Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 18-JAN-11 3QDM TITLE THE COMPLEX BETWEEN TCR DMF4 AND HUMAN CLASS I MHC HLA-A2 WITH THE TITLE 2 BOUND MART-1(26-35)(A27L) DECAMERIC PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MHC CLASS I ANTIGEN A*2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: MART-1(27-35) PEPTIDE; COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES; COMPND 15 MUTATION: YES; COMPND 16 MOL_ID: 4; COMPND 17 MOLECULE: DMF4 ALPHA CHAIN; COMPND 18 CHAIN: D; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 5; COMPND 21 MOLECULE: DMF4 BETA CHAIN; COMPND 22 CHAIN: E; COMPND 23 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: HLA-A, HLAA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHN1; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHN1; SOURCE 21 MOL_ID: 3; SOURCE 22 SYNTHETIC: YES; SOURCE 23 MOL_ID: 4; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_COMMON: HUMAN; SOURCE 26 ORGANISM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 29 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 31 MOL_ID: 5; SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 33 ORGANISM_COMMON: HUMAN; SOURCE 34 ORGANISM_TAXID: 9606; SOURCE 35 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 36 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 37 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 38 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS MART-1 PEPTIDE, NONAPEPTIDE, MHC CLASS I, HLA-A2, TCR DMF5, TCR DMF4, KEYWDS 2 CROSS-REACTIVITY, CANCER, MELANOMA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR O.Y.BORBULEVYCH,B.M.BAKER REVDAT 3 07-SEP-11 3QDM 1 JRNL REVDAT 2 17-AUG-11 3QDM 1 JRNL VERSN REVDAT 1 06-JUL-11 3QDM 0 JRNL AUTH O.Y.BORBULEVYCH,S.M.SANTHANAGOPOLAN,M.HOSSAIN,B.M.BAKER JRNL TITL TCRS USED IN CANCER GENE THERAPY CROSS-REACT WITH JRNL TITL 2 MART-1/MELAN-A TUMOR ANTIGENS VIA DISTINCT MECHANISMS. JRNL REF J.IMMUNOL. V. 187 2453 2011 JRNL REFN ISSN 0022-1767 JRNL PMID 21795600 JRNL DOI 10.4049/JIMMUNOL.1101268 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 21058 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, 5% REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.284 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1064 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) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1336 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.08 REMARK 3 BIN R VALUE (WORKING SET) : 0.2940 REMARK 3 BIN FREE R VALUE SET COUNT : 67 REMARK 3 BIN FREE R VALUE : 0.3910 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6591 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 33 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.82000 REMARK 3 B22 (A**2) : 0.41000 REMARK 3 B33 (A**2) : 0.41000 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): 0.477 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.348 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.318 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.858 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6785 ; 0.010 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9224 ; 1.476 ; 1.929 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 820 ; 7.464 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 347 ;34.868 ;23.890 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1090 ;21.575 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;18.193 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 970 ; 0.106 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5310 ; 0.007 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4101 ; 0.686 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6628 ; 1.211 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2684 ; 0.609 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2594 ; 0.970 ; 3.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 182 REMARK 3 RESIDUE RANGE : C 1 C 9 REMARK 3 ORIGIN FOR THE GROUP (A): 11.0310 20.7440 153.6260 REMARK 3 T TENSOR REMARK 3 T11: 0.0748 T22: 0.0101 REMARK 3 T33: 0.0526 T12: -0.0101 REMARK 3 T13: -0.0589 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 4.1739 L22: 2.7265 REMARK 3 L33: 3.3072 L12: -0.4682 REMARK 3 L13: -1.0925 L23: 0.5337 REMARK 3 S TENSOR REMARK 3 S11: 0.2305 S12: -0.1515 S13: -0.1141 REMARK 3 S21: 0.0090 S22: -0.0801 S23: -0.1300 REMARK 3 S31: 0.1191 S32: -0.0285 S33: -0.1504 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 183 A 275 REMARK 3 ORIGIN FOR THE GROUP (A): 0.0950 25.0750 119.6260 REMARK 3 T TENSOR REMARK 3 T11: 0.3331 T22: 0.2166 REMARK 3 T33: 0.1819 T12: -0.0393 REMARK 3 T13: -0.0329 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 3.9864 L22: 6.0777 REMARK 3 L33: 8.0367 L12: -0.5058 REMARK 3 L13: 1.9439 L23: -3.9237 REMARK 3 S TENSOR REMARK 3 S11: -0.1720 S12: 0.4350 S13: 0.6430 REMARK 3 S21: -0.6839 S22: 0.3617 S23: 0.0750 REMARK 3 S31: -0.3161 S32: -0.1163 S33: -0.1897 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 0 B 99 REMARK 3 ORIGIN FOR THE GROUP (A): -9.5800 13.8750 137.3300 REMARK 3 T TENSOR REMARK 3 T11: 0.1443 T22: 0.1403 REMARK 3 T33: 0.1728 T12: -0.0671 REMARK 3 T13: -0.0964 T23: 0.0687 REMARK 3 L TENSOR REMARK 3 L11: 4.4406 L22: 3.4040 REMARK 3 L33: 5.3593 L12: 0.8631 REMARK 3 L13: 0.5133 L23: 1.2068 REMARK 3 S TENSOR REMARK 3 S11: 0.1740 S12: 0.1465 S13: -0.4755 REMARK 3 S21: -0.2462 S22: -0.0068 S23: 0.2488 REMARK 3 S31: 0.5822 S32: -0.5892 S33: -0.1672 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 2 D 110 REMARK 3 ORIGIN FOR THE GROUP (A): 34.1970 17.6080 173.1820 REMARK 3 T TENSOR REMARK 3 T11: 0.0736 T22: 0.2952 REMARK 3 T33: 0.1058 T12: 0.0333 REMARK 3 T13: 0.0353 T23: 0.0551 REMARK 3 L TENSOR REMARK 3 L11: 4.4925 L22: 1.6612 REMARK 3 L33: 11.0544 L12: 1.4285 REMARK 3 L13: 4.7096 L23: 2.6024 REMARK 3 S TENSOR REMARK 3 S11: 0.0567 S12: 0.5576 S13: -0.0028 REMARK 3 S21: -0.0338 S22: 0.0034 S23: -0.1738 REMARK 3 S31: 0.3064 S32: 1.0125 S33: -0.0600 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 111 D 195 REMARK 3 ORIGIN FOR THE GROUP (A): 50.2900 15.8310 204.2770 REMARK 3 T TENSOR REMARK 3 T11: 0.4161 T22: 0.5211 REMARK 3 T33: 0.3513 T12: 0.0531 REMARK 3 T13: -0.1590 T23: -0.2138 REMARK 3 L TENSOR REMARK 3 L11: 7.1674 L22: 5.5908 REMARK 3 L33: 4.7198 L12: 1.2718 REMARK 3 L13: 0.0954 L23: -1.2880 REMARK 3 S TENSOR REMARK 3 S11: 0.4741 S12: -0.2985 S13: -1.0037 REMARK 3 S21: 0.2166 S22: -0.4608 S23: -0.1923 REMARK 3 S31: 0.4845 S32: 0.8246 S33: -0.0132 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 2 E 115 REMARK 3 ORIGIN FOR THE GROUP (A): 14.1500 12.5750 184.5820 REMARK 3 T TENSOR REMARK 3 T11: 0.0112 T22: 0.1298 REMARK 3 T33: 0.0891 T12: -0.0280 REMARK 3 T13: 0.0078 T23: -0.0222 REMARK 3 L TENSOR REMARK 3 L11: 3.5074 L22: 3.8014 REMARK 3 L33: 7.9376 L12: 0.6917 REMARK 3 L13: 0.3652 L23: -3.1183 REMARK 3 S TENSOR REMARK 3 S11: 0.0113 S12: 0.1588 S13: -0.0005 REMARK 3 S21: 0.1028 S22: 0.1315 S23: 0.1534 REMARK 3 S31: 0.0361 S32: -0.4471 S33: -0.1428 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : E 116 E 243 REMARK 3 ORIGIN FOR THE GROUP (A): 34.1910 19.3020 207.9140 REMARK 3 T TENSOR REMARK 3 T11: 0.2606 T22: 0.1156 REMARK 3 T33: 0.0442 T12: 0.0264 REMARK 3 T13: -0.0024 T23: -0.0289 REMARK 3 L TENSOR REMARK 3 L11: 4.6389 L22: 5.8753 REMARK 3 L33: 3.8265 L12: 2.7247 REMARK 3 L13: 0.3186 L23: 1.1886 REMARK 3 S TENSOR REMARK 3 S11: 0.3788 S12: -0.0826 S13: -0.1659 REMARK 3 S21: 0.2472 S22: -0.0481 S23: -0.1804 REMARK 3 S31: -0.2488 S32: 0.0296 S33: -0.3306 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES RESIDUAL ONLY REMARK 4 REMARK 4 3QDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-11. REMARK 100 THE RCSB ID CODE IS RCSB063511. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-AUG-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : SI111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21235 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.14700 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.30 REMARK 200 R MERGE FOR SHELL (I) : 0.85600 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: NULL REMARK 200 STARTING MODEL: PDB ENTRY 2GJ6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 24%, TRIS 0.1, PH 8.5, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 297K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.00600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.55150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.87250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.55150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.00600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.87250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 38470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ASP A 29 -116.20 52.93 REMARK 500 ARG A 48 11.42 -145.38 REMARK 500 TYR A 123 -70.14 -113.69 REMARK 500 THR A 178 -42.40 -140.08 REMARK 500 ASP A 220 19.68 58.68 REMARK 500 ASP A 227 22.84 -141.11 REMARK 500 ARG A 273 -155.76 -145.32 REMARK 500 ASN B 21 -156.17 -154.14 REMARK 500 PRO B 32 -161.83 -76.21 REMARK 500 LYS B 48 62.06 -115.22 REMARK 500 THR B 73 -160.23 -127.19 REMARK 500 ASP B 98 35.61 -91.52 REMARK 500 SER D 56 160.22 81.82 REMARK 500 ALA D 77 72.07 42.14 REMARK 500 ASN D 94 -15.68 -149.94 REMARK 500 SER D 125 -64.23 67.86 REMARK 500 ASP D 127 30.01 -94.16 REMARK 500 LYS D 146 53.25 -155.19 REMARK 500 ASP D 147 -171.96 55.49 REMARK 500 ASN D 175 -76.03 -63.73 REMARK 500 LYS D 176 70.26 -150.47 REMARK 500 SER D 177 -163.80 -113.06 REMARK 500 ASN D 183 48.92 -88.30 REMARK 500 ALA D 184 -51.87 -130.51 REMARK 500 PRO D 191 -117.00 -70.42 REMARK 500 ASP D 193 -169.64 -112.97 REMARK 500 ASN E 28 -120.38 148.90 REMARK 500 SER E 80 87.77 -151.09 REMARK 500 SER E 87 -178.30 -170.16 REMARK 500 ALA E 242 34.03 -75.54 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 GLN A 226 ASP A 227 149.77 REMARK 500 THR D 55 SER D 56 149.01 REMARK 500 SER D 56 ASN D 57 142.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 SER D 56 24.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3QDG RELATED DB: PDB REMARK 900 RELATED ID: 3QDJ RELATED DB: PDB REMARK 900 RELATED ID: 3QEQ RELATED DB: PDB REMARK 900 RELATED ID: 3QEU RELATED DB: PDB DBREF 3QDM A 1 275 UNP P01892 1A02_HUMAN 25 299 DBREF 3QDM B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 3QDM C 1 10 PDB 3QDM 3QDM 1 10 DBREF 3QDM D 2 196 PDB 3QDM 3QDM 2 196 DBREF 3QDM E 2 243 PDB 3QDM 3QDM 2 243 SEQADV 3QDM MET B 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR SEQRES 12 A 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG SEQRES 22 A 275 TRP GLU SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 C 10 GLU LEU ALA GLY ILE GLY ILE LEU THR VAL SEQRES 1 D 195 GLN LEU ASN GLN SER PRO GLN SER MET PHE ILE GLN GLU SEQRES 2 D 195 GLY GLU ASP VAL SER MET ASN CYS THR SER SER SER ILE SEQRES 3 D 195 PHE ASN THR TRP LEU TRP TYR LYS GLN ASP PRO GLY GLU SEQRES 4 D 195 GLY PRO VAL LEU LEU ILE ALA LEU TYR LYS ALA GLY GLU SEQRES 5 D 195 LEU THR SER ASN GLY ARG LEU THR ALA GLN PHE GLY ILE SEQRES 6 D 195 THR ARG LYS ASP SER PHE LEU ASN ILE SER ALA SER ILE SEQRES 7 D 195 PRO SER ASP VAL GLY ILE TYR PHE CYS ALA GLY GLY THR SEQRES 8 D 195 GLY ASN GLN PHE TYR PHE GLY THR GLY THR SER LEU THR SEQRES 9 D 195 VAL ILE PRO ASN ILE GLN ASN PRO ASP PRO ALA VAL TYR SEQRES 10 D 195 GLN LEU ARG ASP SER LYS SER SER ASP LYS SER VAL CYS SEQRES 11 D 195 LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL SER GLN SEQRES 12 D 195 SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS CYS VAL SEQRES 13 D 195 LEU ASP MET ARG SER MET ASP PHE LYS SER ASN SER ALA SEQRES 14 D 195 VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS ALA ASN SEQRES 15 D 195 ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR PHE PHE SEQRES 1 E 242 ALA GLY ILE THR GLN SER PRO ARG HIS LYS VAL THR GLU SEQRES 2 E 242 THR GLY THR PRO VAL THR LEU ARG CYS HIS GLN THR GLU SEQRES 3 E 242 ASN HIS ARG TYR MET TYR TRP TYR ARG GLN ASP PRO GLY SEQRES 4 E 242 HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY VAL LYS SEQRES 5 E 242 ASP THR ASP LYS GLY GLU VAL SER ASP GLY TYR SER VAL SEQRES 6 E 242 SER ARG SER LYS THR GLU ASP PHE LEU LEU THR LEU GLU SEQRES 7 E 242 SER ALA THR SER SER GLN THR SER VAL TYR PHE CYS ALA SEQRES 8 E 242 ILE SER GLU VAL GLY VAL GLY GLN PRO GLN HIS PHE GLY SEQRES 9 E 242 ASP GLY THR ARG LEU SER ILE LEU GLU ASP LEU ASN LYS SEQRES 10 E 242 VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU SEQRES 11 E 242 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS SEQRES 12 E 242 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER SEQRES 13 E 242 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS SEQRES 14 E 242 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN SEQRES 15 E 242 ASP SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL SER SEQRES 16 E 242 ALA THR PHE TRP GLN ASP PRO ARG ASN HIS PHE ARG CYS SEQRES 17 E 242 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP SEQRES 18 E 242 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER SEQRES 19 E 242 ALA GLU ALA TRP GLY ARG ALA ASP FORMUL 6 HOH *33(H2 O) HELIX 1 1 ALA A 49 GLU A 53 5 5 HELIX 2 2 GLY A 56 TYR A 85 1 30 HELIX 3 3 ALA A 139 ALA A 150 1 12 HELIX 4 4 HIS A 151 GLU A 161 1 11 HELIX 5 5 GLY A 162 GLY A 175 1 14 HELIX 6 6 GLY A 175 GLN A 180 1 6 HELIX 7 7 GLN A 253 GLN A 255 5 3 HELIX 8 8 ILE D 79 VAL D 83 5 5 HELIX 9 9 ARG D 161 ASP D 164 5 4 HELIX 10 10 THR E 82 THR E 86 5 5 HELIX 11 11 ASP E 115 VAL E 119 5 5 HELIX 12 12 SER E 130 GLN E 138 1 9 HELIX 13 13 ALA E 197 GLN E 201 1 5 SHEET 1 A 8 GLU A 46 PRO A 47 0 SHEET 2 A 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 A 8 ARG A 21 VAL A 28 -1 N ALA A 24 O PHE A 36 SHEET 4 A 8 HIS A 3 VAL A 12 -1 N VAL A 12 O ARG A 21 SHEET 5 A 8 THR A 94 VAL A 103 -1 O TYR A 99 N TYR A 7 SHEET 6 A 8 PHE A 109 TYR A 118 -1 O GLN A 115 N MET A 98 SHEET 7 A 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114 SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125 SHEET 1 B 4 LYS A 186 ALA A 193 0 SHEET 2 B 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192 SHEET 3 B 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 B 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 C 4 LYS A 186 ALA A 193 0 SHEET 2 C 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192 SHEET 3 C 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203 SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 D 4 GLU A 222 ASP A 223 0 SHEET 2 D 4 ILE A 213 ARG A 219 -1 N ARG A 219 O GLU A 222 SHEET 3 D 4 TYR A 257 HIS A 263 -1 O THR A 258 N GLN A 218 SHEET 4 D 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259 SHEET 1 E 4 LYS B 6 SER B 11 0 SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 E 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27 SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 F 4 LYS B 6 SER B 11 0 SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 F 4 PHE B 62 PHE B 70 -1 O LEU B 64 N VAL B 27 SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 G 4 GLU B 44 ARG B 45 0 SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ASN B 83 N GLU B 36 SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 H 2 ILE C 7 LEU C 8 0 SHEET 2 H 2 GLY E 97 VAL E 98 -1 O VAL E 98 N ILE C 7 SHEET 1 I 5 ASN D 4 SER D 6 0 SHEET 2 I 5 VAL D 18 THR D 23 -1 O ASN D 21 N SER D 6 SHEET 3 I 5 ASP D 70 ILE D 75 -1 O LEU D 73 N MET D 20 SHEET 4 I 5 LEU D 60 PHE D 64 -1 N THR D 61 O ASN D 74 SHEET 5 I 5 LEU D 54 THR D 55 -1 N LEU D 54 O ALA D 62 SHEET 1 J 5 SER D 9 GLN D 13 0 SHEET 2 J 5 THR D 102 ILE D 107 1 O ILE D 107 N ILE D 12 SHEET 3 J 5 GLY D 84 GLY D 91 -1 N GLY D 84 O LEU D 104 SHEET 4 J 5 THR D 30 GLN D 36 -1 N TYR D 34 O PHE D 87 SHEET 5 J 5 PRO D 42 LEU D 48 -1 O VAL D 43 N LYS D 35 SHEET 1 K 4 SER D 9 GLN D 13 0 SHEET 2 K 4 THR D 102 ILE D 107 1 O ILE D 107 N ILE D 12 SHEET 3 K 4 GLY D 84 GLY D 91 -1 N GLY D 84 O LEU D 104 SHEET 4 K 4 PHE D 96 PHE D 98 -1 O TYR D 97 N GLY D 90 SHEET 1 L 8 VAL D 150 ILE D 152 0 SHEET 2 L 8 PHE D 165 SER D 174 -1 O TRP D 173 N TYR D 151 SHEET 3 L 8 SER D 129 THR D 134 -1 N CYS D 131 O ALA D 172 SHEET 4 L 8 ALA D 116 ASP D 122 -1 N TYR D 118 O LEU D 132 SHEET 5 L 8 GLU E 123 GLU E 128 -1 O GLU E 128 N ARG D 121 SHEET 6 L 8 LYS E 139 PHE E 149 -1 O VAL E 143 N PHE E 127 SHEET 7 L 8 TYR E 187 SER E 196 -1 O LEU E 193 N LEU E 142 SHEET 8 L 8 VAL E 169 THR E 171 -1 N CYS E 170 O ARG E 192 SHEET 1 M 8 CYS D 156 MET D 160 0 SHEET 2 M 8 PHE D 165 SER D 174 -1 O PHE D 165 N MET D 160 SHEET 3 M 8 SER D 129 THR D 134 -1 N CYS D 131 O ALA D 172 SHEET 4 M 8 ALA D 116 ASP D 122 -1 N TYR D 118 O LEU D 132 SHEET 5 M 8 GLU E 123 GLU E 128 -1 O GLU E 128 N ARG D 121 SHEET 6 M 8 LYS E 139 PHE E 149 -1 O VAL E 143 N PHE E 127 SHEET 7 M 8 TYR E 187 SER E 196 -1 O LEU E 193 N LEU E 142 SHEET 8 M 8 LEU E 176 LYS E 177 -1 N LEU E 176 O ALA E 188 SHEET 1 N 4 ILE E 4 SER E 7 0 SHEET 2 N 4 VAL E 19 GLN E 25 -1 O ARG E 22 N SER E 7 SHEET 3 N 4 ASP E 73 LEU E 78 -1 O LEU E 76 N LEU E 21 SHEET 4 N 4 SER E 65 SER E 67 -1 N SER E 65 O THR E 77 SHEET 1 O 6 HIS E 10 GLU E 14 0 SHEET 2 O 6 THR E 108 LEU E 113 1 O SER E 111 N THR E 13 SHEET 3 O 6 SER E 87 GLU E 95 -1 N TYR E 89 O THR E 108 SHEET 4 O 6 ARG E 30 ASP E 38 -1 N TYR E 35 O PHE E 90 SHEET 5 O 6 GLY E 42 GLY E 51 -1 O ILE E 46 N TRP E 34 SHEET 6 O 6 ASP E 54 LYS E 57 -1 O ASP E 56 N TYR E 48 SHEET 1 P 4 HIS E 10 GLU E 14 0 SHEET 2 P 4 THR E 108 LEU E 113 1 O SER E 111 N THR E 13 SHEET 3 P 4 SER E 87 GLU E 95 -1 N TYR E 89 O THR E 108 SHEET 4 P 4 HIS E 103 PHE E 104 -1 O HIS E 103 N ILE E 93 SHEET 1 Q 4 LYS E 163 VAL E 165 0 SHEET 2 Q 4 VAL E 154 VAL E 160 -1 N VAL E 160 O LYS E 163 SHEET 3 Q 4 HIS E 206 PHE E 213 -1 O GLN E 210 N SER E 157 SHEET 4 Q 4 GLN E 232 TRP E 239 -1 O ALA E 238 N PHE E 207 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.06 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04 SSBOND 4 CYS D 22 CYS D 88 1555 1555 1.98 SSBOND 5 CYS D 131 CYS D 181 1555 1555 2.06 SSBOND 6 CYS D 156 CYS E 170 1555 1555 2.07 SSBOND 7 CYS E 23 CYS E 91 1555 1555 2.03 SSBOND 8 CYS E 144 CYS E 209 1555 1555 2.04 CISPEP 1 TYR A 209 PRO A 210 0 -2.70 CISPEP 2 HIS B 31 PRO B 32 0 -4.55 CISPEP 3 SER D 6 PRO D 7 0 14.35 CISPEP 4 SER E 7 PRO E 8 0 -5.52 CISPEP 5 TYR E 150 PRO E 151 0 -6.31 CRYST1 56.012 69.745 227.103 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017853 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014338 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004403 0.00000 ATOM 1 N GLY A 1 21.179 22.308 131.074 1.00 59.31 N ANISOU 1 N GLY A 1 8614 8427 5495 1651 1996 41 N ATOM 2 CA GLY A 1 20.054 22.651 131.996 1.00 56.56 C ANISOU 2 CA GLY A 1 8279 7959 5253 1583 1734 122 C ATOM 3 C GLY A 1 20.453 22.857 133.450 1.00 53.79 C ANISOU 3 C GLY A 1 7764 7348 5323 1412 1681 130 C ATOM 4 O GLY A 1 21.350 22.193 133.974 1.00 53.49 O ANISOU 4 O GLY A 1 7578 7223 5521 1351 1693 -27 O ATOM 5 N SER A 2 19.772 23.794 134.099 1.00 51.67 N ANISOU 5 N SER A 2 7522 6971 5138 1350 1620 312 N ATOM 6 CA SER A 2 19.897 24.023 135.527 1.00 47.97 C ANISOU 6 CA SER A 2 6922 6289 5015 1192 1526 304 C ATOM 7 C SER A 2 19.130 22.919 136.274 1.00 44.81 C ANISOU 7 C SER A 2 6485 5867 4673 1168 1202 114 C ATOM 8 O SER A 2 18.224 22.330 135.700 1.00 45.43 O ANISOU 8 O SER A 2 6657 6075 4528 1257 1050 37 O ATOM 9 CB SER A 2 19.326 25.401 135.833 1.00 48.13 C ANISOU 9 CB SER A 2 7010 6208 5069 1157 1590 545 C ATOM 10 OG SER A 2 19.191 25.606 137.217 1.00 47.31 O ANISOU 10 OG SER A 2 6802 5929 5243 1014 1463 511 O ATOM 11 N HIS A 3 19.491 22.613 137.525 1.00 41.39 N ANISOU 11 N HIS A 3 5914 5284 4527 1046 1099 35 N ATOM 12 CA HIS A 3 18.766 21.578 138.293 1.00 38.74 C ANISOU 12 CA HIS A 3 5557 4906 4258 1015 818 -108 C ATOM 13 C HIS A 3 18.321 22.012 139.693 1.00 36.85 C ANISOU 13 C HIS A 3 5254 4536 4211 890 689 -47 C ATOM 14 O HIS A 3 18.755 23.047 140.194 1.00 37.12 O ANISOU 14 O HIS A 3 5238 4493 4373 812 809 63 O ATOM 15 CB HIS A 3 19.572 20.290 138.393 1.00 38.54 C ANISOU 15 CB HIS A 3 5445 4849 4348 1036 778 -303 C ATOM 16 CG HIS A 3 19.975 19.725 137.066 1.00 40.92 C ANISOU 16 CG HIS A 3 5807 5279 4460 1164 900 -415 C ATOM 17 ND1 HIS A 3 19.201 18.818 136.376 1.00 41.09 N ANISOU 17 ND1 HIS A 3 5936 5386 4291 1238 771 -569 N ATOM 18 CD2 HIS A 3 21.069 19.950 136.297 1.00 42.53 C ANISOU 18 CD2 HIS A 3 5976 5554 4629 1223 1150 -410 C ATOM 19 CE1 HIS A 3 19.804 18.503 135.243 1.00 43.46 C ANISOU 19 CE1 HIS A 3 6275 5809 4429 1348 931 -667 C ATOM 20 NE2 HIS A 3 20.937 19.179 135.169 1.00 44.09 N ANISOU 20 NE2 HIS A 3 6271 5885 4596 1346 1170 -561 N ATOM 21 N SER A 4 17.456 21.221 140.328 1.00 35.07 N ANISOU 21 N SER A 4 5033 4284 4008 859 459 -130 N ATOM 22 CA SER A 4 16.869 21.619 141.610 1.00 32.94 C ANISOU 22 CA SER A 4 4720 3925 3869 751 341 -72 C ATOM 23 C SER A 4 16.442 20.441 142.489 1.00 31.85 C ANISOU 23 C SER A 4 4547 3731 3825 698 128 -178 C ATOM 24 O SER A 4 15.935 19.446 141.987 1.00 32.80 O ANISOU 24 O SER A 4 4718 3881 3863 740 29 -285 O ATOM 25 CB SER A 4 15.650 22.499 141.371 1.00 32.61 C ANISOU 25 CB SER A 4 4766 3936 3686 780 323 46 C ATOM 26 OG SER A 4 14.505 21.702 141.155 1.00 32.79 O ANISOU 26 OG SER A 4 4831 4039 3589 810 138 -32 O ATOM 27 N MET A 5 16.639 20.559 143.799 1.00 30.20 N ANISOU 27 N MET A 5 4256 3438 3781 600 66 -151 N ATOM 28 CA MET A 5 16.069 19.599 144.738 1.00 29.98 C ANISOU 28 CA MET A 5 4214 3353 3822 544 -119 -195 C ATOM 29 C MET A 5 15.105 20.330 145.683 1.00 28.48 C ANISOU 29 C MET A 5 4025 3164 3632 456 -181 -113 C ATOM 30 O MET A 5 15.491 21.312 146.300 1.00 28.33 O ANISOU 30 O MET A 5 3958 3128 3676 403 -110 -56 O ATOM 31 CB MET A 5 17.177 18.870 145.523 1.00 31.09 C ANISOU 31 CB MET A 5 4259 3422 4132 535 -154 -231 C ATOM 32 CG MET A 5 16.662 17.931 146.602 1.00 31.78 C ANISOU 32 CG MET A 5 4347 3436 4291 483 -325 -227 C ATOM 33 SD MET A 5 17.864 16.791 147.347 1.00 34.91 S ANISOU 33 SD MET A 5 4656 3746 4862 538 -391 -244 S ATOM 34 CE MET A 5 18.501 17.711 148.733 1.00 33.49 C ANISOU 34 CE MET A 5 4346 3635 4745 458 -415 -160 C ATOM 35 N ARG A 6 13.849 19.890 145.776 1.00 27.56 N ANISOU 35 N ARG A 6 3951 3069 3451 433 -299 -126 N ATOM 36 CA ARG A 6 12.891 20.545 146.680 1.00 26.68 C ANISOU 36 CA ARG A 6 3825 2971 3340 360 -343 -58 C ATOM 37 C ARG A 6 12.131 19.582 147.564 1.00 25.04 C ANISOU 37 C ARG A 6 3604 2735 3176 276 -483 -80 C ATOM 38 O ARG A 6 11.909 18.449 147.193 1.00 25.55 O ANISOU 38 O ARG A 6 3692 2769 3245 276 -557 -151 O ATOM 39 CB ARG A 6 11.896 21.401 145.902 1.00 28.41 C ANISOU 39 CB ARG A 6 4088 3281 3427 424 -306 -10 C ATOM 40 CG ARG A 6 12.493 22.698 145.396 1.00 31.42 C ANISOU 40 CG ARG A 6 4495 3654 3789 487 -134 76 C ATOM 41 CD ARG A 6 11.576 23.433 144.450 1.00 34.58 C ANISOU 41 CD ARG A 6 4955 4146 4038 600 -100 156 C ATOM 42 NE ARG A 6 12.321 24.007 143.330 1.00 37.87 N ANISOU 42 NE ARG A 6 5436 4579 4375 699 60 223 N ATOM 43 CZ ARG A 6 11.811 24.194 142.111 1.00 40.51 C ANISOU 43 CZ ARG A 6 5841 5039 4510 836 76 279 C ATOM 44 NH1 ARG A 6 10.549 23.856 141.847 1.00 41.32 N ANISOU 44 NH1 ARG A 6 5938 5274 4488 887 -79 253 N ATOM 45 NH2 ARG A 6 12.566 24.706 141.147 1.00 42.38 N ANISOU 45 NH2 ARG A 6 6146 5292 4664 921 247 361 N ATOM 46 N TYR A 7 11.737 20.034 148.744 1.00 23.57 N ANISOU 46 N TYR A 7 3382 2549 3023 197 -502 -24 N ATOM 47 CA TYR A 7 10.832 19.246 149.585 1.00 23.32 C ANISOU 47 CA TYR A 7 3341 2508 3011 108 -604 -17 C ATOM 48 C TYR A 7 9.573 20.028 149.914 1.00 22.62 C ANISOU 48 C TYR A 7 3228 2502 2866 75 -595 15 C ATOM 49 O TYR A 7 9.642 21.217 150.157 1.00 22.82 O ANISOU 49 O TYR A 7 3241 2552 2878 98 -515 49 O ATOM 50 CB TYR A 7 11.516 18.844 150.883 1.00 23.61 C ANISOU 50 CB TYR A 7 3354 2494 3122 49 -640 29 C ATOM 51 CG TYR A 7 12.547 17.770 150.717 1.00 24.46 C ANISOU 51 CG TYR A 7 3472 2512 3310 95 -677 11 C ATOM 52 CD1 TYR A 7 13.865 18.089 150.455 1.00 24.56 C ANISOU 52 CD1 TYR A 7 3444 2522 3364 164 -624 -9 C ATOM 53 CD2 TYR A 7 12.201 16.436 150.817 1.00 25.00 C ANISOU 53 CD2 TYR A 7 3582 2484 3434 71 -750 10 C ATOM 54 CE1 TYR A 7 14.809 17.113 150.310 1.00 25.71 C ANISOU 54 CE1 TYR A 7 3580 2595 3596 233 -653 -28 C ATOM 55 CE2 TYR A 7 13.137 15.456 150.674 1.00 25.89 C ANISOU 55 CE2 TYR A 7 3710 2486 3641 139 -773 -4 C ATOM 56 CZ TYR A 7 14.441 15.804 150.418 1.00 26.08 C ANISOU 56 CZ TYR A 7 3683 2532 3696 233 -728 -23 C ATOM 57 OH TYR A 7 15.393 14.843 150.268 1.00 27.24 O ANISOU 57 OH TYR A 7 3824 2578 3947 328 -745 -40 O ATOM 58 N PHE A 8 8.430 19.355 149.941 1.00 22.49 N ANISOU 58 N PHE A 8 3191 2518 2835 19 -668 -6 N ATOM 59 CA PHE A 8 7.143 20.009 150.129 1.00 22.43 C ANISOU 59 CA PHE A 8 3127 2614 2780 6 -663 12 C ATOM 60 C PHE A 8 6.442 19.316 151.297 1.00 22.78 C ANISOU 60 C PHE A 8 3132 2653 2871 -129 -700 35 C ATOM 61 O PHE A 8 6.365 18.096 151.309 1.00 25.06 O ANISOU 61 O PHE A 8 3435 2873 3214 -205 -760 12 O ATOM 62 CB PHE A 8 6.283 19.851 148.858 1.00 22.82 C ANISOU 62 CB PHE A 8 3153 2763 2756 67 -717 -49 C ATOM 63 CG PHE A 8 6.906 20.420 147.596 1.00 23.15 C ANISOU 63 CG PHE A 8 3252 2835 2711 211 -674 -52 C ATOM 64 CD1 PHE A 8 7.828 19.699 146.842 1.00 22.56 C ANISOU 64 CD1 PHE A 8 3238 2705 2628 239 -681 -116 C ATOM 65 CD2 PHE A 8 6.519 21.673 147.126 1.00 23.59 C ANISOU 65 CD2 PHE A 8 3302 2974 2686 332 -612 18 C ATOM 66 CE1 PHE A 8 8.381 20.250 145.708 1.00 22.88 C ANISOU 66 CE1 PHE A 8 3331 2793 2568 368 -615 -107 C ATOM 67 CE2 PHE A 8 7.070 22.218 145.964 1.00 22.98 C ANISOU 67 CE2 PHE A 8 3292 2925 2512 469 -549 52 C ATOM 68 CZ PHE A 8 7.996 21.507 145.266 1.00 23.39 C ANISOU 68 CZ PHE A 8 3402 2944 2540 478 -547 -11 C ATOM 69 N PHE A 9 5.906 20.064 152.257 1.00 22.43 N ANISOU 69 N PHE A 9 3044 2669 2809 -161 -647 78 N ATOM 70 CA PHE A 9 5.311 19.459 153.477 1.00 23.66 C ANISOU 70 CA PHE A 9 3169 2838 2983 -291 -652 121 C ATOM 71 C PHE A 9 3.925 20.007 153.719 1.00 23.56 C ANISOU 71 C PHE A 9 3056 2952 2945 -311 -613 112 C ATOM 72 O PHE A 9 3.735 21.201 153.651 1.00 24.90 O ANISOU 72 O PHE A 9 3201 3180 3082 -218 -551 104 O ATOM 73 CB PHE A 9 6.155 19.748 154.736 1.00 24.70 C ANISOU 73 CB PHE A 9 3341 2952 3092 -320 -615 176 C ATOM 74 CG PHE A 9 7.608 19.333 154.616 1.00 25.74 C ANISOU 74 CG PHE A 9 3535 2988 3256 -281 -655 187 C ATOM 75 CD1 PHE A 9 8.541 20.169 153.983 1.00 25.53 C ANISOU 75 CD1 PHE A 9 3519 2944 3236 -190 -620 143 C ATOM 76 CD2 PHE A 9 8.043 18.123 155.140 1.00 26.02 C ANISOU 76 CD2 PHE A 9 3611 2948 3327 -328 -714 253 C ATOM 77 CE1 PHE A 9 9.854 19.793 153.854 1.00 26.13 C ANISOU 77 CE1 PHE A 9 3616 2956 3355 -153 -648 142 C ATOM 78 CE2 PHE A 9 9.377 17.739 155.023 1.00 26.59 C ANISOU 78 CE2 PHE A 9 3716 2946 3440 -263 -755 264 C ATOM 79 CZ PHE A 9 10.290 18.577 154.387 1.00 26.36 C ANISOU 79 CZ PHE A 9 3669 2929 3419 -179 -724 198 C ATOM 80 N THR A 10 2.954 19.162 154.031 1.00 23.47 N ANISOU 80 N THR A 10 2978 2974 2967 -430 -633 114 N ATOM 81 CA THR A 10 1.599 19.649 154.201 1.00 23.19 C ANISOU 81 CA THR A 10 2807 3084 2920 -444 -593 94 C ATOM 82 C THR A 10 1.028 19.124 155.495 1.00 23.99 C ANISOU 82 C THR A 10 2871 3212 3032 -597 -529 152 C ATOM 83 O THR A 10 0.930 17.913 155.670 1.00 24.84 O ANISOU 83 O THR A 10 2996 3243 3201 -732 -555 182 O ATOM 84 CB THR A 10 0.701 19.170 153.060 1.00 24.21 C ANISOU 84 CB THR A 10 2832 3288 3080 -450 -680 11 C ATOM 85 OG1 THR A 10 1.242 19.610 151.815 1.00 23.10 O ANISOU 85 OG1 THR A 10 2742 3146 2890 -297 -736 -29 O ATOM 86 CG2 THR A 10 -0.703 19.718 153.221 1.00 25.15 C ANISOU 86 CG2 THR A 10 2771 3588 3196 -443 -647 -12 C ATOM 87 N SER A 11 0.666 20.016 156.408 1.00 23.55 N ANISOU 87 N SER A 11 2777 3254 2919 -576 -428 170 N ATOM 88 CA SER A 11 0.021 19.571 157.635 1.00 25.86 C ANISOU 88 CA SER A 11 3028 3610 3190 -716 -342 230 C ATOM 89 C SER A 11 -1.411 20.042 157.748 1.00 26.78 C ANISOU 89 C SER A 11 2961 3892 3321 -724 -264 184 C ATOM 90 O SER A 11 -1.683 21.214 157.552 1.00 27.80 O ANISOU 90 O SER A 11 3036 4098 3429 -581 -224 128 O ATOM 91 CB SER A 11 0.803 19.982 158.877 1.00 26.28 C ANISOU 91 CB SER A 11 3184 3668 3131 -715 -276 283 C ATOM 92 OG SER A 11 1.473 18.855 159.404 1.00 27.73 O ANISOU 92 OG SER A 11 3473 3759 3303 -810 -315 392 O ATOM 93 N VAL A 12 -2.338 19.143 158.042 1.00 26.60 N ANISOU 93 N VAL A 12 2834 3918 3356 -887 -231 208 N ATOM 94 CA VAL A 12 -3.725 19.560 158.119 1.00 28.57 C ANISOU 94 CA VAL A 12 2867 4351 3636 -894 -155 153 C ATOM 95 C VAL A 12 -4.351 19.092 159.424 1.00 31.19 C ANISOU 95 C VAL A 12 3151 4756 3944 -1064 -1 229 C ATOM 96 O VAL A 12 -4.459 17.895 159.656 1.00 31.68 O ANISOU 96 O VAL A 12 3232 4739 4066 -1251 8 301 O ATOM 97 CB VAL A 12 -4.590 19.041 156.902 1.00 28.91 C ANISOU 97 CB VAL A 12 2736 4454 3795 -929 -266 62 C ATOM 98 CG1 VAL A 12 -6.047 19.419 157.068 1.00 29.67 C ANISOU 98 CG1 VAL A 12 2566 4772 3934 -941 -191 6 C ATOM 99 CG2 VAL A 12 -4.080 19.569 155.575 1.00 27.17 C ANISOU 99 CG2 VAL A 12 2559 4211 3555 -740 -406 -3 C ATOM 100 N SER A 13 -4.775 20.033 160.263 1.00 33.71 N ANISOU 100 N SER A 13 3412 5216 4178 -998 136 212 N ATOM 101 CA SER A 13 -5.442 19.688 161.514 1.00 38.39 C ANISOU 101 CA SER A 13 3950 5921 4717 -1146 311 280 C ATOM 102 C SER A 13 -6.852 19.169 161.258 1.00 42.40 C ANISOU 102 C SER A 13 4199 6551 5359 -1277 366 248 C ATOM 103 O SER A 13 -7.626 19.809 160.568 1.00 43.46 O ANISOU 103 O SER A 13 4137 6809 5566 -1166 337 136 O ATOM 104 CB SER A 13 -5.488 20.890 162.457 1.00 38.53 C ANISOU 104 CB SER A 13 3978 6067 4595 -1028 452 232 C ATOM 105 OG SER A 13 -6.338 21.908 161.969 1.00 39.17 O ANISOU 105 OG SER A 13 3875 6263 4745 -873 488 110 O ATOM 106 N ARG A 14 -7.164 17.988 161.780 1.00 46.00 N ANISOU 106 N ARG A 14 4651 6967 5860 -1512 442 352 N ATOM 107 CA ARG A 14 -8.517 17.449 161.678 1.00 50.72 C ANISOU 107 CA ARG A 14 4982 7685 6603 -1684 526 315 C ATOM 108 C ARG A 14 -9.100 17.271 163.073 1.00 54.28 C ANISOU 108 C ARG A 14 5395 8256 6973 -1826 777 425 C ATOM 109 O ARG A 14 -8.943 16.218 163.697 1.00 55.78 O ANISOU 109 O ARG A 14 5697 8335 7164 -2026 864 583 O ATOM 110 CB ARG A 14 -8.555 16.147 160.860 1.00 51.72 C ANISOU 110 CB ARG A 14 5097 7644 6911 -1875 413 309 C ATOM 111 CG ARG A 14 -7.220 15.430 160.768 1.00 50.77 C ANISOU 111 CG ARG A 14 5275 7249 6764 -1884 313 412 C ATOM 112 CD ARG A 14 -7.223 14.328 159.720 1.00 51.79 C ANISOU 112 CD ARG A 14 5391 7200 7085 -2020 182 340 C ATOM 113 NE ARG A 14 -6.033 13.488 159.843 1.00 51.32 N ANISOU 113 NE ARG A 14 5611 6862 7025 -2043 136 465 N ATOM 114 CZ ARG A 14 -5.805 12.382 159.139 1.00 52.22 C ANISOU 114 CZ ARG A 14 5785 6750 7305 -2164 55 428 C ATOM 115 NH1 ARG A 14 -6.691 11.962 158.240 1.00 53.45 N ANISOU 115 NH1 ARG A 14 5739 6938 7631 -2299 -3 246 N ATOM 116 NH2 ARG A 14 -4.683 11.694 159.338 1.00 51.81 N ANISOU 116 NH2 ARG A 14 5988 6446 7253 -2142 27 557 N ATOM 117 N PRO A 15 -9.796 18.310 163.550 1.00 56.46 N ANISOU 117 N PRO A 15 5516 8759 7180 -1710 910 347 N ATOM 118 CA PRO A 15 -10.250 18.510 164.924 1.00 59.34 C ANISOU 118 CA PRO A 15 5860 9286 7400 -1771 1166 416 C ATOM 119 C PRO A 15 -11.355 17.541 165.311 1.00 63.16 C ANISOU 119 C PRO A 15 6144 9852 8001 -2044 1345 489 C ATOM 120 O PRO A 15 -12.475 17.647 164.811 1.00 64.96 O ANISOU 120 O PRO A 15 6056 10229 8397 -2078 1372 369 O ATOM 121 CB PRO A 15 -10.806 19.941 164.907 1.00 59.43 C ANISOU 121 CB PRO A 15 5705 9493 7381 -1536 1226 248 C ATOM 122 CG PRO A 15 -10.490 20.486 163.526 1.00 57.27 C ANISOU 122 CG PRO A 15 5410 9130 7220 -1340 985 134 C ATOM 123 CD PRO A 15 -10.375 19.310 162.642 1.00 56.37 C ANISOU 123 CD PRO A 15 5292 8874 7250 -1506 823 174 C ATOM 124 N GLY A 16 -11.029 16.597 166.187 1.00 64.90 N ANISOU 124 N GLY A 16 6542 9978 8140 -2235 1467 693 N ATOM 125 CA GLY A 16 -11.995 15.607 166.629 1.00 68.91 C ANISOU 125 CA GLY A 16 6894 10521 8767 -2525 1673 799 C ATOM 126 C GLY A 16 -11.956 14.323 165.828 1.00 69.96 C ANISOU 126 C GLY A 16 7034 10399 9147 -2742 1562 842 C ATOM 127 O GLY A 16 -12.681 13.380 166.119 1.00 73.38 O ANISOU 127 O GLY A 16 7359 10798 9724 -3020 1731 932 O ATOM 128 N ARG A 17 -11.124 14.276 164.799 1.00 67.73 N ANISOU 128 N ARG A 17 6878 9929 8928 -2627 1293 763 N ATOM 129 CA ARG A 17 -10.900 13.023 164.096 1.00 68.61 C ANISOU 129 CA ARG A 17 7054 9762 9252 -2817 1191 793 C ATOM 130 C ARG A 17 -9.445 12.626 164.321 1.00 66.56 C ANISOU 130 C ARG A 17 7172 9248 8871 -2725 1093 961 C ATOM 131 O ARG A 17 -8.862 11.868 163.548 1.00 66.04 O ANISOU 131 O ARG A 17 7223 8925 8946 -2763 941 948 O ATOM 132 CB ARG A 17 -11.253 13.144 162.606 1.00 68.36 C ANISOU 132 CB ARG A 17 6817 9745 9411 -2778 964 536 C ATOM 133 CG ARG A 17 -12.754 13.125 162.300 1.00 71.83 C ANISOU 133 CG ARG A 17 6848 10411 10035 -2937 1041 379 C ATOM 134 CD ARG A 17 -13.102 13.872 160.993 1.00 71.44 C ANISOU 134 CD ARG A 17 6573 10530 10040 -2750 800 124 C ATOM 135 NE ARG A 17 -13.651 15.220 161.221 1.00 71.85 N ANISOU 135 NE ARG A 17 6438 10885 9976 -2510 850 58 N ATOM 136 CZ ARG A 17 -13.102 16.365 160.794 1.00 69.63 C ANISOU 136 CZ ARG A 17 6243 10658 9556 -2181 712 3 C ATOM 137 NH1 ARG A 17 -11.967 16.358 160.090 1.00 67.02 N ANISOU 137 NH1 ARG A 17 6170 10128 9168 -2055 512 5 N ATOM 138 NH2 ARG A 17 -13.694 17.528 161.062 1.00 69.59 N ANISOU 138 NH2 ARG A 17 6063 10895 9484 -1976 792 -55 N ATOM 139 N GLY A 18 -8.865 13.161 165.392 1.00 65.66 N ANISOU 139 N GLY A 18 7234 9226 8489 -2596 1179 1103 N ATOM 140 CA GLY A 18 -7.551 12.736 165.846 1.00 64.35 C ANISOU 140 CA GLY A 18 7397 8871 8182 -2519 1111 1296 C ATOM 141 C GLY A 18 -6.433 13.680 165.478 1.00 60.93 C ANISOU 141 C GLY A 18 7091 8453 7605 -2242 905 1191 C ATOM 142 O GLY A 18 -6.624 14.895 165.433 1.00 60.04 O ANISOU 142 O GLY A 18 6874 8545 7395 -2088 894 1032 O ATOM 143 N GLU A 19 -5.261 13.110 165.209 1.00 59.36 N ANISOU 143 N GLU A 19 7114 8023 7415 -2180 756 1281 N ATOM 144 CA GLU A 19 -4.039 13.885 164.962 1.00 56.39 C ANISOU 144 CA GLU A 19 6874 7646 6906 -1940 576 1212 C ATOM 145 C GLU A 19 -4.005 14.436 163.537 1.00 52.44 C ANISOU 145 C GLU A 19 6263 7111 6551 -1832 404 974 C ATOM 146 O GLU A 19 -4.707 13.918 162.677 1.00 53.03 O ANISOU 146 O GLU A 19 6202 7116 6830 -1944 377 883 O ATOM 147 CB GLU A 19 -2.808 13.004 165.217 1.00 57.64 C ANISOU 147 CB GLU A 19 7283 7587 7030 -1905 489 1408 C ATOM 148 CG GLU A 19 -2.352 12.947 166.663 1.00 59.98 C ANISOU 148 CG GLU A 19 7737 7997 7057 -1879 584 1634 C ATOM 149 CD GLU A 19 -1.598 11.657 166.941 1.00 62.57 C ANISOU 149 CD GLU A 19 8272 8079 7423 -1905 555 1898 C ATOM 150 OE1 GLU A 19 -1.585 10.788 166.041 1.00 62.81 O ANISOU 150 OE1 GLU A 19 8312 7834 7721 -1975 498 1884 O ATOM 151 OE2 GLU A 19 -1.030 11.497 168.049 1.00 64.76 O ANISOU 151 OE2 GLU A 19 8703 8439 7463 -1845 589 2117 O ATOM 152 N PRO A 20 -3.213 15.505 163.296 1.00 48.61 N ANISOU 152 N PRO A 20 5831 6687 5952 -1621 295 869 N ATOM 153 CA PRO A 20 -3.028 16.067 161.946 1.00 45.19 C ANISOU 153 CA PRO A 20 5332 6215 5623 -1492 140 684 C ATOM 154 C PRO A 20 -2.551 15.146 160.813 1.00 43.55 C ANISOU 154 C PRO A 20 5181 5783 5582 -1518 -7 657 C ATOM 155 O PRO A 20 -1.798 14.210 161.029 1.00 44.02 O ANISOU 155 O PRO A 20 5400 5657 5667 -1561 -35 783 O ATOM 156 CB PRO A 20 -2.010 17.197 162.160 1.00 43.00 C ANISOU 156 CB PRO A 20 5161 5989 5188 -1295 87 638 C ATOM 157 CG PRO A 20 -1.823 17.320 163.635 1.00 44.55 C ANISOU 157 CG PRO A 20 5442 6299 5185 -1323 204 753 C ATOM 158 CD PRO A 20 -2.860 16.499 164.325 1.00 47.67 C ANISOU 158 CD PRO A 20 5769 6746 5596 -1512 363 876 C ATOM 159 N ARG A 21 -3.021 15.434 159.608 1.00 42.19 N ANISOU 159 N ARG A 21 4874 5644 5513 -1475 -97 487 N ATOM 160 CA ARG A 21 -2.564 14.761 158.405 1.00 40.74 C ANISOU 160 CA ARG A 21 4736 5290 5451 -1470 -242 406 C ATOM 161 C ARG A 21 -1.212 15.332 158.038 1.00 37.92 C ANISOU 161 C ARG A 21 4534 4867 5005 -1270 -342 399 C ATOM 162 O ARG A 21 -1.056 16.548 157.970 1.00 36.77 O ANISOU 162 O ARG A 21 4363 4847 4760 -1117 -344 347 O ATOM 163 CB ARG A 21 -3.534 15.046 157.266 1.00 41.44 C ANISOU 163 CB ARG A 21 4618 5508 5620 -1464 -315 221 C ATOM 164 CG ARG A 21 -3.190 14.369 155.961 1.00 42.05 C ANISOU 164 CG ARG A 21 4728 5456 5794 -1465 -464 97 C ATOM 165 CD ARG A 21 -3.348 12.878 156.073 1.00 44.91 C ANISOU 165 CD ARG A 21 5129 5609 6324 -1696 -435 117 C ATOM 166 NE ARG A 21 -2.783 12.213 154.906 1.00 46.19 N ANISOU 166 NE ARG A 21 5371 5613 6567 -1677 -567 -17 N ATOM 167 CZ ARG A 21 -3.496 11.715 153.900 1.00 47.93 C ANISOU 167 CZ ARG A 21 5456 5862 6892 -1782 -652 -219 C ATOM 168 NH1 ARG A 21 -4.818 11.780 153.919 1.00 49.81 N ANISOU 168 NH1 ARG A 21 5451 6286 7188 -1921 -626 -303 N ATOM 169 NH2 ARG A 21 -2.879 11.135 152.879 1.00 47.90 N ANISOU 169 NH2 ARG A 21 5550 5718 6933 -1750 -761 -355 N ATOM 170 N PHE A 22 -0.231 14.467 157.799 1.00 36.14 N ANISOU 170 N PHE A 22 4463 4434 4835 -1269 -410 447 N ATOM 171 CA PHE A 22 1.081 14.939 157.386 1.00 32.39 C ANISOU 171 CA PHE A 22 4105 3903 4297 -1090 -497 429 C ATOM 172 C PHE A 22 1.543 14.185 156.137 1.00 32.01 C ANISOU 172 C PHE A 22 4105 3694 4366 -1069 -601 331 C ATOM 173 O PHE A 22 1.592 12.957 156.119 1.00 33.08 O ANISOU 173 O PHE A 22 4301 3643 4625 -1176 -604 363 O ATOM 174 CB PHE A 22 2.068 14.788 158.538 1.00 31.66 C ANISOU 174 CB PHE A 22 4153 3762 4116 -1061 -470 593 C ATOM 175 CG PHE A 22 3.436 15.251 158.220 1.00 30.04 C ANISOU 175 CG PHE A 22 4033 3518 3863 -898 -552 569 C ATOM 176 CD1 PHE A 22 3.735 16.608 158.197 1.00 29.14 C ANISOU 176 CD1 PHE A 22 3885 3538 3648 -787 -546 492 C ATOM 177 CD2 PHE A 22 4.439 14.338 157.940 1.00 30.07 C ANISOU 177 CD2 PHE A 22 4144 3338 3943 -857 -622 618 C ATOM 178 CE1 PHE A 22 5.015 17.048 157.902 1.00 27.32 C ANISOU 178 CE1 PHE A 22 3714 3271 3396 -663 -604 462 C ATOM 179 CE2 PHE A 22 5.703 14.757 157.652 1.00 28.78 C ANISOU 179 CE2 PHE A 22 4027 3159 3748 -713 -686 590 C ATOM 180 CZ PHE A 22 5.996 16.128 157.634 1.00 27.66 C ANISOU 180 CZ PHE A 22 3838 3166 3506 -628 -676 510 C ATOM 181 N ILE A 23 1.849 14.927 155.076 1.00 30.27 N ANISOU 181 N ILE A 23 3860 3536 4104 -928 -672 208 N ATOM 182 CA ILE A 23 2.353 14.338 153.838 1.00 29.86 C ANISOU 182 CA ILE A 23 3857 3370 4117 -883 -762 94 C ATOM 183 C ILE A 23 3.575 15.125 153.446 1.00 27.35 C ANISOU 183 C ILE A 23 3619 3058 3717 -697 -786 93 C ATOM 184 O ILE A 23 3.560 16.336 153.497 1.00 26.93 O ANISOU 184 O ILE A 23 3526 3139 3568 -603 -758 98 O ATOM 185 CB ILE A 23 1.307 14.402 152.686 1.00 31.75 C ANISOU 185 CB ILE A 23 3961 3732 4370 -909 -824 -79 C ATOM 186 CG1 ILE A 23 0.034 13.634 153.055 1.00 34.08 C ANISOU 186 CG1 ILE A 23 4136 4040 4775 -1125 -794 -105 C ATOM 187 CG2 ILE A 23 1.872 13.851 151.347 1.00 31.32 C ANISOU 187 CG2 ILE A 23 3969 3593 4337 -849 -916 -226 C ATOM 188 CD1 ILE A 23 -1.198 14.339 152.599 1.00 35.60 C ANISOU 188 CD1 ILE A 23 4122 4482 4924 -1120 -822 -205 C ATOM 189 N ALA A 24 4.646 14.435 153.094 1.00 26.88 N ANISOU 189 N ALA A 24 3666 2838 3712 -647 -821 88 N ATOM 190 CA ALA A 24 5.893 15.074 152.706 1.00 25.20 C ANISOU 190 CA ALA A 24 3507 2624 3442 -488 -829 83 C ATOM 191 C ALA A 24 6.347 14.447 151.400 1.00 25.83 C ANISOU 191 C ALA A 24 3631 2616 3568 -429 -876 -46 C ATOM 192 O ALA A 24 6.331 13.226 151.258 1.00 26.04 O ANISOU 192 O ALA A 24 3703 2483 3707 -497 -900 -85 O ATOM 193 CB ALA A 24 6.949 14.848 153.773 1.00 24.67 C ANISOU 193 CB ALA A 24 3510 2477 3388 -464 -817 215 C ATOM 194 N VAL A 25 6.728 15.270 150.433 1.00 24.74 N ANISOU 194 N VAL A 25 3486 2574 3342 -303 -875 -115 N ATOM 195 CA VAL A 25 7.194 14.733 149.171 1.00 25.52 C ANISOU 195 CA VAL A 25 3631 2623 3444 -235 -904 -247 C ATOM 196 C VAL A 25 8.496 15.406 148.807 1.00 24.78 C ANISOU 196 C VAL A 25 3575 2537 3302 -88 -852 -223 C ATOM 197 O VAL A 25 8.738 16.556 149.179 1.00 23.92 O ANISOU 197 O VAL A 25 3440 2513 3135 -42 -800 -141 O ATOM 198 CB VAL A 25 6.157 14.930 148.035 1.00 26.41 C ANISOU 198 CB VAL A 25 3684 2890 3462 -233 -955 -382 C ATOM 199 CG1 VAL A 25 5.024 13.977 148.181 1.00 27.91 C ANISOU 199 CG1 VAL A 25 3818 3049 3738 -401 -1012 -464 C ATOM 200 CG2 VAL A 25 5.591 16.299 148.084 1.00 26.34 C ANISOU 200 CG2 VAL A 25 3605 3067 3337 -169 -931 -310 C ATOM 201 N GLY A 26 9.349 14.694 148.088 1.00 25.65 N ANISOU 201 N GLY A 26 3742 2551 3454 -21 -850 -306 N ATOM 202 CA GLY A 26 10.599 15.280 147.643 1.00 25.49 C ANISOU 202 CA GLY A 26 3735 2550 3399 110 -781 -296 C ATOM 203 C GLY A 26 10.773 15.075 146.160 1.00 27.49 C ANISOU 203 C GLY A 26 4026 2847 3570 197 -763 -440 C ATOM 204 O GLY A 26 10.402 14.028 145.616 1.00 28.55 O ANISOU 204 O GLY A 26 4195 2918 3735 165 -814 -579 O ATOM 205 N TYR A 27 11.378 16.075 145.523 1.00 28.21 N ANISOU 205 N TYR A 27 4116 3043 3558 302 -677 -413 N ATOM 206 CA TYR A 27 11.556 16.123 144.078 1.00 30.17 C ANISOU 206 CA TYR A 27 4407 3388 3669 404 -635 -520 C ATOM 207 C TYR A 27 12.984 16.444 143.702 1.00 30.26 C ANISOU 207 C TYR A 27 4425 3382 3692 508 -505 -500 C ATOM 208 O TYR A 27 13.616 17.315 144.309 1.00 29.22 O ANISOU 208 O TYR A 27 4248 3244 3610 508 -430 -379 O ATOM 209 CB TYR A 27 10.693 17.234 143.497 1.00 30.94 C ANISOU 209 CB TYR A 27 4498 3672 3586 445 -628 -465 C ATOM 210 CG TYR A 27 9.233 16.890 143.382 1.00 32.89 C ANISOU 210 CG TYR A 27 4711 4009 3775 376 -759 -536 C ATOM 211 CD1 TYR A 27 8.374 17.045 144.460 1.00 33.16 C ANISOU 211 CD1 TYR A 27 4680 4026 3895 270 -812 -461 C ATOM 212 CD2 TYR A 27 8.714 16.402 142.208 1.00 34.56 C ANISOU 212 CD2 TYR A 27 4941 4345 3844 411 -826 -693 C ATOM 213 CE1 TYR A 27 7.038 16.740 144.366 1.00 33.99 C ANISOU 213 CE1 TYR A 27 4719 4228 3966 196 -919 -532 C ATOM 214 CE2 TYR A 27 7.399 16.084 142.107 1.00 36.18 C ANISOU 214 CE2 TYR A 27 5081 4656 4010 333 -956 -781 C ATOM 215 CZ TYR A 27 6.560 16.257 143.183 1.00 35.70 C ANISOU 215 CZ TYR A 27 4936 4570 4059 223 -998 -695 C ATOM 216 OH TYR A 27 5.227 15.940 143.070 1.00 38.14 O ANISOU 216 OH TYR A 27 5145 5002 4344 136 -1119 -791 O ATOM 217 N VAL A 28 13.501 15.749 142.699 1.00 31.05 N ANISOU 217 N VAL A 28 4568 3480 3751 587 -468 -639 N ATOM 218 CA VAL A 28 14.626 16.296 141.968 1.00 31.26 C ANISOU 218 CA VAL A 28 4594 3566 3718 698 -312 -625 C ATOM 219 C VAL A 28 14.068 16.635 140.608 1.00 32.92 C ANISOU 219 C VAL A 28 4874 3959 3676 773 -284 -684 C ATOM 220 O VAL A 28 13.555 15.757 139.912 1.00 34.83 O ANISOU 220 O VAL A 28 5163 4237 3833 781 -361 -860 O ATOM 221 CB VAL A 28 15.787 15.344 141.827 1.00 32.32 C ANISOU 221 CB VAL A 28 4714 3590 3978 765 -257 -731 C ATOM 222 CG1 VAL A 28 16.855 15.982 140.966 1.00 33.16 C ANISOU 222 CG1 VAL A 28 4802 3794 4003 870 -71 -721 C ATOM 223 CG2 VAL A 28 16.359 15.016 143.191 1.00 31.85 C ANISOU 223 CG2 VAL A 28 4578 3380 4145 720 -305 -646 C ATOM 224 N ASP A 29 14.147 17.920 140.275 1.00 32.38 N ANISOU 224 N ASP A 29 4812 4002 3488 823 -175 -535 N ATOM 225 CA ASP A 29 13.519 18.513 139.116 1.00 33.17 C ANISOU 225 CA ASP A 29 4982 4302 3320 916 -151 -511 C ATOM 226 C ASP A 29 12.027 18.231 139.008 1.00 33.15 C ANISOU 226 C ASP A 29 4983 4405 3210 884 -340 -575 C ATOM 227 O ASP A 29 11.241 18.631 139.867 1.00 32.39 O ANISOU 227 O ASP A 29 4834 4279 3195 812 -421 -484 O ATOM 228 CB ASP A 29 14.309 18.192 137.857 1.00 35.91 C ANISOU 228 CB ASP A 29 5390 4745 3510 1030 -26 -613 C ATOM 229 CG ASP A 29 15.668 18.839 137.880 1.00 36.09 C ANISOU 229 CG ASP A 29 5382 4712 3618 1064 196 -502 C ATOM 230 OD1 ASP A 29 16.618 18.308 137.264 1.00 36.77 O ANISOU 230 OD1 ASP A 29 5471 4809 3692 1128 312 -611 O ATOM 231 OD2 ASP A 29 15.768 19.899 138.545 1.00 35.51 O ANISOU 231 OD2 ASP A 29 5272 4580 3640 1017 261 -318 O ATOM 232 N ASP A 30 11.616 17.529 137.979 1.00 34.41 N ANISOU 232 N ASP A 30 5185 4702 3188 929 -413 -754 N ATOM 233 CA ASP A 30 10.212 17.230 137.893 1.00 34.89 C ANISOU 233 CA ASP A 30 5210 4881 3164 878 -604 -841 C ATOM 234 C ASP A 30 9.940 15.749 138.186 1.00 35.67 C ANISOU 234 C ASP A 30 5286 4849 3417 744 -727 -1086 C ATOM 235 O ASP A 30 8.906 15.213 137.837 1.00 37.96 O ANISOU 235 O ASP A 30 5545 5247 3631 684 -877 -1246 O ATOM 236 CB ASP A 30 9.671 17.714 136.554 1.00 36.42 C ANISOU 236 CB ASP A 30 5450 5375 3014 1021 -630 -850 C ATOM 237 CG ASP A 30 9.790 19.236 136.401 1.00 35.93 C ANISOU 237 CG ASP A 30 5420 5393 2838 1152 -500 -556 C ATOM 238 OD1 ASP A 30 9.601 19.937 137.417 1.00 33.99 O ANISOU 238 OD1 ASP A 30 5125 5021 2770 1101 -480 -389 O ATOM 239 OD2 ASP A 30 10.060 19.737 135.277 1.00 37.23 O ANISOU 239 OD2 ASP A 30 5670 5740 2737 1306 -407 -491 O ATOM 240 N THR A 31 10.878 15.105 138.861 1.00 35.15 N ANISOU 240 N THR A 31 5229 4542 3584 697 -659 -1107 N ATOM 241 CA THR A 31 10.752 13.700 139.202 1.00 36.52 C ANISOU 241 CA THR A 31 5406 4527 3944 585 -740 -1301 C ATOM 242 C THR A 31 10.701 13.552 140.713 1.00 34.72 C ANISOU 242 C THR A 31 5127 4088 3979 468 -765 -1157 C ATOM 243 O THR A 31 11.617 13.973 141.413 1.00 34.39 O ANISOU 243 O THR A 31 5071 3950 4045 505 -675 -999 O ATOM 244 CB THR A 31 11.934 12.883 138.625 1.00 38.25 C ANISOU 244 CB THR A 31 5692 4634 4208 670 -634 -1459 C ATOM 245 OG1 THR A 31 11.919 12.984 137.195 1.00 40.61 O ANISOU 245 OG1 THR A 31 6047 5161 4222 776 -605 -1611 O ATOM 246 CG2 THR A 31 11.840 11.409 139.021 1.00 39.05 C ANISOU 246 CG2 THR A 31 5814 4478 4544 568 -698 -1645 C ATOM 247 N GLN A 32 9.612 12.979 141.207 1.00 34.54 N ANISOU 247 N GLN A 32 5065 4015 4044 321 -887 -1215 N ATOM 248 CA GLN A 32 9.419 12.749 142.626 1.00 32.71 C ANISOU 248 CA GLN A 32 4795 3604 4028 201 -907 -1077 C ATOM 249 C GLN A 32 10.221 11.526 143.054 1.00 33.22 C ANISOU 249 C GLN A 32 4919 3388 4317 183 -876 -1133 C ATOM 250 O GLN A 32 10.196 10.503 142.394 1.00 34.84 O ANISOU 250 O GLN A 32 5175 3495 4566 166 -893 -1347 O ATOM 251 CB GLN A 32 7.937 12.504 142.888 1.00 33.77 C ANISOU 251 CB GLN A 32 4859 3796 4177 43 -1023 -1130 C ATOM 252 CG GLN A 32 7.504 12.595 144.327 1.00 33.32 C ANISOU 252 CG GLN A 32 4750 3639 4272 -76 -1027 -952 C ATOM 253 CD GLN A 32 6.317 11.710 144.601 1.00 35.11 C ANISOU 253 CD GLN A 32 4923 3807 4609 -270 -1106 -1057 C ATOM 254 OE1 GLN A 32 5.615 11.316 143.684 1.00 37.79 O ANISOU 254 OE1 GLN A 32 5228 4248 4883 -319 -1184 -1267 O ATOM 255 NE2 GLN A 32 6.098 11.370 145.861 1.00 35.40 N ANISOU 255 NE2 GLN A 32 4948 3691 4812 -389 -1083 -919 N ATOM 256 N PHE A 33 10.937 11.614 144.164 1.00 32.19 N ANISOU 256 N PHE A 33 4779 3124 4326 198 -833 -947 N ATOM 257 CA PHE A 33 11.754 10.475 144.561 1.00 32.98 C ANISOU 257 CA PHE A 33 4932 2964 4635 226 -807 -967 C ATOM 258 C PHE A 33 11.379 9.879 145.912 1.00 32.83 C ANISOU 258 C PHE A 33 4917 2760 4796 110 -847 -819 C ATOM 259 O PHE A 33 11.561 8.683 146.152 1.00 34.44 O ANISOU 259 O PHE A 33 5186 2711 5188 93 -844 -855 O ATOM 260 CB PHE A 33 13.255 10.759 144.428 1.00 32.54 C ANISOU 260 CB PHE A 33 4865 2905 4593 400 -713 -918 C ATOM 261 CG PHE A 33 13.797 11.791 145.395 1.00 31.39 C ANISOU 261 CG PHE A 33 4644 2844 4439 422 -691 -695 C ATOM 262 CD1 PHE A 33 13.560 13.148 145.223 1.00 29.91 C ANISOU 262 CD1 PHE A 33 4410 2865 4088 417 -661 -624 C ATOM 263 CD2 PHE A 33 14.613 11.405 146.448 1.00 31.40 C ANISOU 263 CD2 PHE A 33 4619 2715 4597 462 -699 -564 C ATOM 264 CE1 PHE A 33 14.087 14.072 146.111 1.00 28.08 C ANISOU 264 CE1 PHE A 33 4111 2687 3870 418 -633 -462 C ATOM 265 CE2 PHE A 33 15.136 12.339 147.321 1.00 29.21 C ANISOU 265 CE2 PHE A 33 4259 2541 4298 470 -693 -402 C ATOM 266 CZ PHE A 33 14.866 13.659 147.154 1.00 27.39 C ANISOU 266 CZ PHE A 33 3986 2496 3925 435 -656 -369 C ATOM 267 N VAL A 34 10.822 10.704 146.789 1.00 30.61 N ANISOU 267 N VAL A 34 4576 2598 4456 35 -872 -649 N ATOM 268 CA VAL A 34 10.403 10.211 148.090 1.00 30.02 C ANISOU 268 CA VAL A 34 4509 2389 4508 -78 -895 -492 C ATOM 269 C VAL A 34 9.018 10.694 148.463 1.00 29.08 C ANISOU 269 C VAL A 34 4327 2404 4318 -235 -928 -460 C ATOM 270 O VAL A 34 8.598 11.775 148.051 1.00 27.42 O ANISOU 270 O VAL A 34 4051 2417 3949 -214 -936 -480 O ATOM 271 CB VAL A 34 11.384 10.632 149.216 1.00 28.61 C ANISOU 271 CB VAL A 34 4311 2212 4346 8 -878 -277 C ATOM 272 CG1 VAL A 34 12.599 9.733 149.254 1.00 29.91 C ANISOU 272 CG1 VAL A 34 4523 2184 4656 144 -861 -263 C ATOM 273 CG2 VAL A 34 11.828 12.058 149.026 1.00 27.26 C ANISOU 273 CG2 VAL A 34 4069 2269 4021 83 -850 -251 C ATOM 274 N ARG A 35 8.310 9.876 149.235 1.00 30.09 N ANISOU 274 N ARG A 35 4472 2386 4574 -383 -934 -400 N ATOM 275 CA ARG A 35 7.161 10.353 149.976 1.00 29.50 C ANISOU 275 CA ARG A 35 4319 2437 4452 -525 -938 -310 C ATOM 276 C ARG A 35 7.178 9.909 151.435 1.00 30.06 C ANISOU 276 C ARG A 35 4429 2383 4610 -595 -899 -86 C ATOM 277 O ARG A 35 7.832 8.949 151.804 1.00 31.35 O ANISOU 277 O ARG A 35 4688 2317 4908 -565 -881 -8 O ATOM 278 CB ARG A 35 5.842 9.931 149.335 1.00 30.93 C ANISOU 278 CB ARG A 35 4436 2651 4663 -687 -973 -487 C ATOM 279 CG ARG A 35 5.644 8.460 149.331 1.00 33.79 C ANISOU 279 CG ARG A 35 4868 2730 5241 -820 -957 -565 C ATOM 280 CD ARG A 35 4.272 7.979 149.770 1.00 36.12 C ANISOU 280 CD ARG A 35 5085 3001 5639 -1065 -944 -580 C ATOM 281 NE ARG A 35 4.249 6.568 149.418 1.00 40.65 N ANISOU 281 NE ARG A 35 5744 3266 6436 -1180 -922 -719 N ATOM 282 CZ ARG A 35 3.615 6.061 148.363 1.00 43.46 C ANISOU 282 CZ ARG A 35 6051 3621 6841 -1294 -974 -1015 C ATOM 283 NH1 ARG A 35 2.851 6.845 147.618 1.00 43.94 N ANISOU 283 NH1 ARG A 35 5963 4006 6726 -1306 -1063 -1170 N ATOM 284 NH2 ARG A 35 3.704 4.767 148.080 1.00 45.82 N ANISOU 284 NH2 ARG A 35 6447 3596 7368 -1396 -938 -1159 N ATOM 285 N PHE A 36 6.465 10.656 152.263 1.00 30.01 N ANISOU 285 N PHE A 36 4350 2540 4510 -669 -879 26 N ATOM 286 CA PHE A 36 6.035 10.193 153.571 1.00 31.21 C ANISOU 286 CA PHE A 36 4525 2620 4712 -787 -828 216 C ATOM 287 C PHE A 36 4.577 10.595 153.662 1.00 32.41 C ANISOU 287 C PHE A 36 4556 2932 4827 -947 -803 169 C ATOM 288 O PHE A 36 4.236 11.698 153.263 1.00 31.90 O ANISOU 288 O PHE A 36 4395 3090 4634 -894 -824 91 O ATOM 289 CB PHE A 36 6.817 10.852 154.723 1.00 28.86 C ANISOU 289 CB PHE A 36 4249 2420 4295 -687 -818 413 C ATOM 290 CG PHE A 36 6.366 10.383 156.081 1.00 29.64 C ANISOU 290 CG PHE A 36 4385 2482 4395 -795 -759 625 C ATOM 291 CD1 PHE A 36 6.746 9.144 156.558 1.00 31.40 C ANISOU 291 CD1 PHE A 36 4725 2457 4747 -802 -738 774 C ATOM 292 CD2 PHE A 36 5.512 11.155 156.861 1.00 29.30 C ANISOU 292 CD2 PHE A 36 4266 2643 4225 -883 -707 681 C ATOM 293 CE1 PHE A 36 6.298 8.689 157.795 1.00 33.22 C ANISOU 293 CE1 PHE A 36 5006 2656 4960 -900 -666 1002 C ATOM 294 CE2 PHE A 36 5.047 10.702 158.089 1.00 30.32 C ANISOU 294 CE2 PHE A 36 4432 2758 4330 -989 -629 879 C ATOM 295 CZ PHE A 36 5.448 9.473 158.559 1.00 32.63 C ANISOU 295 CZ PHE A 36 4852 2814 4732 -1000 -608 1052 C ATOM 296 N ASP A 37 3.730 9.728 154.212 1.00 35.03 N ANISOU 296 N ASP A 37 4885 3148 5279 -1135 -744 227 N ATOM 297 CA ASP A 37 2.301 9.996 154.345 1.00 36.43 C ANISOU 297 CA ASP A 37 4912 3480 5449 -1304 -706 178 C ATOM 298 C ASP A 37 1.909 9.460 155.714 1.00 37.63 C ANISOU 298 C ASP A 37 5100 3550 5646 -1443 -589 402 C ATOM 299 O ASP A 37 2.030 8.254 155.961 1.00 40.13 O ANISOU 299 O ASP A 37 5523 3596 6129 -1539 -540 483 O ATOM 300 CB ASP A 37 1.555 9.241 153.220 1.00 39.73 C ANISOU 300 CB ASP A 37 5262 3824 6011 -1440 -751 -60 C ATOM 301 CG ASP A 37 0.027 9.518 153.164 1.00 42.56 C ANISOU 301 CG ASP A 37 5410 4385 6376 -1614 -737 -158 C ATOM 302 OD1 ASP A 37 -0.700 9.511 154.192 1.00 43.79 O ANISOU 302 OD1 ASP A 37 5500 4583 6553 -1748 -632 -19 O ATOM 303 OD2 ASP A 37 -0.478 9.687 152.031 1.00 44.01 O ANISOU 303 OD2 ASP A 37 5478 4700 6542 -1616 -834 -386 O ATOM 304 N SER A 38 1.382 10.323 156.581 1.00 36.35 N ANISOU 304 N SER A 38 4856 3611 5343 -1458 -528 500 N ATOM 305 CA SER A 38 1.019 9.925 157.951 1.00 38.06 C ANISOU 305 CA SER A 38 5112 3803 5546 -1577 -399 729 C ATOM 306 C SER A 38 -0.128 8.942 158.073 1.00 40.95 C ANISOU 306 C SER A 38 5416 4048 6096 -1837 -292 736 C ATOM 307 O SER A 38 -0.309 8.356 159.121 1.00 43.18 O ANISOU 307 O SER A 38 5769 4240 6396 -1943 -166 955 O ATOM 308 CB SER A 38 0.685 11.139 158.798 1.00 37.39 C ANISOU 308 CB SER A 38 4945 4008 5253 -1529 -345 788 C ATOM 309 OG SER A 38 -0.568 11.658 158.409 1.00 39.01 O ANISOU 309 OG SER A 38 4951 4393 5476 -1621 -315 641 O ATOM 310 N ASP A 39 -0.892 8.755 157.004 1.00 42.56 N ANISOU 310 N ASP A 39 5482 4258 6429 -1946 -341 497 N ATOM 311 CA ASP A 39 -1.950 7.745 156.974 1.00 46.26 C ANISOU 311 CA ASP A 39 5869 4591 7117 -2227 -249 450 C ATOM 312 C ASP A 39 -1.495 6.411 156.402 1.00 48.02 C ANISOU 312 C ASP A 39 6233 4438 7574 -2305 -264 392 C ATOM 313 O ASP A 39 -2.196 5.412 156.557 1.00 50.54 O ANISOU 313 O ASP A 39 6535 4556 8111 -2555 -156 394 O ATOM 314 CB ASP A 39 -3.140 8.229 156.144 1.00 47.38 C ANISOU 314 CB ASP A 39 5745 4977 7282 -2325 -305 191 C ATOM 315 CG ASP A 39 -3.878 9.363 156.792 1.00 47.29 C ANISOU 315 CG ASP A 39 5565 5297 7108 -2291 -244 247 C ATOM 316 OD1 ASP A 39 -3.456 9.809 157.889 1.00 47.06 O ANISOU 316 OD1 ASP A 39 5634 5315 6930 -2203 -155 465 O ATOM 317 OD2 ASP A 39 -4.879 9.807 156.194 1.00 48.06 O ANISOU 317 OD2 ASP A 39 5423 5618 7220 -2342 -289 61 O ATOM 318 N ALA A 40 -0.354 6.405 155.708 1.00 46.69 N ANISOU 318 N ALA A 40 6196 4168 7378 -2099 -383 321 N ATOM 319 CA ALA A 40 0.174 5.171 155.128 1.00 48.68 C ANISOU 319 CA ALA A 40 6593 4051 7853 -2134 -391 242 C ATOM 320 C ALA A 40 0.668 4.203 156.220 1.00 51.63 C ANISOU 320 C ALA A 40 7168 4102 8347 -2158 -258 556 C ATOM 321 O ALA A 40 1.184 4.627 157.259 1.00 51.40 O ANISOU 321 O ALA A 40 7214 4165 8149 -2026 -224 830 O ATOM 322 CB ALA A 40 1.256 5.473 154.133 1.00 45.69 C ANISOU 322 CB ALA A 40 6283 3680 7397 -1893 -529 88 C ATOM 323 N ALA A 41 0.490 2.907 155.976 1.00 55.26 N ANISOU 323 N ALA A 41 7716 4187 9094 -2323 -182 511 N ATOM 324 CA ALA A 41 0.680 1.872 156.993 1.00 58.45 C ANISOU 324 CA ALA A 41 8306 4247 9657 -2390 -21 827 C ATOM 325 C ALA A 41 2.133 1.646 157.440 1.00 58.43 C ANISOU 325 C ALA A 41 8521 4082 9597 -2092 -55 1071 C ATOM 326 O ALA A 41 2.382 1.094 158.510 1.00 59.89 O ANISOU 326 O ALA A 41 8854 4095 9805 -2071 56 1417 O ATOM 327 CB ALA A 41 0.056 0.564 156.520 1.00 61.72 C ANISOU 327 CB ALA A 41 8751 4264 10434 -2663 83 682 C ATOM 328 N SER A 42 3.081 2.101 156.630 1.00 57.10 N ANISOU 328 N SER A 42 8357 3998 9341 -1855 -208 901 N ATOM 329 CA SER A 42 4.494 1.882 156.896 1.00 57.50 C ANISOU 329 CA SER A 42 8568 3915 9363 -1564 -257 1080 C ATOM 330 C SER A 42 5.050 2.752 158.028 1.00 55.92 C ANISOU 330 C SER A 42 8370 4005 8871 -1389 -292 1366 C ATOM 331 O SER A 42 5.833 2.265 158.834 1.00 57.72 O ANISOU 331 O SER A 42 8741 4095 9096 -1236 -273 1656 O ATOM 332 CB SER A 42 5.301 2.131 155.626 1.00 55.93 C ANISOU 332 CB SER A 42 8346 3743 9163 -1385 -388 785 C ATOM 333 OG SER A 42 5.263 3.503 155.288 1.00 53.24 O ANISOU 333 OG SER A 42 7850 3822 8559 -1315 -492 654 O ATOM 334 N GLN A 43 4.631 4.018 158.076 1.00 53.25 N ANISOU 334 N GLN A 43 7873 4065 8295 -1407 -344 1275 N ATOM 335 CA GLN A 43 5.238 5.066 158.927 1.00 51.72 C ANISOU 335 CA GLN A 43 7655 4189 7809 -1235 -403 1436 C ATOM 336 C GLN A 43 6.742 5.262 158.651 1.00 50.60 C ANISOU 336 C GLN A 43 7561 4049 7614 -949 -530 1432 C ATOM 337 O GLN A 43 7.517 5.561 159.559 1.00 50.51 O ANISOU 337 O GLN A 43 7587 4164 7439 -793 -572 1641 O ATOM 338 CB GLN A 43 4.956 4.874 160.436 1.00 53.53 C ANISOU 338 CB GLN A 43 7957 4461 7920 -1288 -296 1783 C ATOM 339 CG GLN A 43 3.486 4.941 160.848 1.00 55.09 C ANISOU 339 CG GLN A 43 8065 4749 8118 -1564 -151 1795 C ATOM 340 CD GLN A 43 2.858 6.308 160.620 1.00 53.31 C ANISOU 340 CD GLN A 43 7641 4904 7708 -1598 -190 1586 C ATOM 341 OE1 GLN A 43 3.376 7.336 161.069 1.00 51.72 O ANISOU 341 OE1 GLN A 43 7412 4974 7266 -1446 -257 1611 O ATOM 342 NE2 GLN A 43 1.732 6.327 159.912 1.00 53.77 N ANISOU 342 NE2 GLN A 43 7555 4982 7893 -1794 -151 1370 N ATOM 343 N ARG A 44 7.128 5.082 157.384 1.00 49.89 N ANISOU 343 N ARG A 44 7457 3840 7659 -887 -588 1179 N ATOM 344 CA ARG A 44 8.511 5.149 156.933 1.00 48.44 C ANISOU 344 CA ARG A 44 7299 3633 7474 -632 -681 1137 C ATOM 345 C ARG A 44 8.553 6.103 155.774 1.00 45.60 C ANISOU 345 C ARG A 44 6817 3478 7030 -605 -746 838 C ATOM 346 O ARG A 44 7.551 6.281 155.090 1.00 45.66 O ANISOU 346 O ARG A 44 6756 3536 7056 -766 -728 645 O ATOM 347 CB ARG A 44 8.961 3.788 156.415 1.00 51.55 C ANISOU 347 CB ARG A 44 7823 3619 8145 -574 -647 1116 C ATOM 348 CG ARG A 44 8.819 2.630 157.385 1.00 55.58 C ANISOU 348 CG ARG A 44 8488 3826 8805 -611 -552 1418 C ATOM 349 CD ARG A 44 9.973 2.584 158.353 1.00 57.23 C ANISOU 349 CD ARG A 44 8757 4076 8911 -354 -609 1721 C ATOM 350 NE ARG A 44 11.235 2.471 157.624 1.00 58.13 N ANISOU 350 NE ARG A 44 8859 4124 9103 -100 -692 1601 N ATOM 351 CZ ARG A 44 12.440 2.666 158.159 1.00 58.66 C ANISOU 351 CZ ARG A 44 8905 4312 9071 162 -786 1766 C ATOM 352 NH1 ARG A 44 12.555 2.984 159.445 1.00 59.23 N ANISOU 352 NH1 ARG A 44 8981 4588 8937 206 -825 2055 N ATOM 353 NH2 ARG A 44 13.534 2.541 157.407 1.00 58.46 N ANISOU 353 NH2 ARG A 44 8841 4228 9143 379 -841 1630 N ATOM 354 N MET A 45 9.701 6.723 155.550 1.00 43.93 N ANISOU 354 N MET A 45 6569 3397 6725 -400 -818 808 N ATOM 355 CA MET A 45 9.929 7.478 154.326 1.00 42.27 C ANISOU 355 CA MET A 45 6274 3327 6459 -345 -856 548 C ATOM 356 C MET A 45 10.115 6.445 153.200 1.00 44.21 C ANISOU 356 C MET A 45 6588 3306 6903 -319 -839 359 C ATOM 357 O MET A 45 10.919 5.532 153.321 1.00 45.99 O ANISOU 357 O MET A 45 6902 3293 7279 -195 -827 434 O ATOM 358 CB MET A 45 11.181 8.330 154.481 1.00 41.02 C ANISOU 358 CB MET A 45 6057 3352 6178 -151 -910 585 C ATOM 359 CG MET A 45 11.412 9.322 153.383 1.00 39.70 C ANISOU 359 CG MET A 45 5803 3361 5921 -102 -920 373 C ATOM 360 SD MET A 45 10.504 10.845 153.666 1.00 39.10 S ANISOU 360 SD MET A 45 5627 3590 5639 -215 -912 357 S ATOM 361 CE MET A 45 11.541 11.996 152.802 1.00 36.75 C ANISOU 361 CE MET A 45 5255 3454 5253 -68 -912 233 C ATOM 362 N GLU A 46 9.349 6.567 152.123 1.00 43.99 N ANISOU 362 N GLU A 46 6518 3323 6872 -429 -838 108 N ATOM 363 CA GLU A 46 9.318 5.533 151.094 1.00 45.80 C ANISOU 363 CA GLU A 46 6815 3308 7279 -449 -819 -114 C ATOM 364 C GLU A 46 9.953 6.043 149.808 1.00 44.86 C ANISOU 364 C GLU A 46 6657 3328 7059 -309 -847 -347 C ATOM 365 O GLU A 46 9.889 7.229 149.525 1.00 42.55 O ANISOU 365 O GLU A 46 6272 3329 6565 -278 -878 -374 O ATOM 366 CB GLU A 46 7.865 5.082 150.852 1.00 47.12 C ANISOU 366 CB GLU A 46 6959 3418 7525 -713 -800 -248 C ATOM 367 CG GLU A 46 7.386 3.964 151.784 1.00 49.25 C ANISOU 367 CG GLU A 46 7322 3380 8012 -864 -720 -75 C ATOM 368 CD GLU A 46 5.864 3.866 151.885 1.00 49.74 C ANISOU 368 CD GLU A 46 7301 3485 8114 -1155 -690 -144 C ATOM 369 OE1 GLU A 46 5.195 4.915 151.942 1.00 47.12 O ANISOU 369 OE1 GLU A 46 6829 3482 7591 -1209 -730 -158 O ATOM 370 OE2 GLU A 46 5.336 2.735 151.929 1.00 52.60 O ANISOU 370 OE2 GLU A 46 7729 3542 8716 -1332 -617 -183 O ATOM 371 N PRO A 47 10.590 5.146 149.034 1.00 47.08 N ANISOU 371 N PRO A 47 7018 3388 7484 -213 -819 -509 N ATOM 372 CA PRO A 47 11.081 5.462 147.684 1.00 47.12 C ANISOU 372 CA PRO A 47 6999 3517 7388 -98 -821 -765 C ATOM 373 C PRO A 47 9.952 5.650 146.672 1.00 47.84 C ANISOU 373 C PRO A 47 7048 3759 7370 -254 -860 -1026 C ATOM 374 O PRO A 47 8.884 5.067 146.826 1.00 48.38 O ANISOU 374 O PRO A 47 7120 3723 7540 -459 -874 -1089 O ATOM 375 CB PRO A 47 11.886 4.215 147.304 1.00 49.36 C ANISOU 375 CB PRO A 47 7391 3469 7893 20 -764 -873 C ATOM 376 CG PRO A 47 11.394 3.145 148.186 1.00 51.14 C ANISOU 376 CG PRO A 47 7709 3366 8356 -101 -736 -740 C ATOM 377 CD PRO A 47 11.007 3.801 149.462 1.00 49.51 C ANISOU 377 CD PRO A 47 7450 3306 8055 -174 -766 -432 C ATOM 378 N ARG A 48 10.195 6.462 145.648 1.00 48.10 N ANISOU 378 N ARG A 48 7033 4051 7193 -155 -876 -1169 N ATOM 379 CA ARG A 48 9.193 6.738 144.625 1.00 49.66 C ANISOU 379 CA ARG A 48 7179 4455 7234 -257 -936 -1403 C ATOM 380 C ARG A 48 9.856 6.917 143.266 1.00 50.56 C ANISOU 380 C ARG A 48 7320 4702 7190 -100 -914 -1620 C ATOM 381 O ARG A 48 9.228 7.353 142.308 1.00 50.87 O ANISOU 381 O ARG A 48 7317 4988 7024 -123 -969 -1790 O ATOM 382 CB ARG A 48 8.380 7.979 144.985 1.00 48.72 C ANISOU 382 CB ARG A 48 6945 4634 6931 -315 -988 -1260 C ATOM 383 CG ARG A 48 7.112 7.722 145.833 1.00 50.86 C ANISOU 383 CG ARG A 48 7155 4865 7303 -540 -1023 -1190 C ATOM 384 CD ARG A 48 6.237 6.597 145.267 1.00 55.14 C ANISOU 384 CD ARG A 48 7700 5272 7979 -730 -1057 -1456 C ATOM 385 NE ARG A 48 4.815 6.945 145.287 1.00 57.00 N ANISOU 385 NE ARG A 48 7790 5714 8153 -910 -1129 -1509 N ATOM 386 CZ ARG A 48 3.897 6.435 144.460 1.00 60.46 C ANISOU 386 CZ ARG A 48 8158 6213 8599 -1062 -1204 -1799 C ATOM 387 NH1 ARG A 48 2.619 6.815 144.540 1.00 60.60 N ANISOU 387 NH1 ARG A 48 8006 6454 8566 -1212 -1275 -1832 N ATOM 388 NH2 ARG A 48 4.255 5.542 143.538 1.00 63.33 N ANISOU 388 NH2 ARG A 48 8608 6431 9022 -1062 -1210 -2080 N ATOM 389 N ALA A 49 11.134 6.567 143.200 1.00 51.55 N ANISOU 389 N ALA A 49 7507 4679 7402 72 -830 -1606 N ATOM 390 CA ALA A 49 11.912 6.591 141.966 1.00 53.14 C ANISOU 390 CA ALA A 49 7740 4974 7477 233 -770 -1811 C ATOM 391 C ALA A 49 12.960 5.497 142.137 1.00 55.68 C ANISOU 391 C ALA A 49 8139 4967 8048 352 -685 -1852 C ATOM 392 O ALA A 49 13.519 5.373 143.230 1.00 55.67 O ANISOU 392 O ALA A 49 8130 4808 8215 403 -668 -1608 O ATOM 393 CB ALA A 49 12.585 7.957 141.788 1.00 50.22 C ANISOU 393 CB ALA A 49 7304 4886 6891 376 -724 -1652 C ATOM 394 N PRO A 50 13.236 4.701 141.074 1.00 58.18 N ANISOU 394 N PRO A 50 8529 5190 8384 411 -633 -2163 N ATOM 395 CA PRO A 50 14.082 3.496 141.218 1.00 60.11 C ANISOU 395 CA PRO A 50 8859 5067 8914 525 -545 -2235 C ATOM 396 C PRO A 50 15.559 3.734 141.583 1.00 58.94 C ANISOU 396 C PRO A 50 8664 4900 8832 774 -455 -2048 C ATOM 397 O PRO A 50 16.204 2.855 142.156 1.00 60.28 O ANISOU 397 O PRO A 50 8874 4759 9269 880 -411 -1978 O ATOM 398 CB PRO A 50 13.965 2.819 139.841 1.00 63.30 C ANISOU 398 CB PRO A 50 9340 5454 9258 531 -505 -2659 C ATOM 399 CG PRO A 50 13.618 3.935 138.903 1.00 62.21 C ANISOU 399 CG PRO A 50 9140 5764 8734 529 -543 -2738 C ATOM 400 CD PRO A 50 12.717 4.838 139.699 1.00 59.40 C ANISOU 400 CD PRO A 50 8698 5579 8293 381 -656 -2475 C ATOM 401 N TRP A 51 16.082 4.915 141.285 1.00 56.48 N ANISOU 401 N TRP A 51 8256 4912 8290 866 -426 -1958 N ATOM 402 CA TRP A 51 17.476 5.199 141.573 1.00 56.14 C ANISOU 402 CA TRP A 51 8129 4889 8310 1076 -340 -1813 C ATOM 403 C TRP A 51 17.753 5.559 143.030 1.00 54.53 C ANISOU 403 C TRP A 51 7847 4652 8221 1075 -405 -1469 C ATOM 404 O TRP A 51 18.905 5.604 143.439 1.00 54.89 O ANISOU 404 O TRP A 51 7806 4685 8366 1245 -361 -1349 O ATOM 405 CB TRP A 51 18.022 6.285 140.642 1.00 55.36 C ANISOU 405 CB TRP A 51 7957 5129 7948 1163 -249 -1862 C ATOM 406 CG TRP A 51 17.114 7.438 140.449 1.00 53.33 C ANISOU 406 CG TRP A 51 7681 5156 7425 1023 -311 -1790 C ATOM 407 CD1 TRP A 51 16.214 7.610 139.438 1.00 54.32 C ANISOU 407 CD1 TRP A 51 7867 5453 7320 944 -340 -1979 C ATOM 408 CD2 TRP A 51 17.011 8.602 141.285 1.00 50.82 C ANISOU 408 CD2 TRP A 51 7274 4991 7042 962 -354 -1514 C ATOM 409 NE1 TRP A 51 15.545 8.810 139.594 1.00 52.54 N ANISOU 409 NE1 TRP A 51 7594 5469 6900 857 -397 -1811 N ATOM 410 CE2 TRP A 51 16.014 9.437 140.719 1.00 49.98 C ANISOU 410 CE2 TRP A 51 7186 5120 6684 861 -396 -1535 C ATOM 411 CE3 TRP A 51 17.651 9.016 142.459 1.00 48.87 C ANISOU 411 CE3 TRP A 51 6932 4716 6921 988 -367 -1265 C ATOM 412 CZ2 TRP A 51 15.642 10.657 141.292 1.00 47.03 C ANISOU 412 CZ2 TRP A 51 6749 4909 6211 792 -429 -1315 C ATOM 413 CZ3 TRP A 51 17.284 10.229 143.019 1.00 46.50 C ANISOU 413 CZ3 TRP A 51 6570 4593 6504 896 -404 -1077 C ATOM 414 CH2 TRP A 51 16.297 11.043 142.428 1.00 45.33 C ANISOU 414 CH2 TRP A 51 6453 4638 6133 803 -423 -1102 C ATOM 415 N ILE A 52 16.714 5.818 143.817 1.00 53.09 N ANISOU 415 N ILE A 52 7681 4479 8013 889 -510 -1322 N ATOM 416 CA ILE A 52 16.922 6.153 145.228 1.00 52.02 C ANISOU 416 CA ILE A 52 7483 4338 7947 882 -573 -1010 C ATOM 417 C ILE A 52 16.926 4.877 146.060 1.00 54.14 C ANISOU 417 C ILE A 52 7837 4255 8479 905 -596 -910 C ATOM 418 O ILE A 52 17.384 4.865 147.203 1.00 54.33 O ANISOU 418 O ILE A 52 7821 4240 8582 970 -640 -653 O ATOM 419 CB ILE A 52 15.880 7.201 145.761 1.00 49.24 C ANISOU 419 CB ILE A 52 7093 4198 7417 692 -650 -877 C ATOM 420 CG1 ILE A 52 16.426 7.992 146.943 1.00 46.82 C ANISOU 420 CG1 ILE A 52 6687 4013 7090 725 -686 -612 C ATOM 421 CG2 ILE A 52 14.583 6.547 146.164 1.00 49.99 C ANISOU 421 CG2 ILE A 52 7272 4138 7585 499 -711 -878 C ATOM 422 CD1 ILE A 52 17.746 8.523 146.695 1.00 46.47 C ANISOU 422 CD1 ILE A 52 6534 4095 7028 891 -625 -607 C ATOM 423 N GLU A 53 16.469 3.788 145.448 1.00 56.50 N ANISOU 423 N GLU A 53 8257 4295 8915 862 -561 -1121 N ATOM 424 CA GLU A 53 16.315 2.507 146.119 1.00 59.02 C ANISOU 424 CA GLU A 53 8691 4220 9513 856 -555 -1040 C ATOM 425 C GLU A 53 17.640 1.861 146.477 1.00 60.21 C ANISOU 425 C GLU A 53 8835 4179 9865 1134 -509 -928 C ATOM 426 O GLU A 53 17.697 1.031 147.375 1.00 61.75 O ANISOU 426 O GLU A 53 9105 4090 10267 1180 -518 -726 O ATOM 427 CB GLU A 53 15.528 1.546 145.238 1.00 62.64 C ANISOU 427 CB GLU A 53 9275 4442 10084 725 -512 -1353 C ATOM 428 CG GLU A 53 14.027 1.726 145.264 1.00 63.49 C ANISOU 428 CG GLU A 53 9397 4619 10107 424 -576 -1411 C ATOM 429 CD GLU A 53 13.303 0.391 145.186 1.00 68.02 C ANISOU 429 CD GLU A 53 10104 4792 10948 267 -536 -1568 C ATOM 430 OE1 GLU A 53 13.694 -0.537 145.936 1.00 70.71 O ANISOU 430 OE1 GLU A 53 10540 4765 11560 343 -482 -1397 O ATOM 431 OE2 GLU A 53 12.358 0.258 144.371 1.00 69.66 O ANISOU 431 OE2 GLU A 53 10319 5049 11100 71 -559 -1863 O ATOM 432 N GLN A 54 18.705 2.269 145.789 1.00 59.68 N ANISOU 432 N GLN A 54 8665 4280 9730 1328 -453 -1040 N ATOM 433 CA GLN A 54 20.044 1.741 146.019 1.00 61.63 C ANISOU 433 CA GLN A 54 8856 4400 10163 1620 -407 -961 C ATOM 434 C GLN A 54 20.736 2.372 147.223 1.00 59.58 C ANISOU 434 C GLN A 54 8451 4323 9864 1719 -499 -627 C ATOM 435 O GLN A 54 21.867 2.011 147.552 1.00 60.91 O ANISOU 435 O GLN A 54 8531 4437 10173 1972 -491 -526 O ATOM 436 CB GLN A 54 20.912 1.926 144.777 1.00 63.55 C ANISOU 436 CB GLN A 54 9022 4775 10349 1779 -290 -1231 C ATOM 437 CG GLN A 54 21.263 3.376 144.473 1.00 61.83 C ANISOU 437 CG GLN A 54 8640 4992 9861 1750 -286 -1214 C ATOM 438 CD GLN A 54 21.459 3.629 142.982 1.00 63.15 C ANISOU 438 CD GLN A 54 8805 5311 9879 1781 -155 -1527 C ATOM 439 OE1 GLN A 54 22.366 4.362 142.581 1.00 63.20 O ANISOU 439 OE1 GLN A 54 8667 5560 9786 1891 -72 -1538 O ATOM 440 NE2 GLN A 54 20.609 3.020 142.154 1.00 64.41 N ANISOU 440 NE2 GLN A 54 9120 5340 10013 1674 -130 -1789 N ATOM 441 N GLU A 55 20.067 3.316 147.875 1.00 55.69 N ANISOU 441 N GLU A 55 7921 4062 9179 1528 -588 -472 N ATOM 442 CA GLU A 55 20.556 3.825 149.136 1.00 53.95 C ANISOU 442 CA GLU A 55 7588 4001 8912 1586 -689 -174 C ATOM 443 C GLU A 55 20.251 2.811 150.219 1.00 54.56 C ANISOU 443 C GLU A 55 7788 3792 9149 1614 -743 74 C ATOM 444 O GLU A 55 19.217 2.146 150.179 1.00 55.20 O ANISOU 444 O GLU A 55 8036 3627 9309 1455 -714 47 O ATOM 445 CB GLU A 55 19.910 5.164 149.459 1.00 51.75 C ANISOU 445 CB GLU A 55 7243 4043 8378 1374 -747 -119 C ATOM 446 CG GLU A 55 20.241 6.271 148.480 1.00 50.95 C ANISOU 446 CG GLU A 55 7027 4219 8114 1353 -681 -305 C ATOM 447 CD GLU A 55 21.645 6.819 148.653 1.00 52.15 C ANISOU 447 CD GLU A 55 6977 4563 8274 1528 -674 -257 C ATOM 448 OE1 GLU A 55 22.235 6.657 149.746 1.00 54.10 O ANISOU 448 OE1 GLU A 55 7143 4827 8586 1631 -768 -53 O ATOM 449 OE2 GLU A 55 22.162 7.431 147.696 1.00 52.14 O ANISOU 449 OE2 GLU A 55 6888 4717 8205 1559 -572 -420 O ATOM 450 N GLY A 56 21.155 2.692 151.183 1.00 54.16 N ANISOU 450 N GLY A 56 7649 3784 9146 1815 -820 322 N ATOM 451 CA GLY A 56 21.079 1.623 152.161 1.00 56.10 C ANISOU 451 CA GLY A 56 8020 3741 9554 1914 -856 594 C ATOM 452 C GLY A 56 20.104 1.918 153.272 1.00 54.57 C ANISOU 452 C GLY A 56 7900 3622 9211 1707 -928 835 C ATOM 453 O GLY A 56 19.539 3.001 153.324 1.00 52.00 O ANISOU 453 O GLY A 56 7511 3585 8663 1503 -959 780 O ATOM 454 N PRO A 57 19.919 0.954 154.187 1.00 56.78 N ANISOU 454 N PRO A 57 8320 3639 9615 1772 -939 1117 N ATOM 455 CA PRO A 57 19.038 1.050 155.353 1.00 55.88 C ANISOU 455 CA PRO A 57 8295 3568 9368 1602 -982 1391 C ATOM 456 C PRO A 57 19.315 2.259 156.249 1.00 53.36 C ANISOU 456 C PRO A 57 7814 3713 8748 1586 -1114 1524 C ATOM 457 O PRO A 57 18.378 2.816 156.828 1.00 52.45 O ANISOU 457 O PRO A 57 7731 3746 8451 1360 -1123 1596 O ATOM 458 CB PRO A 57 19.319 -0.248 156.113 1.00 59.83 C ANISOU 458 CB PRO A 57 8946 3715 10072 1801 -967 1706 C ATOM 459 CG PRO A 57 20.559 -0.819 155.499 1.00 62.12 C ANISOU 459 CG PRO A 57 9171 3859 10573 2126 -957 1616 C ATOM 460 CD PRO A 57 20.561 -0.366 154.095 1.00 60.30 C ANISOU 460 CD PRO A 57 8862 3690 10357 2034 -885 1193 C ATOM 461 N GLU A 58 20.579 2.679 156.317 1.00 52.56 N ANISOU 461 N GLU A 58 7525 3841 8605 1813 -1204 1522 N ATOM 462 CA GLU A 58 21.003 3.847 157.094 1.00 50.41 C ANISOU 462 CA GLU A 58 7071 4013 8070 1800 -1334 1589 C ATOM 463 C GLU A 58 20.431 5.147 156.539 1.00 45.95 C ANISOU 463 C GLU A 58 6428 3695 7336 1544 -1298 1339 C ATOM 464 O GLU A 58 20.153 6.083 157.300 1.00 43.70 O ANISOU 464 O GLU A 58 6081 3697 6826 1417 -1365 1397 O ATOM 465 CB GLU A 58 22.531 3.961 157.144 1.00 52.63 C ANISOU 465 CB GLU A 58 7132 4475 8389 2088 -1431 1594 C ATOM 466 CG GLU A 58 23.260 2.761 157.750 1.00 58.85 C ANISOU 466 CG GLU A 58 7959 5066 9334 2409 -1492 1868 C ATOM 467 CD GLU A 58 23.665 1.703 156.707 1.00 61.98 C ANISOU 467 CD GLU A 58 8420 5075 10055 2595 -1369 1742 C ATOM 468 OE1 GLU A 58 24.277 0.672 157.101 1.00 65.60 O ANISOU 468 OE1 GLU A 58 8919 5320 10687 2889 -1397 1959 O ATOM 469 OE2 GLU A 58 23.362 1.910 155.498 1.00 60.72 O ANISOU 469 OE2 GLU A 58 8275 4828 9967 2460 -1241 1426 O ATOM 470 N TYR A 59 20.270 5.202 155.215 1.00 43.58 N ANISOU 470 N TYR A 59 6136 3285 7137 1484 -1189 1062 N ATOM 471 CA TYR A 59 19.661 6.351 154.577 1.00 38.76 C ANISOU 471 CA TYR A 59 5478 2872 6379 1267 -1142 849 C ATOM 472 C TYR A 59 18.196 6.411 154.974 1.00 37.58 C ANISOU 472 C TYR A 59 5465 2675 6137 1021 -1120 909 C ATOM 473 O TYR A 59 17.735 7.440 155.449 1.00 35.38 O ANISOU 473 O TYR A 59 5133 2644 5666 877 -1148 922 O ATOM 474 CB TYR A 59 19.835 6.283 153.063 1.00 37.50 C ANISOU 474 CB TYR A 59 5311 2616 6322 1289 -1033 565 C ATOM 475 CG TYR A 59 19.156 7.393 152.304 1.00 33.91 C ANISOU 475 CG TYR A 59 4830 2344 5710 1092 -978 373 C ATOM 476 CD1 TYR A 59 19.761 8.624 152.163 1.00 31.74 C ANISOU 476 CD1 TYR A 59 4395 2354 5311 1089 -978 306 C ATOM 477 CD2 TYR A 59 17.897 7.202 151.722 1.00 33.48 C ANISOU 477 CD2 TYR A 59 4906 2173 5642 912 -926 261 C ATOM 478 CE1 TYR A 59 19.126 9.652 151.479 1.00 30.01 C ANISOU 478 CE1 TYR A 59 4169 2277 4954 932 -917 166 C ATOM 479 CE2 TYR A 59 17.255 8.210 151.043 1.00 30.84 C ANISOU 479 CE2 TYR A 59 4544 2021 5155 768 -890 113 C ATOM 480 CZ TYR A 59 17.870 9.433 150.918 1.00 29.50 C ANISOU 480 CZ TYR A 59 4239 2110 4861 789 -880 81 C ATOM 481 OH TYR A 59 17.232 10.428 150.209 1.00 27.79 O ANISOU 481 OH TYR A 59 4013 2046 4500 671 -831 -38 O ATOM 482 N TRP A 60 17.497 5.290 154.826 1.00 39.43 N ANISOU 482 N TRP A 60 5867 2586 6528 975 -1059 943 N ATOM 483 CA TRP A 60 16.059 5.221 155.102 1.00 39.65 C ANISOU 483 CA TRP A 60 6005 2548 6511 724 -1016 979 C ATOM 484 C TRP A 60 15.631 5.487 156.536 1.00 39.88 C ANISOU 484 C TRP A 60 6052 2720 6379 650 -1064 1250 C ATOM 485 O TRP A 60 14.687 6.249 156.764 1.00 37.66 O ANISOU 485 O TRP A 60 5752 2612 5946 451 -1047 1218 O ATOM 486 CB TRP A 60 15.461 3.910 154.576 1.00 42.26 C ANISOU 486 CB TRP A 60 6497 2476 7082 668 -927 924 C ATOM 487 CG TRP A 60 15.632 3.834 153.097 1.00 42.39 C ANISOU 487 CG TRP A 60 6496 2420 7190 690 -876 595 C ATOM 488 CD1 TRP A 60 16.487 3.016 152.406 1.00 44.50 C ANISOU 488 CD1 TRP A 60 6794 2462 7652 884 -835 487 C ATOM 489 CD2 TRP A 60 14.982 4.654 152.119 1.00 40.00 C ANISOU 489 CD2 TRP A 60 6135 2303 6761 536 -858 334 C ATOM 490 NE1 TRP A 60 16.396 3.268 151.056 1.00 43.72 N ANISOU 490 NE1 TRP A 60 6667 2409 7535 845 -786 160 N ATOM 491 CE2 TRP A 60 15.482 4.272 150.855 1.00 41.06 C ANISOU 491 CE2 TRP A 60 6278 2330 6994 637 -807 76 C ATOM 492 CE3 TRP A 60 14.013 5.659 152.184 1.00 37.50 C ANISOU 492 CE3 TRP A 60 5761 2234 6253 341 -875 299 C ATOM 493 CZ2 TRP A 60 15.049 4.867 149.673 1.00 39.60 C ANISOU 493 CZ2 TRP A 60 6054 2301 6691 548 -784 -196 C ATOM 494 CZ3 TRP A 60 13.587 6.246 151.010 1.00 36.78 C ANISOU 494 CZ3 TRP A 60 5625 2277 6072 268 -857 41 C ATOM 495 CH2 TRP A 60 14.108 5.857 149.774 1.00 37.46 C ANISOU 495 CH2 TRP A 60 5728 2276 6228 370 -816 -195 C ATOM 496 N ASP A 61 16.350 4.882 157.481 1.00 42.70 N ANISOU 496 N ASP A 61 6441 3027 6757 830 -1122 1515 N ATOM 497 CA ASP A 61 16.139 5.107 158.911 1.00 43.11 C ANISOU 497 CA ASP A 61 6510 3259 6610 804 -1179 1793 C ATOM 498 C ASP A 61 16.335 6.553 159.336 1.00 40.59 C ANISOU 498 C ASP A 61 6033 3364 6025 753 -1258 1717 C ATOM 499 O ASP A 61 15.547 7.078 160.121 1.00 39.99 O ANISOU 499 O ASP A 61 5976 3455 5762 598 -1248 1795 O ATOM 500 CB ASP A 61 17.067 4.214 159.720 1.00 46.61 C ANISOU 500 CB ASP A 61 7000 3604 7107 1065 -1250 2087 C ATOM 501 CG ASP A 61 16.443 2.887 160.025 1.00 50.33 C ANISOU 501 CG ASP A 61 7685 3682 7755 1044 -1150 2312 C ATOM 502 OD1 ASP A 61 16.946 2.156 160.907 1.00 53.65 O ANISOU 502 OD1 ASP A 61 8183 4019 8183 1238 -1193 2633 O ATOM 503 OD2 ASP A 61 15.421 2.585 159.382 1.00 50.32 O ANISOU 503 OD2 ASP A 61 7772 3459 7888 827 -1027 2169 O ATOM 504 N GLY A 62 17.374 7.183 158.793 1.00 39.00 N ANISOU 504 N GLY A 62 5674 3318 5825 874 -1318 1550 N ATOM 505 CA GLY A 62 17.702 8.555 159.096 1.00 37.04 C ANISOU 505 CA GLY A 62 5268 3430 5375 824 -1380 1444 C ATOM 506 C GLY A 62 16.697 9.509 158.509 1.00 34.93 C ANISOU 506 C GLY A 62 4999 3234 5041 599 -1291 1244 C ATOM 507 O GLY A 62 16.293 10.468 159.169 1.00 33.30 O ANISOU 507 O GLY A 62 4750 3259 4645 482 -1304 1236 O ATOM 508 N GLU A 63 16.261 9.219 157.282 1.00 35.19 N ANISOU 508 N GLU A 63 5079 3069 5221 550 -1201 1079 N ATOM 509 CA GLU A 63 15.231 10.029 156.619 1.00 33.29 C ANISOU 509 CA GLU A 63 4837 2891 4920 364 -1126 903 C ATOM 510 C GLU A 63 13.870 9.899 157.304 1.00 32.77 C ANISOU 510 C GLU A 63 4859 2811 4783 184 -1086 1008 C ATOM 511 O GLU A 63 13.105 10.847 157.301 1.00 31.53 O ANISOU 511 O GLU A 63 4659 2811 4508 53 -1052 923 O ATOM 512 CB GLU A 63 15.101 9.698 155.126 1.00 33.92 C ANISOU 512 CB GLU A 63 4943 2805 5140 369 -1058 698 C ATOM 513 CG GLU A 63 16.299 10.044 154.254 1.00 35.02 C ANISOU 513 CG GLU A 63 4982 2997 5326 517 -1051 555 C ATOM 514 CD GLU A 63 16.625 11.508 154.245 1.00 34.72 C ANISOU 514 CD GLU A 63 4819 3225 5149 481 -1047 478 C ATOM 515 OE1 GLU A 63 17.670 11.914 154.799 1.00 35.70 O ANISOU 515 OE1 GLU A 63 4828 3489 5248 569 -1099 520 O ATOM 516 OE2 GLU A 63 15.835 12.267 153.669 1.00 34.85 O ANISOU 516 OE2 GLU A 63 4844 3307 5089 366 -989 369 O ATOM 517 N THR A 64 13.588 8.742 157.904 1.00 34.14 N ANISOU 517 N THR A 64 5147 2790 5035 184 -1076 1201 N ATOM 518 CA THR A 64 12.342 8.534 158.642 1.00 33.88 C ANISOU 518 CA THR A 64 5189 2742 4943 5 -1014 1327 C ATOM 519 C THR A 64 12.363 9.339 159.934 1.00 33.86 C ANISOU 519 C THR A 64 5144 3029 4694 -9 -1051 1462 C ATOM 520 O THR A 64 11.374 9.987 160.301 1.00 33.11 O ANISOU 520 O THR A 64 5028 3076 4475 -166 -994 1436 O ATOM 521 CB THR A 64 12.125 7.043 158.966 1.00 36.38 C ANISOU 521 CB THR A 64 5654 2740 5429 9 -967 1526 C ATOM 522 OG1 THR A 64 12.176 6.291 157.755 1.00 36.71 O ANISOU 522 OG1 THR A 64 5736 2503 5707 24 -931 1356 O ATOM 523 CG2 THR A 64 10.777 6.798 159.641 1.00 36.77 C ANISOU 523 CG2 THR A 64 5768 2760 5442 -209 -867 1649 C ATOM 524 N ARG A 65 13.516 9.314 160.593 1.00 34.87 N ANISOU 524 N ARG A 65 5243 3259 4745 165 -1152 1584 N ATOM 525 CA ARG A 65 13.729 9.981 161.866 1.00 35.21 C ANISOU 525 CA ARG A 65 5246 3599 4532 176 -1216 1697 C ATOM 526 C ARG A 65 13.595 11.488 161.710 1.00 33.76 C ANISOU 526 C ARG A 65 4939 3670 4219 83 -1211 1465 C ATOM 527 O ARG A 65 12.911 12.154 162.498 1.00 33.54 O ANISOU 527 O ARG A 65 4908 3829 4005 -30 -1175 1475 O ATOM 528 CB ARG A 65 15.129 9.662 162.311 1.00 36.93 C ANISOU 528 CB ARG A 65 5416 3888 4728 402 -1353 1814 C ATOM 529 CG ARG A 65 15.371 9.841 163.751 1.00 38.91 C ANISOU 529 CG ARG A 65 5666 4404 4715 448 -1439 2005 C ATOM 530 CD ARG A 65 16.171 8.678 164.199 1.00 42.08 C ANISOU 530 CD ARG A 65 6128 4693 5169 670 -1525 2275 C ATOM 531 NE ARG A 65 17.303 8.424 163.316 1.00 42.23 N ANISOU 531 NE ARG A 65 6046 4604 5396 851 -1593 2167 N ATOM 532 CZ ARG A 65 17.779 7.211 163.043 1.00 43.88 C ANISOU 532 CZ ARG A 65 6328 4533 5810 1035 -1598 2323 C ATOM 533 NH1 ARG A 65 17.198 6.138 163.566 1.00 45.83 N ANISOU 533 NH1 ARG A 65 6766 4550 6097 1047 -1534 2606 N ATOM 534 NH2 ARG A 65 18.817 7.073 162.224 1.00 43.26 N ANISOU 534 NH2 ARG A 65 6136 4388 5914 1205 -1645 2193 N ATOM 535 N LYS A 66 14.236 11.996 160.662 1.00 32.93 N ANISOU 535 N LYS A 66 4740 3548 4222 135 -1226 1260 N ATOM 536 CA LYS A 66 14.122 13.386 160.254 1.00 31.78 C ANISOU 536 CA LYS A 66 4495 3564 4014 55 -1191 1041 C ATOM 537 C LYS A 66 12.701 13.802 159.881 1.00 31.12 C ANISOU 537 C LYS A 66 4450 3452 3923 -106 -1078 960 C ATOM 538 O LYS A 66 12.232 14.869 160.319 1.00 29.97 O ANISOU 538 O LYS A 66 4261 3481 3645 -189 -1041 885 O ATOM 539 CB LYS A 66 15.088 13.670 159.090 1.00 31.51 C ANISOU 539 CB LYS A 66 4374 3479 4120 148 -1199 876 C ATOM 540 CG LYS A 66 16.502 14.104 159.556 1.00 32.95 C ANISOU 540 CG LYS A 66 4421 3839 4258 258 -1299 854 C ATOM 541 CD LYS A 66 17.629 13.432 158.778 1.00 33.49 C ANISOU 541 CD LYS A 66 4431 3791 4501 425 -1331 836 C ATOM 542 CE LYS A 66 17.832 14.093 157.447 1.00 31.61 C ANISOU 542 CE LYS A 66 4135 3509 4367 403 -1234 631 C ATOM 543 NZ LYS A 66 18.619 13.303 156.482 1.00 31.55 N ANISOU 543 NZ LYS A 66 4105 3349 4532 551 -1218 595 N ATOM 544 N VAL A 67 12.011 12.970 159.092 1.00 31.59 N ANISOU 544 N VAL A 67 4576 3298 4127 -146 -1027 960 N ATOM 545 CA VAL A 67 10.667 13.344 158.617 1.00 30.86 C ANISOU 545 CA VAL A 67 4480 3205 4040 -288 -939 864 C ATOM 546 C VAL A 67 9.593 13.281 159.707 1.00 32.32 C ANISOU 546 C VAL A 67 4695 3471 4115 -416 -881 987 C ATOM 547 O VAL A 67 8.662 14.090 159.709 1.00 32.06 O ANISOU 547 O VAL A 67 4607 3556 4017 -508 -815 901 O ATOM 548 CB VAL A 67 10.250 12.621 157.305 1.00 30.72 C ANISOU 548 CB VAL A 67 4492 2983 4197 -307 -915 761 C ATOM 549 CG1 VAL A 67 9.715 11.206 157.549 1.00 32.27 C ANISOU 549 CG1 VAL A 67 4785 2962 4515 -377 -891 886 C ATOM 550 CG2 VAL A 67 9.265 13.480 156.517 1.00 29.66 C ANISOU 550 CG2 VAL A 67 4294 2941 4035 -386 -866 599 C ATOM 551 N LYS A 68 9.765 12.372 160.669 1.00 34.73 N ANISOU 551 N LYS A 68 5080 3726 4389 -405 -895 1203 N ATOM 552 CA LYS A 68 8.904 12.338 161.848 1.00 36.04 C ANISOU 552 CA LYS A 68 5280 4004 4410 -515 -823 1350 C ATOM 553 C LYS A 68 9.116 13.605 162.700 1.00 35.58 C ANISOU 553 C LYS A 68 5157 4244 4117 -501 -838 1291 C ATOM 554 O LYS A 68 8.156 14.168 163.257 1.00 34.74 O ANISOU 554 O LYS A 68 5027 4281 3893 -608 -745 1270 O ATOM 555 CB LYS A 68 9.152 11.071 162.669 1.00 38.48 C ANISOU 555 CB LYS A 68 5712 4187 4724 -481 -827 1630 C ATOM 556 CG LYS A 68 8.457 9.836 162.129 1.00 39.95 C ANISOU 556 CG LYS A 68 5976 4064 5139 -576 -747 1697 C ATOM 557 CD LYS A 68 8.830 8.612 162.934 1.00 43.40 C ANISOU 557 CD LYS A 68 6555 4333 5601 -515 -739 2002 C ATOM 558 CE LYS A 68 8.023 7.403 162.501 1.00 45.72 C ANISOU 558 CE LYS A 68 6936 4289 6147 -652 -624 2063 C ATOM 559 NZ LYS A 68 8.623 6.123 163.014 1.00 48.90 N ANISOU 559 NZ LYS A 68 7500 4432 6648 -542 -618 2355 N ATOM 560 N ALA A 69 10.364 14.079 162.741 1.00 34.92 N ANISOU 560 N ALA A 69 5031 4252 3984 -376 -946 1233 N ATOM 561 CA ALA A 69 10.684 15.277 163.494 1.00 34.71 C ANISOU 561 CA ALA A 69 4939 4490 3761 -377 -968 1131 C ATOM 562 C ALA A 69 10.136 16.521 162.814 1.00 32.88 C ANISOU 562 C ALA A 69 4630 4294 3569 -441 -888 898 C ATOM 563 O ALA A 69 9.829 17.490 163.496 1.00 33.66 O ANISOU 563 O ALA A 69 4697 4571 3521 -490 -841 808 O ATOM 564 CB ALA A 69 12.181 15.384 163.738 1.00 35.00 C ANISOU 564 CB ALA A 69 4923 4620 3756 -245 -1110 1121 C ATOM 565 N HIS A 70 9.984 16.483 161.490 1.00 31.62 N ANISOU 565 N HIS A 70 4452 3966 3597 -429 -865 804 N ATOM 566 CA HIS A 70 9.236 17.533 160.780 1.00 30.53 C ANISOU 566 CA HIS A 70 4258 3846 3498 -472 -779 636 C ATOM 567 C HIS A 70 7.771 17.517 161.192 1.00 31.72 C ANISOU 567 C HIS A 70 4408 4046 3599 -578 -679 670 C ATOM 568 O HIS A 70 7.242 18.536 161.616 1.00 32.24 O ANISOU 568 O HIS A 70 4430 4244 3575 -608 -605 581 O ATOM 569 CB HIS A 70 9.363 17.398 159.260 1.00 28.60 C ANISOU 569 CB HIS A 70 4001 3443 3423 -421 -785 552 C ATOM 570 CG HIS A 70 10.683 17.866 158.724 1.00 28.27 C ANISOU 570 CG HIS A 70 3925 3388 3428 -326 -831 468 C ATOM 571 ND1 HIS A 70 11.854 17.151 158.893 1.00 28.45 N ANISOU 571 ND1 HIS A 70 3951 3375 3483 -248 -920 534 N ATOM 572 CD2 HIS A 70 11.020 18.983 158.034 1.00 26.94 C ANISOU 572 CD2 HIS A 70 3709 3237 3291 -296 -784 334 C ATOM 573 CE1 HIS A 70 12.851 17.807 158.328 1.00 27.97 C ANISOU 573 CE1 HIS A 70 3826 3328 3473 -187 -925 426 C ATOM 574 NE2 HIS A 70 12.373 18.921 157.802 1.00 27.55 N ANISOU 574 NE2 HIS A 70 3750 3296 3420 -225 -836 310 N ATOM 575 N SER A 71 7.142 16.350 161.093 1.00 33.11 N ANISOU 575 N SER A 71 4624 4108 3850 -639 -664 791 N ATOM 576 CA SER A 71 5.755 16.151 161.509 1.00 34.78 C ANISOU 576 CA SER A 71 4810 4364 4038 -763 -558 838 C ATOM 577 C SER A 71 5.442 16.622 162.936 1.00 36.62 C ANISOU 577 C SER A 71 5048 4803 4062 -808 -485 899 C ATOM 578 O SER A 71 4.413 17.278 163.168 1.00 37.16 O ANISOU 578 O SER A 71 5045 4988 4084 -867 -377 827 O ATOM 579 CB SER A 71 5.403 14.675 161.396 1.00 36.79 C ANISOU 579 CB SER A 71 5124 4437 4415 -842 -551 982 C ATOM 580 OG SER A 71 4.384 14.324 162.316 1.00 39.01 O ANISOU 580 OG SER A 71 5404 4786 4631 -973 -437 1103 O ATOM 581 N GLN A 72 6.332 16.305 163.880 1.00 37.60 N ANISOU 581 N GLN A 72 5248 4992 4047 -764 -545 1022 N ATOM 582 CA GLN A 72 6.199 16.820 165.241 1.00 38.31 C ANISOU 582 CA GLN A 72 5350 5319 3886 -789 -493 1054 C ATOM 583 C GLN A 72 6.329 18.341 165.349 1.00 36.63 C ANISOU 583 C GLN A 72 5067 5262 3589 -760 -472 819 C ATOM 584 O GLN A 72 5.636 18.956 166.161 1.00 37.82 O ANISOU 584 O GLN A 72 5197 5584 3588 -810 -364 766 O ATOM 585 CB GLN A 72 7.155 16.129 166.212 1.00 40.42 C ANISOU 585 CB GLN A 72 5709 5656 3991 -727 -587 1245 C ATOM 586 CG GLN A 72 6.807 14.691 166.538 1.00 43.97 C ANISOU 586 CG GLN A 72 6260 5974 4474 -767 -550 1527 C ATOM 587 CD GLN A 72 5.550 14.533 167.413 1.00 47.69 C ANISOU 587 CD GLN A 72 6749 6555 4816 -903 -373 1641 C ATOM 588 OE1 GLN A 72 4.972 15.512 167.930 1.00 48.51 O ANISOU 588 OE1 GLN A 72 6792 6875 4766 -948 -283 1508 O ATOM 589 NE2 GLN A 72 5.131 13.280 167.599 1.00 49.97 N ANISOU 589 NE2 GLN A 72 7125 6684 5179 -970 -303 1889 N ATOM 590 N THR A 73 7.178 18.946 164.524 1.00 33.73 N ANISOU 590 N THR A 73 4664 4820 3331 -684 -551 675 N ATOM 591 CA THR A 73 7.296 20.398 164.512 1.00 33.20 C ANISOU 591 CA THR A 73 4540 4836 3237 -668 -508 452 C ATOM 592 C THR A 73 5.998 21.035 163.999 1.00 33.71 C ANISOU 592 C THR A 73 4548 4871 3389 -693 -370 361 C ATOM 593 O THR A 73 5.514 22.022 164.566 1.00 34.24 O ANISOU 593 O THR A 73 4586 5053 3370 -705 -268 235 O ATOM 594 CB THR A 73 8.512 20.877 163.670 1.00 31.14 C ANISOU 594 CB THR A 73 4251 4479 3102 -596 -596 338 C ATOM 595 OG1 THR A 73 9.670 20.113 164.019 1.00 31.27 O ANISOU 595 OG1 THR A 73 4289 4522 3072 -552 -735 439 O ATOM 596 CG2 THR A 73 8.807 22.356 163.882 1.00 30.25 C ANISOU 596 CG2 THR A 73 4096 4438 2962 -601 -542 116 C ATOM 597 N HIS A 74 5.409 20.438 162.965 1.00 33.55 N ANISOU 597 N HIS A 74 4506 4710 3533 -694 -369 418 N ATOM 598 CA HIS A 74 4.159 20.962 162.434 1.00 34.33 C ANISOU 598 CA HIS A 74 4522 4811 3711 -699 -266 345 C ATOM 599 C HIS A 74 2.963 20.718 163.379 1.00 36.28 C ANISOU 599 C HIS A 74 4728 5196 3860 -791 -145 404 C ATOM 600 O HIS A 74 2.021 21.511 163.406 1.00 36.17 O ANISOU 600 O HIS A 74 4628 5261 3854 -777 -34 307 O ATOM 601 CB HIS A 74 3.879 20.401 161.045 1.00 33.39 C ANISOU 601 CB HIS A 74 4372 4546 3768 -678 -320 362 C ATOM 602 CG HIS A 74 4.843 20.855 159.998 1.00 33.26 C ANISOU 602 CG HIS A 74 4380 4421 3839 -576 -391 288 C ATOM 603 ND1 HIS A 74 4.873 22.146 159.527 1.00 33.21 N ANISOU 603 ND1 HIS A 74 4345 4412 3861 -492 -338 171 N ATOM 604 CD2 HIS A 74 5.812 20.191 159.323 1.00 33.01 C ANISOU 604 CD2 HIS A 74 4398 4269 3875 -542 -490 322 C ATOM 605 CE1 HIS A 74 5.809 22.261 158.601 1.00 31.99 C ANISOU 605 CE1 HIS A 74 4223 4151 3780 -424 -393 147 C ATOM 606 NE2 HIS A 74 6.403 21.091 158.468 1.00 32.11 N ANISOU 606 NE2 HIS A 74 4278 4106 3816 -450 -487 226 N ATOM 607 N ARG A 75 3.018 19.634 164.155 1.00 37.97 N ANISOU 607 N ARG A 75 5004 5438 3986 -874 -153 573 N ATOM 608 CA ARG A 75 1.934 19.288 165.082 1.00 40.42 C ANISOU 608 CA ARG A 75 5283 5879 4196 -979 -14 661 C ATOM 609 C ARG A 75 1.809 20.322 166.207 1.00 40.53 C ANISOU 609 C ARG A 75 5292 6109 3998 -961 90 558 C ATOM 610 O ARG A 75 0.708 20.703 166.592 1.00 41.86 O ANISOU 610 O ARG A 75 5375 6396 4132 -999 243 510 O ATOM 611 CB ARG A 75 2.132 17.882 165.661 1.00 43.15 C ANISOU 611 CB ARG A 75 5726 6176 4494 -1062 -31 903 C ATOM 612 CG ARG A 75 0.877 17.293 166.258 1.00 46.74 C ANISOU 612 CG ARG A 75 6134 6700 4926 -1203 135 1021 C ATOM 613 CD ARG A 75 1.138 16.522 167.556 1.00 51.04 C ANISOU 613 CD ARG A 75 6805 7327 5259 -1255 185 1258 C ATOM 614 NE ARG A 75 1.424 15.105 167.328 1.00 53.10 N ANISOU 614 NE ARG A 75 7162 7368 5646 -1306 138 1481 N ATOM 615 CZ ARG A 75 1.525 14.194 168.300 1.00 56.27 C ANISOU 615 CZ ARG A 75 7687 7778 5916 -1354 197 1750 C ATOM 616 NH1 ARG A 75 1.363 14.545 169.574 1.00 58.01 N ANISOU 616 NH1 ARG A 75 7945 8258 5838 -1360 299 1827 N ATOM 617 NH2 ARG A 75 1.798 12.928 167.999 1.00 57.39 N ANISOU 617 NH2 ARG A 75 7923 7664 6217 -1385 163 1946 N ATOM 618 N VAL A 76 2.947 20.797 166.693 1.00 39.17 N ANISOU 618 N VAL A 76 5197 5993 3693 -903 6 496 N ATOM 619 CA VAL A 76 2.983 21.897 167.636 1.00 38.68 C ANISOU 619 CA VAL A 76 5134 6119 3442 -886 85 329 C ATOM 620 C VAL A 76 2.569 23.191 166.951 1.00 37.77 C ANISOU 620 C VAL A 76 4936 5938 3476 -817 161 104 C ATOM 621 O VAL A 76 1.741 23.925 167.481 1.00 38.78 O ANISOU 621 O VAL A 76 5014 6181 3540 -814 314 -12 O ATOM 622 CB VAL A 76 4.384 22.036 168.251 1.00 37.88 C ANISOU 622 CB VAL A 76 5114 6100 3179 -855 -52 295 C ATOM 623 CG1 VAL A 76 4.457 23.233 169.164 1.00 38.59 C ANISOU 623 CG1 VAL A 76 5200 6378 3084 -853 21 63 C ATOM 624 CG2 VAL A 76 4.733 20.771 169.002 1.00 38.58 C ANISOU 624 CG2 VAL A 76 5289 6270 3100 -885 -123 553 C ATOM 625 N ASP A 77 3.112 23.423 165.753 1.00 36.89 N ANISOU 625 N ASP A 77 4816 5637 3565 -750 67 61 N ATOM 626 CA ASP A 77 2.911 24.670 164.983 1.00 36.96 C ANISOU 626 CA ASP A 77 4773 5544 3725 -659 129 -113 C ATOM 627 C ASP A 77 1.439 25.072 164.784 1.00 36.97 C ANISOU 627 C ASP A 77 4667 5582 3800 -623 276 -146 C ATOM 628 O ASP A 77 1.060 26.230 164.972 1.00 37.57 O ANISOU 628 O ASP A 77 4711 5671 3893 -552 396 -305 O ATOM 629 CB ASP A 77 3.566 24.546 163.602 1.00 37.31 C ANISOU 629 CB ASP A 77 4826 5390 3958 -597 16 -81 C ATOM 630 CG ASP A 77 4.961 25.163 163.543 1.00 38.67 C ANISOU 630 CG ASP A 77 5056 5496 4142 -576 -52 -186 C ATOM 631 OD1 ASP A 77 5.337 25.859 164.505 1.00 40.45 O ANISOU 631 OD1 ASP A 77 5302 5819 4249 -607 -12 -323 O ATOM 632 OD2 ASP A 77 5.663 24.977 162.510 1.00 38.08 O ANISOU 632 OD2 ASP A 77 4993 5280 4195 -534 -136 -149 O ATOM 633 N LEU A 78 0.623 24.085 164.433 1.00 35.97 N ANISOU 633 N LEU A 78 4472 5467 3727 -673 268 -3 N ATOM 634 CA LEU A 78 -0.802 24.258 164.237 1.00 35.63 C ANISOU 634 CA LEU A 78 4283 5495 3759 -653 386 -20 C ATOM 635 C LEU A 78 -1.521 24.870 165.455 1.00 37.14 C ANISOU 635 C LEU A 78 4431 5871 3811 -665 573 -111 C ATOM 636 O LEU A 78 -2.397 25.718 165.287 1.00 37.95 O ANISOU 636 O LEU A 78 4420 6007 3992 -568 690 -219 O ATOM 637 CB LEU A 78 -1.420 22.919 163.842 1.00 35.31 C ANISOU 637 CB LEU A 78 4176 5452 3789 -762 340 137 C ATOM 638 CG LEU A 78 -1.149 22.488 162.405 1.00 33.19 C ANISOU 638 CG LEU A 78 3899 5024 3689 -722 189 167 C ATOM 639 CD1 LEU A 78 -1.244 20.974 162.222 1.00 33.32 C ANISOU 639 CD1 LEU A 78 3923 4982 3753 -865 120 306 C ATOM 640 CD2 LEU A 78 -2.133 23.181 161.526 1.00 33.83 C ANISOU 640 CD2 LEU A 78 3825 5135 3893 -612 218 84 C ATOM 641 N GLY A 79 -1.106 24.477 166.661 1.00 37.67 N ANISOU 641 N GLY A 79 4589 6065 3660 -762 600 -71 N ATOM 642 CA GLY A 79 -1.688 24.984 167.907 1.00 38.60 C ANISOU 642 CA GLY A 79 4687 6389 3591 -781 783 -165 C ATOM 643 C GLY A 79 -1.186 26.364 168.295 1.00 37.95 C ANISOU 643 C GLY A 79 4658 6306 3454 -689 835 -412 C ATOM 644 O GLY A 79 -1.871 27.112 168.996 1.00 39.85 O ANISOU 644 O GLY A 79 4852 6671 3619 -654 1015 -562 O ATOM 645 N THR A 80 0.013 26.706 167.849 1.00 35.33 N ANISOU 645 N THR A 80 4421 5829 3175 -658 694 -472 N ATOM 646 CA THR A 80 0.576 27.996 168.195 1.00 35.75 C ANISOU 646 CA THR A 80 4527 5848 3209 -605 745 -724 C ATOM 647 C THR A 80 -0.014 29.056 167.281 1.00 35.80 C ANISOU 647 C THR A 80 4464 5672 3466 -462 843 -832 C ATOM 648 O THR A 80 -0.480 30.093 167.752 1.00 37.74 O ANISOU 648 O THR A 80 4692 5932 3716 -395 1008 -1028 O ATOM 649 CB THR A 80 2.107 27.969 168.117 1.00 34.41 C ANISOU 649 CB THR A 80 4459 5604 3011 -646 570 -754 C ATOM 650 OG1 THR A 80 2.606 27.077 169.117 1.00 35.03 O ANISOU 650 OG1 THR A 80 4597 5887 2825 -743 485 -654 O ATOM 651 CG2 THR A 80 2.723 29.356 168.348 1.00 35.06 C ANISOU 651 CG2 THR A 80 4582 5610 3129 -620 628 -1043 C ATOM 652 N LEU A 81 -0.009 28.762 165.979 1.00 34.01 N ANISOU 652 N LEU A 81 4202 5280 3438 -402 743 -698 N ATOM 653 CA LEU A 81 -0.709 29.553 164.959 1.00 33.66 C ANISOU 653 CA LEU A 81 4080 5092 3618 -239 811 -722 C ATOM 654 C LEU A 81 -2.176 29.885 165.306 1.00 35.43 C ANISOU 654 C LEU A 81 4160 5443 3857 -159 985 -765 C ATOM 655 O LEU A 81 -2.596 31.043 165.163 1.00 36.40 O ANISOU 655 O LEU A 81 4255 5475 4099 -6 1116 -896 O ATOM 656 CB LEU A 81 -0.593 28.860 163.598 1.00 31.65 C ANISOU 656 CB LEU A 81 3800 4730 3497 -208 656 -542 C ATOM 657 CG LEU A 81 0.837 29.041 163.084 1.00 30.42 C ANISOU 657 CG LEU A 81 3771 4402 3387 -223 544 -553 C ATOM 658 CD1 LEU A 81 1.286 28.026 162.052 1.00 27.91 C ANISOU 658 CD1 LEU A 81 3462 4022 3120 -246 375 -385 C ATOM 659 CD2 LEU A 81 1.012 30.452 162.580 1.00 30.62 C ANISOU 659 CD2 LEU A 81 3833 4235 3567 -87 646 -671 C ATOM 660 N ARG A 82 -2.911 28.876 165.793 1.00 35.64 N ANISOU 660 N ARG A 82 4097 5669 3776 -262 1001 -655 N ATOM 661 CA ARG A 82 -4.241 29.024 166.410 1.00 37.37 C ANISOU 661 CA ARG A 82 4162 6071 3965 -233 1189 -702 C ATOM 662 C ARG A 82 -4.303 30.146 167.439 1.00 39.06 C ANISOU 662 C ARG A 82 4419 6335 4087 -174 1380 -936 C ATOM 663 O ARG A 82 -5.212 30.966 167.405 1.00 40.31 O ANISOU 663 O ARG A 82 4463 6499 4353 -24 1539 -1044 O ATOM 664 CB ARG A 82 -4.622 27.735 167.134 1.00 38.99 C ANISOU 664 CB ARG A 82 4327 6479 4008 -419 1200 -556 C ATOM 665 CG ARG A 82 -5.549 26.782 166.420 1.00 40.53 C ANISOU 665 CG ARG A 82 4349 6718 4331 -469 1158 -394 C ATOM 666 CD ARG A 82 -6.149 25.843 167.451 1.00 44.90 C ANISOU 666 CD ARG A 82 4853 7479 4729 -648 1279 -294 C ATOM 667 NE ARG A 82 -6.920 26.590 168.468 1.00 49.56 N ANISOU 667 NE ARG A 82 5363 8258 5209 -600 1523 -436 N ATOM 668 CZ ARG A 82 -7.084 26.225 169.746 1.00 52.20 C ANISOU 668 CZ ARG A 82 5737 8793 5303 -722 1676 -411 C ATOM 669 NH1 ARG A 82 -6.536 25.105 170.217 1.00 52.32 N ANISOU 669 NH1 ARG A 82 5879 8840 5160 -894 1608 -219 N ATOM 670 NH2 ARG A 82 -7.806 26.988 170.560 1.00 55.09 N ANISOU 670 NH2 ARG A 82 6022 9331 5580 -656 1908 -571 N ATOM 671 N GLY A 83 -3.327 30.166 168.349 1.00 39.44 N ANISOU 671 N GLY A 83 4624 6427 3932 -284 1359 -1026 N ATOM 672 CA GLY A 83 -3.226 31.178 169.394 1.00 41.01 C ANISOU 672 CA GLY A 83 4888 6687 4009 -260 1522 -1293 C ATOM 673 C GLY A 83 -2.842 32.539 168.861 1.00 41.72 C ANISOU 673 C GLY A 83 5033 6510 4309 -119 1567 -1489 C ATOM 674 O GLY A 83 -3.368 33.539 169.331 1.00 43.62 O ANISOU 674 O GLY A 83 5253 6737 4584 -17 1765 -1704 O ATOM 675 N TYR A 84 -1.941 32.576 167.870 1.00 40.89 N ANISOU 675 N TYR A 84 5000 6180 4358 -110 1405 -1411 N ATOM 676 CA TYR A 84 -1.495 33.830 167.254 1.00 42.28 C ANISOU 676 CA TYR A 84 5245 6062 4759 10 1458 -1553 C ATOM 677 C TYR A 84 -2.637 34.565 166.577 1.00 44.07 C ANISOU 677 C TYR A 84 5364 6172 5211 240 1601 -1537 C ATOM 678 O TYR A 84 -2.771 35.780 166.710 1.00 46.89 O ANISOU 678 O TYR A 84 5758 6358 5700 364 1770 -1730 O ATOM 679 CB TYR A 84 -0.402 33.595 166.207 1.00 40.76 C ANISOU 679 CB TYR A 84 5129 5675 4684 -23 1273 -1422 C ATOM 680 CG TYR A 84 0.987 33.330 166.758 1.00 41.26 C ANISOU 680 CG TYR A 84 5301 5771 4605 -204 1147 -1504 C ATOM 681 CD1 TYR A 84 1.308 33.635 168.087 1.00 43.35 C ANISOU 681 CD1 TYR A 84 5616 6191 4665 -311 1206 -1739 C ATOM 682 CD2 TYR A 84 1.990 32.799 165.941 1.00 38.93 C ANISOU 682 CD2 TYR A 84 5047 5373 4372 -257 967 -1361 C ATOM 683 CE1 TYR A 84 2.571 33.397 168.594 1.00 43.07 C ANISOU 683 CE1 TYR A 84 5651 6228 4487 -464 1066 -1819 C ATOM 684 CE2 TYR A 84 3.265 32.551 166.446 1.00 39.43 C ANISOU 684 CE2 TYR A 84 5175 5491 4315 -406 843 -1436 C ATOM 685 CZ TYR A 84 3.545 32.855 167.779 1.00 41.52 C ANISOU 685 CZ TYR A 84 5472 5929 4375 -507 883 -1663 C ATOM 686 OH TYR A 84 4.803 32.623 168.293 1.00 41.98 O ANISOU 686 OH TYR A 84 5567 6082 4301 -643 737 -1746 O ATOM 687 N TYR A 85 -3.470 33.813 165.868 1.00 43.25 N ANISOU 687 N TYR A 85 5116 6163 5153 301 1531 -1315 N ATOM 688 CA TYR A 85 -4.553 34.392 165.096 1.00 43.96 C ANISOU 688 CA TYR A 85 5071 6186 5448 540 1618 -1263 C ATOM 689 C TYR A 85 -5.902 34.363 165.815 1.00 46.90 C ANISOU 689 C TYR A 85 5256 6791 5770 601 1786 -1324 C ATOM 690 O TYR A 85 -6.932 34.688 165.208 1.00 47.98 O ANISOU 690 O TYR A 85 5226 6937 6067 806 1841 -1264 O ATOM 691 CB TYR A 85 -4.651 33.681 163.753 1.00 40.70 C ANISOU 691 CB TYR A 85 4588 5751 5125 584 1425 -1011 C ATOM 692 CG TYR A 85 -3.523 34.015 162.821 1.00 37.98 C ANISOU 692 CG TYR A 85 4402 5148 4882 607 1317 -950 C ATOM 693 CD1 TYR A 85 -3.491 35.228 162.151 1.00 38.83 C ANISOU 693 CD1 TYR A 85 4567 4999 5187 817 1412 -970 C ATOM 694 CD2 TYR A 85 -2.495 33.116 162.597 1.00 35.31 C ANISOU 694 CD2 TYR A 85 4154 4812 4451 427 1138 -860 C ATOM 695 CE1 TYR A 85 -2.460 35.535 161.284 1.00 37.23 C ANISOU 695 CE1 TYR A 85 4509 4561 5078 826 1342 -897 C ATOM 696 CE2 TYR A 85 -1.466 33.407 161.733 1.00 33.43 C ANISOU 696 CE2 TYR A 85 4041 4356 4306 444 1060 -807 C ATOM 697 CZ TYR A 85 -1.458 34.612 161.075 1.00 34.74 C ANISOU 697 CZ TYR A 85 4261 4280 4657 634 1167 -822 C ATOM 698 OH TYR A 85 -0.426 34.910 160.227 1.00 33.85 O ANISOU 698 OH TYR A 85 4274 3952 4636 637 1120 -756 O ATOM 699 N ASN A 86 -5.871 33.975 167.096 1.00 48.51 N ANISOU 699 N ASN A 86 5483 7203 5745 432 1867 -1435 N ATOM 700 CA ASN A 86 -7.041 33.888 168.004 1.00 51.84 C ANISOU 700 CA ASN A 86 5744 7885 6069 446 2064 -1511 C ATOM 701 C ASN A 86 -8.192 32.995 167.535 1.00 52.13 C ANISOU 701 C ASN A 86 5533 8117 6158 453 2034 -1312 C ATOM 702 O ASN A 86 -9.356 33.285 167.774 1.00 54.08 O ANISOU 702 O ASN A 86 5580 8504 6463 572 2206 -1368 O ATOM 703 CB ASN A 86 -7.550 35.278 168.422 1.00 55.33 C ANISOU 703 CB ASN A 86 6170 8233 6620 653 2311 -1765 C ATOM 704 CG ASN A 86 -7.956 35.338 169.900 1.00 59.08 C ANISOU 704 CG ASN A 86 6630 8958 6860 571 2528 -1971 C ATOM 705 OD1 ASN A 86 -7.114 35.202 170.796 1.00 60.02 O ANISOU 705 OD1 ASN A 86 6917 9150 6739 394 2514 -2091 O ATOM 706 ND2 ASN A 86 -9.242 35.559 170.157 1.00 61.09 N ANISOU 706 ND2 ASN A 86 6675 9368 7170 711 2729 -2017 N ATOM 707 N GLN A 87 -7.835 31.896 166.883 1.00 50.84 N ANISOU 707 N GLN A 87 5375 7962 5980 315 1819 -1100 N ATOM 708 CA GLN A 87 -8.787 30.928 166.347 1.00 52.19 C ANISOU 708 CA GLN A 87 5320 8295 6214 271 1757 -926 C ATOM 709 C GLN A 87 -9.110 29.821 167.364 1.00 54.60 C ANISOU 709 C GLN A 87 5580 8846 6320 27 1832 -860 C ATOM 710 O GLN A 87 -8.229 29.399 168.113 1.00 54.08 O ANISOU 710 O GLN A 87 5708 8791 6049 -136 1805 -848 O ATOM 711 CB GLN A 87 -8.206 30.305 165.068 1.00 48.40 C ANISOU 711 CB GLN A 87 4886 7672 5831 244 1494 -754 C ATOM 712 CG GLN A 87 -7.626 31.331 164.104 1.00 47.08 C ANISOU 712 CG GLN A 87 4826 7248 5816 455 1424 -782 C ATOM 713 CD GLN A 87 -6.696 30.729 163.060 1.00 44.36 C ANISOU 713 CD GLN A 87 4599 6760 5496 394 1187 -639 C ATOM 714 OE1 GLN A 87 -5.879 29.856 163.363 1.00 42.69 O ANISOU 714 OE1 GLN A 87 4510 6549 5162 190 1089 -584 O ATOM 715 NE2 GLN A 87 -6.806 31.207 161.827 1.00 43.48 N ANISOU 715 NE2 GLN A 87 4454 6532 5535 588 1102 -572 N ATOM 716 N SER A 88 -10.364 29.351 167.380 1.00 58.44 N ANISOU 716 N SER A 88 5802 9535 6867 4 1927 -807 N ATOM 717 CA SER A 88 -10.770 28.177 168.185 1.00 61.04 C ANISOU 717 CA SER A 88 6068 10077 7047 -248 2011 -695 C ATOM 718 C SER A 88 -10.196 26.859 167.612 1.00 60.42 C ANISOU 718 C SER A 88 6069 9911 6975 -451 1791 -486 C ATOM 719 O SER A 88 -9.704 26.827 166.470 1.00 58.63 O ANISOU 719 O SER A 88 5886 9504 6886 -385 1575 -442 O ATOM 720 CB SER A 88 -12.295 28.086 168.288 1.00 63.21 C ANISOU 720 CB SER A 88 6005 10584 7428 -227 2191 -710 C ATOM 721 OG SER A 88 -12.841 27.393 167.177 1.00 62.25 O ANISOU 721 OG SER A 88 5680 10466 7508 -264 2030 -595 O ATOM 722 N GLU A 89 -10.251 25.777 168.397 1.00 62.46 N ANISOU 722 N GLU A 89 6358 10286 7086 -687 1859 -354 N ATOM 723 CA GLU A 89 -9.708 24.474 167.946 1.00 61.30 C ANISOU 723 CA GLU A 89 6305 10025 6962 -879 1678 -155 C ATOM 724 C GLU A 89 -10.578 23.775 166.890 1.00 60.32 C ANISOU 724 C GLU A 89 5936 9900 7082 -943 1593 -93 C ATOM 725 O GLU A 89 -10.056 23.036 166.051 1.00 59.40 O ANISOU 725 O GLU A 89 5891 9623 7056 -1015 1389 -4 O ATOM 726 CB GLU A 89 -9.460 23.527 169.133 1.00 64.51 C ANISOU 726 CB GLU A 89 6846 10528 7139 -1096 1787 -1 C ATOM 727 CG GLU A 89 -8.600 22.279 168.819 1.00 64.76 C ANISOU 727 CG GLU A 89 7050 10385 7172 -1255 1602 206 C ATOM 728 CD GLU A 89 -8.584 21.260 169.955 1.00 68.29 C ANISOU 728 CD GLU A 89 7601 10927 7418 -1458 1738 411 C ATOM 729 OE1 GLU A 89 -9.666 20.758 170.350 1.00 71.40 O ANISOU 729 OE1 GLU A 89 7823 11460 7844 -1599 1939 483 O ATOM 730 OE2 GLU A 89 -7.480 20.968 170.466 1.00 68.41 O ANISOU 730 OE2 GLU A 89 7864 10888 7241 -1471 1650 511 O ATOM 731 N ALA A 90 -11.883 24.058 166.896 1.00 59.80 N ANISOU 731 N ALA A 90 5571 10025 7127 -905 1742 -168 N ATOM 732 CA ALA A 90 -12.846 23.285 166.117 1.00 58.55 C ANISOU 732 CA ALA A 90 5132 9934 7178 -1019 1689 -128 C ATOM 733 C ALA A 90 -12.717 23.338 164.599 1.00 55.13 C ANISOU 733 C ALA A 90 4638 9383 6927 -903 1418 -160 C ATOM 734 O ALA A 90 -13.222 22.455 163.913 1.00 55.15 O ANISOU 734 O ALA A 90 4472 9409 7073 -1049 1319 -128 O ATOM 735 CB ALA A 90 -14.221 23.665 166.506 1.00 62.36 C ANISOU 735 CB ALA A 90 5284 10677 7733 -984 1909 -216 C ATOM 736 N GLY A 91 -12.043 24.367 164.088 1.00 51.33 N ANISOU 736 N GLY A 91 4294 8778 6431 -650 1309 -228 N ATOM 737 CA GLY A 91 -11.836 24.519 162.657 1.00 47.20 C ANISOU 737 CA GLY A 91 3747 8154 6034 -510 1067 -240 C ATOM 738 C GLY A 91 -10.591 23.827 162.147 1.00 42.89 C ANISOU 738 C GLY A 91 3469 7382 5444 -609 873 -155 C ATOM 739 O GLY A 91 -9.588 23.739 162.846 1.00 41.97 O ANISOU 739 O GLY A 91 3611 7144 5192 -672 902 -107 O ATOM 740 N SER A 92 -10.662 23.325 160.923 1.00 40.45 N ANISOU 740 N SER A 92 3085 7040 5245 -615 670 -148 N ATOM 741 CA SER A 92 -9.540 22.666 160.301 1.00 36.69 C ANISOU 741 CA SER A 92 2837 6356 4747 -685 490 -88 C ATOM 742 C SER A 92 -8.609 23.713 159.684 1.00 34.09 C ANISOU 742 C SER A 92 2689 5887 4376 -436 399 -108 C ATOM 743 O SER A 92 -9.083 24.698 159.138 1.00 34.05 O ANISOU 743 O SER A 92 2571 5948 4419 -206 393 -159 O ATOM 744 CB SER A 92 -10.057 21.701 159.238 1.00 37.23 C ANISOU 744 CB SER A 92 2742 6463 4941 -801 326 -109 C ATOM 745 OG SER A 92 -8.989 20.968 158.653 1.00 35.57 O ANISOU 745 OG SER A 92 2752 6046 4716 -875 170 -67 O ATOM 746 N HIS A 93 -7.293 23.522 159.791 1.00 31.75 N ANISOU 746 N HIS A 93 2665 5399 4001 -476 341 -58 N ATOM 747 CA HIS A 93 -6.318 24.499 159.270 1.00 30.39 C ANISOU 747 CA HIS A 93 2667 5078 3802 -277 284 -75 C ATOM 748 C HIS A 93 -5.117 23.846 158.608 1.00 29.06 C ANISOU 748 C HIS A 93 2690 4734 3617 -333 126 -23 C ATOM 749 O HIS A 93 -4.818 22.692 158.871 1.00 29.16 O ANISOU 749 O HIS A 93 2758 4705 3617 -524 85 31 O ATOM 750 CB HIS A 93 -5.786 25.406 160.370 1.00 29.85 C ANISOU 750 CB HIS A 93 2735 4963 3644 -227 436 -118 C ATOM 751 CG HIS A 93 -6.815 26.305 160.961 1.00 31.85 C ANISOU 751 CG HIS A 93 2832 5354 3917 -114 613 -200 C ATOM 752 ND1 HIS A 93 -7.081 27.559 160.459 1.00 32.45 N ANISOU 752 ND1 HIS A 93 2866 5393 4071 140 653 -259 N ATOM 753 CD2 HIS A 93 -7.647 26.132 162.014 1.00 33.44 C ANISOU 753 CD2 HIS A 93 2909 5726 4072 -208 778 -229 C ATOM 754 CE1 HIS A 93 -8.041 28.119 161.174 1.00 34.34 C ANISOU 754 CE1 HIS A 93 2953 5768 4326 209 829 -335 C ATOM 755 NE2 HIS A 93 -8.402 27.273 162.124 1.00 35.00 N ANISOU 755 NE2 HIS A 93 2978 5993 4327 -5 911 -326 N ATOM 756 N THR A 94 -4.408 24.600 157.769 1.00 28.23 N ANISOU 756 N THR A 94 2690 4517 3520 -160 59 -30 N ATOM 757 CA THR A 94 -3.303 24.028 156.999 1.00 26.47 C ANISOU 757 CA THR A 94 2622 4147 3287 -190 -80 8 C ATOM 758 C THR A 94 -2.008 24.776 157.246 1.00 25.04 C ANISOU 758 C THR A 94 2639 3810 3065 -125 -43 7 C ATOM 759 O THR A 94 -2.022 25.994 157.318 1.00 25.27 O ANISOU 759 O THR A 94 2683 3809 3108 21 50 -31 O ATOM 760 CB THR A 94 -3.580 24.054 155.469 1.00 25.82 C ANISOU 760 CB THR A 94 2473 4096 3243 -60 -215 4 C ATOM 761 OG1 THR A 94 -4.930 23.686 155.215 1.00 27.04 O ANISOU 761 OG1 THR A 94 2390 4440 3443 -84 -248 -30 O ATOM 762 CG2 THR A 94 -2.696 23.078 154.744 1.00 25.11 C ANISOU 762 CG2 THR A 94 2501 3898 3143 -144 -348 19 C ATOM 763 N VAL A 95 -0.894 24.064 157.424 1.00 24.21 N ANISOU 763 N VAL A 95 2675 3598 2924 -234 -105 40 N ATOM 764 CA VAL A 95 0.388 24.709 157.180 1.00 23.75 C ANISOU 764 CA VAL A 95 2766 3399 2860 -160 -112 29 C ATOM 765 C VAL A 95 1.188 24.020 156.073 1.00 23.67 C ANISOU 765 C VAL A 95 2826 3295 2873 -154 -239 66 C ATOM 766 O VAL A 95 1.152 22.780 155.921 1.00 23.60 O ANISOU 766 O VAL A 95 2809 3288 2871 -263 -327 95 O ATOM 767 CB VAL A 95 1.287 25.024 158.459 1.00 23.30 C ANISOU 767 CB VAL A 95 2813 3310 2732 -236 -44 -8 C ATOM 768 CG1 VAL A 95 0.506 25.121 159.735 1.00 23.98 C ANISOU 768 CG1 VAL A 95 2839 3529 2744 -305 65 -39 C ATOM 769 CG2 VAL A 95 2.363 24.055 158.614 1.00 22.60 C ANISOU 769 CG2 VAL A 95 2816 3163 2609 -336 -143 44 C ATOM 770 N GLN A 96 1.873 24.841 155.271 1.00 23.41 N ANISOU 770 N GLN A 96 2864 3169 2861 -25 -229 62 N ATOM 771 CA GLN A 96 2.782 24.323 154.265 1.00 22.48 C ANISOU 771 CA GLN A 96 2822 2969 2749 -7 -317 86 C ATOM 772 C GLN A 96 4.204 24.837 154.412 1.00 21.94 C ANISOU 772 C GLN A 96 2866 2775 2696 -2 -274 76 C ATOM 773 O GLN A 96 4.430 26.018 154.651 1.00 22.12 O ANISOU 773 O GLN A 96 2917 2742 2746 56 -167 49 O ATOM 774 CB GLN A 96 2.284 24.643 152.883 1.00 23.04 C ANISOU 774 CB GLN A 96 2861 3080 2815 141 -354 107 C ATOM 775 CG GLN A 96 1.110 23.842 152.483 1.00 25.14 C ANISOU 775 CG GLN A 96 2998 3486 3067 112 -449 89 C ATOM 776 CD GLN A 96 0.178 24.653 151.653 1.00 26.39 C ANISOU 776 CD GLN A 96 3065 3758 3204 293 -452 109 C ATOM 777 OE1 GLN A 96 -0.527 25.513 152.175 1.00 27.30 O ANISOU 777 OE1 GLN A 96 3108 3917 3347 370 -364 118 O ATOM 778 NE2 GLN A 96 0.171 24.406 150.347 1.00 26.59 N ANISOU 778 NE2 GLN A 96 3093 3842 3168 383 -553 115 N ATOM 779 N ARG A 97 5.161 23.933 154.251 1.00 21.55 N ANISOU 779 N ARG A 97 2868 2672 2647 -64 -351 87 N ATOM 780 CA ARG A 97 6.564 24.295 154.247 1.00 21.71 C ANISOU 780 CA ARG A 97 2957 2597 2694 -61 -324 71 C ATOM 781 C ARG A 97 7.136 23.812 152.928 1.00 21.25 C ANISOU 781 C ARG A 97 2934 2490 2649 4 -371 92 C ATOM 782 O ARG A 97 6.786 22.732 152.458 1.00 20.75 O ANISOU 782 O ARG A 97 2861 2454 2570 -13 -462 98 O ATOM 783 CB ARG A 97 7.261 23.601 155.412 1.00 22.16 C ANISOU 783 CB ARG A 97 3023 2668 2728 -177 -375 65 C ATOM 784 CG ARG A 97 8.687 23.948 155.648 1.00 22.12 C ANISOU 784 CG ARG A 97 3043 2612 2752 -191 -366 26 C ATOM 785 CD ARG A 97 9.221 23.026 156.768 1.00 24.25 C ANISOU 785 CD ARG A 97 3307 2939 2968 -275 -458 51 C ATOM 786 NE ARG A 97 9.999 23.849 157.677 1.00 25.64 N ANISOU 786 NE ARG A 97 3465 3158 3118 -320 -429 -33 N ATOM 787 CZ ARG A 97 9.623 24.222 158.893 1.00 25.94 C ANISOU 787 CZ ARG A 97 3495 3299 3062 -383 -407 -78 C ATOM 788 NH1 ARG A 97 10.404 25.046 159.576 1.00 28.10 N ANISOU 788 NH1 ARG A 97 3746 3612 3318 -429 -385 -198 N ATOM 789 NH2 ARG A 97 8.504 23.772 159.429 1.00 25.19 N ANISOU 789 NH2 ARG A 97 3405 3277 2888 -410 -401 -20 N ATOM 790 N MET A 98 7.979 24.631 152.318 1.00 21.09 N ANISOU 790 N MET A 98 2958 2397 2661 71 -291 93 N ATOM 791 CA MET A 98 8.739 24.210 151.167 1.00 21.38 C ANISOU 791 CA MET A 98 3032 2398 2694 128 -307 107 C ATOM 792 C MET A 98 10.147 24.718 151.322 1.00 20.88 C ANISOU 792 C MET A 98 2983 2251 2699 102 -228 85 C ATOM 793 O MET A 98 10.354 25.909 151.565 1.00 22.21 O ANISOU 793 O MET A 98 3160 2362 2918 101 -111 76 O ATOM 794 CB MET A 98 8.151 24.761 149.872 1.00 23.90 C ANISOU 794 CB MET A 98 3378 2746 2956 267 -266 157 C ATOM 795 CG MET A 98 8.737 24.136 148.601 1.00 26.29 C ANISOU 795 CG MET A 98 3723 3060 3205 330 -292 157 C ATOM 796 SD MET A 98 10.279 24.840 147.929 1.00 29.59 S ANISOU 796 SD MET A 98 4200 3380 3664 375 -138 188 S ATOM 797 CE MET A 98 9.904 26.602 148.018 1.00 29.50 C ANISOU 797 CE MET A 98 4224 3294 3693 440 27 277 C ATOM 798 N TYR A 99 11.112 23.824 151.145 1.00 19.13 N ANISOU 798 N TYR A 99 2754 2017 2499 82 -284 66 N ATOM 799 CA TYR A 99 12.503 24.216 151.102 1.00 18.60 C ANISOU 799 CA TYR A 99 2664 1897 2506 64 -211 37 C ATOM 800 C TYR A 99 13.337 23.432 150.084 1.00 20.07 C ANISOU 800 C TYR A 99 2854 2071 2699 126 -218 35 C ATOM 801 O TYR A 99 12.942 22.341 149.631 1.00 20.52 O ANISOU 801 O TYR A 99 2938 2149 2710 164 -309 32 O ATOM 802 CB TYR A 99 13.132 24.167 152.490 1.00 17.79 C ANISOU 802 CB TYR A 99 2496 1818 2444 -40 -263 -16 C ATOM 803 CG TYR A 99 13.311 22.812 153.185 1.00 17.32 C ANISOU 803 CG TYR A 99 2412 1807 2362 -65 -414 -2 C ATOM 804 CD1 TYR A 99 14.259 21.872 152.753 1.00 16.99 C ANISOU 804 CD1 TYR A 99 2346 1744 2366 -18 -464 2 C ATOM 805 CD2 TYR A 99 12.579 22.515 154.340 1.00 17.42 C ANISOU 805 CD2 TYR A 99 2427 1880 2312 -128 -486 19 C ATOM 806 CE1 TYR A 99 14.445 20.670 153.428 1.00 18.29 C ANISOU 806 CE1 TYR A 99 2500 1919 2529 -18 -590 40 C ATOM 807 CE2 TYR A 99 12.752 21.316 155.024 1.00 17.94 C ANISOU 807 CE2 TYR A 99 2488 1971 2356 -144 -604 71 C ATOM 808 CZ TYR A 99 13.683 20.395 154.575 1.00 18.74 C ANISOU 808 CZ TYR A 99 2576 2025 2519 -83 -659 89 C ATOM 809 OH TYR A 99 13.845 19.215 155.275 1.00 18.66 O ANISOU 809 OH TYR A 99 2576 2010 2503 -76 -767 167 O ATOM 810 N GLY A 100 14.502 23.976 149.744 1.00 20.56 N ANISOU 810 N GLY A 100 2884 2096 2831 126 -109 17 N ATOM 811 CA GLY A 100 15.401 23.294 148.842 1.00 21.85 C ANISOU 811 CA GLY A 100 3033 2260 3007 189 -87 1 C ATOM 812 C GLY A 100 16.390 24.200 148.139 1.00 24.22 C ANISOU 812 C GLY A 100 3310 2525 3366 197 98 9 C ATOM 813 O GLY A 100 16.484 25.394 148.451 1.00 23.70 O ANISOU 813 O GLY A 100 3237 2405 3362 133 211 22 O ATOM 814 N CYS A 101 17.112 23.642 147.170 1.00 26.21 N ANISOU 814 N CYS A 101 3555 2796 3606 270 150 -4 N ATOM 815 CA CYS A 101 18.200 24.378 146.548 1.00 29.85 C ANISOU 815 CA CYS A 101 3970 3235 4138 262 346 5 C ATOM 816 C CYS A 101 18.362 24.146 145.025 1.00 31.34 C ANISOU 816 C CYS A 101 4233 3462 4215 384 465 41 C ATOM 817 O CYS A 101 17.919 23.124 144.499 1.00 31.86 O ANISOU 817 O CYS A 101 4353 3581 4170 473 364 6 O ATOM 818 CB CYS A 101 19.498 24.057 147.274 1.00 31.56 C ANISOU 818 CB CYS A 101 4016 3470 4505 193 321 -83 C ATOM 819 SG CYS A 101 19.981 22.345 147.072 1.00 33.98 S ANISOU 819 SG CYS A 101 4277 3827 4806 305 186 -143 S ATOM 820 N ASP A 102 18.993 25.109 144.341 1.00 31.98 N ANISOU 820 N ASP A 102 4317 3513 4321 377 691 105 N ATOM 821 CA ASP A 102 19.225 25.075 142.895 1.00 33.18 C ANISOU 821 CA ASP A 102 4546 3723 4338 491 846 161 C ATOM 822 C ASP A 102 20.715 25.011 142.533 1.00 34.17 C ANISOU 822 C ASP A 102 4546 3863 4575 465 1019 114 C ATOM 823 O ASP A 102 21.549 25.633 143.188 1.00 35.60 O ANISOU 823 O ASP A 102 4593 3983 4948 336 1104 89 O ATOM 824 CB ASP A 102 18.665 26.335 142.223 1.00 34.28 C ANISOU 824 CB ASP A 102 4818 3819 4389 530 1017 330 C ATOM 825 CG ASP A 102 17.170 26.459 142.358 1.00 33.76 C ANISOU 825 CG ASP A 102 4861 3770 4198 595 869 390 C ATOM 826 OD1 ASP A 102 16.545 25.456 142.752 1.00 32.90 O ANISOU 826 OD1 ASP A 102 4734 3725 4041 606 650 293 O ATOM 827 OD2 ASP A 102 16.623 27.553 142.062 1.00 33.90 O ANISOU 827 OD2 ASP A 102 4974 3730 4178 640 983 538 O ATOM 828 N VAL A 103 21.045 24.261 141.483 1.00 33.32 N ANISOU 828 N VAL A 103 4466 3849 4345 583 1074 80 N ATOM 829 CA VAL A 103 22.367 24.324 140.874 1.00 33.65 C ANISOU 829 CA VAL A 103 4401 3928 4458 584 1295 56 C ATOM 830 C VAL A 103 22.300 24.710 139.382 1.00 35.23 C ANISOU 830 C VAL A 103 4743 4203 4439 691 1519 166 C ATOM 831 O VAL A 103 21.253 24.611 138.746 1.00 34.29 O ANISOU 831 O VAL A 103 4797 4147 4086 799 1449 224 O ATOM 832 CB VAL A 103 23.156 23.003 141.031 1.00 33.17 C ANISOU 832 CB VAL A 103 4202 3922 4477 642 1198 -109 C ATOM 833 CG1 VAL A 103 23.378 22.687 142.468 1.00 31.07 C ANISOU 833 CG1 VAL A 103 3791 3606 4408 554 1001 -180 C ATOM 834 CG2 VAL A 103 22.465 21.849 140.330 1.00 31.92 C ANISOU 834 CG2 VAL A 103 4177 3825 4127 790 1076 -184 C ATOM 835 N GLY A 104 23.423 25.146 138.829 1.00 36.80 N ANISOU 835 N GLY A 104 4858 4419 4704 662 1789 196 N ATOM 836 CA GLY A 104 23.473 25.553 137.427 1.00 39.56 C ANISOU 836 CA GLY A 104 5344 4856 4830 763 2038 326 C ATOM 837 C GLY A 104 23.915 24.455 136.472 1.00 40.77 C ANISOU 837 C GLY A 104 5497 5175 4820 906 2077 199 C ATOM 838 O GLY A 104 23.821 23.279 136.794 1.00 40.21 O ANISOU 838 O GLY A 104 5377 5131 4769 959 1864 18 O ATOM 839 N SER A 105 24.410 24.842 135.300 1.00 43.39 N ANISOU 839 N SER A 105 5888 5606 4992 969 2367 295 N ATOM 840 CA SER A 105 24.830 23.886 134.270 1.00 45.62 C ANISOU 840 CA SER A 105 6187 6066 5079 1116 2446 163 C ATOM 841 C SER A 105 26.044 23.079 134.686 1.00 46.39 C ANISOU 841 C SER A 105 6040 6160 5426 1093 2472 -37 C ATOM 842 O SER A 105 26.187 21.910 134.316 1.00 47.10 O ANISOU 842 O SER A 105 6120 6334 5440 1220 2399 -229 O ATOM 843 CB SER A 105 25.175 24.617 132.977 1.00 48.46 C ANISOU 843 CB SER A 105 6659 6546 5207 1179 2793 340 C ATOM 844 OG SER A 105 24.009 24.947 132.259 1.00 48.77 O ANISOU 844 OG SER A 105 6948 6677 4906 1298 2733 487 O ATOM 845 N ASP A 106 26.908 23.723 135.464 1.00 46.66 N ANISOU 845 N ASP A 106 5869 6094 5767 934 2575 -2 N ATOM 846 CA ASP A 106 28.133 23.121 135.938 1.00 47.55 C ANISOU 846 CA ASP A 106 5702 6223 6141 910 2601 -169 C ATOM 847 C ASP A 106 27.957 22.519 137.321 1.00 45.08 C ANISOU 847 C ASP A 106 5271 5814 6042 868 2265 -282 C ATOM 848 O ASP A 106 28.921 22.058 137.915 1.00 46.96 O ANISOU 848 O ASP A 106 5261 6066 6515 856 2235 -401 O ATOM 849 CB ASP A 106 29.261 24.159 135.948 1.00 50.23 C ANISOU 849 CB ASP A 106 5847 6549 6691 749 2913 -85 C ATOM 850 CG ASP A 106 28.945 25.398 136.805 1.00 49.77 C ANISOU 850 CG ASP A 106 5790 6324 6798 541 2896 49 C ATOM 851 OD1 ASP A 106 29.858 26.246 136.912 1.00 51.78 O ANISOU 851 OD1 ASP A 106 5871 6538 7265 373 3140 89 O ATOM 852 OD2 ASP A 106 27.825 25.551 137.369 1.00 47.45 O ANISOU 852 OD2 ASP A 106 5655 5935 6439 533 2660 100 O ATOM 853 N TRP A 107 26.725 22.571 137.820 1.00 41.85 N ANISOU 853 N TRP A 107 5034 5324 5544 851 2026 -230 N ATOM 854 CA TRP A 107 26.322 22.124 139.163 1.00 39.48 C ANISOU 854 CA TRP A 107 4672 4932 5396 800 1713 -292 C ATOM 855 C TRP A 107 26.891 22.937 140.327 1.00 40.02 C ANISOU 855 C TRP A 107 4545 4937 5726 617 1700 -269 C ATOM 856 O TRP A 107 26.952 22.442 141.444 1.00 39.16 O ANISOU 856 O TRP A 107 4322 4802 5754 592 1469 -344 O ATOM 857 CB TRP A 107 26.545 20.619 139.439 1.00 38.26 C ANISOU 857 CB TRP A 107 4448 4789 5302 933 1523 -462 C ATOM 858 CG TRP A 107 25.904 19.645 138.504 1.00 38.48 C ANISOU 858 CG TRP A 107 4662 4850 5109 1092 1479 -549 C ATOM 859 CD1 TRP A 107 25.001 19.906 137.503 1.00 38.61 C ANISOU 859 CD1 TRP A 107 4902 4929 4838 1137 1534 -498 C ATOM 860 CD2 TRP A 107 26.093 18.228 138.504 1.00 38.99 C ANISOU 860 CD2 TRP A 107 4702 4887 5224 1230 1360 -720 C ATOM 861 NE1 TRP A 107 24.649 18.744 136.865 1.00 38.82 N ANISOU 861 NE1 TRP A 107 5033 4990 4727 1273 1454 -659 N ATOM 862 CE2 TRP A 107 25.299 17.697 137.461 1.00 39.21 C ANISOU 862 CE2 TRP A 107 4944 4959 4996 1329 1358 -799 C ATOM 863 CE3 TRP A 107 26.865 17.353 139.278 1.00 39.31 C ANISOU 863 CE3 TRP A 107 4563 4868 5507 1292 1255 -813 C ATOM 864 CZ2 TRP A 107 25.251 16.326 137.175 1.00 40.39 C ANISOU 864 CZ2 TRP A 107 5139 5061 5146 1461 1270 -994 C ATOM 865 CZ3 TRP A 107 26.813 15.979 138.992 1.00 40.50 C ANISOU 865 CZ3 TRP A 107 4771 4955 5665 1452 1173 -970 C ATOM 866 CH2 TRP A 107 26.014 15.484 137.948 1.00 40.66 C ANISOU 866 CH2 TRP A 107 5011 4988 5448 1522 1191 -1072 C ATOM 867 N ARG A 108 27.308 24.176 140.091 1.00 42.49 N ANISOU 867 N ARG A 108 4820 5221 6103 483 1947 -171 N ATOM 868 CA ARG A 108 27.659 25.035 141.214 1.00 43.45 C ANISOU 868 CA ARG A 108 4784 5265 6459 281 1919 -179 C ATOM 869 C ARG A 108 26.349 25.582 141.772 1.00 41.37 C ANISOU 869 C ARG A 108 4722 4887 6109 234 1766 -91 C ATOM 870 O ARG A 108 25.372 25.714 141.031 1.00 41.92 O ANISOU 870 O ARG A 108 5029 4936 5962 327 1792 25 O ATOM 871 CB ARG A 108 28.617 26.168 140.807 1.00 47.78 C ANISOU 871 CB ARG A 108 5206 5790 7160 125 2259 -128 C ATOM 872 CG ARG A 108 29.966 25.671 140.249 1.00 53.19 C ANISOU 872 CG ARG A 108 5652 6612 7947 165 2442 -222 C ATOM 873 CD ARG A 108 31.144 26.668 140.371 1.00 57.68 C ANISOU 873 CD ARG A 108 5963 7170 8783 -57 2711 -242 C ATOM 874 NE ARG A 108 30.745 28.074 140.285 1.00 60.34 N ANISOU 874 NE ARG A 108 6442 7330 9155 -236 2908 -95 N ATOM 875 CZ ARG A 108 30.800 28.818 139.180 1.00 63.30 C ANISOU 875 CZ ARG A 108 6953 7647 9449 -253 3259 81 C ATOM 876 NH1 ARG A 108 30.412 30.096 139.211 1.00 64.43 N ANISOU 876 NH1 ARG A 108 7235 7588 9657 -405 3428 227 N ATOM 877 NH2 ARG A 108 31.235 28.288 138.046 1.00 65.05 N ANISOU 877 NH2 ARG A 108 7187 8009 9521 -109 3453 116 N ATOM 878 N PHE A 109 26.331 25.850 143.076 1.00 39.15 N ANISOU 878 N PHE A 109 4333 4558 5984 103 1597 -157 N ATOM 879 CA PHE A 109 25.210 26.444 143.802 1.00 36.26 C ANISOU 879 CA PHE A 109 4113 4087 5577 38 1467 -105 C ATOM 880 C PHE A 109 24.608 27.665 143.096 1.00 37.23 C ANISOU 880 C PHE A 109 4427 4084 5634 8 1692 60 C ATOM 881 O PHE A 109 25.338 28.487 142.551 1.00 39.64 O ANISOU 881 O PHE A 109 4688 4335 6040 -78 1972 115 O ATOM 882 CB PHE A 109 25.727 26.857 145.182 1.00 35.35 C ANISOU 882 CB PHE A 109 3800 3961 5671 -141 1361 -226 C ATOM 883 CG PHE A 109 24.715 27.534 146.053 1.00 32.50 C ANISOU 883 CG PHE A 109 3559 3499 5292 -224 1251 -209 C ATOM 884 CD1 PHE A 109 23.697 26.806 146.640 1.00 30.14 C ANISOU 884 CD1 PHE A 109 3366 3232 4856 -136 995 -206 C ATOM 885 CD2 PHE A 109 24.810 28.889 146.322 1.00 33.53 C ANISOU 885 CD2 PHE A 109 3686 3494 5562 -398 1421 -211 C ATOM 886 CE1 PHE A 109 22.765 27.413 147.466 1.00 29.00 C ANISOU 886 CE1 PHE A 109 3314 3013 4691 -205 910 -201 C ATOM 887 CE2 PHE A 109 23.890 29.505 147.141 1.00 33.07 C ANISOU 887 CE2 PHE A 109 3734 3339 5494 -460 1333 -220 C ATOM 888 CZ PHE A 109 22.852 28.753 147.721 1.00 30.38 C ANISOU 888 CZ PHE A 109 3490 3061 4993 -355 1073 -215 C ATOM 889 N LEU A 110 23.283 27.765 143.085 1.00 35.24 N ANISOU 889 N LEU A 110 4383 3787 5221 88 1580 150 N ATOM 890 CA LEU A 110 22.634 28.948 142.571 1.00 36.36 C ANISOU 890 CA LEU A 110 4702 3799 5313 89 1762 322 C ATOM 891 C LEU A 110 21.920 29.718 143.674 1.00 36.39 C ANISOU 891 C LEU A 110 4738 3669 5420 -13 1671 304 C ATOM 892 O LEU A 110 22.101 30.931 143.808 1.00 37.82 O ANISOU 892 O LEU A 110 4937 3681 5754 -130 1868 352 O ATOM 893 CB LEU A 110 21.633 28.581 141.490 1.00 36.22 C ANISOU 893 CB LEU A 110 4895 3862 5006 297 1734 456 C ATOM 894 CG LEU A 110 21.796 29.133 140.075 1.00 38.61 C ANISOU 894 CG LEU A 110 5329 4177 5164 392 2014 642 C ATOM 895 CD1 LEU A 110 23.151 28.866 139.492 1.00 40.75 C ANISOU 895 CD1 LEU A 110 5468 4518 5497 354 2219 594 C ATOM 896 CD2 LEU A 110 20.749 28.484 139.227 1.00 38.44 C ANISOU 896 CD2 LEU A 110 5475 4305 4826 601 1880 703 C ATOM 897 N ARG A 111 21.139 29.005 144.481 1.00 34.66 N ANISOU 897 N ARG A 111 4524 3515 5130 25 1390 225 N ATOM 898 CA ARG A 111 20.121 29.638 145.297 1.00 34.48 C ANISOU 898 CA ARG A 111 4581 3396 5122 -8 1306 235 C ATOM 899 C ARG A 111 19.599 28.607 146.276 1.00 31.66 C ANISOU 899 C ARG A 111 4174 3151 4706 3 1008 123 C ATOM 900 O ARG A 111 19.613 27.424 145.993 1.00 30.38 O ANISOU 900 O ARG A 111 3995 3108 4441 93 873 98 O ATOM 901 CB ARG A 111 18.972 30.056 144.371 1.00 36.39 C ANISOU 901 CB ARG A 111 5034 3605 5190 157 1370 425 C ATOM 902 CG ARG A 111 18.111 31.229 144.794 1.00 38.39 C ANISOU 902 CG ARG A 111 5389 3693 5504 147 1435 499 C ATOM 903 CD ARG A 111 17.148 31.625 143.669 1.00 40.26 C ANISOU 903 CD ARG A 111 5813 3926 5556 352 1513 722 C ATOM 904 NE ARG A 111 16.978 30.560 142.682 1.00 41.62 N ANISOU 904 NE ARG A 111 6018 4307 5488 499 1412 757 N ATOM 905 CZ ARG A 111 17.253 30.683 141.374 1.00 44.19 C ANISOU 905 CZ ARG A 111 6436 4684 5668 614 1576 906 C ATOM 906 NH1 ARG A 111 17.080 29.643 140.555 1.00 44.03 N ANISOU 906 NH1 ARG A 111 6439 4871 5417 738 1463 884 N ATOM 907 NH2 ARG A 111 17.704 31.839 140.885 1.00 45.74 N ANISOU 907 NH2 ARG A 111 6709 4722 5948 601 1865 1072 N ATOM 908 N GLY A 112 19.115 29.062 147.417 1.00 30.85 N ANISOU 908 N GLY A 112 4058 2997 4666 -87 922 56 N ATOM 909 CA GLY A 112 18.456 28.184 148.372 1.00 29.81 C ANISOU 909 CA GLY A 112 3906 2966 4456 -75 667 -12 C ATOM 910 C GLY A 112 17.216 28.908 148.835 1.00 30.45 C ANISOU 910 C GLY A 112 4093 2976 4501 -66 659 23 C ATOM 911 O GLY A 112 17.098 30.115 148.634 1.00 32.89 O ANISOU 911 O GLY A 112 4465 3142 4891 -88 841 68 O ATOM 912 N TYR A 113 16.258 28.189 149.404 1.00 29.07 N ANISOU 912 N TYR A 113 3940 2887 4216 -24 469 13 N ATOM 913 CA TYR A 113 14.999 28.824 149.803 1.00 28.65 C ANISOU 913 CA TYR A 113 3968 2792 4125 5 468 45 C ATOM 914 C TYR A 113 14.330 28.026 150.914 1.00 26.83 C ANISOU 914 C TYR A 113 3700 2672 3823 -30 269 -20 C ATOM 915 O TYR A 113 14.547 26.820 151.044 1.00 25.11 O ANISOU 915 O TYR A 113 3439 2552 3550 -26 123 -33 O ATOM 916 CB TYR A 113 14.028 29.025 148.598 1.00 29.61 C ANISOU 916 CB TYR A 113 4210 2903 4136 175 524 199 C ATOM 917 CG TYR A 113 14.200 28.021 147.487 1.00 30.00 C ANISOU 917 CG TYR A 113 4279 3057 4064 272 468 250 C ATOM 918 CD1 TYR A 113 13.606 26.782 147.575 1.00 30.10 C ANISOU 918 CD1 TYR A 113 4275 3191 3972 302 274 213 C ATOM 919 CD2 TYR A 113 14.968 28.305 146.360 1.00 31.40 C ANISOU 919 CD2 TYR A 113 4493 3204 4233 324 627 323 C ATOM 920 CE1 TYR A 113 13.770 25.848 146.584 1.00 31.06 C ANISOU 920 CE1 TYR A 113 4417 3391 3992 381 227 218 C ATOM 921 CE2 TYR A 113 15.158 27.375 145.369 1.00 32.09 C ANISOU 921 CE2 TYR A 113 4599 3400 4193 414 585 337 C ATOM 922 CZ TYR A 113 14.557 26.138 145.485 1.00 32.33 C ANISOU 922 CZ TYR A 113 4614 3542 4128 443 378 269 C ATOM 923 OH TYR A 113 14.705 25.170 144.503 1.00 34.00 O ANISOU 923 OH TYR A 113 4851 3849 4219 527 334 242 O ATOM 924 N HIS A 114 13.526 28.715 151.715 1.00 25.98 N ANISOU 924 N HIS A 114 3614 2536 3722 -58 285 -54 N ATOM 925 CA HIS A 114 12.721 28.075 152.740 1.00 24.75 C ANISOU 925 CA HIS A 114 3435 2491 3478 -86 137 -92 C ATOM 926 C HIS A 114 11.527 28.973 152.918 1.00 25.58 C ANISOU 926 C HIS A 114 3593 2549 3579 -33 217 -76 C ATOM 927 O HIS A 114 11.665 30.100 153.381 1.00 26.45 O ANISOU 927 O HIS A 114 3715 2553 3783 -80 343 -150 O ATOM 928 CB HIS A 114 13.497 27.962 154.051 1.00 23.90 C ANISOU 928 CB HIS A 114 3243 2447 3391 -224 67 -221 C ATOM 929 CG HIS A 114 12.724 27.333 155.163 1.00 22.57 C ANISOU 929 CG HIS A 114 3064 2402 3109 -255 -62 -238 C ATOM 930 ND1 HIS A 114 11.806 28.026 155.926 1.00 23.26 N ANISOU 930 ND1 HIS A 114 3175 2499 3165 -276 -11 -291 N ATOM 931 CD2 HIS A 114 12.757 26.078 155.665 1.00 22.27 C ANISOU 931 CD2 HIS A 114 2998 2478 2984 -266 -218 -199 C ATOM 932 CE1 HIS A 114 11.291 27.216 156.835 1.00 23.55 C ANISOU 932 CE1 HIS A 114 3195 2671 3084 -307 -126 -280 C ATOM 933 NE2 HIS A 114 11.864 26.031 156.708 1.00 22.81 N ANISOU 933 NE2 HIS A 114 3077 2632 2959 -305 -253 -214 N ATOM 934 N GLN A 115 10.351 28.500 152.532 1.00 26.00 N ANISOU 934 N GLN A 115 3665 2674 3539 67 150 6 N ATOM 935 CA GLN A 115 9.167 29.354 152.624 1.00 28.08 C ANISOU 935 CA GLN A 115 3953 2909 3807 152 226 31 C ATOM 936 C GLN A 115 8.133 28.629 153.444 1.00 26.90 C ANISOU 936 C GLN A 115 3746 2904 3571 124 111 4 C ATOM 937 O GLN A 115 8.094 27.399 153.455 1.00 26.38 O ANISOU 937 O GLN A 115 3649 2940 3435 82 -25 22 O ATOM 938 CB GLN A 115 8.587 29.672 151.242 1.00 30.28 C ANISOU 938 CB GLN A 115 4284 3166 4056 330 274 173 C ATOM 939 CG GLN A 115 9.485 30.443 150.296 1.00 33.79 C ANISOU 939 CG GLN A 115 4805 3465 4569 378 426 247 C ATOM 940 CD GLN A 115 9.051 30.273 148.846 1.00 36.34 C ANISOU 940 CD GLN A 115 5179 3850 4779 554 414 400 C ATOM 941 OE1 GLN A 115 7.899 29.914 148.574 1.00 38.01 O ANISOU 941 OE1 GLN A 115 5360 4193 4887 659 308 442 O ATOM 942 NE2 GLN A 115 9.965 30.531 147.907 1.00 37.47 N ANISOU 942 NE2 GLN A 115 5386 3921 4929 583 524 477 N ATOM 943 N TYR A 116 7.280 29.384 154.116 1.00 26.78 N ANISOU 943 N TYR A 116 3718 2884 3573 147 185 -38 N ATOM 944 CA TYR A 116 6.343 28.782 155.049 1.00 26.38 C ANISOU 944 CA TYR A 116 3602 2979 3443 98 113 -72 C ATOM 945 C TYR A 116 4.997 29.488 154.958 1.00 26.99 C ANISOU 945 C TYR A 116 3643 3075 3536 227 190 -50 C ATOM 946 O TYR A 116 4.935 30.710 154.903 1.00 29.03 O ANISOU 946 O TYR A 116 3942 3204 3882 312 332 -71 O ATOM 947 CB TYR A 116 6.921 28.884 156.452 1.00 25.99 C ANISOU 947 CB TYR A 116 3547 2955 3372 -46 124 -200 C ATOM 948 CG TYR A 116 6.227 28.097 157.518 1.00 26.04 C ANISOU 948 CG TYR A 116 3503 3126 3264 -123 56 -214 C ATOM 949 CD1 TYR A 116 5.155 28.631 158.230 1.00 27.66 C ANISOU 949 CD1 TYR A 116 3673 3394 3444 -101 145 -269 C ATOM 950 CD2 TYR A 116 6.688 26.852 157.877 1.00 25.66 C ANISOU 950 CD2 TYR A 116 3446 3163 3139 -215 -75 -169 C ATOM 951 CE1 TYR A 116 4.533 27.920 159.240 1.00 27.76 C ANISOU 951 CE1 TYR A 116 3640 3569 3341 -183 112 -271 C ATOM 952 CE2 TYR A 116 6.080 26.134 158.884 1.00 26.28 C ANISOU 952 CE2 TYR A 116 3496 3379 3109 -291 -113 -150 C ATOM 953 CZ TYR A 116 5.005 26.669 159.564 1.00 27.18 C ANISOU 953 CZ TYR A 116 3573 3571 3183 -284 -15 -200 C ATOM 954 OH TYR A 116 4.406 25.945 160.564 1.00 27.51 O ANISOU 954 OH TYR A 116 3586 3759 3106 -368 -26 -167 O ATOM 955 N ALA A 117 3.921 28.719 154.983 1.00 26.02 N ANISOU 955 N ALA A 117 3435 3106 3346 239 106 -13 N ATOM 956 CA ALA A 117 2.589 29.279 154.809 1.00 26.77 C ANISOU 956 CA ALA A 117 3453 3260 3459 380 159 12 C ATOM 957 C ALA A 117 1.584 28.784 155.845 1.00 26.99 C ANISOU 957 C ALA A 117 3369 3448 3437 301 150 -41 C ATOM 958 O ALA A 117 1.663 27.631 156.276 1.00 26.28 O ANISOU 958 O ALA A 117 3254 3450 3282 154 57 -38 O ATOM 959 CB ALA A 117 2.095 28.910 153.470 1.00 26.98 C ANISOU 959 CB ALA A 117 3442 3354 3456 504 65 119 C ATOM 960 N TYR A 118 0.624 29.635 156.206 1.00 27.11 N ANISOU 960 N TYR A 118 3317 3491 3493 409 263 -77 N ATOM 961 CA TYR A 118 -0.499 29.220 157.053 1.00 27.63 C ANISOU 961 CA TYR A 118 3246 3735 3517 356 282 -117 C ATOM 962 C TYR A 118 -1.829 29.571 156.386 1.00 28.86 C ANISOU 962 C TYR A 118 3250 3993 3722 542 290 -70 C ATOM 963 O TYR A 118 -2.036 30.722 155.992 1.00 29.59 O ANISOU 963 O TYR A 118 3360 3988 3894 741 384 -55 O ATOM 964 CB TYR A 118 -0.415 29.865 158.442 1.00 28.20 C ANISOU 964 CB TYR A 118 3350 3796 3570 294 428 -249 C ATOM 965 CG TYR A 118 -1.518 29.467 159.418 1.00 29.39 C ANISOU 965 CG TYR A 118 3368 4145 3656 232 486 -291 C ATOM 966 CD1 TYR A 118 -1.695 28.148 159.807 1.00 28.84 C ANISOU 966 CD1 TYR A 118 3247 4215 3494 60 400 -235 C ATOM 967 CD2 TYR A 118 -2.369 30.425 159.964 1.00 31.29 C ANISOU 967 CD2 TYR A 118 3536 4416 3938 347 651 -384 C ATOM 968 CE1 TYR A 118 -2.686 27.796 160.701 1.00 30.07 C ANISOU 968 CE1 TYR A 118 3283 4549 3594 -13 484 -256 C ATOM 969 CE2 TYR A 118 -3.361 30.086 160.854 1.00 32.16 C ANISOU 969 CE2 TYR A 118 3512 4722 3984 290 730 -425 C ATOM 970 CZ TYR A 118 -3.516 28.773 161.225 1.00 32.07 C ANISOU 970 CZ TYR A 118 3452 4861 3874 101 651 -355 C ATOM 971 OH TYR A 118 -4.514 28.434 162.123 1.00 34.16 O ANISOU 971 OH TYR A 118 3582 5322 4076 29 760 -380 O ATOM 972 N ASP A 119 -2.695 28.562 156.262 1.00 28.84 N ANISOU 972 N ASP A 119 3095 4179 3684 473 193 -44 N ATOM 973 CA ASP A 119 -4.025 28.649 155.661 1.00 30.42 C ANISOU 973 CA ASP A 119 3092 4545 3920 617 160 -16 C ATOM 974 C ASP A 119 -4.066 29.237 154.251 1.00 31.47 C ANISOU 974 C ASP A 119 3236 4649 4073 853 88 76 C ATOM 975 O ASP A 119 -4.955 30.035 153.930 1.00 34.23 O ANISOU 975 O ASP A 119 3469 5065 4472 1076 129 107 O ATOM 976 CB ASP A 119 -4.999 29.397 156.584 1.00 32.44 C ANISOU 976 CB ASP A 119 3221 4881 4224 696 325 -86 C ATOM 977 CG ASP A 119 -5.555 28.518 157.683 1.00 32.57 C ANISOU 977 CG ASP A 119 3125 5058 4193 481 367 -143 C ATOM 978 OD1 ASP A 119 -5.483 27.275 157.550 1.00 31.64 O ANISOU 978 OD1 ASP A 119 2982 5003 4035 293 250 -109 O ATOM 979 OD2 ASP A 119 -6.070 29.079 158.670 1.00 33.55 O ANISOU 979 OD2 ASP A 119 3192 5233 4323 504 533 -222 O ATOM 980 N GLY A 120 -3.096 28.865 153.421 1.00 30.28 N ANISOU 980 N GLY A 120 3224 4405 3875 823 -11 130 N ATOM 981 CA GLY A 120 -3.023 29.377 152.059 1.00 30.09 C ANISOU 981 CA GLY A 120 3240 4366 3827 1041 -70 237 C ATOM 982 C GLY A 120 -2.134 30.568 151.790 1.00 30.18 C ANISOU 982 C GLY A 120 3444 4136 3887 1181 62 310 C ATOM 983 O GLY A 120 -1.623 30.708 150.697 1.00 30.83 O ANISOU 983 O GLY A 120 3622 4172 3919 1284 19 412 O ATOM 984 N LYS A 121 -1.953 31.447 152.763 1.00 30.81 N ANISOU 984 N LYS A 121 3583 4059 4063 1179 238 250 N ATOM 985 CA LYS A 121 -1.226 32.687 152.495 1.00 31.83 C ANISOU 985 CA LYS A 121 3884 3929 4282 1309 391 308 C ATOM 986 C LYS A 121 0.209 32.562 152.967 1.00 29.99 C ANISOU 986 C LYS A 121 3807 3523 4064 1095 437 232 C ATOM 987 O LYS A 121 0.506 31.708 153.774 1.00 28.55 O ANISOU 987 O LYS A 121 3598 3419 3831 881 376 129 O ATOM 988 CB LYS A 121 -1.899 33.894 153.166 1.00 34.31 C ANISOU 988 CB LYS A 121 4171 4139 4725 1464 574 265 C ATOM 989 CG LYS A 121 -3.409 33.987 152.995 1.00 37.04 C ANISOU 989 CG LYS A 121 4308 4693 5075 1669 537 306 C ATOM 990 CD LYS A 121 -4.123 33.579 154.296 1.00 38.16 C ANISOU 990 CD LYS A 121 4296 4983 5219 1527 577 140 C ATOM 991 CE LYS A 121 -4.098 34.707 155.303 1.00 40.14 C ANISOU 991 CE LYS A 121 4616 5045 5592 1576 808 20 C ATOM 992 NZ LYS A 121 -5.039 35.800 154.877 1.00 43.22 N ANISOU 992 NZ LYS A 121 4932 5386 6105 1916 910 100 N ATOM 993 N ASP A 122 1.087 33.407 152.438 1.00 30.70 N ANISOU 993 N ASP A 122 4051 3387 4228 1160 548 297 N ATOM 994 CA ASP A 122 2.456 33.563 152.929 1.00 30.04 C ANISOU 994 CA ASP A 122 4089 3123 4200 970 624 205 C ATOM 995 C ASP A 122 2.476 33.817 154.432 1.00 29.84 C ANISOU 995 C ASP A 122 4043 3071 4222 824 704 5 C ATOM 996 O ASP A 122 1.670 34.597 154.915 1.00 32.44 O ANISOU 996 O ASP A 122 4341 3362 4623 933 820 -45 O ATOM 997 CB ASP A 122 3.106 34.759 152.226 1.00 31.78 C ANISOU 997 CB ASP A 122 4455 3073 4546 1085 796 301 C ATOM 998 CG ASP A 122 3.808 34.366 150.962 1.00 32.07 C ANISOU 998 CG ASP A 122 4560 3116 4508 1114 738 453 C ATOM 999 OD1 ASP A 122 4.366 35.245 150.285 1.00 33.45 O ANISOU 999 OD1 ASP A 122 4858 3083 4767 1201 888 566 O ATOM 1000 OD2 ASP A 122 3.822 33.157 150.653 1.00 31.55 O ANISOU 1000 OD2 ASP A 122 4430 3256 4302 1044 557 454 O ATOM 1001 N TYR A 123 3.345 33.127 155.169 1.00 27.17 N ANISOU 1001 N TYR A 123 3715 2780 3827 597 638 -107 N ATOM 1002 CA TYR A 123 3.526 33.399 156.589 1.00 26.76 C ANISOU 1002 CA TYR A 123 3660 2728 3779 454 707 -303 C ATOM 1003 C TYR A 123 4.925 33.951 156.819 1.00 26.95 C ANISOU 1003 C TYR A 123 3781 2573 3887 320 777 -410 C ATOM 1004 O TYR A 123 5.078 35.117 157.125 1.00 28.47 O ANISOU 1004 O TYR A 123 4034 2572 4213 335 946 -519 O ATOM 1005 CB TYR A 123 3.279 32.155 157.461 1.00 26.28 C ANISOU 1005 CB TYR A 123 3514 2912 3559 305 569 -347 C ATOM 1006 CG TYR A 123 3.355 32.450 158.951 1.00 26.99 C ANISOU 1006 CG TYR A 123 3604 3053 3599 181 641 -539 C ATOM 1007 CD1 TYR A 123 2.323 33.108 159.600 1.00 28.78 C ANISOU 1007 CD1 TYR A 123 3784 3310 3840 261 772 -630 C ATOM 1008 CD2 TYR A 123 4.466 32.081 159.698 1.00 26.72 C ANISOU 1008 CD2 TYR A 123 3606 3058 3489 -2 577 -638 C ATOM 1009 CE1 TYR A 123 2.401 33.405 160.948 1.00 30.33 C ANISOU 1009 CE1 TYR A 123 3991 3573 3962 152 849 -828 C ATOM 1010 CE2 TYR A 123 4.558 32.369 161.036 1.00 27.99 C ANISOU 1010 CE2 TYR A 123 3769 3302 3565 -108 629 -824 C ATOM 1011 CZ TYR A 123 3.520 33.019 161.663 1.00 29.96 C ANISOU 1011 CZ TYR A 123 3990 3582 3811 -37 769 -924 C ATOM 1012 OH TYR A 123 3.610 33.306 163.001 1.00 31.66 O ANISOU 1012 OH TYR A 123 4216 3904 3911 -142 829 -1131 O ATOM 1013 N ILE A 124 5.946 33.111 156.667 1.00 25.41 N ANISOU 1013 N ILE A 124 3588 2437 3632 186 654 -392 N ATOM 1014 CA ILE A 124 7.334 33.577 156.759 1.00 25.51 C ANISOU 1014 CA ILE A 124 3650 2305 3735 55 709 -490 C ATOM 1015 C ILE A 124 8.220 32.983 155.645 1.00 24.85 C ANISOU 1015 C ILE A 124 3581 2203 3656 53 638 -352 C ATOM 1016 O ILE A 124 8.082 31.815 155.277 1.00 23.96 O ANISOU 1016 O ILE A 124 3430 2247 3428 67 483 -254 O ATOM 1017 CB ILE A 124 7.929 33.355 158.206 1.00 25.28 C ANISOU 1017 CB ILE A 124 3581 2397 3627 -142 652 -703 C ATOM 1018 CG1 ILE A 124 9.329 33.963 158.340 1.00 26.16 C ANISOU 1018 CG1 ILE A 124 3707 2377 3855 -288 708 -844 C ATOM 1019 CG2 ILE A 124 7.961 31.896 158.592 1.00 22.91 C ANISOU 1019 CG2 ILE A 124 3218 2341 3145 -208 450 -641 C ATOM 1020 CD1 ILE A 124 9.581 34.645 159.656 1.00 27.46 C ANISOU 1020 CD1 ILE A 124 3860 2554 4018 -427 764 -1118 C ATOM 1021 N ALA A 125 9.099 33.791 155.068 1.00 26.15 N ANISOU 1021 N ALA A 125 3805 2166 3966 35 770 -349 N ATOM 1022 CA ALA A 125 10.061 33.262 154.104 1.00 25.72 C ANISOU 1022 CA ALA A 125 3753 2108 3912 17 731 -245 C ATOM 1023 C ALA A 125 11.479 33.769 154.331 1.00 26.74 C ANISOU 1023 C ALA A 125 3865 2117 4176 -153 819 -372 C ATOM 1024 O ALA A 125 11.704 34.935 154.656 1.00 28.61 O ANISOU 1024 O ALA A 125 4140 2160 4571 -214 989 -481 O ATOM 1025 CB ALA A 125 9.617 33.553 152.675 1.00 25.79 C ANISOU 1025 CB ALA A 125 3839 2032 3929 211 809 -29 C ATOM 1026 N LEU A 126 12.421 32.854 154.151 1.00 26.05 N ANISOU 1026 N LEU A 126 3710 2148 4040 -229 702 -367 N ATOM 1027 CA LEU A 126 13.849 33.123 154.158 1.00 26.75 C ANISOU 1027 CA LEU A 126 3738 2173 4253 -380 762 -465 C ATOM 1028 C LEU A 126 14.239 33.886 152.890 1.00 28.37 C ANISOU 1028 C LEU A 126 4018 2168 4593 -325 973 -331 C ATOM 1029 O LEU A 126 13.901 33.451 151.800 1.00 27.75 O ANISOU 1029 O LEU A 126 3997 2119 4429 -173 966 -139 O ATOM 1030 CB LEU A 126 14.585 31.778 154.205 1.00 23.92 C ANISOU 1030 CB LEU A 126 3278 2020 3791 -416 569 -458 C ATOM 1031 CG LEU A 126 16.093 31.826 154.413 1.00 24.82 C ANISOU 1031 CG LEU A 126 3268 2149 4013 -570 576 -583 C ATOM 1032 CD1 LEU A 126 16.420 32.438 155.781 1.00 25.03 C ANISOU 1032 CD1 LEU A 126 3220 2208 4082 -741 556 -825 C ATOM 1033 CD2 LEU A 126 16.657 30.445 154.294 1.00 23.17 C ANISOU 1033 CD2 LEU A 126 2973 2126 3706 -537 393 -532 C ATOM 1034 N LYS A 127 14.956 35.002 153.026 1.00 31.14 N ANISOU 1034 N LYS A 127 4371 2313 5148 -455 1166 -435 N ATOM 1035 CA LYS A 127 15.402 35.790 151.865 1.00 34.35 C ANISOU 1035 CA LYS A 127 4859 2494 5699 -422 1406 -288 C ATOM 1036 C LYS A 127 16.523 35.114 151.078 1.00 35.32 C ANISOU 1036 C LYS A 127 4901 2710 5809 -464 1399 -223 C ATOM 1037 O LYS A 127 17.126 34.160 151.568 1.00 34.64 O ANISOU 1037 O LYS A 127 4677 2831 5653 -542 1216 -333 O ATOM 1038 CB LYS A 127 15.858 37.182 152.299 1.00 36.94 C ANISOU 1038 CB LYS A 127 5210 2539 6288 -582 1639 -435 C ATOM 1039 CG LYS A 127 14.722 38.118 152.581 1.00 38.32 C ANISOU 1039 CG LYS A 127 5518 2521 6522 -472 1751 -424 C ATOM 1040 CD LYS A 127 15.178 39.550 152.539 1.00 42.19 C ANISOU 1040 CD LYS A 127 6082 2640 7307 -586 2050 -490 C ATOM 1041 CE LYS A 127 13.984 40.450 152.334 1.00 44.27 C ANISOU 1041 CE LYS A 127 6517 2671 7635 -377 2201 -361 C ATOM 1042 NZ LYS A 127 14.090 41.648 153.186 1.00 48.04 N ANISOU 1042 NZ LYS A 127 7031 2854 8367 -525 2388 -607 N ATOM 1043 N GLU A 128 16.810 35.626 149.878 1.00 38.00 N ANISOU 1043 N GLU A 128 5327 2896 6214 -400 1613 -38 N ATOM 1044 CA GLU A 128 17.854 35.058 148.997 1.00 39.98 C ANISOU 1044 CA GLU A 128 5509 3233 6449 -421 1654 33 C ATOM 1045 C GLU A 128 19.281 35.123 149.565 1.00 41.01 C ANISOU 1045 C GLU A 128 5446 3376 6759 -670 1689 -177 C ATOM 1046 O GLU A 128 20.117 34.296 149.220 1.00 40.57 O ANISOU 1046 O GLU A 128 5269 3482 6663 -685 1627 -184 O ATOM 1047 CB GLU A 128 17.832 35.695 147.596 1.00 43.20 C ANISOU 1047 CB GLU A 128 6066 3482 6867 -298 1909 293 C ATOM 1048 CG GLU A 128 17.956 34.668 146.446 1.00 44.70 C ANISOU 1048 CG GLU A 128 6269 3876 6840 -145 1846 448 C ATOM 1049 CD GLU A 128 18.796 35.169 145.244 1.00 48.93 C ANISOU 1049 CD GLU A 128 6854 4307 7429 -145 2136 617 C ATOM 1050 OE1 GLU A 128 19.660 36.075 145.422 1.00 52.22 O ANISOU 1050 OE1 GLU A 128 7225 4521 8096 -334 2367 565 O ATOM 1051 OE2 GLU A 128 18.606 34.644 144.116 1.00 49.05 O ANISOU 1051 OE2 GLU A 128 6951 4454 7233 32 2140 791 O ATOM 1052 N ASP A 129 19.542 36.071 150.467 1.00 42.57 N ANISOU 1052 N ASP A 129 5601 3420 7155 -859 1774 -370 N ATOM 1053 CA ASP A 129 20.841 36.163 151.133 1.00 43.87 C ANISOU 1053 CA ASP A 129 5547 3634 7487 -1112 1772 -613 C ATOM 1054 C ASP A 129 21.064 35.025 152.130 1.00 42.36 C ANISOU 1054 C ASP A 129 5188 3760 7146 -1134 1445 -777 C ATOM 1055 O ASP A 129 22.177 34.830 152.605 1.00 43.74 O ANISOU 1055 O ASP A 129 5149 4061 7409 -1295 1384 -954 O ATOM 1056 CB ASP A 129 21.071 37.551 151.786 1.00 46.92 C ANISOU 1056 CB ASP A 129 5933 3755 8138 -1331 1966 -809 C ATOM 1057 CG ASP A 129 19.957 37.968 152.805 1.00 47.10 C ANISOU 1057 CG ASP A 129 6062 3724 8110 -1298 1879 -931 C ATOM 1058 OD1 ASP A 129 19.425 37.136 153.577 1.00 44.40 O ANISOU 1058 OD1 ASP A 129 5684 3630 7556 -1226 1611 -998 O ATOM 1059 OD2 ASP A 129 19.632 39.178 152.854 1.00 49.39 O ANISOU 1059 OD2 ASP A 129 6473 3703 8589 -1349 2105 -965 O ATOM 1060 N LEU A 130 19.976 34.326 152.455 1.00 39.92 N ANISOU 1060 N LEU A 130 4972 3575 6619 -970 1248 -708 N ATOM 1061 CA LEU A 130 19.918 33.186 153.377 1.00 39.04 C ANISOU 1061 CA LEU A 130 4760 3741 6333 -948 948 -796 C ATOM 1062 C LEU A 130 20.304 33.500 154.811 1.00 40.57 C ANISOU 1062 C LEU A 130 4825 4030 6561 -1131 839 -1068 C ATOM 1063 O LEU A 130 20.643 32.606 155.578 1.00 40.93 O ANISOU 1063 O LEU A 130 4745 4323 6482 -1138 605 -1143 O ATOM 1064 CB LEU A 130 20.718 31.970 152.877 1.00 38.17 C ANISOU 1064 CB LEU A 130 4528 3816 6158 -882 828 -727 C ATOM 1065 CG LEU A 130 20.371 31.252 151.568 1.00 37.34 C ANISOU 1065 CG LEU A 130 4529 3711 5946 -685 859 -499 C ATOM 1066 CD1 LEU A 130 20.913 29.836 151.641 1.00 36.13 C ANISOU 1066 CD1 LEU A 130 4258 3771 5701 -614 655 -501 C ATOM 1067 CD2 LEU A 130 18.880 31.231 151.246 1.00 34.91 C ANISOU 1067 CD2 LEU A 130 4423 3348 5492 -525 840 -350 C ATOM 1068 N ARG A 131 20.249 34.771 155.177 1.00 42.66 N ANISOU 1068 N ARG A 131 5126 4098 6986 -1272 1009 -1218 N ATOM 1069 CA ARG A 131 20.693 35.199 156.485 1.00 44.66 C ANISOU 1069 CA ARG A 131 5252 4442 7276 -1471 926 -1524 C ATOM 1070 C ARG A 131 19.650 36.080 157.138 1.00 44.47 C ANISOU 1070 C ARG A 131 5378 4268 7251 -1480 1007 -1629 C ATOM 1071 O ARG A 131 19.943 36.699 158.159 1.00 46.89 O ANISOU 1071 O ARG A 131 5612 4595 7610 -1660 994 -1919 O ATOM 1072 CB ARG A 131 22.011 35.969 156.366 1.00 48.58 C ANISOU 1072 CB ARG A 131 5580 4841 8037 -1709 1078 -1707 C ATOM 1073 CG ARG A 131 23.227 35.087 156.115 1.00 49.94 C ANISOU 1073 CG ARG A 131 5520 5243 8211 -1734 955 -1699 C ATOM 1074 CD ARG A 131 24.258 35.709 155.166 1.00 53.12 C ANISOU 1074 CD ARG A 131 5823 5471 8887 -1869 1215 -1692 C ATOM 1075 NE ARG A 131 25.166 34.691 154.624 1.00 53.47 N ANISOU 1075 NE ARG A 131 5688 5727 8901 -1800 1124 -1599 N ATOM 1076 CZ ARG A 131 26.431 34.539 155.004 1.00 55.96 C ANISOU 1076 CZ ARG A 131 5705 6230 9326 -1953 1048 -1790 C ATOM 1077 NH1 ARG A 131 26.939 35.359 155.917 1.00 59.22 N ANISOU 1077 NH1 ARG A 131 5967 6655 9879 -2209 1044 -2098 N ATOM 1078 NH2 ARG A 131 27.187 33.582 154.470 1.00 55.48 N ANISOU 1078 NH2 ARG A 131 5487 6353 9242 -1849 977 -1692 N ATOM 1079 N SER A 132 18.450 36.128 156.547 1.00 41.91 N ANISOU 1079 N SER A 132 5248 3811 6864 -1281 1085 -1410 N ATOM 1080 CA SER A 132 17.367 37.047 156.963 1.00 42.27 C ANISOU 1080 CA SER A 132 5445 3672 6943 -1241 1208 -1472 C ATOM 1081 C SER A 132 15.965 36.608 156.493 1.00 39.15 C ANISOU 1081 C SER A 132 5196 3291 6387 -980 1175 -1220 C ATOM 1082 O SER A 132 15.849 35.837 155.541 1.00 37.26 O ANISOU 1082 O SER A 132 4978 3117 6060 -838 1122 -979 O ATOM 1083 CB SER A 132 17.659 38.503 156.519 1.00 45.46 C ANISOU 1083 CB SER A 132 5925 3692 7657 -1345 1524 -1536 C ATOM 1084 OG SER A 132 17.394 38.720 155.147 1.00 46.01 O ANISOU 1084 OG SER A 132 6124 3553 7803 -1186 1703 -1230 O ATOM 1085 N TRP A 133 14.917 37.124 157.147 1.00 38.75 N ANISOU 1085 N TRP A 133 5233 3186 6305 -923 1214 -1299 N ATOM 1086 CA TRP A 133 13.536 36.655 156.951 1.00 36.80 C ANISOU 1086 CA TRP A 133 5071 3015 5894 -698 1152 -1112 C ATOM 1087 C TRP A 133 12.525 37.703 156.461 1.00 39.01 C ANISOU 1087 C TRP A 133 5495 3025 6302 -536 1366 -1015 C ATOM 1088 O TRP A 133 12.615 38.868 156.825 1.00 41.24 O ANISOU 1088 O TRP A 133 5831 3064 6776 -611 1556 -1178 O ATOM 1089 CB TRP A 133 13.004 36.070 158.265 1.00 34.99 C ANISOU 1089 CB TRP A 133 4787 3049 5458 -731 975 -1260 C ATOM 1090 CG TRP A 133 13.876 34.993 158.854 1.00 32.42 C ANISOU 1090 CG TRP A 133 4331 3006 4981 -848 747 -1323 C ATOM 1091 CD1 TRP A 133 14.848 35.157 159.787 1.00 33.29 C ANISOU 1091 CD1 TRP A 133 4335 3223 5092 -1041 682 -1574 C ATOM 1092 CD2 TRP A 133 13.838 33.590 158.555 1.00 29.21 C ANISOU 1092 CD2 TRP A 133 3884 2810 4404 -763 551 -1133 C ATOM 1093 NE1 TRP A 133 15.434 33.951 160.082 1.00 31.71 N ANISOU 1093 NE1 TRP A 133 4027 3295 4726 -1058 453 -1523 N ATOM 1094 CE2 TRP A 133 14.830 32.969 159.346 1.00 29.45 C ANISOU 1094 CE2 TRP A 133 3790 3054 4346 -890 381 -1253 C ATOM 1095 CE3 TRP A 133 13.066 32.802 157.700 1.00 26.67 C ANISOU 1095 CE3 TRP A 133 3615 2517 4004 -593 502 -886 C ATOM 1096 CZ2 TRP A 133 15.082 31.588 159.301 1.00 27.70 C ANISOU 1096 CZ2 TRP A 133 3512 3034 3980 -835 181 -1111 C ATOM 1097 CZ3 TRP A 133 13.320 31.417 157.645 1.00 25.49 C ANISOU 1097 CZ3 TRP A 133 3408 2559 3715 -569 307 -778 C ATOM 1098 CH2 TRP A 133 14.317 30.830 158.443 1.00 25.89 C ANISOU 1098 CH2 TRP A 133 3354 2783 3701 -680 159 -878 C ATOM 1099 N THR A 134 11.542 37.282 155.660 1.00 39.48 N ANISOU 1099 N THR A 134 5612 3130 6259 -308 1331 -760 N ATOM 1100 CA THR A 134 10.390 38.155 155.342 1.00 42.11 C ANISOU 1100 CA THR A 134 6053 3275 6671 -105 1488 -659 C ATOM 1101 C THR A 134 9.132 37.682 156.057 1.00 41.87 C ANISOU 1101 C THR A 134 5980 3452 6474 0 1367 -691 C ATOM 1102 O THR A 134 8.611 36.620 155.760 1.00 40.45 O ANISOU 1102 O THR A 134 5748 3507 6114 84 1193 -552 O ATOM 1103 CB THR A 134 10.058 38.233 153.828 1.00 42.31 C ANISOU 1103 CB THR A 134 6166 3204 6707 114 1557 -335 C ATOM 1104 OG1 THR A 134 11.216 38.625 153.082 1.00 44.63 O ANISOU 1104 OG1 THR A 134 6500 3316 7139 21 1696 -272 O ATOM 1105 CG2 THR A 134 8.964 39.256 153.584 1.00 43.46 C ANISOU 1105 CG2 THR A 134 6412 3142 6957 339 1725 -234 C ATOM 1106 N ALA A 135 8.649 38.476 157.002 1.00 44.44 N ANISOU 1106 N ALA A 135 6325 3688 6872 -16 1476 -890 N ATOM 1107 CA ALA A 135 7.412 38.174 157.685 1.00 44.72 C ANISOU 1107 CA ALA A 135 6314 3906 6770 90 1413 -925 C ATOM 1108 C ALA A 135 6.267 38.850 156.950 1.00 46.71 C ANISOU 1108 C ALA A 135 6623 4006 7118 369 1543 -746 C ATOM 1109 O ALA A 135 6.353 40.034 156.608 1.00 48.34 O ANISOU 1109 O ALA A 135 6935 3890 7544 444 1759 -739 O ATOM 1110 CB ALA A 135 7.479 38.656 159.114 1.00 46.70 C ANISOU 1110 CB ALA A 135 6550 4173 7020 -58 1469 -1251 C ATOM 1111 N ALA A 136 5.188 38.104 156.726 1.00 46.47 N ANISOU 1111 N ALA A 136 6516 4207 6934 523 1416 -601 N ATOM 1112 CA ALA A 136 4.077 38.595 155.914 1.00 48.04 C ANISOU 1112 CA ALA A 136 6728 4333 7193 815 1489 -402 C ATOM 1113 C ALA A 136 3.141 39.519 156.666 1.00 50.70 C ANISOU 1113 C ALA A 136 7061 4566 7638 940 1653 -538 C ATOM 1114 O ALA A 136 2.552 40.403 156.059 1.00 53.17 O ANISOU 1114 O ALA A 136 7427 4678 8096 1184 1794 -407 O ATOM 1115 CB ALA A 136 3.305 37.442 155.312 1.00 45.94 C ANISOU 1115 CB ALA A 136 6351 4369 6735 919 1281 -219 C ATOM 1116 N ASP A 137 3.002 39.313 157.975 1.00 51.17 N ANISOU 1116 N ASP A 137 7057 4768 7616 792 1639 -790 N ATOM 1117 CA ASP A 137 2.079 40.102 158.802 1.00 53.59 C ANISOU 1117 CA ASP A 137 7346 5018 7999 904 1802 -959 C ATOM 1118 C ASP A 137 2.529 40.127 160.249 1.00 54.13 C ANISOU 1118 C ASP A 137 7412 5164 7993 664 1830 -1296 C ATOM 1119 O ASP A 137 3.600 39.636 160.566 1.00 53.28 O ANISOU 1119 O ASP A 137 7318 5131 7796 425 1722 -1385 O ATOM 1120 CB ASP A 137 0.647 39.558 158.711 1.00 53.92 C ANISOU 1120 CB ASP A 137 7236 5321 7929 1102 1725 -834 C ATOM 1121 CG ASP A 137 0.561 38.069 159.012 1.00 51.87 C ANISOU 1121 CG ASP A 137 6854 5436 7418 942 1496 -802 C ATOM 1122 OD1 ASP A 137 0.369 37.697 160.183 1.00 52.41 O ANISOU 1122 OD1 ASP A 137 6865 5690 7359 805 1491 -983 O ATOM 1123 OD2 ASP A 137 0.668 37.259 158.071 1.00 50.68 O ANISOU 1123 OD2 ASP A 137 6672 5389 7193 958 1332 -593 O ATOM 1124 N MET A 138 1.685 40.669 161.122 1.00 56.62 N ANISOU 1124 N MET A 138 7697 5491 8323 743 1968 -1483 N ATOM 1125 CA MET A 138 2.040 40.939 162.518 1.00 57.88 C ANISOU 1125 CA MET A 138 7876 5706 8410 545 2036 -1842 C ATOM 1126 C MET A 138 2.202 39.715 163.401 1.00 55.29 C ANISOU 1126 C MET A 138 7458 5783 7767 346 1842 -1902 C ATOM 1127 O MET A 138 2.956 39.740 164.377 1.00 56.13 O ANISOU 1127 O MET A 138 7594 5969 7765 132 1824 -2156 O ATOM 1128 CB MET A 138 1.025 41.894 163.148 1.00 61.90 C ANISOU 1128 CB MET A 138 8383 6111 9024 716 2265 -2029 C ATOM 1129 CG MET A 138 0.927 43.256 162.469 1.00 65.42 C ANISOU 1129 CG MET A 138 8947 6097 9813 917 2498 -2007 C ATOM 1130 SD MET A 138 2.525 44.047 162.191 1.00 67.45 S ANISOU 1130 SD MET A 138 9379 5957 10293 693 2585 -2132 S ATOM 1131 CE MET A 138 2.672 43.977 160.386 1.00 65.55 C ANISOU 1131 CE MET A 138 9188 5529 10189 881 2541 -1660 C ATOM 1132 N ALA A 139 1.500 38.648 163.058 1.00 52.22 N ANISOU 1132 N ALA A 139 6959 5650 7231 416 1697 -1666 N ATOM 1133 CA ALA A 139 1.665 37.397 163.766 1.00 50.48 C ANISOU 1133 CA ALA A 139 6672 5775 6733 239 1520 -1658 C ATOM 1134 C ALA A 139 3.025 36.814 163.440 1.00 48.97 C ANISOU 1134 C ALA A 139 6529 5577 6501 61 1347 -1599 C ATOM 1135 O ALA A 139 3.745 36.362 164.330 1.00 49.51 O ANISOU 1135 O ALA A 139 6601 5815 6394 -128 1254 -1731 O ATOM 1136 CB ALA A 139 0.583 36.434 163.385 1.00 48.79 C ANISOU 1136 CB ALA A 139 6329 5783 6426 343 1430 -1425 C ATOM 1137 N ALA A 140 3.397 36.890 162.165 1.00 47.63 N ANISOU 1137 N ALA A 140 6393 5215 6489 139 1315 -1407 N ATOM 1138 CA ALA A 140 4.661 36.355 161.682 1.00 45.58 C ANISOU 1138 CA ALA A 140 6162 4935 6220 0 1172 -1334 C ATOM 1139 C ALA A 140 5.908 37.106 162.152 1.00 47.14 C ANISOU 1139 C ALA A 140 6423 4982 6506 -175 1232 -1574 C ATOM 1140 O ALA A 140 7.019 36.591 162.013 1.00 46.29 O ANISOU 1140 O ALA A 140 6303 4923 6364 -316 1103 -1558 O ATOM 1141 CB ALA A 140 4.641 36.274 160.191 1.00 44.22 C ANISOU 1141 CB ALA A 140 6009 4622 6170 141 1149 -1073 C ATOM 1142 N GLN A 141 5.723 38.303 162.713 1.00 49.61 N ANISOU 1142 N GLN A 141 6789 5116 6943 -169 1428 -1813 N ATOM 1143 CA GLN A 141 6.813 39.059 163.330 1.00 51.57 C ANISOU 1143 CA GLN A 141 7080 5239 7277 -369 1492 -2111 C ATOM 1144 C GLN A 141 7.295 38.428 164.641 1.00 51.71 C ANISOU 1144 C GLN A 141 7035 5593 7018 -564 1340 -2322 C ATOM 1145 O GLN A 141 8.457 38.588 165.007 1.00 52.67 O ANISOU 1145 O GLN A 141 7142 5724 7147 -759 1282 -2511 O ATOM 1146 CB GLN A 141 6.393 40.506 163.574 1.00 54.72 C ANISOU 1146 CB GLN A 141 7563 5329 7899 -303 1760 -2330 C ATOM 1147 CG GLN A 141 6.023 41.256 162.307 1.00 55.89 C ANISOU 1147 CG GLN A 141 7791 5114 8330 -95 1926 -2108 C ATOM 1148 CD GLN A 141 7.129 42.176 161.790 1.00 57.73 C ANISOU 1148 CD GLN A 141 8113 4979 8842 -215 2064 -2181 C ATOM 1149 OE1 GLN A 141 8.198 41.725 161.366 1.00 56.23 O ANISOU 1149 OE1 GLN A 141 7894 4824 8645 -367 1953 -2114 O ATOM 1150 NE2 GLN A 141 6.860 43.483 161.813 1.00 60.83 N ANISOU 1150 NE2 GLN A 141 8612 4999 9503 -142 2328 -2317 N ATOM 1151 N THR A 142 6.411 37.707 165.333 1.00 50.74 N ANISOU 1151 N THR A 142 6868 5760 6650 -511 1276 -2279 N ATOM 1152 CA THR A 142 6.789 37.004 166.559 1.00 50.98 C ANISOU 1152 CA THR A 142 6854 6143 6373 -665 1129 -2415 C ATOM 1153 C THR A 142 7.613 35.756 166.241 1.00 48.73 C ANISOU 1153 C THR A 142 6516 6033 5966 -738 883 -2197 C ATOM 1154 O THR A 142 8.474 35.344 167.017 1.00 50.55 O ANISOU 1154 O THR A 142 6711 6480 6014 -882 736 -2310 O ATOM 1155 CB THR A 142 5.557 36.630 167.404 1.00 51.38 C ANISOU 1155 CB THR A 142 6882 6441 6198 -587 1176 -2412 C ATOM 1156 OG1 THR A 142 4.603 37.697 167.346 1.00 53.41 O ANISOU 1156 OG1 THR A 142 7170 6495 6627 -445 1417 -2531 O ATOM 1157 CG2 THR A 142 5.947 36.397 168.866 1.00 53.03 C ANISOU 1157 CG2 THR A 142 7084 6972 6092 -742 1103 -2647 C ATOM 1158 N THR A 143 7.351 35.164 165.087 1.00 45.59 N ANISOU 1158 N THR A 143 6109 5546 5666 -624 836 -1893 N ATOM 1159 CA THR A 143 8.140 34.050 164.608 1.00 42.78 C ANISOU 1159 CA THR A 143 5713 5291 5250 -669 633 -1695 C ATOM 1160 C THR A 143 9.516 34.565 164.189 1.00 42.50 C ANISOU 1160 C THR A 143 5669 5096 5381 -778 619 -1803 C ATOM 1161 O THR A 143 10.537 34.014 164.602 1.00 41.99 O ANISOU 1161 O THR A 143 5545 5198 5210 -896 458 -1848 O ATOM 1162 CB THR A 143 7.425 33.372 163.426 1.00 40.90 C ANISOU 1162 CB THR A 143 5471 4988 5081 -518 607 -1386 C ATOM 1163 OG1 THR A 143 6.180 32.835 163.882 1.00 41.49 O ANISOU 1163 OG1 THR A 143 5520 5234 5010 -450 617 -1304 O ATOM 1164 CG2 THR A 143 8.261 32.260 162.830 1.00 39.10 C ANISOU 1164 CG2 THR A 143 5214 4821 4821 -552 422 -1204 C ATOM 1165 N LYS A 144 9.513 35.663 163.425 1.00 42.46 N ANISOU 1165 N LYS A 144 5717 4773 5641 -735 802 -1846 N ATOM 1166 CA LYS A 144 10.706 36.312 162.867 1.00 42.27 C ANISOU 1166 CA LYS A 144 5689 4536 5835 -842 855 -1931 C ATOM 1167 C LYS A 144 11.702 36.706 163.939 1.00 44.86 C ANISOU 1167 C LYS A 144 5957 4968 6120 -1060 810 -2263 C ATOM 1168 O LYS A 144 12.908 36.598 163.742 1.00 45.13 O ANISOU 1168 O LYS A 144 5913 5012 6222 -1188 731 -2311 O ATOM 1169 CB LYS A 144 10.279 37.559 162.081 1.00 43.08 C ANISOU 1169 CB LYS A 144 5889 4261 6219 -745 1109 -1923 C ATOM 1170 CG LYS A 144 11.354 38.244 161.215 1.00 43.45 C ANISOU 1170 CG LYS A 144 5952 4025 6531 -831 1220 -1926 C ATOM 1171 CD LYS A 144 10.841 39.613 160.778 1.00 45.19 C ANISOU 1171 CD LYS A 144 6295 3858 7018 -741 1501 -1955 C ATOM 1172 CE LYS A 144 11.726 40.306 159.768 1.00 45.85 C ANISOU 1172 CE LYS A 144 6422 3622 7377 -798 1660 -1882 C ATOM 1173 NZ LYS A 144 12.915 40.909 160.377 1.00 48.00 N ANISOU 1173 NZ LYS A 144 6637 3813 7790 -1078 1711 -2202 N ATOM 1174 N HIS A 145 11.171 37.150 165.074 1.00 47.19 N ANISOU 1174 N HIS A 145 6274 5365 6290 -1096 860 -2504 N ATOM 1175 CA HIS A 145 11.955 37.507 166.234 1.00 50.10 C ANISOU 1175 CA HIS A 145 6585 5897 6555 -1296 800 -2859 C ATOM 1176 C HIS A 145 12.547 36.262 166.909 1.00 49.03 C ANISOU 1176 C HIS A 145 6350 6173 6109 -1351 517 -2795 C ATOM 1177 O HIS A 145 13.700 36.285 167.352 1.00 50.27 O ANISOU 1177 O HIS A 145 6404 6466 6231 -1512 391 -2983 O ATOM 1178 CB HIS A 145 11.068 38.300 167.194 1.00 53.79 C ANISOU 1178 CB HIS A 145 7122 6364 6951 -1284 953 -3125 C ATOM 1179 CG HIS A 145 11.761 38.772 168.434 1.00 58.29 C ANISOU 1179 CG HIS A 145 7645 7115 7388 -1490 905 -3544 C ATOM 1180 ND1 HIS A 145 13.025 39.326 168.421 1.00 60.75 N ANISOU 1180 ND1 HIS A 145 7881 7339 7862 -1697 880 -3787 N ATOM 1181 CD2 HIS A 145 11.344 38.813 169.723 1.00 60.87 C ANISOU 1181 CD2 HIS A 145 7983 7718 7428 -1524 886 -3784 C ATOM 1182 CE1 HIS A 145 13.364 39.672 169.653 1.00 64.36 C ANISOU 1182 CE1 HIS A 145 8296 8023 8133 -1854 823 -4175 C ATOM 1183 NE2 HIS A 145 12.361 39.369 170.462 1.00 64.49 N ANISOU 1183 NE2 HIS A 145 8376 8269 7860 -1746 827 -4177 N ATOM 1184 N LYS A 146 11.767 35.181 166.971 1.00 46.52 N ANISOU 1184 N LYS A 146 6053 6045 5580 -1216 421 -2524 N ATOM 1185 CA LYS A 146 12.195 33.952 167.642 1.00 45.86 C ANISOU 1185 CA LYS A 146 5903 6323 5198 -1235 175 -2414 C ATOM 1186 C LYS A 146 13.285 33.297 166.817 1.00 44.53 C ANISOU 1186 C LYS A 146 5651 6127 5144 -1246 30 -2246 C ATOM 1187 O LYS A 146 14.290 32.819 167.343 1.00 45.67 O ANISOU 1187 O LYS A 146 5693 6501 5158 -1323 -161 -2303 O ATOM 1188 CB LYS A 146 11.036 32.963 167.782 1.00 44.30 C ANISOU 1188 CB LYS A 146 5759 6267 4807 -1098 152 -2140 C ATOM 1189 CG LYS A 146 10.136 33.095 169.003 1.00 46.57 C ANISOU 1189 CG LYS A 146 6090 6770 4833 -1098 218 -2268 C ATOM 1190 CD LYS A 146 9.728 31.686 169.470 1.00 46.30 C ANISOU 1190 CD LYS A 146 6061 7014 4517 -1041 80 -1987 C ATOM 1191 CE LYS A 146 9.864 30.672 168.311 1.00 43.88 C ANISOU 1191 CE LYS A 146 5739 6578 4356 -961 -17 -1648 C ATOM 1192 NZ LYS A 146 9.714 29.213 168.653 1.00 43.30 N ANISOU 1192 NZ LYS A 146 5672 6710 4068 -922 -161 -1363 N ATOM 1193 N TRP A 147 13.085 33.331 165.502 1.00 42.41 N ANISOU 1193 N TRP A 147 5417 5580 5115 -1157 129 -2049 N ATOM 1194 CA TRP A 147 13.963 32.676 164.536 1.00 40.03 C ANISOU 1194 CA TRP A 147 5052 5228 4931 -1136 31 -1864 C ATOM 1195 C TRP A 147 15.281 33.439 164.330 1.00 41.35 C ANISOU 1195 C TRP A 147 5118 5297 5297 -1288 58 -2075 C ATOM 1196 O TRP A 147 16.274 32.874 163.867 1.00 41.21 O ANISOU 1196 O TRP A 147 4996 5329 5332 -1304 -53 -1992 O ATOM 1197 CB TRP A 147 13.213 32.439 163.205 1.00 37.08 C ANISOU 1197 CB TRP A 147 4758 4630 4701 -982 131 -1591 C ATOM 1198 CG TRP A 147 12.208 31.285 163.244 1.00 34.96 C ANISOU 1198 CG TRP A 147 4532 4498 4254 -858 43 -1349 C ATOM 1199 CD1 TRP A 147 11.718 30.658 164.352 1.00 35.49 C ANISOU 1199 CD1 TRP A 147 4604 4812 4070 -865 -49 -1342 C ATOM 1200 CD2 TRP A 147 11.577 30.652 162.124 1.00 32.85 C ANISOU 1200 CD2 TRP A 147 4306 4125 4050 -725 53 -1094 C ATOM 1201 NE1 TRP A 147 10.834 29.671 163.998 1.00 33.86 N ANISOU 1201 NE1 TRP A 147 4433 4634 3798 -763 -83 -1095 N ATOM 1202 CE2 TRP A 147 10.733 29.636 162.635 1.00 32.53 C ANISOU 1202 CE2 TRP A 147 4280 4259 3820 -680 -35 -957 C ATOM 1203 CE3 TRP A 147 11.643 30.839 160.743 1.00 30.89 C ANISOU 1203 CE3 TRP A 147 4084 3667 3987 -646 130 -973 C ATOM 1204 CZ2 TRP A 147 9.954 28.820 161.810 1.00 30.63 C ANISOU 1204 CZ2 TRP A 147 4064 3977 3598 -578 -54 -737 C ATOM 1205 CZ3 TRP A 147 10.895 30.025 159.928 1.00 29.20 C ANISOU 1205 CZ3 TRP A 147 3898 3444 3751 -526 94 -755 C ATOM 1206 CH2 TRP A 147 10.048 29.030 160.462 1.00 29.57 C ANISOU 1206 CH2 TRP A 147 3945 3656 3633 -502 -1 -655 C ATOM 1207 N GLU A 148 15.282 34.720 164.675 1.00 43.45 N ANISOU 1207 N GLU A 148 5406 5414 5690 -1404 219 -2358 N ATOM 1208 CA GLU A 148 16.501 35.510 164.697 1.00 46.35 C ANISOU 1208 CA GLU A 148 5661 5704 6246 -1598 254 -2618 C ATOM 1209 C GLU A 148 17.332 35.147 165.917 1.00 48.30 C ANISOU 1209 C GLU A 148 5758 6326 6266 -1727 22 -2840 C ATOM 1210 O GLU A 148 18.551 34.982 165.825 1.00 48.73 O ANISOU 1210 O GLU A 148 5645 6481 6390 -1830 -92 -2912 O ATOM 1211 CB GLU A 148 16.177 37.011 164.711 1.00 49.09 C ANISOU 1211 CB GLU A 148 6096 5734 6824 -1689 519 -2867 C ATOM 1212 CG GLU A 148 16.149 37.648 163.331 1.00 49.61 C ANISOU 1212 CG GLU A 148 6239 5391 7218 -1639 752 -2703 C ATOM 1213 CD GLU A 148 15.234 38.861 163.240 1.00 51.82 C ANISOU 1213 CD GLU A 148 6678 5334 7677 -1594 1023 -2792 C ATOM 1214 OE1 GLU A 148 15.221 39.704 164.166 1.00 54.62 O ANISOU 1214 OE1 GLU A 148 7041 5654 8058 -1726 1099 -3139 O ATOM 1215 OE2 GLU A 148 14.530 38.974 162.213 1.00 51.55 O ANISOU 1215 OE2 GLU A 148 6758 5070 7757 -1413 1159 -2518 O ATOM 1216 N ALA A 149 16.651 34.997 167.052 1.00 49.79 N ANISOU 1216 N ALA A 149 6000 6749 6168 -1705 -48 -2936 N ATOM 1217 CA ALA A 149 17.302 34.811 168.353 1.00 52.37 C ANISOU 1217 CA ALA A 149 6209 7465 6223 -1818 -258 -3178 C ATOM 1218 C ALA A 149 17.888 33.413 168.531 1.00 51.15 C ANISOU 1218 C ALA A 149 5952 7635 5847 -1724 -539 -2933 C ATOM 1219 O ALA A 149 18.804 33.229 169.323 1.00 54.12 O ANISOU 1219 O ALA A 149 6176 8325 6060 -1808 -744 -3099 O ATOM 1220 CB ALA A 149 16.332 35.141 169.489 1.00 53.75 C ANISOU 1220 CB ALA A 149 6495 7789 6139 -1812 -210 -3352 C ATOM 1221 N ALA A 150 17.377 32.443 167.781 1.00 47.32 N ANISOU 1221 N ALA A 150 5542 7069 5366 -1545 -548 -2550 N ATOM 1222 CA ALA A 150 17.895 31.081 167.826 1.00 46.43 C ANISOU 1222 CA ALA A 150 5355 7189 5096 -1434 -783 -2292 C ATOM 1223 C ALA A 150 18.922 30.796 166.739 1.00 45.64 C ANISOU 1223 C ALA A 150 5130 6959 5253 -1422 -813 -2189 C ATOM 1224 O ALA A 150 19.462 29.689 166.691 1.00 45.25 O ANISOU 1224 O ALA A 150 5004 7071 5118 -1316 -997 -1988 O ATOM 1225 CB ALA A 150 16.767 30.094 167.715 1.00 44.01 C ANISOU 1225 CB ALA A 150 5198 6876 4646 -1263 -777 -1958 C ATOM 1226 N HIS A 151 19.161 31.798 165.883 1.00 45.65 N ANISOU 1226 N HIS A 151 5119 6661 5567 -1521 -613 -2318 N ATOM 1227 CA HIS A 151 20.028 31.725 164.690 1.00 44.37 C ANISOU 1227 CA HIS A 151 4857 6325 5678 -1522 -562 -2226 C ATOM 1228 C HIS A 151 19.691 30.572 163.760 1.00 41.32 C ANISOU 1228 C HIS A 151 4543 5866 5291 -1321 -590 -1860 C ATOM 1229 O HIS A 151 20.577 29.829 163.329 1.00 40.83 O ANISOU 1229 O HIS A 151 4356 5879 5279 -1266 -700 -1753 O ATOM 1230 CB HIS A 151 21.514 31.726 165.054 1.00 47.25 C ANISOU 1230 CB HIS A 151 4962 6909 6082 -1644 -720 -2419 C ATOM 1231 CG HIS A 151 21.924 32.894 165.891 1.00 50.89 C ANISOU 1231 CG HIS A 151 5330 7435 6573 -1877 -692 -2828 C ATOM 1232 ND1 HIS A 151 22.128 34.151 165.363 1.00 52.38 N ANISOU 1232 ND1 HIS A 151 5515 7315 7073 -2054 -448 -3038 N ATOM 1233 CD2 HIS A 151 22.160 33.001 167.219 1.00 53.53 C ANISOU 1233 CD2 HIS A 151 5576 8102 6660 -1965 -872 -3078 C ATOM 1234 CE1 HIS A 151 22.474 34.982 166.330 1.00 55.34 C ANISOU 1234 CE1 HIS A 151 5801 7808 7418 -2258 -475 -3425 C ATOM 1235 NE2 HIS A 151 22.500 34.309 167.466 1.00 56.35 N ANISOU 1235 NE2 HIS A 151 5872 8346 7192 -2206 -740 -3468 N ATOM 1236 N VAL A 152 18.397 30.439 163.479 1.00 38.99 N ANISOU 1236 N VAL A 152 4439 5433 4944 -1215 -490 -1693 N ATOM 1237 CA VAL A 152 17.846 29.422 162.588 1.00 36.28 C ANISOU 1237 CA VAL A 152 4186 5000 4599 -1043 -498 -1382 C ATOM 1238 C VAL A 152 18.364 29.557 161.167 1.00 35.61 C ANISOU 1238 C VAL A 152 4077 4693 4759 -1015 -376 -1298 C ATOM 1239 O VAL A 152 18.655 28.553 160.519 1.00 35.13 O ANISOU 1239 O VAL A 152 3996 4646 4706 -903 -452 -1114 O ATOM 1240 CB VAL A 152 16.325 29.532 162.602 1.00 34.68 C ANISOU 1240 CB VAL A 152 4157 4702 4319 -973 -391 -1289 C ATOM 1241 CG1 VAL A 152 15.650 28.430 161.802 1.00 32.28 C ANISOU 1241 CG1 VAL A 152 3934 4338 3993 -820 -420 -1002 C ATOM 1242 CG2 VAL A 152 15.893 29.444 164.002 1.00 36.36 C ANISOU 1242 CG2 VAL A 152 4385 5147 4282 -1010 -481 -1381 C ATOM 1243 N ALA A 153 18.509 30.800 160.713 1.00 37.02 N ANISOU 1243 N ALA A 153 4264 4664 5137 -1117 -176 -1438 N ATOM 1244 CA ALA A 153 19.065 31.120 159.401 1.00 37.51 C ANISOU 1244 CA ALA A 153 4308 4516 5427 -1112 -20 -1367 C ATOM 1245 C ALA A 153 20.446 30.515 159.197 1.00 39.36 C ANISOU 1245 C ALA A 153 4348 4885 5722 -1137 -127 -1379 C ATOM 1246 O ALA A 153 20.709 29.941 158.147 1.00 38.61 O ANISOU 1246 O ALA A 153 4253 4725 5693 -1034 -92 -1210 O ATOM 1247 CB ALA A 153 19.121 32.622 159.194 1.00 38.97 C ANISOU 1247 CB ALA A 153 4526 4458 5822 -1246 219 -1533 C ATOM 1248 N GLU A 154 21.294 30.614 160.221 1.00 42.35 N ANISOU 1248 N GLU A 154 4552 5475 6063 -1261 -265 -1587 N ATOM 1249 CA GLU A 154 22.648 30.060 160.203 1.00 44.10 C ANISOU 1249 CA GLU A 154 4540 5876 6340 -1278 -394 -1624 C ATOM 1250 C GLU A 154 22.689 28.531 160.059 1.00 42.17 C ANISOU 1250 C GLU A 154 4291 5775 5958 -1069 -581 -1387 C ATOM 1251 O GLU A 154 23.546 27.984 159.359 1.00 41.95 O ANISOU 1251 O GLU A 154 4139 5761 6039 -1003 -591 -1316 O ATOM 1252 CB GLU A 154 23.386 30.489 161.471 1.00 48.11 C ANISOU 1252 CB GLU A 154 4859 6631 6790 -1443 -541 -1911 C ATOM 1253 CG GLU A 154 24.881 30.257 161.440 1.00 51.79 C ANISOU 1253 CG GLU A 154 5028 7280 7369 -1501 -645 -2015 C ATOM 1254 CD GLU A 154 25.446 30.044 162.825 1.00 55.60 C ANISOU 1254 CD GLU A 154 5329 8138 7660 -1553 -920 -2199 C ATOM 1255 OE1 GLU A 154 25.695 31.049 163.537 1.00 58.57 O ANISOU 1255 OE1 GLU A 154 5618 8575 8062 -1768 -905 -2512 O ATOM 1256 OE2 GLU A 154 25.633 28.864 163.205 1.00 56.20 O ANISOU 1256 OE2 GLU A 154 5354 8448 7553 -1371 -1150 -2032 O ATOM 1257 N GLN A 155 21.750 27.856 160.712 1.00 40.57 N ANISOU 1257 N GLN A 155 4225 5658 5532 -968 -704 -1267 N ATOM 1258 CA GLN A 155 21.703 26.404 160.690 1.00 39.10 C ANISOU 1258 CA GLN A 155 4059 5569 5227 -782 -868 -1041 C ATOM 1259 C GLN A 155 21.202 25.941 159.358 1.00 37.03 C ANISOU 1259 C GLN A 155 3928 5080 5063 -664 -740 -853 C ATOM 1260 O GLN A 155 21.748 25.010 158.793 1.00 37.75 O ANISOU 1260 O GLN A 155 3964 5176 5202 -543 -796 -739 O ATOM 1261 CB GLN A 155 20.792 25.857 161.780 1.00 38.03 C ANISOU 1261 CB GLN A 155 4044 5573 4834 -732 -1002 -956 C ATOM 1262 CG GLN A 155 21.264 26.163 163.167 1.00 40.43 C ANISOU 1262 CG GLN A 155 4230 6160 4970 -821 -1158 -1129 C ATOM 1263 CD GLN A 155 20.251 25.807 164.236 1.00 40.09 C ANISOU 1263 CD GLN A 155 4331 6251 4650 -789 -1236 -1051 C ATOM 1264 OE1 GLN A 155 19.352 24.977 164.038 1.00 38.42 O ANISOU 1264 OE1 GLN A 155 4274 5953 4370 -677 -1222 -819 O ATOM 1265 NE2 GLN A 155 20.396 26.438 165.385 1.00 41.59 N ANISOU 1265 NE2 GLN A 155 4464 6663 4675 -899 -1307 -1259 N ATOM 1266 N LEU A 156 20.184 26.627 158.850 1.00 35.60 N ANISOU 1266 N LEU A 156 3908 4708 4909 -693 -569 -837 N ATOM 1267 CA LEU A 156 19.541 26.279 157.582 1.00 33.34 C ANISOU 1267 CA LEU A 156 3756 4237 4676 -581 -456 -672 C ATOM 1268 C LEU A 156 20.459 26.517 156.378 1.00 33.12 C ANISOU 1268 C LEU A 156 3651 4105 4829 -574 -321 -677 C ATOM 1269 O LEU A 156 20.462 25.733 155.435 1.00 32.10 O ANISOU 1269 O LEU A 156 3562 3921 4712 -450 -308 -551 O ATOM 1270 CB LEU A 156 18.253 27.087 157.435 1.00 32.91 C ANISOU 1270 CB LEU A 156 3864 4044 4597 -602 -320 -663 C ATOM 1271 CG LEU A 156 17.060 26.565 156.628 1.00 31.13 C ANISOU 1271 CG LEU A 156 3792 3718 4317 -479 -285 -491 C ATOM 1272 CD1 LEU A 156 16.768 25.096 156.874 1.00 29.71 C ANISOU 1272 CD1 LEU A 156 3635 3631 4024 -389 -454 -363 C ATOM 1273 CD2 LEU A 156 15.870 27.418 157.026 1.00 31.65 C ANISOU 1273 CD2 LEU A 156 3958 3730 4338 -509 -198 -525 C ATOM 1274 N ARG A 157 21.273 27.568 156.452 1.00 34.15 N ANISOU 1274 N ARG A 157 3663 4216 5098 -717 -215 -838 N ATOM 1275 CA ARG A 157 22.190 27.941 155.374 1.00 34.43 C ANISOU 1275 CA ARG A 157 3610 4155 5317 -743 -45 -849 C ATOM 1276 C ARG A 157 23.268 26.898 155.175 1.00 34.59 C ANISOU 1276 C ARG A 157 3459 4318 5367 -656 -157 -823 C ATOM 1277 O ARG A 157 23.669 26.619 154.044 1.00 34.94 O ANISOU 1277 O ARG A 157 3493 4291 5490 -579 -40 -747 O ATOM 1278 CB ARG A 157 22.813 29.298 155.660 1.00 36.33 C ANISOU 1278 CB ARG A 157 3747 4335 5724 -952 99 -1046 C ATOM 1279 CG ARG A 157 23.671 29.837 154.569 1.00 38.62 C ANISOU 1279 CG ARG A 157 3959 4499 6217 -1010 325 -1044 C ATOM 1280 CD ARG A 157 24.176 31.226 154.865 1.00 42.07 C ANISOU 1280 CD ARG A 157 4313 4824 6849 -1245 495 -1241 C ATOM 1281 NE ARG A 157 25.181 31.275 155.930 1.00 45.77 N ANISOU 1281 NE ARG A 157 4521 5504 7367 -1401 343 -1482 N ATOM 1282 CZ ARG A 157 24.941 31.685 157.181 1.00 47.19 C ANISOU 1282 CZ ARG A 157 4678 5779 7474 -1514 215 -1674 C ATOM 1283 NH1 ARG A 157 23.709 32.055 157.543 1.00 45.85 N ANISOU 1283 NH1 ARG A 157 4732 5497 7192 -1483 237 -1648 N ATOM 1284 NH2 ARG A 157 25.928 31.707 158.076 1.00 49.62 N ANISOU 1284 NH2 ARG A 157 4727 6321 7807 -1650 61 -1902 N ATOM 1285 N ALA A 158 23.680 26.273 156.278 1.00 34.85 N ANISOU 1285 N ALA A 158 3366 4560 5317 -643 -386 -875 N ATOM 1286 CA ALA A 158 24.633 25.156 156.256 1.00 34.66 C ANISOU 1286 CA ALA A 158 3176 4682 5310 -514 -528 -829 C ATOM 1287 C ALA A 158 24.081 23.959 155.509 1.00 32.46 C ANISOU 1287 C ALA A 158 3051 4312 4972 -314 -549 -635 C ATOM 1288 O ALA A 158 24.827 23.191 154.926 1.00 32.54 O ANISOU 1288 O ALA A 158 2965 4341 5058 -192 -556 -595 O ATOM 1289 CB ALA A 158 24.987 24.747 157.655 1.00 35.47 C ANISOU 1289 CB ALA A 158 3152 5032 5295 -511 -782 -884 C ATOM 1290 N TYR A 159 22.765 23.805 155.542 1.00 30.62 N ANISOU 1290 N TYR A 159 3043 3979 4612 -285 -553 -536 N ATOM 1291 CA TYR A 159 22.121 22.741 154.815 1.00 28.98 C ANISOU 1291 CA TYR A 159 2985 3670 4357 -133 -564 -387 C ATOM 1292 C TYR A 159 21.951 23.100 153.342 1.00 28.92 C ANISOU 1292 C TYR A 159 3061 3512 4415 -109 -356 -367 C ATOM 1293 O TYR A 159 22.290 22.293 152.487 1.00 29.18 O ANISOU 1293 O TYR A 159 3094 3510 4482 14 -333 -324 O ATOM 1294 CB TYR A 159 20.775 22.409 155.435 1.00 26.08 C ANISOU 1294 CB TYR A 159 2794 3280 3836 -128 -650 -298 C ATOM 1295 CG TYR A 159 19.923 21.548 154.552 1.00 24.62 C ANISOU 1295 CG TYR A 159 2769 2964 3623 -22 -626 -184 C ATOM 1296 CD1 TYR A 159 20.177 20.191 154.439 1.00 24.06 C ANISOU 1296 CD1 TYR A 159 2702 2872 3566 108 -727 -104 C ATOM 1297 CD2 TYR A 159 18.847 22.092 153.820 1.00 23.08 C ANISOU 1297 CD2 TYR A 159 2714 2663 3391 -47 -506 -167 C ATOM 1298 CE1 TYR A 159 19.394 19.390 153.630 1.00 23.39 C ANISOU 1298 CE1 TYR A 159 2759 2659 3468 180 -705 -42 C ATOM 1299 CE2 TYR A 159 18.066 21.293 153.009 1.00 21.80 C ANISOU 1299 CE2 TYR A 159 2673 2416 3192 37 -506 -95 C ATOM 1300 CZ TYR A 159 18.342 19.944 152.925 1.00 22.45 C ANISOU 1300 CZ TYR A 159 2760 2474 3297 134 -603 -49 C ATOM 1301 OH TYR A 159 17.561 19.134 152.134 1.00 23.13 O ANISOU 1301 OH TYR A 159 2963 2467 3360 193 -603 -17 O ATOM 1302 N LEU A 160 21.401 24.288 153.069 1.00 28.73 N ANISOU 1302 N LEU A 160 3118 3401 4397 -210 -205 -395 N ATOM 1303 CA LEU A 160 21.042 24.702 151.712 1.00 28.93 C ANISOU 1303 CA LEU A 160 3259 3297 4436 -169 -12 -336 C ATOM 1304 C LEU A 160 22.260 24.914 150.826 1.00 32.11 C ANISOU 1304 C LEU A 160 3538 3696 4965 -168 146 -370 C ATOM 1305 O LEU A 160 22.262 24.503 149.675 1.00 32.33 O ANISOU 1305 O LEU A 160 3631 3686 4965 -60 238 -308 O ATOM 1306 CB LEU A 160 20.188 25.970 151.721 1.00 27.21 C ANISOU 1306 CB LEU A 160 3155 2976 4206 -254 115 -332 C ATOM 1307 CG LEU A 160 18.859 25.887 152.485 1.00 25.44 C ANISOU 1307 CG LEU A 160 3048 2759 3858 -250 3 -300 C ATOM 1308 CD1 LEU A 160 18.379 27.258 152.946 1.00 24.55 C ANISOU 1308 CD1 LEU A 160 2979 2567 3783 -354 115 -359 C ATOM 1309 CD2 LEU A 160 17.779 25.169 151.705 1.00 23.54 C ANISOU 1309 CD2 LEU A 160 2950 2488 3505 -123 -28 -184 C ATOM 1310 N GLU A 161 23.303 25.532 151.367 1.00 35.25 N ANISOU 1310 N GLU A 161 3746 4152 5497 -293 179 -484 N ATOM 1311 CA GLU A 161 24.533 25.708 150.613 1.00 38.71 C ANISOU 1311 CA GLU A 161 4023 4607 6078 -311 338 -527 C ATOM 1312 C GLU A 161 25.376 24.440 150.636 1.00 40.14 C ANISOU 1312 C GLU A 161 4051 4920 6282 -177 206 -542 C ATOM 1313 O GLU A 161 26.232 24.230 149.774 1.00 42.28 O ANISOU 1313 O GLU A 161 4216 5209 6638 -122 338 -552 O ATOM 1314 CB GLU A 161 25.366 26.851 151.176 1.00 41.59 C ANISOU 1314 CB GLU A 161 4205 4986 6609 -521 430 -670 C ATOM 1315 CG GLU A 161 24.687 28.209 151.161 1.00 43.20 C ANISOU 1315 CG GLU A 161 4552 5017 6847 -658 599 -673 C ATOM 1316 CD GLU A 161 25.650 29.329 151.528 1.00 46.77 C ANISOU 1316 CD GLU A 161 4816 5444 7512 -889 736 -840 C ATOM 1317 OE1 GLU A 161 26.705 29.037 152.146 1.00 48.60 O ANISOU 1317 OE1 GLU A 161 4786 5851 7829 -957 622 -983 O ATOM 1318 OE2 GLU A 161 25.359 30.503 151.199 1.00 48.42 O ANISOU 1318 OE2 GLU A 161 5131 5453 7813 -1001 959 -830 O ATOM 1319 N GLY A 162 25.136 23.585 151.619 1.00 39.54 N ANISOU 1319 N GLY A 162 3965 4930 6130 -110 -41 -531 N ATOM 1320 CA GLY A 162 26.047 22.491 151.861 1.00 40.30 C ANISOU 1320 CA GLY A 162 3889 5145 6277 23 -179 -541 C ATOM 1321 C GLY A 162 25.474 21.167 151.464 1.00 39.29 C ANISOU 1321 C GLY A 162 3917 4946 6067 216 -263 -434 C ATOM 1322 O GLY A 162 25.776 20.655 150.382 1.00 39.96 O ANISOU 1322 O GLY A 162 4017 4978 6190 330 -150 -427 O ATOM 1323 N THR A 163 24.634 20.626 152.341 1.00 38.39 N ANISOU 1323 N THR A 163 3921 4825 5839 240 -447 -361 N ATOM 1324 CA THR A 163 24.200 19.240 152.251 1.00 38.24 C ANISOU 1324 CA THR A 163 4021 4731 5779 406 -556 -265 C ATOM 1325 C THR A 163 23.226 19.042 151.106 1.00 36.98 C ANISOU 1325 C THR A 163 4076 4418 5557 435 -439 -237 C ATOM 1326 O THR A 163 23.270 18.024 150.424 1.00 38.16 O ANISOU 1326 O THR A 163 4280 4486 5731 571 -433 -229 O ATOM 1327 CB THR A 163 23.549 18.779 153.555 1.00 37.35 C ANISOU 1327 CB THR A 163 3976 4654 5561 399 -758 -175 C ATOM 1328 OG1 THR A 163 24.175 19.443 154.650 1.00 38.77 O ANISOU 1328 OG1 THR A 163 3984 5016 5730 310 -851 -232 O ATOM 1329 CG2 THR A 163 23.737 17.309 153.741 1.00 38.13 C ANISOU 1329 CG2 THR A 163 4095 4701 5690 583 -883 -76 C ATOM 1330 N CYS A 164 22.382 20.042 150.888 1.00 35.73 N ANISOU 1330 N CYS A 164 4028 4228 5321 314 -347 -237 N ATOM 1331 CA CYS A 164 21.363 20.004 149.849 1.00 35.11 C ANISOU 1331 CA CYS A 164 4138 4052 5152 339 -259 -209 C ATOM 1332 C CYS A 164 22.004 19.867 148.465 1.00 36.13 C ANISOU 1332 C CYS A 164 4253 4164 5311 430 -97 -254 C ATOM 1333 O CYS A 164 21.548 19.068 147.631 1.00 36.91 O ANISOU 1333 O CYS A 164 4468 4206 5349 527 -91 -262 O ATOM 1334 CB CYS A 164 20.479 21.257 149.922 1.00 34.31 C ANISOU 1334 CB CYS A 164 4122 3936 4977 219 -184 -189 C ATOM 1335 SG CYS A 164 19.148 21.386 148.689 1.00 35.08 S ANISOU 1335 SG CYS A 164 4425 3968 4938 266 -100 -141 S ATOM 1336 N VAL A 165 23.075 20.617 148.247 1.00 35.44 N ANISOU 1336 N VAL A 165 4014 4134 5318 389 40 -298 N ATOM 1337 CA VAL A 165 23.741 20.628 146.968 1.00 35.82 C ANISOU 1337 CA VAL A 165 4037 4190 5385 461 234 -331 C ATOM 1338 C VAL A 165 24.496 19.318 146.713 1.00 37.18 C ANISOU 1338 C VAL A 165 4127 4372 5627 624 186 -388 C ATOM 1339 O VAL A 165 24.407 18.758 145.629 1.00 37.66 O ANISOU 1339 O VAL A 165 4279 4403 5627 733 275 -422 O ATOM 1340 CB VAL A 165 24.683 21.820 146.879 1.00 36.67 C ANISOU 1340 CB VAL A 165 3988 4344 5600 345 417 -358 C ATOM 1341 CG1 VAL A 165 25.244 21.933 145.522 1.00 38.29 C ANISOU 1341 CG1 VAL A 165 4191 4561 5794 408 654 -364 C ATOM 1342 CG2 VAL A 165 23.950 23.073 147.186 1.00 35.73 C ANISOU 1342 CG2 VAL A 165 3961 4169 5443 199 471 -309 C ATOM 1343 N GLU A 166 25.190 18.812 147.736 1.00 38.56 N ANISOU 1343 N GLU A 166 4138 4594 5920 655 38 -400 N ATOM 1344 CA GLU A 166 25.972 17.562 147.645 1.00 38.72 C ANISOU 1344 CA GLU A 166 4062 4609 6041 839 -17 -437 C ATOM 1345 C GLU A 166 25.069 16.405 147.329 1.00 36.37 C ANISOU 1345 C GLU A 166 3977 4168 5676 946 -98 -421 C ATOM 1346 O GLU A 166 25.377 15.599 146.475 1.00 36.80 O ANISOU 1346 O GLU A 166 4056 4165 5762 1087 -24 -492 O ATOM 1347 CB GLU A 166 26.693 17.250 148.960 1.00 40.83 C ANISOU 1347 CB GLU A 166 4134 4964 6416 869 -205 -411 C ATOM 1348 CG GLU A 166 27.858 18.171 149.306 1.00 44.08 C ANISOU 1348 CG GLU A 166 4263 5547 6940 778 -149 -477 C ATOM 1349 CD GLU A 166 28.349 17.977 150.749 1.00 46.35 C ANISOU 1349 CD GLU A 166 4371 5968 7270 788 -385 -454 C ATOM 1350 OE1 GLU A 166 28.680 16.819 151.118 1.00 47.34 O ANISOU 1350 OE1 GLU A 166 4453 6090 7443 984 -529 -400 O ATOM 1351 OE2 GLU A 166 28.397 18.983 151.512 1.00 46.89 O ANISOU 1351 OE2 GLU A 166 4350 6146 7320 608 -425 -491 O ATOM 1352 N TRP A 167 23.927 16.358 147.998 1.00 33.78 N ANISOU 1352 N TRP A 167 3798 3779 5259 865 -233 -346 N ATOM 1353 CA TRP A 167 22.998 15.278 147.768 1.00 32.67 C ANISOU 1353 CA TRP A 167 3845 3491 5076 926 -309 -340 C ATOM 1354 C TRP A 167 22.236 15.430 146.461 1.00 31.61 C ANISOU 1354 C TRP A 167 3869 3329 4814 910 -188 -414 C ATOM 1355 O TRP A 167 21.994 14.429 145.793 1.00 31.87 O ANISOU 1355 O TRP A 167 4001 3262 4847 1001 -185 -494 O ATOM 1356 CB TRP A 167 22.103 15.049 148.985 1.00 31.79 C ANISOU 1356 CB TRP A 167 3814 3336 4930 847 -485 -229 C ATOM 1357 CG TRP A 167 22.894 14.361 150.031 1.00 32.81 C ANISOU 1357 CG TRP A 167 3825 3471 5169 944 -616 -155 C ATOM 1358 CD1 TRP A 167 23.694 14.940 150.962 1.00 32.73 C ANISOU 1358 CD1 TRP A 167 3631 3618 5185 922 -684 -119 C ATOM 1359 CD2 TRP A 167 23.033 12.954 150.198 1.00 34.35 C ANISOU 1359 CD2 TRP A 167 4069 3513 5468 1098 -694 -112 C ATOM 1360 NE1 TRP A 167 24.310 13.981 151.718 1.00 34.96 N ANISOU 1360 NE1 TRP A 167 3839 3889 5555 1071 -818 -37 N ATOM 1361 CE2 TRP A 167 23.915 12.748 151.274 1.00 35.81 C ANISOU 1361 CE2 TRP A 167 4098 3786 5723 1188 -817 -15 C ATOM 1362 CE3 TRP A 167 22.482 11.844 149.554 1.00 35.34 C ANISOU 1362 CE3 TRP A 167 4359 3429 5641 1167 -673 -154 C ATOM 1363 CZ2 TRP A 167 24.264 11.476 151.723 1.00 37.94 C ANISOU 1363 CZ2 TRP A 167 4381 3927 6108 1372 -912 81 C ATOM 1364 CZ3 TRP A 167 22.821 10.576 150.005 1.00 37.56 C ANISOU 1364 CZ3 TRP A 167 4661 3546 6064 1324 -750 -81 C ATOM 1365 CH2 TRP A 167 23.713 10.405 151.073 1.00 38.83 C ANISOU 1365 CH2 TRP A 167 4675 3787 6294 1439 -864 53 C ATOM 1366 N LEU A 168 21.932 16.671 146.075 1.00 29.58 N ANISOU 1366 N LEU A 168 3629 3162 4449 807 -83 -394 N ATOM 1367 CA LEU A 168 21.404 16.929 144.746 1.00 28.64 C ANISOU 1367 CA LEU A 168 3636 3067 4180 826 43 -445 C ATOM 1368 C LEU A 168 22.314 16.332 143.703 1.00 31.32 C ANISOU 1368 C LEU A 168 3938 3419 4542 964 176 -557 C ATOM 1369 O LEU A 168 21.849 15.521 142.903 1.00 33.46 O ANISOU 1369 O LEU A 168 4331 3647 4734 1037 173 -656 O ATOM 1370 CB LEU A 168 21.223 18.418 144.479 1.00 27.06 C ANISOU 1370 CB LEU A 168 3442 2951 3890 731 171 -372 C ATOM 1371 CG LEU A 168 20.717 18.903 143.118 1.00 26.44 C ANISOU 1371 CG LEU A 168 3492 2933 3623 768 312 -372 C ATOM 1372 CD1 LEU A 168 19.519 18.102 142.616 1.00 25.81 C ANISOU 1372 CD1 LEU A 168 3566 2840 3400 809 193 -432 C ATOM 1373 CD2 LEU A 168 20.370 20.373 143.210 1.00 24.59 C ANISOU 1373 CD2 LEU A 168 3278 2726 3339 675 405 -252 C ATOM 1374 N ARG A 169 23.598 16.679 143.748 1.00 32.29 N ANISOU 1374 N ARG A 169 3880 3607 4782 994 291 -563 N ATOM 1375 CA ARG A 169 24.553 16.215 142.749 1.00 35.18 C ANISOU 1375 CA ARG A 169 4182 4009 5175 1130 455 -672 C ATOM 1376 C ARG A 169 24.730 14.706 142.738 1.00 37.27 C ANISOU 1376 C ARG A 169 4466 4157 5538 1285 367 -777 C ATOM 1377 O ARG A 169 24.913 14.114 141.681 1.00 40.37 O ANISOU 1377 O ARG A 169 4917 4544 5878 1400 480 -909 O ATOM 1378 CB ARG A 169 25.910 16.861 142.955 1.00 36.27 C ANISOU 1378 CB ARG A 169 4075 4247 5458 1116 587 -659 C ATOM 1379 CG ARG A 169 25.982 18.357 142.728 1.00 36.62 C ANISOU 1379 CG ARG A 169 4092 4374 5447 966 753 -579 C ATOM 1380 CD ARG A 169 27.373 18.771 143.136 1.00 39.25 C ANISOU 1380 CD ARG A 169 4141 4791 5980 932 847 -602 C ATOM 1381 NE ARG A 169 27.541 20.191 143.422 1.00 40.37 N ANISOU 1381 NE ARG A 169 4210 4967 6161 740 957 -534 N ATOM 1382 CZ ARG A 169 28.436 20.659 144.295 1.00 41.95 C ANISOU 1382 CZ ARG A 169 4161 5230 6549 639 935 -562 C ATOM 1383 NH1 ARG A 169 29.217 19.816 144.974 1.00 43.16 N ANISOU 1383 NH1 ARG A 169 4109 5445 6844 736 788 -629 N ATOM 1384 NH2 ARG A 169 28.544 21.963 144.503 1.00 42.03 N ANISOU 1384 NH2 ARG A 169 4121 5239 6610 445 1054 -528 N ATOM 1385 N ARG A 170 24.665 14.099 143.915 1.00 37.66 N ANISOU 1385 N ARG A 170 4478 4108 5722 1293 175 -716 N ATOM 1386 CA ARG A 170 24.736 12.652 144.079 1.00 39.67 C ANISOU 1386 CA ARG A 170 4776 4196 6102 1439 82 -775 C ATOM 1387 C ARG A 170 23.542 11.959 143.422 1.00 39.88 C ANISOU 1387 C ARG A 170 5038 4094 6018 1418 49 -870 C ATOM 1388 O ARG A 170 23.698 10.930 142.750 1.00 41.40 O ANISOU 1388 O ARG A 170 5296 4172 6263 1545 96 -1019 O ATOM 1389 CB ARG A 170 24.787 12.327 145.573 1.00 40.25 C ANISOU 1389 CB ARG A 170 4781 4208 6304 1433 -117 -632 C ATOM 1390 CG ARG A 170 24.485 10.900 145.959 1.00 42.69 C ANISOU 1390 CG ARG A 170 5198 4292 6732 1545 -234 -622 C ATOM 1391 CD ARG A 170 25.224 10.543 147.222 1.00 45.44 C ANISOU 1391 CD ARG A 170 5399 4637 7230 1642 -371 -478 C ATOM 1392 NE ARG A 170 24.854 9.226 147.738 1.00 48.10 N ANISOU 1392 NE ARG A 170 5865 4729 7684 1744 -481 -408 N ATOM 1393 CZ ARG A 170 25.656 8.163 147.733 1.00 51.01 C ANISOU 1393 CZ ARG A 170 6184 4956 8244 1976 -477 -418 C ATOM 1394 NH1 ARG A 170 26.887 8.255 147.241 1.00 52.85 N ANISOU 1394 NH1 ARG A 170 6215 5300 8566 2136 -375 -510 N ATOM 1395 NH2 ARG A 170 25.224 7.007 148.220 1.00 52.02 N ANISOU 1395 NH2 ARG A 170 6459 4819 8488 2053 -559 -331 N ATOM 1396 N TYR A 171 22.359 12.553 143.583 1.00 38.10 N ANISOU 1396 N TYR A 171 4929 3901 5646 1258 -23 -805 N ATOM 1397 CA TYR A 171 21.141 11.990 143.011 1.00 38.29 C ANISOU 1397 CA TYR A 171 5141 3844 5561 1210 -76 -903 C ATOM 1398 C TYR A 171 21.178 12.146 141.501 1.00 39.65 C ANISOU 1398 C TYR A 171 5378 4130 5559 1266 76 -1065 C ATOM 1399 O TYR A 171 20.778 11.235 140.764 1.00 40.76 O ANISOU 1399 O TYR A 171 5632 4192 5663 1310 72 -1246 O ATOM 1400 CB TYR A 171 19.880 12.676 143.543 1.00 36.04 C ANISOU 1400 CB TYR A 171 4926 3606 5161 1038 -185 -792 C ATOM 1401 CG TYR A 171 19.630 12.540 145.020 1.00 34.57 C ANISOU 1401 CG TYR A 171 4707 3336 5093 965 -329 -637 C ATOM 1402 CD1 TYR A 171 20.131 11.471 145.736 1.00 36.26 C ANISOU 1402 CD1 TYR A 171 4899 3386 5493 1048 -400 -604 C ATOM 1403 CD2 TYR A 171 18.882 13.485 145.693 1.00 32.38 C ANISOU 1403 CD2 TYR A 171 4428 3147 4728 827 -386 -515 C ATOM 1404 CE1 TYR A 171 19.922 11.366 147.088 1.00 36.16 C ANISOU 1404 CE1 TYR A 171 4866 3326 5546 994 -526 -438 C ATOM 1405 CE2 TYR A 171 18.656 13.382 147.026 1.00 32.50 C ANISOU 1405 CE2 TYR A 171 4419 3116 4813 763 -503 -383 C ATOM 1406 CZ TYR A 171 19.174 12.320 147.728 1.00 34.69 C ANISOU 1406 CZ TYR A 171 4679 3256 5246 843 -575 -336 C ATOM 1407 OH TYR A 171 18.945 12.212 149.081 1.00 34.99 O ANISOU 1407 OH TYR A 171 4706 3274 5316 790 -690 -180 O ATOM 1408 N LEU A 172 21.686 13.297 141.059 1.00 39.24 N ANISOU 1408 N LEU A 172 5253 4259 5396 1260 219 -1003 N ATOM 1409 CA LEU A 172 21.853 13.578 139.643 1.00 40.68 C ANISOU 1409 CA LEU A 172 5491 4586 5380 1327 394 -1111 C ATOM 1410 C LEU A 172 22.750 12.546 138.993 1.00 43.66 C ANISOU 1410 C LEU A 172 5841 4908 5839 1490 500 -1302 C ATOM 1411 O LEU A 172 22.468 12.107 137.887 1.00 45.53 O ANISOU 1411 O LEU A 172 6194 5194 5912 1550 565 -1480 O ATOM 1412 CB LEU A 172 22.441 14.969 139.432 1.00 39.94 C ANISOU 1412 CB LEU A 172 5308 4654 5213 1292 563 -973 C ATOM 1413 CG LEU A 172 21.483 16.120 139.706 1.00 38.21 C ANISOU 1413 CG LEU A 172 5153 4497 4866 1160 512 -810 C ATOM 1414 CD1 LEU A 172 22.247 17.430 139.875 1.00 38.37 C ANISOU 1414 CD1 LEU A 172 5059 4591 4929 1103 677 -663 C ATOM 1415 CD2 LEU A 172 20.417 16.221 138.634 1.00 38.47 C ANISOU 1415 CD2 LEU A 172 5358 4640 4619 1178 507 -857 C ATOM 1416 N GLU A 173 23.804 12.141 139.699 1.00 44.71 N ANISOU 1416 N GLU A 173 5818 4952 6220 1572 509 -1275 N ATOM 1417 CA GLU A 173 24.751 11.186 139.171 1.00 47.91 C ANISOU 1417 CA GLU A 173 6168 5294 6741 1757 623 -1446 C ATOM 1418 C GLU A 173 24.195 9.774 139.240 1.00 48.81 C ANISOU 1418 C GLU A 173 6419 5168 6960 1815 501 -1595 C ATOM 1419 O GLU A 173 24.389 8.987 138.327 1.00 51.05 O ANISOU 1419 O GLU A 173 6771 5403 7223 1933 601 -1820 O ATOM 1420 CB GLU A 173 26.091 11.297 139.901 1.00 49.77 C ANISOU 1420 CB GLU A 173 6154 5544 7213 1844 668 -1356 C ATOM 1421 CG GLU A 173 27.331 11.098 138.991 1.00 54.24 C ANISOU 1421 CG GLU A 173 6587 6204 7818 2015 910 -1499 C ATOM 1422 CD GLU A 173 28.555 11.913 139.457 1.00 55.85 C ANISOU 1422 CD GLU A 173 6503 6558 8160 2013 1010 -1384 C ATOM 1423 OE1 GLU A 173 28.371 13.049 139.977 1.00 54.49 O ANISOU 1423 OE1 GLU A 173 6280 6482 7941 1837 978 -1223 O ATOM 1424 OE2 GLU A 173 29.702 11.423 139.304 1.00 58.55 O ANISOU 1424 OE2 GLU A 173 6657 6920 8670 2184 1124 -1470 O ATOM 1425 N ASN A 174 23.470 9.457 140.300 1.00 48.02 N ANISOU 1425 N ASN A 174 6368 4909 6967 1721 301 -1479 N ATOM 1426 CA ASN A 174 22.968 8.095 140.456 1.00 50.39 C ANISOU 1426 CA ASN A 174 6798 4935 7413 1757 205 -1596 C ATOM 1427 C ASN A 174 21.750 7.793 139.582 1.00 51.17 C ANISOU 1427 C ASN A 174 7088 5024 7328 1649 175 -1790 C ATOM 1428 O ASN A 174 21.471 6.639 139.253 1.00 53.07 O ANISOU 1428 O ASN A 174 7442 5054 7668 1685 163 -1991 O ATOM 1429 CB ASN A 174 22.682 7.777 141.925 1.00 49.44 C ANISOU 1429 CB ASN A 174 6663 4642 7481 1702 26 -1385 C ATOM 1430 CG ASN A 174 23.945 7.731 142.772 1.00 50.15 C ANISOU 1430 CG ASN A 174 6560 4724 7769 1854 25 -1237 C ATOM 1431 OD1 ASN A 174 25.055 7.900 142.266 1.00 51.33 O ANISOU 1431 OD1 ASN A 174 6567 4984 7952 1997 164 -1306 O ATOM 1432 ND2 ASN A 174 23.777 7.511 144.071 1.00 49.52 N ANISOU 1432 ND2 ASN A 174 6465 4541 7811 1827 -132 -1033 N ATOM 1433 N GLY A 175 21.040 8.840 139.192 1.00 50.19 N ANISOU 1433 N GLY A 175 6993 5131 6945 1521 164 -1739 N ATOM 1434 CA GLY A 175 19.910 8.688 138.294 1.00 51.35 C ANISOU 1434 CA GLY A 175 7287 5349 6877 1432 120 -1922 C ATOM 1435 C GLY A 175 20.107 9.439 136.997 1.00 52.50 C ANISOU 1435 C GLY A 175 7449 5783 6715 1490 266 -2010 C ATOM 1436 O GLY A 175 19.148 9.998 136.470 1.00 52.32 O ANISOU 1436 O GLY A 175 7499 5942 6439 1403 209 -2018 O ATOM 1437 N LYS A 176 21.343 9.430 136.482 1.00 54.53 N ANISOU 1437 N LYS A 176 7633 6092 6991 1648 460 -2066 N ATOM 1438 CA LYS A 176 21.729 10.169 135.262 1.00 56.10 C ANISOU 1438 CA LYS A 176 7843 6574 6899 1719 651 -2115 C ATOM 1439 C LYS A 176 20.894 9.792 134.050 1.00 58.41 C ANISOU 1439 C LYS A 176 8299 6998 6897 1718 633 -2369 C ATOM 1440 O LYS A 176 20.436 10.660 133.305 1.00 57.95 O ANISOU 1440 O LYS A 176 8296 7207 6516 1698 666 -2313 O ATOM 1441 CB LYS A 176 23.239 10.047 134.961 1.00 58.12 C ANISOU 1441 CB LYS A 176 7971 6847 7266 1889 880 -2159 C ATOM 1442 CG LYS A 176 23.807 8.617 134.923 1.00 61.01 C ANISOU 1442 CG LYS A 176 8336 6979 7865 2035 908 -2400 C ATOM 1443 CD LYS A 176 25.152 8.532 134.207 1.00 63.47 C ANISOU 1443 CD LYS A 176 8536 7390 8191 2225 1173 -2510 C ATOM 1444 CE LYS A 176 25.141 7.395 133.170 1.00 67.25 C ANISOU 1444 CE LYS A 176 9144 7806 8602 2351 1260 -2884 C ATOM 1445 NZ LYS A 176 24.618 6.092 133.695 1.00 67.78 N ANISOU 1445 NZ LYS A 176 9309 7522 8923 2349 1091 -3040 N ATOM 1446 N GLU A 177 20.608 8.495 133.941 1.00 60.90 N ANISOU 1446 N GLU A 177 8693 7112 7335 1730 559 -2640 N ATOM 1447 CA GLU A 177 19.846 7.918 132.849 1.00 63.68 C ANISOU 1447 CA GLU A 177 9188 7563 7447 1715 521 -2959 C ATOM 1448 C GLU A 177 18.343 8.197 132.918 1.00 62.15 C ANISOU 1448 C GLU A 177 9057 7466 7092 1536 297 -2938 C ATOM 1449 O GLU A 177 17.583 7.641 132.142 1.00 64.73 O ANISOU 1449 O GLU A 177 9479 7870 7246 1492 216 -3223 O ATOM 1450 CB GLU A 177 20.077 6.419 132.845 1.00 67.16 C ANISOU 1450 CB GLU A 177 9682 7693 8143 1767 525 -3264 C ATOM 1451 CG GLU A 177 19.745 5.759 134.170 1.00 67.18 C ANISOU 1451 CG GLU A 177 9665 7332 8529 1670 370 -3151 C ATOM 1452 CD GLU A 177 19.960 4.253 134.127 1.00 71.62 C ANISOU 1452 CD GLU A 177 10305 7540 9369 1732 396 -3441 C ATOM 1453 OE1 GLU A 177 18.970 3.505 133.902 1.00 73.29 O ANISOU 1453 OE1 GLU A 177 10629 7625 9592 1595 282 -3680 O ATOM 1454 OE2 GLU A 177 21.127 3.816 134.290 1.00 73.57 O ANISOU 1454 OE2 GLU A 177 10491 7631 9833 1921 539 -3441 O ATOM 1455 N THR A 178 17.916 9.053 133.837 1.00 58.30 N ANISOU 1455 N THR A 178 8503 6990 6660 1435 198 -2625 N ATOM 1456 CA THR A 178 16.522 9.417 133.954 1.00 56.83 C ANISOU 1456 CA THR A 178 8344 6916 6335 1285 1 -2580 C ATOM 1457 C THR A 178 16.393 10.904 134.251 1.00 54.61 C ANISOU 1457 C THR A 178 8004 6829 5915 1275 15 -2237 C ATOM 1458 O THR A 178 15.568 11.590 133.650 1.00 55.81 O ANISOU 1458 O THR A 178 8191 7239 5776 1262 -48 -2201 O ATOM 1459 CB THR A 178 15.815 8.525 135.003 1.00 56.11 C ANISOU 1459 CB THR A 178 8245 6519 6555 1129 -169 -2614 C ATOM 1460 OG1 THR A 178 15.270 7.395 134.324 1.00 58.90 O ANISOU 1460 OG1 THR A 178 8685 6802 6894 1078 -232 -2983 O ATOM 1461 CG2 THR A 178 14.675 9.245 135.793 1.00 53.48 C ANISOU 1461 CG2 THR A 178 7862 6252 6207 972 -335 -2391 C ATOM 1462 N LEU A 179 17.236 11.421 135.138 1.00 51.59 N ANISOU 1462 N LEU A 179 7532 6332 5739 1294 103 -1995 N ATOM 1463 CA LEU A 179 17.137 12.821 135.514 1.00 48.55 C ANISOU 1463 CA LEU A 179 7096 6078 5274 1266 130 -1692 C ATOM 1464 C LEU A 179 17.745 13.765 134.473 1.00 49.18 C ANISOU 1464 C LEU A 179 7199 6402 5087 1383 334 -1612 C ATOM 1465 O LEU A 179 17.323 14.917 134.332 1.00 48.21 O ANISOU 1465 O LEU A 179 7091 6435 4792 1376 353 -1405 O ATOM 1466 CB LEU A 179 17.791 13.040 136.870 1.00 46.02 C ANISOU 1466 CB LEU A 179 6663 5561 5262 1221 138 -1493 C ATOM 1467 CG LEU A 179 17.027 12.518 138.077 1.00 44.14 C ANISOU 1467 CG LEU A 179 6408 5128 5237 1090 -56 -1452 C ATOM 1468 CD1 LEU A 179 17.976 12.519 139.246 1.00 43.39 C ANISOU 1468 CD1 LEU A 179 6205 4868 5413 1096 -27 -1303 C ATOM 1469 CD2 LEU A 179 15.810 13.390 138.356 1.00 41.93 C ANISOU 1469 CD2 LEU A 179 6136 4969 4827 984 -170 -1311 C ATOM 1470 N GLN A 180 18.734 13.273 133.742 1.00 50.61 N ANISOU 1470 N GLN A 180 7386 6605 5238 1500 506 -1767 N ATOM 1471 CA GLN A 180 19.431 14.116 132.792 1.00 51.96 C ANISOU 1471 CA GLN A 180 7572 6996 5173 1606 742 -1677 C ATOM 1472 C GLN A 180 19.044 13.744 131.372 1.00 54.49 C ANISOU 1472 C GLN A 180 8025 7557 5121 1700 769 -1899 C ATOM 1473 O GLN A 180 19.724 14.107 130.416 1.00 56.02 O ANISOU 1473 O GLN A 180 8253 7940 5093 1814 992 -1894 O ATOM 1474 CB GLN A 180 20.943 13.995 132.978 1.00 52.96 C ANISOU 1474 CB GLN A 180 7579 7027 5518 1676 959 -1670 C ATOM 1475 CG GLN A 180 21.456 14.372 134.366 1.00 50.47 C ANISOU 1475 CG GLN A 180 7110 6520 5548 1592 928 -1472 C ATOM 1476 CD GLN A 180 22.969 14.245 134.463 1.00 51.87 C ANISOU 1476 CD GLN A 180 7129 6651 5926 1673 1132 -1486 C ATOM 1477 OE1 GLN A 180 23.695 14.608 133.529 1.00 53.94 O ANISOU 1477 OE1 GLN A 180 7380 7076 6041 1756 1376 -1499 O ATOM 1478 NE2 GLN A 180 23.453 13.718 135.587 1.00 50.41 N ANISOU 1478 NE2 GLN A 180 6815 6267 6073 1657 1036 -1477 N ATOM 1479 N ARG A 181 17.952 12.999 131.248 1.00 54.69 N ANISOU 1479 N ARG A 181 8119 7587 5075 1643 545 -2107 N ATOM 1480 CA ARG A 181 17.358 12.732 129.956 1.00 57.00 C ANISOU 1480 CA ARG A 181 8528 8155 4975 1709 510 -2330 C ATOM 1481 C ARG A 181 16.596 13.985 129.559 1.00 55.76 C ANISOU 1481 C ARG A 181 8413 8276 4496 1732 470 -2070 C ATOM 1482 O ARG A 181 16.190 14.796 130.407 1.00 53.08 O ANISOU 1482 O ARG A 181 8019 7859 4292 1659 400 -1794 O ATOM 1483 CB ARG A 181 16.407 11.516 130.015 1.00 58.85 C ANISOU 1483 CB ARG A 181 8794 8291 5276 1608 271 -2662 C ATOM 1484 CG ARG A 181 14.904 11.836 130.351 1.00 57.79 C ANISOU 1484 CG ARG A 181 8645 8246 5067 1481 2 -2592 C ATOM 1485 CD ARG A 181 14.047 10.615 130.734 1.00 58.29 C ANISOU 1485 CD ARG A 181 8697 8123 5327 1324 -213 -2887 C ATOM 1486 NE ARG A 181 12.651 10.988 130.981 1.00 57.43 N ANISOU 1486 NE ARG A 181 8541 8148 5134 1207 -446 -2820 N ATOM 1487 CZ ARG A 181 12.081 11.122 132.182 1.00 54.72 C ANISOU 1487 CZ ARG A 181 8111 7614 5064 1070 -559 -2644 C ATOM 1488 NH1 ARG A 181 10.807 11.475 132.261 1.00 54.55 N ANISOU 1488 NH1 ARG A 181 8030 7760 4935 985 -753 -2608 N ATOM 1489 NH2 ARG A 181 12.759 10.896 133.302 1.00 52.26 N ANISOU 1489 NH2 ARG A 181 7765 6971 5120 1025 -484 -2507 N ATOM 1490 N THR A 182 16.452 14.171 128.259 1.00 57.78 N ANISOU 1490 N THR A 182 8773 8862 4319 1852 531 -2150 N ATOM 1491 CA THR A 182 15.480 15.104 127.740 1.00 57.93 C ANISOU 1491 CA THR A 182 8848 9176 3985 1902 430 -1961 C ATOM 1492 C THR A 182 14.605 14.294 126.808 1.00 60.83 C ANISOU 1492 C THR A 182 9280 9800 4032 1922 235 -2313 C ATOM 1493 O THR A 182 15.106 13.484 126.031 1.00 63.90 O ANISOU 1493 O THR A 182 9729 10264 4286 1978 324 -2622 O ATOM 1494 CB THR A 182 16.131 16.271 126.980 1.00 59.03 C ANISOU 1494 CB THR A 182 9061 9526 3841 2052 698 -1662 C ATOM 1495 OG1 THR A 182 17.139 15.769 126.096 1.00 61.99 O ANISOU 1495 OG1 THR A 182 9490 10000 4062 2152 930 -1852 O ATOM 1496 CG2 THR A 182 16.773 17.226 127.938 1.00 56.05 C ANISOU 1496 CG2 THR A 182 8607 8908 3783 1997 855 -1313 C ATOM 1497 N ASP A 183 13.295 14.457 126.936 1.00 45.53 N ANISOU 1497 N ASP A 183 4791 6774 5736 1245 650 -647 N ATOM 1498 CA ASP A 183 12.360 13.882 125.992 1.00 44.08 C ANISOU 1498 CA ASP A 183 5103 6364 5282 1364 747 -812 C ATOM 1499 C ASP A 183 11.792 15.030 125.208 1.00 42.82 C ANISOU 1499 C ASP A 183 5003 6205 5061 1090 794 -792 C ATOM 1500 O ASP A 183 11.227 15.952 125.773 1.00 40.02 O ANISOU 1500 O ASP A 183 4593 5802 4811 775 593 -795 O ATOM 1501 CB ASP A 183 11.226 13.179 126.716 1.00 41.96 C ANISOU 1501 CB ASP A 183 5181 5823 4938 1288 469 -968 C ATOM 1502 CG ASP A 183 11.688 11.978 127.486 1.00 44.01 C ANISOU 1502 CG ASP A 183 5454 6025 5241 1547 388 -972 C ATOM 1503 OD1 ASP A 183 12.881 11.639 127.374 1.00 47.60 O ANISOU 1503 OD1 ASP A 183 5660 6648 5777 1848 568 -869 O ATOM 1504 OD2 ASP A 183 10.863 11.375 128.209 1.00 42.76 O ANISOU 1504 OD2 ASP A 183 5529 5674 5044 1458 148 -1039 O ATOM 1505 N ALA A 184 11.946 14.981 123.897 1.00 45.84 N ANISOU 1505 N ALA A 184 5536 6634 5249 1243 1066 -767 N ATOM 1506 CA ALA A 184 11.405 16.018 123.043 1.00 45.99 C ANISOU 1506 CA ALA A 184 5644 6647 5182 998 1109 -718 C ATOM 1507 C ALA A 184 9.893 15.871 123.018 1.00 43.72 C ANISOU 1507 C ALA A 184 5777 6080 4755 839 866 -878 C ATOM 1508 O ALA A 184 9.372 14.768 123.230 1.00 43.37 O ANISOU 1508 O ALA A 184 6030 5854 4595 963 746 -1015 O ATOM 1509 CB ALA A 184 11.985 15.900 121.642 1.00 49.36 C ANISOU 1509 CB ALA A 184 6154 7227 5375 1233 1478 -633 C ATOM 1510 N PRO A 185 9.184 16.994 122.837 1.00 42.73 N ANISOU 1510 N PRO A 185 5649 5918 4670 552 764 -823 N ATOM 1511 CA PRO A 185 7.767 16.947 122.531 1.00 41.50 C ANISOU 1511 CA PRO A 185 5827 5570 4371 423 578 -892 C ATOM 1512 C PRO A 185 7.465 16.183 121.236 1.00 44.35 C ANISOU 1512 C PRO A 185 6610 5846 4397 552 662 -945 C ATOM 1513 O PRO A 185 8.160 16.351 120.232 1.00 47.82 O ANISOU 1513 O PRO A 185 7086 6404 4680 675 923 -886 O ATOM 1514 CB PRO A 185 7.395 18.433 122.352 1.00 40.61 C ANISOU 1514 CB PRO A 185 5589 5472 4367 177 535 -771 C ATOM 1515 CG PRO A 185 8.673 19.212 122.452 1.00 41.80 C ANISOU 1515 CG PRO A 185 5395 5793 4696 134 688 -639 C ATOM 1516 CD PRO A 185 9.620 18.353 123.197 1.00 42.60 C ANISOU 1516 CD PRO A 185 5298 6003 4885 316 739 -680 C ATOM 1517 N LYS A 186 6.467 15.310 121.274 1.00 44.30 N ANISOU 1517 N LYS A 186 6938 5637 4256 517 432 -1040 N ATOM 1518 CA LYS A 186 5.837 14.868 120.050 1.00 45.72 C ANISOU 1518 CA LYS A 186 7586 5681 4105 503 376 -1076 C ATOM 1519 C LYS A 186 4.768 15.915 119.775 1.00 44.66 C ANISOU 1519 C LYS A 186 7389 5563 4015 209 206 -936 C ATOM 1520 O LYS A 186 3.964 16.227 120.654 1.00 42.96 O ANISOU 1520 O LYS A 186 6980 5337 4006 48 5 -876 O ATOM 1521 CB LYS A 186 5.203 13.502 120.237 1.00 46.52 C ANISOU 1521 CB LYS A 186 8080 5527 4070 516 120 -1193 C ATOM 1522 CG LYS A 186 6.179 12.394 120.546 1.00 48.99 C ANISOU 1522 CG LYS A 186 8514 5758 4342 854 254 -1330 C ATOM 1523 CD LYS A 186 5.441 11.066 120.671 1.00 50.72 C ANISOU 1523 CD LYS A 186 9214 5640 4419 807 -68 -1425 C ATOM 1524 CE LYS A 186 6.068 10.167 121.735 1.00 51.53 C ANISOU 1524 CE LYS A 186 9235 5662 4682 1021 -71 -1479 C ATOM 1525 NZ LYS A 186 7.545 9.958 121.554 1.00 54.24 N ANISOU 1525 NZ LYS A 186 9485 6120 5002 1487 311 -1550 N ATOM 1526 N THR A 187 4.772 16.479 118.570 1.00 46.74 N ANISOU 1526 N THR A 187 7811 5874 4075 175 309 -860 N ATOM 1527 CA THR A 187 3.847 17.557 118.223 1.00 45.91 C ANISOU 1527 CA THR A 187 7637 5786 4022 -64 161 -690 C ATOM 1528 C THR A 187 2.863 17.206 117.101 1.00 47.75 C ANISOU 1528 C THR A 187 8300 5911 3933 -196 -64 -645 C ATOM 1529 O THR A 187 3.232 16.574 116.116 1.00 51.04 O ANISOU 1529 O THR A 187 9126 6277 3990 -85 22 -736 O ATOM 1530 CB THR A 187 4.605 18.843 117.805 1.00 46.51 C ANISOU 1530 CB THR A 187 7478 6012 4181 -79 407 -548 C ATOM 1531 OG1 THR A 187 5.569 18.525 116.792 1.00 49.61 O ANISOU 1531 OG1 THR A 187 8048 6510 4291 94 700 -559 O ATOM 1532 CG2 THR A 187 5.317 19.450 118.986 1.00 44.69 C ANISOU 1532 CG2 THR A 187 6820 5852 4307 -74 489 -541 C ATOM 1533 N HIS A 188 1.612 17.630 117.270 1.00 46.55 N ANISOU 1533 N HIS A 188 8058 5735 3896 -416 -356 -491 N ATOM 1534 CA HIS A 188 0.627 17.662 116.195 1.00 48.48 C ANISOU 1534 CA HIS A 188 8596 5930 3894 -605 -617 -352 C ATOM 1535 C HIS A 188 -0.304 18.860 116.389 1.00 47.27 C ANISOU 1535 C HIS A 188 8111 5862 3987 -740 -751 -97 C ATOM 1536 O HIS A 188 -0.133 19.643 117.317 1.00 44.70 O ANISOU 1536 O HIS A 188 7412 5594 3977 -660 -622 -74 O ATOM 1537 CB HIS A 188 -0.163 16.349 116.094 1.00 50.61 C ANISOU 1537 CB HIS A 188 9221 6033 3978 -749 -975 -400 C ATOM 1538 CG HIS A 188 -1.172 16.147 117.184 1.00 50.15 C ANISOU 1538 CG HIS A 188 8845 5997 4214 -907 -1238 -262 C ATOM 1539 ND1 HIS A 188 -0.835 15.689 118.441 1.00 48.74 N ANISOU 1539 ND1 HIS A 188 8438 5820 4260 -801 -1148 -362 N ATOM 1540 CD2 HIS A 188 -2.517 16.314 117.194 1.00 51.03 C ANISOU 1540 CD2 HIS A 188 8807 6169 4414 -1154 -1578 11 C ATOM 1541 CE1 HIS A 188 -1.929 15.595 119.179 1.00 48.57 C ANISOU 1541 CE1 HIS A 188 8157 5868 4431 -971 -1391 -162 C ATOM 1542 NE2 HIS A 188 -2.963 15.968 118.446 1.00 49.75 N ANISOU 1542 NE2 HIS A 188 8316 6068 4517 -1178 -1645 79 N ATOM 1543 N MET A 189 -1.290 19.003 115.512 1.00 49.10 N ANISOU 1543 N MET A 189 8511 6087 4056 -923 -1030 98 N ATOM 1544 CA MET A 189 -2.199 20.133 115.592 1.00 48.66 C ANISOU 1544 CA MET A 189 8150 6114 4224 -988 -1153 375 C ATOM 1545 C MET A 189 -3.596 19.641 115.270 1.00 50.36 C ANISOU 1545 C MET A 189 8413 6352 4370 -1219 -1592 604 C ATOM 1546 O MET A 189 -3.736 18.712 114.506 1.00 52.73 O ANISOU 1546 O MET A 189 9125 6562 4348 -1386 -1817 557 O ATOM 1547 CB MET A 189 -1.753 21.211 114.606 1.00 50.75 C ANISOU 1547 CB MET A 189 8511 6395 4378 -969 -1003 484 C ATOM 1548 CG MET A 189 -2.526 22.516 114.659 1.00 51.43 C ANISOU 1548 CG MET A 189 8324 6509 4709 -970 -1094 766 C ATOM 1549 SD MET A 189 -1.835 23.742 113.545 1.00 54.61 S ANISOU 1549 SD MET A 189 8876 6887 4987 -978 -914 913 S ATOM 1550 CE MET A 189 -0.257 24.049 114.281 1.00 52.00 C ANISOU 1550 CE MET A 189 8394 6534 4829 -847 -498 693 C ATOM 1551 N THR A 190 -4.632 20.204 115.890 1.00 50.35 N ANISOU 1551 N THR A 190 7998 6471 4661 -1225 -1728 863 N ATOM 1552 CA THR A 190 -6.005 19.856 115.512 1.00 53.54 C ANISOU 1552 CA THR A 190 8340 6967 5034 -1472 -2167 1189 C ATOM 1553 C THR A 190 -6.787 21.080 115.057 1.00 55.14 C ANISOU 1553 C THR A 190 8301 7287 5365 -1429 -2256 1534 C ATOM 1554 O THR A 190 -6.480 22.210 115.443 1.00 53.81 O ANISOU 1554 O THR A 190 7925 7114 5407 -1170 -1979 1528 O ATOM 1555 CB THR A 190 -6.805 19.173 116.651 1.00 53.77 C ANISOU 1555 CB THR A 190 8017 7118 5295 -1534 -2310 1318 C ATOM 1556 OG1 THR A 190 -7.115 20.131 117.673 1.00 53.01 O ANISOU 1556 OG1 THR A 190 7423 7179 5539 -1255 -2077 1434 O ATOM 1557 CG2 THR A 190 -6.047 17.983 117.249 1.00 51.75 C ANISOU 1557 CG2 THR A 190 7982 6723 4958 -1552 -2230 1004 C ATOM 1558 N HIS A 191 -7.808 20.838 114.243 1.00 58.55 N ANISOU 1558 N HIS A 191 8784 7796 5667 -1693 -2685 1848 N ATOM 1559 CA HIS A 191 -8.632 21.901 113.672 1.00 60.73 C ANISOU 1559 CA HIS A 191 8843 8190 6039 -1663 -2840 2235 C ATOM 1560 C HIS A 191 -10.100 21.633 113.976 1.00 63.87 C ANISOU 1560 C HIS A 191 8794 8836 6638 -1810 -3216 2682 C ATOM 1561 O HIS A 191 -10.624 20.573 113.630 1.00 66.43 O ANISOU 1561 O HIS A 191 9258 9185 6796 -2186 -3629 2798 O ATOM 1562 CB HIS A 191 -8.414 21.975 112.160 1.00 62.73 C ANISOU 1562 CB HIS A 191 9597 8348 5890 -1864 -3036 2267 C ATOM 1563 CG HIS A 191 -9.419 22.820 111.446 1.00 65.67 C ANISOU 1563 CG HIS A 191 9788 8850 6314 -1919 -3334 2730 C ATOM 1564 ND1 HIS A 191 -10.501 22.287 110.780 1.00 69.55 N ANISOU 1564 ND1 HIS A 191 10297 9461 6668 -2266 -3891 3077 N ATOM 1565 CD2 HIS A 191 -9.517 24.162 111.311 1.00 65.92 C ANISOU 1565 CD2 HIS A 191 9618 8894 6534 -1674 -3189 2933 C ATOM 1566 CE1 HIS A 191 -11.221 23.266 110.267 1.00 72.17 C ANISOU 1566 CE1 HIS A 191 10398 9916 7108 -2209 -4059 3488 C ATOM 1567 NE2 HIS A 191 -10.644 24.413 110.571 1.00 69.76 N ANISOU 1567 NE2 HIS A 191 9977 9529 6999 -1832 -3629 3400 N ATOM 1568 N HIS A 192 -10.764 22.579 114.633 1.00 64.96 N ANISOU 1568 N HIS A 192 8401 9153 7126 -1509 -3082 2954 N ATOM 1569 CA HIS A 192 -12.155 22.388 115.043 1.00 69.17 C ANISOU 1569 CA HIS A 192 8378 10012 7893 -1570 -3354 3445 C ATOM 1570 C HIS A 192 -12.999 23.648 114.850 1.00 72.19 C ANISOU 1570 C HIS A 192 8357 10565 8506 -1274 -3363 3872 C ATOM 1571 O HIS A 192 -12.574 24.751 115.178 1.00 70.44 O ANISOU 1571 O HIS A 192 8122 10219 8425 -850 -2996 3735 O ATOM 1572 CB HIS A 192 -12.234 21.887 116.496 1.00 68.43 C ANISOU 1572 CB HIS A 192 7927 10057 8017 -1418 -3111 3368 C ATOM 1573 CG HIS A 192 -11.670 20.510 116.691 1.00 68.01 C ANISOU 1573 CG HIS A 192 8206 9862 7772 -1745 -3211 3075 C ATOM 1574 ND1 HIS A 192 -12.182 19.397 116.049 1.00 71.30 N ANISOU 1574 ND1 HIS A 192 8811 10274 8004 -2256 -3727 3255 N ATOM 1575 CD2 HIS A 192 -10.623 20.070 117.430 1.00 64.39 C ANISOU 1575 CD2 HIS A 192 7968 9226 7272 -1630 -2895 2622 C ATOM 1576 CE1 HIS A 192 -11.480 18.331 116.393 1.00 69.54 C ANISOU 1576 CE1 HIS A 192 8941 9845 7636 -2406 -3703 2909 C ATOM 1577 NE2 HIS A 192 -10.532 18.711 117.234 1.00 65.62 N ANISOU 1577 NE2 HIS A 192 8434 9267 7233 -2019 -3191 2537 N ATOM 1578 N ALA A 193 -14.196 23.473 114.304 1.00 77.32 N ANISOU 1578 N ALA A 193 8699 11480 9199 -1508 -3819 4410 N ATOM 1579 CA ALA A 193 -15.098 24.594 114.063 1.00 81.61 C ANISOU 1579 CA ALA A 193 8815 12220 9974 -1208 -3874 4892 C ATOM 1580 C ALA A 193 -15.753 25.081 115.362 1.00 82.88 C ANISOU 1580 C ALA A 193 8317 12657 10516 -693 -3526 5105 C ATOM 1581 O ALA A 193 -15.805 24.343 116.353 1.00 81.33 O ANISOU 1581 O ALA A 193 7898 12609 10392 -712 -3381 5026 O ATOM 1582 CB ALA A 193 -16.156 24.206 113.047 1.00 86.63 C ANISOU 1582 CB ALA A 193 9300 13087 10529 -1650 -4519 5445 C ATOM 1583 N VAL A 194 -16.219 26.332 115.357 1.00 85.57 N ANISOU 1583 N VAL A 194 8396 13048 11071 -199 -3374 5365 N ATOM 1584 CA VAL A 194 -16.975 26.888 116.481 1.00 88.08 C ANISOU 1584 CA VAL A 194 8106 13651 11709 390 -3037 5622 C ATOM 1585 C VAL A 194 -18.154 27.670 115.948 1.00 94.00 C ANISOU 1585 C VAL A 194 8371 14676 12669 645 -3249 6282 C ATOM 1586 O VAL A 194 -19.122 27.920 116.661 1.00 98.26 O ANISOU 1586 O VAL A 194 8255 15612 13470 1070 -3089 6706 O ATOM 1587 CB VAL A 194 -16.120 27.784 117.413 1.00 85.29 C ANISOU 1587 CB VAL A 194 8024 12970 11412 969 -2459 5117 C ATOM 1588 CG1 VAL A 194 -15.516 26.966 118.572 1.00 81.22 C ANISOU 1588 CG1 VAL A 194 7568 12461 10832 924 -2170 4704 C ATOM 1589 CG2 VAL A 194 -15.044 28.493 116.636 1.00 82.88 C ANISOU 1589 CG2 VAL A 194 8374 12163 10953 912 -2438 4742 C ATOM 1590 N SER A 195 -18.049 28.058 114.682 1.00 95.27 N ANISOU 1590 N SER A 195 8856 14645 12698 411 -3594 6386 N ATOM 1591 CA SER A 195 -19.172 28.573 113.903 1.00100.97 C ANISOU 1591 CA SER A 195 9156 15642 13567 472 -3970 7076 C ATOM 1592 C SER A 195 -18.900 28.191 112.451 1.00100.97 C ANISOU 1592 C SER A 195 9650 15477 13237 -183 -4519 7096 C ATOM 1593 O SER A 195 -18.023 27.375 112.175 1.00 97.07 O ANISOU 1593 O SER A 195 9712 14745 12423 -650 -4588 6634 O ATOM 1594 CB SER A 195 -19.312 30.093 114.047 1.00103.19 C ANISOU 1594 CB SER A 195 9380 15757 14072 1232 -3650 7176 C ATOM 1595 OG SER A 195 -18.538 30.783 113.080 1.00101.96 O ANISOU 1595 OG SER A 195 9869 15139 13731 1132 -3743 6950 O ATOM 1596 N ASP A 196 -19.641 28.773 111.520 1.00105.64 N ANISOU 1596 N ASP A 196 10067 16195 13876 -186 -4904 7634 N ATOM 1597 CA ASP A 196 -19.401 28.495 110.110 1.00106.34 C ANISOU 1597 CA ASP A 196 10685 16130 13590 -773 -5427 7664 C ATOM 1598 C ASP A 196 -18.247 29.341 109.578 1.00102.97 C ANISOU 1598 C ASP A 196 10975 15200 12949 -616 -5155 7214 C ATOM 1599 O ASP A 196 -17.576 28.964 108.616 1.00101.90 O ANISOU 1599 O ASP A 196 11467 14856 12396 -1074 -5375 6980 O ATOM 1600 CB ASP A 196 -20.675 28.728 109.301 1.00113.56 C ANISOU 1600 CB ASP A 196 11117 17412 14617 -900 -6016 8472 C ATOM 1601 CG ASP A 196 -21.650 29.627 110.018 1.00117.69 C ANISOU 1601 CG ASP A 196 10824 18256 15637 -187 -5776 8994 C ATOM 1602 OD1 ASP A 196 -21.503 29.786 111.251 1.00115.17 O ANISOU 1602 OD1 ASP A 196 10260 17955 15545 317 -5205 8752 O ATOM 1603 OD2 ASP A 196 -22.556 30.173 109.355 1.00123.77 O ANISOU 1603 OD2 ASP A 196 11215 19264 16547 -98 -6152 9649 O ATOM 1604 N HIS A 197 -18.014 30.478 110.227 1.00101.61 N ANISOU 1604 N HIS A 197 10726 14832 13048 37 -4673 7105 N ATOM 1605 CA HIS A 197 -16.958 31.402 109.833 1.00 98.75 C ANISOU 1605 CA HIS A 197 10976 13986 12558 190 -4417 6755 C ATOM 1606 C HIS A 197 -15.860 31.556 110.882 1.00 92.79 C ANISOU 1606 C HIS A 197 10485 12912 11858 451 -3836 6115 C ATOM 1607 O HIS A 197 -15.065 32.497 110.819 1.00 91.64 O ANISOU 1607 O HIS A 197 10734 12366 11719 665 -3583 5883 O ATOM 1608 CB HIS A 197 -17.531 32.773 109.472 1.00103.95 C ANISOU 1608 CB HIS A 197 11488 14555 13455 668 -4464 7207 C ATOM 1609 CG HIS A 197 -18.977 32.946 109.824 1.00109.81 C ANISOU 1609 CG HIS A 197 11437 15732 14555 1038 -4624 7844 C ATOM 1610 ND1 HIS A 197 -19.975 32.942 108.871 1.00115.52 N ANISOU 1610 ND1 HIS A 197 11846 16768 15278 835 -5186 8513 N ATOM 1611 CD2 HIS A 197 -19.593 33.150 111.015 1.00111.22 C ANISOU 1611 CD2 HIS A 197 11050 16120 15090 1623 -4284 7952 C ATOM 1612 CE1 HIS A 197 -21.144 33.126 109.460 1.00120.22 C ANISOU 1612 CE1 HIS A 197 11650 17773 16254 1275 -5184 9039 C ATOM 1613 NE2 HIS A 197 -20.941 33.252 110.759 1.00117.84 N ANISOU 1613 NE2 HIS A 197 11190 17426 16160 1781 -4612 8707 N ATOM 1614 N GLU A 198 -15.809 30.630 111.837 1.00 88.78 N ANISOU 1614 N GLU A 198 9768 12577 11388 391 -3666 5864 N ATOM 1615 CA GLU A 198 -14.759 30.642 112.848 1.00 82.54 C ANISOU 1615 CA GLU A 198 9224 11519 10617 577 -3175 5266 C ATOM 1616 C GLU A 198 -14.262 29.237 113.158 1.00 77.98 C ANISOU 1616 C GLU A 198 8750 11046 9832 139 -3181 4920 C ATOM 1617 O GLU A 198 -15.046 28.293 113.221 1.00 79.26 O ANISOU 1617 O GLU A 198 8571 11551 9993 -114 -3453 5176 O ATOM 1618 CB GLU A 198 -15.230 31.338 114.129 1.00 83.59 C ANISOU 1618 CB GLU A 198 8976 11686 11099 1253 -2803 5297 C ATOM 1619 CG GLU A 198 -14.858 32.816 114.217 1.00 84.73 C ANISOU 1619 CG GLU A 198 9412 11394 11387 1749 -2565 5208 C ATOM 1620 CD GLU A 198 -15.028 33.397 115.617 1.00 85.37 C ANISOU 1620 CD GLU A 198 9335 11398 11703 2420 -2138 5040 C ATOM 1621 OE1 GLU A 198 -14.874 34.628 115.774 1.00 87.26 O ANISOU 1621 OE1 GLU A 198 9837 11244 12074 2885 -1979 4991 O ATOM 1622 OE2 GLU A 198 -15.308 32.628 116.563 1.00 84.42 O ANISOU 1622 OE2 GLU A 198 8879 11586 11610 2486 -1969 4958 O ATOM 1623 N ALA A 199 -12.954 29.111 113.359 1.00 72.77 N ANISOU 1623 N ALA A 199 8552 10083 9013 48 -2898 4373 N ATOM 1624 CA ALA A 199 -12.342 27.820 113.658 1.00 68.51 C ANISOU 1624 CA ALA A 199 8174 9581 8274 -301 -2869 4009 C ATOM 1625 C ALA A 199 -11.306 27.905 114.779 1.00 63.50 C ANISOU 1625 C ALA A 199 7667 8741 7720 -74 -2408 3503 C ATOM 1626 O ALA A 199 -10.645 28.928 114.939 1.00 62.33 O ANISOU 1626 O ALA A 199 7716 8311 7656 179 -2158 3330 O ATOM 1627 CB ALA A 199 -11.710 27.241 112.405 1.00 68.44 C ANISOU 1627 CB ALA A 199 8685 9462 7857 -776 -3102 3887 C ATOM 1628 N THR A 200 -11.177 26.829 115.555 1.00 60.57 N ANISOU 1628 N THR A 200 7194 8496 7323 -196 -2343 3295 N ATOM 1629 CA THR A 200 -10.123 26.732 116.575 1.00 56.22 C ANISOU 1629 CA THR A 200 6789 7772 6800 -54 -1967 2816 C ATOM 1630 C THR A 200 -8.937 25.909 116.073 1.00 53.12 C ANISOU 1630 C THR A 200 6835 7226 6122 -406 -1955 2451 C ATOM 1631 O THR A 200 -9.093 24.741 115.728 1.00 53.44 O ANISOU 1631 O THR A 200 6956 7374 5975 -728 -2180 2456 O ATOM 1632 CB THR A 200 -10.613 26.083 117.904 1.00 55.34 C ANISOU 1632 CB THR A 200 6298 7893 6834 96 -1842 2803 C ATOM 1633 OG1 THR A 200 -11.859 26.656 118.310 1.00 59.46 O ANISOU 1633 OG1 THR A 200 6343 8664 7584 441 -1845 3218 O ATOM 1634 CG2 THR A 200 -9.602 26.299 119.011 1.00 51.97 C ANISOU 1634 CG2 THR A 200 6021 7271 6452 325 -1467 2352 C ATOM 1635 N LEU A 201 -7.752 26.510 116.034 1.00 50.69 N ANISOU 1635 N LEU A 201 6817 6664 5781 -337 -1700 2159 N ATOM 1636 CA LEU A 201 -6.536 25.741 115.797 1.00 48.06 C ANISOU 1636 CA LEU A 201 6807 6237 5215 -558 -1585 1813 C ATOM 1637 C LEU A 201 -5.872 25.409 117.137 1.00 45.37 C ANISOU 1637 C LEU A 201 6366 5863 5011 -413 -1323 1483 C ATOM 1638 O LEU A 201 -5.476 26.314 117.878 1.00 44.90 O ANISOU 1638 O LEU A 201 6254 5666 5141 -179 -1117 1371 O ATOM 1639 CB LEU A 201 -5.556 26.527 114.931 1.00 47.89 C ANISOU 1639 CB LEU A 201 7095 6030 5070 -612 -1456 1759 C ATOM 1640 CG LEU A 201 -5.805 26.748 113.445 1.00 50.43 C ANISOU 1640 CG LEU A 201 7659 6367 5136 -806 -1667 2018 C ATOM 1641 CD1 LEU A 201 -4.771 27.729 112.912 1.00 50.76 C ANISOU 1641 CD1 LEU A 201 7918 6233 5136 -806 -1454 1999 C ATOM 1642 CD2 LEU A 201 -5.767 25.442 112.667 1.00 50.57 C ANISOU 1642 CD2 LEU A 201 7955 6490 4769 -1086 -1845 1942 C ATOM 1643 N ARG A 202 -5.751 24.123 117.457 1.00 43.90 N ANISOU 1643 N ARG A 202 6196 5770 4713 -560 -1368 1334 N ATOM 1644 CA ARG A 202 -5.140 23.736 118.728 1.00 41.65 C ANISOU 1644 CA ARG A 202 5817 5472 4538 -434 -1153 1053 C ATOM 1645 C ARG A 202 -3.784 23.086 118.527 1.00 39.80 C ANISOU 1645 C ARG A 202 5855 5133 4135 -547 -1010 741 C ATOM 1646 O ARG A 202 -3.686 22.068 117.866 1.00 39.40 O ANISOU 1646 O ARG A 202 6023 5094 3851 -731 -1133 700 O ATOM 1647 CB ARG A 202 -6.058 22.809 119.533 1.00 42.04 C ANISOU 1647 CB ARG A 202 5605 5721 4649 -455 -1280 1165 C ATOM 1648 CG ARG A 202 -5.460 22.332 120.866 1.00 39.66 C ANISOU 1648 CG ARG A 202 5226 5421 4420 -335 -1078 901 C ATOM 1649 CD ARG A 202 -6.525 21.772 121.809 1.00 40.79 C ANISOU 1649 CD ARG A 202 5030 5806 4663 -289 -1148 1107 C ATOM 1650 NE ARG A 202 -7.429 22.818 122.282 1.00 42.81 N ANISOU 1650 NE ARG A 202 4979 6195 5091 22 -1053 1338 N ATOM 1651 CZ ARG A 202 -8.718 22.894 121.974 1.00 46.07 C ANISOU 1651 CZ ARG A 202 5087 6842 5576 23 -1224 1758 C ATOM 1652 NH1 ARG A 202 -9.271 21.965 121.207 1.00 46.96 N ANISOU 1652 NH1 ARG A 202 5180 7063 5601 -354 -1560 1994 N ATOM 1653 NH2 ARG A 202 -9.455 23.900 122.436 1.00 48.67 N ANISOU 1653 NH2 ARG A 202 5146 7287 6059 410 -1076 1955 N ATOM 1654 N CYS A 203 -2.754 23.684 119.122 1.00 39.11 N ANISOU 1654 N CYS A 203 5760 4937 4161 -421 -766 538 N ATOM 1655 CA CYS A 203 -1.379 23.224 118.988 1.00 39.22 C ANISOU 1655 CA CYS A 203 5933 4904 4067 -479 -591 302 C ATOM 1656 C CYS A 203 -0.971 22.342 120.175 1.00 38.06 C ANISOU 1656 C CYS A 203 5682 4795 3985 -411 -523 86 C ATOM 1657 O CYS A 203 -1.055 22.785 121.298 1.00 37.21 O ANISOU 1657 O CYS A 203 5398 4678 4062 -280 -472 33 O ATOM 1658 CB CYS A 203 -0.458 24.433 118.933 1.00 39.86 C ANISOU 1658 CB CYS A 203 6017 4865 4263 -450 -421 285 C ATOM 1659 SG CYS A 203 1.242 24.003 118.597 1.00 41.06 S ANISOU 1659 SG CYS A 203 6249 5051 4300 -522 -181 124 S ATOM 1660 N TRP A 204 -0.482 21.130 119.915 1.00 38.08 N ANISOU 1660 N TRP A 204 5842 4816 3810 -475 -521 -42 N ATOM 1661 CA TRP A 204 -0.286 20.111 120.947 1.00 37.04 C ANISOU 1661 CA TRP A 204 5644 4709 3720 -426 -522 -192 C ATOM 1662 C TRP A 204 1.164 19.697 121.206 1.00 37.05 C ANISOU 1662 C TRP A 204 5680 4690 3707 -340 -318 -405 C ATOM 1663 O TRP A 204 1.907 19.433 120.263 1.00 38.45 O ANISOU 1663 O TRP A 204 6045 4855 3709 -332 -204 -451 O ATOM 1664 CB TRP A 204 -0.971 18.846 120.484 1.00 38.25 C ANISOU 1664 CB TRP A 204 5998 4850 3684 -563 -748 -144 C ATOM 1665 CG TRP A 204 -2.393 18.759 120.773 1.00 39.02 C ANISOU 1665 CG TRP A 204 5931 5037 3857 -669 -991 94 C ATOM 1666 CD1 TRP A 204 -3.412 18.964 119.910 1.00 40.91 C ANISOU 1666 CD1 TRP A 204 6201 5317 4025 -820 -1219 341 C ATOM 1667 CD2 TRP A 204 -2.980 18.379 122.010 1.00 38.24 C ANISOU 1667 CD2 TRP A 204 5574 5045 3909 -639 -1037 163 C ATOM 1668 NE1 TRP A 204 -4.610 18.754 120.541 1.00 41.56 N ANISOU 1668 NE1 TRP A 204 6000 5551 4239 -886 -1402 591 N ATOM 1669 CE2 TRP A 204 -4.366 18.388 121.834 1.00 39.83 C ANISOU 1669 CE2 TRP A 204 5606 5383 4146 -769 -1269 486 C ATOM 1670 CE3 TRP A 204 -2.463 18.047 123.259 1.00 37.17 C ANISOU 1670 CE3 TRP A 204 5318 4935 3871 -516 -904 17 C ATOM 1671 CZ2 TRP A 204 -5.240 18.082 122.853 1.00 40.72 C ANISOU 1671 CZ2 TRP A 204 5402 5682 4387 -765 -1327 685 C ATOM 1672 CZ3 TRP A 204 -3.332 17.745 124.273 1.00 37.40 C ANISOU 1672 CZ3 TRP A 204 5096 5120 3993 -513 -971 182 C ATOM 1673 CH2 TRP A 204 -4.707 17.755 124.062 1.00 39.49 C ANISOU 1673 CH2 TRP A 204 5167 5546 4290 -631 -1160 522 C ATOM 1674 N ALA A 205 1.558 19.562 122.471 1.00 35.71 N ANISOU 1674 N ALA A 205 5330 4543 3694 -253 -271 -514 N ATOM 1675 CA ALA A 205 2.839 18.910 122.776 1.00 35.78 C ANISOU 1675 CA ALA A 205 5334 4564 3697 -165 -132 -670 C ATOM 1676 C ALA A 205 2.677 17.768 123.786 1.00 35.40 C ANISOU 1676 C ALA A 205 5272 4515 3665 -116 -232 -747 C ATOM 1677 O ALA A 205 2.088 17.952 124.851 1.00 34.39 O ANISOU 1677 O ALA A 205 4989 4430 3647 -116 -311 -717 O ATOM 1678 CB ALA A 205 3.833 19.909 123.271 1.00 35.03 C ANISOU 1678 CB ALA A 205 5034 4497 3779 -146 -2 -698 C ATOM 1679 N LEU A 206 3.193 16.589 123.451 1.00 36.23 N ANISOU 1679 N LEU A 206 5570 4562 3635 -48 -217 -834 N ATOM 1680 CA LEU A 206 3.060 15.428 124.336 1.00 36.50 C ANISOU 1680 CA LEU A 206 5643 4547 3679 -15 -341 -877 C ATOM 1681 C LEU A 206 4.396 14.709 124.585 1.00 37.90 C ANISOU 1681 C LEU A 206 5832 4709 3861 191 -202 -1006 C ATOM 1682 O LEU A 206 5.341 14.847 123.784 1.00 39.80 O ANISOU 1682 O LEU A 206 6108 4980 4034 325 4 -1051 O ATOM 1683 CB LEU A 206 2.073 14.418 123.745 1.00 37.66 C ANISOU 1683 CB LEU A 206 6105 4553 3650 -150 -576 -816 C ATOM 1684 CG LEU A 206 0.762 14.840 123.074 1.00 37.76 C ANISOU 1684 CG LEU A 206 6160 4584 3604 -367 -763 -635 C ATOM 1685 CD1 LEU A 206 0.291 13.775 122.101 1.00 39.86 C ANISOU 1685 CD1 LEU A 206 6867 4655 3625 -510 -1004 -625 C ATOM 1686 CD2 LEU A 206 -0.304 15.127 124.111 1.00 36.71 C ANISOU 1686 CD2 LEU A 206 5716 4595 3638 -464 -880 -447 C ATOM 1687 N SER A 207 4.445 13.952 125.691 1.00 37.01 N ANISOU 1687 N SER A 207 5663 4576 3823 233 -304 -1023 N ATOM 1688 CA SER A 207 5.556 13.048 126.064 1.00 37.95 C ANISOU 1688 CA SER A 207 5801 4660 3959 454 -233 -1105 C ATOM 1689 C SER A 207 6.910 13.697 126.298 1.00 37.43 C ANISOU 1689 C SER A 207 5416 4770 4034 595 -28 -1118 C ATOM 1690 O SER A 207 7.945 13.177 125.876 1.00 39.53 O ANISOU 1690 O SER A 207 5693 5056 4271 835 137 -1146 O ATOM 1691 CB SER A 207 5.715 11.900 125.063 1.00 41.26 C ANISOU 1691 CB SER A 207 6648 4867 4163 605 -226 -1186 C ATOM 1692 OG SER A 207 4.558 11.098 125.041 1.00 43.01 O ANISOU 1692 OG SER A 207 7177 4885 4279 417 -511 -1145 O ATOM 1693 N PHE A 208 6.906 14.825 126.979 1.00 35.14 N ANISOU 1693 N PHE A 208 4850 4606 3894 456 -50 -1077 N ATOM 1694 CA PHE A 208 8.129 15.576 127.152 1.00 35.09 C ANISOU 1694 CA PHE A 208 4540 4754 4037 482 68 -1041 C ATOM 1695 C PHE A 208 8.549 15.725 128.617 1.00 34.72 C ANISOU 1695 C PHE A 208 4274 4782 4134 442 -82 -1040 C ATOM 1696 O PHE A 208 7.713 15.708 129.532 1.00 32.81 O ANISOU 1696 O PHE A 208 4106 4498 3864 366 -240 -1071 O ATOM 1697 CB PHE A 208 8.051 16.931 126.420 1.00 34.99 C ANISOU 1697 CB PHE A 208 4461 4776 4055 319 151 -982 C ATOM 1698 CG PHE A 208 6.958 17.851 126.918 1.00 32.97 C ANISOU 1698 CG PHE A 208 4254 4445 3829 147 2 -992 C ATOM 1699 CD1 PHE A 208 7.214 18.782 127.923 1.00 32.52 C ANISOU 1699 CD1 PHE A 208 4054 4397 3904 47 -102 -1008 C ATOM 1700 CD2 PHE A 208 5.688 17.816 126.354 1.00 31.58 C ANISOU 1700 CD2 PHE A 208 4281 4183 3533 103 -44 -973 C ATOM 1701 CE1 PHE A 208 6.217 19.628 128.370 1.00 31.67 C ANISOU 1701 CE1 PHE A 208 4045 4201 3786 -15 -195 -1035 C ATOM 1702 CE2 PHE A 208 4.696 18.654 126.799 1.00 30.50 C ANISOU 1702 CE2 PHE A 208 4143 4014 3431 26 -137 -946 C ATOM 1703 CZ PHE A 208 4.950 19.554 127.814 1.00 30.59 C ANISOU 1703 CZ PHE A 208 4050 4022 3553 6 -186 -992 C ATOM 1704 N TYR A 209 9.863 15.851 128.800 1.00 37.11 N ANISOU 1704 N TYR A 209 4298 5230 4572 499 -27 -971 N ATOM 1705 CA TYR A 209 10.540 16.028 130.091 1.00 37.74 C ANISOU 1705 CA TYR A 209 4150 5406 4784 437 -206 -938 C ATOM 1706 C TYR A 209 11.762 16.907 129.818 1.00 40.35 C ANISOU 1706 C TYR A 209 4137 5904 5290 326 -157 -793 C ATOM 1707 O TYR A 209 12.486 16.675 128.849 1.00 41.58 O ANISOU 1707 O TYR A 209 4139 6187 5474 466 75 -679 O ATOM 1708 CB TYR A 209 10.991 14.691 130.698 1.00 38.62 C ANISOU 1708 CB TYR A 209 4236 5542 4895 662 -258 -917 C ATOM 1709 CG TYR A 209 11.519 14.843 132.105 1.00 39.80 C ANISOU 1709 CG TYR A 209 4200 5789 5134 573 -499 -875 C ATOM 1710 CD1 TYR A 209 10.647 14.864 133.189 1.00 38.54 C ANISOU 1710 CD1 TYR A 209 4227 5556 4859 471 -689 -956 C ATOM 1711 CD2 TYR A 209 12.887 15.009 132.354 1.00 42.43 C ANISOU 1711 CD2 TYR A 209 4157 6317 5646 580 -544 -722 C ATOM 1712 CE1 TYR A 209 11.120 15.036 134.481 1.00 39.73 C ANISOU 1712 CE1 TYR A 209 4279 5793 5024 388 -926 -931 C ATOM 1713 CE2 TYR A 209 13.363 15.183 133.629 1.00 43.62 C ANISOU 1713 CE2 TYR A 209 4170 6550 5853 453 -830 -674 C ATOM 1714 CZ TYR A 209 12.478 15.200 134.694 1.00 42.42 C ANISOU 1714 CZ TYR A 209 4291 6289 5537 359 -1025 -801 C ATOM 1715 OH TYR A 209 12.955 15.369 135.976 1.00 44.05 O ANISOU 1715 OH TYR A 209 4428 6575 5734 238 -1324 -766 O ATOM 1716 N PRO A 210 12.016 17.913 130.674 1.00 41.59 N ANISOU 1716 N PRO A 210 4187 6066 5550 69 -383 -777 N ATOM 1717 CA PRO A 210 11.263 18.365 131.848 1.00 40.61 C ANISOU 1717 CA PRO A 210 4279 5807 5344 -59 -628 -920 C ATOM 1718 C PRO A 210 10.025 19.183 131.479 1.00 39.33 C ANISOU 1718 C PRO A 210 4405 5462 5076 -128 -585 -1031 C ATOM 1719 O PRO A 210 9.727 19.332 130.303 1.00 39.58 O ANISOU 1719 O PRO A 210 4474 5465 5099 -109 -401 -991 O ATOM 1720 CB PRO A 210 12.283 19.227 132.595 1.00 43.02 C ANISOU 1720 CB PRO A 210 4386 6167 5792 -310 -883 -839 C ATOM 1721 CG PRO A 210 13.220 19.707 131.533 1.00 44.58 C ANISOU 1721 CG PRO A 210 4276 6491 6170 -420 -746 -627 C ATOM 1722 CD PRO A 210 13.317 18.603 130.554 1.00 44.38 C ANISOU 1722 CD PRO A 210 4160 6595 6108 -103 -419 -568 C ATOM 1723 N ALA A 211 9.321 19.715 132.476 1.00 39.52 N ANISOU 1723 N ALA A 211 4638 5377 4999 -174 -744 -1156 N ATOM 1724 CA ALA A 211 8.020 20.344 132.255 1.00 37.98 C ANISOU 1724 CA ALA A 211 4693 5043 4696 -136 -678 -1236 C ATOM 1725 C ALA A 211 8.081 21.747 131.678 1.00 38.87 C ANISOU 1725 C ALA A 211 4883 4992 4891 -292 -696 -1227 C ATOM 1726 O ALA A 211 7.052 22.312 131.338 1.00 39.01 O ANISOU 1726 O ALA A 211 5083 4891 4847 -226 -628 -1259 O ATOM 1727 CB ALA A 211 7.207 20.341 133.547 1.00 37.97 C ANISOU 1727 CB ALA A 211 4887 5023 4516 -36 -774 -1350 C ATOM 1728 N GLU A 212 9.272 22.314 131.571 1.00 41.22 N ANISOU 1728 N GLU A 212 5028 5289 5346 -508 -807 -1142 N ATOM 1729 CA GLU A 212 9.415 23.660 131.044 1.00 43.67 C ANISOU 1729 CA GLU A 212 5431 5409 5755 -716 -871 -1090 C ATOM 1730 C GLU A 212 9.303 23.669 129.512 1.00 43.06 C ANISOU 1730 C GLU A 212 5251 5385 5725 -711 -626 -934 C ATOM 1731 O GLU A 212 10.127 23.099 128.802 1.00 43.88 O ANISOU 1731 O GLU A 212 5078 5696 5897 -724 -480 -778 O ATOM 1732 CB GLU A 212 10.709 24.302 131.564 1.00 47.74 C ANISOU 1732 CB GLU A 212 5816 5898 6423 -1031 -1145 -1002 C ATOM 1733 CG GLU A 212 11.229 25.529 130.814 1.00 52.30 C ANISOU 1733 CG GLU A 212 6381 6322 7170 -1346 -1228 -832 C ATOM 1734 CD GLU A 212 10.351 26.778 130.936 1.00 54.23 C ANISOU 1734 CD GLU A 212 7095 6163 7346 -1374 -1355 -976 C ATOM 1735 OE1 GLU A 212 9.372 26.901 130.154 1.00 53.28 O ANISOU 1735 OE1 GLU A 212 7103 5977 7163 -1185 -1138 -988 O ATOM 1736 OE2 GLU A 212 10.676 27.666 131.769 1.00 57.22 O ANISOU 1736 OE2 GLU A 212 7735 6273 7732 -1586 -1694 -1061 O ATOM 1737 N ILE A 213 8.242 24.299 129.023 1.00 42.39 N ANISOU 1737 N ILE A 213 5404 5126 5575 -650 -570 -968 N ATOM 1738 CA ILE A 213 7.970 24.404 127.596 1.00 42.15 C ANISOU 1738 CA ILE A 213 5353 5122 5539 -653 -380 -822 C ATOM 1739 C ILE A 213 7.339 25.787 127.316 1.00 43.67 C ANISOU 1739 C ILE A 213 5796 5031 5767 -730 -466 -798 C ATOM 1740 O ILE A 213 6.966 26.502 128.248 1.00 43.98 O ANISOU 1740 O ILE A 213 6062 4846 5800 -701 -637 -936 O ATOM 1741 CB ILE A 213 7.078 23.218 127.141 1.00 39.33 C ANISOU 1741 CB ILE A 213 5026 4897 5022 -421 -218 -859 C ATOM 1742 CG1 ILE A 213 7.248 22.902 125.644 1.00 39.68 C ANISOU 1742 CG1 ILE A 213 5030 5046 5002 -427 -22 -714 C ATOM 1743 CG2 ILE A 213 5.652 23.462 127.507 1.00 37.95 C ANISOU 1743 CG2 ILE A 213 5054 4608 4760 -282 -267 -936 C ATOM 1744 CD1 ILE A 213 6.654 21.582 125.199 1.00 37.61 C ANISOU 1744 CD1 ILE A 213 4849 4877 4563 -250 71 -760 C ATOM 1745 N THR A 214 7.276 26.186 126.047 1.00 45.25 N ANISOU 1745 N THR A 214 5990 5222 5980 -809 -352 -618 N ATOM 1746 CA THR A 214 6.705 27.487 125.650 1.00 47.19 C ANISOU 1746 CA THR A 214 6478 5179 6273 -872 -438 -547 C ATOM 1747 C THR A 214 6.019 27.412 124.283 1.00 46.62 C ANISOU 1747 C THR A 214 6432 5174 6107 -809 -279 -386 C ATOM 1748 O THR A 214 6.651 27.564 123.230 1.00 48.08 O ANISOU 1748 O THR A 214 6521 5452 6296 -977 -175 -178 O ATOM 1749 CB THR A 214 7.782 28.571 125.570 1.00 49.96 C ANISOU 1749 CB THR A 214 6822 5360 6801 -1219 -594 -396 C ATOM 1750 OG1 THR A 214 9.048 27.925 125.433 1.00 50.84 O ANISOU 1750 OG1 THR A 214 6570 5768 6977 -1384 -517 -266 O ATOM 1751 CG2 THR A 214 7.794 29.443 126.820 1.00 51.91 C ANISOU 1751 CG2 THR A 214 7351 5264 7109 -1278 -891 -573 C ATOM 1752 N LEU A 215 4.716 27.186 124.313 1.00 44.92 N ANISOU 1752 N LEU A 215 6337 4939 5791 -574 -269 -448 N ATOM 1753 CA LEU A 215 3.916 27.196 123.102 1.00 43.94 C ANISOU 1753 CA LEU A 215 6270 4854 5569 -532 -202 -281 C ATOM 1754 C LEU A 215 3.513 28.639 122.776 1.00 45.90 C ANISOU 1754 C LEU A 215 6715 4808 5918 -561 -306 -150 C ATOM 1755 O LEU A 215 2.964 29.363 123.612 1.00 45.99 O ANISOU 1755 O LEU A 215 6887 4585 6001 -405 -415 -249 O ATOM 1756 CB LEU A 215 2.693 26.300 123.278 1.00 41.95 C ANISOU 1756 CB LEU A 215 6003 4739 5197 -316 -197 -333 C ATOM 1757 CG LEU A 215 2.749 24.773 123.050 1.00 40.65 C ANISOU 1757 CG LEU A 215 5746 4817 4882 -304 -126 -382 C ATOM 1758 CD1 LEU A 215 4.138 24.129 122.986 1.00 40.74 C ANISOU 1758 CD1 LEU A 215 5656 4944 4879 -392 -12 -445 C ATOM 1759 CD2 LEU A 215 1.918 24.079 124.096 1.00 39.16 C ANISOU 1759 CD2 LEU A 215 5502 4701 4676 -146 -184 -479 C ATOM 1760 N THR A 216 3.830 29.058 121.557 1.00 47.54 N ANISOU 1760 N THR A 216 6944 5015 6105 -737 -263 80 N ATOM 1761 CA THR A 216 3.437 30.363 121.047 1.00 49.35 C ANISOU 1761 CA THR A 216 7376 4955 6418 -779 -371 263 C ATOM 1762 C THR A 216 2.768 30.241 119.677 1.00 49.30 C ANISOU 1762 C THR A 216 7399 5074 6258 -769 -319 496 C ATOM 1763 O THR A 216 2.917 29.230 118.983 1.00 47.91 O ANISOU 1763 O THR A 216 7127 5189 5889 -805 -192 519 O ATOM 1764 CB THR A 216 4.634 31.295 120.957 1.00 52.19 C ANISOU 1764 CB THR A 216 7773 5129 6930 -1105 -442 393 C ATOM 1765 OG1 THR A 216 5.824 30.505 120.919 1.00 51.74 O ANISOU 1765 OG1 THR A 216 7440 5371 6847 -1284 -306 399 O ATOM 1766 CG2 THR A 216 4.688 32.183 122.181 1.00 54.10 C ANISOU 1766 CG2 THR A 216 8234 4985 7336 -1086 -660 221 C ATOM 1767 N TRP A 217 2.018 31.277 119.314 1.00 50.69 N ANISOU 1767 N TRP A 217 7756 5003 6502 -698 -441 663 N ATOM 1768 CA TRP A 217 1.242 31.310 118.092 1.00 51.07 C ANISOU 1768 CA TRP A 217 7856 5138 6411 -680 -461 915 C ATOM 1769 C TRP A 217 1.550 32.602 117.359 1.00 55.32 C ANISOU 1769 C TRP A 217 8578 5406 7033 -853 -541 1191 C ATOM 1770 O TRP A 217 1.601 33.661 117.977 1.00 57.91 O ANISOU 1770 O TRP A 217 9075 5360 7570 -822 -668 1174 O ATOM 1771 CB TRP A 217 -0.249 31.284 118.422 1.00 49.80 C ANISOU 1771 CB TRP A 217 7683 4966 6273 -355 -566 922 C ATOM 1772 CG TRP A 217 -0.891 29.936 118.384 1.00 46.93 C ANISOU 1772 CG TRP A 217 7146 4942 5745 -286 -544 861 C ATOM 1773 CD1 TRP A 217 -1.357 29.224 119.448 1.00 45.12 C ANISOU 1773 CD1 TRP A 217 6765 4830 5547 -105 -525 676 C ATOM 1774 CD2 TRP A 217 -1.163 29.140 117.218 1.00 46.76 C ANISOU 1774 CD2 TRP A 217 7132 5156 5479 -425 -576 1006 C ATOM 1775 NE1 TRP A 217 -1.896 28.028 119.022 1.00 43.80 N ANISOU 1775 NE1 TRP A 217 6493 4940 5209 -160 -566 719 N ATOM 1776 CE2 TRP A 217 -1.784 27.950 117.660 1.00 44.60 C ANISOU 1776 CE2 TRP A 217 6722 5096 5128 -354 -614 896 C ATOM 1777 CE3 TRP A 217 -0.946 29.319 115.845 1.00 48.50 C ANISOU 1777 CE3 TRP A 217 7505 5417 5505 -613 -592 1225 C ATOM 1778 CZ2 TRP A 217 -2.194 26.949 116.781 1.00 44.39 C ANISOU 1778 CZ2 TRP A 217 6751 5266 4851 -486 -716 977 C ATOM 1779 CZ3 TRP A 217 -1.339 28.319 114.976 1.00 48.61 C ANISOU 1779 CZ3 TRP A 217 7588 5655 5227 -703 -658 1279 C ATOM 1780 CH2 TRP A 217 -1.955 27.144 115.450 1.00 46.71 C ANISOU 1780 CH2 TRP A 217 7251 5570 4927 -650 -742 1143 C ATOM 1781 N GLN A 218 1.737 32.527 116.046 1.00 57.20 N ANISOU 1781 N GLN A 218 8841 5808 7084 -1033 -482 1450 N ATOM 1782 CA GLN A 218 2.024 33.719 115.259 1.00 61.36 C ANISOU 1782 CA GLN A 218 9539 6105 7668 -1232 -557 1778 C ATOM 1783 C GLN A 218 1.011 33.911 114.137 1.00 63.26 C ANISOU 1783 C GLN A 218 9905 6387 7746 -1154 -655 2056 C ATOM 1784 O GLN A 218 0.413 32.945 113.671 1.00 61.54 O ANISOU 1784 O GLN A 218 9626 6465 7291 -1067 -634 2026 O ATOM 1785 CB GLN A 218 3.421 33.628 114.657 1.00 63.18 C ANISOU 1785 CB GLN A 218 9669 6528 7809 -1578 -372 1932 C ATOM 1786 CG GLN A 218 4.553 33.790 115.645 1.00 63.97 C ANISOU 1786 CG GLN A 218 9630 6542 8132 -1753 -354 1799 C ATOM 1787 CD GLN A 218 5.914 33.790 114.959 1.00 67.17 C ANISOU 1787 CD GLN A 218 9844 7201 8475 -2096 -159 2069 C ATOM 1788 OE1 GLN A 218 6.009 33.746 113.729 1.00 69.20 O ANISOU 1788 OE1 GLN A 218 10123 7678 8494 -2180 -7 2350 O ATOM 1789 NE2 GLN A 218 6.975 33.813 115.753 1.00 67.97 N ANISOU 1789 NE2 GLN A 218 9740 7314 8772 -2287 -157 2013 N ATOM 1790 N ARG A 219 0.812 35.162 113.717 1.00 67.07 N ANISOU 1790 N ARG A 219 10589 6543 8354 -1204 -808 2342 N ATOM 1791 CA ARG A 219 0.067 35.453 112.488 1.00 69.40 C ANISOU 1791 CA ARG A 219 11007 6885 8474 -1201 -918 2692 C ATOM 1792 C ARG A 219 0.896 36.265 111.500 1.00 73.61 C ANISOU 1792 C ARG A 219 11692 7335 8942 -1545 -893 3062 C ATOM 1793 O ARG A 219 1.256 37.410 111.792 1.00 75.99 O ANISOU 1793 O ARG A 219 12144 7225 9505 -1656 -1010 3195 O ATOM 1794 CB ARG A 219 -1.244 36.173 112.763 1.00 70.68 C ANISOU 1794 CB ARG A 219 11260 6769 8827 -858 -1149 2789 C ATOM 1795 CG ARG A 219 -2.002 36.452 111.484 1.00 73.52 C ANISOU 1795 CG ARG A 219 11717 7203 9013 -871 -1305 3192 C ATOM 1796 CD ARG A 219 -3.382 36.989 111.740 1.00 75.44 C ANISOU 1796 CD ARG A 219 11948 7271 9444 -468 -1519 3325 C ATOM 1797 NE ARG A 219 -3.480 38.435 111.601 1.00 79.98 N ANISOU 1797 NE ARG A 219 12793 7357 10241 -381 -1672 3590 N ATOM 1798 CZ ARG A 219 -4.632 39.095 111.646 1.00 82.93 C ANISOU 1798 CZ ARG A 219 13194 7537 10780 16 -1852 3793 C ATOM 1799 NH1 ARG A 219 -5.765 38.426 111.833 1.00 81.84 N ANISOU 1799 NH1 ARG A 219 12758 7717 10621 322 -1895 3795 N ATOM 1800 NH2 ARG A 219 -4.655 40.416 111.508 1.00 87.24 N ANISOU 1800 NH2 ARG A 219 14052 7573 11523 111 -1999 4027 N ATOM 1801 N ASP A 220 1.201 35.649 110.350 1.00 75.01 N ANISOU 1801 N ASP A 220 11864 7892 8746 -1715 -747 3231 N ATOM 1802 CA ASP A 220 2.068 36.197 109.281 1.00 79.61 C ANISOU 1802 CA ASP A 220 12541 8547 9159 -2049 -634 3624 C ATOM 1803 C ASP A 220 3.505 36.552 109.694 1.00 82.10 C ANISOU 1803 C ASP A 220 12708 8833 9654 -2350 -462 3668 C ATOM 1804 O ASP A 220 4.172 37.323 108.994 1.00 86.26 O ANISOU 1804 O ASP A 220 13290 9325 10162 -2661 -426 4076 O ATOM 1805 CB ASP A 220 1.411 37.383 108.551 1.00 82.90 C ANISOU 1805 CB ASP A 220 13213 8657 9627 -2088 -890 4048 C ATOM 1806 CG ASP A 220 0.163 36.987 107.803 1.00 82.43 C ANISOU 1806 CG ASP A 220 13254 8757 9308 -1885 -1057 4144 C ATOM 1807 OD1 ASP A 220 0.278 36.236 106.818 1.00 83.11 O ANISOU 1807 OD1 ASP A 220 13398 9232 8947 -1985 -939 4222 O ATOM 1808 OD2 ASP A 220 -0.934 37.432 108.189 1.00 82.01 O ANISOU 1808 OD2 ASP A 220 13233 8446 9481 -1615 -1316 4159 O ATOM 1809 N GLY A 221 3.975 35.987 110.810 1.00 80.31 N ANISOU 1809 N GLY A 221 12272 8642 9600 -2284 -377 3299 N ATOM 1810 CA GLY A 221 5.280 36.331 111.383 1.00 83.43 C ANISOU 1810 CA GLY A 221 12481 8995 10224 -2581 -297 3343 C ATOM 1811 C GLY A 221 5.202 36.955 112.772 1.00 84.20 C ANISOU 1811 C GLY A 221 12649 8615 10727 -2549 -560 3096 C ATOM 1812 O GLY A 221 6.064 36.718 113.616 1.00 83.35 O ANISOU 1812 O GLY A 221 12343 8550 10774 -2677 -521 2929 O ATOM 1813 N GLU A 222 4.168 37.757 113.014 1.00 86.52 N ANISOU 1813 N GLU A 222 13246 8455 11173 -2348 -832 3080 N ATOM 1814 CA GLU A 222 4.009 38.449 114.297 1.00 88.25 C ANISOU 1814 CA GLU A 222 13657 8160 11712 -2244 -1079 2830 C ATOM 1815 C GLU A 222 3.103 37.664 115.250 1.00 84.54 C ANISOU 1815 C GLU A 222 13131 7768 11224 -1777 -1051 2382 C ATOM 1816 O GLU A 222 2.080 37.119 114.827 1.00 82.51 O ANISOU 1816 O GLU A 222 12824 7726 10801 -1483 -997 2370 O ATOM 1817 CB GLU A 222 3.459 39.861 114.070 1.00 93.21 C ANISOU 1817 CB GLU A 222 14699 8197 12518 -2229 -1371 3082 C ATOM 1818 CG GLU A 222 3.649 40.814 115.247 1.00 96.50 C ANISOU 1818 CG GLU A 222 15449 7978 13237 -2239 -1655 2890 C ATOM 1819 CD GLU A 222 2.820 42.082 115.108 1.00101.35 C ANISOU 1819 CD GLU A 222 16550 7959 13999 -2030 -1931 3054 C ATOM 1820 OE1 GLU A 222 3.100 42.894 114.192 1.00105.44 O ANISOU 1820 OE1 GLU A 222 17230 8273 14558 -2347 -2055 3502 O ATOM 1821 OE2 GLU A 222 1.887 42.264 115.922 1.00101.26 O ANISOU 1821 OE2 GLU A 222 16759 7662 14055 -1519 -2007 2755 O ATOM 1822 N ASP A 223 3.480 37.619 116.531 1.00 84.55 N ANISOU 1822 N ASP A 223 13139 7603 11383 -1743 -1112 2053 N ATOM 1823 CA ASP A 223 2.790 36.787 117.533 1.00 81.48 C ANISOU 1823 CA ASP A 223 12655 7351 10953 -1343 -1046 1648 C ATOM 1824 C ASP A 223 1.434 37.335 117.956 1.00 82.73 C ANISOU 1824 C ASP A 223 13056 7201 11176 -866 -1166 1563 C ATOM 1825 O ASP A 223 1.246 38.543 118.064 1.00 86.43 O ANISOU 1825 O ASP A 223 13887 7154 11801 -807 -1364 1656 O ATOM 1826 CB ASP A 223 3.644 36.579 118.786 1.00 80.65 C ANISOU 1826 CB ASP A 223 12504 7183 10955 -1454 -1082 1343 C ATOM 1827 CG ASP A 223 5.122 36.739 118.524 1.00 82.78 C ANISOU 1827 CG ASP A 223 12624 7526 11303 -1980 -1091 1542 C ATOM 1828 OD1 ASP A 223 5.921 36.408 119.425 1.00 82.04 O ANISOU 1828 OD1 ASP A 223 12401 7486 11283 -2119 -1126 1351 O ATOM 1829 OD2 ASP A 223 5.486 37.208 117.427 1.00 85.68 O ANISOU 1829 OD2 ASP A 223 12978 7920 11656 -2259 -1070 1929 O ATOM 1830 N GLN A 224 0.494 36.430 118.198 1.00 80.33 N ANISOU 1830 N GLN A 224 12548 7219 10756 -515 -1047 1413 N ATOM 1831 CA GLN A 224 -0.851 36.824 118.578 1.00 82.08 C ANISOU 1831 CA GLN A 224 12875 7280 11032 -11 -1103 1397 C ATOM 1832 C GLN A 224 -1.175 36.299 119.952 1.00 80.62 C ANISOU 1832 C GLN A 224 12621 7170 10843 311 -1015 1032 C ATOM 1833 O GLN A 224 -1.223 35.092 120.183 1.00 77.48 O ANISOU 1833 O GLN A 224 11912 7203 10325 300 -879 904 O ATOM 1834 CB GLN A 224 -1.883 36.335 117.567 1.00 81.46 C ANISOU 1834 CB GLN A 224 12579 7544 10828 119 -1082 1669 C ATOM 1835 CG GLN A 224 -2.312 37.398 116.578 1.00 85.48 C ANISOU 1835 CG GLN A 224 13299 7783 11397 136 -1241 2051 C ATOM 1836 CD GLN A 224 -3.755 37.223 116.171 1.00 86.37 C ANISOU 1836 CD GLN A 224 13234 8105 11476 500 -1293 2273 C ATOM 1837 OE1 GLN A 224 -4.411 36.271 116.600 1.00 83.88 O ANISOU 1837 OE1 GLN A 224 12619 8157 11094 687 -1211 2161 O ATOM 1838 NE2 GLN A 224 -4.265 38.139 115.346 1.00 90.09 N ANISOU 1838 NE2 GLN A 224 13869 8354 12008 583 -1454 2635 N ATOM 1839 N THR A 225 -1.407 37.229 120.863 1.00 84.02 N ANISOU 1839 N THR A 225 13395 7149 11380 612 -1100 871 N ATOM 1840 CA THR A 225 -1.531 36.904 122.264 1.00 83.39 C ANISOU 1840 CA THR A 225 13354 7079 11252 900 -1019 507 C ATOM 1841 C THR A 225 -2.974 36.802 122.719 1.00 84.31 C ANISOU 1841 C THR A 225 13361 7344 11328 1527 -883 515 C ATOM 1842 O THR A 225 -3.268 36.120 123.699 1.00 82.72 O ANISOU 1842 O THR A 225 13012 7391 11028 1761 -737 298 O ATOM 1843 CB THR A 225 -0.837 37.972 123.124 1.00 87.12 C ANISOU 1843 CB THR A 225 14358 6943 11799 865 -1205 276 C ATOM 1844 OG1 THR A 225 -1.456 38.012 124.416 1.00 88.35 O ANISOU 1844 OG1 THR A 225 14700 7008 11860 1384 -1121 -34 O ATOM 1845 CG2 THR A 225 -0.951 39.359 122.463 1.00 91.82 C ANISOU 1845 CG2 THR A 225 15377 6972 12539 873 -1410 507 C ATOM 1846 N GLN A 226 -3.876 37.477 122.016 1.00 87.31 N ANISOU 1846 N GLN A 226 13781 7604 11787 1804 -926 810 N ATOM 1847 CA GLN A 226 -5.192 37.721 122.594 1.00 89.90 C ANISOU 1847 CA GLN A 226 14063 7977 12119 2492 -797 845 C ATOM 1848 C GLN A 226 -6.382 37.158 121.837 1.00 89.04 C ANISOU 1848 C GLN A 226 13451 8361 12021 2668 -741 1231 C ATOM 1849 O GLN A 226 -7.420 37.811 121.701 1.00 93.17 O ANISOU 1849 O GLN A 226 13959 8811 12630 3166 -728 1472 O ATOM 1850 CB GLN A 226 -5.375 39.204 122.923 1.00 96.24 C ANISOU 1850 CB GLN A 226 15446 8106 13014 2903 -891 794 C ATOM 1851 CG GLN A 226 -4.757 39.581 124.266 1.00 97.94 C ANISOU 1851 CG GLN A 226 16146 7926 13140 3025 -894 333 C ATOM 1852 CD GLN A 226 -4.248 41.006 124.308 1.00103.27 C ANISOU 1852 CD GLN A 226 17552 7779 13905 3018 -1151 246 C ATOM 1853 OE1 GLN A 226 -3.168 41.272 124.842 1.00103.76 O ANISOU 1853 OE1 GLN A 226 18001 7482 13942 2641 -1337 -24 O ATOM 1854 NE2 GLN A 226 -5.020 41.932 123.741 1.00107.66 N ANISOU 1854 NE2 GLN A 226 18309 8017 14578 3414 -1203 505 N ATOM 1855 N ASP A 227 -6.198 35.942 121.336 1.00 83.90 N ANISOU 1855 N ASP A 227 12409 8192 11277 2251 -736 1301 N ATOM 1856 CA ASP A 227 -7.288 34.994 121.167 1.00 81.99 C ANISOU 1856 CA ASP A 227 11653 8507 10994 2382 -680 1543 C ATOM 1857 C ASP A 227 -6.703 33.642 121.542 1.00 76.34 C ANISOU 1857 C ASP A 227 10729 8134 10140 2019 -612 1321 C ATOM 1858 O ASP A 227 -7.209 32.594 121.147 1.00 74.28 O ANISOU 1858 O ASP A 227 10107 8306 9812 1853 -648 1497 O ATOM 1859 CB ASP A 227 -7.858 35.013 119.750 1.00 83.45 C ANISOU 1859 CB ASP A 227 11661 8846 11200 2213 -870 1983 C ATOM 1860 CG ASP A 227 -9.052 35.953 119.617 1.00 89.11 C ANISOU 1860 CG ASP A 227 12317 9475 12068 2766 -900 2322 C ATOM 1861 OD1 ASP A 227 -9.310 36.454 118.499 1.00 91.50 O ANISOU 1861 OD1 ASP A 227 12659 9691 12416 2671 -1095 2661 O ATOM 1862 OD2 ASP A 227 -9.738 36.198 120.636 1.00 91.64 O ANISOU 1862 OD2 ASP A 227 12550 9825 12445 3334 -714 2267 O ATOM 1863 N THR A 228 -5.632 33.703 122.337 1.00 73.88 N ANISOU 1863 N THR A 228 10684 7593 9795 1896 -549 944 N ATOM 1864 CA THR A 228 -4.841 32.538 122.718 1.00 68.71 C ANISOU 1864 CA THR A 228 9898 7180 9027 1554 -497 714 C ATOM 1865 C THR A 228 -5.296 31.952 124.036 1.00 67.39 C ANISOU 1865 C THR A 228 9573 7238 8795 1856 -337 545 C ATOM 1866 O THR A 228 -5.466 32.669 125.019 1.00 69.95 O ANISOU 1866 O THR A 228 10117 7344 9118 2250 -243 378 O ATOM 1867 CB THR A 228 -3.349 32.893 122.866 1.00 68.01 C ANISOU 1867 CB THR A 228 10123 6770 8949 1216 -546 456 C ATOM 1868 OG1 THR A 228 -2.955 33.764 121.804 1.00 70.45 O ANISOU 1868 OG1 THR A 228 10635 6800 9334 1002 -674 646 O ATOM 1869 CG2 THR A 228 -2.460 31.648 122.854 1.00 63.96 C ANISOU 1869 CG2 THR A 228 9423 6543 8335 833 -507 319 C ATOM 1870 N GLU A 229 -5.484 30.640 124.042 1.00 63.53 N ANISOU 1870 N GLU A 229 8750 7165 8224 1669 -314 595 N ATOM 1871 CA GLU A 229 -5.733 29.902 125.260 1.00 61.78 C ANISOU 1871 CA GLU A 229 8364 7191 7918 1842 -172 458 C ATOM 1872 C GLU A 229 -4.624 28.892 125.499 1.00 56.87 C ANISOU 1872 C GLU A 229 7759 6636 7211 1450 -196 218 C ATOM 1873 O GLU A 229 -4.421 27.979 124.707 1.00 54.99 O ANISOU 1873 O GLU A 229 7384 6571 6937 1111 -284 310 O ATOM 1874 CB GLU A 229 -7.069 29.181 125.158 1.00 63.26 C ANISOU 1874 CB GLU A 229 8101 7829 8107 1976 -149 808 C ATOM 1875 CG GLU A 229 -7.406 28.329 126.353 1.00 62.98 C ANISOU 1875 CG GLU A 229 7841 8110 7977 2113 3 757 C ATOM 1876 CD GLU A 229 -8.883 28.040 126.431 1.00 66.02 C ANISOU 1876 CD GLU A 229 7757 8924 8405 2369 64 1183 C ATOM 1877 OE1 GLU A 229 -9.535 28.000 125.362 1.00 67.11 O ANISOU 1877 OE1 GLU A 229 7678 9184 8636 2232 -112 1531 O ATOM 1878 OE2 GLU A 229 -9.393 27.864 127.557 1.00 67.77 O ANISOU 1878 OE2 GLU A 229 7810 9387 8554 2701 280 1204 O ATOM 1879 N LEU A 230 -3.922 29.060 126.610 1.00 55.20 N ANISOU 1879 N LEU A 230 7749 6276 6949 1527 -131 -88 N ATOM 1880 CA LEU A 230 -2.805 28.200 126.992 1.00 50.51 C ANISOU 1880 CA LEU A 230 7162 5734 6294 1214 -159 -307 C ATOM 1881 C LEU A 230 -3.223 27.395 128.210 1.00 49.33 C ANISOU 1881 C LEU A 230 6864 5853 6026 1397 -49 -377 C ATOM 1882 O LEU A 230 -3.445 27.986 129.263 1.00 52.54 O ANISOU 1882 O LEU A 230 7436 6172 6355 1728 45 -516 O ATOM 1883 CB LEU A 230 -1.637 29.110 127.389 1.00 50.49 C ANISOU 1883 CB LEU A 230 7511 5347 6326 1118 -234 -560 C ATOM 1884 CG LEU A 230 -0.173 28.693 127.336 1.00 48.31 C ANISOU 1884 CG LEU A 230 7254 5031 6072 719 -320 -702 C ATOM 1885 CD1 LEU A 230 0.256 28.411 125.906 1.00 47.47 C ANISOU 1885 CD1 LEU A 230 7023 4993 6020 410 -341 -516 C ATOM 1886 CD2 LEU A 230 0.696 29.774 127.934 1.00 50.17 C ANISOU 1886 CD2 LEU A 230 7830 4880 6353 652 -451 -891 C ATOM 1887 N VAL A 231 -3.348 26.074 128.120 1.00 46.21 N ANISOU 1887 N VAL A 231 6209 5761 5586 1204 -62 -280 N ATOM 1888 CA VAL A 231 -3.638 25.329 129.365 1.00 45.49 C ANISOU 1888 CA VAL A 231 5998 5910 5377 1344 34 -324 C ATOM 1889 C VAL A 231 -2.447 25.086 130.241 1.00 44.29 C ANISOU 1889 C VAL A 231 6031 5647 5151 1234 6 -626 C ATOM 1890 O VAL A 231 -1.310 25.114 129.783 1.00 42.18 O ANISOU 1890 O VAL A 231 5879 5199 4949 965 -99 -758 O ATOM 1891 CB VAL A 231 -4.286 23.950 129.191 1.00 43.66 C ANISOU 1891 CB VAL A 231 5445 6022 5121 1174 -4 -80 C ATOM 1892 CG1 VAL A 231 -5.737 24.107 128.957 1.00 45.60 C ANISOU 1892 CG1 VAL A 231 5408 6513 5406 1371 42 277 C ATOM 1893 CG2 VAL A 231 -3.561 23.097 128.141 1.00 40.52 C ANISOU 1893 CG2 VAL A 231 5080 5563 4753 769 -167 -96 C ATOM 1894 N GLU A 232 -2.753 24.837 131.510 1.00 46.53 N ANISOU 1894 N GLU A 232 6309 6084 5286 1455 108 -687 N ATOM 1895 CA GLU A 232 -1.768 24.468 132.517 1.00 47.13 C ANISOU 1895 CA GLU A 232 6534 6120 5252 1367 56 -930 C ATOM 1896 C GLU A 232 -1.101 23.141 132.130 1.00 42.87 C ANISOU 1896 C GLU A 232 5816 5702 4770 1018 -50 -884 C ATOM 1897 O GLU A 232 -1.777 22.211 131.694 1.00 41.34 O ANISOU 1897 O GLU A 232 5393 5719 4594 935 -44 -660 O ATOM 1898 CB GLU A 232 -2.448 24.431 133.905 1.00 51.75 C ANISOU 1898 CB GLU A 232 7152 6902 5607 1718 217 -949 C ATOM 1899 CG GLU A 232 -1.679 23.748 135.053 1.00 54.86 C ANISOU 1899 CG GLU A 232 7642 7367 5835 1630 157 -1116 C ATOM 1900 CD GLU A 232 -0.474 24.555 135.582 1.00 58.13 C ANISOU 1900 CD GLU A 232 8453 7440 6194 1559 -14 -1452 C ATOM 1901 OE1 GLU A 232 -0.407 25.788 135.323 1.00 61.38 O ANISOU 1901 OE1 GLU A 232 9145 7535 6642 1660 -51 -1579 O ATOM 1902 OE2 GLU A 232 0.402 23.956 136.271 1.00 57.96 O ANISOU 1902 OE2 GLU A 232 8470 7454 6097 1382 -147 -1562 O ATOM 1903 N THR A 233 0.229 23.109 132.207 1.00 41.49 N ANISOU 1903 N THR A 233 5760 5368 4636 815 -167 -1075 N ATOM 1904 CA THR A 233 1.032 21.894 131.976 1.00 39.16 C ANISOU 1904 CA THR A 233 5335 5161 4382 578 -243 -1063 C ATOM 1905 C THR A 233 0.600 20.796 132.959 1.00 38.32 C ANISOU 1905 C THR A 233 5130 5285 4145 643 -227 -994 C ATOM 1906 O THR A 233 0.367 21.070 134.137 1.00 39.57 O ANISOU 1906 O THR A 233 5373 5510 4152 822 -184 -1062 O ATOM 1907 CB THR A 233 2.552 22.199 132.121 1.00 39.38 C ANISOU 1907 CB THR A 233 5447 5032 4482 411 -359 -1235 C ATOM 1908 OG1 THR A 233 2.921 23.269 131.240 1.00 39.99 O ANISOU 1908 OG1 THR A 233 5606 4904 4683 313 -379 -1240 O ATOM 1909 CG2 THR A 233 3.404 20.990 131.795 1.00 38.32 C ANISOU 1909 CG2 THR A 233 5160 4997 4402 258 -394 -1199 C ATOM 1910 N ARG A 234 0.438 19.576 132.459 1.00 36.07 N ANISOU 1910 N ARG A 234 4713 5104 3889 501 -266 -847 N ATOM 1911 CA ARG A 234 -0.204 18.519 133.220 1.00 35.44 C ANISOU 1911 CA ARG A 234 4527 5230 3707 514 -272 -690 C ATOM 1912 C ARG A 234 0.609 17.244 133.085 1.00 33.99 C ANISOU 1912 C ARG A 234 4361 4997 3556 344 -396 -703 C ATOM 1913 O ARG A 234 1.299 17.067 132.087 1.00 33.72 O ANISOU 1913 O ARG A 234 4380 4817 3614 244 -435 -770 O ATOM 1914 CB ARG A 234 -1.610 18.311 132.675 1.00 36.33 C ANISOU 1914 CB ARG A 234 4474 5498 3832 503 -243 -402 C ATOM 1915 CG ARG A 234 -1.660 17.871 131.212 1.00 36.09 C ANISOU 1915 CG ARG A 234 4459 5352 3902 283 -362 -319 C ATOM 1916 CD ARG A 234 -3.004 18.141 130.611 1.00 37.41 C ANISOU 1916 CD ARG A 234 4461 5654 4099 276 -370 -39 C ATOM 1917 NE ARG A 234 -3.184 17.515 129.314 1.00 37.00 N ANISOU 1917 NE ARG A 234 4472 5509 4079 21 -551 71 N ATOM 1918 CZ ARG A 234 -4.330 17.534 128.646 1.00 38.49 C ANISOU 1918 CZ ARG A 234 4516 5814 4296 -79 -654 363 C ATOM 1919 NH1 ARG A 234 -5.390 18.134 129.174 1.00 40.21 N ANISOU 1919 NH1 ARG A 234 4450 6284 4545 100 -549 603 N ATOM 1920 NH2 ARG A 234 -4.420 16.941 127.465 1.00 38.34 N ANISOU 1920 NH2 ARG A 234 4642 5671 4253 -338 -868 430 N ATOM 1921 N PRO A 235 0.565 16.353 134.094 1.00 33.85 N ANISOU 1921 N PRO A 235 4317 5098 3445 346 -443 -628 N ATOM 1922 CA PRO A 235 1.328 15.106 133.930 1.00 32.85 C ANISOU 1922 CA PRO A 235 4245 4874 3363 230 -574 -628 C ATOM 1923 C PRO A 235 0.581 14.057 133.107 1.00 33.42 C ANISOU 1923 C PRO A 235 4345 4897 3458 66 -676 -428 C ATOM 1924 O PRO A 235 -0.647 13.944 133.195 1.00 34.24 O ANISOU 1924 O PRO A 235 4338 5147 3523 -7 -688 -188 O ATOM 1925 CB PRO A 235 1.521 14.619 135.364 1.00 32.98 C ANISOU 1925 CB PRO A 235 4255 5017 3261 286 -616 -595 C ATOM 1926 CG PRO A 235 0.393 15.205 136.118 1.00 34.53 C ANISOU 1926 CG PRO A 235 4374 5436 3311 395 -490 -473 C ATOM 1927 CD PRO A 235 0.002 16.485 135.448 1.00 34.41 C ANISOU 1927 CD PRO A 235 4352 5378 3345 491 -369 -558 C ATOM 1928 N ALA A 236 1.310 13.284 132.312 1.00 33.09 N ANISOU 1928 N ALA A 236 4460 4649 3463 11 -761 -507 N ATOM 1929 CA ALA A 236 0.669 12.208 131.573 1.00 34.31 C ANISOU 1929 CA ALA A 236 4766 4675 3596 -165 -926 -354 C ATOM 1930 C ALA A 236 0.522 10.977 132.478 1.00 36.31 C ANISOU 1930 C ALA A 236 5071 4914 3813 -242 -1081 -192 C ATOM 1931 O ALA A 236 -0.316 10.099 132.221 1.00 38.28 O ANISOU 1931 O ALA A 236 5416 5088 4040 -462 -1275 29 O ATOM 1932 CB ALA A 236 1.435 11.884 130.302 1.00 34.21 C ANISOU 1932 CB ALA A 236 4999 4418 3583 -137 -937 -521 C ATOM 1933 N GLY A 237 1.326 10.927 133.545 1.00 36.10 N ANISOU 1933 N GLY A 237 4988 4950 3777 -98 -1034 -272 N ATOM 1934 CA GLY A 237 1.210 9.883 134.554 1.00 37.25 C ANISOU 1934 CA GLY A 237 5166 5114 3874 -156 -1170 -90 C ATOM 1935 C GLY A 237 2.310 8.854 134.417 1.00 38.23 C ANISOU 1935 C GLY A 237 5515 4967 4044 -62 -1287 -193 C ATOM 1936 O GLY A 237 2.374 7.886 135.179 1.00 39.12 O ANISOU 1936 O GLY A 237 5710 5024 4132 -94 -1432 -45 O ATOM 1937 N ASP A 238 3.179 9.065 133.434 1.00 37.99 N ANISOU 1937 N ASP A 238 5581 4781 4074 83 -1205 -419 N ATOM 1938 CA ASP A 238 4.309 8.173 133.217 1.00 39.97 C ANISOU 1938 CA ASP A 238 6016 4803 4366 281 -1247 -519 C ATOM 1939 C ASP A 238 5.619 8.931 133.358 1.00 39.73 C ANISOU 1939 C ASP A 238 5760 4912 4423 508 -1080 -684 C ATOM 1940 O ASP A 238 6.637 8.523 132.825 1.00 41.63 O ANISOU 1940 O ASP A 238 6063 5036 4717 733 -1017 -774 O ATOM 1941 CB ASP A 238 4.215 7.470 131.857 1.00 41.53 C ANISOU 1941 CB ASP A 238 6581 4680 4517 290 -1301 -592 C ATOM 1942 CG ASP A 238 4.193 8.437 130.670 1.00 40.91 C ANISOU 1942 CG ASP A 238 6476 4654 4415 300 -1126 -735 C ATOM 1943 OD1 ASP A 238 4.002 9.662 130.858 1.00 39.99 O ANISOU 1943 OD1 ASP A 238 6064 4790 4341 244 -996 -743 O ATOM 1944 OD2 ASP A 238 4.344 7.958 129.524 1.00 42.06 O ANISOU 1944 OD2 ASP A 238 6952 4560 4470 373 -1128 -839 O ATOM 1945 N GLY A 239 5.569 10.064 134.047 1.00 38.63 N ANISOU 1945 N GLY A 239 5367 5021 4288 450 -1013 -703 N ATOM 1946 CA GLY A 239 6.757 10.850 134.287 1.00 38.39 C ANISOU 1946 CA GLY A 239 5118 5119 4348 565 -938 -812 C ATOM 1947 C GLY A 239 7.027 11.857 133.193 1.00 37.42 C ANISOU 1947 C GLY A 239 4920 5010 4287 561 -769 -926 C ATOM 1948 O GLY A 239 8.039 12.551 133.244 1.00 38.83 O ANISOU 1948 O GLY A 239 4895 5292 4567 601 -721 -971 O ATOM 1949 N THR A 240 6.134 11.940 132.204 1.00 35.87 N ANISOU 1949 N THR A 240 4876 4719 4033 478 -709 -932 N ATOM 1950 CA THR A 240 6.232 12.943 131.133 1.00 34.48 C ANISOU 1950 CA THR A 240 4658 4558 3886 450 -557 -1004 C ATOM 1951 C THR A 240 5.076 13.938 131.138 1.00 32.70 C ANISOU 1951 C THR A 240 4415 4389 3619 296 -554 -977 C ATOM 1952 O THR A 240 4.056 13.725 131.780 1.00 31.70 O ANISOU 1952 O THR A 240 4310 4309 3426 226 -636 -882 O ATOM 1953 CB THR A 240 6.252 12.307 129.748 1.00 34.78 C ANISOU 1953 CB THR A 240 4926 4435 3853 523 -481 -1034 C ATOM 1954 OG1 THR A 240 5.016 11.626 129.535 1.00 34.72 O ANISOU 1954 OG1 THR A 240 5165 4292 3735 385 -631 -963 O ATOM 1955 CG2 THR A 240 7.383 11.338 129.623 1.00 36.83 C ANISOU 1955 CG2 THR A 240 5238 4625 4133 778 -429 -1066 C ATOM 1956 N PHE A 241 5.216 15.012 130.376 1.00 32.43 N ANISOU 1956 N PHE A 241 4331 4364 3627 263 -444 -1023 N ATOM 1957 CA PHE A 241 4.224 16.069 130.472 1.00 32.13 C ANISOU 1957 CA PHE A 241 4273 4363 3572 185 -436 -995 C ATOM 1958 C PHE A 241 3.437 16.324 129.188 1.00 31.82 C ANISOU 1958 C PHE A 241 4331 4265 3495 115 -399 -929 C ATOM 1959 O PHE A 241 3.777 15.762 128.137 1.00 32.81 O ANISOU 1959 O PHE A 241 4585 4308 3574 115 -369 -940 O ATOM 1960 CB PHE A 241 4.851 17.327 131.075 1.00 32.75 C ANISOU 1960 CB PHE A 241 4252 4468 3723 182 -422 -1082 C ATOM 1961 CG PHE A 241 5.180 17.164 132.518 1.00 34.00 C ANISOU 1961 CG PHE A 241 4373 4699 3847 220 -524 -1125 C ATOM 1962 CD1 PHE A 241 6.434 16.715 132.917 1.00 35.48 C ANISOU 1962 CD1 PHE A 241 4459 4919 4104 230 -593 -1147 C ATOM 1963 CD2 PHE A 241 4.211 17.386 133.484 1.00 34.33 C ANISOU 1963 CD2 PHE A 241 4473 4809 3763 273 -544 -1111 C ATOM 1964 CE1 PHE A 241 6.731 16.519 134.263 1.00 36.50 C ANISOU 1964 CE1 PHE A 241 4576 5121 4172 248 -732 -1167 C ATOM 1965 CE2 PHE A 241 4.490 17.199 134.822 1.00 35.77 C ANISOU 1965 CE2 PHE A 241 4672 5072 3846 316 -635 -1147 C ATOM 1966 CZ PHE A 241 5.759 16.764 135.216 1.00 36.83 C ANISOU 1966 CZ PHE A 241 4738 5212 4045 282 -756 -1181 C ATOM 1967 N GLN A 242 2.348 17.101 129.308 1.00 30.75 N ANISOU 1967 N GLN A 242 4156 4178 3351 89 -405 -848 N ATOM 1968 CA GLN A 242 1.467 17.485 128.190 1.00 30.38 C ANISOU 1968 CA GLN A 242 4160 4104 3278 18 -411 -734 C ATOM 1969 C GLN A 242 1.034 18.943 128.305 1.00 30.67 C ANISOU 1969 C GLN A 242 4127 4151 3375 84 -345 -717 C ATOM 1970 O GLN A 242 0.774 19.439 129.411 1.00 31.42 O ANISOU 1970 O GLN A 242 4161 4304 3475 202 -318 -746 O ATOM 1971 CB GLN A 242 0.210 16.622 128.136 1.00 30.69 C ANISOU 1971 CB GLN A 242 4204 4204 3251 -81 -549 -538 C ATOM 1972 CG GLN A 242 0.439 15.164 127.837 1.00 31.74 C ANISOU 1972 CG GLN A 242 4522 4230 3307 -177 -679 -539 C ATOM 1973 CD GLN A 242 -0.831 14.364 127.820 1.00 33.03 C ANISOU 1973 CD GLN A 242 4692 4431 3424 -364 -888 -294 C ATOM 1974 OE1 GLN A 242 -1.822 14.750 128.419 1.00 33.48 O ANISOU 1974 OE1 GLN A 242 4512 4685 3524 -379 -890 -94 O ATOM 1975 NE2 GLN A 242 -0.809 13.237 127.131 1.00 35.03 N ANISOU 1975 NE2 GLN A 242 5231 4496 3584 -505 -1070 -289 N ATOM 1976 N LYS A 243 0.950 19.620 127.159 1.00 30.35 N ANISOU 1976 N LYS A 243 4145 4036 3351 32 -322 -669 N ATOM 1977 CA LYS A 243 0.445 20.999 127.089 1.00 30.86 C ANISOU 1977 CA LYS A 243 4195 4052 3479 110 -285 -619 C ATOM 1978 C LYS A 243 -0.161 21.300 125.694 1.00 31.21 C ANISOU 1978 C LYS A 243 4293 4066 3500 26 -324 -453 C ATOM 1979 O LYS A 243 0.249 20.711 124.691 1.00 31.24 O ANISOU 1979 O LYS A 243 4406 4047 3418 -103 -343 -448 O ATOM 1980 CB LYS A 243 1.554 22.013 127.424 1.00 30.96 C ANISOU 1980 CB LYS A 243 4262 3924 3579 116 -238 -774 C ATOM 1981 CG LYS A 243 1.064 23.347 127.995 1.00 32.69 C ANISOU 1981 CG LYS A 243 4555 4022 3843 264 -235 -796 C ATOM 1982 CD LYS A 243 2.122 24.441 127.855 1.00 33.84 C ANISOU 1982 CD LYS A 243 4823 3947 4088 154 -269 -885 C ATOM 1983 CE LYS A 243 1.799 25.705 128.624 1.00 35.61 C ANISOU 1983 CE LYS A 243 5247 3954 4328 313 -314 -974 C ATOM 1984 NZ LYS A 243 1.890 25.467 130.096 1.00 36.21 N ANISOU 1984 NZ LYS A 243 5386 4071 4303 443 -340 -1151 N ATOM 1985 N TRP A 244 -1.150 22.191 125.652 1.00 31.50 N ANISOU 1985 N TRP A 244 4275 4110 3586 133 -334 -310 N ATOM 1986 CA TRP A 244 -1.645 22.726 124.407 1.00 31.93 C ANISOU 1986 CA TRP A 244 4380 4120 3632 69 -392 -135 C ATOM 1987 C TRP A 244 -1.863 24.228 124.382 1.00 33.94 C ANISOU 1987 C TRP A 244 4671 4231 3994 223 -349 -88 C ATOM 1988 O TRP A 244 -2.075 24.858 125.420 1.00 34.63 O ANISOU 1988 O TRP A 244 4743 4273 4143 445 -284 -161 O ATOM 1989 CB TRP A 244 -2.879 21.992 123.877 1.00 32.80 C ANISOU 1989 CB TRP A 244 4394 4391 3677 -19 -549 117 C ATOM 1990 CG TRP A 244 -4.124 21.918 124.717 1.00 34.55 C ANISOU 1990 CG TRP A 244 4354 4816 3959 125 -571 318 C ATOM 1991 CD1 TRP A 244 -4.541 20.839 125.425 1.00 34.62 C ANISOU 1991 CD1 TRP A 244 4223 4996 3936 64 -625 390 C ATOM 1992 CD2 TRP A 244 -5.150 22.921 124.881 1.00 37.06 C ANISOU 1992 CD2 TRP A 244 4493 5216 4373 371 -528 530 C ATOM 1993 NE1 TRP A 244 -5.740 21.097 126.038 1.00 37.43 N ANISOU 1993 NE1 TRP A 244 4281 5586 4354 237 -593 655 N ATOM 1994 CE2 TRP A 244 -6.141 22.368 125.723 1.00 38.60 C ANISOU 1994 CE2 TRP A 244 4394 5691 4580 465 -518 737 C ATOM 1995 CE3 TRP A 244 -5.319 24.229 124.415 1.00 38.62 C ANISOU 1995 CE3 TRP A 244 4752 5274 4649 544 -488 589 C ATOM 1996 CZ2 TRP A 244 -7.293 23.066 126.094 1.00 41.25 C ANISOU 1996 CZ2 TRP A 244 4456 6222 4995 772 -429 1007 C ATOM 1997 CZ3 TRP A 244 -6.462 24.926 124.801 1.00 41.94 C ANISOU 1997 CZ3 TRP A 244 4956 5825 5155 866 -427 823 C ATOM 1998 CH2 TRP A 244 -7.429 24.343 125.637 1.00 43.09 C ANISOU 1998 CH2 TRP A 244 4772 6299 5303 1003 -376 1029 C ATOM 1999 N ALA A 245 -1.815 24.792 123.177 1.00 34.74 N ANISOU 1999 N ALA A 245 4875 4238 4087 119 -391 36 N ATOM 2000 CA ALA A 245 -2.212 26.176 122.959 1.00 36.63 C ANISOU 2000 CA ALA A 245 5179 4308 4431 260 -397 150 C ATOM 2001 C ALA A 245 -3.284 26.272 121.874 1.00 37.81 C ANISOU 2001 C ALA A 245 5274 4547 4547 241 -523 458 C ATOM 2002 O ALA A 245 -3.197 25.577 120.859 1.00 37.37 O ANISOU 2002 O ALA A 245 5274 4577 4349 9 -612 538 O ATOM 2003 CB ALA A 245 -1.011 27.005 122.583 1.00 37.92 C ANISOU 2003 CB ALA A 245 5528 4237 4642 121 -361 62 C ATOM 2004 N ALA A 246 -4.279 27.137 122.074 1.00 39.62 N ANISOU 2004 N ALA A 246 5420 4750 4884 506 -540 636 N ATOM 2005 CA ALA A 246 -5.391 27.266 121.119 1.00 41.80 C ANISOU 2005 CA ALA A 246 5577 5147 5157 508 -696 991 C ATOM 2006 C ALA A 246 -5.518 28.668 120.552 1.00 44.42 C ANISOU 2006 C ALA A 246 6056 5234 5588 653 -720 1137 C ATOM 2007 O ALA A 246 -5.035 29.598 121.162 1.00 45.24 O ANISOU 2007 O ALA A 246 6332 5065 5791 832 -616 973 O ATOM 2008 CB ALA A 246 -6.682 26.881 121.771 1.00 42.86 C ANISOU 2008 CB ALA A 246 5372 5564 5350 721 -714 1203 C ATOM 2009 N VAL A 247 -6.168 28.811 119.393 1.00 46.57 N ANISOU 2009 N VAL A 247 6297 5575 5821 557 -897 1454 N ATOM 2010 CA VAL A 247 -6.553 30.136 118.851 1.00 49.92 C ANISOU 2010 CA VAL A 247 6823 5786 6358 744 -956 1683 C ATOM 2011 C VAL A 247 -7.881 30.135 118.124 1.00 52.62 C ANISOU 2011 C VAL A 247 6925 6351 6718 813 -1164 2119 C ATOM 2012 O VAL A 247 -8.129 29.290 117.273 1.00 52.46 O ANISOU 2012 O VAL A 247 6852 6545 6535 494 -1362 2272 O ATOM 2013 CB VAL A 247 -5.549 30.745 117.826 1.00 50.55 C ANISOU 2013 CB VAL A 247 7232 5610 6364 472 -989 1678 C ATOM 2014 CG1 VAL A 247 -4.581 31.716 118.504 1.00 51.27 C ANISOU 2014 CG1 VAL A 247 7568 5326 6588 551 -857 1443 C ATOM 2015 CG2 VAL A 247 -4.842 29.671 116.997 1.00 48.13 C ANISOU 2015 CG2 VAL A 247 7007 5477 5802 67 -1014 1606 C ATOM 2016 N VAL A 248 -8.721 31.112 118.444 1.00 55.68 N ANISOU 2016 N VAL A 248 7196 6669 7292 1244 -1140 2327 N ATOM 2017 CA VAL A 248 -9.952 31.334 117.711 1.00 58.88 C ANISOU 2017 CA VAL A 248 7341 7274 7759 1354 -1352 2810 C ATOM 2018 C VAL A 248 -9.566 32.087 116.436 1.00 60.39 C ANISOU 2018 C VAL A 248 7848 7210 7886 1158 -1520 2962 C ATOM 2019 O VAL A 248 -8.926 33.132 116.505 1.00 61.94 O ANISOU 2019 O VAL A 248 8361 7011 8162 1286 -1420 2837 O ATOM 2020 CB VAL A 248 -10.964 32.127 118.572 1.00 62.35 C ANISOU 2020 CB VAL A 248 7524 7747 8422 1990 -1208 2993 C ATOM 2021 CG1 VAL A 248 -12.109 32.682 117.717 1.00 66.97 C ANISOU 2021 CG1 VAL A 248 7862 8464 9119 2171 -1429 3540 C ATOM 2022 CG2 VAL A 248 -11.505 31.247 119.706 1.00 60.83 C ANISOU 2022 CG2 VAL A 248 6939 7931 8242 2146 -1047 2959 C ATOM 2023 N VAL A 249 -9.911 31.529 115.275 1.00 60.60 N ANISOU 2023 N VAL A 249 7833 7450 7742 808 -1798 3232 N ATOM 2024 CA VAL A 249 -9.404 31.996 113.969 1.00 61.18 C ANISOU 2024 CA VAL A 249 8250 7348 7646 529 -1948 3359 C ATOM 2025 C VAL A 249 -10.564 32.088 112.939 1.00 64.54 C ANISOU 2025 C VAL A 249 8503 7985 8033 484 -2312 3887 C ATOM 2026 O VAL A 249 -11.392 31.178 112.871 1.00 65.34 O ANISOU 2026 O VAL A 249 8303 8438 8084 350 -2525 4073 O ATOM 2027 CB VAL A 249 -8.284 31.002 113.485 1.00 57.83 C ANISOU 2027 CB VAL A 249 8101 6968 6904 61 -1902 3056 C ATOM 2028 CG1 VAL A 249 -8.079 31.007 111.980 1.00 59.93 C ANISOU 2028 CG1 VAL A 249 8656 7250 6865 -272 -2102 3264 C ATOM 2029 CG2 VAL A 249 -6.972 31.268 114.191 1.00 55.24 C ANISOU 2029 CG2 VAL A 249 7974 6385 6630 75 -1588 2651 C ATOM 2030 N PRO A 250 -10.649 33.198 112.166 1.00 67.12 N ANISOU 2030 N PRO A 250 9011 8094 8399 575 -2422 4166 N ATOM 2031 CA PRO A 250 -11.645 33.305 111.069 1.00 70.98 C ANISOU 2031 CA PRO A 250 9376 8780 8814 485 -2815 4694 C ATOM 2032 C PRO A 250 -11.411 32.263 109.967 1.00 70.08 C ANISOU 2032 C PRO A 250 9479 8874 8273 -83 -3075 4704 C ATOM 2033 O PRO A 250 -10.272 32.049 109.570 1.00 67.33 O ANISOU 2033 O PRO A 250 9535 8386 7661 -352 -2922 4406 O ATOM 2034 CB PRO A 250 -11.431 34.718 110.508 1.00 73.73 C ANISOU 2034 CB PRO A 250 10005 8756 9251 662 -2827 4903 C ATOM 2035 CG PRO A 250 -10.488 35.410 111.435 1.00 71.98 C ANISOU 2035 CG PRO A 250 10017 8126 9206 881 -2467 4511 C ATOM 2036 CD PRO A 250 -9.766 34.376 112.241 1.00 67.33 C ANISOU 2036 CD PRO A 250 9398 7660 8525 704 -2232 4028 C ATOM 2037 N SER A 251 -12.476 31.613 109.503 1.00 72.77 N ANISOU 2037 N SER A 251 9562 9551 8538 -253 -3467 5055 N ATOM 2038 CA SER A 251 -12.349 30.438 108.636 1.00 73.22 C ANISOU 2038 CA SER A 251 9880 9780 8161 -785 -3755 5002 C ATOM 2039 C SER A 251 -11.729 30.723 107.273 1.00 75.71 C ANISOU 2039 C SER A 251 10739 9965 8063 -1066 -3872 5054 C ATOM 2040 O SER A 251 -11.997 31.755 106.653 1.00 78.90 O ANISOU 2040 O SER A 251 11185 10276 8518 -950 -3991 5410 O ATOM 2041 CB SER A 251 -13.692 29.738 108.467 1.00 76.44 C ANISOU 2041 CB SER A 251 9892 10552 8600 -958 -4235 5422 C ATOM 2042 OG SER A 251 -14.066 29.117 109.680 1.00 75.05 O ANISOU 2042 OG SER A 251 9278 10550 8688 -824 -4095 5318 O ATOM 2043 N GLY A 252 -10.860 29.818 106.839 1.00 74.34 N ANISOU 2043 N GLY A 252 10998 9780 7468 -1393 -3802 4700 N ATOM 2044 CA GLY A 252 -10.138 30.009 105.596 1.00 76.64 C ANISOU 2044 CA GLY A 252 11834 9989 7297 -1622 -3811 4709 C ATOM 2045 C GLY A 252 -8.892 30.855 105.783 1.00 74.97 C ANISOU 2045 C GLY A 252 11793 9531 7159 -1463 -3322 4498 C ATOM 2046 O GLY A 252 -8.304 31.321 104.811 1.00 77.17 O ANISOU 2046 O GLY A 252 12438 9750 7133 -1596 -3271 4613 O ATOM 2047 N GLN A 253 -8.479 31.063 107.029 1.00 71.66 N ANISOU 2047 N GLN A 253 11116 8979 7131 -1208 -2981 4221 N ATOM 2048 CA GLN A 253 -7.278 31.857 107.280 1.00 70.59 C ANISOU 2048 CA GLN A 253 11126 8597 7098 -1123 -2581 4043 C ATOM 2049 C GLN A 253 -6.237 31.124 108.119 1.00 66.37 C ANISOU 2049 C GLN A 253 10589 8058 6572 -1134 -2217 3548 C ATOM 2050 O GLN A 253 -5.271 31.734 108.554 1.00 65.56 O ANISOU 2050 O GLN A 253 10514 7768 6628 -1076 -1916 3404 O ATOM 2051 CB GLN A 253 -7.619 33.227 107.886 1.00 71.91 C ANISOU 2051 CB GLN A 253 11095 8491 7736 -793 -2549 4243 C ATOM 2052 CG GLN A 253 -8.066 34.241 106.850 1.00 77.03 C ANISOU 2052 CG GLN A 253 11894 9038 8335 -804 -2795 4733 C ATOM 2053 CD GLN A 253 -8.911 35.364 107.411 1.00 79.42 C ANISOU 2053 CD GLN A 253 11965 9114 9099 -386 -2894 4999 C ATOM 2054 OE1 GLN A 253 -8.392 36.350 107.928 1.00 79.81 O ANISOU 2054 OE1 GLN A 253 12119 8794 9412 -200 -2704 4932 O ATOM 2055 NE2 GLN A 253 -10.223 35.238 107.269 1.00 82.20 N ANISOU 2055 NE2 GLN A 253 12020 9676 9537 -234 -3216 5334 N ATOM 2056 N GLU A 254 -6.418 29.809 108.276 1.00 64.23 N ANISOU 2056 N GLU A 254 10311 7980 6113 -1243 -2290 3326 N ATOM 2057 CA GLU A 254 -5.517 28.908 109.022 1.00 60.27 C ANISOU 2057 CA GLU A 254 9817 7498 5583 -1245 -1995 2875 C ATOM 2058 C GLU A 254 -4.067 28.859 108.512 1.00 60.17 C ANISOU 2058 C GLU A 254 10102 7467 5292 -1348 -1648 2691 C ATOM 2059 O GLU A 254 -3.140 28.503 109.247 1.00 58.23 O ANISOU 2059 O GLU A 254 9782 7203 5139 -1286 -1344 2379 O ATOM 2060 CB GLU A 254 -6.089 27.485 108.989 1.00 59.60 C ANISOU 2060 CB GLU A 254 9783 7586 5277 -1393 -2234 2754 C ATOM 2061 CG GLU A 254 -7.415 27.303 109.729 1.00 59.82 C ANISOU 2061 CG GLU A 254 9397 7713 5618 -1314 -2520 2934 C ATOM 2062 CD GLU A 254 -8.660 27.501 108.861 1.00 64.23 C ANISOU 2062 CD GLU A 254 9910 8399 6094 -1446 -2993 3400 C ATOM 2063 OE1 GLU A 254 -8.542 28.003 107.716 1.00 67.22 O ANISOU 2063 OE1 GLU A 254 10592 8748 6202 -1565 -3106 3600 O ATOM 2064 OE2 GLU A 254 -9.764 27.163 109.342 1.00 64.66 O ANISOU 2064 OE2 GLU A 254 9593 8616 6360 -1437 -3258 3609 O ATOM 2065 N GLN A 255 -3.915 29.212 107.245 1.00 62.97 N ANISOU 2065 N GLN A 255 10765 7866 5297 -1495 -1700 2932 N ATOM 2066 CA GLN A 255 -2.680 29.241 106.492 1.00 64.67 C ANISOU 2066 CA GLN A 255 11259 8147 5167 -1590 -1374 2892 C ATOM 2067 C GLN A 255 -1.715 30.295 107.024 1.00 63.79 C ANISOU 2067 C GLN A 255 10949 7890 5399 -1547 -1063 2935 C ATOM 2068 O GLN A 255 -0.505 30.073 107.058 1.00 63.23 O ANISOU 2068 O GLN A 255 10888 7907 5228 -1574 -705 2788 O ATOM 2069 CB GLN A 255 -3.003 29.578 105.029 1.00 70.13 C ANISOU 2069 CB GLN A 255 12308 8920 5417 -1750 -1565 3242 C ATOM 2070 CG GLN A 255 -4.068 28.689 104.375 1.00 72.66 C ANISOU 2070 CG GLN A 255 12881 9350 5375 -1869 -2002 3279 C ATOM 2071 CD GLN A 255 -5.493 29.159 104.662 1.00 73.40 C ANISOU 2071 CD GLN A 255 12677 9389 5823 -1853 -2459 3582 C ATOM 2072 OE1 GLN A 255 -6.346 28.377 105.110 1.00 72.19 O ANISOU 2072 OE1 GLN A 255 12378 9294 5759 -1879 -2745 3511 O ATOM 2073 NE2 GLN A 255 -5.738 30.454 104.457 1.00 74.91 N ANISOU 2073 NE2 GLN A 255 12747 9469 6247 -1793 -2516 3950 N ATOM 2074 N ARG A 256 -2.253 31.437 107.454 1.00 63.83 N ANISOU 2074 N ARG A 256 10778 7662 5813 -1474 -1220 3152 N ATOM 2075 CA ARG A 256 -1.428 32.521 107.988 1.00 63.90 C ANISOU 2075 CA ARG A 256 10676 7438 6163 -1481 -1028 3207 C ATOM 2076 C ARG A 256 -1.054 32.348 109.467 1.00 60.47 C ANISOU 2076 C ARG A 256 9983 6887 6107 -1342 -892 2851 C ATOM 2077 O ARG A 256 -0.501 33.253 110.070 1.00 60.52 O ANISOU 2077 O ARG A 256 9926 6643 6426 -1355 -823 2869 O ATOM 2078 CB ARG A 256 -2.134 33.863 107.841 1.00 66.40 C ANISOU 2078 CB ARG A 256 11023 7466 6742 -1423 -1272 3568 C ATOM 2079 CG ARG A 256 -3.243 33.917 106.828 1.00 69.29 C ANISOU 2079 CG ARG A 256 11526 7923 6878 -1427 -1594 3899 C ATOM 2080 CD ARG A 256 -4.251 34.988 107.239 1.00 71.03 C ANISOU 2080 CD ARG A 256 11632 7850 7507 -1185 -1854 4143 C ATOM 2081 NE ARG A 256 -3.669 36.332 107.305 1.00 73.47 N ANISOU 2081 NE ARG A 256 12065 7784 8068 -1209 -1794 4334 N ATOM 2082 CZ ARG A 256 -4.289 37.387 107.828 1.00 75.22 C ANISOU 2082 CZ ARG A 256 12271 7633 8677 -943 -1955 4478 C ATOM 2083 NH1 ARG A 256 -3.703 38.577 107.841 1.00 77.56 N ANISOU 2083 NH1 ARG A 256 12770 7524 9177 -1015 -1945 4648 N ATOM 2084 NH2 ARG A 256 -5.502 37.248 108.343 1.00 75.02 N ANISOU 2084 NH2 ARG A 256 12035 7637 8833 -592 -2128 4474 N ATOM 2085 N TYR A 257 -1.354 31.197 110.048 1.00 58.34 N ANISOU 2085 N TYR A 257 9601 6774 5791 -1236 -891 2545 N ATOM 2086 CA TYR A 257 -1.091 30.963 111.452 1.00 56.14 C ANISOU 2086 CA TYR A 257 9094 6413 5824 -1096 -787 2226 C ATOM 2087 C TYR A 257 -0.101 29.831 111.702 1.00 54.94 C ANISOU 2087 C TYR A 257 8905 6464 5506 -1146 -535 1922 C ATOM 2088 O TYR A 257 -0.309 28.695 111.260 1.00 54.89 O ANISOU 2088 O TYR A 257 9010 6657 5190 -1153 -552 1811 O ATOM 2089 CB TYR A 257 -2.387 30.648 112.170 1.00 54.66 C ANISOU 2089 CB TYR A 257 8741 6225 5802 -880 -1003 2170 C ATOM 2090 CG TYR A 257 -3.266 31.834 112.431 1.00 56.62 C ANISOU 2090 CG TYR A 257 8933 6238 6342 -682 -1175 2401 C ATOM 2091 CD1 TYR A 257 -3.109 32.592 113.575 1.00 56.26 C ANISOU 2091 CD1 TYR A 257 8821 5923 6634 -482 -1103 2264 C ATOM 2092 CD2 TYR A 257 -4.271 32.182 111.550 1.00 59.60 C ANISOU 2092 CD2 TYR A 257 9356 6651 6640 -661 -1426 2756 C ATOM 2093 CE1 TYR A 257 -3.927 33.670 113.834 1.00 58.80 C ANISOU 2093 CE1 TYR A 257 9155 5989 7197 -211 -1237 2450 C ATOM 2094 CE2 TYR A 257 -5.094 33.267 111.791 1.00 62.08 C ANISOU 2094 CE2 TYR A 257 9607 6746 7233 -401 -1569 2990 C ATOM 2095 CZ TYR A 257 -4.922 33.998 112.947 1.00 61.68 C ANISOU 2095 CZ TYR A 257 9521 6406 7509 -146 -1453 2821 C ATOM 2096 OH TYR A 257 -5.730 35.071 113.221 1.00 64.54 O ANISOU 2096 OH TYR A 257 9886 6510 8125 198 -1565 3022 O ATOM 2097 N THR A 258 0.955 30.141 112.448 1.00 54.70 N ANISOU 2097 N THR A 258 8736 6357 5691 -1175 -338 1796 N ATOM 2098 CA THR A 258 1.995 29.168 112.760 1.00 53.79 C ANISOU 2098 CA THR A 258 8525 6439 5475 -1183 -87 1552 C ATOM 2099 C THR A 258 2.197 28.985 114.261 1.00 51.31 C ANISOU 2099 C THR A 258 7991 6028 5476 -1076 -84 1273 C ATOM 2100 O THR A 258 2.192 29.949 115.024 1.00 51.35 O ANISOU 2100 O THR A 258 7934 5788 5789 -1073 -173 1288 O ATOM 2101 CB THR A 258 3.329 29.590 112.142 1.00 56.32 C ANISOU 2101 CB THR A 258 8820 6870 5710 -1359 178 1734 C ATOM 2102 OG1 THR A 258 3.466 31.010 112.259 1.00 58.12 O ANISOU 2102 OG1 THR A 258 9025 6837 6221 -1513 75 1979 O ATOM 2103 CG2 THR A 258 3.365 29.218 110.677 1.00 58.91 C ANISOU 2103 CG2 THR A 258 9393 7425 5563 -1401 292 1910 C ATOM 2104 N CYS A 259 2.383 27.739 114.677 1.00 49.84 N ANISOU 2104 N CYS A 259 7744 6010 5184 -980 3 1017 N ATOM 2105 CA CYS A 259 2.638 27.430 116.082 1.00 47.66 C ANISOU 2105 CA CYS A 259 7272 5684 5153 -885 11 763 C ATOM 2106 C CYS A 259 4.109 27.174 116.315 1.00 47.91 C ANISOU 2106 C CYS A 259 7149 5842 5214 -952 243 695 C ATOM 2107 O CYS A 259 4.703 26.330 115.656 1.00 48.79 O ANISOU 2107 O CYS A 259 7292 6173 5074 -920 441 677 O ATOM 2108 CB CYS A 259 1.864 26.189 116.521 1.00 45.60 C ANISOU 2108 CB CYS A 259 7014 5517 4794 -745 -79 565 C ATOM 2109 SG CYS A 259 2.140 25.807 118.262 1.00 44.85 S ANISOU 2109 SG CYS A 259 6699 5386 4957 -624 -68 290 S ATOM 2110 N HIS A 260 4.690 27.875 117.276 1.00 48.33 N ANISOU 2110 N HIS A 260 7046 5756 5561 -1025 207 662 N ATOM 2111 CA HIS A 260 6.117 27.726 117.566 1.00 49.68 C ANISOU 2111 CA HIS A 260 6987 6073 5814 -1132 377 669 C ATOM 2112 C HIS A 260 6.340 27.032 118.905 1.00 47.23 C ANISOU 2112 C HIS A 260 6528 5776 5640 -1018 330 394 C ATOM 2113 O HIS A 260 5.716 27.385 119.907 1.00 45.59 O ANISOU 2113 O HIS A 260 6374 5359 5588 -963 136 250 O ATOM 2114 CB HIS A 260 6.810 29.085 117.500 1.00 53.00 C ANISOU 2114 CB HIS A 260 7348 6338 6450 -1412 317 924 C ATOM 2115 CG HIS A 260 6.725 29.718 116.148 1.00 56.73 C ANISOU 2115 CG HIS A 260 7951 6833 6770 -1543 387 1247 C ATOM 2116 ND1 HIS A 260 7.766 29.680 115.245 1.00 60.09 N ANISOU 2116 ND1 HIS A 260 8229 7544 7060 -1684 649 1515 N ATOM 2117 CD2 HIS A 260 5.707 30.358 115.522 1.00 57.47 C ANISOU 2117 CD2 HIS A 260 8299 6738 6799 -1531 244 1375 C ATOM 2118 CE1 HIS A 260 7.400 30.290 114.130 1.00 62.45 C ANISOU 2118 CE1 HIS A 260 8719 7814 7195 -1778 658 1786 C ATOM 2119 NE2 HIS A 260 6.151 30.698 114.267 1.00 60.71 N ANISOU 2119 NE2 HIS A 260 8748 7297 7022 -1692 394 1704 N ATOM 2120 N VAL A 261 7.196 26.012 118.901 1.00 47.15 N ANISOU 2120 N VAL A 261 6354 6021 5540 -938 524 330 N ATOM 2121 CA VAL A 261 7.430 25.188 120.089 1.00 45.58 C ANISOU 2121 CA VAL A 261 6022 5861 5435 -812 480 96 C ATOM 2122 C VAL A 261 8.901 25.240 120.523 1.00 48.02 C ANISOU 2122 C VAL A 261 6000 6333 5912 -920 570 189 C ATOM 2123 O VAL A 261 9.784 24.855 119.748 1.00 50.06 O ANISOU 2123 O VAL A 261 6096 6857 6066 -883 832 348 O ATOM 2124 CB VAL A 261 7.018 23.709 119.846 1.00 44.10 C ANISOU 2124 CB VAL A 261 5957 5798 5002 -571 570 -73 C ATOM 2125 CG1 VAL A 261 7.288 22.859 121.067 1.00 42.70 C ANISOU 2125 CG1 VAL A 261 5649 5649 4926 -450 516 -272 C ATOM 2126 CG2 VAL A 261 5.548 23.597 119.468 1.00 42.76 C ANISOU 2126 CG2 VAL A 261 6058 5500 4689 -530 414 -110 C ATOM 2127 N GLN A 262 9.164 25.727 121.744 1.00 47.95 N ANISOU 2127 N GLN A 262 5892 6185 6143 -1042 352 114 N ATOM 2128 CA GLN A 262 10.511 25.678 122.329 1.00 50.58 C ANISOU 2128 CA GLN A 262 5877 6686 6656 -1173 351 214 C ATOM 2129 C GLN A 262 10.579 24.731 123.525 1.00 48.63 C ANISOU 2129 C GLN A 262 5558 6483 6436 -1000 260 -24 C ATOM 2130 O GLN A 262 9.694 24.745 124.370 1.00 47.22 O ANISOU 2130 O GLN A 262 5598 6099 6245 -929 74 -247 O ATOM 2131 CB GLN A 262 10.966 27.069 122.760 1.00 53.56 C ANISOU 2131 CB GLN A 262 6223 6849 7276 -1546 93 369 C ATOM 2132 CG GLN A 262 11.226 28.029 121.615 1.00 57.09 C ANISOU 2132 CG GLN A 262 6663 7285 7745 -1791 171 703 C ATOM 2133 CD GLN A 262 11.432 29.453 122.093 1.00 59.80 C ANISOU 2133 CD GLN A 262 7120 7275 8325 -2176 -171 823 C ATOM 2134 OE1 GLN A 262 10.922 29.845 123.141 1.00 58.51 O ANISOU 2134 OE1 GLN A 262 7223 6780 8230 -2167 -458 573 O ATOM 2135 NE2 GLN A 262 12.186 30.238 121.324 1.00 64.00 N ANISOU 2135 NE2 GLN A 262 7488 7866 8962 -2514 -145 1220 N ATOM 2136 N HIS A 263 11.637 23.927 123.600 1.00 49.84 N ANISOU 2136 N HIS A 263 5392 6924 6621 -909 406 58 N ATOM 2137 CA HIS A 263 11.837 22.972 124.696 1.00 49.14 C ANISOU 2137 CA HIS A 263 5212 6896 6564 -742 316 -116 C ATOM 2138 C HIS A 263 13.327 22.699 124.753 1.00 52.67 C ANISOU 2138 C HIS A 263 5188 7662 7162 -766 415 124 C ATOM 2139 O HIS A 263 13.993 22.901 123.750 1.00 55.94 O ANISOU 2139 O HIS A 263 5387 8296 7571 -792 663 388 O ATOM 2140 CB HIS A 263 11.076 21.674 124.420 1.00 46.98 C ANISOU 2140 CB HIS A 263 5161 6631 6057 -397 462 -313 C ATOM 2141 CG HIS A 263 11.039 20.723 125.579 1.00 45.81 C ANISOU 2141 CG HIS A 263 5000 6479 5926 -242 333 -485 C ATOM 2142 ND1 HIS A 263 11.908 19.658 125.694 1.00 47.06 N ANISOU 2142 ND1 HIS A 263 4954 6834 6091 -18 458 -448 N ATOM 2143 CD2 HIS A 263 10.235 20.670 126.668 1.00 43.48 C ANISOU 2143 CD2 HIS A 263 4875 6019 5626 -253 105 -666 C ATOM 2144 CE1 HIS A 263 11.648 18.996 126.807 1.00 45.52 C ANISOU 2144 CE1 HIS A 263 4815 6571 5909 64 277 -595 C ATOM 2145 NE2 HIS A 263 10.636 19.588 127.417 1.00 43.47 N ANISOU 2145 NE2 HIS A 263 4777 6112 5629 -85 73 -724 N ATOM 2146 N GLU A 264 13.863 22.243 125.890 1.00 53.30 N ANISOU 2146 N GLU A 264 5078 7808 7366 -747 237 77 N ATOM 2147 CA GLU A 264 15.315 22.012 125.986 1.00 58.02 C ANISOU 2147 CA GLU A 264 5144 8754 8148 -771 301 372 C ATOM 2148 C GLU A 264 15.797 20.721 125.312 1.00 59.15 C ANISOU 2148 C GLU A 264 5118 9190 8168 -308 696 428 C ATOM 2149 O GLU A 264 16.994 20.538 125.117 1.00 63.29 O ANISOU 2149 O GLU A 264 5152 10071 8825 -239 861 735 O ATOM 2150 CB GLU A 264 15.860 22.161 127.427 1.00 60.01 C ANISOU 2150 CB GLU A 264 5219 8989 8595 -981 -97 374 C ATOM 2151 CG GLU A 264 15.870 20.901 128.308 1.00 59.78 C ANISOU 2151 CG GLU A 264 5181 9020 8512 -663 -141 207 C ATOM 2152 CD GLU A 264 17.111 20.817 129.228 1.00 64.28 C ANISOU 2152 CD GLU A 264 5281 9829 9314 -803 -389 441 C ATOM 2153 OE1 GLU A 264 17.997 21.705 129.138 1.00 68.40 O ANISOU 2153 OE1 GLU A 264 5446 10493 10050 -1172 -527 757 O ATOM 2154 OE2 GLU A 264 17.211 19.856 130.035 1.00 63.75 O ANISOU 2154 OE2 GLU A 264 5188 9812 9222 -571 -474 349 O ATOM 2155 N GLY A 265 14.860 19.855 124.933 1.00 56.32 N ANISOU 2155 N GLY A 265 5176 8673 7552 10 839 155 N ATOM 2156 CA GLY A 265 15.147 18.663 124.145 1.00 57.95 C ANISOU 2156 CA GLY A 265 5417 9038 7562 477 1202 144 C ATOM 2157 C GLY A 265 14.966 18.824 122.637 1.00 60.18 C ANISOU 2157 C GLY A 265 5884 9385 7596 583 1546 212 C ATOM 2158 O GLY A 265 14.799 17.835 121.922 1.00 61.72 O ANISOU 2158 O GLY A 265 6363 9573 7516 975 1796 84 O ATOM 2159 N LEU A 266 15.006 20.059 122.139 1.00 60.75 N ANISOU 2159 N LEU A 266 5850 9496 7735 235 1539 415 N ATOM 2160 CA LEU A 266 14.911 20.323 120.700 1.00 62.21 C ANISOU 2160 CA LEU A 266 6185 9784 7669 298 1860 540 C ATOM 2161 C LEU A 266 16.100 21.153 120.239 1.00 67.14 C ANISOU 2161 C LEU A 266 6276 10781 8453 107 2059 1000 C ATOM 2162 O LEU A 266 16.329 22.245 120.762 1.00 67.55 O ANISOU 2162 O LEU A 266 6090 10783 8793 -353 1780 1187 O ATOM 2163 CB LEU A 266 13.622 21.080 120.367 1.00 58.87 C ANISOU 2163 CB LEU A 266 6200 9028 7139 35 1653 402 C ATOM 2164 CG LEU A 266 12.294 20.325 120.319 1.00 54.97 C ANISOU 2164 CG LEU A 266 6245 8235 6405 201 1529 53 C ATOM 2165 CD1 LEU A 266 11.129 21.300 120.383 1.00 51.98 C ANISOU 2165 CD1 LEU A 266 6109 7576 6066 -104 1250 0 C ATOM 2166 CD2 LEU A 266 12.210 19.461 119.076 1.00 56.57 C ANISOU 2166 CD2 LEU A 266 6771 8511 6210 537 1837 -3 C ATOM 2167 N PRO A 267 16.853 20.634 119.257 1.00 71.63 N ANISOU 2167 N PRO A 267 6679 11717 8819 464 2537 1200 N ATOM 2168 CA PRO A 267 18.049 21.265 118.678 1.00 77.47 C ANISOU 2168 CA PRO A 267 6838 12927 9669 352 2831 1722 C ATOM 2169 C PRO A 267 17.720 22.639 118.113 1.00 77.81 C ANISOU 2169 C PRO A 267 6944 12874 9747 -161 2713 1947 C ATOM 2170 O PRO A 267 18.234 23.651 118.589 1.00 79.68 O ANISOU 2170 O PRO A 267 6796 13148 10331 -652 2461 2256 O ATOM 2171 CB PRO A 267 18.442 20.309 117.542 1.00 81.18 C ANISOU 2171 CB PRO A 267 7402 13710 9733 967 3422 1753 C ATOM 2172 CG PRO A 267 17.804 19.001 117.889 1.00 78.12 C ANISOU 2172 CG PRO A 267 7518 13020 9146 1413 3364 1263 C ATOM 2173 CD PRO A 267 16.531 19.349 118.610 1.00 71.83 C ANISOU 2173 CD PRO A 267 7136 11710 8446 1029 2833 927 C ATOM 2174 N LYS A 268 16.845 22.661 117.117 1.00 76.45 N ANISOU 2174 N LYS A 268 7298 12541 9210 -62 2848 1794 N ATOM 2175 CA LYS A 268 16.212 23.886 116.677 1.00 75.21 C ANISOU 2175 CA LYS A 268 7353 12157 9067 -510 2648 1914 C ATOM 2176 C LYS A 268 14.746 23.753 117.109 1.00 68.92 C ANISOU 2176 C LYS A 268 7148 10844 8196 -518 2282 1442 C ATOM 2177 O LYS A 268 14.227 22.633 117.156 1.00 66.93 O ANISOU 2177 O LYS A 268 7210 10500 7721 -145 2332 1098 O ATOM 2178 CB LYS A 268 16.358 24.030 115.156 1.00 79.05 C ANISOU 2178 CB LYS A 268 7946 12918 9171 -384 3086 2176 C ATOM 2179 CG LYS A 268 16.500 25.470 114.662 1.00 81.61 C ANISOU 2179 CG LYS A 268 8121 13254 9631 -911 2998 2616 C ATOM 2180 CD LYS A 268 17.287 25.558 113.355 1.00 87.52 C ANISOU 2180 CD LYS A 268 8651 14518 10086 -788 3543 3074 C ATOM 2181 CE LYS A 268 18.788 25.444 113.593 1.00 92.57 C ANISOU 2181 CE LYS A 268 8495 15714 10963 -757 3832 3527 C ATOM 2182 NZ LYS A 268 19.538 25.344 112.311 1.00 98.76 N ANISOU 2182 NZ LYS A 268 9055 17079 11389 -499 4470 3966 N ATOM 2183 N PRO A 269 14.104 24.875 117.496 1.00 66.27 N ANISOU 2183 N PRO A 269 6946 10167 8066 -934 1900 1449 N ATOM 2184 CA PRO A 269 12.665 24.989 117.748 1.00 61.25 C ANISOU 2184 CA PRO A 269 6809 9101 7363 -948 1596 1114 C ATOM 2185 C PRO A 269 11.777 24.565 116.573 1.00 60.29 C ANISOU 2185 C PRO A 269 7135 8947 6826 -737 1751 1015 C ATOM 2186 O PRO A 269 12.141 24.769 115.415 1.00 64.09 O ANISOU 2186 O PRO A 269 7628 9648 7075 -725 2033 1268 O ATOM 2187 CB PRO A 269 12.478 26.491 118.008 1.00 61.79 C ANISOU 2187 CB PRO A 269 6882 8898 7696 -1397 1285 1296 C ATOM 2188 CG PRO A 269 13.794 27.140 117.636 1.00 67.14 C ANISOU 2188 CG PRO A 269 7107 9871 8531 -1677 1434 1767 C ATOM 2189 CD PRO A 269 14.800 26.093 117.936 1.00 68.76 C ANISOU 2189 CD PRO A 269 6907 10472 8748 -1416 1685 1787 C ATOM 2190 N LEU A 270 10.620 23.989 116.883 1.00 55.89 N ANISOU 2190 N LEU A 270 6939 8134 6163 -597 1548 680 N ATOM 2191 CA LEU A 270 9.712 23.463 115.877 1.00 55.44 C ANISOU 2191 CA LEU A 270 7329 8020 5714 -438 1593 572 C ATOM 2192 C LEU A 270 8.693 24.482 115.443 1.00 55.31 C ANISOU 2192 C LEU A 270 7536 7780 5698 -673 1362 679 C ATOM 2193 O LEU A 270 8.346 25.372 116.204 1.00 54.02 O ANISOU 2193 O LEU A 270 7281 7399 5844 -871 1106 700 O ATOM 2194 CB LEU A 270 8.954 22.265 116.427 1.00 51.70 C ANISOU 2194 CB LEU A 270 7101 7393 5148 -220 1439 221 C ATOM 2195 CG LEU A 270 9.718 20.959 116.551 1.00 52.24 C ANISOU 2195 CG LEU A 270 7146 7618 5085 119 1668 74 C ATOM 2196 CD1 LEU A 270 8.787 19.881 117.111 1.00 49.04 C ANISOU 2196 CD1 LEU A 270 7046 6978 4610 241 1424 -235 C ATOM 2197 CD2 LEU A 270 10.311 20.561 115.206 1.00 56.25 C ANISOU 2197 CD2 LEU A 270 7833 8357 5184 357 2054 175 C ATOM 2198 N THR A 271 8.191 24.320 114.224 1.00 57.99 N ANISOU 2198 N THR A 271 8212 8158 5662 -617 1437 738 N ATOM 2199 CA THR A 271 7.162 25.203 113.676 1.00 59.04 C ANISOU 2199 CA THR A 271 8572 8102 5759 -804 1206 877 C ATOM 2200 C THR A 271 6.083 24.404 112.944 1.00 59.86 C ANISOU 2200 C THR A 271 9113 8147 5484 -687 1075 738 C ATOM 2201 O THR A 271 6.378 23.721 111.967 1.00 62.56 O ANISOU 2201 O THR A 271 9716 8650 5405 -545 1282 725 O ATOM 2202 CB THR A 271 7.771 26.234 112.711 1.00 62.47 C ANISOU 2202 CB THR A 271 8947 8667 6123 -994 1381 1264 C ATOM 2203 OG1 THR A 271 8.697 27.055 113.426 1.00 63.10 O ANISOU 2203 OG1 THR A 271 8629 8753 6593 -1198 1402 1438 O ATOM 2204 CG2 THR A 271 6.697 27.121 112.114 1.00 62.93 C ANISOU 2204 CG2 THR A 271 9262 8510 6137 -1157 1123 1430 C ATOM 2205 N LEU A 272 4.838 24.475 113.414 1.00 58.45 N ANISOU 2205 N LEU A 272 9024 7749 5436 -742 726 650 N ATOM 2206 CA LEU A 272 3.755 23.753 112.744 1.00 59.96 C ANISOU 2206 CA LEU A 272 9589 7887 5304 -716 513 583 C ATOM 2207 C LEU A 272 2.716 24.709 112.157 1.00 61.68 C ANISOU 2207 C LEU A 272 9906 8002 5525 -881 254 835 C ATOM 2208 O LEU A 272 2.485 25.787 112.701 1.00 60.32 O ANISOU 2208 O LEU A 272 9513 7707 5701 -955 159 968 O ATOM 2209 CB LEU A 272 3.059 22.778 113.696 1.00 57.11 C ANISOU 2209 CB LEU A 272 9223 7420 5055 -644 295 335 C ATOM 2210 CG LEU A 272 3.693 21.692 114.569 1.00 55.64 C ANISOU 2210 CG LEU A 272 8952 7256 4931 -475 412 70 C ATOM 2211 CD1 LEU A 272 4.976 21.081 113.961 1.00 58.68 C ANISOU 2211 CD1 LEU A 272 9445 7805 5046 -280 783 3 C ATOM 2212 CD2 LEU A 272 3.927 22.208 115.964 1.00 52.68 C ANISOU 2212 CD2 LEU A 272 8176 6842 5000 -484 398 32 C ATOM 2213 N ARG A 273 2.084 24.311 111.055 1.00 65.17 N ANISOU 2213 N ARG A 273 10721 8475 5568 -924 114 900 N ATOM 2214 CA ARG A 273 1.039 25.139 110.454 1.00 68.13 C ANISOU 2214 CA ARG A 273 11179 8774 5933 -1070 -176 1178 C ATOM 2215 C ARG A 273 -0.079 24.336 109.830 1.00 70.46 C ANISOU 2215 C ARG A 273 11800 9056 5914 -1144 -528 1174 C ATOM 2216 O ARG A 273 -0.315 23.197 110.200 1.00 69.12 O ANISOU 2216 O ARG A 273 11737 8860 5665 -1110 -636 943 O ATOM 2217 CB ARG A 273 1.624 26.070 109.396 1.00 71.85 C ANISOU 2217 CB ARG A 273 11757 9326 6218 -1159 4 1464 C ATOM 2218 CG ARG A 273 2.675 25.433 108.511 1.00 75.00 C ANISOU 2218 CG ARG A 273 12408 9940 6148 -1076 360 1407 C ATOM 2219 CD ARG A 273 3.031 26.343 107.346 1.00 79.14 C ANISOU 2219 CD ARG A 273 13065 10584 6421 -1193 502 1765 C ATOM 2220 NE ARG A 273 4.477 26.529 107.262 1.00 81.14 N ANISOU 2220 NE ARG A 273 13118 11056 6654 -1136 979 1848 N ATOM 2221 CZ ARG A 273 5.088 27.710 107.264 1.00 82.32 C ANISOU 2221 CZ ARG A 273 12987 11231 7060 -1308 1108 2176 C ATOM 2222 NH1 ARG A 273 4.382 28.831 107.308 1.00 81.86 N ANISOU 2222 NH1 ARG A 273 12894 10939 7270 -1504 806 2416 N ATOM 2223 NH2 ARG A 273 6.409 27.767 107.199 1.00 84.68 N ANISOU 2223 NH2 ARG A 273 13041 11787 7346 -1283 1528 2299 N ATOM 2224 N TRP A 274 -0.763 24.950 108.871 1.00 75.45 N ANISOU 2224 N TRP A 274 12603 9692 6372 -1277 -747 1462 N ATOM 2225 CA TRP A 274 -1.805 24.266 108.111 1.00 79.76 C ANISOU 2225 CA TRP A 274 13492 10239 6574 -1417 -1151 1522 C ATOM 2226 C TRP A 274 -1.758 24.350 106.568 1.00 85.78 C ANISOU 2226 C TRP A 274 14751 11078 6765 -1525 -1205 1688 C ATOM 2227 O TRP A 274 -2.236 23.424 105.908 1.00 88.79 O ANISOU 2227 O TRP A 274 15577 11444 6716 -1628 -1481 1605 O ATOM 2228 CB TRP A 274 -3.195 24.608 108.649 1.00 79.29 C ANISOU 2228 CB TRP A 274 13123 10132 6873 -1497 -1563 1737 C ATOM 2229 CG TRP A 274 -3.834 23.436 109.303 1.00 78.25 C ANISOU 2229 CG TRP A 274 12957 9983 6791 -1549 -1808 1570 C ATOM 2230 CD1 TRP A 274 -3.466 22.858 110.472 1.00 75.10 C ANISOU 2230 CD1 TRP A 274 12339 9553 6644 -1428 -1639 1306 C ATOM 2231 CD2 TRP A 274 -4.945 22.679 108.811 1.00 80.84 C ANISOU 2231 CD2 TRP A 274 13488 10324 6904 -1784 -2307 1696 C ATOM 2232 NE1 TRP A 274 -4.278 21.786 110.749 1.00 75.56 N ANISOU 2232 NE1 TRP A 274 12448 9596 6664 -1567 -1977 1270 N ATOM 2233 CE2 TRP A 274 -5.198 21.658 109.744 1.00 79.14 C ANISOU 2233 CE2 TRP A 274 13152 10072 6845 -1808 -2406 1513 C ATOM 2234 CE3 TRP A 274 -5.750 22.767 107.671 1.00 85.29 C ANISOU 2234 CE3 TRP A 274 14327 10924 7154 -2013 -2719 1977 C ATOM 2235 CZ2 TRP A 274 -6.218 20.726 109.574 1.00 81.58 C ANISOU 2235 CZ2 TRP A 274 13598 10368 7029 -2085 -2910 1619 C ATOM 2236 CZ3 TRP A 274 -6.768 21.847 107.504 1.00 87.65 C ANISOU 2236 CZ3 TRP A 274 14761 11219 7322 -2288 -3244 2070 C ATOM 2237 CH2 TRP A 274 -6.995 20.841 108.454 1.00 85.95 C ANISOU 2237 CH2 TRP A 274 14409 10956 7293 -2338 -3339 1900 C ATOM 2238 N GLU A 275 -1.199 25.431 105.996 1.00 88.94 N ANISOU 2238 N GLU A 275 15118 11544 7131 -1526 -975 1933 N ATOM 2239 CA GLU A 275 -1.008 25.544 104.517 1.00 94.90 C ANISOU 2239 CA GLU A 275 16359 12416 7283 -1607 -950 2112 C ATOM 2240 C GLU A 275 0.099 24.617 103.990 1.00 97.83 C ANISOU 2240 C GLU A 275 17125 12919 7128 -1439 -546 1836 C ATOM 2241 O GLU A 275 1.175 24.535 104.598 1.00 96.77 O ANISOU 2241 O GLU A 275 16730 12856 7182 -1259 -105 1682 O ATOM 2242 CB GLU A 275 -0.698 26.987 104.059 1.00 96.38 C ANISOU 2242 CB GLU A 275 16390 12641 7588 -1674 -808 2512 C ATOM 2243 CG GLU A 275 -0.719 27.185 102.510 1.00101.80 C ANISOU 2243 CG GLU A 275 17579 13467 7635 -1787 -852 2777 C ATOM 2244 CD GLU A 275 -0.756 28.651 102.042 1.00103.88 C ANISOU 2244 CD GLU A 275 17705 13713 8050 -1912 -869 3261 C ATOM 2245 OE1 GLU A 275 -0.399 29.557 102.824 1.00101.81 O ANISOU 2245 OE1 GLU A 275 17013 13332 8338 -1896 -724 3368 O ATOM 2246 OE2 GLU A 275 -1.138 28.897 100.875 1.00107.65 O ANISOU 2246 OE2 GLU A 275 18557 14270 8074 -2038 -1058 3541 O ATOM 2247 OXT GLU A 275 -0.041 23.946 102.952 1.00102.00 O ANISOU 2247 OXT GLU A 275 18249 13486 7019 -1453 -647 1771 O TER 2248 GLU A 275 ATOM 2249 N MET B 0 -8.114 32.860 156.172 1.00 56.27 N ANISOU 2249 N MET B 0 6364 8352 6664 109 1241 -2035 N ATOM 2250 CA MET B 0 -8.411 31.502 155.623 1.00 54.63 C ANISOU 2250 CA MET B 0 6053 8302 6403 50 1146 -1655 C ATOM 2251 C MET B 0 -8.832 31.621 154.151 1.00 52.49 C ANISOU 2251 C MET B 0 5796 7711 6438 252 1066 -1470 C ATOM 2252 O MET B 0 -9.850 32.220 153.848 1.00 54.63 O ANISOU 2252 O MET B 0 5977 7906 6872 488 1133 -1584 O ATOM 2253 CB MET B 0 -9.503 30.809 156.450 1.00 57.35 C ANISOU 2253 CB MET B 0 6186 9086 6519 4 1270 -1669 C ATOM 2254 CG MET B 0 -9.295 29.304 156.655 1.00 57.70 C ANISOU 2254 CG MET B 0 6207 9385 6333 -232 1177 -1335 C ATOM 2255 SD MET B 0 -9.618 28.260 155.197 1.00 57.73 S ANISOU 2255 SD MET B 0 6179 9214 6542 -190 1024 -941 S ATOM 2256 CE MET B 0 -11.395 27.985 155.314 1.00 58.94 C ANISOU 2256 CE MET B 0 6046 9666 6684 -127 1179 -979 C ATOM 2257 N ILE B 1 -8.055 31.042 153.238 1.00 48.24 N ANISOU 2257 N ILE B 1 5359 7006 5964 171 917 -1194 N ATOM 2258 CA ILE B 1 -8.263 31.279 151.817 1.00 45.39 C ANISOU 2258 CA ILE B 1 5062 6332 5853 334 834 -1034 C ATOM 2259 C ILE B 1 -8.969 30.110 151.118 1.00 42.89 C ANISOU 2259 C ILE B 1 4617 6153 5527 345 753 -762 C ATOM 2260 O ILE B 1 -8.925 28.984 151.586 1.00 41.99 O ANISOU 2260 O ILE B 1 4427 6296 5233 175 732 -637 O ATOM 2261 CB ILE B 1 -6.926 31.696 151.132 1.00 44.10 C ANISOU 2261 CB ILE B 1 5114 5856 5787 242 755 -969 C ATOM 2262 CG1 ILE B 1 -7.149 32.845 150.181 1.00 45.28 C ANISOU 2262 CG1 ILE B 1 5409 5609 6186 430 752 -995 C ATOM 2263 CG2 ILE B 1 -6.255 30.575 150.364 1.00 41.53 C ANISOU 2263 CG2 ILE B 1 4803 5556 5422 119 630 -682 C ATOM 2264 CD1 ILE B 1 -5.938 33.144 149.432 1.00 44.52 C ANISOU 2264 CD1 ILE B 1 5508 5250 6159 295 699 -895 C ATOM 2265 N GLN B 2 -9.670 30.383 150.024 1.00 42.32 N ANISOU 2265 N GLN B 2 4529 5908 5642 541 698 -675 N ATOM 2266 CA GLN B 2 -10.324 29.318 149.280 1.00 40.14 C ANISOU 2266 CA GLN B 2 4136 5754 5362 532 605 -445 C ATOM 2267 C GLN B 2 -10.074 29.448 147.799 1.00 39.12 C ANISOU 2267 C GLN B 2 4144 5341 5378 623 472 -264 C ATOM 2268 O GLN B 2 -10.167 30.530 147.241 1.00 40.53 O ANISOU 2268 O GLN B 2 4429 5258 5711 807 458 -313 O ATOM 2269 CB GLN B 2 -11.825 29.286 149.539 1.00 41.90 C ANISOU 2269 CB GLN B 2 4095 6219 5606 667 668 -533 C ATOM 2270 CG GLN B 2 -12.216 28.570 150.809 1.00 42.37 C ANISOU 2270 CG GLN B 2 3983 6670 5446 481 792 -604 C ATOM 2271 CD GLN B 2 -13.628 28.848 151.182 1.00 45.19 C ANISOU 2271 CD GLN B 2 4052 7283 5833 623 909 -775 C ATOM 2272 OE1 GLN B 2 -14.523 28.697 150.365 1.00 46.43 O ANISOU 2272 OE1 GLN B 2 4053 7466 6122 754 836 -701 O ATOM 2273 NE2 GLN B 2 -13.848 29.275 152.414 1.00 47.51 N ANISOU 2273 NE2 GLN B 2 4254 7800 5999 604 1091 -1029 N ATOM 2274 N ARG B 3 -9.741 28.336 147.161 1.00 37.03 N ANISOU 2274 N ARG B 3 3900 5116 5053 490 372 -54 N ATOM 2275 CA ARG B 3 -9.473 28.336 145.744 1.00 36.16 C ANISOU 2275 CA ARG B 3 3921 4792 5026 544 256 111 C ATOM 2276 C ARG B 3 -10.152 27.162 145.047 1.00 36.17 C ANISOU 2276 C ARG B 3 3813 4938 4991 505 149 272 C ATOM 2277 O ARG B 3 -10.052 26.013 145.498 1.00 36.12 O ANISOU 2277 O ARG B 3 3743 5101 4880 330 142 327 O ATOM 2278 CB ARG B 3 -7.975 28.289 145.511 1.00 34.57 C ANISOU 2278 CB ARG B 3 3907 4438 4789 395 253 156 C ATOM 2279 CG ARG B 3 -7.305 29.635 145.603 1.00 35.41 C ANISOU 2279 CG ARG B 3 4173 4302 4978 428 323 36 C ATOM 2280 CD ARG B 3 -5.789 29.548 145.671 1.00 33.09 C ANISOU 2280 CD ARG B 3 3989 3951 4634 230 345 29 C ATOM 2281 NE ARG B 3 -5.249 30.747 146.302 1.00 34.08 N ANISOU 2281 NE ARG B 3 4211 3926 4811 196 435 -158 N ATOM 2282 CZ ARG B 3 -4.987 31.874 145.653 1.00 35.01 C ANISOU 2282 CZ ARG B 3 4517 3737 5050 227 461 -165 C ATOM 2283 NH1 ARG B 3 -5.199 31.956 144.351 1.00 36.19 N ANISOU 2283 NH1 ARG B 3 4778 3725 5249 301 401 26 N ATOM 2284 NH2 ARG B 3 -4.517 32.920 146.300 1.00 36.12 N ANISOU 2284 NH2 ARG B 3 4756 3722 5247 167 543 -358 N ATOM 2285 N THR B 4 -10.850 27.468 143.956 1.00 36.59 N ANISOU 2285 N THR B 4 3861 4913 5130 665 50 347 N ATOM 2286 CA THR B 4 -11.574 26.477 143.173 1.00 36.06 C ANISOU 2286 CA THR B 4 3688 4980 5034 631 -72 469 C ATOM 2287 C THR B 4 -10.579 25.695 142.361 1.00 33.32 C ANISOU 2287 C THR B 4 3516 4527 4617 485 -138 595 C ATOM 2288 O THR B 4 -9.647 26.266 141.829 1.00 32.67 O ANISOU 2288 O THR B 4 3627 4244 4541 501 -127 623 O ATOM 2289 CB THR B 4 -12.525 27.149 142.177 1.00 38.38 C ANISOU 2289 CB THR B 4 3937 5226 5421 866 -192 510 C ATOM 2290 OG1 THR B 4 -13.009 28.379 142.734 1.00 42.31 O ANISOU 2290 OG1 THR B 4 4378 5663 6034 1091 -127 372 O ATOM 2291 CG2 THR B 4 -13.697 26.254 141.849 1.00 38.86 C ANISOU 2291 CG2 THR B 4 3757 5545 5463 838 -294 546 C ATOM 2292 N PRO B 5 -10.752 24.373 142.303 1.00 32.01 N ANISOU 2292 N PRO B 5 3283 4494 4386 329 -193 655 N ATOM 2293 CA PRO B 5 -9.933 23.542 141.439 1.00 30.64 C ANISOU 2293 CA PRO B 5 3257 4223 4160 226 -264 738 C ATOM 2294 C PRO B 5 -10.155 23.829 139.952 1.00 31.99 C ANISOU 2294 C PRO B 5 3516 4315 4324 322 -374 808 C ATOM 2295 O PRO B 5 -11.287 24.095 139.544 1.00 33.59 O ANISOU 2295 O PRO B 5 3604 4605 4553 430 -461 826 O ATOM 2296 CB PRO B 5 -10.413 22.121 141.764 1.00 30.71 C ANISOU 2296 CB PRO B 5 3167 4372 4130 56 -313 772 C ATOM 2297 CG PRO B 5 -11.633 22.282 142.630 1.00 31.67 C ANISOU 2297 CG PRO B 5 3063 4703 4267 55 -265 725 C ATOM 2298 CD PRO B 5 -11.522 23.585 143.283 1.00 31.80 C ANISOU 2298 CD PRO B 5 3063 4698 4322 205 -156 628 C ATOM 2299 N LYS B 6 -9.067 23.832 139.177 1.00 31.41 N ANISOU 2299 N LYS B 6 3632 4103 4200 287 -367 841 N ATOM 2300 CA LYS B 6 -9.119 23.692 137.729 1.00 31.91 C ANISOU 2300 CA LYS B 6 3803 4136 4184 305 -468 912 C ATOM 2301 C LYS B 6 -9.233 22.201 137.527 1.00 31.02 C ANISOU 2301 C LYS B 6 3644 4114 4030 170 -539 889 C ATOM 2302 O LYS B 6 -8.672 21.458 138.313 1.00 30.77 O ANISOU 2302 O LYS B 6 3594 4072 4023 70 -485 846 O ATOM 2303 CB LYS B 6 -7.808 24.149 137.094 1.00 33.00 C ANISOU 2303 CB LYS B 6 4145 4132 4262 270 -386 929 C ATOM 2304 CG LYS B 6 -7.810 25.581 136.555 1.00 35.55 C ANISOU 2304 CG LYS B 6 4613 4315 4581 378 -372 1012 C ATOM 2305 CD LYS B 6 -6.935 26.500 137.374 1.00 35.72 C ANISOU 2305 CD LYS B 6 4696 4195 4680 351 -223 959 C ATOM 2306 CE LYS B 6 -5.499 26.012 137.381 1.00 35.35 C ANISOU 2306 CE LYS B 6 4693 4153 4585 183 -112 896 C ATOM 2307 NZ LYS B 6 -4.589 27.162 137.627 1.00 37.01 N ANISOU 2307 NZ LYS B 6 5017 4211 4833 122 17 874 N ATOM 2308 N ILE B 7 -9.967 21.740 136.519 1.00 31.11 N ANISOU 2308 N ILE B 7 3644 4200 3976 163 -675 913 N ATOM 2309 CA ILE B 7 -10.157 20.302 136.348 1.00 30.96 C ANISOU 2309 CA ILE B 7 3595 4232 3936 12 -749 866 C ATOM 2310 C ILE B 7 -9.798 19.928 134.936 1.00 31.59 C ANISOU 2310 C ILE B 7 3826 4290 3889 -9 -823 844 C ATOM 2311 O ILE B 7 -10.272 20.565 134.021 1.00 33.64 O ANISOU 2311 O ILE B 7 4118 4607 4056 72 -908 899 O ATOM 2312 CB ILE B 7 -11.618 19.882 136.599 1.00 32.47 C ANISOU 2312 CB ILE B 7 3575 4593 4167 -40 -854 866 C ATOM 2313 CG1 ILE B 7 -12.036 20.183 138.029 1.00 32.26 C ANISOU 2313 CG1 ILE B 7 3382 4641 4235 -42 -753 865 C ATOM 2314 CG2 ILE B 7 -11.809 18.387 136.408 1.00 33.40 C ANISOU 2314 CG2 ILE B 7 3699 4717 4274 -241 -932 816 C ATOM 2315 CD1 ILE B 7 -13.498 20.263 138.187 1.00 34.45 C ANISOU 2315 CD1 ILE B 7 3404 5135 4550 -36 -821 853 C ATOM 2316 N GLN B 8 -8.952 18.918 134.737 1.00 31.01 N ANISOU 2316 N GLN B 8 3850 4137 3796 -103 -795 759 N ATOM 2317 CA GLN B 8 -8.644 18.479 133.373 1.00 31.72 C ANISOU 2317 CA GLN B 8 4075 4235 3741 -131 -848 690 C ATOM 2318 C GLN B 8 -8.749 16.972 133.179 1.00 32.70 C ANISOU 2318 C GLN B 8 4221 4320 3886 -257 -928 565 C ATOM 2319 O GLN B 8 -8.034 16.212 133.823 1.00 31.78 O ANISOU 2319 O GLN B 8 4131 4072 3870 -287 -871 506 O ATOM 2320 CB GLN B 8 -7.248 18.925 132.943 1.00 30.23 C ANISOU 2320 CB GLN B 8 4026 3982 3480 -91 -702 658 C ATOM 2321 CG GLN B 8 -7.106 20.364 132.569 1.00 29.15 C ANISOU 2321 CG GLN B 8 3959 3857 3261 -15 -644 778 C ATOM 2322 CD GLN B 8 -5.747 20.632 131.951 1.00 29.98 C ANISOU 2322 CD GLN B 8 4195 3936 3258 -48 -488 730 C ATOM 2323 OE1 GLN B 8 -5.482 20.240 130.817 1.00 30.79 O ANISOU 2323 OE1 GLN B 8 4401 4111 3187 -95 -491 664 O ATOM 2324 NE2 GLN B 8 -4.873 21.299 132.703 1.00 29.63 N ANISOU 2324 NE2 GLN B 8 4134 3819 3306 -44 -343 742 N ATOM 2325 N VAL B 9 -9.623 16.558 132.259 1.00 34.31 N ANISOU 2325 N VAL B 9 4423 4624 3990 -326 -1076 520 N ATOM 2326 CA VAL B 9 -9.763 15.154 131.887 1.00 35.36 C ANISOU 2326 CA VAL B 9 4612 4693 4131 -468 -1164 369 C ATOM 2327 C VAL B 9 -9.094 14.864 130.548 1.00 36.92 C ANISOU 2327 C VAL B 9 4980 4899 4148 -457 -1162 218 C ATOM 2328 O VAL B 9 -9.363 15.551 129.556 1.00 38.81 O ANISOU 2328 O VAL B 9 5259 5300 4188 -423 -1212 251 O ATOM 2329 CB VAL B 9 -11.223 14.767 131.749 1.00 36.72 C ANISOU 2329 CB VAL B 9 4649 4999 4305 -602 -1339 372 C ATOM 2330 CG1 VAL B 9 -11.393 13.265 131.923 1.00 37.51 C ANISOU 2330 CG1 VAL B 9 4798 4952 4501 -801 -1403 244 C ATOM 2331 CG2 VAL B 9 -12.036 15.522 132.747 1.00 36.20 C ANISOU 2331 CG2 VAL B 9 4372 5042 4340 -566 -1326 521 C ATOM 2332 N TYR B 10 -8.255 13.830 130.513 1.00 36.70 N ANISOU 2332 N TYR B 10 5058 4705 4180 -480 -1112 49 N ATOM 2333 CA TYR B 10 -7.447 13.530 129.328 1.00 37.93 C ANISOU 2333 CA TYR B 10 5362 4883 4168 -452 -1059 -146 C ATOM 2334 C TYR B 10 -6.854 12.135 129.422 1.00 38.64 C ANISOU 2334 C TYR B 10 5541 4750 4391 -468 -1056 -368 C ATOM 2335 O TYR B 10 -6.835 11.525 130.494 1.00 38.23 O ANISOU 2335 O TYR B 10 5462 4499 4564 -479 -1078 -322 O ATOM 2336 CB TYR B 10 -6.308 14.554 129.148 1.00 36.55 C ANISOU 2336 CB TYR B 10 5213 4775 3899 -330 -868 -97 C ATOM 2337 CG TYR B 10 -5.378 14.696 130.350 1.00 34.92 C ANISOU 2337 CG TYR B 10 4933 4434 3900 -241 -737 -48 C ATOM 2338 CD1 TYR B 10 -5.705 15.520 131.434 1.00 33.47 C ANISOU 2338 CD1 TYR B 10 4642 4245 3828 -217 -725 157 C ATOM 2339 CD2 TYR B 10 -4.175 14.024 130.398 1.00 34.51 C ANISOU 2339 CD2 TYR B 10 4906 4281 3924 -167 -635 -226 C ATOM 2340 CE1 TYR B 10 -4.868 15.651 132.521 1.00 31.46 C ANISOU 2340 CE1 TYR B 10 4324 3901 3728 -152 -626 189 C ATOM 2341 CE2 TYR B 10 -3.341 14.155 131.462 1.00 33.33 C ANISOU 2341 CE2 TYR B 10 4671 4046 3945 -79 -552 -182 C ATOM 2342 CZ TYR B 10 -3.681 14.972 132.528 1.00 31.45 C ANISOU 2342 CZ TYR B 10 4343 3817 3789 -86 -552 30 C ATOM 2343 OH TYR B 10 -2.835 15.103 133.608 1.00 29.57 O ANISOU 2343 OH TYR B 10 4022 3521 3693 -13 -486 62 O ATOM 2344 N SER B 11 -6.324 11.660 128.306 1.00 39.91 N ANISOU 2344 N SER B 11 5822 4937 4403 -456 -1025 -608 N ATOM 2345 CA SER B 11 -5.723 10.345 128.260 1.00 41.60 C ANISOU 2345 CA SER B 11 6138 4916 4751 -428 -1025 -865 C ATOM 2346 C SER B 11 -4.205 10.449 128.311 1.00 41.81 C ANISOU 2346 C SER B 11 6154 4914 4817 -236 -831 -980 C ATOM 2347 O SER B 11 -3.654 11.510 128.037 1.00 41.73 O ANISOU 2347 O SER B 11 6086 5111 4657 -185 -685 -904 O ATOM 2348 CB SER B 11 -6.147 9.666 126.982 1.00 44.42 C ANISOU 2348 CB SER B 11 6623 5334 4922 -537 -1114 -1124 C ATOM 2349 OG SER B 11 -5.746 10.450 125.877 1.00 45.25 O ANISOU 2349 OG SER B 11 6757 5723 4715 -503 -1009 -1179 O ATOM 2350 N ARG B 12 -3.523 9.365 128.667 1.00 42.98 N ANISOU 2350 N ARG B 12 6352 4804 5175 -129 -834 -1161 N ATOM 2351 CA ARG B 12 -2.058 9.389 128.708 1.00 43.56 C ANISOU 2351 CA ARG B 12 6363 4881 5308 82 -664 -1308 C ATOM 2352 C ARG B 12 -1.513 9.323 127.273 1.00 46.21 C ANISOU 2352 C ARG B 12 6750 5410 5398 105 -531 -1619 C ATOM 2353 O ARG B 12 -0.625 10.081 126.888 1.00 45.65 O ANISOU 2353 O ARG B 12 6587 5573 5186 164 -332 -1657 O ATOM 2354 CB ARG B 12 -1.507 8.246 129.588 1.00 44.74 C ANISOU 2354 CB ARG B 12 6543 4681 5777 237 -742 -1390 C ATOM 2355 CG ARG B 12 0.019 8.059 129.536 1.00 46.37 C ANISOU 2355 CG ARG B 12 6651 4895 6074 500 -599 -1613 C ATOM 2356 CD ARG B 12 0.501 6.758 130.195 1.00 48.61 C ANISOU 2356 CD ARG B 12 7007 4790 6673 699 -728 -1731 C ATOM 2357 NE ARG B 12 0.290 6.765 131.641 1.00 46.81 N ANISOU 2357 NE ARG B 12 6762 4389 6636 698 -859 -1406 N ATOM 2358 CZ ARG B 12 0.565 5.757 132.465 1.00 47.60 C ANISOU 2358 CZ ARG B 12 6955 4133 6999 841 -1013 -1379 C ATOM 2359 NH1 ARG B 12 1.084 4.628 132.014 1.00 51.11 N ANISOU 2359 NH1 ARG B 12 7514 4305 7599 1033 -1066 -1675 N ATOM 2360 NH2 ARG B 12 0.305 5.884 133.753 1.00 45.90 N ANISOU 2360 NH2 ARG B 12 6733 3825 6882 795 -1119 -1053 N ATOM 2361 N HIS B 13 -2.087 8.434 126.476 1.00 49.21 N ANISOU 2361 N HIS B 13 7281 5711 5707 23 -635 -1845 N ATOM 2362 CA HIS B 13 -1.716 8.325 125.076 1.00 52.70 C ANISOU 2362 CA HIS B 13 7794 6365 5864 14 -519 -2161 C ATOM 2363 C HIS B 13 -2.855 8.812 124.173 1.00 52.74 C ANISOU 2363 C HIS B 13 7887 6610 5540 -214 -620 -2076 C ATOM 2364 O HIS B 13 -3.994 8.918 124.621 1.00 50.90 O ANISOU 2364 O HIS B 13 7654 6319 5366 -347 -809 -1848 O ATOM 2365 CB HIS B 13 -1.338 6.875 124.758 1.00 56.90 C ANISOU 2365 CB HIS B 13 8443 6627 6550 126 -556 -2569 C ATOM 2366 CG HIS B 13 -0.227 6.349 125.609 1.00 58.10 C ANISOU 2366 CG HIS B 13 8506 6534 7034 398 -498 -2653 C ATOM 2367 ND1 HIS B 13 1.088 6.723 125.430 1.00 59.03 N ANISOU 2367 ND1 HIS B 13 8458 6849 7123 593 -269 -2805 N ATOM 2368 CD2 HIS B 13 -0.234 5.484 126.652 1.00 58.42 C ANISOU 2368 CD2 HIS B 13 8596 6165 7437 506 -654 -2593 C ATOM 2369 CE1 HIS B 13 1.842 6.105 126.321 1.00 59.83 C ANISOU 2369 CE1 HIS B 13 8484 6682 7565 840 -306 -2851 C ATOM 2370 NE2 HIS B 13 1.064 5.347 127.074 1.00 59.34 N ANISOU 2370 NE2 HIS B 13 8575 6235 7738 798 -545 -2709 N ATOM 2371 N PRO B 14 -2.538 9.164 122.916 1.00 54.70 N ANISOU 2371 N PRO B 14 8193 7166 5424 -257 -493 -2246 N ATOM 2372 CA PRO B 14 -3.589 9.345 121.925 1.00 56.53 C ANISOU 2372 CA PRO B 14 8541 7614 5323 -453 -637 -2236 C ATOM 2373 C PRO B 14 -4.460 8.086 121.770 1.00 58.81 C ANISOU 2373 C PRO B 14 8942 7688 5715 -560 -863 -2466 C ATOM 2374 O PRO B 14 -3.946 7.005 121.460 1.00 61.17 O ANISOU 2374 O PRO B 14 9333 7810 6100 -493 -822 -2851 O ATOM 2375 CB PRO B 14 -2.797 9.620 120.652 1.00 59.48 C ANISOU 2375 CB PRO B 14 8984 8313 5304 -458 -425 -2467 C ATOM 2376 CG PRO B 14 -1.602 10.354 121.153 1.00 57.62 C ANISOU 2376 CG PRO B 14 8606 8132 5155 -327 -168 -2357 C ATOM 2377 CD PRO B 14 -1.246 9.694 122.439 1.00 55.34 C ANISOU 2377 CD PRO B 14 8205 7477 5343 -157 -206 -2367 C ATOM 2378 N ALA B 15 -5.758 8.241 122.032 1.00 57.88 N ANISOU 2378 N ALA B 15 8803 7575 5614 -723 -1095 -2241 N ATOM 2379 CA ALA B 15 -6.676 7.113 122.140 1.00 59.53 C ANISOU 2379 CA ALA B 15 9081 7554 5982 -880 -1318 -2395 C ATOM 2380 C ALA B 15 -6.943 6.439 120.802 1.00 64.11 C ANISOU 2380 C ALA B 15 9822 8266 6272 -1012 -1395 -2782 C ATOM 2381 O ALA B 15 -7.383 7.062 119.842 1.00 65.64 O ANISOU 2381 O ALA B 15 10034 8832 6075 -1111 -1451 -2754 O ATOM 2382 CB ALA B 15 -7.971 7.548 122.782 1.00 57.23 C ANISOU 2382 CB ALA B 15 8663 7307 5773 -1031 -1519 -2059 C ATOM 2383 N GLU B 16 -6.634 5.155 120.749 1.00 66.92 N ANISOU 2383 N GLU B 16 10311 8300 6815 -1002 -1403 -3151 N ATOM 2384 CA GLU B 16 -6.930 4.336 119.601 1.00 71.29 C ANISOU 2384 CA GLU B 16 11035 8906 7146 -1145 -1491 -3579 C ATOM 2385 C GLU B 16 -8.033 3.416 120.107 1.00 72.49 C ANISOU 2385 C GLU B 16 11232 8746 7565 -1378 -1749 -3594 C ATOM 2386 O GLU B 16 -7.842 2.730 121.104 1.00 71.66 O ANISOU 2386 O GLU B 16 11159 8202 7868 -1325 -1755 -3555 O ATOM 2387 CB GLU B 16 -5.677 3.544 119.201 1.00 74.11 C ANISOU 2387 CB GLU B 16 11516 9085 7559 -938 -1288 -4029 C ATOM 2388 CG GLU B 16 -5.318 3.582 117.702 1.00 78.28 C ANISOU 2388 CG GLU B 16 12148 9987 7606 -965 -1174 -4413 C ATOM 2389 CD GLU B 16 -3.807 3.467 117.433 1.00 79.64 C ANISOU 2389 CD GLU B 16 12308 10180 7770 -685 -854 -4712 C ATOM 2390 OE1 GLU B 16 -3.034 4.239 118.057 1.00 76.11 O ANISOU 2390 OE1 GLU B 16 11695 9796 7427 -509 -674 -4442 O ATOM 2391 OE2 GLU B 16 -3.401 2.618 116.589 1.00 83.57 O ANISOU 2391 OE2 GLU B 16 12944 10654 8153 -648 -781 -5239 O ATOM 2392 N ASN B 17 -9.192 3.454 119.447 1.00 74.99 N ANISOU 2392 N ASN B 17 11541 9312 7640 -1648 -1967 -3620 N ATOM 2393 CA ASN B 17 -10.393 2.716 119.861 1.00 76.58 C ANISOU 2393 CA ASN B 17 11732 9314 8050 -1943 -2218 -3613 C ATOM 2394 C ASN B 17 -10.183 1.219 120.048 1.00 80.15 C ANISOU 2394 C ASN B 17 12408 9228 8815 -2018 -2249 -3975 C ATOM 2395 O ASN B 17 -9.712 0.532 119.140 1.00 83.69 O ANISOU 2395 O ASN B 17 13052 9610 9135 -1993 -2213 -4434 O ATOM 2396 CB ASN B 17 -11.530 2.947 118.864 1.00 79.40 C ANISOU 2396 CB ASN B 17 12036 10094 8038 -2207 -2452 -3686 C ATOM 2397 CG ASN B 17 -12.457 4.071 119.282 1.00 76.89 C ANISOU 2397 CG ASN B 17 11446 10111 7657 -2251 -2575 -3224 C ATOM 2398 OD1 ASN B 17 -12.327 4.621 120.369 1.00 73.24 O ANISOU 2398 OD1 ASN B 17 10845 9541 7443 -2121 -2481 -2869 O ATOM 2399 ND2 ASN B 17 -13.408 4.409 118.419 1.00 79.44 N ANISOU 2399 ND2 ASN B 17 11688 10849 7646 -2422 -2800 -3246 N ATOM 2400 N GLY B 18 -10.491 0.733 121.249 1.00 79.24 N ANISOU 2400 N GLY B 18 12281 8717 9109 -2099 -2306 -3763 N ATOM 2401 CA GLY B 18 -10.314 -0.678 121.574 1.00 82.78 C ANISOU 2401 CA GLY B 18 12981 8570 9902 -2171 -2355 -4029 C ATOM 2402 C GLY B 18 -8.888 -1.068 121.932 1.00 82.76 C ANISOU 2402 C GLY B 18 13117 8198 10130 -1785 -2164 -4151 C ATOM 2403 O GLY B 18 -8.567 -2.250 122.037 1.00 86.19 O ANISOU 2403 O GLY B 18 13798 8112 10837 -1763 -2202 -4429 O ATOM 2404 N LYS B 19 -8.029 -0.080 122.137 1.00 79.25 N ANISOU 2404 N LYS B 19 12510 8008 9594 -1478 -1970 -3947 N ATOM 2405 CA LYS B 19 -6.662 -0.345 122.549 1.00 79.38 C ANISOU 2405 CA LYS B 19 12582 7745 9834 -1097 -1796 -4038 C ATOM 2406 C LYS B 19 -6.458 0.366 123.879 1.00 74.58 C ANISOU 2406 C LYS B 19 11796 7119 9422 -976 -1746 -3532 C ATOM 2407 O LYS B 19 -6.757 1.551 123.996 1.00 71.20 O ANISOU 2407 O LYS B 19 11154 7103 8794 -1012 -1699 -3219 O ATOM 2408 CB LYS B 19 -5.680 0.149 121.484 1.00 80.61 C ANISOU 2408 CB LYS B 19 12691 8266 9672 -860 -1581 -4332 C ATOM 2409 CG LYS B 19 -4.223 -0.174 121.752 1.00 81.79 C ANISOU 2409 CG LYS B 19 12847 8190 10038 -454 -1391 -4518 C ATOM 2410 CD LYS B 19 -3.309 0.693 120.891 1.00 81.48 C ANISOU 2410 CD LYS B 19 12661 8654 9644 -272 -1130 -4666 C ATOM 2411 CE LYS B 19 -1.963 0.921 121.569 1.00 79.75 C ANISOU 2411 CE LYS B 19 12286 8367 9649 104 -936 -4610 C ATOM 2412 NZ LYS B 19 -1.091 1.811 120.760 1.00 79.69 N ANISOU 2412 NZ LYS B 19 12113 8876 9288 219 -657 -4733 N ATOM 2413 N SER B 20 -5.967 -0.374 124.869 1.00 74.90 N ANISOU 2413 N SER B 20 11944 6667 9847 -832 -1771 -3461 N ATOM 2414 CA SER B 20 -5.957 0.050 126.271 1.00 71.45 C ANISOU 2414 CA SER B 20 11390 6140 9616 -788 -1777 -2986 C ATOM 2415 C SER B 20 -5.103 1.280 126.547 1.00 67.58 C ANISOU 2415 C SER B 20 10656 6014 9009 -521 -1588 -2781 C ATOM 2416 O SER B 20 -4.129 1.533 125.840 1.00 68.31 O ANISOU 2416 O SER B 20 10699 6283 8973 -281 -1427 -3032 O ATOM 2417 CB SER B 20 -5.456 -1.091 127.143 1.00 73.81 C ANISOU 2417 CB SER B 20 11905 5822 10318 -651 -1861 -2988 C ATOM 2418 OG SER B 20 -4.067 -1.277 126.948 1.00 74.94 O ANISOU 2418 OG SER B 20 12054 5864 10555 -225 -1739 -3237 O ATOM 2419 N ASN B 21 -5.471 2.028 127.586 1.00 63.58 N ANISOU 2419 N ASN B 21 9993 5619 8545 -586 -1596 -2345 N ATOM 2420 CA ASN B 21 -4.864 3.324 127.858 1.00 59.58 C ANISOU 2420 CA ASN B 21 9255 5475 7909 -409 -1432 -2130 C ATOM 2421 C ASN B 21 -4.948 3.686 129.340 1.00 55.82 C ANISOU 2421 C ASN B 21 8682 4911 7615 -402 -1457 -1717 C ATOM 2422 O ASN B 21 -5.078 2.814 130.197 1.00 56.99 O ANISOU 2422 O ASN B 21 8963 4676 8014 -441 -1573 -1618 O ATOM 2423 CB ASN B 21 -5.580 4.399 127.032 1.00 58.83 C ANISOU 2423 CB ASN B 21 9030 5860 7461 -573 -1400 -2068 C ATOM 2424 CG ASN B 21 -4.628 5.236 126.207 1.00 58.76 C ANISOU 2424 CG ASN B 21 8935 6185 7206 -384 -1199 -2197 C ATOM 2425 OD1 ASN B 21 -3.821 4.697 125.449 1.00 62.13 O ANISOU 2425 OD1 ASN B 21 9445 6570 7591 -244 -1109 -2554 O ATOM 2426 ND2 ASN B 21 -4.729 6.555 126.329 1.00 55.54 N ANISOU 2426 ND2 ASN B 21 8366 6108 6629 -392 -1118 -1921 N ATOM 2427 N PHE B 22 -4.892 4.980 129.632 1.00 50.89 N ANISOU 2427 N PHE B 22 7848 4639 6848 -367 -1349 -1478 N ATOM 2428 CA PHE B 22 -5.019 5.458 130.994 1.00 47.80 C ANISOU 2428 CA PHE B 22 7351 4234 6577 -375 -1356 -1116 C ATOM 2429 C PHE B 22 -5.835 6.726 131.008 1.00 44.39 C ANISOU 2429 C PHE B 22 6737 4181 5948 -511 -1317 -892 C ATOM 2430 O PHE B 22 -5.543 7.647 130.269 1.00 43.55 O ANISOU 2430 O PHE B 22 6544 4365 5638 -435 -1210 -940 O ATOM 2431 CB PHE B 22 -3.646 5.764 131.578 1.00 47.56 C ANISOU 2431 CB PHE B 22 7240 4186 6647 -74 -1245 -1089 C ATOM 2432 CG PHE B 22 -3.041 4.628 132.314 1.00 50.29 C ANISOU 2432 CG PHE B 22 7726 4113 7270 74 -1345 -1114 C ATOM 2433 CD1 PHE B 22 -2.222 3.722 131.665 1.00 53.76 C ANISOU 2433 CD1 PHE B 22 8282 4324 7819 283 -1351 -1452 C ATOM 2434 CD2 PHE B 22 -3.293 4.457 133.669 1.00 50.30 C ANISOU 2434 CD2 PHE B 22 7753 3944 7415 16 -1441 -798 C ATOM 2435 CE1 PHE B 22 -1.664 2.655 132.353 1.00 56.58 C ANISOU 2435 CE1 PHE B 22 8789 4248 8459 464 -1476 -1463 C ATOM 2436 CE2 PHE B 22 -2.736 3.394 134.368 1.00 52.93 C ANISOU 2436 CE2 PHE B 22 8255 3865 7993 162 -1566 -776 C ATOM 2437 CZ PHE B 22 -1.918 2.492 133.708 1.00 55.97 C ANISOU 2437 CZ PHE B 22 8764 3983 8520 403 -1597 -1102 C ATOM 2438 N LEU B 23 -6.860 6.781 131.845 1.00 42.97 N ANISOU 2438 N LEU B 23 6502 3997 5827 -709 -1400 -649 N ATOM 2439 CA LEU B 23 -7.710 7.959 131.904 1.00 40.98 C ANISOU 2439 CA LEU B 23 6059 4089 5422 -802 -1377 -458 C ATOM 2440 C LEU B 23 -7.295 8.840 133.065 1.00 38.90 C ANISOU 2440 C LEU B 23 5666 3902 5211 -684 -1275 -213 C ATOM 2441 O LEU B 23 -7.310 8.388 134.202 1.00 39.46 O ANISOU 2441 O LEU B 23 5760 3801 5434 -728 -1303 -66 O ATOM 2442 CB LEU B 23 -9.167 7.539 132.084 1.00 41.56 C ANISOU 2442 CB LEU B 23 6092 4182 5516 -1101 -1514 -382 C ATOM 2443 CG LEU B 23 -10.188 8.643 132.368 1.00 39.20 C ANISOU 2443 CG LEU B 23 5555 4223 5118 -1179 -1511 -181 C ATOM 2444 CD1 LEU B 23 -10.352 9.610 131.193 1.00 38.09 C ANISOU 2444 CD1 LEU B 23 5340 4387 4745 -1089 -1514 -248 C ATOM 2445 CD2 LEU B 23 -11.510 8.010 132.743 1.00 40.77 C ANISOU 2445 CD2 LEU B 23 5682 4423 5384 -1491 -1629 -126 C ATOM 2446 N ASN B 24 -6.930 10.090 132.796 1.00 37.33 N ANISOU 2446 N ASN B 24 5354 3952 4877 -556 -1162 -165 N ATOM 2447 CA ASN B 24 -6.453 10.971 133.860 1.00 35.56 C ANISOU 2447 CA ASN B 24 5019 3793 4700 -450 -1061 22 C ATOM 2448 C ASN B 24 -7.417 12.090 134.197 1.00 35.20 C ANISOU 2448 C ASN B 24 4817 3978 4578 -515 -1048 204 C ATOM 2449 O ASN B 24 -8.042 12.654 133.310 1.00 36.45 O ANISOU 2449 O ASN B 24 4938 4315 4597 -540 -1077 185 O ATOM 2450 CB ASN B 24 -5.135 11.620 133.460 1.00 34.20 C ANISOU 2450 CB ASN B 24 4835 3692 4469 -254 -919 -68 C ATOM 2451 CG ASN B 24 -4.015 10.638 133.324 1.00 35.30 C ANISOU 2451 CG ASN B 24 5064 3633 4717 -122 -909 -260 C ATOM 2452 OD1 ASN B 24 -3.942 9.657 134.045 1.00 36.36 O ANISOU 2452 OD1 ASN B 24 5272 3523 5022 -115 -1002 -241 O ATOM 2453 ND2 ASN B 24 -3.112 10.908 132.403 1.00 36.01 N ANISOU 2453 ND2 ASN B 24 5150 3828 4705 -8 -792 -444 N ATOM 2454 N CYS B 25 -7.517 12.421 135.477 1.00 34.92 N ANISOU 2454 N CYS B 25 4695 3948 4626 -522 -1010 371 N ATOM 2455 CA CYS B 25 -8.141 13.669 135.899 1.00 34.71 C ANISOU 2455 CA CYS B 25 4511 4132 4545 -508 -956 505 C ATOM 2456 C CYS B 25 -7.186 14.423 136.824 1.00 33.08 C ANISOU 2456 C CYS B 25 4272 3925 4373 -382 -834 574 C ATOM 2457 O CYS B 25 -6.762 13.897 137.859 1.00 33.54 O ANISOU 2457 O CYS B 25 4349 3879 4515 -395 -834 627 O ATOM 2458 CB CYS B 25 -9.478 13.433 136.605 1.00 36.96 C ANISOU 2458 CB CYS B 25 4675 4500 4869 -684 -1016 608 C ATOM 2459 SG CYS B 25 -10.348 14.969 137.047 1.00 37.86 S ANISOU 2459 SG CYS B 25 4566 4883 4938 -614 -952 714 S ATOM 2460 N TYR B 26 -6.847 15.649 136.453 1.00 31.32 N ANISOU 2460 N TYR B 26 4014 3811 4076 -276 -745 578 N ATOM 2461 CA TYR B 26 -5.823 16.392 137.161 1.00 30.15 C ANISOU 2461 CA TYR B 26 3842 3661 3955 -183 -630 599 C ATOM 2462 C TYR B 26 -6.433 17.655 137.752 1.00 29.99 C ANISOU 2462 C TYR B 26 3722 3754 3920 -163 -574 695 C ATOM 2463 O TYR B 26 -6.654 18.651 137.052 1.00 30.01 O ANISOU 2463 O TYR B 26 3733 3812 3858 -107 -545 710 O ATOM 2464 CB TYR B 26 -4.637 16.683 136.214 1.00 30.04 C ANISOU 2464 CB TYR B 26 3894 3637 3881 -100 -545 488 C ATOM 2465 CG TYR B 26 -3.564 17.666 136.689 1.00 28.32 C ANISOU 2465 CG TYR B 26 3631 3454 3673 -41 -413 488 C ATOM 2466 CD1 TYR B 26 -2.711 17.367 137.756 1.00 28.13 C ANISOU 2466 CD1 TYR B 26 3550 3396 3743 -6 -400 471 C ATOM 2467 CD2 TYR B 26 -3.380 18.875 136.034 1.00 27.69 C ANISOU 2467 CD2 TYR B 26 3580 3438 3502 -36 -315 507 C ATOM 2468 CE1 TYR B 26 -1.719 18.277 138.173 1.00 27.05 C ANISOU 2468 CE1 TYR B 26 3348 3317 3612 17 -290 444 C ATOM 2469 CE2 TYR B 26 -2.403 19.776 136.434 1.00 27.32 C ANISOU 2469 CE2 TYR B 26 3500 3408 3471 -32 -189 494 C ATOM 2470 CZ TYR B 26 -1.575 19.477 137.494 1.00 27.13 C ANISOU 2470 CZ TYR B 26 3385 3379 3545 -13 -175 445 C ATOM 2471 OH TYR B 26 -0.619 20.408 137.860 1.00 27.55 O ANISOU 2471 OH TYR B 26 3385 3473 3608 -39 -59 409 O ATOM 2472 N VAL B 27 -6.743 17.586 139.044 1.00 30.21 N ANISOU 2472 N VAL B 27 3671 3808 4001 -207 -563 758 N ATOM 2473 CA VAL B 27 -7.224 18.751 139.771 1.00 29.42 C ANISOU 2473 CA VAL B 27 3470 3812 3898 -171 -490 800 C ATOM 2474 C VAL B 27 -6.042 19.541 140.296 1.00 28.76 C ANISOU 2474 C VAL B 27 3411 3697 3822 -108 -387 765 C ATOM 2475 O VAL B 27 -5.080 18.975 140.843 1.00 28.20 O ANISOU 2475 O VAL B 27 3362 3583 3769 -121 -387 744 O ATOM 2476 CB VAL B 27 -8.242 18.416 140.898 1.00 29.84 C ANISOU 2476 CB VAL B 27 3403 3971 3963 -270 -498 858 C ATOM 2477 CG1 VAL B 27 -9.522 17.925 140.289 1.00 31.36 C ANISOU 2477 CG1 VAL B 27 3520 4242 4155 -349 -587 873 C ATOM 2478 CG2 VAL B 27 -7.705 17.388 141.897 1.00 29.52 C ANISOU 2478 CG2 VAL B 27 3414 3874 3928 -369 -518 906 C ATOM 2479 N SER B 28 -6.100 20.851 140.085 1.00 28.07 N ANISOU 2479 N SER B 28 3322 3618 3726 -38 -315 755 N ATOM 2480 CA SER B 28 -4.986 21.716 140.450 1.00 27.19 C ANISOU 2480 CA SER B 28 3242 3466 3624 -19 -212 703 C ATOM 2481 C SER B 28 -5.526 23.086 140.793 1.00 27.31 C ANISOU 2481 C SER B 28 3242 3473 3663 39 -148 700 C ATOM 2482 O SER B 28 -6.658 23.419 140.440 1.00 27.88 O ANISOU 2482 O SER B 28 3285 3565 3744 108 -191 742 O ATOM 2483 CB SER B 28 -3.938 21.808 139.318 1.00 26.04 C ANISOU 2483 CB SER B 28 3191 3258 3446 -20 -172 666 C ATOM 2484 OG SER B 28 -4.291 22.755 138.328 1.00 25.49 O ANISOU 2484 OG SER B 28 3210 3143 3330 12 -147 713 O ATOM 2485 N GLY B 29 -4.718 23.862 141.503 1.00 26.75 N ANISOU 2485 N GLY B 29 3181 3372 3611 20 -57 631 N ATOM 2486 CA GLY B 29 -5.064 25.228 141.830 1.00 26.98 C ANISOU 2486 CA GLY B 29 3235 3334 3684 78 12 592 C ATOM 2487 C GLY B 29 -6.035 25.394 142.978 1.00 27.24 C ANISOU 2487 C GLY B 29 3148 3472 3731 120 26 541 C ATOM 2488 O GLY B 29 -6.666 26.434 143.092 1.00 28.22 O ANISOU 2488 O GLY B 29 3275 3537 3912 225 63 496 O ATOM 2489 N PHE B 30 -6.148 24.391 143.844 1.00 26.85 N ANISOU 2489 N PHE B 30 3002 3574 3627 42 1 546 N ATOM 2490 CA PHE B 30 -7.144 24.441 144.917 1.00 28.47 C ANISOU 2490 CA PHE B 30 3078 3936 3803 45 39 501 C ATOM 2491 C PHE B 30 -6.614 24.672 146.344 1.00 29.65 C ANISOU 2491 C PHE B 30 3202 4189 3876 -30 112 400 C ATOM 2492 O PHE B 30 -5.478 24.316 146.666 1.00 29.96 O ANISOU 2492 O PHE B 30 3292 4222 3869 -110 86 401 O ATOM 2493 CB PHE B 30 -8.111 23.245 144.850 1.00 28.44 C ANISOU 2493 CB PHE B 30 2977 4064 3765 -18 -32 599 C ATOM 2494 CG PHE B 30 -7.466 21.897 145.042 1.00 28.18 C ANISOU 2494 CG PHE B 30 2997 4035 3675 -151 -105 689 C ATOM 2495 CD1 PHE B 30 -6.784 21.265 144.008 1.00 27.67 C ANISOU 2495 CD1 PHE B 30 3033 3834 3645 -146 -187 737 C ATOM 2496 CD2 PHE B 30 -7.589 21.230 146.251 1.00 29.15 C ANISOU 2496 CD2 PHE B 30 3079 4294 3701 -274 -95 727 C ATOM 2497 CE1 PHE B 30 -6.196 20.014 144.191 1.00 27.22 C ANISOU 2497 CE1 PHE B 30 3034 3742 3569 -224 -268 800 C ATOM 2498 CE2 PHE B 30 -7.018 19.981 146.436 1.00 29.09 C ANISOU 2498 CE2 PHE B 30 3154 4241 3657 -371 -191 837 C ATOM 2499 CZ PHE B 30 -6.320 19.371 145.397 1.00 27.91 C ANISOU 2499 CZ PHE B 30 3101 3918 3584 -327 -284 864 C ATOM 2500 N HIS B 31 -7.437 25.312 147.171 1.00 30.86 N ANISOU 2500 N HIS B 31 3263 4455 4009 11 199 291 N ATOM 2501 CA HIS B 31 -7.180 25.451 148.601 1.00 32.27 C ANISOU 2501 CA HIS B 31 3403 4797 4060 -76 273 180 C ATOM 2502 C HIS B 31 -8.549 25.514 149.310 1.00 33.94 C ANISOU 2502 C HIS B 31 3452 5228 4216 -57 364 111 C ATOM 2503 O HIS B 31 -9.471 26.143 148.810 1.00 34.86 O ANISOU 2503 O HIS B 31 3488 5309 4448 96 397 51 O ATOM 2504 CB HIS B 31 -6.328 26.686 148.919 1.00 33.13 C ANISOU 2504 CB HIS B 31 3598 4787 4203 -51 338 2 C ATOM 2505 CG HIS B 31 -5.311 26.454 149.994 1.00 33.89 C ANISOU 2505 CG HIS B 31 3710 5012 4153 -194 327 -56 C ATOM 2506 ND1 HIS B 31 -5.633 26.417 151.334 1.00 35.85 N ANISOU 2506 ND1 HIS B 31 3894 5502 4225 -268 385 -151 N ATOM 2507 CD2 HIS B 31 -3.972 26.245 149.927 1.00 33.57 C ANISOU 2507 CD2 HIS B 31 3727 4927 4102 -273 254 -38 C ATOM 2508 CE1 HIS B 31 -4.543 26.178 152.045 1.00 35.96 C ANISOU 2508 CE1 HIS B 31 3943 5606 4113 -384 323 -169 C ATOM 2509 NE2 HIS B 31 -3.519 26.081 151.216 1.00 34.40 N ANISOU 2509 NE2 HIS B 31 3802 5238 4030 -378 238 -109 N ATOM 2510 N PRO B 32 -8.714 24.816 150.445 1.00 34.53 N ANISOU 2510 N PRO B 32 3467 5549 4105 -213 401 132 N ATOM 2511 CA PRO B 32 -7.814 23.891 151.127 1.00 33.86 C ANISOU 2511 CA PRO B 32 3469 5536 3861 -381 326 250 C ATOM 2512 C PRO B 32 -7.734 22.516 150.458 1.00 32.36 C ANISOU 2512 C PRO B 32 3333 5266 3698 -456 189 487 C ATOM 2513 O PRO B 32 -8.117 22.371 149.289 1.00 31.92 O ANISOU 2513 O PRO B 32 3268 5070 3789 -382 143 539 O ATOM 2514 CB PRO B 32 -8.409 23.795 152.537 1.00 35.87 C ANISOU 2514 CB PRO B 32 3638 6102 3887 -508 438 189 C ATOM 2515 CG PRO B 32 -9.853 24.070 152.363 1.00 37.22 C ANISOU 2515 CG PRO B 32 3628 6397 4117 -449 557 114 C ATOM 2516 CD PRO B 32 -9.935 25.070 151.235 1.00 36.99 C ANISOU 2516 CD PRO B 32 3598 6117 4337 -213 541 12 C ATOM 2517 N SER B 33 -7.250 21.533 151.207 1.00 31.42 N ANISOU 2517 N SER B 33 3285 5224 3428 -597 113 625 N ATOM 2518 CA SER B 33 -6.761 20.296 150.640 1.00 29.83 C ANISOU 2518 CA SER B 33 3191 4867 3278 -634 -45 819 C ATOM 2519 C SER B 33 -7.808 19.223 150.443 1.00 30.79 C ANISOU 2519 C SER B 33 3299 5008 3392 -766 -66 978 C ATOM 2520 O SER B 33 -7.578 18.304 149.677 1.00 29.34 O ANISOU 2520 O SER B 33 3207 4637 3306 -771 -189 1093 O ATOM 2521 CB SER B 33 -5.688 19.734 151.558 1.00 30.84 C ANISOU 2521 CB SER B 33 3422 5033 3265 -693 -155 907 C ATOM 2522 OG SER B 33 -6.195 19.606 152.885 1.00 31.63 O ANISOU 2522 OG SER B 33 3510 5385 3122 -848 -93 950 O ATOM 2523 N ASP B 34 -8.928 19.314 151.160 1.00 33.65 N ANISOU 2523 N ASP B 34 3542 5608 3634 -892 60 966 N ATOM 2524 CA ASP B 34 -9.942 18.251 151.148 1.00 37.06 C ANISOU 2524 CA ASP B 34 3946 6103 4034 -1094 56 1122 C ATOM 2525 C ASP B 34 -10.742 18.248 149.840 1.00 37.21 C ANISOU 2525 C ASP B 34 3858 6033 4248 -1031 36 1078 C ATOM 2526 O ASP B 34 -11.515 19.160 149.584 1.00 38.01 O ANISOU 2526 O ASP B 34 3772 6260 4409 -925 135 925 O ATOM 2527 CB ASP B 34 -10.919 18.401 152.321 1.00 40.53 C ANISOU 2527 CB ASP B 34 4245 6888 4265 -1274 231 1098 C ATOM 2528 CG ASP B 34 -10.226 18.487 153.665 1.00 43.96 C ANISOU 2528 CG ASP B 34 4784 7472 4448 -1352 255 1126 C ATOM 2529 OD1 ASP B 34 -10.939 18.436 154.697 1.00 47.21 O ANISOU 2529 OD1 ASP B 34 5118 8188 4631 -1543 401 1133 O ATOM 2530 OD2 ASP B 34 -8.978 18.613 153.712 1.00 43.95 O ANISOU 2530 OD2 ASP B 34 4924 7319 4454 -1234 133 1130 O ATOM 2531 N ILE B 35 -10.594 17.211 149.031 1.00 37.21 N ANISOU 2531 N ILE B 35 3975 5821 4343 -1088 -105 1203 N ATOM 2532 CA ILE B 35 -11.264 17.198 147.744 1.00 37.77 C ANISOU 2532 CA ILE B 35 3960 5822 4568 -1033 -151 1150 C ATOM 2533 C ILE B 35 -11.843 15.802 147.422 1.00 39.77 C ANISOU 2533 C ILE B 35 4270 5997 4843 -1271 -242 1288 C ATOM 2534 O ILE B 35 -11.238 14.795 147.775 1.00 41.10 O ANISOU 2534 O ILE B 35 4643 5995 4978 -1385 -329 1436 O ATOM 2535 CB ILE B 35 -10.275 17.747 146.669 1.00 35.61 C ANISOU 2535 CB ILE B 35 3787 5326 4417 -791 -229 1068 C ATOM 2536 CG1 ILE B 35 -10.962 18.062 145.334 1.00 34.98 C ANISOU 2536 CG1 ILE B 35 3619 5221 4451 -696 -272 999 C ATOM 2537 CG2 ILE B 35 -9.032 16.860 146.532 1.00 34.37 C ANISOU 2537 CG2 ILE B 35 3846 4933 4279 -787 -351 1155 C ATOM 2538 CD1 ILE B 35 -10.128 18.989 144.461 1.00 33.54 C ANISOU 2538 CD1 ILE B 35 3514 4893 4335 -471 -288 916 C ATOM 2539 N GLU B 36 -13.032 15.729 146.816 1.00 40.64 N ANISOU 2539 N GLU B 36 4199 6230 5012 -1355 -233 1240 N ATOM 2540 CA GLU B 36 -13.587 14.434 146.376 1.00 42.51 C ANISOU 2540 CA GLU B 36 4492 6370 5289 -1610 -330 1338 C ATOM 2541 C GLU B 36 -13.384 14.329 144.893 1.00 40.67 C ANISOU 2541 C GLU B 36 4318 5945 5191 -1472 -471 1255 C ATOM 2542 O GLU B 36 -13.776 15.230 144.183 1.00 40.58 O ANISOU 2542 O GLU B 36 4147 6048 5224 -1296 -467 1133 O ATOM 2543 CB GLU B 36 -15.087 14.351 146.628 1.00 46.07 C ANISOU 2543 CB GLU B 36 4663 7133 5707 -1841 -236 1315 C ATOM 2544 CG GLU B 36 -15.516 13.918 148.020 1.00 50.40 C ANISOU 2544 CG GLU B 36 5181 7881 6087 -2136 -94 1438 C ATOM 2545 CD GLU B 36 -17.034 13.739 148.119 1.00 55.03 C ANISOU 2545 CD GLU B 36 5448 8804 6656 -2403 10 1393 C ATOM 2546 OE1 GLU B 36 -17.499 12.951 148.984 1.00 58.42 O ANISOU 2546 OE1 GLU B 36 5893 9348 6955 -2771 101 1536 O ATOM 2547 OE2 GLU B 36 -17.766 14.377 147.317 1.00 55.57 O ANISOU 2547 OE2 GLU B 36 5244 9035 6836 -2254 -7 1222 O ATOM 2548 N VAL B 37 -12.752 13.265 144.406 1.00 39.81 N ANISOU 2548 N VAL B 37 4449 5539 5137 -1532 -601 1313 N ATOM 2549 CA VAL B 37 -12.616 13.067 142.951 1.00 38.38 C ANISOU 2549 CA VAL B 37 4329 5204 5050 -1433 -725 1204 C ATOM 2550 C VAL B 37 -12.986 11.633 142.529 1.00 40.39 C ANISOU 2550 C VAL B 37 4718 5266 5362 -1691 -845 1237 C ATOM 2551 O VAL B 37 -12.354 10.680 142.967 1.00 41.68 O ANISOU 2551 O VAL B 37 5116 5170 5551 -1773 -897 1339 O ATOM 2552 CB VAL B 37 -11.184 13.387 142.414 1.00 35.28 C ANISOU 2552 CB VAL B 37 4111 4605 4689 -1159 -761 1145 C ATOM 2553 CG1 VAL B 37 -11.106 13.150 140.916 1.00 35.05 C ANISOU 2553 CG1 VAL B 37 4145 4464 4708 -1090 -864 1023 C ATOM 2554 CG2 VAL B 37 -10.756 14.809 142.712 1.00 33.38 C ANISOU 2554 CG2 VAL B 37 3770 4505 4408 -938 -652 1099 C ATOM 2555 N ASP B 38 -14.007 11.473 141.693 1.00 41.12 N ANISOU 2555 N ASP B 38 4669 5473 5481 -1817 -905 1147 N ATOM 2556 CA ASP B 38 -14.285 10.164 141.129 1.00 43.03 C ANISOU 2556 CA ASP B 38 5060 5501 5788 -2061 -1031 1129 C ATOM 2557 C ASP B 38 -14.116 10.222 139.634 1.00 41.67 C ANISOU 2557 C ASP B 38 4927 5264 5640 -1916 -1150 948 C ATOM 2558 O ASP B 38 -14.151 11.300 139.024 1.00 39.66 O ANISOU 2558 O ASP B 38 4531 5201 5337 -1689 -1138 870 O ATOM 2559 CB ASP B 38 -15.705 9.681 141.437 1.00 47.73 C ANISOU 2559 CB ASP B 38 5459 6300 6376 -2437 -1016 1161 C ATOM 2560 CG ASP B 38 -16.240 10.213 142.751 1.00 49.81 C ANISOU 2560 CG ASP B 38 5517 6856 6553 -2535 -842 1278 C ATOM 2561 OD1 ASP B 38 -16.279 11.461 142.931 1.00 49.16 O ANISOU 2561 OD1 ASP B 38 5228 7025 6426 -2282 -749 1222 O ATOM 2562 OD2 ASP B 38 -16.639 9.383 143.599 1.00 52.28 O ANISOU 2562 OD2 ASP B 38 5887 7143 6835 -2876 -793 1421 O ATOM 2563 N LEU B 39 -13.943 9.048 139.045 1.00 42.12 N ANISOU 2563 N LEU B 39 5202 5040 5763 -2057 -1268 883 N ATOM 2564 CA LEU B 39 -13.870 8.927 137.610 1.00 41.76 C ANISOU 2564 CA LEU B 39 5210 4951 5707 -1978 -1382 685 C ATOM 2565 C LEU B 39 -15.080 8.126 137.211 1.00 45.08 C ANISOU 2565 C LEU B 39 5551 5427 6149 -2330 -1488 615 C ATOM 2566 O LEU B 39 -15.360 7.095 137.829 1.00 48.56 O ANISOU 2566 O LEU B 39 6107 5675 6668 -2628 -1501 694 O ATOM 2567 CB LEU B 39 -12.602 8.191 137.210 1.00 41.17 C ANISOU 2567 CB LEU B 39 5450 4498 5694 -1837 -1427 601 C ATOM 2568 CG LEU B 39 -11.370 9.074 137.300 1.00 38.17 C ANISOU 2568 CG LEU B 39 5097 4125 5280 -1486 -1333 612 C ATOM 2569 CD1 LEU B 39 -10.270 8.487 136.477 1.00 38.76 C ANISOU 2569 CD1 LEU B 39 5393 3938 5394 -1322 -1377 441 C ATOM 2570 CD2 LEU B 39 -11.720 10.435 136.771 1.00 36.42 C ANISOU 2570 CD2 LEU B 39 4661 4236 4942 -1338 -1284 584 C ATOM 2571 N LEU B 40 -15.820 8.598 136.210 1.00 44.62 N ANISOU 2571 N LEU B 40 5299 5638 6016 -2318 -1574 481 N ATOM 2572 CA LEU B 40 -17.080 7.948 135.863 1.00 46.55 C ANISOU 2572 CA LEU B 40 5393 6021 6275 -2674 -1686 398 C ATOM 2573 C LEU B 40 -17.048 7.269 134.505 1.00 47.62 C ANISOU 2573 C LEU B 40 5682 6032 6378 -2740 -1858 168 C ATOM 2574 O LEU B 40 -16.605 7.853 133.512 1.00 45.38 O ANISOU 2574 O LEU B 40 5433 5826 5982 -2478 -1909 57 O ATOM 2575 CB LEU B 40 -18.246 8.934 135.939 1.00 47.11 C ANISOU 2575 CB LEU B 40 5038 6575 6288 -2665 -1679 417 C ATOM 2576 CG LEU B 40 -18.350 9.829 137.180 1.00 45.83 C ANISOU 2576 CG LEU B 40 4679 6604 6131 -2547 -1496 585 C ATOM 2577 CD1 LEU B 40 -19.482 10.842 137.031 1.00 46.72 C ANISOU 2577 CD1 LEU B 40 4362 7180 6207 -2458 -1515 544 C ATOM 2578 CD2 LEU B 40 -18.541 9.001 138.438 1.00 47.39 C ANISOU 2578 CD2 LEU B 40 4925 6695 6386 -2879 -1379 725 C ATOM 2579 N LYS B 41 -17.499 6.018 134.480 1.00 50.32 N ANISOU 2579 N LYS B 41 6142 6171 6808 -3113 -1939 94 N ATOM 2580 CA LYS B 41 -17.721 5.317 133.228 1.00 52.93 C ANISOU 2580 CA LYS B 41 6582 6428 7102 -3253 -2114 -166 C ATOM 2581 C LYS B 41 -19.218 5.230 133.033 1.00 56.92 C ANISOU 2581 C LYS B 41 6754 7288 7583 -3602 -2222 -226 C ATOM 2582 O LYS B 41 -19.910 4.551 133.808 1.00 59.25 O ANISOU 2582 O LYS B 41 6985 7542 7987 -3988 -2189 -145 O ATOM 2583 CB LYS B 41 -17.112 3.914 133.245 1.00 54.08 C ANISOU 2583 CB LYS B 41 7128 6033 7388 -3424 -2150 -257 C ATOM 2584 CG LYS B 41 -17.380 3.128 131.964 1.00 56.10 C ANISOU 2584 CG LYS B 41 7513 6198 7606 -3600 -2327 -577 C ATOM 2585 CD LYS B 41 -16.854 1.710 132.040 1.00 58.10 C ANISOU 2585 CD LYS B 41 8175 5863 8036 -3770 -2367 -685 C ATOM 2586 CE LYS B 41 -16.848 1.053 130.666 1.00 60.43 C ANISOU 2586 CE LYS B 41 8639 6051 8270 -3844 -2521 -1067 C ATOM 2587 NZ LYS B 41 -16.583 -0.406 130.768 1.00 63.75 N ANISOU 2587 NZ LYS B 41 9449 5871 8901 -4075 -2582 -1197 N ATOM 2588 N ASN B 42 -19.700 5.953 132.017 1.00 58.10 N ANISOU 2588 N ASN B 42 6686 7810 7579 -3466 -2352 -352 N ATOM 2589 CA ASN B 42 -21.136 6.129 131.701 1.00 62.24 C ANISOU 2589 CA ASN B 42 6804 8788 8058 -3702 -2491 -424 C ATOM 2590 C ASN B 42 -22.003 6.609 132.868 1.00 63.25 C ANISOU 2590 C ASN B 42 6548 9217 8268 -3811 -2365 -240 C ATOM 2591 O ASN B 42 -23.180 6.260 132.958 1.00 67.10 O ANISOU 2591 O ASN B 42 6727 9977 8792 -4168 -2431 -302 O ATOM 2592 CB ASN B 42 -21.749 4.880 131.038 1.00 66.14 C ANISOU 2592 CB ASN B 42 7370 9184 8575 -4155 -2665 -662 C ATOM 2593 CG ASN B 42 -21.120 4.560 129.693 1.00 66.57 C ANISOU 2593 CG ASN B 42 7718 9082 8493 -4034 -2814 -914 C ATOM 2594 OD1 ASN B 42 -20.556 5.429 129.030 1.00 64.36 O ANISOU 2594 OD1 ASN B 42 7473 8935 8046 -3643 -2830 -917 O ATOM 2595 ND2 ASN B 42 -21.212 3.305 129.287 1.00 69.91 N ANISOU 2595 ND2 ASN B 42 8370 9216 8978 -4387 -2912 -1134 N ATOM 2596 N GLY B 43 -21.410 7.398 133.758 1.00 60.59 N ANISOU 2596 N GLY B 43 6220 8850 7953 -3519 -2174 -40 N ATOM 2597 CA GLY B 43 -22.115 7.916 134.917 1.00 62.56 C ANISOU 2597 CA GLY B 43 6129 9387 8256 -3582 -2019 109 C ATOM 2598 C GLY B 43 -21.897 7.133 136.200 1.00 64.41 C ANISOU 2598 C GLY B 43 6526 9361 8585 -3876 -1834 271 C ATOM 2599 O GLY B 43 -22.182 7.636 137.285 1.00 64.39 O ANISOU 2599 O GLY B 43 6318 9558 8588 -3873 -1656 413 O ATOM 2600 N GLU B 44 -21.403 5.902 136.095 1.00 66.78 N ANISOU 2600 N GLU B 44 7209 9213 8950 -4127 -1879 250 N ATOM 2601 CA GLU B 44 -21.177 5.094 137.292 1.00 68.92 C ANISOU 2601 CA GLU B 44 7694 9191 9302 -4412 -1737 445 C ATOM 2602 C GLU B 44 -19.706 5.145 137.663 1.00 66.10 C ANISOU 2602 C GLU B 44 7728 8427 8958 -4069 -1671 567 C ATOM 2603 O GLU B 44 -18.857 5.208 136.775 1.00 64.98 O ANISOU 2603 O GLU B 44 7797 8084 8809 -3774 -1765 437 O ATOM 2604 CB GLU B 44 -21.633 3.653 137.082 1.00 73.62 C ANISOU 2604 CB GLU B 44 8477 9505 9991 -4936 -1836 375 C ATOM 2605 CG GLU B 44 -22.017 2.956 138.372 1.00 77.17 C ANISOU 2605 CG GLU B 44 8979 9853 10488 -5376 -1686 606 C ATOM 2606 CD GLU B 44 -22.030 1.443 138.244 1.00 82.02 C ANISOU 2606 CD GLU B 44 9975 9963 11226 -5832 -1784 590 C ATOM 2607 OE1 GLU B 44 -21.833 0.757 139.274 1.00 83.87 O ANISOU 2607 OE1 GLU B 44 10471 9893 11502 -6088 -1686 838 O ATOM 2608 OE2 GLU B 44 -22.235 0.937 137.116 1.00 84.10 O ANISOU 2608 OE2 GLU B 44 10300 10120 11535 -5939 -1968 330 O ATOM 2609 N ARG B 45 -19.416 5.118 138.966 1.00 65.98 N ANISOU 2609 N ARG B 45 7790 8332 8947 -4117 -1511 805 N ATOM 2610 CA ARG B 45 -18.060 5.315 139.500 1.00 63.17 C ANISOU 2610 CA ARG B 45 7729 7683 8592 -3776 -1450 938 C ATOM 2611 C ARG B 45 -17.112 4.141 139.253 1.00 63.52 C ANISOU 2611 C ARG B 45 8245 7142 8749 -3787 -1561 930 C ATOM 2612 O ARG B 45 -17.447 3.006 139.566 1.00 67.12 O ANISOU 2612 O ARG B 45 8898 7319 9284 -4170 -1604 1004 O ATOM 2613 CB ARG B 45 -18.140 5.592 141.006 1.00 63.90 C ANISOU 2613 CB ARG B 45 7751 7909 8618 -3865 -1266 1191 C ATOM 2614 CG ARG B 45 -16.805 5.957 141.645 1.00 62.53 C ANISOU 2614 CG ARG B 45 7809 7530 8418 -3506 -1213 1323 C ATOM 2615 CD ARG B 45 -16.940 6.183 143.143 1.00 64.27 C ANISOU 2615 CD ARG B 45 7973 7916 8529 -3634 -1044 1561 C ATOM 2616 NE ARG B 45 -16.885 4.956 143.933 1.00 68.41 N ANISOU 2616 NE ARG B 45 8809 8117 9067 -3987 -1062 1787 N ATOM 2617 CZ ARG B 45 -15.775 4.482 144.489 1.00 68.51 C ANISOU 2617 CZ ARG B 45 9186 7753 9094 -3845 -1120 1957 C ATOM 2618 NH1 ARG B 45 -14.629 5.139 144.326 1.00 65.02 N ANISOU 2618 NH1 ARG B 45 8797 7249 8658 -3377 -1149 1895 N ATOM 2619 NH2 ARG B 45 -15.811 3.356 145.204 1.00 72.16 N ANISOU 2619 NH2 ARG B 45 9954 7900 9562 -4177 -1157 2197 N ATOM 2620 N ILE B 46 -15.934 4.414 138.696 1.00 60.39 N ANISOU 2620 N ILE B 46 8026 6553 8365 -3371 -1604 834 N ATOM 2621 CA ILE B 46 -14.890 3.390 138.570 1.00 61.53 C ANISOU 2621 CA ILE B 46 8592 6152 8634 -3285 -1696 812 C ATOM 2622 C ILE B 46 -14.232 3.150 139.934 1.00 62.34 C ANISOU 2622 C ILE B 46 8883 6040 8761 -3249 -1634 1103 C ATOM 2623 O ILE B 46 -13.877 4.095 140.638 1.00 59.87 O ANISOU 2623 O ILE B 46 8422 5974 8351 -3035 -1520 1230 O ATOM 2624 CB ILE B 46 -13.841 3.769 137.498 1.00 58.38 C ANISOU 2624 CB ILE B 46 8273 5680 8229 -2857 -1740 583 C ATOM 2625 CG1 ILE B 46 -14.542 4.198 136.213 1.00 58.43 C ANISOU 2625 CG1 ILE B 46 8073 5988 8140 -2885 -1801 339 C ATOM 2626 CG2 ILE B 46 -12.910 2.605 137.190 1.00 59.97 C ANISOU 2626 CG2 ILE B 46 8867 5335 8583 -2772 -1846 478 C ATOM 2627 CD1 ILE B 46 -13.606 4.494 135.072 1.00 56.70 C ANISOU 2627 CD1 ILE B 46 7951 5725 7868 -2537 -1831 109 C ATOM 2628 N GLU B 47 -14.087 1.884 140.311 1.00 66.65 N ANISOU 2628 N GLU B 47 9775 6120 9430 -3467 -1723 1212 N ATOM 2629 CA GLU B 47 -13.657 1.538 141.660 1.00 68.71 C ANISOU 2629 CA GLU B 47 10237 6187 9683 -3509 -1696 1539 C ATOM 2630 C GLU B 47 -12.154 1.391 141.896 1.00 68.33 C ANISOU 2630 C GLU B 47 10446 5805 9711 -3072 -1773 1585 C ATOM 2631 O GLU B 47 -11.722 1.295 143.043 1.00 69.42 O ANISOU 2631 O GLU B 47 10713 5860 9803 -3046 -1768 1865 O ATOM 2632 CB GLU B 47 -14.397 0.292 142.146 1.00 73.42 C ANISOU 2632 CB GLU B 47 11079 6469 10349 -4026 -1750 1715 C ATOM 2633 CG GLU B 47 -15.488 0.624 143.138 1.00 74.84 C ANISOU 2633 CG GLU B 47 11017 7053 10364 -4430 -1588 1941 C ATOM 2634 CD GLU B 47 -16.677 -0.307 143.044 1.00 79.85 C ANISOU 2634 CD GLU B 47 11691 7600 11051 -5036 -1602 1959 C ATOM 2635 OE1 GLU B 47 -16.753 -1.262 143.848 1.00 83.70 O ANISOU 2635 OE1 GLU B 47 12501 7741 11560 -5373 -1624 2234 O ATOM 2636 OE2 GLU B 47 -17.538 -0.086 142.164 1.00 80.11 O ANISOU 2636 OE2 GLU B 47 11434 7912 11094 -5190 -1602 1707 O ATOM 2637 N LYS B 48 -11.352 1.377 140.836 1.00 67.79 N ANISOU 2637 N LYS B 48 10436 5580 9741 -2732 -1846 1307 N ATOM 2638 CA LYS B 48 -9.898 1.244 141.015 1.00 67.53 C ANISOU 2638 CA LYS B 48 10587 5275 9796 -2297 -1915 1311 C ATOM 2639 C LYS B 48 -9.145 2.489 140.553 1.00 63.17 C ANISOU 2639 C LYS B 48 9767 5081 9155 -1898 -1815 1143 C ATOM 2640 O LYS B 48 -8.324 2.438 139.636 1.00 63.57 O ANISOU 2640 O LYS B 48 9856 5018 9281 -1602 -1848 887 O ATOM 2641 CB LYS B 48 -9.327 -0.037 140.364 1.00 71.16 C ANISOU 2641 CB LYS B 48 11405 5149 10482 -2202 -2084 1143 C ATOM 2642 CG LYS B 48 -10.108 -0.577 139.163 1.00 73.44 C ANISOU 2642 CG LYS B 48 11732 5341 10831 -2447 -2126 851 C ATOM 2643 CD LYS B 48 -10.966 -1.792 139.542 1.00 78.08 C ANISOU 2643 CD LYS B 48 12604 5536 11529 -2926 -2224 996 C ATOM 2644 CE LYS B 48 -12.207 -1.866 138.671 1.00 79.11 C ANISOU 2644 CE LYS B 48 12584 5862 11613 -3325 -2210 785 C ATOM 2645 NZ LYS B 48 -12.963 -0.578 138.694 1.00 75.21 N ANISOU 2645 NZ LYS B 48 11629 6047 10900 -3395 -2062 814 N ATOM 2646 N VAL B 49 -9.431 3.608 141.209 1.00 59.54 N ANISOU 2646 N VAL B 49 9041 5052 8529 -1909 -1682 1280 N ATOM 2647 CA VAL B 49 -8.777 4.859 140.906 1.00 54.17 C ANISOU 2647 CA VAL B 49 8127 4692 7762 -1585 -1579 1161 C ATOM 2648 C VAL B 49 -7.638 5.094 141.889 1.00 52.88 C ANISOU 2648 C VAL B 49 8009 4490 7593 -1327 -1586 1311 C ATOM 2649 O VAL B 49 -7.861 5.261 143.085 1.00 53.04 O ANISOU 2649 O VAL B 49 8016 4619 7519 -1450 -1557 1559 O ATOM 2650 CB VAL B 49 -9.761 6.028 141.011 1.00 51.86 C ANISOU 2650 CB VAL B 49 7518 4876 7311 -1719 -1439 1188 C ATOM 2651 CG1 VAL B 49 -9.083 7.328 140.606 1.00 48.88 C ANISOU 2651 CG1 VAL B 49 6949 4765 6859 -1400 -1343 1066 C ATOM 2652 CG2 VAL B 49 -10.970 5.775 140.150 1.00 52.99 C ANISOU 2652 CG2 VAL B 49 7578 5105 7451 -1989 -1464 1062 C ATOM 2653 N GLU B 50 -6.414 5.097 141.374 1.00 51.73 N ANISOU 2653 N GLU B 50 7900 4222 7535 -977 -1624 1143 N ATOM 2654 CA GLU B 50 -5.251 5.500 142.147 1.00 49.91 C ANISOU 2654 CA GLU B 50 7632 4039 7294 -700 -1633 1226 C ATOM 2655 C GLU B 50 -5.038 6.989 141.946 1.00 45.35 C ANISOU 2655 C GLU B 50 6763 3881 6585 -581 -1469 1127 C ATOM 2656 O GLU B 50 -5.491 7.556 140.953 1.00 43.35 O ANISOU 2656 O GLU B 50 6388 3797 6287 -614 -1378 958 O ATOM 2657 CB GLU B 50 -4.011 4.719 141.708 1.00 52.08 C ANISOU 2657 CB GLU B 50 8052 3986 7750 -376 -1757 1073 C ATOM 2658 CG GLU B 50 -3.865 3.372 142.393 1.00 56.86 C ANISOU 2658 CG GLU B 50 8975 4133 8497 -394 -1957 1260 C ATOM 2659 CD GLU B 50 -3.316 2.301 141.465 1.00 60.62 C ANISOU 2659 CD GLU B 50 9649 4187 9198 -196 -2075 1017 C ATOM 2660 OE1 GLU B 50 -2.669 1.341 141.950 1.00 63.90 O ANISOU 2660 OE1 GLU B 50 10297 4206 9776 -19 -2260 1113 O ATOM 2661 OE2 GLU B 50 -3.535 2.418 140.239 1.00 60.82 O ANISOU 2661 OE2 GLU B 50 9604 4274 9230 -206 -1990 721 O ATOM 2662 N HIS B 51 -4.360 7.615 142.905 1.00 43.53 N ANISOU 2662 N HIS B 51 6444 3808 6287 -456 -1445 1241 N ATOM 2663 CA HIS B 51 -4.069 9.044 142.858 1.00 39.67 C ANISOU 2663 CA HIS B 51 5713 3669 5691 -358 -1295 1156 C ATOM 2664 C HIS B 51 -2.659 9.360 143.340 1.00 38.89 C ANISOU 2664 C HIS B 51 5551 3613 5613 -96 -1324 1128 C ATOM 2665 O HIS B 51 -2.027 8.556 144.017 1.00 41.31 O ANISOU 2665 O HIS B 51 5981 3730 5985 7 -1475 1236 O ATOM 2666 CB HIS B 51 -5.091 9.861 143.658 1.00 38.76 C ANISOU 2666 CB HIS B 51 5474 3832 5420 -574 -1188 1300 C ATOM 2667 CG HIS B 51 -5.056 9.598 145.129 1.00 40.49 C ANISOU 2667 CG HIS B 51 5764 4067 5554 -664 -1239 1537 C ATOM 2668 ND1 HIS B 51 -4.345 10.383 146.009 1.00 39.52 N ANISOU 2668 ND1 HIS B 51 5543 4140 5331 -552 -1207 1572 N ATOM 2669 CD2 HIS B 51 -5.626 8.618 145.871 1.00 43.45 C ANISOU 2669 CD2 HIS B 51 6315 4290 5903 -878 -1324 1757 C ATOM 2670 CE1 HIS B 51 -4.491 9.907 147.231 1.00 42.08 C ANISOU 2670 CE1 HIS B 51 5979 4459 5550 -679 -1276 1802 C ATOM 2671 NE2 HIS B 51 -5.263 8.834 147.174 1.00 44.16 N ANISOU 2671 NE2 HIS B 51 6419 4507 5854 -882 -1342 1935 N ATOM 2672 N SER B 52 -2.168 10.543 143.001 1.00 36.06 N ANISOU 2672 N SER B 52 4999 3502 5200 4 -1191 990 N ATOM 2673 CA SER B 52 -0.789 10.887 143.304 1.00 35.64 C ANISOU 2673 CA SER B 52 4840 3526 5177 227 -1207 915 C ATOM 2674 C SER B 52 -0.657 11.420 144.735 1.00 35.07 C ANISOU 2674 C SER B 52 4710 3628 4987 177 -1228 1082 C ATOM 2675 O SER B 52 -1.659 11.699 145.389 1.00 35.45 O ANISOU 2675 O SER B 52 4781 3774 4916 -26 -1182 1226 O ATOM 2676 CB SER B 52 -0.272 11.914 142.297 1.00 33.54 C ANISOU 2676 CB SER B 52 4408 3441 4894 304 -1043 695 C ATOM 2677 OG SER B 52 -0.887 13.175 142.504 1.00 31.58 O ANISOU 2677 OG SER B 52 4063 3416 4522 166 -907 735 O ATOM 2678 N ASP B 53 0.577 11.540 145.213 1.00 34.39 N ANISOU 2678 N ASP B 53 4533 3609 4926 362 -1299 1040 N ATOM 2679 CA ASP B 53 0.861 12.138 146.506 1.00 33.71 C ANISOU 2679 CA ASP B 53 4374 3732 4703 324 -1327 1150 C ATOM 2680 C ASP B 53 0.642 13.648 146.453 1.00 30.55 C ANISOU 2680 C ASP B 53 3809 3599 4200 215 -1123 1038 C ATOM 2681 O ASP B 53 1.060 14.290 145.493 1.00 30.19 O ANISOU 2681 O ASP B 53 3653 3602 4215 273 -1003 850 O ATOM 2682 CB ASP B 53 2.298 11.818 146.912 1.00 36.03 C ANISOU 2682 CB ASP B 53 4583 4039 5066 567 -1488 1106 C ATOM 2683 CG ASP B 53 2.548 10.328 147.040 1.00 40.14 C ANISOU 2683 CG ASP B 53 5292 4247 5712 724 -1722 1230 C ATOM 2684 OD1 ASP B 53 3.687 9.874 146.787 1.00 42.51 O ANISOU 2684 OD1 ASP B 53 5510 4482 6161 1001 -1842 1110 O ATOM 2685 OD2 ASP B 53 1.598 9.595 147.388 1.00 41.62 O ANISOU 2685 OD2 ASP B 53 5711 4244 5860 568 -1785 1443 O ATOM 2686 N LEU B 54 -0.027 14.201 147.464 1.00 29.40 N ANISOU 2686 N LEU B 54 3665 3613 3892 54 -1078 1148 N ATOM 2687 CA LEU B 54 -0.345 15.632 147.506 1.00 27.70 C ANISOU 2687 CA LEU B 54 3326 3604 3597 -37 -893 1035 C ATOM 2688 C LEU B 54 0.879 16.525 147.452 1.00 28.65 C ANISOU 2688 C LEU B 54 3292 3852 3741 54 -854 859 C ATOM 2689 O LEU B 54 1.877 16.268 148.134 1.00 30.22 O ANISOU 2689 O LEU B 54 3436 4123 3924 139 -984 860 O ATOM 2690 CB LEU B 54 -1.117 15.964 148.773 1.00 27.02 C ANISOU 2690 CB LEU B 54 3258 3684 3324 -197 -862 1149 C ATOM 2691 CG LEU B 54 -1.634 17.393 148.916 1.00 24.79 C ANISOU 2691 CG LEU B 54 2869 3578 2972 -275 -674 1018 C ATOM 2692 CD1 LEU B 54 -2.687 17.690 147.818 1.00 22.58 C ANISOU 2692 CD1 LEU B 54 2582 3218 2779 -299 -556 977 C ATOM 2693 CD2 LEU B 54 -2.182 17.613 150.326 1.00 25.18 C ANISOU 2693 CD2 LEU B 54 2925 3831 2813 -411 -649 1092 C ATOM 2694 N SER B 55 0.817 17.551 146.612 1.00 28.22 N ANISOU 2694 N SER B 55 3170 3827 3727 28 -687 715 N ATOM 2695 CA SER B 55 1.874 18.544 146.574 1.00 29.73 C ANISOU 2695 CA SER B 55 3223 4140 3931 40 -614 549 C ATOM 2696 C SER B 55 1.226 19.864 146.221 1.00 29.59 C ANISOU 2696 C SER B 55 3214 4139 3889 -66 -431 480 C ATOM 2697 O SER B 55 0.001 19.946 146.044 1.00 28.66 O ANISOU 2697 O SER B 55 3176 3967 3748 -108 -383 555 O ATOM 2698 CB SER B 55 2.953 18.163 145.540 1.00 30.85 C ANISOU 2698 CB SER B 55 3284 4237 4200 163 -619 428 C ATOM 2699 OG SER B 55 4.182 18.855 145.754 1.00 31.36 O ANISOU 2699 OG SER B 55 3172 4464 4278 160 -589 276 O ATOM 2700 N PHE B 56 2.041 20.907 146.118 1.00 30.82 N ANISOU 2700 N PHE B 56 3284 4365 4062 -109 -338 335 N ATOM 2701 CA PHE B 56 1.501 22.238 145.887 1.00 30.90 C ANISOU 2701 CA PHE B 56 3338 4340 4064 -200 -182 276 C ATOM 2702 C PHE B 56 2.411 23.085 145.019 1.00 31.56 C ANISOU 2702 C PHE B 56 3383 4398 4211 -257 -63 154 C ATOM 2703 O PHE B 56 3.592 22.776 144.895 1.00 32.84 O ANISOU 2703 O PHE B 56 3422 4648 4407 -249 -89 70 O ATOM 2704 CB PHE B 56 1.155 22.955 147.215 1.00 30.83 C ANISOU 2704 CB PHE B 56 3321 4435 3960 -276 -168 233 C ATOM 2705 CG PHE B 56 2.275 22.987 148.218 1.00 31.49 C ANISOU 2705 CG PHE B 56 3295 4686 3982 -318 -249 141 C ATOM 2706 CD1 PHE B 56 3.234 23.991 148.185 1.00 32.33 C ANISOU 2706 CD1 PHE B 56 3323 4836 4125 -414 -177 -33 C ATOM 2707 CD2 PHE B 56 2.340 22.040 149.231 1.00 32.17 C ANISOU 2707 CD2 PHE B 56 3364 4896 3962 -284 -411 238 C ATOM 2708 CE1 PHE B 56 4.261 24.022 149.115 1.00 34.16 C ANISOU 2708 CE1 PHE B 56 3423 5263 4295 -464 -275 -136 C ATOM 2709 CE2 PHE B 56 3.359 22.071 150.166 1.00 33.87 C ANISOU 2709 CE2 PHE B 56 3474 5297 4100 -308 -523 164 C ATOM 2710 CZ PHE B 56 4.319 23.066 150.113 1.00 34.81 C ANISOU 2710 CZ PHE B 56 3476 5489 4260 -395 -460 -39 C ATOM 2711 N SER B 57 1.858 24.157 144.448 1.00 31.44 N ANISOU 2711 N SER B 57 3469 4267 4211 -315 64 147 N ATOM 2712 CA SER B 57 2.621 25.063 143.599 1.00 32.62 C ANISOU 2712 CA SER B 57 3633 4363 4398 -419 196 70 C ATOM 2713 C SER B 57 3.207 26.247 144.358 1.00 34.35 C ANISOU 2713 C SER B 57 3826 4600 4628 -567 266 -65 C ATOM 2714 O SER B 57 3.019 26.364 145.571 1.00 34.68 O ANISOU 2714 O SER B 57 3831 4717 4630 -571 207 -119 O ATOM 2715 CB SER B 57 1.727 25.553 142.481 1.00 32.55 C ANISOU 2715 CB SER B 57 3793 4185 4391 -401 267 172 C ATOM 2716 OG SER B 57 1.366 24.447 141.684 1.00 32.66 O ANISOU 2716 OG SER B 57 3819 4208 4384 -301 202 255 O ATOM 2717 N LYS B 58 3.880 27.144 143.634 1.00 35.51 N ANISOU 2717 N LYS B 58 4008 4674 4810 -715 400 -123 N ATOM 2718 CA LYS B 58 4.561 28.319 144.212 1.00 37.92 C ANISOU 2718 CA LYS B 58 4302 4963 5144 -912 480 -273 C ATOM 2719 C LYS B 58 3.651 29.298 144.962 1.00 37.85 C ANISOU 2719 C LYS B 58 4443 4790 5148 -911 495 -307 C ATOM 2720 O LYS B 58 4.092 30.047 145.840 1.00 38.93 O ANISOU 2720 O LYS B 58 4556 4945 5292 -1044 515 -473 O ATOM 2721 CB LYS B 58 5.302 29.077 143.111 1.00 40.81 C ANISOU 2721 CB LYS B 58 4725 5241 5541 -1105 641 -284 C ATOM 2722 CG LYS B 58 6.538 29.855 143.591 1.00 45.21 C ANISOU 2722 CG LYS B 58 5160 5886 6132 -1368 716 -476 C ATOM 2723 CD LYS B 58 7.230 30.610 142.450 1.00 48.41 C ANISOU 2723 CD LYS B 58 5638 6205 6552 -1615 906 -462 C ATOM 2724 CE LYS B 58 7.288 29.761 141.160 1.00 48.49 C ANISOU 2724 CE LYS B 58 5627 6297 6499 -1525 954 -341 C ATOM 2725 NZ LYS B 58 8.126 28.518 141.266 1.00 48.39 N ANISOU 2725 NZ LYS B 58 5300 6604 6481 -1417 886 -451 N ATOM 2726 N ASP B 59 2.369 29.268 144.616 1.00 36.76 N ANISOU 2726 N ASP B 59 4443 4510 5014 -751 480 -175 N ATOM 2727 CA ASP B 59 1.380 30.150 145.198 1.00 36.86 C ANISOU 2727 CA ASP B 59 4578 4369 5059 -690 502 -219 C ATOM 2728 C ASP B 59 0.586 29.419 146.275 1.00 35.63 C ANISOU 2728 C ASP B 59 4319 4392 4826 -560 413 -232 C ATOM 2729 O ASP B 59 -0.503 29.862 146.662 1.00 35.80 O ANISOU 2729 O ASP B 59 4398 4344 4862 -452 431 -255 O ATOM 2730 CB ASP B 59 0.461 30.690 144.098 1.00 37.51 C ANISOU 2730 CB ASP B 59 4852 4198 5201 -584 536 -70 C ATOM 2731 CG ASP B 59 -0.434 29.610 143.467 1.00 36.24 C ANISOU 2731 CG ASP B 59 4654 4121 4995 -408 446 101 C ATOM 2732 OD1 ASP B 59 -0.201 28.381 143.639 1.00 34.41 O ANISOU 2732 OD1 ASP B 59 4280 4093 4701 -390 375 126 O ATOM 2733 OD2 ASP B 59 -1.402 30.011 142.784 1.00 36.88 O ANISOU 2733 OD2 ASP B 59 4856 4045 5110 -284 432 211 O ATOM 2734 N TRP B 60 1.136 28.269 146.692 1.00 34.02 N ANISOU 2734 N TRP B 60 3966 4419 4543 -566 317 -208 N ATOM 2735 CA TRP B 60 0.614 27.375 147.746 1.00 32.40 C ANISOU 2735 CA TRP B 60 3675 4410 4225 -497 220 -179 C ATOM 2736 C TRP B 60 -0.625 26.555 147.379 1.00 31.73 C ANISOU 2736 C TRP B 60 3611 4315 4129 -363 180 -10 C ATOM 2737 O TRP B 60 -1.162 25.827 148.217 1.00 32.56 O ANISOU 2737 O TRP B 60 3665 4571 4134 -344 121 38 O ATOM 2738 CB TRP B 60 0.392 28.112 149.065 1.00 32.01 C ANISOU 2738 CB TRP B 60 3622 4444 4098 -552 253 -350 C ATOM 2739 CG TRP B 60 1.541 28.936 149.500 1.00 33.00 C ANISOU 2739 CG TRP B 60 3723 4588 4227 -716 279 -546 C ATOM 2740 CD1 TRP B 60 1.660 30.293 149.426 1.00 33.69 C ANISOU 2740 CD1 TRP B 60 3916 4480 4404 -809 391 -709 C ATOM 2741 CD2 TRP B 60 2.753 28.457 150.082 1.00 33.62 C ANISOU 2741 CD2 TRP B 60 3658 4889 4228 -815 175 -607 C ATOM 2742 NE1 TRP B 60 2.871 30.690 149.937 1.00 35.00 N ANISOU 2742 NE1 TRP B 60 4006 4746 4545 -1002 377 -883 N ATOM 2743 CE2 TRP B 60 3.559 29.580 150.352 1.00 35.08 C ANISOU 2743 CE2 TRP B 60 3841 5040 4449 -998 238 -827 C ATOM 2744 CE3 TRP B 60 3.231 27.184 150.416 1.00 33.09 C ANISOU 2744 CE3 TRP B 60 3465 5035 4072 -759 17 -497 C ATOM 2745 CZ2 TRP B 60 4.812 29.467 150.947 1.00 36.65 C ANISOU 2745 CZ2 TRP B 60 3875 5464 4587 -1133 145 -954 C ATOM 2746 CZ3 TRP B 60 4.468 27.073 150.999 1.00 34.36 C ANISOU 2746 CZ3 TRP B 60 3476 5399 4180 -848 -88 -605 C ATOM 2747 CH2 TRP B 60 5.248 28.207 151.260 1.00 36.44 C ANISOU 2747 CH2 TRP B 60 3698 5676 4469 -1038 -25 -839 C ATOM 2748 N SER B 61 -1.081 26.649 146.142 1.00 31.49 N ANISOU 2748 N SER B 61 3657 4125 4181 -297 208 85 N ATOM 2749 CA SER B 61 -2.296 25.941 145.764 1.00 31.45 C ANISOU 2749 CA SER B 61 3652 4129 4169 -193 160 219 C ATOM 2750 C SER B 61 -1.987 24.485 145.423 1.00 30.50 C ANISOU 2750 C SER B 61 3491 4077 4019 -191 54 331 C ATOM 2751 O SER B 61 -0.934 24.187 144.854 1.00 30.69 O ANISOU 2751 O SER B 61 3512 4081 4069 -213 39 319 O ATOM 2752 CB SER B 61 -3.010 26.645 144.611 1.00 31.54 C ANISOU 2752 CB SER B 61 3761 3962 4261 -108 197 274 C ATOM 2753 OG SER B 61 -2.123 26.897 143.543 1.00 31.69 O ANISOU 2753 OG SER B 61 3866 3866 4308 -160 226 302 O ATOM 2754 N PHE B 62 -2.915 23.599 145.776 1.00 29.42 N ANISOU 2754 N PHE B 62 3323 4017 3837 -171 -9 425 N ATOM 2755 CA PHE B 62 -2.664 22.171 145.757 1.00 29.35 C ANISOU 2755 CA PHE B 62 3308 4038 3805 -181 -124 526 C ATOM 2756 C PHE B 62 -2.876 21.550 144.397 1.00 28.89 C ANISOU 2756 C PHE B 62 3301 3869 3809 -136 -164 588 C ATOM 2757 O PHE B 62 -3.628 22.083 143.573 1.00 28.84 O ANISOU 2757 O PHE B 62 3323 3806 3828 -102 -125 599 O ATOM 2758 CB PHE B 62 -3.572 21.483 146.771 1.00 30.17 C ANISOU 2758 CB PHE B 62 3385 4261 3819 -236 -165 613 C ATOM 2759 CG PHE B 62 -3.193 21.757 148.198 1.00 31.22 C ANISOU 2759 CG PHE B 62 3484 4548 3831 -298 -155 564 C ATOM 2760 CD1 PHE B 62 -2.024 21.247 148.724 1.00 31.38 C ANISOU 2760 CD1 PHE B 62 3506 4610 3807 -308 -258 577 C ATOM 2761 CD2 PHE B 62 -3.998 22.521 149.008 1.00 32.14 C ANISOU 2761 CD2 PHE B 62 3555 4787 3869 -332 -52 487 C ATOM 2762 CE1 PHE B 62 -1.676 21.489 150.025 1.00 32.78 C ANISOU 2762 CE1 PHE B 62 3656 4959 3838 -372 -275 535 C ATOM 2763 CE2 PHE B 62 -3.648 22.758 150.321 1.00 33.45 C ANISOU 2763 CE2 PHE B 62 3701 5125 3884 -405 -41 421 C ATOM 2764 CZ PHE B 62 -2.484 22.246 150.826 1.00 33.39 C ANISOU 2764 CZ PHE B 62 3712 5168 3808 -435 -162 454 C ATOM 2765 N TYR B 63 -2.218 20.417 144.156 1.00 28.79 N ANISOU 2765 N TYR B 63 3303 3821 3814 -120 -255 619 N ATOM 2766 CA TYR B 63 -2.470 19.681 142.922 1.00 28.78 C ANISOU 2766 CA TYR B 63 3360 3721 3852 -87 -298 645 C ATOM 2767 C TYR B 63 -2.474 18.173 143.103 1.00 29.52 C ANISOU 2767 C TYR B 63 3497 3752 3969 -86 -429 711 C ATOM 2768 O TYR B 63 -1.662 17.647 143.829 1.00 31.04 O ANISOU 2768 O TYR B 63 3678 3946 4170 -55 -499 721 O ATOM 2769 CB TYR B 63 -1.579 20.152 141.745 1.00 28.26 C ANISOU 2769 CB TYR B 63 3315 3615 3809 -50 -225 551 C ATOM 2770 CG TYR B 63 -0.093 19.893 141.835 1.00 28.66 C ANISOU 2770 CG TYR B 63 3300 3697 3893 -16 -221 453 C ATOM 2771 CD1 TYR B 63 0.445 18.659 141.486 1.00 29.50 C ANISOU 2771 CD1 TYR B 63 3404 3757 4047 64 -307 420 C ATOM 2772 CD2 TYR B 63 0.781 20.898 142.219 1.00 29.24 C ANISOU 2772 CD2 TYR B 63 3300 3844 3964 -61 -133 370 C ATOM 2773 CE1 TYR B 63 1.790 18.424 141.557 1.00 30.53 C ANISOU 2773 CE1 TYR B 63 3430 3943 4227 134 -311 308 C ATOM 2774 CE2 TYR B 63 2.145 20.669 142.294 1.00 30.08 C ANISOU 2774 CE2 TYR B 63 3292 4029 4108 -36 -134 260 C ATOM 2775 CZ TYR B 63 2.632 19.431 141.955 1.00 30.75 C ANISOU 2775 CZ TYR B 63 3345 4094 4244 79 -224 230 C ATOM 2776 OH TYR B 63 3.970 19.185 142.009 1.00 32.70 O ANISOU 2776 OH TYR B 63 3436 4442 4547 144 -234 100 O ATOM 2777 N LEU B 64 -3.391 17.489 142.423 1.00 30.66 N ANISOU 2777 N LEU B 64 3697 3826 4126 -120 -478 757 N ATOM 2778 CA LEU B 64 -3.489 16.029 142.477 1.00 32.24 C ANISOU 2778 CA LEU B 64 3980 3902 4369 -144 -605 815 C ATOM 2779 C LEU B 64 -3.738 15.407 141.096 1.00 33.29 C ANISOU 2779 C LEU B 64 4186 3924 4540 -132 -642 743 C ATOM 2780 O LEU B 64 -4.561 15.920 140.318 1.00 33.78 O ANISOU 2780 O LEU B 64 4229 4045 4559 -171 -605 727 O ATOM 2781 CB LEU B 64 -4.643 15.620 143.396 1.00 32.40 C ANISOU 2781 CB LEU B 64 4004 3963 4342 -292 -640 956 C ATOM 2782 CG LEU B 64 -4.416 15.605 144.902 1.00 33.14 C ANISOU 2782 CG LEU B 64 4087 4141 4362 -340 -653 1057 C ATOM 2783 CD1 LEU B 64 -5.689 15.252 145.635 1.00 33.75 C ANISOU 2783 CD1 LEU B 64 4157 4303 4362 -528 -642 1186 C ATOM 2784 CD2 LEU B 64 -3.325 14.622 145.250 1.00 34.15 C ANISOU 2784 CD2 LEU B 64 4312 4129 4535 -258 -789 1102 C ATOM 2785 N LEU B 65 -3.061 14.295 140.799 1.00 33.67 N ANISOU 2785 N LEU B 65 4319 3813 4663 -66 -729 691 N ATOM 2786 CA LEU B 65 -3.412 13.511 139.616 1.00 34.59 C ANISOU 2786 CA LEU B 65 4528 3810 4806 -80 -778 600 C ATOM 2787 C LEU B 65 -4.178 12.242 139.974 1.00 36.58 C ANISOU 2787 C LEU B 65 4897 3885 5117 -202 -910 688 C ATOM 2788 O LEU B 65 -3.675 11.409 140.699 1.00 37.49 O ANISOU 2788 O LEU B 65 5096 3841 5309 -163 -1002 752 O ATOM 2789 CB LEU B 65 -2.173 13.138 138.798 1.00 35.04 C ANISOU 2789 CB LEU B 65 4606 3796 4912 81 -762 416 C ATOM 2790 CG LEU B 65 -2.501 12.293 137.556 1.00 36.54 C ANISOU 2790 CG LEU B 65 4909 3869 5108 67 -807 274 C ATOM 2791 CD1 LEU B 65 -3.322 13.093 136.546 1.00 35.95 C ANISOU 2791 CD1 LEU B 65 4816 3954 4889 -30 -742 254 C ATOM 2792 CD2 LEU B 65 -1.276 11.680 136.887 1.00 38.32 C ANISOU 2792 CD2 LEU B 65 5152 4009 5398 246 -791 57 C ATOM 2793 N TYR B 66 -5.383 12.082 139.436 1.00 37.91 N ANISOU 2793 N TYR B 66 5077 4077 5251 -358 -933 696 N ATOM 2794 CA TYR B 66 -6.143 10.841 139.621 1.00 40.59 C ANISOU 2794 CA TYR B 66 5536 4235 5652 -532 -1050 758 C ATOM 2795 C TYR B 66 -6.158 10.043 138.318 1.00 41.83 C ANISOU 2795 C TYR B 66 5808 4235 5849 -531 -1118 572 C ATOM 2796 O TYR B 66 -6.257 10.625 137.242 1.00 40.72 O ANISOU 2796 O TYR B 66 5612 4236 5624 -489 -1071 441 O ATOM 2797 CB TYR B 66 -7.590 11.143 140.024 1.00 41.23 C ANISOU 2797 CB TYR B 66 5507 4491 5668 -757 -1031 876 C ATOM 2798 CG TYR B 66 -7.795 11.543 141.463 1.00 41.49 C ANISOU 2798 CG TYR B 66 5462 4649 5653 -825 -972 1052 C ATOM 2799 CD1 TYR B 66 -8.432 10.690 142.361 1.00 43.68 C ANISOU 2799 CD1 TYR B 66 5807 4859 5930 -1051 -1017 1212 C ATOM 2800 CD2 TYR B 66 -7.370 12.783 141.928 1.00 40.13 C ANISOU 2800 CD2 TYR B 66 5165 4667 5416 -691 -864 1052 C ATOM 2801 CE1 TYR B 66 -8.615 11.060 143.684 1.00 43.65 C ANISOU 2801 CE1 TYR B 66 5739 5012 5833 -1130 -947 1366 C ATOM 2802 CE2 TYR B 66 -7.551 13.153 143.240 1.00 40.13 C ANISOU 2802 CE2 TYR B 66 5100 4802 5345 -756 -805 1174 C ATOM 2803 CZ TYR B 66 -8.175 12.297 144.103 1.00 41.82 C ANISOU 2803 CZ TYR B 66 5372 4986 5529 -970 -842 1328 C ATOM 2804 OH TYR B 66 -8.363 12.701 145.391 1.00 43.08 O ANISOU 2804 OH TYR B 66 5468 5326 5572 -1049 -766 1438 O ATOM 2805 N TYR B 67 -6.111 8.719 138.423 1.00 44.15 N ANISOU 2805 N TYR B 67 6283 4232 6259 -589 -1236 563 N ATOM 2806 CA TYR B 67 -6.012 7.876 137.237 1.00 46.44 C ANISOU 2806 CA TYR B 67 6709 4338 6600 -573 -1302 337 C ATOM 2807 C TYR B 67 -6.524 6.433 137.357 1.00 49.60 C ANISOU 2807 C TYR B 67 7325 4392 7130 -755 -1446 346 C ATOM 2808 O TYR B 67 -6.538 5.844 138.438 1.00 50.99 O ANISOU 2808 O TYR B 67 7608 4375 7391 -829 -1512 545 O ATOM 2809 CB TYR B 67 -4.582 7.874 136.698 1.00 46.88 C ANISOU 2809 CB TYR B 67 6783 4332 6696 -277 -1258 143 C ATOM 2810 CG TYR B 67 -3.539 7.249 137.586 1.00 48.72 C ANISOU 2810 CG TYR B 67 7093 4335 7082 -90 -1324 200 C ATOM 2811 CD1 TYR B 67 -3.079 5.962 137.335 1.00 52.19 C ANISOU 2811 CD1 TYR B 67 7730 4412 7689 16 -1443 68 C ATOM 2812 CD2 TYR B 67 -2.974 7.957 138.640 1.00 47.34 C ANISOU 2812 CD2 TYR B 67 6797 4303 6886 4 -1284 366 C ATOM 2813 CE1 TYR B 67 -2.114 5.385 138.126 1.00 54.33 C ANISOU 2813 CE1 TYR B 67 8069 4463 8111 234 -1539 130 C ATOM 2814 CE2 TYR B 67 -2.012 7.394 139.439 1.00 49.47 C ANISOU 2814 CE2 TYR B 67 7123 4396 7279 191 -1381 424 C ATOM 2815 CZ TYR B 67 -1.579 6.104 139.177 1.00 53.05 C ANISOU 2815 CZ TYR B 67 7766 4483 7906 323 -1517 318 C ATOM 2816 OH TYR B 67 -0.610 5.528 139.970 1.00 55.31 O ANISOU 2816 OH TYR B 67 8108 4581 8328 555 -1649 389 O ATOM 2817 N THR B 68 -6.936 5.879 136.217 1.00 51.03 N ANISOU 2817 N THR B 68 7590 4491 7309 -844 -1499 129 N ATOM 2818 CA THR B 68 -7.192 4.441 136.073 1.00 53.83 C ANISOU 2818 CA THR B 68 8195 4445 7813 -988 -1637 50 C ATOM 2819 C THR B 68 -6.964 3.936 134.646 1.00 55.14 C ANISOU 2819 C THR B 68 8464 4512 7973 -921 -1667 -308 C ATOM 2820 O THR B 68 -7.000 4.696 133.682 1.00 53.84 O ANISOU 2820 O THR B 68 8166 4654 7637 -868 -1591 -462 O ATOM 2821 CB THR B 68 -8.609 4.029 136.512 1.00 54.78 C ANISOU 2821 CB THR B 68 8327 4555 7932 -1395 -1701 211 C ATOM 2822 OG1 THR B 68 -8.775 2.630 136.272 1.00 58.63 O ANISOU 2822 OG1 THR B 68 9094 4607 8576 -1552 -1836 109 O ATOM 2823 CG2 THR B 68 -9.668 4.797 135.741 1.00 53.25 C ANISOU 2823 CG2 THR B 68 7908 4754 7571 -1560 -1667 132 C ATOM 2824 N GLU B 69 -6.718 2.643 134.535 1.00 58.46 N ANISOU 2824 N GLU B 69 9146 4492 8574 -923 -1781 -438 N ATOM 2825 CA GLU B 69 -6.615 1.986 133.248 1.00 61.29 C ANISOU 2825 CA GLU B 69 9638 4713 8937 -900 -1819 -814 C ATOM 2826 C GLU B 69 -8.008 1.922 132.616 1.00 61.80 C ANISOU 2826 C GLU B 69 9672 4931 8879 -1283 -1880 -874 C ATOM 2827 O GLU B 69 -8.995 1.632 133.296 1.00 62.03 O ANISOU 2827 O GLU B 69 9709 4901 8957 -1601 -1949 -664 O ATOM 2828 CB GLU B 69 -5.990 0.586 133.439 1.00 65.84 C ANISOU 2828 CB GLU B 69 10525 4709 9782 -781 -1941 -934 C ATOM 2829 CG GLU B 69 -6.463 -0.527 132.489 1.00 71.02 C ANISOU 2829 CG GLU B 69 11422 5052 10510 -958 -2047 -1259 C ATOM 2830 CD GLU B 69 -5.553 -0.726 131.278 1.00 73.19 C ANISOU 2830 CD GLU B 69 11735 5315 10757 -660 -1988 -1712 C ATOM 2831 OE1 GLU B 69 -5.841 -1.627 130.460 1.00 76.66 O ANISOU 2831 OE1 GLU B 69 12381 5500 11244 -774 -2067 -2034 O ATOM 2832 OE2 GLU B 69 -4.550 0.010 131.145 1.00 71.70 O ANISOU 2832 OE2 GLU B 69 11367 5383 10492 -333 -1851 -1765 O ATOM 2833 N PHE B 70 -8.083 2.263 131.332 1.00 61.71 N ANISOU 2833 N PHE B 70 9598 5170 8681 -1259 -1850 -1151 N ATOM 2834 CA PHE B 70 -9.307 2.092 130.556 1.00 63.05 C ANISOU 2834 CA PHE B 70 9743 5489 8723 -1591 -1948 -1274 C ATOM 2835 C PHE B 70 -9.011 1.673 129.127 1.00 65.50 C ANISOU 2835 C PHE B 70 10178 5793 8915 -1533 -1969 -1700 C ATOM 2836 O PHE B 70 -7.919 1.924 128.619 1.00 65.36 O ANISOU 2836 O PHE B 70 10175 5825 8834 -1222 -1855 -1875 O ATOM 2837 CB PHE B 70 -10.228 3.328 130.644 1.00 60.18 C ANISOU 2837 CB PHE B 70 9076 5630 8162 -1713 -1919 -1053 C ATOM 2838 CG PHE B 70 -9.882 4.483 129.709 1.00 57.97 C ANISOU 2838 CG PHE B 70 8648 5761 7618 -1506 -1830 -1135 C ATOM 2839 CD1 PHE B 70 -8.594 4.982 129.569 1.00 56.19 C ANISOU 2839 CD1 PHE B 70 8435 5561 7354 -1176 -1683 -1183 C ATOM 2840 CD2 PHE B 70 -10.904 5.133 129.031 1.00 58.18 C ANISOU 2840 CD2 PHE B 70 8506 6170 7430 -1659 -1902 -1129 C ATOM 2841 CE1 PHE B 70 -8.342 6.061 128.730 1.00 54.89 C ANISOU 2841 CE1 PHE B 70 8159 5766 6930 -1048 -1594 -1219 C ATOM 2842 CE2 PHE B 70 -10.649 6.216 128.197 1.00 56.55 C ANISOU 2842 CE2 PHE B 70 8203 6317 6965 -1487 -1842 -1149 C ATOM 2843 CZ PHE B 70 -9.369 6.678 128.051 1.00 54.81 C ANISOU 2843 CZ PHE B 70 8036 6091 6699 -1201 -1677 -1184 C ATOM 2844 N THR B 71 -9.976 1.022 128.492 1.00 68.25 N ANISOU 2844 N THR B 71 10604 6103 9223 -1852 -2107 -1884 N ATOM 2845 CA THR B 71 -9.882 0.716 127.074 1.00 70.60 C ANISOU 2845 CA THR B 71 11003 6483 9340 -1850 -2139 -2304 C ATOM 2846 C THR B 71 -11.009 1.466 126.373 1.00 70.59 C ANISOU 2846 C THR B 71 10788 6988 9045 -2082 -2221 -2277 C ATOM 2847 O THR B 71 -12.173 1.063 126.432 1.00 72.09 O ANISOU 2847 O THR B 71 10937 7190 9264 -2441 -2372 -2260 O ATOM 2848 CB THR B 71 -9.947 -0.796 126.819 1.00 75.26 C ANISOU 2848 CB THR B 71 11907 6554 10133 -2008 -2261 -2618 C ATOM 2849 OG1 THR B 71 -8.851 -1.432 127.482 1.00 75.75 O ANISOU 2849 OG1 THR B 71 12162 6139 10479 -1724 -2208 -2619 O ATOM 2850 CG2 THR B 71 -9.840 -1.098 125.350 1.00 78.18 C ANISOU 2850 CG2 THR B 71 12382 7039 10286 -2008 -2284 -3095 C ATOM 2851 N PRO B 72 -10.661 2.601 125.747 1.00 68.91 N ANISOU 2851 N PRO B 72 10427 7204 8552 -1876 -2125 -2251 N ATOM 2852 CA PRO B 72 -11.589 3.532 125.108 1.00 68.63 C ANISOU 2852 CA PRO B 72 10183 7673 8221 -1997 -2210 -2163 C ATOM 2853 C PRO B 72 -12.252 2.934 123.876 1.00 73.09 C ANISOU 2853 C PRO B 72 10835 8357 8579 -2234 -2380 -2512 C ATOM 2854 O PRO B 72 -11.615 2.236 123.085 1.00 75.88 O ANISOU 2854 O PRO B 72 11410 8552 8868 -2180 -2353 -2881 O ATOM 2855 CB PRO B 72 -10.695 4.717 124.722 1.00 65.82 C ANISOU 2855 CB PRO B 72 9759 7607 7642 -1681 -2041 -2076 C ATOM 2856 CG PRO B 72 -9.320 4.161 124.648 1.00 66.23 C ANISOU 2856 CG PRO B 72 9997 7373 7796 -1444 -1881 -2300 C ATOM 2857 CD PRO B 72 -9.264 3.061 125.662 1.00 67.08 C ANISOU 2857 CD PRO B 72 10224 6977 8284 -1501 -1927 -2289 C ATOM 2858 N THR B 73 -13.549 3.170 123.751 1.00 74.60 N ANISOU 2858 N THR B 73 10836 8833 8676 -2500 -2561 -2419 N ATOM 2859 CA THR B 73 -14.313 2.659 122.627 1.00 79.20 C ANISOU 2859 CA THR B 73 11458 9590 9045 -2763 -2763 -2735 C ATOM 2860 C THR B 73 -15.067 3.806 121.964 1.00 79.59 C ANISOU 2860 C THR B 73 11261 10224 8754 -2750 -2890 -2588 C ATOM 2861 O THR B 73 -14.722 4.970 122.140 1.00 76.27 O ANISOU 2861 O THR B 73 10725 10020 8233 -2485 -2785 -2307 O ATOM 2862 CB THR B 73 -15.313 1.567 123.062 1.00 81.93 C ANISOU 2862 CB THR B 73 11807 9690 9631 -3181 -2927 -2822 C ATOM 2863 OG1 THR B 73 -16.105 2.045 124.155 1.00 79.66 O ANISOU 2863 OG1 THR B 73 11241 9516 9510 -3292 -2938 -2444 O ATOM 2864 CG2 THR B 73 -14.591 0.292 123.483 1.00 83.44 C ANISOU 2864 CG2 THR B 73 12327 9244 10132 -3206 -2853 -3017 C ATOM 2865 N GLU B 74 -16.102 3.474 121.203 1.00 84.56 N ANISOU 2865 N GLU B 74 11817 11098 9214 -3037 -3133 -2777 N ATOM 2866 CA GLU B 74 -16.883 4.481 120.497 1.00 86.05 C ANISOU 2866 CA GLU B 74 11778 11848 9070 -3014 -3313 -2650 C ATOM 2867 C GLU B 74 -18.061 4.982 121.340 1.00 84.98 C ANISOU 2867 C GLU B 74 11266 11919 9105 -3125 -3431 -2343 C ATOM 2868 O GLU B 74 -18.262 6.193 121.495 1.00 82.61 O ANISOU 2868 O GLU B 74 10760 11917 8712 -2896 -3435 -2037 O ATOM 2869 CB GLU B 74 -17.333 3.931 119.128 1.00 92.08 C ANISOU 2869 CB GLU B 74 12642 12845 9502 -3235 -3538 -3039 C ATOM 2870 CG GLU B 74 -18.552 4.609 118.471 1.00 95.80 C ANISOU 2870 CG GLU B 74 12830 13887 9682 -3337 -3844 -2949 C ATOM 2871 CD GLU B 74 -18.293 6.034 117.952 1.00 94.72 C ANISOU 2871 CD GLU B 74 12644 14139 9208 -2996 -3843 -2661 C ATOM 2872 OE1 GLU B 74 -17.116 6.455 117.825 1.00 92.56 O ANISOU 2872 OE1 GLU B 74 12588 13745 8834 -2731 -3601 -2603 O ATOM 2873 OE2 GLU B 74 -19.290 6.735 117.655 1.00 96.47 O ANISOU 2873 OE2 GLU B 74 12602 14788 9263 -2999 -4097 -2493 O ATOM 2874 N LYS B 75 -18.806 4.038 121.913 1.00 86.90 N ANISOU 2874 N LYS B 75 11429 11981 9609 -3480 -3510 -2434 N ATOM 2875 CA LYS B 75 -20.035 4.329 122.659 1.00 86.69 C ANISOU 2875 CA LYS B 75 11008 12194 9736 -3664 -3617 -2219 C ATOM 2876 C LYS B 75 -19.841 4.815 124.107 1.00 82.00 C ANISOU 2876 C LYS B 75 10286 11442 9429 -3519 -3397 -1860 C ATOM 2877 O LYS B 75 -20.754 5.410 124.671 1.00 82.05 O ANISOU 2877 O LYS B 75 9927 11745 9502 -3555 -3447 -1656 O ATOM 2878 CB LYS B 75 -20.960 3.098 122.648 1.00 91.47 C ANISOU 2878 CB LYS B 75 11567 12706 10479 -4180 -3780 -2474 C ATOM 2879 CG LYS B 75 -20.216 1.769 122.809 1.00 92.99 C ANISOU 2879 CG LYS B 75 12173 12284 10874 -4352 -3668 -2716 C ATOM 2880 CD LYS B 75 -20.923 0.797 123.756 1.00 95.14 C ANISOU 2880 CD LYS B 75 12395 12271 11481 -4803 -3672 -2694 C ATOM 2881 CE LYS B 75 -19.954 -0.284 124.238 1.00 95.02 C ANISOU 2881 CE LYS B 75 12826 11550 11728 -4828 -3516 -2787 C ATOM 2882 NZ LYS B 75 -20.503 -1.098 125.354 1.00 96.35 N ANISOU 2882 NZ LYS B 75 12995 11392 12223 -5229 -3479 -2648 N ATOM 2883 N ASP B 76 -18.676 4.573 124.707 1.00 78.25 N ANISOU 2883 N ASP B 76 10086 10533 9112 -3348 -3163 -1802 N ATOM 2884 CA ASP B 76 -18.504 4.806 126.149 1.00 74.33 C ANISOU 2884 CA ASP B 76 9504 9853 8885 -3282 -2972 -1498 C ATOM 2885 C ASP B 76 -18.057 6.214 126.511 1.00 69.73 C ANISOU 2885 C ASP B 76 8791 9469 8233 -2880 -2840 -1212 C ATOM 2886 O ASP B 76 -16.932 6.607 126.216 1.00 67.62 O ANISOU 2886 O ASP B 76 8731 9088 7874 -2585 -2716 -1208 O ATOM 2887 CB ASP B 76 -17.511 3.804 126.748 1.00 74.04 C ANISOU 2887 CB ASP B 76 9817 9239 9077 -3302 -2819 -1554 C ATOM 2888 CG ASP B 76 -18.042 2.376 126.765 1.00 78.75 C ANISOU 2888 CG ASP B 76 10557 9529 9837 -3743 -2928 -1766 C ATOM 2889 OD1 ASP B 76 -19.252 2.167 126.523 1.00 81.98 O ANISOU 2889 OD1 ASP B 76 10741 10197 10212 -4090 -3095 -1842 O ATOM 2890 OD2 ASP B 76 -17.239 1.454 127.025 1.00 79.45 O ANISOU 2890 OD2 ASP B 76 10983 9104 10101 -3743 -2854 -1862 O ATOM 2891 N GLU B 77 -18.926 6.971 127.171 1.00 68.32 N ANISOU 2891 N GLU B 77 8265 9583 8110 -2876 -2855 -990 N ATOM 2892 CA GLU B 77 -18.527 8.269 127.705 1.00 64.55 C ANISOU 2892 CA GLU B 77 7682 9221 7622 -2514 -2716 -724 C ATOM 2893 C GLU B 77 -17.726 8.143 129.007 1.00 61.03 C ANISOU 2893 C GLU B 77 7352 8437 7398 -2446 -2474 -560 C ATOM 2894 O GLU B 77 -17.936 7.221 129.786 1.00 62.03 O ANISOU 2894 O GLU B 77 7512 8344 7713 -2713 -2433 -558 O ATOM 2895 CB GLU B 77 -19.737 9.181 127.905 1.00 65.81 C ANISOU 2895 CB GLU B 77 7421 9819 7765 -2479 -2825 -582 C ATOM 2896 CG GLU B 77 -19.910 10.202 126.782 1.00 67.62 C ANISOU 2896 CG GLU B 77 7588 10376 7727 -2216 -2994 -564 C ATOM 2897 CD GLU B 77 -21.283 10.863 126.781 1.00 70.41 C ANISOU 2897 CD GLU B 77 7502 11176 8073 -2202 -3186 -491 C ATOM 2898 OE1 GLU B 77 -21.878 10.993 125.682 1.00 72.87 O ANISOU 2898 OE1 GLU B 77 7728 11787 8172 -2206 -3450 -587 O ATOM 2899 OE2 GLU B 77 -21.765 11.241 127.876 1.00 69.83 O ANISOU 2899 OE2 GLU B 77 7159 11176 8199 -2178 -3077 -353 O ATOM 2900 N TYR B 78 -16.802 9.069 129.228 1.00 56.75 N ANISOU 2900 N TYR B 78 6885 7857 6822 -2107 -2325 -416 N ATOM 2901 CA TYR B 78 -15.990 9.045 130.425 1.00 53.82 C ANISOU 2901 CA TYR B 78 6609 7213 6626 -2017 -2121 -268 C ATOM 2902 C TYR B 78 -15.913 10.421 131.034 1.00 50.86 C ANISOU 2902 C TYR B 78 6060 7022 6242 -1752 -2010 -49 C ATOM 2903 O TYR B 78 -15.682 11.395 130.341 1.00 50.13 O ANISOU 2903 O TYR B 78 5964 7088 5996 -1517 -2028 -21 O ATOM 2904 CB TYR B 78 -14.582 8.549 130.113 1.00 53.40 C ANISOU 2904 CB TYR B 78 6891 6825 6574 -1878 -2029 -383 C ATOM 2905 CG TYR B 78 -14.500 7.056 129.912 1.00 56.87 C ANISOU 2905 CG TYR B 78 7549 6944 7115 -2117 -2098 -590 C ATOM 2906 CD1 TYR B 78 -14.349 6.194 130.992 1.00 57.51 C ANISOU 2906 CD1 TYR B 78 7735 6693 7423 -2262 -2045 -507 C ATOM 2907 CD2 TYR B 78 -14.585 6.505 128.644 1.00 59.57 C ANISOU 2907 CD2 TYR B 78 8016 7301 7317 -2204 -2227 -868 C ATOM 2908 CE1 TYR B 78 -14.282 4.819 130.804 1.00 60.71 C ANISOU 2908 CE1 TYR B 78 8383 6738 7947 -2476 -2123 -688 C ATOM 2909 CE2 TYR B 78 -14.518 5.142 128.449 1.00 62.80 C ANISOU 2909 CE2 TYR B 78 8648 7374 7838 -2419 -2293 -1091 C ATOM 2910 CZ TYR B 78 -14.370 4.301 129.525 1.00 63.37 C ANISOU 2910 CZ TYR B 78 8839 7069 8170 -2551 -2245 -997 C ATOM 2911 OH TYR B 78 -14.308 2.939 129.312 1.00 67.12 O ANISOU 2911 OH TYR B 78 9576 7149 8779 -2760 -2326 -1213 O ATOM 2912 N ALA B 79 -16.100 10.518 132.338 1.00 49.58 N ANISOU 2912 N ALA B 79 5775 6830 6231 -1798 -1891 106 N ATOM 2913 CA ALA B 79 -16.048 11.826 132.966 1.00 46.89 C ANISOU 2913 CA ALA B 79 5276 6650 5892 -1550 -1780 274 C ATOM 2914 C ALA B 79 -15.188 11.842 134.220 1.00 44.65 C ANISOU 2914 C ALA B 79 5092 6152 5722 -1489 -1590 396 C ATOM 2915 O ALA B 79 -14.684 10.807 134.653 1.00 44.47 O ANISOU 2915 O ALA B 79 5253 5858 5784 -1632 -1560 383 O ATOM 2916 CB ALA B 79 -17.445 12.314 133.272 1.00 48.04 C ANISOU 2916 CB ALA B 79 5053 7141 6060 -1619 -1844 321 C ATOM 2917 N CYS B 80 -15.018 13.030 134.788 1.00 43.29 N ANISOU 2917 N CYS B 80 4810 6093 5547 -1268 -1480 512 N ATOM 2918 CA CYS B 80 -14.375 13.196 136.089 1.00 42.64 C ANISOU 2918 CA CYS B 80 4765 5890 5545 -1223 -1313 626 C ATOM 2919 C CYS B 80 -15.322 14.004 136.967 1.00 42.61 C ANISOU 2919 C CYS B 80 4468 6154 5569 -1210 -1243 705 C ATOM 2920 O CYS B 80 -15.864 15.006 136.511 1.00 43.69 O ANISOU 2920 O CYS B 80 4438 6494 5670 -1036 -1286 694 O ATOM 2921 CB CYS B 80 -13.037 13.923 135.931 1.00 41.18 C ANISOU 2921 CB CYS B 80 4753 5571 5324 -958 -1221 638 C ATOM 2922 SG CYS B 80 -12.253 14.401 137.499 1.00 41.86 S ANISOU 2922 SG CYS B 80 4845 5582 5478 -872 -1041 758 S ATOM 2923 N ARG B 81 -15.566 13.568 138.200 1.00 42.56 N ANISOU 2923 N ARG B 81 4397 6156 5617 -1390 -1142 780 N ATOM 2924 CA ARG B 81 -16.535 14.277 139.053 1.00 43.00 C ANISOU 2924 CA ARG B 81 4142 6513 5684 -1396 -1049 812 C ATOM 2925 C ARG B 81 -15.913 14.756 140.362 1.00 41.19 C ANISOU 2925 C ARG B 81 3953 6251 5449 -1319 -868 896 C ATOM 2926 O ARG B 81 -15.372 13.965 141.131 1.00 40.48 O ANISOU 2926 O ARG B 81 4031 5997 5352 -1480 -815 980 O ATOM 2927 CB ARG B 81 -17.769 13.426 139.310 1.00 46.33 C ANISOU 2927 CB ARG B 81 4352 7122 6130 -1743 -1078 798 C ATOM 2928 CG ARG B 81 -18.799 14.077 140.228 1.00 48.48 C ANISOU 2928 CG ARG B 81 4257 7756 6407 -1767 -951 797 C ATOM 2929 CD ARG B 81 -19.973 13.137 140.508 1.00 51.98 C ANISOU 2929 CD ARG B 81 4476 8407 6866 -2180 -953 783 C ATOM 2930 NE ARG B 81 -19.586 11.998 141.337 1.00 53.26 N ANISOU 2930 NE ARG B 81 4875 8349 7011 -2515 -872 909 N ATOM 2931 CZ ARG B 81 -20.330 10.908 141.519 1.00 56.93 C ANISOU 2931 CZ ARG B 81 5290 8851 7490 -2952 -883 935 C ATOM 2932 NH1 ARG B 81 -21.513 10.788 140.922 1.00 59.85 N ANISOU 2932 NH1 ARG B 81 5337 9511 7893 -3125 -969 812 N ATOM 2933 NH2 ARG B 81 -19.886 9.927 142.296 1.00 57.81 N ANISOU 2933 NH2 ARG B 81 5680 8703 7583 -3229 -822 1091 N ATOM 2934 N VAL B 82 -15.971 16.067 140.586 1.00 40.04 N ANISOU 2934 N VAL B 82 3672 6244 5299 -1062 -791 869 N ATOM 2935 CA VAL B 82 -15.154 16.720 141.611 1.00 38.30 C ANISOU 2935 CA VAL B 82 3532 5963 5058 -938 -640 905 C ATOM 2936 C VAL B 82 -15.995 17.519 142.592 1.00 39.16 C ANISOU 2936 C VAL B 82 3364 6356 5160 -899 -500 861 C ATOM 2937 O VAL B 82 -16.837 18.307 142.173 1.00 40.59 O ANISOU 2937 O VAL B 82 3316 6719 5387 -738 -530 779 O ATOM 2938 CB VAL B 82 -14.107 17.693 140.982 1.00 36.44 C ANISOU 2938 CB VAL B 82 3465 5552 4826 -645 -651 880 C ATOM 2939 CG1 VAL B 82 -13.222 18.354 142.057 1.00 34.66 C ANISOU 2939 CG1 VAL B 82 3316 5269 4582 -552 -506 890 C ATOM 2940 CG2 VAL B 82 -13.237 16.973 139.967 1.00 35.67 C ANISOU 2940 CG2 VAL B 82 3614 5221 4718 -663 -757 885 C ATOM 2941 N ASN B 83 -15.772 17.317 143.891 1.00 38.31 N ANISOU 2941 N ASN B 83 3274 6297 4985 -1033 -356 906 N ATOM 2942 CA ASN B 83 -16.369 18.170 144.897 1.00 38.91 C ANISOU 2942 CA ASN B 83 3116 6641 5026 -971 -189 825 C ATOM 2943 C ASN B 83 -15.308 18.717 145.829 1.00 36.63 C ANISOU 2943 C ASN B 83 2998 6252 4666 -875 -78 828 C ATOM 2944 O ASN B 83 -14.292 18.070 146.079 1.00 35.72 O ANISOU 2944 O ASN B 83 3136 5938 4499 -967 -113 935 O ATOM 2945 CB ASN B 83 -17.451 17.425 145.683 1.00 42.60 C ANISOU 2945 CB ASN B 83 3359 7400 5427 -1292 -91 846 C ATOM 2946 CG ASN B 83 -18.565 18.350 146.167 1.00 45.67 C ANISOU 2946 CG ASN B 83 3362 8164 5827 -1182 48 683 C ATOM 2947 OD1 ASN B 83 -18.375 19.566 146.344 1.00 45.40 O ANISOU 2947 OD1 ASN B 83 3283 8138 5828 -872 111 562 O ATOM 2948 ND2 ASN B 83 -19.736 17.775 146.386 1.00 48.72 N ANISOU 2948 ND2 ASN B 83 3460 8858 6195 -1440 102 662 N ATOM 2949 N HIS B 84 -15.571 19.908 146.350 1.00 36.33 N ANISOU 2949 N HIS B 84 2811 6361 4633 -681 43 691 N ATOM 2950 CA HIS B 84 -14.630 20.672 147.164 1.00 34.27 C ANISOU 2950 CA HIS B 84 2686 6022 4312 -567 143 636 C ATOM 2951 C HIS B 84 -15.523 21.678 147.892 1.00 36.40 C ANISOU 2951 C HIS B 84 2689 6562 4578 -444 306 447 C ATOM 2952 O HIS B 84 -16.714 21.810 147.559 1.00 38.44 O ANISOU 2952 O HIS B 84 2670 7024 4910 -395 310 373 O ATOM 2953 CB HIS B 84 -13.621 21.360 146.226 1.00 32.01 C ANISOU 2953 CB HIS B 84 2605 5431 4125 -335 43 627 C ATOM 2954 CG HIS B 84 -12.502 22.086 146.912 1.00 30.56 C ANISOU 2954 CG HIS B 84 2578 5136 3899 -256 119 567 C ATOM 2955 ND1 HIS B 84 -12.413 23.462 146.924 1.00 30.75 N ANISOU 2955 ND1 HIS B 84 2590 5098 3994 -30 182 420 N ATOM 2956 CD2 HIS B 84 -11.408 21.631 147.570 1.00 29.57 C ANISOU 2956 CD2 HIS B 84 2624 4939 3674 -371 121 628 C ATOM 2957 CE1 HIS B 84 -11.325 23.823 147.581 1.00 30.45 C ANISOU 2957 CE1 HIS B 84 2702 4971 3896 -48 234 376 C ATOM 2958 NE2 HIS B 84 -10.698 22.730 147.987 1.00 29.53 N ANISOU 2958 NE2 HIS B 84 2680 4870 3670 -244 191 501 N ATOM 2959 N VAL B 85 -14.979 22.386 148.874 1.00 36.06 N ANISOU 2959 N VAL B 85 2707 6541 4452 -384 435 342 N ATOM 2960 CA VAL B 85 -15.766 23.361 149.622 1.00 38.93 C ANISOU 2960 CA VAL B 85 2833 7149 4809 -248 607 113 C ATOM 2961 C VAL B 85 -16.156 24.590 148.765 1.00 40.13 C ANISOU 2961 C VAL B 85 2899 7168 5180 124 551 -30 C ATOM 2962 O VAL B 85 -17.142 25.276 149.046 1.00 42.15 O ANISOU 2962 O VAL B 85 2885 7629 5499 293 648 -222 O ATOM 2963 CB VAL B 85 -15.063 23.740 150.976 1.00 39.00 C ANISOU 2963 CB VAL B 85 2951 7232 4635 -315 759 12 C ATOM 2964 CG1 VAL B 85 -13.930 24.754 150.779 1.00 36.66 C ANISOU 2964 CG1 VAL B 85 2884 6624 4422 -108 713 -73 C ATOM 2965 CG2 VAL B 85 -16.070 24.224 152.004 1.00 41.48 C ANISOU 2965 CG2 VAL B 85 2983 7925 4852 -312 983 -213 C ATOM 2966 N THR B 86 -15.412 24.828 147.687 1.00 39.16 N ANISOU 2966 N THR B 86 3003 6707 5167 252 390 72 N ATOM 2967 CA THR B 86 -15.697 25.956 146.811 1.00 41.03 C ANISOU 2967 CA THR B 86 3231 6769 5590 587 307 -1 C ATOM 2968 C THR B 86 -16.896 25.702 145.901 1.00 42.29 C ANISOU 2968 C THR B 86 3146 7076 5846 679 178 37 C ATOM 2969 O THR B 86 -17.606 26.637 145.536 1.00 44.71 O ANISOU 2969 O THR B 86 3310 7381 6295 984 135 -68 O ATOM 2970 CB THR B 86 -14.466 26.374 145.970 1.00 39.69 C ANISOU 2970 CB THR B 86 3401 6208 5470 660 198 105 C ATOM 2971 OG1 THR B 86 -14.022 25.271 145.168 1.00 38.56 O ANISOU 2971 OG1 THR B 86 3377 6001 5273 479 71 302 O ATOM 2972 CG2 THR B 86 -13.332 26.848 146.881 1.00 38.71 C ANISOU 2972 CG2 THR B 86 3467 5961 5278 597 317 18 C ATOM 2973 N LEU B 87 -17.137 24.441 145.559 1.00 41.29 N ANISOU 2973 N LEU B 87 2968 7073 5646 421 103 177 N ATOM 2974 CA LEU B 87 -18.285 24.098 144.720 1.00 42.54 C ANISOU 2974 CA LEU B 87 2870 7415 5877 453 -33 197 C ATOM 2975 C LEU B 87 -19.529 23.786 145.553 1.00 46.04 C ANISOU 2975 C LEU B 87 2904 8291 6297 336 102 66 C ATOM 2976 O LEU B 87 -19.459 23.102 146.584 1.00 46.99 O ANISOU 2976 O LEU B 87 3001 8578 6276 42 267 71 O ATOM 2977 CB LEU B 87 -17.946 22.927 143.804 1.00 40.24 C ANISOU 2977 CB LEU B 87 2737 7020 5533 224 -194 379 C ATOM 2978 CG LEU B 87 -16.705 23.135 142.931 1.00 37.65 C ANISOU 2978 CG LEU B 87 2783 6319 5203 310 -302 492 C ATOM 2979 CD1 LEU B 87 -16.242 21.829 142.287 1.00 35.64 C ANISOU 2979 CD1 LEU B 87 2692 5974 4875 54 -409 622 C ATOM 2980 CD2 LEU B 87 -16.947 24.222 141.885 1.00 38.51 C ANISOU 2980 CD2 LEU B 87 2915 6306 5412 641 -442 491 C ATOM 2981 N SER B 88 -20.678 24.274 145.095 1.00 48.59 N ANISOU 2981 N SER B 88 2895 8820 6748 561 28 -44 N ATOM 2982 CA SER B 88 -21.926 24.054 145.810 1.00 51.85 C ANISOU 2982 CA SER B 88 2848 9697 7154 466 168 -203 C ATOM 2983 C SER B 88 -22.653 22.796 145.366 1.00 52.93 C ANISOU 2983 C SER B 88 2785 10077 7248 124 79 -109 C ATOM 2984 O SER B 88 -23.734 22.493 145.881 1.00 56.97 O ANISOU 2984 O SER B 88 2884 11014 7749 -23 197 -229 O ATOM 2985 CB SER B 88 -22.846 25.268 145.695 1.00 54.72 C ANISOU 2985 CB SER B 88 2887 10204 7699 913 150 -420 C ATOM 2986 OG SER B 88 -22.830 25.772 144.381 1.00 54.29 O ANISOU 2986 OG SER B 88 2940 9910 7779 1214 -130 -325 O ATOM 2987 N GLN B 89 -22.068 22.087 144.404 1.00 49.96 N ANISOU 2987 N GLN B 89 2691 9440 6850 -10 -118 82 N ATOM 2988 CA GLN B 89 -22.511 20.756 144.002 1.00 50.79 C ANISOU 2988 CA GLN B 89 2720 9675 6903 -398 -206 177 C ATOM 2989 C GLN B 89 -21.349 20.205 143.202 1.00 47.18 C ANISOU 2989 C GLN B 89 2723 8800 6402 -472 -360 355 C ATOM 2990 O GLN B 89 -20.524 20.998 142.743 1.00 44.56 O ANISOU 2990 O GLN B 89 2647 8182 6103 -183 -425 385 O ATOM 2991 CB GLN B 89 -23.832 20.795 143.192 1.00 54.76 C ANISOU 2991 CB GLN B 89 2796 10499 7513 -317 -374 80 C ATOM 2992 CG GLN B 89 -23.775 21.196 141.734 1.00 54.59 C ANISOU 2992 CG GLN B 89 2874 10303 7565 -33 -680 133 C ATOM 2993 CD GLN B 89 -25.180 21.261 141.145 1.00 59.64 C ANISOU 2993 CD GLN B 89 3021 11345 8296 51 -847 17 C ATOM 2994 OE1 GLN B 89 -25.553 22.239 140.492 1.00 61.60 O ANISOU 2994 OE1 GLN B 89 3148 11610 8647 477 -1022 -27 O ATOM 2995 NE2 GLN B 89 -25.981 20.226 141.405 1.00 61.90 N ANISOU 2995 NE2 GLN B 89 3010 11960 8548 -361 -799 -31 N ATOM 2996 N PRO B 90 -21.244 18.858 143.081 1.00 47.07 N ANISOU 2996 N PRO B 90 2827 8739 6319 -865 -400 463 N ATOM 2997 CA PRO B 90 -20.181 18.228 142.277 1.00 44.15 C ANISOU 2997 CA PRO B 90 2867 7989 5920 -927 -544 591 C ATOM 2998 C PRO B 90 -20.111 18.730 140.836 1.00 43.71 C ANISOU 2998 C PRO B 90 2879 7819 5911 -659 -772 582 C ATOM 2999 O PRO B 90 -21.143 18.897 140.189 1.00 47.06 O ANISOU 2999 O PRO B 90 3017 8481 6381 -592 -910 513 O ATOM 3000 CB PRO B 90 -20.576 16.749 142.279 1.00 45.35 C ANISOU 3000 CB PRO B 90 3014 8183 6034 -1375 -578 650 C ATOM 3001 CG PRO B 90 -21.314 16.563 143.541 1.00 47.90 C ANISOU 3001 CG PRO B 90 3076 8814 6310 -1611 -366 627 C ATOM 3002 CD PRO B 90 -22.029 17.847 143.825 1.00 49.16 C ANISOU 3002 CD PRO B 90 2877 9278 6524 -1293 -281 468 C ATOM 3003 N LYS B 91 -18.905 18.997 140.354 1.00 41.11 N ANISOU 3003 N LYS B 91 2910 7156 5554 -511 -812 652 N ATOM 3004 CA LYS B 91 -18.703 19.458 138.977 1.00 40.90 C ANISOU 3004 CA LYS B 91 3010 7011 5520 -292 -1008 672 C ATOM 3005 C LYS B 91 -18.326 18.253 138.117 1.00 40.46 C ANISOU 3005 C LYS B 91 3159 6820 5394 -531 -1135 703 C ATOM 3006 O LYS B 91 -17.374 17.538 138.425 1.00 38.73 O ANISOU 3006 O LYS B 91 3195 6373 5147 -683 -1060 745 O ATOM 3007 CB LYS B 91 -17.603 20.515 138.935 1.00 38.62 C ANISOU 3007 CB LYS B 91 2986 6459 5229 -22 -947 717 C ATOM 3008 CG LYS B 91 -17.592 21.417 137.734 1.00 39.88 C ANISOU 3008 CG LYS B 91 3234 6541 5375 257 -1111 757 C ATOM 3009 CD LYS B 91 -16.548 22.514 137.958 1.00 38.91 C ANISOU 3009 CD LYS B 91 3357 6156 5269 464 -1000 798 C ATOM 3010 CE LYS B 91 -15.800 22.915 136.671 1.00 38.87 C ANISOU 3010 CE LYS B 91 3649 5945 5174 570 -1114 899 C ATOM 3011 NZ LYS B 91 -16.261 24.212 136.081 1.00 41.43 N ANISOU 3011 NZ LYS B 91 3975 6234 5534 886 -1231 959 N ATOM 3012 N ILE B 92 -19.099 18.002 137.066 1.00 42.43 N ANISOU 3012 N ILE B 92 3286 7219 5618 -557 -1339 664 N ATOM 3013 CA ILE B 92 -18.798 16.906 136.162 1.00 42.14 C ANISOU 3013 CA ILE B 92 3445 7058 5506 -773 -1468 646 C ATOM 3014 C ILE B 92 -18.188 17.453 134.878 1.00 42.65 C ANISOU 3014 C ILE B 92 3740 7001 5462 -549 -1602 670 C ATOM 3015 O ILE B 92 -18.792 18.288 134.199 1.00 44.53 O ANISOU 3015 O ILE B 92 3852 7401 5668 -332 -1748 685 O ATOM 3016 CB ILE B 92 -20.042 16.070 135.848 1.00 44.22 C ANISOU 3016 CB ILE B 92 3437 7586 5780 -1041 -1608 560 C ATOM 3017 CG1 ILE B 92 -20.765 15.713 137.148 1.00 45.18 C ANISOU 3017 CG1 ILE B 92 3286 7892 5988 -1270 -1446 550 C ATOM 3018 CG2 ILE B 92 -19.659 14.821 135.079 1.00 43.65 C ANISOU 3018 CG2 ILE B 92 3610 7330 5645 -1304 -1716 507 C ATOM 3019 CD1 ILE B 92 -21.930 14.773 136.979 1.00 48.69 C ANISOU 3019 CD1 ILE B 92 3458 8590 6453 -1626 -1544 464 C ATOM 3020 N VAL B 93 -16.962 17.016 134.585 1.00 41.13 N ANISOU 3020 N VAL B 93 3885 6532 5210 -592 -1547 679 N ATOM 3021 CA VAL B 93 -16.294 17.336 133.330 1.00 41.23 C ANISOU 3021 CA VAL B 93 4138 6448 5080 -457 -1639 687 C ATOM 3022 C VAL B 93 -16.112 16.068 132.476 1.00 42.60 C ANISOU 3022 C VAL B 93 4464 6559 5162 -684 -1742 571 C ATOM 3023 O VAL B 93 -15.424 15.136 132.900 1.00 41.44 O ANISOU 3023 O VAL B 93 4469 6204 5071 -840 -1645 522 O ATOM 3024 CB VAL B 93 -14.920 17.963 133.582 1.00 38.66 C ANISOU 3024 CB VAL B 93 4062 5882 4746 -306 -1467 751 C ATOM 3025 CG1 VAL B 93 -14.360 18.531 132.285 1.00 38.42 C ANISOU 3025 CG1 VAL B 93 4245 5810 4542 -170 -1539 784 C ATOM 3026 CG2 VAL B 93 -15.027 19.053 134.645 1.00 38.26 C ANISOU 3026 CG2 VAL B 93 3884 5845 4809 -134 -1340 822 C ATOM 3027 N LYS B 94 -16.726 16.042 131.287 1.00 44.75 N ANISOU 3027 N LYS B 94 4704 7005 5294 -689 -1951 520 N ATOM 3028 CA LYS B 94 -16.600 14.913 130.348 1.00 46.01 C ANISOU 3028 CA LYS B 94 5019 7125 5340 -898 -2063 365 C ATOM 3029 C LYS B 94 -15.250 14.890 129.599 1.00 44.72 C ANISOU 3029 C LYS B 94 5197 6762 5031 -813 -1981 324 C ATOM 3030 O LYS B 94 -14.573 15.912 129.490 1.00 42.60 O ANISOU 3030 O LYS B 94 5033 6455 4699 -598 -1889 440 O ATOM 3031 CB LYS B 94 -17.737 14.944 129.327 1.00 49.15 C ANISOU 3031 CB LYS B 94 5248 7827 5599 -937 -2332 308 C ATOM 3032 CG LYS B 94 -18.973 15.720 129.767 1.00 50.92 C ANISOU 3032 CG LYS B 94 5095 8339 5915 -825 -2428 394 C ATOM 3033 CD LYS B 94 -20.199 15.302 128.939 1.00 55.01 C ANISOU 3033 CD LYS B 94 5378 9183 6342 -967 -2714 282 C ATOM 3034 CE LYS B 94 -21.280 16.384 128.936 1.00 57.18 C ANISOU 3034 CE LYS B 94 5301 9778 6645 -715 -2873 376 C ATOM 3035 NZ LYS B 94 -22.618 15.886 128.510 1.00 60.24 N ANISOU 3035 NZ LYS B 94 5331 10539 7017 -892 -3129 248 N ATOM 3036 N TRP B 95 -14.878 13.720 129.078 1.00 45.64 N ANISOU 3036 N TRP B 95 5481 6757 5101 -995 -2006 142 N ATOM 3037 CA TRP B 95 -13.604 13.544 128.378 1.00 45.39 C ANISOU 3037 CA TRP B 95 5736 6570 4941 -927 -1906 45 C ATOM 3038 C TRP B 95 -13.780 13.740 126.890 1.00 48.48 C ANISOU 3038 C TRP B 95 6225 7163 5032 -915 -2055 -33 C ATOM 3039 O TRP B 95 -14.385 12.912 126.218 1.00 51.47 O ANISOU 3039 O TRP B 95 6602 7631 5324 -1095 -2220 -207 O ATOM 3040 CB TRP B 95 -13.004 12.152 128.661 1.00 45.17 C ANISOU 3040 CB TRP B 95 5856 6266 5042 -1084 -1842 -139 C ATOM 3041 CG TRP B 95 -11.855 11.717 127.767 1.00 45.80 C ANISOU 3041 CG TRP B 95 6189 6226 4987 -1031 -1766 -331 C ATOM 3042 CD1 TRP B 95 -10.648 12.342 127.614 1.00 44.59 C ANISOU 3042 CD1 TRP B 95 6148 6033 4761 -844 -1589 -304 C ATOM 3043 CD2 TRP B 95 -11.804 10.551 126.929 1.00 48.83 C ANISOU 3043 CD2 TRP B 95 6725 6529 5299 -1177 -1848 -612 C ATOM 3044 NE1 TRP B 95 -9.856 11.647 126.729 1.00 45.86 N ANISOU 3044 NE1 TRP B 95 6495 6129 4802 -851 -1543 -553 N ATOM 3045 CE2 TRP B 95 -10.541 10.546 126.290 1.00 48.79 C ANISOU 3045 CE2 TRP B 95 6908 6461 5171 -1039 -1702 -755 C ATOM 3046 CE3 TRP B 95 -12.710 9.517 126.642 1.00 51.76 C ANISOU 3046 CE3 TRP B 95 7087 6881 5697 -1427 -2026 -781 C ATOM 3047 CZ2 TRP B 95 -10.158 9.546 125.384 1.00 51.64 C ANISOU 3047 CZ2 TRP B 95 7447 6740 5433 -1108 -1721 -1078 C ATOM 3048 CZ3 TRP B 95 -12.327 8.524 125.742 1.00 54.39 C ANISOU 3048 CZ3 TRP B 95 7628 7098 5941 -1514 -2062 -1094 C ATOM 3049 CH2 TRP B 95 -11.063 8.551 125.120 1.00 54.33 C ANISOU 3049 CH2 TRP B 95 7806 7030 5807 -1337 -1907 -1248 C ATOM 3050 N ASP B 96 -13.253 14.836 126.366 1.00 49.27 N ANISOU 3050 N ASP B 96 6427 7337 4956 -726 -2000 98 N ATOM 3051 CA ASP B 96 -13.218 15.007 124.921 1.00 53.45 C ANISOU 3051 CA ASP B 96 7111 8054 5143 -726 -2114 42 C ATOM 3052 C ASP B 96 -11.841 14.630 124.354 1.00 54.53 C ANISOU 3052 C ASP B 96 7505 8074 5141 -736 -1917 -119 C ATOM 3053 O ASP B 96 -10.847 15.328 124.579 1.00 53.78 O ANISOU 3053 O ASP B 96 7497 7887 5049 -615 -1712 -14 O ATOM 3054 CB ASP B 96 -13.603 16.431 124.535 1.00 54.11 C ANISOU 3054 CB ASP B 96 7176 8311 5071 -538 -2208 305 C ATOM 3055 CG ASP B 96 -13.495 16.677 123.055 1.00 56.74 C ANISOU 3055 CG ASP B 96 7711 8845 5001 -544 -2323 298 C ATOM 3056 OD1 ASP B 96 -13.944 15.819 122.277 1.00 59.86 O ANISOU 3056 OD1 ASP B 96 8120 9393 5230 -701 -2485 95 O ATOM 3057 OD2 ASP B 96 -12.970 17.735 122.666 1.00 56.70 O ANISOU 3057 OD2 ASP B 96 7865 8848 4829 -413 -2252 497 O ATOM 3058 N ARG B 97 -11.805 13.515 123.627 1.00 57.75 N ANISOU 3058 N ARG B 97 8014 8494 5437 -889 -1977 -401 N ATOM 3059 CA ARG B 97 -10.592 12.992 122.993 1.00 59.12 C ANISOU 3059 CA ARG B 97 8400 8590 5473 -894 -1798 -633 C ATOM 3060 C ARG B 97 -10.112 13.902 121.876 1.00 61.54 C ANISOU 3060 C ARG B 97 8862 9129 5390 -833 -1743 -554 C ATOM 3061 O ARG B 97 -8.918 14.109 121.699 1.00 61.16 O ANISOU 3061 O ARG B 97 8930 9041 5266 -775 -1502 -602 O ATOM 3062 CB ARG B 97 -10.862 11.594 122.424 1.00 61.62 C ANISOU 3062 CB ARG B 97 8792 8867 5755 -1074 -1908 -984 C ATOM 3063 CG ARG B 97 -12.206 11.464 121.692 1.00 64.10 C ANISOU 3063 CG ARG B 97 9036 9441 5879 -1229 -2212 -1016 C ATOM 3064 CD ARG B 97 -12.713 10.056 121.689 1.00 65.73 C ANISOU 3064 CD ARG B 97 9246 9511 6218 -1454 -2335 -1318 C ATOM 3065 NE ARG B 97 -11.913 9.192 120.837 1.00 67.27 N ANISOU 3065 NE ARG B 97 9675 9627 6256 -1501 -2249 -1683 N ATOM 3066 CZ ARG B 97 -12.086 7.880 120.763 1.00 69.52 C ANISOU 3066 CZ ARG B 97 10041 9705 6667 -1678 -2318 -2005 C ATOM 3067 NH1 ARG B 97 -13.022 7.297 121.495 1.00 69.39 N ANISOU 3067 NH1 ARG B 97 9894 9549 6921 -1863 -2467 -1973 N ATOM 3068 NH2 ARG B 97 -11.328 7.151 119.959 1.00 72.39 N ANISOU 3068 NH2 ARG B 97 10620 9997 6887 -1683 -2229 -2371 N ATOM 3069 N ASP B 98 -11.063 14.489 121.160 1.00 64.85 N ANISOU 3069 N ASP B 98 9272 9807 5562 -848 -1972 -410 N ATOM 3070 CA ASP B 98 -10.787 15.257 119.964 1.00 67.91 C ANISOU 3070 CA ASP B 98 9851 10439 5515 -830 -1977 -313 C ATOM 3071 C ASP B 98 -10.580 16.729 120.248 1.00 67.27 C ANISOU 3071 C ASP B 98 9796 10340 5424 -674 -1907 67 C ATOM 3072 O ASP B 98 -11.027 17.552 119.446 1.00 69.61 O ANISOU 3072 O ASP B 98 10195 10836 5417 -637 -2066 279 O ATOM 3073 CB ASP B 98 -11.940 15.109 118.973 1.00 71.71 C ANISOU 3073 CB ASP B 98 10331 11216 5697 -919 -2311 -344 C ATOM 3074 CG ASP B 98 -11.670 14.059 117.916 1.00 75.16 C ANISOU 3074 CG ASP B 98 10926 11786 5844 -1093 -2317 -723 C ATOM 3075 OD1 ASP B 98 -12.289 12.969 117.970 1.00 76.05 O ANISOU 3075 OD1 ASP B 98 10951 11865 6077 -1234 -2465 -990 O ATOM 3076 OD2 ASP B 98 -10.837 14.330 117.025 1.00 77.20 O ANISOU 3076 OD2 ASP B 98 11404 12185 5745 -1106 -2164 -766 O ATOM 3077 N MET B 99 -9.963 17.064 121.388 1.00 64.34 N ANISOU 3077 N MET B 99 9344 9722 5381 -584 -1700 158 N ATOM 3078 CA AMET B 99 -9.556 18.446 121.628 0.50 63.88 C ANISOU 3078 CA AMET B 99 9354 9603 5315 -467 -1590 470 C ATOM 3079 CA BMET B 99 -9.519 18.426 121.654 0.50 64.10 C ANISOU 3079 CA BMET B 99 9381 9624 5351 -468 -1580 464 C ATOM 3080 C MET B 99 -8.467 18.810 120.619 1.00 66.55 C ANISOU 3080 C MET B 99 9943 10051 5292 -544 -1390 466 C ATOM 3081 O MET B 99 -8.563 19.821 119.911 1.00 69.06 O ANISOU 3081 O MET B 99 10434 10479 5327 -530 -1444 725 O ATOM 3082 CB AMET B 99 -9.057 18.676 123.063 0.50 59.64 C ANISOU 3082 CB AMET B 99 8679 8801 5182 -385 -1405 521 C ATOM 3083 CB BMET B 99 -8.890 18.529 123.037 0.50 60.41 C ANISOU 3083 CB BMET B 99 8785 8892 5275 -401 -1373 478 C ATOM 3084 CG AMET B 99 -10.137 18.609 124.132 0.50 57.62 C ANISOU 3084 CG AMET B 99 8182 8466 5246 -310 -1564 588 C ATOM 3085 CG BMET B 99 -9.847 18.551 124.194 0.50 58.67 C ANISOU 3085 CG BMET B 99 8333 8568 5392 -319 -1504 562 C ATOM 3086 SD AMET B 99 -10.227 20.038 125.232 0.50 55.13 S ANISOU 3086 SD AMET B 99 7788 7989 5172 -129 -1501 880 S ATOM 3087 SD BMET B 99 -8.884 18.619 125.711 0.50 55.28 S ANISOU 3087 SD BMET B 99 7807 7870 5329 -271 -1240 552 S ATOM 3088 CE AMET B 99 -11.113 21.217 124.209 0.50 58.12 C ANISOU 3088 CE AMET B 99 8279 8521 5283 -3 -1750 1158 C ATOM 3089 CE BMET B 99 -8.008 17.050 125.649 0.50 54.49 C ANISOU 3089 CE BMET B 99 7731 7697 5277 -382 -1119 207 C ATOM 3090 OXTAMET B 99 -7.483 18.085 120.473 0.50 66.76 O ANISOU 3090 OXTAMET B 99 10002 10068 5295 -625 -1170 202 O ATOM 3091 OXTBMET B 99 -7.484 18.087 120.452 0.50 66.89 O ANISOU 3091 OXTBMET B 99 10022 10089 5305 -627 -1171 202 O TER 3092 MET B 99 ATOM 3093 N GLU C 1 18.070 14.145 150.440 1.00 34.37 N ANISOU 3093 N GLU C 1 4570 3444 5044 561 -741 -36 N ATOM 3094 CA GLU C 1 18.288 14.315 151.896 1.00 33.86 C ANISOU 3094 CA GLU C 1 4444 3452 4971 529 -838 94 C ATOM 3095 C GLU C 1 17.533 15.496 152.480 1.00 32.54 C ANISOU 3095 C GLU C 1 4275 3412 4677 384 -833 116 C ATOM 3096 O GLU C 1 17.762 16.652 152.095 1.00 31.46 O ANISOU 3096 O GLU C 1 4080 3370 4504 345 -749 49 O ATOM 3097 CB GLU C 1 19.761 14.499 152.174 1.00 35.49 C ANISOU 3097 CB GLU C 1 4487 3751 5247 630 -851 90 C ATOM 3098 CG GLU C 1 20.427 13.280 152.767 1.00 37.87 C ANISOU 3098 CG GLU C 1 4765 3970 5654 777 -951 186 C ATOM 3099 CD GLU C 1 21.464 13.700 153.751 1.00 38.98 C ANISOU 3099 CD GLU C 1 4728 4293 5789 819 -1040 239 C ATOM 3100 OE1 GLU C 1 21.375 14.877 154.182 1.00 37.68 O ANISOU 3100 OE1 GLU C 1 4498 4292 5527 687 -1035 202 O ATOM 3101 OE2 GLU C 1 22.350 12.882 154.093 1.00 41.40 O ANISOU 3101 OE2 GLU C 1 4955 4584 6191 987 -1118 306 O ATOM 3102 N LEU C 2 16.645 15.198 153.430 1.00 31.84 N ANISOU 3102 N LEU C 2 4252 3313 4533 307 -903 215 N ATOM 3103 CA LEU C 2 15.944 16.222 154.191 1.00 29.93 C ANISOU 3103 CA LEU C 2 4003 3196 4175 185 -898 235 C ATOM 3104 C LEU C 2 16.927 16.939 155.094 1.00 29.89 C ANISOU 3104 C LEU C 2 3878 3340 4139 185 -937 235 C ATOM 3105 O LEU C 2 18.022 16.454 155.333 1.00 30.87 O ANISOU 3105 O LEU C 2 3920 3485 4323 281 -1000 259 O ATOM 3106 CB LEU C 2 14.910 15.585 155.095 1.00 30.11 C ANISOU 3106 CB LEU C 2 4108 3188 4144 114 -952 349 C ATOM 3107 CG LEU C 2 13.730 14.818 154.536 1.00 29.61 C ANISOU 3107 CG LEU C 2 4144 2991 4114 61 -930 349 C ATOM 3108 CD1 LEU C 2 13.402 13.774 155.549 1.00 31.16 C ANISOU 3108 CD1 LEU C 2 4404 3110 4325 33 -984 504 C ATOM 3109 CD2 LEU C 2 12.565 15.725 154.380 1.00 28.20 C ANISOU 3109 CD2 LEU C 2 3966 2900 3849 -42 -875 298 C ATOM 3110 N ALA C 3 16.525 18.100 155.597 1.00 28.87 N ANISOU 3110 N ALA C 3 3727 3319 3922 80 -901 193 N ATOM 3111 CA ALA C 3 17.324 18.823 156.557 1.00 28.28 C ANISOU 3111 CA ALA C 3 3540 3400 3806 44 -946 154 C ATOM 3112 C ALA C 3 17.221 18.098 157.876 1.00 29.40 C ANISOU 3112 C ALA C 3 3699 3626 3844 55 -1077 277 C ATOM 3113 O ALA C 3 16.219 17.454 158.176 1.00 29.22 O ANISOU 3113 O ALA C 3 3791 3544 3767 33 -1086 385 O ATOM 3114 CB ALA C 3 16.827 20.246 156.696 1.00 28.20 C ANISOU 3114 CB ALA C 3 3526 3445 3745 -73 -850 53 C ATOM 3115 N GLY C 4 18.285 18.180 158.649 1.00 30.38 N ANISOU 3115 N GLY C 4 3702 3902 3939 90 -1177 268 N ATOM 3116 CA GLY C 4 18.289 17.585 159.938 1.00 30.72 C ANISOU 3116 CA GLY C 4 3759 4068 3843 121 -1310 400 C ATOM 3117 C GLY C 4 18.620 18.664 160.933 1.00 31.47 C ANISOU 3117 C GLY C 4 3755 4401 3802 26 -1355 281 C ATOM 3118 O GLY C 4 18.837 18.376 162.119 1.00 33.47 O ANISOU 3118 O GLY C 4 3987 4837 3892 53 -1485 361 O ATOM 3119 N ILE C 5 18.715 19.900 160.440 1.00 29.50 N ANISOU 3119 N ILE C 5 3444 4146 3617 -79 -1247 89 N ATOM 3120 CA ILE C 5 18.964 21.072 161.280 1.00 30.51 C ANISOU 3120 CA ILE C 5 3485 4457 3651 -202 -1257 -82 C ATOM 3121 C ILE C 5 18.158 22.211 160.713 1.00 30.23 C ANISOU 3121 C ILE C 5 3518 4295 3674 -316 -1074 -206 C ATOM 3122 O ILE C 5 17.592 22.080 159.631 1.00 29.96 O ANISOU 3122 O ILE C 5 3569 4074 3742 -283 -965 -153 O ATOM 3123 CB ILE C 5 20.454 21.551 161.304 1.00 31.00 C ANISOU 3123 CB ILE C 5 3327 4651 3801 -213 -1320 -235 C ATOM 3124 CG1 ILE C 5 20.969 21.879 159.905 1.00 29.06 C ANISOU 3124 CG1 ILE C 5 3024 4232 3786 -209 -1177 -304 C ATOM 3125 CG2 ILE C 5 21.387 20.564 162.001 1.00 32.50 C ANISOU 3125 CG2 ILE C 5 3402 5023 3922 -76 -1528 -127 C ATOM 3126 CD1 ILE C 5 22.460 22.017 159.866 1.00 29.91 C ANISOU 3126 CD1 ILE C 5 2893 4467 4005 -197 -1239 -412 C ATOM 3127 N GLY C 6 18.098 23.322 161.438 1.00 31.62 N ANISOU 3127 N GLY C 6 3659 4575 3780 -439 -1041 -375 N ATOM 3128 CA GLY C 6 17.484 24.541 160.923 1.00 31.84 C ANISOU 3128 CA GLY C 6 3740 4462 3896 -530 -855 -502 C ATOM 3129 C GLY C 6 15.982 24.617 160.774 1.00 31.52 C ANISOU 3129 C GLY C 6 3853 4320 3804 -521 -754 -426 C ATOM 3130 O GLY C 6 15.486 25.495 160.064 1.00 31.97 O ANISOU 3130 O GLY C 6 3956 4228 3964 -543 -599 -484 O ATOM 3131 N ILE C 7 15.267 23.695 161.419 1.00 31.64 N ANISOU 3131 N ILE C 7 3938 4415 3667 -483 -834 -284 N ATOM 3132 CA ILE C 7 13.808 23.699 161.472 1.00 30.88 C ANISOU 3132 CA ILE C 7 3951 4271 3510 -491 -747 -221 C ATOM 3133 C ILE C 7 13.433 23.961 162.921 1.00 33.05 C ANISOU 3133 C ILE C 7 4237 4743 3577 -557 -771 -276 C ATOM 3134 O ILE C 7 13.924 23.293 163.814 1.00 33.94 O ANISOU 3134 O ILE C 7 4330 5024 3542 -545 -903 -209 O ATOM 3135 CB ILE C 7 13.271 22.318 161.102 1.00 30.25 C ANISOU 3135 CB ILE C 7 3937 4127 3428 -420 -799 -13 C ATOM 3136 CG1 ILE C 7 13.867 21.822 159.772 1.00 30.05 C ANISOU 3136 CG1 ILE C 7 3898 3946 3573 -340 -807 28 C ATOM 3137 CG2 ILE C 7 11.760 22.261 161.131 1.00 28.42 C ANISOU 3137 CG2 ILE C 7 3780 3866 3153 -445 -712 44 C ATOM 3138 CD1 ILE C 7 13.357 22.520 158.520 1.00 29.24 C ANISOU 3138 CD1 ILE C 7 3821 3701 3587 -327 -675 -26 C ATOM 3139 N LEU C 8 12.576 24.938 163.164 1.00 33.82 N ANISOU 3139 N LEU C 8 4367 4830 3652 -610 -639 -394 N ATOM 3140 CA LEU C 8 12.199 25.301 164.521 1.00 36.12 C ANISOU 3140 CA LEU C 8 4672 5319 3734 -674 -634 -486 C ATOM 3141 C LEU C 8 10.721 25.678 164.479 1.00 37.33 C ANISOU 3141 C LEU C 8 4886 5414 3881 -672 -477 -481 C ATOM 3142 O LEU C 8 10.216 26.014 163.402 1.00 37.14 O ANISOU 3142 O LEU C 8 4874 5203 4034 -627 -381 -464 O ATOM 3143 CB LEU C 8 13.064 26.476 165.006 1.00 36.43 C ANISOU 3143 CB LEU C 8 4640 5425 3776 -759 -626 -757 C ATOM 3144 CG LEU C 8 12.940 26.918 166.476 1.00 38.12 C ANISOU 3144 CG LEU C 8 4855 5887 3741 -835 -644 -919 C ATOM 3145 CD1 LEU C 8 13.351 25.813 167.430 1.00 38.56 C ANISOU 3145 CD1 LEU C 8 4902 6206 3542 -803 -830 -770 C ATOM 3146 CD2 LEU C 8 13.707 28.159 166.767 1.00 38.85 C ANISOU 3146 CD2 LEU C 8 4875 5994 3890 -942 -614 -1233 C ATOM 3147 N THR C 9 10.022 25.586 165.612 1.00 40.12 N ANISOU 3147 N THR C 9 5271 5947 4026 -706 -450 -482 N ATOM 3148 CA THR C 9 8.623 25.999 165.692 1.00 42.48 C ANISOU 3148 CA THR C 9 5596 6227 4318 -702 -287 -500 C ATOM 3149 C THR C 9 8.446 27.485 165.587 1.00 44.57 C ANISOU 3149 C THR C 9 5850 6400 4684 -709 -143 -741 C ATOM 3150 O THR C 9 9.335 28.245 165.941 1.00 46.01 O ANISOU 3150 O THR C 9 6014 6601 4867 -763 -159 -938 O ATOM 3151 CB THR C 9 7.960 25.621 167.014 1.00 44.46 C ANISOU 3151 CB THR C 9 5876 6713 4303 -744 -261 -461 C ATOM 3152 OG1 THR C 9 8.951 25.376 168.020 1.00 46.48 O ANISOU 3152 OG1 THR C 9 6137 7177 4344 -779 -395 -489 O ATOM 3153 CG2 THR C 9 7.122 24.420 166.837 1.00 43.94 C ANISOU 3153 CG2 THR C 9 5832 6636 4228 -732 -257 -206 C ATOM 3154 N VAL C 10 7.263 27.884 165.140 1.00 33.97 N ATOM 3155 CA VAL C 10 6.955 29.288 164.881 1.00 36.34 C ATOM 3156 C VAL C 10 6.608 30.053 166.167 1.00 37.73 C ATOM 3157 O VAL C 10 6.432 29.441 167.229 1.00 37.79 O ATOM 3158 CB VAL C 10 5.814 29.449 163.826 1.00 36.26 C ATOM 3159 CG1 VAL C 10 6.057 28.550 162.610 1.00 35.83 C ATOM 3160 CG2 VAL C 10 4.441 29.177 164.450 1.00 36.39 C ATOM 3161 OXT VAL C 10 6.512 31.298 166.163 1.00 39.00 O TER 3162 VAL C 10 ATOM 3163 N GLN D 2 25.340 5.287 172.742 1.00 63.57 N ANISOU 3163 N GLN D 2 11276 6629 6247 -1526 -1246 336 N ATOM 3164 CA GLN D 2 26.703 4.920 173.229 1.00 64.87 C ANISOU 3164 CA GLN D 2 11740 6413 6493 -1039 -1508 325 C ATOM 3165 C GLN D 2 27.741 5.216 172.132 1.00 62.82 C ANISOU 3165 C GLN D 2 11188 6243 6439 -271 -1452 85 C ATOM 3166 O GLN D 2 27.855 4.440 171.178 1.00 65.62 O ANISOU 3166 O GLN D 2 11823 6359 6749 -11 -1667 -88 O ATOM 3167 CB GLN D 2 26.698 3.431 173.613 1.00 71.03 C ANISOU 3167 CB GLN D 2 13427 6520 7040 -1261 -2044 403 C ATOM 3168 CG GLN D 2 27.996 2.893 174.211 1.00 73.83 C ANISOU 3168 CG GLN D 2 14203 6421 7428 -753 -2431 372 C ATOM 3169 CD GLN D 2 28.803 2.064 173.212 1.00 76.82 C ANISOU 3169 CD GLN D 2 14926 6409 7855 -40 -2799 76 C ATOM 3170 OE1 GLN D 2 30.039 2.003 173.289 1.00 77.69 O ANISOU 3170 OE1 GLN D 2 15015 6441 8061 655 -2977 -107 O ATOM 3171 NE2 GLN D 2 28.106 1.420 172.272 1.00 78.43 N ANISOU 3171 NE2 GLN D 2 15416 6421 7963 -192 -2927 -14 N ATOM 3172 N LEU D 3 28.471 6.334 172.249 1.00 58.05 N ANISOU 3172 N LEU D 3 10019 6022 6014 43 -1175 62 N ATOM 3173 CA LEU D 3 29.454 6.777 171.217 1.00 55.76 C ANISOU 3173 CA LEU D 3 9344 5996 5847 644 -1066 -144 C ATOM 3174 C LEU D 3 30.923 6.654 171.645 1.00 56.54 C ANISOU 3174 C LEU D 3 9436 6068 5979 1171 -1232 -259 C ATOM 3175 O LEU D 3 31.246 6.870 172.815 1.00 56.55 O ANISOU 3175 O LEU D 3 9475 6010 6001 1074 -1263 -125 O ATOM 3176 CB LEU D 3 29.223 8.243 170.833 1.00 51.69 C ANISOU 3176 CB LEU D 3 8175 6001 5462 559 -648 -85 C ATOM 3177 CG LEU D 3 28.078 8.726 169.938 1.00 50.35 C ANISOU 3177 CG LEU D 3 7779 6058 5294 300 -442 -72 C ATOM 3178 CD1 LEU D 3 28.363 10.151 169.449 1.00 46.87 C ANISOU 3178 CD1 LEU D 3 6791 6041 4978 420 -162 -44 C ATOM 3179 CD2 LEU D 3 27.848 7.771 168.769 1.00 52.67 C ANISOU 3179 CD2 LEU D 3 8325 6203 5483 430 -597 -234 C ATOM 3180 N ASN D 4 31.814 6.355 170.696 1.00 57.35 N ANISOU 3180 N ASN D 4 9426 6305 6058 1736 -1327 -536 N ATOM 3181 CA ASN D 4 33.238 6.123 170.999 1.00 58.63 C ANISOU 3181 CA ASN D 4 9531 6547 6198 2316 -1527 -740 C ATOM 3182 C ASN D 4 34.009 7.405 171.210 1.00 55.10 C ANISOU 3182 C ASN D 4 8423 6680 5831 2354 -1189 -687 C ATOM 3183 O ASN D 4 34.242 8.136 170.269 1.00 53.80 O ANISOU 3183 O ASN D 4 7769 7014 5660 2409 -921 -757 O ATOM 3184 CB ASN D 4 33.910 5.348 169.873 1.00 62.68 C ANISOU 3184 CB ASN D 4 10078 7138 6598 2938 -1755 -1142 C ATOM 3185 CG ASN D 4 33.224 4.038 169.585 1.00 66.63 C ANISOU 3185 CG ASN D 4 11308 7002 7008 2940 -2162 -1231 C ATOM 3186 OD1 ASN D 4 32.413 3.568 170.378 1.00 67.16 O ANISOU 3186 OD1 ASN D 4 11922 6537 7057 2472 -2342 -980 O ATOM 3187 ND2 ASN D 4 33.549 3.432 168.443 1.00 70.07 N ANISOU 3187 ND2 ASN D 4 11762 7517 7344 3429 -2329 -1601 N ATOM 3188 N GLN D 5 34.416 7.663 172.446 1.00 54.05 N ANISOU 3188 N GLN D 5 8316 6477 5744 2284 -1229 -552 N ATOM 3189 CA GLN D 5 35.130 8.889 172.801 1.00 51.07 C ANISOU 3189 CA GLN D 5 7376 6593 5434 2245 -946 -479 C ATOM 3190 C GLN D 5 36.530 8.540 173.276 1.00 54.23 C ANISOU 3190 C GLN D 5 7699 7147 5757 2761 -1173 -691 C ATOM 3191 O GLN D 5 36.687 7.752 174.190 1.00 56.96 O ANISOU 3191 O GLN D 5 8496 7071 6077 2898 -1508 -690 O ATOM 3192 CB GLN D 5 34.381 9.630 173.909 1.00 47.22 C ANISOU 3192 CB GLN D 5 6913 5974 5055 1711 -781 -168 C ATOM 3193 CG GLN D 5 34.921 11.020 174.242 1.00 44.21 C ANISOU 3193 CG GLN D 5 6017 6023 4757 1588 -504 -71 C ATOM 3194 CD GLN D 5 33.900 11.883 174.960 1.00 40.95 C ANISOU 3194 CD GLN D 5 5578 5532 4450 1091 -318 159 C ATOM 3195 OE1 GLN D 5 32.808 11.431 175.283 1.00 41.30 O ANISOU 3195 OE1 GLN D 5 5921 5297 4473 813 -366 239 O ATOM 3196 NE2 GLN D 5 34.238 13.129 175.189 1.00 39.10 N ANISOU 3196 NE2 GLN D 5 4982 5581 4293 968 -128 236 N ATOM 3197 N SER D 6 37.552 9.117 172.658 1.00 55.24 N ANISOU 3197 N SER D 6 7258 7922 5810 3026 -1016 -879 N ATOM 3198 CA SER D 6 38.921 8.802 173.042 1.00 58.96 C ANISOU 3198 CA SER D 6 7545 8694 6163 3556 -1228 -1152 C ATOM 3199 C SER D 6 39.668 10.087 173.296 1.00 57.75 C ANISOU 3199 C SER D 6 6774 9171 5998 3332 -916 -1055 C ATOM 3200 O SER D 6 39.741 10.940 172.417 1.00 58.51 O ANISOU 3200 O SER D 6 6425 9773 6034 3097 -614 -1022 O ATOM 3201 CB SER D 6 39.623 8.013 171.944 1.00 63.40 C ANISOU 3201 CB SER D 6 7969 9588 6531 4194 -1421 -1616 C ATOM 3202 OG SER D 6 39.125 6.686 171.920 1.00 66.48 O ANISOU 3202 OG SER D 6 9054 9286 6920 4492 -1849 -1747 O ATOM 3203 N PRO D 7 40.292 10.219 174.466 1.00 58.10 N ANISOU 3203 N PRO D 7 6808 9204 6061 3388 -1022 -1012 N ATOM 3204 CA PRO D 7 40.627 9.234 175.479 1.00 61.15 C ANISOU 3204 CA PRO D 7 7639 9159 6435 3767 -1441 -1107 C ATOM 3205 C PRO D 7 39.523 9.066 176.502 1.00 59.59 C ANISOU 3205 C PRO D 7 8024 8238 6379 3314 -1511 -750 C ATOM 3206 O PRO D 7 38.451 9.624 176.338 1.00 56.35 O ANISOU 3206 O PRO D 7 7641 7693 6075 2787 -1242 -499 O ATOM 3207 CB PRO D 7 41.855 9.848 176.154 1.00 61.87 C ANISOU 3207 CB PRO D 7 7252 9806 6451 3898 -1401 -1190 C ATOM 3208 CG PRO D 7 42.128 11.131 175.418 1.00 59.65 C ANISOU 3208 CG PRO D 7 6307 10235 6122 3522 -962 -1126 C ATOM 3209 CD PRO D 7 40.863 11.526 174.794 1.00 56.19 C ANISOU 3209 CD PRO D 7 6048 9484 5819 3048 -730 -867 C ATOM 3210 N GLN D 8 39.768 8.269 177.529 1.00 63.41 N ANISOU 3210 N GLN D 8 8973 8297 6822 3520 -1899 -749 N ATOM 3211 CA GLN D 8 38.775 8.083 178.569 1.00 62.77 C ANISOU 3211 CA GLN D 8 9425 7635 6791 3012 -1973 -406 C ATOM 3212 C GLN D 8 39.117 9.042 179.685 1.00 60.61 C ANISOU 3212 C GLN D 8 8852 7609 6567 2739 -1781 -229 C ATOM 3213 O GLN D 8 38.233 9.556 180.375 1.00 57.51 O ANISOU 3213 O GLN D 8 8546 7072 6234 2173 -1592 50 O ATOM 3214 CB GLN D 8 38.796 6.644 179.069 1.00 68.49 C ANISOU 3214 CB GLN D 8 10939 7694 7391 3297 -2564 -454 C ATOM 3215 CG GLN D 8 37.673 6.270 180.028 1.00 69.54 C ANISOU 3215 CG GLN D 8 11698 7247 7477 2657 -2680 -83 C ATOM 3216 CD GLN D 8 37.703 4.787 180.362 1.00 76.49 C ANISOU 3216 CD GLN D 8 13480 7393 8188 2888 -3348 -105 C ATOM 3217 OE1 GLN D 8 38.664 4.287 180.967 1.00 80.62 O ANISOU 3217 OE1 GLN D 8 14238 7762 8632 3381 -3773 -232 O ATOM 3218 NE2 GLN D 8 36.664 4.067 179.942 1.00 77.83 N ANISOU 3218 NE2 GLN D 8 14194 7093 8284 2540 -3491 7 N ATOM 3219 N SER D 9 40.417 9.294 179.827 1.00 62.68 N ANISOU 3219 N SER D 9 8716 8321 6778 3157 -1832 -436 N ATOM 3220 CA SER D 9 40.956 10.123 180.898 1.00 61.71 C ANISOU 3220 CA SER D 9 8312 8459 6676 2975 -1714 -319 C ATOM 3221 C SER D 9 42.308 10.683 180.500 1.00 63.53 C ANISOU 3221 C SER D 9 7874 9434 6829 3324 -1616 -585 C ATOM 3222 O SER D 9 43.166 9.945 180.025 1.00 68.18 O ANISOU 3222 O SER D 9 8383 10241 7281 3948 -1884 -930 O ATOM 3223 CB SER D 9 41.123 9.294 182.170 1.00 63.95 C ANISOU 3223 CB SER D 9 9139 8283 6874 3098 -2136 -243 C ATOM 3224 OG SER D 9 42.083 8.275 181.972 1.00 68.99 O ANISOU 3224 OG SER D 9 9947 8883 7385 3837 -2598 -565 O ATOM 3225 N MET D 10 42.512 11.979 180.693 1.00 61.19 N ANISOU 3225 N MET D 10 7100 9564 6586 2922 -1266 -454 N ATOM 3226 CA MET D 10 43.841 12.534 180.495 1.00 64.05 C ANISOU 3226 CA MET D 10 6833 10692 6812 3119 -1191 -671 C ATOM 3227 C MET D 10 44.274 13.521 181.571 1.00 62.71 C ANISOU 3227 C MET D 10 6430 10731 6667 2775 -1068 -513 C ATOM 3228 O MET D 10 43.480 14.302 182.094 1.00 59.19 O ANISOU 3228 O MET D 10 6114 10005 6369 2252 -877 -229 O ATOM 3229 CB MET D 10 44.012 13.118 179.097 1.00 65.11 C ANISOU 3229 CB MET D 10 6485 11388 6866 3007 -908 -772 C ATOM 3230 CG MET D 10 43.072 14.255 178.765 1.00 62.61 C ANISOU 3230 CG MET D 10 6148 10945 6697 2339 -562 -450 C ATOM 3231 SD MET D 10 42.848 14.416 176.983 1.00 64.50 S ANISOU 3231 SD MET D 10 6133 11536 6837 2278 -361 -534 S ATOM 3232 CE MET D 10 44.490 13.948 176.372 1.00 70.21 C ANISOU 3232 CE MET D 10 6255 13211 7210 2818 -465 -995 C ATOM 3233 N PHE D 11 45.556 13.436 181.902 1.00 66.36 N ANISOU 3233 N PHE D 11 6533 11719 6961 3125 -1214 -750 N ATOM 3234 CA PHE D 11 46.201 14.261 182.900 1.00 66.37 C ANISOU 3234 CA PHE D 11 6265 12015 6936 2876 -1150 -669 C ATOM 3235 C PHE D 11 47.143 15.151 182.127 1.00 67.08 C ANISOU 3235 C PHE D 11 5644 12997 6848 2702 -912 -807 C ATOM 3236 O PHE D 11 48.040 14.659 181.440 1.00 71.52 O ANISOU 3236 O PHE D 11 5814 14180 7181 3152 -1009 -1159 O ATOM 3237 CB PHE D 11 47.009 13.395 183.873 1.00 71.63 C ANISOU 3237 CB PHE D 11 7058 12668 7490 3423 -1553 -859 C ATOM 3238 CG PHE D 11 46.331 12.108 184.237 1.00 74.04 C ANISOU 3238 CG PHE D 11 8104 12179 7848 3758 -1929 -822 C ATOM 3239 CD1 PHE D 11 45.325 12.092 185.185 1.00 71.71 C ANISOU 3239 CD1 PHE D 11 8350 11220 7678 3340 -1945 -478 C ATOM 3240 CD2 PHE D 11 46.702 10.906 183.632 1.00 79.35 C ANISOU 3240 CD2 PHE D 11 8950 12794 8404 4467 -2302 -1149 C ATOM 3241 CE1 PHE D 11 44.679 10.914 185.521 1.00 73.84 C ANISOU 3241 CE1 PHE D 11 9346 10778 7931 3502 -2309 -395 C ATOM 3242 CE2 PHE D 11 46.062 9.718 183.960 1.00 81.33 C ANISOU 3242 CE2 PHE D 11 9999 12222 8678 4702 -2717 -1082 C ATOM 3243 CZ PHE D 11 45.051 9.718 184.910 1.00 78.60 C ANISOU 3243 CZ PHE D 11 10216 11217 8433 4165 -2718 -673 C ATOM 3244 N ILE D 12 46.951 16.458 182.224 1.00 63.13 N ANISOU 3244 N ILE D 12 4982 12594 6409 2037 -634 -553 N ATOM 3245 CA ILE D 12 47.706 17.364 181.376 1.00 63.42 C ANISOU 3245 CA ILE D 12 4441 13421 6233 1690 -417 -603 C ATOM 3246 C ILE D 12 48.355 18.480 182.198 1.00 62.92 C ANISOU 3246 C ILE D 12 4124 13676 6109 1207 -344 -480 C ATOM 3247 O ILE D 12 47.816 18.907 183.209 1.00 60.80 O ANISOU 3247 O ILE D 12 4190 12870 6043 975 -363 -269 O ATOM 3248 CB ILE D 12 46.807 17.837 180.185 1.00 60.58 C ANISOU 3248 CB ILE D 12 4194 12879 5944 1314 -198 -420 C ATOM 3249 CG1 ILE D 12 47.391 17.347 178.865 1.00 64.12 C ANISOU 3249 CG1 ILE D 12 4235 14010 6119 1580 -161 -700 C ATOM 3250 CG2 ILE D 12 46.499 19.333 180.200 1.00 58.38 C ANISOU 3250 CG2 ILE D 12 3928 12529 5726 550 -11 -99 C ATOM 3251 CD1 ILE D 12 46.343 16.899 177.889 1.00 62.46 C ANISOU 3251 CD1 ILE D 12 4341 13362 6027 1663 -112 -649 C ATOM 3252 N GLN D 13 49.545 18.911 181.819 1.00 65.82 N ANISOU 3252 N GLN D 13 3879 14973 6157 1057 -280 -645 N ATOM 3253 CA GLN D 13 50.141 20.027 182.523 1.00 65.77 C ANISOU 3253 CA GLN D 13 3660 15263 6067 498 -221 -509 C ATOM 3254 C GLN D 13 49.558 21.340 182.035 1.00 63.14 C ANISOU 3254 C GLN D 13 3497 14697 5795 -307 -39 -160 C ATOM 3255 O GLN D 13 49.200 21.482 180.864 1.00 62.53 O ANISOU 3255 O GLN D 13 3414 14691 5654 -494 79 -91 O ATOM 3256 CB GLN D 13 51.664 20.016 182.404 1.00 71.93 C ANISOU 3256 CB GLN D 13 3699 17202 6429 565 -243 -822 C ATOM 3257 CG GLN D 13 52.361 19.115 183.427 1.00 74.45 C ANISOU 3257 CG GLN D 13 3906 17674 6710 1261 -510 -1123 C ATOM 3258 CD GLN D 13 52.775 19.853 184.698 1.00 74.85 C ANISOU 3258 CD GLN D 13 3937 17721 6781 908 -553 -991 C ATOM 3259 OE1 GLN D 13 52.371 20.994 184.938 1.00 72.38 O ANISOU 3259 OE1 GLN D 13 3820 17101 6581 188 -412 -665 O ATOM 3260 NE2 GLN D 13 53.593 19.197 185.521 1.00 78.32 N ANISOU 3260 NE2 GLN D 13 4164 18490 7102 1453 -792 -1270 N ATOM 3261 N GLU D 14 49.460 22.280 182.967 1.00 61.54 N ANISOU 3261 N GLU D 14 3488 14184 5709 -745 -63 42 N ATOM 3262 CA GLU D 14 48.842 23.586 182.769 1.00 60.09 C ANISOU 3262 CA GLU D 14 3617 13587 5627 -1442 -9 358 C ATOM 3263 C GLU D 14 49.582 24.442 181.738 1.00 63.42 C ANISOU 3263 C GLU D 14 3704 14703 5690 -2108 75 455 C ATOM 3264 O GLU D 14 50.803 24.546 181.772 1.00 67.67 O ANISOU 3264 O GLU D 14 3711 16120 5879 -2300 92 319 O ATOM 3265 CB GLU D 14 48.785 24.306 184.123 1.00 59.69 C ANISOU 3265 CB GLU D 14 3796 13154 5728 -1667 -114 453 C ATOM 3266 CG GLU D 14 48.244 25.723 184.102 1.00 59.82 C ANISOU 3266 CG GLU D 14 4187 12698 5842 -2322 -162 717 C ATOM 3267 CD GLU D 14 48.698 26.537 185.300 1.00 61.54 C ANISOU 3267 CD GLU D 14 4453 12870 6060 -2636 -283 740 C ATOM 3268 OE1 GLU D 14 49.341 25.971 186.213 1.00 62.26 O ANISOU 3268 OE1 GLU D 14 4290 13268 6100 -2332 -306 570 O ATOM 3269 OE2 GLU D 14 48.407 27.750 185.328 1.00 62.70 O ANISOU 3269 OE2 GLU D 14 4930 12641 6250 -3172 -396 919 O ATOM 3270 N GLY D 15 48.831 25.032 180.814 1.00 61.66 N ANISOU 3270 N GLY D 15 3788 14126 5515 -2481 111 687 N ATOM 3271 CA GLY D 15 49.399 25.859 179.774 1.00 65.41 C ANISOU 3271 CA GLY D 15 4060 15177 5616 -3212 158 848 C ATOM 3272 C GLY D 15 49.488 25.118 178.452 1.00 67.30 C ANISOU 3272 C GLY D 15 3977 15966 5628 -3007 302 718 C ATOM 3273 O GLY D 15 49.536 25.725 177.383 1.00 70.12 O ANISOU 3273 O GLY D 15 4317 16603 5721 -3590 345 908 O ATOM 3274 N GLU D 16 49.503 23.795 178.517 1.00 66.14 N ANISOU 3274 N GLU D 16 3616 15954 5561 -2183 339 391 N ATOM 3275 CA GLU D 16 49.500 22.994 177.311 1.00 67.38 C ANISOU 3275 CA GLU D 16 3512 16553 5536 -1869 442 204 C ATOM 3276 C GLU D 16 48.104 22.837 176.737 1.00 63.52 C ANISOU 3276 C GLU D 16 3576 15193 5367 -1726 449 379 C ATOM 3277 O GLU D 16 47.122 23.315 177.314 1.00 59.34 O ANISOU 3277 O GLU D 16 3596 13753 5196 -1819 370 609 O ATOM 3278 CB GLU D 16 50.089 21.631 177.593 1.00 68.40 C ANISOU 3278 CB GLU D 16 3263 17117 5608 -996 392 -254 C ATOM 3279 CG GLU D 16 51.568 21.669 177.774 1.00 73.94 C ANISOU 3279 CG GLU D 16 3239 18984 5872 -1066 399 -532 C ATOM 3280 CD GLU D 16 52.106 20.307 178.064 1.00 75.90 C ANISOU 3280 CD GLU D 16 3180 19582 6077 -81 259 -1031 C ATOM 3281 OE1 GLU D 16 51.295 19.447 178.501 1.00 71.96 O ANISOU 3281 OE1 GLU D 16 3190 18193 5957 552 113 -1061 O ATOM 3282 OE2 GLU D 16 53.321 20.104 177.851 1.00 81.20 O ANISOU 3282 OE2 GLU D 16 3120 21425 6307 44 263 -1401 O ATOM 3283 N ASP D 17 48.026 22.158 175.593 1.00 65.21 N ANISOU 3283 N ASP D 17 3598 15757 5420 -1476 535 224 N ATOM 3284 CA ASP D 17 46.752 21.963 174.894 1.00 62.22 C ANISOU 3284 CA ASP D 17 3675 14678 5287 -1358 549 363 C ATOM 3285 C ASP D 17 46.144 20.570 175.108 1.00 58.97 C ANISOU 3285 C ASP D 17 3446 13822 5140 -513 488 106 C ATOM 3286 O ASP D 17 46.845 19.592 175.386 1.00 60.80 O ANISOU 3286 O ASP D 17 3386 14447 5269 56 422 -241 O ATOM 3287 CB ASP D 17 46.882 22.261 173.391 1.00 66.33 C ANISOU 3287 CB ASP D 17 3982 15770 5452 -1766 664 433 C ATOM 3288 CG ASP D 17 47.761 23.479 173.098 1.00 71.99 C ANISOU 3288 CG ASP D 17 4444 17157 5751 -2676 696 658 C ATOM 3289 OD1 ASP D 17 47.833 24.390 173.955 1.00 72.09 O ANISOU 3289 OD1 ASP D 17 4700 16818 5874 -3101 591 887 O ATOM 3290 OD2 ASP D 17 48.385 23.528 172.011 1.00 76.31 O ANISOU 3290 OD2 ASP D 17 4557 18612 5824 -3009 810 601 O ATOM 3291 N VAL D 18 44.822 20.499 174.990 1.00 54.46 N ANISOU 3291 N VAL D 18 3388 12418 4885 -448 469 273 N ATOM 3292 CA VAL D 18 44.085 19.268 175.219 1.00 51.55 C ANISOU 3292 CA VAL D 18 3302 11529 4754 187 387 106 C ATOM 3293 C VAL D 18 43.369 18.910 173.936 1.00 50.54 C ANISOU 3293 C VAL D 18 3273 11330 4599 251 450 98 C ATOM 3294 O VAL D 18 42.792 19.775 173.323 1.00 48.74 O ANISOU 3294 O VAL D 18 3188 10947 4385 -205 519 350 O ATOM 3295 CB VAL D 18 42.972 19.458 176.269 1.00 47.34 C ANISOU 3295 CB VAL D 18 3285 10109 4594 155 316 298 C ATOM 3296 CG1 VAL D 18 42.680 18.147 176.939 1.00 46.50 C ANISOU 3296 CG1 VAL D 18 3405 9643 4622 723 180 118 C ATOM 3297 CG2 VAL D 18 43.335 20.517 177.305 1.00 47.32 C ANISOU 3297 CG2 VAL D 18 3278 10063 4637 -229 292 454 C ATOM 3298 N SER D 19 43.393 17.642 173.543 1.00 51.64 N ANISOU 3298 N SER D 19 3383 11541 4696 831 383 -199 N ATOM 3299 CA SER D 19 42.648 17.189 172.376 1.00 51.40 C ANISOU 3299 CA SER D 19 3483 11394 4655 934 424 -235 C ATOM 3300 C SER D 19 41.831 15.958 172.735 1.00 49.87 C ANISOU 3300 C SER D 19 3727 10528 4693 1444 260 -362 C ATOM 3301 O SER D 19 42.310 15.088 173.457 1.00 51.69 O ANISOU 3301 O SER D 19 4009 10701 4932 1905 74 -580 O ATOM 3302 CB SER D 19 43.595 16.854 171.219 1.00 56.12 C ANISOU 3302 CB SER D 19 3559 12916 4849 1084 488 -530 C ATOM 3303 OG SER D 19 42.863 16.380 170.101 1.00 55.43 O ANISOU 3303 OG SER D 19 3610 12707 4746 1202 518 -582 O ATOM 3304 N MET D 20 40.581 15.905 172.277 1.00 47.48 N ANISOU 3304 N MET D 20 3777 9705 4559 1323 292 -211 N ATOM 3305 CA MET D 20 39.719 14.726 172.452 1.00 46.78 C ANISOU 3305 CA MET D 20 4126 9020 4627 1676 133 -307 C ATOM 3306 C MET D 20 38.884 14.566 171.204 1.00 45.80 C ANISOU 3306 C MET D 20 4094 8826 4481 1616 206 -299 C ATOM 3307 O MET D 20 38.562 15.557 170.560 1.00 44.12 O ANISOU 3307 O MET D 20 3764 8755 4243 1211 367 -101 O ATOM 3308 CB MET D 20 38.712 14.905 173.591 1.00 44.56 C ANISOU 3308 CB MET D 20 4251 8070 4610 1457 96 -75 C ATOM 3309 CG MET D 20 39.129 15.766 174.750 1.00 45.21 C ANISOU 3309 CG MET D 20 4241 8174 4761 1223 125 68 C ATOM 3310 SD MET D 20 37.720 16.653 175.400 1.00 42.95 S ANISOU 3310 SD MET D 20 4240 7365 4716 793 199 336 S ATOM 3311 CE MET D 20 38.588 17.884 176.363 1.00 44.04 C ANISOU 3311 CE MET D 20 4156 7719 4860 528 230 444 C ATOM 3312 N ASN D 21 38.465 13.342 170.902 1.00 46.34 N ANISOU 3312 N ASN D 21 4442 8606 4559 1989 47 -494 N ATOM 3313 CA ASN D 21 37.605 13.119 169.750 1.00 46.16 C ANISOU 3313 CA ASN D 21 4531 8492 4517 1933 102 -499 C ATOM 3314 C ASN D 21 36.557 12.046 169.928 1.00 45.44 C ANISOU 3314 C ASN D 21 4959 7754 4554 2067 -78 -532 C ATOM 3315 O ASN D 21 36.692 11.163 170.779 1.00 45.61 O ANISOU 3315 O ASN D 21 5294 7421 4614 2319 -316 -623 O ATOM 3316 CB ASN D 21 38.439 12.759 168.535 1.00 50.20 C ANISOU 3316 CB ASN D 21 4681 9651 4740 2226 118 -802 C ATOM 3317 CG ASN D 21 39.577 11.860 168.883 1.00 54.28 C ANISOU 3317 CG ASN D 21 5072 10437 5114 2809 -97 -1182 C ATOM 3318 OD1 ASN D 21 39.383 10.718 169.311 1.00 55.76 O ANISOU 3318 OD1 ASN D 21 5675 10130 5381 3225 -386 -1357 O ATOM 3319 ND2 ASN D 21 40.785 12.373 168.731 1.00 57.12 N ANISOU 3319 ND2 ASN D 21 4876 11594 5231 2829 3 -1319 N ATOM 3320 N CYS D 22 35.543 12.113 169.069 1.00 44.17 N ANISOU 3320 N CYS D 22 4901 7465 4417 1870 8 -455 N ATOM 3321 CA CYS D 22 34.492 11.121 169.035 1.00 44.16 C ANISOU 3321 CA CYS D 22 5360 6941 4479 1900 -147 -487 C ATOM 3322 C CYS D 22 34.444 10.410 167.719 1.00 46.38 C ANISOU 3322 C CYS D 22 5650 7360 4613 2152 -206 -725 C ATOM 3323 O CYS D 22 34.861 10.945 166.703 1.00 47.88 O ANISOU 3323 O CYS D 22 5458 8071 4664 2158 -45 -784 O ATOM 3324 CB CYS D 22 33.134 11.735 169.339 1.00 41.30 C ANISOU 3324 CB CYS D 22 5132 6292 4267 1431 -24 -221 C ATOM 3325 SG CYS D 22 32.919 11.942 171.135 1.00 41.52 S ANISOU 3325 SG CYS D 22 5346 5997 4432 1210 -74 -44 S ATOM 3326 N THR D 23 33.924 9.193 167.744 1.00 47.66 N ANISOU 3326 N THR D 23 6282 7052 4773 2318 -461 -855 N ATOM 3327 CA THR D 23 33.759 8.406 166.538 1.00 49.13 C ANISOU 3327 CA THR D 23 6564 7277 4825 2570 -567 -1111 C ATOM 3328 C THR D 23 32.359 7.832 166.519 1.00 48.37 C ANISOU 3328 C THR D 23 6941 6640 4796 2258 -662 -990 C ATOM 3329 O THR D 23 31.820 7.460 167.558 1.00 48.01 O ANISOU 3329 O THR D 23 7288 6124 4829 2026 -803 -835 O ATOM 3330 CB THR D 23 34.888 7.346 166.406 1.00 53.64 C ANISOU 3330 CB THR D 23 7218 7922 5243 3246 -887 -1536 C ATOM 3331 OG1 THR D 23 35.776 7.771 165.373 1.00 55.21 O ANISOU 3331 OG1 THR D 23 6833 8906 5239 3490 -716 -1775 O ATOM 3332 CG2 THR D 23 34.385 5.921 166.068 1.00 56.67 C ANISOU 3332 CG2 THR D 23 8214 7742 5576 3510 -1276 -1767 C ATOM 3333 N SER D 24 31.735 7.827 165.350 1.00 48.81 N ANISOU 3333 N SER D 24 6928 6832 4784 2177 -569 -1044 N ATOM 3334 CA SER D 24 30.463 7.148 165.218 1.00 49.28 C ANISOU 3334 CA SER D 24 7418 6452 4855 1895 -689 -990 C ATOM 3335 C SER D 24 30.432 6.199 164.029 1.00 51.90 C ANISOU 3335 C SER D 24 7931 6753 5035 2193 -871 -1297 C ATOM 3336 O SER D 24 31.383 6.107 163.250 1.00 54.40 O ANISOU 3336 O SER D 24 7983 7462 5224 2649 -882 -1582 O ATOM 3337 CB SER D 24 29.319 8.152 165.127 1.00 46.62 C ANISOU 3337 CB SER D 24 6863 6246 4603 1387 -409 -717 C ATOM 3338 OG SER D 24 28.086 7.497 165.367 1.00 48.05 O ANISOU 3338 OG SER D 24 7430 6058 4769 1031 -527 -652 O ATOM 3339 N SER D 25 29.325 5.483 163.917 1.00 51.86 N ANISOU 3339 N SER D 25 8364 6330 5010 1908 -1022 -1261 N ATOM 3340 CA SER D 25 29.103 4.564 162.828 1.00 54.53 C ANISOU 3340 CA SER D 25 8950 6560 5209 2114 -1222 -1538 C ATOM 3341 C SER D 25 27.887 5.032 162.026 1.00 52.21 C ANISOU 3341 C SER D 25 8482 6455 4901 1679 -988 -1399 C ATOM 3342 O SER D 25 27.704 4.688 160.849 1.00 53.17 O ANISOU 3342 O SER D 25 8584 6717 4900 1818 -1016 -1603 O ATOM 3343 CB SER D 25 28.868 3.178 163.393 1.00 58.30 C ANISOU 3343 CB SER D 25 10213 6306 5634 2123 -1702 -1627 C ATOM 3344 OG SER D 25 27.941 2.484 162.591 1.00 60.66 O ANISOU 3344 OG SER D 25 10838 6383 5827 1919 -1840 -1713 O ATOM 3345 N SER D 26 27.055 5.826 162.682 1.00 48.64 N ANISOU 3345 N SER D 26 7885 6040 4555 1187 -776 -1086 N ATOM 3346 CA SER D 26 25.961 6.474 162.009 1.00 47.58 C ANISOU 3346 CA SER D 26 7495 6171 4414 847 -559 -971 C ATOM 3347 C SER D 26 26.330 7.924 161.772 1.00 44.68 C ANISOU 3347 C SER D 26 6571 6283 4124 895 -259 -829 C ATOM 3348 O SER D 26 27.044 8.529 162.587 1.00 43.39 O ANISOU 3348 O SER D 26 6255 6175 4059 959 -185 -719 O ATOM 3349 CB SER D 26 24.676 6.365 162.830 1.00 47.65 C ANISOU 3349 CB SER D 26 7698 5977 4432 287 -575 -790 C ATOM 3350 OG SER D 26 24.972 6.067 164.184 1.00 49.24 O ANISOU 3350 OG SER D 26 8162 5872 4673 173 -699 -682 O ATOM 3351 N ILE D 27 25.863 8.440 160.633 1.00 43.50 N ANISOU 3351 N ILE D 27 6174 6449 3905 846 -131 -829 N ATOM 3352 CA ILE D 27 25.947 9.846 160.257 1.00 41.19 C ANISOU 3352 CA ILE D 27 5469 6538 3644 785 79 -649 C ATOM 3353 C ILE D 27 25.120 10.697 161.243 1.00 39.33 C ANISOU 3353 C ILE D 27 5165 6211 3567 490 144 -438 C ATOM 3354 O ILE D 27 23.986 10.325 161.555 1.00 40.50 O ANISOU 3354 O ILE D 27 5445 6225 3717 246 93 -452 O ATOM 3355 CB ILE D 27 25.408 10.014 158.786 1.00 41.99 C ANISOU 3355 CB ILE D 27 5440 6919 3596 761 120 -698 C ATOM 3356 CG1 ILE D 27 26.471 9.608 157.746 1.00 44.65 C ANISOU 3356 CG1 ILE D 27 5669 7567 3730 1076 118 -907 C ATOM 3357 CG2 ILE D 27 24.895 11.422 158.490 1.00 39.70 C ANISOU 3357 CG2 ILE D 27 4892 6851 3342 576 229 -465 C ATOM 3358 CD1 ILE D 27 26.258 8.230 157.101 1.00 47.13 C ANISOU 3358 CD1 ILE D 27 6262 7729 3915 1259 -58 -1221 C ATOM 3359 N PHE D 28 25.689 11.790 161.771 1.00 37.30 N ANISOU 3359 N PHE D 28 4701 6062 3408 501 235 -276 N ATOM 3360 CA PHE D 28 24.894 12.809 162.478 1.00 35.72 C ANISOU 3360 CA PHE D 28 4390 5846 3336 308 268 -134 C ATOM 3361 C PHE D 28 24.886 14.176 161.792 1.00 35.40 C ANISOU 3361 C PHE D 28 4148 6007 3296 308 291 12 C ATOM 3362 O PHE D 28 25.781 14.497 161.009 1.00 36.54 O ANISOU 3362 O PHE D 28 4208 6341 3334 375 324 77 O ATOM 3363 CB PHE D 28 25.362 12.978 163.913 1.00 35.64 C ANISOU 3363 CB PHE D 28 4409 5681 3451 279 277 -69 C ATOM 3364 CG PHE D 28 25.131 11.771 164.765 1.00 36.96 C ANISOU 3364 CG PHE D 28 4849 5596 3598 177 194 -154 C ATOM 3365 CD1 PHE D 28 23.860 11.218 164.875 1.00 37.88 C ANISOU 3365 CD1 PHE D 28 5079 5673 3640 -96 148 -213 C ATOM 3366 CD2 PHE D 28 26.177 11.186 165.457 1.00 37.20 C ANISOU 3366 CD2 PHE D 28 5041 5449 3642 320 128 -169 C ATOM 3367 CE1 PHE D 28 23.633 10.094 165.662 1.00 39.40 C ANISOU 3367 CE1 PHE D 28 5601 5616 3752 -313 29 -241 C ATOM 3368 CE2 PHE D 28 25.957 10.075 166.248 1.00 39.26 C ANISOU 3368 CE2 PHE D 28 5659 5403 3854 191 -23 -208 C ATOM 3369 CZ PHE D 28 24.679 9.519 166.345 1.00 39.92 C ANISOU 3369 CZ PHE D 28 5915 5412 3842 -170 -78 -222 C ATOM 3370 N ASN D 29 23.889 14.998 162.106 1.00 34.49 N ANISOU 3370 N ASN D 29 3967 5875 3261 226 239 50 N ATOM 3371 CA ASN D 29 23.736 16.282 161.410 1.00 34.85 C ANISOU 3371 CA ASN D 29 3941 6006 3293 247 151 186 C ATOM 3372 C ASN D 29 24.066 17.473 162.272 1.00 34.34 C ANISOU 3372 C ASN D 29 3869 5819 3361 250 79 311 C ATOM 3373 O ASN D 29 24.231 18.568 161.764 1.00 35.45 O ANISOU 3373 O ASN D 29 4055 5939 3474 236 -52 470 O ATOM 3374 CB ASN D 29 22.334 16.434 160.811 1.00 35.32 C ANISOU 3374 CB ASN D 29 3959 6150 3310 258 46 86 C ATOM 3375 CG ASN D 29 22.000 15.323 159.843 1.00 35.79 C ANISOU 3375 CG ASN D 29 4048 6332 3220 223 95 -32 C ATOM 3376 OD1 ASN D 29 22.733 15.099 158.870 1.00 36.86 O ANISOU 3376 OD1 ASN D 29 4212 6566 3225 252 132 20 O ATOM 3377 ND2 ASN D 29 20.903 14.609 160.102 1.00 35.19 N ANISOU 3377 ND2 ASN D 29 3953 6298 3120 128 88 -209 N ATOM 3378 N THR D 30 24.131 17.256 163.578 1.00 33.85 N ANISOU 3378 N THR D 30 3792 5652 3419 240 130 245 N ATOM 3379 CA THR D 30 24.702 18.227 164.492 1.00 34.16 C ANISOU 3379 CA THR D 30 3834 5571 3575 243 80 346 C ATOM 3380 C THR D 30 25.697 17.513 165.357 1.00 33.40 C ANISOU 3380 C THR D 30 3743 5440 3508 212 211 350 C ATOM 3381 O THR D 30 25.467 16.369 165.781 1.00 32.80 O ANISOU 3381 O THR D 30 3710 5340 3413 195 277 230 O ATOM 3382 CB THR D 30 23.714 18.704 165.525 1.00 35.10 C ANISOU 3382 CB THR D 30 3888 5646 3803 298 -5 198 C ATOM 3383 OG1 THR D 30 22.381 18.577 165.037 1.00 37.13 O ANISOU 3383 OG1 THR D 30 4060 6049 3999 352 -75 28 O ATOM 3384 CG2 THR D 30 23.999 20.119 165.872 1.00 36.23 C ANISOU 3384 CG2 THR D 30 4095 5632 4040 369 -185 288 C ATOM 3385 N TRP D 31 26.787 18.195 165.668 1.00 33.24 N ANISOU 3385 N TRP D 31 3713 5403 3512 182 209 491 N ATOM 3386 CA TRP D 31 27.627 17.720 166.739 1.00 32.58 C ANISOU 3386 CA TRP D 31 3616 5285 3478 191 289 473 C ATOM 3387 C TRP D 31 27.692 18.758 167.855 1.00 32.47 C ANISOU 3387 C TRP D 31 3597 5144 3595 147 219 524 C ATOM 3388 O TRP D 31 27.860 19.948 167.595 1.00 33.70 O ANISOU 3388 O TRP D 31 3789 5251 3766 89 101 648 O ATOM 3389 CB TRP D 31 28.996 17.310 166.221 1.00 32.94 C ANISOU 3389 CB TRP D 31 3592 5531 3394 226 364 513 C ATOM 3390 CG TRP D 31 28.959 16.083 165.345 1.00 33.45 C ANISOU 3390 CG TRP D 31 3679 5700 3330 356 403 369 C ATOM 3391 CD1 TRP D 31 28.537 16.019 164.060 1.00 34.09 C ANISOU 3391 CD1 TRP D 31 3744 5918 3289 348 401 356 C ATOM 3392 CD2 TRP D 31 29.361 14.749 165.698 1.00 33.61 C ANISOU 3392 CD2 TRP D 31 3793 5658 3320 534 396 200 C ATOM 3393 NE1 TRP D 31 28.651 14.744 163.580 1.00 34.84 N ANISOU 3393 NE1 TRP D 31 3893 6061 3284 512 412 168 N ATOM 3394 CE2 TRP D 31 29.155 13.942 164.570 1.00 34.59 C ANISOU 3394 CE2 TRP D 31 3960 5874 3310 643 381 66 C ATOM 3395 CE3 TRP D 31 29.859 14.159 166.866 1.00 33.36 C ANISOU 3395 CE3 TRP D 31 3861 5466 3350 622 353 147 C ATOM 3396 CZ2 TRP D 31 29.439 12.582 164.565 1.00 35.88 C ANISOU 3396 CZ2 TRP D 31 4296 5931 3407 865 292 -140 C ATOM 3397 CZ3 TRP D 31 30.150 12.814 166.855 1.00 34.63 C ANISOU 3397 CZ3 TRP D 31 4210 5509 3437 833 250 -29 C ATOM 3398 CH2 TRP D 31 29.940 12.039 165.710 1.00 35.92 C ANISOU 3398 CH2 TRP D 31 4448 5724 3476 967 204 -182 C ATOM 3399 N LEU D 32 27.504 18.304 169.090 1.00 31.83 N ANISOU 3399 N LEU D 32 3516 4994 3585 150 257 427 N ATOM 3400 CA LEU D 32 27.597 19.174 170.262 1.00 31.95 C ANISOU 3400 CA LEU D 32 3508 4925 3707 129 200 428 C ATOM 3401 C LEU D 32 28.716 18.718 171.177 1.00 30.94 C ANISOU 3401 C LEU D 32 3376 4795 3584 105 273 472 C ATOM 3402 O LEU D 32 29.002 17.530 171.241 1.00 30.12 O ANISOU 3402 O LEU D 32 3323 4704 3415 139 332 434 O ATOM 3403 CB LEU D 32 26.314 19.095 171.085 1.00 32.20 C ANISOU 3403 CB LEU D 32 3485 4989 3762 130 179 236 C ATOM 3404 CG LEU D 32 24.962 19.371 170.467 1.00 32.96 C ANISOU 3404 CG LEU D 32 3511 5184 3826 199 95 88 C ATOM 3405 CD1 LEU D 32 24.005 19.445 171.593 1.00 33.21 C ANISOU 3405 CD1 LEU D 32 3393 5389 3835 184 87 -140 C ATOM 3406 CD2 LEU D 32 24.983 20.677 169.729 1.00 34.48 C ANISOU 3406 CD2 LEU D 32 3770 5253 4077 331 -101 155 C ATOM 3407 N TRP D 33 29.306 19.656 171.917 1.00 31.27 N ANISOU 3407 N TRP D 33 3393 4791 3696 64 222 533 N ATOM 3408 CA TRP D 33 30.283 19.320 172.963 1.00 30.92 C ANISOU 3408 CA TRP D 33 3324 4767 3658 50 270 552 C ATOM 3409 C TRP D 33 29.884 19.926 174.300 1.00 30.73 C ANISOU 3409 C TRP D 33 3292 4663 3720 12 220 478 C ATOM 3410 O TRP D 33 29.586 21.118 174.376 1.00 31.91 O ANISOU 3410 O TRP D 33 3452 4733 3941 10 102 462 O ATOM 3411 CB TRP D 33 31.691 19.785 172.590 1.00 31.65 C ANISOU 3411 CB TRP D 33 3335 4998 3691 -5 276 686 C ATOM 3412 CG TRP D 33 32.423 18.847 171.680 1.00 32.88 C ANISOU 3412 CG TRP D 33 3413 5377 3704 92 352 671 C ATOM 3413 CD1 TRP D 33 32.539 18.950 170.330 1.00 34.34 C ANISOU 3413 CD1 TRP D 33 3541 5741 3766 56 373 718 C ATOM 3414 CD2 TRP D 33 33.151 17.660 172.054 1.00 33.71 C ANISOU 3414 CD2 TRP D 33 3496 5567 3745 283 375 564 C ATOM 3415 NE1 TRP D 33 33.300 17.911 169.835 1.00 35.89 N ANISOU 3415 NE1 TRP D 33 3628 6190 3820 232 432 605 N ATOM 3416 CE2 TRP D 33 33.684 17.106 170.874 1.00 35.30 C ANISOU 3416 CE2 TRP D 33 3594 6027 3790 410 407 498 C ATOM 3417 CE3 TRP D 33 33.415 17.024 173.272 1.00 33.22 C ANISOU 3417 CE3 TRP D 33 3515 5386 3720 377 333 505 C ATOM 3418 CZ2 TRP D 33 34.456 15.940 170.877 1.00 36.96 C ANISOU 3418 CZ2 TRP D 33 3781 6364 3898 705 367 323 C ATOM 3419 CZ3 TRP D 33 34.177 15.873 173.271 1.00 34.25 C ANISOU 3419 CZ3 TRP D 33 3678 5581 3753 634 271 385 C ATOM 3420 CH2 TRP D 33 34.689 15.339 172.084 1.00 36.10 C ANISOU 3420 CH2 TRP D 33 3809 6057 3849 834 274 270 C ATOM 3421 N TYR D 34 29.895 19.109 175.349 1.00 30.02 N ANISOU 3421 N TYR D 34 3221 4588 3599 -13 270 421 N ATOM 3422 CA TYR D 34 29.506 19.560 176.687 1.00 30.77 C ANISOU 3422 CA TYR D 34 3273 4698 3720 -73 244 324 C ATOM 3423 C TYR D 34 30.638 19.502 177.720 1.00 30.70 C ANISOU 3423 C TYR D 34 3269 4683 3712 -102 247 392 C ATOM 3424 O TYR D 34 31.515 18.645 177.634 1.00 31.36 O ANISOU 3424 O TYR D 34 3408 4766 3742 -56 266 472 O ATOM 3425 CB TYR D 34 28.391 18.676 177.227 1.00 31.65 C ANISOU 3425 CB TYR D 34 3397 4915 3715 -190 290 204 C ATOM 3426 CG TYR D 34 27.033 18.853 176.591 1.00 32.56 C ANISOU 3426 CG TYR D 34 3419 5157 3794 -185 282 54 C ATOM 3427 CD1 TYR D 34 26.702 18.186 175.413 1.00 32.18 C ANISOU 3427 CD1 TYR D 34 3439 5083 3704 -181 304 93 C ATOM 3428 CD2 TYR D 34 26.057 19.640 177.204 1.00 33.43 C ANISOU 3428 CD2 TYR D 34 3349 5471 3884 -155 235 -176 C ATOM 3429 CE1 TYR D 34 25.461 18.316 174.857 1.00 33.03 C ANISOU 3429 CE1 TYR D 34 3438 5352 3759 -178 288 -56 C ATOM 3430 CE2 TYR D 34 24.809 19.785 176.640 1.00 34.29 C ANISOU 3430 CE2 TYR D 34 3319 5780 3931 -99 204 -368 C ATOM 3431 CZ TYR D 34 24.522 19.120 175.466 1.00 34.15 C ANISOU 3431 CZ TYR D 34 3373 5723 3879 -129 236 -289 C ATOM 3432 OH TYR D 34 23.286 19.248 174.889 1.00 35.80 O ANISOU 3432 OH TYR D 34 3423 6168 4011 -74 196 -488 O ATOM 3433 N LYS D 35 30.585 20.377 178.722 1.00 30.01 N ANISOU 3433 N LYS D 35 3122 4608 3672 -136 199 319 N ATOM 3434 CA LYS D 35 31.487 20.299 179.874 1.00 30.17 C ANISOU 3434 CA LYS D 35 3137 4655 3673 -184 197 358 C ATOM 3435 C LYS D 35 30.676 19.983 181.135 1.00 30.73 C ANISOU 3435 C LYS D 35 3191 4839 3647 -294 216 226 C ATOM 3436 O LYS D 35 29.587 20.537 181.312 1.00 31.25 O ANISOU 3436 O LYS D 35 3155 5018 3700 -295 202 40 O ATOM 3437 CB LYS D 35 32.244 21.632 180.016 1.00 31.25 C ANISOU 3437 CB LYS D 35 3229 4741 3903 -196 109 390 C ATOM 3438 CG LYS D 35 32.697 22.059 181.406 1.00 31.54 C ANISOU 3438 CG LYS D 35 3229 4813 3940 -252 70 337 C ATOM 3439 CD LYS D 35 34.187 21.921 181.617 1.00 31.84 C ANISOU 3439 CD LYS D 35 3226 4923 3949 -295 76 476 C ATOM 3440 CE LYS D 35 34.678 23.036 182.561 1.00 32.71 C ANISOU 3440 CE LYS D 35 3312 5016 4100 -392 -21 437 C ATOM 3441 NZ LYS D 35 35.548 22.495 183.626 1.00 32.34 N ANISOU 3441 NZ LYS D 35 3200 5109 3977 -408 4 460 N ATOM 3442 N GLN D 36 31.177 19.085 181.993 1.00 30.36 N ANISOU 3442 N GLN D 36 3238 4807 3492 -383 223 302 N ATOM 3443 CA GLN D 36 30.534 18.831 183.296 1.00 31.08 C ANISOU 3443 CA GLN D 36 3320 5066 3424 -584 234 214 C ATOM 3444 C GLN D 36 31.428 19.008 184.549 1.00 31.94 C ANISOU 3444 C GLN D 36 3432 5203 3501 -621 190 252 C ATOM 3445 O GLN D 36 32.452 18.340 184.715 1.00 31.54 O ANISOU 3445 O GLN D 36 3522 5034 3428 -571 129 402 O ATOM 3446 CB GLN D 36 29.888 17.450 183.331 1.00 31.03 C ANISOU 3446 CB GLN D 36 3507 5070 3212 -805 236 282 C ATOM 3447 CG GLN D 36 29.175 17.170 184.640 1.00 31.99 C ANISOU 3447 CG GLN D 36 3614 5460 3081 -1138 251 219 C ATOM 3448 CD GLN D 36 28.345 15.932 184.567 1.00 33.96 C ANISOU 3448 CD GLN D 36 4078 5751 3075 -1486 231 299 C ATOM 3449 OE1 GLN D 36 28.665 15.012 183.814 1.00 34.33 O ANISOU 3449 OE1 GLN D 36 4418 5486 3141 -1441 140 450 O ATOM 3450 NE2 GLN D 36 27.258 15.893 185.334 1.00 35.67 N ANISOU 3450 NE2 GLN D 36 4148 6391 3014 -1859 297 174 N ATOM 3451 N ASP D 37 31.023 19.903 185.438 1.00 32.81 N ANISOU 3451 N ASP D 37 3378 5496 3590 -670 195 77 N ATOM 3452 CA ASP D 37 31.722 20.048 186.693 1.00 34.59 C ANISOU 3452 CA ASP D 37 3598 5793 3752 -739 158 91 C ATOM 3453 C ASP D 37 31.091 19.130 187.748 1.00 36.35 C ANISOU 3453 C ASP D 37 3893 6237 3681 -1042 179 96 C ATOM 3454 O ASP D 37 29.903 18.830 187.664 1.00 38.12 O ANISOU 3454 O ASP D 37 4056 6681 3746 -1222 242 -10 O ATOM 3455 CB ASP D 37 31.692 21.515 187.115 1.00 35.83 C ANISOU 3455 CB ASP D 37 3578 6016 4019 -632 112 -121 C ATOM 3456 CG ASP D 37 32.481 22.398 186.175 1.00 35.83 C ANISOU 3456 CG ASP D 37 3607 5762 4246 -468 36 -47 C ATOM 3457 OD1 ASP D 37 33.210 21.863 185.328 1.00 35.72 O ANISOU 3457 OD1 ASP D 37 3667 5628 4276 -439 58 155 O ATOM 3458 OD2 ASP D 37 32.379 23.631 186.268 1.00 37.37 O ANISOU 3458 OD2 ASP D 37 3767 5891 4542 -385 -76 -202 O ATOM 3459 N PRO D 38 31.899 18.634 188.702 1.00 36.85 N ANISOU 3459 N PRO D 38 4098 6270 3633 -1139 106 235 N ATOM 3460 CA PRO D 38 31.421 17.881 189.858 1.00 39.18 C ANISOU 3460 CA PRO D 38 4509 6779 3597 -1505 83 281 C ATOM 3461 C PRO D 38 30.322 18.605 190.615 1.00 40.30 C ANISOU 3461 C PRO D 38 4337 7410 3563 -1691 194 -7 C ATOM 3462 O PRO D 38 30.549 19.714 191.083 1.00 40.95 O ANISOU 3462 O PRO D 38 4197 7610 3754 -1513 201 -211 O ATOM 3463 CB PRO D 38 32.658 17.801 190.765 1.00 39.31 C ANISOU 3463 CB PRO D 38 4641 6694 3601 -1448 -37 408 C ATOM 3464 CG PRO D 38 33.822 18.268 189.941 1.00 37.47 C ANISOU 3464 CG PRO D 38 4355 6213 3670 -1065 -72 444 C ATOM 3465 CD PRO D 38 33.353 18.490 188.542 1.00 36.21 C ANISOU 3465 CD PRO D 38 4124 5947 3685 -921 8 396 C ATOM 3466 N GLY D 39 29.148 17.987 190.708 1.00 40.94 N ANISOU 3466 N GLY D 39 4395 7809 3351 -2045 259 -53 N ATOM 3467 CA GLY D 39 28.036 18.566 191.441 1.00 42.53 C ANISOU 3467 CA GLY D 39 4216 8646 3296 -2228 368 -393 C ATOM 3468 C GLY D 39 26.973 19.175 190.550 1.00 42.73 C ANISOU 3468 C GLY D 39 3934 8896 3407 -2027 444 -703 C ATOM 3469 O GLY D 39 25.836 19.377 190.983 1.00 45.01 O ANISOU 3469 O GLY D 39 3875 9822 3403 -2201 528 -1021 O ATOM 3470 N GLU D 40 27.334 19.454 189.298 1.00 40.35 N ANISOU 3470 N GLU D 40 3735 8133 3464 -1664 401 -629 N ATOM 3471 CA GLU D 40 26.426 20.131 188.369 1.00 40.27 C ANISOU 3471 CA GLU D 40 3484 8248 3570 -1399 415 -908 C ATOM 3472 C GLU D 40 25.947 19.291 187.190 1.00 38.27 C ANISOU 3472 C GLU D 40 3363 7861 3318 -1500 450 -751 C ATOM 3473 O GLU D 40 26.229 18.106 187.103 1.00 37.91 O ANISOU 3473 O GLU D 40 3623 7624 3159 -1800 450 -443 O ATOM 3474 CB GLU D 40 27.079 21.401 187.839 1.00 40.12 C ANISOU 3474 CB GLU D 40 3468 7843 3931 -909 293 -998 C ATOM 3475 CG GLU D 40 26.760 22.624 188.663 1.00 44.36 C ANISOU 3475 CG GLU D 40 3746 8656 4451 -681 206 -1408 C ATOM 3476 CD GLU D 40 27.968 23.516 188.850 1.00 44.63 C ANISOU 3476 CD GLU D 40 3953 8251 4753 -465 65 -1324 C ATOM 3477 OE1 GLU D 40 29.007 23.275 188.185 1.00 42.64 O ANISOU 3477 OE1 GLU D 40 3955 7549 4699 -472 53 -971 O ATOM 3478 OE2 GLU D 40 27.879 24.450 189.680 1.00 47.49 O ANISOU 3478 OE2 GLU D 40 4179 8773 5092 -303 -41 -1640 O ATOM 3479 N GLY D 41 25.207 19.927 186.288 1.00 37.03 N ANISOU 3479 N GLY D 41 3008 7783 3281 -1223 436 -986 N ATOM 3480 CA GLY D 41 24.803 19.296 185.053 1.00 35.32 C ANISOU 3480 CA GLY D 41 2900 7415 3103 -1254 457 -862 C ATOM 3481 C GLY D 41 25.820 19.520 183.962 1.00 32.44 C ANISOU 3481 C GLY D 41 2791 6440 3095 -940 383 -626 C ATOM 3482 O GLY D 41 26.802 20.231 184.172 1.00 31.37 O ANISOU 3482 O GLY D 41 2723 6037 3158 -731 314 -566 O ATOM 3483 N PRO D 42 25.617 18.891 182.790 1.00 31.81 N ANISOU 3483 N PRO D 42 2843 6187 3057 -950 397 -493 N ATOM 3484 CA PRO D 42 26.446 19.223 181.627 1.00 29.81 C ANISOU 3484 CA PRO D 42 2745 5495 3084 -658 338 -329 C ATOM 3485 C PRO D 42 26.080 20.603 181.089 1.00 30.40 C ANISOU 3485 C PRO D 42 2664 5559 3329 -326 233 -538 C ATOM 3486 O PRO D 42 24.934 20.989 181.152 1.00 33.00 O ANISOU 3486 O PRO D 42 2766 6210 3562 -254 204 -833 O ATOM 3487 CB PRO D 42 26.077 18.143 180.621 1.00 29.15 C ANISOU 3487 CB PRO D 42 2809 5336 2931 -781 375 -206 C ATOM 3488 CG PRO D 42 25.510 17.041 181.445 1.00 31.09 C ANISOU 3488 CG PRO D 42 3130 5808 2875 -1207 417 -180 C ATOM 3489 CD PRO D 42 24.807 17.686 182.564 1.00 32.25 C ANISOU 3489 CD PRO D 42 2968 6426 2858 -1316 458 -436 C ATOM 3490 N VAL D 43 27.050 21.365 180.615 1.00 29.98 N ANISOU 3490 N VAL D 43 2741 5162 3488 -139 137 -404 N ATOM 3491 CA VAL D 43 26.768 22.693 180.082 1.00 31.52 C ANISOU 3491 CA VAL D 43 2927 5225 3825 135 -55 -551 C ATOM 3492 C VAL D 43 27.259 22.704 178.654 1.00 30.44 C ANISOU 3492 C VAL D 43 2965 4809 3793 170 -90 -309 C ATOM 3493 O VAL D 43 28.408 22.339 178.409 1.00 30.46 O ANISOU 3493 O VAL D 43 3078 4669 3827 57 -21 -51 O ATOM 3494 CB VAL D 43 27.494 23.830 180.886 1.00 32.57 C ANISOU 3494 CB VAL D 43 3122 5189 4064 228 -210 -601 C ATOM 3495 CG1 VAL D 43 27.168 25.205 180.311 1.00 34.11 C ANISOU 3495 CG1 VAL D 43 3440 5135 4387 505 -512 -745 C ATOM 3496 CG2 VAL D 43 27.129 23.787 182.388 1.00 33.51 C ANISOU 3496 CG2 VAL D 43 3047 5639 4047 180 -159 -849 C ATOM 3497 N LEU D 44 26.398 23.102 177.720 1.00 30.47 N ANISOU 3497 N LEU D 44 2962 4799 3815 333 -204 -418 N ATOM 3498 CA LEU D 44 26.756 23.160 176.301 1.00 29.54 C ANISOU 3498 CA LEU D 44 3007 4467 3751 338 -249 -194 C ATOM 3499 C LEU D 44 27.855 24.169 175.997 1.00 29.82 C ANISOU 3499 C LEU D 44 3256 4196 3880 298 -413 15 C ATOM 3500 O LEU D 44 27.671 25.368 176.194 1.00 31.78 O ANISOU 3500 O LEU D 44 3635 4243 4197 430 -683 -90 O ATOM 3501 CB LEU D 44 25.504 23.491 175.478 1.00 31.07 C ANISOU 3501 CB LEU D 44 3158 4722 3926 542 -390 -384 C ATOM 3502 CG LEU D 44 25.581 23.555 173.946 1.00 30.90 C ANISOU 3502 CG LEU D 44 3292 4534 3915 550 -460 -189 C ATOM 3503 CD1 LEU D 44 26.013 22.216 173.338 1.00 28.79 C ANISOU 3503 CD1 LEU D 44 2998 4375 3568 350 -200 3 C ATOM 3504 CD2 LEU D 44 24.252 23.985 173.392 1.00 31.67 C ANISOU 3504 CD2 LEU D 44 3330 4717 3988 810 -652 -440 C ATOM 3505 N LEU D 45 28.999 23.680 175.532 1.00 28.90 N ANISOU 3505 N LEU D 45 3179 4070 3730 107 -281 285 N ATOM 3506 CA LEU D 45 30.087 24.567 175.083 1.00 30.53 C ANISOU 3506 CA LEU D 45 3549 4112 3939 -59 -412 515 C ATOM 3507 C LEU D 45 29.908 25.069 173.657 1.00 32.33 C ANISOU 3507 C LEU D 45 3947 4220 4119 -108 -561 663 C ATOM 3508 O LEU D 45 29.851 26.257 173.425 1.00 34.07 O ANISOU 3508 O LEU D 45 4422 4164 4360 -143 -861 719 O ATOM 3509 CB LEU D 45 31.419 23.848 175.140 1.00 29.35 C ANISOU 3509 CB LEU D 45 3285 4160 3709 -237 -211 689 C ATOM 3510 CG LEU D 45 31.784 23.293 176.505 1.00 28.67 C ANISOU 3510 CG LEU D 45 3078 4174 3641 -210 -96 596 C ATOM 3511 CD1 LEU D 45 32.906 22.278 176.381 1.00 27.75 C ANISOU 3511 CD1 LEU D 45 2839 4279 3425 -251 69 699 C ATOM 3512 CD2 LEU D 45 32.156 24.443 177.424 1.00 29.90 C ANISOU 3512 CD2 LEU D 45 3310 4190 3860 -285 -259 573 C ATOM 3513 N ILE D 46 29.873 24.147 172.699 1.00 33.11 N ANISOU 3513 N ILE D 46 3947 4505 4129 -127 -387 733 N ATOM 3514 CA ILE D 46 29.819 24.481 171.266 1.00 35.80 C ANISOU 3514 CA ILE D 46 4420 4811 4370 -223 -491 900 C ATOM 3515 C ILE D 46 28.749 23.682 170.511 1.00 34.95 C ANISOU 3515 C ILE D 46 4232 4805 4243 -41 -410 776 C ATOM 3516 O ILE D 46 28.613 22.471 170.701 1.00 33.52 O ANISOU 3516 O ILE D 46 3878 4812 4046 22 -183 673 O ATOM 3517 CB ILE D 46 31.185 24.217 170.557 1.00 37.13 C ANISOU 3517 CB ILE D 46 4511 5241 4356 -517 -350 1141 C ATOM 3518 CG1 ILE D 46 32.337 24.930 171.272 1.00 39.06 C ANISOU 3518 CG1 ILE D 46 4782 5492 4569 -772 -407 1267 C ATOM 3519 CG2 ILE D 46 31.173 24.673 169.082 1.00 39.58 C ANISOU 3519 CG2 ILE D 46 4967 5576 4496 -710 -471 1341 C ATOM 3520 CD1 ILE D 46 33.616 25.065 170.440 1.00 41.49 C ANISOU 3520 CD1 ILE D 46 5003 6147 4614 -1158 -345 1504 C ATOM 3521 N ALA D 47 27.994 24.372 169.657 1.00 36.75 N ANISOU 3521 N ALA D 47 4630 4878 4455 29 -642 791 N ATOM 3522 CA ALA D 47 27.101 23.719 168.703 1.00 36.65 C ANISOU 3522 CA ALA D 47 4547 4993 4384 147 -588 714 C ATOM 3523 C ALA D 47 27.636 23.838 167.245 1.00 38.21 C ANISOU 3523 C ALA D 47 4860 5251 4407 -62 -618 975 C ATOM 3524 O ALA D 47 27.773 24.948 166.726 1.00 40.67 O ANISOU 3524 O ALA D 47 5444 5349 4658 -192 -902 1159 O ATOM 3525 CB ALA D 47 25.698 24.316 168.830 1.00 37.29 C ANISOU 3525 CB ALA D 47 4673 4955 4543 445 -840 466 C ATOM 3526 N LEU D 48 27.936 22.704 166.598 1.00 36.93 N ANISOU 3526 N LEU D 48 4521 5378 4131 -110 -361 983 N ATOM 3527 CA LEU D 48 28.472 22.688 165.221 1.00 38.77 C ANISOU 3527 CA LEU D 48 4782 5806 4143 -312 -343 1180 C ATOM 3528 C LEU D 48 27.445 22.359 164.130 1.00 39.62 C ANISOU 3528 C LEU D 48 4914 5953 4186 -192 -390 1117 C ATOM 3529 O LEU D 48 26.626 21.464 164.292 1.00 38.10 O ANISOU 3529 O LEU D 48 4597 5811 4067 10 -278 894 O ATOM 3530 CB LEU D 48 29.580 21.656 165.108 1.00 37.68 C ANISOU 3530 CB LEU D 48 4405 6039 3875 -382 -61 1164 C ATOM 3531 CG LEU D 48 30.699 21.700 166.119 1.00 36.68 C ANISOU 3531 CG LEU D 48 4171 5992 3773 -465 25 1185 C ATOM 3532 CD1 LEU D 48 31.311 20.337 166.172 1.00 35.79 C ANISOU 3532 CD1 LEU D 48 3832 6172 3595 -301 249 1016 C ATOM 3533 CD2 LEU D 48 31.719 22.715 165.717 1.00 39.16 C ANISOU 3533 CD2 LEU D 48 4531 6457 3890 -849 -65 1444 C ATOM 3534 N TYR D 49 27.510 23.051 162.997 1.00 43.06 N ANISOU 3534 N TYR D 49 5525 6392 4445 -373 -566 1328 N ATOM 3535 CA TYR D 49 26.479 22.857 161.968 1.00 44.37 C ANISOU 3535 CA TYR D 49 5734 6580 4545 -244 -656 1270 C ATOM 3536 C TYR D 49 26.936 22.455 160.562 1.00 46.06 C ANISOU 3536 C TYR D 49 5897 7131 4471 -453 -554 1410 C ATOM 3537 O TYR D 49 26.140 21.913 159.802 1.00 46.15 O ANISOU 3537 O TYR D 49 5863 7238 4435 -317 -538 1298 O ATOM 3538 CB TYR D 49 25.522 24.044 161.930 1.00 47.11 C ANISOU 3538 CB TYR D 49 6376 6554 4971 -100 -1072 1286 C ATOM 3539 CG TYR D 49 24.765 24.189 163.227 1.00 46.60 C ANISOU 3539 CG TYR D 49 6242 6308 5157 222 -1140 1000 C ATOM 3540 CD1 TYR D 49 23.747 23.303 163.555 1.00 45.10 C ANISOU 3540 CD1 TYR D 49 5784 6305 5046 469 -985 685 C ATOM 3541 CD2 TYR D 49 25.100 25.177 164.142 1.00 47.77 C ANISOU 3541 CD2 TYR D 49 6576 6157 5416 226 -1354 1034 C ATOM 3542 CE1 TYR D 49 23.063 23.414 164.733 1.00 44.79 C ANISOU 3542 CE1 TYR D 49 5618 6243 5158 698 -1024 406 C ATOM 3543 CE2 TYR D 49 24.425 25.293 165.334 1.00 47.42 C ANISOU 3543 CE2 TYR D 49 6419 6040 5559 529 -1403 728 C ATOM 3544 CZ TYR D 49 23.402 24.407 165.629 1.00 46.10 C ANISOU 3544 CZ TYR D 49 5934 6149 5434 757 -1224 409 C ATOM 3545 OH TYR D 49 22.713 24.516 166.826 1.00 46.28 O ANISOU 3545 OH TYR D 49 5783 6233 5568 1002 -1255 82 O ATOM 3546 N LYS D 50 28.196 22.724 160.217 1.00 48.40 N ANISOU 3546 N LYS D 50 6170 7680 4541 -804 -486 1629 N ATOM 3547 CA LYS D 50 28.806 22.180 158.990 1.00 50.89 C ANISOU 3547 CA LYS D 50 6315 8497 4523 -1002 -320 1686 C ATOM 3548 C LYS D 50 30.257 21.769 159.239 1.00 52.65 C ANISOU 3548 C LYS D 50 6245 9183 4576 -1174 -71 1667 C ATOM 3549 O LYS D 50 30.765 21.933 160.355 1.00 52.28 O ANISOU 3549 O LYS D 50 6162 9016 4686 -1159 -40 1648 O ATOM 3550 CB LYS D 50 28.749 23.206 157.864 1.00 53.77 C ANISOU 3550 CB LYS D 50 6960 8864 4606 -1368 -587 2012 C ATOM 3551 CG LYS D 50 29.067 24.617 158.328 1.00 55.08 C ANISOU 3551 CG LYS D 50 7496 8662 4771 -1681 -912 2315 C ATOM 3552 CD LYS D 50 29.002 25.625 157.196 1.00 58.70 C ANISOU 3552 CD LYS D 50 8350 9045 4908 -2103 -1260 2685 C ATOM 3553 CE LYS D 50 30.281 25.656 156.397 1.00 61.64 C ANISOU 3553 CE LYS D 50 8564 10063 4793 -2724 -1097 2930 C ATOM 3554 NZ LYS D 50 30.529 27.038 155.910 1.00 67.09 N ANISOU 3554 NZ LYS D 50 9793 10510 5187 -3337 -1532 3403 N ATOM 3555 N ALA D 51 30.929 21.252 158.205 1.00 56.05 N ANISOU 3555 N ALA D 51 6434 10201 4659 -1316 92 1639 N ATOM 3556 CA ALA D 51 32.375 20.929 158.295 1.00 59.09 C ANISOU 3556 CA ALA D 51 6460 11199 4792 -1468 303 1569 C ATOM 3557 C ALA D 51 33.289 22.176 158.382 1.00 62.95 C ANISOU 3557 C ALA D 51 7017 11864 5036 -2062 195 1916 C ATOM 3558 O ALA D 51 32.849 23.304 158.189 1.00 65.08 O ANISOU 3558 O ALA D 51 7687 11751 5290 -2391 -84 2245 O ATOM 3559 CB ALA D 51 32.797 20.019 157.158 1.00 60.68 C ANISOU 3559 CB ALA D 51 6335 12072 4650 -1399 488 1356 C ATOM 3560 N GLY D 52 34.556 22.000 158.706 1.00 64.99 N ANISOU 3560 N GLY D 52 6919 12682 5090 -2208 369 1836 N ATOM 3561 CA GLY D 52 35.338 23.179 159.024 1.00 69.91 C ANISOU 3561 CA GLY D 52 7646 13390 5527 -2805 246 2164 C ATOM 3562 C GLY D 52 35.158 23.534 160.491 1.00 68.64 C ANISOU 3562 C GLY D 52 7690 12595 5794 -2613 140 2161 C ATOM 3563 O GLY D 52 34.461 22.832 161.227 1.00 64.79 O ANISOU 3563 O GLY D 52 7223 11693 5703 -2054 187 1911 O ATOM 3564 N GLU D 53 35.795 24.621 160.931 1.00 72.66 N ANISOU 3564 N GLU D 53 8361 13056 6190 -3125 -15 2441 N ATOM 3565 CA GLU D 53 36.015 24.834 162.374 1.00 71.89 C ANISOU 3565 CA GLU D 53 8307 12601 6407 -2973 -47 2374 C ATOM 3566 C GLU D 53 35.290 26.000 163.012 1.00 72.36 C ANISOU 3566 C GLU D 53 8936 11822 6735 -3068 -414 2592 C ATOM 3567 O GLU D 53 35.691 27.149 162.853 1.00 75.74 O ANISOU 3567 O GLU D 53 9682 12146 6950 -3657 -674 2926 O ATOM 3568 CB GLU D 53 37.507 24.960 162.683 1.00 75.14 C ANISOU 3568 CB GLU D 53 8342 13707 6502 -3373 98 2392 C ATOM 3569 CG GLU D 53 38.381 24.089 161.810 1.00 78.22 C ANISOU 3569 CG GLU D 53 8149 15103 6467 -3393 387 2182 C ATOM 3570 CD GLU D 53 39.609 23.576 162.516 1.00 79.60 C ANISOU 3570 CD GLU D 53 7795 15928 6522 -3286 590 1918 C ATOM 3571 OE1 GLU D 53 40.639 23.405 161.823 1.00 84.58 O ANISOU 3571 OE1 GLU D 53 7934 17558 6644 -3585 751 1828 O ATOM 3572 OE2 GLU D 53 39.550 23.341 163.746 1.00 76.24 O ANISOU 3572 OE2 GLU D 53 7416 15080 6472 -2903 580 1779 O ATOM 3573 N LEU D 54 34.236 25.688 163.760 1.00 70.32 N ANISOU 3573 N LEU D 54 8809 10996 6914 -2497 -460 2377 N ATOM 3574 CA LEU D 54 33.536 26.703 164.529 1.00 71.44 C ANISOU 3574 CA LEU D 54 9408 10409 7326 -2436 -809 2451 C ATOM 3575 C LEU D 54 34.375 27.054 165.736 1.00 72.17 C ANISOU 3575 C LEU D 54 9441 10489 7493 -2575 -794 2445 C ATOM 3576 O LEU D 54 34.682 26.222 166.601 1.00 68.64 O ANISOU 3576 O LEU D 54 8647 10235 7198 -2270 -531 2201 O ATOM 3577 CB LEU D 54 32.115 26.287 164.917 1.00 68.34 C ANISOU 3577 CB LEU D 54 9090 9577 7298 -1817 -855 2178 C ATOM 3578 CG LEU D 54 30.992 26.487 163.876 1.00 70.09 C ANISOU 3578 CG LEU D 54 9563 9569 7497 -1688 -1070 2217 C ATOM 3579 CD1 LEU D 54 31.091 27.863 163.189 1.00 74.79 C ANISOU 3579 CD1 LEU D 54 10683 9855 7880 -2138 -1518 2583 C ATOM 3580 CD2 LEU D 54 30.909 25.357 162.822 1.00 69.24 C ANISOU 3580 CD2 LEU D 54 9144 9938 7225 -1607 -779 2132 C ATOM 3581 N THR D 55 34.785 28.307 165.743 1.00 77.37 N ANISOU 3581 N THR D 55 10484 10910 8005 -3086 -1116 2740 N ATOM 3582 CA THR D 55 35.724 28.777 166.725 1.00 79.92 C ANISOU 3582 CA THR D 55 10773 11281 8311 -3368 -1133 2788 C ATOM 3583 C THR D 55 35.049 29.366 167.956 1.00 79.10 C ANISOU 3583 C THR D 55 10990 10478 8588 -3024 -1393 2643 C ATOM 3584 O THR D 55 34.595 30.517 167.952 1.00 82.39 O ANISOU 3584 O THR D 55 11975 10287 9043 -3155 -1856 2788 O ATOM 3585 CB THR D 55 36.732 29.789 166.121 1.00 85.83 C ANISOU 3585 CB THR D 55 11747 12253 8612 -4251 -1337 3196 C ATOM 3586 OG1 THR D 55 37.146 30.705 167.143 1.00 87.62 O ANISOU 3586 OG1 THR D 55 12261 12112 8919 -4503 -1588 3280 O ATOM 3587 CG2 THR D 55 36.117 30.561 164.926 1.00 89.26 C ANISOU 3587 CG2 THR D 55 12727 12338 8849 -4570 -1716 3508 C ATOM 3588 N SER D 56 34.914 28.521 168.969 1.00 75.74 N ANISOU 3588 N SER D 56 10215 10140 8423 -2542 -1124 2327 N ATOM 3589 CA SER D 56 34.935 28.964 170.359 1.00 75.85 C ANISOU 3589 CA SER D 56 10325 9829 8665 -2401 -1238 2192 C ATOM 3590 C SER D 56 33.739 29.545 171.070 1.00 75.76 C ANISOU 3590 C SER D 56 10646 9183 8958 -1971 -1545 1986 C ATOM 3591 O SER D 56 32.748 29.989 170.481 1.00 77.22 O ANISOU 3591 O SER D 56 11147 8998 9197 -1784 -1828 1971 O ATOM 3592 CB SER D 56 36.129 29.900 170.581 1.00 79.77 C ANISOU 3592 CB SER D 56 10975 10398 8937 -3039 -1399 2451 C ATOM 3593 OG SER D 56 37.327 29.159 170.691 1.00 79.72 O ANISOU 3593 OG SER D 56 10444 11115 8731 -3237 -1031 2440 O ATOM 3594 N ASN D 57 33.865 29.480 172.387 1.00 74.34 N ANISOU 3594 N ASN D 57 10337 8957 8953 -1779 -1479 1783 N ATOM 3595 CA ASN D 57 33.391 30.543 173.220 1.00 76.27 C ANISOU 3595 CA ASN D 57 10958 8662 9359 -1638 -1870 1657 C ATOM 3596 C ASN D 57 34.669 31.301 173.602 1.00 77.67 C ANISOU 3596 C ASN D 57 11288 8839 9382 -2200 -1993 1892 C ATOM 3597 O ASN D 57 34.679 32.534 173.646 1.00 81.97 O ANISOU 3597 O ASN D 57 12367 8876 9900 -2425 -2464 2006 O ATOM 3598 CB ASN D 57 32.618 30.019 174.437 1.00 75.09 C ANISOU 3598 CB ASN D 57 10554 8524 9453 -1096 -1729 1254 C ATOM 3599 CG ASN D 57 31.409 30.902 174.786 1.00 78.21 C ANISOU 3599 CG ASN D 57 11274 8433 10009 -673 -2155 972 C ATOM 3600 OD1 ASN D 57 30.641 31.307 173.902 1.00 80.48 O ANISOU 3600 OD1 ASN D 57 11829 8462 10286 -525 -2433 979 O ATOM 3601 ND2 ASN D 57 31.243 31.207 176.078 1.00 78.80 N ANISOU 3601 ND2 ASN D 57 11313 8418 10210 -442 -2232 687 N ATOM 3602 N GLY D 58 35.759 30.561 173.828 1.00 74.06 N ANISOU 3602 N GLY D 58 10384 8959 8794 -2434 -1609 1955 N ATOM 3603 CA GLY D 58 37.060 31.190 174.077 1.00 74.04 C ANISOU 3603 CA GLY D 58 10425 9133 8575 -3041 -1679 2179 C ATOM 3604 C GLY D 58 38.291 30.538 173.459 1.00 72.18 C ANISOU 3604 C GLY D 58 9730 9684 8012 -3458 -1337 2347 C ATOM 3605 O GLY D 58 38.710 30.889 172.353 1.00 75.07 O ANISOU 3605 O GLY D 58 10195 10263 8066 -3974 -1409 2626 O ATOM 3606 N ARG D 59 38.884 29.599 174.193 1.00 66.89 N ANISOU 3606 N ARG D 59 8553 9486 7377 -3230 -994 2153 N ATOM 3607 CA ARG D 59 40.125 28.951 173.790 1.00 65.06 C ANISOU 3607 CA ARG D 59 7809 10082 6828 -3498 -700 2197 C ATOM 3608 C ARG D 59 39.838 27.525 173.335 1.00 61.02 C ANISOU 3608 C ARG D 59 6912 9913 6361 -2974 -382 1987 C ATOM 3609 O ARG D 59 40.741 26.683 173.282 1.00 60.98 O ANISOU 3609 O ARG D 59 6425 10571 6175 -2903 -137 1865 O ATOM 3610 CB ARG D 59 41.104 28.937 174.961 1.00 64.35 C ANISOU 3610 CB ARG D 59 7455 10278 6717 -3578 -625 2100 C ATOM 3611 CG ARG D 59 41.166 30.241 175.761 1.00 65.57 C ANISOU 3611 CG ARG D 59 8050 9928 6937 -3934 -968 2215 C ATOM 3612 CD ARG D 59 41.809 30.033 177.137 1.00 64.07 C ANISOU 3612 CD ARG D 59 7599 9914 6830 -3802 -873 2034 C ATOM 3613 NE ARG D 59 40.871 29.465 178.119 1.00 59.52 N ANISOU 3613 NE ARG D 59 7047 8946 6620 -3121 -817 1758 N ATOM 3614 CZ ARG D 59 40.870 28.201 178.556 1.00 55.49 C ANISOU 3614 CZ ARG D 59 6160 8728 6196 -2637 -538 1549 C ATOM 3615 NH1 ARG D 59 41.766 27.323 178.122 1.00 55.82 N ANISOU 3615 NH1 ARG D 59 5755 9431 6025 -2622 -306 1522 N ATOM 3616 NH2 ARG D 59 39.960 27.811 179.435 1.00 51.87 N ANISOU 3616 NH2 ARG D 59 5787 7916 6003 -2169 -527 1347 N ATOM 3617 N LEU D 60 38.565 27.278 173.015 1.00 57.41 N ANISOU 3617 N LEU D 60 6685 8999 6129 -2592 -429 1917 N ATOM 3618 CA LEU D 60 38.045 25.965 172.633 1.00 53.28 C ANISOU 3618 CA LEU D 60 5926 8634 5685 -2100 -194 1719 C ATOM 3619 C LEU D 60 37.704 25.948 171.157 1.00 53.30 C ANISOU 3619 C LEU D 60 5989 8750 5513 -2236 -199 1845 C ATOM 3620 O LEU D 60 36.919 26.737 170.734 1.00 53.40 O ANISOU 3620 O LEU D 60 6386 8320 5583 -2348 -433 1983 O ATOM 3621 CB LEU D 60 36.746 25.703 173.386 1.00 50.70 C ANISOU 3621 CB LEU D 60 5796 7765 5702 -1630 -245 1535 C ATOM 3622 CG LEU D 60 36.758 26.039 174.872 1.00 50.18 C ANISOU 3622 CG LEU D 60 5791 7458 5818 -1536 -320 1426 C ATOM 3623 CD1 LEU D 60 35.527 26.866 175.274 1.00 50.15 C ANISOU 3623 CD1 LEU D 60 6147 6879 6029 -1385 -576 1348 C ATOM 3624 CD2 LEU D 60 36.896 24.756 175.680 1.00 47.88 C ANISOU 3624 CD2 LEU D 60 5224 7370 5596 -1176 -98 1222 C ATOM 3625 N THR D 61 38.260 25.054 170.357 1.00 52.94 N ANISOU 3625 N THR D 61 5578 9296 5240 -2185 25 1770 N ATOM 3626 CA THR D 61 37.866 25.034 168.954 1.00 53.50 C ANISOU 3626 CA THR D 61 5710 9487 5132 -2312 21 1877 C ATOM 3627 C THR D 61 37.349 23.638 168.632 1.00 50.36 C ANISOU 3627 C THR D 61 5116 9188 4833 -1759 215 1608 C ATOM 3628 O THR D 61 37.875 22.647 169.139 1.00 49.49 O ANISOU 3628 O THR D 61 4714 9353 4739 -1429 369 1371 O ATOM 3629 CB THR D 61 39.028 25.464 168.023 1.00 58.77 C ANISOU 3629 CB THR D 61 6149 10866 5313 -2922 63 2065 C ATOM 3630 OG1 THR D 61 39.740 26.569 168.593 1.00 62.04 O ANISOU 3630 OG1 THR D 61 6699 11261 5612 -3467 -101 2281 O ATOM 3631 CG2 THR D 61 38.536 25.888 166.652 1.00 61.19 C ANISOU 3631 CG2 THR D 61 6682 11160 5407 -3233 -45 2288 C ATOM 3632 N ALA D 62 36.289 23.552 167.833 1.00 48.68 N ANISOU 3632 N ALA D 62 5110 8701 4685 -1644 159 1634 N ATOM 3633 CA ALA D 62 35.717 22.253 167.516 1.00 45.66 C ANISOU 3633 CA ALA D 62 4609 8353 4388 -1177 304 1389 C ATOM 3634 C ALA D 62 35.474 22.034 166.028 1.00 47.02 C ANISOU 3634 C ALA D 62 4743 8788 4333 -1254 340 1426 C ATOM 3635 O ALA D 62 35.271 22.981 165.263 1.00 49.00 O ANISOU 3635 O ALA D 62 5191 8987 4441 -1630 198 1677 O ATOM 3636 CB ALA D 62 34.456 22.010 168.310 1.00 42.19 C ANISOU 3636 CB ALA D 62 4407 7326 4296 -845 236 1278 C ATOM 3637 N GLN D 63 35.486 20.765 165.639 1.00 46.00 N ANISOU 3637 N GLN D 63 4408 8909 4162 -889 489 1169 N ATOM 3638 CA GLN D 63 35.461 20.365 164.248 1.00 47.43 C ANISOU 3638 CA GLN D 63 4464 9475 4081 -911 556 1126 C ATOM 3639 C GLN D 63 34.439 19.264 164.112 1.00 44.05 C ANISOU 3639 C GLN D 63 4155 8736 3847 -467 573 906 C ATOM 3640 O GLN D 63 34.024 18.715 165.094 1.00 41.23 O ANISOU 3640 O GLN D 63 3911 8005 3749 -192 555 782 O ATOM 3641 CB GLN D 63 36.826 19.797 163.877 1.00 51.56 C ANISOU 3641 CB GLN D 63 4527 10805 4259 -883 707 930 C ATOM 3642 CG GLN D 63 37.448 20.376 162.628 1.00 56.86 C ANISOU 3642 CG GLN D 63 4984 12155 4467 -1363 757 1075 C ATOM 3643 CD GLN D 63 37.099 19.593 161.386 1.00 58.70 C ANISOU 3643 CD GLN D 63 5108 12681 4516 -1160 829 894 C ATOM 3644 OE1 GLN D 63 36.207 18.744 161.411 1.00 56.03 O ANISOU 3644 OE1 GLN D 63 4948 11903 4436 -710 806 714 O ATOM 3645 NE2 GLN D 63 37.811 19.867 160.282 1.00 63.17 N ANISOU 3645 NE2 GLN D 63 5371 14044 4589 -1540 912 934 N ATOM 3646 N PHE D 64 34.077 18.918 162.887 1.00 45.10 N ANISOU 3646 N PHE D 64 4261 9065 3810 -449 600 862 N ATOM 3647 CA PHE D 64 32.939 18.051 162.601 1.00 42.78 C ANISOU 3647 CA PHE D 64 4136 8445 3672 -144 581 704 C ATOM 3648 C PHE D 64 33.319 17.526 161.226 1.00 44.84 C ANISOU 3648 C PHE D 64 4189 9245 3603 -115 660 574 C ATOM 3649 O PHE D 64 33.464 18.306 160.281 1.00 47.28 O ANISOU 3649 O PHE D 64 4447 9860 3659 -471 656 774 O ATOM 3650 CB PHE D 64 31.667 18.936 162.691 1.00 42.51 C ANISOU 3650 CB PHE D 64 4405 7910 3839 -295 436 910 C ATOM 3651 CG PHE D 64 30.409 18.449 161.963 1.00 42.67 C ANISOU 3651 CG PHE D 64 4556 7751 3905 -153 397 824 C ATOM 3652 CD1 PHE D 64 29.350 19.348 161.824 1.00 42.58 C ANISOU 3652 CD1 PHE D 64 4754 7428 3998 -252 230 971 C ATOM 3653 CD2 PHE D 64 30.253 17.174 161.430 1.00 43.04 C ANISOU 3653 CD2 PHE D 64 4543 7927 3883 90 476 580 C ATOM 3654 CE1 PHE D 64 28.187 18.995 161.177 1.00 42.28 C ANISOU 3654 CE1 PHE D 64 4794 7290 3980 -135 179 883 C ATOM 3655 CE2 PHE D 64 29.092 16.814 160.771 1.00 42.53 C ANISOU 3655 CE2 PHE D 64 4600 7719 3842 153 429 517 C ATOM 3656 CZ PHE D 64 28.052 17.722 160.656 1.00 42.32 C ANISOU 3656 CZ PHE D 64 4716 7455 3909 31 298 669 C ATOM 3657 N GLY D 65 33.503 16.208 161.139 1.00 43.82 N ANISOU 3657 N GLY D 65 3973 9225 3451 300 696 232 N ATOM 3658 CA GLY D 65 34.054 15.555 159.946 1.00 45.75 C ANISOU 3658 CA GLY D 65 3957 10070 3355 444 762 -13 C ATOM 3659 C GLY D 65 33.210 15.708 158.705 1.00 45.34 C ANISOU 3659 C GLY D 65 3996 10052 3178 283 758 75 C ATOM 3660 O GLY D 65 32.008 15.897 158.813 1.00 43.15 O ANISOU 3660 O GLY D 65 4021 9238 3137 229 677 218 O ATOM 3661 N ILE D 66 33.839 15.649 157.533 1.00 48.09 N ANISOU 3661 N ILE D 66 4049 11103 3122 201 841 -29 N ATOM 3662 CA ILE D 66 33.136 15.761 156.253 1.00 48.18 C ANISOU 3662 CA ILE D 66 4121 11235 2950 38 834 44 C ATOM 3663 C ILE D 66 32.191 14.574 156.070 1.00 45.90 C ANISOU 3663 C ILE D 66 4046 10546 2848 459 767 -236 C ATOM 3664 O ILE D 66 31.037 14.740 155.648 1.00 44.09 O ANISOU 3664 O ILE D 66 4056 9972 2724 352 700 -98 O ATOM 3665 CB ILE D 66 34.148 15.945 155.064 1.00 53.88 C ANISOU 3665 CB ILE D 66 4419 12943 3109 -199 956 -26 C ATOM 3666 CG1 ILE D 66 34.387 17.429 154.819 1.00 56.00 C ANISOU 3666 CG1 ILE D 66 4717 13399 3160 -901 939 462 C ATOM 3667 CG2 ILE D 66 33.718 15.274 153.756 1.00 54.88 C ANISOU 3667 CG2 ILE D 66 4488 13367 2996 -55 973 -246 C ATOM 3668 CD1 ILE D 66 35.601 17.968 155.588 1.00 59.01 C ANISOU 3668 CD1 ILE D 66 4846 14154 3420 -1143 1002 533 C ATOM 3669 N THR D 67 32.654 13.397 156.494 1.00 45.69 N ANISOU 3669 N THR D 67 3979 10511 2870 932 737 -625 N ATOM 3670 CA THR D 67 31.846 12.178 156.484 1.00 44.99 C ANISOU 3670 CA THR D 67 4189 9955 2950 1291 609 -890 C ATOM 3671 C THR D 67 30.708 12.144 157.519 1.00 41.44 C ANISOU 3671 C THR D 67 4138 8709 2899 1209 515 -706 C ATOM 3672 O THR D 67 29.900 11.218 157.511 1.00 41.11 O ANISOU 3672 O THR D 67 4380 8279 2962 1355 400 -861 O ATOM 3673 CB THR D 67 32.716 10.924 156.684 1.00 47.46 C ANISOU 3673 CB THR D 67 4447 10405 3179 1846 502 -1369 C ATOM 3674 OG1 THR D 67 33.219 10.899 158.021 1.00 46.32 O ANISOU 3674 OG1 THR D 67 4373 9984 3243 1963 444 -1339 O ATOM 3675 CG2 THR D 67 33.875 10.912 155.704 1.00 52.18 C ANISOU 3675 CG2 THR D 67 4547 11951 3329 1983 600 -1653 C ATOM 3676 N ARG D 68 30.664 13.154 158.392 1.00 39.67 N ANISOU 3676 N ARG D 68 3922 8301 2850 946 552 -398 N ATOM 3677 CA ARG D 68 29.658 13.333 159.450 1.00 37.57 C ANISOU 3677 CA ARG D 68 3928 7440 2906 836 487 -239 C ATOM 3678 C ARG D 68 29.609 12.238 160.531 1.00 37.50 C ANISOU 3678 C ARG D 68 4159 7023 3068 1063 384 -418 C ATOM 3679 O ARG D 68 28.600 12.079 161.212 1.00 35.18 O ANISOU 3679 O ARG D 68 4095 6318 2953 937 326 -350 O ATOM 3680 CB ARG D 68 28.262 13.600 158.866 1.00 36.99 C ANISOU 3680 CB ARG D 68 3990 7182 2881 661 448 -134 C ATOM 3681 CG ARG D 68 28.229 14.633 157.747 1.00 38.31 C ANISOU 3681 CG ARG D 68 4023 7675 2857 438 473 65 C ATOM 3682 CD ARG D 68 27.460 14.070 156.552 1.00 40.37 C ANISOU 3682 CD ARG D 68 4328 8035 2975 479 444 -62 C ATOM 3683 NE ARG D 68 26.041 14.397 156.581 1.00 38.94 N ANISOU 3683 NE ARG D 68 4298 7554 2943 376 350 29 N ATOM 3684 CZ ARG D 68 25.118 13.829 155.809 1.00 40.15 C ANISOU 3684 CZ ARG D 68 4516 7709 3029 400 304 -98 C ATOM 3685 NH1 ARG D 68 25.442 12.859 154.960 1.00 41.73 N ANISOU 3685 NH1 ARG D 68 4697 8123 3037 535 333 -324 N ATOM 3686 NH2 ARG D 68 23.856 14.220 155.906 1.00 39.49 N ANISOU 3686 NH2 ARG D 68 4500 7448 3056 317 211 -41 N ATOM 3687 N LYS D 69 30.704 11.495 160.683 1.00 40.45 N ANISOU 3687 N LYS D 69 4477 7549 3342 1386 332 -657 N ATOM 3688 CA LYS D 69 30.799 10.438 161.684 1.00 41.38 C ANISOU 3688 CA LYS D 69 4904 7238 3581 1622 152 -815 C ATOM 3689 C LYS D 69 31.843 10.798 162.735 1.00 41.87 C ANISOU 3689 C LYS D 69 4828 7382 3699 1709 164 -771 C ATOM 3690 O LYS D 69 32.183 9.978 163.586 1.00 43.15 O ANISOU 3690 O LYS D 69 5227 7246 3923 1948 -16 -904 O ATOM 3691 CB LYS D 69 31.180 9.112 161.024 1.00 44.35 C ANISOU 3691 CB LYS D 69 5429 7629 3794 2052 -38 -1207 C ATOM 3692 CG LYS D 69 30.091 8.505 160.169 1.00 44.61 C ANISOU 3692 CG LYS D 69 5706 7459 3785 1971 -109 -1282 C ATOM 3693 CD LYS D 69 30.503 7.138 159.679 1.00 49.07 C ANISOU 3693 CD LYS D 69 6515 7926 4204 2439 -376 -1705 C ATOM 3694 CE LYS D 69 29.586 6.645 158.563 1.00 50.95 C ANISOU 3694 CE LYS D 69 6907 8112 4339 2361 -421 -1815 C ATOM 3695 NZ LYS D 69 30.305 5.725 157.600 1.00 55.83 N ANISOU 3695 NZ LYS D 69 7516 8979 4717 2893 -600 -2297 N ATOM 3696 N ASP D 70 32.319 12.040 162.687 1.00 41.71 N ANISOU 3696 N ASP D 70 4472 7733 3642 1477 340 -567 N ATOM 3697 CA ASP D 70 33.526 12.453 163.399 1.00 42.80 C ANISOU 3697 CA ASP D 70 4371 8144 3747 1542 373 -564 C ATOM 3698 C ASP D 70 33.409 13.846 163.953 1.00 40.10 C ANISOU 3698 C ASP D 70 3937 7781 3518 1127 486 -217 C ATOM 3699 O ASP D 70 32.874 14.728 163.267 1.00 38.94 O ANISOU 3699 O ASP D 70 3751 7708 3336 821 556 -12 O ATOM 3700 CB ASP D 70 34.697 12.478 162.417 1.00 47.54 C ANISOU 3700 CB ASP D 70 4543 9507 4011 1698 448 -777 C ATOM 3701 CG ASP D 70 35.282 11.120 162.204 1.00 52.12 C ANISOU 3701 CG ASP D 70 5148 10193 4464 2280 271 -1235 C ATOM 3702 OD1 ASP D 70 35.274 10.359 163.200 1.00 52.72 O ANISOU 3702 OD1 ASP D 70 5544 9775 4712 2547 68 -1329 O ATOM 3703 OD2 ASP D 70 35.735 10.808 161.072 1.00 55.70 O ANISOU 3703 OD2 ASP D 70 5332 11206 4626 2477 297 -1510 O ATOM 3704 N SER D 71 33.935 14.046 165.165 1.00 38.36 N ANISOU 3704 N SER D 71 3715 7445 3415 1138 461 -165 N ATOM 3705 CA SER D 71 34.204 15.392 165.666 1.00 37.87 C ANISOU 3705 CA SER D 71 3522 7465 3401 788 538 103 C ATOM 3706 C SER D 71 35.378 15.413 166.628 1.00 39.29 C ANISOU 3706 C SER D 71 3533 7835 3560 890 526 42 C ATOM 3707 O SER D 71 35.743 14.385 167.187 1.00 40.21 O ANISOU 3707 O SER D 71 3725 7852 3701 1256 421 -178 O ATOM 3708 CB SER D 71 32.965 16.029 166.310 1.00 35.70 C ANISOU 3708 CB SER D 71 3506 6678 3379 562 506 312 C ATOM 3709 OG SER D 71 32.753 15.601 167.637 1.00 36.72 O ANISOU 3709 OG SER D 71 3806 6457 3688 654 445 277 O ATOM 3710 N PHE D 72 35.997 16.577 166.792 1.00 40.77 N ANISOU 3710 N PHE D 72 3522 8292 3677 559 593 235 N ATOM 3711 CA PHE D 72 36.990 16.744 167.843 1.00 41.89 C ANISOU 3711 CA PHE D 72 3512 8583 3823 590 580 209 C ATOM 3712 C PHE D 72 36.961 18.069 168.560 1.00 40.99 C ANISOU 3712 C PHE D 72 3451 8306 3817 175 581 494 C ATOM 3713 O PHE D 72 36.426 19.053 168.044 1.00 39.62 O ANISOU 3713 O PHE D 72 3389 8022 3643 -176 573 723 O ATOM 3714 CB PHE D 72 38.418 16.362 167.419 1.00 46.58 C ANISOU 3714 CB PHE D 72 3665 9940 4094 775 618 -41 C ATOM 3715 CG PHE D 72 39.018 17.192 166.337 1.00 50.14 C ANISOU 3715 CG PHE D 72 3774 11074 4204 371 742 58 C ATOM 3716 CD1 PHE D 72 39.560 18.442 166.601 1.00 51.38 C ANISOU 3716 CD1 PHE D 72 3810 11458 4255 -164 781 327 C ATOM 3717 CD2 PHE D 72 39.160 16.658 165.062 1.00 53.65 C ANISOU 3717 CD2 PHE D 72 4007 12007 4370 505 796 -144 C ATOM 3718 CE1 PHE D 72 40.165 19.178 165.595 1.00 55.61 C ANISOU 3718 CE1 PHE D 72 4065 12669 4396 -651 867 452 C ATOM 3719 CE2 PHE D 72 39.774 17.387 164.034 1.00 57.49 C ANISOU 3719 CE2 PHE D 72 4147 13246 4452 57 915 -51 C ATOM 3720 CZ PHE D 72 40.281 18.647 164.305 1.00 58.54 C ANISOU 3720 CZ PHE D 72 4196 13590 4458 -559 947 269 C ATOM 3721 N LEU D 73 37.565 18.079 169.750 1.00 40.91 N ANISOU 3721 N LEU D 73 3396 8263 3886 242 547 463 N ATOM 3722 CA LEU D 73 37.629 19.271 170.585 1.00 39.64 C ANISOU 3722 CA LEU D 73 3301 7932 3829 -107 518 682 C ATOM 3723 C LEU D 73 39.079 19.562 170.893 1.00 42.16 C ANISOU 3723 C LEU D 73 3273 8810 3935 -227 549 647 C ATOM 3724 O LEU D 73 39.839 18.665 171.243 1.00 43.73 O ANISOU 3724 O LEU D 73 3267 9292 4055 133 544 404 O ATOM 3725 CB LEU D 73 36.882 19.058 171.900 1.00 36.28 C ANISOU 3725 CB LEU D 73 3143 6953 3689 40 447 671 C ATOM 3726 CG LEU D 73 35.948 20.138 172.462 1.00 34.75 C ANISOU 3726 CG LEU D 73 3187 6323 3692 -201 378 836 C ATOM 3727 CD1 LEU D 73 35.812 19.966 173.948 1.00 33.52 C ANISOU 3727 CD1 LEU D 73 3121 5919 3695 -100 339 778 C ATOM 3728 CD2 LEU D 73 36.379 21.558 172.191 1.00 36.93 C ANISOU 3728 CD2 LEU D 73 3456 6690 3887 -607 315 1041 C ATOM 3729 N ASN D 74 39.461 20.821 170.731 1.00 43.33 N ANISOU 3729 N ASN D 74 3376 9127 3960 -741 541 879 N ATOM 3730 CA AASN D 74 40.764 21.288 171.172 0.50 45.91 C ANISOU 3730 CA AASN D 74 3389 9980 4075 -990 560 884 C ATOM 3731 CA BASN D 74 40.772 21.292 171.170 0.50 45.84 C ANISOU 3731 CA BASN D 74 3377 9975 4063 -992 560 884 C ATOM 3732 C ASN D 74 40.603 22.395 172.191 1.00 45.05 C ANISOU 3732 C ASN D 74 3537 9436 4146 -1316 444 1097 C ATOM 3733 O ASN D 74 39.850 23.326 171.968 1.00 45.41 O ANISOU 3733 O ASN D 74 3922 9044 4288 -1613 331 1320 O ATOM 3734 CB AASN D 74 41.603 21.778 169.993 0.50 49.58 C ANISOU 3734 CB AASN D 74 3529 11207 4103 -1440 635 961 C ATOM 3735 CB BASN D 74 41.618 21.815 170.002 0.50 49.37 C ANISOU 3735 CB BASN D 74 3502 11183 4072 -1458 634 968 C ATOM 3736 CG AASN D 74 42.356 20.657 169.315 0.50 51.96 C ANISOU 3736 CG AASN D 74 3355 12264 4122 -1056 753 609 C ATOM 3737 CG BASN D 74 42.829 22.618 170.471 0.50 52.30 C ANISOU 3737 CG BASN D 74 3599 12081 4191 -1934 630 1056 C ATOM 3738 OD1AASN D 74 43.133 19.949 169.950 0.50 52.99 O ANISOU 3738 OD1AASN D 74 3200 12719 4214 -660 752 323 O ATOM 3739 OD1BASN D 74 43.786 22.069 171.016 0.50 53.30 O ANISOU 3739 OD1BASN D 74 3331 12719 4201 -1687 683 805 O ATOM 3740 ND2AASN D 74 42.135 20.494 168.019 0.50 53.20 N ANISOU 3740 ND2AASN D 74 3432 12717 4063 -1131 820 596 N ATOM 3741 ND2BASN D 74 42.784 23.927 170.266 0.50 54.02 N ANISOU 3741 ND2BASN D 74 4060 12158 4306 -2624 525 1407 N ATOM 3742 N ILE D 75 41.290 22.286 173.322 1.00 45.28 N ANISOU 3742 N ILE D 75 3427 9563 4215 -1216 433 1000 N ATOM 3743 CA ILE D 75 41.329 23.406 174.258 1.00 44.79 C ANISOU 3743 CA ILE D 75 3562 9192 4263 -1567 314 1175 C ATOM 3744 C ILE D 75 42.767 23.846 174.257 1.00 48.47 C ANISOU 3744 C ILE D 75 3647 10377 4392 -1957 346 1197 C ATOM 3745 O ILE D 75 43.639 23.042 174.541 1.00 50.32 O ANISOU 3745 O ILE D 75 3484 11142 4493 -1663 428 960 O ATOM 3746 CB ILE D 75 40.916 23.020 175.695 1.00 41.31 C ANISOU 3746 CB ILE D 75 3274 8304 4117 -1210 268 1056 C ATOM 3747 CG1 ILE D 75 39.682 22.119 175.686 1.00 38.68 C ANISOU 3747 CG1 ILE D 75 3171 7517 4011 -784 285 952 C ATOM 3748 CG2 ILE D 75 40.645 24.262 176.522 1.00 40.45 C ANISOU 3748 CG2 ILE D 75 3443 7779 4149 -1533 118 1204 C ATOM 3749 CD1 ILE D 75 39.117 21.859 177.067 1.00 37.03 C ANISOU 3749 CD1 ILE D 75 3146 6895 4028 -573 232 877 C ATOM 3750 N SER D 76 43.042 25.094 173.913 1.00 50.91 N ANISOU 3750 N SER D 76 4079 10741 4523 -2626 248 1465 N ATOM 3751 CA SER D 76 44.438 25.532 173.965 1.00 55.82 C ANISOU 3751 CA SER D 76 4307 12138 4764 -3110 280 1492 C ATOM 3752 C SER D 76 44.711 26.412 175.183 1.00 55.44 C ANISOU 3752 C SER D 76 4451 11781 4831 -3394 126 1595 C ATOM 3753 O SER D 76 43.768 26.975 175.749 1.00 52.47 O ANISOU 3753 O SER D 76 4580 10575 4783 -3342 -45 1696 O ATOM 3754 CB SER D 76 44.882 26.209 172.652 1.00 60.38 C ANISOU 3754 CB SER D 76 4795 13250 4896 -3817 283 1721 C ATOM 3755 OG SER D 76 43.939 27.170 172.222 1.00 60.05 O ANISOU 3755 OG SER D 76 5368 12473 4974 -4173 68 2042 O ATOM 3756 N ALA D 77 46.003 26.517 175.542 1.00 58.58 N ANISOU 3756 N ALA D 77 4409 12922 4928 -3675 178 1526 N ATOM 3757 CA ALA D 77 46.525 27.233 176.727 1.00 58.76 C ANISOU 3757 CA ALA D 77 4494 12842 4988 -3956 53 1574 C ATOM 3758 C ALA D 77 45.671 26.984 177.960 1.00 54.04 C ANISOU 3758 C ALA D 77 4230 11437 4865 -3399 -24 1464 C ATOM 3759 O ALA D 77 44.915 27.866 178.388 1.00 52.83 O ANISOU 3759 O ALA D 77 4590 10543 4941 -3567 -221 1612 O ATOM 3760 CB ALA D 77 46.666 28.728 176.458 1.00 62.05 C ANISOU 3760 CB ALA D 77 5289 13072 5216 -4865 -169 1933 C ATOM 3761 N SER D 78 45.765 25.770 178.494 1.00 51.27 N ANISOU 3761 N SER D 78 3608 11244 4628 -2733 97 1188 N ATOM 3762 CA SER D 78 44.845 25.341 179.525 1.00 46.59 C ANISOU 3762 CA SER D 78 3322 9959 4420 -2232 47 1094 C ATOM 3763 C SER D 78 45.078 26.019 180.857 1.00 47.05 C ANISOU 3763 C SER D 78 3500 9798 4578 -2393 -75 1107 C ATOM 3764 O SER D 78 46.104 26.653 181.109 1.00 50.54 O ANISOU 3764 O SER D 78 3736 10668 4796 -2826 -119 1154 O ATOM 3765 CB SER D 78 44.859 23.826 179.704 1.00 44.85 C ANISOU 3765 CB SER D 78 2895 9892 4253 -1541 140 839 C ATOM 3766 OG SER D 78 46.060 23.402 180.310 1.00 46.37 O ANISOU 3766 OG SER D 78 2679 10679 4259 -1396 140 660 O ATOM 3767 N ILE D 79 44.088 25.848 181.709 1.00 44.32 N ANISOU 3767 N ILE D 79 3469 8832 4540 -2058 -129 1047 N ATOM 3768 CA ILE D 79 43.873 26.698 182.842 1.00 44.03 C ANISOU 3768 CA ILE D 79 3679 8406 4642 -2213 -277 1058 C ATOM 3769 C ILE D 79 43.357 25.718 183.925 1.00 41.53 C ANISOU 3769 C ILE D 79 3378 7899 4503 -1684 -227 881 C ATOM 3770 O ILE D 79 42.808 24.669 183.595 1.00 38.94 O ANISOU 3770 O ILE D 79 3053 7509 4235 -1305 -135 816 O ATOM 3771 CB ILE D 79 42.911 27.863 182.370 1.00 43.49 C ANISOU 3771 CB ILE D 79 4085 7738 4702 -2489 -461 1196 C ATOM 3772 CG1 ILE D 79 43.524 29.239 182.617 1.00 46.88 C ANISOU 3772 CG1 ILE D 79 4703 8091 5017 -3080 -690 1332 C ATOM 3773 CG2 ILE D 79 41.491 27.715 182.850 1.00 39.93 C ANISOU 3773 CG2 ILE D 79 3923 6714 4535 -2081 -504 1064 C ATOM 3774 CD1 ILE D 79 44.460 29.682 181.503 1.00 50.74 C ANISOU 3774 CD1 ILE D 79 5061 9052 5166 -3685 -697 1556 C ATOM 3775 N PRO D 80 43.644 25.989 185.209 1.00 42.93 N ANISOU 3775 N PRO D 80 3561 8039 4711 -1704 -302 811 N ATOM 3776 CA PRO D 80 43.192 25.083 186.279 1.00 41.42 C ANISOU 3776 CA PRO D 80 3412 7707 4618 -1301 -278 681 C ATOM 3777 C PRO D 80 41.692 24.914 186.372 1.00 39.06 C ANISOU 3777 C PRO D 80 3408 6929 4503 -1115 -267 637 C ATOM 3778 O PRO D 80 41.233 23.846 186.747 1.00 37.97 O ANISOU 3778 O PRO D 80 3306 6743 4377 -827 -215 581 O ATOM 3779 CB PRO D 80 43.736 25.743 187.551 1.00 42.27 C ANISOU 3779 CB PRO D 80 3497 7864 4701 -1476 -380 633 C ATOM 3780 CG PRO D 80 45.034 26.334 187.103 1.00 45.54 C ANISOU 3780 CG PRO D 80 3648 8742 4911 -1848 -405 707 C ATOM 3781 CD PRO D 80 44.820 26.774 185.637 1.00 46.55 C ANISOU 3781 CD PRO D 80 3846 8842 5000 -2102 -382 847 C ATOM 3782 N SER D 81 40.931 25.928 185.974 1.00 39.44 N ANISOU 3782 N SER D 81 3678 6648 4659 -1285 -348 655 N ATOM 3783 CA SER D 81 39.474 25.821 185.999 1.00 38.02 C ANISOU 3783 CA SER D 81 3701 6128 4618 -1083 -346 553 C ATOM 3784 C SER D 81 38.869 24.991 184.855 1.00 36.67 C ANISOU 3784 C SER D 81 3537 5936 4460 -916 -233 603 C ATOM 3785 O SER D 81 37.654 24.874 184.774 1.00 35.51 O ANISOU 3785 O SER D 81 3515 5580 4396 -779 -225 513 O ATOM 3786 CB SER D 81 38.819 27.202 186.075 1.00 39.31 C ANISOU 3786 CB SER D 81 4113 5937 4887 -1205 -548 473 C ATOM 3787 OG SER D 81 38.985 27.942 184.881 1.00 40.60 O ANISOU 3787 OG SER D 81 4422 5962 5042 -1429 -660 627 O ATOM 3788 N ASP D 82 39.716 24.401 184.007 1.00 36.86 N ANISOU 3788 N ASP D 82 3392 6240 4375 -917 -152 706 N ATOM 3789 CA ASP D 82 39.269 23.547 182.920 1.00 36.06 C ANISOU 3789 CA ASP D 82 3289 6148 4263 -742 -57 729 C ATOM 3790 C ASP D 82 39.050 22.085 183.295 1.00 36.06 C ANISOU 3790 C ASP D 82 3296 6167 4236 -431 -1 657 C ATOM 3791 O ASP D 82 38.606 21.297 182.439 1.00 36.04 O ANISOU 3791 O ASP D 82 3344 6126 4226 -276 49 655 O ATOM 3792 CB ASP D 82 40.231 23.632 181.741 1.00 37.33 C ANISOU 3792 CB ASP D 82 3256 6655 4273 -882 -18 827 C ATOM 3793 CG ASP D 82 40.048 24.904 180.946 1.00 38.73 C ANISOU 3793 CG ASP D 82 3575 6695 4448 -1243 -108 964 C ATOM 3794 OD1 ASP D 82 38.962 25.521 181.042 1.00 38.20 O ANISOU 3794 OD1 ASP D 82 3784 6194 4535 -1233 -214 945 O ATOM 3795 OD2 ASP D 82 40.980 25.297 180.226 1.00 40.51 O ANISOU 3795 OD2 ASP D 82 3644 7266 4480 -1545 -105 1078 O ATOM 3796 N VAL D 83 39.379 21.719 184.539 1.00 36.53 N ANISOU 3796 N VAL D 83 3354 6264 4260 -364 -45 609 N ATOM 3797 CA VAL D 83 39.118 20.364 185.075 1.00 36.86 C ANISOU 3797 CA VAL D 83 3533 6228 4242 -139 -78 579 C ATOM 3798 C VAL D 83 37.624 19.985 184.983 1.00 35.25 C ANISOU 3798 C VAL D 83 3547 5762 4084 -171 -35 566 C ATOM 3799 O VAL D 83 36.756 20.818 185.245 1.00 34.78 O ANISOU 3799 O VAL D 83 3502 5617 4095 -319 -3 511 O ATOM 3800 CB VAL D 83 39.592 20.256 186.552 1.00 37.99 C ANISOU 3800 CB VAL D 83 3690 6429 4317 -150 -165 559 C ATOM 3801 CG1 VAL D 83 39.244 18.898 187.178 1.00 37.68 C ANISOU 3801 CG1 VAL D 83 3908 6237 4172 -8 -267 579 C ATOM 3802 CG2 VAL D 83 41.083 20.485 186.621 1.00 40.87 C ANISOU 3802 CG2 VAL D 83 3797 7130 4601 -97 -217 543 C ATOM 3803 N GLY D 84 37.335 18.759 184.550 1.00 34.05 N ANISOU 3803 N GLY D 84 3556 5511 3870 -22 -64 584 N ATOM 3804 CA GLY D 84 35.975 18.275 184.511 1.00 31.97 C ANISOU 3804 CA GLY D 84 3487 5072 3588 -126 -33 578 C ATOM 3805 C GLY D 84 35.861 17.139 183.525 1.00 31.98 C ANISOU 3805 C GLY D 84 3652 4952 3545 36 -78 600 C ATOM 3806 O GLY D 84 36.863 16.615 183.058 1.00 32.76 O ANISOU 3806 O GLY D 84 3727 5110 3612 292 -162 584 O ATOM 3807 N ILE D 85 34.629 16.758 183.218 1.00 31.90 N ANISOU 3807 N ILE D 85 3788 4822 3509 -101 -39 597 N ATOM 3808 CA ILE D 85 34.342 15.685 182.276 1.00 33.36 C ANISOU 3808 CA ILE D 85 4179 4852 3646 5 -99 608 C ATOM 3809 C ILE D 85 33.751 16.304 181.012 1.00 32.24 C ANISOU 3809 C ILE D 85 3870 4773 3609 6 40 564 C ATOM 3810 O ILE D 85 32.960 17.241 181.098 1.00 32.50 O ANISOU 3810 O ILE D 85 3765 4879 3704 -149 137 524 O ATOM 3811 CB ILE D 85 33.382 14.661 182.908 1.00 34.70 C ANISOU 3811 CB ILE D 85 4694 4847 3645 -247 -197 665 C ATOM 3812 CG1 ILE D 85 33.943 14.204 184.265 1.00 35.72 C ANISOU 3812 CG1 ILE D 85 5021 4911 3639 -309 -363 744 C ATOM 3813 CG2 ILE D 85 33.182 13.453 181.999 1.00 35.95 C ANISOU 3813 CG2 ILE D 85 5162 4763 3736 -146 -333 677 C ATOM 3814 CD1 ILE D 85 33.038 13.309 185.041 1.00 37.39 C ANISOU 3814 CD1 ILE D 85 5598 4998 3608 -700 -479 850 C ATOM 3815 N TYR D 86 34.175 15.816 179.848 1.00 32.44 N ANISOU 3815 N TYR D 86 3902 4790 3633 219 17 544 N ATOM 3816 CA TYR D 86 33.780 16.393 178.567 1.00 31.24 C ANISOU 3816 CA TYR D 86 3600 4721 3548 220 128 526 C ATOM 3817 C TYR D 86 33.037 15.377 177.682 1.00 32.17 C ANISOU 3817 C TYR D 86 3914 4702 3606 263 96 490 C ATOM 3818 O TYR D 86 33.469 14.239 177.529 1.00 33.31 O ANISOU 3818 O TYR D 86 4265 4726 3664 449 -43 451 O ATOM 3819 CB TYR D 86 35.003 16.927 177.841 1.00 31.42 C ANISOU 3819 CB TYR D 86 3378 4989 3570 361 159 525 C ATOM 3820 CG TYR D 86 35.610 18.166 178.444 1.00 30.81 C ANISOU 3820 CG TYR D 86 3111 5052 3543 215 190 580 C ATOM 3821 CD1 TYR D 86 35.362 19.418 177.898 1.00 30.19 C ANISOU 3821 CD1 TYR D 86 2940 5004 3526 30 233 643 C ATOM 3822 CD2 TYR D 86 36.458 18.085 179.540 1.00 31.14 C ANISOU 3822 CD2 TYR D 86 3113 5166 3554 256 129 572 C ATOM 3823 CE1 TYR D 86 35.919 20.553 178.449 1.00 30.89 C ANISOU 3823 CE1 TYR D 86 2942 5151 3645 -141 201 698 C ATOM 3824 CE2 TYR D 86 37.015 19.202 180.096 1.00 31.20 C ANISOU 3824 CE2 TYR D 86 2967 5295 3594 91 141 614 C ATOM 3825 CZ TYR D 86 36.753 20.433 179.556 1.00 31.17 C ANISOU 3825 CZ TYR D 86 2908 5284 3651 -121 171 677 C ATOM 3826 OH TYR D 86 37.317 21.544 180.139 1.00 31.69 O ANISOU 3826 OH TYR D 86 2902 5405 3735 -320 125 722 O ATOM 3827 N PHE D 87 31.917 15.802 177.105 1.00 32.32 N ANISOU 3827 N PHE D 87 3888 4730 3662 116 184 478 N ATOM 3828 CA PHE D 87 31.013 14.899 176.379 1.00 33.22 C ANISOU 3828 CA PHE D 87 4183 4736 3703 72 159 442 C ATOM 3829 C PHE D 87 30.786 15.423 175.006 1.00 31.78 C ANISOU 3829 C PHE D 87 3845 4663 3568 148 238 419 C ATOM 3830 O PHE D 87 30.490 16.596 174.847 1.00 30.87 O ANISOU 3830 O PHE D 87 3549 4645 3535 87 299 435 O ATOM 3831 CB PHE D 87 29.624 14.870 177.022 1.00 33.86 C ANISOU 3831 CB PHE D 87 4313 4834 3718 -239 189 418 C ATOM 3832 CG PHE D 87 29.538 14.014 178.217 1.00 36.21 C ANISOU 3832 CG PHE D 87 4861 5026 3869 -448 87 469 C ATOM 3833 CD1 PHE D 87 29.477 12.634 178.086 1.00 39.33 C ANISOU 3833 CD1 PHE D 87 5651 5172 4123 -515 -83 515 C ATOM 3834 CD2 PHE D 87 29.509 14.573 179.483 1.00 36.35 C ANISOU 3834 CD2 PHE D 87 4774 5173 3864 -600 119 474 C ATOM 3835 CE1 PHE D 87 29.389 11.790 179.222 1.00 42.04 C ANISOU 3835 CE1 PHE D 87 6337 5357 4278 -787 -247 614 C ATOM 3836 CE2 PHE D 87 29.419 13.756 180.619 1.00 39.02 C ANISOU 3836 CE2 PHE D 87 5374 5441 4010 -864 9 553 C ATOM 3837 CZ PHE D 87 29.361 12.357 180.488 1.00 41.48 C ANISOU 3837 CZ PHE D 87 6134 5468 4160 -983 -187 647 C ATOM 3838 N CYS D 88 30.880 14.551 174.016 1.00 32.25 N ANISOU 3838 N CYS D 88 4016 4681 3559 285 195 372 N ATOM 3839 CA CYS D 88 30.380 14.901 172.699 1.00 31.39 C ANISOU 3839 CA CYS D 88 3798 4677 3453 296 263 352 C ATOM 3840 C CYS D 88 28.977 14.350 172.526 1.00 30.29 C ANISOU 3840 C CYS D 88 3801 4444 3263 119 250 305 C ATOM 3841 O CYS D 88 28.593 13.369 173.170 1.00 30.16 O ANISOU 3841 O CYS D 88 4033 4269 3159 -16 164 292 O ATOM 3842 CB CYS D 88 31.274 14.368 171.591 1.00 33.21 C ANISOU 3842 CB CYS D 88 3995 5027 3597 545 241 285 C ATOM 3843 SG CYS D 88 31.072 12.629 171.317 1.00 36.28 S ANISOU 3843 SG CYS D 88 4743 5167 3874 703 68 144 S ATOM 3844 N ALA D 89 28.218 14.979 171.641 1.00 29.48 N ANISOU 3844 N ALA D 89 3561 4456 3182 84 307 287 N ATOM 3845 CA ALA D 89 26.854 14.542 171.385 1.00 30.45 C ANISOU 3845 CA ALA D 89 3741 4598 3231 -90 303 211 C ATOM 3846 C ALA D 89 26.550 14.594 169.906 1.00 30.72 C ANISOU 3846 C ALA D 89 3725 4708 3241 5 314 182 C ATOM 3847 O ALA D 89 26.970 15.513 169.223 1.00 30.56 O ANISOU 3847 O ALA D 89 3561 4779 3273 121 336 239 O ATOM 3848 CB ALA D 89 25.849 15.393 172.166 1.00 29.40 C ANISOU 3848 CB ALA D 89 3427 4624 3120 -240 333 146 C ATOM 3849 N GLY D 90 25.810 13.615 169.411 1.00 31.97 N ANISOU 3849 N GLY D 90 4030 4830 3288 -98 279 108 N ATOM 3850 CA GLY D 90 25.436 13.624 168.014 1.00 33.40 C ANISOU 3850 CA GLY D 90 4159 5105 3425 -21 286 65 C ATOM 3851 C GLY D 90 23.940 13.513 167.827 1.00 35.01 C ANISOU 3851 C GLY D 90 4312 5441 3549 -231 281 -29 C ATOM 3852 O GLY D 90 23.324 12.624 168.398 1.00 36.45 O ANISOU 3852 O GLY D 90 4646 5588 3616 -493 246 -76 O ATOM 3853 N GLY D 91 23.371 14.400 167.006 1.00 35.37 N ANISOU 3853 N GLY D 91 4160 5661 3619 -143 287 -55 N ATOM 3854 CA GLY D 91 21.931 14.497 166.829 1.00 36.83 C ANISOU 3854 CA GLY D 91 4200 6076 3718 -273 265 -196 C ATOM 3855 C GLY D 91 21.387 13.950 165.538 1.00 38.61 C ANISOU 3855 C GLY D 91 4464 6372 3833 -289 240 -252 C ATOM 3856 O GLY D 91 21.911 14.233 164.460 1.00 38.37 O ANISOU 3856 O GLY D 91 4450 6305 3823 -102 227 -184 O ATOM 3857 N THR D 92 20.304 13.190 165.650 1.00 41.04 N ANISOU 3857 N THR D 92 4770 6837 3985 -566 231 -378 N ATOM 3858 CA THR D 92 19.801 12.437 164.521 1.00 43.67 C ANISOU 3858 CA THR D 92 5193 7210 4189 -645 196 -442 C ATOM 3859 C THR D 92 18.489 12.960 163.987 1.00 45.46 C ANISOU 3859 C THR D 92 5127 7820 4327 -668 169 -597 C ATOM 3860 O THR D 92 18.000 12.511 162.962 1.00 48.02 O ANISOU 3860 O THR D 92 5476 8227 4542 -712 134 -659 O ATOM 3861 CB THR D 92 19.596 10.989 164.882 1.00 46.00 C ANISOU 3861 CB THR D 92 5800 7357 4322 -1006 147 -464 C ATOM 3862 OG1 THR D 92 19.123 10.297 163.716 1.00 48.57 O ANISOU 3862 OG1 THR D 92 6234 7699 4522 -1070 88 -545 O ATOM 3863 CG2 THR D 92 18.593 10.865 166.049 1.00 47.40 C ANISOU 3863 CG2 THR D 92 5854 7814 4343 -1436 168 -531 C ATOM 3864 N GLY D 93 17.912 13.914 164.678 1.00 45.78 N ANISOU 3864 N GLY D 93 4878 8118 4398 -598 157 -699 N ATOM 3865 CA GLY D 93 16.765 14.580 164.148 1.00 47.38 C ANISOU 3865 CA GLY D 93 4774 8700 4527 -472 72 -896 C ATOM 3866 C GLY D 93 16.138 15.193 165.350 1.00 48.96 C ANISOU 3866 C GLY D 93 4673 9236 4694 -476 63 -1091 C ATOM 3867 O GLY D 93 15.860 16.379 165.398 1.00 50.18 O ANISOU 3867 O GLY D 93 4626 9504 4934 -112 -68 -1222 O ATOM 3868 N ASN D 94 16.009 14.375 166.370 1.00 49.91 N ANISOU 3868 N ASN D 94 4810 9480 4674 -889 172 -1107 N ATOM 3869 CA ASN D 94 14.973 14.578 167.322 1.00 52.25 C ANISOU 3869 CA ASN D 94 4717 10367 4770 -1068 193 -1381 C ATOM 3870 C ASN D 94 15.522 14.045 168.617 1.00 52.07 C ANISOU 3870 C ASN D 94 4855 10233 4697 -1416 293 -1253 C ATOM 3871 O ASN D 94 15.023 14.343 169.693 1.00 53.50 O ANISOU 3871 O ASN D 94 4740 10855 4733 -1550 334 -1437 O ATOM 3872 CB ASN D 94 13.793 13.768 166.803 1.00 55.28 C ANISOU 3872 CB ASN D 94 4934 11222 4849 -1452 205 -1545 C ATOM 3873 CG ASN D 94 12.557 13.960 167.595 1.00 58.61 C ANISOU 3873 CG ASN D 94 4829 12472 4967 -1671 232 -1900 C ATOM 3874 OD1 ASN D 94 12.391 13.327 168.620 1.00 60.70 O ANISOU 3874 OD1 ASN D 94 5075 12990 4998 -2199 334 -1891 O ATOM 3875 ND2 ASN D 94 11.646 14.788 167.105 1.00 60.29 N ANISOU 3875 ND2 ASN D 94 4603 13173 5132 -1288 118 -2234 N ATOM 3876 N GLN D 95 16.593 13.270 168.507 1.00 50.79 N ANISOU 3876 N GLN D 95 5162 9498 4640 -1522 310 -959 N ATOM 3877 CA GLN D 95 17.248 12.739 169.696 1.00 51.21 C ANISOU 3877 CA GLN D 95 5451 9347 4657 -1800 349 -806 C ATOM 3878 C GLN D 95 18.769 12.840 169.619 1.00 47.49 C ANISOU 3878 C GLN D 95 5311 8267 4465 -1469 326 -569 C ATOM 3879 O GLN D 95 19.332 13.201 168.591 1.00 45.96 O ANISOU 3879 O GLN D 95 5175 7837 4448 -1107 298 -507 O ATOM 3880 CB GLN D 95 16.821 11.291 169.928 1.00 55.04 C ANISOU 3880 CB GLN D 95 6231 9843 4838 -2449 322 -727 C ATOM 3881 CG GLN D 95 16.483 10.986 171.373 1.00 58.19 C ANISOU 3881 CG GLN D 95 6585 10551 4973 -2966 359 -727 C ATOM 3882 CD GLN D 95 15.113 10.383 171.495 1.00 62.84 C ANISOU 3882 CD GLN D 95 6970 11777 5127 -3620 379 -878 C ATOM 3883 OE1 GLN D 95 14.876 9.254 171.058 1.00 65.52 O ANISOU 3883 OE1 GLN D 95 7688 11933 5275 -4079 281 -757 O ATOM 3884 NE2 GLN D 95 14.187 11.141 172.074 1.00 64.62 N ANISOU 3884 NE2 GLN D 95 6584 12802 5165 -3668 482 -1177 N ATOM 3885 N PHE D 96 19.428 12.547 170.728 1.00 46.36 N ANISOU 3885 N PHE D 96 5351 7946 4319 -1617 333 -448 N ATOM 3886 CA PHE D 96 20.871 12.708 170.820 1.00 43.20 C ANISOU 3886 CA PHE D 96 5176 7090 4148 -1299 310 -272 C ATOM 3887 C PHE D 96 21.558 11.503 171.453 1.00 42.66 C ANISOU 3887 C PHE D 96 5558 6661 3990 -1535 219 -113 C ATOM 3888 O PHE D 96 21.060 10.896 172.410 1.00 45.03 O ANISOU 3888 O PHE D 96 5977 7064 4066 -1993 186 -87 O ATOM 3889 CB PHE D 96 21.219 13.978 171.602 1.00 42.80 C ANISOU 3889 CB PHE D 96 4863 7145 4252 -1057 356 -308 C ATOM 3890 CG PHE D 96 21.209 15.211 170.765 1.00 42.62 C ANISOU 3890 CG PHE D 96 4624 7163 4405 -657 332 -373 C ATOM 3891 CD1 PHE D 96 22.386 15.723 170.260 1.00 40.93 C ANISOU 3891 CD1 PHE D 96 4524 6647 4381 -373 308 -215 C ATOM 3892 CD2 PHE D 96 20.025 15.857 170.471 1.00 44.39 C ANISOU 3892 CD2 PHE D 96 4544 7756 4566 -585 295 -598 C ATOM 3893 CE1 PHE D 96 22.379 16.852 169.481 1.00 40.74 C ANISOU 3893 CE1 PHE D 96 4393 6619 4467 -105 234 -221 C ATOM 3894 CE2 PHE D 96 20.011 16.970 169.675 1.00 44.09 C ANISOU 3894 CE2 PHE D 96 4415 7667 4672 -212 187 -635 C ATOM 3895 CZ PHE D 96 21.188 17.481 169.189 1.00 42.51 C ANISOU 3895 CZ PHE D 96 4407 7095 4648 -9 147 -418 C ATOM 3896 N TYR D 97 22.715 11.169 170.910 1.00 39.43 N ANISOU 3896 N TYR D 97 5403 5859 3720 -1217 146 -21 N ATOM 3897 CA TYR D 97 23.517 10.106 171.457 1.00 38.99 C ANISOU 3897 CA TYR D 97 5803 5406 3607 -1276 -20 87 C ATOM 3898 C TYR D 97 24.762 10.721 172.002 1.00 35.21 C ANISOU 3898 C TYR D 97 5244 4827 3309 -933 7 148 C ATOM 3899 O TYR D 97 25.320 11.610 171.398 1.00 32.43 O ANISOU 3899 O TYR D 97 4626 4574 3123 -593 105 126 O ATOM 3900 CB TYR D 97 23.830 9.074 170.388 1.00 40.91 C ANISOU 3900 CB TYR D 97 6401 5332 3813 -1129 -184 51 C ATOM 3901 CG TYR D 97 22.573 8.433 169.891 1.00 43.72 C ANISOU 3901 CG TYR D 97 6863 5781 3966 -1539 -227 -3 C ATOM 3902 CD1 TYR D 97 21.902 7.497 170.670 1.00 47.37 C ANISOU 3902 CD1 TYR D 97 7682 6150 4168 -2119 -376 74 C ATOM 3903 CD2 TYR D 97 22.026 8.790 168.665 1.00 43.34 C ANISOU 3903 CD2 TYR D 97 6562 5959 3947 -1413 -131 -115 C ATOM 3904 CE1 TYR D 97 20.729 6.917 170.227 1.00 50.63 C ANISOU 3904 CE1 TYR D 97 8173 6719 4346 -2588 -417 27 C ATOM 3905 CE2 TYR D 97 20.861 8.214 168.210 1.00 45.92 C ANISOU 3905 CE2 TYR D 97 6951 6426 4071 -1804 -171 -181 C ATOM 3906 CZ TYR D 97 20.217 7.281 168.992 1.00 49.46 C ANISOU 3906 CZ TYR D 97 7727 6811 4255 -2403 -306 -117 C ATOM 3907 OH TYR D 97 19.057 6.711 168.547 1.00 52.57 O ANISOU 3907 OH TYR D 97 8166 7405 4402 -2876 -349 -180 O ATOM 3908 N PHE D 98 25.189 10.246 173.158 1.00 35.26 N ANISOU 3908 N PHE D 98 5499 4652 3247 -1076 -102 241 N ATOM 3909 CA PHE D 98 26.253 10.906 173.876 1.00 33.29 C ANISOU 3909 CA PHE D 98 5121 4386 3140 -819 -66 290 C ATOM 3910 C PHE D 98 27.471 10.030 173.910 1.00 34.97 C ANISOU 3910 C PHE D 98 5692 4235 3359 -531 -282 315 C ATOM 3911 O PHE D 98 27.355 8.809 173.929 1.00 37.46 O ANISOU 3911 O PHE D 98 6485 4222 3526 -649 -525 331 O ATOM 3912 CB PHE D 98 25.803 11.253 175.296 1.00 32.79 C ANISOU 3912 CB PHE D 98 4971 4501 2985 -1162 -15 340 C ATOM 3913 CG PHE D 98 24.732 12.299 175.345 1.00 30.82 C ANISOU 3913 CG PHE D 98 4277 4698 2735 -1295 171 219 C ATOM 3914 CD1 PHE D 98 23.387 11.936 175.341 1.00 31.98 C ANISOU 3914 CD1 PHE D 98 4367 5129 2655 -1709 198 139 C ATOM 3915 CD2 PHE D 98 25.069 13.642 175.383 1.00 27.89 C ANISOU 3915 CD2 PHE D 98 3558 4477 2561 -999 277 158 C ATOM 3916 CE1 PHE D 98 22.397 12.892 175.361 1.00 31.72 C ANISOU 3916 CE1 PHE D 98 3878 5576 2599 -1731 329 -53 C ATOM 3917 CE2 PHE D 98 24.081 14.613 175.427 1.00 28.12 C ANISOU 3917 CE2 PHE D 98 3227 4869 2587 -1018 361 -11 C ATOM 3918 CZ PHE D 98 22.734 14.236 175.409 1.00 30.00 C ANISOU 3918 CZ PHE D 98 3350 5445 2603 -1338 389 -145 C ATOM 3919 N GLY D 99 28.643 10.664 173.916 1.00 34.74 N ANISOU 3919 N GLY D 99 5446 4278 3476 -150 -231 298 N ATOM 3920 CA GLY D 99 29.912 9.959 174.123 1.00 37.36 C ANISOU 3920 CA GLY D 99 6015 4384 3797 204 -447 260 C ATOM 3921 C GLY D 99 30.058 9.469 175.551 1.00 39.66 C ANISOU 3921 C GLY D 99 6626 4445 3997 15 -627 375 C ATOM 3922 O GLY D 99 29.269 9.829 176.427 1.00 40.17 O ANISOU 3922 O GLY D 99 6640 4619 4003 -412 -526 483 O ATOM 3923 N THR D 100 31.080 8.660 175.806 1.00 42.61 N ANISOU 3923 N THR D 100 7315 4545 4329 352 -916 325 N ATOM 3924 CA THR D 100 31.266 8.073 177.139 1.00 44.09 C ANISOU 3924 CA THR D 100 7910 4444 4396 182 -1167 456 C ATOM 3925 C THR D 100 31.913 9.031 178.102 1.00 41.56 C ANISOU 3925 C THR D 100 7237 4390 4164 221 -1011 512 C ATOM 3926 O THR D 100 31.842 8.840 179.308 1.00 42.97 O ANISOU 3926 O THR D 100 7642 4452 4234 -44 -1125 651 O ATOM 3927 CB THR D 100 32.095 6.794 177.084 1.00 48.66 C ANISOU 3927 CB THR D 100 9047 4559 4882 593 -1638 357 C ATOM 3928 OG1 THR D 100 33.000 6.863 175.966 1.00 48.95 O ANISOU 3928 OG1 THR D 100 8799 4783 5017 1219 -1625 88 O ATOM 3929 CG2 THR D 100 31.173 5.586 176.924 1.00 51.94 C ANISOU 3929 CG2 THR D 100 10140 4491 5106 241 -1947 432 C ATOM 3930 N GLY D 101 32.542 10.071 177.569 1.00 38.53 N ANISOU 3930 N GLY D 101 6321 4373 3944 500 -767 416 N ATOM 3931 CA GLY D 101 33.150 11.087 178.419 1.00 36.16 C ANISOU 3931 CA GLY D 101 5682 4331 3728 498 -622 463 C ATOM 3932 C GLY D 101 34.649 10.970 178.394 1.00 36.76 C ANISOU 3932 C GLY D 101 5648 4502 3816 987 -756 342 C ATOM 3933 O GLY D 101 35.181 9.867 178.382 1.00 39.14 O ANISOU 3933 O GLY D 101 6300 4548 4021 1307 -1078 245 O ATOM 3934 N THR D 102 35.333 12.104 178.358 1.00 35.26 N ANISOU 3934 N THR D 102 4981 4697 3718 1050 -547 321 N ATOM 3935 CA THR D 102 36.704 12.122 178.842 1.00 37.45 C ANISOU 3935 CA THR D 102 5106 5162 3961 1375 -663 232 C ATOM 3936 C THR D 102 36.891 13.021 180.043 1.00 36.41 C ANISOU 3936 C THR D 102 4810 5146 3877 1130 -563 354 C ATOM 3937 O THR D 102 36.543 14.195 180.013 1.00 33.59 O ANISOU 3937 O THR D 102 4174 4971 3616 857 -323 427 O ATOM 3938 CB THR D 102 37.771 12.437 177.779 1.00 38.65 C ANISOU 3938 CB THR D 102 4828 5777 4080 1715 -587 41 C ATOM 3939 OG1 THR D 102 38.772 13.296 178.345 1.00 38.86 O ANISOU 3939 OG1 THR D 102 4479 6185 4101 1708 -504 42 O ATOM 3940 CG2 THR D 102 37.183 13.075 176.591 1.00 37.18 C ANISOU 3940 CG2 THR D 102 4427 5762 3938 1526 -346 69 C ATOM 3941 N SER D 103 37.447 12.443 181.103 1.00 39.40 N ANISOU 3941 N SER D 103 5410 5385 4175 1255 -797 364 N ATOM 3942 CA SER D 103 37.755 13.182 182.315 1.00 39.31 C ANISOU 3942 CA SER D 103 5257 5500 4180 1065 -739 454 C ATOM 3943 C SER D 103 39.099 13.877 182.175 1.00 40.54 C ANISOU 3943 C SER D 103 4955 6102 4347 1303 -681 336 C ATOM 3944 O SER D 103 40.125 13.222 182.024 1.00 43.97 O ANISOU 3944 O SER D 103 5353 6669 4683 1737 -886 170 O ATOM 3945 CB SER D 103 37.787 12.245 183.518 1.00 41.42 C ANISOU 3945 CB SER D 103 5981 5445 4313 1059 -1043 536 C ATOM 3946 OG SER D 103 38.337 12.911 184.640 1.00 41.49 O ANISOU 3946 OG SER D 103 5808 5642 4316 965 -1011 582 O ATOM 3947 N LEU D 104 39.088 15.207 182.218 1.00 39.09 N ANISOU 3947 N LEU D 104 4430 6169 4252 1014 -435 399 N ATOM 3948 CA LEU D 104 40.317 16.005 182.133 1.00 39.95 C ANISOU 3948 CA LEU D 104 4108 6745 4327 1070 -369 329 C ATOM 3949 C LEU D 104 40.701 16.448 183.536 1.00 39.98 C ANISOU 3949 C LEU D 104 4092 6771 4328 939 -418 385 C ATOM 3950 O LEU D 104 39.868 16.973 184.288 1.00 39.24 O ANISOU 3950 O LEU D 104 4132 6467 4311 628 -347 496 O ATOM 3951 CB LEU D 104 40.095 17.251 181.270 1.00 38.26 C ANISOU 3951 CB LEU D 104 3628 6729 4181 759 -137 396 C ATOM 3952 CG LEU D 104 41.194 18.008 180.505 1.00 39.98 C ANISOU 3952 CG LEU D 104 3414 7489 4285 689 -46 351 C ATOM 3953 CD1 LEU D 104 41.075 19.510 180.815 1.00 38.80 C ANISOU 3953 CD1 LEU D 104 3190 7342 4209 224 50 506 C ATOM 3954 CD2 LEU D 104 42.630 17.526 180.743 1.00 42.60 C ANISOU 3954 CD2 LEU D 104 3451 8305 4432 999 -159 166 C ATOM 3955 N THR D 105 41.957 16.214 183.894 1.00 41.52 N ANISOU 3955 N THR D 105 4094 7275 4408 1204 -554 268 N ATOM 3956 CA THR D 105 42.507 16.798 185.104 1.00 41.19 C ANISOU 3956 CA THR D 105 3942 7362 4346 1065 -582 305 C ATOM 3957 C THR D 105 43.820 17.523 184.783 1.00 42.92 C ANISOU 3957 C THR D 105 3649 8196 4462 1067 -520 195 C ATOM 3958 O THR D 105 44.572 17.099 183.897 1.00 44.45 O ANISOU 3958 O THR D 105 3583 8782 4525 1359 -553 21 O ATOM 3959 CB THR D 105 42.596 15.770 186.287 1.00 42.53 C ANISOU 3959 CB THR D 105 4467 7261 4431 1285 -865 313 C ATOM 3960 OG1 THR D 105 43.777 16.008 187.060 1.00 43.69 O ANISOU 3960 OG1 THR D 105 4364 7756 4481 1412 -972 231 O ATOM 3961 CG2 THR D 105 42.575 14.335 185.778 1.00 44.34 C ANISOU 3961 CG2 THR D 105 5026 7239 4581 1720 -1131 219 C ATOM 3962 N VAL D 106 44.059 18.634 185.490 1.00 42.12 N ANISOU 3962 N VAL D 106 3396 8220 4386 708 -435 277 N ATOM 3963 CA VAL D 106 45.108 19.593 185.129 1.00 43.46 C ANISOU 3963 CA VAL D 106 3115 8958 4439 478 -346 239 C ATOM 3964 C VAL D 106 46.232 19.599 186.173 1.00 45.69 C ANISOU 3964 C VAL D 106 3171 9602 4589 573 -475 140 C ATOM 3965 O VAL D 106 46.005 19.939 187.330 1.00 46.03 O ANISOU 3965 O VAL D 106 3383 9402 4702 421 -521 219 O ATOM 3966 CB VAL D 106 44.512 21.035 184.886 1.00 41.77 C ANISOU 3966 CB VAL D 106 2951 8580 4339 -84 -196 416 C ATOM 3967 CG1 VAL D 106 45.593 22.105 184.791 1.00 44.23 C ANISOU 3967 CG1 VAL D 106 2913 9401 4492 -475 -166 435 C ATOM 3968 CG2 VAL D 106 43.643 21.066 183.617 1.00 40.25 C ANISOU 3968 CG2 VAL D 106 2885 8187 4219 -145 -92 484 C ATOM 3969 N ILE D 107 47.433 19.183 185.780 1.00 47.91 N ANISOU 3969 N ILE D 107 3040 10514 4648 859 -547 -72 N ATOM 3970 CA ILE D 107 48.564 19.242 186.684 1.00 49.93 C ANISOU 3970 CA ILE D 107 3005 11222 4745 957 -676 -200 C ATOM 3971 C ILE D 107 48.990 20.701 186.818 1.00 49.97 C ANISOU 3971 C ILE D 107 2740 11553 4694 305 -522 -83 C ATOM 3972 O ILE D 107 49.217 21.371 185.824 1.00 50.65 O ANISOU 3972 O ILE D 107 2577 11997 4671 -57 -374 -45 O ATOM 3973 CB ILE D 107 49.737 18.406 186.177 1.00 54.28 C ANISOU 3973 CB ILE D 107 3119 12474 5033 1499 -821 -537 C ATOM 3974 CG1 ILE D 107 49.274 17.033 185.692 1.00 54.81 C ANISOU 3974 CG1 ILE D 107 3509 12172 5145 2127 -1008 -673 C ATOM 3975 CG2 ILE D 107 50.726 18.193 187.270 1.00 57.25 C ANISOU 3975 CG2 ILE D 107 3296 13190 5267 1757 -1036 -695 C ATOM 3976 CD1 ILE D 107 50.417 16.202 185.041 1.00 60.07 C ANISOU 3976 CD1 ILE D 107 3720 13572 5532 2780 -1195 -1107 C ATOM 3977 N PRO D 108 49.042 21.215 188.055 1.00 49.81 N ANISOU 3977 N PRO D 108 2830 11365 4730 105 -583 -7 N ATOM 3978 CA PRO D 108 49.344 22.641 188.264 1.00 49.96 C ANISOU 3978 CA PRO D 108 2718 11551 4713 -544 -497 111 C ATOM 3979 C PRO D 108 50.839 22.991 188.270 1.00 53.82 C ANISOU 3979 C PRO D 108 2626 12938 4884 -720 -520 -31 C ATOM 3980 O PRO D 108 51.648 22.215 188.760 1.00 55.86 O ANISOU 3980 O PRO D 108 2615 13614 4994 -271 -653 -246 O ATOM 3981 CB PRO D 108 48.721 22.919 189.637 1.00 47.34 C ANISOU 3981 CB PRO D 108 2751 10677 4559 -609 -575 194 C ATOM 3982 CG PRO D 108 48.823 21.597 190.334 1.00 48.00 C ANISOU 3982 CG PRO D 108 2928 10695 4615 -24 -737 82 C ATOM 3983 CD PRO D 108 48.557 20.569 189.292 1.00 48.21 C ANISOU 3983 CD PRO D 108 3004 10672 4642 385 -742 17 C ATOM 3984 N ASN D 109 51.186 24.160 187.733 1.00 55.32 N ANISOU 3984 N ASN D 109 2650 13429 4942 -1394 -424 88 N ATOM 3985 CA ASN D 109 52.571 24.632 187.690 1.00 60.78 C ANISOU 3985 CA ASN D 109 2765 15063 5266 -1747 -426 -21 C ATOM 3986 C ASN D 109 53.047 25.190 189.027 1.00 61.54 C ANISOU 3986 C ASN D 109 2855 15176 5350 -1960 -542 -23 C ATOM 3987 O ASN D 109 52.516 26.196 189.499 1.00 59.73 O ANISOU 3987 O ASN D 109 3015 14399 5280 -2433 -573 172 O ATOM 3988 CB ASN D 109 52.739 25.693 186.597 1.00 63.62 C ANISOU 3988 CB ASN D 109 3027 15718 5426 -2532 -316 163 C ATOM 3989 CG ASN D 109 53.036 25.090 185.233 1.00 66.06 C ANISOU 3989 CG ASN D 109 2950 16655 5495 -2379 -191 39 C ATOM 3990 OD1 ASN D 109 54.069 24.457 185.042 1.00 70.62 O ANISOU 3990 OD1 ASN D 109 2909 18169 5754 -2086 -183 -261 O ATOM 3991 ND2 ASN D 109 52.139 25.303 184.273 1.00 63.80 N ANISOU 3991 ND2 ASN D 109 3002 15905 5334 -2553 -111 233 N ATOM 3992 N ILE D 110 54.056 24.543 189.617 1.00 64.29 N ANISOU 3992 N ILE D 110 2764 16168 5496 -1574 -641 -276 N ATOM 3993 CA ILE D 110 54.514 24.868 190.974 1.00 64.84 C ANISOU 3993 CA ILE D 110 2817 16269 5549 -1655 -773 -309 C ATOM 3994 C ILE D 110 55.863 25.592 190.993 1.00 70.33 C ANISOU 3994 C ILE D 110 2912 17961 5850 -2191 -774 -409 C ATOM 3995 O ILE D 110 56.914 25.023 190.676 1.00 73.28 O ANISOU 3995 O ILE D 110 2645 19304 5892 -1918 -793 -690 O ATOM 3996 CB ILE D 110 54.589 23.621 191.868 1.00 64.42 C ANISOU 3996 CB ILE D 110 2812 16106 5558 -829 -957 -497 C ATOM 3997 CG1 ILE D 110 53.249 22.920 191.910 1.00 60.01 C ANISOU 3997 CG1 ILE D 110 2872 14602 5328 -439 -970 -368 C ATOM 3998 CG2 ILE D 110 54.934 23.998 193.283 1.00 65.48 C ANISOU 3998 CG2 ILE D 110 2989 16209 5682 -947 -1090 -499 C ATOM 3999 CD1 ILE D 110 52.240 23.606 192.789 1.00 57.12 C ANISOU 3999 CD1 ILE D 110 3027 13457 5217 -770 -950 -153 C ATOM 4000 N GLN D 111 55.792 26.854 191.399 1.00 59.51 N ANISOU 4000 N GLN D 111 6635 11404 4573 233 -45 -1577 N ATOM 4001 CA GLN D 111 56.906 27.792 191.395 1.00 62.83 C ANISOU 4001 CA GLN D 111 6818 12055 5002 -20 112 -1272 C ATOM 4002 C GLN D 111 57.989 27.490 192.420 1.00 63.05 C ANISOU 4002 C GLN D 111 6559 12169 5229 -78 136 -1298 C ATOM 4003 O GLN D 111 59.152 27.281 192.067 1.00 65.41 O ANISOU 4003 O GLN D 111 6555 12863 5436 -28 324 -1210 O ATOM 4004 CB GLN D 111 56.374 29.211 191.646 1.00 63.05 C ANISOU 4004 CB GLN D 111 6975 11773 5209 -355 24 -1011 C ATOM 4005 CG GLN D 111 55.410 29.738 190.579 1.00 64.58 C ANISOU 4005 CG GLN D 111 7391 11908 5238 -333 -20 -851 C ATOM 4006 CD GLN D 111 56.129 30.408 189.410 1.00 68.96 C ANISOU 4006 CD GLN D 111 7838 12857 5506 -450 171 -492 C ATOM 4007 OE1 GLN D 111 56.265 31.631 189.378 1.00 70.78 O ANISOU 4007 OE1 GLN D 111 8056 12961 5876 -743 189 -142 O ATOM 4008 NE2 GLN D 111 56.597 29.608 188.452 1.00 71.20 N ANISOU 4008 NE2 GLN D 111 8052 13609 5392 -228 334 -581 N ATOM 4009 N ASN D 112 57.616 27.509 193.696 1.00 60.71 N ANISOU 4009 N ASN D 112 6338 11533 5196 -199 -52 -1395 N ATOM 4010 CA ASN D 112 58.603 27.356 194.756 1.00 61.42 C ANISOU 4010 CA ASN D 112 6169 11715 5452 -321 -96 -1369 C ATOM 4011 C ASN D 112 58.252 26.264 195.731 1.00 59.49 C ANISOU 4011 C ASN D 112 5987 11286 5332 -139 -261 -1601 C ATOM 4012 O ASN D 112 57.715 26.528 196.800 1.00 56.81 O ANISOU 4012 O ASN D 112 5799 10658 5128 -325 -419 -1655 O ATOM 4013 CB ASN D 112 58.796 28.672 195.483 1.00 61.95 C ANISOU 4013 CB ASN D 112 6235 11624 5680 -772 -164 -1192 C ATOM 4014 CG ASN D 112 59.292 29.757 194.567 1.00 65.24 C ANISOU 4014 CG ASN D 112 6550 12210 6027 -992 -3 -893 C ATOM 4015 OD1 ASN D 112 58.548 30.676 194.221 1.00 65.21 O ANISOU 4015 OD1 ASN D 112 6776 11944 6056 -1138 -11 -787 O ATOM 4016 ND2 ASN D 112 60.539 29.631 194.120 1.00 68.45 N ANISOU 4016 ND2 ASN D 112 6591 13062 6354 -997 157 -725 N ATOM 4017 N PRO D 113 58.580 25.020 195.362 1.00 61.30 N ANISOU 4017 N PRO D 113 6099 11676 5515 227 -205 -1737 N ATOM 4018 CA PRO D 113 58.162 23.838 196.105 1.00 60.37 C ANISOU 4018 CA PRO D 113 6064 11341 5532 446 -356 -1931 C ATOM 4019 C PRO D 113 59.124 23.423 197.223 1.00 61.76 C ANISOU 4019 C PRO D 113 5963 11627 5877 408 -468 -1826 C ATOM 4020 O PRO D 113 60.218 22.934 196.949 1.00 65.34 O ANISOU 4020 O PRO D 113 6080 12380 6368 592 -369 -1754 O ATOM 4021 CB PRO D 113 58.132 22.747 195.022 1.00 61.79 C ANISOU 4021 CB PRO D 113 6253 11618 5605 863 -226 -2134 C ATOM 4022 CG PRO D 113 58.979 23.296 193.853 1.00 64.71 C ANISOU 4022 CG PRO D 113 6424 12409 5753 872 37 -2011 C ATOM 4023 CD PRO D 113 59.435 24.671 194.213 1.00 64.53 C ANISOU 4023 CD PRO D 113 6278 12485 5757 455 37 -1710 C ATOM 4024 N ASP D 114 58.732 23.602 198.477 1.00 60.02 N ANISOU 4024 N ASP D 114 5864 11193 5749 178 -669 -1806 N ATOM 4025 CA ASP D 114 59.501 22.978 199.557 1.00 61.10 C ANISOU 4025 CA ASP D 114 5775 11432 6008 179 -835 -1698 C ATOM 4026 C ASP D 114 58.650 22.057 200.439 1.00 58.60 C ANISOU 4026 C ASP D 114 5684 10808 5772 282 -1009 -1795 C ATOM 4027 O ASP D 114 58.002 22.485 201.409 1.00 55.97 O ANISOU 4027 O ASP D 114 5566 10300 5402 5 -1131 -1805 O ATOM 4028 CB ASP D 114 60.349 23.978 200.361 1.00 63.26 C ANISOU 4028 CB ASP D 114 5852 11911 6271 -244 -940 -1498 C ATOM 4029 CG ASP D 114 59.518 25.028 201.067 1.00 61.68 C ANISOU 4029 CG ASP D 114 5977 11454 6004 -641 -1016 -1570 C ATOM 4030 OD1 ASP D 114 59.998 25.546 202.098 1.00 63.28 O ANISOU 4030 OD1 ASP D 114 6116 11740 6187 -988 -1177 -1490 O ATOM 4031 OD2 ASP D 114 58.384 25.310 200.606 1.00 59.40 O ANISOU 4031 OD2 ASP D 114 5998 10881 5688 -599 -923 -1719 O ATOM 4032 N PRO D 115 58.675 20.766 200.086 1.00 58.66 N ANISOU 4032 N PRO D 115 5641 10747 5900 683 -998 -1871 N ATOM 4033 CA PRO D 115 57.966 19.683 200.738 1.00 57.53 C ANISOU 4033 CA PRO D 115 5673 10299 5888 832 -1144 -1927 C ATOM 4034 C PRO D 115 58.246 19.637 202.248 1.00 57.82 C ANISOU 4034 C PRO D 115 5654 10371 5945 597 -1377 -1707 C ATOM 4035 O PRO D 115 59.372 19.885 202.693 1.00 59.22 O ANISOU 4035 O PRO D 115 5527 10852 6123 490 -1464 -1498 O ATOM 4036 CB PRO D 115 58.509 18.437 200.024 1.00 60.08 C ANISOU 4036 CB PRO D 115 5820 10622 6387 1301 -1070 -1999 C ATOM 4037 CG PRO D 115 59.837 18.852 199.490 1.00 62.84 C ANISOU 4037 CG PRO D 115 5782 11383 6709 1356 -927 -1883 C ATOM 4038 CD PRO D 115 59.632 20.269 199.083 1.00 61.26 C ANISOU 4038 CD PRO D 115 5674 11326 6275 1013 -823 -1880 C ATOM 4039 N ALA D 116 57.188 19.386 203.010 1.00 56.15 N ANISOU 4039 N ALA D 116 5731 9882 5720 484 -1474 -1748 N ATOM 4040 CA ALA D 116 57.248 19.342 204.450 1.00 56.67 C ANISOU 4040 CA ALA D 116 5825 9990 5716 230 -1678 -1559 C ATOM 4041 C ALA D 116 56.052 18.562 204.957 1.00 55.82 C ANISOU 4041 C ALA D 116 5998 9543 5667 271 -1722 -1602 C ATOM 4042 O ALA D 116 54.988 18.547 204.335 1.00 53.22 O ANISOU 4042 O ALA D 116 5882 8955 5383 343 -1595 -1814 O ATOM 4043 CB ALA D 116 57.219 20.729 205.006 1.00 55.44 C ANISOU 4043 CB ALA D 116 5761 9971 5332 -216 -1672 -1584 C ATOM 4044 N VAL D 117 56.240 17.908 206.094 1.00 58.46 N ANISOU 4044 N VAL D 117 6309 9902 6000 207 -1919 -1361 N ATOM 4045 CA VAL D 117 55.146 17.262 206.796 1.00 58.27 C ANISOU 4045 CA VAL D 117 6540 9606 5995 153 -1959 -1329 C ATOM 4046 C VAL D 117 54.940 18.009 208.117 1.00 59.44 C ANISOU 4046 C VAL D 117 6831 9935 5819 -286 -2022 -1241 C ATOM 4047 O VAL D 117 55.882 18.182 208.886 1.00 62.10 O ANISOU 4047 O VAL D 117 7019 10580 5997 -456 -2206 -1026 O ATOM 4048 CB VAL D 117 55.426 15.758 207.047 1.00 60.58 C ANISOU 4048 CB VAL D 117 6730 9734 6553 444 -2125 -1085 C ATOM 4049 CG1 VAL D 117 54.313 15.125 207.865 1.00 60.28 C ANISOU 4049 CG1 VAL D 117 6944 9434 6525 321 -2167 -984 C ATOM 4050 CG2 VAL D 117 55.612 15.014 205.728 1.00 60.29 C ANISOU 4050 CG2 VAL D 117 6589 9487 6831 886 -2029 -1260 C ATOM 4051 N TYR D 118 53.720 18.476 208.366 1.00 58.27 N ANISOU 4051 N TYR D 118 6959 9616 5565 -474 -1867 -1425 N ATOM 4052 CA TYR D 118 53.405 19.185 209.608 1.00 59.64 C ANISOU 4052 CA TYR D 118 7312 9943 5406 -878 -1859 -1420 C ATOM 4053 C TYR D 118 52.414 18.410 210.466 1.00 60.67 C ANISOU 4053 C TYR D 118 7631 9925 5496 -945 -1844 -1301 C ATOM 4054 O TYR D 118 51.638 17.616 209.943 1.00 60.10 O ANISOU 4054 O TYR D 118 7594 9546 5694 -722 -1781 -1317 O ATOM 4055 CB TYR D 118 52.836 20.562 209.279 1.00 57.59 C ANISOU 4055 CB TYR D 118 7199 9624 5059 -1064 -1631 -1748 C ATOM 4056 CG TYR D 118 53.816 21.416 208.532 1.00 57.62 C ANISOU 4056 CG TYR D 118 7030 9783 5081 -1074 -1641 -1814 C ATOM 4057 CD1 TYR D 118 55.035 21.767 209.107 1.00 60.53 C ANISOU 4057 CD1 TYR D 118 7239 10487 5274 -1287 -1827 -1671 C ATOM 4058 CD2 TYR D 118 53.545 21.862 207.255 1.00 55.23 C ANISOU 4058 CD2 TYR D 118 6703 9320 4963 -897 -1483 -1984 C ATOM 4059 CE1 TYR D 118 55.954 22.547 208.426 1.00 60.66 C ANISOU 4059 CE1 TYR D 118 7058 10655 5335 -1331 -1827 -1699 C ATOM 4060 CE2 TYR D 118 54.449 22.649 206.570 1.00 55.85 C ANISOU 4060 CE2 TYR D 118 6615 9558 5047 -934 -1471 -1995 C ATOM 4061 CZ TYR D 118 55.649 22.993 207.158 1.00 58.26 C ANISOU 4061 CZ TYR D 118 6746 10177 5213 -1155 -1629 -1855 C ATOM 4062 OH TYR D 118 56.550 23.766 206.457 1.00 58.66 O ANISOU 4062 OH TYR D 118 6597 10391 5302 -1218 -1604 -1837 O ATOM 4063 N GLN D 119 52.429 18.638 211.777 1.00 62.95 N ANISOU 4063 N GLN D 119 8043 10446 5430 -1277 -1901 -1181 N ATOM 4064 CA GLN D 119 51.403 18.059 212.635 1.00 64.43 C ANISOU 4064 CA GLN D 119 8423 10540 5518 -1397 -1821 -1068 C ATOM 4065 C GLN D 119 50.434 19.114 213.119 1.00 64.51 C ANISOU 4065 C GLN D 119 8667 10559 5283 -1678 -1527 -1377 C ATOM 4066 O GLN D 119 50.794 19.980 213.908 1.00 66.34 O ANISOU 4066 O GLN D 119 9007 11064 5136 -1992 -1520 -1480 O ATOM 4067 CB GLN D 119 51.989 17.313 213.837 1.00 68.27 C ANISOU 4067 CB GLN D 119 8898 11290 5751 -1548 -2081 -642 C ATOM 4068 CG GLN D 119 50.892 16.690 214.709 1.00 69.78 C ANISOU 4068 CG GLN D 119 9291 11401 5823 -1695 -1964 -478 C ATOM 4069 CD GLN D 119 51.413 15.776 215.799 1.00 74.04 C ANISOU 4069 CD GLN D 119 9818 12164 6150 -1811 -2246 40 C ATOM 4070 OE1 GLN D 119 52.242 14.900 215.555 1.00 75.19 O ANISOU 4070 OE1 GLN D 119 9756 12256 6557 -1566 -2530 368 O ATOM 4071 NE2 GLN D 119 50.906 15.965 217.010 1.00 76.82 N ANISOU 4071 NE2 GLN D 119 10390 12770 6028 -2173 -2157 128 N ATOM 4072 N LEU D 120 49.194 19.017 212.658 1.00 63.45 N ANISOU 4072 N LEU D 120 8601 10119 5386 -1566 -1288 -1536 N ATOM 4073 CA LEU D 120 48.158 19.973 213.034 1.00 64.43 C ANISOU 4073 CA LEU D 120 8901 10201 5380 -1761 -963 -1835 C ATOM 4074 C LEU D 120 47.322 19.449 214.219 1.00 68.32 C ANISOU 4074 C LEU D 120 9536 10776 5647 -1965 -824 -1685 C ATOM 4075 O LEU D 120 47.055 18.243 214.322 1.00 69.67 O ANISOU 4075 O LEU D 120 9655 10849 5966 -1873 -923 -1373 O ATOM 4076 CB LEU D 120 47.271 20.286 211.832 1.00 60.72 C ANISOU 4076 CB LEU D 120 8370 9390 5312 -1527 -785 -2074 C ATOM 4077 CG LEU D 120 47.971 20.575 210.502 1.00 58.38 C ANISOU 4077 CG LEU D 120 7928 9008 5247 -1290 -911 -2159 C ATOM 4078 CD1 LEU D 120 46.945 20.867 209.467 1.00 56.27 C ANISOU 4078 CD1 LEU D 120 7632 8450 5300 -1110 -754 -2351 C ATOM 4079 CD2 LEU D 120 48.918 21.736 210.568 1.00 58.92 C ANISOU 4079 CD2 LEU D 120 8006 9269 5110 -1454 -934 -2290 C ATOM 4080 N ARG D 121 46.912 20.349 215.113 1.00 70.81 N ANISOU 4080 N ARG D 121 10038 11261 5606 -2251 -575 -1909 N ATOM 4081 CA ARG D 121 46.242 19.929 216.345 1.00 74.78 C ANISOU 4081 CA ARG D 121 10689 11946 5779 -2490 -410 -1763 C ATOM 4082 C ARG D 121 44.762 20.291 216.406 1.00 74.69 C ANISOU 4082 C ARG D 121 10720 11754 5905 -2494 34 -2006 C ATOM 4083 O ARG D 121 44.332 21.259 215.787 1.00 72.50 O ANISOU 4083 O ARG D 121 10422 11276 5848 -2393 239 -2370 O ATOM 4084 CB ARG D 121 46.967 20.502 217.559 1.00 79.33 C ANISOU 4084 CB ARG D 121 11463 12957 5721 -2859 -466 -1801 C ATOM 4085 CG ARG D 121 48.412 20.072 217.654 1.00 81.56 C ANISOU 4085 CG ARG D 121 11650 13480 5859 -2885 -934 -1487 C ATOM 4086 CD ARG D 121 48.872 20.108 219.097 1.00 87.90 C ANISOU 4086 CD ARG D 121 12645 14769 5985 -3285 -1048 -1335 C ATOM 4087 NE ARG D 121 49.912 19.129 219.404 1.00 90.90 N ANISOU 4087 NE ARG D 121 12886 15374 6276 -3276 -1511 -801 N ATOM 4088 CZ ARG D 121 49.692 17.838 219.655 1.00 92.77 C ANISOU 4088 CZ ARG D 121 13062 15565 6623 -3172 -1633 -304 C ATOM 4089 NH1 ARG D 121 50.718 17.048 219.943 1.00 95.59 N ANISOU 4089 NH1 ARG D 121 13277 16111 6934 -3143 -2071 187 N ATOM 4090 NH2 ARG D 121 48.462 17.326 219.622 1.00 92.10 N ANISOU 4090 NH2 ARG D 121 13031 15229 6733 -3099 -1332 -268 N ATOM 4091 N ASP D 122 44.002 19.518 217.181 1.00 77.28 N ANISOU 4091 N ASP D 122 11084 12163 6115 -2617 181 -1766 N ATOM 4092 CA ASP D 122 42.562 19.710 217.323 1.00 78.16 C ANISOU 4092 CA ASP D 122 11171 12147 6381 -2628 621 -1928 C ATOM 4093 C ASP D 122 42.200 20.932 218.143 1.00 81.72 C ANISOU 4093 C ASP D 122 11811 12792 6447 -2841 1023 -2341 C ATOM 4094 O ASP D 122 42.694 21.122 219.265 1.00 85.53 O ANISOU 4094 O ASP D 122 12519 13655 6324 -3141 1040 -2339 O ATOM 4095 CB ASP D 122 41.930 18.456 217.917 1.00 80.32 C ANISOU 4095 CB ASP D 122 11404 12466 6650 -2727 656 -1494 C ATOM 4096 CG ASP D 122 40.462 18.615 218.219 1.00 81.73 C ANISOU 4096 CG ASP D 122 11514 12591 6948 -2786 1139 -1616 C ATOM 4097 OD1 ASP D 122 39.687 19.104 217.370 1.00 78.66 O ANISOU 4097 OD1 ASP D 122 10956 11912 7020 -2581 1313 -1886 O ATOM 4098 OD2 ASP D 122 40.085 18.213 219.329 1.00 86.26 O ANISOU 4098 OD2 ASP D 122 12185 13443 7147 -3046 1342 -1399 O ATOM 4099 N SER D 123 41.318 21.749 217.568 1.00 81.02 N ANISOU 4099 N SER D 123 11630 12433 6720 -2678 1340 -2698 N ATOM 4100 CA SER D 123 40.869 22.980 218.208 1.00 84.89 C ANISOU 4100 CA SER D 123 12280 12994 6979 -2807 1777 -3160 C ATOM 4101 C SER D 123 39.908 22.717 219.350 1.00 90.06 C ANISOU 4101 C SER D 123 13000 13892 7326 -3006 2216 -3138 C ATOM 4102 O SER D 123 39.733 23.576 220.200 1.00 94.33 O ANISOU 4102 O SER D 123 13749 14613 7478 -3186 2577 -3507 O ATOM 4103 CB SER D 123 40.229 23.941 217.200 1.00 82.57 C ANISOU 4103 CB SER D 123 11835 12295 7245 -2529 1968 -3501 C ATOM 4104 OG SER D 123 39.107 23.356 216.568 1.00 81.81 O ANISOU 4104 OG SER D 123 11450 11969 7664 -2312 2073 -3336 O ATOM 4105 N LYS D 124 39.281 21.545 219.380 1.00 90.98 N ANISOU 4105 N LYS D 124 12944 14012 7613 -2989 2209 -2721 N ATOM 4106 CA LYS D 124 38.449 21.211 220.530 1.00 97.12 C ANISOU 4106 CA LYS D 124 13775 15086 8041 -3224 2628 -2619 C ATOM 4107 C LYS D 124 39.162 20.362 221.584 1.00101.13 C ANISOU 4107 C LYS D 124 14496 16024 7907 -3543 2411 -2199 C ATOM 4108 O LYS D 124 38.844 19.183 221.774 1.00102.32 O ANISOU 4108 O LYS D 124 14538 16209 8130 -3606 2326 -1695 O ATOM 4109 CB LYS D 124 37.072 20.651 220.128 1.00 96.85 C ANISOU 4109 CB LYS D 124 13407 14827 8563 -3080 2895 -2458 C ATOM 4110 CG LYS D 124 36.035 21.744 219.801 1.00 97.21 C ANISOU 4110 CG LYS D 124 13287 14662 8986 -2885 3376 -2929 C ATOM 4111 CD LYS D 124 36.347 23.088 220.510 1.00100.06 C ANISOU 4111 CD LYS D 124 13944 15182 8893 -2985 3702 -3477 C ATOM 4112 CE LYS D 124 35.612 23.284 221.844 1.00106.68 C ANISOU 4112 CE LYS D 124 14902 16393 9238 -3222 4321 -3640 C ATOM 4113 NZ LYS D 124 34.451 24.205 221.729 1.00108.80 N ANISOU 4113 NZ LYS D 124 14973 16454 9914 -3007 4909 -4070 N ATOM 4114 N SER D 125 40.125 21.006 222.251 1.00104.08 N ANISOU 4114 N SER D 125 15165 16707 7673 -3758 2302 -2402 N ATOM 4115 CA SER D 125 40.941 20.468 223.363 1.00108.96 C ANISOU 4115 CA SER D 125 16026 17821 7553 -4103 2063 -2060 C ATOM 4116 C SER D 125 41.928 19.349 223.020 1.00107.55 C ANISOU 4116 C SER D 125 15752 17614 7499 -4045 1433 -1472 C ATOM 4117 O SER D 125 43.143 19.549 223.125 1.00107.60 O ANISOU 4117 O SER D 125 15867 17798 7219 -4129 1030 -1447 O ATOM 4118 CB SER D 125 40.096 20.062 224.584 1.00114.88 C ANISOU 4118 CB SER D 125 16889 18965 7795 -4394 2496 -1880 C ATOM 4119 OG SER D 125 39.141 21.055 224.889 1.00117.41 O ANISOU 4119 OG SER D 125 17262 19299 8051 -4403 3135 -2441 O ATOM 4120 N SER D 126 41.393 18.202 222.594 1.00106.83 N ANISOU 4120 N SER D 126 15438 17275 7877 -3896 1358 -1023 N ATOM 4121 CA SER D 126 42.075 16.895 222.651 1.00107.51 C ANISOU 4121 CA SER D 126 15469 17369 8010 -3899 875 -366 C ATOM 4122 C SER D 126 43.366 16.706 221.842 1.00103.49 C ANISOU 4122 C SER D 126 14870 16687 7765 -3673 311 -268 C ATOM 4123 O SER D 126 43.759 17.554 221.032 1.00 99.86 O ANISOU 4123 O SER D 126 14361 16057 7524 -3491 260 -693 O ATOM 4124 CB SER D 126 41.087 15.770 222.291 1.00107.58 C ANISOU 4124 CB SER D 126 15261 17048 8565 -3793 965 16 C ATOM 4125 OG SER D 126 40.767 15.783 220.905 1.00102.51 O ANISOU 4125 OG SER D 126 14381 15887 8683 -3437 900 -207 O ATOM 4126 N ASP D 127 44.008 15.561 222.073 1.00104.75 N ANISOU 4126 N ASP D 127 14990 16885 7927 -3679 -94 330 N ATOM 4127 CA ASP D 127 45.203 15.166 221.332 1.00101.52 C ANISOU 4127 CA ASP D 127 14439 16302 7833 -3425 -606 501 C ATOM 4128 C ASP D 127 44.856 14.272 220.131 1.00 97.30 C ANISOU 4128 C ASP D 127 13671 15187 8111 -3056 -712 620 C ATOM 4129 O ASP D 127 45.638 13.396 219.750 1.00 96.89 O ANISOU 4129 O ASP D 127 13502 14956 8356 -2856 -1107 968 O ATOM 4130 CB ASP D 127 46.226 14.495 222.262 1.00106.35 C ANISOU 4130 CB ASP D 127 15116 17281 8010 -3606 -1024 1073 C ATOM 4131 CG ASP D 127 45.568 13.673 223.372 1.00112.02 C ANISOU 4131 CG ASP D 127 15959 18212 8391 -3891 -901 1591 C ATOM 4132 OD1 ASP D 127 44.342 13.417 223.296 1.00112.00 O ANISOU 4132 OD1 ASP D 127 15935 17997 8622 -3905 -518 1562 O ATOM 4133 OD2 ASP D 127 46.286 13.280 224.323 1.00116.91 O ANISOU 4133 OD2 ASP D 127 16679 19233 8509 -4115 -1202 2065 O ATOM 4134 N LYS D 128 43.659 14.490 219.580 1.00 94.36 N ANISOU 4134 N LYS D 128 13230 14533 8089 -2977 -354 325 N ATOM 4135 CA LYS D 128 43.298 14.094 218.230 1.00 89.62 C ANISOU 4135 CA LYS D 128 12430 13414 8208 -2640 -423 197 C ATOM 4136 C LYS D 128 44.199 14.895 217.301 1.00 85.06 C ANISOU 4136 C LYS D 128 11800 12788 7729 -2406 -595 -177 C ATOM 4137 O LYS D 128 44.117 16.114 217.269 1.00 83.37 O ANISOU 4137 O LYS D 128 11649 12716 7313 -2465 -382 -601 O ATOM 4138 CB LYS D 128 41.849 14.488 217.952 1.00 88.76 C ANISOU 4138 CB LYS D 128 12246 13138 8340 -2661 6 -95 C ATOM 4139 CG LYS D 128 40.826 13.358 217.915 1.00 90.63 C ANISOU 4139 CG LYS D 128 12362 13092 8982 -2699 74 235 C ATOM 4140 CD LYS D 128 39.421 13.944 217.692 1.00 90.24 C ANISOU 4140 CD LYS D 128 12181 12962 9144 -2733 514 -81 C ATOM 4141 CE LYS D 128 38.619 13.211 216.606 1.00 88.60 C ANISOU 4141 CE LYS D 128 11742 12269 9652 -2564 418 -62 C ATOM 4142 NZ LYS D 128 38.050 11.901 217.050 1.00 92.68 N ANISOU 4142 NZ LYS D 128 12200 12628 10386 -2747 385 440 N ATOM 4143 N SER D 129 45.070 14.210 216.563 1.00 83.50 N ANISOU 4143 N SER D 129 11487 12384 7857 -2142 -962 -13 N ATOM 4144 CA SER D 129 46.034 14.888 215.690 1.00 80.10 C ANISOU 4144 CA SER D 129 10978 11955 7502 -1930 -1123 -303 C ATOM 4145 C SER D 129 45.960 14.381 214.260 1.00 76.36 C ANISOU 4145 C SER D 129 10347 11047 7618 -1566 -1230 -428 C ATOM 4146 O SER D 129 45.436 13.300 213.997 1.00 77.09 O ANISOU 4146 O SER D 129 10393 10817 8081 -1466 -1290 -232 O ATOM 4147 CB SER D 129 47.467 14.746 216.217 1.00 82.56 C ANISOU 4147 CB SER D 129 11273 12572 7524 -1968 -1465 -26 C ATOM 4148 OG SER D 129 47.593 15.260 217.536 1.00 86.82 O ANISOU 4148 OG SER D 129 11985 13565 7437 -2343 -1408 59 O ATOM 4149 N VAL D 130 46.501 15.181 213.347 1.00 72.51 N ANISOU 4149 N VAL D 130 9792 10562 7195 -1397 -1254 -759 N ATOM 4150 CA VAL D 130 46.406 14.962 211.914 1.00 69.07 C ANISOU 4150 CA VAL D 130 9239 9798 7206 -1079 -1307 -968 C ATOM 4151 C VAL D 130 47.738 15.403 211.298 1.00 67.89 C ANISOU 4151 C VAL D 130 8991 9796 7006 -906 -1476 -1063 C ATOM 4152 O VAL D 130 48.235 16.488 211.613 1.00 67.88 O ANISOU 4152 O VAL D 130 9019 10082 6690 -1063 -1422 -1195 O ATOM 4153 CB VAL D 130 45.240 15.818 211.322 1.00 66.45 C ANISOU 4153 CB VAL D 130 8918 9340 6990 -1097 -1031 -1333 C ATOM 4154 CG1 VAL D 130 45.441 16.121 209.864 1.00 63.56 C ANISOU 4154 CG1 VAL D 130 8459 8812 6878 -826 -1096 -1602 C ATOM 4155 CG2 VAL D 130 43.899 15.143 211.509 1.00 67.55 C ANISOU 4155 CG2 VAL D 130 9052 9250 7366 -1176 -899 -1243 C ATOM 4156 N CYS D 131 48.347 14.552 210.466 1.00 67.84 N ANISOU 4156 N CYS D 131 8863 9599 7316 -598 -1669 -997 N ATOM 4157 CA CYS D 131 49.529 14.962 209.701 1.00 66.43 C ANISOU 4157 CA CYS D 131 8543 9560 7138 -402 -1768 -1113 C ATOM 4158 C CYS D 131 49.127 15.590 208.375 1.00 61.90 C ANISOU 4158 C CYS D 131 7956 8857 6707 -252 -1628 -1490 C ATOM 4159 O CYS D 131 48.210 15.114 207.705 1.00 61.31 O ANISOU 4159 O CYS D 131 7921 8484 6890 -141 -1581 -1619 O ATOM 4160 CB CYS D 131 50.488 13.794 209.447 1.00 69.96 C ANISOU 4160 CB CYS D 131 8838 9900 7844 -108 -2002 -877 C ATOM 4161 SG CYS D 131 51.109 12.927 210.936 1.00 77.22 S ANISOU 4161 SG CYS D 131 9729 10964 8648 -233 -2252 -311 S ATOM 4162 N LEU D 132 49.813 16.665 208.005 1.00 59.02 N ANISOU 4162 N LEU D 132 7530 8727 6168 -278 -1582 -1640 N ATOM 4163 CA LEU D 132 49.624 17.293 206.703 1.00 55.40 C ANISOU 4163 CA LEU D 132 7045 8197 5807 -133 -1477 -1923 C ATOM 4164 C LEU D 132 50.940 17.282 205.932 1.00 55.67 C ANISOU 4164 C LEU D 132 6899 8398 5856 79 -1560 -1919 C ATOM 4165 O LEU D 132 51.966 17.696 206.447 1.00 56.82 O ANISOU 4165 O LEU D 132 6934 8823 5834 -26 -1627 -1786 O ATOM 4166 CB LEU D 132 49.091 18.722 206.858 1.00 53.30 C ANISOU 4166 CB LEU D 132 6871 8014 5365 -369 -1293 -2100 C ATOM 4167 CG LEU D 132 49.362 19.784 205.784 1.00 51.22 C ANISOU 4167 CG LEU D 132 6560 7807 5093 -311 -1213 -2286 C ATOM 4168 CD1 LEU D 132 48.483 19.569 204.574 1.00 50.09 C ANISOU 4168 CD1 LEU D 132 6430 7438 5162 -109 -1178 -2437 C ATOM 4169 CD2 LEU D 132 49.161 21.193 206.347 1.00 50.56 C ANISOU 4169 CD2 LEU D 132 6569 7800 4840 -591 -1063 -2391 C ATOM 4170 N PHE D 133 50.893 16.781 204.702 1.00 54.94 N ANISOU 4170 N PHE D 133 6766 8152 5956 366 -1552 -2072 N ATOM 4171 CA PHE D 133 52.017 16.789 203.786 1.00 55.24 C ANISOU 4171 CA PHE D 133 6628 8358 6003 598 -1551 -2120 C ATOM 4172 C PHE D 133 51.695 17.884 202.792 1.00 53.48 C ANISOU 4172 C PHE D 133 6447 8210 5662 554 -1407 -2328 C ATOM 4173 O PHE D 133 50.682 17.816 202.111 1.00 52.44 O ANISOU 4173 O PHE D 133 6442 7881 5604 605 -1370 -2499 O ATOM 4174 CB PHE D 133 52.059 15.428 203.098 1.00 56.68 C ANISOU 4174 CB PHE D 133 6789 8293 6454 944 -1611 -2192 C ATOM 4175 CG PHE D 133 53.171 15.245 202.097 1.00 57.90 C ANISOU 4175 CG PHE D 133 6756 8605 6638 1246 -1557 -2284 C ATOM 4176 CD1 PHE D 133 52.965 14.440 200.983 1.00 58.80 C ANISOU 4176 CD1 PHE D 133 6926 8513 6903 1542 -1517 -2541 C ATOM 4177 CD2 PHE D 133 54.419 15.825 202.274 1.00 58.84 C ANISOU 4177 CD2 PHE D 133 6635 9084 6639 1225 -1538 -2131 C ATOM 4178 CE1 PHE D 133 53.972 14.228 200.053 1.00 60.61 C ANISOU 4178 CE1 PHE D 133 6988 8905 7136 1841 -1410 -2663 C ATOM 4179 CE2 PHE D 133 55.430 15.624 201.341 1.00 60.56 C ANISOU 4179 CE2 PHE D 133 6638 9473 6901 1516 -1440 -2208 C ATOM 4180 CZ PHE D 133 55.201 14.824 200.227 1.00 61.54 C ANISOU 4180 CZ PHE D 133 6833 9401 7149 1839 -1352 -2484 C ATOM 4181 N THR D 134 52.531 18.910 202.724 1.00 53.81 N ANISOU 4181 N THR D 134 6376 8534 5537 434 -1350 -2283 N ATOM 4182 CA THR D 134 52.232 20.046 201.857 1.00 53.01 C ANISOU 4182 CA THR D 134 6322 8484 5337 359 -1220 -2408 C ATOM 4183 C THR D 134 53.461 20.575 201.117 1.00 54.68 C ANISOU 4183 C THR D 134 6331 8999 5446 412 -1153 -2359 C ATOM 4184 O THR D 134 54.598 20.159 201.410 1.00 57.56 O ANISOU 4184 O THR D 134 6482 9563 5824 485 -1205 -2228 O ATOM 4185 CB THR D 134 51.556 21.192 202.648 1.00 51.85 C ANISOU 4185 CB THR D 134 6311 8278 5112 30 -1161 -2413 C ATOM 4186 OG1 THR D 134 50.923 22.108 201.748 1.00 51.00 O ANISOU 4186 OG1 THR D 134 6276 8093 5009 14 -1056 -2515 O ATOM 4187 CG2 THR D 134 52.567 21.936 203.496 1.00 53.19 C ANISOU 4187 CG2 THR D 134 6390 8686 5133 -224 -1184 -2293 C ATOM 4188 N ASP D 135 53.204 21.459 200.144 1.00 53.59 N ANISOU 4188 N ASP D 135 6238 8899 5223 380 -1041 -2428 N ATOM 4189 CA ASP D 135 54.211 22.204 199.355 1.00 54.76 C ANISOU 4189 CA ASP D 135 6215 9341 5252 362 -934 -2348 C ATOM 4190 C ASP D 135 55.151 21.341 198.499 1.00 57.45 C ANISOU 4190 C ASP D 135 6354 9900 5573 678 -870 -2371 C ATOM 4191 O ASP D 135 56.261 21.763 198.140 1.00 59.41 O ANISOU 4191 O ASP D 135 6367 10458 5748 662 -771 -2253 O ATOM 4192 CB ASP D 135 55.025 23.182 200.220 1.00 54.75 C ANISOU 4192 CB ASP D 135 6093 9502 5206 38 -948 -2187 C ATOM 4193 CG ASP D 135 54.164 24.201 200.940 1.00 53.08 C ANISOU 4193 CG ASP D 135 6096 9070 5000 -268 -948 -2228 C ATOM 4194 OD1 ASP D 135 52.959 24.300 200.614 1.00 51.50 O ANISOU 4194 OD1 ASP D 135 6090 8620 4859 -212 -911 -2338 O ATOM 4195 OD2 ASP D 135 54.704 24.913 201.827 1.00 53.25 O ANISOU 4195 OD2 ASP D 135 6083 9173 4979 -567 -985 -2164 O ATOM 4196 N PHE D 136 54.710 20.135 198.174 1.00 57.72 N ANISOU 4196 N PHE D 136 6472 9762 5697 962 -909 -2535 N ATOM 4197 CA PHE D 136 55.524 19.253 197.361 1.00 61.06 C ANISOU 4197 CA PHE D 136 6737 10336 6129 1302 -814 -2630 C ATOM 4198 C PHE D 136 55.337 19.601 195.892 1.00 62.82 C ANISOU 4198 C PHE D 136 7037 10710 6122 1394 -659 -2777 C ATOM 4199 O PHE D 136 54.411 20.337 195.523 1.00 61.72 O ANISOU 4199 O PHE D 136 7092 10491 5867 1226 -686 -2791 O ATOM 4200 CB PHE D 136 55.272 17.756 197.655 1.00 61.40 C ANISOU 4200 CB PHE D 136 6836 10090 6404 1574 -919 -2758 C ATOM 4201 CG PHE D 136 53.819 17.347 197.652 1.00 59.10 C ANISOU 4201 CG PHE D 136 6846 9428 6180 1534 -1035 -2923 C ATOM 4202 CD1 PHE D 136 53.223 16.871 196.489 1.00 59.74 C ANISOU 4202 CD1 PHE D 136 7088 9411 6199 1709 -1006 -3204 C ATOM 4203 CD2 PHE D 136 53.056 17.410 198.813 1.00 56.55 C ANISOU 4203 CD2 PHE D 136 6632 8883 5971 1308 -1171 -2800 C ATOM 4204 CE1 PHE D 136 51.900 16.490 196.476 1.00 58.16 C ANISOU 4204 CE1 PHE D 136 7117 8889 6090 1642 -1143 -3339 C ATOM 4205 CE2 PHE D 136 51.737 17.028 198.802 1.00 55.17 C ANISOU 4205 CE2 PHE D 136 6674 8396 5894 1263 -1257 -2925 C ATOM 4206 CZ PHE D 136 51.158 16.567 197.635 1.00 55.96 C ANISOU 4206 CZ PHE D 136 6898 8389 5976 1423 -1261 -3185 C ATOM 4207 N ASP D 137 56.231 19.073 195.066 1.00 66.40 N ANISOU 4207 N ASP D 137 7325 11400 6505 1670 -492 -2872 N ATOM 4208 CA ASP D 137 56.241 19.349 193.648 1.00 68.41 C ANISOU 4208 CA ASP D 137 7638 11896 6459 1761 -312 -3002 C ATOM 4209 C ASP D 137 55.083 18.617 193.014 1.00 68.19 C ANISOU 4209 C ASP D 137 7924 11608 6376 1892 -413 -3312 C ATOM 4210 O ASP D 137 54.559 17.667 193.579 1.00 67.43 O ANISOU 4210 O ASP D 137 7932 11160 6527 1991 -566 -3449 O ATOM 4211 CB ASP D 137 57.546 18.826 193.052 1.00 73.12 C ANISOU 4211 CB ASP D 137 7951 12820 7009 2054 -64 -3062 C ATOM 4212 CG ASP D 137 57.974 19.586 191.819 1.00 75.61 C ANISOU 4212 CG ASP D 137 8211 13566 6952 2019 189 -3025 C ATOM 4213 OD1 ASP D 137 57.175 19.681 190.863 1.00 76.05 O ANISOU 4213 OD1 ASP D 137 8541 13631 6724 2017 192 -3187 O ATOM 4214 OD2 ASP D 137 59.124 20.081 191.806 1.00 77.87 O ANISOU 4214 OD2 ASP D 137 8162 14206 7220 1976 374 -2806 O ATOM 4215 N SER D 138 54.700 19.046 191.819 1.00 69.66 N ANISOU 4215 N SER D 138 8253 11983 6230 1873 -343 -3401 N ATOM 4216 CA SER D 138 53.667 18.343 191.068 1.00 70.50 C ANISOU 4216 CA SER D 138 8645 11911 6231 1978 -465 -3720 C ATOM 4217 C SER D 138 54.222 17.162 190.265 1.00 74.77 C ANISOU 4217 C SER D 138 9204 12528 6676 2333 -310 -4099 C ATOM 4218 O SER D 138 53.496 16.491 189.541 1.00 76.26 O ANISOU 4218 O SER D 138 9641 12592 6743 2422 -402 -4433 O ATOM 4219 CB SER D 138 52.885 19.309 190.184 1.00 70.65 C ANISOU 4219 CB SER D 138 8826 12091 5925 1779 -525 -3628 C ATOM 4220 OG SER D 138 51.780 19.860 190.894 1.00 67.26 O ANISOU 4220 OG SER D 138 8488 11359 5707 1543 -752 -3465 O ATOM 4221 N GLN D 139 55.517 16.911 190.404 1.00 77.23 N ANISOU 4221 N GLN D 139 9238 13039 7065 2535 -76 -4061 N ATOM 4222 CA GLN D 139 56.091 15.653 189.975 1.00 81.50 C ANISOU 4222 CA GLN D 139 9753 13528 7686 2929 82 -4426 C ATOM 4223 C GLN D 139 55.881 14.554 191.031 1.00 80.26 C ANISOU 4223 C GLN D 139 9604 12847 8043 3067 -111 -4491 C ATOM 4224 O GLN D 139 55.916 13.376 190.699 1.00 83.53 O ANISOU 4224 O GLN D 139 10115 13018 8606 3369 -73 -4853 O ATOM 4225 CB GLN D 139 57.579 15.821 189.662 1.00 85.71 C ANISOU 4225 CB GLN D 139 9924 14503 8138 3125 439 -4336 C ATOM 4226 CG GLN D 139 57.887 16.253 188.218 1.00 90.29 C ANISOU 4226 CG GLN D 139 10549 15588 8169 3165 737 -4477 C ATOM 4227 CD GLN D 139 58.306 17.716 188.096 1.00 89.53 C ANISOU 4227 CD GLN D 139 10267 15926 7823 2846 841 -4025 C ATOM 4228 OE1 GLN D 139 59.037 18.243 188.941 1.00 88.07 O ANISOU 4228 OE1 GLN D 139 9760 15811 7889 2727 856 -3673 O ATOM 4229 NE2 GLN D 139 57.859 18.371 187.027 1.00 90.90 N ANISOU 4229 NE2 GLN D 139 10646 16390 7501 2691 895 -4020 N ATOM 4230 N THR D 140 55.642 14.943 192.287 1.00 75.49 N ANISOU 4230 N THR D 140 8922 12064 7699 2834 -313 -4144 N ATOM 4231 CA THR D 140 55.531 13.994 193.410 1.00 74.28 C ANISOU 4231 CA THR D 140 8746 11474 8005 2922 -496 -4088 C ATOM 4232 C THR D 140 54.187 13.248 193.438 1.00 72.99 C ANISOU 4232 C THR D 140 8917 10833 7984 2864 -728 -4316 C ATOM 4233 O THR D 140 53.140 13.874 193.381 1.00 70.13 O ANISOU 4233 O THR D 140 8730 10441 7473 2580 -866 -4278 O ATOM 4234 CB THR D 140 55.746 14.731 194.785 1.00 70.68 C ANISOU 4234 CB THR D 140 8106 11061 7688 2643 -626 -3631 C ATOM 4235 OG1 THR D 140 56.944 15.522 194.742 1.00 71.24 O ANISOU 4235 OG1 THR D 140 7855 11581 7630 2621 -448 -3409 O ATOM 4236 CG2 THR D 140 55.827 13.756 195.956 1.00 70.59 C ANISOU 4236 CG2 THR D 140 8036 10693 8093 2738 -801 -3494 C ATOM 4237 N ASN D 141 54.216 11.919 193.528 1.00 75.49 N ANISOU 4237 N ASN D 141 9295 10757 8630 3131 -773 -4536 N ATOM 4238 CA ASN D 141 52.986 11.143 193.745 1.00 75.31 C ANISOU 4238 CA ASN D 141 9548 10230 8836 3030 -1019 -4691 C ATOM 4239 C ASN D 141 52.755 10.824 195.223 1.00 73.51 C ANISOU 4239 C ASN D 141 9252 9684 8996 2898 -1208 -4327 C ATOM 4240 O ASN D 141 53.714 10.665 195.975 1.00 74.65 O ANISOU 4240 O ASN D 141 9157 9877 9328 3030 -1168 -4061 O ATOM 4241 CB ASN D 141 53.019 9.828 192.959 1.00 80.32 C ANISOU 4241 CB ASN D 141 10349 10534 9635 3353 -981 -5173 C ATOM 4242 CG ASN D 141 52.617 9.992 191.507 1.00 82.05 C ANISOU 4242 CG ASN D 141 10794 10964 9415 3354 -908 -5615 C ATOM 4243 OD1 ASN D 141 51.947 10.951 191.135 1.00 79.60 O ANISOU 4243 OD1 ASN D 141 10566 10928 8750 3069 -982 -5533 O ATOM 4244 ND2 ASN D 141 53.021 9.044 190.681 1.00 87.16 N ANISOU 4244 ND2 ASN D 141 11551 11481 10086 3680 -765 -6087 N ATOM 4245 N VAL D 142 51.489 10.718 195.631 1.00 71.32 N ANISOU 4245 N VAL D 142 9164 9110 8824 2631 -1416 -4294 N ATOM 4246 CA VAL D 142 51.138 10.349 197.009 1.00 70.46 C ANISOU 4246 CA VAL D 142 9026 8708 9038 2476 -1576 -3952 C ATOM 4247 C VAL D 142 50.431 8.987 197.056 1.00 74.10 C ANISOU 4247 C VAL D 142 9670 8587 9899 2536 -1736 -4119 C ATOM 4248 O VAL D 142 49.277 8.875 196.658 1.00 74.07 O ANISOU 4248 O VAL D 142 9854 8396 9894 2349 -1855 -4311 O ATOM 4249 CB VAL D 142 50.235 11.430 197.686 1.00 65.78 C ANISOU 4249 CB VAL D 142 8457 8261 8276 2070 -1641 -3699 C ATOM 4250 CG1 VAL D 142 49.913 11.069 199.137 1.00 64.77 C ANISOU 4250 CG1 VAL D 142 8306 7904 8399 1895 -1760 -3346 C ATOM 4251 CG2 VAL D 142 50.888 12.802 197.632 1.00 63.19 C ANISOU 4251 CG2 VAL D 142 7979 8428 7601 1978 -1497 -3552 C ATOM 4252 N SER D 143 51.123 7.955 197.535 1.00 78.60 N ANISOU 4252 N SER D 143 10165 8853 10844 2791 -1756 -4024 N ATOM 4253 CA SER D 143 50.539 6.610 197.664 1.00 83.04 C ANISOU 4253 CA SER D 143 10900 8784 11869 2846 -1913 -4135 C ATOM 4254 C SER D 143 49.815 6.480 198.992 1.00 82.64 C ANISOU 4254 C SER D 143 10851 8523 12024 2531 -2084 -3681 C ATOM 4255 O SER D 143 50.114 7.221 199.923 1.00 80.09 O ANISOU 4255 O SER D 143 10375 8525 11529 2378 -2065 -3281 O ATOM 4256 CB SER D 143 51.623 5.537 197.586 1.00 87.63 C ANISOU 4256 CB SER D 143 11391 9075 12828 3296 -1850 -4205 C ATOM 4257 OG SER D 143 52.220 5.508 196.308 1.00 89.76 O ANISOU 4257 OG SER D 143 11680 9502 12921 3605 -1646 -4692 O ATOM 4258 N GLN D 144 48.884 5.531 199.096 1.00 86.30 N ANISOU 4258 N GLN D 144 11492 8456 12844 2415 -2244 -3744 N ATOM 4259 CA GLN D 144 48.053 5.429 200.305 1.00 86.61 C ANISOU 4259 CA GLN D 144 11535 8331 13041 2068 -2371 -3308 C ATOM 4260 C GLN D 144 47.892 4.050 200.945 1.00 91.49 C ANISOU 4260 C GLN D 144 12223 8323 14218 2098 -2525 -3091 C ATOM 4261 O GLN D 144 46.880 3.379 200.728 1.00 93.21 O ANISOU 4261 O GLN D 144 12599 8104 14711 1920 -2648 -3237 O ATOM 4262 CB GLN D 144 46.674 6.088 200.089 1.00 84.33 C ANISOU 4262 CB GLN D 144 11330 8150 12560 1689 -2407 -3417 C ATOM 4263 CG GLN D 144 46.079 6.004 198.679 1.00 85.98 C ANISOU 4263 CG GLN D 144 11690 8277 12699 1710 -2457 -3964 C ATOM 4264 CD GLN D 144 45.126 7.174 198.389 1.00 82.74 C ANISOU 4264 CD GLN D 144 11253 8238 11948 1419 -2451 -3999 C ATOM 4265 OE1 GLN D 144 43.991 6.981 197.935 1.00 83.69 O ANISOU 4265 OE1 GLN D 144 11450 8182 12165 1209 -2596 -4179 O ATOM 4266 NE2 GLN D 144 45.589 8.394 198.665 1.00 79.04 N ANISOU 4266 NE2 GLN D 144 10653 8263 11116 1403 -2297 -3813 N ATOM 4267 N SER D 145 48.877 3.658 201.758 1.00 94.41 N ANISOU 4267 N SER D 145 12454 8652 14764 2298 -2540 -2698 N ATOM 4268 CA SER D 145 48.837 2.389 202.509 1.00 99.97 C ANISOU 4268 CA SER D 145 13200 8767 16016 2335 -2700 -2356 C ATOM 4269 C SER D 145 49.765 2.337 203.740 1.00101.49 C ANISOU 4269 C SER D 145 13193 9125 16242 2414 -2757 -1724 C ATOM 4270 O SER D 145 50.963 2.613 203.638 1.00101.90 O ANISOU 4270 O SER D 145 13049 9470 16197 2725 -2694 -1696 O ATOM 4271 CB SER D 145 49.166 1.201 201.596 1.00105.51 C ANISOU 4271 CB SER D 145 14019 8861 17210 2714 -2728 -2768 C ATOM 4272 OG SER D 145 50.440 1.360 200.999 1.00106.90 O ANISOU 4272 OG SER D 145 14046 9268 17302 3167 -2577 -2985 O ATOM 4273 N LYS D 146 49.186 1.972 204.887 1.00102.98 N ANISOU 4273 N LYS D 146 13419 9150 16557 2111 -2885 -1204 N ATOM 4274 CA LYS D 146 49.909 1.642 206.133 1.00105.85 C ANISOU 4274 CA LYS D 146 13642 9567 17010 2142 -3014 -529 C ATOM 4275 C LYS D 146 48.973 0.711 206.934 1.00108.91 C ANISOU 4275 C LYS D 146 14175 9454 17753 1851 -3156 -112 C ATOM 4276 O LYS D 146 48.643 0.974 208.100 1.00108.73 O ANISOU 4276 O LYS D 146 14137 9694 17481 1506 -3193 411 O ATOM 4277 CB LYS D 146 50.253 2.915 206.937 1.00102.03 C ANISOU 4277 CB LYS D 146 13017 9853 15896 1909 -2958 -252 C ATOM 4278 CG LYS D 146 51.352 2.750 208.015 1.00105.17 C ANISOU 4278 CG LYS D 146 13216 10471 16275 2009 -3120 365 C ATOM 4279 CD LYS D 146 51.369 3.935 208.979 1.00101.86 C ANISOU 4279 CD LYS D 146 12745 10752 15206 1630 -3094 631 C ATOM 4280 CE LYS D 146 51.483 3.496 210.439 1.00105.38 C ANISOU 4280 CE LYS D 146 13175 11265 15599 1415 -3297 1367 C ATOM 4281 NZ LYS D 146 52.722 2.723 210.712 1.00110.40 N ANISOU 4281 NZ LYS D 146 13592 11775 16582 1785 -3531 1778 N ATOM 4282 N ASP D 147 48.529 -0.360 206.270 1.00111.86 N ANISOU 4282 N ASP D 147 14700 9112 18690 1966 -3221 -372 N ATOM 4283 CA ASP D 147 47.310 -1.124 206.629 1.00113.56 C ANISOU 4283 CA ASP D 147 15082 8812 19251 1603 -3315 -182 C ATOM 4284 C ASP D 147 46.015 -0.282 206.714 1.00108.39 C ANISOU 4284 C ASP D 147 14475 8512 18197 1107 -3201 -297 C ATOM 4285 O ASP D 147 45.984 0.901 206.351 1.00102.88 O ANISOU 4285 O ASP D 147 13718 8393 16979 1062 -3052 -600 O ATOM 4286 CB ASP D 147 47.497 -2.036 207.862 1.00118.76 C ANISOU 4286 CB ASP D 147 15721 9141 20263 1535 -3491 607 C ATOM 4287 CG ASP D 147 47.912 -3.454 207.489 1.00125.54 C ANISOU 4287 CG ASP D 147 16654 9124 21923 1894 -3646 602 C ATOM 4288 OD1 ASP D 147 48.197 -3.706 206.300 1.00126.27 O ANISOU 4288 OD1 ASP D 147 16808 8917 22251 2237 -3593 -54 O ATOM 4289 OD2 ASP D 147 47.949 -4.322 208.388 1.00130.53 O ANISOU 4289 OD2 ASP D 147 17293 9355 22948 1833 -3814 1256 O ATOM 4290 N SER D 148 44.941 -0.902 207.193 1.00110.21 N ANISOU 4290 N SER D 148 14790 8372 18714 738 -3265 -30 N ATOM 4291 CA SER D 148 43.604 -0.307 207.091 1.00106.22 C ANISOU 4291 CA SER D 148 14291 8072 17995 308 -3159 -201 C ATOM 4292 C SER D 148 43.280 0.773 208.130 1.00101.73 C ANISOU 4292 C SER D 148 13613 8197 16844 -9 -2980 159 C ATOM 4293 O SER D 148 42.249 1.440 208.030 1.00 99.00 O ANISOU 4293 O SER D 148 13225 8095 16294 -306 -2845 -9 O ATOM 4294 CB SER D 148 42.532 -1.406 207.121 1.00110.94 C ANISOU 4294 CB SER D 148 14983 7996 19174 10 -3283 -88 C ATOM 4295 OG SER D 148 42.691 -2.248 208.250 1.00115.60 O ANISOU 4295 OG SER D 148 15582 8289 20051 -97 -3372 624 O ATOM 4296 N ASP D 149 44.160 0.954 209.108 1.00100.97 N ANISOU 4296 N ASP D 149 13461 8420 16482 59 -2982 633 N ATOM 4297 CA ASP D 149 43.868 1.822 210.239 1.00 97.88 C ANISOU 4297 CA ASP D 149 13014 8636 15541 -274 -2820 998 C ATOM 4298 C ASP D 149 44.404 3.240 210.059 1.00 91.77 C ANISOU 4298 C ASP D 149 12169 8531 14170 -181 -2672 686 C ATOM 4299 O ASP D 149 44.122 4.127 210.867 1.00 89.98 O ANISOU 4299 O ASP D 149 11918 8816 13454 -451 -2503 841 O ATOM 4300 CB ASP D 149 44.413 1.188 211.516 1.00102.44 C ANISOU 4300 CB ASP D 149 13596 9207 16119 -344 -2942 1744 C ATOM 4301 CG ASP D 149 43.899 -0.224 211.718 1.00108.37 C ANISOU 4301 CG ASP D 149 14423 9243 17510 -451 -3094 2117 C ATOM 4302 OD1 ASP D 149 42.800 -0.532 211.208 1.00108.52 O ANISOU 4302 OD1 ASP D 149 14479 8911 17843 -656 -3045 1874 O ATOM 4303 OD2 ASP D 149 44.588 -1.028 212.381 1.00113.14 O ANISOU 4303 OD2 ASP D 149 15037 9621 18330 -342 -3282 2674 O ATOM 4304 N VAL D 150 45.175 3.445 208.994 1.00 88.64 N ANISOU 4304 N VAL D 150 11745 8113 13820 192 -2717 237 N ATOM 4305 CA VAL D 150 45.762 4.751 208.680 1.00 82.68 C ANISOU 4305 CA VAL D 150 10916 7932 12568 292 -2591 -60 C ATOM 4306 C VAL D 150 45.258 5.253 207.312 1.00 78.63 C ANISOU 4306 C VAL D 150 10422 7382 12072 382 -2507 -692 C ATOM 4307 O VAL D 150 45.367 4.545 206.305 1.00 80.16 O ANISOU 4307 O VAL D 150 10665 7170 12620 626 -2605 -1007 O ATOM 4308 CB VAL D 150 47.310 4.672 208.736 1.00 83.69 C ANISOU 4308 CB VAL D 150 10942 8205 12653 640 -2709 71 C ATOM 4309 CG1 VAL D 150 47.967 5.893 208.104 1.00 79.27 C ANISOU 4309 CG1 VAL D 150 10291 8132 11697 776 -2591 -307 C ATOM 4310 CG2 VAL D 150 47.771 4.504 210.177 1.00 86.45 C ANISOU 4310 CG2 VAL D 150 11253 8777 12817 479 -2811 724 C ATOM 4311 N TYR D 151 44.695 6.464 207.286 1.00 73.43 N ANISOU 4311 N TYR D 151 9733 7138 11028 184 -2330 -872 N ATOM 4312 CA TYR D 151 44.041 7.000 206.090 1.00 69.35 C ANISOU 4312 CA TYR D 151 9223 6621 10507 211 -2274 -1374 C ATOM 4313 C TYR D 151 44.793 8.139 205.439 1.00 65.59 C ANISOU 4313 C TYR D 151 8698 6562 9662 393 -2184 -1662 C ATOM 4314 O TYR D 151 44.804 9.243 205.955 1.00 63.27 O ANISOU 4314 O TYR D 151 8358 6677 9004 244 -2040 -1595 O ATOM 4315 CB TYR D 151 42.668 7.545 206.442 1.00 67.04 C ANISOU 4315 CB TYR D 151 8894 6432 10145 -141 -2135 -1348 C ATOM 4316 CG TYR D 151 41.844 6.667 207.331 1.00 69.85 C ANISOU 4316 CG TYR D 151 9257 6511 10774 -419 -2150 -972 C ATOM 4317 CD1 TYR D 151 41.653 6.993 208.667 1.00 70.31 C ANISOU 4317 CD1 TYR D 151 9290 6853 10570 -678 -1989 -568 C ATOM 4318 CD2 TYR D 151 41.229 5.531 206.835 1.00 72.71 C ANISOU 4318 CD2 TYR D 151 9657 6336 11635 -454 -2314 -1026 C ATOM 4319 CE1 TYR D 151 40.887 6.206 209.490 1.00 73.72 C ANISOU 4319 CE1 TYR D 151 9719 7076 11217 -958 -1970 -179 C ATOM 4320 CE2 TYR D 151 40.458 4.736 207.648 1.00 76.31 C ANISOU 4320 CE2 TYR D 151 10100 6527 12367 -747 -2319 -638 C ATOM 4321 CZ TYR D 151 40.288 5.077 208.978 1.00 76.78 C ANISOU 4321 CZ TYR D 151 10118 6910 12145 -996 -2135 -190 C ATOM 4322 OH TYR D 151 39.518 4.287 209.802 1.00 80.68 O ANISOU 4322 OH TYR D 151 10592 7181 12882 -1311 -2110 243 O ATOM 4323 N ILE D 152 45.381 7.890 204.284 1.00 65.80 N ANISOU 4323 N ILE D 152 8742 6477 9782 697 -2251 -2000 N ATOM 4324 CA ILE D 152 46.031 8.949 203.540 1.00 63.40 C ANISOU 4324 CA ILE D 152 8385 6565 9140 847 -2152 -2260 C ATOM 4325 C ILE D 152 45.120 9.355 202.387 1.00 61.98 C ANISOU 4325 C ILE D 152 8255 6365 8929 804 -2144 -2650 C ATOM 4326 O ILE D 152 44.727 8.511 201.594 1.00 64.37 O ANISOU 4326 O ILE D 152 8645 6325 9487 886 -2266 -2899 O ATOM 4327 CB ILE D 152 47.389 8.459 202.996 1.00 65.77 C ANISOU 4327 CB ILE D 152 8639 6842 9510 1230 -2191 -2358 C ATOM 4328 CG1 ILE D 152 48.289 8.000 204.150 1.00 68.08 C ANISOU 4328 CG1 ILE D 152 8837 7151 9879 1283 -2256 -1909 C ATOM 4329 CG2 ILE D 152 48.077 9.541 202.167 1.00 63.60 C ANISOU 4329 CG2 ILE D 152 8289 6994 8882 1362 -2065 -2601 C ATOM 4330 CD1 ILE D 152 49.545 7.238 203.714 1.00 71.33 C ANISOU 4330 CD1 ILE D 152 9153 7429 10522 1703 -2309 -1947 C ATOM 4331 N THR D 153 44.775 10.637 202.298 1.00 59.04 N ANISOU 4331 N THR D 153 7834 6343 8257 668 -2023 -2699 N ATOM 4332 CA THR D 153 43.921 11.134 201.217 1.00 58.42 C ANISOU 4332 CA THR D 153 7772 6294 8130 629 -2046 -2997 C ATOM 4333 C THR D 153 44.702 11.360 199.942 1.00 59.09 C ANISOU 4333 C THR D 153 7891 6538 8021 888 -2055 -3301 C ATOM 4334 O THR D 153 45.926 11.311 199.942 1.00 59.64 O ANISOU 4334 O THR D 153 7931 6742 7987 1095 -1994 -3277 O ATOM 4335 CB THR D 153 43.343 12.524 201.514 1.00 55.38 C ANISOU 4335 CB THR D 153 7307 6210 7525 438 -1901 -2922 C ATOM 4336 OG1 THR D 153 44.331 13.521 201.219 1.00 53.36 O ANISOU 4336 OG1 THR D 153 7027 6296 6952 555 -1797 -2959 O ATOM 4337 CG2 THR D 153 42.888 12.652 202.953 1.00 55.45 C ANISOU 4337 CG2 THR D 153 7273 6229 7567 196 -1782 -2615 C ATOM 4338 N ASP D 154 43.975 11.655 198.864 1.00 59.74 N ANISOU 4338 N ASP D 154 8013 6651 8036 861 -2128 -3559 N ATOM 4339 CA ASP D 154 44.551 12.201 197.633 1.00 59.97 C ANISOU 4339 CA ASP D 154 8074 6953 7758 1039 -2100 -3805 C ATOM 4340 C ASP D 154 45.184 13.585 197.827 1.00 57.03 C ANISOU 4340 C ASP D 154 7603 6988 7077 1024 -1923 -3633 C ATOM 4341 O ASP D 154 44.998 14.255 198.860 1.00 54.71 O ANISOU 4341 O ASP D 154 7234 6764 6791 851 -1831 -3381 O ATOM 4342 CB ASP D 154 43.467 12.349 196.567 1.00 61.38 C ANISOU 4342 CB ASP D 154 8308 7124 7892 943 -2258 -4033 C ATOM 4343 CG ASP D 154 43.385 11.161 195.644 1.00 65.99 C ANISOU 4343 CG ASP D 154 9047 7452 8574 1053 -2428 -4399 C ATOM 4344 OD1 ASP D 154 44.277 10.290 195.710 1.00 68.50 O ANISOU 4344 OD1 ASP D 154 9432 7598 8997 1266 -2379 -4505 O ATOM 4345 OD2 ASP D 154 42.425 11.101 194.843 1.00 67.73 O ANISOU 4345 OD2 ASP D 154 9318 7636 8779 928 -2622 -4592 O ATOM 4346 N LYS D 155 45.920 14.014 196.810 1.00 56.95 N ANISOU 4346 N LYS D 155 7605 7246 6790 1187 -1864 -3785 N ATOM 4347 CA LYS D 155 46.417 15.372 196.771 1.00 54.42 C ANISOU 4347 CA LYS D 155 7199 7281 6198 1137 -1719 -3635 C ATOM 4348 C LYS D 155 45.363 16.237 196.087 1.00 53.63 C ANISOU 4348 C LYS D 155 7120 7257 6001 1002 -1787 -3655 C ATOM 4349 O LYS D 155 44.588 15.738 195.272 1.00 55.23 O ANISOU 4349 O LYS D 155 7400 7356 6229 1009 -1953 -3848 O ATOM 4350 CB LYS D 155 47.785 15.437 196.060 1.00 55.52 C ANISOU 4350 CB LYS D 155 7297 7699 6098 1361 -1595 -3719 C ATOM 4351 CG LYS D 155 47.759 15.354 194.530 1.00 57.33 C ANISOU 4351 CG LYS D 155 7625 8081 6077 1495 -1615 -3999 C ATOM 4352 CD LYS D 155 48.948 14.588 193.952 1.00 60.30 C ANISOU 4352 CD LYS D 155 7989 8554 6369 1794 -1492 -4206 C ATOM 4353 CE LYS D 155 48.710 13.076 194.014 1.00 63.37 C ANISOU 4353 CE LYS D 155 8490 8527 7061 1942 -1606 -4459 C ATOM 4354 NZ LYS D 155 49.497 12.285 193.001 1.00 67.35 N ANISOU 4354 NZ LYS D 155 9058 9078 7456 2258 -1495 -4826 N ATOM 4355 N CYS D 156 45.273 17.502 196.489 1.00 52.07 N ANISOU 4355 N CYS D 156 6847 7205 5732 866 -1681 -3449 N ATOM 4356 CA CYS D 156 44.674 18.540 195.641 1.00 52.87 C ANISOU 4356 CA CYS D 156 6941 7447 5701 808 -1716 -3413 C ATOM 4357 C CYS D 156 45.427 19.854 195.750 1.00 51.12 C ANISOU 4357 C CYS D 156 6663 7452 5310 759 -1545 -3225 C ATOM 4358 O CYS D 156 46.329 20.008 196.585 1.00 49.66 O ANISOU 4358 O CYS D 156 6433 7322 5113 730 -1410 -3136 O ATOM 4359 CB CYS D 156 43.160 18.748 195.856 1.00 54.18 C ANISOU 4359 CB CYS D 156 7057 7414 6114 664 -1828 -3360 C ATOM 4360 SG CYS D 156 42.565 19.064 197.534 1.00 53.72 S ANISOU 4360 SG CYS D 156 6908 7155 6350 485 -1673 -3187 S ATOM 4361 N VAL D 157 45.024 20.800 194.906 1.00 51.13 N ANISOU 4361 N VAL D 157 6661 7570 5196 728 -1579 -3141 N ATOM 4362 CA VAL D 157 45.696 22.084 194.776 1.00 50.48 C ANISOU 4362 CA VAL D 157 6540 7669 4971 668 -1438 -2946 C ATOM 4363 C VAL D 157 44.901 23.216 195.386 1.00 49.12 C ANISOU 4363 C VAL D 157 6322 7316 5025 522 -1390 -2780 C ATOM 4364 O VAL D 157 43.798 23.517 194.935 1.00 49.08 O ANISOU 4364 O VAL D 157 6293 7211 5144 521 -1510 -2729 O ATOM 4365 CB VAL D 157 45.859 22.483 193.300 1.00 52.84 C ANISOU 4365 CB VAL D 157 6876 8231 4968 735 -1497 -2903 C ATOM 4366 CG1 VAL D 157 47.129 23.313 193.126 1.00 52.70 C ANISOU 4366 CG1 VAL D 157 6810 8467 4745 702 -1307 -2738 C ATOM 4367 CG2 VAL D 157 45.802 21.256 192.396 1.00 54.57 C ANISOU 4367 CG2 VAL D 157 7187 8542 5006 885 -1631 -3167 C ATOM 4368 N LEU D 158 45.463 23.873 196.387 1.00 48.50 N ANISOU 4368 N LEU D 158 6223 7198 5008 402 -1220 -2703 N ATOM 4369 CA LEU D 158 44.840 25.094 196.866 1.00 49.06 C ANISOU 4369 CA LEU D 158 6275 7083 5282 281 -1128 -2587 C ATOM 4370 C LEU D 158 45.513 26.309 196.220 1.00 51.04 C ANISOU 4370 C LEU D 158 6527 7445 5420 226 -1066 -2401 C ATOM 4371 O LEU D 158 46.718 26.273 195.883 1.00 52.16 O ANISOU 4371 O LEU D 158 6662 7834 5323 216 -1021 -2362 O ATOM 4372 CB LEU D 158 44.820 25.164 198.395 1.00 47.19 C ANISOU 4372 CB LEU D 158 6051 6693 5185 143 -978 -2656 C ATOM 4373 CG LEU D 158 46.113 25.063 199.202 1.00 46.73 C ANISOU 4373 CG LEU D 158 6015 6783 4958 35 -893 -2672 C ATOM 4374 CD1 LEU D 158 46.747 26.430 199.394 1.00 46.83 C ANISOU 4374 CD1 LEU D 158 6044 6803 4948 -133 -771 -2587 C ATOM 4375 CD2 LEU D 158 45.832 24.433 200.549 1.00 46.10 C ANISOU 4375 CD2 LEU D 158 5964 6610 4942 -53 -843 -2756 C ATOM 4376 N ASP D 159 44.737 27.381 196.075 1.00 51.81 N ANISOU 4376 N ASP D 159 6609 7345 5730 193 -1052 -2263 N ATOM 4377 CA ASP D 159 45.177 28.566 195.346 1.00 52.99 C ANISOU 4377 CA ASP D 159 6765 7535 5834 138 -1024 -2022 C ATOM 4378 C ASP D 159 45.068 29.825 196.232 1.00 53.00 C ANISOU 4378 C ASP D 159 6788 7218 6133 -10 -854 -1978 C ATOM 4379 O ASP D 159 43.971 30.228 196.640 1.00 53.30 O ANISOU 4379 O ASP D 159 6800 6956 6496 32 -821 -2002 O ATOM 4380 CB ASP D 159 44.370 28.684 194.032 1.00 54.80 C ANISOU 4380 CB ASP D 159 6966 7824 6030 263 -1222 -1839 C ATOM 4381 CG ASP D 159 44.873 29.791 193.105 1.00 57.43 C ANISOU 4381 CG ASP D 159 7314 8254 6254 208 -1218 -1513 C ATOM 4382 OD1 ASP D 159 46.063 30.162 193.186 1.00 57.75 O ANISOU 4382 OD1 ASP D 159 7374 8429 6141 85 -1075 -1453 O ATOM 4383 OD2 ASP D 159 44.072 30.282 192.273 1.00 59.49 O ANISOU 4383 OD2 ASP D 159 7545 8470 6587 275 -1374 -1277 O ATOM 4384 N MET D 160 46.218 30.425 196.549 1.00 52.76 N ANISOU 4384 N MET D 160 6791 7246 6008 -186 -737 -1938 N ATOM 4385 CA MET D 160 46.259 31.733 197.211 1.00 53.17 C ANISOU 4385 CA MET D 160 6900 6980 6324 -362 -590 -1910 C ATOM 4386 C MET D 160 46.752 32.776 196.214 1.00 55.04 C ANISOU 4386 C MET D 160 7130 7216 6566 -433 -608 -1584 C ATOM 4387 O MET D 160 47.942 33.084 196.183 1.00 55.63 O ANISOU 4387 O MET D 160 7197 7456 6483 -616 -554 -1506 O ATOM 4388 CB MET D 160 47.188 31.699 198.424 1.00 52.54 C ANISOU 4388 CB MET D 160 6870 6945 6149 -583 -476 -2111 C ATOM 4389 CG MET D 160 46.847 30.627 199.454 1.00 50.58 C ANISOU 4389 CG MET D 160 6637 6746 5834 -546 -463 -2369 C ATOM 4390 SD MET D 160 48.195 30.320 200.622 1.00 50.62 S ANISOU 4390 SD MET D 160 6664 6978 5589 -796 -433 -2503 S ATOM 4391 CE MET D 160 48.218 31.882 201.531 1.00 52.30 C ANISOU 4391 CE MET D 160 7022 6848 6002 -1092 -266 -2626 C ATOM 4392 N ARG D 161 45.847 33.317 195.398 1.00 56.24 N ANISOU 4392 N ARG D 161 7262 7198 6911 -301 -694 -1354 N ATOM 4393 CA ARG D 161 46.267 34.133 194.249 1.00 59.41 C ANISOU 4393 CA ARG D 161 7654 7671 7248 -350 -751 -957 C ATOM 4394 C ARG D 161 46.604 35.585 194.592 1.00 61.79 C ANISOU 4394 C ARG D 161 8015 7584 7880 -556 -622 -804 C ATOM 4395 O ARG D 161 47.258 36.271 193.810 1.00 64.20 O ANISOU 4395 O ARG D 161 8315 7962 8115 -679 -633 -461 O ATOM 4396 CB ARG D 161 45.248 34.063 193.105 1.00 61.20 C ANISOU 4396 CB ARG D 161 7829 7943 7479 -138 -958 -700 C ATOM 4397 CG ARG D 161 45.840 34.022 191.695 1.00 62.95 C ANISOU 4397 CG ARG D 161 8048 8585 7287 -146 -1071 -369 C ATOM 4398 CD ARG D 161 44.716 34.012 190.668 1.00 65.40 C ANISOU 4398 CD ARG D 161 8320 8932 7598 34 -1325 -116 C ATOM 4399 NE ARG D 161 43.399 33.894 191.305 1.00 64.74 N ANISOU 4399 NE ARG D 161 8162 8500 7938 184 -1394 -278 N ATOM 4400 CZ ARG D 161 42.340 34.648 190.999 1.00 67.57 C ANISOU 4400 CZ ARG D 161 8433 8561 8678 298 -1525 3 C ATOM 4401 NH1 ARG D 161 42.431 35.562 190.040 1.00 71.11 N ANISOU 4401 NH1 ARG D 161 8887 9009 9121 273 -1635 490 N ATOM 4402 NH2 ARG D 161 41.184 34.480 191.640 1.00 66.58 N ANISOU 4402 NH2 ARG D 161 8189 8152 8956 442 -1543 -168 N ATOM 4403 N SER D 162 46.201 36.044 195.774 1.00 61.53 N ANISOU 4403 N SER D 162 8047 7138 8193 -615 -483 -1071 N ATOM 4404 CA SER D 162 46.633 37.359 196.260 1.00 64.69 C ANISOU 4404 CA SER D 162 8544 7128 8908 -851 -345 -1038 C ATOM 4405 C SER D 162 48.041 37.333 196.871 1.00 64.45 C ANISOU 4405 C SER D 162 8548 7304 8636 -1174 -273 -1184 C ATOM 4406 O SER D 162 48.555 38.360 197.317 1.00 66.41 O ANISOU 4406 O SER D 162 8882 7246 9105 -1441 -182 -1196 O ATOM 4407 CB SER D 162 45.614 37.963 197.229 1.00 65.80 C ANISOU 4407 CB SER D 162 8758 6719 9522 -779 -196 -1302 C ATOM 4408 OG SER D 162 44.813 36.957 197.818 1.00 63.42 O ANISOU 4408 OG SER D 162 8411 6537 9150 -595 -176 -1598 O ATOM 4409 N MET D 163 48.648 36.144 196.867 1.00 62.38 N ANISOU 4409 N MET D 163 8204 7549 7951 -1147 -331 -1288 N ATOM 4410 CA MET D 163 50.030 35.933 197.269 1.00 62.70 C ANISOU 4410 CA MET D 163 8191 7897 7736 -1404 -309 -1352 C ATOM 4411 C MET D 163 50.841 35.281 196.157 1.00 61.77 C ANISOU 4411 C MET D 163 7914 8304 7251 -1335 -372 -1096 C ATOM 4412 O MET D 163 52.005 34.936 196.382 1.00 61.13 O ANISOU 4412 O MET D 163 7717 8551 6958 -1489 -353 -1121 O ATOM 4413 CB MET D 163 50.092 35.057 198.517 1.00 61.59 C ANISOU 4413 CB MET D 163 8076 7869 7456 -1423 -295 -1743 C ATOM 4414 CG MET D 163 49.818 35.820 199.786 1.00 64.71 C ANISOU 4414 CG MET D 163 8636 7861 8090 -1630 -184 -2037 C ATOM 4415 SD MET D 163 50.705 35.125 201.187 1.00 65.59 S ANISOU 4415 SD MET D 163 8758 8267 7897 -1871 -210 -2352 S ATOM 4416 CE MET D 163 51.377 36.631 201.947 1.00 68.91 C ANISOU 4416 CE MET D 163 9325 8344 8515 -2341 -143 -2485 C ATOM 4417 N ASP D 164 50.206 35.125 194.987 1.00 61.66 N ANISOU 4417 N ASP D 164 7887 8379 7164 -1103 -444 -861 N ATOM 4418 CA ASP D 164 50.774 34.499 193.772 1.00 62.17 C ANISOU 4418 CA ASP D 164 7842 8952 6829 -995 -478 -648 C ATOM 4419 C ASP D 164 51.259 33.071 194.049 1.00 59.04 C ANISOU 4419 C ASP D 164 7360 8944 6130 -857 -483 -932 C ATOM 4420 O ASP D 164 52.351 32.662 193.662 1.00 58.95 O ANISOU 4420 O ASP D 164 7209 9340 5850 -886 -418 -871 O ATOM 4421 CB ASP D 164 51.866 35.386 193.140 1.00 66.25 C ANISOU 4421 CB ASP D 164 8274 9619 7281 -1251 -389 -279 C ATOM 4422 CG ASP D 164 52.149 35.045 191.672 1.00 68.72 C ANISOU 4422 CG ASP D 164 8514 10407 7190 -1128 -390 19 C ATOM 4423 OD1 ASP D 164 51.402 34.234 191.080 1.00 67.89 O ANISOU 4423 OD1 ASP D 164 8458 10462 6874 -852 -494 -65 O ATOM 4424 OD2 ASP D 164 53.138 35.582 191.118 1.00 71.79 O ANISOU 4424 OD2 ASP D 164 8795 11029 7454 -1332 -279 328 O ATOM 4425 N PHE D 165 50.416 32.316 194.732 1.00 56.48 N ANISOU 4425 N PHE D 165 7102 8469 5890 -697 -549 -1228 N ATOM 4426 CA PHE D 165 50.862 31.089 195.341 1.00 54.98 C ANISOU 4426 CA PHE D 165 6851 8504 5535 -613 -557 -1493 C ATOM 4427 C PHE D 165 49.864 29.966 195.103 1.00 53.76 C ANISOU 4427 C PHE D 165 6747 8353 5326 -335 -667 -1669 C ATOM 4428 O PHE D 165 48.657 30.135 195.314 1.00 52.83 O ANISOU 4428 O PHE D 165 6711 7934 5428 -273 -725 -1721 O ATOM 4429 CB PHE D 165 51.073 31.321 196.844 1.00 53.82 C ANISOU 4429 CB PHE D 165 6736 8150 5563 -818 -517 -1689 C ATOM 4430 CG PHE D 165 51.879 30.251 197.520 1.00 52.93 C ANISOU 4430 CG PHE D 165 6520 8310 5279 -800 -542 -1847 C ATOM 4431 CD1 PHE D 165 53.264 30.281 197.480 1.00 54.39 C ANISOU 4431 CD1 PHE D 165 6525 8810 5330 -934 -511 -1736 C ATOM 4432 CD2 PHE D 165 51.258 29.211 198.204 1.00 51.11 C ANISOU 4432 CD2 PHE D 165 6344 8019 5055 -652 -602 -2065 C ATOM 4433 CE1 PHE D 165 54.020 29.297 198.109 1.00 53.85 C ANISOU 4433 CE1 PHE D 165 6320 8986 5152 -889 -558 -1835 C ATOM 4434 CE2 PHE D 165 52.012 28.228 198.841 1.00 50.37 C ANISOU 4434 CE2 PHE D 165 6151 8147 4840 -625 -648 -2149 C ATOM 4435 CZ PHE D 165 53.393 28.271 198.787 1.00 51.61 C ANISOU 4435 CZ PHE D 165 6118 8612 4880 -726 -636 -2031 C ATOM 4436 N LYS D 166 50.386 28.827 194.650 1.00 54.07 N ANISOU 4436 N LYS D 166 6720 8719 5104 -170 -688 -1766 N ATOM 4437 CA LYS D 166 49.634 27.576 194.590 1.00 53.48 C ANISOU 4437 CA LYS D 166 6696 8629 4998 55 -800 -1990 C ATOM 4438 C LYS D 166 50.383 26.541 195.421 1.00 53.37 C ANISOU 4438 C LYS D 166 6609 8717 4953 100 -776 -2172 C ATOM 4439 O LYS D 166 51.611 26.628 195.564 1.00 54.45 O ANISOU 4439 O LYS D 166 6616 9082 4992 29 -687 -2103 O ATOM 4440 CB LYS D 166 49.498 27.086 193.154 1.00 54.72 C ANISOU 4440 CB LYS D 166 6875 9042 4875 237 -866 -1967 C ATOM 4441 CG LYS D 166 48.536 27.896 192.320 1.00 56.28 C ANISOU 4441 CG LYS D 166 7144 9146 5094 223 -972 -1761 C ATOM 4442 CD LYS D 166 48.576 27.465 190.865 1.00 58.84 C ANISOU 4442 CD LYS D 166 7509 9821 5026 354 -1043 -1726 C ATOM 4443 CE LYS D 166 47.952 28.524 189.993 1.00 61.37 C ANISOU 4443 CE LYS D 166 7870 10131 5317 290 -1144 -1383 C ATOM 4444 NZ LYS D 166 47.840 28.057 188.588 1.00 64.91 N ANISOU 4444 NZ LYS D 166 8393 10959 5312 395 -1255 -1363 N ATOM 4445 N SER D 167 49.658 25.576 195.984 1.00 52.46 N ANISOU 4445 N SER D 167 6552 8433 4948 206 -865 -2363 N ATOM 4446 CA SER D 167 50.303 24.518 196.771 1.00 51.95 C ANISOU 4446 CA SER D 167 6424 8430 4884 268 -873 -2481 C ATOM 4447 C SER D 167 49.499 23.235 196.737 1.00 51.40 C ANISOU 4447 C SER D 167 6427 8214 4889 453 -988 -2664 C ATOM 4448 O SER D 167 48.271 23.252 196.678 1.00 50.72 O ANISOU 4448 O SER D 167 6429 7913 4930 447 -1064 -2711 O ATOM 4449 CB SER D 167 50.546 24.943 198.231 1.00 50.65 C ANISOU 4449 CB SER D 167 6250 8157 4836 43 -842 -2454 C ATOM 4450 OG SER D 167 49.519 24.497 199.090 1.00 49.12 O ANISOU 4450 OG SER D 167 6157 7711 4795 28 -888 -2561 O ATOM 4451 N ASN D 168 50.217 22.124 196.766 1.00 52.15 N ANISOU 4451 N ASN D 168 6460 8411 4944 617 -1002 -2753 N ATOM 4452 CA ASN D 168 49.606 20.821 196.863 1.00 52.61 C ANISOU 4452 CA ASN D 168 6590 8275 5126 770 -1114 -2922 C ATOM 4453 C ASN D 168 49.546 20.374 198.335 1.00 51.87 C ANISOU 4453 C ASN D 168 6486 8010 5214 670 -1149 -2866 C ATOM 4454 O ASN D 168 50.320 20.867 199.174 1.00 51.95 O ANISOU 4454 O ASN D 168 6413 8139 5186 531 -1096 -2731 O ATOM 4455 CB ASN D 168 50.393 19.828 196.010 1.00 55.48 C ANISOU 4455 CB ASN D 168 6910 8788 5381 1036 -1096 -3068 C ATOM 4456 CG ASN D 168 50.463 20.238 194.547 1.00 57.19 C ANISOU 4456 CG ASN D 168 7162 9242 5326 1115 -1041 -3129 C ATOM 4457 OD1 ASN D 168 49.537 20.847 194.011 1.00 57.31 O ANISOU 4457 OD1 ASN D 168 7277 9217 5281 1021 -1114 -3101 O ATOM 4458 ND2 ASN D 168 51.566 19.906 193.897 1.00 59.48 N ANISOU 4458 ND2 ASN D 168 7352 9803 5444 1294 -907 -3189 N ATOM 4459 N SER D 169 48.615 19.468 198.650 1.00 50.70 N ANISOU 4459 N SER D 169 6421 7601 5242 706 -1248 -2951 N ATOM 4460 CA SER D 169 48.413 19.008 200.037 1.00 48.85 C ANISOU 4460 CA SER D 169 6197 7216 5149 588 -1274 -2856 C ATOM 4461 C SER D 169 47.746 17.638 200.151 1.00 49.29 C ANISOU 4461 C SER D 169 6313 6999 5418 686 -1392 -2926 C ATOM 4462 O SER D 169 46.755 17.357 199.492 1.00 49.62 O ANISOU 4462 O SER D 169 6419 6876 5558 714 -1462 -3059 O ATOM 4463 CB SER D 169 47.616 20.031 200.856 1.00 46.62 C ANISOU 4463 CB SER D 169 5961 6867 4885 335 -1189 -2791 C ATOM 4464 OG SER D 169 46.840 20.878 200.027 1.00 45.18 O ANISOU 4464 OG SER D 169 5803 6643 4718 323 -1160 -2848 O ATOM 4465 N ALA D 170 48.298 16.781 200.993 1.00 49.72 N ANISOU 4465 N ALA D 170 6336 6996 5560 721 -1440 -2810 N ATOM 4466 CA ALA D 170 47.630 15.536 201.330 1.00 50.00 C ANISOU 4466 CA ALA D 170 6435 6716 5845 754 -1549 -2807 C ATOM 4467 C ALA D 170 47.530 15.484 202.836 1.00 49.99 C ANISOU 4467 C ALA D 170 6435 6702 5858 545 -1536 -2553 C ATOM 4468 O ALA D 170 48.333 16.101 203.541 1.00 49.53 O ANISOU 4468 O ALA D 170 6320 6889 5610 447 -1492 -2409 O ATOM 4469 CB ALA D 170 48.393 14.365 200.811 1.00 52.35 C ANISOU 4469 CB ALA D 170 6712 6904 6276 1036 -1630 -2888 C ATOM 4470 N VAL D 171 46.524 14.766 203.327 1.00 50.24 N ANISOU 4470 N VAL D 171 6529 6470 6089 446 -1579 -2495 N ATOM 4471 CA VAL D 171 46.220 14.734 204.749 1.00 50.35 C ANISOU 4471 CA VAL D 171 6566 6500 6065 210 -1532 -2246 C ATOM 4472 C VAL D 171 46.274 13.281 205.252 1.00 53.14 C ANISOU 4472 C VAL D 171 6940 6595 6658 263 -1673 -2043 C ATOM 4473 O VAL D 171 45.758 12.378 204.595 1.00 53.94 O ANISOU 4473 O VAL D 171 7073 6377 7047 373 -1768 -2153 O ATOM 4474 CB VAL D 171 44.829 15.360 204.990 1.00 49.18 C ANISOU 4474 CB VAL D 171 6444 6296 5945 -3 -1393 -2305 C ATOM 4475 CG1 VAL D 171 44.351 15.144 206.406 1.00 50.57 C ANISOU 4475 CG1 VAL D 171 6655 6481 6079 -247 -1302 -2071 C ATOM 4476 CG2 VAL D 171 44.844 16.844 204.678 1.00 46.78 C ANISOU 4476 CG2 VAL D 171 6125 6201 5447 -53 -1251 -2449 C ATOM 4477 N ALA D 172 46.935 13.040 206.384 1.00 54.58 N ANISOU 4477 N ALA D 172 7107 6901 6728 179 -1713 -1738 N ATOM 4478 CA ALA D 172 46.886 11.708 206.991 1.00 58.15 C ANISOU 4478 CA ALA D 172 7583 7085 7427 196 -1849 -1456 C ATOM 4479 C ALA D 172 46.526 11.740 208.466 1.00 59.99 C ANISOU 4479 C ALA D 172 7867 7452 7473 -115 -1799 -1112 C ATOM 4480 O ALA D 172 46.897 12.676 209.166 1.00 59.47 O ANISOU 4480 O ALA D 172 7807 7755 7035 -285 -1716 -1061 O ATOM 4481 CB ALA D 172 48.186 10.976 206.794 1.00 60.08 C ANISOU 4481 CB ALA D 172 7740 7289 7800 487 -2012 -1342 C ATOM 4482 N TRP D 173 45.812 10.712 208.926 1.00 63.19 N ANISOU 4482 N TRP D 173 8320 7562 8125 -208 -1847 -882 N ATOM 4483 CA TRP D 173 45.426 10.593 210.335 1.00 66.45 C ANISOU 4483 CA TRP D 173 8791 8116 8342 -517 -1784 -505 C ATOM 4484 C TRP D 173 45.149 9.145 210.747 1.00 71.62 C ANISOU 4484 C TRP D 173 9472 8394 9345 -536 -1930 -129 C ATOM 4485 O TRP D 173 44.820 8.310 209.903 1.00 72.09 O ANISOU 4485 O TRP D 173 9527 8010 9855 -373 -2029 -254 O ATOM 4486 CB TRP D 173 44.211 11.485 210.653 1.00 64.44 C ANISOU 4486 CB TRP D 173 8568 8010 7908 -791 -1500 -662 C ATOM 4487 CG TRP D 173 42.858 11.009 210.116 1.00 64.11 C ANISOU 4487 CG TRP D 173 8488 7620 8250 -841 -1433 -771 C ATOM 4488 CD1 TRP D 173 41.894 10.338 210.816 1.00 66.45 C ANISOU 4488 CD1 TRP D 173 8782 7772 8694 -1079 -1353 -501 C ATOM 4489 CD2 TRP D 173 42.321 11.210 208.793 1.00 61.26 C ANISOU 4489 CD2 TRP D 173 8066 7058 8151 -688 -1452 -1153 C ATOM 4490 NE1 TRP D 173 40.808 10.096 210.013 1.00 66.00 N ANISOU 4490 NE1 TRP D 173 8640 7422 9014 -1087 -1336 -699 N ATOM 4491 CE2 TRP D 173 41.043 10.618 208.768 1.00 62.79 C ANISOU 4491 CE2 TRP D 173 8206 6985 8668 -849 -1415 -1102 C ATOM 4492 CE3 TRP D 173 42.797 11.824 207.631 1.00 58.26 C ANISOU 4492 CE3 TRP D 173 7665 6727 7744 -454 -1507 -1502 C ATOM 4493 CZ2 TRP D 173 40.235 10.621 207.624 1.00 61.30 C ANISOU 4493 CZ2 TRP D 173 7938 6582 8771 -785 -1473 -1404 C ATOM 4494 CZ3 TRP D 173 41.985 11.822 206.492 1.00 57.28 C ANISOU 4494 CZ3 TRP D 173 7493 6402 7869 -384 -1548 -1787 C ATOM 4495 CH2 TRP D 173 40.724 11.225 206.503 1.00 58.18 C ANISOU 4495 CH2 TRP D 173 7550 6258 8298 -550 -1551 -1742 C ATOM 4496 N SER D 174 45.292 8.854 212.044 1.00 76.51 N ANISOU 4496 N SER D 174 10137 9187 9747 -753 -1955 337 N ATOM 4497 CA SER D 174 44.924 7.537 212.597 1.00 82.47 C ANISOU 4497 CA SER D 174 10927 9593 10814 -840 -2073 792 C ATOM 4498 C SER D 174 43.969 7.624 213.794 1.00 85.65 C ANISOU 4498 C SER D 174 11397 10201 10944 -1259 -1870 1107 C ATOM 4499 O SER D 174 43.825 8.689 214.397 1.00 84.39 O ANISOU 4499 O SER D 174 11275 10510 10280 -1464 -1654 1004 O ATOM 4500 CB SER D 174 46.161 6.729 212.981 1.00 85.86 C ANISOU 4500 CB SER D 174 11326 9958 11341 -644 -2367 1207 C ATOM 4501 OG SER D 174 45.788 5.468 213.511 1.00 90.73 O ANISOU 4501 OG SER D 174 11988 10185 12301 -731 -2488 1689 O ATOM 4502 N ASN D 175 43.342 6.491 214.127 1.00 90.73 N ANISOU 4502 N ASN D 175 12060 10480 11933 -1387 -1923 1483 N ATOM 4503 CA ASN D 175 42.257 6.408 215.123 1.00 94.70 C ANISOU 4503 CA ASN D 175 12595 11118 12269 -1794 -1687 1794 C ATOM 4504 C ASN D 175 42.652 6.775 216.559 1.00 98.25 C ANISOU 4504 C ASN D 175 13142 12124 12066 -2059 -1612 2203 C ATOM 4505 O ASN D 175 42.312 7.856 217.040 1.00 97.27 O ANISOU 4505 O ASN D 175 13054 12465 11441 -2254 -1323 1986 O ATOM 4506 CB ASN D 175 41.617 5.009 215.108 1.00 99.07 C ANISOU 4506 CB ASN D 175 13137 11106 13398 -1882 -1803 2163 C ATOM 4507 CG ASN D 175 41.039 4.630 213.745 1.00 97.34 C ANISOU 4507 CG ASN D 175 12846 10350 13787 -1708 -1873 1723 C ATOM 4508 OD1 ASN D 175 40.671 5.494 212.948 1.00 93.25 O ANISOU 4508 OD1 ASN D 175 12265 9953 13214 -1629 -1745 1194 O ATOM 4509 ND2 ASN D 175 40.949 3.329 213.482 1.00100.79 N ANISOU 4509 ND2 ASN D 175 13306 10183 14807 -1665 -2094 1952 N ATOM 4510 N LYS D 176 43.349 5.864 217.236 1.00103.62 N ANISOU 4510 N LYS D 176 13869 12743 12760 -2066 -1879 2790 N ATOM 4511 CA LYS D 176 43.946 6.121 218.559 1.00107.78 C ANISOU 4511 CA LYS D 176 14496 13830 12628 -2299 -1919 3227 C ATOM 4512 C LYS D 176 45.193 5.240 218.670 1.00111.45 C ANISOU 4512 C LYS D 176 14926 14124 13296 -2059 -2367 3699 C ATOM 4513 O LYS D 176 45.222 4.262 219.428 1.00117.15 O ANISOU 4513 O LYS D 176 15689 14725 14099 -2187 -2531 4370 O ATOM 4514 CB LYS D 176 42.955 5.828 219.704 1.00112.13 C ANISOU 4514 CB LYS D 176 15135 14578 12893 -2745 -1669 3676 C ATOM 4515 CG LYS D 176 43.200 6.622 221.007 1.00114.26 C ANISOU 4515 CG LYS D 176 15551 15607 12256 -3075 -1524 3839 C ATOM 4516 CD LYS D 176 43.812 5.771 222.117 1.00120.51 C ANISOU 4516 CD LYS D 176 16432 16578 12776 -3249 -1812 4659 C ATOM 4517 CE LYS D 176 42.835 4.708 222.604 1.00125.41 C ANISOU 4517 CE LYS D 176 17067 16927 13655 -3506 -1693 5233 C ATOM 4518 NZ LYS D 176 43.434 3.807 223.628 1.00132.13 N ANISOU 4518 NZ LYS D 176 18004 17898 14300 -3659 -2010 6117 N ATOM 4519 N SER D 177 46.219 5.591 217.897 1.00108.57 N ANISOU 4519 N SER D 177 14462 13746 13043 -1703 -2554 3371 N ATOM 4520 CA SER D 177 47.379 4.722 217.727 1.00111.50 C ANISOU 4520 CA SER D 177 14725 13855 13784 -1367 -2951 3723 C ATOM 4521 C SER D 177 48.665 5.291 218.333 1.00112.73 C ANISOU 4521 C SER D 177 14812 14579 13440 -1348 -3181 3908 C ATOM 4522 O SER D 177 48.635 6.199 219.166 1.00112.64 O ANISOU 4522 O SER D 177 14898 15178 12724 -1685 -3072 3894 O ATOM 4523 CB SER D 177 47.583 4.427 216.235 1.00108.02 C ANISOU 4523 CB SER D 177 14175 12870 13998 -918 -2995 3229 C ATOM 4524 OG SER D 177 46.397 3.911 215.656 1.00107.05 O ANISOU 4524 OG SER D 177 14113 12239 14321 -974 -2833 3035 O ATOM 4525 N ASP D 178 49.791 4.716 217.921 1.00114.44 N ANISOU 4525 N ASP D 178 14849 14581 14052 -956 -3504 4080 N ATOM 4526 CA ASP D 178 51.102 5.290 218.177 1.00114.90 C ANISOU 4526 CA ASP D 178 14748 15129 13779 -864 -3742 4152 C ATOM 4527 C ASP D 178 51.713 5.673 216.829 1.00110.46 C ANISOU 4527 C ASP D 178 14001 14394 13574 -445 -3700 3558 C ATOM 4528 O ASP D 178 52.925 5.603 216.630 1.00111.81 O ANISOU 4528 O ASP D 178 13933 14666 13882 -158 -3943 3669 O ATOM 4529 CB ASP D 178 51.991 4.303 218.936 1.00121.71 C ANISOU 4529 CB ASP D 178 15484 15968 14790 -755 -4168 4955 C ATOM 4530 CG ASP D 178 51.880 2.887 218.402 1.00124.80 C ANISOU 4530 CG ASP D 178 15821 15551 16047 -395 -4284 5218 C ATOM 4531 OD1 ASP D 178 50.825 2.544 217.816 1.00122.62 O ANISOU 4531 OD1 ASP D 178 15685 14782 16123 -409 -4038 4923 O ATOM 4532 OD2 ASP D 178 52.853 2.119 218.574 1.00129.58 O ANISOU 4532 OD2 ASP D 178 16232 15999 17003 -99 -4633 5719 O ATOM 4533 N PHE D 179 50.831 6.067 215.912 1.00105.55 N ANISOU 4533 N PHE D 179 13475 13534 13096 -423 -3386 2955 N ATOM 4534 CA PHE D 179 51.167 6.517 214.569 1.00100.96 C ANISOU 4534 CA PHE D 179 12776 12817 12768 -90 -3279 2347 C ATOM 4535 C PHE D 179 51.830 7.887 214.629 1.00 97.71 C ANISOU 4535 C PHE D 179 12288 13011 11826 -210 -3232 2073 C ATOM 4536 O PHE D 179 51.372 8.762 215.358 1.00 96.41 O ANISOU 4536 O PHE D 179 12270 13248 11113 -604 -3096 2015 O ATOM 4537 CB PHE D 179 49.866 6.559 213.763 1.00 98.00 C ANISOU 4537 CB PHE D 179 12552 12074 12610 -133 -2994 1880 C ATOM 4538 CG PHE D 179 49.817 7.612 212.684 1.00 93.27 C ANISOU 4538 CG PHE D 179 11923 11603 11913 -32 -2788 1221 C ATOM 4539 CD1 PHE D 179 50.353 7.359 211.431 1.00 92.55 C ANISOU 4539 CD1 PHE D 179 11714 11243 12208 378 -2814 886 C ATOM 4540 CD2 PHE D 179 49.170 8.832 212.895 1.00 89.98 C ANISOU 4540 CD2 PHE D 179 11607 11547 11035 -343 -2546 936 C ATOM 4541 CE1 PHE D 179 50.286 8.314 210.422 1.00 88.11 C ANISOU 4541 CE1 PHE D 179 11134 10819 11524 450 -2630 338 C ATOM 4542 CE2 PHE D 179 49.114 9.790 211.899 1.00 85.67 C ANISOU 4542 CE2 PHE D 179 11033 11081 10437 -248 -2379 398 C ATOM 4543 CZ PHE D 179 49.667 9.530 210.660 1.00 84.65 C ANISOU 4543 CZ PHE D 179 10788 10724 10652 133 -2432 125 C ATOM 4544 N ALA D 180 52.893 8.082 213.856 1.00 96.64 N ANISOU 4544 N ALA D 180 11922 12928 11868 118 -3319 1885 N ATOM 4545 CA ALA D 180 53.609 9.360 213.870 1.00 94.36 C ANISOU 4545 CA ALA D 180 11531 13183 11139 -13 -3298 1655 C ATOM 4546 C ALA D 180 53.739 9.973 212.471 1.00 89.92 C ANISOU 4546 C ALA D 180 10882 12528 10755 234 -3092 1070 C ATOM 4547 O ALA D 180 53.475 9.305 211.474 1.00 89.09 O ANISOU 4547 O ALA D 180 10767 11974 11109 560 -3010 860 O ATOM 4548 CB ALA D 180 54.982 9.192 214.518 1.00 98.46 C ANISOU 4548 CB ALA D 180 11787 14050 11575 45 -3648 2116 C ATOM 4549 N CYS D 181 54.167 11.235 212.402 1.00 87.45 N ANISOU 4549 N CYS D 181 10517 12643 10069 61 -3018 819 N ATOM 4550 CA CYS D 181 54.272 11.954 211.127 1.00 83.69 C ANISOU 4550 CA CYS D 181 9973 12139 9688 233 -2811 318 C ATOM 4551 C CYS D 181 55.526 11.653 210.298 1.00 85.42 C ANISOU 4551 C CYS D 181 9862 12381 10214 636 -2899 316 C ATOM 4552 O CYS D 181 55.688 12.195 209.210 1.00 83.10 O ANISOU 4552 O CYS D 181 9500 12100 9973 784 -2719 -59 O ATOM 4553 CB CYS D 181 54.174 13.462 211.337 1.00 80.87 C ANISOU 4553 CB CYS D 181 9702 12162 8863 -125 -2673 54 C ATOM 4554 SG CYS D 181 52.545 14.139 211.784 1.00 78.49 S ANISOU 4554 SG CYS D 181 9761 11781 8281 -493 -2394 -197 S ATOM 4555 N ALA D 182 56.422 10.820 210.814 1.00 90.13 N ANISOU 4555 N ALA D 182 10233 13006 11005 814 -3164 756 N ATOM 4556 CA ALA D 182 57.534 10.326 210.011 1.00 92.71 C ANISOU 4556 CA ALA D 182 10212 13281 11731 1274 -3207 764 C ATOM 4557 C ALA D 182 57.177 8.936 209.515 1.00 94.98 C ANISOU 4557 C ALA D 182 10555 12963 12569 1675 -3194 777 C ATOM 4558 O ALA D 182 57.538 8.544 208.404 1.00 95.67 O ANISOU 4558 O ALA D 182 10515 12829 13008 2087 -3056 494 O ATOM 4559 CB ALA D 182 58.823 10.301 210.820 1.00 97.05 C ANISOU 4559 CB ALA D 182 10411 14233 12232 1264 -3517 1241 C ATOM 4560 N ASN D 183 56.430 8.209 210.348 1.00 96.80 N ANISOU 4560 N ASN D 183 10997 12924 12857 1527 -3321 1091 N ATOM 4561 CA ASN D 183 55.859 6.908 209.998 1.00 98.81 C ANISOU 4561 CA ASN D 183 11379 12526 13639 1800 -3320 1109 C ATOM 4562 C ASN D 183 54.494 7.093 209.344 1.00 94.49 C ANISOU 4562 C ASN D 183 11153 11695 13053 1650 -3075 641 C ATOM 4563 O ASN D 183 53.518 6.448 209.727 1.00 94.89 O ANISOU 4563 O ASN D 183 11422 11388 13243 1502 -3097 774 O ATOM 4564 CB ASN D 183 55.711 6.033 211.250 1.00103.30 C ANISOU 4564 CB ASN D 183 12002 12945 14302 1669 -3590 1755 C ATOM 4565 CG ASN D 183 57.052 5.562 211.810 1.00108.87 C ANISOU 4565 CG ASN D 183 12353 13819 15194 1908 -3897 2290 C ATOM 4566 OD1 ASN D 183 57.872 4.985 211.094 1.00111.66 O ANISOU 4566 OD1 ASN D 183 12443 13945 16037 2399 -3906 2230 O ATOM 4567 ND2 ASN D 183 57.267 5.789 213.104 1.00110.94 N ANISOU 4567 ND2 ASN D 183 12597 14494 15063 1564 -4151 2821 N ATOM 4568 N ALA D 184 54.442 7.988 208.363 1.00 90.50 N ANISOU 4568 N ALA D 184 10650 11371 12365 1672 -2854 134 N ATOM 4569 CA ALA D 184 53.204 8.394 207.736 1.00 86.91 C ANISOU 4569 CA ALA D 184 10452 10762 11809 1502 -2651 -289 C ATOM 4570 C ALA D 184 53.349 8.317 206.229 1.00 86.15 C ANISOU 4570 C ALA D 184 10328 10496 11908 1841 -2495 -792 C ATOM 4571 O ALA D 184 52.540 7.691 205.553 1.00 85.67 O ANISOU 4571 O ALA D 184 10443 10008 12100 1927 -2447 -1062 O ATOM 4572 CB ALA D 184 52.862 9.806 208.152 1.00 82.95 C ANISOU 4572 CB ALA D 184 10019 10724 10773 1102 -2540 -375 C ATOM 4573 N PHE D 185 54.401 8.945 205.714 1.00 86.54 N ANISOU 4573 N PHE D 185 10152 10907 11822 2008 -2421 -909 N ATOM 4574 CA PHE D 185 54.577 9.074 204.271 1.00 86.59 C ANISOU 4574 CA PHE D 185 10137 10886 11879 2284 -2226 -1389 C ATOM 4575 C PHE D 185 55.835 8.417 203.715 1.00 91.35 C ANISOU 4575 C PHE D 185 10463 11461 12787 2762 -2197 -1411 C ATOM 4576 O PHE D 185 56.258 8.733 202.603 1.00 91.16 O ANISOU 4576 O PHE D 185 10356 11589 12691 2971 -1995 -1766 O ATOM 4577 CB PHE D 185 54.537 10.544 203.856 1.00 82.46 C ANISOU 4577 CB PHE D 185 9609 10817 10905 2050 -2067 -1596 C ATOM 4578 CG PHE D 185 53.223 11.200 204.119 1.00 78.76 C ANISOU 4578 CG PHE D 185 9401 10317 10207 1669 -2032 -1683 C ATOM 4579 CD1 PHE D 185 53.058 12.035 205.205 1.00 77.27 C ANISOU 4579 CD1 PHE D 185 9235 10400 9723 1297 -2069 -1448 C ATOM 4580 CD2 PHE D 185 52.144 10.966 203.289 1.00 77.64 C ANISOU 4580 CD2 PHE D 185 9469 9879 10153 1684 -1962 -2014 C ATOM 4581 CE1 PHE D 185 51.845 12.626 205.460 1.00 74.45 C ANISOU 4581 CE1 PHE D 185 9088 10000 9199 989 -1991 -1544 C ATOM 4582 CE2 PHE D 185 50.931 11.560 203.535 1.00 74.72 C ANISOU 4582 CE2 PHE D 185 9274 9487 9629 1361 -1927 -2066 C ATOM 4583 CZ PHE D 185 50.780 12.390 204.623 1.00 73.10 C ANISOU 4583 CZ PHE D 185 9072 9534 9167 1034 -1917 -1833 C ATOM 4584 N ASN D 186 56.425 7.488 204.462 1.00 96.40 N ANISOU 4584 N ASN D 186 10945 11907 13775 2951 -2382 -1021 N ATOM 4585 CA ASN D 186 57.554 6.722 203.926 1.00101.82 C ANISOU 4585 CA ASN D 186 11344 12477 14864 3475 -2336 -1049 C ATOM 4586 C ASN D 186 57.111 5.564 203.010 1.00104.78 C ANISOU 4586 C ASN D 186 11916 12221 15674 3830 -2237 -1447 C ATOM 4587 O ASN D 186 57.942 4.869 202.418 1.00109.21 O ANISOU 4587 O ASN D 186 12284 12609 16601 4313 -2134 -1589 O ATOM 4588 CB ASN D 186 58.531 6.269 205.030 1.00106.55 C ANISOU 4588 CB ASN D 186 11622 13166 15699 3585 -2591 -439 C ATOM 4589 CG ASN D 186 57.831 5.651 206.237 1.00107.96 C ANISOU 4589 CG ASN D 186 11997 13046 15979 3339 -2865 19 C ATOM 4590 OD1 ASN D 186 56.749 6.092 206.648 1.00104.35 O ANISOU 4590 OD1 ASN D 186 11840 12605 15202 2908 -2873 -2 O ATOM 4591 ND2 ASN D 186 58.462 4.629 206.821 1.00113.46 N ANISOU 4591 ND2 ASN D 186 12499 13478 17133 3620 -3079 468 N ATOM 4592 N ASN D 187 55.793 5.381 202.898 1.00102.68 N ANISOU 4592 N ASN D 187 12024 11617 15374 3579 -2262 -1647 N ATOM 4593 CA ASN D 187 55.177 4.547 201.867 1.00104.42 C ANISOU 4593 CA ASN D 187 12495 11308 15873 3786 -2168 -2152 C ATOM 4594 C ASN D 187 55.199 5.249 200.508 1.00102.25 C ANISOU 4594 C ASN D 187 12268 11337 15246 3860 -1908 -2726 C ATOM 4595 O ASN D 187 55.192 4.595 199.468 1.00105.12 O ANISOU 4595 O ASN D 187 12748 11403 15789 4158 -1779 -3205 O ATOM 4596 CB ASN D 187 53.737 4.178 202.263 1.00103.32 C ANISOU 4596 CB ASN D 187 12689 10760 15809 3424 -2317 -2119 C ATOM 4597 CG ASN D 187 52.859 5.408 202.556 1.00 97.89 C ANISOU 4597 CG ASN D 187 12109 10495 14591 2925 -2298 -2086 C ATOM 4598 OD1 ASN D 187 52.253 5.984 201.650 1.00 95.38 O ANISOU 4598 OD1 ASN D 187 11928 10297 14013 2822 -2178 -2507 O ATOM 4599 ND2 ASN D 187 52.772 5.792 203.830 1.00 96.44 N ANISOU 4599 ND2 ASN D 187 11867 10527 14250 2622 -2418 -1585 N ATOM 4600 N SER D 188 55.231 6.584 200.538 1.00 97.74 N ANISOU 4600 N SER D 188 11623 11352 14163 3575 -1835 -2669 N ATOM 4601 CA SER D 188 55.305 7.424 199.340 1.00 95.94 C ANISOU 4601 CA SER D 188 11414 11496 13541 3592 -1602 -3089 C ATOM 4602 C SER D 188 56.744 7.720 198.919 1.00 98.39 C ANISOU 4602 C SER D 188 11365 12218 13801 3908 -1400 -3084 C ATOM 4603 O SER D 188 57.691 7.498 199.678 1.00100.73 O ANISOU 4603 O SER D 188 11350 12599 14324 4056 -1474 -2703 O ATOM 4604 CB SER D 188 54.592 8.763 199.579 1.00 90.35 C ANISOU 4604 CB SER D 188 10800 11164 12364 3119 -1618 -2996 C ATOM 4605 OG SER D 188 53.220 8.592 199.890 1.00 88.49 O ANISOU 4605 OG SER D 188 10847 10612 12164 2826 -1759 -3016 O ATOM 4606 N ILE D 189 56.895 8.235 197.702 1.00 98.29 N ANISOU 4606 N ILE D 189 11376 12493 13479 3994 -1152 -3480 N ATOM 4607 CA ILE D 189 58.192 8.691 197.213 1.00100.39 C ANISOU 4607 CA ILE D 189 11281 13237 13627 4231 -906 -3475 C ATOM 4608 C ILE D 189 58.356 10.200 197.448 1.00 96.00 C ANISOU 4608 C ILE D 189 10596 13253 12626 3837 -889 -3222 C ATOM 4609 O ILE D 189 58.292 11.012 196.522 1.00 94.69 O ANISOU 4609 O ILE D 189 10483 13418 12076 3742 -696 -3437 O ATOM 4610 CB ILE D 189 58.441 8.307 195.725 1.00104.32 C ANISOU 4610 CB ILE D 189 11847 13755 14035 4589 -590 -4039 C ATOM 4611 CG1 ILE D 189 57.133 8.312 194.912 1.00102.80 C ANISOU 4611 CG1 ILE D 189 12120 13367 13574 4392 -624 -4469 C ATOM 4612 CG2 ILE D 189 59.077 6.934 195.635 1.00110.14 C ANISOU 4612 CG2 ILE D 189 12469 14068 15312 5120 -514 -4195 C ATOM 4613 CD1 ILE D 189 56.678 6.936 194.443 1.00107.35 C ANISOU 4613 CD1 ILE D 189 12965 13332 14493 4670 -649 -4908 C ATOM 4614 N ILE D 190 58.562 10.552 198.712 1.00 94.21 N ANISOU 4614 N ILE D 190 10217 13124 12455 3595 -1104 -2756 N ATOM 4615 CA ILE D 190 58.759 11.929 199.161 1.00 90.74 C ANISOU 4615 CA ILE D 190 9662 13150 11665 3193 -1130 -2501 C ATOM 4616 C ILE D 190 60.133 12.458 198.693 1.00 93.44 C ANISOU 4616 C ILE D 190 9576 13992 11935 3338 -926 -2425 C ATOM 4617 O ILE D 190 61.046 11.662 198.495 1.00 98.06 O ANISOU 4617 O ILE D 190 9869 14565 12824 3750 -834 -2420 O ATOM 4618 CB ILE D 190 58.604 11.961 200.696 1.00 89.47 C ANISOU 4618 CB ILE D 190 9488 12923 11582 2909 -1431 -2070 C ATOM 4619 CG1 ILE D 190 59.474 10.884 201.345 1.00 94.22 C ANISOU 4619 CG1 ILE D 190 9808 13385 12606 3228 -1574 -1780 C ATOM 4620 CG2 ILE D 190 57.182 11.640 201.065 1.00 86.69 C ANISOU 4620 CG2 ILE D 190 9539 12159 11239 2707 -1562 -2146 C ATOM 4621 CD1 ILE D 190 59.145 10.609 202.795 1.00 93.97 C ANISOU 4621 CD1 ILE D 190 9845 13211 12649 2983 -1892 -1359 C ATOM 4622 N PRO D 191 60.270 13.784 198.453 1.00 91.26 N ANISOU 4622 N PRO D 191 9248 14132 11295 3014 -831 -2373 N ATOM 4623 CA PRO D 191 61.544 14.375 197.966 1.00 94.56 C ANISOU 4623 CA PRO D 191 9239 15052 11637 3085 -619 -2272 C ATOM 4624 C PRO D 191 62.730 14.423 198.954 1.00 98.24 C ANISOU 4624 C PRO D 191 9229 15781 12318 3058 -776 -1843 C ATOM 4625 O PRO D 191 63.260 13.386 199.347 1.00101.95 O ANISOU 4625 O PRO D 191 9477 16098 13162 3400 -864 -1721 O ATOM 4626 CB PRO D 191 61.139 15.802 197.576 1.00 90.55 C ANISOU 4626 CB PRO D 191 8882 14807 10715 2662 -538 -2287 C ATOM 4627 CG PRO D 191 59.693 15.724 197.310 1.00 86.84 C ANISOU 4627 CG PRO D 191 8903 13978 10113 2562 -598 -2542 C ATOM 4628 CD PRO D 191 59.153 14.731 198.292 1.00 86.46 C ANISOU 4628 CD PRO D 191 8995 13502 10354 2627 -851 -2481 C ATOM 4629 N GLU D 192 63.181 15.628 199.292 1.00 98.53 N ANISOU 4629 N GLU D 192 9088 16209 12139 2657 -819 -1613 N ATOM 4630 CA GLU D 192 64.123 15.823 200.402 1.00102.02 C ANISOU 4630 CA GLU D 192 9137 16911 12716 2488 -1070 -1193 C ATOM 4631 C GLU D 192 63.622 16.984 201.257 1.00 99.65 C ANISOU 4631 C GLU D 192 9060 16687 12116 1886 -1283 -1064 C ATOM 4632 O GLU D 192 63.957 18.144 201.012 1.00 98.95 O ANISOU 4632 O GLU D 192 8873 16900 11824 1564 -1195 -1029 O ATOM 4633 CB GLU D 192 65.549 16.064 199.911 1.00106.28 C ANISOU 4633 CB GLU D 192 9085 17927 13371 2636 -884 -1044 C ATOM 4634 CG GLU D 192 66.332 14.787 199.627 1.00111.41 C ANISOU 4634 CG GLU D 192 9365 18517 14449 3248 -775 -1035 C ATOM 4635 CD GLU D 192 67.791 14.873 200.072 1.00116.41 C ANISOU 4635 CD GLU D 192 9301 19592 15339 3297 -858 -634 C ATOM 4636 OE1 GLU D 192 68.256 13.952 200.781 1.00119.67 O ANISOU 4636 OE1 GLU D 192 9448 19885 16136 3577 -1085 -379 O ATOM 4637 OE2 GLU D 192 68.472 15.863 199.722 1.00117.08 O ANISOU 4637 OE2 GLU D 192 9080 20141 15264 3043 -714 -538 O ATOM 4638 N ASP D 193 62.831 16.639 202.274 1.00 99.46 N ANISOU 4638 N ASP D 193 9335 16372 12083 1739 -1547 -993 N ATOM 4639 CA ASP D 193 61.854 17.549 202.878 1.00 97.22 C ANISOU 4639 CA ASP D 193 9446 15993 11500 1259 -1647 -1049 C ATOM 4640 C ASP D 193 62.106 18.003 204.318 1.00 99.38 C ANISOU 4640 C ASP D 193 9680 16438 11642 840 -1963 -766 C ATOM 4641 O ASP D 193 63.181 17.772 204.863 1.00103.57 O ANISOU 4641 O ASP D 193 9818 17246 12288 856 -2155 -466 O ATOM 4642 CB ASP D 193 60.462 16.923 202.785 1.00 94.06 C ANISOU 4642 CB ASP D 193 9503 15125 11112 1368 -1623 -1276 C ATOM 4643 CG ASP D 193 60.496 15.437 202.694 1.00 96.26 C ANISOU 4643 CG ASP D 193 9733 15121 11720 1821 -1663 -1266 C ATOM 4644 OD1 ASP D 193 60.144 14.901 201.622 1.00 95.71 O ANISOU 4644 OD1 ASP D 193 9775 14841 11749 2139 -1462 -1562 O ATOM 4645 OD2 ASP D 193 60.872 14.809 203.701 1.00 99.05 O ANISOU 4645 OD2 ASP D 193 9952 15454 12231 1845 -1909 -959 O ATOM 4646 N THR D 194 61.103 18.653 204.917 1.00 98.28 N ANISOU 4646 N THR D 194 9941 16149 11252 468 -2013 -873 N ATOM 4647 CA THR D 194 61.213 19.224 206.272 1.00101.36 C ANISOU 4647 CA THR D 194 10385 16713 11414 9 -2275 -696 C ATOM 4648 C THR D 194 60.343 18.485 207.283 1.00102.56 C ANISOU 4648 C THR D 194 10835 16629 11504 -26 -2436 -617 C ATOM 4649 O THR D 194 59.216 18.098 206.989 1.00 99.59 O ANISOU 4649 O THR D 194 10772 15896 11172 104 -2295 -806 O ATOM 4650 CB THR D 194 60.799 20.724 206.307 1.00 99.11 C ANISOU 4650 CB THR D 194 10331 16464 10861 -452 -2173 -902 C ATOM 4651 OG1 THR D 194 61.252 21.374 205.116 1.00 99.26 O ANISOU 4651 OG1 THR D 194 10174 16589 10950 -388 -1947 -1000 O ATOM 4652 CG2 THR D 194 61.362 21.457 207.541 1.00101.27 C ANISOU 4652 CG2 THR D 194 10553 17028 10897 -948 -2438 -756 C ATOM 4653 N PHE D 195 60.891 18.277 208.473 1.00108.25 N ANISOU 4653 N PHE D 195 11436 17579 12116 -222 -2745 -306 N ATOM 4654 CA PHE D 195 60.138 17.761 209.591 1.00111.10 C ANISOU 4654 CA PHE D 195 12084 17813 12317 -366 -2904 -173 C ATOM 4655 C PHE D 195 60.391 18.737 210.731 1.00115.25 C ANISOU 4655 C PHE D 195 12688 18682 12420 -920 -3097 -118 C ATOM 4656 O PHE D 195 60.972 19.801 210.506 1.00115.51 O ANISOU 4656 O PHE D 195 12597 18938 12353 -1167 -3074 -241 O ATOM 4657 CB PHE D 195 60.600 16.340 209.933 1.00113.88 C ANISOU 4657 CB PHE D 195 12218 18105 12946 -21 -3129 213 C ATOM 4658 CG PHE D 195 60.083 15.282 208.978 1.00112.24 C ANISOU 4658 CG PHE D 195 12062 17447 13137 481 -2938 89 C ATOM 4659 CD1 PHE D 195 58.983 14.510 209.309 1.00111.06 C ANISOU 4659 CD1 PHE D 195 12237 16920 13042 529 -2926 99 C ATOM 4660 CD2 PHE D 195 60.691 15.061 207.749 1.00112.36 C ANISOU 4660 CD2 PHE D 195 11807 17425 13459 881 -2759 -57 C ATOM 4661 CE1 PHE D 195 58.506 13.545 208.438 1.00110.07 C ANISOU 4661 CE1 PHE D 195 12174 16355 13291 942 -2782 -49 C ATOM 4662 CE2 PHE D 195 60.210 14.099 206.879 1.00111.63 C ANISOU 4662 CE2 PHE D 195 11805 16917 13692 1313 -2590 -237 C ATOM 4663 CZ PHE D 195 59.118 13.340 207.227 1.00110.46 C ANISOU 4663 CZ PHE D 195 11991 16361 13618 1333 -2622 -241 C ATOM 4664 N PHE D 196 59.936 18.385 211.933 1.00 63.33 N ATOM 4665 CA PHE D 196 60.250 19.122 213.166 1.00 66.21 C ATOM 4666 C PHE D 196 60.046 18.136 214.309 1.00 66.77 C ATOM 4667 O PHE D 196 59.474 17.075 214.052 1.00 66.95 O ATOM 4668 CB PHE D 196 59.359 20.370 213.343 1.00 68.25 C ATOM 4669 CG PHE D 196 59.849 21.349 214.412 1.00 70.01 C ATOM 4670 CD1 PHE D 196 61.000 22.119 214.205 1.00 70.36 C ATOM 4671 CD2 PHE D 196 59.138 21.510 215.614 1.00 70.55 C ATOM 4672 CE1 PHE D 196 61.438 23.018 215.181 1.00 71.00 C ATOM 4673 CE2 PHE D 196 59.568 22.410 216.596 1.00 70.84 C ATOM 4674 CZ PHE D 196 60.718 23.163 216.381 1.00 71.11 C ATOM 4675 OXT PHE D 196 60.431 18.349 215.473 1.00 67.14 O TER 4676 PHE D 196 ATOM 4677 N ALA E 2 15.397 31.478 185.423 1.00 71.92 N ANISOU 4677 N ALA E 2 13126 5372 8829 657 -14 116 N ATOM 4678 CA ALA E 2 15.934 30.394 186.314 1.00 68.71 C ANISOU 4678 CA ALA E 2 12496 5274 8336 388 -54 -71 C ATOM 4679 C ALA E 2 15.840 28.978 185.701 1.00 63.06 C ANISOU 4679 C ALA E 2 10984 5220 7758 364 -27 18 C ATOM 4680 O ALA E 2 15.685 27.998 186.446 1.00 60.74 O ANISOU 4680 O ALA E 2 10469 5189 7422 397 53 -120 O ATOM 4681 CB ALA E 2 15.252 30.443 187.709 1.00 71.00 C ANISOU 4681 CB ALA E 2 13172 5357 8449 720 158 -336 C ATOM 4682 N GLY E 3 15.920 28.908 184.358 1.00 60.58 N ANISOU 4682 N GLY E 3 10302 5134 7580 302 -95 246 N ATOM 4683 CA GLY E 3 16.027 27.667 183.540 1.00 54.50 C ANISOU 4683 CA GLY E 3 8871 4929 6908 202 -111 335 C ATOM 4684 C GLY E 3 15.207 26.415 183.846 1.00 50.26 C ANISOU 4684 C GLY E 3 7923 4776 6398 432 47 245 C ATOM 4685 O GLY E 3 14.022 26.338 183.550 1.00 50.41 O ANISOU 4685 O GLY E 3 7763 4925 6466 795 197 316 O ATOM 4686 N ILE E 4 15.879 25.423 184.426 1.00 46.64 N ANISOU 4686 N ILE E 4 7302 4514 5905 193 -7 125 N ATOM 4687 CA ILE E 4 15.303 24.127 184.786 1.00 42.38 C ANISOU 4687 CA ILE E 4 6415 4308 5381 311 101 46 C ATOM 4688 C ILE E 4 15.546 23.915 186.270 1.00 42.12 C ANISOU 4688 C ILE E 4 6623 4147 5232 259 123 -138 C ATOM 4689 O ILE E 4 16.589 24.289 186.788 1.00 42.60 O ANISOU 4689 O ILE E 4 6951 4021 5215 -28 -24 -190 O ATOM 4690 CB ILE E 4 16.013 22.996 184.031 1.00 39.18 C ANISOU 4690 CB ILE E 4 5604 4250 5031 67 5 91 C ATOM 4691 CG1 ILE E 4 15.858 23.176 182.538 1.00 38.72 C ANISOU 4691 CG1 ILE E 4 5335 4344 5032 78 -24 262 C ATOM 4692 CG2 ILE E 4 15.464 21.650 184.378 1.00 37.05 C ANISOU 4692 CG2 ILE E 4 5052 4253 4774 144 87 15 C ATOM 4693 CD1 ILE E 4 16.829 22.354 181.734 1.00 37.74 C ANISOU 4693 CD1 ILE E 4 4938 4489 4914 -169 -109 299 C ATOM 4694 N THR E 5 14.576 23.335 186.962 1.00 41.68 N ANISOU 4694 N THR E 5 6472 4221 5145 508 293 -209 N ATOM 4695 CA THR E 5 14.723 23.031 188.363 1.00 41.62 C ANISOU 4695 CA THR E 5 6669 4148 4998 467 330 -367 C ATOM 4696 C THR E 5 14.399 21.570 188.577 1.00 38.54 C ANISOU 4696 C THR E 5 5879 4120 4645 450 375 -363 C ATOM 4697 O THR E 5 13.427 21.065 188.031 1.00 38.23 O ANISOU 4697 O THR E 5 5520 4320 4685 630 480 -272 O ATOM 4698 CB THR E 5 13.768 23.894 189.165 1.00 45.24 C ANISOU 4698 CB THR E 5 7492 4367 5330 832 540 -451 C ATOM 4699 OG1 THR E 5 13.926 25.248 188.739 1.00 48.09 O ANISOU 4699 OG1 THR E 5 8242 4347 5685 894 504 -427 O ATOM 4700 CG2 THR E 5 14.059 23.812 190.672 1.00 47.19 C ANISOU 4700 CG2 THR E 5 8085 4485 5360 752 565 -639 C ATOM 4701 N GLN E 6 15.226 20.876 189.343 1.00 37.21 N ANISOU 4701 N GLN E 6 5728 3995 4414 206 272 -434 N ATOM 4702 CA GLN E 6 14.871 19.533 189.763 1.00 35.93 C ANISOU 4702 CA GLN E 6 5287 4100 4264 203 322 -430 C ATOM 4703 C GLN E 6 14.514 19.531 191.236 1.00 37.95 C ANISOU 4703 C GLN E 6 5782 4301 4335 279 428 -531 C ATOM 4704 O GLN E 6 15.075 20.285 192.037 1.00 40.25 O ANISOU 4704 O GLN E 6 6470 4354 4469 193 376 -635 O ATOM 4705 CB GLN E 6 16.000 18.549 189.481 1.00 33.86 C ANISOU 4705 CB GLN E 6 4821 3968 4077 -71 149 -393 C ATOM 4706 CG GLN E 6 16.617 18.734 188.100 1.00 33.54 C ANISOU 4706 CG GLN E 6 4620 3966 4157 -162 52 -308 C ATOM 4707 CD GLN E 6 17.414 17.543 187.636 1.00 31.99 C ANISOU 4707 CD GLN E 6 4156 3959 4038 -297 -30 -262 C ATOM 4708 OE1 GLN E 6 18.241 17.649 186.736 1.00 31.83 O ANISOU 4708 OE1 GLN E 6 4029 3994 4072 -396 -106 -193 O ATOM 4709 NE2 GLN E 6 17.165 16.396 188.243 1.00 32.03 N ANISOU 4709 NE2 GLN E 6 4068 4062 4041 -282 1 -287 N ATOM 4710 N SER E 7 13.544 18.706 191.587 1.00 37.82 N ANISOU 4710 N SER E 7 5545 4513 4310 416 574 -491 N ATOM 4711 CA SER E 7 13.201 18.509 192.979 1.00 39.70 C ANISOU 4711 CA SER E 7 5955 4775 4353 472 691 -558 C ATOM 4712 C SER E 7 12.881 17.034 193.134 1.00 38.43 C ANISOU 4712 C SER E 7 5451 4902 4249 368 687 -458 C ATOM 4713 O SER E 7 12.214 16.452 192.279 1.00 37.26 O ANISOU 4713 O SER E 7 4970 4945 4244 403 713 -344 O ATOM 4714 CB SER E 7 12.028 19.382 193.396 1.00 42.51 C ANISOU 4714 CB SER E 7 6475 5094 4584 853 964 -585 C ATOM 4715 OG SER E 7 10.985 19.231 192.462 1.00 43.35 O ANISOU 4715 OG SER E 7 6204 5423 4844 1059 1075 -427 O ATOM 4716 N PRO E 8 13.418 16.396 194.187 1.00 38.91 N ANISOU 4716 N PRO E 8 5614 4981 4190 196 620 -485 N ATOM 4717 CA PRO E 8 14.371 16.969 195.129 1.00 40.47 C ANISOU 4717 CA PRO E 8 6191 4984 4202 57 515 -599 C ATOM 4718 C PRO E 8 15.765 16.960 194.514 1.00 40.25 C ANISOU 4718 C PRO E 8 6134 4863 4296 -202 250 -576 C ATOM 4719 O PRO E 8 15.932 16.423 193.423 1.00 37.59 O ANISOU 4719 O PRO E 8 5498 4615 4169 -225 194 -492 O ATOM 4720 CB PRO E 8 14.295 16.018 196.313 1.00 40.50 C ANISOU 4720 CB PRO E 8 6188 5143 4058 -38 530 -560 C ATOM 4721 CG PRO E 8 13.849 14.717 195.736 1.00 38.35 C ANISOU 4721 CG PRO E 8 5509 5084 3978 -69 530 -409 C ATOM 4722 CD PRO E 8 13.044 15.009 194.532 1.00 37.73 C ANISOU 4722 CD PRO E 8 5214 5057 4064 100 627 -374 C ATOM 4723 N ARG E 9 16.740 17.597 195.158 1.00 43.13 N ANISOU 4723 N ARG E 9 6809 5070 4510 -401 93 -637 N ATOM 4724 CA ARG E 9 18.093 17.581 194.613 1.00 43.10 C ANISOU 4724 CA ARG E 9 6703 5059 4613 -663 -157 -555 C ATOM 4725 C ARG E 9 18.816 16.378 195.186 1.00 41.84 C ANISOU 4725 C ARG E 9 6350 5088 4460 -822 -292 -439 C ATOM 4726 O ARG E 9 19.794 15.907 194.611 1.00 40.80 O ANISOU 4726 O ARG E 9 5973 5055 4472 -941 -441 -313 O ATOM 4727 CB ARG E 9 18.848 18.879 194.906 1.00 47.53 C ANISOU 4727 CB ARG E 9 7659 5382 5019 -871 -310 -622 C ATOM 4728 CG ARG E 9 18.034 20.169 194.637 1.00 52.07 C ANISOU 4728 CG ARG E 9 8576 5676 5532 -664 -154 -754 C ATOM 4729 CD ARG E 9 17.648 20.954 195.944 1.00 57.69 C ANISOU 4729 CD ARG E 9 9857 6151 5912 -618 -71 -941 C ATOM 4730 NE ARG E 9 17.212 20.092 197.061 1.00 59.24 N ANISOU 4730 NE ARG E 9 10022 6539 5946 -556 33 -966 N ATOM 4731 CZ ARG E 9 15.967 20.007 197.537 1.00 60.24 C ANISOU 4731 CZ ARG E 9 10196 6722 5969 -213 333 -1035 C ATOM 4732 NH1 ARG E 9 14.983 20.738 197.015 1.00 61.07 N ANISOU 4732 NH1 ARG E 9 10371 6710 6122 147 571 -1083 N ATOM 4733 NH2 ARG E 9 15.711 19.184 198.550 1.00 60.42 N ANISOU 4733 NH2 ARG E 9 10174 6950 5832 -226 397 -1018 N ATOM 4734 N HIS E 10 18.294 15.876 196.308 1.00 41.77 N ANISOU 4734 N HIS E 10 6444 5139 4287 -789 -217 -461 N ATOM 4735 CA HIS E 10 18.887 14.770 197.057 1.00 40.94 C ANISOU 4735 CA HIS E 10 6217 5187 4151 -927 -345 -330 C ATOM 4736 C HIS E 10 17.793 13.976 197.757 1.00 40.47 C ANISOU 4736 C HIS E 10 6136 5229 4010 -796 -165 -321 C ATOM 4737 O HIS E 10 16.897 14.557 198.369 1.00 41.64 O ANISOU 4737 O HIS E 10 6510 5347 3963 -680 14 -432 O ATOM 4738 CB HIS E 10 19.835 15.298 198.141 1.00 43.84 C ANISOU 4738 CB HIS E 10 6866 5525 4266 -1200 -558 -325 C ATOM 4739 CG HIS E 10 21.163 15.769 197.629 1.00 44.40 C ANISOU 4739 CG HIS E 10 6861 5597 4411 -1436 -808 -228 C ATOM 4740 ND1 HIS E 10 21.485 17.106 197.517 1.00 46.11 N ANISOU 4740 ND1 HIS E 10 7380 5627 4513 -1601 -899 -325 N ATOM 4741 CD2 HIS E 10 22.253 15.082 197.214 1.00 43.73 C ANISOU 4741 CD2 HIS E 10 6429 5692 4493 -1533 -980 -16 C ATOM 4742 CE1 HIS E 10 22.715 17.222 197.049 1.00 46.53 C ANISOU 4742 CE1 HIS E 10 7238 5781 4659 -1842 -1133 -155 C ATOM 4743 NE2 HIS E 10 23.205 16.008 196.863 1.00 45.25 N ANISOU 4743 NE2 HIS E 10 6659 5868 4667 -1776 -1171 38 N ATOM 4744 N LYS E 11 17.875 12.651 197.692 1.00 38.36 N ANISOU 4744 N LYS E 11 5618 5080 3878 -807 -202 -173 N ATOM 4745 CA LYS E 11 16.925 11.809 198.405 1.00 38.33 C ANISOU 4745 CA LYS E 11 5588 5186 3792 -760 -69 -110 C ATOM 4746 C LYS E 11 17.617 10.523 198.781 1.00 37.59 C ANISOU 4746 C LYS E 11 5372 5147 3762 -873 -228 78 C ATOM 4747 O LYS E 11 18.263 9.895 197.950 1.00 36.12 O ANISOU 4747 O LYS E 11 5000 4923 3802 -855 -325 155 O ATOM 4748 CB LYS E 11 15.676 11.521 197.551 1.00 37.95 C ANISOU 4748 CB LYS E 11 5341 5186 3891 -599 126 -115 C ATOM 4749 CG LYS E 11 14.630 10.584 198.198 1.00 38.77 C ANISOU 4749 CG LYS E 11 5361 5448 3923 -606 252 6 C ATOM 4750 CD LYS E 11 13.610 11.344 199.012 1.00 41.16 C ANISOU 4750 CD LYS E 11 5794 5870 3975 -477 486 -52 C ATOM 4751 CE LYS E 11 12.832 10.422 199.973 1.00 43.80 C ANISOU 4751 CE LYS E 11 6063 6415 4166 -545 589 114 C ATOM 4752 NZ LYS E 11 11.819 9.517 199.332 1.00 43.10 N ANISOU 4752 NZ LYS E 11 5662 6471 4243 -578 657 275 N ATOM 4753 N VAL E 12 17.508 10.152 200.054 1.00 39.11 N ANISOU 4753 N VAL E 12 5696 5427 3736 -966 -243 159 N ATOM 4754 CA VAL E 12 18.036 8.891 200.535 1.00 38.95 C ANISOU 4754 CA VAL E 12 5587 5451 3761 -1053 -385 377 C ATOM 4755 C VAL E 12 16.856 8.121 201.033 1.00 40.05 C ANISOU 4755 C VAL E 12 5717 5670 3831 -1049 -227 459 C ATOM 4756 O VAL E 12 16.210 8.546 201.981 1.00 41.80 O ANISOU 4756 O VAL E 12 6094 6010 3780 -1072 -103 425 O ATOM 4757 CB VAL E 12 18.991 9.075 201.712 1.00 40.62 C ANISOU 4757 CB VAL E 12 5956 5741 3737 -1226 -584 470 C ATOM 4758 CG1 VAL E 12 19.528 7.724 202.163 1.00 41.31 C ANISOU 4758 CG1 VAL E 12 5928 5872 3897 -1269 -731 744 C ATOM 4759 CG2 VAL E 12 20.123 10.009 201.348 1.00 39.68 C ANISOU 4759 CG2 VAL E 12 5854 5591 3631 -1312 -761 415 C ATOM 4760 N THR E 13 16.557 6.991 200.403 1.00 40.26 N ANISOU 4760 N THR E 13 5584 5635 4080 -1031 -226 574 N ATOM 4761 CA THR E 13 15.354 6.236 200.785 1.00 42.18 C ANISOU 4761 CA THR E 13 5794 5968 4266 -1095 -95 690 C ATOM 4762 C THR E 13 15.559 4.717 200.716 1.00 42.33 C ANISOU 4762 C THR E 13 5784 5858 4442 -1184 -221 903 C ATOM 4763 O THR E 13 16.554 4.263 200.167 1.00 41.93 O ANISOU 4763 O THR E 13 5721 5634 4576 -1115 -365 930 O ATOM 4764 CB THR E 13 14.152 6.681 199.929 1.00 41.59 C ANISOU 4764 CB THR E 13 5582 5960 4260 -1015 101 582 C ATOM 4765 OG1 THR E 13 12.924 6.323 200.590 1.00 44.92 O ANISOU 4765 OG1 THR E 13 5946 6590 4531 -1090 261 716 O ATOM 4766 CG2 THR E 13 14.231 6.072 198.532 1.00 39.26 C ANISOU 4766 CG2 THR E 13 5160 5502 4255 -1003 29 566 C ATOM 4767 N GLU E 14 14.655 3.920 201.276 1.00 43.93 N ANISOU 4767 N GLU E 14 5991 6136 4565 -1324 -161 1074 N ATOM 4768 CA GLU E 14 14.896 2.471 201.227 1.00 45.56 C ANISOU 4768 CA GLU E 14 6254 6141 4918 -1421 -302 1284 C ATOM 4769 C GLU E 14 14.197 1.740 200.111 1.00 44.86 C ANISOU 4769 C GLU E 14 6124 5889 5031 -1489 -287 1275 C ATOM 4770 O GLU E 14 13.333 2.300 199.440 1.00 43.94 O ANISOU 4770 O GLU E 14 5874 5894 4927 -1498 -164 1155 O ATOM 4771 CB GLU E 14 14.625 1.755 202.545 1.00 48.97 C ANISOU 4771 CB GLU E 14 6779 6674 5154 -1597 -330 1548 C ATOM 4772 CG GLU E 14 13.188 1.591 202.918 1.00 51.83 C ANISOU 4772 CG GLU E 14 7064 7257 5371 -1779 -164 1656 C ATOM 4773 CD GLU E 14 13.016 0.564 204.026 1.00 56.09 C ANISOU 4773 CD GLU E 14 7707 7834 5770 -1993 -231 1977 C ATOM 4774 OE1 GLU E 14 13.950 -0.251 204.242 1.00 57.41 O ANISOU 4774 OE1 GLU E 14 8022 7759 6032 -1989 -430 2123 O ATOM 4775 OE2 GLU E 14 11.948 0.568 204.681 1.00 58.46 O ANISOU 4775 OE2 GLU E 14 7927 8423 5860 -2148 -75 2113 O ATOM 4776 N THR E 15 14.604 0.486 199.937 1.00 44.99 N ANISOU 4776 N THR E 15 6286 5618 5189 -1535 -426 1416 N ATOM 4777 CA THR E 15 14.116 -0.384 198.885 1.00 44.63 C ANISOU 4777 CA THR E 15 6322 5323 5313 -1635 -463 1402 C ATOM 4778 C THR E 15 12.621 -0.619 199.023 1.00 45.08 C ANISOU 4778 C THR E 15 6295 5564 5271 -1946 -394 1521 C ATOM 4779 O THR E 15 12.146 -0.897 200.113 1.00 46.91 O ANISOU 4779 O THR E 15 6517 5964 5343 -2116 -371 1740 O ATOM 4780 CB THR E 15 14.845 -1.737 198.941 1.00 47.28 C ANISOU 4780 CB THR E 15 6925 5267 5773 -1609 -617 1560 C ATOM 4781 OG1 THR E 15 16.254 -1.513 199.039 1.00 46.59 O ANISOU 4781 OG1 THR E 15 6833 5116 5752 -1302 -672 1537 O ATOM 4782 CG2 THR E 15 14.563 -2.576 197.701 1.00 48.60 C ANISOU 4782 CG2 THR E 15 7286 5082 6097 -1668 -663 1469 C ATOM 4783 N GLY E 16 11.887 -0.445 197.927 1.00 43.57 N ANISOU 4783 N GLY E 16 6006 5396 5152 -2024 -359 1401 N ATOM 4784 CA GLY E 16 10.461 -0.736 197.892 1.00 44.87 C ANISOU 4784 CA GLY E 16 6033 5773 5241 -2354 -326 1560 C ATOM 4785 C GLY E 16 9.605 0.511 197.909 1.00 43.70 C ANISOU 4785 C GLY E 16 5543 6080 4979 -2274 -128 1510 C ATOM 4786 O GLY E 16 8.431 0.476 197.545 1.00 45.25 O ANISOU 4786 O GLY E 16 5530 6518 5145 -2486 -90 1625 O ATOM 4787 N THR E 17 10.208 1.611 198.341 1.00 41.92 N ANISOU 4787 N THR E 17 5275 5968 4685 -1968 -12 1357 N ATOM 4788 CA THR E 17 9.543 2.905 198.460 1.00 41.56 C ANISOU 4788 CA THR E 17 4994 6281 4517 -1797 203 1282 C ATOM 4789 C THR E 17 9.295 3.510 197.091 1.00 39.11 C ANISOU 4789 C THR E 17 4548 5967 4346 -1699 211 1117 C ATOM 4790 O THR E 17 10.162 3.447 196.229 1.00 36.66 O ANISOU 4790 O THR E 17 4370 5371 4187 -1616 91 947 O ATOM 4791 CB THR E 17 10.439 3.898 199.250 1.00 41.13 C ANISOU 4791 CB THR E 17 5058 6233 4336 -1529 276 1128 C ATOM 4792 OG1 THR E 17 11.203 3.177 200.236 1.00 42.25 O ANISOU 4792 OG1 THR E 17 5398 6249 4406 -1615 160 1248 O ATOM 4793 CG2 THR E 17 9.606 5.015 199.911 1.00 42.25 C ANISOU 4793 CG2 THR E 17 5069 6732 4251 -1370 539 1113 C ATOM 4794 N PRO E 18 8.097 4.073 196.878 1.00 40.15 N ANISOU 4794 N PRO E 18 4392 6447 4415 -1696 359 1199 N ATOM 4795 CA PRO E 18 7.891 4.849 195.670 1.00 38.69 C ANISOU 4795 CA PRO E 18 4068 6297 4337 -1554 377 1059 C ATOM 4796 C PRO E 18 8.676 6.153 195.750 1.00 37.03 C ANISOU 4796 C PRO E 18 3955 6009 4107 -1193 479 824 C ATOM 4797 O PRO E 18 8.751 6.750 196.825 1.00 37.89 O ANISOU 4797 O PRO E 18 4129 6218 4051 -1039 625 811 O ATOM 4798 CB PRO E 18 6.391 5.128 195.675 1.00 40.90 C ANISOU 4798 CB PRO E 18 3978 7033 4531 -1608 526 1281 C ATOM 4799 CG PRO E 18 5.801 4.064 196.547 1.00 44.12 C ANISOU 4799 CG PRO E 18 4338 7590 4836 -1930 506 1562 C ATOM 4800 CD PRO E 18 6.837 3.822 197.597 1.00 43.54 C ANISOU 4800 CD PRO E 18 4578 7272 4691 -1863 491 1482 C ATOM 4801 N VAL E 19 9.321 6.536 194.646 1.00 34.64 N ANISOU 4801 N VAL E 19 3709 5507 3947 -1095 389 644 N ATOM 4802 CA VAL E 19 10.031 7.812 194.552 1.00 33.95 C ANISOU 4802 CA VAL E 19 3711 5335 3852 -815 455 448 C ATOM 4803 C VAL E 19 9.610 8.566 193.285 1.00 33.18 C ANISOU 4803 C VAL E 19 3457 5299 3848 -702 478 391 C ATOM 4804 O VAL E 19 9.621 7.996 192.206 1.00 32.53 O ANISOU 4804 O VAL E 19 3332 5148 3881 -841 346 387 O ATOM 4805 CB VAL E 19 11.594 7.640 194.490 1.00 32.37 C ANISOU 4805 CB VAL E 19 3743 4827 3728 -799 300 310 C ATOM 4806 CG1 VAL E 19 12.301 8.967 194.724 1.00 31.69 C ANISOU 4806 CG1 VAL E 19 3771 4687 3581 -601 348 159 C ATOM 4807 CG2 VAL E 19 12.099 6.646 195.486 1.00 33.28 C ANISOU 4807 CG2 VAL E 19 3996 4854 3794 -931 215 410 C ATOM 4808 N THR E 20 9.254 9.843 193.410 1.00 33.75 N ANISOU 4808 N THR E 20 3488 5481 3855 -443 643 347 N ATOM 4809 CA THR E 20 9.039 10.683 192.241 1.00 32.84 C ANISOU 4809 CA THR E 20 3266 5381 3830 -301 651 302 C ATOM 4810 C THR E 20 10.095 11.759 192.149 1.00 32.17 C ANISOU 4810 C THR E 20 3418 5051 3754 -127 642 111 C ATOM 4811 O THR E 20 10.354 12.452 193.119 1.00 32.27 O ANISOU 4811 O THR E 20 3624 4996 3639 7 740 37 O ATOM 4812 CB THR E 20 7.696 11.391 192.275 1.00 34.71 C ANISOU 4812 CB THR E 20 3252 5931 4004 -100 850 452 C ATOM 4813 OG1 THR E 20 6.670 10.447 192.576 1.00 36.67 O ANISOU 4813 OG1 THR E 20 3242 6481 4211 -296 869 683 O ATOM 4814 CG2 THR E 20 7.397 12.039 190.928 1.00 34.28 C ANISOU 4814 CG2 THR E 20 3046 5920 4060 0 809 470 C ATOM 4815 N LEU E 21 10.709 11.904 190.985 1.00 31.88 N ANISOU 4815 N LEU E 21 3387 4887 3841 -157 517 39 N ATOM 4816 CA LEU E 21 11.536 13.067 190.752 1.00 33.22 C ANISOU 4816 CA LEU E 21 3732 4872 4018 -21 508 -86 C ATOM 4817 C LEU E 21 10.794 14.017 189.826 1.00 35.64 C ANISOU 4817 C LEU E 21 3916 5258 4365 156 581 -37 C ATOM 4818 O LEU E 21 10.221 13.604 188.814 1.00 36.48 O ANISOU 4818 O LEU E 21 3803 5514 4544 87 528 56 O ATOM 4819 CB LEU E 21 12.878 12.679 190.153 1.00 31.68 C ANISOU 4819 CB LEU E 21 3616 4509 3913 -157 337 -164 C ATOM 4820 CG LEU E 21 13.628 11.573 190.887 1.00 31.31 C ANISOU 4820 CG LEU E 21 3642 4396 3858 -301 248 -160 C ATOM 4821 CD1 LEU E 21 14.964 11.343 190.211 1.00 30.00 C ANISOU 4821 CD1 LEU E 21 3508 4110 3782 -347 121 -206 C ATOM 4822 CD2 LEU E 21 13.803 11.930 192.342 1.00 32.38 C ANISOU 4822 CD2 LEU E 21 3945 4509 3849 -282 293 -173 C ATOM 4823 N ARG E 22 10.816 15.294 190.177 1.00 38.23 N ANISOU 4823 N ARG E 22 4425 5469 4631 376 687 -93 N ATOM 4824 CA ARG E 22 10.035 16.302 189.492 1.00 41.21 C ANISOU 4824 CA ARG E 22 4722 5898 5038 620 786 -16 C ATOM 4825 C ARG E 22 10.979 17.255 188.768 1.00 40.61 C ANISOU 4825 C ARG E 22 4850 5563 5015 623 684 -98 C ATOM 4826 O ARG E 22 11.999 17.662 189.321 1.00 40.94 O ANISOU 4826 O ARG E 22 5184 5368 5004 544 624 -225 O ATOM 4827 CB ARG E 22 9.186 17.038 190.530 1.00 45.31 C ANISOU 4827 CB ARG E 22 5339 6457 5422 933 1032 3 C ATOM 4828 CG ARG E 22 8.352 18.209 190.031 1.00 49.63 C ANISOU 4828 CG ARG E 22 5851 7021 5986 1299 1185 101 C ATOM 4829 CD ARG E 22 7.331 18.626 191.111 1.00 54.12 C ANISOU 4829 CD ARG E 22 6441 7721 6400 1661 1488 153 C ATOM 4830 NE ARG E 22 6.810 17.458 191.833 1.00 55.28 N ANISOU 4830 NE ARG E 22 6334 8190 6478 1508 1540 247 N ATOM 4831 CZ ARG E 22 5.716 17.449 192.604 1.00 58.90 C ANISOU 4831 CZ ARG E 22 6621 8948 6813 1760 1805 387 C ATOM 4832 NH1 ARG E 22 4.987 18.550 192.775 1.00 62.19 N ANISOU 4832 NH1 ARG E 22 7093 9380 7157 2250 2075 438 N ATOM 4833 NH2 ARG E 22 5.346 16.325 193.208 1.00 58.89 N ANISOU 4833 NH2 ARG E 22 6391 9233 6750 1537 1813 498 N ATOM 4834 N CYS E 23 10.655 17.588 187.523 1.00 40.52 N ANISOU 4834 N CYS E 23 4676 5625 5095 670 643 2 N ATOM 4835 CA CYS E 23 11.463 18.521 186.744 1.00 39.19 C ANISOU 4835 CA CYS E 23 4676 5243 4971 658 551 -27 C ATOM 4836 C CYS E 23 10.587 19.607 186.195 1.00 40.23 C ANISOU 4836 C CYS E 23 4785 5375 5124 948 648 103 C ATOM 4837 O CYS E 23 9.565 19.336 185.559 1.00 40.24 O ANISOU 4837 O CYS E 23 4470 5654 5164 1037 678 270 O ATOM 4838 CB CYS E 23 12.131 17.821 185.566 1.00 38.60 C ANISOU 4838 CB CYS E 23 4440 5256 4968 416 386 -12 C ATOM 4839 SG CYS E 23 12.955 18.934 184.375 1.00 40.06 S ANISOU 4839 SG CYS E 23 4737 5289 5193 384 286 31 S ATOM 4840 N HIS E 24 11.012 20.841 186.402 1.00 40.41 N ANISOU 4840 N HIS E 24 5156 5080 5118 1075 674 49 N ATOM 4841 CA HIS E 24 10.185 21.964 186.039 1.00 42.65 C ANISOU 4841 CA HIS E 24 5498 5288 5418 1424 792 178 C ATOM 4842 C HIS E 24 10.950 22.960 185.163 1.00 43.98 C ANISOU 4842 C HIS E 24 5892 5184 5635 1350 660 211 C ATOM 4843 O HIS E 24 12.095 23.291 185.446 1.00 43.56 O ANISOU 4843 O HIS E 24 6146 4861 5544 1119 548 86 O ATOM 4844 CB HIS E 24 9.629 22.630 187.304 1.00 43.69 C ANISOU 4844 CB HIS E 24 5925 5245 5431 1764 1022 99 C ATOM 4845 CG HIS E 24 8.812 23.854 187.037 1.00 46.10 C ANISOU 4845 CG HIS E 24 6360 5408 5748 2216 1183 227 C ATOM 4846 ND1 HIS E 24 7.491 23.799 186.650 1.00 47.74 N ANISOU 4846 ND1 HIS E 24 6170 5960 6009 2552 1333 469 N ATOM 4847 CD2 HIS E 24 9.130 25.168 187.103 1.00 48.24 C ANISOU 4847 CD2 HIS E 24 7127 5219 5982 2395 1212 171 C ATOM 4848 CE1 HIS E 24 7.030 25.026 186.491 1.00 51.10 C ANISOU 4848 CE1 HIS E 24 6820 6153 6442 2978 1469 564 C ATOM 4849 NE2 HIS E 24 8.004 25.875 186.761 1.00 51.42 N ANISOU 4849 NE2 HIS E 24 7442 5667 6426 2891 1400 371 N ATOM 4850 N GLN E 25 10.297 23.425 184.099 1.00 46.12 N ANISOU 4850 N GLN E 25 5984 5560 5978 1519 660 418 N ATOM 4851 CA GLN E 25 10.817 24.479 183.247 1.00 48.13 C ANISOU 4851 CA GLN E 25 6453 5564 6271 1496 556 508 C ATOM 4852 C GLN E 25 9.768 25.567 182.969 1.00 52.88 C ANISOU 4852 C GLN E 25 7121 6065 6906 1953 690 706 C ATOM 4853 O GLN E 25 8.577 25.288 182.940 1.00 54.00 O ANISOU 4853 O GLN E 25 6932 6515 7069 2240 819 856 O ATOM 4854 CB GLN E 25 11.325 23.868 181.953 1.00 45.97 C ANISOU 4854 CB GLN E 25 5884 5544 6039 1182 375 599 C ATOM 4855 CG GLN E 25 10.793 24.517 180.683 1.00 48.00 C ANISOU 4855 CG GLN E 25 6009 5891 6339 1310 328 857 C ATOM 4856 CD GLN E 25 9.872 23.622 179.966 1.00 47.40 C ANISOU 4856 CD GLN E 25 5467 6279 6264 1312 305 996 C ATOM 4857 OE1 GLN E 25 9.980 22.413 180.094 1.00 45.76 O ANISOU 4857 OE1 GLN E 25 5066 6296 6025 1090 270 881 O ATOM 4858 NE2 GLN E 25 8.967 24.184 179.195 1.00 49.75 N ANISOU 4858 NE2 GLN E 25 5596 6720 6588 1539 306 1263 N ATOM 4859 N THR E 26 10.213 26.808 182.796 1.00 56.87 N ANISOU 4859 N THR E 26 8056 6140 7414 2021 656 732 N ATOM 4860 CA THR E 26 9.305 27.920 182.555 1.00 62.91 C ANISOU 4860 CA THR E 26 8964 6724 8217 2505 788 928 C ATOM 4861 C THR E 26 8.955 28.081 181.091 1.00 64.68 C ANISOU 4861 C THR E 26 8859 7186 8529 2514 668 1239 C ATOM 4862 O THR E 26 7.781 28.212 180.741 1.00 66.98 O ANISOU 4862 O THR E 26 8856 7725 8868 2897 774 1484 O ATOM 4863 CB THR E 26 9.966 29.234 182.942 1.00 65.58 C ANISOU 4863 CB THR E 26 9998 6411 8506 2543 774 835 C ATOM 4864 OG1 THR E 26 10.932 28.986 183.968 1.00 63.52 O ANISOU 4864 OG1 THR E 26 10062 5938 8134 2214 719 538 O ATOM 4865 CG2 THR E 26 8.915 30.266 183.399 1.00 71.12 C ANISOU 4865 CG2 THR E 26 11008 6820 9195 3197 1032 913 C ATOM 4866 N GLU E 27 10.000 28.018 180.264 1.00 64.41 N ANISOU 4866 N GLU E 27 8846 7129 8496 2074 448 1247 N ATOM 4867 CA GLU E 27 10.088 28.674 178.951 1.00 67.19 C ANISOU 4867 CA GLU E 27 9164 7476 8887 2029 310 1519 C ATOM 4868 C GLU E 27 8.869 28.590 178.038 1.00 69.13 C ANISOU 4868 C GLU E 27 8967 8125 9175 2309 325 1837 C ATOM 4869 O GLU E 27 8.491 29.614 177.457 1.00 73.38 O ANISOU 4869 O GLU E 27 9632 8492 9759 2571 317 2100 O ATOM 4870 CB GLU E 27 11.338 28.204 178.216 1.00 65.73 C ANISOU 4870 CB GLU E 27 8906 7408 8660 1485 107 1472 C ATOM 4871 CG GLU E 27 12.289 27.381 179.097 1.00 64.74 C ANISOU 4871 CG GLU E 27 8835 7275 8487 1164 91 1168 C ATOM 4872 CD GLU E 27 13.559 28.102 179.549 1.00 66.51 C ANISOU 4872 CD GLU E 27 9513 7081 8678 876 -9 1071 C ATOM 4873 OE1 GLU E 27 13.785 29.262 179.135 1.00 69.74 O ANISOU 4873 OE1 GLU E 27 10242 7159 9096 870 -79 1227 O ATOM 4874 OE2 GLU E 27 14.341 27.486 180.322 1.00 65.40 O ANISOU 4874 OE2 GLU E 27 9403 6953 8494 625 -37 862 O ATOM 4875 N ASN E 28 8.314 27.370 177.929 1.00 66.43 N ANISOU 4875 N ASN E 28 8133 8299 8809 2214 322 1828 N ATOM 4876 CA ASN E 28 6.953 26.992 177.426 1.00 68.09 C ANISOU 4876 CA ASN E 28 7833 9004 9033 2446 344 2109 C ATOM 4877 C ASN E 28 6.980 25.616 176.766 1.00 65.11 C ANISOU 4877 C ASN E 28 7046 9117 8575 2015 183 2073 C ATOM 4878 O ASN E 28 7.343 24.619 177.392 1.00 63.09 O ANISOU 4878 O ASN E 28 6763 8923 8285 1778 200 1814 O ATOM 4879 CB ASN E 28 6.270 27.991 176.456 1.00 71.86 C ANISOU 4879 CB ASN E 28 8232 9517 9555 2753 301 2510 C ATOM 4880 CG ASN E 28 4.727 27.955 176.539 1.00 75.18 C ANISOU 4880 CG ASN E 28 8206 10342 10017 3202 421 2818 C ATOM 4881 OD1 ASN E 28 4.095 26.912 176.331 1.00 73.87 O ANISOU 4881 OD1 ASN E 28 7549 10714 9804 3025 354 2895 O ATOM 4882 ND2 ASN E 28 4.127 29.106 176.822 1.00 79.56 N ANISOU 4882 ND2 ASN E 28 8939 10637 10652 3782 594 3020 N ATOM 4883 N HIS E 29 6.609 25.592 175.486 1.00 65.28 N ANISOU 4883 N HIS E 29 6799 9457 8547 1913 20 2340 N ATOM 4884 CA HIS E 29 6.326 24.375 174.748 1.00 62.50 C ANISOU 4884 CA HIS E 29 6077 9591 8078 1554 -141 2359 C ATOM 4885 C HIS E 29 7.632 23.796 174.252 1.00 57.95 C ANISOU 4885 C HIS E 29 5695 8923 7401 1113 -249 2103 C ATOM 4886 O HIS E 29 8.309 24.426 173.422 1.00 58.19 O ANISOU 4886 O HIS E 29 5886 8837 7387 1019 -329 2183 O ATOM 4887 CB HIS E 29 5.482 24.739 173.541 1.00 66.71 C ANISOU 4887 CB HIS E 29 6310 10479 8558 1617 -289 2762 C ATOM 4888 CG HIS E 29 4.244 23.923 173.386 1.00 68.98 C ANISOU 4888 CG HIS E 29 6103 11314 8790 1567 -366 2964 C ATOM 4889 ND1 HIS E 29 3.049 24.469 172.967 1.00 73.42 N ANISOU 4889 ND1 HIS E 29 6306 12211 9381 1864 -401 3409 N ATOM 4890 CD2 HIS E 29 4.010 22.606 173.586 1.00 67.71 C ANISOU 4890 CD2 HIS E 29 5746 11438 8544 1231 -434 2817 C ATOM 4891 CE1 HIS E 29 2.131 23.522 172.913 1.00 74.62 C ANISOU 4891 CE1 HIS E 29 6020 12874 9458 1674 -501 3542 C ATOM 4892 NE2 HIS E 29 2.688 22.382 173.285 1.00 71.41 N ANISOU 4892 NE2 HIS E 29 5735 12418 8979 1272 -527 3177 N ATOM 4893 N ARG E 30 7.970 22.601 174.748 1.00 52.96 N ANISOU 4893 N ARG E 30 5039 8358 6726 865 -240 1826 N ATOM 4894 CA ARG E 30 9.218 21.935 174.388 1.00 47.68 C ANISOU 4894 CA ARG E 30 4535 7617 5964 519 -297 1578 C ATOM 4895 C ARG E 30 9.349 20.444 174.718 1.00 43.83 C ANISOU 4895 C ARG E 30 3983 7261 5410 269 -310 1331 C ATOM 4896 O ARG E 30 8.512 19.843 175.366 1.00 43.49 O ANISOU 4896 O ARG E 30 3778 7350 5397 302 -284 1330 O ATOM 4897 CB ARG E 30 10.417 22.697 174.954 1.00 46.83 C ANISOU 4897 CB ARG E 30 4768 7091 5934 553 -217 1444 C ATOM 4898 CG ARG E 30 10.558 22.702 176.429 1.00 45.28 C ANISOU 4898 CG ARG E 30 4734 6629 5841 686 -85 1256 C ATOM 4899 CD ARG E 30 11.569 23.752 176.757 1.00 44.97 C ANISOU 4899 CD ARG E 30 5046 6193 5849 691 -68 1219 C ATOM 4900 NE ARG E 30 11.499 24.868 175.831 1.00 47.32 N ANISOU 4900 NE ARG E 30 5420 6414 6144 766 -132 1474 N ATOM 4901 CZ ARG E 30 12.439 25.800 175.701 1.00 47.76 C ANISOU 4901 CZ ARG E 30 5769 6168 6209 661 -176 1515 C ATOM 4902 NH1 ARG E 30 13.553 25.756 176.433 1.00 46.24 N ANISOU 4902 NH1 ARG E 30 5790 5757 6021 458 -176 1324 N ATOM 4903 NH2 ARG E 30 12.264 26.775 174.821 1.00 49.01 N ANISOU 4903 NH2 ARG E 30 5995 6263 6364 729 -243 1785 N ATOM 4904 N TYR E 31 10.439 19.862 174.248 1.00 41.22 N ANISOU 4904 N TYR E 31 3790 6890 4980 29 -341 1143 N ATOM 4905 CA TYR E 31 10.698 18.457 174.444 1.00 38.92 C ANISOU 4905 CA TYR E 31 3516 6656 4616 -180 -350 907 C ATOM 4906 C TYR E 31 11.423 18.284 175.763 1.00 36.39 C ANISOU 4906 C TYR E 31 3345 6059 4425 -109 -229 708 C ATOM 4907 O TYR E 31 12.335 19.066 176.078 1.00 35.31 O ANISOU 4907 O TYR E 31 3362 5700 4354 -39 -173 685 O ATOM 4908 CB TYR E 31 11.565 17.899 173.314 1.00 38.31 C ANISOU 4908 CB TYR E 31 3542 6664 4352 -395 -399 799 C ATOM 4909 CG TYR E 31 10.932 17.942 171.946 1.00 40.69 C ANISOU 4909 CG TYR E 31 3742 7260 4457 -527 -540 969 C ATOM 4910 CD1 TYR E 31 9.552 17.962 171.794 1.00 42.20 C ANISOU 4910 CD1 TYR E 31 3710 7690 4634 -538 -660 1179 C ATOM 4911 CD2 TYR E 31 11.718 17.947 170.798 1.00 41.58 C ANISOU 4911 CD2 TYR E 31 3963 7462 4374 -651 -555 946 C ATOM 4912 CE1 TYR E 31 8.974 18.004 170.560 1.00 44.69 C ANISOU 4912 CE1 TYR E 31 3922 8308 4749 -692 -825 1365 C ATOM 4913 CE2 TYR E 31 11.138 17.983 169.546 1.00 43.96 C ANISOU 4913 CE2 TYR E 31 4200 8051 4453 -796 -699 1103 C ATOM 4914 CZ TYR E 31 9.763 18.005 169.437 1.00 45.43 C ANISOU 4914 CZ TYR E 31 4174 8458 4631 -832 -852 1312 C ATOM 4915 OH TYR E 31 9.169 18.026 168.199 1.00 48.05 O ANISOU 4915 OH TYR E 31 4427 9112 4718 -1013 -1033 1498 O ATOM 4916 N MET E 32 11.015 17.272 176.533 1.00 34.47 N ANISOU 4916 N MET E 32 3060 5838 4200 -164 -211 592 N ATOM 4917 CA MET E 32 11.627 16.990 177.833 1.00 33.10 C ANISOU 4917 CA MET E 32 3015 5437 4123 -114 -115 423 C ATOM 4918 C MET E 32 12.111 15.537 177.974 1.00 31.95 C ANISOU 4918 C MET E 32 2939 5276 3923 -296 -132 227 C ATOM 4919 O MET E 32 11.510 14.624 177.420 1.00 32.89 O ANISOU 4919 O MET E 32 3009 5545 3944 -460 -214 217 O ATOM 4920 CB MET E 32 10.672 17.344 178.972 1.00 34.28 C ANISOU 4920 CB MET E 32 3091 5572 4364 72 -32 500 C ATOM 4921 CG MET E 32 10.124 18.745 178.920 1.00 36.82 C ANISOU 4921 CG MET E 32 3394 5858 4739 335 21 689 C ATOM 4922 SD MET E 32 9.307 19.207 180.435 1.00 39.40 S ANISOU 4922 SD MET E 32 3732 6102 5138 639 198 717 S ATOM 4923 CE MET E 32 10.719 19.351 181.505 1.00 37.02 C ANISOU 4923 CE MET E 32 3793 5420 4852 581 243 461 C ATOM 4924 N TYR E 33 13.206 15.335 178.706 1.00 29.89 N ANISOU 4924 N TYR E 33 2816 4823 3717 -274 -70 90 N ATOM 4925 CA TYR E 33 13.908 14.061 178.728 1.00 29.48 C ANISOU 4925 CA TYR E 33 2861 4717 3622 -375 -68 -74 C ATOM 4926 C TYR E 33 14.403 13.776 180.133 1.00 28.79 C ANISOU 4926 C TYR E 33 2842 4463 3634 -322 -16 -146 C ATOM 4927 O TYR E 33 14.939 14.668 180.775 1.00 30.16 O ANISOU 4927 O TYR E 33 3048 4539 3872 -242 16 -116 O ATOM 4928 CB TYR E 33 15.156 14.119 177.825 1.00 30.05 C ANISOU 4928 CB TYR E 33 2994 4799 3623 -376 -40 -119 C ATOM 4929 CG TYR E 33 14.942 14.574 176.396 1.00 31.06 C ANISOU 4929 CG TYR E 33 3082 5101 3618 -427 -81 -36 C ATOM 4930 CD1 TYR E 33 14.794 13.655 175.364 1.00 32.02 C ANISOU 4930 CD1 TYR E 33 3279 5328 3559 -536 -111 -125 C ATOM 4931 CD2 TYR E 33 14.934 15.925 176.073 1.00 31.74 C ANISOU 4931 CD2 TYR E 33 3104 5222 3736 -377 -94 132 C ATOM 4932 CE1 TYR E 33 14.591 14.072 174.056 1.00 33.46 C ANISOU 4932 CE1 TYR E 33 3440 5698 3577 -604 -160 -41 C ATOM 4933 CE2 TYR E 33 14.723 16.343 174.786 1.00 33.07 C ANISOU 4933 CE2 TYR E 33 3231 5562 3771 -430 -142 242 C ATOM 4934 CZ TYR E 33 14.555 15.422 173.786 1.00 33.98 C ANISOU 4934 CZ TYR E 33 3389 5830 3691 -548 -176 159 C ATOM 4935 OH TYR E 33 14.379 15.889 172.515 1.00 36.59 O ANISOU 4935 OH TYR E 33 3692 6357 3855 -617 -232 281 O ATOM 4936 N TRP E 34 14.256 12.541 180.609 1.00 28.36 N ANISOU 4936 N TRP E 34 2843 4359 3573 -394 -26 -231 N ATOM 4937 CA TRP E 34 14.883 12.114 181.866 1.00 26.54 C ANISOU 4937 CA TRP E 34 2687 3982 3414 -355 8 -283 C ATOM 4938 C TRP E 34 16.003 11.128 181.581 1.00 26.62 C ANISOU 4938 C TRP E 34 2801 3907 3406 -341 22 -380 C ATOM 4939 O TRP E 34 15.773 10.074 180.991 1.00 28.06 O ANISOU 4939 O TRP E 34 3085 4057 3518 -404 3 -457 O ATOM 4940 CB TRP E 34 13.862 11.469 182.828 1.00 27.47 C ANISOU 4940 CB TRP E 34 2792 4101 3546 -422 0 -258 C ATOM 4941 CG TRP E 34 13.223 12.429 183.803 1.00 27.30 C ANISOU 4941 CG TRP E 34 2701 4117 3555 -325 60 -173 C ATOM 4942 CD1 TRP E 34 11.924 12.857 183.816 1.00 28.51 C ANISOU 4942 CD1 TRP E 34 2707 4432 3693 -291 91 -55 C ATOM 4943 CD2 TRP E 34 13.867 13.086 184.897 1.00 26.63 C ANISOU 4943 CD2 TRP E 34 2711 3912 3494 -231 108 -196 C ATOM 4944 NE1 TRP E 34 11.724 13.743 184.848 1.00 28.13 N ANISOU 4944 NE1 TRP E 34 2686 4346 3655 -124 194 -25 N ATOM 4945 CE2 TRP E 34 12.909 13.903 185.518 1.00 27.55 C ANISOU 4945 CE2 TRP E 34 2797 4080 3592 -114 191 -129 C ATOM 4946 CE3 TRP E 34 15.170 13.077 185.401 1.00 25.49 C ANISOU 4946 CE3 TRP E 34 2676 3643 3368 -238 81 -249 C ATOM 4947 CZ2 TRP E 34 13.217 14.684 186.618 1.00 28.09 C ANISOU 4947 CZ2 TRP E 34 3019 4023 3629 -17 251 -163 C ATOM 4948 CZ3 TRP E 34 15.465 13.852 186.481 1.00 25.33 C ANISOU 4948 CZ3 TRP E 34 2765 3536 3324 -201 98 -252 C ATOM 4949 CH2 TRP E 34 14.503 14.641 187.081 1.00 26.74 C ANISOU 4949 CH2 TRP E 34 2990 3713 3456 -98 183 -233 C ATOM 4950 N TYR E 35 17.215 11.480 181.995 1.00 26.61 N ANISOU 4950 N TYR E 35 2785 3871 3454 -255 53 -361 N ATOM 4951 CA TYR E 35 18.405 10.649 181.818 1.00 27.04 C ANISOU 4951 CA TYR E 35 2876 3892 3507 -162 97 -398 C ATOM 4952 C TYR E 35 18.968 10.213 183.154 1.00 28.17 C ANISOU 4952 C TYR E 35 3032 3943 3729 -124 78 -361 C ATOM 4953 O TYR E 35 18.732 10.853 184.170 1.00 28.14 O ANISOU 4953 O TYR E 35 3010 3923 3758 -185 33 -310 O ATOM 4954 CB TYR E 35 19.524 11.462 181.211 1.00 26.32 C ANISOU 4954 CB TYR E 35 2665 3933 3403 -107 135 -321 C ATOM 4955 CG TYR E 35 19.389 11.868 179.781 1.00 26.40 C ANISOU 4955 CG TYR E 35 2652 4072 3309 -119 169 -325 C ATOM 4956 CD1 TYR E 35 18.878 13.114 179.447 1.00 25.47 C ANISOU 4956 CD1 TYR E 35 2477 4017 3185 -206 121 -240 C ATOM 4957 CD2 TYR E 35 19.849 11.039 178.753 1.00 27.32 C ANISOU 4957 CD2 TYR E 35 2829 4240 3310 -21 262 -405 C ATOM 4958 CE1 TYR E 35 18.777 13.503 178.120 1.00 26.16 C ANISOU 4958 CE1 TYR E 35 2537 4243 3161 -228 139 -209 C ATOM 4959 CE2 TYR E 35 19.761 11.427 177.424 1.00 27.13 C ANISOU 4959 CE2 TYR E 35 2799 4365 3145 -46 297 -404 C ATOM 4960 CZ TYR E 35 19.224 12.658 177.114 1.00 26.64 C ANISOU 4960 CZ TYR E 35 2645 4391 3084 -167 223 -291 C ATOM 4961 OH TYR E 35 19.128 13.072 175.801 1.00 27.63 O ANISOU 4961 OH TYR E 35 2760 4681 3057 -206 240 -255 O ATOM 4962 N ARG E 36 19.772 9.158 183.149 1.00 30.68 N ANISOU 4962 N ARG E 36 3399 4201 4059 1 120 -376 N ATOM 4963 CA ARG E 36 20.593 8.863 184.315 1.00 31.81 C ANISOU 4963 CA ARG E 36 3500 4313 4273 61 89 -280 C ATOM 4964 C ARG E 36 22.085 8.748 183.972 1.00 34.80 C ANISOU 4964 C ARG E 36 3731 4821 4671 241 150 -179 C ATOM 4965 O ARG E 36 22.474 8.361 182.865 1.00 35.77 O ANISOU 4965 O ARG E 36 3861 4989 4742 393 264 -226 O ATOM 4966 CB ARG E 36 20.090 7.631 185.071 1.00 31.67 C ANISOU 4966 CB ARG E 36 3650 4104 4278 61 65 -309 C ATOM 4967 CG ARG E 36 20.279 6.304 184.376 1.00 33.15 C ANISOU 4967 CG ARG E 36 4023 4128 4445 208 133 -392 C ATOM 4968 CD ARG E 36 19.666 5.165 185.196 1.00 34.21 C ANISOU 4968 CD ARG E 36 4367 4029 4602 140 75 -392 C ATOM 4969 NE ARG E 36 20.653 4.438 185.985 1.00 35.67 N ANISOU 4969 NE ARG E 36 4568 4125 4861 331 79 -275 N ATOM 4970 CZ ARG E 36 20.352 3.502 186.881 1.00 37.45 C ANISOU 4970 CZ ARG E 36 4959 4153 5118 290 18 -215 C ATOM 4971 NH1 ARG E 36 19.087 3.184 187.117 1.00 37.53 N ANISOU 4971 NH1 ARG E 36 5115 4057 5088 34 -48 -258 N ATOM 4972 NH2 ARG E 36 21.312 2.880 187.555 1.00 39.24 N ANISOU 4972 NH2 ARG E 36 5181 4316 5413 497 16 -71 N ATOM 4973 N GLN E 37 22.919 9.103 184.944 1.00 36.70 N ANISOU 4973 N GLN E 37 3830 5155 4961 216 73 -21 N ATOM 4974 CA GLN E 37 24.359 9.089 184.758 1.00 39.19 C ANISOU 4974 CA GLN E 37 3912 5679 5299 359 108 153 C ATOM 4975 C GLN E 37 25.022 8.044 185.657 1.00 41.30 C ANISOU 4975 C GLN E 37 4150 5911 5630 530 89 277 C ATOM 4976 O GLN E 37 24.789 8.011 186.861 1.00 40.64 O ANISOU 4976 O GLN E 37 4122 5754 5564 400 -39 326 O ATOM 4977 CB GLN E 37 24.935 10.474 185.012 1.00 38.60 C ANISOU 4977 CB GLN E 37 3653 5802 5210 135 -6 303 C ATOM 4978 CG GLN E 37 26.219 10.721 184.281 1.00 41.16 C ANISOU 4978 CG GLN E 37 3685 6427 5528 221 55 494 C ATOM 4979 CD GLN E 37 26.742 12.111 184.514 1.00 42.15 C ANISOU 4979 CD GLN E 37 3669 6720 5627 -89 -97 660 C ATOM 4980 OE1 GLN E 37 27.076 12.487 185.641 1.00 42.72 O ANISOU 4980 OE1 GLN E 37 3725 6806 5701 -288 -276 772 O ATOM 4981 NE2 GLN E 37 26.821 12.894 183.445 1.00 42.92 N ANISOU 4981 NE2 GLN E 37 3699 6932 5677 -163 -44 683 N ATOM 4982 N ASP E 38 25.830 7.177 185.052 1.00 44.44 N ANISOU 4982 N ASP E 38 4478 6360 6045 851 233 334 N ATOM 4983 CA ASP E 38 26.474 6.068 185.758 1.00 47.58 C ANISOU 4983 CA ASP E 38 4864 6698 6515 1104 244 474 C ATOM 4984 C ASP E 38 27.925 5.970 185.308 1.00 50.90 C ANISOU 4984 C ASP E 38 4948 7436 6958 1405 362 709 C ATOM 4985 O ASP E 38 28.193 5.990 184.103 1.00 52.20 O ANISOU 4985 O ASP E 38 5072 7702 7060 1587 551 646 O ATOM 4986 CB ASP E 38 25.737 4.752 185.461 1.00 48.69 C ANISOU 4986 CB ASP E 38 5388 6461 6651 1287 344 276 C ATOM 4987 CG ASP E 38 24.317 4.755 185.986 1.00 47.45 C ANISOU 4987 CG ASP E 38 5494 6062 6473 974 222 115 C ATOM 4988 OD1 ASP E 38 24.149 4.852 187.220 1.00 47.04 O ANISOU 4988 OD1 ASP E 38 5417 6001 6454 815 80 223 O ATOM 4989 OD2 ASP E 38 23.364 4.698 185.170 1.00 47.48 O ANISOU 4989 OD2 ASP E 38 5705 5928 6408 873 264 -95 O ATOM 4990 N PRO E 39 28.860 5.856 186.270 1.00 52.57 N ANISOU 4990 N PRO E 39 4894 7843 7236 1459 256 1007 N ATOM 4991 CA PRO E 39 30.311 5.815 186.094 1.00 56.30 C ANISOU 4991 CA PRO E 39 4931 8720 7742 1719 329 1337 C ATOM 4992 C PRO E 39 30.874 5.184 184.818 1.00 59.53 C ANISOU 4992 C PRO E 39 5284 9211 8122 2203 649 1319 C ATOM 4993 O PRO E 39 31.806 5.738 184.246 1.00 62.10 O ANISOU 4993 O PRO E 39 5213 9964 8416 2268 737 1533 O ATOM 4994 CB PRO E 39 30.771 5.070 187.342 1.00 58.06 C ANISOU 4994 CB PRO E 39 5082 8930 8049 1838 199 1578 C ATOM 4995 CG PRO E 39 29.865 5.632 188.396 1.00 54.89 C ANISOU 4995 CG PRO E 39 4892 8352 7610 1366 -56 1467 C ATOM 4996 CD PRO E 39 28.523 5.925 187.703 1.00 51.34 C ANISOU 4996 CD PRO E 39 4809 7595 7103 1198 20 1078 C ATOM 4997 N GLY E 40 30.312 4.078 184.340 1.00 60.19 N ANISOU 4997 N GLY E 40 5781 8900 8188 2514 827 1067 N ATOM 4998 CA GLY E 40 30.810 3.504 183.078 1.00 63.48 C ANISOU 4998 CA GLY E 40 6237 9362 8520 2988 1158 999 C ATOM 4999 C GLY E 40 29.938 3.793 181.865 1.00 61.40 C ANISOU 4999 C GLY E 40 6286 8944 8100 2848 1264 647 C ATOM 5000 O GLY E 40 30.415 3.912 180.739 1.00 62.40 O ANISOU 5000 O GLY E 40 6322 9287 8102 3072 1499 628 O ATOM 5001 N HIS E 41 28.645 3.926 182.106 1.00 58.07 N ANISOU 5001 N HIS E 41 6208 8188 7666 2468 1087 396 N ATOM 5002 CA HIS E 41 27.688 3.921 181.021 1.00 57.11 C ANISOU 5002 CA HIS E 41 6444 7864 7391 2354 1160 69 C ATOM 5003 C HIS E 41 27.452 5.302 180.384 1.00 54.19 C ANISOU 5003 C HIS E 41 5859 7788 6944 2015 1102 68 C ATOM 5004 O HIS E 41 27.028 5.388 179.234 1.00 54.86 O ANISOU 5004 O HIS E 41 6123 7855 6867 2003 1211 -122 O ATOM 5005 CB HIS E 41 26.362 3.319 181.506 1.00 56.03 C ANISOU 5005 CB HIS E 41 6753 7265 7270 2112 1001 -156 C ATOM 5006 CG HIS E 41 26.460 1.901 181.989 1.00 59.49 C ANISOU 5006 CG HIS E 41 7513 7328 7760 2407 1050 -177 C ATOM 5007 ND1 HIS E 41 26.740 0.841 181.151 1.00 63.80 N ANISOU 5007 ND1 HIS E 41 8416 7627 8197 2814 1280 -330 N ATOM 5008 CD2 HIS E 41 26.273 1.363 183.220 1.00 59.63 C ANISOU 5008 CD2 HIS E 41 7605 7141 7911 2349 897 -66 C ATOM 5009 CE1 HIS E 41 26.740 -0.284 181.846 1.00 66.11 C ANISOU 5009 CE1 HIS E 41 9000 7545 8574 3004 1260 -304 C ATOM 5010 NE2 HIS E 41 26.454 0.004 183.104 1.00 63.55 N ANISOU 5010 NE2 HIS E 41 8490 7257 8401 2714 1023 -130 N ATOM 5011 N GLY E 42 27.722 6.371 181.131 1.00 51.43 N ANISOU 5011 N GLY E 42 5168 7682 6690 1729 920 285 N ATOM 5012 CA GLY E 42 27.434 7.736 180.685 1.00 47.94 C ANISOU 5012 CA GLY E 42 4583 7435 6195 1379 829 302 C ATOM 5013 C GLY E 42 25.987 8.153 180.928 1.00 43.75 C ANISOU 5013 C GLY E 42 4325 6634 5664 1039 659 97 C ATOM 5014 O GLY E 42 25.318 7.677 181.846 1.00 42.81 O ANISOU 5014 O GLY E 42 4389 6262 5617 963 548 24 O ATOM 5015 N LEU E 43 25.497 9.061 180.104 1.00 41.42 N ANISOU 5015 N LEU E 43 4032 6423 5282 845 647 40 N ATOM 5016 CA LEU E 43 24.092 9.374 180.120 1.00 38.60 C ANISOU 5016 CA LEU E 43 3903 5856 4909 604 529 -130 C ATOM 5017 C LEU E 43 23.283 8.345 179.287 1.00 39.33 C ANISOU 5017 C LEU E 43 4316 5748 4880 696 613 -369 C ATOM 5018 O LEU E 43 23.442 8.241 178.070 1.00 39.54 O ANISOU 5018 O LEU E 43 4401 5871 4751 794 742 -441 O ATOM 5019 CB LEU E 43 23.849 10.798 179.624 1.00 37.42 C ANISOU 5019 CB LEU E 43 3638 5857 4721 370 459 -57 C ATOM 5020 CG LEU E 43 24.617 11.954 180.254 1.00 37.14 C ANISOU 5020 CG LEU E 43 3370 5983 4759 198 349 169 C ATOM 5021 CD1 LEU E 43 24.760 13.068 179.225 1.00 37.90 C ANISOU 5021 CD1 LEU E 43 3368 6260 4773 63 360 267 C ATOM 5022 CD2 LEU E 43 23.916 12.461 181.502 1.00 35.20 C ANISOU 5022 CD2 LEU E 43 3239 5538 4597 1 177 145 C ATOM 5023 N ARG E 44 22.437 7.576 179.973 1.00 38.82 N ANISOU 5023 N ARG E 44 4475 5410 4863 631 528 -478 N ATOM 5024 CA ARG E 44 21.460 6.705 179.326 1.00 39.15 C ANISOU 5024 CA ARG E 44 4853 5238 4785 576 527 -686 C ATOM 5025 C ARG E 44 20.057 7.297 179.542 1.00 36.45 C ANISOU 5025 C ARG E 44 4515 4881 4453 252 361 -702 C ATOM 5026 O ARG E 44 19.738 7.776 180.630 1.00 34.02 O ANISOU 5026 O ARG E 44 4085 4572 4269 144 268 -605 O ATOM 5027 CB ARG E 44 21.541 5.287 179.889 1.00 41.11 C ANISOU 5027 CB ARG E 44 5369 5183 5068 723 550 -758 C ATOM 5028 CG ARG E 44 22.791 4.492 179.518 1.00 44.96 C ANISOU 5028 CG ARG E 44 5921 5642 5521 1133 754 -758 C ATOM 5029 CD ARG E 44 22.767 3.089 180.162 1.00 47.42 C ANISOU 5029 CD ARG E 44 6559 5575 5885 1285 756 -812 C ATOM 5030 NE ARG E 44 22.928 3.139 181.622 1.00 46.96 N ANISOU 5030 NE ARG E 44 6313 5510 6018 1239 635 -617 N ATOM 5031 CZ ARG E 44 22.757 2.103 182.448 1.00 48.45 C ANISOU 5031 CZ ARG E 44 6735 5392 6280 1281 579 -599 C ATOM 5032 NH1 ARG E 44 22.399 0.914 181.979 1.00 51.48 N ANISOU 5032 NH1 ARG E 44 7586 5398 6575 1357 622 -771 N ATOM 5033 NH2 ARG E 44 22.941 2.253 183.752 1.00 47.11 N ANISOU 5033 NH2 ARG E 44 6372 5277 6251 1224 466 -403 N ATOM 5034 N LEU E 45 19.242 7.274 178.490 1.00 36.46 N ANISOU 5034 N LEU E 45 4650 4901 4301 116 333 -807 N ATOM 5035 CA LEU E 45 17.916 7.878 178.495 1.00 34.78 C ANISOU 5035 CA LEU E 45 4376 4756 4083 -151 190 -772 C ATOM 5036 C LEU E 45 16.887 6.929 179.100 1.00 35.31 C ANISOU 5036 C LEU E 45 4618 4635 4162 -331 81 -818 C ATOM 5037 O LEU E 45 16.858 5.739 178.788 1.00 36.92 O ANISOU 5037 O LEU E 45 5125 4631 4273 -348 79 -949 O ATOM 5038 CB LEU E 45 17.513 8.243 177.063 1.00 35.93 C ANISOU 5038 CB LEU E 45 4557 5057 4038 -245 179 -814 C ATOM 5039 CG LEU E 45 16.181 8.928 176.736 1.00 35.66 C ANISOU 5039 CG LEU E 45 4416 5170 3965 -484 34 -729 C ATOM 5040 CD1 LEU E 45 16.175 10.419 177.099 1.00 33.66 C ANISOU 5040 CD1 LEU E 45 3880 5070 3841 -443 29 -550 C ATOM 5041 CD2 LEU E 45 15.856 8.743 175.264 1.00 37.62 C ANISOU 5041 CD2 LEU E 45 4808 5525 3962 -598 0 -805 C ATOM 5042 N ILE E 46 16.034 7.458 179.964 1.00 34.01 N ANISOU 5042 N ILE E 46 4286 4539 4098 -467 -4 -702 N ATOM 5043 CA ILE E 46 15.016 6.633 180.578 1.00 35.06 C ANISOU 5043 CA ILE E 46 4518 4566 4237 -672 -105 -689 C ATOM 5044 C ILE E 46 13.670 6.791 179.880 1.00 35.95 C ANISOU 5044 C ILE E 46 4573 4845 4241 -938 -227 -640 C ATOM 5045 O ILE E 46 13.053 5.809 179.454 1.00 38.30 O ANISOU 5045 O ILE E 46 5082 5049 4421 -1172 -335 -697 O ATOM 5046 CB ILE E 46 14.852 6.952 182.059 1.00 33.64 C ANISOU 5046 CB ILE E 46 4185 4397 4200 -653 -101 -567 C ATOM 5047 CG1 ILE E 46 16.221 7.049 182.741 1.00 32.70 C ANISOU 5047 CG1 ILE E 46 4055 4194 4174 -420 -17 -563 C ATOM 5048 CG2 ILE E 46 14.006 5.897 182.689 1.00 35.16 C ANISOU 5048 CG2 ILE E 46 4500 4475 4384 -861 -185 -534 C ATOM 5049 CD1 ILE E 46 16.186 6.823 184.241 1.00 31.57 C ANISOU 5049 CD1 ILE E 46 3893 3985 4116 -431 -36 -475 C ATOM 5050 N HIS E 47 13.228 8.037 179.770 1.00 34.67 N ANISOU 5050 N HIS E 47 4136 4925 4112 -909 -224 -515 N ATOM 5051 CA HIS E 47 11.958 8.362 179.141 1.00 35.96 C ANISOU 5051 CA HIS E 47 4151 5321 4189 -1110 -339 -398 C ATOM 5052 C HIS E 47 12.047 9.757 178.534 1.00 35.31 C ANISOU 5052 C HIS E 47 3870 5431 4116 -962 -298 -307 C ATOM 5053 O HIS E 47 12.819 10.600 179.007 1.00 33.31 O ANISOU 5053 O HIS E 47 3556 5129 3970 -747 -193 -296 O ATOM 5054 CB HIS E 47 10.825 8.369 180.171 1.00 35.99 C ANISOU 5054 CB HIS E 47 3956 5447 4271 -1220 -377 -227 C ATOM 5055 CG HIS E 47 10.244 7.024 180.475 1.00 37.69 C ANISOU 5055 CG HIS E 47 4324 5564 4431 -1511 -489 -230 C ATOM 5056 ND1 HIS E 47 9.492 6.313 179.564 1.00 40.30 N ANISOU 5056 ND1 HIS E 47 4758 5955 4599 -1849 -666 -221 N ATOM 5057 CD2 HIS E 47 10.266 6.280 181.609 1.00 37.89 C ANISOU 5057 CD2 HIS E 47 4434 5436 4528 -1557 -472 -216 C ATOM 5058 CE1 HIS E 47 9.101 5.176 180.115 1.00 42.37 C ANISOU 5058 CE1 HIS E 47 5185 6070 4843 -2106 -757 -208 C ATOM 5059 NE2 HIS E 47 9.554 5.132 181.357 1.00 40.56 N ANISOU 5059 NE2 HIS E 47 4937 5714 4761 -1921 -634 -195 N ATOM 5060 N TYR E 48 11.243 10.005 177.502 1.00 37.02 N ANISOU 5060 N TYR E 48 3998 5860 4206 -1109 -407 -217 N ATOM 5061 CA TYR E 48 11.161 11.343 176.897 1.00 36.88 C ANISOU 5061 CA TYR E 48 3792 6026 4195 -977 -390 -78 C ATOM 5062 C TYR E 48 9.717 11.767 176.638 1.00 38.86 C ANISOU 5062 C TYR E 48 3776 6571 4418 -1085 -506 163 C ATOM 5063 O TYR E 48 8.799 10.980 176.875 1.00 40.02 O ANISOU 5063 O TYR E 48 3862 6819 4524 -1309 -611 226 O ATOM 5064 CB TYR E 48 12.031 11.490 175.633 1.00 36.36 C ANISOU 5064 CB TYR E 48 3867 5969 3981 -959 -375 -170 C ATOM 5065 CG TYR E 48 11.694 10.601 174.471 1.00 38.99 C ANISOU 5065 CG TYR E 48 4380 6373 4062 -1208 -498 -258 C ATOM 5066 CD1 TYR E 48 12.160 9.289 174.416 1.00 40.25 C ANISOU 5066 CD1 TYR E 48 4865 6311 4116 -1293 -485 -488 C ATOM 5067 CD2 TYR E 48 10.934 11.075 173.401 1.00 41.28 C ANISOU 5067 CD2 TYR E 48 4557 6932 4194 -1355 -633 -110 C ATOM 5068 CE1 TYR E 48 11.859 8.462 173.347 1.00 43.17 C ANISOU 5068 CE1 TYR E 48 5503 6691 4210 -1538 -601 -606 C ATOM 5069 CE2 TYR E 48 10.626 10.254 172.319 1.00 43.97 C ANISOU 5069 CE2 TYR E 48 5116 7341 4250 -1634 -774 -205 C ATOM 5070 CZ TYR E 48 11.098 8.954 172.302 1.00 45.18 C ANISOU 5070 CZ TYR E 48 5651 7234 4282 -1731 -753 -473 C ATOM 5071 OH TYR E 48 10.807 8.132 171.250 1.00 48.59 O ANISOU 5071 OH TYR E 48 6395 7674 4393 -2019 -893 -603 O ATOM 5072 N SER E 49 9.533 13.004 176.166 1.00 38.77 N ANISOU 5072 N SER E 49 3595 6705 4430 -927 -492 331 N ATOM 5073 CA SER E 49 8.205 13.582 175.980 1.00 40.63 C ANISOU 5073 CA SER E 49 3522 7248 4669 -926 -573 619 C ATOM 5074 C SER E 49 8.144 14.689 174.918 1.00 41.84 C ANISOU 5074 C SER E 49 3578 7550 4770 -819 -616 792 C ATOM 5075 O SER E 49 8.853 15.697 175.007 1.00 40.93 O ANISOU 5075 O SER E 49 3532 7274 4747 -579 -503 792 O ATOM 5076 CB SER E 49 7.694 14.145 177.299 1.00 40.20 C ANISOU 5076 CB SER E 49 3294 7186 4795 -677 -434 736 C ATOM 5077 OG SER E 49 6.320 14.475 177.206 1.00 43.47 O ANISOU 5077 OG SER E 49 3360 7949 5206 -655 -489 1042 O ATOM 5078 N TYR E 50 7.271 14.511 173.932 1.00 43.83 N ANISOU 5078 N TYR E 50 3676 8114 4862 -1032 -801 969 N ATOM 5079 CA TYR E 50 7.092 15.513 172.903 1.00 45.11 C ANISOU 5079 CA TYR E 50 3724 8457 4957 -947 -868 1187 C ATOM 5080 C TYR E 50 6.103 16.579 173.347 1.00 46.68 C ANISOU 5080 C TYR E 50 3591 8828 5316 -650 -824 1524 C ATOM 5081 O TYR E 50 6.192 17.753 172.957 1.00 47.05 O ANISOU 5081 O TYR E 50 3605 8859 5415 -404 -788 1695 O ATOM 5082 CB TYR E 50 6.592 14.870 171.621 1.00 48.19 C ANISOU 5082 CB TYR E 50 4107 9135 5068 -1319 -1110 1250 C ATOM 5083 CG TYR E 50 7.576 13.947 170.959 1.00 47.86 C ANISOU 5083 CG TYR E 50 4456 8918 4812 -1545 -1125 918 C ATOM 5084 CD1 TYR E 50 8.929 14.232 170.977 1.00 46.06 C ANISOU 5084 CD1 TYR E 50 4457 8418 4624 -1350 -939 713 C ATOM 5085 CD2 TYR E 50 7.152 12.800 170.288 1.00 50.46 C ANISOU 5085 CD2 TYR E 50 4937 9362 4875 -1953 -1323 827 C ATOM 5086 CE1 TYR E 50 9.831 13.405 170.369 1.00 46.07 C ANISOU 5086 CE1 TYR E 50 4786 8295 4423 -1476 -905 435 C ATOM 5087 CE2 TYR E 50 8.057 11.958 169.662 1.00 50.62 C ANISOU 5087 CE2 TYR E 50 5381 9184 4670 -2093 -1298 501 C ATOM 5088 CZ TYR E 50 9.399 12.276 169.700 1.00 48.43 C ANISOU 5088 CZ TYR E 50 5282 8668 4450 -1813 -1066 313 C ATOM 5089 OH TYR E 50 10.329 11.465 169.095 1.00 49.10 O ANISOU 5089 OH TYR E 50 5755 8588 4311 -1866 -989 13 O ATOM 5090 N GLY E 51 5.146 16.162 174.158 1.00 47.23 N ANISOU 5090 N GLY E 51 3423 9065 5456 -657 -816 1639 N ATOM 5091 CA GLY E 51 4.143 17.075 174.641 1.00 49.67 C ANISOU 5091 CA GLY E 51 3393 9577 5902 -315 -729 1970 C ATOM 5092 C GLY E 51 3.329 16.428 175.731 1.00 51.36 C ANISOU 5092 C GLY E 51 3383 9952 6179 -338 -663 2034 C ATOM 5093 O GLY E 51 3.729 15.400 176.299 1.00 50.15 O ANISOU 5093 O GLY E 51 3411 9639 6004 -578 -659 1785 O ATOM 5094 N VAL E 52 2.187 17.044 176.013 1.00 54.30 N ANISOU 5094 N VAL E 52 3352 10655 6625 -65 -599 2399 N ATOM 5095 CA VAL E 52 1.298 16.636 177.079 1.00 55.96 C ANISOU 5095 CA VAL E 52 3268 11105 6891 -8 -486 2545 C ATOM 5096 C VAL E 52 0.739 15.251 176.761 1.00 58.10 C ANISOU 5096 C VAL E 52 3376 11688 7013 -600 -745 2607 C ATOM 5097 O VAL E 52 0.426 14.967 175.601 1.00 60.39 O ANISOU 5097 O VAL E 52 3570 12225 7152 -939 -1019 2742 O ATOM 5098 CB VAL E 52 0.171 17.681 177.218 1.00 59.59 C ANISOU 5098 CB VAL E 52 3285 11920 7438 468 -353 2984 C ATOM 5099 CG1 VAL E 52 -0.836 17.305 178.325 1.00 61.83 C ANISOU 5099 CG1 VAL E 52 3186 12549 7757 571 -193 3194 C ATOM 5100 CG2 VAL E 52 0.786 19.054 177.458 1.00 58.05 C ANISOU 5100 CG2 VAL E 52 3381 11307 7367 1023 -123 2891 C ATOM 5101 N LYS E 53 0.720 14.382 177.779 1.00 57.62 N ANISOU 5101 N LYS E 53 3362 11559 6971 -759 -672 2481 N ATOM 5102 CA LYS E 53 0.143 13.029 177.727 1.00 59.33 C ANISOU 5102 CA LYS E 53 3468 12014 7060 -1337 -900 2553 C ATOM 5103 C LYS E 53 0.779 12.129 176.661 1.00 58.30 C ANISOU 5103 C LYS E 53 3726 11676 6748 -1844 -1182 2295 C ATOM 5104 O LYS E 53 0.154 11.197 176.165 1.00 60.58 O ANISOU 5104 O LYS E 53 3940 12206 6874 -2374 -1458 2416 O ATOM 5105 CB LYS E 53 -1.384 13.085 177.577 1.00 64.69 C ANISOU 5105 CB LYS E 53 3507 13373 7699 -1434 -1010 3086 C ATOM 5106 CG LYS E 53 -2.118 13.715 178.765 1.00 66.69 C ANISOU 5106 CG LYS E 53 3361 13884 8094 -945 -690 3351 C ATOM 5107 CD LYS E 53 -3.610 13.424 178.674 1.00 72.17 C ANISOU 5107 CD LYS E 53 3374 15322 8724 -1161 -822 3905 C ATOM 5108 CE LYS E 53 -4.436 14.291 179.605 1.00 75.01 C ANISOU 5108 CE LYS E 53 3259 16037 9203 -537 -465 4247 C ATOM 5109 NZ LYS E 53 -5.884 14.227 179.240 1.00 80.99 N ANISOU 5109 NZ LYS E 53 3253 17617 9904 -676 -608 4878 N ATOM 5110 N ASP E 54 2.040 12.417 176.344 1.00 54.77 N ANISOU 5110 N ASP E 54 3715 10779 6315 -1677 -1100 1944 N ATOM 5111 CA ASP E 54 2.708 11.856 175.187 1.00 54.08 C ANISOU 5111 CA ASP E 54 3993 10520 6037 -2004 -1297 1712 C ATOM 5112 C ASP E 54 4.174 11.564 175.512 1.00 50.11 C ANISOU 5112 C ASP E 54 3984 9475 5580 -1879 -1138 1276 C ATOM 5113 O ASP E 54 5.060 12.406 175.356 1.00 47.71 O ANISOU 5113 O ASP E 54 3816 8966 5345 -1555 -993 1154 O ATOM 5114 CB ASP E 54 2.588 12.824 174.013 1.00 55.21 C ANISOU 5114 CB ASP E 54 4004 10872 6100 -1885 -1384 1890 C ATOM 5115 CG ASP E 54 3.288 12.324 172.768 1.00 55.39 C ANISOU 5115 CG ASP E 54 4414 10755 5877 -2192 -1556 1652 C ATOM 5116 OD1 ASP E 54 3.355 11.095 172.552 1.00 56.57 O ANISOU 5116 OD1 ASP E 54 4842 10801 5851 -2621 -1711 1461 O ATOM 5117 OD2 ASP E 54 3.772 13.169 172.001 1.00 55.05 O ANISOU 5117 OD2 ASP E 54 4426 10694 5797 -1996 -1526 1661 O ATOM 5118 N THR E 55 4.410 10.343 175.976 1.00 49.71 N ANISOU 5118 N THR E 55 4190 9209 5489 -2153 -1180 1078 N ATOM 5119 CA THR E 55 5.711 9.922 176.454 1.00 46.60 C ANISOU 5119 CA THR E 55 4204 8346 5154 -2019 -1029 723 C ATOM 5120 C THR E 55 6.198 8.647 175.769 1.00 48.03 C ANISOU 5120 C THR E 55 4829 8284 5137 -2368 -1173 462 C ATOM 5121 O THR E 55 5.393 7.820 175.359 1.00 51.49 O ANISOU 5121 O THR E 55 5300 8853 5409 -2804 -1403 541 O ATOM 5122 CB THR E 55 5.669 9.657 177.980 1.00 45.21 C ANISOU 5122 CB THR E 55 3974 8053 5150 -1900 -877 725 C ATOM 5123 OG1 THR E 55 4.956 8.444 178.247 1.00 48.01 O ANISOU 5123 OG1 THR E 55 4351 8467 5425 -2320 -1037 791 O ATOM 5124 CG2 THR E 55 5.005 10.812 178.754 1.00 44.37 C ANISOU 5124 CG2 THR E 55 3469 8195 5195 -1554 -713 981 C ATOM 5125 N ASP E 56 7.511 8.467 175.654 1.00 46.97 N ANISOU 5125 N ASP E 56 5050 7793 5002 -2179 -1039 163 N ATOM 5126 CA ASP E 56 8.037 7.192 175.157 1.00 49.01 C ANISOU 5126 CA ASP E 56 5790 7754 5078 -2410 -1115 -108 C ATOM 5127 C ASP E 56 9.308 6.746 175.869 1.00 46.86 C ANISOU 5127 C ASP E 56 5798 7081 4927 -2135 -913 -352 C ATOM 5128 O ASP E 56 9.981 7.546 176.511 1.00 44.22 O ANISOU 5128 O ASP E 56 5304 6719 4780 -1787 -730 -337 O ATOM 5129 CB ASP E 56 8.230 7.199 173.635 1.00 51.74 C ANISOU 5129 CB ASP E 56 6346 8167 5144 -2539 -1214 -212 C ATOM 5130 CG ASP E 56 7.663 5.944 172.980 1.00 56.77 C ANISOU 5130 CG ASP E 56 7346 8725 5498 -3035 -1462 -312 C ATOM 5131 OD1 ASP E 56 7.672 4.866 173.634 1.00 58.09 O ANISOU 5131 OD1 ASP E 56 7786 8595 5691 -3192 -1490 -425 O ATOM 5132 OD2 ASP E 56 7.174 6.037 171.829 1.00 59.53 O ANISOU 5132 OD2 ASP E 56 7731 9303 5587 -3299 -1649 -261 O ATOM 5133 N LYS E 57 9.631 5.462 175.735 1.00 49.11 N ANISOU 5133 N LYS E 57 6523 7048 5089 -2301 -961 -562 N ATOM 5134 CA LYS E 57 10.736 4.837 176.470 1.00 48.17 C ANISOU 5134 CA LYS E 57 6667 6550 5085 -2046 -792 -746 C ATOM 5135 C LYS E 57 12.134 5.144 175.925 1.00 47.16 C ANISOU 5135 C LYS E 57 6678 6310 4932 -1669 -588 -927 C ATOM 5136 O LYS E 57 12.326 5.350 174.727 1.00 47.91 O ANISOU 5136 O LYS E 57 6882 6500 4824 -1677 -589 -1012 O ATOM 5137 CB LYS E 57 10.529 3.316 176.533 1.00 51.40 C ANISOU 5137 CB LYS E 57 7540 6615 5374 -2335 -916 -879 C ATOM 5138 CG LYS E 57 9.138 2.929 176.987 1.00 53.92 C ANISOU 5138 CG LYS E 57 7715 7085 5687 -2794 -1144 -660 C ATOM 5139 CD LYS E 57 9.058 1.520 177.539 1.00 56.84 C ANISOU 5139 CD LYS E 57 8505 7058 6032 -3042 -1238 -733 C ATOM 5140 CE LYS E 57 7.805 1.359 178.416 1.00 58.30 C ANISOU 5140 CE LYS E 57 8380 7475 6296 -3420 -1398 -425 C ATOM 5141 NZ LYS E 57 7.889 0.243 179.416 1.00 59.41 N ANISOU 5141 NZ LYS E 57 8808 7252 6512 -3550 -1423 -419 N ATOM 5142 N GLY E 58 13.109 5.175 176.825 1.00 45.53 N ANISOU 5142 N GLY E 58 6440 5943 4915 -1353 -417 -955 N ATOM 5143 CA GLY E 58 14.508 5.265 176.430 1.00 45.97 C ANISOU 5143 CA GLY E 58 6602 5910 4953 -1002 -219 -1087 C ATOM 5144 C GLY E 58 15.150 3.893 176.457 1.00 48.64 C ANISOU 5144 C GLY E 58 7388 5871 5224 -895 -150 -1282 C ATOM 5145 O GLY E 58 14.459 2.882 176.355 1.00 50.94 O ANISOU 5145 O GLY E 58 8014 5941 5398 -1164 -287 -1366 O ATOM 5146 N GLU E 59 16.469 3.853 176.606 1.00 49.14 N ANISOU 5146 N GLU E 59 7459 5855 5355 -505 57 -1329 N ATOM 5147 CA GLU E 59 17.215 2.594 176.557 1.00 53.04 C ANISOU 5147 CA GLU E 59 8380 5988 5785 -281 173 -1498 C ATOM 5148 C GLU E 59 17.100 1.801 177.864 1.00 52.65 C ANISOU 5148 C GLU E 59 8423 5659 5922 -301 110 -1430 C ATOM 5149 O GLU E 59 17.326 0.596 177.888 1.00 54.96 O ANISOU 5149 O GLU E 59 9158 5567 6157 -219 137 -1555 O ATOM 5150 CB GLU E 59 18.685 2.868 176.214 1.00 54.64 C ANISOU 5150 CB GLU E 59 8476 6294 5990 183 435 -1510 C ATOM 5151 CG GLU E 59 19.249 4.114 176.940 1.00 52.97 C ANISOU 5151 CG GLU E 59 7718 6403 6005 294 472 -1275 C ATOM 5152 CD GLU E 59 20.424 4.798 176.211 1.00 54.44 C ANISOU 5152 CD GLU E 59 7687 6867 6131 580 674 -1225 C ATOM 5153 OE1 GLU E 59 20.365 6.048 176.032 1.00 52.22 O ANISOU 5153 OE1 GLU E 59 7073 6884 5882 464 633 -1088 O ATOM 5154 OE2 GLU E 59 21.397 4.089 175.830 1.00 57.36 O ANISOU 5154 OE2 GLU E 59 8220 7157 6417 931 880 -1302 O ATOM 5155 N VAL E 60 16.752 2.480 178.953 1.00 49.49 N ANISOU 5155 N VAL E 60 7643 5434 5727 -399 35 -1230 N ATOM 5156 CA VAL E 60 16.704 1.833 180.260 1.00 49.49 C ANISOU 5156 CA VAL E 60 7688 5228 5887 -412 -15 -1130 C ATOM 5157 C VAL E 60 15.478 2.202 181.074 1.00 47.59 C ANISOU 5157 C VAL E 60 7223 5140 5720 -763 -177 -971 C ATOM 5158 O VAL E 60 15.586 2.665 182.198 1.00 46.13 O ANISOU 5158 O VAL E 60 6778 5062 5686 -703 -163 -821 O ATOM 5159 CB VAL E 60 17.952 2.157 181.108 1.00 48.04 C ANISOU 5159 CB VAL E 60 7268 5103 5881 -44 121 -1014 C ATOM 5160 CG1 VAL E 60 19.090 1.203 180.778 1.00 51.21 C ANISOU 5160 CG1 VAL E 60 7957 5247 6252 338 280 -1106 C ATOM 5161 CG2 VAL E 60 18.380 3.588 180.917 1.00 45.68 C ANISOU 5161 CG2 VAL E 60 6555 5179 5624 43 182 -931 C ATOM 5162 N SER E 61 14.303 1.962 180.525 1.00 48.81 N ANISOU 5162 N SER E 61 7480 5324 5743 -1134 -331 -987 N ATOM 5163 CA SER E 61 13.090 2.451 181.153 1.00 47.39 C ANISOU 5163 CA SER E 61 6992 5400 5614 -1429 -452 -793 C ATOM 5164 C SER E 61 12.584 1.603 182.331 1.00 48.31 C ANISOU 5164 C SER E 61 7194 5358 5804 -1625 -535 -665 C ATOM 5165 O SER E 61 11.728 2.067 183.072 1.00 47.16 O ANISOU 5165 O SER E 61 6738 5468 5713 -1784 -575 -475 O ATOM 5166 CB SER E 61 11.988 2.582 180.105 1.00 48.67 C ANISOU 5166 CB SER E 61 7138 5753 5602 -1774 -606 -785 C ATOM 5167 OG SER E 61 11.407 1.317 179.864 1.00 51.78 O ANISOU 5167 OG SER E 61 7925 5888 5860 -2132 -774 -838 O ATOM 5168 N ASP E 62 13.111 0.384 182.494 1.00 50.52 N ANISOU 5168 N ASP E 62 7897 5223 6075 -1589 -544 -753 N ATOM 5169 CA ASP E 62 12.582 -0.602 183.474 1.00 52.24 C ANISOU 5169 CA ASP E 62 8286 5230 6331 -1844 -657 -618 C ATOM 5170 C ASP E 62 12.649 -0.185 184.940 1.00 49.59 C ANISOU 5170 C ASP E 62 7629 5061 6150 -1741 -595 -413 C ATOM 5171 O ASP E 62 13.709 0.210 185.434 1.00 47.85 O ANISOU 5171 O ASP E 62 7308 4837 6034 -1371 -464 -424 O ATOM 5172 CB ASP E 62 13.272 -1.964 183.323 1.00 56.06 C ANISOU 5172 CB ASP E 62 9355 5165 6781 -1749 -662 -755 C ATOM 5173 CG ASP E 62 12.504 -2.914 182.422 1.00 60.72 C ANISOU 5173 CG ASP E 62 10420 5482 7168 -2167 -847 -869 C ATOM 5174 OD1 ASP E 62 11.547 -2.455 181.759 1.00 61.05 O ANISOU 5174 OD1 ASP E 62 10288 5821 7088 -2514 -974 -844 O ATOM 5175 OD2 ASP E 62 12.854 -4.119 182.378 1.00 64.29 O ANISOU 5175 OD2 ASP E 62 11442 5413 7574 -2157 -878 -970 O ATOM 5176 N GLY E 63 11.508 -0.280 185.621 1.00 49.17 N ANISOU 5176 N GLY E 63 7412 5185 6084 -2090 -695 -211 N ATOM 5177 CA GLY E 63 11.386 0.194 186.988 1.00 46.58 C ANISOU 5177 CA GLY E 63 6780 5076 5841 -2023 -622 -18 C ATOM 5178 C GLY E 63 11.126 1.683 187.099 1.00 43.70 C ANISOU 5178 C GLY E 63 5966 5142 5495 -1864 -508 21 C ATOM 5179 O GLY E 63 11.331 2.269 188.173 1.00 43.08 O ANISOU 5179 O GLY E 63 5700 5206 5463 -1701 -407 110 O ATOM 5180 N TYR E 64 10.689 2.301 185.997 1.00 42.22 N ANISOU 5180 N TYR E 64 5649 5139 5252 -1907 -527 -43 N ATOM 5181 CA TYR E 64 10.395 3.742 185.961 1.00 39.00 C ANISOU 5181 CA TYR E 64 4863 5093 4864 -1734 -423 3 C ATOM 5182 C TYR E 64 9.102 4.060 185.212 1.00 39.95 C ANISOU 5182 C TYR E 64 4749 5529 4902 -1979 -507 124 C ATOM 5183 O TYR E 64 8.728 3.366 184.271 1.00 42.38 O ANISOU 5183 O TYR E 64 5219 5766 5116 -2260 -663 90 O ATOM 5184 CB TYR E 64 11.508 4.534 185.274 1.00 36.84 C ANISOU 5184 CB TYR E 64 4612 4760 4626 -1413 -337 -173 C ATOM 5185 CG TYR E 64 12.911 4.394 185.823 1.00 35.50 C ANISOU 5185 CG TYR E 64 4588 4365 4534 -1145 -261 -258 C ATOM 5186 CD1 TYR E 64 13.361 5.213 186.854 1.00 33.53 C ANISOU 5186 CD1 TYR E 64 4183 4214 4341 -965 -175 -201 C ATOM 5187 CD2 TYR E 64 13.802 3.485 185.271 1.00 36.33 C ANISOU 5187 CD2 TYR E 64 4990 4177 4637 -1059 -274 -386 C ATOM 5188 CE1 TYR E 64 14.646 5.113 187.339 1.00 32.81 C ANISOU 5188 CE1 TYR E 64 4178 3981 4308 -764 -144 -231 C ATOM 5189 CE2 TYR E 64 15.094 3.383 185.741 1.00 35.86 C ANISOU 5189 CE2 TYR E 64 4988 3982 4654 -782 -202 -407 C ATOM 5190 CZ TYR E 64 15.511 4.197 186.776 1.00 34.29 C ANISOU 5190 CZ TYR E 64 4579 3932 4518 -662 -156 -312 C ATOM 5191 OH TYR E 64 16.798 4.082 187.245 1.00 34.32 O ANISOU 5191 OH TYR E 64 4600 3856 4586 -433 -123 -286 O ATOM 5192 N SER E 65 8.426 5.125 185.616 1.00 38.47 N ANISOU 5192 N SER E 65 4192 5692 4732 -1861 -406 274 N ATOM 5193 CA SER E 65 7.299 5.620 184.850 1.00 39.44 C ANISOU 5193 CA SER E 65 4022 6170 4796 -1997 -468 428 C ATOM 5194 C SER E 65 7.483 7.087 184.712 1.00 37.91 C ANISOU 5194 C SER E 65 3622 6130 4653 -1625 -319 414 C ATOM 5195 O SER E 65 8.362 7.668 185.346 1.00 35.95 O ANISOU 5195 O SER E 65 3462 5728 4471 -1333 -183 300 O ATOM 5196 CB SER E 65 5.976 5.383 185.551 1.00 41.43 C ANISOU 5196 CB SER E 65 3968 6765 5010 -2228 -482 728 C ATOM 5197 OG SER E 65 5.731 4.008 185.641 1.00 43.99 O ANISOU 5197 OG SER E 65 4506 6932 5277 -2651 -656 775 O ATOM 5198 N VAL E 66 6.606 7.688 183.927 1.00 39.42 N ANISOU 5198 N VAL E 66 3543 6631 4804 -1658 -363 561 N ATOM 5199 CA VAL E 66 6.766 9.062 183.582 1.00 38.76 C ANISOU 5199 CA VAL E 66 3320 6641 4764 -1317 -249 559 C ATOM 5200 C VAL E 66 5.407 9.696 183.211 1.00 41.47 C ANISOU 5200 C VAL E 66 3247 7431 5078 -1311 -258 854 C ATOM 5201 O VAL E 66 4.468 9.006 182.825 1.00 43.61 O ANISOU 5201 O VAL E 66 3343 7954 5272 -1653 -417 1040 O ATOM 5202 CB VAL E 66 7.895 9.182 182.521 1.00 37.54 C ANISOU 5202 CB VAL E 66 3428 6238 4600 -1264 -305 331 C ATOM 5203 CG1 VAL E 66 7.375 9.438 181.178 1.00 38.62 C ANISOU 5203 CG1 VAL E 66 3451 6574 4649 -1384 -433 409 C ATOM 5204 CG2 VAL E 66 8.919 10.218 182.939 1.00 35.87 C ANISOU 5204 CG2 VAL E 66 3299 5854 4473 -912 -150 213 C ATOM 5205 N SER E 67 5.296 11.007 183.381 1.00 41.73 N ANISOU 5205 N SER E 67 3128 7561 5168 -921 -91 921 N ATOM 5206 CA SER E 67 4.012 11.682 183.315 1.00 44.53 C ANISOU 5206 CA SER E 67 3058 8345 5515 -783 -31 1240 C ATOM 5207 C SER E 67 4.201 13.139 182.882 1.00 44.19 C ANISOU 5207 C SER E 67 2999 8264 5529 -366 81 1250 C ATOM 5208 O SER E 67 5.073 13.838 183.405 1.00 42.31 O ANISOU 5208 O SER E 67 3026 7709 5342 -92 224 1056 O ATOM 5209 CB SER E 67 3.359 11.627 184.698 1.00 46.44 C ANISOU 5209 CB SER E 67 3120 8767 5756 -655 165 1384 C ATOM 5210 OG SER E 67 2.310 12.568 184.809 1.00 50.08 O ANISOU 5210 OG SER E 67 3197 9606 6224 -327 327 1671 O ATOM 5211 N ARG E 68 3.390 13.592 181.930 1.00 46.02 N ANISOU 5211 N ARG E 68 2934 8810 5740 -348 -6 1498 N ATOM 5212 CA ARG E 68 3.463 14.966 181.448 1.00 46.00 C ANISOU 5212 CA ARG E 68 2917 8770 5792 44 83 1563 C ATOM 5213 C ARG E 68 2.042 15.542 181.406 1.00 50.96 C ANISOU 5213 C ARG E 68 3057 9877 6428 280 156 1974 C ATOM 5214 O ARG E 68 1.327 15.451 180.401 1.00 53.76 O ANISOU 5214 O ARG E 68 3109 10584 6734 108 -32 2234 O ATOM 5215 CB ARG E 68 4.128 15.002 180.080 1.00 44.22 C ANISOU 5215 CB ARG E 68 2855 8422 5522 -144 -118 1463 C ATOM 5216 CG ARG E 68 4.366 16.388 179.516 1.00 44.99 C ANISOU 5216 CG ARG E 68 3001 8421 5672 205 -56 1530 C ATOM 5217 CD ARG E 68 5.812 16.830 179.628 1.00 42.03 C ANISOU 5217 CD ARG E 68 3054 7577 5337 286 4 1228 C ATOM 5218 NE ARG E 68 6.000 18.199 179.144 1.00 42.75 N ANISOU 5218 NE ARG E 68 3222 7544 5476 584 52 1324 N ATOM 5219 CZ ARG E 68 6.601 18.522 178.003 1.00 42.03 C ANISOU 5219 CZ ARG E 68 3236 7392 5343 478 -73 1318 C ATOM 5220 NH1 ARG E 68 7.081 17.583 177.201 1.00 40.91 N ANISOU 5220 NH1 ARG E 68 3145 7310 5090 116 -232 1195 N ATOM 5221 NH2 ARG E 68 6.730 19.793 177.665 1.00 42.95 N ANISOU 5221 NH2 ARG E 68 3440 7369 5508 742 -29 1438 N ATOM 5222 N SER E 69 1.614 16.104 182.527 1.00 52.54 N ANISOU 5222 N SER E 69 3172 10122 6667 681 436 2051 N ATOM 5223 CA SER E 69 0.270 16.624 182.638 1.00 56.92 C ANISOU 5223 CA SER E 69 3234 11163 7229 994 570 2463 C ATOM 5224 C SER E 69 0.213 18.064 182.152 1.00 58.62 C ANISOU 5224 C SER E 69 3483 11276 7514 1510 684 2571 C ATOM 5225 O SER E 69 -0.773 18.490 181.555 1.00 62.99 O ANISOU 5225 O SER E 69 3608 12244 8081 1690 663 2960 O ATOM 5226 CB SER E 69 -0.225 16.513 184.078 1.00 58.88 C ANISOU 5226 CB SER E 69 3377 11545 7450 1223 861 2512 C ATOM 5227 OG SER E 69 0.846 16.657 184.995 1.00 56.32 O ANISOU 5227 OG SER E 69 3573 10706 7120 1330 1002 2119 O ATOM 5228 N LYS E 70 1.266 18.824 182.424 1.00 56.05 N ANISOU 5228 N LYS E 70 3668 10400 7228 1739 790 2258 N ATOM 5229 CA LYS E 70 1.384 20.185 181.907 1.00 57.44 C ANISOU 5229 CA LYS E 70 3997 10360 7469 2164 860 2329 C ATOM 5230 C LYS E 70 2.679 20.233 181.123 1.00 53.56 C ANISOU 5230 C LYS E 70 3905 9461 6984 1865 651 2058 C ATOM 5231 O LYS E 70 3.546 19.373 181.330 1.00 50.12 O ANISOU 5231 O LYS E 70 3686 8844 6513 1484 551 1771 O ATOM 5232 CB LYS E 70 1.438 21.205 183.045 1.00 59.24 C ANISOU 5232 CB LYS E 70 4533 10265 7709 2728 1202 2221 C ATOM 5233 CG LYS E 70 0.329 21.067 184.056 1.00 63.75 C ANISOU 5233 CG LYS E 70 4774 11215 8232 3048 1481 2422 C ATOM 5234 CD LYS E 70 0.745 21.563 185.433 1.00 64.89 C ANISOU 5234 CD LYS E 70 5382 10967 8305 3383 1786 2136 C ATOM 5235 CE LYS E 70 1.089 23.044 185.407 1.00 67.47 C ANISOU 5235 CE LYS E 70 6180 10795 8660 3889 1936 2047 C ATOM 5236 NZ LYS E 70 0.402 23.757 186.533 1.00 72.56 N ANISOU 5236 NZ LYS E 70 6937 11420 9212 4535 2355 2081 N ATOM 5237 N THR E 71 2.825 21.232 180.245 1.00 53.97 N ANISOU 5237 N THR E 71 4046 9381 7078 2056 598 2174 N ATOM 5238 CA THR E 71 4.055 21.387 179.462 1.00 50.77 C ANISOU 5238 CA THR E 71 3991 8636 6664 1791 424 1965 C ATOM 5239 C THR E 71 5.267 21.683 180.358 1.00 47.91 C ANISOU 5239 C THR E 71 4139 7745 6318 1806 530 1605 C ATOM 5240 O THR E 71 6.374 21.226 180.084 1.00 44.95 O ANISOU 5240 O THR E 71 3973 7188 5916 1460 398 1379 O ATOM 5241 CB THR E 71 3.929 22.448 178.311 1.00 52.93 C ANISOU 5241 CB THR E 71 4251 8897 6965 1974 336 2217 C ATOM 5242 OG1 THR E 71 4.328 23.742 178.773 1.00 54.06 O ANISOU 5242 OG1 THR E 71 4789 8571 7179 2374 505 2165 O ATOM 5243 CG2 THR E 71 2.501 22.525 177.764 1.00 57.85 C ANISOU 5243 CG2 THR E 71 4341 10051 7587 2155 300 2663 C ATOM 5244 N GLU E 72 5.031 22.409 181.443 1.00 49.31 N ANISOU 5244 N GLU E 72 4506 7712 6516 2205 770 1567 N ATOM 5245 CA GLU E 72 6.071 22.761 182.393 1.00 48.10 C ANISOU 5245 CA GLU E 72 4855 7079 6342 2205 853 1251 C ATOM 5246 C GLU E 72 6.637 21.596 183.195 1.00 45.01 C ANISOU 5246 C GLU E 72 4497 6706 5897 1869 825 1004 C ATOM 5247 O GLU E 72 7.779 21.662 183.623 1.00 42.92 O ANISOU 5247 O GLU E 72 4589 6107 5611 1699 780 762 O ATOM 5248 CB GLU E 72 5.553 23.801 183.384 1.00 52.18 C ANISOU 5248 CB GLU E 72 5618 7368 6841 2734 1131 1261 C ATOM 5249 CG GLU E 72 5.225 25.151 182.785 1.00 55.97 C ANISOU 5249 CG GLU E 72 6247 7641 7378 3137 1185 1461 C ATOM 5250 CD GLU E 72 3.750 25.343 182.546 1.00 60.33 C ANISOU 5250 CD GLU E 72 6341 8614 7967 3580 1333 1832 C ATOM 5251 OE1 GLU E 72 3.093 24.401 182.057 1.00 60.16 O ANISOU 5251 OE1 GLU E 72 5771 9136 7952 3370 1227 2029 O ATOM 5252 OE2 GLU E 72 3.245 26.447 182.839 1.00 64.82 O ANISOU 5252 OE2 GLU E 72 7110 8969 8550 4141 1552 1944 O ATOM 5253 N ASP E 73 5.860 20.535 183.403 1.00 44.98 N ANISOU 5253 N ASP E 73 4124 7097 5869 1754 833 1096 N ATOM 5254 CA ASP E 73 6.307 19.460 184.309 1.00 43.07 C ANISOU 5254 CA ASP E 73 3947 6841 5577 1485 828 893 C ATOM 5255 C ASP E 73 6.510 18.083 183.683 1.00 40.79 C ANISOU 5255 C ASP E 73 3465 6750 5282 1028 615 871 C ATOM 5256 O ASP E 73 5.685 17.624 182.909 1.00 43.36 O ANISOU 5256 O ASP E 73 3453 7419 5602 909 517 1076 O ATOM 5257 CB ASP E 73 5.341 19.331 185.488 1.00 45.31 C ANISOU 5257 CB ASP E 73 4090 7327 5800 1731 1062 976 C ATOM 5258 CG ASP E 73 5.107 20.646 186.179 1.00 47.93 C ANISOU 5258 CG ASP E 73 4688 7429 6095 2237 1315 962 C ATOM 5259 OD1 ASP E 73 4.108 21.305 185.829 1.00 51.60 O ANISOU 5259 OD1 ASP E 73 4926 8091 6590 2612 1442 1218 O ATOM 5260 OD2 ASP E 73 5.930 21.028 187.040 1.00 46.48 O ANISOU 5260 OD2 ASP E 73 4958 6860 5841 2262 1377 706 O ATOM 5261 N PHE E 74 7.589 17.412 184.066 1.00 37.64 N ANISOU 5261 N PHE E 74 3300 6133 4869 777 543 634 N ATOM 5262 CA PHE E 74 7.888 16.068 183.591 1.00 35.36 C ANISOU 5262 CA PHE E 74 2935 5937 4565 396 373 573 C ATOM 5263 C PHE E 74 8.292 15.209 184.798 1.00 35.32 C ANISOU 5263 C PHE E 74 3060 5827 4535 279 414 432 C ATOM 5264 O PHE E 74 9.417 15.290 185.278 1.00 33.88 O ANISOU 5264 O PHE E 74 3143 5373 4357 260 411 251 O ATOM 5265 CB PHE E 74 9.015 16.155 182.565 1.00 32.20 C ANISOU 5265 CB PHE E 74 2703 5358 4174 254 238 452 C ATOM 5266 CG PHE E 74 9.198 14.924 181.727 1.00 30.68 C ANISOU 5266 CG PHE E 74 2464 5261 3931 -65 80 401 C ATOM 5267 CD1 PHE E 74 10.444 14.597 181.225 1.00 28.59 C ANISOU 5267 CD1 PHE E 74 2396 4816 3653 -184 17 232 C ATOM 5268 CD2 PHE E 74 8.135 14.102 181.424 1.00 31.80 C ANISOU 5268 CD2 PHE E 74 2385 5676 4021 -250 -3 533 C ATOM 5269 CE1 PHE E 74 10.615 13.471 180.452 1.00 28.07 C ANISOU 5269 CE1 PHE E 74 2362 4794 3510 -421 -93 157 C ATOM 5270 CE2 PHE E 74 8.315 12.981 180.653 1.00 30.77 C ANISOU 5270 CE2 PHE E 74 2318 5564 3809 -562 -158 454 C ATOM 5271 CZ PHE E 74 9.551 12.665 180.170 1.00 28.72 C ANISOU 5271 CZ PHE E 74 2311 5075 3524 -619 -187 248 C ATOM 5272 N LEU E 75 7.365 14.396 185.297 1.00 37.68 N ANISOU 5272 N LEU E 75 3149 6370 4798 180 440 553 N ATOM 5273 CA LEU E 75 7.581 13.659 186.545 1.00 38.06 C ANISOU 5273 CA LEU E 75 3304 6350 4807 93 498 475 C ATOM 5274 C LEU E 75 8.167 12.279 186.325 1.00 37.21 C ANISOU 5274 C LEU E 75 3291 6142 4705 -255 327 382 C ATOM 5275 O LEU E 75 7.505 11.421 185.751 1.00 38.34 O ANISOU 5275 O LEU E 75 3280 6459 4829 -503 210 490 O ATOM 5276 CB LEU E 75 6.258 13.402 187.232 1.00 41.73 C ANISOU 5276 CB LEU E 75 3482 7156 5216 135 621 696 C ATOM 5277 CG LEU E 75 5.350 14.478 187.782 1.00 45.43 C ANISOU 5277 CG LEU E 75 3801 7815 5644 538 867 845 C ATOM 5278 CD1 LEU E 75 4.678 13.820 188.979 1.00 48.04 C ANISOU 5278 CD1 LEU E 75 3996 8378 5880 496 1003 959 C ATOM 5279 CD2 LEU E 75 6.109 15.713 188.201 1.00 45.29 C ANISOU 5279 CD2 LEU E 75 4141 7454 5615 862 993 654 C ATOM 5280 N LEU E 76 9.370 12.033 186.815 1.00 35.37 N ANISOU 5280 N LEU E 76 3322 5631 4485 -279 305 202 N ATOM 5281 CA LEU E 76 9.913 10.689 186.743 1.00 35.39 C ANISOU 5281 CA LEU E 76 3441 5509 4495 -529 179 132 C ATOM 5282 C LEU E 76 9.479 9.956 187.995 1.00 36.61 C ANISOU 5282 C LEU E 76 3589 5716 4606 -621 225 212 C ATOM 5283 O LEU E 76 9.755 10.403 189.096 1.00 36.58 O ANISOU 5283 O LEU E 76 3668 5666 4564 -479 332 186 O ATOM 5284 CB LEU E 76 11.443 10.718 186.661 1.00 34.01 C ANISOU 5284 CB LEU E 76 3495 5066 4361 -480 138 -39 C ATOM 5285 CG LEU E 76 12.155 9.361 186.604 1.00 33.90 C ANISOU 5285 CG LEU E 76 3635 4882 4364 -634 42 -110 C ATOM 5286 CD1 LEU E 76 11.848 8.641 185.302 1.00 34.76 C ANISOU 5286 CD1 LEU E 76 3759 5000 4448 -794 -57 -134 C ATOM 5287 CD2 LEU E 76 13.658 9.521 186.775 1.00 32.60 C ANISOU 5287 CD2 LEU E 76 3609 4539 4240 -519 37 -210 C ATOM 5288 N THR E 77 8.799 8.832 187.842 1.00 38.31 N ANISOU 5288 N THR E 77 3732 6023 4801 -892 131 319 N ATOM 5289 CA THR E 77 8.353 8.101 189.019 1.00 40.09 C ANISOU 5289 CA THR E 77 3941 6316 4975 -1019 168 438 C ATOM 5290 C THR E 77 8.854 6.647 189.060 1.00 40.76 C ANISOU 5290 C THR E 77 4257 6154 5076 -1288 15 403 C ATOM 5291 O THR E 77 8.898 5.970 188.033 1.00 41.42 O ANISOU 5291 O THR E 77 4440 6122 5174 -1473 -129 353 O ATOM 5292 CB THR E 77 6.819 8.267 189.286 1.00 42.58 C ANISOU 5292 CB THR E 77 3907 7046 5224 -1069 256 699 C ATOM 5293 OG1 THR E 77 6.349 7.157 190.044 1.00 44.73 O ANISOU 5293 OG1 THR E 77 4162 7391 5443 -1350 215 853 O ATOM 5294 CG2 THR E 77 6.010 8.365 187.996 1.00 43.97 C ANISOU 5294 CG2 THR E 77 3852 7442 5414 -1193 148 814 C ATOM 5295 N LEU E 78 9.268 6.209 190.255 1.00 40.81 N ANISOU 5295 N LEU E 78 4391 6056 5060 -1285 51 424 N ATOM 5296 CA LEU E 78 9.873 4.895 190.520 1.00 40.97 C ANISOU 5296 CA LEU E 78 4670 5792 5105 -1460 -72 414 C ATOM 5297 C LEU E 78 9.014 4.172 191.536 1.00 43.40 C ANISOU 5297 C LEU E 78 4915 6238 5336 -1693 -68 639 C ATOM 5298 O LEU E 78 9.173 4.414 192.722 1.00 43.94 O ANISOU 5298 O LEU E 78 4978 6376 5341 -1588 35 696 O ATOM 5299 CB LEU E 78 11.222 5.068 191.206 1.00 39.00 C ANISOU 5299 CB LEU E 78 4597 5334 4885 -1240 -46 307 C ATOM 5300 CG LEU E 78 12.536 5.382 190.504 1.00 37.46 C ANISOU 5300 CG LEU E 78 4522 4939 4771 -1038 -75 129 C ATOM 5301 CD1 LEU E 78 12.668 6.854 190.187 1.00 35.50 C ANISOU 5301 CD1 LEU E 78 4138 4833 4518 -846 12 46 C ATOM 5302 CD2 LEU E 78 13.682 4.940 191.403 1.00 37.30 C ANISOU 5302 CD2 LEU E 78 4655 4746 4771 -948 -108 145 C ATOM 5303 N GLU E 79 8.167 3.251 191.091 1.00 44.91 N ANISOU 5303 N GLU E 79 5091 6464 5509 -2044 -195 775 N ATOM 5304 CA GLU E 79 7.057 2.732 191.899 1.00 47.36 C ANISOU 5304 CA GLU E 79 5228 7038 5731 -2327 -185 1061 C ATOM 5305 C GLU E 79 7.462 1.795 193.049 1.00 47.15 C ANISOU 5305 C GLU E 79 5426 6815 5675 -2444 -216 1161 C ATOM 5306 O GLU E 79 6.761 1.681 194.056 1.00 49.21 O ANISOU 5306 O GLU E 79 5520 7344 5832 -2563 -132 1394 O ATOM 5307 CB GLU E 79 5.974 2.098 191.000 1.00 51.12 C ANISOU 5307 CB GLU E 79 5591 7654 6179 -2749 -355 1218 C ATOM 5308 CG GLU E 79 6.462 1.636 189.616 1.00 52.21 C ANISOU 5308 CG GLU E 79 6021 7455 6363 -2857 -543 1005 C ATOM 5309 CD GLU E 79 6.486 2.757 188.553 1.00 51.17 C ANISOU 5309 CD GLU E 79 5706 7485 6251 -2618 -494 867 C ATOM 5310 OE1 GLU E 79 5.407 3.160 188.067 1.00 53.37 O ANISOU 5310 OE1 GLU E 79 5650 8149 6480 -2760 -522 1040 O ATOM 5311 OE2 GLU E 79 7.596 3.229 188.208 1.00 48.31 O ANISOU 5311 OE2 GLU E 79 5516 6888 5952 -2295 -434 621 O ATOM 5312 N SER E 80 8.610 1.155 192.900 1.00 44.50 N ANISOU 5312 N SER E 80 5453 6034 5420 -2375 -320 1007 N ATOM 5313 CA SER E 80 9.187 0.355 193.962 1.00 43.57 C ANISOU 5313 CA SER E 80 5562 5699 5292 -2405 -355 1106 C ATOM 5314 C SER E 80 10.699 0.373 193.792 1.00 40.62 C ANISOU 5314 C SER E 80 5433 4981 5019 -2081 -376 900 C ATOM 5315 O SER E 80 11.252 -0.506 193.129 1.00 40.98 O ANISOU 5315 O SER E 80 5776 4648 5147 -2099 -492 819 O ATOM 5316 CB SER E 80 8.672 -1.074 193.874 1.00 46.71 C ANISOU 5316 CB SER E 80 6188 5875 5686 -2832 -537 1279 C ATOM 5317 OG SER E 80 9.305 -1.901 194.821 1.00 47.61 O ANISOU 5317 OG SER E 80 6564 5721 5805 -2836 -587 1390 O ATOM 5318 N ALA E 81 11.347 1.377 194.383 1.00 37.33 N ANISOU 5318 N ALA E 81 4901 4706 4578 -1788 -261 827 N ATOM 5319 CA ALA E 81 12.783 1.618 194.197 1.00 35.41 C ANISOU 5319 CA ALA E 81 4780 4253 4420 -1491 -280 673 C ATOM 5320 C ALA E 81 13.667 0.428 194.511 1.00 36.00 C ANISOU 5320 C ALA E 81 5130 3984 4564 -1461 -393 753 C ATOM 5321 O ALA E 81 13.557 -0.157 195.564 1.00 37.37 O ANISOU 5321 O ALA E 81 5377 4144 4680 -1577 -431 946 O ATOM 5322 CB ALA E 81 13.240 2.822 195.002 1.00 33.63 C ANISOU 5322 CB ALA E 81 4419 4247 4113 -1295 -183 636 C ATOM 5323 N THR E 82 14.504 0.061 193.551 1.00 35.36 N ANISOU 5323 N THR E 82 5207 3631 4598 -1284 -430 617 N ATOM 5324 CA THR E 82 15.439 -1.022 193.725 1.00 37.32 C ANISOU 5324 CA THR E 82 5722 3531 4927 -1144 -504 690 C ATOM 5325 C THR E 82 16.781 -0.382 193.945 1.00 36.45 C ANISOU 5325 C THR E 82 5475 3511 4863 -807 -471 670 C ATOM 5326 O THR E 82 16.949 0.788 193.633 1.00 35.19 O ANISOU 5326 O THR E 82 5093 3594 4684 -726 -406 549 O ATOM 5327 CB THR E 82 15.535 -1.885 192.476 1.00 38.63 C ANISOU 5327 CB THR E 82 6186 3332 5160 -1112 -534 550 C ATOM 5328 OG1 THR E 82 16.303 -1.198 191.489 1.00 36.86 O ANISOU 5328 OG1 THR E 82 5861 3164 4980 -827 -448 353 O ATOM 5329 CG2 THR E 82 14.165 -2.179 191.923 1.00 39.59 C ANISOU 5329 CG2 THR E 82 6381 3454 5209 -1507 -592 526 C ATOM 5330 N SER E 83 17.747 -1.150 194.442 1.00 38.44 N ANISOU 5330 N SER E 83 5856 3570 5179 -620 -528 815 N ATOM 5331 CA SER E 83 19.043 -0.597 194.820 1.00 37.88 C ANISOU 5331 CA SER E 83 5596 3658 5138 -351 -535 882 C ATOM 5332 C SER E 83 19.901 -0.249 193.609 1.00 38.01 C ANISOU 5332 C SER E 83 5530 3666 5247 -65 -456 726 C ATOM 5333 O SER E 83 20.799 0.578 193.709 1.00 38.12 O ANISOU 5333 O SER E 83 5298 3921 5266 72 -455 757 O ATOM 5334 CB SER E 83 19.799 -1.559 195.728 1.00 39.88 C ANISOU 5334 CB SER E 83 5966 3757 5431 -218 -630 1147 C ATOM 5335 OG SER E 83 20.490 -2.507 194.951 1.00 41.61 O ANISOU 5335 OG SER E 83 6382 3642 5787 88 -599 1142 O ATOM 5336 N SER E 84 19.590 -0.845 192.456 1.00 39.10 N ANISOU 5336 N SER E 84 5881 3547 5428 -18 -395 565 N ATOM 5337 CA SER E 84 20.309 -0.580 191.207 1.00 38.47 C ANISOU 5337 CA SER E 84 5755 3467 5396 253 -288 406 C ATOM 5338 C SER E 84 19.962 0.778 190.596 1.00 35.62 C ANISOU 5338 C SER E 84 5143 3413 4979 133 -240 250 C ATOM 5339 O SER E 84 20.577 1.208 189.611 1.00 34.55 O ANISOU 5339 O SER E 84 4911 3357 4860 322 -153 146 O ATOM 5340 CB SER E 84 20.035 -1.691 190.194 1.00 40.31 C ANISOU 5340 CB SER E 84 6386 3297 5635 322 -241 262 C ATOM 5341 OG SER E 84 18.681 -1.660 189.797 1.00 39.26 O ANISOU 5341 OG SER E 84 6374 3127 5416 -58 -289 133 O ATOM 5342 N GLN E 85 18.981 1.458 191.182 1.00 34.70 N ANISOU 5342 N GLN E 85 4924 3474 4788 -156 -282 252 N ATOM 5343 CA GLN E 85 18.534 2.744 190.652 1.00 33.25 C ANISOU 5343 CA GLN E 85 4543 3536 4554 -247 -235 124 C ATOM 5344 C GLN E 85 19.131 3.888 191.432 1.00 32.38 C ANISOU 5344 C GLN E 85 4215 3676 4412 -226 -255 195 C ATOM 5345 O GLN E 85 18.759 5.044 191.208 1.00 31.45 O ANISOU 5345 O GLN E 85 3978 3728 4245 -298 -222 110 O ATOM 5346 CB GLN E 85 17.021 2.840 190.674 1.00 32.71 C ANISOU 5346 CB GLN E 85 4497 3519 4414 -528 -240 89 C ATOM 5347 CG GLN E 85 16.370 1.790 189.840 1.00 35.09 C ANISOU 5347 CG GLN E 85 5031 3588 4714 -651 -268 24 C ATOM 5348 CD GLN E 85 14.889 1.760 190.047 1.00 36.50 C ANISOU 5348 CD GLN E 85 5172 3879 4819 -978 -305 80 C ATOM 5349 OE1 GLN E 85 14.405 1.418 191.136 1.00 37.76 O ANISOU 5349 OE1 GLN E 85 5329 4075 4945 -1130 -336 239 O ATOM 5350 NE2 GLN E 85 14.140 2.135 189.005 1.00 36.62 N ANISOU 5350 NE2 GLN E 85 5123 3999 4793 -1097 -303 -17 N ATOM 5351 N THR E 86 20.012 3.549 192.376 1.00 32.84 N ANISOU 5351 N THR E 86 4254 3741 4481 -145 -327 363 N ATOM 5352 CA THR E 86 20.921 4.503 192.953 1.00 32.36 C ANISOU 5352 CA THR E 86 4011 3902 4381 -131 -388 447 C ATOM 5353 C THR E 86 21.675 5.121 191.779 1.00 32.20 C ANISOU 5353 C THR E 86 3836 3975 4423 10 -334 375 C ATOM 5354 O THR E 86 22.276 4.382 190.998 1.00 34.06 O ANISOU 5354 O THR E 86 4073 4121 4746 236 -273 387 O ATOM 5355 CB THR E 86 21.956 3.803 193.853 1.00 34.44 C ANISOU 5355 CB THR E 86 4243 4174 4668 -24 -494 686 C ATOM 5356 OG1 THR E 86 21.294 2.904 194.747 1.00 36.23 O ANISOU 5356 OG1 THR E 86 4652 4259 4855 -123 -534 780 O ATOM 5357 CG2 THR E 86 22.742 4.809 194.650 1.00 33.68 C ANISOU 5357 CG2 THR E 86 3982 4339 4477 -130 -615 797 C ATOM 5358 N SER E 87 21.606 6.444 191.629 1.00 30.18 N ANISOU 5358 N SER E 87 3481 3878 4107 -110 -339 301 N ATOM 5359 CA SER E 87 22.219 7.119 190.493 1.00 30.11 C ANISOU 5359 CA SER E 87 3326 3974 4139 -29 -290 256 C ATOM 5360 C SER E 87 22.204 8.621 190.685 1.00 29.91 C ANISOU 5360 C SER E 87 3252 4080 4033 -212 -344 225 C ATOM 5361 O SER E 87 21.740 9.135 191.713 1.00 30.32 O ANISOU 5361 O SER E 87 3413 4127 3981 -368 -403 214 O ATOM 5362 CB SER E 87 21.451 6.816 189.198 1.00 29.36 C ANISOU 5362 CB SER E 87 3317 3767 4073 36 -168 84 C ATOM 5363 OG SER E 87 22.299 6.301 188.194 1.00 30.53 O ANISOU 5363 OG SER E 87 3407 3920 4275 261 -87 92 O ATOM 5364 N VAL E 88 22.714 9.315 189.675 1.00 29.98 N ANISOU 5364 N VAL E 88 3134 4188 4069 -186 -314 213 N ATOM 5365 CA VAL E 88 22.515 10.742 189.521 1.00 30.52 C ANISOU 5365 CA VAL E 88 3223 4299 4073 -350 -345 159 C ATOM 5366 C VAL E 88 21.621 10.921 188.288 1.00 30.48 C ANISOU 5366 C VAL E 88 3250 4236 4094 -284 -221 15 C ATOM 5367 O VAL E 88 21.931 10.410 187.211 1.00 31.07 O ANISOU 5367 O VAL E 88 3238 4349 4216 -153 -144 6 O ATOM 5368 CB VAL E 88 23.845 11.491 189.317 1.00 31.73 C ANISOU 5368 CB VAL E 88 3193 4639 4224 -439 -442 317 C ATOM 5369 CG1 VAL E 88 23.624 12.971 189.378 1.00 31.84 C ANISOU 5369 CG1 VAL E 88 3330 4613 4153 -657 -511 268 C ATOM 5370 CG2 VAL E 88 24.837 11.111 190.384 1.00 33.74 C ANISOU 5370 CG2 VAL E 88 3346 5019 4457 -496 -587 515 C ATOM 5371 N TYR E 89 20.516 11.641 188.456 1.00 30.35 N ANISOU 5371 N TYR E 89 3360 4146 4025 -358 -195 -83 N ATOM 5372 CA TYR E 89 19.473 11.730 187.448 1.00 30.43 C ANISOU 5372 CA TYR E 89 3380 4135 4049 -308 -103 -178 C ATOM 5373 C TYR E 89 19.387 13.131 186.873 1.00 31.39 C ANISOU 5373 C TYR E 89 3507 4273 4146 -350 -104 -182 C ATOM 5374 O TYR E 89 19.430 14.114 187.604 1.00 32.82 O ANISOU 5374 O TYR E 89 3804 4394 4273 -425 -149 -174 O ATOM 5375 CB TYR E 89 18.132 11.396 188.082 1.00 30.68 C ANISOU 5375 CB TYR E 89 3498 4114 4045 -323 -58 -226 C ATOM 5376 CG TYR E 89 17.924 9.928 188.390 1.00 31.73 C ANISOU 5376 CG TYR E 89 3659 4196 4202 -320 -60 -214 C ATOM 5377 CD1 TYR E 89 18.328 9.374 189.605 1.00 32.54 C ANISOU 5377 CD1 TYR E 89 3817 4262 4286 -345 -110 -143 C ATOM 5378 CD2 TYR E 89 17.308 9.098 187.473 1.00 32.15 C ANISOU 5378 CD2 TYR E 89 3720 4218 4276 -321 -31 -260 C ATOM 5379 CE1 TYR E 89 18.123 8.032 189.881 1.00 33.08 C ANISOU 5379 CE1 TYR E 89 3948 4241 4380 -348 -120 -106 C ATOM 5380 CE2 TYR E 89 17.113 7.756 187.741 1.00 33.36 C ANISOU 5380 CE2 TYR E 89 3973 4258 4442 -353 -51 -247 C ATOM 5381 CZ TYR E 89 17.519 7.231 188.941 1.00 33.57 C ANISOU 5381 CZ TYR E 89 4055 4226 4475 -354 -89 -163 C ATOM 5382 OH TYR E 89 17.305 5.897 189.178 1.00 35.01 O ANISOU 5382 OH TYR E 89 4372 4256 4675 -392 -117 -128 O ATOM 5383 N PHE E 90 19.237 13.240 185.559 1.00 31.70 N ANISOU 5383 N PHE E 90 3470 4372 4205 -306 -58 -194 N ATOM 5384 CA PHE E 90 19.238 14.559 184.943 1.00 31.26 C ANISOU 5384 CA PHE E 90 3425 4322 4132 -347 -70 -157 C ATOM 5385 C PHE E 90 18.052 14.762 184.041 1.00 31.15 C ANISOU 5385 C PHE E 90 3396 4330 4108 -284 -12 -186 C ATOM 5386 O PHE E 90 17.718 13.912 183.241 1.00 30.31 O ANISOU 5386 O PHE E 90 3224 4300 3993 -257 18 -221 O ATOM 5387 CB PHE E 90 20.501 14.790 184.131 1.00 31.09 C ANISOU 5387 CB PHE E 90 3275 4421 4116 -391 -96 -61 C ATOM 5388 CG PHE E 90 21.745 14.892 184.950 1.00 31.11 C ANISOU 5388 CG PHE E 90 3230 4469 4122 -495 -190 43 C ATOM 5389 CD1 PHE E 90 22.169 16.110 185.440 1.00 31.84 C ANISOU 5389 CD1 PHE E 90 3421 4501 4174 -685 -304 117 C ATOM 5390 CD2 PHE E 90 22.525 13.778 185.187 1.00 31.26 C ANISOU 5390 CD2 PHE E 90 3116 4591 4172 -412 -178 91 C ATOM 5391 CE1 PHE E 90 23.346 16.206 186.184 1.00 32.56 C ANISOU 5391 CE1 PHE E 90 3449 4680 4243 -851 -437 248 C ATOM 5392 CE2 PHE E 90 23.697 13.878 185.915 1.00 32.74 C ANISOU 5392 CE2 PHE E 90 3195 4886 4358 -514 -286 245 C ATOM 5393 CZ PHE E 90 24.103 15.096 186.418 1.00 33.02 C ANISOU 5393 CZ PHE E 90 3299 4906 4339 -764 -431 329 C ATOM 5394 N CYS E 91 17.427 15.916 184.196 1.00 32.48 N ANISOU 5394 N CYS E 91 3654 4423 4264 -261 -6 -161 N ATOM 5395 CA CYS E 91 16.360 16.340 183.342 1.00 33.35 C ANISOU 5395 CA CYS E 91 3717 4587 4370 -182 34 -124 C ATOM 5396 C CYS E 91 16.954 17.170 182.201 1.00 33.94 C ANISOU 5396 C CYS E 91 3769 4690 4435 -226 -4 -37 C ATOM 5397 O CYS E 91 17.848 17.983 182.434 1.00 34.67 O ANISOU 5397 O CYS E 91 3957 4688 4529 -311 -55 10 O ATOM 5398 CB CYS E 91 15.438 17.228 184.150 1.00 35.38 C ANISOU 5398 CB CYS E 91 4094 4733 4616 -60 90 -112 C ATOM 5399 SG CYS E 91 13.995 17.635 183.209 1.00 38.77 S ANISOU 5399 SG CYS E 91 4385 5295 5052 90 142 0 S ATOM 5400 N ALA E 92 16.463 16.991 180.978 1.00 33.20 N ANISOU 5400 N ALA E 92 3564 4740 4311 -209 3 4 N ATOM 5401 CA ALA E 92 16.926 17.830 179.873 1.00 33.92 C ANISOU 5401 CA ALA E 92 3636 4882 4369 -254 -27 117 C ATOM 5402 C ALA E 92 15.820 18.412 178.991 1.00 34.89 C ANISOU 5402 C ALA E 92 3713 5079 4465 -180 -36 226 C ATOM 5403 O ALA E 92 14.675 17.968 179.021 1.00 35.29 O ANISOU 5403 O ALA E 92 3683 5215 4511 -112 -24 222 O ATOM 5404 CB ALA E 92 17.973 17.112 179.017 1.00 34.13 C ANISOU 5404 CB ALA E 92 3563 5072 4333 -329 -12 103 C ATOM 5405 N ILE E 93 16.201 19.374 178.165 1.00 35.12 N ANISOU 5405 N ILE E 93 3766 5109 4468 -219 -71 362 N ATOM 5406 CA ILE E 93 15.262 20.257 177.516 1.00 35.96 C ANISOU 5406 CA ILE E 93 3866 5228 4570 -119 -95 522 C ATOM 5407 C ILE E 93 15.728 20.550 176.108 1.00 36.73 C ANISOU 5407 C ILE E 93 3901 5487 4568 -229 -141 654 C ATOM 5408 O ILE E 93 16.894 20.866 175.887 1.00 36.29 O ANISOU 5408 O ILE E 93 3884 5415 4489 -361 -149 692 O ATOM 5409 CB ILE E 93 15.204 21.559 178.305 1.00 37.58 C ANISOU 5409 CB ILE E 93 4295 5129 4854 -16 -89 586 C ATOM 5410 CG1 ILE E 93 13.940 21.666 179.080 1.00 38.38 C ANISOU 5410 CG1 ILE E 93 4411 5170 5004 228 -14 575 C ATOM 5411 CG2 ILE E 93 15.160 22.841 177.451 1.00 39.76 C ANISOU 5411 CG2 ILE E 93 4669 5315 5125 7 -142 802 C ATOM 5412 CD1 ILE E 93 13.848 23.086 179.431 1.00 41.66 C ANISOU 5412 CD1 ILE E 93 5102 5270 5458 376 3 662 C ATOM 5413 N SER E 94 14.806 20.430 175.158 1.00 37.43 N ANISOU 5413 N SER E 94 3870 5772 4578 -196 -177 751 N ATOM 5414 CA SER E 94 15.091 20.703 173.773 1.00 37.91 C ANISOU 5414 CA SER E 94 3882 6021 4502 -299 -223 891 C ATOM 5415 C SER E 94 13.952 21.511 173.230 1.00 38.98 C ANISOU 5415 C SER E 94 3964 6207 4637 -185 -294 1121 C ATOM 5416 O SER E 94 12.809 21.214 173.523 1.00 38.39 O ANISOU 5416 O SER E 94 3782 6207 4598 -71 -308 1137 O ATOM 5417 CB SER E 94 15.111 19.381 173.019 1.00 38.40 C ANISOU 5417 CB SER E 94 3860 6340 4391 -407 -217 753 C ATOM 5418 OG SER E 94 16.135 19.348 172.059 1.00 40.35 O ANISOU 5418 OG SER E 94 4114 6732 4486 -515 -180 776 O ATOM 5419 N GLU E 95 14.256 22.510 172.414 1.00 40.38 N ANISOU 5419 N GLU E 95 4193 6379 4772 -219 -342 1337 N ATOM 5420 CA GLU E 95 13.224 23.215 171.658 1.00 41.60 C ANISOU 5420 CA GLU E 95 4272 6637 4899 -107 -426 1608 C ATOM 5421 C GLU E 95 12.634 22.359 170.561 1.00 40.65 C ANISOU 5421 C GLU E 95 3962 6912 4574 -230 -508 1636 C ATOM 5422 O GLU E 95 13.313 21.493 170.014 1.00 40.08 O ANISOU 5422 O GLU E 95 3897 7001 4331 -422 -490 1476 O ATOM 5423 CB GLU E 95 13.806 24.438 171.028 1.00 44.34 C ANISOU 5423 CB GLU E 95 4754 6861 5232 -152 -470 1846 C ATOM 5424 CG GLU E 95 14.543 25.237 172.012 1.00 46.88 C ANISOU 5424 CG GLU E 95 5327 6780 5705 -137 -429 1806 C ATOM 5425 CD GLU E 95 14.024 26.641 172.050 1.00 51.59 C ANISOU 5425 CD GLU E 95 6125 7074 6403 55 -470 2058 C ATOM 5426 OE1 GLU E 95 13.884 27.267 170.965 1.00 54.16 O ANISOU 5426 OE1 GLU E 95 6430 7495 6652 26 -553 2338 O ATOM 5427 OE2 GLU E 95 13.733 27.113 173.174 1.00 52.98 O ANISOU 5427 OE2 GLU E 95 6508 6902 6719 255 -411 1977 O ATOM 5428 N VAL E 96 11.367 22.613 170.258 1.00 40.47 N ANISOU 5428 N VAL E 96 3781 7046 4551 -110 -597 1851 N ATOM 5429 CA VAL E 96 10.643 21.863 169.252 1.00 40.42 C ANISOU 5429 CA VAL E 96 3596 7433 4328 -276 -729 1917 C ATOM 5430 C VAL E 96 11.129 22.213 167.866 1.00 41.41 C ANISOU 5430 C VAL E 96 3765 7743 4225 -441 -807 2070 C ATOM 5431 O VAL E 96 10.998 23.349 167.414 1.00 43.17 O ANISOU 5431 O VAL E 96 3990 7934 4480 -339 -858 2373 O ATOM 5432 CB VAL E 96 9.148 22.162 169.294 1.00 42.34 C ANISOU 5432 CB VAL E 96 3591 7862 4635 -107 -825 2193 C ATOM 5433 CG1 VAL E 96 8.429 21.265 168.319 1.00 43.32 C ANISOU 5433 CG1 VAL E 96 3538 8417 4506 -375 -1008 2253 C ATOM 5434 CG2 VAL E 96 8.625 21.943 170.681 1.00 41.19 C ANISOU 5434 CG2 VAL E 96 3384 7566 4698 94 -713 2086 C ATOM 5435 N GLY E 97 11.700 21.223 167.199 1.00 40.35 N ANISOU 5435 N GLY E 97 3698 7790 3845 -681 -803 1863 N ATOM 5436 CA GLY E 97 12.232 21.412 165.869 1.00 41.61 C ANISOU 5436 CA GLY E 97 3915 8170 3725 -848 -841 1972 C ATOM 5437 C GLY E 97 13.044 20.219 165.445 1.00 40.41 C ANISOU 5437 C GLY E 97 3903 8126 3323 -1023 -747 1651 C ATOM 5438 O GLY E 97 12.874 19.132 165.958 1.00 39.38 O ANISOU 5438 O GLY E 97 3821 7946 3195 -1057 -722 1380 O ATOM 5439 N VAL E 98 13.915 20.403 164.475 1.00 41.85 N ANISOU 5439 N VAL E 98 4168 8463 3269 -1120 -683 1695 N ATOM 5440 CA VAL E 98 14.739 19.302 164.030 1.00 41.63 C ANISOU 5440 CA VAL E 98 4298 8542 2978 -1207 -541 1394 C ATOM 5441 C VAL E 98 16.205 19.618 164.329 1.00 40.52 C ANISOU 5441 C VAL E 98 4165 8306 2926 -1120 -323 1366 C ATOM 5442 O VAL E 98 16.739 20.626 163.866 1.00 41.38 O ANISOU 5442 O VAL E 98 4217 8491 3015 -1154 -307 1631 O ATOM 5443 CB VAL E 98 14.528 18.994 162.520 1.00 45.04 C ANISOU 5443 CB VAL E 98 4831 9333 2950 -1402 -618 1435 C ATOM 5444 CG1 VAL E 98 15.275 17.757 162.135 1.00 45.72 C ANISOU 5444 CG1 VAL E 98 5153 9474 2744 -1432 -442 1074 C ATOM 5445 CG2 VAL E 98 13.053 18.791 162.200 1.00 46.60 C ANISOU 5445 CG2 VAL E 98 4970 9684 3052 -1550 -890 1543 C ATOM 5446 N GLY E 99 16.837 18.763 165.129 1.00 38.59 N ANISOU 5446 N GLY E 99 3972 7906 2783 -1025 -174 1082 N ATOM 5447 CA GLY E 99 18.252 18.884 165.441 1.00 38.61 C ANISOU 5447 CA GLY E 99 3930 7888 2854 -950 26 1068 C ATOM 5448 C GLY E 99 18.610 19.964 166.438 1.00 38.04 C ANISOU 5448 C GLY E 99 3749 7582 3122 -927 -8 1255 C ATOM 5449 O GLY E 99 19.710 20.514 166.396 1.00 38.73 O ANISOU 5449 O GLY E 99 3759 7733 3226 -971 82 1403 O ATOM 5450 N GLN E 100 17.691 20.256 167.355 1.00 37.44 N ANISOU 5450 N GLN E 100 3683 7246 3297 -870 -137 1254 N ATOM 5451 CA GLN E 100 17.916 21.284 168.363 1.00 36.65 C ANISOU 5451 CA GLN E 100 3579 6860 3486 -841 -176 1389 C ATOM 5452 C GLN E 100 18.698 20.740 169.557 1.00 34.91 C ANISOU 5452 C GLN E 100 3356 6476 3432 -790 -80 1190 C ATOM 5453 O GLN E 100 18.430 19.627 169.989 1.00 33.25 O ANISOU 5453 O GLN E 100 3162 6245 3226 -709 -35 943 O ATOM 5454 CB GLN E 100 16.568 21.843 168.808 1.00 36.85 C ANISOU 5454 CB GLN E 100 3630 6700 3671 -739 -313 1480 C ATOM 5455 CG GLN E 100 15.881 22.616 167.709 1.00 39.77 C ANISOU 5455 CG GLN E 100 3976 7222 3915 -771 -431 1768 C ATOM 5456 CD GLN E 100 16.822 23.540 166.968 1.00 41.62 C ANISOU 5456 CD GLN E 100 4239 7516 4057 -907 -421 2017 C ATOM 5457 OE1 GLN E 100 17.405 24.448 167.556 1.00 42.18 O ANISOU 5457 OE1 GLN E 100 4396 7331 4301 -934 -425 2136 O ATOM 5458 NE2 GLN E 100 16.959 23.327 165.665 1.00 43.56 N ANISOU 5458 NE2 GLN E 100 4440 8108 4005 -1026 -418 2110 N ATOM 5459 N PRO E 101 19.660 21.527 170.091 1.00 35.05 N ANISOU 5459 N PRO E 101 3365 6377 3575 -872 -74 1322 N ATOM 5460 CA PRO E 101 20.484 21.136 171.252 1.00 33.75 C ANISOU 5460 CA PRO E 101 3175 6092 3557 -862 -22 1194 C ATOM 5461 C PRO E 101 19.716 20.948 172.576 1.00 32.42 C ANISOU 5461 C PRO E 101 3115 5617 3588 -751 -77 1022 C ATOM 5462 O PRO E 101 18.775 21.679 172.876 1.00 33.02 O ANISOU 5462 O PRO E 101 3303 5486 3757 -697 -163 1082 O ATOM 5463 CB PRO E 101 21.466 22.304 171.396 1.00 35.18 C ANISOU 5463 CB PRO E 101 3349 6222 3797 -1065 -79 1451 C ATOM 5464 CG PRO E 101 20.797 23.469 170.768 1.00 36.63 C ANISOU 5464 CG PRO E 101 3657 6296 3966 -1126 -192 1675 C ATOM 5465 CD PRO E 101 19.933 22.916 169.664 1.00 36.92 C ANISOU 5465 CD PRO E 101 3643 6565 3822 -1017 -160 1637 C ATOM 5466 N GLN E 102 20.126 19.964 173.361 1.00 31.64 N ANISOU 5466 N GLN E 102 2979 5505 3540 -689 -9 829 N ATOM 5467 CA GLN E 102 19.486 19.687 174.632 1.00 29.53 C ANISOU 5467 CA GLN E 102 2802 4992 3426 -601 -44 676 C ATOM 5468 C GLN E 102 20.194 20.413 175.766 1.00 29.54 C ANISOU 5468 C GLN E 102 2881 4787 3557 -695 -103 731 C ATOM 5469 O GLN E 102 21.402 20.300 175.886 1.00 29.94 O ANISOU 5469 O GLN E 102 2828 4952 3595 -804 -87 791 O ATOM 5470 CB GLN E 102 19.489 18.198 174.915 1.00 28.19 C ANISOU 5470 CB GLN E 102 2593 4888 3230 -503 37 454 C ATOM 5471 CG GLN E 102 18.411 17.457 174.199 1.00 28.57 C ANISOU 5471 CG GLN E 102 2666 5024 3166 -456 36 352 C ATOM 5472 CD GLN E 102 18.496 15.955 174.415 1.00 28.55 C ANISOU 5472 CD GLN E 102 2706 5024 3118 -394 106 133 C ATOM 5473 OE1 GLN E 102 19.162 15.476 175.336 1.00 28.03 O ANISOU 5473 OE1 GLN E 102 2638 4862 3152 -337 151 61 O ATOM 5474 NE2 GLN E 102 17.824 15.202 173.560 1.00 29.52 N ANISOU 5474 NE2 GLN E 102 2899 5242 3076 -420 96 37 N ATOM 5475 N HIS E 103 19.452 21.160 176.588 1.00 29.08 N ANISOU 5475 N HIS E 103 3007 4442 3599 -653 -168 723 N ATOM 5476 CA HIS E 103 20.056 21.856 177.727 1.00 29.56 C ANISOU 5476 CA HIS E 103 3235 4260 3735 -773 -244 739 C ATOM 5477 C HIS E 103 19.673 21.112 178.995 1.00 28.26 C ANISOU 5477 C HIS E 103 3123 3987 3628 -662 -213 536 C ATOM 5478 O HIS E 103 18.553 20.639 179.113 1.00 27.63 O ANISOU 5478 O HIS E 103 3037 3898 3565 -480 -154 434 O ATOM 5479 CB HIS E 103 19.640 23.329 177.765 1.00 31.17 C ANISOU 5479 CB HIS E 103 3710 4164 3968 -801 -324 869 C ATOM 5480 CG HIS E 103 20.016 24.088 176.525 1.00 33.89 C ANISOU 5480 CG HIS E 103 4019 4607 4252 -938 -370 1109 C ATOM 5481 ND1 HIS E 103 21.193 24.805 176.417 1.00 35.64 N ANISOU 5481 ND1 HIS E 103 4280 4815 4445 -1241 -467 1292 N ATOM 5482 CD2 HIS E 103 19.384 24.219 175.330 1.00 34.02 C ANISOU 5482 CD2 HIS E 103 3947 4770 4209 -846 -346 1226 C ATOM 5483 CE1 HIS E 103 21.262 25.355 175.216 1.00 37.14 C ANISOU 5483 CE1 HIS E 103 4417 5127 4567 -1317 -483 1511 C ATOM 5484 NE2 HIS E 103 20.180 25.013 174.536 1.00 36.41 N ANISOU 5484 NE2 HIS E 103 4255 5131 4449 -1072 -411 1469 N ATOM 5485 N PHE E 104 20.602 20.980 179.936 1.00 28.26 N ANISOU 5485 N PHE E 104 3148 3945 3645 -796 -265 511 N ATOM 5486 CA PHE E 104 20.391 20.070 181.059 1.00 26.14 C ANISOU 5486 CA PHE E 104 2888 3639 3406 -707 -235 344 C ATOM 5487 C PHE E 104 20.129 20.737 182.410 1.00 27.44 C ANISOU 5487 C PHE E 104 3342 3511 3572 -737 -293 274 C ATOM 5488 O PHE E 104 20.668 21.800 182.706 1.00 28.87 O ANISOU 5488 O PHE E 104 3733 3512 3723 -923 -402 351 O ATOM 5489 CB PHE E 104 21.619 19.223 181.242 1.00 25.91 C ANISOU 5489 CB PHE E 104 2658 3814 3372 -796 -245 374 C ATOM 5490 CG PHE E 104 21.732 18.081 180.298 1.00 25.04 C ANISOU 5490 CG PHE E 104 2327 3951 3238 -658 -128 343 C ATOM 5491 CD1 PHE E 104 22.367 18.233 179.081 1.00 26.44 C ANISOU 5491 CD1 PHE E 104 2348 4349 3350 -695 -84 471 C ATOM 5492 CD2 PHE E 104 21.291 16.840 180.662 1.00 23.83 C ANISOU 5492 CD2 PHE E 104 2156 3798 3102 -506 -61 192 C ATOM 5493 CE1 PHE E 104 22.503 17.183 178.234 1.00 26.47 C ANISOU 5493 CE1 PHE E 104 2220 4551 3285 -545 45 412 C ATOM 5494 CE2 PHE E 104 21.427 15.778 179.817 1.00 24.61 C ANISOU 5494 CE2 PHE E 104 2147 4052 3151 -383 43 137 C ATOM 5495 CZ PHE E 104 22.028 15.946 178.597 1.00 25.76 C ANISOU 5495 CZ PHE E 104 2175 4402 3210 -385 106 229 C ATOM 5496 N GLY E 105 19.362 20.055 183.260 1.00 27.08 N ANISOU 5496 N GLY E 105 3331 3425 3535 -583 -223 128 N ATOM 5497 CA GLY E 105 19.160 20.472 184.645 1.00 29.36 C ANISOU 5497 CA GLY E 105 3897 3483 3776 -590 -246 35 C ATOM 5498 C GLY E 105 20.401 20.278 185.507 1.00 31.15 C ANISOU 5498 C GLY E 105 4147 3731 3958 -833 -378 53 C ATOM 5499 O GLY E 105 21.449 19.887 185.006 1.00 31.37 O ANISOU 5499 O GLY E 105 3938 3968 4012 -971 -441 170 O ATOM 5500 N ASP E 106 20.286 20.541 186.809 1.00 32.97 N ANISOU 5500 N ASP E 106 4650 3779 4098 -875 -414 -44 N ATOM 5501 CA ASP E 106 21.449 20.543 187.702 1.00 34.74 C ANISOU 5501 CA ASP E 106 4936 4020 4242 -1162 -590 3 C ATOM 5502 C ASP E 106 21.698 19.195 188.372 1.00 33.31 C ANISOU 5502 C ASP E 106 4537 4047 4073 -1119 -580 -11 C ATOM 5503 O ASP E 106 22.718 18.993 189.017 1.00 34.43 O ANISOU 5503 O ASP E 106 4628 4289 4163 -1332 -733 81 O ATOM 5504 CB ASP E 106 21.297 21.624 188.770 1.00 38.63 C ANISOU 5504 CB ASP E 106 5925 4180 4574 -1284 -667 -98 C ATOM 5505 CG ASP E 106 21.826 22.976 188.322 1.00 42.77 C ANISOU 5505 CG ASP E 106 6711 4482 5059 -1531 -809 -8 C ATOM 5506 OD1 ASP E 106 22.712 23.016 187.426 1.00 43.81 O ANISOU 5506 OD1 ASP E 106 6574 4807 5266 -1728 -908 188 O ATOM 5507 OD2 ASP E 106 21.368 24.005 188.889 1.00 45.59 O ANISOU 5507 OD2 ASP E 106 7570 4460 5292 -1527 -814 -124 O ATOM 5508 N GLY E 107 20.753 18.278 188.235 1.00 31.74 N ANISOU 5508 N GLY E 107 4212 3912 3934 -861 -419 -95 N ATOM 5509 CA GLY E 107 20.928 16.930 188.754 1.00 31.40 C ANISOU 5509 CA GLY E 107 3992 4023 3918 -809 -405 -91 C ATOM 5510 C GLY E 107 20.216 16.597 190.039 1.00 31.81 C ANISOU 5510 C GLY E 107 4220 3993 3872 -756 -363 -189 C ATOM 5511 O GLY E 107 20.070 17.446 190.912 1.00 34.09 O ANISOU 5511 O GLY E 107 4809 4123 4019 -833 -397 -255 O ATOM 5512 N THR E 108 19.781 15.349 190.146 1.00 30.53 N ANISOU 5512 N THR E 108 3906 3930 3764 -635 -287 -195 N ATOM 5513 CA THR E 108 19.197 14.828 191.368 1.00 31.34 C ANISOU 5513 CA THR E 108 4122 4014 3770 -610 -248 -237 C ATOM 5514 C THR E 108 19.936 13.558 191.755 1.00 31.66 C ANISOU 5514 C THR E 108 4010 4165 3855 -649 -328 -135 C ATOM 5515 O THR E 108 20.022 12.606 190.972 1.00 30.96 O ANISOU 5515 O THR E 108 3737 4133 3894 -553 -291 -97 O ATOM 5516 CB THR E 108 17.685 14.546 191.204 1.00 30.67 C ANISOU 5516 CB THR E 108 4015 3939 3699 -434 -69 -300 C ATOM 5517 OG1 THR E 108 16.979 15.791 191.226 1.00 31.37 O ANISOU 5517 OG1 THR E 108 4286 3921 3713 -340 21 -370 O ATOM 5518 CG2 THR E 108 17.140 13.636 192.336 1.00 30.48 C ANISOU 5518 CG2 THR E 108 4018 3970 3594 -430 -22 -286 C ATOM 5519 N ARG E 109 20.493 13.560 192.959 1.00 33.47 N ANISOU 5519 N ARG E 109 4352 4407 3960 -782 -443 -85 N ATOM 5520 CA ARG E 109 21.274 12.428 193.428 1.00 34.52 C ANISOU 5520 CA ARG E 109 4340 4646 4129 -801 -539 61 C ATOM 5521 C ARG E 109 20.463 11.558 194.387 1.00 34.68 C ANISOU 5521 C ARG E 109 4451 4648 4078 -760 -478 57 C ATOM 5522 O ARG E 109 20.064 11.995 195.462 1.00 35.50 O ANISOU 5522 O ARG E 109 4763 4733 3992 -844 -479 11 O ATOM 5523 CB ARG E 109 22.574 12.896 194.083 1.00 36.72 C ANISOU 5523 CB ARG E 109 4617 5021 4314 -1015 -756 198 C ATOM 5524 CG ARG E 109 23.413 11.730 194.497 1.00 38.51 C ANISOU 5524 CG ARG E 109 4642 5391 4597 -979 -853 401 C ATOM 5525 CD ARG E 109 24.725 12.094 195.137 1.00 41.49 C ANISOU 5525 CD ARG E 109 4935 5947 4882 -1207 -1097 605 C ATOM 5526 NE ARG E 109 25.337 10.875 195.654 1.00 43.00 N ANISOU 5526 NE ARG E 109 4938 6274 5128 -1106 -1169 826 N ATOM 5527 CZ ARG E 109 26.529 10.808 196.236 1.00 45.86 C ANISOU 5527 CZ ARG E 109 5120 6866 5439 -1246 -1389 1093 C ATOM 5528 NH1 ARG E 109 27.275 11.904 196.386 1.00 48.10 N ANISOU 5528 NH1 ARG E 109 5394 7281 5602 -1563 -1587 1170 N ATOM 5529 NH2 ARG E 109 26.974 9.635 196.659 1.00 46.56 N ANISOU 5529 NH2 ARG E 109 5042 7053 5596 -1082 -1428 1310 N ATOM 5530 N LEU E 110 20.241 10.311 193.988 1.00 34.58 N ANISOU 5530 N LEU E 110 4311 4630 4197 -642 -423 110 N ATOM 5531 CA LEU E 110 19.307 9.438 194.680 1.00 34.65 C ANISOU 5531 CA LEU E 110 4393 4612 4159 -634 -356 128 C ATOM 5532 C LEU E 110 19.987 8.179 195.208 1.00 35.86 C ANISOU 5532 C LEU E 110 4506 4760 4358 -622 -455 302 C ATOM 5533 O LEU E 110 20.559 7.424 194.445 1.00 36.20 O ANISOU 5533 O LEU E 110 4444 4753 4558 -498 -466 359 O ATOM 5534 CB LEU E 110 18.193 9.083 193.713 1.00 33.56 C ANISOU 5534 CB LEU E 110 4203 4430 4119 -556 -218 46 C ATOM 5535 CG LEU E 110 17.130 8.087 194.114 1.00 34.67 C ANISOU 5535 CG LEU E 110 4372 4561 4241 -597 -155 98 C ATOM 5536 CD1 LEU E 110 16.448 8.503 195.410 1.00 36.80 C ANISOU 5536 CD1 LEU E 110 4739 4930 4313 -662 -93 119 C ATOM 5537 CD2 LEU E 110 16.119 8.004 193.012 1.00 33.54 C ANISOU 5537 CD2 LEU E 110 4150 4421 4174 -580 -66 31 C ATOM 5538 N SER E 111 19.928 7.974 196.523 1.00 37.23 N ANISOU 5538 N SER E 111 4788 4982 4377 -726 -515 395 N ATOM 5539 CA SER E 111 20.478 6.774 197.162 1.00 38.42 C ANISOU 5539 CA SER E 111 4922 5121 4557 -712 -619 602 C ATOM 5540 C SER E 111 19.363 5.851 197.643 1.00 38.95 C ANISOU 5540 C SER E 111 5094 5117 4587 -754 -538 644 C ATOM 5541 O SER E 111 18.473 6.261 198.414 1.00 38.89 O ANISOU 5541 O SER E 111 5184 5196 4394 -864 -461 603 O ATOM 5542 CB SER E 111 21.364 7.137 198.359 1.00 40.83 C ANISOU 5542 CB SER E 111 5260 5569 4685 -849 -798 744 C ATOM 5543 OG SER E 111 22.714 7.362 197.981 1.00 42.23 O ANISOU 5543 OG SER E 111 5255 5843 4949 -818 -939 860 O ATOM 5544 N ILE E 112 19.409 4.602 197.175 1.00 39.00 N ANISOU 5544 N ILE E 112 5099 4964 4756 -666 -545 735 N ATOM 5545 CA ILE E 112 18.420 3.590 197.538 1.00 39.35 C ANISOU 5545 CA ILE E 112 5258 4908 4783 -763 -505 816 C ATOM 5546 C ILE E 112 19.102 2.436 198.254 1.00 41.63 C ANISOU 5546 C ILE E 112 5628 5088 5103 -730 -631 1062 C ATOM 5547 O ILE E 112 20.005 1.799 197.714 1.00 43.04 O ANISOU 5547 O ILE E 112 5795 5116 5443 -534 -684 1130 O ATOM 5548 CB ILE E 112 17.614 3.109 196.321 1.00 38.31 C ANISOU 5548 CB ILE E 112 5148 4623 4786 -758 -418 701 C ATOM 5549 CG1 ILE E 112 16.872 4.291 195.701 1.00 35.97 C ANISOU 5549 CG1 ILE E 112 4743 4476 4447 -781 -303 512 C ATOM 5550 CG2 ILE E 112 16.600 2.048 196.738 1.00 39.99 C ANISOU 5550 CG2 ILE E 112 5484 4743 4967 -944 -416 828 C ATOM 5551 CD1 ILE E 112 16.844 4.252 194.225 1.00 35.12 C ANISOU 5551 CD1 ILE E 112 4600 4265 4477 -700 -270 375 C ATOM 5552 N LEU E 113 18.684 2.197 199.492 1.00 43.08 N ANISOU 5552 N LEU E 113 5893 5362 5113 -893 -665 1213 N ATOM 5553 CA LEU E 113 19.438 1.351 200.417 1.00 45.68 C ANISOU 5553 CA LEU E 113 6284 5653 5419 -877 -815 1490 C ATOM 5554 C LEU E 113 18.610 0.180 200.918 1.00 48.08 C ANISOU 5554 C LEU E 113 6756 5810 5702 -1019 -814 1667 C ATOM 5555 O LEU E 113 17.398 0.297 201.094 1.00 47.60 O ANISOU 5555 O LEU E 113 6720 5835 5531 -1216 -706 1619 O ATOM 5556 CB LEU E 113 19.921 2.179 201.616 1.00 45.39 C ANISOU 5556 CB LEU E 113 6219 5896 5133 -989 -911 1564 C ATOM 5557 CG LEU E 113 20.764 3.426 201.334 1.00 43.50 C ANISOU 5557 CG LEU E 113 5856 5813 4860 -952 -962 1428 C ATOM 5558 CD1 LEU E 113 21.239 4.013 202.631 1.00 45.05 C ANISOU 5558 CD1 LEU E 113 6111 6236 4768 -1131 -1108 1533 C ATOM 5559 CD2 LEU E 113 21.951 3.104 200.441 1.00 43.29 C ANISOU 5559 CD2 LEU E 113 5656 5713 5077 -723 -1039 1505 C ATOM 5560 N GLU E 114 19.267 -0.946 201.162 1.00 51.16 N ANISOU 5560 N GLU E 114 7252 5991 6197 -917 -935 1905 N ATOM 5561 CA GLU E 114 18.552 -2.121 201.627 1.00 55.01 C ANISOU 5561 CA GLU E 114 7947 6282 6673 -1081 -962 2108 C ATOM 5562 C GLU E 114 18.132 -1.963 203.094 1.00 56.25 C ANISOU 5562 C GLU E 114 8108 6714 6549 -1323 -995 2303 C ATOM 5563 O GLU E 114 17.085 -2.462 203.508 1.00 57.49 O ANISOU 5563 O GLU E 114 8360 6874 6609 -1570 -948 2413 O ATOM 5564 CB GLU E 114 19.350 -3.422 201.378 1.00 59.15 C ANISOU 5564 CB GLU E 114 8655 6418 7402 -855 -1068 2306 C ATOM 5565 CG GLU E 114 20.676 -3.594 202.139 1.00 62.66 C ANISOU 5565 CG GLU E 114 9015 6946 7847 -635 -1217 2581 C ATOM 5566 CD GLU E 114 21.069 -5.070 202.310 1.00 67.90 C ANISOU 5566 CD GLU E 114 9931 7214 8655 -465 -1312 2879 C ATOM 5567 OE1 GLU E 114 20.497 -5.928 201.595 1.00 69.43 O ANISOU 5567 OE1 GLU E 114 10408 6994 8977 -473 -1257 2806 O ATOM 5568 OE2 GLU E 114 21.942 -5.377 203.164 1.00 70.90 O ANISOU 5568 OE2 GLU E 114 10252 7680 9006 -334 -1456 3199 O ATOM 5569 N ASP E 115 18.930 -1.210 203.846 1.00 55.61 N ANISOU 5569 N ASP E 115 7923 6896 6309 -1280 -1074 2344 N ATOM 5570 CA ASP E 115 18.664 -0.961 205.242 1.00 56.43 C ANISOU 5570 CA ASP E 115 8070 7280 6089 -1493 -1107 2498 C ATOM 5571 C ASP E 115 18.944 0.497 205.575 1.00 54.23 C ANISOU 5571 C ASP E 115 7712 7308 5586 -1518 -1083 2291 C ATOM 5572 O ASP E 115 20.047 0.995 205.342 1.00 53.35 O ANISOU 5572 O ASP E 115 7502 7233 5534 -1398 -1208 2257 O ATOM 5573 CB ASP E 115 19.547 -1.858 206.106 1.00 60.36 C ANISOU 5573 CB ASP E 115 8637 7730 6567 -1462 -1322 2875 C ATOM 5574 CG ASP E 115 19.129 -1.855 207.569 1.00 63.42 C ANISOU 5574 CG ASP E 115 9120 8387 6591 -1725 -1357 3082 C ATOM 5575 OD1 ASP E 115 17.943 -1.571 207.855 1.00 63.52 O ANISOU 5575 OD1 ASP E 115 9174 8547 6414 -1920 -1176 2987 O ATOM 5576 OD2 ASP E 115 19.983 -2.151 208.433 1.00 66.38 O ANISOU 5576 OD2 ASP E 115 9511 8856 6853 -1726 -1561 3366 O ATOM 5577 N LEU E 116 17.954 1.163 206.162 1.00 57.33 N ANISOU 5577 N LEU E 116 7304 6764 7714 -2131 -1012 -159 N ATOM 5578 CA LEU E 116 18.104 2.547 206.575 1.00 54.30 C ANISOU 5578 CA LEU E 116 6837 6611 7183 -1908 -858 -107 C ATOM 5579 C LEU E 116 18.842 2.703 207.885 1.00 53.88 C ANISOU 5579 C LEU E 116 7051 6423 6999 -1949 -765 97 C ATOM 5580 O LEU E 116 19.085 3.814 208.306 1.00 52.79 O ANISOU 5580 O LEU E 116 6890 6437 6730 -1785 -632 128 O ATOM 5581 CB LEU E 116 16.742 3.235 206.693 1.00 55.30 C ANISOU 5581 CB LEU E 116 6608 7078 7326 -1988 -676 -163 C ATOM 5582 CG LEU E 116 15.996 3.563 205.394 1.00 55.22 C ANISOU 5582 CG LEU E 116 6272 7292 7416 -1863 -803 -339 C ATOM 5583 CD1 LEU E 116 14.791 4.464 205.635 1.00 56.16 C ANISOU 5583 CD1 LEU E 116 5998 7728 7612 -1853 -634 -379 C ATOM 5584 CD2 LEU E 116 16.930 4.173 204.343 1.00 52.48 C ANISOU 5584 CD2 LEU E 116 6016 6935 6990 -1516 -971 -400 C ATOM 5585 N ASN E 117 19.205 1.605 208.539 1.00 56.57 N ANISOU 5585 N ASN E 117 7663 6463 7368 -2180 -856 246 N ATOM 5586 CA ASN E 117 19.915 1.679 209.826 1.00 57.68 C ANISOU 5586 CA ASN E 117 8096 6469 7349 -2262 -832 480 C ATOM 5587 C ASN E 117 21.407 1.939 209.675 1.00 55.27 C ANISOU 5587 C ASN E 117 7958 5984 7060 -1947 -1017 512 C ATOM 5588 O ASN E 117 22.097 2.161 210.660 1.00 55.87 O ANISOU 5588 O ASN E 117 8250 5981 6997 -1972 -1042 695 O ATOM 5589 CB ASN E 117 19.710 0.411 210.679 1.00 61.86 C ANISOU 5589 CB ASN E 117 8889 6727 7889 -2663 -898 689 C ATOM 5590 CG ASN E 117 18.255 0.198 211.103 1.00 65.49 C ANISOU 5590 CG ASN E 117 9201 7387 8295 -3059 -650 680 C ATOM 5591 OD1 ASN E 117 17.511 1.153 211.350 1.00 65.68 O ANISOU 5591 OD1 ASN E 117 8986 7761 8209 -3069 -375 587 O ATOM 5592 ND2 ASN E 117 17.849 -1.071 211.199 1.00 68.71 N ANISOU 5592 ND2 ASN E 117 9739 7554 8814 -3396 -737 762 N ATOM 5593 N LYS E 118 21.913 1.909 208.450 1.00 53.60 N ANISOU 5593 N LYS E 118 7641 5719 7004 -1677 -1145 321 N ATOM 5594 CA LYS E 118 23.327 2.182 208.233 1.00 51.54 C ANISOU 5594 CA LYS E 118 7479 5312 6791 -1386 -1279 304 C ATOM 5595 C LYS E 118 23.578 3.621 207.765 1.00 48.01 C ANISOU 5595 C LYS E 118 6880 5151 6209 -1115 -1148 190 C ATOM 5596 O LYS E 118 24.699 3.984 207.430 1.00 46.45 O ANISOU 5596 O LYS E 118 6717 4886 6044 -882 -1218 134 O ATOM 5597 CB LYS E 118 23.934 1.133 207.298 1.00 52.94 C ANISOU 5597 CB LYS E 118 7686 5189 7239 -1292 -1477 155 C ATOM 5598 CG LYS E 118 23.939 -0.237 207.951 1.00 57.25 C ANISOU 5598 CG LYS E 118 8444 5353 7955 -1530 -1646 320 C ATOM 5599 CD LYS E 118 24.386 -1.340 207.019 1.00 59.69 C ANISOU 5599 CD LYS E 118 8767 5328 8586 -1453 -1813 126 C ATOM 5600 CE LYS E 118 24.774 -2.591 207.809 1.00 63.48 C ANISOU 5600 CE LYS E 118 9503 5325 9292 -1604 -2042 343 C ATOM 5601 NZ LYS E 118 26.059 -3.158 207.310 1.00 64.64 N ANISOU 5601 NZ LYS E 118 9671 5100 9790 -1323 -2239 205 N ATOM 5602 N VAL E 119 22.528 4.440 207.774 1.00 46.83 N ANISOU 5602 N VAL E 119 6553 5304 5937 -1155 -955 156 N ATOM 5603 CA VAL E 119 22.660 5.874 207.546 1.00 43.71 C ANISOU 5603 CA VAL E 119 6046 5140 5421 -924 -827 97 C ATOM 5604 C VAL E 119 23.208 6.553 208.808 1.00 43.50 C ANISOU 5604 C VAL E 119 6179 5116 5232 -945 -726 241 C ATOM 5605 O VAL E 119 22.632 6.401 209.891 1.00 44.74 O ANISOU 5605 O VAL E 119 6407 5306 5285 -1193 -609 356 O ATOM 5606 CB VAL E 119 21.308 6.499 207.172 1.00 43.54 C ANISOU 5606 CB VAL E 119 5754 5398 5393 -938 -684 14 C ATOM 5607 CG1 VAL E 119 21.462 7.964 206.861 1.00 41.14 C ANISOU 5607 CG1 VAL E 119 5355 5265 5010 -678 -588 -32 C ATOM 5608 CG2 VAL E 119 20.706 5.774 205.989 1.00 44.25 C ANISOU 5608 CG2 VAL E 119 5698 5504 5610 -975 -822 -119 C ATOM 5609 N PHE E 120 24.323 7.280 208.653 1.00 41.75 N ANISOU 5609 N PHE E 120 6023 4870 4971 -723 -764 220 N ATOM 5610 CA PHE E 120 24.982 8.039 209.734 1.00 41.58 C ANISOU 5610 CA PHE E 120 6152 4862 4784 -731 -696 324 C ATOM 5611 C PHE E 120 25.296 9.479 209.296 1.00 39.59 C ANISOU 5611 C PHE E 120 5814 4762 4465 -494 -570 219 C ATOM 5612 O PHE E 120 25.749 9.690 208.172 1.00 38.64 O ANISOU 5612 O PHE E 120 5616 4639 4428 -296 -635 111 O ATOM 5613 CB PHE E 120 26.327 7.396 210.089 1.00 42.24 C ANISOU 5613 CB PHE E 120 6422 4697 4930 -713 -935 424 C ATOM 5614 CG PHE E 120 26.226 6.150 210.902 1.00 44.94 C ANISOU 5614 CG PHE E 120 6942 4831 5303 -964 -1092 610 C ATOM 5615 CD1 PHE E 120 26.233 6.211 212.288 1.00 46.73 C ANISOU 5615 CD1 PHE E 120 7386 5061 5310 -1203 -1081 811 C ATOM 5616 CD2 PHE E 120 26.160 4.908 210.283 1.00 46.24 C ANISOU 5616 CD2 PHE E 120 7091 4778 5702 -985 -1259 586 C ATOM 5617 CE1 PHE E 120 26.164 5.047 213.047 1.00 49.52 C ANISOU 5617 CE1 PHE E 120 7955 5198 5661 -1469 -1257 1031 C ATOM 5618 CE2 PHE E 120 26.083 3.746 211.033 1.00 48.94 C ANISOU 5618 CE2 PHE E 120 7629 4873 6093 -1226 -1427 785 C ATOM 5619 CZ PHE E 120 26.085 3.818 212.416 1.00 50.53 C ANISOU 5619 CZ PHE E 120 8063 5076 6060 -1470 -1437 1030 C ATOM 5620 N PRO E 121 25.140 10.464 210.205 1.00 39.63 N ANISOU 5620 N PRO E 121 5870 4880 4308 -539 -383 246 N ATOM 5621 CA PRO E 121 25.528 11.853 209.927 1.00 37.83 C ANISOU 5621 CA PRO E 121 5606 4736 4030 -335 -268 162 C ATOM 5622 C PRO E 121 27.060 12.039 210.023 1.00 37.00 C ANISOU 5622 C PRO E 121 5649 4514 3896 -256 -404 186 C ATOM 5623 O PRO E 121 27.782 11.095 210.383 1.00 37.33 O ANISOU 5623 O PRO E 121 5798 4407 3978 -340 -601 274 O ATOM 5624 CB PRO E 121 24.832 12.609 211.064 1.00 38.74 C ANISOU 5624 CB PRO E 121 5749 4969 4001 -469 -12 157 C ATOM 5625 CG PRO E 121 24.927 11.676 212.201 1.00 39.85 C ANISOU 5625 CG PRO E 121 6083 5046 4011 -765 -65 292 C ATOM 5626 CD PRO E 121 24.677 10.314 211.600 1.00 41.20 C ANISOU 5626 CD PRO E 121 6203 5113 4340 -820 -259 349 C ATOM 5627 N PRO E 122 27.574 13.238 209.703 1.00 35.96 N ANISOU 5627 N PRO E 122 5510 4429 3725 -98 -314 112 N ATOM 5628 CA PRO E 122 29.014 13.345 209.902 1.00 35.94 C ANISOU 5628 CA PRO E 122 5613 4331 3713 -70 -438 125 C ATOM 5629 C PRO E 122 29.421 13.951 211.240 1.00 37.29 C ANISOU 5629 C PRO E 122 5950 4516 3701 -213 -385 182 C ATOM 5630 O PRO E 122 28.717 14.794 211.787 1.00 38.68 O ANISOU 5630 O PRO E 122 6157 4790 3748 -269 -164 144 O ATOM 5631 CB PRO E 122 29.467 14.283 208.763 1.00 34.43 C ANISOU 5631 CB PRO E 122 5346 4175 3562 131 -371 10 C ATOM 5632 CG PRO E 122 28.237 14.609 207.963 1.00 34.41 C ANISOU 5632 CG PRO E 122 5222 4271 3582 216 -267 -27 C ATOM 5633 CD PRO E 122 27.073 14.325 208.850 1.00 35.62 C ANISOU 5633 CD PRO E 122 5347 4480 3705 80 -178 22 C ATOM 5634 N GLU E 123 30.558 13.515 211.764 1.00 38.22 N ANISOU 5634 N GLU E 123 6166 4533 3822 -276 -596 256 N ATOM 5635 CA GLU E 123 31.222 14.268 212.805 1.00 38.80 C ANISOU 5635 CA GLU E 123 6393 4636 3715 -395 -588 282 C ATOM 5636 C GLU E 123 32.294 15.129 212.155 1.00 37.60 C ANISOU 5636 C GLU E 123 6165 4473 3646 -236 -584 165 C ATOM 5637 O GLU E 123 33.177 14.631 211.433 1.00 38.39 O ANISOU 5637 O GLU E 123 6149 4491 3947 -117 -746 134 O ATOM 5638 CB GLU E 123 31.843 13.352 213.832 1.00 41.35 C ANISOU 5638 CB GLU E 123 6868 4862 3980 -582 -873 460 C ATOM 5639 CG GLU E 123 30.837 12.677 214.721 1.00 44.26 C ANISOU 5639 CG GLU E 123 7391 5253 4173 -833 -842 598 C ATOM 5640 CD GLU E 123 31.505 11.980 215.872 1.00 47.55 C ANISOU 5640 CD GLU E 123 8035 5576 4455 -1063 -1147 818 C ATOM 5641 OE1 GLU E 123 31.682 10.749 215.786 1.00 49.41 O ANISOU 5641 OE1 GLU E 123 8281 5634 4859 -1071 -1421 971 O ATOM 5642 OE2 GLU E 123 31.885 12.665 216.850 1.00 49.44 O ANISOU 5642 OE2 GLU E 123 8456 5903 4428 -1241 -1138 842 O ATOM 5643 N VAL E 124 32.197 16.427 212.411 1.00 35.53 N ANISOU 5643 N VAL E 124 5967 4286 3247 -249 -370 80 N ATOM 5644 CA VAL E 124 33.056 17.419 211.801 1.00 32.89 C ANISOU 5644 CA VAL E 124 5591 3942 2965 -140 -308 -29 C ATOM 5645 C VAL E 124 34.019 18.000 212.832 1.00 33.08 C ANISOU 5645 C VAL E 124 5745 3969 2856 -301 -371 -36 C ATOM 5646 O VAL E 124 33.612 18.443 213.880 1.00 33.95 O ANISOU 5646 O VAL E 124 6019 4125 2753 -470 -273 -32 O ATOM 5647 CB VAL E 124 32.203 18.541 211.163 1.00 31.88 C ANISOU 5647 CB VAL E 124 5443 3846 2824 -19 -35 -117 C ATOM 5648 CG1 VAL E 124 33.063 19.612 210.519 1.00 30.36 C ANISOU 5648 CG1 VAL E 124 5255 3617 2664 55 39 -203 C ATOM 5649 CG2 VAL E 124 31.235 17.940 210.159 1.00 31.03 C ANISOU 5649 CG2 VAL E 124 5198 3758 2833 116 -30 -98 C ATOM 5650 N ALA E 125 35.305 17.969 212.528 1.00 33.11 N ANISOU 5650 N ALA E 125 5661 3932 2988 -268 -533 -67 N ATOM 5651 CA ALA E 125 36.307 18.582 213.365 1.00 34.75 C ANISOU 5651 CA ALA E 125 5950 4154 3099 -421 -621 -92 C ATOM 5652 C ALA E 125 37.138 19.539 212.520 1.00 34.93 C ANISOU 5652 C ALA E 125 5871 4169 3233 -342 -498 -238 C ATOM 5653 O ALA E 125 37.214 19.396 211.300 1.00 33.46 O ANISOU 5653 O ALA E 125 5537 3961 3214 -181 -429 -294 O ATOM 5654 CB ALA E 125 37.193 17.517 213.998 1.00 35.70 C ANISOU 5654 CB ALA E 125 6029 4230 3304 -500 -1006 32 C ATOM 5655 N VAL E 126 37.757 20.511 213.187 1.00 37.34 N ANISOU 5655 N VAL E 126 6278 4493 3416 -497 -464 -305 N ATOM 5656 CA VAL E 126 38.674 21.468 212.562 1.00 37.29 C ANISOU 5656 CA VAL E 126 6199 4471 3499 -495 -354 -439 C ATOM 5657 C VAL E 126 40.050 21.440 213.243 1.00 39.65 C ANISOU 5657 C VAL E 126 6419 4800 3847 -656 -603 -468 C ATOM 5658 O VAL E 126 40.144 21.328 214.463 1.00 41.76 O ANISOU 5658 O VAL E 126 6820 5103 3945 -835 -784 -403 O ATOM 5659 CB VAL E 126 38.041 22.872 212.512 1.00 36.74 C ANISOU 5659 CB VAL E 126 6313 4358 3287 -520 -36 -523 C ATOM 5660 CG1 VAL E 126 38.896 23.938 213.167 1.00 38.45 C ANISOU 5660 CG1 VAL E 126 6635 4561 3413 -726 0 -634 C ATOM 5661 CG2 VAL E 126 37.793 23.228 211.110 1.00 35.65 C ANISOU 5661 CG2 VAL E 126 6106 4170 3268 -347 140 -546 C ATOM 5662 N PHE E 127 41.119 21.476 212.452 1.00 40.41 N ANISOU 5662 N PHE E 127 6286 4895 4175 -609 -627 -568 N ATOM 5663 CA PHE E 127 42.458 21.386 213.021 1.00 43.00 C ANISOU 5663 CA PHE E 127 6454 5258 4627 -740 -893 -609 C ATOM 5664 C PHE E 127 43.296 22.628 212.692 1.00 44.31 C ANISOU 5664 C PHE E 127 6581 5443 4811 -874 -703 -782 C ATOM 5665 O PHE E 127 43.387 23.026 211.538 1.00 43.17 O ANISOU 5665 O PHE E 127 6359 5280 4764 -799 -448 -878 O ATOM 5666 CB PHE E 127 43.178 20.106 212.581 1.00 43.70 C ANISOU 5666 CB PHE E 127 6219 5321 5066 -588 -1153 -599 C ATOM 5667 CG PHE E 127 42.478 18.830 212.985 1.00 43.81 C ANISOU 5667 CG PHE E 127 6284 5272 5090 -489 -1386 -414 C ATOM 5668 CD1 PHE E 127 42.855 18.160 214.128 1.00 45.91 C ANISOU 5668 CD1 PHE E 127 6574 5514 5354 -586 -1794 -254 C ATOM 5669 CD2 PHE E 127 41.467 18.275 212.194 1.00 42.18 C ANISOU 5669 CD2 PHE E 127 6109 5021 4897 -322 -1222 -387 C ATOM 5670 CE1 PHE E 127 42.228 16.988 214.512 1.00 46.17 C ANISOU 5670 CE1 PHE E 127 6693 5460 5389 -532 -2013 -57 C ATOM 5671 CE2 PHE E 127 40.833 17.104 212.572 1.00 42.00 C ANISOU 5671 CE2 PHE E 127 6141 4925 4893 -268 -1426 -222 C ATOM 5672 CZ PHE E 127 41.219 16.459 213.737 1.00 44.26 C ANISOU 5672 CZ PHE E 127 6476 5166 5173 -377 -1813 -51 C ATOM 5673 N GLU E 128 43.905 23.219 213.725 1.00 46.86 N ANISOU 5673 N GLU E 128 6981 5807 5016 -1108 -840 -814 N ATOM 5674 CA GLU E 128 44.643 24.486 213.634 1.00 48.44 C ANISOU 5674 CA GLU E 128 7196 6011 5198 -1301 -667 -979 C ATOM 5675 C GLU E 128 46.054 24.289 213.068 1.00 50.83 C ANISOU 5675 C GLU E 128 7109 6370 5834 -1325 -772 -1104 C ATOM 5676 O GLU E 128 46.655 23.232 213.292 1.00 52.01 O ANISOU 5676 O GLU E 128 6987 6560 6216 -1246 -1106 -1062 O ATOM 5677 CB GLU E 128 44.737 25.120 215.030 1.00 50.11 C ANISOU 5677 CB GLU E 128 7646 6256 5139 -1578 -793 -992 C ATOM 5678 CG GLU E 128 43.409 25.367 215.694 1.00 48.59 C ANISOU 5678 CG GLU E 128 7815 6023 4625 -1596 -641 -931 C ATOM 5679 CD GLU E 128 43.553 26.192 216.940 1.00 50.18 C ANISOU 5679 CD GLU E 128 8277 6255 4534 -1912 -668 -1021 C ATOM 5680 OE1 GLU E 128 44.693 26.579 217.251 1.00 52.07 O ANISOU 5680 OE1 GLU E 128 8415 6547 4822 -2119 -836 -1113 O ATOM 5681 OE2 GLU E 128 42.531 26.459 217.597 1.00 50.01 O ANISOU 5681 OE2 GLU E 128 8548 6212 4242 -1971 -506 -1026 O ATOM 5682 N PRO E 129 46.591 25.309 212.354 1.00 51.70 N ANISOU 5682 N PRO E 129 7183 6468 5992 -1443 -484 -1263 N ATOM 5683 CA PRO E 129 47.910 25.216 211.720 1.00 54.16 C ANISOU 5683 CA PRO E 129 7099 6852 6627 -1501 -491 -1428 C ATOM 5684 C PRO E 129 49.072 25.067 212.689 1.00 57.98 C ANISOU 5684 C PRO E 129 7331 7429 7270 -1673 -867 -1485 C ATOM 5685 O PRO E 129 48.959 25.470 213.844 1.00 59.58 O ANISOU 5685 O PRO E 129 7756 7643 7238 -1852 -1055 -1426 O ATOM 5686 CB PRO E 129 48.026 26.533 210.954 1.00 54.06 C ANISOU 5686 CB PRO E 129 7233 6787 6519 -1670 -80 -1545 C ATOM 5687 CG PRO E 129 47.014 27.425 211.553 1.00 52.51 C ANISOU 5687 CG PRO E 129 7485 6474 5993 -1732 37 -1458 C ATOM 5688 CD PRO E 129 45.905 26.553 211.960 1.00 50.56 C ANISOU 5688 CD PRO E 129 7362 6216 5633 -1509 -107 -1290 C ATOM 5689 N SER E 130 50.173 24.491 212.208 1.00 60.51 N ANISOU 5689 N SER E 130 7180 7820 7993 -1626 -975 -1617 N ATOM 5690 CA SER E 130 51.286 24.096 213.067 1.00 64.48 C ANISOU 5690 CA SER E 130 7344 8405 8749 -1720 -1427 -1648 C ATOM 5691 C SER E 130 52.324 25.200 213.240 1.00 68.03 C ANISOU 5691 C SER E 130 7663 8942 9243 -2053 -1358 -1843 C ATOM 5692 O SER E 130 52.537 26.000 212.328 1.00 68.12 O ANISOU 5692 O SER E 130 7665 8953 9266 -2168 -928 -2007 O ATOM 5693 CB SER E 130 51.974 22.851 212.511 1.00 65.82 C ANISOU 5693 CB SER E 130 6999 8580 9428 -1468 -1608 -1720 C ATOM 5694 OG SER E 130 53.013 23.206 211.620 1.00 67.81 O ANISOU 5694 OG SER E 130 6850 8912 10004 -1554 -1346 -2003 O ATOM 5695 N GLU E 131 52.966 25.199 214.415 1.00 71.23 N ANISOU 5695 N GLU E 131 7980 9424 9662 -2228 -1808 -1809 N ATOM 5696 CA GLU E 131 54.055 26.101 214.813 1.00 74.61 C ANISOU 5696 CA GLU E 131 8232 9955 10162 -2575 -1876 -1990 C ATOM 5697 C GLU E 131 55.184 26.116 213.786 1.00 76.32 C ANISOU 5697 C GLU E 131 7893 10247 10858 -2589 -1672 -2251 C ATOM 5698 O GLU E 131 55.715 27.177 213.439 1.00 77.71 O ANISOU 5698 O GLU E 131 8044 10462 11019 -2879 -1365 -2445 O ATOM 5699 CB GLU E 131 54.602 25.636 216.174 1.00 78.74 C ANISOU 5699 CB GLU E 131 8646 10566 10705 -2683 -2534 -1870 C ATOM 5700 CG GLU E 131 55.989 26.165 216.578 1.00 84.51 C ANISOU 5700 CG GLU E 131 8988 11440 11680 -2989 -2778 -2060 C ATOM 5701 CD GLU E 131 55.924 27.180 217.709 1.00 86.80 C ANISOU 5701 CD GLU E 131 9687 11781 11513 -3397 -2904 -2058 C ATOM 5702 OE1 GLU E 131 54.935 27.148 218.478 1.00 85.46 O ANISOU 5702 OE1 GLU E 131 10031 11560 10881 -3414 -2985 -1871 O ATOM 5703 OE2 GLU E 131 56.862 28.001 217.842 1.00 90.31 O ANISOU 5703 OE2 GLU E 131 9936 12320 12057 -3723 -2908 -2267 O ATOM 5704 N ALA E 132 55.517 24.923 213.297 1.00 76.06 N ANISOU 5704 N ALA E 132 7426 10219 11255 -2285 -1818 -2271 N ATOM 5705 CA ALA E 132 56.513 24.742 212.258 1.00 78.00 C ANISOU 5705 CA ALA E 132 7105 10538 11992 -2255 -1579 -2558 C ATOM 5706 C ALA E 132 56.126 25.433 210.955 1.00 75.26 C ANISOU 5706 C ALA E 132 6959 10169 11467 -2331 -896 -2692 C ATOM 5707 O ALA E 132 56.960 26.090 210.358 1.00 77.75 O ANISOU 5707 O ALA E 132 7024 10575 11941 -2575 -586 -2938 O ATOM 5708 CB ALA E 132 56.775 23.260 212.021 1.00 79.38 C ANISOU 5708 CB ALA E 132 6831 10671 12661 -1873 -1854 -2560 C ATOM 5709 N GLU E 133 54.858 25.322 210.556 1.00 70.17 N ANISOU 5709 N GLU E 133 6779 9407 10476 -2156 -683 -2516 N ATOM 5710 CA GLU E 133 54.362 25.925 209.315 1.00 67.31 C ANISOU 5710 CA GLU E 133 6668 9007 9899 -2213 -106 -2579 C ATOM 5711 C GLU E 133 54.407 27.457 209.318 1.00 67.08 C ANISOU 5711 C GLU E 133 6971 8950 9568 -2585 189 -2609 C ATOM 5712 O GLU E 133 54.672 28.085 208.291 1.00 68.30 O ANISOU 5712 O GLU E 133 7140 9116 9696 -2766 634 -2741 O ATOM 5713 CB GLU E 133 52.938 25.450 209.038 1.00 63.33 C ANISOU 5713 CB GLU E 133 6577 8383 9104 -1937 -46 -2353 C ATOM 5714 CG GLU E 133 52.452 25.696 207.632 1.00 62.33 C ANISOU 5714 CG GLU E 133 6625 8231 8826 -1923 449 -2401 C ATOM 5715 CD GLU E 133 51.008 25.283 207.435 1.00 59.33 C ANISOU 5715 CD GLU E 133 6636 7742 8163 -1668 456 -2171 C ATOM 5716 OE1 GLU E 133 50.250 25.156 208.436 1.00 57.49 O ANISOU 5716 OE1 GLU E 133 6647 7436 7759 -1567 174 -1966 O ATOM 5717 OE2 GLU E 133 50.632 25.081 206.258 1.00 58.97 O ANISOU 5717 OE2 GLU E 133 6652 7699 8054 -1595 754 -2208 O ATOM 5718 N ILE E 134 54.175 28.047 210.484 1.00 65.87 N ANISOU 5718 N ILE E 134 7096 8747 9183 -2725 -58 -2494 N ATOM 5719 CA ILE E 134 54.222 29.486 210.647 1.00 65.55 C ANISOU 5719 CA ILE E 134 7383 8633 8889 -3077 176 -2538 C ATOM 5720 C ILE E 134 55.658 29.978 210.475 1.00 69.48 C ANISOU 5720 C ILE E 134 7455 9262 9683 -3414 253 -2803 C ATOM 5721 O ILE E 134 55.916 30.979 209.803 1.00 70.57 O ANISOU 5721 O ILE E 134 7721 9352 9741 -3697 660 -2908 O ATOM 5722 CB ILE E 134 53.684 29.862 212.027 1.00 64.95 C ANISOU 5722 CB ILE E 134 7669 8491 8520 -3151 -124 -2408 C ATOM 5723 CG1 ILE E 134 52.259 29.338 212.190 1.00 61.18 C ANISOU 5723 CG1 ILE E 134 7563 7905 7780 -2835 -163 -2172 C ATOM 5724 CG2 ILE E 134 53.705 31.357 212.230 1.00 66.38 C ANISOU 5724 CG2 ILE E 134 8205 8550 8466 -3508 126 -2487 C ATOM 5725 CD1 ILE E 134 51.859 29.082 213.630 1.00 61.55 C ANISOU 5725 CD1 ILE E 134 7802 7966 7617 -2845 -566 -2050 C ATOM 5726 N SER E 135 56.596 29.223 211.035 1.00 71.64 N ANISOU 5726 N SER E 135 7198 9694 10327 -3381 -146 -2905 N ATOM 5727 CA SER E 135 57.998 29.612 211.028 1.00 75.44 C ANISOU 5727 CA SER E 135 7186 10327 11151 -3697 -147 -3174 C ATOM 5728 C SER E 135 58.772 29.146 209.794 1.00 76.88 C ANISOU 5728 C SER E 135 6840 10626 11745 -3659 184 -3419 C ATOM 5729 O SER E 135 59.889 29.592 209.567 1.00 81.07 O ANISOU 5729 O SER E 135 6964 11285 12552 -3963 325 -3679 O ATOM 5730 CB SER E 135 58.695 29.146 212.318 1.00 78.60 C ANISOU 5730 CB SER E 135 7248 10844 11771 -3719 -793 -3168 C ATOM 5731 OG SER E 135 58.327 27.823 212.672 1.00 77.15 O ANISOU 5731 OG SER E 135 6936 10651 11728 -3313 -1205 -2993 O ATOM 5732 N HIS E 136 58.189 28.261 208.992 1.00 74.15 N ANISOU 5732 N HIS E 136 6494 10244 11437 -3317 334 -3368 N ATOM 5733 CA HIS E 136 58.896 27.735 207.815 1.00 75.94 C ANISOU 5733 CA HIS E 136 6226 10588 12040 -3283 679 -3648 C ATOM 5734 C HIS E 136 58.502 28.477 206.545 1.00 74.76 C ANISOU 5734 C HIS E 136 6443 10401 11559 -3485 1324 -3682 C ATOM 5735 O HIS E 136 59.337 28.741 205.683 1.00 77.77 O ANISOU 5735 O HIS E 136 6519 10907 12121 -3742 1732 -3957 O ATOM 5736 CB HIS E 136 58.641 26.227 207.643 1.00 74.20 C ANISOU 5736 CB HIS E 136 5726 10351 12115 -2813 457 -3631 C ATOM 5737 CG HIS E 136 59.646 25.528 206.783 1.00 77.65 C ANISOU 5737 CG HIS E 136 5481 10919 13104 -2758 677 -3998 C ATOM 5738 ND1 HIS E 136 60.985 25.472 207.097 1.00 82.98 N ANISOU 5738 ND1 HIS E 136 5471 11737 14322 -2887 521 -4272 N ATOM 5739 CD2 HIS E 136 59.502 24.838 205.628 1.00 77.26 C ANISOU 5739 CD2 HIS E 136 5309 10882 13165 -2592 1049 -4168 C ATOM 5740 CE1 HIS E 136 61.626 24.795 206.162 1.00 85.75 C ANISOU 5740 CE1 HIS E 136 5284 12175 15123 -2791 824 -4614 C ATOM 5741 NE2 HIS E 136 60.748 24.395 205.262 1.00 82.35 N ANISOU 5741 NE2 HIS E 136 5202 11668 14420 -2621 1157 -4565 N ATOM 5742 N THR E 137 57.223 28.815 206.439 1.00 70.91 N ANISOU 5742 N THR E 137 6612 9743 10588 -3384 1404 -3396 N ATOM 5743 CA THR E 137 56.668 29.272 205.171 1.00 70.42 C ANISOU 5743 CA THR E 137 6926 9624 10207 -3483 1918 -3357 C ATOM 5744 C THR E 137 55.951 30.609 205.263 1.00 69.24 C ANISOU 5744 C THR E 137 7434 9277 9596 -3706 2071 -3132 C ATOM 5745 O THR E 137 55.538 31.160 204.239 1.00 69.10 O ANISOU 5745 O THR E 137 7773 9184 9298 -3839 2461 -3058 O ATOM 5746 CB THR E 137 55.673 28.226 204.570 1.00 66.93 C ANISOU 5746 CB THR E 137 6622 9143 9665 -3082 1914 -3233 C ATOM 5747 OG1 THR E 137 54.789 27.734 205.587 1.00 62.95 O ANISOU 5747 OG1 THR E 137 6315 8527 9076 -2763 1459 -2982 O ATOM 5748 CG2 THR E 137 56.427 27.046 203.932 1.00 69.64 C ANISOU 5748 CG2 THR E 137 6360 9649 10451 -2934 1995 -3535 C ATOM 5749 N GLN E 138 55.788 31.093 206.495 1.00 68.93 N ANISOU 5749 N GLN E 138 7565 9143 9484 -3741 1745 -3025 N ATOM 5750 CA GLN E 138 54.934 32.242 206.831 1.00 67.86 C ANISOU 5750 CA GLN E 138 8060 8764 8959 -3856 1812 -2815 C ATOM 5751 C GLN E 138 53.468 32.082 206.413 1.00 64.31 C ANISOU 5751 C GLN E 138 8086 8148 8201 -3541 1866 -2543 C ATOM 5752 O GLN E 138 52.765 33.062 206.162 1.00 63.90 O ANISOU 5752 O GLN E 138 8534 7873 7870 -3629 2057 -2384 O ATOM 5753 CB GLN E 138 55.522 33.564 206.325 1.00 70.89 C ANISOU 5753 CB GLN E 138 8616 9064 9255 -4329 2194 -2906 C ATOM 5754 CG GLN E 138 55.588 34.601 207.404 1.00 72.15 C ANISOU 5754 CG GLN E 138 9027 9071 9318 -4571 2052 -2900 C ATOM 5755 CD GLN E 138 56.538 34.198 208.512 1.00 74.07 C ANISOU 5755 CD GLN E 138 8788 9513 9843 -4654 1662 -3088 C ATOM 5756 OE1 GLN E 138 57.651 33.738 208.253 1.00 76.80 O ANISOU 5756 OE1 GLN E 138 8562 10087 10534 -4770 1663 -3311 O ATOM 5757 NE2 GLN E 138 56.103 34.367 209.754 1.00 73.13 N ANISOU 5757 NE2 GLN E 138 8891 9314 9583 -4605 1321 -3008 N ATOM 5758 N LYS E 139 53.022 30.833 206.325 1.00 62.26 N ANISOU 5758 N LYS E 139 7646 7980 8029 -3173 1682 -2492 N ATOM 5759 CA LYS E 139 51.653 30.524 205.969 1.00 59.39 C ANISOU 5759 CA LYS E 139 7650 7497 7419 -2867 1687 -2255 C ATOM 5760 C LYS E 139 51.077 29.594 207.028 1.00 57.48 C ANISOU 5760 C LYS E 139 7341 7271 7227 -2552 1268 -2155 C ATOM 5761 O LYS E 139 51.786 29.196 207.965 1.00 58.93 O ANISOU 5761 O LYS E 139 7216 7555 7620 -2580 964 -2249 O ATOM 5762 CB LYS E 139 51.568 29.885 204.575 1.00 58.94 C ANISOU 5762 CB LYS E 139 7502 7533 7361 -2777 1944 -2292 C ATOM 5763 CG LYS E 139 52.034 30.802 203.455 1.00 61.47 C ANISOU 5763 CG LYS E 139 7971 7841 7543 -3133 2383 -2353 C ATOM 5764 CD LYS E 139 51.656 30.298 202.080 1.00 60.75 C ANISOU 5764 CD LYS E 139 7958 7820 7303 -3069 2637 -2335 C ATOM 5765 CE LYS E 139 52.013 31.328 201.036 1.00 63.05 C ANISOU 5765 CE LYS E 139 8515 8077 7365 -3475 3056 -2331 C ATOM 5766 NZ LYS E 139 53.469 31.307 200.815 1.00 67.05 N ANISOU 5766 NZ LYS E 139 8559 8784 8131 -3800 3294 -2671 N ATOM 5767 N ALA E 140 49.803 29.241 206.853 1.00 54.22 N ANISOU 5767 N ALA E 140 7214 6765 6621 -2274 1241 -1953 N ATOM 5768 CA ALA E 140 49.015 28.600 207.888 1.00 51.91 C ANISOU 5768 CA ALA E 140 6997 6447 6280 -2034 909 -1816 C ATOM 5769 C ALA E 140 47.832 27.838 207.279 1.00 49.43 C ANISOU 5769 C ALA E 140 6818 6099 5863 -1722 925 -1659 C ATOM 5770 O ALA E 140 46.947 28.441 206.672 1.00 47.69 O ANISOU 5770 O ALA E 140 6933 5758 5430 -1685 1127 -1533 O ATOM 5771 CB ALA E 140 48.519 29.654 208.872 1.00 51.57 C ANISOU 5771 CB ALA E 140 7325 6254 6014 -2160 879 -1743 C ATOM 5772 N THR E 141 47.814 26.518 207.456 1.00 49.16 N ANISOU 5772 N THR E 141 6522 6156 6001 -1504 686 -1660 N ATOM 5773 CA THR E 141 46.770 25.677 206.875 1.00 46.93 C ANISOU 5773 CA THR E 141 6324 5854 5653 -1235 685 -1541 C ATOM 5774 C THR E 141 45.870 25.030 207.918 1.00 44.77 C ANISOU 5774 C THR E 141 6158 5539 5312 -1053 391 -1376 C ATOM 5775 O THR E 141 46.349 24.373 208.832 1.00 44.98 O ANISOU 5775 O THR E 141 5994 5609 5487 -1039 88 -1383 O ATOM 5776 CB THR E 141 47.378 24.541 206.043 1.00 48.12 C ANISOU 5776 CB THR E 141 6101 6111 6071 -1129 698 -1698 C ATOM 5777 OG1 THR E 141 48.550 25.014 205.364 1.00 50.64 O ANISOU 5777 OG1 THR E 141 6202 6515 6523 -1356 944 -1918 O ATOM 5778 CG2 THR E 141 46.372 24.002 205.039 1.00 46.54 C ANISOU 5778 CG2 THR E 141 6052 5896 5737 -951 823 -1622 C ATOM 5779 N LEU E 142 44.564 25.203 207.752 1.00 43.08 N ANISOU 5779 N LEU E 142 6245 5243 4882 -926 474 -1221 N ATOM 5780 CA LEU E 142 43.579 24.577 208.616 1.00 42.11 C ANISOU 5780 CA LEU E 142 6230 5094 4675 -777 267 -1076 C ATOM 5781 C LEU E 142 42.960 23.382 207.909 1.00 41.62 C ANISOU 5781 C LEU E 142 6068 5057 4690 -555 217 -1024 C ATOM 5782 O LEU E 142 42.419 23.542 206.828 1.00 41.87 O ANISOU 5782 O LEU E 142 6188 5076 4645 -488 411 -1008 O ATOM 5783 CB LEU E 142 42.464 25.567 208.962 1.00 41.03 C ANISOU 5783 CB LEU E 142 6448 4846 4297 -781 411 -975 C ATOM 5784 CG LEU E 142 42.644 26.690 210.003 1.00 42.47 C ANISOU 5784 CG LEU E 142 6824 4958 4354 -982 445 -1021 C ATOM 5785 CD1 LEU E 142 43.367 27.940 209.465 1.00 44.01 C ANISOU 5785 CD1 LEU E 142 7095 5072 4554 -1174 672 -1120 C ATOM 5786 CD2 LEU E 142 41.294 27.098 210.525 1.00 41.28 C ANISOU 5786 CD2 LEU E 142 6945 4706 4034 -894 531 -939 C ATOM 5787 N VAL E 143 43.020 22.186 208.486 1.00 42.33 N ANISOU 5787 N VAL E 143 5996 5166 4920 -457 -58 -988 N ATOM 5788 CA VAL E 143 42.230 21.104 207.902 1.00 41.65 C ANISOU 5788 CA VAL E 143 5876 5069 4882 -263 -97 -932 C ATOM 5789 C VAL E 143 40.895 20.861 208.590 1.00 40.82 C ANISOU 5789 C VAL E 143 5987 4925 4598 -194 -178 -752 C ATOM 5790 O VAL E 143 40.723 21.058 209.806 1.00 40.87 O ANISOU 5790 O VAL E 143 6118 4923 4489 -285 -303 -669 O ATOM 5791 CB VAL E 143 42.992 19.777 207.707 1.00 43.33 C ANISOU 5791 CB VAL E 143 5764 5279 5420 -161 -292 -1026 C ATOM 5792 CG1 VAL E 143 44.278 20.016 206.936 1.00 45.97 C ANISOU 5792 CG1 VAL E 143 5831 5670 5964 -233 -144 -1258 C ATOM 5793 CG2 VAL E 143 43.283 19.113 209.011 1.00 44.74 C ANISOU 5793 CG2 VAL E 143 5879 5414 5705 -166 -661 -918 C ATOM 5794 N CYS E 144 39.939 20.445 207.774 1.00 40.17 N ANISOU 5794 N CYS E 144 5948 4837 4477 -61 -90 -711 N ATOM 5795 CA CYS E 144 38.641 20.069 208.261 1.00 39.89 C ANISOU 5795 CA CYS E 144 6051 4783 4325 6 -146 -569 C ATOM 5796 C CYS E 144 38.428 18.600 207.990 1.00 39.46 C ANISOU 5796 C CYS E 144 5857 4710 4426 114 -314 -550 C ATOM 5797 O CYS E 144 38.493 18.173 206.857 1.00 39.16 O ANISOU 5797 O CYS E 144 5716 4683 4481 194 -244 -642 O ATOM 5798 CB CYS E 144 37.546 20.857 207.557 1.00 40.40 C ANISOU 5798 CB CYS E 144 6271 4842 4238 70 68 -525 C ATOM 5799 SG CYS E 144 35.963 20.615 208.350 1.00 41.71 S ANISOU 5799 SG CYS E 144 6552 5000 4295 122 46 -393 S ATOM 5800 N LEU E 145 38.172 17.821 209.029 1.00 39.81 N ANISOU 5800 N LEU E 145 5926 4716 4484 89 -531 -435 N ATOM 5801 CA LEU E 145 37.804 16.426 208.822 1.00 39.87 C ANISOU 5801 CA LEU E 145 5847 4660 4642 178 -691 -393 C ATOM 5802 C LEU E 145 36.311 16.276 208.995 1.00 38.16 C ANISOU 5802 C LEU E 145 5778 4464 4257 177 -624 -276 C ATOM 5803 O LEU E 145 35.745 16.822 209.926 1.00 37.94 O ANISOU 5803 O LEU E 145 5906 4471 4039 77 -579 -188 O ATOM 5804 CB LEU E 145 38.515 15.499 209.812 1.00 41.45 C ANISOU 5804 CB LEU E 145 5981 4765 5003 139 -1022 -306 C ATOM 5805 CG LEU E 145 39.948 15.107 209.474 1.00 43.20 C ANISOU 5805 CG LEU E 145 5935 4926 5553 207 -1160 -444 C ATOM 5806 CD1 LEU E 145 40.397 13.989 210.393 1.00 45.64 C ANISOU 5806 CD1 LEU E 145 6185 5089 6068 214 -1559 -304 C ATOM 5807 CD2 LEU E 145 40.017 14.663 208.047 1.00 42.89 C ANISOU 5807 CD2 LEU E 145 5728 4872 5695 342 -992 -639 C ATOM 5808 N ALA E 146 35.683 15.540 208.091 1.00 36.81 N ANISOU 5808 N ALA E 146 5543 4280 4164 271 -604 -305 N ATOM 5809 CA ALA E 146 34.306 15.151 208.261 1.00 36.51 C ANISOU 5809 CA ALA E 146 5580 4261 4033 258 -585 -205 C ATOM 5810 C ALA E 146 34.308 13.641 208.243 1.00 37.99 C ANISOU 5810 C ALA E 146 5695 4332 4405 269 -790 -178 C ATOM 5811 O ALA E 146 34.482 13.039 207.180 1.00 39.02 O ANISOU 5811 O ALA E 146 5711 4426 4688 359 -792 -303 O ATOM 5812 CB ALA E 146 33.479 15.679 207.129 1.00 35.60 C ANISOU 5812 CB ALA E 146 5454 4226 3845 342 -407 -259 C ATOM 5813 N THR E 147 34.124 13.015 209.401 1.00 38.48 N ANISOU 5813 N THR E 147 5850 4324 4448 156 -959 -20 N ATOM 5814 CA THR E 147 34.299 11.564 209.485 1.00 39.69 C ANISOU 5814 CA THR E 147 5962 4300 4820 160 -1201 35 C ATOM 5815 C THR E 147 33.008 10.787 209.716 1.00 40.15 C ANISOU 5815 C THR E 147 6108 4333 4814 58 -1207 148 C ATOM 5816 O THR E 147 32.015 11.351 210.191 1.00 39.45 O ANISOU 5816 O THR E 147 6114 4378 4497 -50 -1047 213 O ATOM 5817 CB THR E 147 35.260 11.199 210.621 1.00 41.34 C ANISOU 5817 CB THR E 147 6221 4386 5100 87 -1488 175 C ATOM 5818 OG1 THR E 147 34.838 11.860 211.814 1.00 41.33 O ANISOU 5818 OG1 THR E 147 6426 4492 4785 -105 -1453 324 O ATOM 5819 CG2 THR E 147 36.655 11.646 210.282 1.00 41.69 C ANISOU 5819 CG2 THR E 147 6094 4422 5324 197 -1533 33 C ATOM 5820 N GLY E 148 33.053 9.494 209.378 1.00 41.16 N ANISOU 5820 N GLY E 148 6185 4276 5176 87 -1378 146 N ATOM 5821 CA GLY E 148 32.012 8.511 209.715 1.00 42.36 C ANISOU 5821 CA GLY E 148 6430 4344 5320 -54 -1442 274 C ATOM 5822 C GLY E 148 30.587 8.702 209.206 1.00 41.94 C ANISOU 5822 C GLY E 148 6350 4454 5129 -110 -1223 224 C ATOM 5823 O GLY E 148 29.639 8.406 209.930 1.00 43.44 O ANISOU 5823 O GLY E 148 6636 4670 5198 -299 -1194 358 O ATOM 5824 N PHE E 149 30.414 9.177 207.972 1.00 40.58 N ANISOU 5824 N PHE E 149 6045 4400 4974 29 -1078 37 N ATOM 5825 CA PHE E 149 29.062 9.358 207.408 1.00 40.43 C ANISOU 5825 CA PHE E 149 5963 4537 4860 -7 -934 -3 C ATOM 5826 C PHE E 149 28.710 8.326 206.341 1.00 40.97 C ANISOU 5826 C PHE E 149 5951 4533 5084 2 -1007 -129 C ATOM 5827 O PHE E 149 29.565 7.913 205.573 1.00 41.32 O ANISOU 5827 O PHE E 149 5955 4470 5275 104 -1068 -278 O ATOM 5828 CB PHE E 149 28.839 10.789 206.861 1.00 39.32 C ANISOU 5828 CB PHE E 149 5768 4602 4571 108 -746 -72 C ATOM 5829 CG PHE E 149 29.823 11.206 205.794 1.00 38.82 C ANISOU 5829 CG PHE E 149 5666 4543 4542 254 -730 -219 C ATOM 5830 CD1 PHE E 149 31.012 11.835 206.140 1.00 37.95 C ANISOU 5830 CD1 PHE E 149 5592 4401 4427 303 -715 -230 C ATOM 5831 CD2 PHE E 149 29.544 10.996 204.437 1.00 39.30 C ANISOU 5831 CD2 PHE E 149 5659 4661 4614 304 -719 -356 C ATOM 5832 CE1 PHE E 149 31.913 12.206 205.180 1.00 38.20 C ANISOU 5832 CE1 PHE E 149 5576 4450 4488 394 -659 -379 C ATOM 5833 CE2 PHE E 149 30.447 11.367 203.462 1.00 39.10 C ANISOU 5833 CE2 PHE E 149 5624 4659 4572 383 -663 -502 C ATOM 5834 CZ PHE E 149 31.632 11.976 203.829 1.00 38.79 C ANISOU 5834 CZ PHE E 149 5605 4584 4550 427 -615 -517 C ATOM 5835 N TYR E 150 27.446 7.922 206.295 1.00 42.03 N ANISOU 5835 N TYR E 150 6047 4732 5192 -123 -981 -99 N ATOM 5836 CA TYR E 150 26.927 7.097 205.201 1.00 42.97 C ANISOU 5836 CA TYR E 150 6085 4828 5414 -146 -1038 -243 C ATOM 5837 C TYR E 150 25.514 7.574 204.916 1.00 43.51 C ANISOU 5837 C TYR E 150 6032 5128 5371 -208 -946 -234 C ATOM 5838 O TYR E 150 24.789 7.896 205.848 1.00 44.35 O ANISOU 5838 O TYR E 150 6122 5315 5413 -307 -856 -109 O ATOM 5839 CB TYR E 150 26.924 5.610 205.565 1.00 44.75 C ANISOU 5839 CB TYR E 150 6380 4788 5834 -287 -1192 -209 C ATOM 5840 CG TYR E 150 26.637 4.694 204.387 1.00 46.38 C ANISOU 5840 CG TYR E 150 6526 4922 6173 -313 -1252 -415 C ATOM 5841 CD1 TYR E 150 27.649 4.358 203.488 1.00 46.65 C ANISOU 5841 CD1 TYR E 150 6551 4830 6344 -178 -1285 -634 C ATOM 5842 CD2 TYR E 150 25.358 4.184 204.151 1.00 47.10 C ANISOU 5842 CD2 TYR E 150 6558 5085 6255 -492 -1257 -425 C ATOM 5843 CE1 TYR E 150 27.404 3.544 202.402 1.00 47.94 C ANISOU 5843 CE1 TYR E 150 6684 4934 6598 -228 -1311 -867 C ATOM 5844 CE2 TYR E 150 25.110 3.360 203.064 1.00 48.41 C ANISOU 5844 CE2 TYR E 150 6686 5190 6517 -546 -1322 -637 C ATOM 5845 CZ TYR E 150 26.139 3.046 202.195 1.00 48.80 C ANISOU 5845 CZ TYR E 150 6764 5108 6669 -416 -1344 -862 C ATOM 5846 OH TYR E 150 25.918 2.235 201.109 1.00 50.79 O ANISOU 5846 OH TYR E 150 7005 5302 6992 -495 -1381 -1117 O ATOM 5847 N PRO E 151 25.131 7.694 203.634 1.00 43.92 N ANISOU 5847 N PRO E 151 5991 5303 5394 -153 -967 -374 N ATOM 5848 CA PRO E 151 25.916 7.549 202.411 1.00 44.28 C ANISOU 5848 CA PRO E 151 6066 5321 5436 -63 -1009 -560 C ATOM 5849 C PRO E 151 26.671 8.829 202.111 1.00 43.63 C ANISOU 5849 C PRO E 151 6020 5344 5212 97 -911 -560 C ATOM 5850 O PRO E 151 26.630 9.769 202.919 1.00 42.87 O ANISOU 5850 O PRO E 151 5933 5304 5053 149 -829 -420 O ATOM 5851 CB PRO E 151 24.859 7.300 201.336 1.00 45.33 C ANISOU 5851 CB PRO E 151 6106 5606 5513 -144 -1078 -659 C ATOM 5852 CG PRO E 151 23.525 7.543 201.985 1.00 45.71 C ANISOU 5852 CG PRO E 151 6017 5783 5567 -227 -1066 -516 C ATOM 5853 CD PRO E 151 23.743 8.087 203.346 1.00 44.62 C ANISOU 5853 CD PRO E 151 5918 5603 5431 -200 -945 -354 C ATOM 5854 N ASP E 152 27.354 8.890 200.972 1.00 44.39 N ANISOU 5854 N ASP E 152 6153 5466 5249 144 -897 -730 N ATOM 5855 CA ASP E 152 28.241 10.031 200.734 1.00 44.08 C ANISOU 5855 CA ASP E 152 6171 5493 5084 254 -785 -731 C ATOM 5856 C ASP E 152 27.595 11.242 200.053 1.00 43.34 C ANISOU 5856 C ASP E 152 6095 5604 4770 294 -763 -646 C ATOM 5857 O ASP E 152 28.084 11.762 199.051 1.00 44.21 O ANISOU 5857 O ASP E 152 6287 5793 4716 301 -718 -721 O ATOM 5858 CB ASP E 152 29.562 9.619 200.077 1.00 46.17 C ANISOU 5858 CB ASP E 152 6466 5664 5411 272 -725 -953 C ATOM 5859 CG ASP E 152 29.380 9.011 198.704 1.00 49.67 C ANISOU 5859 CG ASP E 152 6931 6171 5772 184 -730 -1177 C ATOM 5860 OD1 ASP E 152 28.504 8.115 198.505 1.00 51.10 O ANISOU 5860 OD1 ASP E 152 7083 6329 6002 89 -843 -1218 O ATOM 5861 OD2 ASP E 152 30.125 9.473 197.812 1.00 51.22 O ANISOU 5861 OD2 ASP E 152 7186 6450 5825 176 -608 -1323 O ATOM 5862 N HIS E 153 26.507 11.709 200.646 1.00 41.85 N ANISOU 5862 N HIS E 153 5828 5484 4591 316 -790 -485 N ATOM 5863 CA HIS E 153 25.833 12.879 200.170 1.00 41.81 C ANISOU 5863 CA HIS E 153 5807 5616 4463 396 -806 -375 C ATOM 5864 C HIS E 153 26.255 14.079 201.008 1.00 40.48 C ANISOU 5864 C HIS E 153 5689 5399 4291 505 -669 -265 C ATOM 5865 O HIS E 153 25.460 14.552 201.823 1.00 40.69 O ANISOU 5865 O HIS E 153 5623 5437 4399 551 -627 -170 O ATOM 5866 CB HIS E 153 24.325 12.687 200.338 1.00 43.42 C ANISOU 5866 CB HIS E 153 5829 5913 4757 373 -907 -303 C ATOM 5867 CG HIS E 153 23.678 11.831 199.287 1.00 44.95 C ANISOU 5867 CG HIS E 153 5966 6200 4913 260 -1082 -395 C ATOM 5868 ND1 HIS E 153 22.462 12.149 198.724 1.00 46.47 N ANISOU 5868 ND1 HIS E 153 6012 6545 5098 270 -1244 -325 N ATOM 5869 CD2 HIS E 153 24.055 10.657 198.724 1.00 45.65 C ANISOU 5869 CD2 HIS E 153 6114 6241 4989 126 -1131 -567 C ATOM 5870 CE1 HIS E 153 22.125 11.216 197.852 1.00 48.55 C ANISOU 5870 CE1 HIS E 153 6265 6878 5305 120 -1396 -443 C ATOM 5871 NE2 HIS E 153 23.074 10.299 197.833 1.00 47.50 N ANISOU 5871 NE2 HIS E 153 6266 6615 5165 28 -1310 -606 N ATOM 5872 N VAL E 154 27.479 14.583 200.844 1.00 39.35 N ANISOU 5872 N VAL E 154 5680 5204 4069 527 -575 -305 N ATOM 5873 CA VAL E 154 27.898 15.741 201.660 1.00 39.10 C ANISOU 5873 CA VAL E 154 5709 5114 4033 600 -447 -218 C ATOM 5874 C VAL E 154 28.381 16.968 200.885 1.00 40.02 C ANISOU 5874 C VAL E 154 5962 5242 4003 648 -392 -174 C ATOM 5875 O VAL E 154 28.830 16.858 199.753 1.00 42.66 O ANISOU 5875 O VAL E 154 6380 5629 4200 590 -414 -236 O ATOM 5876 CB VAL E 154 28.977 15.374 202.673 1.00 37.96 C ANISOU 5876 CB VAL E 154 5595 4863 3966 553 -379 -270 C ATOM 5877 CG1 VAL E 154 28.419 14.490 203.796 1.00 36.97 C ANISOU 5877 CG1 VAL E 154 5397 4694 3954 487 -424 -231 C ATOM 5878 CG2 VAL E 154 30.139 14.724 201.964 1.00 38.44 C ANISOU 5878 CG2 VAL E 154 5679 4890 4037 511 -387 -422 C ATOM 5879 N GLU E 155 28.273 18.143 201.493 1.00 39.86 N ANISOU 5879 N GLU E 155 5984 5160 4002 728 -305 -76 N ATOM 5880 CA GLU E 155 28.686 19.396 200.846 1.00 40.96 C ANISOU 5880 CA GLU E 155 6284 5259 4021 761 -256 -1 C ATOM 5881 C GLU E 155 29.471 20.240 201.836 1.00 39.93 C ANISOU 5881 C GLU E 155 6229 5012 3929 760 -90 -12 C ATOM 5882 O GLU E 155 28.910 20.788 202.795 1.00 39.63 O ANISOU 5882 O GLU E 155 6154 4907 3995 832 -29 25 O ATOM 5883 CB GLU E 155 27.480 20.211 200.338 1.00 43.76 C ANISOU 5883 CB GLU E 155 6624 5611 4391 887 -373 160 C ATOM 5884 CG GLU E 155 26.789 19.689 199.055 1.00 46.89 C ANISOU 5884 CG GLU E 155 7001 6139 4678 860 -590 205 C ATOM 5885 CD GLU E 155 25.430 20.368 198.778 1.00 50.27 C ANISOU 5885 CD GLU E 155 7327 6560 5212 1016 -775 378 C ATOM 5886 OE1 GLU E 155 25.185 21.471 199.321 1.00 51.67 O ANISOU 5886 OE1 GLU E 155 7506 6595 5533 1161 -711 468 O ATOM 5887 OE2 GLU E 155 24.602 19.807 198.016 1.00 52.19 O ANISOU 5887 OE2 GLU E 155 7475 6930 5425 997 -994 411 O ATOM 5888 N LEU E 156 30.768 20.359 201.591 1.00 39.06 N ANISOU 5888 N LEU E 156 6217 4886 3739 661 -3 -90 N ATOM 5889 CA LEU E 156 31.659 21.026 202.525 1.00 37.65 C ANISOU 5889 CA LEU E 156 6095 4616 3595 617 128 -128 C ATOM 5890 C LEU E 156 31.962 22.485 202.150 1.00 38.47 C ANISOU 5890 C LEU E 156 6380 4619 3617 609 230 -51 C ATOM 5891 O LEU E 156 32.484 22.774 201.091 1.00 38.84 O ANISOU 5891 O LEU E 156 6540 4687 3531 530 256 -37 O ATOM 5892 CB LEU E 156 32.940 20.221 202.629 1.00 37.30 C ANISOU 5892 CB LEU E 156 5988 4604 3582 508 147 -277 C ATOM 5893 CG LEU E 156 33.669 20.233 203.962 1.00 37.30 C ANISOU 5893 CG LEU E 156 5954 4548 3672 456 168 -323 C ATOM 5894 CD1 LEU E 156 34.336 18.883 204.166 1.00 37.35 C ANISOU 5894 CD1 LEU E 156 5813 4574 3804 423 58 -425 C ATOM 5895 CD2 LEU E 156 34.672 21.365 204.066 1.00 37.76 C ANISOU 5895 CD2 LEU E 156 6111 4551 3686 370 299 -357 C ATOM 5896 N SER E 157 31.652 23.404 203.046 1.00 39.19 N ANISOU 5896 N SER E 157 6519 4587 3782 666 306 -13 N ATOM 5897 CA SER E 157 31.942 24.806 202.812 1.00 40.03 C ANISOU 5897 CA SER E 157 6816 4540 3856 656 402 57 C ATOM 5898 C SER E 157 32.732 25.379 203.985 1.00 39.97 C ANISOU 5898 C SER E 157 6857 4442 3888 562 546 -50 C ATOM 5899 O SER E 157 32.502 25.002 205.133 1.00 39.02 O ANISOU 5899 O SER E 157 6648 4347 3830 565 560 -125 O ATOM 5900 CB SER E 157 30.644 25.563 202.650 1.00 41.51 C ANISOU 5900 CB SER E 157 7024 4607 4141 842 344 197 C ATOM 5901 OG SER E 157 29.699 25.093 203.592 1.00 41.26 O ANISOU 5901 OG SER E 157 6809 4613 4257 945 341 140 O ATOM 5902 N TRP E 158 33.675 26.273 203.667 1.00 41.09 N ANISOU 5902 N TRP E 158 7157 4490 3965 438 650 -55 N ATOM 5903 CA TRP E 158 34.516 26.994 204.641 1.00 40.41 C ANISOU 5903 CA TRP E 158 7144 4309 3903 308 779 -162 C ATOM 5904 C TRP E 158 34.001 28.418 204.788 1.00 41.91 C ANISOU 5904 C TRP E 158 7524 4247 4152 372 877 -96 C ATOM 5905 O TRP E 158 33.606 29.044 203.807 1.00 43.52 O ANISOU 5905 O TRP E 158 7858 4332 4345 441 849 59 O ATOM 5906 CB TRP E 158 35.971 27.077 204.154 1.00 40.57 C ANISOU 5906 CB TRP E 158 7189 4378 3847 95 849 -238 C ATOM 5907 CG TRP E 158 36.886 25.947 204.537 1.00 38.95 C ANISOU 5907 CG TRP E 158 6771 4348 3681 6 787 -383 C ATOM 5908 CD1 TRP E 158 37.341 24.953 203.723 1.00 38.81 C ANISOU 5908 CD1 TRP E 158 6610 4474 3663 -14 745 -441 C ATOM 5909 CD2 TRP E 158 37.478 25.717 205.819 1.00 38.61 C ANISOU 5909 CD2 TRP E 158 6637 4330 3701 -76 743 -490 C ATOM 5910 NE1 TRP E 158 38.173 24.105 204.421 1.00 38.28 N ANISOU 5910 NE1 TRP E 158 6340 4490 3716 -64 665 -573 N ATOM 5911 CE2 TRP E 158 38.264 24.548 205.714 1.00 38.17 C ANISOU 5911 CE2 TRP E 158 6363 4414 3726 -109 634 -580 C ATOM 5912 CE3 TRP E 158 37.402 26.369 207.054 1.00 39.01 C ANISOU 5912 CE3 TRP E 158 6782 4297 3745 -134 772 -526 C ATOM 5913 CZ2 TRP E 158 38.999 24.046 206.783 1.00 37.92 C ANISOU 5913 CZ2 TRP E 158 6201 4427 3779 -186 505 -658 C ATOM 5914 CZ3 TRP E 158 38.127 25.856 208.119 1.00 38.75 C ANISOU 5914 CZ3 TRP E 158 6648 4346 3730 -253 660 -615 C ATOM 5915 CH2 TRP E 158 38.911 24.705 207.973 1.00 38.17 C ANISOU 5915 CH2 TRP E 158 6353 4400 3749 -269 501 -656 C ATOM 5916 N TRP E 159 33.999 28.929 206.015 1.00 42.42 N ANISOU 5916 N TRP E 159 7622 4216 4280 339 981 -214 N ATOM 5917 CA TRP E 159 33.436 30.254 206.302 1.00 43.94 C ANISOU 5917 CA TRP E 159 7977 4129 4589 422 1101 -207 C ATOM 5918 C TRP E 159 34.391 31.105 207.154 1.00 44.63 C ANISOU 5918 C TRP E 159 8213 4094 4650 209 1254 -363 C ATOM 5919 O TRP E 159 34.683 30.743 208.291 1.00 43.22 O ANISOU 5919 O TRP E 159 7978 4025 4419 94 1285 -522 O ATOM 5920 CB TRP E 159 32.073 30.119 206.995 1.00 43.87 C ANISOU 5920 CB TRP E 159 7847 4098 4726 626 1122 -249 C ATOM 5921 CG TRP E 159 30.997 29.516 206.128 1.00 43.55 C ANISOU 5921 CG TRP E 159 7655 4135 4758 840 962 -94 C ATOM 5922 CD1 TRP E 159 30.871 28.206 205.750 1.00 41.62 C ANISOU 5922 CD1 TRP E 159 7243 4143 4428 836 817 -53 C ATOM 5923 CD2 TRP E 159 29.877 30.199 205.561 1.00 45.74 C ANISOU 5923 CD2 TRP E 159 7922 4223 5235 1084 905 32 C ATOM 5924 NE1 TRP E 159 29.763 28.045 204.956 1.00 42.49 N ANISOU 5924 NE1 TRP E 159 7250 4257 4636 1032 679 83 N ATOM 5925 CE2 TRP E 159 29.132 29.252 204.830 1.00 44.71 C ANISOU 5925 CE2 TRP E 159 7610 4277 5100 1197 711 149 C ATOM 5926 CE3 TRP E 159 29.436 31.523 205.592 1.00 48.68 C ANISOU 5926 CE3 TRP E 159 8414 4262 5819 1225 979 56 C ATOM 5927 CZ2 TRP E 159 27.975 29.582 204.145 1.00 46.84 C ANISOU 5927 CZ2 TRP E 159 7796 4445 5557 1436 561 300 C ATOM 5928 CZ3 TRP E 159 28.287 31.849 204.900 1.00 50.84 C ANISOU 5928 CZ3 TRP E 159 8600 4401 6314 1496 826 218 C ATOM 5929 CH2 TRP E 159 27.570 30.883 204.187 1.00 49.90 C ANISOU 5929 CH2 TRP E 159 8281 4506 6173 1595 605 344 C ATOM 5930 N VAL E 160 34.900 32.210 206.591 1.00 46.42 N ANISOU 5930 N VAL E 160 8650 4097 4890 124 1332 -308 N ATOM 5931 CA VAL E 160 35.716 33.167 207.365 1.00 47.77 C ANISOU 5931 CA VAL E 160 8982 4107 5060 -92 1486 -467 C ATOM 5932 C VAL E 160 34.938 34.448 207.687 1.00 50.01 C ANISOU 5932 C VAL E 160 9455 4018 5529 34 1619 -495 C ATOM 5933 O VAL E 160 34.406 35.121 206.800 1.00 51.65 O ANISOU 5933 O VAL E 160 9787 3982 5857 188 1588 -310 O ATOM 5934 CB VAL E 160 37.196 33.394 206.810 1.00 48.72 C ANISOU 5934 CB VAL E 160 9172 4272 5068 -388 1517 -472 C ATOM 5935 CG1 VAL E 160 37.795 32.095 206.306 1.00 46.65 C ANISOU 5935 CG1 VAL E 160 8678 4343 4704 -439 1396 -457 C ATOM 5936 CG2 VAL E 160 37.299 34.456 205.712 1.00 51.97 C ANISOU 5936 CG2 VAL E 160 9835 4417 5494 -432 1581 -299 C ATOM 5937 N ASN E 161 34.816 34.717 208.984 1.00 50.51 N ANISOU 5937 N ASN E 161 9533 4038 5619 -26 1753 -731 N ATOM 5938 CA ASN E 161 33.999 35.820 209.531 1.00 53.75 C ANISOU 5938 CA ASN E 161 10076 4101 6245 107 1929 -854 C ATOM 5939 C ASN E 161 32.566 35.984 208.988 1.00 54.68 C ANISOU 5939 C ASN E 161 10105 4044 6626 486 1889 -722 C ATOM 5940 O ASN E 161 32.091 37.105 208.837 1.00 57.82 O ANISOU 5940 O ASN E 161 10643 4049 7278 632 1970 -716 O ATOM 5941 CB ASN E 161 34.756 37.160 209.458 1.00 56.90 C ANISOU 5941 CB ASN E 161 10763 4155 6701 -75 2054 -903 C ATOM 5942 CG ASN E 161 36.186 37.059 209.983 1.00 56.63 C ANISOU 5942 CG ASN E 161 10776 4299 6442 -466 2077 -1048 C ATOM 5943 OD1 ASN E 161 36.481 36.248 210.866 1.00 55.16 O ANISOU 5943 OD1 ASN E 161 10452 4415 6091 -595 2038 -1193 O ATOM 5944 ND2 ASN E 161 37.079 37.879 209.438 1.00 57.57 N ANISOU 5944 ND2 ASN E 161 11086 4228 6560 -672 2119 -997 N ATOM 5945 N GLY E 162 31.897 34.875 208.682 1.00 52.43 N ANISOU 5945 N GLY E 162 9578 4030 6313 643 1745 -616 N ATOM 5946 CA GLY E 162 30.521 34.918 208.198 1.00 54.35 C ANISOU 5946 CA GLY E 162 9672 4160 6819 989 1670 -501 C ATOM 5947 C GLY E 162 30.364 34.883 206.680 1.00 55.57 C ANISOU 5947 C GLY E 162 9856 4271 6988 1122 1414 -161 C ATOM 5948 O GLY E 162 29.239 34.797 206.165 1.00 56.60 O ANISOU 5948 O GLY E 162 9834 4351 7322 1403 1272 -27 O ATOM 5949 N LYS E 163 31.477 34.951 205.950 1.00 54.68 N ANISOU 5949 N LYS E 163 9932 4192 6652 900 1351 -27 N ATOM 5950 CA LYS E 163 31.403 34.860 204.492 1.00 55.39 C ANISOU 5950 CA LYS E 163 10096 4284 6663 951 1126 286 C ATOM 5951 C LYS E 163 31.964 33.539 204.007 1.00 52.75 C ANISOU 5951 C LYS E 163 9632 4365 6044 799 1029 312 C ATOM 5952 O LYS E 163 33.001 33.096 204.491 1.00 50.80 O ANISOU 5952 O LYS E 163 9361 4302 5638 562 1134 152 O ATOM 5953 CB LYS E 163 32.127 36.034 203.829 1.00 57.33 C ANISOU 5953 CB LYS E 163 10692 4214 6877 800 1150 440 C ATOM 5954 CG LYS E 163 31.286 37.290 203.791 1.00 61.04 C ANISOU 5954 CG LYS E 163 11304 4201 7687 1044 1125 542 C ATOM 5955 CD LYS E 163 32.124 38.522 203.593 1.00 63.36 C ANISOU 5955 CD LYS E 163 11967 4129 7978 836 1229 604 C ATOM 5956 CE LYS E 163 31.246 39.747 203.559 1.00 67.73 C ANISOU 5956 CE LYS E 163 12660 4142 8932 1115 1179 710 C ATOM 5957 NZ LYS E 163 31.940 40.891 202.919 1.00 71.01 N ANISOU 5957 NZ LYS E 163 13496 4165 9320 918 1179 918 N ATOM 5958 N GLU E 164 31.270 32.907 203.061 1.00 53.33 N ANISOU 5958 N GLU E 164 9609 4573 6081 937 814 500 N ATOM 5959 CA GLU E 164 31.737 31.649 202.485 1.00 51.77 C ANISOU 5959 CA GLU E 164 9299 4734 5637 803 729 503 C ATOM 5960 C GLU E 164 32.856 31.918 201.486 1.00 53.29 C ANISOU 5960 C GLU E 164 9725 4940 5583 541 756 603 C ATOM 5961 O GLU E 164 32.658 32.645 200.513 1.00 55.74 O ANISOU 5961 O GLU E 164 10266 5075 5839 542 658 841 O ATOM 5962 CB GLU E 164 30.595 30.906 201.790 1.00 51.97 C ANISOU 5962 CB GLU E 164 9159 4898 5689 1002 495 643 C ATOM 5963 CG GLU E 164 30.915 29.437 201.538 1.00 49.79 C ANISOU 5963 CG GLU E 164 8712 4980 5226 891 443 557 C ATOM 5964 CD GLU E 164 30.078 28.801 200.437 1.00 50.61 C ANISOU 5964 CD GLU E 164 8750 5223 5257 984 196 720 C ATOM 5965 OE1 GLU E 164 28.895 29.168 200.273 1.00 52.63 O ANISOU 5965 OE1 GLU E 164 8940 5365 5693 1210 33 858 O ATOM 5966 OE2 GLU E 164 30.616 27.916 199.738 1.00 49.78 O ANISOU 5966 OE2 GLU E 164 8642 5342 4929 826 163 688 O ATOM 5967 N VAL E 165 34.033 31.345 201.727 1.00 52.54 N ANISOU 5967 N VAL E 165 9566 5048 5348 305 885 425 N ATOM 5968 CA VAL E 165 35.188 31.619 200.864 1.00 55.14 C ANISOU 5968 CA VAL E 165 10073 5409 5468 17 982 457 C ATOM 5969 C VAL E 165 35.682 30.450 199.989 1.00 55.11 C ANISOU 5969 C VAL E 165 9952 5728 5259 -111 959 406 C ATOM 5970 O VAL E 165 35.478 29.263 200.302 1.00 52.74 O ANISOU 5970 O VAL E 165 9393 5643 5001 -16 890 280 O ATOM 5971 CB VAL E 165 36.387 32.229 201.647 1.00 55.40 C ANISOU 5971 CB VAL E 165 10151 5362 5534 -217 1194 276 C ATOM 5972 CG1 VAL E 165 35.990 33.555 202.296 1.00 57.65 C ANISOU 5972 CG1 VAL E 165 10633 5277 5994 -144 1252 315 C ATOM 5973 CG2 VAL E 165 36.925 31.250 202.674 1.00 52.94 C ANISOU 5973 CG2 VAL E 165 9549 5285 5280 -247 1219 23 C ATOM 5974 N HIS E 166 36.348 30.819 198.896 1.00 57.91 N ANISOU 5974 N HIS E 166 10517 6095 5391 -353 1040 491 N ATOM 5975 CA HIS E 166 36.826 29.868 197.909 1.00 58.88 C ANISOU 5975 CA HIS E 166 10578 6501 5295 -513 1072 416 C ATOM 5976 C HIS E 166 38.356 29.888 197.733 1.00 59.81 C ANISOU 5976 C HIS E 166 10664 6730 5329 -845 1343 209 C ATOM 5977 O HIS E 166 38.960 28.853 197.447 1.00 59.73 O ANISOU 5977 O HIS E 166 10437 6970 5286 -931 1422 -5 O ATOM 5978 CB HIS E 166 36.114 30.093 196.565 1.00 62.41 C ANISOU 5978 CB HIS E 166 11293 6934 5485 -538 923 688 C ATOM 5979 CG HIS E 166 34.705 29.577 196.532 1.00 62.65 C ANISOU 5979 CG HIS E 166 11221 6987 5597 -235 635 816 C ATOM 5980 ND1 HIS E 166 33.603 30.401 196.655 1.00 64.54 N ANISOU 5980 ND1 HIS E 166 11571 6971 5981 -2 431 1067 N ATOM 5981 CD2 HIS E 166 34.218 28.319 196.393 1.00 61.16 C ANISOU 5981 CD2 HIS E 166 10805 7034 5400 -132 519 712 C ATOM 5982 CE1 HIS E 166 32.501 29.674 196.588 1.00 63.80 C ANISOU 5982 CE1 HIS E 166 11294 6985 5962 223 204 1108 C ATOM 5983 NE2 HIS E 166 32.846 28.408 196.429 1.00 61.78 N ANISOU 5983 NE2 HIS E 166 10850 7025 5597 133 254 901 N ATOM 5984 N SER E 167 38.980 31.051 197.899 1.00 61.10 N ANISOU 5984 N SER E 167 11022 6698 5494 -1035 1491 252 N ATOM 5985 CA SER E 167 40.434 31.150 197.760 1.00 61.82 C ANISOU 5985 CA SER E 167 11049 6900 5540 -1376 1761 43 C ATOM 5986 C SER E 167 41.113 30.556 198.971 1.00 58.81 C ANISOU 5986 C SER E 167 10295 6625 5427 -1322 1784 -241 C ATOM 5987 O SER E 167 40.755 30.863 200.107 1.00 57.84 O ANISOU 5987 O SER E 167 10136 6359 5483 -1163 1683 -238 O ATOM 5988 CB SER E 167 40.897 32.605 197.576 1.00 65.50 C ANISOU 5988 CB SER E 167 11852 7107 5930 -1637 1910 181 C ATOM 5989 OG SER E 167 42.309 32.682 197.396 1.00 66.73 O ANISOU 5989 OG SER E 167 11909 7397 6047 -2004 2193 -40 O ATOM 5990 N GLY E 168 42.087 29.688 198.715 1.00 58.05 N ANISOU 5990 N GLY E 168 9920 6778 5359 -1461 1910 -493 N ATOM 5991 CA GLY E 168 42.836 29.028 199.772 1.00 54.93 C ANISOU 5991 CA GLY E 168 9145 6490 5237 -1417 1879 -745 C ATOM 5992 C GLY E 168 42.281 27.658 200.075 1.00 51.56 C ANISOU 5992 C GLY E 168 8469 6194 4929 -1138 1677 -807 C ATOM 5993 O GLY E 168 42.837 26.923 200.886 1.00 51.15 O ANISOU 5993 O GLY E 168 8105 6224 5104 -1077 1593 -983 O ATOM 5994 N VAL E 169 41.169 27.301 199.444 1.00 49.73 N ANISOU 5994 N VAL E 169 8376 5965 4553 -975 1567 -649 N ATOM 5995 CA VAL E 169 40.617 25.978 199.684 1.00 47.26 C ANISOU 5995 CA VAL E 169 7841 5762 4353 -743 1387 -711 C ATOM 5996 C VAL E 169 40.823 24.952 198.553 1.00 47.96 C ANISOU 5996 C VAL E 169 7824 6038 4361 -796 1461 -859 C ATOM 5997 O VAL E 169 40.932 25.302 197.363 1.00 50.50 O ANISOU 5997 O VAL E 169 8343 6418 4426 -988 1619 -834 O ATOM 5998 CB VAL E 169 39.126 26.005 200.181 1.00 45.45 C ANISOU 5998 CB VAL E 169 7725 5422 4121 -479 1165 -493 C ATOM 5999 CG1 VAL E 169 38.820 27.294 200.937 1.00 45.91 C ANISOU 5999 CG1 VAL E 169 7978 5263 4203 -465 1173 -356 C ATOM 6000 CG2 VAL E 169 38.148 25.830 199.044 1.00 45.94 C ANISOU 6000 CG2 VAL E 169 7950 5522 3985 -418 1093 -340 C ATOM 6001 N CYS E 170 40.962 23.694 198.959 1.00 45.34 N ANISOU 6001 N CYS E 170 7193 5786 4247 -655 1357 -1030 N ATOM 6002 CA CYS E 170 40.567 22.579 198.126 1.00 44.75 C ANISOU 6002 CA CYS E 170 7055 5826 4123 -596 1331 -1126 C ATOM 6003 C CYS E 170 39.986 21.510 199.026 1.00 41.20 C ANISOU 6003 C CYS E 170 6412 5336 3905 -347 1080 -1123 C ATOM 6004 O CYS E 170 40.463 21.285 200.140 1.00 40.06 O ANISOU 6004 O CYS E 170 6078 5136 4007 -277 982 -1169 O ATOM 6005 CB CYS E 170 41.689 22.037 197.215 1.00 47.93 C ANISOU 6005 CB CYS E 170 7289 6374 4548 -787 1588 -1444 C ATOM 6006 SG CYS E 170 43.013 21.034 197.969 1.00 50.41 S ANISOU 6006 SG CYS E 170 7098 6706 5349 -720 1603 -1789 S ATOM 6007 N THR E 171 38.923 20.887 198.538 1.00 39.36 N ANISOU 6007 N THR E 171 6254 5133 3569 -243 959 -1049 N ATOM 6008 CA THR E 171 38.321 19.744 199.183 1.00 36.86 C ANISOU 6008 CA THR E 171 5777 4784 3445 -55 747 -1057 C ATOM 6009 C THR E 171 38.596 18.535 198.295 1.00 39.05 C ANISOU 6009 C THR E 171 5920 5141 3777 -81 801 -1303 C ATOM 6010 O THR E 171 38.575 18.656 197.065 1.00 41.25 O ANISOU 6010 O THR E 171 6334 5528 3812 -224 947 -1376 O ATOM 6011 CB THR E 171 36.812 19.960 199.337 1.00 34.13 C ANISOU 6011 CB THR E 171 5591 4404 2974 68 576 -806 C ATOM 6012 OG1 THR E 171 36.573 21.212 199.987 1.00 32.70 O ANISOU 6012 OG1 THR E 171 5551 4129 2745 84 585 -622 O ATOM 6013 CG2 THR E 171 36.175 18.861 200.137 1.00 32.30 C ANISOU 6013 CG2 THR E 171 5207 4133 2931 215 382 -797 C ATOM 6014 N ASP E 172 38.894 17.399 198.926 1.00 39.54 N ANISOU 6014 N ASP E 172 5737 5135 4152 37 683 -1435 N ATOM 6015 CA ASP E 172 39.082 16.118 198.257 1.00 42.36 C ANISOU 6015 CA ASP E 172 5945 5500 4648 54 709 -1692 C ATOM 6016 C ASP E 172 37.978 15.819 197.276 1.00 43.63 C ANISOU 6016 C ASP E 172 6295 5743 4540 15 685 -1656 C ATOM 6017 O ASP E 172 36.809 15.938 197.612 1.00 42.04 O ANISOU 6017 O ASP E 172 6212 5525 4237 93 498 -1415 O ATOM 6018 CB ASP E 172 39.130 14.996 199.288 1.00 41.94 C ANISOU 6018 CB ASP E 172 5680 5290 4967 227 477 -1708 C ATOM 6019 CG ASP E 172 40.288 15.131 200.237 1.00 42.62 C ANISOU 6019 CG ASP E 172 5550 5298 5344 262 433 -1752 C ATOM 6020 OD1 ASP E 172 41.336 15.705 199.847 1.00 44.36 O ANISOU 6020 OD1 ASP E 172 5672 5592 5592 152 643 -1921 O ATOM 6021 OD2 ASP E 172 40.145 14.658 201.380 1.00 41.83 O ANISOU 6021 OD2 ASP E 172 5386 5072 5435 373 177 -1612 O ATOM 6022 N PRO E 173 38.356 15.446 196.052 1.00 47.48 N ANISOU 6022 N PRO E 173 6800 6335 4906 -128 884 -1917 N ATOM 6023 CA PRO E 173 37.409 15.256 194.970 1.00 49.51 C ANISOU 6023 CA PRO E 173 7270 6707 4834 -229 861 -1900 C ATOM 6024 C PRO E 173 36.418 14.132 195.231 1.00 49.96 C ANISOU 6024 C PRO E 173 7267 6688 5028 -101 621 -1882 C ATOM 6025 O PRO E 173 35.270 14.258 194.833 1.00 51.05 O ANISOU 6025 O PRO E 173 7572 6900 4924 -126 473 -1707 O ATOM 6026 CB PRO E 173 38.303 14.943 193.770 1.00 52.53 C ANISOU 6026 CB PRO E 173 7645 7210 5105 -440 1174 -2271 C ATOM 6027 CG PRO E 173 39.571 14.446 194.348 1.00 53.14 C ANISOU 6027 CG PRO E 173 7384 7179 5626 -357 1305 -2544 C ATOM 6028 CD PRO E 173 39.742 15.203 195.621 1.00 50.32 C ANISOU 6028 CD PRO E 173 6962 6723 5433 -227 1157 -2272 C ATOM 6029 N GLN E 174 36.850 13.074 195.922 1.00 51.06 N ANISOU 6029 N GLN E 174 7165 6664 5570 31 561 -2039 N ATOM 6030 CA GLN E 174 35.995 11.937 196.305 1.00 51.15 C ANISOU 6030 CA GLN E 174 7121 6554 5759 132 336 -2015 C ATOM 6031 C GLN E 174 36.334 11.496 197.736 1.00 49.37 C ANISOU 6031 C GLN E 174 6714 6120 5925 303 168 -1913 C ATOM 6032 O GLN E 174 37.487 11.577 198.148 1.00 50.06 O ANISOU 6032 O GLN E 174 6638 6135 6247 350 237 -2020 O ATOM 6033 CB GLN E 174 36.163 10.757 195.327 1.00 54.69 C ANISOU 6033 CB GLN E 174 7521 6981 6277 56 434 -2384 C ATOM 6034 CG GLN E 174 35.320 10.846 194.038 1.00 57.44 C ANISOU 6034 CG GLN E 174 8101 7531 6192 -137 468 -2427 C ATOM 6035 CD GLN E 174 36.130 11.317 192.825 1.00 61.28 C ANISOU 6035 CD GLN E 174 8695 8198 6391 -353 784 -2680 C ATOM 6036 OE1 GLN E 174 37.216 11.875 192.974 1.00 62.40 O ANISOU 6036 OE1 GLN E 174 8746 8345 6619 -362 991 -2762 O ATOM 6037 NE2 GLN E 174 35.609 11.078 191.619 1.00 63.99 N ANISOU 6037 NE2 GLN E 174 9237 8702 6374 -563 828 -2816 N ATOM 6038 N PRO E 175 35.330 11.050 198.508 1.00 47.45 N ANISOU 6038 N PRO E 175 6500 5790 5740 370 -63 -1698 N ATOM 6039 CA PRO E 175 35.578 10.603 199.883 1.00 45.74 C ANISOU 6039 CA PRO E 175 6175 5381 5824 480 -246 -1563 C ATOM 6040 C PRO E 175 36.258 9.241 200.018 1.00 46.91 C ANISOU 6040 C PRO E 175 6149 5290 6385 557 -332 -1768 C ATOM 6041 O PRO E 175 36.131 8.387 199.143 1.00 48.60 O ANISOU 6041 O PRO E 175 6342 5456 6668 529 -276 -2009 O ATOM 6042 CB PRO E 175 34.168 10.534 200.488 1.00 44.65 C ANISOU 6042 CB PRO E 175 6148 5253 5564 467 -411 -1295 C ATOM 6043 CG PRO E 175 33.335 11.428 199.632 1.00 44.55 C ANISOU 6043 CG PRO E 175 6269 5455 5204 400 -323 -1232 C ATOM 6044 CD PRO E 175 33.891 11.221 198.250 1.00 46.67 C ANISOU 6044 CD PRO E 175 6547 5799 5385 322 -166 -1515 C ATOM 6045 N LEU E 176 36.964 9.068 201.132 1.00 46.16 N ANISOU 6045 N LEU E 176 5941 5033 6566 650 -489 -1667 N ATOM 6046 CA LEU E 176 37.670 7.845 201.503 1.00 48.07 C ANISOU 6046 CA LEU E 176 6006 4987 7272 764 -654 -1787 C ATOM 6047 C LEU E 176 36.761 6.874 202.212 1.00 47.58 C ANISOU 6047 C LEU E 176 6050 4729 7301 760 -909 -1580 C ATOM 6048 O LEU E 176 35.966 7.283 203.053 1.00 45.27 O ANISOU 6048 O LEU E 176 5910 4506 6786 689 -1014 -1273 O ATOM 6049 CB LEU E 176 38.734 8.203 202.536 1.00 49.66 C ANISOU 6049 CB LEU E 176 6068 5114 7687 842 -794 -1679 C ATOM 6050 CG LEU E 176 40.237 8.018 202.370 1.00 52.92 C ANISOU 6050 CG LEU E 176 6173 5428 8506 952 -759 -1946 C ATOM 6051 CD1 LEU E 176 40.733 8.228 200.921 1.00 54.86 C ANISOU 6051 CD1 LEU E 176 6306 5822 8718 906 -377 -2354 C ATOM 6052 CD2 LEU E 176 40.918 8.969 203.348 1.00 52.28 C ANISOU 6052 CD2 LEU E 176 6044 5429 8390 937 -864 -1757 C ATOM 6053 N LYS E 177 36.907 5.587 201.923 1.00 49.68 N ANISOU 6053 N LYS E 177 6233 4731 7911 820 -995 -1758 N ATOM 6054 CA LYS E 177 36.250 4.566 202.732 1.00 50.95 C ANISOU 6054 CA LYS E 177 6494 4634 8229 803 -1270 -1541 C ATOM 6055 C LYS E 177 37.006 4.370 204.055 1.00 52.67 C ANISOU 6055 C LYS E 177 6663 4636 8713 889 -1569 -1298 C ATOM 6056 O LYS E 177 38.238 4.226 204.072 1.00 54.21 O ANISOU 6056 O LYS E 177 6637 4694 9265 1041 -1627 -1448 O ATOM 6057 CB LYS E 177 36.157 3.236 201.975 1.00 53.43 C ANISOU 6057 CB LYS E 177 6763 4687 8853 830 -1275 -1816 C ATOM 6058 CG LYS E 177 35.188 3.248 200.801 1.00 52.76 C ANISOU 6058 CG LYS E 177 6782 4803 8462 685 -1064 -2004 C ATOM 6059 CD LYS E 177 34.898 1.838 200.274 1.00 55.38 C ANISOU 6059 CD LYS E 177 7121 4842 9079 662 -1113 -2237 C ATOM 6060 CE LYS E 177 33.862 1.864 199.157 1.00 54.69 C ANISOU 6060 CE LYS E 177 7154 4986 8642 476 -952 -2404 C ATOM 6061 NZ LYS E 177 33.717 0.550 198.462 1.00 57.68 N ANISOU 6061 NZ LYS E 177 7536 5095 9283 429 -946 -2729 N ATOM 6062 N GLU E 178 36.268 4.358 205.161 1.00 52.33 N ANISOU 6062 N GLU E 178 6817 4572 8492 774 -1763 -930 N ATOM 6063 CA GLU E 178 36.891 4.179 206.472 1.00 54.06 C ANISOU 6063 CA GLU E 178 7058 4609 8873 798 -2087 -652 C ATOM 6064 C GLU E 178 37.120 2.729 206.810 1.00 58.27 C ANISOU 6064 C GLU E 178 7587 4703 9851 866 -2400 -590 C ATOM 6065 O GLU E 178 38.181 2.365 207.294 1.00 61.12 O ANISOU 6065 O GLU E 178 7809 4828 10587 1010 -2665 -552 O ATOM 6066 CB GLU E 178 36.058 4.807 207.586 1.00 51.74 C ANISOU 6066 CB GLU E 178 7013 4487 8157 599 -2140 -293 C ATOM 6067 CG GLU E 178 36.177 6.298 207.695 1.00 48.41 C ANISOU 6067 CG GLU E 178 6596 4404 7396 563 -1939 -289 C ATOM 6068 CD GLU E 178 35.350 6.825 208.829 1.00 47.56 C ANISOU 6068 CD GLU E 178 6725 4432 6913 364 -1965 11 C ATOM 6069 OE1 GLU E 178 34.743 5.988 209.534 1.00 49.24 O ANISOU 6069 OE1 GLU E 178 7100 4488 7121 234 -2141 227 O ATOM 6070 OE2 GLU E 178 35.301 8.062 209.018 1.00 45.60 O ANISOU 6070 OE2 GLU E 178 6512 4432 6380 319 -1791 19 O ATOM 6071 N GLN E 179 36.124 1.889 206.583 1.00 60.05 N ANISOU 6071 N GLN E 179 7959 4793 10064 760 -2399 -567 N ATOM 6072 CA GLN E 179 36.285 0.492 206.943 1.00 65.10 C ANISOU 6072 CA GLN E 179 8639 4959 11136 804 -2711 -478 C ATOM 6073 C GLN E 179 36.076 -0.412 205.727 1.00 66.64 C ANISOU 6073 C GLN E 179 8745 4966 11611 867 -2557 -853 C ATOM 6074 O GLN E 179 35.054 -1.089 205.631 1.00 67.59 O ANISOU 6074 O GLN E 179 9040 4985 11658 702 -2560 -798 O ATOM 6075 CB GLN E 179 35.316 0.143 208.083 1.00 66.45 C ANISOU 6075 CB GLN E 179 9130 5058 11060 550 -2915 -42 C ATOM 6076 CG GLN E 179 35.963 -0.570 209.284 1.00 71.11 C ANISOU 6076 CG GLN E 179 9828 5268 11921 565 -3384 309 C ATOM 6077 CD GLN E 179 35.773 -2.087 209.264 1.00 75.66 C ANISOU 6077 CD GLN E 179 10503 5326 12916 564 -3627 364 C ATOM 6078 OE1 GLN E 179 34.827 -2.603 208.661 1.00 75.52 O ANISOU 6078 OE1 GLN E 179 10569 5275 12849 437 -3448 237 O ATOM 6079 NE2 GLN E 179 36.670 -2.806 209.941 1.00 79.99 N ANISOU 6079 NE2 GLN E 179 11047 5451 13896 699 -4067 566 N ATOM 6080 N PRO E 180 37.071 -0.477 204.817 1.00 67.81 N ANISOU 6080 N PRO E 180 8615 5052 12097 1083 -2418 -1260 N ATOM 6081 CA PRO E 180 36.890 -1.060 203.480 1.00 69.19 C ANISOU 6081 CA PRO E 180 8708 5164 12415 1104 -2160 -1712 C ATOM 6082 C PRO E 180 36.685 -2.576 203.414 1.00 73.35 C ANISOU 6082 C PRO E 180 9294 5180 13394 1127 -2343 -1787 C ATOM 6083 O PRO E 180 36.466 -3.112 202.332 1.00 74.68 O ANISOU 6083 O PRO E 180 9427 5285 13663 1108 -2128 -2181 O ATOM 6084 CB PRO E 180 38.191 -0.677 202.753 1.00 70.32 C ANISOU 6084 CB PRO E 180 8527 5370 12823 1314 -1959 -2112 C ATOM 6085 CG PRO E 180 38.897 0.291 203.659 1.00 68.56 C ANISOU 6085 CG PRO E 180 8222 5318 12511 1373 -2092 -1846 C ATOM 6086 CD PRO E 180 38.473 -0.089 205.026 1.00 68.81 C ANISOU 6086 CD PRO E 180 8472 5145 12527 1302 -2498 -1345 C ATOM 6087 N ALA E 181 36.760 -3.251 204.559 1.00 76.09 N ANISOU 6087 N ALA E 181 9759 5157 13996 1143 -2743 -1409 N ATOM 6088 CA ALA E 181 36.436 -4.666 204.657 1.00 80.69 C ANISOU 6088 CA ALA E 181 10469 5213 14977 1121 -2959 -1383 C ATOM 6089 C ALA E 181 34.945 -4.881 204.892 1.00 79.80 C ANISOU 6089 C ALA E 181 10677 5197 14447 781 -2942 -1136 C ATOM 6090 O ALA E 181 34.459 -6.003 204.761 1.00 82.93 O ANISOU 6090 O ALA E 181 11204 5214 15090 689 -3038 -1170 O ATOM 6091 CB ALA E 181 37.243 -5.332 205.754 1.00 84.35 C ANISOU 6091 CB ALA E 181 10930 5191 15929 1285 -3439 -1060 C ATOM 6092 N LEU E 182 34.222 -3.821 205.257 1.00 76.19 N ANISOU 6092 N LEU E 182 10328 5225 13396 589 -2815 -904 N ATOM 6093 CA LEU E 182 32.767 -3.909 205.361 1.00 76.09 C ANISOU 6093 CA LEU E 182 10537 5376 12997 267 -2732 -741 C ATOM 6094 C LEU E 182 32.171 -3.266 204.122 1.00 73.50 C ANISOU 6094 C LEU E 182 10106 5474 12347 211 -2368 -1090 C ATOM 6095 O LEU E 182 32.796 -2.396 203.518 1.00 72.07 O ANISOU 6095 O LEU E 182 9753 5567 12064 366 -2177 -1309 O ATOM 6096 CB LEU E 182 32.238 -3.240 206.638 1.00 75.02 C ANISOU 6096 CB LEU E 182 10588 5468 12449 71 -2830 -262 C ATOM 6097 CG LEU E 182 30.839 -3.654 207.138 1.00 76.23 C ANISOU 6097 CG LEU E 182 10980 5643 12341 -289 -2829 -11 C ATOM 6098 CD1 LEU E 182 30.784 -5.112 207.654 1.00 80.50 C ANISOU 6098 CD1 LEU E 182 11727 5608 13252 -403 -3132 180 C ATOM 6099 CD2 LEU E 182 30.307 -2.660 208.181 1.00 74.18 C ANISOU 6099 CD2 LEU E 182 10839 5754 11591 -478 -2773 329 C ATOM 6100 N ASN E 183 30.976 -3.697 203.733 1.00 73.46 N ANISOU 6100 N ASN E 183 10208 5522 12182 -31 -2289 -1133 N ATOM 6101 CA ASN E 183 30.408 -3.265 202.467 1.00 72.23 C ANISOU 6101 CA ASN E 183 9966 5718 11758 -97 -2017 -1470 C ATOM 6102 C ASN E 183 29.687 -1.926 202.570 1.00 68.18 C ANISOU 6102 C ASN E 183 9437 5742 10725 -187 -1870 -1300 C ATOM 6103 O ASN E 183 29.609 -1.155 201.601 1.00 66.91 O ANISOU 6103 O ASN E 183 9185 5922 10316 -154 -1673 -1521 O ATOM 6104 CB ASN E 183 29.467 -4.339 201.907 1.00 74.75 C ANISOU 6104 CB ASN E 183 10376 5859 12167 -322 -2025 -1633 C ATOM 6105 CG ASN E 183 29.492 -4.407 200.387 1.00 75.60 C ANISOU 6105 CG ASN E 183 10393 6101 12229 -316 -1814 -2133 C ATOM 6106 OD1 ASN E 183 29.760 -3.413 199.692 1.00 73.29 O ANISOU 6106 OD1 ASN E 183 10000 6191 11655 -235 -1625 -2291 O ATOM 6107 ND2 ASN E 183 29.217 -5.593 199.858 1.00 79.29 N ANISOU 6107 ND2 ASN E 183 10925 6243 12958 -433 -1844 -2389 N ATOM 6108 N ASP E 184 29.162 -1.644 203.752 1.00 66.37 N ANISOU 6108 N ASP E 184 9311 5574 10333 -311 -1965 -907 N ATOM 6109 CA ASP E 184 28.353 -0.461 203.912 1.00 62.52 C ANISOU 6109 CA ASP E 184 8795 5543 9417 -399 -1816 -767 C ATOM 6110 C ASP E 184 29.095 0.501 204.814 1.00 59.32 C ANISOU 6110 C ASP E 184 8397 5243 8900 -269 -1829 -550 C ATOM 6111 O ASP E 184 28.510 1.180 205.666 1.00 57.50 O ANISOU 6111 O ASP E 184 8224 5218 8406 -384 -1788 -299 O ATOM 6112 CB ASP E 184 26.988 -0.850 204.451 1.00 64.53 C ANISOU 6112 CB ASP E 184 9133 5840 9546 -695 -1835 -570 C ATOM 6113 CG ASP E 184 26.153 -1.598 203.417 1.00 67.73 C ANISOU 6113 CG ASP E 184 9496 6232 10006 -848 -1806 -821 C ATOM 6114 OD1 ASP E 184 25.656 -0.947 202.468 1.00 67.09 O ANISOU 6114 OD1 ASP E 184 9291 6491 9708 -840 -1680 -1002 O ATOM 6115 OD2 ASP E 184 25.992 -2.837 203.540 1.00 71.38 O ANISOU 6115 OD2 ASP E 184 10063 6332 10726 -990 -1930 -830 O ATOM 6116 N SER E 185 30.405 0.547 204.581 1.00 58.01 N ANISOU 6116 N SER E 185 8152 4936 8954 -40 -1869 -690 N ATOM 6117 CA SER E 185 31.347 1.321 205.370 1.00 55.50 C ANISOU 6117 CA SER E 185 7817 4664 8607 91 -1926 -529 C ATOM 6118 C SER E 185 31.103 2.811 205.282 1.00 51.10 C ANISOU 6118 C SER E 185 7219 4534 7664 100 -1714 -506 C ATOM 6119 O SER E 185 30.721 3.341 204.238 1.00 50.10 O ANISOU 6119 O SER E 185 7016 4648 7371 116 -1523 -707 O ATOM 6120 CB SER E 185 32.777 1.031 204.920 1.00 57.17 C ANISOU 6120 CB SER E 185 7874 4654 9193 336 -1983 -763 C ATOM 6121 OG SER E 185 33.280 2.014 204.028 1.00 55.46 O ANISOU 6121 OG SER E 185 7511 4725 8837 452 -1742 -1015 O ATOM 6122 N ARG E 186 31.344 3.481 206.397 1.00 48.68 N ANISOU 6122 N ARG E 186 6984 4299 7211 77 -1770 -253 N ATOM 6123 CA ARG E 186 31.147 4.909 206.491 1.00 44.27 C ANISOU 6123 CA ARG E 186 6411 4087 6325 85 -1580 -217 C ATOM 6124 C ARG E 186 32.350 5.597 205.868 1.00 42.92 C ANISOU 6124 C ARG E 186 6108 3977 6224 279 -1503 -413 C ATOM 6125 O ARG E 186 33.371 4.960 205.592 1.00 44.26 O ANISOU 6125 O ARG E 186 6179 3927 6710 404 -1606 -555 O ATOM 6126 CB ARG E 186 30.915 5.293 207.947 1.00 44.04 C ANISOU 6126 CB ARG E 186 6534 4099 6101 -60 -1644 87 C ATOM 6127 CG ARG E 186 29.903 4.348 208.638 1.00 45.69 C ANISOU 6127 CG ARG E 186 6888 4185 6287 -300 -1732 282 C ATOM 6128 CD ARG E 186 30.110 4.247 210.147 1.00 47.18 C ANISOU 6128 CD ARG E 186 7286 4281 6358 -471 -1896 593 C ATOM 6129 NE ARG E 186 29.932 5.557 210.760 1.00 45.75 N ANISOU 6129 NE ARG E 186 7142 4397 5846 -524 -1711 645 N ATOM 6130 CZ ARG E 186 29.682 5.779 212.041 1.00 45.97 C ANISOU 6130 CZ ARG E 186 7368 4482 5616 -751 -1721 868 C ATOM 6131 NH1 ARG E 186 29.533 7.026 212.454 1.00 44.03 N ANISOU 6131 NH1 ARG E 186 7133 4496 5101 -777 -1509 838 N ATOM 6132 NH2 ARG E 186 29.560 4.769 212.891 1.00 48.96 N ANISOU 6132 NH2 ARG E 186 7956 4650 5997 -974 -1929 1111 N ATOM 6133 N TYR E 187 32.208 6.889 205.612 1.00 40.55 N ANISOU 6133 N TYR E 187 5792 3960 5654 299 -1308 -435 N ATOM 6134 CA TYR E 187 33.117 7.596 204.725 1.00 39.85 C ANISOU 6134 CA TYR E 187 5594 3975 5572 426 -1166 -651 C ATOM 6135 C TYR E 187 33.789 8.765 205.414 1.00 38.94 C ANISOU 6135 C TYR E 187 5493 3971 5331 450 -1124 -550 C ATOM 6136 O TYR E 187 33.227 9.347 206.336 1.00 38.47 O ANISOU 6136 O TYR E 187 5547 4000 5072 363 -1124 -347 O ATOM 6137 CB TYR E 187 32.345 8.179 203.540 1.00 38.39 C ANISOU 6137 CB TYR E 187 5411 4022 5155 406 -970 -777 C ATOM 6138 CG TYR E 187 31.836 7.218 202.494 1.00 39.30 C ANISOU 6138 CG TYR E 187 5501 4089 5342 367 -971 -968 C ATOM 6139 CD1 TYR E 187 30.475 6.927 202.399 1.00 39.33 C ANISOU 6139 CD1 TYR E 187 5548 4167 5230 252 -1005 -887 C ATOM 6140 CD2 TYR E 187 32.696 6.652 201.558 1.00 40.17 C ANISOU 6140 CD2 TYR E 187 5530 4100 5632 425 -915 -1264 C ATOM 6141 CE1 TYR E 187 29.993 6.080 201.412 1.00 40.74 C ANISOU 6141 CE1 TYR E 187 5712 4318 5451 183 -1019 -1078 C ATOM 6142 CE2 TYR E 187 32.221 5.804 200.581 1.00 41.82 C ANISOU 6142 CE2 TYR E 187 5743 4274 5875 358 -897 -1477 C ATOM 6143 CZ TYR E 187 30.872 5.524 200.509 1.00 41.96 C ANISOU 6143 CZ TYR E 187 5826 4364 5752 231 -965 -1374 C ATOM 6144 OH TYR E 187 30.395 4.679 199.543 1.00 43.87 O ANISOU 6144 OH TYR E 187 6079 4577 6013 133 -966 -1598 O ATOM 6145 N ALA E 188 34.967 9.151 204.933 1.00 39.59 N ANISOU 6145 N ALA E 188 5455 4062 5523 544 -1056 -724 N ATOM 6146 CA ALA E 188 35.607 10.361 205.449 1.00 39.37 C ANISOU 6146 CA ALA E 188 5439 4156 5365 538 -993 -661 C ATOM 6147 C ALA E 188 35.933 11.350 204.336 1.00 39.19 C ANISOU 6147 C ALA E 188 5379 4311 5202 556 -735 -842 C ATOM 6148 O ALA E 188 36.187 10.945 203.205 1.00 40.96 O ANISOU 6148 O ALA E 188 5519 4538 5506 586 -630 -1068 O ATOM 6149 CB ALA E 188 36.853 10.019 206.233 1.00 40.90 C ANISOU 6149 CB ALA E 188 5522 4192 5828 585 -1199 -642 C ATOM 6150 N LEU E 189 35.936 12.643 204.656 1.00 37.48 N ANISOU 6150 N LEU E 189 5249 4229 4764 513 -624 -749 N ATOM 6151 CA LEU E 189 36.249 13.662 203.665 1.00 36.59 C ANISOU 6151 CA LEU E 189 5150 4256 4496 497 -395 -870 C ATOM 6152 C LEU E 189 36.999 14.825 204.295 1.00 36.31 C ANISOU 6152 C LEU E 189 5139 4261 4395 452 -334 -822 C ATOM 6153 O LEU E 189 36.553 15.406 205.278 1.00 35.64 O ANISOU 6153 O LEU E 189 5171 4184 4188 415 -377 -652 O ATOM 6154 CB LEU E 189 34.976 14.171 202.993 1.00 35.05 C ANISOU 6154 CB LEU E 189 5096 4182 4041 480 -300 -791 C ATOM 6155 CG LEU E 189 35.219 15.137 201.835 1.00 35.25 C ANISOU 6155 CG LEU E 189 5191 4329 3874 439 -103 -873 C ATOM 6156 CD1 LEU E 189 35.579 14.393 200.577 1.00 36.91 C ANISOU 6156 CD1 LEU E 189 5340 4572 4112 406 -28 -1106 C ATOM 6157 CD2 LEU E 189 34.015 15.995 201.591 1.00 34.84 C ANISOU 6157 CD2 LEU E 189 5288 4358 3591 446 -82 -702 C ATOM 6158 N SER E 190 38.139 15.176 203.723 1.00 37.23 N ANISOU 6158 N SER E 190 5145 4409 4591 427 -209 -999 N ATOM 6159 CA SER E 190 38.875 16.300 204.247 1.00 37.78 C ANISOU 6159 CA SER E 190 5234 4517 4604 350 -143 -974 C ATOM 6160 C SER E 190 38.866 17.491 203.313 1.00 38.14 C ANISOU 6160 C SER E 190 5408 4666 4418 266 115 -1010 C ATOM 6161 O SER E 190 38.523 17.372 202.134 1.00 38.28 O ANISOU 6161 O SER E 190 5473 4746 4326 257 239 -1084 O ATOM 6162 CB SER E 190 40.305 15.918 204.563 1.00 39.37 C ANISOU 6162 CB SER E 190 5186 4667 5108 350 -226 -1124 C ATOM 6163 OG SER E 190 40.958 15.551 203.381 1.00 41.71 O ANISOU 6163 OG SER E 190 5313 4994 5541 358 -53 -1385 O ATOM 6164 N SER E 191 39.232 18.644 203.865 1.00 38.31 N ANISOU 6164 N SER E 191 5513 4693 4348 181 180 -948 N ATOM 6165 CA SER E 191 39.405 19.857 203.088 1.00 39.48 C ANISOU 6165 CA SER E 191 5803 4891 4307 74 410 -960 C ATOM 6166 C SER E 191 40.383 20.746 203.811 1.00 40.80 C ANISOU 6166 C SER E 191 5948 5038 4517 -48 453 -991 C ATOM 6167 O SER E 191 40.569 20.616 205.009 1.00 41.18 O ANISOU 6167 O SER E 191 5945 5044 4657 -42 284 -946 O ATOM 6168 CB SER E 191 38.099 20.608 202.927 1.00 38.26 C ANISOU 6168 CB SER E 191 5898 4717 3922 116 438 -765 C ATOM 6169 OG SER E 191 38.289 21.738 202.096 1.00 38.96 O ANISOU 6169 OG SER E 191 6153 4811 3838 10 623 -743 O ATOM 6170 N ARG E 192 41.008 21.654 203.078 1.00 42.26 N ANISOU 6170 N ARG E 192 6191 5255 4611 -195 674 -1065 N ATOM 6171 CA ARG E 192 42.049 22.484 203.638 1.00 43.44 C ANISOU 6171 CA ARG E 192 6292 5392 4820 -353 735 -1132 C ATOM 6172 C ARG E 192 41.702 23.932 203.343 1.00 43.45 C ANISOU 6172 C ARG E 192 6596 5327 4588 -469 913 -1015 C ATOM 6173 O ARG E 192 41.188 24.231 202.279 1.00 43.39 O ANISOU 6173 O ARG E 192 6760 5322 4404 -481 1038 -947 O ATOM 6174 CB ARG E 192 43.418 22.158 203.030 1.00 46.37 C ANISOU 6174 CB ARG E 192 6381 5853 5385 -469 864 -1386 C ATOM 6175 CG ARG E 192 43.813 20.680 202.990 1.00 48.18 C ANISOU 6175 CG ARG E 192 6286 6108 5912 -328 724 -1546 C ATOM 6176 CD ARG E 192 43.515 20.087 201.614 1.00 49.74 C ANISOU 6176 CD ARG E 192 6493 6368 6036 -308 905 -1668 C ATOM 6177 NE ARG E 192 44.191 18.822 201.370 1.00 52.64 N ANISOU 6177 NE ARG E 192 6518 6740 6744 -214 871 -1919 N ATOM 6178 CZ ARG E 192 43.574 17.649 201.360 1.00 53.06 C ANISOU 6178 CZ ARG E 192 6528 6725 6909 -34 705 -1915 C ATOM 6179 NH1 ARG E 192 42.273 17.599 201.603 1.00 51.28 N ANISOU 6179 NH1 ARG E 192 6560 6459 6466 48 565 -1671 N ATOM 6180 NH2 ARG E 192 44.247 16.528 201.107 1.00 55.74 N ANISOU 6180 NH2 ARG E 192 6551 7021 7608 60 686 -2170 N ATOM 6181 N LEU E 193 41.955 24.817 204.302 1.00 42.92 N ANISOU 6181 N LEU E 193 6612 5180 4516 -561 900 -984 N ATOM 6182 CA LEU E 193 41.875 26.249 204.070 1.00 43.01 C ANISOU 6182 CA LEU E 193 6895 5075 4373 -697 1079 -909 C ATOM 6183 C LEU E 193 43.216 26.839 204.462 1.00 44.86 C ANISOU 6183 C LEU E 193 7022 5323 4700 -939 1161 -1062 C ATOM 6184 O LEU E 193 43.711 26.623 205.581 1.00 44.82 O ANISOU 6184 O LEU E 193 6866 5344 4820 -968 1001 -1135 O ATOM 6185 CB LEU E 193 40.766 26.895 204.899 1.00 41.86 C ANISOU 6185 CB LEU E 193 6977 4779 4147 -587 1017 -759 C ATOM 6186 CG LEU E 193 40.822 28.419 205.056 1.00 43.26 C ANISOU 6186 CG LEU E 193 7417 4769 4252 -724 1170 -720 C ATOM 6187 CD1 LEU E 193 40.442 29.118 203.774 1.00 44.63 C ANISOU 6187 CD1 LEU E 193 7817 4841 4301 -740 1307 -581 C ATOM 6188 CD2 LEU E 193 39.949 28.888 206.186 1.00 42.79 C ANISOU 6188 CD2 LEU E 193 7496 4576 4187 -627 1120 -676 C ATOM 6189 N ARG E 194 43.815 27.583 203.544 1.00 46.00 N ANISOU 6189 N ARG E 194 7249 5458 4770 -1146 1398 -1105 N ATOM 6190 CA ARG E 194 45.080 28.209 203.849 1.00 47.31 C ANISOU 6190 CA ARG E 194 7300 5642 5034 -1415 1503 -1263 C ATOM 6191 C ARG E 194 44.965 29.726 203.826 1.00 48.58 C ANISOU 6191 C ARG E 194 7812 5603 5044 -1602 1666 -1164 C ATOM 6192 O ARG E 194 44.311 30.301 202.949 1.00 48.77 O ANISOU 6192 O ARG E 194 8132 5509 4889 -1599 1789 -998 O ATOM 6193 CB ARG E 194 46.154 27.719 202.886 1.00 48.45 C ANISOU 6193 CB ARG E 194 7169 5958 5280 -1567 1681 -1467 C ATOM 6194 CG ARG E 194 47.558 27.844 203.406 1.00 49.96 C ANISOU 6194 CG ARG E 194 7038 6237 5709 -1780 1700 -1694 C ATOM 6195 CD ARG E 194 48.470 26.984 202.612 1.00 51.43 C ANISOU 6195 CD ARG E 194 6838 6608 6095 -1826 1835 -1942 C ATOM 6196 NE ARG E 194 49.832 27.023 203.099 1.00 54.27 N ANISOU 6196 NE ARG E 194 6800 7064 6756 -2005 1827 -2179 N ATOM 6197 CZ ARG E 194 50.797 26.234 202.648 1.00 56.46 C ANISOU 6197 CZ ARG E 194 6620 7497 7335 -2025 1916 -2457 C ATOM 6198 NH1 ARG E 194 50.532 25.338 201.706 1.00 56.26 N ANISOU 6198 NH1 ARG E 194 6520 7539 7317 -1887 2040 -2545 N ATOM 6199 NH2 ARG E 194 52.021 26.339 203.147 1.00 59.15 N ANISOU 6199 NH2 ARG E 194 6561 7922 7992 -2183 1877 -2668 N ATOM 6200 N VAL E 195 45.573 30.366 204.821 1.00 49.69 N ANISOU 6200 N VAL E 195 7932 5684 5262 -1765 1635 -1255 N ATOM 6201 CA VAL E 195 45.706 31.825 204.846 1.00 52.33 C ANISOU 6201 CA VAL E 195 8573 5804 5507 -1996 1810 -1217 C ATOM 6202 C VAL E 195 47.135 32.187 205.231 1.00 54.65 C ANISOU 6202 C VAL E 195 8652 6179 5932 -2328 1875 -1435 C ATOM 6203 O VAL E 195 47.951 31.302 205.517 1.00 54.99 O ANISOU 6203 O VAL E 195 8293 6444 6158 -2337 1753 -1602 O ATOM 6204 CB VAL E 195 44.756 32.499 205.870 1.00 52.00 C ANISOU 6204 CB VAL E 195 8804 5536 5416 -1875 1717 -1126 C ATOM 6205 CG1 VAL E 195 43.280 32.461 205.396 1.00 50.63 C ANISOU 6205 CG1 VAL E 195 8859 5230 5148 -1573 1692 -905 C ATOM 6206 CG2 VAL E 195 44.948 31.889 207.275 1.00 50.74 C ANISOU 6206 CG2 VAL E 195 8440 5500 5336 -1835 1483 -1250 C ATOM 6207 N SER E 196 47.427 33.486 205.260 1.00 56.30 N ANISOU 6207 N SER E 196 9119 6192 6082 -2597 2045 -1435 N ATOM 6208 CA SER E 196 48.719 33.969 205.727 1.00 59.03 C ANISOU 6208 CA SER E 196 9280 6596 6551 -2949 2099 -1648 C ATOM 6209 C SER E 196 48.805 33.792 207.229 1.00 58.71 C ANISOU 6209 C SER E 196 9124 6594 6589 -2912 1821 -1749 C ATOM 6210 O SER E 196 47.778 33.731 207.913 1.00 57.12 O ANISOU 6210 O SER E 196 9124 6286 6292 -2686 1684 -1645 O ATOM 6211 CB SER E 196 48.887 35.448 205.415 1.00 61.57 C ANISOU 6211 CB SER E 196 9970 6647 6777 -3261 2348 -1605 C ATOM 6212 OG SER E 196 48.275 36.221 206.435 1.00 61.40 O ANISOU 6212 OG SER E 196 10235 6373 6719 -3220 2260 -1576 O ATOM 6213 N ALA E 197 50.032 33.737 207.742 1.00 60.91 N ANISOU 6213 N ALA E 197 9080 7033 7031 -3164 1739 -1957 N ATOM 6214 CA ALA E 197 50.266 33.568 209.176 1.00 60.73 C ANISOU 6214 CA ALA E 197 8950 7079 7048 -3197 1428 -2050 C ATOM 6215 C ALA E 197 49.885 34.818 209.952 1.00 61.70 C ANISOU 6215 C ALA E 197 9487 6951 7006 -3376 1494 -2064 C ATOM 6216 O ALA E 197 49.505 34.721 211.106 1.00 61.43 O ANISOU 6216 O ALA E 197 9546 6917 6879 -3331 1282 -2084 O ATOM 6217 CB ALA E 197 51.711 33.178 209.454 1.00 63.43 C ANISOU 6217 CB ALA E 197 8798 7662 7642 -3418 1277 -2262 C ATOM 6218 N THR E 198 49.980 35.977 209.300 1.00 63.13 N ANISOU 6218 N THR E 198 9936 6904 7146 -3594 1799 -2060 N ATOM 6219 CA THR E 198 49.449 37.234 209.815 1.00 64.00 C ANISOU 6219 CA THR E 198 10499 6682 7138 -3714 1920 -2063 C ATOM 6220 C THR E 198 47.939 37.128 210.063 1.00 61.51 C ANISOU 6220 C THR E 198 10473 6195 6705 -3336 1890 -1904 C ATOM 6221 O THR E 198 47.456 37.504 211.140 1.00 62.55 O ANISOU 6221 O THR E 198 10798 6211 6757 -3335 1830 -1989 O ATOM 6222 CB THR E 198 49.731 38.389 208.830 1.00 66.40 C ANISOU 6222 CB THR E 198 11060 6724 7444 -3973 2251 -2019 C ATOM 6223 OG1 THR E 198 51.142 38.532 208.661 1.00 69.13 O ANISOU 6223 OG1 THR E 198 11114 7242 7910 -4371 2316 -2202 O ATOM 6224 CG2 THR E 198 49.154 39.714 209.325 1.00 67.69 C ANISOU 6224 CG2 THR E 198 11704 6469 7547 -4069 2376 -2026 C ATOM 6225 N PHE E 199 47.217 36.576 209.089 1.00 58.68 N ANISOU 6225 N PHE E 199 10117 5845 6333 -3038 1935 -1702 N ATOM 6226 CA PHE E 199 45.761 36.439 209.174 1.00 56.04 C ANISOU 6226 CA PHE E 199 9997 5365 5931 -2671 1910 -1546 C ATOM 6227 C PHE E 199 45.282 35.502 210.297 1.00 53.43 C ANISOU 6227 C PHE E 199 9523 5225 5553 -2487 1671 -1598 C ATOM 6228 O PHE E 199 44.335 35.832 211.021 1.00 52.68 O ANISOU 6228 O PHE E 199 9646 4976 5393 -2364 1691 -1611 O ATOM 6229 CB PHE E 199 45.190 35.986 207.827 1.00 54.41 C ANISOU 6229 CB PHE E 199 9793 5169 5711 -2437 1969 -1322 C ATOM 6230 CG PHE E 199 43.720 36.233 207.682 1.00 53.45 C ANISOU 6230 CG PHE E 199 9931 4815 5563 -2113 1981 -1145 C ATOM 6231 CD1 PHE E 199 43.258 37.467 207.261 1.00 55.40 C ANISOU 6231 CD1 PHE E 199 10539 4679 5833 -2131 2138 -1036 C ATOM 6232 CD2 PHE E 199 42.796 35.227 207.953 1.00 50.66 C ANISOU 6232 CD2 PHE E 199 9444 4609 5196 -1790 1824 -1083 C ATOM 6233 CE1 PHE E 199 41.910 37.702 207.110 1.00 54.90 C ANISOU 6233 CE1 PHE E 199 10658 4387 5814 -1804 2120 -878 C ATOM 6234 CE2 PHE E 199 41.447 35.455 207.813 1.00 50.26 C ANISOU 6234 CE2 PHE E 199 9571 4361 5165 -1498 1837 -942 C ATOM 6235 CZ PHE E 199 41.002 36.696 207.382 1.00 52.62 C ANISOU 6235 CZ PHE E 199 10188 4282 5522 -1487 1976 -843 C ATOM 6236 N TRP E 200 45.939 34.349 210.424 1.00 52.04 N ANISOU 6236 N TRP E 200 8984 5366 5422 -2480 1459 -1630 N ATOM 6237 CA TRP E 200 45.632 33.373 211.474 1.00 50.63 C ANISOU 6237 CA TRP E 200 8678 5374 5187 -2356 1190 -1640 C ATOM 6238 C TRP E 200 46.032 33.874 212.876 1.00 52.85 C ANISOU 6238 C TRP E 200 9062 5659 5359 -2628 1080 -1814 C ATOM 6239 O TRP E 200 45.402 33.530 213.868 1.00 52.33 O ANISOU 6239 O TRP E 200 9097 5641 5147 -2570 956 -1818 O ATOM 6240 CB TRP E 200 46.296 32.021 211.161 1.00 49.55 C ANISOU 6240 CB TRP E 200 8128 5517 5182 -2269 966 -1614 C ATOM 6241 CG TRP E 200 46.372 31.092 212.337 1.00 49.67 C ANISOU 6241 CG TRP E 200 8003 5710 5161 -2246 625 -1619 C ATOM 6242 CD1 TRP E 200 47.485 30.770 213.063 1.00 52.45 C ANISOU 6242 CD1 TRP E 200 8111 6229 5591 -2448 350 -1719 C ATOM 6243 CD2 TRP E 200 45.285 30.397 212.951 1.00 47.69 C ANISOU 6243 CD2 TRP E 200 7867 5479 4776 -2039 502 -1502 C ATOM 6244 NE1 TRP E 200 47.153 29.905 214.086 1.00 51.84 N ANISOU 6244 NE1 TRP E 200 8028 6260 5409 -2378 35 -1638 N ATOM 6245 CE2 TRP E 200 45.807 29.666 214.036 1.00 49.06 C ANISOU 6245 CE2 TRP E 200 7904 5823 4914 -2145 151 -1512 C ATOM 6246 CE3 TRP E 200 43.924 30.311 212.684 1.00 45.55 C ANISOU 6246 CE3 TRP E 200 7786 5102 4419 -1790 644 -1385 C ATOM 6247 CZ2 TRP E 200 45.011 28.859 214.839 1.00 48.30 C ANISOU 6247 CZ2 TRP E 200 7901 5788 4663 -2039 -32 -1397 C ATOM 6248 CZ3 TRP E 200 43.133 29.521 213.491 1.00 44.36 C ANISOU 6248 CZ3 TRP E 200 7680 5028 4147 -1680 490 -1308 C ATOM 6249 CH2 TRP E 200 43.676 28.805 214.550 1.00 45.70 C ANISOU 6249 CH2 TRP E 200 7755 5361 4246 -1818 170 -1308 C ATOM 6250 N GLN E 201 47.056 34.720 212.951 1.00 55.18 N ANISOU 6250 N GLN E 201 9355 5909 5701 -2962 1144 -1966 N ATOM 6251 CA GLN E 201 47.483 35.276 214.226 1.00 57.73 C ANISOU 6251 CA GLN E 201 9798 6237 5900 -3270 1038 -2154 C ATOM 6252 C GLN E 201 46.796 36.583 214.616 1.00 59.43 C ANISOU 6252 C GLN E 201 10453 6124 6004 -3366 1309 -2265 C ATOM 6253 O GLN E 201 47.258 37.282 215.532 1.00 62.77 O ANISOU 6253 O GLN E 201 11018 6506 6326 -3691 1291 -2471 O ATOM 6254 CB GLN E 201 49.010 35.416 214.282 1.00 60.61 C ANISOU 6254 CB GLN E 201 9879 6757 6393 -3616 907 -2298 C ATOM 6255 CG GLN E 201 49.710 34.077 214.443 1.00 60.45 C ANISOU 6255 CG GLN E 201 9407 7063 6498 -3539 536 -2250 C ATOM 6256 CD GLN E 201 51.173 34.086 214.048 1.00 62.97 C ANISOU 6256 CD GLN E 201 9319 7535 7073 -3780 466 -2379 C ATOM 6257 OE1 GLN E 201 51.608 34.882 213.219 1.00 64.14 O ANISOU 6257 OE1 GLN E 201 9479 7571 7319 -3950 766 -2455 O ATOM 6258 NE2 GLN E 201 51.939 33.174 214.635 1.00 64.42 N ANISOU 6258 NE2 GLN E 201 9124 7969 7383 -3801 60 -2398 N ATOM 6259 N ASP E 202 45.705 36.907 213.923 1.00 57.40 N ANISOU 6259 N ASP E 202 10399 5623 5788 -3084 1543 -2140 N ATOM 6260 CA ASP E 202 44.850 38.045 214.258 1.00 58.86 C ANISOU 6260 CA ASP E 202 10972 5447 5946 -3071 1796 -2238 C ATOM 6261 C ASP E 202 43.585 37.508 214.926 1.00 56.70 C ANISOU 6261 C ASP E 202 10771 5210 5563 -2800 1782 -2222 C ATOM 6262 O ASP E 202 42.721 36.944 214.253 1.00 54.83 O ANISOU 6262 O ASP E 202 10460 4976 5398 -2453 1796 -2029 O ATOM 6263 CB ASP E 202 44.513 38.831 212.985 1.00 59.89 C ANISOU 6263 CB ASP E 202 11262 5247 6245 -2940 2034 -2088 C ATOM 6264 CG ASP E 202 43.475 39.925 213.211 1.00 62.09 C ANISOU 6264 CG ASP E 202 11906 5094 6590 -2821 2269 -2152 C ATOM 6265 OD1 ASP E 202 43.792 40.948 213.841 1.00 64.45 O ANISOU 6265 OD1 ASP E 202 12434 5162 6890 -3090 2399 -2376 O ATOM 6266 OD2 ASP E 202 42.340 39.768 212.712 1.00 61.61 O ANISOU 6266 OD2 ASP E 202 11887 4908 6615 -2451 2320 -1989 O ATOM 6267 N PRO E 203 43.469 37.685 216.261 1.00 57.95 N ANISOU 6267 N PRO E 203 11078 5411 5527 -2993 1766 -2441 N ATOM 6268 CA PRO E 203 42.448 37.085 217.151 1.00 55.98 C ANISOU 6268 CA PRO E 203 10890 5279 5102 -2859 1754 -2478 C ATOM 6269 C PRO E 203 41.004 37.497 216.870 1.00 54.61 C ANISOU 6269 C PRO E 203 10862 4829 5057 -2525 2041 -2472 C ATOM 6270 O PRO E 203 40.077 36.839 217.323 1.00 53.13 O ANISOU 6270 O PRO E 203 10644 4764 4778 -2361 2051 -2457 O ATOM 6271 CB PRO E 203 42.871 37.568 218.545 1.00 59.42 C ANISOU 6271 CB PRO E 203 11533 5766 5280 -3263 1739 -2770 C ATOM 6272 CG PRO E 203 44.302 37.948 218.413 1.00 61.50 C ANISOU 6272 CG PRO E 203 11708 6076 5581 -3592 1588 -2825 C ATOM 6273 CD PRO E 203 44.422 38.511 217.026 1.00 61.12 C ANISOU 6273 CD PRO E 203 11615 5772 5834 -3431 1764 -2694 C ATOM 6274 N ARG E 204 40.831 38.567 216.101 1.00 55.49 N ANISOU 6274 N ARG E 204 11117 4564 5402 -2431 2256 -2470 N ATOM 6275 CA ARG E 204 39.532 39.006 215.617 1.00 55.36 C ANISOU 6275 CA ARG E 204 11188 4242 5605 -2067 2470 -2418 C ATOM 6276 C ARG E 204 38.908 38.092 214.566 1.00 52.67 C ANISOU 6276 C ARG E 204 10618 4024 5370 -1699 2344 -2100 C ATOM 6277 O ARG E 204 37.709 38.174 214.307 1.00 53.13 O ANISOU 6277 O ARG E 204 10674 3923 5591 -1377 2453 -2048 O ATOM 6278 CB ARG E 204 39.670 40.382 214.995 1.00 57.05 C ANISOU 6278 CB ARG E 204 11633 3989 6055 -2087 2658 -2442 C ATOM 6279 CG ARG E 204 39.915 41.466 215.973 1.00 60.08 C ANISOU 6279 CG ARG E 204 12290 4127 6410 -2377 2859 -2794 C ATOM 6280 CD ARG E 204 40.193 42.723 215.228 1.00 62.22 C ANISOU 6280 CD ARG E 204 12787 3924 6931 -2420 2999 -2761 C ATOM 6281 NE ARG E 204 41.509 42.672 214.621 1.00 61.14 N ANISOU 6281 NE ARG E 204 12585 3925 6722 -2711 2854 -2628 N ATOM 6282 CZ ARG E 204 42.110 43.722 214.083 1.00 63.89 C ANISOU 6282 CZ ARG E 204 13140 3930 7205 -2913 2961 -2616 C ATOM 6283 NH1 ARG E 204 43.316 43.602 213.548 1.00 63.91 N ANISOU 6283 NH1 ARG E 204 13038 4107 7138 -3207 2860 -2520 N ATOM 6284 NH2 ARG E 204 41.507 44.903 214.074 1.00 67.03 N ANISOU 6284 NH2 ARG E 204 13843 3788 7836 -2827 3181 -2707 N ATOM 6285 N ASN E 205 39.712 37.236 213.947 1.00 50.28 N ANISOU 6285 N ASN E 205 10106 3997 5003 -1749 2117 -1912 N ATOM 6286 CA ASN E 205 39.214 36.403 212.872 1.00 48.39 C ANISOU 6286 CA ASN E 205 9675 3865 4847 -1445 2006 -1639 C ATOM 6287 C ASN E 205 38.573 35.069 213.281 1.00 47.28 C ANISOU 6287 C ASN E 205 9329 4031 4604 -1285 1860 -1580 C ATOM 6288 O ASN E 205 39.127 34.309 214.086 1.00 47.10 O ANISOU 6288 O ASN E 205 9211 4281 4405 -1467 1700 -1642 O ATOM 6289 CB ASN E 205 40.313 36.202 211.824 1.00 47.37 C ANISOU 6289 CB ASN E 205 9431 3834 4734 -1563 1899 -1492 C ATOM 6290 CG ASN E 205 40.509 37.434 210.944 1.00 48.87 C ANISOU 6290 CG ASN E 205 9846 3671 5053 -1619 2062 -1425 C ATOM 6291 OD1 ASN E 205 39.608 37.807 210.183 1.00 48.20 O ANISOU 6291 OD1 ASN E 205 9870 3350 5094 -1362 2121 -1257 O ATOM 6292 ND2 ASN E 205 41.683 38.072 211.050 1.00 49.98 N ANISOU 6292 ND2 ASN E 205 10056 3765 5169 -1971 2113 -1542 N ATOM 6293 N HIS E 206 37.408 34.784 212.700 1.00 47.42 N ANISOU 6293 N HIS E 206 9281 3992 4744 -955 1891 -1441 N ATOM 6294 CA HIS E 206 36.681 33.543 212.977 1.00 46.74 C ANISOU 6294 CA HIS E 206 9007 4164 4589 -805 1777 -1373 C ATOM 6295 C HIS E 206 36.656 32.583 211.772 1.00 44.84 C ANISOU 6295 C HIS E 206 8561 4073 4404 -620 1595 -1126 C ATOM 6296 O HIS E 206 36.355 32.983 210.654 1.00 45.36 O ANISOU 6296 O HIS E 206 8651 3983 4599 -454 1621 -982 O ATOM 6297 CB HIS E 206 35.260 33.872 213.426 1.00 48.19 C ANISOU 6297 CB HIS E 206 9231 4204 4874 -603 1972 -1467 C ATOM 6298 CG HIS E 206 34.434 32.669 213.737 1.00 47.62 C ANISOU 6298 CG HIS E 206 8975 4383 4735 -488 1896 -1410 C ATOM 6299 ND1 HIS E 206 33.173 32.475 213.216 1.00 48.07 N ANISOU 6299 ND1 HIS E 206 8897 4388 4978 -184 1943 -1324 N ATOM 6300 CD2 HIS E 206 34.692 31.585 214.508 1.00 47.02 C ANISOU 6300 CD2 HIS E 206 8830 4600 4435 -655 1757 -1412 C ATOM 6301 CE1 HIS E 206 32.687 31.328 213.660 1.00 46.76 C ANISOU 6301 CE1 HIS E 206 8587 4481 4700 -188 1871 -1296 C ATOM 6302 NE2 HIS E 206 33.589 30.769 214.446 1.00 45.89 N ANISOU 6302 NE2 HIS E 206 8535 4568 4335 -471 1756 -1335 N ATOM 6303 N PHE E 207 36.964 31.313 212.016 1.00 43.79 N ANISOU 6303 N PHE E 207 8248 4227 4164 -663 1400 -1077 N ATOM 6304 CA PHE E 207 36.985 30.269 210.977 1.00 42.18 C ANISOU 6304 CA PHE E 207 7843 4174 4007 -514 1237 -898 C ATOM 6305 C PHE E 207 35.949 29.187 211.259 1.00 41.60 C ANISOU 6305 C PHE E 207 7643 4243 3918 -355 1156 -834 C ATOM 6306 O PHE E 207 35.886 28.678 212.370 1.00 41.97 O ANISOU 6306 O PHE E 207 7691 4411 3845 -472 1107 -901 O ATOM 6307 CB PHE E 207 38.365 29.613 210.922 1.00 40.99 C ANISOU 6307 CB PHE E 207 7550 4205 3820 -696 1063 -912 C ATOM 6308 CG PHE E 207 39.464 30.576 210.628 1.00 42.65 C ANISOU 6308 CG PHE E 207 7837 4315 4054 -898 1149 -990 C ATOM 6309 CD1 PHE E 207 40.251 31.089 211.647 1.00 44.02 C ANISOU 6309 CD1 PHE E 207 8082 4487 4156 -1162 1141 -1147 C ATOM 6310 CD2 PHE E 207 39.692 30.997 209.323 1.00 42.27 C ANISOU 6310 CD2 PHE E 207 7811 4176 4075 -863 1241 -904 C ATOM 6311 CE1 PHE E 207 41.240 32.004 211.361 1.00 46.02 C ANISOU 6311 CE1 PHE E 207 8397 4642 4447 -1376 1232 -1230 C ATOM 6312 CE2 PHE E 207 40.686 31.891 209.038 1.00 44.17 C ANISOU 6312 CE2 PHE E 207 8134 4321 4329 -1090 1348 -971 C ATOM 6313 CZ PHE E 207 41.468 32.399 210.054 1.00 45.86 C ANISOU 6313 CZ PHE E 207 8388 4526 4513 -1344 1349 -1141 C ATOM 6314 N ARG E 208 35.142 28.838 210.264 1.00 41.38 N ANISOU 6314 N ARG E 208 7524 4208 3990 -123 1132 -698 N ATOM 6315 CA ARG E 208 34.122 27.827 210.453 1.00 41.34 C ANISOU 6315 CA ARG E 208 7383 4332 3993 8 1065 -643 C ATOM 6316 C ARG E 208 34.025 26.891 209.266 1.00 41.18 C ANISOU 6316 C ARG E 208 7207 4415 4023 140 909 -499 C ATOM 6317 O ARG E 208 33.804 27.310 208.129 1.00 41.81 O ANISOU 6317 O ARG E 208 7307 4412 4165 261 920 -408 O ATOM 6318 CB ARG E 208 32.768 28.466 210.714 1.00 43.18 C ANISOU 6318 CB ARG E 208 7644 4432 4329 167 1239 -686 C ATOM 6319 CG ARG E 208 31.625 27.471 210.768 1.00 43.03 C ANISOU 6319 CG ARG E 208 7450 4551 4349 293 1192 -632 C ATOM 6320 CD ARG E 208 30.353 28.113 211.249 1.00 45.22 C ANISOU 6320 CD ARG E 208 7701 4717 4763 421 1403 -738 C ATOM 6321 NE ARG E 208 29.213 27.559 210.535 1.00 45.67 N ANISOU 6321 NE ARG E 208 7547 4829 4977 638 1329 -630 N ATOM 6322 CZ ARG E 208 28.597 28.182 209.537 1.00 46.85 C ANISOU 6322 CZ ARG E 208 7640 4826 5336 878 1291 -535 C ATOM 6323 NH1 ARG E 208 29.010 29.378 209.150 1.00 48.17 N ANISOU 6323 NH1 ARG E 208 7973 4750 5579 930 1339 -520 N ATOM 6324 NH2 ARG E 208 27.560 27.620 208.938 1.00 46.93 N ANISOU 6324 NH2 ARG E 208 7437 4914 5479 1051 1185 -442 N ATOM 6325 N CYS E 209 34.206 25.609 209.550 1.00 41.23 N ANISOU 6325 N CYS E 209 7083 4592 3989 96 752 -479 N ATOM 6326 CA CYS E 209 33.997 24.561 208.577 1.00 40.58 C ANISOU 6326 CA CYS E 209 6852 4607 3961 207 615 -388 C ATOM 6327 C CYS E 209 32.560 24.066 208.664 1.00 39.61 C ANISOU 6327 C CYS E 209 6651 4520 3879 339 614 -333 C ATOM 6328 O CYS E 209 32.070 23.808 209.747 1.00 40.66 O ANISOU 6328 O CYS E 209 6789 4691 3970 274 652 -371 O ATOM 6329 CB CYS E 209 34.935 23.411 208.886 1.00 41.09 C ANISOU 6329 CB CYS E 209 6806 4784 4023 101 437 -406 C ATOM 6330 SG CYS E 209 34.754 22.126 207.712 1.00 42.86 S ANISOU 6330 SG CYS E 209 6860 5089 4335 220 303 -356 S ATOM 6331 N GLN E 210 31.885 23.939 207.532 1.00 38.69 N ANISOU 6331 N GLN E 210 6465 4407 3828 494 572 -251 N ATOM 6332 CA GLN E 210 30.476 23.547 207.522 1.00 37.95 C ANISOU 6332 CA GLN E 210 6253 4354 3813 619 560 -208 C ATOM 6333 C GLN E 210 30.231 22.392 206.544 1.00 36.62 C ANISOU 6333 C GLN E 210 5957 4300 3658 665 387 -142 C ATOM 6334 O GLN E 210 30.666 22.450 205.390 1.00 36.60 O ANISOU 6334 O GLN E 210 5985 4300 3620 690 322 -103 O ATOM 6335 CB GLN E 210 29.620 24.745 207.146 1.00 39.50 C ANISOU 6335 CB GLN E 210 6476 4409 4122 785 655 -176 C ATOM 6336 CG GLN E 210 28.209 24.390 206.749 1.00 40.96 C ANISOU 6336 CG GLN E 210 6476 4643 4442 947 591 -119 C ATOM 6337 CD GLN E 210 27.361 25.602 206.428 1.00 43.61 C ANISOU 6337 CD GLN E 210 6802 4805 4964 1150 644 -80 C ATOM 6338 OE1 GLN E 210 27.868 26.716 206.337 1.00 45.18 O ANISOU 6338 OE1 GLN E 210 7174 4817 5175 1168 718 -72 O ATOM 6339 NE2 GLN E 210 26.058 25.396 206.278 1.00 45.05 N ANISOU 6339 NE2 GLN E 210 6765 5026 5326 1302 597 -59 N ATOM 6340 N VAL E 211 29.583 21.326 207.020 1.00 34.99 N ANISOU 6340 N VAL E 211 5631 4184 3478 635 327 -143 N ATOM 6341 CA VAL E 211 29.224 20.192 206.175 1.00 33.41 C ANISOU 6341 CA VAL E 211 5313 4073 3309 661 171 -107 C ATOM 6342 C VAL E 211 27.718 19.996 206.160 1.00 34.41 C ANISOU 6342 C VAL E 211 5290 4254 3531 739 166 -75 C ATOM 6343 O VAL E 211 27.107 19.716 207.193 1.00 35.60 O ANISOU 6343 O VAL E 211 5382 4433 3710 671 251 -104 O ATOM 6344 CB VAL E 211 29.860 18.899 206.662 1.00 32.71 C ANISOU 6344 CB VAL E 211 5200 4016 3212 534 66 -134 C ATOM 6345 CG1 VAL E 211 29.401 17.718 205.806 1.00 32.28 C ANISOU 6345 CG1 VAL E 211 5033 4019 3214 552 -75 -130 C ATOM 6346 CG2 VAL E 211 31.374 19.011 206.627 1.00 32.34 C ANISOU 6346 CG2 VAL E 211 5224 3925 3138 474 43 -186 C ATOM 6347 N GLN E 212 27.111 20.178 204.993 1.00 34.37 N ANISOU 6347 N GLN E 212 5220 4274 3567 858 67 -17 N ATOM 6348 CA GLN E 212 25.698 19.917 204.831 1.00 34.26 C ANISOU 6348 CA GLN E 212 5007 4329 3680 934 12 10 C ATOM 6349 C GLN E 212 25.540 18.459 204.427 1.00 32.94 C ANISOU 6349 C GLN E 212 4754 4269 3492 830 -135 -6 C ATOM 6350 O GLN E 212 26.168 17.993 203.480 1.00 31.63 O ANISOU 6350 O GLN E 212 4660 4125 3235 798 -252 -13 O ATOM 6351 CB GLN E 212 25.115 20.845 203.774 1.00 36.38 C ANISOU 6351 CB GLN E 212 5252 4561 4010 1109 -90 107 C ATOM 6352 CG GLN E 212 23.772 20.412 203.234 1.00 37.72 C ANISOU 6352 CG GLN E 212 5183 4834 4314 1184 -249 147 C ATOM 6353 CD GLN E 212 22.647 20.687 204.191 1.00 39.10 C ANISOU 6353 CD GLN E 212 5124 5007 4724 1257 -109 84 C ATOM 6354 OE1 GLN E 212 22.178 21.815 204.283 1.00 41.36 O ANISOU 6354 OE1 GLN E 212 5355 5179 5182 1435 -52 101 O ATOM 6355 NE2 GLN E 212 22.192 19.660 204.896 1.00 38.51 N ANISOU 6355 NE2 GLN E 212 4911 5044 4678 1113 -40 0 N ATOM 6356 N PHE E 213 24.717 17.736 205.175 1.00 33.25 N ANISOU 6356 N PHE E 213 4650 4366 3616 750 -100 -34 N ATOM 6357 CA PHE E 213 24.525 16.304 204.972 1.00 32.63 C ANISOU 6357 CA PHE E 213 4507 4346 3544 620 -225 -53 C ATOM 6358 C PHE E 213 23.114 16.062 204.523 1.00 34.09 C ANISOU 6358 C PHE E 213 4456 4639 3857 647 -302 -47 C ATOM 6359 O PHE E 213 22.194 16.699 205.014 1.00 35.98 O ANISOU 6359 O PHE E 213 4537 4910 4223 714 -191 -53 O ATOM 6360 CB PHE E 213 24.770 15.566 206.284 1.00 32.22 C ANISOU 6360 CB PHE E 213 4512 4259 3472 443 -139 -64 C ATOM 6361 CG PHE E 213 24.400 14.094 206.264 1.00 32.83 C ANISOU 6361 CG PHE E 213 4530 4348 3596 289 -254 -64 C ATOM 6362 CD1 PHE E 213 25.155 13.170 205.521 1.00 32.04 C ANISOU 6362 CD1 PHE E 213 4498 4180 3497 266 -419 -94 C ATOM 6363 CD2 PHE E 213 23.321 13.624 207.026 1.00 33.51 C ANISOU 6363 CD2 PHE E 213 4497 4495 3740 145 -169 -56 C ATOM 6364 CE1 PHE E 213 24.830 11.801 205.528 1.00 32.42 C ANISOU 6364 CE1 PHE E 213 4512 4184 3620 120 -525 -105 C ATOM 6365 CE2 PHE E 213 22.992 12.277 207.033 1.00 34.27 C ANISOU 6365 CE2 PHE E 213 4567 4571 3882 -30 -271 -44 C ATOM 6366 CZ PHE E 213 23.744 11.358 206.277 1.00 33.49 C ANISOU 6366 CZ PHE E 213 4555 4369 3803 -34 -464 -63 C ATOM 6367 N TYR E 214 22.947 15.136 203.593 1.00 34.29 N ANISOU 6367 N TYR E 214 4439 4720 3868 588 -486 -63 N ATOM 6368 CA TYR E 214 21.630 14.752 203.141 1.00 36.25 C ANISOU 6368 CA TYR E 214 4446 5089 4238 571 -601 -67 C ATOM 6369 C TYR E 214 21.438 13.307 203.543 1.00 37.13 C ANISOU 6369 C TYR E 214 4525 5201 4381 352 -617 -123 C ATOM 6370 O TYR E 214 22.215 12.425 203.146 1.00 35.95 O ANISOU 6370 O TYR E 214 4522 4981 4158 265 -706 -166 O ATOM 6371 CB TYR E 214 21.498 14.928 201.623 1.00 36.63 C ANISOU 6371 CB TYR E 214 4499 5209 4212 647 -838 -38 C ATOM 6372 CG TYR E 214 21.695 16.364 201.182 1.00 36.26 C ANISOU 6372 CG TYR E 214 4531 5122 4125 843 -854 64 C ATOM 6373 CD1 TYR E 214 22.942 16.832 200.807 1.00 33.73 C ANISOU 6373 CD1 TYR E 214 4478 4720 3618 858 -811 80 C ATOM 6374 CD2 TYR E 214 20.630 17.256 201.166 1.00 37.99 C ANISOU 6374 CD2 TYR E 214 4543 5363 4529 1010 -907 139 C ATOM 6375 CE1 TYR E 214 23.117 18.121 200.434 1.00 34.02 C ANISOU 6375 CE1 TYR E 214 4618 4691 3617 1000 -820 189 C ATOM 6376 CE2 TYR E 214 20.806 18.553 200.780 1.00 38.04 C ANISOU 6376 CE2 TYR E 214 4646 5276 4532 1192 -944 253 C ATOM 6377 CZ TYR E 214 22.052 18.973 200.413 1.00 36.40 C ANISOU 6377 CZ TYR E 214 4751 4980 4099 1170 -900 288 C ATOM 6378 OH TYR E 214 22.239 20.269 200.022 1.00 38.05 O ANISOU 6378 OH TYR E 214 5092 5069 4297 1318 -934 420 O ATOM 6379 N GLY E 215 20.424 13.076 204.366 1.00 38.93 N ANISOU 6379 N GLY E 215 4562 5490 4739 253 -507 -133 N ATOM 6380 CA GLY E 215 20.117 11.746 204.805 1.00 41.14 C ANISOU 6380 CA GLY E 215 4823 5755 5053 7 -513 -159 C ATOM 6381 C GLY E 215 18.626 11.586 204.776 1.00 46.03 C ANISOU 6381 C GLY E 215 5115 6528 5847 -68 -505 -199 C ATOM 6382 O GLY E 215 17.987 11.678 203.716 1.00 47.97 O ANISOU 6382 O GLY E 215 5179 6881 6169 11 -698 -220 O ATOM 6383 N LEU E 216 18.056 11.375 205.951 1.00 48.45 N ANISOU 6383 N LEU E 216 5337 6861 6209 -241 -283 -211 N ATOM 6384 CA LEU E 216 16.660 11.011 206.021 1.00 52.42 C ANISOU 6384 CA LEU E 216 5500 7515 6903 -379 -239 -278 C ATOM 6385 C LEU E 216 15.742 12.210 205.994 1.00 55.16 C ANISOU 6385 C LEU E 216 5511 7994 7455 -169 -142 -337 C ATOM 6386 O LEU E 216 16.137 13.324 206.312 1.00 54.42 O ANISOU 6386 O LEU E 216 5486 7847 7343 33 -17 -330 O ATOM 6387 CB LEU E 216 16.394 10.159 207.257 1.00 53.64 C ANISOU 6387 CB LEU E 216 5713 7648 7019 -719 -19 -275 C ATOM 6388 CG LEU E 216 17.181 8.853 207.219 1.00 52.62 C ANISOU 6388 CG LEU E 216 5888 7337 6767 -917 -176 -199 C ATOM 6389 CD1 LEU E 216 16.877 8.005 208.432 1.00 54.55 C ANISOU 6389 CD1 LEU E 216 6234 7537 6957 -1285 4 -145 C ATOM 6390 CD2 LEU E 216 16.849 8.097 205.938 1.00 53.48 C ANISOU 6390 CD2 LEU E 216 5883 7461 6977 -930 -449 -258 C ATOM 6391 N SER E 217 14.511 11.954 205.576 1.00 59.64 N ANISOU 6391 N SER E 217 5696 8715 8249 -217 -221 -403 N ATOM 6392 CA SER E 217 13.411 12.887 205.722 1.00 63.87 C ANISOU 6392 CA SER E 217 5808 9375 9086 -52 -108 -490 C ATOM 6393 C SER E 217 13.024 12.893 207.203 1.00 66.26 C ANISOU 6393 C SER E 217 6039 9713 9423 -257 338 -604 C ATOM 6394 O SER E 217 13.282 11.926 207.925 1.00 66.34 O ANISOU 6394 O SER E 217 6263 9698 9247 -589 474 -585 O ATOM 6395 CB SER E 217 12.241 12.415 204.846 1.00 67.00 C ANISOU 6395 CB SER E 217 5793 9941 9724 -95 -362 -534 C ATOM 6396 OG SER E 217 10.976 12.748 205.397 1.00 71.24 O ANISOU 6396 OG SER E 217 5836 10624 10609 -105 -154 -675 O ATOM 6397 N GLU E 218 12.377 13.949 207.674 1.00 68.92 N ANISOU 6397 N GLU E 218 6086 10101 10001 -85 574 -728 N ATOM 6398 CA GLU E 218 11.971 13.954 209.074 1.00 71.81 C ANISOU 6398 CA GLU E 218 6389 10529 10365 -326 1048 -881 C ATOM 6399 C GLU E 218 10.674 13.153 209.372 1.00 75.87 C ANISOU 6399 C GLU E 218 6488 11244 11095 -628 1210 -1019 C ATOM 6400 O GLU E 218 10.147 13.213 210.483 1.00 78.66 O ANISOU 6400 O GLU E 218 6719 11690 11477 -852 1648 -1184 O ATOM 6401 CB GLU E 218 11.902 15.394 209.611 1.00 73.58 C ANISOU 6401 CB GLU E 218 6510 10699 10746 -57 1323 -1019 C ATOM 6402 CG GLU E 218 12.520 15.560 211.007 1.00 73.35 C ANISOU 6402 CG GLU E 218 6830 10625 10415 -285 1734 -1091 C ATOM 6403 CD GLU E 218 13.134 16.931 211.230 1.00 72.51 C ANISOU 6403 CD GLU E 218 6876 10364 10310 10 1846 -1146 C ATOM 6404 OE1 GLU E 218 12.394 17.832 211.690 1.00 75.99 O ANISOU 6404 OE1 GLU E 218 7009 10823 11041 142 2156 -1378 O ATOM 6405 OE2 GLU E 218 14.353 17.095 210.965 1.00 68.10 O ANISOU 6405 OE2 GLU E 218 6732 9657 9488 96 1644 -980 O ATOM 6406 N ASN E 219 10.190 12.382 208.397 1.00 76.47 N ANISOU 6406 N ASN E 219 6366 11395 11293 -677 874 -965 N ATOM 6407 CA ASN E 219 8.992 11.562 208.564 1.00 80.58 C ANISOU 6407 CA ASN E 219 6484 12105 12028 -991 984 -1091 C ATOM 6408 C ASN E 219 9.261 10.068 208.565 1.00 79.32 C ANISOU 6408 C ASN E 219 6612 11906 11621 -1406 879 -984 C ATOM 6409 O ASN E 219 8.334 9.265 208.543 1.00 81.82 O ANISOU 6409 O ASN E 219 6635 12357 12096 -1702 910 -1066 O ATOM 6410 CB ASN E 219 8.004 11.869 207.451 1.00 84.08 C ANISOU 6410 CB ASN E 219 6381 12682 12884 -749 663 -1146 C ATOM 6411 CG ASN E 219 7.732 13.338 207.323 1.00 86.13 C ANISOU 6411 CG ASN E 219 6352 12920 13454 -294 684 -1217 C ATOM 6412 OD1 ASN E 219 7.746 14.063 208.315 1.00 87.46 O ANISOU 6412 OD1 ASN E 219 6508 13053 13669 -247 1103 -1354 O ATOM 6413 ND2 ASN E 219 7.481 13.795 206.102 1.00 87.15 N ANISOU 6413 ND2 ASN E 219 6268 13053 13791 30 223 -1125 N ATOM 6414 N ASP E 220 10.529 9.690 208.593 1.00 75.53 N ANISOU 6414 N ASP E 220 6690 11222 10787 -1429 753 -812 N ATOM 6415 CA ASP E 220 10.882 8.293 208.408 1.00 75.02 C ANISOU 6415 CA ASP E 220 6908 11047 10547 -1744 575 -704 C ATOM 6416 C ASP E 220 10.915 7.466 209.690 1.00 76.29 C ANISOU 6416 C ASP E 220 7321 11154 10512 -2204 886 -660 C ATOM 6417 O ASP E 220 11.008 7.999 210.793 1.00 76.63 O ANISOU 6417 O ASP E 220 7462 11227 10427 -2282 1235 -685 O ATOM 6418 CB ASP E 220 12.189 8.181 207.625 1.00 71.08 C ANISOU 6418 CB ASP E 220 6824 10341 9840 -1528 236 -560 C ATOM 6419 CG ASP E 220 12.086 8.814 206.247 1.00 70.83 C ANISOU 6419 CG ASP E 220 6592 10378 9943 -1173 -98 -582 C ATOM 6420 OD1 ASP E 220 13.130 9.065 205.600 1.00 67.65 O ANISOU 6420 OD1 ASP E 220 6485 9845 9371 -954 -307 -497 O ATOM 6421 OD2 ASP E 220 10.942 9.069 205.812 1.00 74.19 O ANISOU 6421 OD2 ASP E 220 6550 10994 10645 -1129 -158 -681 O ATOM 6422 N GLU E 221 10.826 6.153 209.502 1.00 77.35 N ANISOU 6422 N GLU E 221 7579 11198 10613 -2528 741 -593 N ATOM 6423 CA GLU E 221 10.745 5.159 210.568 1.00 79.71 C ANISOU 6423 CA GLU E 221 8132 11414 10741 -3028 962 -507 C ATOM 6424 C GLU E 221 12.085 5.023 211.296 1.00 76.87 C ANISOU 6424 C GLU E 221 8364 10803 10040 -3046 938 -296 C ATOM 6425 O GLU E 221 13.102 4.717 210.675 1.00 73.93 O ANISOU 6425 O GLU E 221 8273 10211 9607 -2849 608 -185 O ATOM 6426 CB GLU E 221 10.302 3.819 209.936 1.00 82.17 C ANISOU 6426 CB GLU E 221 8404 11645 11170 -3320 737 -495 C ATOM 6427 CG GLU E 221 10.557 2.525 210.729 1.00 84.03 C ANISOU 6427 CG GLU E 221 9060 11648 11221 -3807 791 -323 C ATOM 6428 CD GLU E 221 9.291 1.932 211.335 1.00 89.34 C ANISOU 6428 CD GLU E 221 9477 12482 11988 -4325 1096 -404 C ATOM 6429 OE1 GLU E 221 8.832 2.442 212.380 1.00 91.77 O ANISOU 6429 OE1 GLU E 221 9694 12972 12202 -4513 1516 -456 O ATOM 6430 OE2 GLU E 221 8.764 0.943 210.779 1.00 91.41 O ANISOU 6430 OE2 GLU E 221 9635 12689 12409 -4575 940 -437 O ATOM 6431 N TRP E 222 12.091 5.270 212.605 1.00 78.29 N ANISOU 6431 N TRP E 222 8718 11028 9999 -3290 1285 -259 N ATOM 6432 CA TRP E 222 13.325 5.168 213.386 1.00 76.31 C ANISOU 6432 CA TRP E 222 9020 10563 9411 -3339 1229 -43 C ATOM 6433 C TRP E 222 13.124 4.606 214.797 1.00 80.41 C ANISOU 6433 C TRP E 222 9837 11077 9638 -3883 1516 80 C ATOM 6434 O TRP E 222 12.553 5.263 215.667 1.00 82.67 O ANISOU 6434 O TRP E 222 10014 11585 9811 -4054 1935 -50 O ATOM 6435 CB TRP E 222 14.045 6.516 213.446 1.00 72.71 C ANISOU 6435 CB TRP E 222 8601 10150 8875 -2936 1269 -96 C ATOM 6436 CG TRP E 222 15.502 6.385 213.794 1.00 69.63 C ANISOU 6436 CG TRP E 222 8716 9516 8226 -2868 1046 120 C ATOM 6437 CD1 TRP E 222 16.083 6.663 214.991 1.00 70.10 C ANISOU 6437 CD1 TRP E 222 9125 9551 7960 -3046 1194 226 C ATOM 6438 CD2 TRP E 222 16.558 5.924 212.936 1.00 66.31 C ANISOU 6438 CD2 TRP E 222 8481 8850 7863 -2620 630 236 C ATOM 6439 NE1 TRP E 222 17.432 6.412 214.937 1.00 67.29 N ANISOU 6439 NE1 TRP E 222 9131 8949 7486 -2906 858 422 N ATOM 6440 CE2 TRP E 222 17.749 5.958 213.685 1.00 64.96 C ANISOU 6440 CE2 TRP E 222 8727 8511 7444 -2635 532 416 C ATOM 6441 CE3 TRP E 222 16.610 5.487 211.609 1.00 64.90 C ANISOU 6441 CE3 TRP E 222 8150 8590 7919 -2406 341 183 C ATOM 6442 CZ2 TRP E 222 18.981 5.571 213.152 1.00 62.53 C ANISOU 6442 CZ2 TRP E 222 8634 7948 7176 -2415 169 531 C ATOM 6443 CZ3 TRP E 222 17.836 5.105 211.081 1.00 62.34 C ANISOU 6443 CZ3 TRP E 222 8079 8016 7593 -2209 23 276 C ATOM 6444 CH2 TRP E 222 19.002 5.145 211.853 1.00 61.21 C ANISOU 6444 CH2 TRP E 222 8297 7700 7260 -2203 -54 443 C ATOM 6445 N THR E 223 13.624 3.387 215.004 1.00 81.84 N ANISOU 6445 N THR E 223 10416 10983 9696 -4159 1282 330 N ATOM 6446 CA THR E 223 13.473 2.643 216.259 1.00 86.05 C ANISOU 6446 CA THR E 223 11316 11454 9926 -4734 1465 525 C ATOM 6447 C THR E 223 14.764 2.675 217.080 1.00 85.20 C ANISOU 6447 C THR E 223 11768 11137 9466 -4745 1290 797 C ATOM 6448 O THR E 223 14.771 2.310 218.263 1.00 88.88 O ANISOU 6448 O THR E 223 12606 11581 9583 -5210 1436 985 O ATOM 6449 CB THR E 223 13.149 1.154 215.976 1.00 88.37 C ANISOU 6449 CB THR E 223 11721 11514 10341 -5076 1268 671 C ATOM 6450 OG1 THR E 223 12.612 1.022 214.657 1.00 86.93 O ANISOU 6450 OG1 THR E 223 11101 11380 10549 -4829 1116 465 O ATOM 6451 CG2 THR E 223 12.157 0.573 217.007 1.00 94.19 C ANISOU 6451 CG2 THR E 223 12526 12367 10895 -5747 1647 717 C ATOM 6452 N GLN E 224 15.850 3.110 216.443 1.00 80.71 N ANISOU 6452 N GLN E 224 11257 10428 8983 -4257 968 819 N ATOM 6453 CA GLN E 224 17.204 2.942 216.980 1.00 79.47 C ANISOU 6453 CA GLN E 224 11580 10013 8601 -4212 670 1090 C ATOM 6454 C GLN E 224 17.528 3.934 218.096 1.00 79.76 C ANISOU 6454 C GLN E 224 11814 10231 8261 -4303 907 1095 C ATOM 6455 O GLN E 224 16.805 4.913 218.290 1.00 80.58 O ANISOU 6455 O GLN E 224 11644 10641 8334 -4287 1312 837 O ATOM 6456 CB GLN E 224 18.239 3.045 215.854 1.00 75.41 C ANISOU 6456 CB GLN E 224 11004 9304 8344 -3681 279 1065 C ATOM 6457 CG GLN E 224 17.791 2.423 214.525 1.00 74.74 C ANISOU 6457 CG GLN E 224 10624 9142 8633 -3519 126 926 C ATOM 6458 CD GLN E 224 17.563 0.933 214.605 1.00 77.97 C ANISOU 6458 CD GLN E 224 11232 9268 9125 -3872 -42 1098 C ATOM 6459 OE1 GLN E 224 18.372 0.199 215.169 1.00 79.25 O ANISOU 6459 OE1 GLN E 224 11800 9113 9199 -4000 -291 1370 O ATOM 6460 NE2 GLN E 224 16.456 0.474 214.029 1.00 79.70 N ANISOU 6460 NE2 GLN E 224 11161 9582 9539 -4031 68 946 N ATOM 6461 N ASP E 225 18.612 3.677 218.826 1.00 79.39 N ANISOU 6461 N ASP E 225 12233 9982 7950 -4398 642 1376 N ATOM 6462 CA ASP E 225 18.930 4.461 220.018 1.00 80.04 C ANISOU 6462 CA ASP E 225 12588 10227 7598 -4598 837 1410 C ATOM 6463 C ASP E 225 19.693 5.752 219.764 1.00 76.10 C ANISOU 6463 C ASP E 225 11975 9823 7116 -4153 826 1237 C ATOM 6464 O ASP E 225 19.627 6.681 220.572 1.00 77.61 O ANISOU 6464 O ASP E 225 12246 10228 7014 -4276 1127 1115 O ATOM 6465 CB ASP E 225 19.651 3.609 221.064 1.00 82.96 C ANISOU 6465 CB ASP E 225 13541 10367 7614 -4991 543 1820 C ATOM 6466 CG ASP E 225 18.729 3.178 222.188 1.00 88.51 C ANISOU 6466 CG ASP E 225 14491 11212 7926 -5664 887 1916 C ATOM 6467 OD1 ASP E 225 17.567 2.817 221.900 1.00 90.12 O ANISOU 6467 OD1 ASP E 225 14422 11527 8290 -5854 1188 1767 O ATOM 6468 OD2 ASP E 225 19.156 3.212 223.361 1.00 91.33 O ANISOU 6468 OD2 ASP E 225 15314 11588 7800 -6033 864 2132 O ATOM 6469 N ARG E 226 20.416 5.824 218.652 1.00 71.51 N ANISOU 6469 N ARG E 226 11222 9083 6867 -3665 505 1206 N ATOM 6470 CA ARG E 226 21.082 7.076 218.281 1.00 67.24 C ANISOU 6470 CA ARG E 226 10546 8628 6375 -3251 517 1030 C ATOM 6471 C ARG E 226 20.066 8.044 217.680 1.00 65.54 C ANISOU 6471 C ARG E 226 9882 8664 6358 -3043 893 693 C ATOM 6472 O ARG E 226 18.971 7.619 217.278 1.00 67.32 O ANISOU 6472 O ARG E 226 9839 8971 6770 -3135 1045 598 O ATOM 6473 CB ARG E 226 22.229 6.824 217.298 1.00 63.74 C ANISOU 6473 CB ARG E 226 10078 7940 6202 -2842 78 1102 C ATOM 6474 CG ARG E 226 21.859 5.987 216.086 1.00 62.25 C ANISOU 6474 CG ARG E 226 9649 7621 6383 -2679 -75 1057 C ATOM 6475 CD ARG E 226 23.111 5.538 215.357 1.00 59.78 C ANISOU 6475 CD ARG E 226 9396 7032 6286 -2374 -491 1138 C ATOM 6476 NE ARG E 226 22.804 4.791 214.148 1.00 58.42 N ANISOU 6476 NE ARG E 226 9013 6741 6443 -2224 -612 1042 N ATOM 6477 CZ ARG E 226 22.684 5.337 212.947 1.00 55.98 C ANISOU 6477 CZ ARG E 226 8405 6538 6327 -1900 -569 814 C ATOM 6478 NH1 ARG E 226 22.409 4.570 211.906 1.00 56.38 N ANISOU 6478 NH1 ARG E 226 8312 6485 6624 -1829 -694 726 N ATOM 6479 NH2 ARG E 226 22.859 6.643 212.778 1.00 53.75 N ANISOU 6479 NH2 ARG E 226 7997 6451 5976 -1669 -416 680 N ATOM 6480 N ALA E 227 20.420 9.329 217.633 1.00 61.82 N ANISOU 6480 N ALA E 227 9326 8294 5867 -2774 1021 521 N ATOM 6481 CA ALA E 227 19.543 10.343 217.065 1.00 60.02 C ANISOU 6481 CA ALA E 227 8683 8250 5871 -2525 1326 224 C ATOM 6482 C ALA E 227 19.318 10.044 215.591 1.00 57.55 C ANISOU 6482 C ALA E 227 8050 7873 5943 -2191 1099 189 C ATOM 6483 O ALA E 227 20.254 9.629 214.893 1.00 55.92 O ANISOU 6483 O ALA E 227 7949 7484 5815 -1994 738 314 O ATOM 6484 CB ALA E 227 20.138 11.709 217.237 1.00 57.88 C ANISOU 6484 CB ALA E 227 8445 8018 5528 -2289 1436 85 C ATOM 6485 N LYS E 228 18.064 10.190 215.160 1.00 57.62 N ANISOU 6485 N LYS E 228 7668 8041 6185 -2164 1310 11 N ATOM 6486 CA LYS E 228 17.649 10.023 213.766 1.00 54.87 C ANISOU 6486 CA LYS E 228 6986 7686 6175 -1882 1111 -48 C ATOM 6487 C LYS E 228 18.518 10.868 212.836 1.00 50.38 C ANISOU 6487 C LYS E 228 6407 7037 5696 -1440 899 -67 C ATOM 6488 O LYS E 228 18.650 12.070 213.055 1.00 50.30 O ANISOU 6488 O LYS E 228 6365 7079 5669 -1262 1067 -173 O ATOM 6489 CB LYS E 228 16.180 10.445 213.639 1.00 57.72 C ANISOU 6489 CB LYS E 228 6888 8268 6776 -1889 1402 -267 C ATOM 6490 CG LYS E 228 15.495 10.166 212.296 1.00 57.31 C ANISOU 6490 CG LYS E 228 6461 8257 7057 -1689 1185 -323 C ATOM 6491 CD LYS E 228 13.978 10.196 212.464 1.00 61.12 C ANISOU 6491 CD LYS E 228 6492 8959 7772 -1841 1465 -508 C ATOM 6492 CE LYS E 228 13.258 10.569 211.184 1.00 61.24 C ANISOU 6492 CE LYS E 228 6054 9062 8152 -1521 1271 -610 C ATOM 6493 NZ LYS E 228 11.776 10.607 211.374 1.00 65.59 N ANISOU 6493 NZ LYS E 228 6096 9833 8992 -1657 1528 -807 N ATOM 6494 N PRO E 229 19.142 10.230 211.820 1.00 47.25 N ANISOU 6494 N PRO E 229 6063 6502 5389 -1292 551 22 N ATOM 6495 CA PRO E 229 20.053 10.869 210.881 1.00 43.89 C ANISOU 6495 CA PRO E 229 5666 6000 5012 -939 354 13 C ATOM 6496 C PRO E 229 19.320 11.611 209.755 1.00 43.00 C ANISOU 6496 C PRO E 229 5219 6004 5116 -662 337 -108 C ATOM 6497 O PRO E 229 19.369 11.224 208.592 1.00 41.91 O ANISOU 6497 O PRO E 229 5004 5842 5076 -542 99 -107 O ATOM 6498 CB PRO E 229 20.908 9.704 210.357 1.00 42.16 C ANISOU 6498 CB PRO E 229 5630 5589 4801 -967 42 122 C ATOM 6499 CG PRO E 229 20.093 8.507 210.548 1.00 44.44 C ANISOU 6499 CG PRO E 229 5874 5863 5147 -1258 31 160 C ATOM 6500 CD PRO E 229 18.968 8.808 211.501 1.00 47.84 C ANISOU 6500 CD PRO E 229 6174 6475 5526 -1491 357 111 C ATOM 6501 N VAL E 230 18.655 12.688 210.134 1.00 44.05 N ANISOU 6501 N VAL E 230 5168 6250 5319 -570 582 -216 N ATOM 6502 CA VAL E 230 18.027 13.591 209.201 1.00 45.20 C ANISOU 6502 CA VAL E 230 5016 6467 5691 -273 540 -298 C ATOM 6503 C VAL E 230 19.043 14.420 208.398 1.00 43.26 C ANISOU 6503 C VAL E 230 4931 6113 5394 18 366 -244 C ATOM 6504 O VAL E 230 20.218 14.506 208.749 1.00 41.84 O ANISOU 6504 O VAL E 230 5050 5823 5025 0 355 -189 O ATOM 6505 CB VAL E 230 17.115 14.552 209.965 1.00 47.28 C ANISOU 6505 CB VAL E 230 5041 6827 6095 -239 878 -449 C ATOM 6506 CG1 VAL E 230 15.846 13.848 210.356 1.00 50.38 C ANISOU 6506 CG1 VAL E 230 5137 7375 6629 -484 1040 -540 C ATOM 6507 CG2 VAL E 230 17.838 15.081 211.203 1.00 46.19 C ANISOU 6507 CG2 VAL E 230 5198 6630 5722 -352 1135 -478 C ATOM 6508 N THR E 231 18.566 14.995 207.303 1.00 44.28 N ANISOU 6508 N THR E 231 4853 6279 5692 260 213 -251 N ATOM 6509 CA THR E 231 19.253 16.052 206.567 1.00 43.49 C ANISOU 6509 CA THR E 231 4870 6089 5565 526 102 -200 C ATOM 6510 C THR E 231 19.581 17.187 207.536 1.00 44.29 C ANISOU 6510 C THR E 231 5073 6108 5649 597 372 -257 C ATOM 6511 O THR E 231 18.677 17.714 208.193 1.00 47.45 O ANISOU 6511 O THR E 231 5257 6549 6222 621 600 -370 O ATOM 6512 CB THR E 231 18.305 16.622 205.473 1.00 45.07 C ANISOU 6512 CB THR E 231 4785 6352 5988 751 -86 -181 C ATOM 6513 OG1 THR E 231 17.919 15.575 204.569 1.00 45.12 O ANISOU 6513 OG1 THR E 231 4695 6459 5991 648 -343 -154 O ATOM 6514 CG2 THR E 231 18.944 17.776 204.716 1.00 43.91 C ANISOU 6514 CG2 THR E 231 4795 6089 5800 997 -205 -91 C ATOM 6515 N GLN E 232 20.859 17.537 207.657 1.00 41.92 N ANISOU 6515 N GLN E 232 5080 5692 5155 609 365 -212 N ATOM 6516 CA GLN E 232 21.275 18.516 208.665 1.00 41.60 C ANISOU 6516 CA GLN E 232 5180 5571 5056 614 617 -285 C ATOM 6517 C GLN E 232 22.595 19.170 208.314 1.00 39.23 C ANISOU 6517 C GLN E 232 5148 5142 4616 702 535 -227 C ATOM 6518 O GLN E 232 23.295 18.719 207.400 1.00 38.19 O ANISOU 6518 O GLN E 232 5109 4997 4405 723 315 -140 O ATOM 6519 CB GLN E 232 21.408 17.849 210.033 1.00 41.23 C ANISOU 6519 CB GLN E 232 5257 5573 4834 314 805 -331 C ATOM 6520 CG GLN E 232 22.575 16.923 210.133 1.00 39.02 C ANISOU 6520 CG GLN E 232 5239 5248 4340 154 625 -219 C ATOM 6521 CD GLN E 232 22.417 15.917 211.245 1.00 40.39 C ANISOU 6521 CD GLN E 232 5506 5472 4370 -165 702 -193 C ATOM 6522 OE1 GLN E 232 23.118 15.976 212.267 1.00 40.40 O ANISOU 6522 OE1 GLN E 232 5749 5441 4160 -337 770 -173 O ATOM 6523 NE2 GLN E 232 21.479 14.987 211.066 1.00 41.67 N ANISOU 6523 NE2 GLN E 232 5490 5711 4630 -277 676 -181 N ATOM 6524 N ILE E 233 22.930 20.228 209.047 1.00 38.41 N ANISOU 6524 N ILE E 233 5161 4945 4486 730 739 -304 N ATOM 6525 CA ILE E 233 24.228 20.880 208.921 1.00 36.14 C ANISOU 6525 CA ILE E 233 5131 4539 4062 754 703 -272 C ATOM 6526 C ILE E 233 25.062 20.609 210.177 1.00 35.80 C ANISOU 6526 C ILE E 233 5299 4504 3799 510 810 -319 C ATOM 6527 O ILE E 233 24.587 20.820 211.286 1.00 37.93 O ANISOU 6527 O ILE E 233 5577 4807 4029 385 1039 -429 O ATOM 6528 CB ILE E 233 24.036 22.386 208.673 1.00 37.21 C ANISOU 6528 CB ILE E 233 5268 4522 4348 967 807 -312 C ATOM 6529 CG1 ILE E 233 23.570 22.610 207.232 1.00 37.76 C ANISOU 6529 CG1 ILE E 233 5216 4563 4567 1189 579 -183 C ATOM 6530 CG2 ILE E 233 25.306 23.169 208.907 1.00 35.74 C ANISOU 6530 CG2 ILE E 233 5355 4207 4016 920 858 -325 C ATOM 6531 CD1 ILE E 233 22.929 23.959 206.983 1.00 40.14 C ANISOU 6531 CD1 ILE E 233 5440 4693 5120 1436 633 -190 C ATOM 6532 N VAL E 234 26.273 20.083 210.027 1.00 33.81 N ANISOU 6532 N VAL E 234 5205 4235 3405 422 638 -244 N ATOM 6533 CA VAL E 234 27.148 19.908 211.182 1.00 34.41 C ANISOU 6533 CA VAL E 234 5480 4309 3285 203 665 -259 C ATOM 6534 C VAL E 234 28.413 20.733 210.964 1.00 34.41 C ANISOU 6534 C VAL E 234 5627 4214 3234 240 626 -273 C ATOM 6535 O VAL E 234 29.059 20.613 209.923 1.00 33.50 O ANISOU 6535 O VAL E 234 5489 4068 3173 341 477 -221 O ATOM 6536 CB VAL E 234 27.489 18.408 211.451 1.00 34.08 C ANISOU 6536 CB VAL E 234 5468 4314 3166 34 462 -152 C ATOM 6537 CG1 VAL E 234 28.372 18.247 212.683 1.00 34.03 C ANISOU 6537 CG1 VAL E 234 5679 4300 2953 -199 422 -125 C ATOM 6538 CG2 VAL E 234 26.222 17.572 211.629 1.00 34.64 C ANISOU 6538 CG2 VAL E 234 5402 4471 3288 -46 512 -135 C ATOM 6539 N SER E 235 28.749 21.577 211.942 1.00 36.30 N ANISOU 6539 N SER E 235 6018 4415 3359 128 784 -368 N ATOM 6540 CA SER E 235 29.869 22.519 211.840 1.00 36.51 C ANISOU 6540 CA SER E 235 6181 4345 3347 127 785 -409 C ATOM 6541 C SER E 235 30.893 22.389 212.968 1.00 37.55 C ANISOU 6541 C SER E 235 6486 4508 3274 -124 723 -433 C ATOM 6542 O SER E 235 30.578 21.916 214.056 1.00 39.57 O ANISOU 6542 O SER E 235 6821 4843 3369 -318 752 -438 O ATOM 6543 CB SER E 235 29.366 23.971 211.845 1.00 38.16 C ANISOU 6543 CB SER E 235 6428 4426 3646 240 1028 -528 C ATOM 6544 OG SER E 235 28.262 24.161 210.978 1.00 38.84 O ANISOU 6544 OG SER E 235 6342 4475 3942 475 1058 -494 O ATOM 6545 N ALA E 236 32.114 22.841 212.697 1.00 37.28 N ANISOU 6545 N ALA E 236 6511 4417 3235 -144 633 -444 N ATOM 6546 CA ALA E 236 33.173 22.950 213.692 1.00 37.99 C ANISOU 6546 CA ALA E 236 6744 4530 3158 -376 544 -478 C ATOM 6547 C ALA E 236 33.885 24.270 213.416 1.00 38.83 C ANISOU 6547 C ALA E 236 6929 4529 3296 -371 659 -588 C ATOM 6548 O ALA E 236 34.000 24.673 212.266 1.00 37.61 O ANISOU 6548 O ALA E 236 6701 4296 3291 -205 689 -569 O ATOM 6549 CB ALA E 236 34.139 21.796 213.571 1.00 36.57 C ANISOU 6549 CB ALA E 236 6482 4399 3012 -420 225 -361 C ATOM 6550 N GLU E 237 34.359 24.938 214.463 1.00 41.45 N ANISOU 6550 N GLU E 237 7434 4854 3463 -588 720 -701 N ATOM 6551 CA GLU E 237 34.914 26.281 214.314 1.00 42.85 C ANISOU 6551 CA GLU E 237 7714 4896 3670 -619 866 -830 C ATOM 6552 C GLU E 237 36.314 26.541 214.912 1.00 44.17 C ANISOU 6552 C GLU E 237 7961 5097 3724 -870 720 -889 C ATOM 6553 O GLU E 237 36.881 25.690 215.591 1.00 44.63 O ANISOU 6553 O GLU E 237 8003 5286 3667 -1025 469 -823 O ATOM 6554 CB GLU E 237 33.909 27.334 214.795 1.00 44.96 C ANISOU 6554 CB GLU E 237 8113 5042 3927 -598 1189 -991 C ATOM 6555 CG GLU E 237 33.556 27.302 216.275 1.00 47.93 C ANISOU 6555 CG GLU E 237 8651 5509 4050 -848 1300 -1127 C ATOM 6556 CD GLU E 237 32.487 28.344 216.623 1.00 50.59 C ANISOU 6556 CD GLU E 237 9063 5704 4454 -785 1679 -1345 C ATOM 6557 OE1 GLU E 237 31.413 28.339 215.976 1.00 50.40 O ANISOU 6557 OE1 GLU E 237 8878 5616 4657 -520 1796 -1317 O ATOM 6558 OE2 GLU E 237 32.720 29.172 217.533 1.00 53.11 O ANISOU 6558 OE2 GLU E 237 9588 5969 4624 -998 1853 -1561 O ATOM 6559 N ALA E 238 36.862 27.725 214.635 1.00 45.02 N ANISOU 6559 N ALA E 238 8150 5071 3886 -913 853 -1002 N ATOM 6560 CA ALA E 238 38.197 28.109 215.121 1.00 46.18 C ANISOU 6560 CA ALA E 238 8343 5246 3958 -1169 729 -1086 C ATOM 6561 C ALA E 238 38.365 29.617 215.195 1.00 47.50 C ANISOU 6561 C ALA E 238 8696 5223 4129 -1272 976 -1263 C ATOM 6562 O ALA E 238 37.941 30.346 214.307 1.00 46.87 O ANISOU 6562 O ALA E 238 8641 4957 4209 -1099 1169 -1257 O ATOM 6563 CB ALA E 238 39.279 27.541 214.227 1.00 45.34 C ANISOU 6563 CB ALA E 238 8003 5202 4021 -1123 521 -997 C ATOM 6564 N TRP E 239 39.007 30.080 216.254 1.00 49.74 N ANISOU 6564 N TRP E 239 9126 5538 4233 -1572 943 -1411 N ATOM 6565 CA TRP E 239 39.287 31.491 216.394 1.00 51.77 C ANISOU 6565 CA TRP E 239 9575 5596 4498 -1716 1164 -1606 C ATOM 6566 C TRP E 239 40.768 31.678 216.229 1.00 53.02 C ANISOU 6566 C TRP E 239 9643 5806 4694 -1930 984 -1629 C ATOM 6567 O TRP E 239 41.548 30.779 216.535 1.00 52.50 O ANISOU 6567 O TRP E 239 9410 5953 4583 -2032 672 -1553 O ATOM 6568 CB TRP E 239 38.831 31.995 217.757 1.00 54.05 C ANISOU 6568 CB TRP E 239 10121 5875 4539 -1940 1314 -1823 C ATOM 6569 CG TRP E 239 37.353 32.155 217.851 1.00 53.83 C ANISOU 6569 CG TRP E 239 10162 5740 4550 -1736 1603 -1883 C ATOM 6570 CD1 TRP E 239 36.448 31.234 218.297 1.00 52.79 C ANISOU 6570 CD1 TRP E 239 9985 5771 4304 -1673 1597 -1820 C ATOM 6571 CD2 TRP E 239 36.601 33.309 217.474 1.00 55.25 C ANISOU 6571 CD2 TRP E 239 10441 5612 4939 -1564 1936 -2022 C ATOM 6572 NE1 TRP E 239 35.177 31.751 218.236 1.00 53.68 N ANISOU 6572 NE1 TRP E 239 10123 5723 4549 -1478 1928 -1941 N ATOM 6573 CE2 TRP E 239 35.243 33.025 217.732 1.00 55.34 C ANISOU 6573 CE2 TRP E 239 10415 5631 4980 -1384 2123 -2063 C ATOM 6574 CE3 TRP E 239 36.944 34.561 216.941 1.00 56.78 C ANISOU 6574 CE3 TRP E 239 10749 5500 5324 -1549 2087 -2110 C ATOM 6575 CZ2 TRP E 239 34.222 33.950 217.476 1.00 57.17 C ANISOU 6575 CZ2 TRP E 239 10677 5574 5471 -1153 2438 -2201 C ATOM 6576 CZ3 TRP E 239 35.925 35.488 216.693 1.00 58.31 C ANISOU 6576 CZ3 TRP E 239 11026 5374 5756 -1323 2383 -2219 C ATOM 6577 CH2 TRP E 239 34.581 35.173 216.959 1.00 58.37 C ANISOU 6577 CH2 TRP E 239 10950 5396 5831 -1108 2546 -2269 C ATOM 6578 N GLY E 240 41.148 32.837 215.714 1.00 55.49 N ANISOU 6578 N GLY E 240 10051 5908 5125 -1993 1174 -1727 N ATOM 6579 CA GLY E 240 42.550 33.158 215.524 1.00 58.52 C ANISOU 6579 CA GLY E 240 10337 6331 5567 -2236 1061 -1783 C ATOM 6580 C GLY E 240 43.317 33.306 216.828 1.00 62.65 C ANISOU 6580 C GLY E 240 10935 6983 5886 -2602 888 -1949 C ATOM 6581 O GLY E 240 42.765 33.736 217.848 1.00 64.16 O ANISOU 6581 O GLY E 240 11385 7129 5863 -2737 992 -2098 O ATOM 6582 N ARG E 241 44.591 32.932 216.791 1.00 64.74 N ANISOU 6582 N ARG E 241 10960 7419 6220 -2774 620 -1939 N ATOM 6583 CA ARG E 241 45.434 32.932 217.971 1.00 69.09 C ANISOU 6583 CA ARG E 241 11527 8132 6591 -3127 350 -2056 C ATOM 6584 C ARG E 241 46.776 33.557 217.631 1.00 71.64 C ANISOU 6584 C ARG E 241 11683 8454 7082 -3378 305 -2175 C ATOM 6585 O ARG E 241 47.454 33.073 216.737 1.00 69.91 O ANISOU 6585 O ARG E 241 11130 8313 7118 -3274 222 -2091 O ATOM 6586 CB ARG E 241 45.636 31.495 218.450 1.00 69.28 C ANISOU 6586 CB ARG E 241 11342 8418 6563 -3068 -71 -1877 C ATOM 6587 CG ARG E 241 44.498 30.937 219.324 1.00 70.32 C ANISOU 6587 CG ARG E 241 11711 8604 6404 -3018 -87 -1803 C ATOM 6588 CD ARG E 241 44.438 29.384 219.361 1.00 69.84 C ANISOU 6588 CD ARG E 241 11439 8716 6380 -2841 -444 -1545 C ATOM 6589 NE ARG E 241 45.722 28.730 219.080 1.00 71.47 N ANISOU 6589 NE ARG E 241 11277 9042 6837 -2851 -829 -1465 N ATOM 6590 CZ ARG E 241 46.693 28.520 219.972 1.00 75.14 C ANISOU 6590 CZ ARG E 241 11674 9656 7220 -3121 -1242 -1463 C ATOM 6591 NH1 ARG E 241 47.819 27.923 219.590 1.00 76.15 N ANISOU 6591 NH1 ARG E 241 11390 9866 7675 -3069 -1571 -1407 N ATOM 6592 NH2 ARG E 241 46.557 28.926 221.234 1.00 77.90 N ANISOU 6592 NH2 ARG E 241 12354 10074 7170 -3454 -1328 -1534 N ATOM 6593 N ALA E 242 47.179 34.591 218.382 1.00 76.47 N ANISOU 6593 N ALA E 242 12513 8992 7549 -3735 366 -2398 N ATOM 6594 CA ALA E 242 48.425 35.369 218.134 1.00 80.41 C ANISOU 6594 CA ALA E 242 12886 9467 8199 -4045 366 -2551 C ATOM 6595 C ALA E 242 49.769 34.705 218.531 1.00 83.72 C ANISOU 6595 C ALA E 242 12920 10185 8706 -4258 -87 -2556 C ATOM 6596 O ALA E 242 50.711 35.384 218.953 1.00 86.82 O ANISOU 6596 O ALA E 242 13282 10610 9096 -4635 -173 -2741 O ATOM 6597 CB ALA E 242 48.314 36.753 218.764 1.00 83.00 C ANISOU 6597 CB ALA E 242 13605 9568 8365 -4359 612 -2810 C ATOM 6598 N ASP E 243 49.824 33.380 218.383 1.00 83.80 N ANISOU 6598 N ASP E 243 12628 10390 8824 -4007 -386 -2355 N ATOM 6599 CA ASP E 243 51.016 32.537 218.544 1.00 86.95 C ANISOU 6599 CA ASP E 243 12569 11036 9431 -4076 -843 -2314 C ATOM 6600 C ASP E 243 50.826 31.227 217.735 1.00 84.73 C ANISOU 6600 C ASP E 243 11964 10822 9407 -3659 -946 -2105 C ATOM 6601 O ASP E 243 50.220 30.249 218.201 1.00 83.57 O ANISOU 6601 O ASP E 243 11869 10738 9146 -3472 -1181 -1922 O ATOM 6602 CB ASP E 243 51.301 32.231 220.027 1.00 90.41 C ANISOU 6602 CB ASP E 243 13104 11655 9590 -4342 -1313 -2306 C ATOM 6603 CG ASP E 243 50.027 32.107 220.868 1.00 89.64 C ANISOU 6603 CG ASP E 243 13477 11517 9065 -4308 -1249 -2232 C ATOM 6604 OD1 ASP E 243 49.526 33.147 221.356 1.00 90.94 O ANISOU 6604 OD1 ASP E 243 14045 11552 8955 -4522 -957 -2420 O ATOM 6605 OD2 ASP E 243 49.539 30.970 221.060 1.00 88.09 O ANISOU 6605 OD2 ASP E 243 13242 11409 8819 -4085 -1477 -2005 O ATOM 6606 OXT ASP E 243 51.253 31.106 216.574 1.00 84.09 O ANISOU 6606 OXT ASP E 243 11581 10724 9645 -3519 -773 -2126 O TER 6607 ASP E 243 HETATM 6608 O HOH A 276 5.196 26.743 168.438 1.00 11.55 O HETATM 6609 O HOH A 277 16.716 8.423 128.982 1.00 2.00 O HETATM 6610 O HOH A 278 -6.494 26.144 155.119 1.00 16.27 O HETATM 6611 O HOH A 279 -6.007 21.940 153.973 1.00 9.30 O HETATM 6612 O HOH A 280 8.439 19.706 140.577 1.00 12.83 O HETATM 6613 O HOH A 281 6.108 27.211 171.558 1.00 16.52 O HETATM 6614 O HOH A 282 12.917 31.156 150.950 1.00 11.59 O HETATM 6615 O HOH A 283 27.515 11.693 149.332 1.00 14.97 O HETATM 6616 O HOH A 284 9.467 21.289 141.924 1.00 31.13 O HETATM 6617 O HOH A 285 15.682 6.222 166.197 1.00 5.63 O HETATM 6618 O HOH A 286 -2.071 21.108 106.871 1.00 15.39 O HETATM 6619 O HOH A 287 17.693 6.350 136.825 1.00 18.73 O HETATM 6620 O HOH A 288 -7.723 19.280 128.755 1.00 2.71 O HETATM 6621 O HOH A 289 1.519 25.402 133.037 1.00 18.99 O HETATM 6622 O HOH B 100 0.052 15.517 143.637 1.00 12.59 O HETATM 6623 O HOH B 101 -6.510 20.808 136.393 1.00 24.62 O HETATM 6624 O HOH B 102 -11.008 11.110 146.540 1.00 17.34 O HETATM 6625 O HOH B 103 -1.994 12.725 148.323 1.00 27.63 O HETATM 6626 O HOH B 104 -10.403 18.886 130.421 1.00 26.78 O HETATM 6627 O HOH B 105 -19.191 8.898 132.192 1.00 2.00 O HETATM 6628 O HOH C 11 19.387 15.713 162.334 1.00 21.36 O HETATM 6629 O HOH D 197 46.253 6.586 183.574 1.00 2.00 O HETATM 6630 O HOH D 198 22.260 22.083 167.582 1.00 11.66 O HETATM 6631 O HOH D 199 25.601 5.187 168.106 1.00 21.29 O HETATM 6632 O HOH D 200 41.968 28.395 186.276 1.00 3.97 O HETATM 6633 O HOH D 201 24.339 16.137 191.518 1.00 7.47 O HETATM 6634 O HOH D 202 36.863 16.592 158.451 1.00 6.30 O HETATM 6635 O HOH D 203 37.075 24.027 179.732 1.00 22.83 O HETATM 6636 O HOH E 244 20.875 20.918 192.191 1.00 18.40 O HETATM 6637 O HOH E 245 30.713 16.948 214.902 1.00 9.72 O HETATM 6638 O HOH E 246 38.348 -2.509 207.386 1.00 2.48 O HETATM 6639 O HOH E 247 15.298 22.352 193.878 1.00 21.73 O HETATM 6640 O HOH E 248 23.881 8.439 193.908 1.00 14.97 O CONECT 819 1335 CONECT 1335 819 CONECT 1659 2109 CONECT 2109 1659 CONECT 2459 2922 CONECT 2922 2459 CONECT 3325 3843 CONECT 3843 3325 CONECT 4161 4554 CONECT 4360 6006 CONECT 4554 4161 CONECT 4839 5399 CONECT 5399 4839 CONECT 5799 6330 CONECT 6006 4360 CONECT 6330 5799 MASTER 444 0 0 13 82 0 0 6 6624 5 16 65 END
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Related entries of code: 3qdm
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3qeq
RCSB PDB
PDBbind
194aa, >3QEQ_4|Chain... at 95%
5w1v
RCSB PDB
PDBbind
207aa, >5W1V_4|Chains... *
5w1w
RCSB PDB
PDBbind
207aa, >5W1W_4|Chains... at 100%
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
3qdm
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
TCR DMF4 protein
Ligand Name
human Class I MHC HLA-A2 with the bound MART-1(26-35)(A27L) decameric peptide
EC.Number
E.C.-.-.-.-
Resolution
2.8(Å)
Affinity (Kd/Ki/IC50)
Kd=29uM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) J.Immunol. Vol. 187: pp. 2453-2463
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):
Q16655
P01848
P04439
P61769
Entrez Gene ID
NCBI Entrez Gene ID:
2315
3105
567
ASD
Information of known allosteric effects of PDB entries
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