.305 17.956 -18.668 1.00 46.71 O ANISOU 2908 O LYS D 116 5307 7089 5351 689 325 707 O ATOM 2909 CB LYS D 116 -43.823 15.807 -16.458 1.00 51.59 C ANISOU 2909 CB LYS D 116 5832 8057 5713 621 530 885 C ATOM 2910 CG LYS D 116 -44.994 14.892 -16.900 1.00 59.17 C ANISOU 2910 CG LYS D 116 6471 9234 6777 519 609 1121 C ATOM 2911 CD LYS D 116 -46.091 14.783 -15.844 1.00 71.71 C ANISOU 2911 CD LYS D 116 7930 11084 8231 693 841 1276 C ATOM 2912 CE LYS D 116 -47.069 13.568 -16.122 1.00 76.97 C ANISOU 2912 CE LYS D 116 8258 11958 9028 492 875 1563 C ATOM 2913 NZ LYS D 116 -46.254 12.315 -16.285 1.00 76.95 N ANISOU 2913 NZ LYS D 116 8320 11825 9093 190 712 1572 N ATOM 2914 N ALA D 117 -43.640 16.050 -19.823 1.00 44.36 N ANISOU 2914 N ALA D 117 4703 6944 5207 345 257 913 N ATOM 2915 CA ALA D 117 -43.930 16.772 -21.033 1.00 45.52 C ANISOU 2915 CA ALA D 117 4789 7049 5459 374 200 926 C ATOM 2916 C ALA D 117 -45.174 16.183 -21.721 1.00 46.75 C ANISOU 2916 C ALA D 117 4676 7397 5690 305 206 1104 C ATOM 2917 O ALA D 117 -45.555 15.070 -21.435 1.00 46.33 O ANISOU 2917 O ALA D 117 4506 7457 5641 166 215 1207 O ATOM 2918 CB ALA D 117 -42.682 16.684 -21.992 1.00 41.81 C ANISOU 2918 CB ALA D 117 4435 6393 5060 216 53 850 C ATOM 2919 N ARG D 118 -45.725 16.923 -22.669 1.00 47.58 N ANISOU 2919 N ARG D 118 4695 7519 5866 378 168 1151 N ATOM 2920 CA ARG D 118 -46.816 16.460 -23.523 1.00 48.90 C ANISOU 2920 CA ARG D 118 4610 7852 6116 284 106 1323 C ATOM 2921 C ARG D 118 -46.504 16.748 -25.008 1.00 48.55 C ANISOU 2921 C ARG D 118 4614 7710 6121 202 -55 1303 C ATOM 2922 O ARG D 118 -46.111 17.861 -25.385 1.00 46.83 O ANISOU 2922 O ARG D 118 4509 7375 5909 340 -56 1242 O ATOM 2923 CB ARG D 118 -48.123 17.133 -23.162 1.00 51.66 C ANISOU 2923 CB ARG D 118 4740 8399 6491 508 236 1468 C ATOM 2924 CG ARG D 118 -49.279 16.698 -24.037 1.00 53.92 C ANISOU 2924 CG ARG D 118 4723 8878 6887 394 136 1682 C ATOM 2925 CD ARG D 118 -50.645 17.131 -23.482 1.00 62.59 C ANISOU 2925 CD ARG D 118 5518 10234 8028 614 299 1889 C ATOM 2926 NE ARG D 118 -50.738 18.572 -23.282 1.00 66.62 N ANISOU 2926 NE ARG D 118 6115 10689 8510 971 430 1826 N ATOM 2927 CZ ARG D 118 -50.966 19.173 -22.107 1.00 68.84 C ANISOU 2927 CZ ARG D 118 6444 11015 8699 1273 666 1795 C ATOM 2928 NH1 ARG D 118 -51.142 18.476 -20.969 1.00 69.22 N ANISOU 2928 NH1 ARG D 118 6438 11205 8658 1272 824 1845 N ATOM 2929 NH2 ARG D 118 -51.045 20.501 -22.078 1.00 71.27 N ANISOU 2929 NH2 ARG D 118 6873 11216 8989 1597 747 1720 N ATOM 2930 N SER D 119 -46.653 15.728 -25.838 1.00 49.07 N ANISOU 2930 N SER D 119 4624 7812 6209 -24 -198 1356 N ATOM 2931 CA SER D 119 -46.470 15.893 -27.264 1.00 51.06 C ANISOU 2931 CA SER D 119 4934 8009 6458 -93 -348 1348 C ATOM 2932 C SER D 119 -47.548 16.792 -27.876 1.00 53.37 C ANISOU 2932 C SER D 119 5045 8431 6801 35 -384 1489 C ATOM 2933 O SER D 119 -48.690 16.547 -27.625 1.00 55.86 O ANISOU 2933 O SER D 119 5114 8932 7177 30 -385 1643 O ATOM 2934 CB SER D 119 -46.460 14.503 -27.919 1.00 51.81 C ANISOU 2934 CB SER D 119 5056 8098 6531 -352 -507 1351 C ATOM 2935 OG SER D 119 -46.782 14.623 -29.279 1.00 56.34 O ANISOU 2935 OG SER D 119 5633 8696 7076 -408 -671 1389 O ATOM 2936 N LEU D 120 -47.199 17.847 -28.634 1.00 54.38 N ANISOU 2936 N LEU D 120 5272 8469 6920 156 -408 1469 N ATOM 2937 CA LEU D 120 -48.221 18.739 -29.260 1.00 59.75 C ANISOU 2937 CA LEU D 120 5782 9264 7655 299 -453 1625 C ATOM 2938 C LEU D 120 -48.909 18.044 -30.437 1.00 61.85 C ANISOU 2938 C LEU D 120 5930 9665 7906 110 -673 1743 C ATOM 2939 O LEU D 120 -50.050 18.365 -30.789 1.00 66.60 O ANISOU 2939 O LEU D 120 6293 10438 8572 168 -747 1924 O ATOM 2940 CB LEU D 120 -47.627 20.063 -29.769 1.00 60.48 C ANISOU 2940 CB LEU D 120 6036 9196 7749 468 -433 1594 C ATOM 2941 CG LEU D 120 -47.222 21.141 -28.757 1.00 62.93 C ANISOU 2941 CG LEU D 120 6466 9347 8096 696 -273 1507 C ATOM 2942 CD1 LEU D 120 -46.819 22.492 -29.520 1.00 61.71 C ANISOU 2942 CD1 LEU D 120 6449 9017 7980 830 -309 1536 C ATOM 2943 CD2 LEU D 120 -48.359 21.366 -27.712 1.00 67.23 C ANISOU 2943 CD2 LEU D 120 6821 10040 8684 906 -133 1578 C ATOM 2944 N ALA D 121 -48.257 17.041 -31.011 1.00 61.35 N ANISOU 2944 N ALA D 121 6031 9527 7750 -112 -790 1644 N ATOM 2945 CA ALA D 121 -48.837 16.281 -32.112 1.00 62.40 C ANISOU 2945 CA ALA D 121 6130 9750 7831 -311 -1035 1712 C ATOM 2946 C ALA D 121 -49.901 15.315 -31.591 1.00 63.32 C ANISOU 2946 C ALA D 121 5999 10015 8042 -484 -1122 1833 C ATOM 2947 O ALA D 121 -50.947 15.293 -32.138 1.00 65.43 O ANISOU 2947 O ALA D 121 6059 10442 8358 -552 -1294 2001 O ATOM 2948 CB ALA D 121 -47.730 15.505 -32.898 1.00 61.90 C ANISOU 2948 CB ALA D 121 6383 9529 7609 -453 -1115 1542 C ATOM 2949 N THR D 122 -49.623 14.545 -30.525 1.00 60.99 N ANISOU 2949 N THR D 122 5713 9675 7784 -559 -1010 1776 N ATOM 2950 CA THR D 122 -50.470 13.407 -30.084 1.00 62.91 C ANISOU 2950 CA THR D 122 5759 10024 8119 -786 -1109 1904 C ATOM 2951 C THR D 122 -51.175 13.555 -28.695 1.00 63.27 C ANISOU 2951 C THR D 122 5517 10238 8286 -677 -896 2062 C ATOM 2952 O THR D 122 -52.200 12.865 -28.403 1.00 66.65 O ANISOU 2952 O THR D 122 5662 10833 8829 -842 -970 2273 O ATOM 2953 CB THR D 122 -49.687 12.085 -30.041 1.00 61.30 C ANISOU 2953 CB THR D 122 5804 9631 7855 -1010 -1187 1753 C ATOM 2954 OG1 THR D 122 -48.730 12.137 -28.985 1.00 58.66 O ANISOU 2954 OG1 THR D 122 5599 9189 7501 -888 -950 1633 O ATOM 2955 CG2 THR D 122 -48.918 11.837 -31.350 1.00 61.68 C ANISOU 2955 CG2 THR D 122 6175 9516 7745 -1076 -1353 1582 C ATOM 2956 N ARG D 123 -50.673 14.498 -27.890 1.00 60.41 N ANISOU 2956 N ARG D 123 5223 9839 7891 -397 -641 1979 N ATOM 2957 CA AARG D 123 -51.175 14.805 -26.557 0.60 60.71 C ANISOU 2957 CA AARG D 123 5076 10018 7972 -214 -396 2081 C ATOM 2958 CA BARG D 123 -51.208 14.770 -26.548 0.40 60.17 C ANISOU 2958 CA BARG D 123 4998 9956 7907 -221 -399 2088 C ATOM 2959 C ARG D 123 -50.750 13.700 -25.585 1.00 58.25 C ANISOU 2959 C ARG D 123 4836 9660 7637 -369 -328 2046 C ATOM 2960 O ARG D 123 -51.108 13.740 -24.449 1.00 57.88 O ANISOU 2960 O ARG D 123 4664 9739 7591 -249 -128 2135 O ATOM 2961 CB AARG D 123 -52.705 15.088 -26.564 0.60 64.18 C ANISOU 2961 CB AARG D 123 5094 10751 8540 -142 -389 2377 C ATOM 2962 CB BARG D 123 -52.758 14.881 -26.492 0.40 63.10 C ANISOU 2962 CB BARG D 123 4935 10627 8411 -184 -397 2395 C ATOM 2963 CG AARG D 123 -53.035 16.272 -27.533 0.60 67.06 C ANISOU 2963 CG AARG D 123 5416 11140 8925 50 -460 2413 C ATOM 2964 CG BARG D 123 -53.248 16.304 -26.631 0.40 64.37 C ANISOU 2964 CG BARG D 123 4987 10875 8595 161 -283 2457 C ATOM 2965 CD AARG D 123 -54.373 16.976 -27.286 0.60 75.10 C ANISOU 2965 CD AARG D 123 6038 12434 10063 285 -353 2686 C ATOM 2966 CD BARG D 123 -53.040 16.755 -28.036 0.40 64.71 C ANISOU 2966 CD BARG D 123 5144 10821 8623 115 -508 2407 C ATOM 2967 NE AARG D 123 -54.219 18.198 -26.475 0.60 80.37 N ANISOU 2967 NE AARG D 123 6793 13061 10685 702 -64 2609 N ATOM 2968 NE BARG D 123 -53.525 15.772 -29.015 0.40 68.28 N ANISOU 2968 NE BARG D 123 5485 11342 9117 -224 -818 2516 N ATOM 2969 CZ AARG D 123 -54.400 18.302 -25.154 0.60 81.05 C ANISOU 2969 CZ AARG D 123 6829 13234 10734 911 220 2624 C ATOM 2970 CZ BARG D 123 -54.749 15.764 -29.525 0.40 71.73 C ANISOU 2970 CZ BARG D 123 5573 12010 9673 -284 -975 2781 C ATOM 2971 NH1AARG D 123 -54.756 17.248 -24.416 0.60 84.33 N ANISOU 2971 NH1AARG D 123 7065 13809 11167 740 283 2752 N ATOM 2972 NH1BARG D 123 -55.621 16.680 -29.152 0.40 76.85 N ANISOU 2972 NH1BARG D 123 5921 12859 10420 6 -816 2980 N ATOM 2973 NH2AARG D 123 -54.236 19.485 -24.562 0.60 80.40 N ANISOU 2973 NH2AARG D 123 6897 13067 10584 1300 438 2517 N ATOM 2974 NH2BARG D 123 -55.103 14.843 -30.413 0.40 71.91 N ANISOU 2974 NH2BARG D 123 5553 12055 9714 -625 -1305 2849 N ATOM 2975 N LYS D 124 -49.926 12.750 -26.045 1.00 56.67 N ANISOU 2975 N LYS D 124 4866 9270 7397 -603 -483 1911 N ATOM 2976 CA LYS D 124 -49.318 11.762 -25.128 1.00 55.83 C ANISOU 2976 CA LYS D 124 4879 9070 7264 -718 -418 1860 C ATOM 2977 C LYS D 124 -48.358 12.461 -24.116 1.00 52.50 C ANISOU 2977 C LYS D 124 4642 8566 6738 -479 -196 1705 C ATOM 2978 O LYS D 124 -47.688 13.435 -24.488 1.00 48.82 O ANISOU 2978 O LYS D 124 4336 7992 6221 -319 -175 1558 O ATOM 2979 CB LYS D 124 -48.596 10.701 -25.920 1.00 56.66 C ANISOU 2979 CB LYS D 124 5220 8963 7346 -960 -623 1735 C ATOM 2980 CG LYS D 124 -49.489 9.723 -26.577 1.00 63.28 C ANISOU 2980 CG LYS D 124 5933 9837 8274 -1248 -866 1876 C ATOM 2981 CD LYS D 124 -48.895 9.071 -27.829 1.00 67.12 C ANISOU 2981 CD LYS D 124 6707 10106 8688 -1411 -1107 1707 C ATOM 2982 CE LYS D 124 -48.134 7.769 -27.505 1.00 68.30 C ANISOU 2982 CE LYS D 124 7097 10029 8826 -1568 -1150 1608 C ATOM 2983 NZ LYS D 124 -48.627 6.733 -28.508 1.00 74.81 N ANISOU 2983 NZ LYS D 124 8018 10738 9670 -1858 -1474 1614 N ATOM 2984 N GLU D 125 -48.321 11.983 -22.875 1.00 51.36 N ANISOU 2984 N GLU D 125 4479 8472 6563 -469 -56 1756 N ATOM 2985 CA GLU D 125 -47.602 12.651 -21.792 1.00 51.45 C ANISOU 2985 CA GLU D 125 4653 8439 6455 -245 128 1631 C ATOM 2986 C GLU D 125 -46.637 11.612 -21.165 1.00 49.42 C ANISOU 2986 C GLU D 125 4578 8048 6149 -387 108 1565 C ATOM 2987 O GLU D 125 -46.904 10.403 -21.192 1.00 49.93 O ANISOU 2987 O GLU D 125 4576 8117 6279 -612 26 1681 O ATOM 2988 CB GLU D 125 -48.522 13.142 -20.662 1.00 54.57 C ANISOU 2988 CB GLU D 125 4869 9066 6800 -28 356 1773 C ATOM 2989 CG GLU D 125 -49.366 14.313 -21.065 1.00 58.68 C ANISOU 2989 CG GLU D 125 5234 9704 7355 201 421 1829 C ATOM 2990 CD GLU D 125 -50.290 14.793 -19.977 1.00 65.58 C ANISOU 2990 CD GLU D 125 5934 10817 8165 472 682 1972 C ATOM 2991 OE1 GLU D 125 -50.272 14.207 -18.900 1.00 73.84 O ANISOU 2991 OE1 GLU D 125 6986 11951 9119 467 815 2033 O ATOM 2992 OE2 GLU D 125 -51.048 15.759 -20.215 1.00 71.28 O ANISOU 2992 OE2 GLU D 125 6516 11646 8920 711 766 2038 O ATOM 2993 N GLY D 126 -45.564 12.120 -20.581 1.00 46.58 N ANISOU 2993 N GLY D 126 4442 7567 5689 -256 166 1397 N ATOM 2994 CA GLY D 126 -44.597 11.303 -19.833 1.00 44.65 C ANISOU 2994 CA GLY D 126 4361 7216 5389 -338 157 1347 C ATOM 2995 C GLY D 126 -43.305 12.097 -19.595 1.00 43.87 C ANISOU 2995 C GLY D 126 4495 6960 5216 -215 147 1150 C ATOM 2996 O GLY D 126 -43.165 13.279 -20.005 1.00 42.60 O ANISOU 2996 O GLY D 126 4384 6751 5054 -81 146 1052 O ATOM 2997 N TYR D 127 -42.382 11.452 -18.906 1.00 42.23 N ANISOU 2997 N TYR D 127 4418 6669 4961 -270 123 1117 N ATOM 2998 CA TYR D 127 -41.077 12.026 -18.671 1.00 41.04 C ANISOU 2998 CA TYR D 127 4453 6371 4768 -207 70 968 C ATOM 2999 C TYR D 127 -40.161 11.932 -19.852 1.00 39.05 C ANISOU 2999 C TYR D 127 4250 5962 4623 -290 -42 900 C ATOM 3000 O TYR D 127 -40.185 10.975 -20.643 1.00 38.42 O ANISOU 3000 O TYR D 127 4140 5844 4616 -416 -94 941 O ATOM 3001 CB TYR D 127 -40.412 11.376 -17.414 1.00 41.87 C ANISOU 3001 CB TYR D 127 4663 6472 4775 -222 73 987 C ATOM 3002 CG TYR D 127 -41.067 11.857 -16.152 1.00 43.14 C ANISOU 3002 CG TYR D 127 4848 6784 4761 -69 200 1013 C ATOM 3003 CD1 TYR D 127 -42.127 11.114 -15.559 1.00 55.00 C ANISOU 3003 CD1 TYR D 127 6211 8472 6213 -86 327 1196 C ATOM 3004 CD2 TYR D 127 -40.742 13.076 -15.598 1.00 51.18 C ANISOU 3004 CD2 TYR D 127 6024 7763 5660 101 203 871 C ATOM 3005 CE1 TYR D 127 -42.825 11.614 -14.424 1.00 58.74 C ANISOU 3005 CE1 TYR D 127 6697 9127 6493 105 496 1238 C ATOM 3006 CE2 TYR D 127 -41.396 13.570 -14.454 1.00 52.14 C ANISOU 3006 CE2 TYR D 127 6215 8021 5575 293 340 869 C ATOM 3007 CZ TYR D 127 -42.438 12.841 -13.892 1.00 57.52 C ANISOU 3007 CZ TYR D 127 6746 8922 6185 313 507 1056 C ATOM 3008 OH TYR D 127 -43.044 13.315 -12.787 1.00 60.38 O ANISOU 3008 OH TYR D 127 7180 9443 6319 536 677 1067 O ATOM 3009 N ILE D 128 -39.344 12.955 -19.960 1.00 39.46 N ANISOU 3009 N ILE D 128 4395 5919 4678 -214 -79 799 N ATOM 3010 CA ILE D 128 -38.375 13.115 -21.033 1.00 38.70 C ANISOU 3010 CA ILE D 128 4331 5699 4674 -259 -152 759 C ATOM 3011 C ILE D 128 -37.007 13.581 -20.501 1.00 37.71 C ANISOU 3011 C ILE D 128 4301 5467 4561 -248 -219 708 C ATOM 3012 O ILE D 128 -36.931 14.318 -19.517 1.00 38.26 O ANISOU 3012 O ILE D 128 4452 5524 4560 -183 -240 655 O ATOM 3013 CB ILE D 128 -38.850 14.178 -22.101 1.00 40.00 C ANISOU 3013 CB ILE D 128 4457 5859 4882 -202 -150 745 C ATOM 3014 CG1 ILE D 128 -38.964 15.573 -21.538 1.00 40.46 C ANISOU 3014 CG1 ILE D 128 4578 5883 4914 -72 -141 688 C ATOM 3015 CG2 ILE D 128 -40.195 13.731 -22.759 1.00 41.47 C ANISOU 3015 CG2 ILE D 128 4520 6166 5072 -233 -128 819 C ATOM 3016 CD1 ILE D 128 -39.076 16.656 -22.615 1.00 41.08 C ANISOU 3016 CD1 ILE D 128 4646 5901 5061 -22 -163 691 C ATOM 3017 N PRO D 129 -35.927 13.212 -21.205 1.00 36.75 N ANISOU 3017 N PRO D 129 4171 5268 4526 -303 -260 730 N ATOM 3018 CA PRO D 129 -34.586 13.627 -20.765 1.00 36.20 C ANISOU 3018 CA PRO D 129 4133 5115 4507 -317 -344 729 C ATOM 3019 C PRO D 129 -34.407 15.042 -21.179 1.00 35.62 C ANISOU 3019 C PRO D 129 4076 4971 4487 -296 -386 702 C ATOM 3020 O PRO D 129 -34.373 15.305 -22.395 1.00 36.82 O ANISOU 3020 O PRO D 129 4173 5111 4705 -296 -349 741 O ATOM 3021 CB PRO D 129 -33.685 12.626 -21.519 1.00 36.58 C ANISOU 3021 CB PRO D 129 4125 5138 4635 -348 -325 798 C ATOM 3022 CG PRO D 129 -34.483 12.277 -22.804 1.00 36.74 C ANISOU 3022 CG PRO D 129 4131 5184 4643 -339 -249 792 C ATOM 3023 CD PRO D 129 -35.855 12.132 -22.229 1.00 35.25 C ANISOU 3023 CD PRO D 129 3950 5069 4375 -350 -233 768 C ATOM 3024 N SER D 130 -34.317 15.979 -20.230 1.00 38.51 N ANISOU 3024 N SER D 130 4543 5275 4813 -274 -470 636 N ATOM 3025 CA SER D 130 -34.303 17.404 -20.537 1.00 40.11 C ANISOU 3025 CA SER D 130 4806 5363 5072 -250 -529 601 C ATOM 3026 C SER D 130 -33.084 17.782 -21.443 1.00 41.34 C ANISOU 3026 C SER D 130 4874 5433 5399 -349 -594 705 C ATOM 3027 O SER D 130 -33.113 18.827 -22.142 1.00 42.40 O ANISOU 3027 O SER D 130 5017 5479 5614 -349 -614 733 O ATOM 3028 CB SER D 130 -34.192 18.259 -19.267 1.00 41.28 C ANISOU 3028 CB SER D 130 5138 5409 5137 -218 -650 490 C ATOM 3029 OG SER D 130 -33.053 17.976 -18.482 1.00 41.67 O ANISOU 3029 OG SER D 130 5217 5420 5197 -320 -797 504 O ATOM 3030 N ASN D 131 -31.993 17.029 -21.362 1.00 40.53 N ANISOU 3030 N ASN D 131 4682 5357 5361 -424 -628 788 N ATOM 3031 CA ASN D 131 -30.818 17.446 -22.116 1.00 41.24 C ANISOU 3031 CA ASN D 131 4653 5397 5620 -504 -670 926 C ATOM 3032 C ASN D 131 -30.945 17.029 -23.641 1.00 42.12 C ANISOU 3032 C ASN D 131 4660 5592 5752 -451 -498 1015 C ATOM 3033 O ASN D 131 -30.024 17.197 -24.409 1.00 41.84 O ANISOU 3033 O ASN D 131 4505 5563 5828 -481 -469 1158 O ATOM 3034 CB ASN D 131 -29.518 16.953 -21.486 1.00 41.59 C ANISOU 3034 CB ASN D 131 4605 5449 5748 -585 -776 1017 C ATOM 3035 CG ASN D 131 -29.372 15.423 -21.478 1.00 42.29 C ANISOU 3035 CG ASN D 131 4626 5654 5790 -522 -666 1050 C ATOM 3036 OD1 ASN D 131 -30.368 14.675 -21.581 1.00 39.48 O ANISOU 3036 OD1 ASN D 131 4338 5352 5311 -447 -553 968 O ATOM 3037 ND2 ASN D 131 -28.119 14.948 -21.223 1.00 44.00 N ANISOU 3037 ND2 ASN D 131 4708 5895 6115 -558 -726 1183 N ATOM 3038 N TYR D 132 -32.075 16.454 -24.049 1.00 40.92 N ANISOU 3038 N TYR D 132 4556 5513 5480 -373 -392 940 N ATOM 3039 CA TYR D 132 -32.329 16.127 -25.468 1.00 40.03 C ANISOU 3039 CA TYR D 132 4405 5467 5338 -323 -270 992 C ATOM 3040 C TYR D 132 -33.164 17.232 -26.172 1.00 40.09 C ANISOU 3040 C TYR D 132 4446 5453 5335 -296 -269 995 C ATOM 3041 O TYR D 132 -33.353 17.116 -27.378 1.00 40.17 O ANISOU 3041 O TYR D 132 4441 5522 5301 -259 -193 1049 O ATOM 3042 CB TYR D 132 -33.158 14.839 -25.601 1.00 36.55 C ANISOU 3042 CB TYR D 132 4010 5100 4777 -285 -206 918 C ATOM 3043 CG TYR D 132 -32.417 13.570 -25.527 1.00 36.41 C ANISOU 3043 CG TYR D 132 3981 5094 4760 -270 -164 939 C ATOM 3044 CD1 TYR D 132 -31.394 13.385 -24.599 1.00 38.13 C ANISOU 3044 CD1 TYR D 132 4146 5284 5057 -294 -215 986 C ATOM 3045 CD2 TYR D 132 -32.711 12.547 -26.392 1.00 34.59 C ANISOU 3045 CD2 TYR D 132 3809 4887 4448 -224 -92 913 C ATOM 3046 CE1 TYR D 132 -30.658 12.135 -24.528 1.00 37.74 C ANISOU 3046 CE1 TYR D 132 4078 5240 5022 -245 -169 1027 C ATOM 3047 CE2 TYR D 132 -32.010 11.308 -26.332 1.00 37.55 C ANISOU 3047 CE2 TYR D 132 4209 5234 4824 -174 -47 924 C ATOM 3048 CZ TYR D 132 -30.973 11.107 -25.425 1.00 38.21 C ANISOU 3048 CZ TYR D 132 4216 5300 5004 -171 -71 991 C ATOM 3049 OH TYR D 132 -30.279 9.851 -25.372 1.00 38.84 O ANISOU 3049 OH TYR D 132 4316 5344 5096 -88 -20 1019 O ATOM 3050 N VAL D 133 -33.572 18.296 -25.496 1.00 41.00 N ANISOU 3050 N VAL D 133 4623 5475 5479 -297 -355 945 N ATOM 3051 CA VAL D 133 -34.522 19.224 -26.093 1.00 41.46 C ANISOU 3051 CA VAL D 133 4718 5512 5524 -233 -346 948 C ATOM 3052 C VAL D 133 -33.976 20.649 -25.917 1.00 44.36 C ANISOU 3052 C VAL D 133 5136 5699 6018 -270 -449 994 C ATOM 3053 O VAL D 133 -33.074 20.888 -25.090 1.00 43.70 O ANISOU 3053 O VAL D 133 5080 5513 6012 -356 -556 985 O ATOM 3054 CB VAL D 133 -35.962 19.100 -25.516 1.00 41.10 C ANISOU 3054 CB VAL D 133 4715 5527 5376 -142 -326 841 C ATOM 3055 CG1 VAL D 133 -36.439 17.613 -25.605 1.00 39.52 C ANISOU 3055 CG1 VAL D 133 4460 5474 5081 -161 -263 820 C ATOM 3056 CG2 VAL D 133 -36.057 19.634 -24.051 1.00 40.96 C ANISOU 3056 CG2 VAL D 133 4805 5417 5339 -103 -388 732 C ATOM 3057 N ALA D 134 -34.540 21.568 -26.674 1.00 42.46 N ANISOU 3057 N ALA D 134 4920 5409 5803 -215 -443 1049 N ATOM 3058 CA ALA D 134 -34.199 22.954 -26.578 1.00 45.98 C ANISOU 3058 CA ALA D 134 5447 5644 6378 -245 -551 1096 C ATOM 3059 C ALA D 134 -35.477 23.756 -26.544 1.00 46.72 C ANISOU 3059 C ALA D 134 5643 5676 6431 -90 -549 1030 C ATOM 3060 O ALA D 134 -36.460 23.473 -27.246 1.00 45.78 O ANISOU 3060 O ALA D 134 5463 5701 6232 9 -460 1056 O ATOM 3061 CB ALA D 134 -33.249 23.386 -27.734 1.00 44.48 C ANISOU 3061 CB ALA D 134 5157 5433 6311 -343 -539 1320 C ATOM 3062 N ARG D 135 -35.463 24.758 -25.704 1.00 48.92 N ANISOU 3062 N ARG D 135 6087 5735 6765 -61 -661 944 N ATOM 3063 CA ARG D 135 -36.575 25.654 -25.645 1.00 52.32 C ANISOU 3063 CA ARG D 135 6632 6071 7176 127 -650 891 C ATOM 3064 C ARG D 135 -36.711 26.508 -26.938 1.00 53.49 C ANISOU 3064 C ARG D 135 6746 6149 7429 143 -652 1075 C ATOM 3065 O ARG D 135 -35.730 26.987 -27.500 1.00 50.17 O ANISOU 3065 O ARG D 135 6310 5611 7143 -8 -722 1223 O ATOM 3066 CB ARG D 135 -36.449 26.557 -24.436 1.00 56.64 C ANISOU 3066 CB ARG D 135 7430 6356 7737 177 -779 733 C ATOM 3067 CG ARG D 135 -37.713 27.398 -24.221 1.00 64.22 C ANISOU 3067 CG ARG D 135 8527 7228 8645 450 -727 651 C ATOM 3068 CD ARG D 135 -37.693 28.189 -22.928 1.00 74.45 C ANISOU 3068 CD ARG D 135 10133 8266 9889 558 -832 444 C ATOM 3069 NE ARG D 135 -39.016 28.744 -22.635 1.00 79.70 N ANISOU 3069 NE ARG D 135 10902 8919 10463 889 -713 359 N ATOM 3070 CZ ARG D 135 -39.286 29.479 -21.555 1.00 86.70 C ANISOU 3070 CZ ARG D 135 12097 9594 11253 1086 -751 159 C ATOM 3071 NH1 ARG D 135 -38.327 29.741 -20.680 1.00 88.55 N ANISOU 3071 NH1 ARG D 135 12581 9602 11463 949 -944 14 N ATOM 3072 NH2 ARG D 135 -40.511 29.961 -21.349 1.00 89.32 N ANISOU 3072 NH2 ARG D 135 12494 9940 11502 1434 -602 108 N ATOM 3073 N VAL D 136 -37.948 26.707 -27.378 1.00 55.07 N ANISOU 3073 N VAL D 136 6918 6433 7572 328 -576 1093 N ATOM 3074 CA VAL D 136 -38.239 27.442 -28.617 1.00 61.01 C ANISOU 3074 CA VAL D 136 7634 7153 8392 371 -577 1282 C ATOM 3075 C VAL D 136 -38.629 28.847 -28.246 1.00 67.38 C ANISOU 3075 C VAL D 136 8634 7666 9301 521 -655 1257 C ATOM 3076 O VAL D 136 -39.390 29.024 -27.281 1.00 68.79 O ANISOU 3076 O VAL D 136 8918 7801 9418 710 -630 1089 O ATOM 3077 CB VAL D 136 -39.451 26.822 -29.386 1.00 59.78 C ANISOU 3077 CB VAL D 136 7322 7277 8116 492 -483 1340 C ATOM 3078 CG1 VAL D 136 -39.753 27.564 -30.698 1.00 64.66 C ANISOU 3078 CG1 VAL D 136 7910 7882 8776 540 -503 1552 C ATOM 3079 CG2 VAL D 136 -39.209 25.377 -29.643 1.00 57.60 C ANISOU 3079 CG2 VAL D 136 6913 7250 7723 366 -423 1321 C ATOM 3080 N ASP D 137 -38.086 29.793 -29.031 1.00 72.27 N ANISOU 3080 N ASP D 137 9304 8090 10067 443 -736 1437 N ATOM 3081 CA ASP D 137 -38.483 31.248 -29.206 1.00 78.27 C ANISOU 3081 CA ASP D 137 10239 8542 10958 582 -819 1507 C ATOM 3082 C ASP D 137 -37.232 32.092 -29.001 1.00 81.00 C ANISOU 3082 C ASP D 137 10740 8543 11495 367 -990 1565 C ATOM 3083 O ASP D 137 -36.132 31.504 -28.917 1.00 80.67 O ANISOU 3083 O ASP D 137 10601 8571 11479 123 -1019 1599 O ATOM 3084 CB ASP D 137 -39.695 31.708 -28.366 1.00 79.75 C ANISOU 3084 CB ASP D 137 10567 8645 11089 898 -784 1328 C ATOM 3085 CG ASP D 137 -40.996 31.317 -29.022 1.00 81.35 C ANISOU 3085 CG ASP D 137 10571 9145 11196 1102 -654 1416 C ATOM 3086 OD1 ASP D 137 -41.187 31.803 -30.155 1.00 84.83 O ANISOU 3086 OD1 ASP D 137 10948 9584 11700 1118 -676 1636 O ATOM 3087 OD2 ASP D 137 -41.791 30.509 -28.483 1.00 82.90 O ANISOU 3087 OD2 ASP D 137 10653 9587 11259 1220 -545 1303 O TER 3088 ASP D 137 HETATM 3089 O HOH A 301 -29.362 11.414 -3.022 1.00 47.55 O ANISOU 3089 O HOH A 301 6087 6403 5576 -338 -125 425 O HETATM 3090 O HOH A 302 -30.591 11.506 -9.101 1.00 51.92 O ANISOU 3090 O HOH A 302 6449 6965 6312 -350 -96 499 O HETATM 3091 O HOH A 303 -14.411 1.982 -1.427 1.00 39.32 O ANISOU 3091 O HOH A 303 4892 5141 4908 -601 -637 718 O HETATM 3092 O HOH A 304 -16.169 4.680 -11.439 1.00 36.25 O ANISOU 3092 O HOH A 304 4363 4737 4673 -506 -367 553 O HETATM 3093 O HOH A 305 -10.455 17.117 -3.138 1.00 39.96 O ANISOU 3093 O HOH A 305 5056 4887 5240 -804 -897 411 O HETATM 3094 O HOH A 306 -22.146 4.119 4.945 1.00 54.13 O ANISOU 3094 O HOH A 306 7035 7331 6203 -542 -472 661 O HETATM 3095 O HOH A 307 -18.127 8.950 -21.880 1.00 51.84 O ANISOU 3095 O HOH A 307 6167 7008 6521 -362 -128 597 O HETATM 3096 O HOH A 308 -18.543 2.169 9.570 1.00 51.83 O ANISOU 3096 O HOH A 308 6796 7177 5721 -587 -704 831 O HETATM 3097 O HOH A 309 -4.062 12.458 5.721 1.00 47.09 O ANISOU 3097 O HOH A 309 5934 6104 5856 -1006 -1504 523 O HETATM 3098 O HOH A 310 -25.882 12.734 -18.246 1.00 42.16 O ANISOU 3098 O HOH A 310 5046 5743 5230 -368 -144 592 O HETATM 3099 O HOH A 311 -5.654 0.585 -13.758 1.00 53.87 O ANISOU 3099 O HOH A 311 6230 6939 7299 -327 -362 776 O HETATM 3100 O HOH A 312 -18.349 1.260 -21.227 1.00 51.87 O ANISOU 3100 O HOH A 312 6263 6907 6538 -358 -169 352 O HETATM 3101 O HOH A 313 -20.847 12.942 -13.699 1.00 37.60 O ANISOU 3101 O HOH A 313 4576 4941 4770 -454 -260 543 O HETATM 3102 O HOH A 314 -18.209 2.991 -7.465 1.00 45.73 O ANISOU 3102 O HOH A 314 5660 5935 5782 -549 -413 573 O HETATM 3103 O HOH A 315 -28.451 10.468 0.108 1.00 46.04 O ANISOU 3103 O HOH A 315 5983 6258 5251 -354 -165 418 O HETATM 3104 O HOH A 316 -12.538 20.477 -1.769 1.00 43.63 O ANISOU 3104 O HOH A 316 5719 5208 5650 -780 -909 219 O HETATM 3105 O HOH A 317 -21.578 12.157 -20.209 1.00 55.58 O ANISOU 3105 O HOH A 317 6695 7436 6988 -382 -149 631 O HETATM 3106 O HOH A 318 -16.113 10.348 -23.031 1.00 59.49 O ANISOU 3106 O HOH A 318 7063 8004 7534 -342 -94 694 O HETATM 3107 O HOH A 319 -31.442 7.415 -4.345 1.00 77.51 O ANISOU 3107 O HOH A 319 9731 10300 9420 -420 -88 565 O HETATM 3108 O HOH A 320 -16.868 6.650 14.092 1.00 58.30 O ANISOU 3108 O HOH A 320 7883 8181 6088 -580 -934 549 O HETATM 3109 O HOH A 321 -19.760 8.428 -24.153 1.00 50.90 O ANISOU 3109 O HOH A 321 6037 7009 6293 -328 -95 566 O HETATM 3110 O HOH A 322 -2.607 -2.554 -7.795 1.00 39.61 O ANISOU 3110 O HOH A 322 4365 5045 5642 -355 -618 1000 O HETATM 3111 O HOH A 323 -11.123 0.947 4.961 1.00 43.14 O ANISOU 3111 O HOH A 323 5416 5774 5201 -657 -929 907 O HETATM 3112 O HOH A 324 -8.037 2.330 1.475 1.00 40.42 O ANISOU 3112 O HOH A 324 4914 5312 5131 -665 -945 870 O HETATM 3113 O HOH A 325 -9.388 -3.163 -5.980 1.00 49.93 O ANISOU 3113 O HOH A 325 5984 6311 6678 -462 -585 836 O HETATM 3114 O HOH A 326 -8.193 -2.862 -3.539 1.00 38.22 O ANISOU 3114 O HOH A 326 4492 4864 5166 -497 -694 928 O HETATM 3115 O HOH A 327 -15.896 1.209 -22.430 1.00 55.40 O ANISOU 3115 O HOH A 327 6661 7381 7009 -287 -120 370 O HETATM 3116 O HOH A 328 -20.969 22.152 -12.153 1.00 49.41 O ANISOU 3116 O HOH A 328 6210 6066 6497 -417 -310 533 O HETATM 3117 O HOH A 329 -26.571 16.969 -6.186 1.00 64.11 O ANISOU 3117 O HOH A 329 8223 8233 7901 -308 -199 334 O HETATM 3118 O HOH A 330 -9.646 12.544 9.694 1.00 53.10 O ANISOU 3118 O HOH A 330 7093 7030 6053 -848 -1354 273 O HETATM 3119 O HOH A 331 -8.620 1.413 3.828 1.00 42.31 O ANISOU 3119 O HOH A 331 5214 5619 5242 -672 -998 921 O HETATM 3120 O HOH A 332 -4.694 16.788 -9.586 1.00 46.40 O ANISOU 3120 O HOH A 332 5368 5745 6517 -863 -808 835 O HETATM 3121 O HOH A 333 -12.944 16.681 4.867 1.00 43.82 O ANISOU 3121 O HOH A 333 5947 5545 5159 -758 -1057 102 O HETATM 3122 O HOH A 334 -10.813 10.577 -20.690 1.00 37.06 O ANISOU 3122 O HOH A 334 4118 5036 4925 -397 -159 808 O HETATM 3123 O HOH A 335 -5.065 4.366 -13.340 1.00 51.71 O ANISOU 3123 O HOH A 335 5919 6705 7026 -435 -426 839 O HETATM 3124 O HOH A 336 -14.325 -0.799 -11.061 1.00 43.15 O ANISOU 3124 O HOH A 336 5203 5517 5674 -465 -386 586 O HETATM 3125 O HOH A 337 -21.705 -4.474 -9.758 1.00 66.62 O ANISOU 3125 O HOH A 337 8274 8456 8583 -592 -357 563 O HETATM 3126 O HOH A 338 -7.886 12.451 7.636 1.00 49.90 O ANISOU 3126 O HOH A 338 6536 6534 5890 -899 -1376 364 O HETATM 3127 O HOH A 339 0.882 2.650 -0.715 1.00 44.06 O ANISOU 3127 O HOH A 339 4887 5772 6083 -688 -1154 1157 O HETATM 3128 O HOH A 340 3.730 4.924 -9.367 1.00 53.55 O ANISOU 3128 O HOH A 340 5710 6985 7652 -555 -766 1246 O HETATM 3129 O HOH A 341 -5.719 -4.875 -6.328 1.00 47.60 O ANISOU 3129 O HOH A 341 5542 5974 6571 -369 -612 953 O HETATM 3130 O HOH A 342 -10.702 7.398 11.305 1.00 53.34 O ANISOU 3130 O HOH A 342 7050 7296 5922 -758 -1253 571 O HETATM 3131 O HOH A 343 -21.480 2.589 0.499 1.00 46.35 O ANISOU 3131 O HOH A 343 5911 6182 5516 -575 -445 674 O HETATM 3132 O HOH A 344 -16.767 22.357 -6.038 1.00 48.85 O ANISOU 3132 O HOH A 344 6339 5820 6403 -600 -609 295 O HETATM 3133 O HOH A 345 -16.416 24.931 -5.454 1.00 55.77 O ANISOU 3133 O HOH A 345 7289 6523 7377 -623 -673 226 O HETATM 3134 O HOH A 346 -12.691 16.394 -15.896 1.00 60.98 O ANISOU 3134 O HOH A 346 7325 7770 8075 -565 -356 780 O HETATM 3135 O HOH A 347 -15.200 12.604 -18.633 1.00 58.43 O ANISOU 3135 O HOH A 347 6994 7654 7554 -447 -217 715 O HETATM 3136 O HOH A 348 -20.611 11.987 -16.241 1.00 72.12 O ANISOU 3136 O HOH A 348 8876 9387 9139 -436 -221 576 O HETATM 3137 O HOH A 349 -25.362 17.345 -12.524 1.00 57.75 O ANISOU 3137 O HOH A 349 7211 7442 7288 -338 -181 514 O HETATM 3138 O HOH A 350 -21.159 9.922 -21.381 1.00 62.08 O ANISOU 3138 O HOH A 350 7502 8320 7767 -376 -140 584 O HETATM 3139 O HOH A 351 -20.468 5.215 -24.106 1.00 56.22 O ANISOU 3139 O HOH A 351 6758 7667 6935 -338 -121 430 O HETATM 3140 O HOH A 352 -10.087 -4.048 -1.584 1.00 40.03 O ANISOU 3140 O HOH A 352 4802 5100 5306 -525 -707 968 O HETATM 3141 O HOH A 353 1.762 4.923 -0.725 1.00 53.91 O ANISOU 3141 O HOH A 353 6104 7021 7357 -779 -1236 1132 O HETATM 3142 O HOH A 354 -1.717 13.289 -8.220 1.00 59.33 O ANISOU 3142 O HOH A 354 6860 7502 8180 -853 -893 933 O HETATM 3143 O HOH A 355 -2.191 15.594 -9.756 1.00 58.26 O ANISOU 3143 O HOH A 355 6717 7307 8112 -883 -845 949 O HETATM 3144 O HOH A 356 -6.403 21.084 -2.975 1.00 76.58 O ANISOU 3144 O HOH A 356 9613 9299 10183 -1024 -1159 436 O HETATM 3145 O HOH A 357 -8.016 15.373 4.725 1.00 52.63 O ANISOU 3145 O HOH A 357 6851 6671 6474 -926 -1305 284 O HETATM 3146 O HOH A 358 -26.187 11.685 5.007 1.00 59.65 O ANISOU 3146 O HOH A 358 7927 8025 6712 -338 -289 291 O HETATM 3147 O HOH A 359 -20.774 -3.581 -5.637 1.00 76.40 O ANISOU 3147 O HOH A 359 9547 9742 9739 -602 -405 699 O HETATM 3148 O HOH A 360 -22.751 5.773 3.107 1.00 60.28 O ANISOU 3148 O HOH A 360 7805 8050 7048 -522 -428 568 O HETATM 3149 O HOH A 361 -17.844 3.700 12.138 1.00 75.51 O ANISOU 3149 O HOH A 361 9908 10299 8484 -579 -802 759 O HETATM 3150 O HOH A 362 -10.969 9.627 13.349 1.00 66.89 O ANISOU 3150 O HOH A 362 8927 9067 7422 -772 -1348 390 O HETATM 3151 O HOH A 363 4.010 4.714 6.091 1.00 76.97 O ANISOU 3151 O HOH A 363 9069 10137 10038 -946 -1735 1238 O HETATM 3152 O HOH A 364 -9.485 14.695 -22.366 1.00 57.20 O ANISOU 3152 O HOH A 364 6547 7594 7593 -439 -129 1026 O HETATM 3153 O HOH A 365 -26.260 18.131 -8.830 1.00 63.45 O ANISOU 3153 O HOH A 365 8068 8108 7933 -304 -188 397 O HETATM 3154 O HOH A 366 -24.624 13.860 4.294 1.00 45.05 O ANISOU 3154 O HOH A 366 6129 6040 4949 -355 -371 180 O HETATM 3155 O HOH A 367 -20.575 16.408 -21.409 1.00 63.18 O ANISOU 3155 O HOH A 367 7605 8345 8055 -360 -125 792 O HETATM 3156 O HOH A 368 -16.275 -4.094 -5.995 1.00 82.13 O ANISOU 3156 O HOH A 368 10226 10392 10588 -541 -472 726 O HETATM 3157 O HOH A 369 -6.919 -1.817 -14.287 1.00 50.80 O ANISOU 3157 O HOH A 369 5907 6497 6897 -272 -316 695 O HETATM 3158 O HOH A 370 -27.718 15.530 -3.620 1.00 49.60 O ANISOU 3158 O HOH A 370 6437 6492 5916 -290 -173 307 O HETATM 3159 O HOH A 371 -16.923 -4.341 -11.347 1.00 69.33 O ANISOU 3159 O HOH A 371 8571 8749 9024 -483 -364 539 O HETATM 3160 O HOH A 372 -3.665 -0.279 -11.837 1.00 55.37 O ANISOU 3160 O HOH A 372 6356 7101 7582 -331 -449 874 O HETATM 3161 O HOH A 373 -12.948 -3.841 -10.941 1.00 69.75 O ANISOU 3161 O HOH A 373 8548 8794 9159 -418 -394 614 O HETATM 3162 O HOH A 374 -0.499 7.506 2.416 1.00 51.94 O ANISOU 3162 O HOH A 374 6125 6776 6832 -904 -1387 930 O HETATM 3163 O HOH A 375 -7.884 5.928 9.175 1.00 60.78 O ANISOU 3163 O HOH A 375 7781 8142 7172 -799 -1310 732 O HETATM 3164 O HOH A 376 0.125 8.503 6.610 1.00 64.72 O ANISOU 3164 O HOH A 376 7870 8497 8223 -1019 -1676 868 O HETATM 3165 O HOH A 377 -5.439 18.152 -11.492 1.00 60.60 O ANISOU 3165 O HOH A 377 7145 7521 8361 -841 -719 878 O HETATM 3166 O HOH A 378 -29.379 7.957 0.843 1.00 67.36 O ANISOU 3166 O HOH A 378 8631 9045 7920 -389 -137 526 O HETATM 3167 O HOH A 379 -3.025 3.490 -11.485 1.00 67.72 O ANISOU 3167 O HOH A 379 7880 8714 9137 -450 -522 921 O HETATM 3168 O HOH A 380 -22.327 5.408 -6.202 1.00 55.28 O ANISOU 3168 O HOH A 380 6943 7229 6833 -536 -341 528 O HETATM 3169 O HOH A 381 -14.059 -1.561 -13.974 1.00 45.47 O ANISOU 3169 O HOH A 381 5464 5820 5994 -404 -314 519 O HETATM 3170 O HOH A 382 -15.371 -3.633 -15.549 1.00 57.15 O ANISOU 3170 O HOH A 382 6973 7263 7477 -384 -280 427 O HETATM 3171 O HOH A 383 -28.859 14.693 6.069 1.00 71.02 O ANISOU 3171 O HOH A 383 9472 9492 8021 -171 -149 141 O HETATM 3172 O HOH A 384 -2.173 14.064 -3.660 1.00 66.58 O ANISOU 3172 O HOH A 384 7974 8371 8952 -964 -1143 779 O HETATM 3173 O HOH A 385 -7.057 -5.941 2.523 1.00 66.59 O ANISOU 3173 O HOH A 385 8098 8525 8679 -522 -912 1242 O HETATM 3174 O HOH A 386 -25.581 2.959 6.964 1.00 75.55 O ANISOU 3174 O HOH A 386 9751 10215 8739 -498 -327 773 O HETATM 3175 O HOH A 387 -27.004 14.969 1.734 1.00 50.37 O ANISOU 3175 O HOH A 387 6722 6674 5742 -281 -232 198 O HETATM 3176 O HOH A 388 -24.132 14.615 11.561 1.00 56.64 O ANISOU 3176 O HOH A 388 7918 7763 5840 -277 -482 -19 O HETATM 3177 O HOH A 389 -0.584 7.701 -6.068 1.00 62.31 O ANISOU 3177 O HOH A 389 7195 7997 8485 -732 -923 996 O HETATM 3178 O HOH A 390 -16.623 21.682 -16.353 1.00 68.95 O ANISOU 3178 O HOH A 390 8446 8614 9138 -513 -313 790 O HETATM 3179 O HOH A 391 -6.647 -3.231 -18.595 1.00 73.42 O ANISOU 3179 O HOH A 391 8745 9418 9736 -112 -139 570 O HETATM 3180 O HOH A 392 -22.047 5.070 0.136 1.00 55.11 O ANISOU 3180 O HOH A 392 7060 7299 6581 -547 -422 578 O HETATM 3181 O HOH A 393 -0.250 13.478 -5.592 1.00 64.55 O ANISOU 3181 O HOH A 393 7526 8150 8851 -950 -1090 928 O HETATM 3182 O HOH A 394 -4.254 -1.966 -17.784 1.00 78.19 O ANISOU 3182 O HOH A 394 9226 10061 10422 -117 -164 711 O HETATM 3183 O HOH A 395 -7.127 -6.070 -0.365 1.00 70.12 O ANISOU 3183 O HOH A 395 8510 8881 9251 -476 -802 1141 O HETATM 3184 O HOH A 396 -28.176 12.511 1.807 1.00 71.07 O ANISOU 3184 O HOH A 396 9265 9413 8327 -298 -176 314 O HETATM 3185 O HOH A 397 -30.053 13.836 -3.275 1.00 63.19 O ANISOU 3185 O HOH A 397 8100 8345 7564 -264 -88 370 O HETATM 3186 O HOH A 398 -32.417 11.183 -6.430 1.00 76.11 O ANISOU 3186 O HOH A 398 9542 10097 9280 -314 -37 506 O HETATM 3187 O HOH A 399 -15.692 -2.353 -2.618 1.00 62.96 O ANISOU 3187 O HOH A 399 7840 8057 8023 -574 -555 798 O HETATM 3188 O HOH A 400 -14.098 4.823 13.945 1.00 74.97 O ANISOU 3188 O HOH A 400 9877 10266 8342 -652 -1085 712 O HETATM 3189 O HOH A 401 -13.393 -4.623 2.112 1.00 68.03 O ANISOU 3189 O HOH A 401 8479 8749 8621 -586 -718 1049 O HETATM 3190 O HOH A 402 -13.154 -6.803 3.483 1.00 69.26 O ANISOU 3190 O HOH A 402 8617 8886 8812 -579 -747 1197 O HETATM 3191 O HOH A 403 -30.112 9.702 -8.068 1.00 60.03 O ANISOU 3191 O HOH A 403 7489 8000 7320 -397 -120 506 O HETATM 3192 O HOH A 404 -14.936 -1.142 -22.898 1.00 55.49 O ANISOU 3192 O HOH A 404 6686 7341 7058 -235 -104 295 O HETATM 3193 O HOH A 405 -23.234 12.104 -18.261 1.00 45.68 O ANISOU 3193 O HOH A 405 5494 6142 5719 -394 -167 588 O HETATM 3194 O HOH A 406 -8.954 17.214 -21.947 1.00 61.84 O ANISOU 3194 O HOH A 406 7107 8089 8299 -508 -174 1122 O HETATM 3195 O HOH A 407 -22.689 -0.103 -8.801 1.00 56.14 O ANISOU 3195 O HOH A 407 6965 7273 7091 -576 -328 559 O HETATM 3196 O HOH A 408 -7.907 17.463 -15.035 1.00 63.94 O ANISOU 3196 O HOH A 408 7552 8065 8678 -692 -486 915 O HETATM 3197 O HOH A 409 -20.201 5.930 -21.821 1.00 46.85 O ANISOU 3197 O HOH A 409 5590 6389 5823 -374 -149 470 O HETATM 3198 O HOH A 410 -13.827 8.954 -22.026 1.00 52.34 O ANISOU 3198 O HOH A 410 6136 7048 6704 -346 -111 687 O HETATM 3199 O HOH A 411 -4.671 0.360 -16.784 1.00 56.44 O ANISOU 3199 O HOH A 411 6475 7333 7638 -223 -231 764 O HETATM 3200 O HOH A 412 -11.780 -3.017 -21.853 1.00 53.94 O ANISOU 3200 O HOH A 412 6445 7038 7012 -157 -89 329 O HETATM 3201 O HOH A 413 -8.394 18.295 -1.753 1.00 45.99 O ANISOU 3201 O HOH A 413 5823 5590 6063 -907 -1065 388 O HETATM 3202 O HOH A 414 -30.543 9.548 -5.098 1.00 64.49 O ANISOU 3202 O HOH A 414 8118 8594 7790 -379 -101 502 O HETATM 3203 O HOH A 415 -16.880 18.523 -16.815 1.00 65.10 O ANISOU 3203 O HOH A 415 7932 8285 8518 -487 -275 751 O HETATM 3204 O HOH A 416 -24.386 20.802 0.293 1.00 56.76 O ANISOU 3204 O HOH A 416 7656 7109 6800 -288 -370 -3 O HETATM 3205 O HOH A 417 -28.940 4.343 -7.140 1.00 56.39 O ANISOU 3205 O HOH A 417 7003 7519 6903 -528 -191 570 O HETATM 3206 O HOH A 418 -22.209 9.486 -23.729 1.00 51.74 O ANISOU 3206 O HOH A 418 6160 7130 6371 -345 -113 577 O HETATM 3207 O HOH A 419 -26.843 18.611 -23.546 1.00 66.74 O ANISOU 3207 O HOH A 419 8009 8957 8392 -233 -62 886 O HETATM 3208 O HOH A 420 -16.087 16.438 -23.788 1.00 78.25 O ANISOU 3208 O HOH A 420 9372 10316 10046 -371 -83 943 O HETATM 3209 O HOH A 421 -6.376 -4.602 -3.532 1.00 62.42 O ANISOU 3209 O HOH A 421 7477 7888 8351 -442 -714 1017 O HETATM 3210 O HOH A 422 -3.183 21.304 0.675 1.00 90.25 O ANISOU 3210 O HOH A 422 11358 11032 11899 -1213 -1513 370 O HETATM 3211 O HOH A 423 -9.939 23.581 -3.809 1.00 75.01 O ANISOU 3211 O HOH A 423 9580 8964 9956 -912 -1008 310 O HETATM 3212 O HOH A 424 -26.275 19.621 1.643 1.00 65.74 O ANISOU 3212 O HOH A 424 8810 8391 7778 -217 -279 -1 O HETATM 3213 O HOH A 425 -34.316 7.191 -4.381 1.00 68.31 O ANISOU 3213 O HOH A 425 8485 9237 8233 -396 -5 627 O HETATM 3214 O HOH A 426 -15.540 -5.008 -1.070 1.00 80.64 O ANISOU 3214 O HOH A 426 10072 10259 10310 -577 -584 926 O HETATM 3215 O HOH A 427 -21.604 -1.230 3.109 1.00 65.45 O ANISOU 3215 O HOH A 427 8312 8644 7913 -608 -470 886 O HETATM 3216 O HOH A 428 -1.580 13.828 3.647 1.00 64.12 O ANISOU 3216 O HOH A 428 7909 8159 8295 -1097 -1562 605 O HETATM 3217 O HOH A 429 -3.552 15.174 3.845 1.00 76.17 O ANISOU 3217 O HOH A 429 9584 9629 9728 -1072 -1503 464 O HETATM 3218 O HOH B 301 -10.384 16.130 -27.392 1.00 42.59 O ANISOU 3218 O HOH B 301 4586 5996 5602 -326 54 1207 O HETATM 3219 O HOH B 302 13.812 7.915 -23.569 1.00 67.46 O ANISOU 3219 O HOH B 302 6271 9466 9894 -108 137 2110 O HETATM 3220 O HOH B 303 -3.489 15.874 -21.647 1.00 54.15 O ANISOU 3220 O HOH B 303 5883 7166 7526 -548 -196 1291 O HETATM 3221 O HOH B 304 -5.625 19.520 -28.082 1.00 54.02 O ANISOU 3221 O HOH B 304 5751 7400 7374 -431 78 1607 O HETATM 3222 O HOH B 305 4.297 14.100 -31.678 1.00 48.41 O ANISOU 3222 O HOH B 305 4398 7255 6740 -121 481 1958 O HETATM 3223 O HOH B 306 -5.420 7.669 -15.275 1.00 40.16 O ANISOU 3223 O HOH B 306 4422 5282 5557 -475 -376 870 O HETATM 3224 O HOH B 307 -9.055 4.538 -33.786 1.00 67.05 O ANISOU 3224 O HOH B 307 7771 9585 8118 146 366 626 O HETATM 3225 O HOH B 308 7.856 7.731 -17.984 1.00 61.41 O ANISOU 3225 O HOH B 308 6177 8263 8894 -380 -301 1592 O HETATM 3226 O HOH B 309 5.393 -5.649 -25.176 1.00 73.25 O ANISOU 3226 O HOH B 309 8044 9762 10023 596 409 869 O HETATM 3227 O HOH B 310 2.922 2.326 -37.436 1.00 69.22 O ANISOU 3227 O HOH B 310 7425 10304 8571 722 977 1031 O HETATM 3228 O HOH B 311 -2.173 10.408 -9.043 1.00 43.46 O ANISOU 3228 O HOH B 311 4832 5570 6112 -733 -778 944 O HETATM 3229 O HOH B 312 -6.428 2.814 -36.468 1.00 64.14 O ANISOU 3229 O HOH B 312 7327 9417 7626 368 563 585 O HETATM 3230 O HOH B 313 4.599 3.860 -13.748 1.00 66.92 O ANISOU 3230 O HOH B 313 7253 8765 9410 -358 -479 1291 O HETATM 3231 O HOH B 314 -5.308 -3.504 -21.319 1.00 68.81 O ANISOU 3231 O HOH B 314 8092 8923 9130 16 -13 537 O HETATM 3232 O HOH B 315 -2.608 16.570 -19.291 1.00 66.75 O ANISOU 3232 O HOH B 315 7497 8636 9231 -653 -339 1273 O HETATM 3233 O HOH B 316 -2.059 -1.606 -33.758 1.00 81.46 O ANISOU 3233 O HOH B 316 9449 11324 10176 544 618 486 O HETATM 3234 O HOH B 317 1.588 11.588 -18.553 1.00 51.41 O ANISOU 3234 O HOH B 317 5338 6842 7352 -532 -320 1328 O HETATM 3235 O HOH B 318 -6.816 6.712 -13.218 1.00 52.89 O ANISOU 3235 O HOH B 318 6145 6844 7106 -500 -440 796 O HETATM 3236 O HOH B 319 -4.185 -0.844 -34.711 1.00 75.77 O ANISOU 3236 O HOH B 319 8818 10668 9302 482 580 422 O HETATM 3237 O HOH B 320 3.429 8.682 -17.852 1.00 64.76 O ANISOU 3237 O HOH B 320 6941 8578 9088 -436 -313 1342 O HETATM 3238 O HOH B 321 -3.877 19.364 -30.142 1.00 53.13 O ANISOU 3238 O HOH B 321 5483 7458 7246 -374 197 1772 O HETATM 3239 O HOH B 322 0.537 11.074 -15.338 1.00 64.52 O ANISOU 3239 O HOH B 322 7157 8384 8974 -610 -490 1193 O HETATM 3240 O HOH B 323 -2.605 1.899 -15.432 1.00 48.82 O ANISOU 3240 O HOH B 323 5406 6381 6762 -284 -312 893 O HETATM 3241 O HOH B 324 2.874 -4.608 -29.438 1.00 81.44 O ANISOU 3241 O HOH B 324 9233 11014 10695 653 580 654 O HETATM 3242 O HOH B 325 -10.921 15.625 -31.725 1.00 56.29 O ANISOU 3242 O HOH B 325 6244 8048 7095 -186 216 1292 O HETATM 3243 O HOH B 326 6.279 -0.406 -31.740 1.00 62.08 O ANISOU 3243 O HOH B 326 6387 8961 8240 674 776 1090 O HETATM 3244 O HOH B 327 4.112 12.888 -28.668 1.00 60.55 O ANISOU 3244 O HOH B 327 6046 8584 8376 -197 302 1781 O HETATM 3245 O HOH B 328 -0.119 17.466 -30.526 1.00 56.84 O ANISOU 3245 O HOH B 328 5742 8066 7787 -317 285 1870 O HETATM 3246 O HOH B 329 -0.810 11.274 -11.327 1.00 59.09 O ANISOU 3246 O HOH B 329 6667 7577 8206 -721 -701 1048 O HETATM 3247 O HOH B 330 -4.770 19.776 -32.821 1.00 49.64 O ANISOU 3247 O HOH B 330 5006 7208 6646 -282 320 1875 O HETATM 3248 O HOH B 331 0.566 13.602 -17.018 1.00 73.08 O ANISOU 3248 O HOH B 331 8183 9469 10116 -656 -443 1284 O HETATM 3249 O HOH B 332 -1.585 -3.245 -23.210 1.00 59.10 O ANISOU 3249 O HOH B 332 6657 7826 7971 180 129 656 O HETATM 3250 O HOH B 333 -2.740 14.980 -15.515 1.00 59.82 O ANISOU 3250 O HOH B 333 6750 7663 8316 -707 -511 1104 O HETATM 3251 O HOH B 334 7.659 15.055 -31.070 1.00 95.82 O ANISOU 3251 O HOH B 334 10117 13273 13016 -197 472 2234 O HETATM 3252 O HOH B 335 -1.559 12.572 -13.508 1.00 58.65 O ANISOU 3252 O HOH B 335 6593 7533 8156 -698 -593 1071 O HETATM 3253 O HOH B 336 -8.884 -4.821 -22.272 1.00 53.97 O ANISOU 3253 O HOH B 336 6385 6997 7126 -26 -29 337 O HETATM 3254 O HOH B 337 -5.816 18.113 -22.076 1.00 72.33 O ANISOU 3254 O HOH B 337 8281 9402 9800 -571 -196 1283 O HETATM 3255 O HOH B 338 -9.474 15.244 -15.858 1.00 49.00 O ANISOU 3255 O HOH B 338 5693 6275 6649 -601 -396 855 O HETATM 3256 O HOH B 339 -9.001 12.510 -20.056 1.00 43.72 O ANISOU 3256 O HOH B 339 4896 5827 5891 -456 -203 915 O HETATM 3257 O HOH B 340 -10.186 14.694 -18.540 1.00 50.67 O ANISOU 3257 O HOH B 340 5852 6597 6801 -524 -275 897 O HETATM 3258 O HOH B 341 -0.545 16.130 -22.667 1.00 55.08 O ANISOU 3258 O HOH B 341 5791 7361 7778 -555 -154 1482 O HETATM 3259 O HOH B 342 1.778 -6.596 -27.212 1.00 67.05 O ANISOU 3259 O HOH B 342 7543 8947 8987 598 442 547 O HETATM 3260 O HOH B 343 -14.844 4.276 -29.517 1.00 65.02 O ANISOU 3260 O HOH B 343 7741 9017 7946 -115 78 452 O HETATM 3261 O HOH B 344 9.269 -0.265 -30.383 1.00 71.27 O ANISOU 3261 O HOH B 344 7303 10126 9651 687 771 1323 O HETATM 3262 O HOH B 345 7.831 -3.204 -27.991 1.00 85.79 O ANISOU 3262 O HOH B 345 9366 11672 11559 687 615 1082 O HETATM 3263 O HOH B 346 1.782 -8.820 -24.233 1.00 79.90 O ANISOU 3263 O HOH B 346 9225 10315 10817 563 302 551 O HETATM 3264 O HOH B 347 -4.376 17.292 -14.910 1.00 72.71 O ANISOU 3264 O HOH B 347 8495 9186 9945 -764 -556 1047 O HETATM 3265 O HOH B 348 2.364 12.733 -25.771 1.00 70.81 O ANISOU 3265 O HOH B 348 7545 9659 9699 -314 102 1589 O HETATM 3266 O HOH B 349 -7.036 20.762 -32.471 1.00 59.18 O ANISOU 3266 O HOH B 349 6326 8335 7826 -303 263 1821 O HETATM 3267 O HOH B 350 13.015 12.600 -20.931 1.00 73.28 O ANISOU 3267 O HOH B 350 7077 9969 10796 -550 -224 2181 O HETATM 3268 O HOH B 351 10.725 4.326 -19.017 1.00 85.54 O ANISOU 3268 O HOH B 351 9004 11441 12054 -124 -141 1699 O HETATM 3269 O HOH B 352 -6.812 2.210 -32.104 1.00 64.72 O ANISOU 3269 O HOH B 352 7458 9137 7996 199 372 564 O HETATM 3270 O HOH C 301 -38.536 -13.185 -23.053 1.00 58.44 O ANISOU 3270 O HOH C 301 7015 7467 7721 -1272 -816 -36 O HETATM 3271 O HOH C 302 -39.318 -9.993 -5.801 1.00 47.77 O ANISOU 3271 O HOH C 302 5470 6343 6338 -1113 -255 1130 O HETATM 3272 O HOH C 303 -31.520 7.092 -24.734 1.00 40.37 O ANISOU 3272 O HOH C 303 4660 5925 4752 -431 -214 488 O HETATM 3273 O HOH C 304 -43.587 -16.061 -15.376 1.00 60.81 O ANISOU 3273 O HOH C 304 6980 7624 8499 -1632 -767 665 O HETATM 3274 O HOH C 305 -37.909 -1.486 -5.391 1.00 46.21 O ANISOU 3274 O HOH C 305 5413 6458 5687 -726 -73 913 O HETATM 3275 O HOH C 306 -26.206 10.313 -16.491 1.00 40.06 O ANISOU 3275 O HOH C 306 4816 5464 4942 -411 -168 531 O HETATM 3276 O HOH C 307 -38.609 4.416 -16.523 1.00 41.63 O ANISOU 3276 O HOH C 307 4717 6030 5069 -584 -180 630 O HETATM 3277 O HOH C 308 -30.256 3.012 -9.767 1.00 46.72 O ANISOU 3277 O HOH C 308 5700 6311 5740 -565 -191 564 O HETATM 3278 O HOH C 309 -43.042 -15.428 -5.271 1.00 62.47 O ANISOU 3278 O HOH C 309 7101 8010 8625 -1478 -362 1442 O HETATM 3279 O HOH C 310 -22.428 7.358 -20.491 1.00 50.44 O ANISOU 3279 O HOH C 310 6068 6834 6265 -404 -167 494 O HETATM 3280 O HOH C 311 -40.245 5.518 -11.712 1.00 44.47 O ANISOU 3280 O HOH C 311 5079 6417 5401 -506 -34 749 O HETATM 3281 O HOH C 312 -30.201 13.715 -12.958 1.00 41.05 O ANISOU 3281 O HOH C 312 5000 5572 5024 -313 -93 538 O HETATM 3282 O HOH C 313 -44.725 -2.036 -19.215 1.00 73.30 O ANISOU 3282 O HOH C 313 8424 10171 9256 -987 -447 665 O HETATM 3283 O HOH C 314 -24.337 0.005 -23.830 1.00 65.54 O ANISOU 3283 O HOH C 314 8027 8776 8101 -440 -225 205 O HETATM 3284 O HOH C 315 -48.424 -14.442 -11.546 1.00 51.00 O ANISOU 3284 O HOH C 315 5362 6757 7260 -1714 -593 1198 O HETATM 3285 O HOH C 316 -40.441 -5.299 -0.312 1.00 66.68 O ANISOU 3285 O HOH C 316 7881 9167 8289 -845 30 1321 O HETATM 3286 O HOH C 317 -28.438 0.290 -14.833 1.00 38.66 O ANISOU 3286 O HOH C 317 4643 5223 4823 -602 -261 439 O HETATM 3287 O HOH C 318 -46.381 0.803 -9.280 1.00 67.58 O ANISOU 3287 O HOH C 318 7661 9560 8457 -733 6 1078 O HETATM 3288 O HOH C 319 -24.989 14.205 -32.862 1.00 63.98 O ANISOU 3288 O HOH C 319 7492 9248 7571 -169 -7 920 O HETATM 3289 O HOH C 320 -32.439 -6.982 -8.269 1.00 45.41 O ANISOU 3289 O HOH C 320 5444 5919 5889 -857 -302 750 O HETATM 3290 O HOH C 321 -23.114 -2.486 -22.201 1.00 59.40 O ANISOU 3290 O HOH C 321 7293 7833 7444 -456 -247 166 O HETATM 3291 O HOH C 322 -24.599 7.165 -23.572 1.00 49.01 O ANISOU 3291 O HOH C 322 5843 6810 5966 -379 -150 474 O HETATM 3292 O HOH C 323 -38.263 9.085 -14.105 1.00 47.07 O ANISOU 3292 O HOH C 323 5476 6695 5713 -384 -40 677 O HETATM 3293 O HOH C 324 -27.933 3.969 -30.832 1.00 87.05 O ANISOU 3293 O HOH C 324 10623 12026 10426 -362 -222 266 O HETATM 3294 O HOH C 325 -18.025 -4.702 -16.462 1.00 58.65 O ANISOU 3294 O HOH C 325 7210 7445 7629 -426 -279 343 O HETATM 3295 O HOH C 326 -39.831 -13.970 6.607 1.00 50.76 O ANISOU 3295 O HOH C 326 5762 7019 6505 -1120 21 2141 O HETATM 3296 O HOH C 327 -37.982 6.616 -12.731 1.00 46.03 O ANISOU 3296 O HOH C 327 5364 6535 5592 -471 -64 671 O HETATM 3297 O HOH C 328 -48.027 2.588 -16.002 1.00 62.71 O ANISOU 3297 O HOH C 328 6888 9085 7855 -750 -188 969 O HETATM 3298 O HOH C 329 -26.254 8.174 -25.469 1.00 50.76 O ANISOU 3298 O HOH C 329 6022 7158 6106 -357 -143 510 O HETATM 3299 O HOH C 330 -36.141 0.403 -6.338 1.00 53.47 O ANISOU 3299 O HOH C 330 6413 7340 6563 -650 -90 793 O HETATM 3300 O HOH C 331 -28.544 8.262 -23.409 1.00 37.54 O ANISOU 3300 O HOH C 331 4357 5440 4468 -394 -167 514 O HETATM 3301 O HOH C 332 -46.668 -10.186 -13.068 1.00 54.27 O ANISOU 3301 O HOH C 332 5903 7377 7338 -1420 -495 988 O HETATM 3302 O HOH C 333 -44.036 -9.346 -0.986 1.00 56.17 O ANISOU 3302 O HOH C 333 6285 7792 7265 -1116 -11 1595 O HETATM 3303 O HOH C 334 -34.150 -6.364 -1.022 1.00 67.78 O ANISOU 3303 O HOH C 334 8263 8992 8498 -822 -158 1122 O HETATM 3304 O HOH C 335 -44.872 -17.729 -4.680 1.00 59.63 O ANISOU 3304 O HOH C 335 6613 7565 8480 -1661 -404 1634 O HETATM 3305 O HOH C 336 -30.754 -17.473 -3.049 1.00 62.29 O ANISOU 3305 O HOH C 336 7579 7464 8622 -1087 -439 1266 O HETATM 3306 O HOH C 337 -47.403 -4.146 -10.158 1.00 54.28 O ANISOU 3306 O HOH C 337 5865 7756 7005 -1048 -169 1149 O HETATM 3307 O HOH C 338 -20.777 11.372 -27.257 1.00 60.98 O ANISOU 3307 O HOH C 338 7235 8456 7478 -273 -38 710 O HETATM 3308 O HOH C 339 -34.742 -22.722 -15.768 1.00 70.31 O ANISOU 3308 O HOH C 339 8700 7888 10128 -1428 -834 272 O HETATM 3309 O HOH C 340 -46.719 -6.401 -3.399 1.00 68.14 O ANISOU 3309 O HOH C 340 7665 9505 8720 -1044 31 1489 O HETATM 3310 O HOH C 341 -38.959 -19.686 -7.199 1.00 54.36 O ANISOU 3310 O HOH C 341 6311 6412 7932 -1529 -563 1202 O HETATM 3311 O HOH C 342 -23.879 -19.237 -15.338 1.00 68.78 O ANISOU 3311 O HOH C 342 8685 7819 9630 -736 -528 188 O HETATM 3312 O HOH C 343 -39.460 -17.767 -17.136 1.00 60.72 O ANISOU 3312 O HOH C 343 7238 7309 8522 -1511 -815 346 O HETATM 3313 O HOH C 344 -25.783 -10.025 -7.020 1.00 52.11 O ANISOU 3313 O HOH C 344 6420 6462 6918 -764 -390 760 O HETATM 3314 O HOH C 345 -23.302 5.265 -24.557 1.00 53.93 O ANISOU 3314 O HOH C 345 6476 7437 6576 -367 -147 403 O HETATM 3315 O HOH C 346 -32.858 -0.850 -6.134 1.00 58.36 O ANISOU 3315 O HOH C 346 7127 7818 7228 -671 -169 744 O HETATM 3316 O HOH C 347 -39.971 -0.803 -3.730 1.00 62.39 O ANISOU 3316 O HOH C 347 7398 8644 7664 -688 24 1018 O HETATM 3317 O HOH C 348 -36.190 7.622 -10.737 1.00 46.88 O ANISOU 3317 O HOH C 348 5581 6562 5669 -424 -39 635 O HETATM 3318 O HOH C 349 -41.752 10.322 -11.108 1.00 72.94 O ANISOU 3318 O HOH C 349 8676 10088 8952 -272 106 780 O HETATM 3319 O HOH C 350 -37.097 -11.331 -4.888 1.00 45.94 O ANISOU 3319 O HOH C 350 5327 5969 6157 -1101 -286 1142 O HETATM 3320 O HOH C 351 -40.073 2.637 -5.554 1.00 51.03 O ANISOU 3320 O HOH C 351 5980 7242 6167 -559 52 885 O HETATM 3321 O HOH C 352 -27.092 -2.984 -11.349 1.00 52.27 O ANISOU 3321 O HOH C 352 6416 6793 6652 -657 -301 518 O HETATM 3322 O HOH C 353 -39.334 -8.264 -7.992 1.00 46.45 O ANISOU 3322 O HOH C 353 5313 6231 6107 -1060 -271 973 O HETATM 3323 O HOH C 354 -42.298 2.936 -7.870 1.00 50.60 O ANISOU 3323 O HOH C 354 5786 7264 6176 -580 42 911 O HETATM 3324 O HOH C 355 -47.030 -13.977 -6.492 1.00 56.86 O ANISOU 3324 O HOH C 355 6153 7560 7893 -1556 -343 1506 O HETATM 3325 O HOH C 356 -36.741 -2.979 -3.354 1.00 50.33 O ANISOU 3325 O HOH C 356 5985 6933 6207 -752 -83 987 O HETATM 3326 O HOH C 357 -40.810 3.480 -15.326 1.00 56.81 O ANISOU 3326 O HOH C 357 6556 8009 7020 -632 -165 707 O HETATM 3327 O HOH C 358 -36.198 -11.774 -22.555 1.00 64.14 O ANISOU 3327 O HOH C 358 7799 8212 8358 -1113 -700 -19 O HETATM 3328 O HOH C 359 -23.049 11.168 -25.661 1.00 54.85 O ANISOU 3328 O HOH C 359 6507 7626 6710 -308 -84 655 O HETATM 3329 O HOH C 360 -41.210 -16.522 -6.848 1.00 62.89 O ANISOU 3329 O HOH C 360 7270 7859 8767 -1481 -458 1261 O HETATM 3330 O HOH C 361 -19.086 -14.630 -14.121 1.00 73.68 O ANISOU 3330 O HOH C 361 9228 8765 10004 -497 -399 331 O HETATM 3331 O HOH C 362 -44.857 -2.605 -16.922 1.00 65.58 O ANISOU 3331 O HOH C 362 7444 9140 8334 -1000 -385 750 O HETATM 3332 O HOH C 363 -25.272 6.540 -30.914 1.00 75.30 O ANISOU 3332 O HOH C 363 9098 10541 8971 -278 -119 423 O HETATM 3333 O HOH C 364 -41.626 -19.131 -6.174 1.00 58.64 O ANISOU 3333 O HOH C 364 6697 7133 8449 -1616 -515 1388 O HETATM 3334 O HOH C 365 -27.224 6.636 -27.233 1.00 61.05 O ANISOU 3334 O HOH C 365 7317 8559 7320 -364 -170 437 O HETATM 3335 O HOH C 366 -29.461 5.775 -26.486 1.00 56.32 O ANISOU 3335 O HOH C 366 6713 7960 6727 -418 -217 408 O HETATM 3336 O HOH C 367 -37.723 8.735 -8.898 1.00 64.84 O ANISOU 3336 O HOH C 367 7852 8891 7894 -353 40 669 O HETATM 3337 O HOH C 368 -38.831 4.995 -4.981 1.00 70.86 O ANISOU 3337 O HOH C 368 8593 9730 8599 -450 79 799 O HETATM 3338 O HOH C 369 -30.048 5.219 -10.511 1.00 54.46 O ANISOU 3338 O HOH C 369 6687 7308 6697 -512 -172 538 O HETATM 3339 O HOH C 370 -45.576 -1.987 -5.051 1.00 76.81 O ANISOU 3339 O HOH C 370 8887 10672 9627 -808 72 1235 O HETATM 3340 O HOH C 371 -48.227 -5.414 -12.322 1.00 53.02 O ANISOU 3340 O HOH C 371 5640 7568 6938 -1175 -299 1096 O HETATM 3341 O HOH C 372 -47.125 -7.190 -13.606 1.00 52.37 O ANISOU 3341 O HOH C 372 5632 7336 6929 -1270 -415 978 O HETATM 3342 O HOH C 373 -45.877 -9.951 -15.831 1.00 78.49 O ANISOU 3342 O HOH C 373 9041 10423 10357 -1411 -596 778 O HETATM 3343 O HOH C 374 -48.094 -3.691 -14.783 1.00 79.05 O ANISOU 3343 O HOH C 374 8948 10938 10149 -1105 -346 975 O HETATM 3344 O HOH C 375 -44.598 2.156 -7.120 1.00 66.75 O ANISOU 3344 O HOH C 375 7705 9414 8242 -612 90 1035 O HETATM 3345 O HOH C 376 -21.943 -12.075 -24.235 1.00 65.00 O ANISOU 3345 O HOH C 376 8195 8068 8435 -431 -343 -269 O HETATM 3346 O HOH C 377 -38.618 11.059 -12.724 1.00 61.42 O ANISOU 3346 O HOH C 377 7326 8497 7515 -290 27 688 O HETATM 3347 O HOH C 378 -25.353 -4.079 -9.076 1.00 61.07 O ANISOU 3347 O HOH C 378 7562 7835 7806 -656 -327 592 O HETATM 3348 O HOH C 379 -33.045 12.254 -11.636 1.00 60.32 O ANISOU 3348 O HOH C 379 7404 8117 7400 -307 -46 556 O HETATM 3349 O HOH C 380 -40.893 7.667 -10.023 1.00 62.59 O ANISOU 3349 O HOH C 380 7395 8745 7641 -388 62 773 O HETATM 3350 O HOH C 381 -40.012 -4.684 -25.812 1.00 61.41 O ANISOU 3350 O HOH C 381 7204 8540 7590 -991 -660 157 O HETATM 3351 O HOH C 382 -42.177 -3.600 -24.868 1.00 65.22 O ANISOU 3351 O HOH C 382 7561 9124 8094 -1017 -648 306 O HETATM 3352 O HOH C 383 -19.725 -13.982 -20.798 1.00 71.23 O ANISOU 3352 O HOH C 383 8980 8599 9486 -401 -338 -104 O HETATM 3353 O HOH C 384 -37.631 -3.104 -1.159 1.00 72.36 O ANISOU 3353 O HOH C 384 8758 9814 8921 -736 -18 1103 O HETATM 3354 O HOH C 385 -51.522 -5.404 -11.237 1.00 68.37 O ANISOU 3354 O HOH C 385 7342 9694 8941 -1228 -239 1326 O HETATM 3355 O HOH C 386 -23.438 9.218 -36.938 1.00 80.77 O ANISOU 3355 O HOH C 386 9670 11680 9338 -99 16 628 O HETATM 3356 O HOH C 387 -30.862 -4.237 -4.552 1.00 58.18 O ANISOU 3356 O HOH C 387 7140 7659 7307 -740 -237 833 O HETATM 3357 O HOH C 388 -37.890 -6.988 5.438 1.00 96.12 O ANISOU 3357 O HOH C 388 11745 12972 11804 -797 69 1583 O HETATM 3358 O HOH C 389 -39.776 11.964 -10.840 1.00 77.52 O ANISOU 3358 O HOH C 389 9372 10558 9524 -218 103 705 O HETATM 3359 O HOH D 301 -30.783 11.041 -32.607 1.00 36.81 O ANISOU 3359 O HOH D 301 4068 5927 3990 -256 -171 701 O HETATM 3360 O HOH D 302 -41.380 5.269 -14.151 1.00 57.36 O ANISOU 3360 O HOH D 302 6620 8114 7059 -544 -88 755 O HETATM 3361 O HOH D 303 -45.380 9.802 -16.522 1.00 51.74 O ANISOU 3361 O HOH D 303 5685 7645 6328 -344 -11 915 O HETATM 3362 O HOH D 304 -47.469 5.035 -13.697 1.00 74.77 O ANISOU 3362 O HOH D 304 8489 10605 9317 -568 -26 1001 O HETATM 3363 O HOH D 305 -53.338 12.914 -17.037 1.00 82.90 O ANISOU 3363 O HOH D 305 9109 12024 10364 -108 137 1320 O HETATM 3364 O HOH D 306 -34.037 1.238 -27.084 1.00 49.78 O ANISOU 3364 O HOH D 306 5853 7177 5886 -607 -392 239 O HETATM 3365 O HOH D 307 -38.644 7.462 -30.458 1.00 49.26 O ANISOU 3365 O HOH D 307 5518 7578 5620 -472 -393 587 O HETATM 3366 O HOH D 308 -32.760 21.410 -22.171 1.00 57.71 O ANISOU 3366 O HOH D 308 6834 7814 7279 -74 -4 952 O HETATM 3367 O HOH D 309 -44.510 17.880 -32.728 1.00 61.63 O ANISOU 3367 O HOH D 309 6656 9502 7259 -58 -274 1363 O HETATM 3368 O HOH D 310 -42.319 -1.619 -20.415 1.00 45.98 O ANISOU 3368 O HOH D 310 5091 6649 5729 -919 -451 541 O HETATM 3369 O HOH D 311 -46.879 8.463 -23.298 1.00 66.09 O ANISOU 3369 O HOH D 311 7310 9724 8076 -493 -278 924 O HETATM 3370 O HOH D 312 -29.361 16.836 -17.566 1.00 53.72 O ANISOU 3370 O HOH D 312 6509 7183 6719 -256 -81 663 O HETATM 3371 O HOH D 313 -42.516 19.207 -35.390 1.00 42.67 O ANISOU 3371 O HOH D 313 4279 7186 4748 -6 -271 1467 O HETATM 3372 O HOH D 314 -37.961 4.408 -20.361 1.00 40.65 O ANISOU 3372 O HOH D 314 4577 5971 4897 -592 -258 555 O HETATM 3373 O HOH D 315 -44.272 7.368 -25.888 1.00 54.01 O ANISOU 3373 O HOH D 315 5906 8167 6448 -546 -374 771 O HETATM 3374 O HOH D 316 -32.416 15.000 -11.774 1.00 52.43 O ANISOU 3374 O HOH D 316 6447 7039 6437 -238 -32 544 O HETATM 3375 O HOH D 317 -41.962 22.202 -12.348 1.00 62.03 O ANISOU 3375 O HOH D 317 7428 8396 7746 278 299 765 O HETATM 3376 O HOH D 318 -35.889 14.717 -12.475 1.00 57.77 O ANISOU 3376 O HOH D 318 7006 7858 7085 -187 36 619 O HETATM 3377 O HOH D 319 -33.004 25.632 -24.155 1.00 67.38 O ANISOU 3377 O HOH D 319 7996 8947 8658 47 37 1189 O HETATM 3378 O HOH D 320 -39.950 17.127 -13.578 1.00 61.81 O ANISOU 3378 O HOH D 320 7368 8493 7625 -24 141 744 O HETATM 3379 O HOH D 321 -32.608 7.398 -29.341 1.00 49.57 O ANISOU 3379 O HOH D 321 5749 7361 5725 -397 -257 494 O HETATM 3380 O HOH D 322 -40.664 7.788 -15.257 1.00 48.90 O ANISOU 3380 O HOH D 322 5578 7044 5957 -440 -65 735 O HETATM 3381 O HOH D 323 -32.831 3.814 -27.709 1.00 47.93 O ANISOU 3381 O HOH D 323 5605 7008 5597 -506 -319 331 O HETATM 3382 O HOH D 324 -44.623 9.092 -28.165 1.00 54.40 O ANISOU 3382 O HOH D 324 5897 8360 6413 -474 -398 844 O HETATM 3383 O HOH D 325 -33.520 20.879 -15.109 1.00 65.11 O ANISOU 3383 O HOH D 325 7988 8543 8206 -58 31 676 O HETATM 3384 O HOH D 326 -43.299 -3.388 -22.580 1.00 62.68 O ANISOU 3384 O HOH D 326 7172 8786 7859 -1036 -589 446 O HETATM 3385 O HOH D 327 -54.334 11.486 -29.138 1.00 57.82 O ANISOU 3385 O HOH D 327 5655 9360 6952 -410 -498 1372 O HETATM 3386 O HOH D 328 -42.997 8.209 -13.594 1.00 68.34 O ANISOU 3386 O HOH D 328 7958 9590 8417 -397 13 824 O HETATM 3387 O HOH D 329 -33.478 5.965 -31.576 1.00 56.78 O ANISOU 3387 O HOH D 329 6649 8412 6514 -424 -327 409 O HETATM 3388 O HOH D 330 -29.423 15.324 -33.770 1.00 55.65 O ANISOU 3388 O HOH D 330 6377 8339 6428 -152 -76 997 O HETATM 3389 O HOH D 331 -31.314 18.267 -34.176 1.00 52.84 O ANISOU 3389 O HOH D 331 5940 8009 6127 -88 -68 1210 O HETATM 3390 O HOH D 332 -51.325 19.718 -26.347 1.00 78.78 O ANISOU 3390 O HOH D 332 8556 11591 9788 157 -59 1544 O HETATM 3391 O HOH D 333 -45.551 -4.979 -21.558 1.00 81.66 O ANISOU 3391 O HOH D 333 9460 11182 10386 -1178 -642 534 O HETATM 3392 O HOH D 334 -41.611 8.763 -31.258 1.00 54.75 O ANISOU 3392 O HOH D 334 6063 8450 6290 -458 -439 728 O HETATM 3393 O HOH D 335 -27.023 16.832 -33.825 1.00 65.47 O ANISOU 3393 O HOH D 335 7613 9509 7755 -127 -9 1106 O HETATM 3394 O HOH D 336 -41.400 28.209 -25.341 1.00 70.57 O ANISOU 3394 O HOH D 336 8113 9608 9093 389 137 1488 O HETATM 3395 O HOH D 337 -52.570 14.821 -22.522 1.00 66.29 O ANISOU 3395 O HOH D 337 6963 10011 8214 -89 -55 1364 O HETATM 3396 O HOH D 338 -49.494 11.932 -17.453 1.00 83.13 O ANISOU 3396 O HOH D 338 9401 11847 10339 -213 51 1117 O HETATM 3397 O HOH D 339 -45.726 24.880 -20.108 1.00 65.43 O ANISOU 3397 O HOH D 339 7426 9102 8332 418 246 1246 O HETATM 3398 O HOH D 340 -50.619 9.939 -22.206 1.00 64.54 O ANISOU 3398 O HOH D 340 6881 9692 7948 -406 -204 1135 O HETATM 3399 O HOH D 341 -33.538 6.134 -26.463 1.00 50.98 O ANISOU 3399 O HOH D 341 5952 7396 6023 -466 -271 461 O HETATM 3400 O HOH D 342 -32.548 20.072 -12.005 1.00 71.63 O ANISOU 3400 O HOH D 342 8936 9303 8978 -92 13 545 O HETATM 3401 O HOH D 343 -42.558 11.145 -32.571 1.00 58.27 O ANISOU 3401 O HOH D 343 6416 9034 6691 -363 -425 895 O HETATM 3402 O HOH D 344 -47.126 8.720 -19.144 1.00 57.83 O ANISOU 3402 O HOH D 344 6305 8562 7105 -434 -121 963 O HETATM 3403 O HOH D 345 -49.860 9.375 -18.892 1.00 65.30 O ANISOU 3403 O HOH D 345 7079 9649 8083 -392 -84 1097 O HETATM 3404 O HOH D 346 -37.125 2.698 -18.451 1.00 54.11 O ANISOU 3404 O HOH D 346 6337 7563 6659 -642 -257 533 O HETATM 3405 O HOH D 347 -37.379 25.583 -19.479 1.00 80.30 O ANISOU 3405 O HOH D 347 9696 10529 10286 191 126 1004 O HETATM 3406 O HOH D 348 -27.435 19.290 -31.117 1.00 61.60 O ANISOU 3406 O HOH D 348 7146 8764 7495 -133 -6 1176 O HETATM 3407 O HOH D 349 -48.185 6.438 -17.358 1.00 66.43 O ANISOU 3407 O HOH D 349 7346 9651 8245 -544 -120 990 O HETATM 3408 O HOH D 350 -35.753 11.168 -36.427 1.00 58.23 O ANISOU 3408 O HOH D 350 6624 9066 6436 -263 -327 781 O HETATM 3409 O HOH D 351 -43.909 7.603 -30.155 1.00 59.33 O ANISOU 3409 O HOH D 351 6558 9045 6940 -542 -492 737 O HETATM 3410 O HOH D 352 -44.310 21.362 -34.568 1.00 60.05 O ANISOU 3410 O HOH D 352 6388 9345 7084 104 -225 1634 O HETATM 3411 O HOH D 353 -42.863 24.005 -16.130 1.00 81.62 O ANISOU 3411 O HOH D 353 9755 10916 10339 338 271 958 O HETATM 3412 O HOH D 354 -48.415 17.073 -14.837 1.00 78.95 O ANISOU 3412 O HOH D 354 9056 11115 9826 131 277 1078 O HETATM 3413 O HOH D 355 -48.620 5.973 -21.473 1.00 70.53 O ANISOU 3413 O HOH D 355 7789 10285 8722 -628 -299 946 O HETATM 3414 O HOH D 356 -49.730 1.442 -20.386 1.00 77.72 O ANISOU 3414 O HOH D 356 8645 11122 9763 -901 -416 917 O HETATM 3415 O HOH D 357 -45.459 9.050 -13.945 1.00 63.40 O ANISOU 3415 O HOH D 357 7199 9088 7803 -348 54 919 O HETATM 3416 O HOH D 358 -39.864 5.110 -30.490 1.00 59.53 O ANISOU 3416 O HOH D 358 6808 8883 6927 -582 -485 485 O HETATM 3417 O HOH D 359 -46.216 11.287 -29.256 1.00 70.85 O ANISOU 3417 O HOH D 359 7857 10586 8476 -379 -389 1006 O HETATM 3418 O HOH D 360 -44.874 16.121 -30.906 1.00 73.38 O ANISOU 3418 O HOH D 360 8179 10913 8790 -138 -277 1232 O HETATM 3419 O HOH D 361 -45.270 6.627 -23.281 1.00 60.43 O ANISOU 3419 O HOH D 361 6696 8911 7354 -579 -322 805 O MASTER 586 0 0 11 14 0 0 6 3377 4 0 36 END
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Related entries of code: 3rea
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2jkr
RCSB PDB
PDBbind
11aa, >2JKR_5|Chains... at 100%
3rbb
RCSB PDB
PDBbind
61aa, >3RBB_2|Chains... at 91%
3reb
RCSB PDB
PDBbind
90aa, >3REB_2|Chains... *
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3rea
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
HIV-1 Nef protein (delta 1-44)
Ligand Name
engineered Tyrosine-protein kinase Hck-SH3 domain (NI1-2)
EC.Number
E.C.-.-.-.-
Resolution
2(Å)
Affinity (Kd/Ki/IC50)
Kd=179nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) PLOS ONE Vol. 6: pp. e20033
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):
P08631
P03407
Entrez Gene ID
NCBI Entrez Gene ID:
3055
ASD
Information of known allosteric effects of PDB entries
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