Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM 24-FEB-11 3QUX TITLE STRUCTURE OF THE MOUSE CD1D-ALPHA-C-GALCER-INKT TCR COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 19-297; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-2 MICROGLOBULIN; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: UNP RESIDUES 21-119; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: VALPHA14 (MOUSE VARIABLE DOMAIN, HUMAN CONSTANT DOMAIN); COMPND 13 CHAIN: C; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: VBETA8.2 (MOUSE VARIABLE DOMAIN, HUMAN CONSTANT DOMAIN); COMPND 17 CHAIN: D; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: CD1.1, CD1D, CD1D1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PBACP10PH; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_COMMON: MOUSE; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 GENE: B2M, BETA-2-MICROGLOBULIN, MCG_11606, RP23-34E24.5-001; SOURCE 17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 20 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS TRANSFER VECTOR; SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PBACP10PH; SOURCE 23 MOL_ID: 3; SOURCE 24 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 25 ORGANISM_COMMON: MOUSE; SOURCE 26 ORGANISM_TAXID: 10090; SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 29 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET22B; SOURCE 31 MOL_ID: 4; SOURCE 32 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 33 ORGANISM_COMMON: MOUSE; SOURCE 34 ORGANISM_TAXID: 10090; SOURCE 35 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 36 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 37 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 38 EXPRESSION_SYSTEM_PLASMID: PET30A KEYWDS ANTIGEN PRESENTATION, GLYCOLIPID, NKT CELLS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.LI,E.GIRARDI,E.D.YU,D.M.ZAJONC REVDAT 2 29-JUL-20 3QUX 1 COMPND REMARK SEQADV HETNAM REVDAT 2 2 1 LINK SITE ATOM REVDAT 1 29-JUN-11 3QUX 0 JRNL AUTH S.ASPESLAGH,Y.LI,E.D.YU,N.PAUWELS,M.TRAPPENIERS,E.GIRARDI, JRNL AUTH 2 T.DECRUY,K.VAN BENEDEN,K.VENKEN,M.DRENNAN,L.LEYBAERT,J.WANG, JRNL AUTH 3 R.W.FRANCK,S.VAN CALENBERGH,D.M.ZAJONC,D.ELEWAUT JRNL TITL GALACTOSE-MODIFIED INKT CELL AGONISTS STABILIZED BY AN JRNL TITL 2 INDUCED FIT OF CD1D PREVENT TUMOUR METASTASIS. JRNL REF EMBO J. V. 30 2294 2011 JRNL REFN ISSN 0261-4189 JRNL PMID 21552205 JRNL DOI 10.1038/EMBOJ.2011.145 REMARK 2 REMARK 2 RESOLUTION. 2.91 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.19 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 24083 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1041 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) : 2.91 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1693 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.79 REMARK 3 BIN R VALUE (WORKING SET) : 0.3110 REMARK 3 BIN FREE R VALUE SET COUNT : 78 REMARK 3 BIN FREE R VALUE : 0.3830 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6344 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 126 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.58 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.01000 REMARK 3 B22 (A**2) : -0.06000 REMARK 3 B33 (A**2) : 0.07000 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): 0.386 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.302 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.271 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6650 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9051 ; 1.197 ; 1.950 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 799 ; 5.980 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 309 ;36.102 ;24.369 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1036 ;17.521 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;16.853 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 990 ; 0.074 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5076 ; 0.005 ; 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): 4013 ; 0.333 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6491 ; 0.664 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2637 ; 1.006 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2560 ; 1.727 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 7 A 185 REMARK 3 RESIDUE RANGE : A 500 A 513 REMARK 3 RESIDUE RANGE : A 1 A 1 REMARK 3 ORIGIN FOR THE GROUP (A): 5.3398 19.7654 17.7741 REMARK 3 T TENSOR REMARK 3 T11: 0.0883 T22: 0.0964 REMARK 3 T33: 0.0608 T12: 0.0152 REMARK 3 T13: -0.0273 T23: -0.0240 REMARK 3 L TENSOR REMARK 3 L11: 2.3376 L22: 1.7310 REMARK 3 L33: 2.9537 L12: 1.3557 REMARK 3 L13: -0.9038 L23: -0.9021 REMARK 3 S TENSOR REMARK 3 S11: -0.0194 S12: 0.0076 S13: -0.1327 REMARK 3 S21: -0.0046 S22: -0.0502 S23: -0.0125 REMARK 3 S31: 0.1775 S32: 0.1517 S33: 0.0695 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 186 A 279 REMARK 3 ORIGIN FOR THE GROUP (A): -26.2358 -1.3923 16.5092 REMARK 3 T TENSOR REMARK 3 T11: 0.1760 T22: 0.3229 REMARK 3 T33: 0.7848 T12: -0.0413 REMARK 3 T13: 0.0812 T23: -0.2125 REMARK 3 L TENSOR REMARK 3 L11: 9.2128 L22: 5.0483 REMARK 3 L33: 3.6359 L12: -0.1500 REMARK 3 L13: 0.6117 L23: 1.5161 REMARK 3 S TENSOR REMARK 3 S11: 0.0369 S12: 1.0871 S13: -1.0998 REMARK 3 S21: -0.3063 S22: -0.1447 S23: 0.9226 REMARK 3 S31: 0.2328 S32: -0.6018 S33: 0.1078 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 96 REMARK 3 ORIGIN FOR THE GROUP (A): -23.0259 20.1356 20.8153 REMARK 3 T TENSOR REMARK 3 T11: 0.1225 T22: 0.1229 REMARK 3 T33: 0.2735 T12: 0.0159 REMARK 3 T13: 0.0007 T23: -0.0640 REMARK 3 L TENSOR REMARK 3 L11: 7.6272 L22: 4.5082 REMARK 3 L33: 2.9099 L12: 0.6871 REMARK 3 L13: -2.7196 L23: -2.2655 REMARK 3 S TENSOR REMARK 3 S11: -0.0542 S12: 0.1054 S13: 0.1375 REMARK 3 S21: 0.1128 S22: 0.1513 S23: 0.8049 REMARK 3 S31: -0.1832 S32: -0.2126 S33: -0.0971 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 2 C 113 REMARK 3 ORIGIN FOR THE GROUP (A): 33.0593 38.9911 26.2663 REMARK 3 T TENSOR REMARK 3 T11: 0.0911 T22: 0.0776 REMARK 3 T33: 0.0171 T12: 0.0129 REMARK 3 T13: -0.0015 T23: 0.0131 REMARK 3 L TENSOR REMARK 3 L11: 4.5530 L22: 1.6664 REMARK 3 L33: 1.7253 L12: 1.9118 REMARK 3 L13: 1.8052 L23: 0.4150 REMARK 3 S TENSOR REMARK 3 S11: -0.0695 S12: 0.0996 S13: -0.0795 REMARK 3 S21: 0.1165 S22: 0.1053 S23: 0.0358 REMARK 3 S31: -0.1305 S32: 0.0194 S33: -0.0359 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 114 C 204 REMARK 3 ORIGIN FOR THE GROUP (A): 55.8560 67.5432 28.7773 REMARK 3 T TENSOR REMARK 3 T11: 0.4026 T22: 0.3887 REMARK 3 T33: 0.1146 T12: -0.1680 REMARK 3 T13: -0.0639 T23: -0.0124 REMARK 3 L TENSOR REMARK 3 L11: 6.6080 L22: 8.5600 REMARK 3 L33: 5.9275 L12: -2.2459 REMARK 3 L13: 1.6608 L23: -0.8611 REMARK 3 S TENSOR REMARK 3 S11: -0.1456 S12: -0.9628 S13: 0.4362 REMARK 3 S21: 0.9827 S22: 0.0314 S23: -0.5429 REMARK 3 S31: -0.4831 S32: -0.0634 S33: 0.1142 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 3 D 113 REMARK 3 ORIGIN FOR THE GROUP (A): 20.6752 52.9749 12.1436 REMARK 3 T TENSOR REMARK 3 T11: 0.1139 T22: 0.1044 REMARK 3 T33: 0.1211 T12: 0.0094 REMARK 3 T13: -0.0170 T23: 0.0793 REMARK 3 L TENSOR REMARK 3 L11: 1.0474 L22: 5.0961 REMARK 3 L33: 1.8806 L12: 1.1280 REMARK 3 L13: 0.7417 L23: 0.4563 REMARK 3 S TENSOR REMARK 3 S11: -0.1500 S12: 0.1693 S13: 0.2781 REMARK 3 S21: -0.1458 S22: 0.1307 S23: 0.1110 REMARK 3 S31: -0.3051 S32: 0.1279 S33: 0.0193 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 114 D 240 REMARK 3 ORIGIN FOR THE GROUP (A): 45.6345 69.6421 14.6078 REMARK 3 T TENSOR REMARK 3 T11: 0.1699 T22: 0.0589 REMARK 3 T33: 0.0458 T12: -0.0455 REMARK 3 T13: 0.0158 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 6.4339 L22: 3.7363 REMARK 3 L33: 2.5961 L12: -1.1284 REMARK 3 L13: 0.0184 L23: 0.1455 REMARK 3 S TENSOR REMARK 3 S11: -0.0369 S12: -0.3861 S13: 0.3158 REMARK 3 S21: 0.2167 S22: 0.0408 S23: 0.0921 REMARK 3 S31: -0.1812 S32: 0.0231 S33: -0.0039 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3QUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-11. REMARK 100 THE DEPOSITION ID IS D_1000064134. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-ROOT I REMARK 200 -BEAM SINGLE CRYSTAL, ASYMMETRIC REMARK 200 CUT 4.965 DEGS REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25140 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.910 REMARK 200 RESOLUTION RANGE LOW (A) : 35.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.13100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.57200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRIES 2Q7Y, 3HE6 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL 3350, 8% REMARK 280 TACSIMATE, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.40050 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.40050 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.25100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 94.95950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.25100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 94.95950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.40050 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.25100 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 94.95950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.40050 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.25100 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 94.95950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 1 REMARK 465 GLU A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLN A 5 REMARK 465 LYS A 6 REMARK 465 SER A 198 REMARK 465 SER A 199 REMARK 465 ALA A 200 REMARK 465 HIS A 201 REMARK 465 GLY A 202 REMARK 465 HIS A 203 REMARK 465 ARG A 204 REMARK 465 HIS A 280 REMARK 465 HIS A 281 REMARK 465 HIS A 282 REMARK 465 HIS A 283 REMARK 465 HIS A 284 REMARK 465 HIS A 285 REMARK 465 ILE B 1 REMARK 465 ASP B 98 REMARK 465 MET B 99 REMARK 465 MET C -1 REMARK 465 LYS C 0 REMARK 465 PRO C 207 REMARK 465 GLU C 208 REMARK 465 SER C 209 REMARK 465 SER C 210 REMARK 465 MET D 0 REMARK 465 GLU D 1 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 64 CG CD OE1 OE2 REMARK 470 LEU A 206 CG CD1 CD2 REMARK 470 GLU A 254 CG CD OE1 OE2 REMARK 470 GLN A 273 CG CD OE1 NE2 REMARK 470 LYS B 3 CG CD CE NZ REMARK 470 LYS B 19 CG CD CE NZ REMARK 470 LYS B 48 CG CD CE NZ REMARK 470 LYS C 132 CG CD CE NZ REMARK 470 LYS C 154 CG CD CE NZ REMARK 470 ILE C 197 CG1 CG2 CD1 REMARK 470 LYS D 129 CG CD CE NZ REMARK 470 ASP D 182 CG OD1 OD2 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 SER A 89 131.83 -31.22 REMARK 500 PRO A 90 34.64 -90.34 REMARK 500 VAL A 125 -31.24 -134.75 REMARK 500 THR A 232 108.24 -36.48 REMARK 500 TRP B 60 0.90 82.66 REMARK 500 SER B 86 -4.10 -55.93 REMARK 500 ALA C 79 80.59 47.81 REMARK 500 ASP C 122 62.49 -150.23 REMARK 500 SER C 146 30.43 -85.12 REMARK 500 ASN C 183 25.50 -71.08 REMARK 500 ASP C 186 34.06 -85.20 REMARK 500 PRO C 199 151.29 -49.23 REMARK 500 THR C 202 118.57 -19.26 REMARK 500 PRO C 205 -148.67 -71.69 REMARK 500 ASP D 95 -147.52 -85.41 REMARK 500 ASP D 150 34.91 -74.61 REMARK 500 HIS D 151 79.93 -104.42 REMARK 500 ASP D 170 131.49 -39.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3QUY RELATED DB: PDB REMARK 900 RELATED ID: 3QUZ RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 D219H CONFLICT IN UNP ENTRY P11609 DBREF 3QUX A 1 279 UNP P11609 CD1D1_MOUSE 19 297 DBREF 3QUX B 1 99 UNP Q91XJ8 Q91XJ8_MOUSE 21 119 DBREF 3QUX C -1 210 PDB 3QUX 3QUX -1 210 DBREF 3QUX D 0 240 PDB 3QUX 3QUX 0 240 SEQADV 3QUX HIS A 201 UNP P11609 ASP 219 SEE REMARK 999 SEQADV 3QUX HIS A 280 UNP P11609 EXPRESSION TAG SEQADV 3QUX HIS A 281 UNP P11609 EXPRESSION TAG SEQADV 3QUX HIS A 282 UNP P11609 EXPRESSION TAG SEQADV 3QUX HIS A 283 UNP P11609 EXPRESSION TAG SEQADV 3QUX HIS A 284 UNP P11609 EXPRESSION TAG SEQADV 3QUX HIS A 285 UNP P11609 EXPRESSION TAG SEQRES 1 A 285 SER GLU ALA GLN GLN LYS ASN TYR THR PHE ARG CYS LEU SEQRES 2 A 285 GLN MET SER SER PHE ALA ASN ARG SER TRP SER ARG THR SEQRES 3 A 285 ASP SER VAL VAL TRP LEU GLY ASP LEU GLN THR HIS ARG SEQRES 4 A 285 TRP SER ASN ASP SER ALA THR ILE SER PHE THR LYS PRO SEQRES 5 A 285 TRP SER GLN GLY LYS LEU SER ASN GLN GLN TRP GLU LYS SEQRES 6 A 285 LEU GLN HIS MET PHE GLN VAL TYR ARG VAL SER PHE THR SEQRES 7 A 285 ARG ASP ILE GLN GLU LEU VAL LYS MET MET SER PRO LYS SEQRES 8 A 285 GLU ASP TYR PRO ILE GLU ILE GLN LEU SER ALA GLY CYS SEQRES 9 A 285 GLU MET TYR PRO GLY ASN ALA SER GLU SER PHE LEU HIS SEQRES 10 A 285 VAL ALA PHE GLN GLY LYS TYR VAL VAL ARG PHE TRP GLY SEQRES 11 A 285 THR SER TRP GLN THR VAL PRO GLY ALA PRO SER TRP LEU SEQRES 12 A 285 ASP LEU PRO ILE LYS VAL LEU ASN ALA ASP GLN GLY THR SEQRES 13 A 285 SER ALA THR VAL GLN MET LEU LEU ASN ASP THR CYS PRO SEQRES 14 A 285 LEU PHE VAL ARG GLY LEU LEU GLU ALA GLY LYS SER ASP SEQRES 15 A 285 LEU GLU LYS GLN GLU LYS PRO VAL ALA TRP LEU SER SER SEQRES 16 A 285 VAL PRO SER SER ALA HIS GLY HIS ARG GLN LEU VAL CYS SEQRES 17 A 285 HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL MET SEQRES 18 A 285 TRP MET ARG GLY ASP GLN GLU GLN GLN GLY THR HIS ARG SEQRES 19 A 285 GLY ASP PHE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU SEQRES 20 A 285 GLN ALA THR LEU ASP VAL GLU ALA GLY GLU GLU ALA GLY SEQRES 21 A 285 LEU ALA CYS ARG VAL LYS HIS SER SER LEU GLY GLY GLN SEQRES 22 A 285 ASP ILE ILE LEU TYR TRP HIS HIS HIS HIS HIS HIS SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET SEQRES 1 C 209 MET LYS THR GLN VAL GLU GLN SER PRO GLN SER LEU VAL SEQRES 2 C 209 VAL ARG GLN GLY GLU ASN CYS VAL LEU GLN CYS ASN TYR SEQRES 3 C 209 SER VAL THR PRO ASP ASN HIS LEU ARG TRP PHE LYS GLN SEQRES 4 C 209 ASP THR GLY LYS GLY LEU VAL SER LEU THR VAL LEU VAL SEQRES 5 C 209 ASP GLN LYS ASP LYS THR SER ASN GLY ARG TYR SER ALA SEQRES 6 C 209 THR LEU ASP LYS ASP ALA LYS HIS SER THR LEU HIS ILE SEQRES 7 C 209 THR ALA THR LEU LEU ASP ASP THR ALA THR TYR ILE CYS SEQRES 8 C 209 VAL VAL GLY ASP ARG GLY SER ALA LEU GLY ARG LEU HIS SEQRES 9 C 209 PHE GLY ALA GLY THR GLN LEU ILE VAL ILE PRO ASP ILE SEQRES 10 C 209 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER SEQRES 11 C 209 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE SEQRES 12 C 209 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP SEQRES 13 C 209 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER SEQRES 14 C 209 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN SEQRES 15 C 209 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER SEQRES 16 C 209 ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SEQRES 17 C 209 SER SEQRES 1 D 241 MET GLU ALA ALA VAL THR GLN SER PRO ARG ASN LYS VAL SEQRES 2 D 241 ALA VAL THR GLY GLY LYS VAL THR LEU SER CYS ASN GLN SEQRES 3 D 241 THR ASN ASN HIS ASN ASN MET TYR TRP TYR ARG GLN ASP SEQRES 4 D 241 THR GLY HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY SEQRES 5 D 241 ALA GLY SER THR GLU LYS GLY ASP ILE PRO ASP GLY TYR SEQRES 6 D 241 LYS ALA SER ARG PRO SER GLN GLU ASN PHE SER LEU ILE SEQRES 7 D 241 LEU GLU LEU ALA THR PRO SER GLN THR SER VAL TYR PHE SEQRES 8 D 241 CYS ALA SER GLY ASP GLU GLY TYR THR GLN TYR PHE GLY SEQRES 9 D 241 PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU ARG ASN SEQRES 10 D 241 VAL THR PRO PRO LYS VAL SER LEU PHE GLU PRO SER LYS SEQRES 11 D 241 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS SEQRES 12 D 241 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER SEQRES 13 D 241 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS SEQRES 14 D 241 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN SEQRES 15 D 241 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER SEQRES 16 D 241 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS SEQRES 17 D 241 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP SEQRES 18 D 241 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER SEQRES 19 D 241 ALA GLU ALA TRP GLY ARG ALA MODRES 3QUX ASN A 42 ASN GLYCOSYLATION SITE MODRES 3QUX ASN A 165 ASN GLYCOSYLATION SITE MODRES 3QUX ASN A 20 ASN GLYCOSYLATION SITE HET NAG E 1 14 HET NAG E 2 14 HET FUC E 3 10 HET NAG A 500 14 HET NAG A 501 14 HET QUX A 286 60 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM QUX N-[(3S,4S,5R)-4,5-DIHYDROXY-1-[(2R,3R,4R,5R,6R)-3,4,5- HETNAM 2 QUX TRIHYDROXY-6-(HYDROXYMETHYL)OXAN-2-YL]NONADECAN-3- HETNAM 3 QUX YL]HEXACOSANAMIDE FORMUL 5 NAG 4(C8 H15 N O6) FORMUL 5 FUC C6 H12 O5 FORMUL 8 QUX C51 H101 N O8 HELIX 1 1 SER A 59 SER A 89 1 31 HELIX 2 2 PRO A 140 TRP A 142 5 3 HELIX 3 3 LEU A 143 ASN A 151 1 9 HELIX 4 4 ASP A 153 ASP A 166 1 14 HELIX 5 5 ASP A 166 GLY A 179 1 14 HELIX 6 6 GLY A 179 GLU A 184 1 6 HELIX 7 7 LEU C 81 THR C 85 5 5 HELIX 8 8 ARG C 169 ASP C 172 5 4 HELIX 9 9 THR D 82 THR D 86 5 5 HELIX 10 10 SER D 128 GLN D 136 1 9 HELIX 11 11 ALA D 195 GLN D 199 1 5 SHEET 1 A 8 SER A 48 PHE A 49 0 SHEET 2 A 8 LEU A 35 TRP A 40 -1 N ARG A 39 O SER A 48 SHEET 3 A 8 SER A 24 LEU A 32 -1 N VAL A 30 O THR A 37 SHEET 4 A 8 TYR A 8 PHE A 18 -1 N ARG A 11 O TRP A 31 SHEET 5 A 8 ILE A 96 MET A 106 -1 O MET A 106 N TYR A 8 SHEET 6 A 8 SER A 112 PHE A 120 -1 O ALA A 119 N GLN A 99 SHEET 7 A 8 LYS A 123 TRP A 129 -1 O VAL A 126 N VAL A 118 SHEET 8 A 8 SER A 132 THR A 135 -1 O GLN A 134 N ARG A 127 SHEET 1 B 4 VAL A 190 SER A 195 0 SHEET 2 B 4 LEU A 206 PHE A 213 -1 O VAL A 207 N SER A 194 SHEET 3 B 4 TRP A 245 LEU A 251 -1 O TRP A 245 N PHE A 213 SHEET 4 B 4 HIS A 233 ARG A 234 -1 N HIS A 233 O THR A 250 SHEET 1 C 4 VAL A 190 SER A 195 0 SHEET 2 C 4 LEU A 206 PHE A 213 -1 O VAL A 207 N SER A 194 SHEET 3 C 4 TRP A 245 LEU A 251 -1 O TRP A 245 N PHE A 213 SHEET 4 C 4 LEU A 238 PRO A 239 -1 N LEU A 238 O TYR A 246 SHEET 1 D 4 GLN A 227 GLU A 228 0 SHEET 2 D 4 TRP A 219 ARG A 224 -1 N ARG A 224 O GLN A 227 SHEET 3 D 4 LEU A 261 LYS A 266 -1 O LYS A 266 N TRP A 219 SHEET 4 D 4 ILE A 275 TYR A 278 -1 O ILE A 275 N VAL A 265 SHEET 1 E 4 GLN B 6 SER B 11 0 SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 E 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25 SHEET 4 E 4 VAL B 49 MET B 51 -1 N GLU B 50 O HIS B 67 SHEET 1 F 4 GLN B 6 SER B 11 0 SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10 SHEET 3 F 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25 SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 G 4 LYS B 44 LYS B 45 0 SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O LYS B 44 SHEET 3 G 4 TYR B 78 LYS B 83 -1 O ARG B 81 N GLN B 38 SHEET 4 G 4 LYS B 91 TYR B 94 -1 O VAL B 93 N CYS B 80 SHEET 1 H 5 VAL C 3 SER C 6 0 SHEET 2 H 5 CYS C 18 TYR C 24 -1 O ASN C 23 N GLU C 4 SHEET 3 H 5 HIS C 72 ILE C 77 -1 O SER C 73 N CYS C 22 SHEET 4 H 5 TYR C 62 ASP C 67 -1 N SER C 63 O HIS C 76 SHEET 5 H 5 LYS C 53 ASN C 58 -1 N ASN C 58 O TYR C 62 SHEET 1 I 5 SER C 9 ARG C 13 0 SHEET 2 I 5 THR C 110 ILE C 115 1 O ILE C 115 N VAL C 12 SHEET 3 I 5 ALA C 86 GLY C 93 -1 N ALA C 86 O LEU C 112 SHEET 4 I 5 HIS C 31 GLN C 37 -1 N PHE C 35 O ILE C 89 SHEET 5 I 5 VAL C 44 LEU C 49 -1 O LEU C 49 N LEU C 32 SHEET 1 J 4 SER C 9 ARG C 13 0 SHEET 2 J 4 THR C 110 ILE C 115 1 O ILE C 115 N VAL C 12 SHEET 3 J 4 ALA C 86 GLY C 93 -1 N ALA C 86 O LEU C 112 SHEET 4 J 4 LEU C 104 PHE C 106 -1 O HIS C 105 N VAL C 92 SHEET 1 K 8 VAL C 158 ILE C 160 0 SHEET 2 K 8 PHE C 173 SER C 182 -1 O TRP C 181 N TYR C 159 SHEET 3 K 8 SER C 133 THR C 142 -1 N CYS C 139 O ALA C 180 SHEET 4 K 8 ALA C 124 ASP C 130 -1 N ALA C 124 O THR C 142 SHEET 5 K 8 LYS D 121 GLU D 126 -1 O GLU D 126 N ARG C 129 SHEET 6 K 8 LYS D 137 PHE D 147 -1 O VAL D 141 N PHE D 125 SHEET 7 K 8 TYR D 185 SER D 194 -1 O TYR D 185 N PHE D 147 SHEET 8 K 8 VAL D 167 THR D 169 -1 N CYS D 168 O ARG D 190 SHEET 1 L 8 CYS C 164 MET C 168 0 SHEET 2 L 8 PHE C 173 SER C 182 -1 O PHE C 173 N MET C 168 SHEET 3 L 8 SER C 133 THR C 142 -1 N CYS C 139 O ALA C 180 SHEET 4 L 8 ALA C 124 ASP C 130 -1 N ALA C 124 O THR C 142 SHEET 5 L 8 LYS D 121 GLU D 126 -1 O GLU D 126 N ARG C 129 SHEET 6 L 8 LYS D 137 PHE D 147 -1 O VAL D 141 N PHE D 125 SHEET 7 L 8 TYR D 185 SER D 194 -1 O TYR D 185 N PHE D 147 SHEET 8 L 8 LEU D 174 LYS D 175 -1 N LEU D 174 O SER D 186 SHEET 1 M 4 THR D 5 SER D 7 0 SHEET 2 M 4 VAL D 19 ASN D 24 -1 O ASN D 24 N THR D 5 SHEET 3 M 4 ASN D 73 LEU D 78 -1 O LEU D 78 N VAL D 19 SHEET 4 M 4 LYS D 65 SER D 67 -1 N LYS D 65 O ILE D 77 SHEET 1 N 6 ASN D 10 VAL D 14 0 SHEET 2 N 6 THR D 106 LEU D 111 1 O LEU D 109 N ALA D 13 SHEET 3 N 6 SER D 87 GLY D 94 -1 N TYR D 89 O THR D 106 SHEET 4 N 6 ASN D 31 GLN D 37 -1 N TYR D 35 O PHE D 90 SHEET 5 N 6 ARG D 44 SER D 49 -1 O ILE D 46 N TRP D 34 SHEET 6 N 6 GLU D 56 LYS D 57 -1 O GLU D 56 N TYR D 48 SHEET 1 O 4 ASN D 10 VAL D 14 0 SHEET 2 O 4 THR D 106 LEU D 111 1 O LEU D 109 N ALA D 13 SHEET 3 O 4 SER D 87 GLY D 94 -1 N TYR D 89 O THR D 106 SHEET 4 O 4 TYR D 101 PHE D 102 -1 O TYR D 101 N SER D 93 SHEET 1 P 4 LYS D 161 VAL D 163 0 SHEET 2 P 4 VAL D 152 VAL D 158 -1 N VAL D 158 O LYS D 161 SHEET 3 P 4 HIS D 204 PHE D 211 -1 O ARG D 206 N TRP D 157 SHEET 4 P 4 GLN D 230 TRP D 237 -1 O ALA D 236 N PHE D 205 SSBOND 1 CYS A 104 CYS A 168 1555 1555 2.96 SSBOND 2 CYS A 208 CYS A 263 1555 1555 2.04 SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03 SSBOND 4 CYS C 22 CYS C 90 1555 1555 2.04 SSBOND 5 CYS C 139 CYS C 189 1555 1555 2.06 SSBOND 6 CYS C 164 CYS D 168 1555 1555 2.04 SSBOND 7 CYS D 23 CYS D 91 1555 1555 2.01 SSBOND 8 CYS D 142 CYS D 207 1555 1555 2.03 LINK ND2 ASN A 20 C1 NAG A 500 1555 1555 1.45 LINK ND2 ASN A 42 C1 NAG A 501 1555 1555 1.45 LINK ND2 ASN A 165 C1 NAG E 1 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O6 NAG E 1 C1 FUC E 3 1555 1555 1.46 CISPEP 1 SER A 89 PRO A 90 0 7.03 CISPEP 2 TYR A 94 PRO A 95 0 -3.06 CISPEP 3 TYR A 214 PRO A 215 0 10.78 CISPEP 4 HIS B 31 PRO B 32 0 3.18 CISPEP 5 SER C 6 PRO C 7 0 -6.32 CISPEP 6 THR C 27 PRO C 28 0 -7.57 CISPEP 7 SER D 7 PRO D 8 0 -6.51 CISPEP 8 TYR D 148 PRO D 149 0 -10.02 CRYST1 78.502 189.919 150.801 90.00 90.00 90.00 C 2 2 21 8 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 0.012739 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005265 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006631 0.00000 ATOM 1 N ASN A 7 -0.312 -2.098 17.128 1.00 60.26 N ANISOU 1 N ASN A 7 10337 4694 7865 -602 1078 -739 N ATOM 2 CA ASN A 7 0.223 -0.825 16.543 1.00 58.44 C ANISOU 2 CA ASN A 7 9882 4736 7585 -495 994 -775 C ATOM 3 C ASN A 7 -0.411 0.436 17.139 1.00 55.14 C ANISOU 3 C ASN A 7 9200 4668 7082 -556 778 -688 C ATOM 4 O ASN A 7 -1.636 0.588 17.145 1.00 54.71 O ANISOU 4 O ASN A 7 9130 4741 6916 -803 692 -728 O ATOM 5 CB ASN A 7 0.073 -0.824 15.014 1.00 59.49 C ANISOU 5 CB ASN A 7 10127 4873 7605 -654 1075 -1008 C ATOM 6 CG ASN A 7 0.877 -1.932 14.348 1.00 63.62 C ANISOU 6 CG ASN A 7 10906 5050 8217 -559 1324 -1119 C ATOM 7 OD1 ASN A 7 1.607 -2.676 15.015 1.00 65.47 O ANISOU 7 OD1 ASN A 7 11216 5036 8625 -338 1436 -1002 O ATOM 8 ND2 ASN A 7 0.746 -2.049 13.022 1.00 66.08 N ANISOU 8 ND2 ASN A 7 11353 5344 8411 -727 1420 -1341 N ATOM 9 N TYR A 8 0.431 1.338 17.635 1.00 52.79 N ANISOU 9 N TYR A 8 8695 4524 6838 -334 702 -568 N ATOM 10 CA TYR A 8 -0.047 2.550 18.299 1.00 49.76 C ANISOU 10 CA TYR A 8 8079 4436 6391 -364 527 -486 C ATOM 11 C TYR A 8 0.560 3.795 17.693 1.00 47.58 C ANISOU 11 C TYR A 8 7626 4370 6084 -263 467 -517 C ATOM 12 O TYR A 8 1.763 3.829 17.410 1.00 47.98 O ANISOU 12 O TYR A 8 7658 4368 6205 -67 531 -502 O ATOM 13 CB TYR A 8 0.263 2.508 19.797 1.00 49.33 C ANISOU 13 CB TYR A 8 7950 4385 6409 -239 475 -286 C ATOM 14 CG TYR A 8 -0.745 1.729 20.612 1.00 50.63 C ANISOU 14 CG TYR A 8 8218 4463 6555 -406 469 -232 C ATOM 15 CD1 TYR A 8 -0.474 0.426 21.050 1.00 53.10 C ANISOU 15 CD1 TYR A 8 8721 4493 6962 -362 574 -155 C ATOM 16 CD2 TYR A 8 -1.975 2.295 20.944 1.00 50.25 C ANISOU 16 CD2 TYR A 8 8075 4613 6405 -604 368 -248 C ATOM 17 CE1 TYR A 8 -1.411 -0.293 21.802 1.00 54.61 C ANISOU 17 CE1 TYR A 8 9016 4606 7129 -535 569 -98 C ATOM 18 CE2 TYR A 8 -2.916 1.594 21.686 1.00 51.84 C ANISOU 18 CE2 TYR A 8 8360 4757 6581 -771 367 -198 C ATOM 19 CZ TYR A 8 -2.633 0.303 22.116 1.00 54.11 C ANISOU 19 CZ TYR A 8 8847 4767 6947 -749 463 -125 C ATOM 20 OH TYR A 8 -3.586 -0.364 22.857 1.00 55.06 O ANISOU 20 OH TYR A 8 9052 4838 7032 -935 459 -70 O ATOM 21 N THR A 9 -0.270 4.816 17.493 1.00 45.25 N ANISOU 21 N THR A 9 7194 4310 5690 -395 349 -551 N ATOM 22 CA THR A 9 0.231 6.109 17.031 1.00 42.67 C ANISOU 22 CA THR A 9 6695 4182 5335 -308 280 -558 C ATOM 23 C THR A 9 0.230 7.138 18.157 1.00 40.71 C ANISOU 23 C THR A 9 6263 4106 5100 -236 170 -434 C ATOM 24 O THR A 9 -0.798 7.416 18.787 1.00 40.31 O ANISOU 24 O THR A 9 6156 4148 5012 -351 104 -402 O ATOM 25 CB THR A 9 -0.553 6.637 15.821 1.00 42.24 C ANISOU 25 CB THR A 9 6617 4265 5167 -486 237 -678 C ATOM 26 OG1 THR A 9 -0.861 5.546 14.959 1.00 44.26 O ANISOU 26 OG1 THR A 9 7074 4365 5377 -632 336 -803 O ATOM 27 CG2 THR A 9 0.269 7.663 15.049 1.00 40.36 C ANISOU 27 CG2 THR A 9 6268 4155 4911 -381 214 -701 C ATOM 28 N PHE A 10 1.406 7.692 18.405 1.00 39.60 N ANISOU 28 N PHE A 10 6030 4010 5005 -54 162 -367 N ATOM 29 CA PHE A 10 1.562 8.782 19.346 1.00 37.86 C ANISOU 29 CA PHE A 10 5651 3958 4777 -2 69 -273 C ATOM 30 C PHE A 10 1.472 10.119 18.608 1.00 36.41 C ANISOU 30 C PHE A 10 5346 3948 4540 -24 9 -331 C ATOM 31 O PHE A 10 2.251 10.377 17.702 1.00 36.39 O ANISOU 31 O PHE A 10 5331 3957 4537 42 35 -376 O ATOM 32 CB PHE A 10 2.908 8.641 20.050 1.00 38.10 C ANISOU 32 CB PHE A 10 5642 3960 4873 179 83 -153 C ATOM 33 CG PHE A 10 3.112 9.609 21.162 1.00 36.54 C ANISOU 33 CG PHE A 10 5311 3926 4647 198 -4 -56 C ATOM 34 CD1 PHE A 10 2.424 9.471 22.351 1.00 35.47 C ANISOU 34 CD1 PHE A 10 5181 3811 4486 119 -40 12 C ATOM 35 CD2 PHE A 10 4.005 10.660 21.023 1.00 36.21 C ANISOU 35 CD2 PHE A 10 5148 4019 4590 275 -44 -40 C ATOM 36 CE1 PHE A 10 2.609 10.368 23.383 1.00 34.78 C ANISOU 36 CE1 PHE A 10 4991 3874 4351 112 -105 82 C ATOM 37 CE2 PHE A 10 4.201 11.556 22.059 1.00 34.95 C ANISOU 37 CE2 PHE A 10 4890 4002 4388 261 -115 32 C ATOM 38 CZ PHE A 10 3.501 11.404 23.242 1.00 34.00 C ANISOU 38 CZ PHE A 10 4786 3898 4234 179 -142 88 C ATOM 39 N ARG A 11 0.517 10.959 18.996 1.00 35.73 N ANISOU 39 N ARG A 11 5170 3989 4415 -113 -59 -324 N ATOM 40 CA ARG A 11 0.319 12.270 18.362 1.00 34.90 C ANISOU 40 CA ARG A 11 4952 4031 4277 -127 -113 -356 C ATOM 41 C ARG A 11 0.413 13.443 19.320 1.00 33.27 C ANISOU 41 C ARG A 11 4632 3933 4076 -83 -157 -296 C ATOM 42 O ARG A 11 -0.260 13.475 20.348 1.00 33.15 O ANISOU 42 O ARG A 11 4599 3938 4059 -128 -164 -260 O ATOM 43 CB ARG A 11 -1.038 12.339 17.676 1.00 35.43 C ANISOU 43 CB ARG A 11 5004 4156 4300 -278 -141 -406 C ATOM 44 CG ARG A 11 -1.040 11.852 16.274 1.00 38.67 C ANISOU 44 CG ARG A 11 5490 4539 4664 -350 -119 -490 C ATOM 45 CD ARG A 11 -2.447 11.892 15.741 1.00 44.89 C ANISOU 45 CD ARG A 11 6243 5420 5395 -525 -167 -511 C ATOM 46 NE ARG A 11 -2.639 10.853 14.730 1.00 51.34 N ANISOU 46 NE ARG A 11 7197 6166 6144 -662 -127 -602 N ATOM 47 CZ ARG A 11 -2.852 9.565 15.005 1.00 55.03 C ANISOU 47 CZ ARG A 11 7814 6483 6612 -740 -61 -641 C ATOM 48 NH1 ARG A 11 -2.904 9.140 16.273 1.00 56.61 N ANISOU 48 NH1 ARG A 11 8033 6600 6876 -689 -40 -577 N ATOM 49 NH2 ARG A 11 -3.019 8.697 14.012 1.00 56.56 N ANISOU 49 NH2 ARG A 11 8152 6605 6732 -885 -10 -745 N ATOM 50 N CYS A 12 1.245 14.410 18.966 1.00 32.09 N ANISOU 50 N CYS A 12 4418 3852 3924 -11 -177 -293 N ATOM 51 CA CYS A 12 1.238 15.695 19.632 1.00 31.08 C ANISOU 51 CA CYS A 12 4201 3818 3790 0 -208 -265 C ATOM 52 C CYS A 12 0.639 16.655 18.644 1.00 30.19 C ANISOU 52 C CYS A 12 4027 3771 3673 -31 -233 -299 C ATOM 53 O CYS A 12 1.180 16.868 17.565 1.00 30.33 O ANISOU 53 O CYS A 12 4043 3805 3676 -11 -242 -321 O ATOM 54 CB CYS A 12 2.647 16.146 19.999 1.00 31.05 C ANISOU 54 CB CYS A 12 4169 3848 3780 83 -216 -223 C ATOM 55 SG CYS A 12 3.605 14.949 20.943 1.00 33.75 S ANISOU 55 SG CYS A 12 4555 4133 4137 149 -199 -137 S ATOM 56 N LEU A 13 -0.494 17.229 19.003 1.00 29.90 N ANISOU 56 N LEU A 13 3934 3776 3650 -78 -238 -291 N ATOM 57 CA LEU A 13 -1.216 18.077 18.078 1.00 29.56 C ANISOU 57 CA LEU A 13 3816 3798 3618 -100 -266 -289 C ATOM 58 C LEU A 13 -1.172 19.502 18.561 1.00 29.27 C ANISOU 58 C LEU A 13 3716 3789 3616 -50 -254 -265 C ATOM 59 O LEU A 13 -1.646 19.787 19.656 1.00 29.93 O ANISOU 59 O LEU A 13 3784 3867 3721 -52 -213 -262 O ATOM 60 CB LEU A 13 -2.663 17.599 17.953 1.00 30.16 C ANISOU 60 CB LEU A 13 3855 3906 3698 -190 -274 -280 C ATOM 61 CG LEU A 13 -2.886 16.145 17.534 1.00 29.35 C ANISOU 61 CG LEU A 13 3840 3758 3553 -281 -275 -316 C ATOM 62 CD1 LEU A 13 -4.354 15.890 17.309 1.00 29.11 C ANISOU 62 CD1 LEU A 13 3746 3800 3513 -399 -297 -297 C ATOM 63 CD2 LEU A 13 -2.079 15.814 16.293 1.00 29.45 C ANISOU 63 CD2 LEU A 13 3918 3750 3521 -284 -285 -360 C ATOM 64 N GLN A 14 -0.593 20.391 17.756 1.00 28.91 N ANISOU 64 N GLN A 14 3647 3767 3571 -14 -276 -256 N ATOM 65 CA GLN A 14 -0.494 21.809 18.117 1.00 28.87 C ANISOU 65 CA GLN A 14 3607 3759 3604 26 -252 -238 C ATOM 66 C GLN A 14 -1.432 22.688 17.280 1.00 29.04 C ANISOU 66 C GLN A 14 3544 3810 3680 39 -268 -184 C ATOM 67 O GLN A 14 -1.574 22.486 16.072 1.00 29.35 O ANISOU 67 O GLN A 14 3556 3900 3694 12 -326 -155 O ATOM 68 CB GLN A 14 0.953 22.308 17.997 1.00 28.51 C ANISOU 68 CB GLN A 14 3599 3711 3522 49 -260 -247 C ATOM 69 CG GLN A 14 1.158 23.702 18.579 1.00 29.59 C ANISOU 69 CG GLN A 14 3737 3822 3684 60 -220 -246 C ATOM 70 CD GLN A 14 2.534 24.259 18.332 1.00 30.91 C ANISOU 70 CD GLN A 14 3930 4008 3806 53 -237 -247 C ATOM 71 OE1 GLN A 14 3.533 23.594 18.575 1.00 32.45 O ANISOU 71 OE1 GLN A 14 4144 4239 3948 45 -255 -253 O ATOM 72 NE2 GLN A 14 2.595 25.497 17.859 1.00 31.02 N ANISOU 72 NE2 GLN A 14 3940 3999 3848 56 -227 -228 N ATOM 73 N MET A 15 -2.081 23.649 17.929 1.00 28.96 N ANISOU 73 N MET A 15 3492 3771 3742 79 -210 -164 N ATOM 74 CA MET A 15 -2.856 24.649 17.212 1.00 29.70 C ANISOU 74 CA MET A 15 3496 3877 3913 125 -214 -84 C ATOM 75 C MET A 15 -2.378 25.999 17.661 1.00 29.39 C ANISOU 75 C MET A 15 3494 3747 3924 181 -144 -90 C ATOM 76 O MET A 15 -2.345 26.289 18.866 1.00 29.34 O ANISOU 76 O MET A 15 3537 3680 3932 185 -54 -151 O ATOM 77 CB MET A 15 -4.345 24.558 17.530 1.00 30.94 C ANISOU 77 CB MET A 15 3545 4067 4143 140 -181 -37 C ATOM 78 CG MET A 15 -4.904 23.192 17.450 1.00 32.95 C ANISOU 78 CG MET A 15 3782 4396 4341 55 -227 -50 C ATOM 79 SD MET A 15 -5.871 22.834 18.908 1.00 37.37 S ANISOU 79 SD MET A 15 4312 4947 4941 47 -130 -80 S ATOM 80 CE MET A 15 -5.342 21.137 19.180 1.00 35.83 C ANISOU 80 CE MET A 15 4231 4750 4631 -62 -173 -150 C ATOM 81 N SER A 16 -2.024 26.835 16.699 1.00 28.89 N ANISOU 81 N SER A 16 3421 3677 3880 205 -178 -30 N ATOM 82 CA SER A 16 -1.666 28.188 17.030 1.00 28.96 C ANISOU 82 CA SER A 16 3478 3578 3947 247 -103 -28 C ATOM 83 C SER A 16 -2.437 29.141 16.133 1.00 30.11 C ANISOU 83 C SER A 16 3538 3703 4199 324 -109 101 C ATOM 84 O SER A 16 -2.485 28.976 14.908 1.00 30.41 O ANISOU 84 O SER A 16 3518 3830 4208 307 -211 189 O ATOM 85 CB SER A 16 -0.160 28.391 16.908 1.00 28.19 C ANISOU 85 CB SER A 16 3477 3473 3760 189 -130 -76 C ATOM 86 OG SER A 16 0.557 27.272 17.396 1.00 26.42 O ANISOU 86 OG SER A 16 3292 3309 3438 132 -160 -149 O ATOM 87 N SER A 17 -3.060 30.133 16.754 1.00 31.01 N ANISOU 87 N SER A 17 3645 3700 4436 407 7 119 N ATOM 88 CA SER A 17 -3.822 31.121 16.013 1.00 32.30 C ANISOU 88 CA SER A 17 3720 3821 4733 511 20 269 C ATOM 89 C SER A 17 -3.225 32.505 16.224 1.00 33.00 C ANISOU 89 C SER A 17 3923 3728 4886 547 120 259 C ATOM 90 O SER A 17 -3.009 32.925 17.354 1.00 33.21 O ANISOU 90 O SER A 17 4057 3631 4930 540 254 141 O ATOM 91 CB SER A 17 -5.290 31.085 16.444 1.00 33.42 C ANISOU 91 CB SER A 17 3725 3973 5000 608 92 329 C ATOM 92 OG SER A 17 -5.766 29.749 16.472 1.00 32.26 O ANISOU 92 OG SER A 17 3502 3982 4773 537 14 307 O ATOM 93 N PHE A 18 -2.951 33.197 15.127 1.00 33.51 N ANISOU 93 N PHE A 18 3978 3780 4975 564 57 382 N ATOM 94 CA PHE A 18 -2.406 34.540 15.184 1.00 34.80 C ANISOU 94 CA PHE A 18 4260 3758 5204 587 148 393 C ATOM 95 C PHE A 18 -3.387 35.506 14.531 1.00 37.14 C ANISOU 95 C PHE A 18 4460 3970 5683 737 182 591 C ATOM 96 O PHE A 18 -3.508 35.547 13.303 1.00 37.46 O ANISOU 96 O PHE A 18 4409 4110 5715 743 53 757 O ATOM 97 CB PHE A 18 -1.051 34.590 14.478 1.00 33.87 C ANISOU 97 CB PHE A 18 4230 3690 4950 463 51 377 C ATOM 98 CG PHE A 18 -0.059 33.571 14.985 1.00 32.26 C ANISOU 98 CG PHE A 18 4084 3594 4579 337 5 222 C ATOM 99 CD1 PHE A 18 -0.224 32.206 14.706 1.00 31.01 C ANISOU 99 CD1 PHE A 18 3841 3608 4335 309 -95 207 C ATOM 100 CD2 PHE A 18 1.057 33.975 15.710 1.00 31.31 C ANISOU 100 CD2 PHE A 18 4103 3406 4387 241 62 105 C ATOM 101 CE1 PHE A 18 0.693 31.258 15.151 1.00 28.61 C ANISOU 101 CE1 PHE A 18 3585 3386 3901 219 -127 88 C ATOM 102 CE2 PHE A 18 1.976 33.035 16.161 1.00 30.91 C ANISOU 102 CE2 PHE A 18 4077 3474 4194 140 12 -1 C ATOM 103 CZ PHE A 18 1.789 31.664 15.882 1.00 29.24 C ANISOU 103 CZ PHE A 18 3774 3413 3921 146 -78 -3 C ATOM 104 N ALA A 19 -4.094 36.271 15.358 1.00 39.04 N ANISOU 104 N ALA A 19 4717 4029 6087 860 361 580 N ATOM 105 CA ALA A 19 -5.169 37.135 14.879 1.00 41.91 C ANISOU 105 CA ALA A 19 4960 4303 6661 1044 419 786 C ATOM 106 C ALA A 19 -4.632 38.341 14.124 1.00 43.68 C ANISOU 106 C ALA A 19 5275 4371 6950 1069 425 908 C ATOM 107 O ALA A 19 -5.046 38.631 13.005 1.00 44.90 O ANISOU 107 O ALA A 19 5306 4589 7166 1137 321 1138 O ATOM 108 CB ALA A 19 -6.033 37.583 16.038 1.00 43.22 C ANISOU 108 CB ALA A 19 5127 4304 6992 1179 643 721 C ATOM 109 N ASN A 20 -3.718 39.043 14.775 1.00 44.51 N ANISOU 109 N ASN A 20 5601 4279 7030 995 547 756 N ATOM 110 CA ASN A 20 -3.075 40.225 14.253 1.00 46.52 C ANISOU 110 CA ASN A 20 5991 4351 7333 983 581 833 C ATOM 111 C ASN A 20 -1.648 40.159 14.782 1.00 45.37 C ANISOU 111 C ASN A 20 6049 4192 6999 767 585 619 C ATOM 112 O ASN A 20 -1.268 39.132 15.351 1.00 43.47 O ANISOU 112 O ASN A 20 5800 4110 6606 660 532 464 O ATOM 113 CB ASN A 20 -3.824 41.488 14.707 1.00 49.51 C ANISOU 113 CB ASN A 20 6426 4421 7964 1168 811 895 C ATOM 114 CG ASN A 20 -4.393 41.363 16.116 1.00 51.32 C ANISOU 114 CG ASN A 20 6696 4548 8255 1222 1016 707 C ATOM 115 OD1 ASN A 20 -3.686 40.962 17.038 1.00 50.54 O ANISOU 115 OD1 ASN A 20 6735 4467 8000 1059 1055 471 O ATOM 116 ND2 ASN A 20 -5.681 41.713 16.283 1.00 55.65 N ANISOU 116 ND2 ASN A 20 7111 5004 9030 1449 1149 825 N ATOM 117 N ARG A 21 -0.861 41.224 14.606 1.00 46.86 N ANISOU 117 N ARG A 21 6409 4199 7196 698 644 622 N ATOM 118 CA ARG A 21 0.559 41.202 14.988 1.00 45.98 C ANISOU 118 CA ARG A 21 6466 4113 6892 469 626 449 C ATOM 119 C ARG A 21 0.797 41.074 16.505 1.00 45.67 C ANISOU 119 C ARG A 21 6557 4004 6790 377 769 203 C ATOM 120 O ARG A 21 1.864 40.637 16.930 1.00 44.65 O ANISOU 120 O ARG A 21 6499 3995 6472 187 712 66 O ATOM 121 CB ARG A 21 1.336 42.386 14.382 1.00 47.23 C ANISOU 121 CB ARG A 21 6775 4108 7064 389 649 523 C ATOM 122 CG ARG A 21 1.165 43.717 15.114 1.00 52.20 C ANISOU 122 CG ARG A 21 7612 4379 7842 418 889 465 C ATOM 123 CD ARG A 21 1.889 44.879 14.401 1.00 56.97 C ANISOU 123 CD ARG A 21 8368 4811 8466 332 904 565 C ATOM 124 NE ARG A 21 3.344 44.876 14.612 1.00 57.82 N ANISOU 124 NE ARG A 21 8614 5002 8353 53 854 418 N ATOM 125 CZ ARG A 21 4.256 44.537 13.695 1.00 56.72 C ANISOU 125 CZ ARG A 21 8414 5078 8059 -76 672 490 C ATOM 126 NH1 ARG A 21 3.894 44.167 12.466 1.00 56.16 N ANISOU 126 NH1 ARG A 21 8169 5160 8009 26 519 696 N ATOM 127 NH2 ARG A 21 5.546 44.574 14.009 1.00 55.52 N ANISOU 127 NH2 ARG A 21 8371 5003 7720 -322 648 358 N ATOM 128 N SER A 22 -0.198 41.416 17.315 1.00 46.78 N ANISOU 128 N SER A 22 6718 3976 7082 508 952 158 N ATOM 129 CA SER A 22 -0.019 41.351 18.757 1.00 46.84 C ANISOU 129 CA SER A 22 6863 3920 7014 402 1101 -75 C ATOM 130 C SER A 22 -0.638 40.116 19.408 1.00 45.57 C ANISOU 130 C SER A 22 6562 3950 6801 438 1065 -143 C ATOM 131 O SER A 22 0.008 39.490 20.258 1.00 44.98 O ANISOU 131 O SER A 22 6548 3992 6549 274 1043 -303 O ATOM 132 CB SER A 22 -0.531 42.627 19.428 1.00 49.66 C ANISOU 132 CB SER A 22 7395 3932 7541 475 1378 -138 C ATOM 133 OG SER A 22 -1.921 42.792 19.215 1.00 51.02 O ANISOU 133 OG SER A 22 7423 4013 7949 743 1471 -1 O ATOM 134 N TRP A 23 -1.863 39.758 19.005 1.00 45.32 N ANISOU 134 N TRP A 23 6338 3965 6916 639 1052 -8 N ATOM 135 CA TRP A 23 -2.648 38.690 19.654 1.00 43.90 C ANISOU 135 CA TRP A 23 6028 3937 6715 682 1049 -61 C ATOM 136 C TRP A 23 -2.399 37.301 19.066 1.00 41.34 C ANISOU 136 C TRP A 23 5553 3906 6247 620 811 -12 C ATOM 137 O TRP A 23 -2.472 37.116 17.846 1.00 40.86 O ANISOU 137 O TRP A 23 5374 3947 6205 668 660 151 O ATOM 138 CB TRP A 23 -4.134 39.011 19.550 1.00 45.63 C ANISOU 138 CB TRP A 23 6100 4071 7167 919 1167 64 C ATOM 139 CG TRP A 23 -5.052 38.137 20.362 1.00 45.51 C ANISOU 139 CG TRP A 23 5966 4171 7153 963 1219 0 C ATOM 140 CD1 TRP A 23 -5.634 38.458 21.552 1.00 46.88 C ANISOU 140 CD1 TRP A 23 6208 4213 7393 1003 1455 -135 C ATOM 141 CD2 TRP A 23 -5.532 36.827 20.024 1.00 44.22 C ANISOU 141 CD2 TRP A 23 5605 4274 6924 961 1046 68 C ATOM 142 NE1 TRP A 23 -6.430 37.431 21.987 1.00 45.78 N ANISOU 142 NE1 TRP A 23 5914 4252 7230 1026 1433 -146 N ATOM 143 CE2 TRP A 23 -6.388 36.415 21.070 1.00 44.54 C ANISOU 143 CE2 TRP A 23 5596 4334 6994 997 1181 -21 C ATOM 144 CE3 TRP A 23 -5.318 35.957 18.942 1.00 43.23 C ANISOU 144 CE3 TRP A 23 5353 4366 6708 916 803 187 C ATOM 145 CZ2 TRP A 23 -7.035 35.164 21.070 1.00 43.63 C ANISOU 145 CZ2 TRP A 23 5308 4446 6825 985 1071 14 C ATOM 146 CZ3 TRP A 23 -5.955 34.706 18.944 1.00 42.05 C ANISOU 146 CZ3 TRP A 23 5047 4428 6502 901 703 207 C ATOM 147 CH2 TRP A 23 -6.806 34.328 20.003 1.00 42.40 C ANISOU 147 CH2 TRP A 23 5044 4483 6583 934 832 126 C ATOM 148 N SER A 24 -2.127 36.331 19.944 1.00 39.56 N ANISOU 148 N SER A 24 5344 3809 5877 509 788 -152 N ATOM 149 CA SER A 24 -2.011 34.922 19.552 1.00 37.09 C ANISOU 149 CA SER A 24 4906 3740 5448 465 600 -122 C ATOM 150 C SER A 24 -2.241 33.940 20.716 1.00 36.32 C ANISOU 150 C SER A 24 4805 3733 5262 404 632 -246 C ATOM 151 O SER A 24 -2.179 34.322 21.883 1.00 36.94 O ANISOU 151 O SER A 24 5002 3718 5315 347 779 -379 O ATOM 152 CB SER A 24 -0.669 34.654 18.873 1.00 35.52 C ANISOU 152 CB SER A 24 4752 3643 5102 339 447 -118 C ATOM 153 OG SER A 24 0.328 34.337 19.813 1.00 35.01 O ANISOU 153 OG SER A 24 4798 3619 4884 186 453 -261 O ATOM 154 N ARG A 25 -2.530 32.682 20.390 1.00 35.06 N ANISOU 154 N ARG A 25 4520 3752 5048 402 501 -202 N ATOM 155 CA ARG A 25 -2.637 31.635 21.403 1.00 34.47 C ANISOU 155 CA ARG A 25 4448 3772 4876 329 506 -297 C ATOM 156 C ARG A 25 -2.206 30.305 20.822 1.00 33.19 C ANISOU 156 C ARG A 25 4222 3781 4607 275 328 -261 C ATOM 157 O ARG A 25 -2.309 30.099 19.607 1.00 32.91 O ANISOU 157 O ARG A 25 4101 3806 4596 315 219 -157 O ATOM 158 CB ARG A 25 -4.047 31.559 22.021 1.00 35.56 C ANISOU 158 CB ARG A 25 4499 3890 5122 419 631 -296 C ATOM 159 CG ARG A 25 -5.120 30.790 21.230 1.00 35.28 C ANISOU 159 CG ARG A 25 4269 3980 5155 500 539 -166 C ATOM 160 CD ARG A 25 -6.415 30.642 22.051 1.00 37.02 C ANISOU 160 CD ARG A 25 4399 4207 5460 562 673 -178 C ATOM 161 NE ARG A 25 -6.206 29.886 23.294 1.00 37.31 N ANISOU 161 NE ARG A 25 4519 4287 5369 443 718 -312 N ATOM 162 CZ ARG A 25 -6.793 30.134 24.465 1.00 37.37 C ANISOU 162 CZ ARG A 25 4557 4243 5398 445 897 -402 C ATOM 163 NH1 ARG A 25 -7.649 31.136 24.606 1.00 39.44 N ANISOU 163 NH1 ARG A 25 4773 4389 5823 578 1075 -387 N ATOM 164 NH2 ARG A 25 -6.501 29.381 25.512 1.00 36.99 N ANISOU 164 NH2 ARG A 25 4590 4259 5207 313 908 -504 N ATOM 165 N THR A 26 -1.713 29.421 21.695 1.00 32.71 N ANISOU 165 N THR A 26 4213 3792 4425 178 308 -343 N ATOM 166 CA THR A 26 -1.200 28.100 21.307 1.00 31.69 C ANISOU 166 CA THR A 26 4050 3791 4200 131 169 -321 C ATOM 167 C THR A 26 -1.643 27.046 22.312 1.00 31.63 C ANISOU 167 C THR A 26 4038 3839 4141 87 187 -363 C ATOM 168 O THR A 26 -1.352 27.163 23.499 1.00 32.05 O ANISOU 168 O THR A 26 4171 3878 4129 17 257 -437 O ATOM 169 CB THR A 26 0.356 28.083 21.180 1.00 31.04 C ANISOU 169 CB THR A 26 4042 3744 4007 53 97 -343 C ATOM 170 OG1 THR A 26 0.759 28.794 20.007 1.00 31.12 O ANISOU 170 OG1 THR A 26 4040 3733 4052 83 53 -286 O ATOM 171 CG2 THR A 26 0.907 26.653 21.095 1.00 30.45 C ANISOU 171 CG2 THR A 26 3945 3778 3846 21 -4 -331 C ATOM 172 N ASP A 27 -2.336 26.019 21.817 1.00 31.31 N ANISOU 172 N ASP A 27 3912 3869 4117 107 122 -312 N ATOM 173 CA ASP A 27 -2.819 24.924 22.639 1.00 31.30 C ANISOU 173 CA ASP A 27 3906 3916 4069 57 131 -334 C ATOM 174 C ASP A 27 -2.441 23.585 22.005 1.00 30.76 C ANISOU 174 C ASP A 27 3832 3910 3944 26 14 -302 C ATOM 175 O ASP A 27 -2.598 23.401 20.784 1.00 30.90 O ANISOU 175 O ASP A 27 3799 3954 3988 51 -55 -255 O ATOM 176 CB ASP A 27 -4.338 25.010 22.783 1.00 32.30 C ANISOU 176 CB ASP A 27 3932 4051 4290 100 206 -309 C ATOM 177 CG ASP A 27 -4.800 26.314 23.435 1.00 34.31 C ANISOU 177 CG ASP A 27 4195 4218 4625 155 361 -347 C ATOM 178 OD1 ASP A 27 -5.466 27.126 22.752 1.00 35.10 O ANISOU 178 OD1 ASP A 27 4209 4280 4848 256 395 -283 O ATOM 179 OD2 ASP A 27 -4.501 26.530 24.631 1.00 35.83 O ANISOU 179 OD2 ASP A 27 4484 4376 4754 94 455 -437 O ATOM 180 N SER A 28 -1.953 22.653 22.832 1.00 30.21 N ANISOU 180 N SER A 28 3825 3860 3795 -32 0 -323 N ATOM 181 CA SER A 28 -1.643 21.290 22.380 1.00 29.48 C ANISOU 181 CA SER A 28 3748 3790 3664 -51 -78 -296 C ATOM 182 C SER A 28 -2.358 20.203 23.186 1.00 29.40 C ANISOU 182 C SER A 28 3751 3788 3630 -109 -58 -291 C ATOM 183 O SER A 28 -2.658 20.377 24.367 1.00 29.72 O ANISOU 183 O SER A 28 3809 3837 3645 -148 5 -310 O ATOM 184 CB SER A 28 -0.142 21.034 22.416 1.00 29.08 C ANISOU 184 CB SER A 28 3756 3743 3551 -48 -125 -290 C ATOM 185 OG SER A 28 0.570 22.251 22.330 1.00 30.58 O ANISOU 185 OG SER A 28 3950 3933 3735 -36 -114 -305 O ATOM 186 N VAL A 29 -2.644 19.089 22.521 1.00 29.07 N ANISOU 186 N VAL A 29 3713 3744 3590 -131 -106 -270 N ATOM 187 CA VAL A 29 -3.148 17.875 23.174 1.00 29.21 C ANISOU 187 CA VAL A 29 3769 3751 3578 -200 -97 -257 C ATOM 188 C VAL A 29 -2.332 16.683 22.691 1.00 28.79 C ANISOU 188 C VAL A 29 3797 3640 3501 -197 -144 -241 C ATOM 189 O VAL A 29 -1.780 16.710 21.578 1.00 28.59 O ANISOU 189 O VAL A 29 3777 3601 3486 -156 -178 -254 O ATOM 190 CB VAL A 29 -4.644 17.603 22.891 1.00 29.74 C ANISOU 190 CB VAL A 29 3763 3858 3679 -258 -81 -250 C ATOM 191 CG1 VAL A 29 -5.493 18.793 23.278 1.00 30.34 C ANISOU 191 CG1 VAL A 29 3737 3983 3808 -228 -12 -254 C ATOM 192 CG2 VAL A 29 -4.875 17.240 21.426 1.00 30.68 C ANISOU 192 CG2 VAL A 29 3858 3989 3810 -276 -144 -244 C ATOM 193 N VAL A 30 -2.252 15.642 23.517 1.00 28.56 N ANISOU 193 N VAL A 30 3837 3571 3443 -237 -134 -210 N ATOM 194 CA VAL A 30 -1.422 14.487 23.174 1.00 28.07 C ANISOU 194 CA VAL A 30 3863 3423 3381 -209 -154 -183 C ATOM 195 C VAL A 30 -2.175 13.153 23.211 1.00 28.73 C ANISOU 195 C VAL A 30 4020 3430 3465 -292 -137 -174 C ATOM 196 O VAL A 30 -2.713 12.756 24.240 1.00 29.20 O ANISOU 196 O VAL A 30 4099 3493 3502 -359 -117 -137 O ATOM 197 CB VAL A 30 -0.132 14.463 23.994 1.00 27.71 C ANISOU 197 CB VAL A 30 3840 3378 3311 -146 -167 -120 C ATOM 198 CG1 VAL A 30 0.720 13.310 23.586 1.00 27.68 C ANISOU 198 CG1 VAL A 30 3907 3275 3336 -81 -169 -77 C ATOM 199 CG2 VAL A 30 0.631 15.757 23.766 1.00 26.99 C ANISOU 199 CG2 VAL A 30 3685 3360 3210 -94 -185 -141 C ATOM 200 N TRP A 31 -2.212 12.487 22.058 1.00 28.78 N ANISOU 200 N TRP A 31 4080 3368 3486 -307 -138 -214 N ATOM 201 CA TRP A 31 -2.925 11.230 21.896 1.00 29.57 C ANISOU 201 CA TRP A 31 4275 3381 3581 -414 -115 -225 C ATOM 202 C TRP A 31 -1.973 10.050 21.761 1.00 30.36 C ANISOU 202 C TRP A 31 4514 3315 3708 -356 -78 -206 C ATOM 203 O TRP A 31 -0.942 10.137 21.097 1.00 29.88 O ANISOU 203 O TRP A 31 4466 3216 3671 -249 -68 -223 O ATOM 204 CB TRP A 31 -3.834 11.284 20.664 1.00 29.91 C ANISOU 204 CB TRP A 31 4291 3471 3604 -517 -132 -293 C ATOM 205 CG TRP A 31 -4.831 12.392 20.696 1.00 29.51 C ANISOU 205 CG TRP A 31 4084 3578 3551 -552 -161 -286 C ATOM 206 CD1 TRP A 31 -4.710 13.624 20.111 1.00 29.26 C ANISOU 206 CD1 TRP A 31 3945 3639 3535 -482 -192 -291 C ATOM 207 CD2 TRP A 31 -6.099 12.385 21.353 1.00 30.61 C ANISOU 207 CD2 TRP A 31 4151 3796 3684 -653 -150 -259 C ATOM 208 NE1 TRP A 31 -5.825 14.388 20.368 1.00 29.62 N ANISOU 208 NE1 TRP A 31 3855 3799 3599 -515 -194 -263 N ATOM 209 CE2 TRP A 31 -6.696 13.655 21.129 1.00 30.86 C ANISOU 209 CE2 TRP A 31 4021 3961 3742 -617 -166 -246 C ATOM 210 CE3 TRP A 31 -6.794 11.435 22.111 1.00 31.65 C ANISOU 210 CE3 TRP A 31 4335 3896 3793 -769 -121 -237 C ATOM 211 CZ2 TRP A 31 -7.956 13.998 21.639 1.00 31.29 C ANISOU 211 CZ2 TRP A 31 3951 4124 3813 -676 -142 -214 C ATOM 212 CZ3 TRP A 31 -8.052 11.777 22.619 1.00 33.19 C ANISOU 212 CZ3 TRP A 31 4407 4217 3987 -851 -106 -212 C ATOM 213 CH2 TRP A 31 -8.617 13.051 22.378 1.00 32.10 C ANISOU 213 CH2 TRP A 31 4093 4217 3886 -796 -112 -201 C ATOM 214 N LEU A 32 -2.338 8.950 22.412 1.00 31.56 N ANISOU 214 N LEU A 32 4766 3363 3863 -424 -46 -163 N ATOM 215 CA LEU A 32 -1.725 7.646 22.199 1.00 32.80 C ANISOU 215 CA LEU A 32 5081 3318 4064 -387 12 -146 C ATOM 216 C LEU A 32 -2.863 6.731 21.792 1.00 34.18 C ANISOU 216 C LEU A 32 5364 3411 4211 -572 45 -208 C ATOM 217 O LEU A 32 -3.612 6.242 22.641 1.00 35.23 O ANISOU 217 O LEU A 32 5528 3533 4326 -679 47 -156 O ATOM 218 CB LEU A 32 -1.057 7.130 23.484 1.00 33.06 C ANISOU 218 CB LEU A 32 5146 3287 4128 -304 17 -5 C ATOM 219 CG LEU A 32 -0.362 5.759 23.425 1.00 33.83 C ANISOU 219 CG LEU A 32 5401 3150 4301 -227 91 53 C ATOM 220 CD1 LEU A 32 0.680 5.690 22.321 1.00 32.22 C ANISOU 220 CD1 LEU A 32 5222 2864 4157 -84 144 -3 C ATOM 221 CD2 LEU A 32 0.273 5.436 24.748 1.00 33.93 C ANISOU 221 CD2 LEU A 32 5405 3150 4338 -144 69 233 C ATOM 222 N GLY A 33 -3.006 6.508 20.492 1.00 34.65 N ANISOU 222 N GLY A 33 5483 3430 4251 -634 70 -319 N ATOM 223 CA GLY A 33 -4.201 5.849 19.974 1.00 35.79 C ANISOU 223 CA GLY A 33 5707 3555 4338 -859 83 -390 C ATOM 224 C GLY A 33 -5.354 6.834 20.060 1.00 34.84 C ANISOU 224 C GLY A 33 5402 3674 4163 -966 1 -384 C ATOM 225 O GLY A 33 -5.207 7.998 19.702 1.00 33.48 O ANISOU 225 O GLY A 33 5083 3649 3987 -887 -49 -389 O ATOM 226 N ASP A 34 -6.493 6.373 20.557 1.00 35.76 N ANISOU 226 N ASP A 34 5520 3825 4244 -1139 -2 -362 N ATOM 227 CA ASP A 34 -7.633 7.247 20.761 1.00 35.54 C ANISOU 227 CA ASP A 34 5296 4024 4184 -1223 -60 -336 C ATOM 228 C ASP A 34 -7.807 7.701 22.239 1.00 35.30 C ANISOU 228 C ASP A 34 5173 4061 4178 -1159 -54 -247 C ATOM 229 O ASP A 34 -8.906 8.097 22.634 1.00 36.04 O ANISOU 229 O ASP A 34 5135 4308 4252 -1253 -65 -222 O ATOM 230 CB ASP A 34 -8.907 6.579 20.223 1.00 36.92 C ANISOU 230 CB ASP A 34 5488 4253 4287 -1483 -72 -372 C ATOM 231 CG ASP A 34 -9.194 5.243 20.890 1.00 38.85 C ANISOU 231 CG ASP A 34 5908 4336 4519 -1620 -13 -356 C ATOM 232 OD1 ASP A 34 -8.780 5.065 22.054 1.00 38.70 O ANISOU 232 OD1 ASP A 34 5924 4237 4544 -1523 17 -280 O ATOM 233 OD2 ASP A 34 -9.829 4.365 20.256 1.00 41.40 O ANISOU 233 OD2 ASP A 34 6340 4612 4778 -1842 0 -414 O ATOM 234 N LEU A 35 -6.740 7.651 23.045 1.00 34.57 N ANISOU 234 N LEU A 35 5142 3871 4123 -1010 -32 -196 N ATOM 235 CA LEU A 35 -6.796 8.123 24.439 1.00 33.89 C ANISOU 235 CA LEU A 35 4984 3862 4031 -970 -25 -120 C ATOM 236 C LEU A 35 -5.901 9.340 24.661 1.00 32.62 C ANISOU 236 C LEU A 35 4728 3776 3891 -796 -46 -112 C ATOM 237 O LEU A 35 -4.749 9.327 24.259 1.00 32.59 O ANISOU 237 O LEU A 35 4775 3693 3915 -673 -57 -112 O ATOM 238 CB LEU A 35 -6.391 7.014 25.408 1.00 34.68 C ANISOU 238 CB LEU A 35 5230 3816 4129 -987 5 -35 C ATOM 239 CG LEU A 35 -7.142 5.678 25.389 1.00 36.30 C ANISOU 239 CG LEU A 35 5574 3902 4316 -1167 40 -27 C ATOM 240 CD1 LEU A 35 -6.638 4.759 26.491 1.00 36.40 C ANISOU 240 CD1 LEU A 35 5718 3775 4338 -1152 67 91 C ATOM 241 CD2 LEU A 35 -8.632 5.877 25.535 1.00 37.48 C ANISOU 241 CD2 LEU A 35 5614 4213 4412 -1354 38 -48 C ATOM 242 N GLN A 36 -6.423 10.393 25.290 1.00 31.89 N ANISOU 242 N GLN A 36 4501 3830 3784 -792 -39 -110 N ATOM 243 CA GLN A 36 -5.623 11.593 25.515 1.00 30.77 C ANISOU 243 CA GLN A 36 4291 3748 3652 -658 -48 -116 C ATOM 244 C GLN A 36 -4.660 11.371 26.674 1.00 31.03 C ANISOU 244 C GLN A 36 4392 3746 3651 -615 -46 -45 C ATOM 245 O GLN A 36 -5.069 10.938 27.755 1.00 32.07 O ANISOU 245 O GLN A 36 4554 3896 3736 -700 -20 5 O ATOM 246 CB GLN A 36 -6.505 12.833 25.754 1.00 30.50 C ANISOU 246 CB GLN A 36 4108 3855 3625 -663 -15 -148 C ATOM 247 CG GLN A 36 -5.717 14.161 25.832 1.00 29.56 C ANISOU 247 CG GLN A 36 3939 3773 3520 -541 -13 -172 C ATOM 248 CD GLN A 36 -6.585 15.402 26.147 1.00 29.75 C ANISOU 248 CD GLN A 36 3837 3896 3570 -529 51 -205 C ATOM 249 OE1 GLN A 36 -7.817 15.332 26.162 1.00 30.90 O ANISOU 249 OE1 GLN A 36 3898 4106 3737 -592 88 -202 O ATOM 250 NE2 GLN A 36 -5.928 16.545 26.387 1.00 27.21 N ANISOU 250 NE2 GLN A 36 3503 3582 3253 -447 75 -234 N ATOM 251 N THR A 37 -3.387 11.679 26.452 1.00 30.41 N ANISOU 251 N THR A 37 4327 3640 3586 -495 -77 -30 N ATOM 252 CA THR A 37 -2.381 11.520 27.494 1.00 30.70 C ANISOU 252 CA THR A 37 4402 3679 3583 -456 -95 62 C ATOM 253 C THR A 37 -1.925 12.828 28.119 1.00 30.32 C ANISOU 253 C THR A 37 4281 3756 3484 -435 -99 45 C ATOM 254 O THR A 37 -1.532 12.852 29.279 1.00 30.84 O ANISOU 254 O THR A 37 4363 3880 3474 -477 -106 112 O ATOM 255 CB THR A 37 -1.146 10.744 27.009 1.00 30.82 C ANISOU 255 CB THR A 37 4482 3582 3646 -344 -123 126 C ATOM 256 OG1 THR A 37 -0.555 11.430 25.904 1.00 30.09 O ANISOU 256 OG1 THR A 37 4339 3501 3592 -250 -136 58 O ATOM 257 CG2 THR A 37 -1.517 9.327 26.604 1.00 31.07 C ANISOU 257 CG2 THR A 37 4631 3452 3724 -377 -93 145 C ATOM 258 N HIS A 38 -1.968 13.914 27.359 1.00 29.88 N ANISOU 258 N HIS A 38 4154 3740 3459 -387 -94 -39 N ATOM 259 CA HIS A 38 -1.506 15.211 27.866 1.00 30.04 C ANISOU 259 CA HIS A 38 4129 3850 3435 -378 -83 -70 C ATOM 260 C HIS A 38 -2.360 16.322 27.320 1.00 30.20 C ANISOU 260 C HIS A 38 4076 3897 3501 -368 -35 -163 C ATOM 261 O HIS A 38 -2.978 16.181 26.271 1.00 30.22 O ANISOU 261 O HIS A 38 4043 3870 3570 -344 -42 -188 O ATOM 262 CB HIS A 38 -0.053 15.492 27.471 1.00 29.36 C ANISOU 262 CB HIS A 38 4038 3769 3349 -291 -140 -38 C ATOM 263 CG HIS A 38 0.912 14.464 27.954 1.00 29.52 C ANISOU 263 CG HIS A 38 4100 3770 3345 -265 -188 83 C ATOM 264 ND1 HIS A 38 1.075 13.252 27.325 1.00 28.87 N ANISOU 264 ND1 HIS A 38 4064 3573 3332 -202 -197 131 N ATOM 265 CD2 HIS A 38 1.744 14.454 29.021 1.00 30.14 C ANISOU 265 CD2 HIS A 38 4179 3930 3342 -297 -226 179 C ATOM 266 CE1 HIS A 38 1.971 12.538 27.983 1.00 30.55 C ANISOU 266 CE1 HIS A 38 4297 3782 3528 -167 -232 264 C ATOM 267 NE2 HIS A 38 2.400 13.249 29.009 1.00 30.86 N ANISOU 267 NE2 HIS A 38 4298 3956 3470 -227 -262 306 N ATOM 268 N ARG A 39 -2.373 17.435 28.037 1.00 30.99 N ANISOU 268 N ARG A 39 4159 4053 3561 -393 18 -208 N ATOM 269 CA ARG A 39 -3.078 18.630 27.613 1.00 31.31 C ANISOU 269 CA ARG A 39 4135 4099 3664 -358 84 -283 C ATOM 270 C ARG A 39 -2.196 19.780 27.996 1.00 31.04 C ANISOU 270 C ARG A 39 4129 4080 3586 -355 105 -323 C ATOM 271 O ARG A 39 -1.723 19.816 29.129 1.00 32.04 O ANISOU 271 O ARG A 39 4312 4253 3608 -439 121 -321 O ATOM 272 CB ARG A 39 -4.400 18.780 28.370 1.00 32.40 C ANISOU 272 CB ARG A 39 4236 4271 3805 -417 188 -316 C ATOM 273 CG ARG A 39 -5.092 20.128 28.124 1.00 33.82 C ANISOU 273 CG ARG A 39 4343 4444 4064 -358 285 -380 C ATOM 274 CD ARG A 39 -6.054 20.541 29.234 1.00 36.55 C ANISOU 274 CD ARG A 39 4672 4824 4393 -411 431 -432 C ATOM 275 NE ARG A 39 -6.851 19.422 29.727 1.00 37.99 N ANISOU 275 NE ARG A 39 4836 5058 4540 -496 436 -393 N ATOM 276 CZ ARG A 39 -6.855 19.008 30.989 1.00 39.34 C ANISOU 276 CZ ARG A 39 5076 5273 4598 -610 484 -400 C ATOM 277 NH1 ARG A 39 -6.115 19.635 31.909 1.00 37.47 N ANISOU 277 NH1 ARG A 39 4928 5048 4260 -663 530 -450 N ATOM 278 NH2 ARG A 39 -7.614 17.970 31.329 1.00 40.67 N ANISOU 278 NH2 ARG A 39 5228 5485 4741 -692 485 -353 N ATOM 279 N TRP A 40 -1.989 20.717 27.077 1.00 30.12 N ANISOU 279 N TRP A 40 3978 3931 3535 -281 103 -353 N ATOM 280 CA TRP A 40 -1.246 21.926 27.391 1.00 30.06 C ANISOU 280 CA TRP A 40 4009 3921 3490 -297 138 -402 C ATOM 281 C TRP A 40 -1.940 23.149 26.841 1.00 30.60 C ANISOU 281 C TRP A 40 4039 3928 3658 -232 222 -454 C ATOM 282 O TRP A 40 -1.828 23.454 25.659 1.00 30.45 O ANISOU 282 O TRP A 40 3975 3880 3715 -153 174 -428 O ATOM 283 CB TRP A 40 0.187 21.846 26.872 1.00 28.98 C ANISOU 283 CB TRP A 40 3888 3806 3318 -279 37 -359 C ATOM 284 CG TRP A 40 1.053 22.974 27.343 1.00 29.04 C ANISOU 284 CG TRP A 40 3944 3834 3255 -342 61 -403 C ATOM 285 CD1 TRP A 40 0.798 23.833 28.380 1.00 29.28 C ANISOU 285 CD1 TRP A 40 4039 3862 3225 -437 165 -482 C ATOM 286 CD2 TRP A 40 2.335 23.347 26.823 1.00 27.58 C ANISOU 286 CD2 TRP A 40 3757 3680 3042 -339 -8 -376 C ATOM 287 NE1 TRP A 40 1.834 24.718 28.524 1.00 29.71 N ANISOU 287 NE1 TRP A 40 4144 3938 3208 -508 157 -510 N ATOM 288 CE2 TRP A 40 2.792 24.439 27.582 1.00 28.15 C ANISOU 288 CE2 TRP A 40 3894 3770 3030 -450 44 -438 C ATOM 289 CE3 TRP A 40 3.144 22.858 25.791 1.00 26.47 C ANISOU 289 CE3 TRP A 40 3567 3557 2932 -264 -100 -313 C ATOM 290 CZ2 TRP A 40 4.020 25.055 27.339 1.00 27.91 C ANISOU 290 CZ2 TRP A 40 3873 3787 2944 -499 -5 -427 C ATOM 291 CZ3 TRP A 40 4.363 23.478 25.545 1.00 25.01 C ANISOU 291 CZ3 TRP A 40 3377 3424 2700 -293 -141 -299 C ATOM 292 CH2 TRP A 40 4.787 24.559 26.317 1.00 26.81 C ANISOU 292 CH2 TRP A 40 3662 3681 2844 -414 -101 -350 C ATOM 293 N SER A 41 -2.644 23.865 27.702 1.00 32.23 N ANISOU 293 N SER A 41 4266 4113 3868 -263 357 -522 N ATOM 294 CA SER A 41 -3.364 25.053 27.271 1.00 33.75 C ANISOU 294 CA SER A 41 4420 4223 4180 -177 463 -558 C ATOM 295 C SER A 41 -2.462 26.290 27.234 1.00 34.49 C ANISOU 295 C SER A 41 4599 4246 4258 -191 499 -611 C ATOM 296 O SER A 41 -1.476 26.370 27.981 1.00 35.13 O ANISOU 296 O SER A 41 4778 4361 4208 -308 485 -652 O ATOM 297 CB SER A 41 -4.556 25.279 28.191 1.00 35.16 C ANISOU 297 CB SER A 41 4580 4393 4387 -188 624 -613 C ATOM 298 OG SER A 41 -4.781 26.661 28.389 1.00 37.76 O ANISOU 298 OG SER A 41 4947 4616 4783 -144 779 -687 O ATOM 299 N ASN A 42 -2.800 27.260 26.382 1.00 35.03 N ANISOU 299 N ASN A 42 4632 4224 4454 -86 543 -599 N ATOM 300 CA ASN A 42 -2.055 28.527 26.339 1.00 35.79 C ANISOU 300 CA ASN A 42 4825 4225 4549 -107 599 -651 C ATOM 301 C ASN A 42 -2.020 29.193 27.703 1.00 37.25 C ANISOU 301 C ASN A 42 5140 4358 4654 -218 760 -779 C ATOM 302 O ASN A 42 -1.032 29.836 28.047 1.00 37.90 O ANISOU 302 O ASN A 42 5341 4417 4641 -330 770 -840 O ATOM 303 CB ASN A 42 -2.643 29.512 25.311 1.00 36.51 C ANISOU 303 CB ASN A 42 4859 4202 4810 35 648 -601 C ATOM 304 CG ASN A 42 -1.721 30.706 25.042 1.00 36.49 C ANISOU 304 CG ASN A 42 4967 4094 4804 4 676 -632 C ATOM 305 OD1 ASN A 42 -0.796 30.594 24.259 1.00 35.76 O ANISOU 305 OD1 ASN A 42 4871 4048 4668 -18 544 -581 O ATOM 306 ND2 ASN A 42 -1.981 31.844 25.686 1.00 38.81 N ANISOU 306 ND2 ASN A 42 5364 4239 5143 -3 860 -722 N ATOM 307 N ASP A 43 -3.110 29.034 28.459 1.00 38.11 N ANISOU 307 N ASP A 43 5226 4462 4792 -203 889 -822 N ATOM 308 CA ASP A 43 -3.275 29.641 29.784 1.00 39.89 C ANISOU 308 CA ASP A 43 5579 4638 4938 -312 1077 -961 C ATOM 309 C ASP A 43 -2.308 29.057 30.796 1.00 38.88 C ANISOU 309 C ASP A 43 5551 4639 4583 -520 1005 -1001 C ATOM 310 O ASP A 43 -1.983 29.716 31.777 1.00 40.35 O ANISOU 310 O ASP A 43 5880 4799 4651 -668 1124 -1122 O ATOM 311 CB ASP A 43 -4.711 29.456 30.317 1.00 41.72 C ANISOU 311 CB ASP A 43 5736 4865 5252 -244 1233 -986 C ATOM 312 CG ASP A 43 -5.795 29.710 29.244 1.00 44.42 C ANISOU 312 CG ASP A 43 5911 5145 5823 -27 1259 -887 C ATOM 313 OD1 ASP A 43 -5.802 30.801 28.614 1.00 47.61 O ANISOU 313 OD1 ASP A 43 6327 5406 6357 80 1326 -877 O ATOM 314 OD2 ASP A 43 -6.654 28.814 29.043 1.00 45.41 O ANISOU 314 OD2 ASP A 43 5889 5372 5992 23 1209 -807 O ATOM 315 N SER A 44 -1.847 27.831 30.552 1.00 36.48 N ANISOU 315 N SER A 44 5174 4470 4216 -536 816 -894 N ATOM 316 CA SER A 44 -1.011 27.111 31.506 1.00 35.61 C ANISOU 316 CA SER A 44 5124 4501 3907 -709 730 -883 C ATOM 317 C SER A 44 0.494 27.155 31.222 1.00 34.71 C ANISOU 317 C SER A 44 5038 4455 3697 -784 581 -833 C ATOM 318 O SER A 44 0.935 26.970 30.077 1.00 33.56 O ANISOU 318 O SER A 44 4816 4299 3636 -675 466 -751 O ATOM 319 CB SER A 44 -1.474 25.660 31.598 1.00 34.94 C ANISOU 319 CB SER A 44 4949 4511 3814 -682 638 -784 C ATOM 320 OG SER A 44 -0.559 24.899 32.362 1.00 34.71 O ANISOU 320 OG SER A 44 4960 4615 3614 -820 529 -727 O ATOM 321 N ALA A 45 1.278 27.367 32.280 1.00 35.11 N ANISOU 321 N ALA A 45 5188 4597 3556 -985 583 -876 N ATOM 322 CA ALA A 45 2.754 27.388 32.186 1.00 34.28 C ANISOU 322 CA ALA A 45 5089 4602 3335 -1087 439 -813 C ATOM 323 C ALA A 45 3.369 26.006 31.954 1.00 32.90 C ANISOU 323 C ALA A 45 4799 4563 3139 -1036 251 -645 C ATOM 324 O ALA A 45 4.498 25.895 31.485 1.00 32.21 O ANISOU 324 O ALA A 45 4662 4554 3024 -1038 126 -561 O ATOM 325 CB ALA A 45 3.353 28.011 33.427 1.00 35.49 C ANISOU 325 CB ALA A 45 5373 4840 3271 -1345 492 -899 C ATOM 326 N THR A 46 2.615 24.962 32.295 1.00 32.43 N ANISOU 326 N THR A 46 4700 4525 3097 -989 245 -594 N ATOM 327 CA THR A 46 3.121 23.597 32.322 1.00 31.51 C ANISOU 327 CA THR A 46 4508 4512 2953 -957 98 -437 C ATOM 328 C THR A 46 2.167 22.706 31.547 1.00 30.58 C ANISOU 328 C THR A 46 4323 4303 2993 -788 95 -398 C ATOM 329 O THR A 46 0.984 23.031 31.420 1.00 30.62 O ANISOU 329 O THR A 46 4334 4218 3083 -742 208 -481 O ATOM 330 CB THR A 46 3.240 23.065 33.772 1.00 32.61 C ANISOU 330 CB THR A 46 4693 4790 2907 -1133 83 -391 C ATOM 331 OG1 THR A 46 2.061 23.398 34.499 1.00 33.60 O ANISOU 331 OG1 THR A 46 4892 4866 3008 -1199 240 -512 O ATOM 332 CG2 THR A 46 4.419 23.675 34.500 1.00 33.43 C ANISOU 332 CG2 THR A 46 4841 5040 2821 -1329 32 -383 C ATOM 333 N ILE A 47 2.691 21.600 31.014 1.00 29.70 N ANISOU 333 N ILE A 47 4146 4217 2923 -699 -24 -271 N ATOM 334 CA ILE A 47 1.893 20.549 30.386 1.00 28.65 C ANISOU 334 CA ILE A 47 3973 4008 2906 -583 -36 -228 C ATOM 335 C ILE A 47 1.205 19.738 31.473 1.00 29.08 C ANISOU 335 C ILE A 47 4061 4097 2891 -667 -9 -193 C ATOM 336 O ILE A 47 1.832 19.354 32.453 1.00 29.85 O ANISOU 336 O ILE A 47 4185 4296 2861 -768 -58 -113 O ATOM 337 CB ILE A 47 2.804 19.590 29.607 1.00 28.55 C ANISOU 337 CB ILE A 47 3909 3995 2942 -479 -149 -111 C ATOM 338 CG1 ILE A 47 3.597 20.354 28.547 1.00 28.62 C ANISOU 338 CG1 ILE A 47 3880 3994 3001 -410 -178 -137 C ATOM 339 CG2 ILE A 47 2.008 18.438 28.979 1.00 28.19 C ANISOU 339 CG2 ILE A 47 3854 3856 3000 -390 -151 -81 C ATOM 340 CD1 ILE A 47 4.944 19.738 28.246 1.00 30.41 C ANISOU 340 CD1 ILE A 47 4054 4284 3218 -356 -275 -20 C ATOM 341 N SER A 48 -0.083 19.481 31.294 1.00 28.80 N ANISOU 341 N SER A 48 4015 3996 2933 -637 64 -239 N ATOM 342 CA SER A 48 -0.876 18.711 32.252 1.00 29.18 C ANISOU 342 CA SER A 48 4091 4075 2921 -725 103 -210 C ATOM 343 C SER A 48 -1.003 17.259 31.818 1.00 28.85 C ANISOU 343 C SER A 48 4037 3984 2940 -668 27 -100 C ATOM 344 O SER A 48 -1.225 16.977 30.628 1.00 28.08 O ANISOU 344 O SER A 48 3902 3804 2962 -562 4 -108 O ATOM 345 CB SER A 48 -2.267 19.330 32.404 1.00 29.47 C ANISOU 345 CB SER A 48 4110 4083 3003 -740 247 -324 C ATOM 346 OG SER A 48 -2.195 20.586 33.064 1.00 29.81 O ANISOU 346 OG SER A 48 4200 4150 2977 -812 352 -433 O ATOM 347 N PHE A 49 -0.844 16.344 32.777 1.00 29.44 N ANISOU 347 N PHE A 49 4155 4106 2923 -752 -6 3 N ATOM 348 CA PHE A 49 -1.094 14.925 32.544 1.00 29.47 C ANISOU 348 CA PHE A 49 4178 4037 2983 -721 -50 106 C ATOM 349 C PHE A 49 -2.598 14.675 32.535 1.00 29.81 C ANISOU 349 C PHE A 49 4215 4048 3063 -772 35 42 C ATOM 350 O PHE A 49 -3.292 15.060 33.466 1.00 30.84 O ANISOU 350 O PHE A 49 4352 4253 3114 -881 117 -3 O ATOM 351 CB PHE A 49 -0.476 14.058 33.646 1.00 30.42 C ANISOU 351 CB PHE A 49 4347 4216 2996 -797 -112 264 C ATOM 352 CG PHE A 49 1.029 14.117 33.726 1.00 30.82 C ANISOU 352 CG PHE A 49 4375 4328 3009 -750 -212 373 C ATOM 353 CD1 PHE A 49 1.812 14.340 32.596 1.00 29.55 C ANISOU 353 CD1 PHE A 49 4164 4113 2949 -607 -251 360 C ATOM 354 CD2 PHE A 49 1.673 13.909 34.951 1.00 31.33 C ANISOU 354 CD2 PHE A 49 4455 4524 2926 -859 -270 507 C ATOM 355 CE1 PHE A 49 3.210 14.377 32.697 1.00 29.45 C ANISOU 355 CE1 PHE A 49 4105 4181 2903 -565 -339 476 C ATOM 356 CE2 PHE A 49 3.060 13.941 35.048 1.00 30.57 C ANISOU 356 CE2 PHE A 49 4307 4516 2792 -823 -373 636 C ATOM 357 CZ PHE A 49 3.829 14.181 33.919 1.00 29.06 C ANISOU 357 CZ PHE A 49 4053 4273 2715 -670 -403 619 C ATOM 358 N THR A 50 -3.121 14.034 31.501 1.00 29.43 N ANISOU 358 N THR A 50 4151 3904 3126 -710 23 37 N ATOM 359 CA THR A 50 -4.531 13.667 31.540 1.00 29.98 C ANISOU 359 CA THR A 50 4201 3972 3218 -785 90 3 C ATOM 360 C THR A 50 -4.708 12.183 31.893 1.00 31.17 C ANISOU 360 C THR A 50 4432 4062 3349 -858 60 111 C ATOM 361 O THR A 50 -5.830 11.657 31.922 1.00 32.26 O ANISOU 361 O THR A 50 4564 4197 3497 -946 104 101 O ATOM 362 CB THR A 50 -5.271 14.046 30.245 1.00 29.22 C ANISOU 362 CB THR A 50 4023 3844 3235 -720 106 -76 C ATOM 363 OG1 THR A 50 -4.682 13.361 29.135 1.00 29.06 O ANISOU 363 OG1 THR A 50 4038 3726 3279 -646 29 -47 O ATOM 364 CG2 THR A 50 -5.200 15.550 30.020 1.00 27.93 C ANISOU 364 CG2 THR A 50 3787 3726 3098 -650 151 -164 C ATOM 365 N LYS A 51 -3.591 11.518 32.176 1.00 31.20 N ANISOU 365 N LYS A 51 4505 4020 3329 -822 -11 227 N ATOM 366 CA LYS A 51 -3.592 10.129 32.631 1.00 31.97 C ANISOU 366 CA LYS A 51 4697 4038 3414 -876 -35 358 C ATOM 367 C LYS A 51 -2.655 10.017 33.812 1.00 32.30 C ANISOU 367 C LYS A 51 4769 4154 3350 -904 -85 496 C ATOM 368 O LYS A 51 -1.714 10.812 33.921 1.00 32.03 O ANISOU 368 O LYS A 51 4690 4201 3280 -849 -124 496 O ATOM 369 CB LYS A 51 -3.108 9.205 31.512 1.00 32.21 C ANISOU 369 CB LYS A 51 4784 3894 3561 -767 -71 392 C ATOM 370 CG LYS A 51 -4.162 8.285 30.979 1.00 33.41 C ANISOU 370 CG LYS A 51 4994 3938 3761 -848 -32 361 C ATOM 371 CD LYS A 51 -5.335 9.024 30.420 1.00 33.20 C ANISOU 371 CD LYS A 51 4874 3996 3745 -909 10 222 C ATOM 372 CE LYS A 51 -6.506 8.103 30.264 1.00 34.76 C ANISOU 372 CE LYS A 51 5114 4145 3947 -1052 44 217 C ATOM 373 NZ LYS A 51 -7.349 8.629 29.163 1.00 36.35 N ANISOU 373 NZ LYS A 51 5219 4399 4195 -1068 56 103 N ATOM 374 N PRO A 52 -2.894 9.036 34.704 1.00 33.04 N ANISOU 374 N PRO A 52 4937 4234 3384 -1004 -91 626 N ATOM 375 CA PRO A 52 -1.945 8.832 35.805 1.00 33.58 C ANISOU 375 CA PRO A 52 5026 4388 3344 -1036 -159 798 C ATOM 376 C PRO A 52 -0.534 8.560 35.286 1.00 33.20 C ANISOU 376 C PRO A 52 4961 4277 3377 -862 -245 914 C ATOM 377 O PRO A 52 0.435 9.054 35.849 1.00 33.49 O ANISOU 377 O PRO A 52 4946 4447 3330 -858 -310 996 O ATOM 378 CB PRO A 52 -2.502 7.602 36.527 1.00 34.87 C ANISOU 378 CB PRO A 52 5284 4492 3473 -1147 -152 937 C ATOM 379 CG PRO A 52 -3.955 7.603 36.203 1.00 34.64 C ANISOU 379 CG PRO A 52 5258 4436 3467 -1244 -57 791 C ATOM 380 CD PRO A 52 -4.063 8.141 34.808 1.00 33.64 C ANISOU 380 CD PRO A 52 5072 4239 3470 -1119 -38 633 C ATOM 381 N TRP A 53 -0.442 7.820 34.185 1.00 32.69 N ANISOU 381 N TRP A 53 4933 4019 3467 -731 -234 909 N ATOM 382 CA TRP A 53 0.829 7.342 33.649 1.00 32.95 C ANISOU 382 CA TRP A 53 4956 3961 3603 -548 -284 1027 C ATOM 383 C TRP A 53 1.389 8.155 32.472 1.00 31.59 C ANISOU 383 C TRP A 53 4708 3789 3507 -417 -281 894 C ATOM 384 O TRP A 53 2.185 7.644 31.682 1.00 31.84 O ANISOU 384 O TRP A 53 4743 3700 3654 -257 -283 941 O ATOM 385 CB TRP A 53 0.657 5.890 33.212 1.00 33.96 C ANISOU 385 CB TRP A 53 5204 3845 3855 -488 -246 1109 C ATOM 386 CG TRP A 53 -0.669 5.625 32.565 1.00 32.55 C ANISOU 386 CG TRP A 53 5099 3560 3710 -586 -168 945 C ATOM 387 CD1 TRP A 53 -1.798 5.173 33.176 1.00 31.92 C ANISOU 387 CD1 TRP A 53 5084 3477 3567 -761 -134 947 C ATOM 388 CD2 TRP A 53 -1.007 5.818 31.185 1.00 30.33 C ANISOU 388 CD2 TRP A 53 4819 3189 3515 -537 -122 766 C ATOM 389 NE1 TRP A 53 -2.817 5.059 32.261 1.00 31.06 N ANISOU 389 NE1 TRP A 53 5006 3289 3507 -823 -73 787 N ATOM 390 CE2 TRP A 53 -2.358 5.448 31.032 1.00 29.73 C ANISOU 390 CE2 TRP A 53 4802 3069 3424 -692 -70 676 C ATOM 391 CE3 TRP A 53 -0.299 6.263 30.064 1.00 28.85 C ANISOU 391 CE3 TRP A 53 4584 2972 3405 -392 -121 682 C ATOM 392 CZ2 TRP A 53 -3.015 5.504 29.805 1.00 28.52 C ANISOU 392 CZ2 TRP A 53 4657 2854 3324 -714 -30 515 C ATOM 393 CZ3 TRP A 53 -0.958 6.327 28.842 1.00 27.63 C ANISOU 393 CZ3 TRP A 53 4452 2746 3299 -412 -75 514 C ATOM 394 CH2 TRP A 53 -2.302 5.946 28.725 1.00 27.30 C ANISOU 394 CH2 TRP A 53 4465 2672 3234 -576 -36 437 C ATOM 395 N SER A 54 0.982 9.412 32.357 1.00 30.27 N ANISOU 395 N SER A 54 4476 3748 3279 -480 -264 733 N ATOM 396 CA SER A 54 1.399 10.248 31.240 1.00 29.01 C ANISOU 396 CA SER A 54 4251 3590 3182 -377 -260 609 C ATOM 397 C SER A 54 2.915 10.531 31.227 1.00 29.69 C ANISOU 397 C SER A 54 4262 3751 3268 -267 -328 713 C ATOM 398 O SER A 54 3.504 10.765 30.154 1.00 29.24 O ANISOU 398 O SER A 54 4165 3649 3294 -145 -324 659 O ATOM 399 CB SER A 54 0.598 11.546 31.228 1.00 27.94 C ANISOU 399 CB SER A 54 4068 3560 2989 -467 -220 440 C ATOM 400 OG SER A 54 -0.792 11.309 31.085 1.00 27.10 O ANISOU 400 OG SER A 54 3994 3403 2901 -549 -155 354 O ATOM 401 N GLN A 55 3.545 10.498 32.404 1.00 30.64 N ANISOU 401 N GLN A 55 4355 4003 3285 -324 -393 869 N ATOM 402 CA GLN A 55 4.991 10.658 32.508 1.00 31.27 C ANISOU 402 CA GLN A 55 4339 4186 3355 -237 -471 1007 C ATOM 403 C GLN A 55 5.731 9.446 31.926 1.00 32.87 C ANISOU 403 C GLN A 55 4543 4236 3712 -42 -471 1156 C ATOM 404 O GLN A 55 6.955 9.494 31.733 1.00 34.13 O ANISOU 404 O GLN A 55 4600 4461 3907 76 -517 1270 O ATOM 405 CB GLN A 55 5.414 10.895 33.969 1.00 32.43 C ANISOU 405 CB GLN A 55 4451 4542 3328 -382 -551 1154 C ATOM 406 CG GLN A 55 6.854 11.405 34.151 1.00 32.23 C ANISOU 406 CG GLN A 55 4298 4699 3249 -352 -646 1278 C ATOM 407 CD GLN A 55 7.187 11.772 35.590 1.00 34.00 C ANISOU 407 CD GLN A 55 4494 5164 3259 -550 -731 1400 C ATOM 408 OE1 GLN A 55 6.320 12.200 36.353 1.00 34.16 O ANISOU 408 OE1 GLN A 55 4593 5242 3146 -738 -693 1300 O ATOM 409 NE2 GLN A 55 8.455 11.612 35.966 1.00 34.49 N ANISOU 409 NE2 GLN A 55 4436 5385 3282 -518 -842 1622 N ATOM 410 N GLY A 56 5.008 8.362 31.652 1.00 33.34 N ANISOU 410 N GLY A 56 4716 4089 3863 -11 -408 1157 N ATOM 411 CA GLY A 56 5.633 7.155 31.129 1.00 35.15 C ANISOU 411 CA GLY A 56 4980 4127 4248 173 -374 1284 C ATOM 412 C GLY A 56 6.695 6.637 32.078 1.00 37.88 C ANISOU 412 C GLY A 56 5250 4556 4585 244 -453 1573 C ATOM 413 O GLY A 56 6.469 6.567 33.285 1.00 39.04 O ANISOU 413 O GLY A 56 5403 4820 4611 109 -518 1700 O ATOM 414 N LYS A 57 7.859 6.285 31.547 1.00 39.37 N ANISOU 414 N LYS A 57 5356 4704 4897 451 -447 1690 N ATOM 415 CA LYS A 57 8.929 5.742 32.383 1.00 42.32 C ANISOU 415 CA LYS A 57 5626 5168 5286 547 -527 2004 C ATOM 416 C LYS A 57 10.048 6.754 32.641 1.00 42.62 C ANISOU 416 C LYS A 57 5462 5502 5230 541 -633 2081 C ATOM 417 O LYS A 57 11.147 6.377 33.052 1.00 44.68 O ANISOU 417 O LYS A 57 5586 5862 5528 659 -699 2347 O ATOM 418 CB LYS A 57 9.509 4.456 31.769 1.00 44.38 C ANISOU 418 CB LYS A 57 5922 5168 5772 806 -434 2140 C ATOM 419 CG LYS A 57 8.616 3.219 31.845 1.00 46.25 C ANISOU 419 CG LYS A 57 6366 5112 6095 800 -346 2159 C ATOM 420 CD LYS A 57 8.433 2.724 33.276 1.00 50.04 C ANISOU 420 CD LYS A 57 6862 5667 6484 693 -439 2411 C ATOM 421 CE LYS A 57 7.606 1.437 33.323 1.00 52.32 C ANISOU 421 CE LYS A 57 7366 5645 6870 687 -344 2446 C ATOM 422 NZ LYS A 57 7.161 1.100 34.708 1.00 54.11 N ANISOU 422 NZ LYS A 57 7629 5963 6966 519 -434 2646 N ATOM 423 N LEU A 58 9.777 8.035 32.401 1.00 40.89 N ANISOU 423 N LEU A 58 5218 5426 4893 400 -648 1863 N ATOM 424 CA LEU A 58 10.775 9.068 32.667 1.00 41.35 C ANISOU 424 CA LEU A 58 5107 5764 4840 347 -744 1914 C ATOM 425 C LEU A 58 10.885 9.381 34.165 1.00 42.93 C ANISOU 425 C LEU A 58 5264 6216 4832 138 -870 2072 C ATOM 426 O LEU A 58 9.887 9.372 34.886 1.00 42.63 O ANISOU 426 O LEU A 58 5346 6166 4686 -31 -862 2012 O ATOM 427 CB LEU A 58 10.443 10.347 31.900 1.00 38.98 C ANISOU 427 CB LEU A 58 4819 5504 4489 260 -706 1630 C ATOM 428 CG LEU A 58 10.066 10.321 30.410 1.00 37.34 C ANISOU 428 CG LEU A 58 4676 5086 4427 387 -589 1419 C ATOM 429 CD1 LEU A 58 9.923 11.740 29.904 1.00 33.04 C ANISOU 429 CD1 LEU A 58 4109 4644 3801 280 -587 1207 C ATOM 430 CD2 LEU A 58 11.065 9.535 29.539 1.00 38.31 C ANISOU 430 CD2 LEU A 58 4726 5104 4726 639 -538 1525 C ATOM 431 N SER A 59 12.100 9.647 34.633 1.00 44.89 N ANISOU 431 N SER A 59 5336 6710 5012 137 -982 2277 N ATOM 432 CA SER A 59 12.288 10.162 35.988 1.00 46.52 C ANISOU 432 CA SER A 59 5496 7206 4975 -111 -1110 2399 C ATOM 433 C SER A 59 11.800 11.608 36.052 1.00 45.16 C ANISOU 433 C SER A 59 5384 7146 4628 -348 -1091 2116 C ATOM 434 O SER A 59 11.670 12.273 35.016 1.00 43.40 O ANISOU 434 O SER A 59 5179 6828 4483 -290 -1013 1893 O ATOM 435 CB SER A 59 13.755 10.097 36.399 1.00 48.60 C ANISOU 435 CB SER A 59 5533 7730 5204 -65 -1245 2702 C ATOM 436 OG SER A 59 14.532 10.990 35.626 1.00 47.61 O ANISOU 436 OG SER A 59 5286 7712 5091 -35 -1246 2601 O ATOM 437 N ASN A 60 11.532 12.092 37.259 1.00 46.36 N ANISOU 437 N ASN A 60 5577 7492 4545 -617 -1152 2129 N ATOM 438 CA ASN A 60 11.089 13.462 37.428 1.00 45.89 C ANISOU 438 CA ASN A 60 5594 7524 4320 -846 -1111 1866 C ATOM 439 C ASN A 60 12.078 14.422 36.778 1.00 46.04 C ANISOU 439 C ASN A 60 5495 7663 4334 -838 -1143 1810 C ATOM 440 O ASN A 60 11.680 15.301 36.007 1.00 44.19 O ANISOU 440 O ASN A 60 5324 7325 4140 -842 -1051 1554 O ATOM 441 CB ASN A 60 10.874 13.796 38.909 1.00 47.60 C ANISOU 441 CB ASN A 60 5863 7962 4259 -1152 -1170 1913 C ATOM 442 CG ASN A 60 9.600 13.167 39.479 1.00 48.22 C ANISOU 442 CG ASN A 60 6095 7907 4320 -1209 -1096 1872 C ATOM 443 OD1 ASN A 60 8.674 12.805 38.744 1.00 48.87 O ANISOU 443 OD1 ASN A 60 6264 7732 4572 -1069 -982 1728 O ATOM 444 ND2 ASN A 60 9.548 13.047 40.793 1.00 49.12 N ANISOU 444 ND2 ASN A 60 6237 8215 4211 -1436 -1163 2000 N ATOM 445 N GLN A 61 13.368 14.223 37.060 1.00 48.55 N ANISOU 445 N GLN A 61 5632 8204 4612 -822 -1273 2067 N ATOM 446 CA GLN A 61 14.423 15.044 36.461 1.00 48.94 C ANISOU 446 CA GLN A 61 5542 8398 4655 -820 -1313 2050 C ATOM 447 C GLN A 61 14.367 15.041 34.922 1.00 47.03 C ANISOU 447 C GLN A 61 5299 7920 4652 -567 -1201 1897 C ATOM 448 O GLN A 61 14.511 16.093 34.294 1.00 46.02 O ANISOU 448 O GLN A 61 5178 7806 4503 -627 -1164 1711 O ATOM 449 CB GLN A 61 15.814 14.640 36.985 1.00 51.71 C ANISOU 449 CB GLN A 61 5659 9038 4949 -812 -1474 2398 C ATOM 450 CG GLN A 61 16.981 15.418 36.334 1.00 52.74 C ANISOU 450 CG GLN A 61 5616 9344 5079 -809 -1518 2406 C ATOM 451 CD GLN A 61 18.197 15.609 37.243 1.00 56.73 C ANISOU 451 CD GLN A 61 5913 10252 5388 -992 -1700 2685 C ATOM 452 OE1 GLN A 61 19.338 15.531 36.785 1.00 58.79 O ANISOU 452 OE1 GLN A 61 5948 10665 5725 -872 -1760 2861 O ATOM 453 NE2 GLN A 61 17.957 15.876 38.527 1.00 57.42 N ANISOU 453 NE2 GLN A 61 6071 10534 5213 -1298 -1785 2728 N ATOM 454 N GLN A 62 14.146 13.869 34.327 1.00 46.94 N ANISOU 454 N GLN A 62 5292 7687 4855 -303 -1143 1972 N ATOM 455 CA GLN A 62 14.027 13.736 32.868 1.00 45.38 C ANISOU 455 CA GLN A 62 5114 7260 4868 -78 -1028 1824 C ATOM 456 C GLN A 62 12.850 14.508 32.302 1.00 42.74 C ANISOU 456 C GLN A 62 4951 6758 4529 -159 -923 1504 C ATOM 457 O GLN A 62 12.975 15.177 31.283 1.00 41.47 O ANISOU 457 O GLN A 62 4781 6548 4426 -112 -870 1350 O ATOM 458 CB GLN A 62 13.873 12.274 32.466 1.00 46.26 C ANISOU 458 CB GLN A 62 5246 7143 5188 178 -967 1946 C ATOM 459 CG GLN A 62 15.164 11.514 32.334 1.00 49.35 C ANISOU 459 CG GLN A 62 5442 7611 5698 388 -1008 2226 C ATOM 460 CD GLN A 62 14.923 10.025 32.268 1.00 51.46 C ANISOU 460 CD GLN A 62 5766 7636 6149 608 -943 2371 C ATOM 461 OE1 GLN A 62 14.636 9.386 33.278 1.00 53.44 O ANISOU 461 OE1 GLN A 62 6055 7898 6350 554 -1000 2543 O ATOM 462 NE2 GLN A 62 15.032 9.464 31.075 1.00 51.48 N ANISOU 462 NE2 GLN A 62 5790 7411 6359 845 -813 2298 N ATOM 463 N TRP A 63 11.699 14.390 32.956 1.00 42.17 N ANISOU 463 N TRP A 63 5025 6603 4393 -274 -890 1422 N ATOM 464 CA TRP A 63 10.510 15.120 32.541 1.00 40.03 C ANISOU 464 CA TRP A 63 4895 6193 4120 -348 -789 1147 C ATOM 465 C TRP A 63 10.677 16.630 32.745 1.00 39.59 C ANISOU 465 C TRP A 63 4846 6279 3916 -544 -794 1002 C ATOM 466 O TRP A 63 10.347 17.412 31.861 1.00 37.88 O ANISOU 466 O TRP A 63 4669 5967 3757 -521 -724 816 O ATOM 467 CB TRP A 63 9.277 14.600 33.285 1.00 40.02 C ANISOU 467 CB TRP A 63 5025 6098 4083 -429 -746 1116 C ATOM 468 CG TRP A 63 8.039 15.355 32.957 1.00 38.27 C ANISOU 468 CG TRP A 63 4917 5761 3862 -501 -641 861 C ATOM 469 CD1 TRP A 63 7.364 16.224 33.770 1.00 38.18 C ANISOU 469 CD1 TRP A 63 4982 5820 3706 -701 -601 736 C ATOM 470 CD2 TRP A 63 7.330 15.331 31.721 1.00 36.15 C ANISOU 470 CD2 TRP A 63 4690 5298 3749 -373 -556 709 C ATOM 471 NE1 TRP A 63 6.271 16.733 33.117 1.00 36.65 N ANISOU 471 NE1 TRP A 63 4858 5478 3589 -678 -493 531 N ATOM 472 CE2 TRP A 63 6.228 16.200 31.853 1.00 35.97 C ANISOU 472 CE2 TRP A 63 4746 5242 3679 -487 -477 520 C ATOM 473 CE3 TRP A 63 7.510 14.650 30.516 1.00 35.62 C ANISOU 473 CE3 TRP A 63 4602 5085 3847 -180 -532 715 C ATOM 474 CZ2 TRP A 63 5.321 16.417 30.817 1.00 34.50 C ANISOU 474 CZ2 TRP A 63 4595 4905 3610 -411 -397 367 C ATOM 475 CZ3 TRP A 63 6.605 14.859 29.492 1.00 34.97 C ANISOU 475 CZ3 TRP A 63 4576 4856 3855 -135 -453 543 C ATOM 476 CH2 TRP A 63 5.524 15.733 29.650 1.00 34.29 C ANISOU 476 CH2 TRP A 63 4545 4763 3722 -248 -398 385 C ATOM 477 N GLU A 64 11.201 17.032 33.904 1.00 41.23 N ANISOU 477 N GLU A 64 5024 6714 3928 -748 -876 1095 N ATOM 478 CA GLU A 64 11.390 18.448 34.196 1.00 41.53 C ANISOU 478 CA GLU A 64 5097 6877 3807 -968 -870 952 C ATOM 479 C GLU A 64 12.161 19.069 33.048 1.00 41.18 C ANISOU 479 C GLU A 64 4969 6829 3850 -877 -868 902 C ATOM 480 O GLU A 64 11.792 20.136 32.556 1.00 40.47 O ANISOU 480 O GLU A 64 4958 6660 3759 -937 -792 700 O ATOM 481 CB GLU A 64 12.114 18.664 35.527 1.00 43.33 C ANISOU 481 CB GLU A 64 5282 7388 3795 -1214 -980 1094 C ATOM 482 N LYS A 65 13.198 18.365 32.599 1.00 42.37 N ANISOU 482 N LYS A 65 4959 7053 4088 -717 -941 1094 N ATOM 483 CA LYS A 65 14.065 18.827 31.518 1.00 42.58 C ANISOU 483 CA LYS A 65 4880 7107 4193 -626 -942 1078 C ATOM 484 C LYS A 65 13.350 18.833 30.167 1.00 40.24 C ANISOU 484 C LYS A 65 4658 6556 4076 -448 -827 902 C ATOM 485 O LYS A 65 13.585 19.704 29.325 1.00 39.28 O ANISOU 485 O LYS A 65 4532 6419 3974 -458 -794 786 O ATOM 486 CB LYS A 65 15.347 17.986 31.451 1.00 44.53 C ANISOU 486 CB LYS A 65 4916 7507 4496 -484 -1031 1346 C ATOM 487 CG LYS A 65 16.397 18.527 30.466 1.00 46.54 C ANISOU 487 CG LYS A 65 5032 7851 4799 -424 -1035 1348 C ATOM 488 CD LYS A 65 17.703 17.695 30.468 1.00 50.91 C ANISOU 488 CD LYS A 65 5345 8582 5417 -271 -1112 1635 C ATOM 489 CE LYS A 65 18.745 18.235 29.465 1.00 51.19 C ANISOU 489 CE LYS A 65 5229 8722 5498 -215 -1101 1633 C ATOM 490 NZ LYS A 65 18.176 18.560 28.110 1.00 48.04 N ANISOU 490 NZ LYS A 65 4945 8085 5223 -105 -970 1398 N ATOM 491 N LEU A 66 12.472 17.863 29.973 1.00 39.54 N ANISOU 491 N LEU A 66 4643 6277 4105 -309 -771 890 N ATOM 492 CA LEU A 66 11.758 17.753 28.715 1.00 38.04 C ANISOU 492 CA LEU A 66 4520 5867 4065 -164 -674 740 C ATOM 493 C LEU A 66 10.667 18.816 28.613 1.00 36.76 C ANISOU 493 C LEU A 66 4486 5617 3863 -285 -608 525 C ATOM 494 O LEU A 66 10.464 19.391 27.540 1.00 35.79 O ANISOU 494 O LEU A 66 4382 5407 3810 -235 -557 403 O ATOM 495 CB LEU A 66 11.186 16.340 28.525 1.00 38.02 C ANISOU 495 CB LEU A 66 4561 5691 4192 -1 -634 797 C ATOM 496 CG LEU A 66 10.467 16.049 27.204 1.00 36.68 C ANISOU 496 CG LEU A 66 4464 5311 4162 127 -540 654 C ATOM 497 CD1 LEU A 66 11.397 16.272 26.020 1.00 36.09 C ANISOU 497 CD1 LEU A 66 4300 5256 4155 240 -522 643 C ATOM 498 CD2 LEU A 66 9.897 14.638 27.188 1.00 36.49 C ANISOU 498 CD2 LEU A 66 4507 5117 4239 238 -499 708 C ATOM 499 N GLN A 67 9.981 19.077 29.725 1.00 36.87 N ANISOU 499 N GLN A 67 4583 5658 3768 -440 -601 488 N ATOM 500 CA GLN A 67 8.945 20.097 29.761 1.00 36.10 C ANISOU 500 CA GLN A 67 4598 5475 3642 -542 -515 296 C ATOM 501 C GLN A 67 9.527 21.475 29.509 1.00 36.30 C ANISOU 501 C GLN A 67 4624 5566 3604 -649 -509 210 C ATOM 502 O GLN A 67 8.950 22.259 28.764 1.00 35.49 O ANISOU 502 O GLN A 67 4575 5342 3568 -624 -436 73 O ATOM 503 CB GLN A 67 8.205 20.084 31.094 1.00 37.00 C ANISOU 503 CB GLN A 67 4797 5623 3638 -696 -490 276 C ATOM 504 CG GLN A 67 7.277 21.282 31.301 1.00 36.62 C ANISOU 504 CG GLN A 67 4858 5504 3551 -810 -379 80 C ATOM 505 CD GLN A 67 6.307 21.088 32.444 1.00 36.99 C ANISOU 505 CD GLN A 67 4990 5550 3513 -923 -318 41 C ATOM 506 OE1 GLN A 67 5.107 20.933 32.228 1.00 38.00 O ANISOU 506 OE1 GLN A 67 5160 5548 3731 -860 -230 -41 O ATOM 507 NE2 GLN A 67 6.818 21.083 33.662 1.00 37.43 N ANISOU 507 NE2 GLN A 67 5063 5771 3387 -1103 -364 109 N ATOM 508 N HIS A 68 10.670 21.758 30.128 1.00 37.92 N ANISOU 508 N HIS A 68 4764 5966 3678 -775 -590 305 N ATOM 509 CA HIS A 68 11.318 23.064 30.005 1.00 38.85 C ANISOU 509 CA HIS A 68 4891 6161 3708 -922 -589 231 C ATOM 510 C HIS A 68 11.750 23.350 28.562 1.00 38.15 C ANISOU 510 C HIS A 68 4742 6010 3745 -785 -579 208 C ATOM 511 O HIS A 68 11.755 24.494 28.108 1.00 37.77 O ANISOU 511 O HIS A 68 4749 5915 3686 -859 -533 95 O ATOM 512 CB HIS A 68 12.506 23.161 30.971 1.00 40.80 C ANISOU 512 CB HIS A 68 5059 6670 3774 -1107 -697 365 C ATOM 513 CG HIS A 68 13.278 24.440 30.859 1.00 41.87 C ANISOU 513 CG HIS A 68 5203 6903 3804 -1289 -704 299 C ATOM 514 ND1 HIS A 68 14.609 24.475 30.498 1.00 42.92 N ANISOU 514 ND1 HIS A 68 5179 7222 3907 -1303 -799 431 N ATOM 515 CD2 HIS A 68 12.903 25.728 31.041 1.00 42.24 C ANISOU 515 CD2 HIS A 68 5401 6876 3774 -1468 -616 117 C ATOM 516 CE1 HIS A 68 15.021 25.729 30.467 1.00 43.37 C ANISOU 516 CE1 HIS A 68 5293 7325 3860 -1504 -781 331 C ATOM 517 NE2 HIS A 68 14.006 26.510 30.789 1.00 43.30 N ANISOU 517 NE2 HIS A 68 5482 7145 3825 -1604 -666 138 N ATOM 518 N MET A 69 12.097 22.290 27.845 1.00 38.21 N ANISOU 518 N MET A 69 4644 6005 3868 -588 -611 316 N ATOM 519 CA MET A 69 12.451 22.376 26.439 1.00 37.43 C ANISOU 519 CA MET A 69 4490 5848 3882 -451 -590 294 C ATOM 520 C MET A 69 11.247 22.818 25.601 1.00 35.50 C ANISOU 520 C MET A 69 4358 5399 3733 -395 -501 136 C ATOM 521 O MET A 69 11.387 23.604 24.657 1.00 35.34 O ANISOU 521 O MET A 69 4342 5342 3743 -390 -476 71 O ATOM 522 CB MET A 69 12.954 21.017 25.983 1.00 38.10 C ANISOU 522 CB MET A 69 4466 5939 4070 -252 -613 429 C ATOM 523 CG MET A 69 13.493 20.989 24.593 1.00 39.96 C ANISOU 523 CG MET A 69 4635 6147 4400 -121 -582 415 C ATOM 524 SD MET A 69 12.613 19.712 23.681 1.00 44.37 S ANISOU 524 SD MET A 69 5252 6487 5118 89 -505 375 S ATOM 525 CE MET A 69 11.198 20.625 23.064 1.00 41.60 C ANISOU 525 CE MET A 69 5044 5982 4782 24 -449 182 C ATOM 526 N PHE A 70 10.066 22.307 25.944 1.00 34.30 N ANISOU 526 N PHE A 70 4283 5127 3622 -359 -459 91 N ATOM 527 CA PHE A 70 8.833 22.724 25.291 1.00 32.23 C ANISOU 527 CA PHE A 70 4102 4701 3443 -317 -383 -33 C ATOM 528 C PHE A 70 8.439 24.099 25.752 1.00 32.01 C ANISOU 528 C PHE A 70 4160 4646 3358 -455 -328 -139 C ATOM 529 O PHE A 70 8.074 24.948 24.936 1.00 31.86 O ANISOU 529 O PHE A 70 4172 4535 3399 -433 -281 -211 O ATOM 530 CB PHE A 70 7.709 21.731 25.546 1.00 31.82 C ANISOU 530 CB PHE A 70 4089 4553 3449 -251 -354 -37 C ATOM 531 CG PHE A 70 7.823 20.500 24.725 1.00 31.35 C ANISOU 531 CG PHE A 70 3988 4445 3480 -104 -370 20 C ATOM 532 CD1 PHE A 70 7.581 20.540 23.362 1.00 30.85 C ANISOU 532 CD1 PHE A 70 3919 4304 3498 -19 -346 -32 C ATOM 533 CD2 PHE A 70 8.213 19.309 25.297 1.00 32.66 C ANISOU 533 CD2 PHE A 70 4127 4638 3644 -58 -403 133 C ATOM 534 CE1 PHE A 70 7.711 19.412 22.583 1.00 30.72 C ANISOU 534 CE1 PHE A 70 3889 4233 3551 94 -340 -2 C ATOM 535 CE2 PHE A 70 8.344 18.168 24.527 1.00 33.28 C ANISOU 535 CE2 PHE A 70 4191 4638 3817 80 -391 175 C ATOM 536 CZ PHE A 70 8.087 18.222 23.166 1.00 32.31 C ANISOU 536 CZ PHE A 70 4080 4432 3764 149 -352 93 C ATOM 537 N GLN A 71 8.537 24.326 27.056 1.00 32.03 N ANISOU 537 N GLN A 71 4206 4724 3239 -603 -326 -142 N ATOM 538 CA GLN A 71 8.278 25.640 27.608 1.00 32.06 C ANISOU 538 CA GLN A 71 4316 4694 3173 -757 -249 -258 C ATOM 539 C GLN A 71 9.033 26.716 26.844 1.00 31.81 C ANISOU 539 C GLN A 71 4286 4662 3140 -801 -251 -286 C ATOM 540 O GLN A 71 8.461 27.745 26.524 1.00 32.12 O ANISOU 540 O GLN A 71 4411 4565 3227 -816 -162 -387 O ATOM 541 CB GLN A 71 8.633 25.692 29.086 1.00 33.38 C ANISOU 541 CB GLN A 71 4526 4991 3164 -953 -263 -248 C ATOM 542 CG GLN A 71 7.624 25.005 29.969 1.00 33.28 C ANISOU 542 CG GLN A 71 4558 4949 3137 -955 -219 -261 C ATOM 543 CD GLN A 71 7.981 25.060 31.431 1.00 33.97 C ANISOU 543 CD GLN A 71 4695 5186 3025 -1173 -235 -246 C ATOM 544 OE1 GLN A 71 9.135 25.278 31.800 1.00 35.84 O ANISOU 544 OE1 GLN A 71 4895 5592 3130 -1310 -321 -176 O ATOM 545 NE2 GLN A 71 6.988 24.854 32.278 1.00 33.84 N ANISOU 545 NE2 GLN A 71 4756 5130 2973 -1221 -155 -304 N ATOM 546 N VAL A 72 10.303 26.463 26.537 1.00 31.71 N ANISOU 546 N VAL A 72 4171 4798 3081 -815 -346 -186 N ATOM 547 CA VAL A 72 11.130 27.410 25.776 1.00 31.54 C ANISOU 547 CA VAL A 72 4135 4801 3046 -871 -356 -197 C ATOM 548 C VAL A 72 10.653 27.477 24.316 1.00 30.44 C ANISOU 548 C VAL A 72 3981 4527 3057 -701 -326 -217 C ATOM 549 O VAL A 72 10.636 28.555 23.702 1.00 30.60 O ANISOU 549 O VAL A 72 4058 4467 3100 -741 -283 -272 O ATOM 550 CB VAL A 72 12.641 27.038 25.840 1.00 32.11 C ANISOU 550 CB VAL A 72 4068 5104 3030 -926 -466 -64 C ATOM 551 CG1 VAL A 72 13.436 27.825 24.840 1.00 32.01 C ANISOU 551 CG1 VAL A 72 4018 5119 3024 -955 -473 -64 C ATOM 552 CG2 VAL A 72 13.200 27.274 27.225 1.00 33.81 C ANISOU 552 CG2 VAL A 72 4299 5484 3063 -1152 -509 -37 C ATOM 553 N TYR A 73 10.243 26.332 23.773 1.00 29.10 N ANISOU 553 N TYR A 73 3748 4329 2980 -529 -346 -171 N ATOM 554 CA TYR A 73 9.813 26.267 22.379 1.00 27.79 C ANISOU 554 CA TYR A 73 3564 4068 2928 -393 -328 -184 C ATOM 555 C TYR A 73 8.559 27.120 22.097 1.00 27.17 C ANISOU 555 C TYR A 73 3577 3823 2923 -381 -252 -268 C ATOM 556 O TYR A 73 8.528 27.905 21.147 1.00 26.63 O ANISOU 556 O TYR A 73 3523 3698 2899 -367 -236 -278 O ATOM 557 CB TYR A 73 9.636 24.808 21.941 1.00 27.22 C ANISOU 557 CB TYR A 73 3427 3996 2920 -243 -354 -131 C ATOM 558 CG TYR A 73 8.675 24.618 20.804 1.00 25.84 C ANISOU 558 CG TYR A 73 3270 3705 2842 -140 -324 -170 C ATOM 559 CD1 TYR A 73 9.035 24.928 19.502 1.00 24.30 C ANISOU 559 CD1 TYR A 73 3046 3515 2670 -104 -329 -167 C ATOM 560 CD2 TYR A 73 7.388 24.139 21.041 1.00 25.95 C ANISOU 560 CD2 TYR A 73 3325 3625 2910 -99 -294 -202 C ATOM 561 CE1 TYR A 73 8.135 24.759 18.455 1.00 24.44 C ANISOU 561 CE1 TYR A 73 3078 3454 2753 -38 -315 -192 C ATOM 562 CE2 TYR A 73 6.483 23.961 20.005 1.00 25.37 C ANISOU 562 CE2 TYR A 73 3253 3477 2909 -31 -281 -224 C ATOM 563 CZ TYR A 73 6.863 24.271 18.716 1.00 25.07 C ANISOU 563 CZ TYR A 73 3189 3453 2882 -5 -296 -217 C ATOM 564 OH TYR A 73 5.953 24.097 17.697 1.00 26.17 O ANISOU 564 OH TYR A 73 3328 3545 3069 34 -296 -227 O ATOM 565 N ARG A 74 7.544 26.974 22.940 1.00 27.04 N ANISOU 565 N ARG A 74 3615 3738 2922 -384 -201 -313 N ATOM 566 CA ARG A 74 6.289 27.704 22.759 1.00 26.63 C ANISOU 566 CA ARG A 74 3622 3536 2960 -347 -115 -374 C ATOM 567 C ARG A 74 6.482 29.214 22.637 1.00 27.30 C ANISOU 567 C ARG A 74 3788 3540 3046 -424 -52 -421 C ATOM 568 O ARG A 74 5.867 29.863 21.782 1.00 26.97 O ANISOU 568 O ARG A 74 3755 3389 3105 -351 -16 -415 O ATOM 569 CB ARG A 74 5.319 27.407 23.893 1.00 26.58 C ANISOU 569 CB ARG A 74 3659 3492 2950 -364 -50 -421 C ATOM 570 CG ARG A 74 3.915 27.746 23.527 1.00 25.45 C ANISOU 570 CG ARG A 74 3518 3221 2930 -272 28 -449 C ATOM 571 CD ARG A 74 2.981 27.267 24.561 1.00 25.92 C ANISOU 571 CD ARG A 74 3594 3269 2984 -282 91 -486 C ATOM 572 NE ARG A 74 3.189 27.963 25.815 1.00 27.52 N ANISOU 572 NE ARG A 74 3898 3463 3095 -416 177 -567 N ATOM 573 CZ ARG A 74 2.325 27.940 26.819 1.00 29.62 C ANISOU 573 CZ ARG A 74 4206 3700 3349 -450 278 -628 C ATOM 574 NH1 ARG A 74 1.193 27.236 26.715 1.00 30.89 N ANISOU 574 NH1 ARG A 74 4301 3845 3592 -355 298 -605 N ATOM 575 NH2 ARG A 74 2.593 28.614 27.923 1.00 29.83 N ANISOU 575 NH2 ARG A 74 4343 3723 3268 -598 365 -717 N ATOM 576 N VAL A 75 7.333 29.762 23.496 1.00 28.02 N ANISOU 576 N VAL A 75 3940 3686 3021 -584 -42 -456 N ATOM 577 CA VAL A 75 7.651 31.179 23.444 1.00 29.05 C ANISOU 577 CA VAL A 75 4172 3729 3136 -692 23 -509 C ATOM 578 C VAL A 75 8.359 31.498 22.128 1.00 28.58 C ANISOU 578 C VAL A 75 4060 3694 3106 -661 -38 -442 C ATOM 579 O VAL A 75 8.058 32.493 21.468 1.00 28.51 O ANISOU 579 O VAL A 75 4110 3551 3171 -644 15 -448 O ATOM 580 CB VAL A 75 8.490 31.609 24.680 1.00 30.33 C ANISOU 580 CB VAL A 75 4416 3976 3131 -917 37 -566 C ATOM 581 CG1 VAL A 75 9.279 32.886 24.414 1.00 31.40 C ANISOU 581 CG1 VAL A 75 4640 4073 3219 -1067 65 -598 C ATOM 582 CG2 VAL A 75 7.588 31.783 25.875 1.00 30.72 C ANISOU 582 CG2 VAL A 75 4572 3941 3160 -971 153 -667 C ATOM 583 N SER A 76 9.286 30.627 21.751 1.00 28.37 N ANISOU 583 N SER A 76 3920 3835 3024 -646 -144 -368 N ATOM 584 CA SER A 76 10.107 30.858 20.582 1.00 28.58 C ANISOU 584 CA SER A 76 3888 3920 3051 -639 -195 -310 C ATOM 585 C SER A 76 9.260 30.742 19.341 1.00 28.10 C ANISOU 585 C SER A 76 3801 3767 3110 -486 -191 -280 C ATOM 586 O SER A 76 9.232 31.654 18.492 1.00 28.83 O ANISOU 586 O SER A 76 3928 3785 3240 -495 -173 -261 O ATOM 587 CB SER A 76 11.233 29.856 20.536 1.00 28.17 C ANISOU 587 CB SER A 76 3706 4069 2927 -634 -284 -238 C ATOM 588 OG SER A 76 12.045 30.003 21.671 1.00 30.21 O ANISOU 588 OG SER A 76 3967 4448 3062 -793 -308 -237 O ATOM 589 N PHE A 77 8.542 29.626 19.251 1.00 27.33 N ANISOU 589 N PHE A 77 3647 3675 3062 -363 -210 -268 N ATOM 590 CA PHE A 77 7.646 29.387 18.129 1.00 26.62 C ANISOU 590 CA PHE A 77 3526 3526 3064 -244 -217 -238 C ATOM 591 C PHE A 77 6.809 30.620 17.845 1.00 26.92 C ANISOU 591 C PHE A 77 3629 3416 3184 -235 -157 -236 C ATOM 592 O PHE A 77 6.663 31.034 16.698 1.00 26.95 O ANISOU 592 O PHE A 77 3613 3398 3227 -200 -178 -177 O ATOM 593 CB PHE A 77 6.724 28.213 18.414 1.00 25.84 C ANISOU 593 CB PHE A 77 3393 3421 3005 -155 -222 -246 C ATOM 594 CG PHE A 77 5.650 28.055 17.405 1.00 25.97 C ANISOU 594 CG PHE A 77 3378 3389 3100 -70 -230 -216 C ATOM 595 CD1 PHE A 77 4.362 28.524 17.665 1.00 25.93 C ANISOU 595 CD1 PHE A 77 3387 3283 3181 -29 -179 -217 C ATOM 596 CD2 PHE A 77 5.922 27.457 16.169 1.00 26.50 C ANISOU 596 CD2 PHE A 77 3396 3524 3149 -38 -283 -182 C ATOM 597 CE1 PHE A 77 3.352 28.388 16.714 1.00 25.77 C ANISOU 597 CE1 PHE A 77 3311 3252 3227 37 -203 -162 C ATOM 598 CE2 PHE A 77 4.910 27.312 15.203 1.00 25.57 C ANISOU 598 CE2 PHE A 77 3248 3390 3077 5 -305 -146 C ATOM 599 CZ PHE A 77 3.626 27.782 15.480 1.00 25.17 C ANISOU 599 CZ PHE A 77 3191 3261 3112 41 -275 -125 C ATOM 600 N THR A 78 6.278 31.204 18.915 1.00 27.39 N ANISOU 600 N THR A 78 3766 3372 3268 -268 -73 -294 N ATOM 601 CA THR A 78 5.335 32.298 18.802 1.00 27.76 C ANISOU 601 CA THR A 78 3874 3248 3426 -224 15 -291 C ATOM 602 C THR A 78 6.031 33.481 18.187 1.00 28.63 C ANISOU 602 C THR A 78 4049 3299 3531 -293 27 -261 C ATOM 603 O THR A 78 5.505 34.084 17.252 1.00 29.55 O ANISOU 603 O THR A 78 4156 3331 3741 -220 33 -183 O ATOM 604 CB THR A 78 4.693 32.642 20.160 1.00 28.23 C ANISOU 604 CB THR A 78 4017 3204 3505 -250 135 -381 C ATOM 605 OG1 THR A 78 4.009 31.483 20.656 1.00 27.30 O ANISOU 605 OG1 THR A 78 3831 3154 3389 -190 118 -393 O ATOM 606 CG2 THR A 78 3.701 33.770 20.024 1.00 28.60 C ANISOU 606 CG2 THR A 78 4119 3054 3695 -172 255 -372 C ATOM 607 N ARG A 79 7.232 33.778 18.674 1.00 28.86 N ANISOU 607 N ARG A 79 4132 3388 3444 -445 19 -306 N ATOM 608 CA ARG A 79 7.973 34.929 18.189 1.00 29.62 C ANISOU 608 CA ARG A 79 4305 3430 3519 -549 36 -286 C ATOM 609 C ARG A 79 8.450 34.678 16.778 1.00 29.17 C ANISOU 609 C ARG A 79 4154 3478 3451 -512 -60 -186 C ATOM 610 O ARG A 79 8.466 35.596 15.958 1.00 29.64 O ANISOU 610 O ARG A 79 4257 3452 3553 -523 -47 -123 O ATOM 611 CB ARG A 79 9.156 35.220 19.094 1.00 30.26 C ANISOU 611 CB ARG A 79 4450 3591 3456 -753 40 -355 C ATOM 612 CG ARG A 79 9.308 36.684 19.420 1.00 32.53 C ANISOU 612 CG ARG A 79 4912 3704 3745 -890 148 -409 C ATOM 613 CD ARG A 79 10.534 37.298 18.795 1.00 33.94 C ANISOU 613 CD ARG A 79 5104 3956 3837 -1043 98 -366 C ATOM 614 NE ARG A 79 11.736 37.131 19.620 1.00 35.09 N ANISOU 614 NE ARG A 79 5241 4285 3807 -1252 53 -413 N ATOM 615 CZ ARG A 79 12.802 36.422 19.256 1.00 34.88 C ANISOU 615 CZ ARG A 79 5064 4505 3684 -1290 -62 -346 C ATOM 616 NH1 ARG A 79 12.824 35.796 18.071 1.00 34.13 N ANISOU 616 NH1 ARG A 79 4838 4486 3642 -1140 -130 -256 N ATOM 617 NH2 ARG A 79 13.843 36.342 20.073 1.00 33.12 N ANISOU 617 NH2 ARG A 79 4818 4460 3307 -1483 -105 -366 N ATOM 618 N ASP A 80 8.823 33.430 16.491 1.00 28.15 N ANISOU 618 N ASP A 80 3907 3524 3266 -468 -145 -169 N ATOM 619 CA ASP A 80 9.352 33.086 15.178 1.00 28.15 C ANISOU 619 CA ASP A 80 3823 3638 3235 -446 -217 -98 C ATOM 620 C ASP A 80 8.318 33.297 14.080 1.00 28.02 C ANISOU 620 C ASP A 80 3793 3545 3309 -344 -227 -21 C ATOM 621 O ASP A 80 8.573 33.983 13.094 1.00 28.89 O ANISOU 621 O ASP A 80 3914 3650 3414 -377 -245 51 O ATOM 622 CB ASP A 80 9.923 31.674 15.175 1.00 27.66 C ANISOU 622 CB ASP A 80 3653 3748 3109 -407 -272 -109 C ATOM 623 CG ASP A 80 11.323 31.607 15.795 1.00 30.24 C ANISOU 623 CG ASP A 80 3947 4212 3329 -521 -290 -123 C ATOM 624 OD1 ASP A 80 11.753 32.613 16.418 1.00 33.77 O ANISOU 624 OD1 ASP A 80 4470 4625 3735 -658 -262 -145 O ATOM 625 OD2 ASP A 80 12.005 30.558 15.650 1.00 30.78 O ANISOU 625 OD2 ASP A 80 3913 4426 3356 -479 -327 -106 O ATOM 626 N ILE A 81 7.132 32.745 14.272 1.00 27.60 N ANISOU 626 N ILE A 81 3710 3445 3333 -234 -220 -23 N ATOM 627 CA ILE A 81 6.062 32.939 13.313 1.00 27.79 C ANISOU 627 CA ILE A 81 3697 3422 3440 -146 -241 69 C ATOM 628 C ILE A 81 5.854 34.425 13.078 1.00 29.35 C ANISOU 628 C ILE A 81 3970 3466 3716 -157 -190 141 C ATOM 629 O ILE A 81 5.861 34.885 11.927 1.00 29.74 O ANISOU 629 O ILE A 81 4001 3531 3768 -160 -235 251 O ATOM 630 CB ILE A 81 4.760 32.241 13.762 1.00 27.32 C ANISOU 630 CB ILE A 81 3587 3335 3457 -44 -228 58 C ATOM 631 CG1 ILE A 81 4.961 30.721 13.769 1.00 25.83 C ANISOU 631 CG1 ILE A 81 3339 3283 3193 -40 -281 4 C ATOM 632 CG2 ILE A 81 3.592 32.617 12.859 1.00 27.17 C ANISOU 632 CG2 ILE A 81 3511 3281 3532 37 -252 182 C ATOM 633 CD1 ILE A 81 5.621 30.159 12.511 1.00 24.67 C ANISOU 633 CD1 ILE A 81 3149 3266 2957 -71 -351 33 C ATOM 634 N GLN A 82 5.716 35.167 14.179 1.00 30.29 N ANISOU 634 N GLN A 82 4185 3432 3890 -173 -88 78 N ATOM 635 CA GLN A 82 5.488 36.615 14.133 1.00 32.09 C ANISOU 635 CA GLN A 82 4518 3460 4215 -176 -2 129 C ATOM 636 C GLN A 82 6.510 37.319 13.258 1.00 32.60 C ANISOU 636 C GLN A 82 4627 3547 4212 -287 -42 193 C ATOM 637 O GLN A 82 6.157 38.223 12.508 1.00 34.13 O ANISOU 637 O GLN A 82 4852 3628 4488 -253 -29 314 O ATOM 638 CB GLN A 82 5.489 37.217 15.536 1.00 32.74 C ANISOU 638 CB GLN A 82 4732 3387 4322 -228 132 4 C ATOM 639 CG GLN A 82 4.135 37.193 16.209 1.00 34.70 C ANISOU 639 CG GLN A 82 4967 3511 4705 -89 230 -14 C ATOM 640 CD GLN A 82 4.203 37.470 17.707 1.00 37.33 C ANISOU 640 CD GLN A 82 5426 3742 5014 -166 364 -173 C ATOM 641 OE1 GLN A 82 5.232 37.913 18.238 1.00 37.87 O ANISOU 641 OE1 GLN A 82 5613 3804 4973 -339 391 -261 O ATOM 642 NE2 GLN A 82 3.094 37.205 18.401 1.00 38.37 N ANISOU 642 NE2 GLN A 82 5530 3814 5236 -57 450 -210 N ATOM 643 N GLU A 83 7.764 36.878 13.341 1.00 31.77 N ANISOU 643 N GLU A 83 4512 3599 3960 -417 -91 128 N ATOM 644 CA GLU A 83 8.845 37.472 12.564 1.00 32.13 C ANISOU 644 CA GLU A 83 4585 3701 3921 -545 -125 180 C ATOM 645 C GLU A 83 8.840 36.954 11.132 1.00 31.96 C ANISOU 645 C GLU A 83 4455 3826 3861 -503 -223 287 C ATOM 646 O GLU A 83 9.033 37.726 10.172 1.00 32.92 O ANISOU 646 O GLU A 83 4604 3925 3978 -549 -242 396 O ATOM 647 CB GLU A 83 10.205 37.233 13.233 1.00 31.86 C ANISOU 647 CB GLU A 83 4557 3803 3746 -705 -134 84 C ATOM 648 CG GLU A 83 10.400 37.997 14.550 1.00 31.16 C ANISOU 648 CG GLU A 83 4607 3582 3652 -822 -39 -17 C ATOM 649 CD GLU A 83 10.482 39.500 14.355 1.00 31.81 C ANISOU 649 CD GLU A 83 4849 3459 3779 -919 39 15 C ATOM 650 OE1 GLU A 83 9.959 40.238 15.204 1.00 31.80 O ANISOU 650 OE1 GLU A 83 4989 3244 3850 -932 157 -51 O ATOM 651 OE2 GLU A 83 11.070 39.951 13.350 1.00 32.48 O ANISOU 651 OE2 GLU A 83 4928 3585 3827 -986 -3 107 O ATOM 652 N LEU A 84 8.602 35.654 10.976 1.00 30.58 N ANISOU 652 N LEU A 84 4170 3797 3651 -429 -278 255 N ATOM 653 CA LEU A 84 8.478 35.098 9.629 1.00 30.29 C ANISOU 653 CA LEU A 84 4048 3896 3563 -405 -356 335 C ATOM 654 C LEU A 84 7.404 35.816 8.793 1.00 30.90 C ANISOU 654 C LEU A 84 4128 3882 3730 -343 -380 486 C ATOM 655 O LEU A 84 7.553 35.926 7.582 1.00 31.45 O ANISOU 655 O LEU A 84 4168 4045 3736 -387 -440 586 O ATOM 656 CB LEU A 84 8.282 33.584 9.665 1.00 29.08 C ANISOU 656 CB LEU A 84 3807 3874 3368 -341 -390 263 C ATOM 657 CG LEU A 84 9.516 32.790 10.137 1.00 28.99 C ANISOU 657 CG LEU A 84 3763 3990 3261 -390 -380 162 C ATOM 658 CD1 LEU A 84 9.143 31.351 10.479 1.00 27.99 C ANISOU 658 CD1 LEU A 84 3580 3920 3135 -304 -387 91 C ATOM 659 CD2 LEU A 84 10.671 32.817 9.124 1.00 29.29 C ANISOU 659 CD2 LEU A 84 3767 4176 3187 -478 -397 188 C ATOM 660 N VAL A 85 6.359 36.328 9.447 1.00 31.03 N ANISOU 660 N VAL A 85 4174 3725 3892 -244 -326 513 N ATOM 661 CA VAL A 85 5.348 37.152 8.785 1.00 32.22 C ANISOU 661 CA VAL A 85 4313 3770 4160 -163 -336 687 C ATOM 662 C VAL A 85 5.911 38.508 8.323 1.00 34.20 C ANISOU 662 C VAL A 85 4667 3901 4428 -237 -308 788 C ATOM 663 O VAL A 85 5.717 38.922 7.178 1.00 35.01 O ANISOU 663 O VAL A 85 4739 4039 4524 -244 -373 957 O ATOM 664 CB VAL A 85 4.144 37.383 9.694 1.00 32.52 C ANISOU 664 CB VAL A 85 4348 3643 4367 -22 -256 686 C ATOM 665 CG1 VAL A 85 3.186 38.385 9.074 1.00 33.30 C ANISOU 665 CG1 VAL A 85 4426 3612 4614 82 -247 892 C ATOM 666 CG2 VAL A 85 3.436 36.070 9.977 1.00 31.03 C ANISOU 666 CG2 VAL A 85 4048 3581 4162 41 -296 623 C ATOM 667 N LYS A 86 6.618 39.186 9.219 1.00 35.01 N ANISOU 667 N LYS A 86 4897 3867 4540 -314 -212 688 N ATOM 668 CA LYS A 86 7.317 40.423 8.889 1.00 36.85 C ANISOU 668 CA LYS A 86 5252 3981 4769 -425 -175 755 C ATOM 669 C LYS A 86 8.298 40.243 7.737 1.00 37.62 C ANISOU 669 C LYS A 86 5306 4282 4705 -557 -270 814 C ATOM 670 O LYS A 86 8.564 41.181 6.985 1.00 39.11 O ANISOU 670 O LYS A 86 5558 4409 4894 -626 -277 945 O ATOM 671 CB LYS A 86 8.087 40.935 10.101 1.00 36.66 C ANISOU 671 CB LYS A 86 5368 3836 4724 -542 -68 598 C ATOM 672 CG LYS A 86 7.286 41.041 11.364 1.00 35.46 C ANISOU 672 CG LYS A 86 5276 3504 4693 -448 47 496 C ATOM 673 CD LYS A 86 8.006 41.906 12.357 1.00 34.68 C ANISOU 673 CD LYS A 86 5360 3248 4569 -604 165 371 C ATOM 674 CE LYS A 86 7.535 41.636 13.752 1.00 33.33 C ANISOU 674 CE LYS A 86 5234 2996 4434 -569 266 212 C ATOM 675 NZ LYS A 86 8.180 42.601 14.647 1.00 34.95 N ANISOU 675 NZ LYS A 86 5643 3036 4602 -750 390 92 N ATOM 676 N MET A 87 8.850 39.043 7.623 1.00 37.37 N ANISOU 676 N MET A 87 5174 4484 4540 -592 -330 717 N ATOM 677 CA MET A 87 9.835 38.742 6.598 1.00 38.72 C ANISOU 677 CA MET A 87 5295 4864 4551 -711 -393 743 C ATOM 678 C MET A 87 9.174 38.586 5.238 1.00 40.50 C ANISOU 678 C MET A 87 5453 5184 4753 -676 -478 897 C ATOM 679 O MET A 87 9.675 39.083 4.231 1.00 41.74 O ANISOU 679 O MET A 87 5624 5411 4826 -781 -513 1003 O ATOM 680 CB MET A 87 10.587 37.470 6.968 1.00 37.11 C ANISOU 680 CB MET A 87 5006 4856 4238 -730 -403 590 C ATOM 681 CG MET A 87 11.953 37.336 6.322 1.00 36.78 C ANISOU 681 CG MET A 87 4926 5005 4042 -871 -416 576 C ATOM 682 SD MET A 87 12.880 35.907 6.919 1.00 33.51 S ANISOU 682 SD MET A 87 4401 4790 3541 -857 -402 418 S ATOM 683 CE MET A 87 13.380 36.455 8.543 1.00 31.99 C ANISOU 683 CE MET A 87 4273 4495 3387 -921 -351 335 C ATOM 684 N MET A 88 8.039 37.902 5.213 1.00 41.61 N ANISOU 684 N MET A 88 5516 5340 4953 -548 -515 916 N ATOM 685 CA MET A 88 7.320 37.688 3.966 1.00 43.90 C ANISOU 685 CA MET A 88 5730 5748 5201 -536 -610 1067 C ATOM 686 C MET A 88 6.500 38.893 3.537 1.00 46.52 C ANISOU 686 C MET A 88 6087 5930 5658 -483 -628 1293 C ATOM 687 O MET A 88 6.522 39.259 2.362 1.00 47.71 O ANISOU 687 O MET A 88 6221 6172 5733 -555 -702 1457 O ATOM 688 CB MET A 88 6.469 36.421 4.043 1.00 43.05 C ANISOU 688 CB MET A 88 5524 5747 5085 -455 -651 1003 C ATOM 689 CG MET A 88 7.321 35.193 4.254 1.00 42.77 C ANISOU 689 CG MET A 88 5469 5855 4925 -503 -629 809 C ATOM 690 SD MET A 88 8.800 35.310 3.209 1.00 47.24 S ANISOU 690 SD MET A 88 6055 6590 5305 -671 -631 804 S ATOM 691 CE MET A 88 10.053 35.146 4.460 1.00 46.16 C ANISOU 691 CE MET A 88 5945 6421 5174 -685 -541 630 C ATOM 692 N SER A 89 5.793 39.500 4.495 1.00 48.12 N ANISOU 692 N SER A 89 6330 5902 6050 -355 -552 1304 N ATOM 693 CA SER A 89 4.959 40.693 4.266 1.00 51.06 C ANISOU 693 CA SER A 89 6728 6080 6592 -258 -535 1523 C ATOM 694 C SER A 89 5.481 41.629 3.155 1.00 53.30 C ANISOU 694 C SER A 89 7067 6365 6818 -368 -581 1712 C ATOM 695 O SER A 89 6.667 41.988 3.149 1.00 52.96 O ANISOU 695 O SER A 89 7126 6318 6678 -516 -546 1636 O ATOM 696 CB SER A 89 4.742 41.463 5.578 1.00 51.55 C ANISOU 696 CB SER A 89 6901 5845 6839 -163 -383 1444 C ATOM 697 OG SER A 89 4.870 42.864 5.384 1.00 53.77 O ANISOU 697 OG SER A 89 7307 5898 7224 -171 -318 1586 O ATOM 698 N PRO A 90 4.582 42.042 2.228 1.00 55.75 N ANISOU 698 N PRO A 90 7302 6694 7186 -302 -664 1976 N ATOM 699 CA PRO A 90 3.128 41.794 2.273 1.00 56.91 C ANISOU 699 CA PRO A 90 7309 6842 7471 -124 -703 2104 C ATOM 700 C PRO A 90 2.656 40.500 1.582 1.00 56.70 C ANISOU 700 C PRO A 90 7125 7131 7289 -169 -840 2099 C ATOM 701 O PRO A 90 1.556 40.469 1.014 1.00 58.19 O ANISOU 701 O PRO A 90 7178 7407 7526 -97 -932 2307 O ATOM 702 CB PRO A 90 2.553 43.022 1.562 1.00 59.43 C ANISOU 702 CB PRO A 90 7627 7029 7924 -50 -728 2427 C ATOM 703 CG PRO A 90 3.609 43.406 0.571 1.00 59.76 C ANISOU 703 CG PRO A 90 7750 7167 7788 -250 -789 2496 C ATOM 704 CD PRO A 90 4.947 42.850 1.049 1.00 57.57 C ANISOU 704 CD PRO A 90 7568 6959 7348 -409 -731 2196 C ATOM 705 N LYS A 91 3.467 39.444 1.647 1.00 55.31 N ANISOU 705 N LYS A 91 6964 7121 6931 -291 -847 1868 N ATOM 706 CA LYS A 91 3.107 38.166 1.038 1.00 55.26 C ANISOU 706 CA LYS A 91 6847 7382 6768 -355 -947 1823 C ATOM 707 C LYS A 91 1.889 37.552 1.734 1.00 55.06 C ANISOU 707 C LYS A 91 6715 7341 6863 -216 -947 1801 C ATOM 708 O LYS A 91 0.851 37.326 1.106 1.00 56.21 O ANISOU 708 O LYS A 91 6731 7621 7006 -199 -1050 1968 O ATOM 709 CB LYS A 91 4.297 37.184 1.043 1.00 53.73 C ANISOU 709 CB LYS A 91 6706 7324 6384 -489 -917 1573 C ATOM 710 CG LYS A 91 4.115 35.960 0.128 1.00 53.62 C ANISOU 710 CG LYS A 91 6621 7578 6173 -599 -1004 1529 C ATOM 711 CD LYS A 91 4.297 36.343 -1.329 1.00 55.63 C ANISOU 711 CD LYS A 91 6868 8003 6266 -750 -1097 1705 C ATOM 712 CE LYS A 91 3.310 35.628 -2.228 1.00 56.58 C ANISOU 712 CE LYS A 91 6887 8344 6268 -823 -1220 1801 C ATOM 713 NZ LYS A 91 3.135 36.405 -3.498 1.00 59.04 N ANISOU 713 NZ LYS A 91 7171 8781 6480 -935 -1332 2071 N ATOM 714 N GLU A 92 2.027 37.294 3.032 1.00 53.94 N ANISOU 714 N GLU A 92 6622 7054 6817 -132 -834 1604 N ATOM 715 CA GLU A 92 0.951 36.698 3.819 1.00 53.61 C ANISOU 715 CA GLU A 92 6491 6993 6887 -10 -813 1560 C ATOM 716 C GLU A 92 0.535 37.579 4.990 1.00 53.55 C ANISOU 716 C GLU A 92 6525 6713 7109 153 -680 1561 C ATOM 717 O GLU A 92 1.336 38.336 5.544 1.00 53.50 O ANISOU 717 O GLU A 92 6657 6525 7145 144 -580 1485 O ATOM 718 CB GLU A 92 1.308 35.276 4.288 1.00 51.88 C ANISOU 718 CB GLU A 92 6278 6888 6547 -72 -803 1314 C ATOM 719 CG GLU A 92 1.312 34.237 3.160 1.00 53.40 C ANISOU 719 CG GLU A 92 6415 7338 6535 -213 -915 1310 C ATOM 720 CD GLU A 92 -0.024 34.144 2.406 1.00 57.18 C ANISOU 720 CD GLU A 92 6749 7957 7020 -211 -1032 1516 C ATOM 721 OE1 GLU A 92 -1.088 34.040 3.066 1.00 57.96 O ANISOU 721 OE1 GLU A 92 6755 8008 7258 -95 -1019 1555 O ATOM 722 OE2 GLU A 92 -0.005 34.164 1.150 1.00 58.49 O ANISOU 722 OE2 GLU A 92 6885 8300 7040 -339 -1139 1643 O ATOM 723 N ASP A 93 -0.736 37.446 5.350 1.00 53.63 N ANISOU 723 N ASP A 93 6413 6709 7256 289 -674 1641 N ATOM 724 CA ASP A 93 -1.415 38.340 6.266 1.00 53.84 C ANISOU 724 CA ASP A 93 6447 6488 7520 470 -539 1690 C ATOM 725 C ASP A 93 -2.145 37.548 7.359 1.00 51.69 C ANISOU 725 C ASP A 93 6111 6216 7311 550 -471 1547 C ATOM 726 O ASP A 93 -2.591 36.414 7.144 1.00 50.59 O ANISOU 726 O ASP A 93 5862 6284 7074 499 -564 1514 O ATOM 727 CB ASP A 93 -2.429 39.166 5.457 1.00 56.94 C ANISOU 727 CB ASP A 93 6709 6871 8053 588 -594 2015 C ATOM 728 CG ASP A 93 -2.572 40.604 5.959 1.00 60.09 C ANISOU 728 CG ASP A 93 7198 6946 8688 746 -438 2113 C ATOM 729 OD1 ASP A 93 -3.707 41.138 5.897 1.00 62.58 O ANISOU 729 OD1 ASP A 93 7381 7194 9203 930 -412 2332 O ATOM 730 OD2 ASP A 93 -1.557 41.200 6.399 1.00 61.20 O ANISOU 730 OD2 ASP A 93 7537 6899 8816 683 -335 1978 O ATOM 731 N TYR A 94 -2.260 38.159 8.531 1.00 50.63 N ANISOU 731 N TYR A 94 6061 5844 7333 659 -301 1455 N ATOM 732 CA TYR A 94 -3.140 37.665 9.578 1.00 49.13 C ANISOU 732 CA TYR A 94 5801 5629 7239 760 -212 1363 C ATOM 733 C TYR A 94 -4.593 37.738 9.086 1.00 50.31 C ANISOU 733 C TYR A 94 5728 5861 7525 902 -261 1605 C ATOM 734 O TYR A 94 -4.899 38.539 8.202 1.00 52.55 O ANISOU 734 O TYR A 94 5948 6129 7889 965 -312 1850 O ATOM 735 CB TYR A 94 -2.949 38.499 10.844 1.00 49.50 C ANISOU 735 CB TYR A 94 6000 5390 7417 835 -1 1229 C ATOM 736 CG TYR A 94 -1.535 38.479 11.394 1.00 47.47 C ANISOU 736 CG TYR A 94 5944 5075 7017 675 38 1008 C ATOM 737 CD1 TYR A 94 -0.728 39.611 11.344 1.00 47.57 C ANISOU 737 CD1 TYR A 94 6123 4899 7054 630 110 1013 C ATOM 738 CD2 TYR A 94 -1.003 37.321 11.962 1.00 45.09 C ANISOU 738 CD2 TYR A 94 5660 4915 6558 564 0 812 C ATOM 739 CE1 TYR A 94 0.577 39.590 11.847 1.00 46.23 C ANISOU 739 CE1 TYR A 94 6114 4712 6741 462 135 825 C ATOM 740 CE2 TYR A 94 0.298 37.290 12.467 1.00 43.81 C ANISOU 740 CE2 TYR A 94 5648 4730 6266 421 25 640 C ATOM 741 CZ TYR A 94 1.086 38.426 12.411 1.00 43.84 C ANISOU 741 CZ TYR A 94 5798 4575 6283 363 88 646 C ATOM 742 OH TYR A 94 2.373 38.385 12.921 1.00 41.23 O ANISOU 742 OH TYR A 94 5595 4257 5814 202 103 489 O ATOM 743 N PRO A 95 -5.494 36.890 9.616 1.00 49.03 N ANISOU 743 N PRO A 95 5436 5808 7385 943 -255 1560 N ATOM 744 CA PRO A 95 -5.294 35.819 10.591 1.00 46.43 C ANISOU 744 CA PRO A 95 5157 5526 6959 866 -215 1309 C ATOM 745 C PRO A 95 -4.421 34.685 10.052 1.00 43.75 C ANISOU 745 C PRO A 95 4868 5378 6377 670 -355 1191 C ATOM 746 O PRO A 95 -4.523 34.332 8.880 1.00 44.31 O ANISOU 746 O PRO A 95 4856 5634 6347 590 -506 1314 O ATOM 747 CB PRO A 95 -6.720 35.314 10.853 1.00 47.09 C ANISOU 747 CB PRO A 95 5034 5720 7138 960 -212 1395 C ATOM 748 CG PRO A 95 -7.492 35.742 9.680 1.00 49.37 C ANISOU 748 CG PRO A 95 5139 6128 7492 1019 -329 1692 C ATOM 749 CD PRO A 95 -6.913 37.032 9.254 1.00 50.70 C ANISOU 749 CD PRO A 95 5411 6108 7743 1083 -288 1803 C ATOM 750 N ILE A 96 -3.563 34.136 10.901 1.00 40.98 N ANISOU 750 N ILE A 96 4653 4983 5933 592 -298 959 N ATOM 751 CA ILE A 96 -2.783 32.968 10.534 1.00 38.57 C ANISOU 751 CA ILE A 96 4389 4837 5428 440 -398 840 C ATOM 752 C ILE A 96 -3.128 31.772 11.422 1.00 37.41 C ANISOU 752 C ILE A 96 4225 4746 5244 416 -374 694 C ATOM 753 O ILE A 96 -3.329 31.899 12.634 1.00 37.20 O ANISOU 753 O ILE A 96 4235 4603 5295 476 -255 600 O ATOM 754 CB ILE A 96 -1.260 33.278 10.521 1.00 37.60 C ANISOU 754 CB ILE A 96 4427 4652 5207 352 -381 732 C ATOM 755 CG1 ILE A 96 -0.822 33.675 9.111 1.00 37.76 C ANISOU 755 CG1 ILE A 96 4437 4759 5150 286 -485 867 C ATOM 756 CG2 ILE A 96 -0.422 32.093 11.007 1.00 35.28 C ANISOU 756 CG2 ILE A 96 4198 4434 4773 256 -390 541 C ATOM 757 CD1 ILE A 96 0.355 34.649 9.074 1.00 36.55 C ANISOU 757 CD1 ILE A 96 4418 4488 4980 242 -438 847 C ATOM 758 N GLU A 97 -3.193 30.609 10.788 1.00 36.54 N ANISOU 758 N GLU A 97 4070 4810 5002 314 -482 674 N ATOM 759 CA GLU A 97 -3.480 29.374 11.470 1.00 35.48 C ANISOU 759 CA GLU A 97 3932 4730 4818 270 -471 550 C ATOM 760 C GLU A 97 -2.360 28.348 11.232 1.00 33.88 C ANISOU 760 C GLU A 97 3836 4584 4454 155 -511 411 C ATOM 761 O GLU A 97 -2.161 27.868 10.105 1.00 33.94 O ANISOU 761 O GLU A 97 3835 4711 4348 63 -600 438 O ATOM 762 CB GLU A 97 -4.807 28.838 10.947 1.00 36.71 C ANISOU 762 CB GLU A 97 3929 5036 4983 250 -548 665 C ATOM 763 CG GLU A 97 -5.797 28.509 12.010 1.00 37.04 C ANISOU 763 CG GLU A 97 3899 5058 5118 307 -473 638 C ATOM 764 CD GLU A 97 -6.241 29.722 12.776 1.00 38.29 C ANISOU 764 CD GLU A 97 4023 5066 5460 468 -346 694 C ATOM 765 OE1 GLU A 97 -6.779 30.671 12.162 1.00 39.90 O ANISOU 765 OE1 GLU A 97 4124 5265 5770 558 -360 875 O ATOM 766 OE2 GLU A 97 -6.061 29.711 14.006 1.00 38.22 O ANISOU 766 OE2 GLU A 97 4095 4941 5487 502 -225 561 O ATOM 767 N ILE A 98 -1.631 28.022 12.292 1.00 32.28 N ANISOU 767 N ILE A 98 3730 4298 4238 160 -437 270 N ATOM 768 CA ILE A 98 -0.632 26.967 12.219 1.00 31.27 C ANISOU 768 CA ILE A 98 3682 4212 3987 85 -456 154 C ATOM 769 C ILE A 98 -1.097 25.733 12.992 1.00 31.09 C ANISOU 769 C ILE A 98 3663 4199 3950 65 -436 72 C ATOM 770 O ILE A 98 -1.622 25.841 14.108 1.00 31.33 O ANISOU 770 O ILE A 98 3683 4168 4054 111 -373 51 O ATOM 771 CB ILE A 98 0.747 27.415 12.782 1.00 30.36 C ANISOU 771 CB ILE A 98 3663 4025 3849 89 -405 79 C ATOM 772 CG1 ILE A 98 1.175 28.774 12.212 1.00 31.67 C ANISOU 772 CG1 ILE A 98 3841 4151 4041 98 -406 159 C ATOM 773 CG2 ILE A 98 1.809 26.370 12.512 1.00 28.56 C ANISOU 773 CG2 ILE A 98 3484 3857 3510 36 -424 -4 C ATOM 774 CD1 ILE A 98 2.015 28.721 10.944 1.00 30.76 C ANISOU 774 CD1 ILE A 98 3737 4130 3820 30 -469 185 C ATOM 775 N GLN A 99 -0.901 24.566 12.385 1.00 30.86 N ANISOU 775 N GLN A 99 3662 4240 3825 -10 -479 23 N ATOM 776 CA GLN A 99 -1.005 23.299 13.092 1.00 30.64 C ANISOU 776 CA GLN A 99 3678 4191 3772 -37 -451 -63 C ATOM 777 C GLN A 99 0.288 22.490 12.953 1.00 30.56 C ANISOU 777 C GLN A 99 3764 4163 3685 -53 -433 -151 C ATOM 778 O GLN A 99 0.958 22.534 11.910 1.00 30.66 O ANISOU 778 O GLN A 99 3797 4221 3631 -83 -454 -155 O ATOM 779 CB GLN A 99 -2.182 22.479 12.567 1.00 31.35 C ANISOU 779 CB GLN A 99 3718 4360 3832 -121 -498 -40 C ATOM 780 CG GLN A 99 -3.538 23.035 12.932 1.00 31.56 C ANISOU 780 CG GLN A 99 3621 4420 3949 -93 -503 53 C ATOM 781 CD GLN A 99 -4.572 22.739 11.887 1.00 30.73 C ANISOU 781 CD GLN A 99 3423 4455 3799 -192 -588 137 C ATOM 782 OE1 GLN A 99 -4.720 23.477 10.922 1.00 30.94 O ANISOU 782 OE1 GLN A 99 3381 4559 3817 -198 -651 242 O ATOM 783 NE2 GLN A 99 -5.301 21.655 12.073 1.00 32.02 N ANISOU 783 NE2 GLN A 99 3581 4661 3924 -287 -597 101 N ATOM 784 N LEU A 100 0.634 21.764 14.015 1.00 30.30 N ANISOU 784 N LEU A 100 3781 4069 3664 -27 -386 -209 N ATOM 785 CA LEU A 100 1.678 20.758 13.952 1.00 30.38 C ANISOU 785 CA LEU A 100 3864 4053 3625 -22 -359 -272 C ATOM 786 C LEU A 100 1.136 19.433 14.396 1.00 30.64 C ANISOU 786 C LEU A 100 3946 4038 3657 -52 -337 -311 C ATOM 787 O LEU A 100 0.336 19.364 15.320 1.00 30.81 O ANISOU 787 O LEU A 100 3949 4039 3719 -58 -331 -294 O ATOM 788 CB LEU A 100 2.846 21.110 14.859 1.00 30.17 C ANISOU 788 CB LEU A 100 3849 4001 3613 41 -329 -273 C ATOM 789 CG LEU A 100 3.944 21.996 14.296 1.00 30.59 C ANISOU 789 CG LEU A 100 3886 4099 3639 54 -336 -257 C ATOM 790 CD1 LEU A 100 3.492 23.441 14.357 1.00 31.49 C ANISOU 790 CD1 LEU A 100 3963 4212 3788 46 -353 -209 C ATOM 791 CD2 LEU A 100 5.190 21.794 15.123 1.00 30.43 C ANISOU 791 CD2 LEU A 100 3871 4080 3610 95 -310 -260 C ATOM 792 N SER A 101 1.594 18.379 13.739 1.00 31.32 N ANISOU 792 N SER A 101 4106 4098 3697 -76 -311 -366 N ATOM 793 CA SER A 101 1.283 17.019 14.137 1.00 31.99 C ANISOU 793 CA SER A 101 4270 4100 3784 -104 -271 -408 C ATOM 794 C SER A 101 2.597 16.278 14.228 1.00 32.45 C ANISOU 794 C SER A 101 4395 4085 3851 -19 -206 -437 C ATOM 795 O SER A 101 3.285 16.120 13.222 1.00 33.22 O ANISOU 795 O SER A 101 4523 4191 3909 -14 -172 -481 O ATOM 796 CB SER A 101 0.404 16.367 13.081 1.00 32.77 C ANISOU 796 CB SER A 101 4412 4221 3818 -234 -284 -453 C ATOM 797 OG SER A 101 -0.098 15.140 13.548 1.00 33.86 O ANISOU 797 OG SER A 101 4634 4270 3962 -288 -246 -489 O ATOM 798 N ALA A 102 2.970 15.846 15.425 1.00 32.69 N ANISOU 798 N ALA A 102 4437 4054 3931 48 -183 -401 N ATOM 799 CA ALA A 102 4.241 15.156 15.601 1.00 33.80 C ANISOU 799 CA ALA A 102 4609 4134 4098 152 -124 -391 C ATOM 800 C ALA A 102 4.125 13.974 16.545 1.00 35.16 C ANISOU 800 C ALA A 102 4851 4193 4317 181 -86 -361 C ATOM 801 O ALA A 102 3.289 13.964 17.450 1.00 34.97 O ANISOU 801 O ALA A 102 4824 4165 4298 129 -119 -329 O ATOM 802 CB ALA A 102 5.295 16.110 16.088 1.00 33.13 C ANISOU 802 CB ALA A 102 4431 4136 4020 226 -151 -328 C ATOM 803 N GLY A 103 4.978 12.982 16.325 1.00 36.92 N ANISOU 803 N GLY A 103 5134 4316 4577 269 -6 -364 N ATOM 804 CA GLY A 103 5.017 11.792 17.159 1.00 38.91 C ANISOU 804 CA GLY A 103 5461 4434 4889 318 39 -312 C ATOM 805 C GLY A 103 5.564 10.623 16.379 1.00 41.23 C ANISOU 805 C GLY A 103 5866 4573 5226 385 162 -366 C ATOM 806 O GLY A 103 6.439 10.797 15.530 1.00 41.68 O ANISOU 806 O GLY A 103 5898 4656 5284 455 216 -403 O ATOM 807 N CYS A 104 5.053 9.427 16.657 1.00 43.22 N ANISOU 807 N CYS A 104 6250 4655 5515 358 221 -374 N ATOM 808 CA CYS A 104 5.507 8.234 15.945 1.00 46.18 C ANISOU 808 CA CYS A 104 6767 4836 5942 418 370 -440 C ATOM 809 C CYS A 104 4.487 7.102 15.951 1.00 47.89 C ANISOU 809 C CYS A 104 7168 4872 6157 292 425 -502 C ATOM 810 O CYS A 104 3.640 7.021 16.841 1.00 47.43 O ANISOU 810 O CYS A 104 7110 4822 6088 206 353 -443 O ATOM 811 CB CYS A 104 6.859 7.752 16.489 1.00 47.16 C ANISOU 811 CB CYS A 104 6843 4891 6183 644 439 -315 C ATOM 812 SG CYS A 104 6.905 7.571 18.264 1.00 48.28 S ANISOU 812 SG CYS A 104 6918 5046 6382 706 349 -107 S ATOM 813 N GLU A 105 4.573 6.245 14.935 1.00 50.44 N ANISOU 813 N GLU A 105 7653 5034 6479 263 564 -631 N ATOM 814 CA GLU A 105 3.757 5.045 14.851 1.00 53.27 C ANISOU 814 CA GLU A 105 8220 5185 6835 132 646 -704 C ATOM 815 C GLU A 105 4.642 3.923 15.368 1.00 55.70 C ANISOU 815 C GLU A 105 8624 5245 7294 330 786 -625 C ATOM 816 O GLU A 105 5.703 3.675 14.787 1.00 57.36 O ANISOU 816 O GLU A 105 8850 5374 7572 492 916 -653 O ATOM 817 CB GLU A 105 3.336 4.768 13.399 1.00 54.35 C ANISOU 817 CB GLU A 105 8501 5286 6864 -43 729 -905 C ATOM 818 CG GLU A 105 2.667 5.951 12.664 1.00 54.58 C ANISOU 818 CG GLU A 105 8410 5581 6748 -209 593 -960 C ATOM 819 CD GLU A 105 2.995 6.010 11.154 1.00 58.57 C ANISOU 819 CD GLU A 105 8988 6112 7153 -285 679 -1118 C ATOM 820 OE1 GLU A 105 3.135 4.937 10.518 1.00 62.84 O ANISOU 820 OE1 GLU A 105 9739 6451 7685 -336 846 -1250 O ATOM 821 OE2 GLU A 105 3.115 7.128 10.591 1.00 57.41 O ANISOU 821 OE2 GLU A 105 8702 6181 6931 -303 590 -1113 O ATOM 822 N MET A 106 4.227 3.269 16.460 1.00 56.61 N ANISOU 822 N MET A 106 8793 5248 7469 325 765 -511 N ATOM 823 CA MET A 106 4.996 2.167 17.079 1.00 58.90 C ANISOU 823 CA MET A 106 9171 5292 7917 520 886 -389 C ATOM 824 C MET A 106 4.684 0.811 16.462 1.00 61.83 C ANISOU 824 C MET A 106 9825 5339 8327 451 1076 -515 C ATOM 825 O MET A 106 3.513 0.433 16.354 1.00 62.42 O ANISOU 825 O MET A 106 10041 5362 8315 206 1060 -609 O ATOM 826 CB MET A 106 4.723 2.081 18.584 1.00 58.29 C ANISOU 826 CB MET A 106 9028 5246 7875 536 773 -186 C ATOM 827 CG MET A 106 4.964 3.367 19.351 1.00 55.92 C ANISOU 827 CG MET A 106 8478 5246 7522 573 597 -67 C ATOM 828 SD MET A 106 6.621 4.061 19.187 1.00 55.10 S ANISOU 828 SD MET A 106 8174 5279 7484 829 601 24 S ATOM 829 CE MET A 106 7.612 2.852 20.062 1.00 57.61 C ANISOU 829 CE MET A 106 8517 5390 7983 1074 692 255 C ATOM 830 N TYR A 107 5.728 0.076 16.079 1.00 64.36 N ANISOU 830 N TYR A 107 10228 5443 8782 661 1266 -516 N ATOM 831 CA TYR A 107 5.583 -1.294 15.564 1.00 67.67 C ANISOU 831 CA TYR A 107 10946 5497 9267 628 1489 -633 C ATOM 832 C TYR A 107 6.283 -2.282 16.495 1.00 69.88 C ANISOU 832 C TYR A 107 11276 5517 9758 878 1590 -425 C ATOM 833 O TYR A 107 7.098 -1.863 17.320 1.00 69.17 O ANISOU 833 O TYR A 107 10965 5560 9756 1098 1502 -202 O ATOM 834 CB TYR A 107 6.145 -1.407 14.142 1.00 69.06 C ANISOU 834 CB TYR A 107 11222 5595 9424 652 1678 -846 C ATOM 835 CG TYR A 107 5.757 -0.262 13.232 1.00 67.98 C ANISOU 835 CG TYR A 107 10977 5763 9091 464 1561 -995 C ATOM 836 CD1 TYR A 107 4.453 -0.138 12.737 1.00 68.04 C ANISOU 836 CD1 TYR A 107 11084 5853 8916 126 1478 -1143 C ATOM 837 CD2 TYR A 107 6.695 0.698 12.861 1.00 67.63 C ANISOU 837 CD2 TYR A 107 10720 5935 9043 618 1528 -969 C ATOM 838 CE1 TYR A 107 4.095 0.923 11.903 1.00 66.62 C ANISOU 838 CE1 TYR A 107 10791 5959 8564 -34 1362 -1244 C ATOM 839 CE2 TYR A 107 6.352 1.757 12.023 1.00 66.68 C ANISOU 839 CE2 TYR A 107 10506 6081 8747 449 1421 -1084 C ATOM 840 CZ TYR A 107 5.051 1.866 11.550 1.00 66.29 C ANISOU 840 CZ TYR A 107 10554 6104 8528 132 1336 -1213 C ATOM 841 OH TYR A 107 4.723 2.923 10.724 1.00 64.88 O ANISOU 841 OH TYR A 107 10269 6195 8186 -20 1223 -1293 O ATOM 842 N PRO A 108 5.978 -3.596 16.366 1.00 72.95 N ANISOU 842 N PRO A 108 11956 5535 10225 835 1777 -486 N ATOM 843 CA PRO A 108 6.567 -4.609 17.258 1.00 75.24 C ANISOU 843 CA PRO A 108 12313 5545 10730 1073 1880 -264 C ATOM 844 C PRO A 108 8.097 -4.631 17.219 1.00 76.46 C ANISOU 844 C PRO A 108 12316 5662 11073 1457 1996 -124 C ATOM 845 O PRO A 108 8.713 -4.175 16.245 1.00 76.22 O ANISOU 845 O PRO A 108 12221 5719 11022 1529 2082 -265 O ATOM 846 CB PRO A 108 5.994 -5.931 16.725 1.00 78.09 C ANISOU 846 CB PRO A 108 13054 5490 11125 932 2107 -432 C ATOM 847 CG PRO A 108 5.608 -5.643 15.319 1.00 77.84 C ANISOU 847 CG PRO A 108 13134 5513 10928 712 2184 -752 C ATOM 848 CD PRO A 108 5.114 -4.228 15.348 1.00 74.51 C ANISOU 848 CD PRO A 108 12448 5547 10316 558 1912 -759 C ATOM 849 N GLY A 109 8.689 -5.158 18.287 1.00 77.84 N ANISOU 849 N GLY A 109 12423 5728 11425 1693 1993 167 N ATOM 850 CA GLY A 109 10.137 -5.158 18.464 1.00 78.83 C ANISOU 850 CA GLY A 109 12347 5868 11738 2069 2066 371 C ATOM 851 C GLY A 109 10.657 -3.773 18.813 1.00 75.48 C ANISOU 851 C GLY A 109 11563 5901 11216 2108 1833 483 C ATOM 852 O GLY A 109 10.198 -3.140 19.769 1.00 73.06 O ANISOU 852 O GLY A 109 11120 5839 10799 1982 1592 613 O ATOM 853 N ASN A 110 11.621 -3.308 18.025 1.00 75.31 N ANISOU 853 N ASN A 110 11399 5987 11228 2271 1921 421 N ATOM 854 CA ASN A 110 12.229 -1.999 18.242 1.00 72.59 C ANISOU 854 CA ASN A 110 10725 6060 10795 2306 1726 514 C ATOM 855 C ASN A 110 11.718 -0.910 17.292 1.00 69.23 C ANISOU 855 C ASN A 110 10281 5868 10155 2066 1650 245 C ATOM 856 O ASN A 110 11.749 0.270 17.640 1.00 66.87 O ANISOU 856 O ASN A 110 9765 5908 9734 1987 1440 299 O ATOM 857 CB ASN A 110 13.777 -2.081 18.230 1.00 74.78 C ANISOU 857 CB ASN A 110 10781 6376 11257 2664 1830 707 C ATOM 858 CG ASN A 110 14.342 -2.757 16.968 1.00 77.75 C ANISOU 858 CG ASN A 110 11299 6488 11756 2823 2152 521 C ATOM 859 OD1 ASN A 110 14.553 -3.972 16.938 1.00 80.72 O ANISOU 859 OD1 ASN A 110 11851 6493 12327 3002 2379 563 O ATOM 860 ND2 ASN A 110 14.617 -1.958 15.937 1.00 77.03 N ANISOU 860 ND2 ASN A 110 11133 6582 11551 2761 2183 319 N ATOM 861 N ALA A 111 11.214 -1.314 16.125 1.00 69.23 N ANISOU 861 N ALA A 111 10520 5680 10104 1935 1820 -35 N ATOM 862 CA ALA A 111 10.963 -0.393 15.002 1.00 66.81 C ANISOU 862 CA ALA A 111 10194 5575 9616 1752 1793 -276 C ATOM 863 C ALA A 111 9.850 0.669 15.193 1.00 63.03 C ANISOU 863 C ALA A 111 9654 5371 8924 1455 1538 -336 C ATOM 864 O ALA A 111 8.827 0.413 15.850 1.00 62.36 O ANISOU 864 O ALA A 111 9664 5237 8793 1290 1440 -311 O ATOM 865 CB ALA A 111 10.733 -1.189 13.707 1.00 68.94 C ANISOU 865 CB ALA A 111 10749 5574 9870 1670 2052 -555 C ATOM 866 N SER A 112 10.082 1.854 14.611 1.00 60.15 N ANISOU 866 N SER A 112 9125 5290 8439 1398 1445 -407 N ATOM 867 CA SER A 112 9.081 2.925 14.506 1.00 56.29 C ANISOU 867 CA SER A 112 8583 5045 7758 1136 1244 -490 C ATOM 868 C SER A 112 9.430 3.938 13.405 1.00 54.64 C ANISOU 868 C SER A 112 8275 5049 7435 1084 1233 -618 C ATOM 869 O SER A 112 10.538 3.925 12.868 1.00 55.58 O ANISOU 869 O SER A 112 8329 5170 7618 1256 1360 -623 O ATOM 870 CB SER A 112 8.918 3.640 15.843 1.00 54.31 C ANISOU 870 CB SER A 112 8146 4992 7496 1137 1023 -287 C ATOM 871 OG SER A 112 10.127 4.252 16.229 1.00 53.97 O ANISOU 871 OG SER A 112 7874 5120 7512 1332 979 -130 O ATOM 872 N GLU A 113 8.468 4.791 13.057 1.00 52.12 N ANISOU 872 N GLU A 113 7943 4908 6951 846 1087 -711 N ATOM 873 CA GLU A 113 8.706 5.948 12.180 1.00 50.39 C ANISOU 873 CA GLU A 113 7605 4927 6615 780 1028 -786 C ATOM 874 C GLU A 113 8.225 7.195 12.891 1.00 46.58 C ANISOU 874 C GLU A 113 6946 4688 6063 698 797 -682 C ATOM 875 O GLU A 113 7.081 7.259 13.313 1.00 45.80 O ANISOU 875 O GLU A 113 6891 4601 5911 542 694 -684 O ATOM 876 CB GLU A 113 7.941 5.848 10.857 1.00 51.14 C ANISOU 876 CB GLU A 113 7864 5005 6561 551 1085 -1005 C ATOM 877 CG GLU A 113 8.194 4.618 10.008 1.00 56.82 C ANISOU 877 CG GLU A 113 8815 5468 7307 560 1334 -1168 C ATOM 878 CD GLU A 113 7.117 4.433 8.923 1.00 61.22 C ANISOU 878 CD GLU A 113 9561 6020 7680 252 1351 -1375 C ATOM 879 OE1 GLU A 113 6.291 5.365 8.731 1.00 60.69 O ANISOU 879 OE1 GLU A 113 9404 6182 7475 62 1162 -1371 O ATOM 880 OE2 GLU A 113 7.097 3.361 8.262 1.00 64.53 O ANISOU 880 OE2 GLU A 113 10217 6208 8092 194 1556 -1537 O ATOM 881 N SER A 114 9.089 8.189 13.017 1.00 44.39 N ANISOU 881 N SER A 114 6476 4604 5788 795 729 -594 N ATOM 882 CA SER A 114 8.692 9.453 13.611 1.00 40.95 C ANISOU 882 CA SER A 114 5895 4381 5284 711 537 -517 C ATOM 883 C SER A 114 8.342 10.442 12.516 1.00 39.29 C ANISOU 883 C SER A 114 5661 4322 4945 566 487 -623 C ATOM 884 O SER A 114 8.907 10.390 11.424 1.00 40.34 O ANISOU 884 O SER A 114 5821 4462 5043 577 588 -715 O ATOM 885 CB SER A 114 9.809 10.005 14.488 1.00 40.53 C ANISOU 885 CB SER A 114 5653 4454 5293 866 481 -349 C ATOM 886 OG SER A 114 10.159 9.080 15.492 1.00 41.25 O ANISOU 886 OG SER A 114 5752 4424 5498 1001 516 -219 O ATOM 887 N PHE A 115 7.413 11.342 12.811 1.00 36.68 N ANISOU 887 N PHE A 115 5279 4112 4547 434 340 -603 N ATOM 888 CA PHE A 115 6.972 12.347 11.848 1.00 34.82 C ANISOU 888 CA PHE A 115 5009 4021 4199 300 273 -665 C ATOM 889 C PHE A 115 6.827 13.690 12.545 1.00 32.69 C ANISOU 889 C PHE A 115 4595 3904 3921 289 132 -565 C ATOM 890 O PHE A 115 6.692 13.752 13.768 1.00 31.99 O ANISOU 890 O PHE A 115 4463 3805 3885 330 80 -478 O ATOM 891 CB PHE A 115 5.628 11.940 11.243 1.00 34.97 C ANISOU 891 CB PHE A 115 5147 4002 4138 112 258 -760 C ATOM 892 CG PHE A 115 4.580 11.670 12.272 1.00 34.10 C ANISOU 892 CG PHE A 115 5051 3845 4061 58 189 -709 C ATOM 893 CD1 PHE A 115 4.380 10.388 12.751 1.00 34.55 C ANISOU 893 CD1 PHE A 115 5235 3720 4174 69 269 -726 C ATOM 894 CD2 PHE A 115 3.823 12.706 12.803 1.00 32.56 C ANISOU 894 CD2 PHE A 115 4743 3778 3850 3 59 -638 C ATOM 895 CE1 PHE A 115 3.423 10.140 13.721 1.00 34.24 C ANISOU 895 CE1 PHE A 115 5204 3649 4155 6 208 -673 C ATOM 896 CE2 PHE A 115 2.873 12.462 13.780 1.00 31.68 C ANISOU 896 CE2 PHE A 115 4635 3635 3767 -44 13 -593 C ATOM 897 CZ PHE A 115 2.676 11.185 14.240 1.00 32.73 C ANISOU 897 CZ PHE A 115 4888 3609 3939 -50 81 -609 C ATOM 898 N LEU A 116 6.863 14.756 11.748 1.00 31.79 N ANISOU 898 N LEU A 116 4421 3923 3735 225 82 -579 N ATOM 899 CA LEU A 116 6.600 16.120 12.199 1.00 29.81 C ANISOU 899 CA LEU A 116 4063 3792 3473 194 -32 -504 C ATOM 900 C LEU A 116 6.079 16.908 11.004 1.00 29.92 C ANISOU 900 C LEU A 116 4069 3901 3399 77 -78 -536 C ATOM 901 O LEU A 116 6.859 17.422 10.183 1.00 30.28 O ANISOU 901 O LEU A 116 4084 4024 3396 79 -59 -545 O ATOM 902 CB LEU A 116 7.860 16.777 12.746 1.00 29.07 C ANISOU 902 CB LEU A 116 3866 3771 3410 293 -39 -428 C ATOM 903 CG LEU A 116 7.666 17.981 13.671 1.00 27.77 C ANISOU 903 CG LEU A 116 3622 3678 3250 267 -133 -354 C ATOM 904 CD1 LEU A 116 9.006 18.575 14.083 1.00 27.12 C ANISOU 904 CD1 LEU A 116 3447 3687 3172 325 -137 -288 C ATOM 905 CD2 LEU A 116 6.797 19.057 13.049 1.00 27.03 C ANISOU 905 CD2 LEU A 116 3519 3637 3114 168 -196 -363 C ATOM 906 N HIS A 117 4.756 16.993 10.910 1.00 29.52 N ANISOU 906 N HIS A 117 4035 3859 3324 -27 -141 -537 N ATOM 907 CA HIS A 117 4.107 17.680 9.810 1.00 29.46 C ANISOU 907 CA HIS A 117 4007 3955 3233 -145 -202 -533 C ATOM 908 C HIS A 117 3.557 19.020 10.243 1.00 28.07 C ANISOU 908 C HIS A 117 3726 3845 3093 -141 -295 -432 C ATOM 909 O HIS A 117 3.120 19.176 11.379 1.00 27.55 O ANISOU 909 O HIS A 117 3629 3736 3102 -96 -313 -393 O ATOM 910 CB HIS A 117 3.022 16.794 9.237 1.00 30.59 C ANISOU 910 CB HIS A 117 4227 4083 3312 -282 -204 -593 C ATOM 911 CG HIS A 117 3.543 15.486 8.727 1.00 33.45 C ANISOU 911 CG HIS A 117 4726 4348 3636 -299 -84 -713 C ATOM 912 ND1 HIS A 117 2.853 14.300 8.863 1.00 36.46 N ANISOU 912 ND1 HIS A 117 5218 4625 4010 -377 -41 -781 N ATOM 913 CD2 HIS A 117 4.703 15.176 8.104 1.00 34.02 C ANISOU 913 CD2 HIS A 117 4847 4396 3682 -245 19 -780 C ATOM 914 CE1 HIS A 117 3.560 13.319 8.333 1.00 36.86 C ANISOU 914 CE1 HIS A 117 5397 4571 4038 -366 92 -891 C ATOM 915 NE2 HIS A 117 4.683 13.826 7.859 1.00 36.55 N ANISOU 915 NE2 HIS A 117 5315 4583 3989 -278 135 -893 N ATOM 916 N VAL A 118 3.613 19.992 9.342 1.00 27.64 N ANISOU 916 N VAL A 118 3627 3887 2988 -186 -342 -388 N ATOM 917 CA VAL A 118 3.212 21.352 9.662 1.00 26.80 C ANISOU 917 CA VAL A 118 3435 3815 2933 -165 -409 -285 C ATOM 918 C VAL A 118 2.185 21.812 8.660 1.00 27.48 C ANISOU 918 C VAL A 118 3479 3995 2969 -263 -486 -217 C ATOM 919 O VAL A 118 2.360 21.651 7.460 1.00 28.31 O ANISOU 919 O VAL A 118 3609 4180 2966 -354 -499 -233 O ATOM 920 CB VAL A 118 4.409 22.335 9.670 1.00 26.48 C ANISOU 920 CB VAL A 118 3370 3795 2898 -113 -396 -255 C ATOM 921 CG1 VAL A 118 3.942 23.746 9.998 1.00 25.73 C ANISOU 921 CG1 VAL A 118 3217 3695 2863 -98 -444 -158 C ATOM 922 CG2 VAL A 118 5.460 21.905 10.691 1.00 25.99 C ANISOU 922 CG2 VAL A 118 3320 3678 2876 -27 -336 -294 C ATOM 923 N ALA A 119 1.098 22.378 9.161 1.00 27.60 N ANISOU 923 N ALA A 119 3420 4009 3059 -247 -534 -133 N ATOM 924 CA ALA A 119 0.056 22.884 8.291 1.00 28.61 C ANISOU 924 CA ALA A 119 3470 4242 3158 -322 -619 -26 C ATOM 925 C ALA A 119 -0.129 24.393 8.470 1.00 28.93 C ANISOU 925 C ALA A 119 3429 4270 3294 -240 -646 104 C ATOM 926 O ALA A 119 0.031 24.941 9.569 1.00 28.24 O ANISOU 926 O ALA A 119 3340 4079 3312 -138 -595 101 O ATOM 927 CB ALA A 119 -1.232 22.145 8.529 1.00 28.85 C ANISOU 927 CB ALA A 119 3462 4303 3196 -383 -647 -19 C ATOM 928 N PHE A 120 -0.465 25.047 7.364 1.00 30.19 N ANISOU 928 N PHE A 120 3533 4531 3407 -297 -721 222 N ATOM 929 CA PHE A 120 -0.600 26.490 7.296 1.00 30.86 C ANISOU 929 CA PHE A 120 3554 4592 3580 -224 -744 367 C ATOM 930 C PHE A 120 -1.937 26.780 6.636 1.00 32.34 C ANISOU 930 C PHE A 120 3613 4893 3781 -259 -837 536 C ATOM 931 O PHE A 120 -2.206 26.285 5.540 1.00 33.56 O ANISOU 931 O PHE A 120 3751 5202 3800 -397 -917 568 O ATOM 932 CB PHE A 120 0.544 27.057 6.461 1.00 30.92 C ANISOU 932 CB PHE A 120 3617 4625 3506 -264 -749 378 C ATOM 933 CG PHE A 120 0.587 28.548 6.409 1.00 32.12 C ANISOU 933 CG PHE A 120 3738 4717 3748 -197 -758 519 C ATOM 934 CD1 PHE A 120 1.008 29.289 7.511 1.00 31.81 C ANISOU 934 CD1 PHE A 120 3739 4520 3828 -95 -676 489 C ATOM 935 CD2 PHE A 120 0.250 29.222 5.238 1.00 35.06 C ANISOU 935 CD2 PHE A 120 4057 5189 4076 -253 -843 687 C ATOM 936 CE1 PHE A 120 1.070 30.688 7.465 1.00 32.28 C ANISOU 936 CE1 PHE A 120 3799 4490 3975 -43 -663 608 C ATOM 937 CE2 PHE A 120 0.310 30.631 5.177 1.00 36.04 C ANISOU 937 CE2 PHE A 120 4167 5228 4298 -184 -842 833 C ATOM 938 CZ PHE A 120 0.722 31.357 6.299 1.00 34.29 C ANISOU 938 CZ PHE A 120 4002 4818 4209 -77 -743 784 C ATOM 939 N GLN A 121 -2.779 27.561 7.312 1.00 32.52 N ANISOU 939 N GLN A 121 3541 4851 3963 -140 -821 645 N ATOM 940 CA GLN A 121 -4.127 27.851 6.836 1.00 33.55 C ANISOU 940 CA GLN A 121 3510 5097 4139 -142 -903 833 C ATOM 941 C GLN A 121 -4.846 26.571 6.395 1.00 34.25 C ANISOU 941 C GLN A 121 3558 5353 4102 -298 -974 798 C ATOM 942 O GLN A 121 -5.511 26.554 5.362 1.00 35.81 O ANISOU 942 O GLN A 121 3659 5733 4216 -408 -1088 937 O ATOM 943 CB GLN A 121 -4.101 28.888 5.709 1.00 34.69 C ANISOU 943 CB GLN A 121 3600 5313 4268 -153 -985 1031 C ATOM 944 CG GLN A 121 -3.128 30.072 5.926 1.00 34.04 C ANISOU 944 CG GLN A 121 3606 5062 4266 -53 -914 1043 C ATOM 945 CD GLN A 121 -3.612 31.130 6.930 1.00 32.85 C ANISOU 945 CD GLN A 121 3416 4727 4340 134 -818 1115 C ATOM 946 OE1 GLN A 121 -3.990 30.819 8.064 1.00 31.32 O ANISOU 946 OE1 GLN A 121 3219 4448 4234 207 -731 1016 O ATOM 947 NE2 GLN A 121 -3.569 32.391 6.514 1.00 32.59 N ANISOU 947 NE2 GLN A 121 3368 4620 4394 206 -819 1284 N ATOM 948 N GLY A 122 -4.700 25.499 7.184 1.00 33.47 N ANISOU 948 N GLY A 122 3541 5194 3981 -323 -909 619 N ATOM 949 CA GLY A 122 -5.405 24.230 6.952 1.00 33.86 C ANISOU 949 CA GLY A 122 3579 5361 3925 -479 -953 564 C ATOM 950 C GLY A 122 -4.866 23.347 5.833 1.00 34.45 C ANISOU 950 C GLY A 122 3765 5531 3792 -671 -994 469 C ATOM 951 O GLY A 122 -5.536 22.402 5.411 1.00 35.11 O ANISOU 951 O GLY A 122 3846 5731 3765 -841 -1041 441 O ATOM 952 N LYS A 123 -3.664 23.657 5.346 1.00 34.05 N ANISOU 952 N LYS A 123 3817 5436 3683 -659 -965 414 N ATOM 953 CA LYS A 123 -3.033 22.888 4.277 1.00 35.08 C ANISOU 953 CA LYS A 123 4066 5644 3619 -828 -969 307 C ATOM 954 C LYS A 123 -1.639 22.441 4.713 1.00 33.55 C ANISOU 954 C LYS A 123 4024 5297 3428 -755 -845 125 C ATOM 955 O LYS A 123 -0.882 23.211 5.315 1.00 32.57 O ANISOU 955 O LYS A 123 3900 5069 3407 -607 -798 137 O ATOM 956 CB LYS A 123 -2.922 23.705 2.990 1.00 36.45 C ANISOU 956 CB LYS A 123 4194 5967 3687 -913 -1060 446 C ATOM 957 CG LYS A 123 -4.221 24.282 2.453 1.00 40.71 C ANISOU 957 CG LYS A 123 4556 6686 4227 -974 -1200 678 C ATOM 958 CD LYS A 123 -3.940 25.626 1.712 1.00 45.82 C ANISOU 958 CD LYS A 123 5138 7387 4883 -930 -1266 873 C ATOM 959 CE LYS A 123 -5.202 26.251 1.083 1.00 49.13 C ANISOU 959 CE LYS A 123 5358 8000 5308 -977 -1416 1152 C ATOM 960 NZ LYS A 123 -5.752 25.413 -0.040 1.00 51.36 N ANISOU 960 NZ LYS A 123 5628 8537 5349 -1258 -1527 1165 N ATOM 961 N TYR A 124 -1.305 21.195 4.396 1.00 33.39 N ANISOU 961 N TYR A 124 4128 5264 3293 -864 -787 -36 N ATOM 962 CA TYR A 124 -0.025 20.612 4.794 1.00 32.04 C ANISOU 962 CA TYR A 124 4084 4954 3137 -782 -660 -194 C ATOM 963 C TYR A 124 1.065 21.140 3.865 1.00 32.20 C ANISOU 963 C TYR A 124 4137 5028 3068 -798 -638 -201 C ATOM 964 O TYR A 124 0.943 21.051 2.636 1.00 33.54 O ANISOU 964 O TYR A 124 4333 5332 3078 -961 -674 -198 O ATOM 965 CB TYR A 124 -0.152 19.085 4.767 1.00 32.46 C ANISOU 965 CB TYR A 124 4265 4950 3120 -882 -587 -352 C ATOM 966 CG TYR A 124 1.106 18.254 4.888 1.00 30.95 C ANISOU 966 CG TYR A 124 4209 4626 2925 -816 -443 -510 C ATOM 967 CD1 TYR A 124 2.027 18.462 5.919 1.00 28.87 C ANISOU 967 CD1 TYR A 124 3932 4243 2796 -621 -379 -515 C ATOM 968 CD2 TYR A 124 1.336 17.204 3.994 1.00 30.62 C ANISOU 968 CD2 TYR A 124 4309 4579 2746 -955 -361 -654 C ATOM 969 CE1 TYR A 124 3.167 17.664 6.025 1.00 28.79 C ANISOU 969 CE1 TYR A 124 4017 4127 2796 -545 -249 -630 C ATOM 970 CE2 TYR A 124 2.454 16.406 4.091 1.00 30.39 C ANISOU 970 CE2 TYR A 124 4396 4413 2736 -870 -207 -789 C ATOM 971 CZ TYR A 124 3.363 16.629 5.110 1.00 30.52 C ANISOU 971 CZ TYR A 124 4368 4325 2902 -654 -155 -764 C ATOM 972 OH TYR A 124 4.476 15.821 5.189 1.00 32.11 O ANISOU 972 OH TYR A 124 4658 4407 3135 -553 -3 -870 O ATOM 973 N VAL A 125 2.114 21.709 4.457 1.00 30.54 N ANISOU 973 N VAL A 125 3922 4732 2948 -650 -582 -205 N ATOM 974 CA VAL A 125 3.080 22.496 3.696 1.00 30.41 C ANISOU 974 CA VAL A 125 3905 4781 2870 -658 -575 -173 C ATOM 975 C VAL A 125 4.538 22.199 4.014 1.00 29.85 C ANISOU 975 C VAL A 125 3886 4637 2817 -565 -455 -281 C ATOM 976 O VAL A 125 5.397 22.331 3.149 1.00 30.82 O ANISOU 976 O VAL A 125 4037 4832 2843 -614 -413 -310 O ATOM 977 CB VAL A 125 2.836 24.036 3.842 1.00 30.12 C ANISOU 977 CB VAL A 125 3766 4764 2915 -600 -660 4 C ATOM 978 CG1 VAL A 125 1.654 24.481 3.015 1.00 30.89 C ANISOU 978 CG1 VAL A 125 3790 4990 2956 -708 -781 152 C ATOM 979 CG2 VAL A 125 2.664 24.444 5.304 1.00 28.59 C ANISOU 979 CG2 VAL A 125 3532 4433 2898 -447 -642 28 C ATOM 980 N VAL A 126 4.823 21.821 5.251 1.00 28.79 N ANISOU 980 N VAL A 126 3754 4379 2805 -435 -403 -324 N ATOM 981 CA VAL A 126 6.195 21.642 5.708 1.00 28.16 C ANISOU 981 CA VAL A 126 3685 4251 2764 -330 -308 -382 C ATOM 982 C VAL A 126 6.300 20.379 6.544 1.00 28.07 C ANISOU 982 C VAL A 126 3725 4123 2818 -251 -229 -473 C ATOM 983 O VAL A 126 5.354 19.993 7.232 1.00 27.84 O ANISOU 983 O VAL A 126 3706 4029 2844 -248 -262 -467 O ATOM 984 CB VAL A 126 6.647 22.859 6.547 1.00 27.33 C ANISOU 984 CB VAL A 126 3504 4130 2749 -249 -346 -288 C ATOM 985 CG1 VAL A 126 7.917 22.575 7.321 1.00 26.50 C ANISOU 985 CG1 VAL A 126 3384 3990 2693 -147 -268 -328 C ATOM 986 CG2 VAL A 126 6.839 24.069 5.655 1.00 28.08 C ANISOU 986 CG2 VAL A 126 3568 4319 2783 -320 -398 -199 C ATOM 987 N ARG A 127 7.455 19.728 6.470 1.00 28.52 N ANISOU 987 N ARG A 127 3809 4154 2873 -182 -117 -546 N ATOM 988 CA ARG A 127 7.778 18.638 7.385 1.00 28.17 C ANISOU 988 CA ARG A 127 3799 3987 2918 -70 -37 -595 C ATOM 989 C ARG A 127 9.237 18.686 7.755 1.00 28.33 C ANISOU 989 C ARG A 127 3754 4022 2987 56 34 -576 C ATOM 990 O ARG A 127 10.052 19.262 7.043 1.00 28.72 O ANISOU 990 O ARG A 127 3760 4172 2979 39 58 -570 O ATOM 991 CB ARG A 127 7.445 17.271 6.774 1.00 29.24 C ANISOU 991 CB ARG A 127 4063 4041 3006 -121 58 -718 C ATOM 992 CG ARG A 127 8.478 16.738 5.799 1.00 29.43 C ANISOU 992 CG ARG A 127 4138 4075 2968 -109 202 -816 C ATOM 993 CD ARG A 127 8.061 15.403 5.222 1.00 29.16 C ANISOU 993 CD ARG A 127 4266 3930 2884 -180 315 -957 C ATOM 994 NE ARG A 127 8.944 15.032 4.119 1.00 31.24 N ANISOU 994 NE ARG A 127 4590 4215 3063 -196 468 -1068 N ATOM 995 CZ ARG A 127 9.091 13.801 3.638 1.00 32.20 C ANISOU 995 CZ ARG A 127 4863 4207 3163 -207 640 -1216 C ATOM 996 NH1 ARG A 127 8.424 12.784 4.155 1.00 33.48 N ANISOU 996 NH1 ARG A 127 5139 4200 3382 -212 675 -1265 N ATOM 997 NH2 ARG A 127 9.925 13.585 2.644 1.00 32.36 N ANISOU 997 NH2 ARG A 127 4930 4258 3106 -217 794 -1319 N ATOM 998 N PHE A 128 9.558 18.089 8.891 1.00 28.38 N ANISOU 998 N PHE A 128 3743 3945 3094 175 62 -552 N ATOM 999 CA PHE A 128 10.935 17.807 9.203 1.00 28.89 C ANISOU 999 CA PHE A 128 3738 4029 3211 304 143 -525 C ATOM 1000 C PHE A 128 11.172 16.420 8.671 1.00 30.39 C ANISOU 1000 C PHE A 128 4019 4109 3417 366 293 -622 C ATOM 1001 O PHE A 128 10.401 15.503 8.936 1.00 31.15 O ANISOU 1001 O PHE A 128 4220 4071 3546 360 317 -667 O ATOM 1002 CB PHE A 128 11.204 17.863 10.709 1.00 28.20 C ANISOU 1002 CB PHE A 128 3577 3924 3215 393 91 -425 C ATOM 1003 CG PHE A 128 12.664 17.936 11.046 1.00 29.40 C ANISOU 1003 CG PHE A 128 3605 4164 3403 499 132 -352 C ATOM 1004 CD1 PHE A 128 13.309 19.174 11.131 1.00 29.24 C ANISOU 1004 CD1 PHE A 128 3481 4290 3340 445 66 -287 C ATOM 1005 CD2 PHE A 128 13.408 16.772 11.240 1.00 30.05 C ANISOU 1005 CD2 PHE A 128 3669 4184 3565 648 244 -338 C ATOM 1006 CE1 PHE A 128 14.673 19.255 11.415 1.00 30.42 C ANISOU 1006 CE1 PHE A 128 3495 4556 3509 519 96 -208 C ATOM 1007 CE2 PHE A 128 14.769 16.838 11.522 1.00 31.89 C ANISOU 1007 CE2 PHE A 128 3753 4528 3837 754 279 -245 C ATOM 1008 CZ PHE A 128 15.409 18.087 11.613 1.00 31.92 C ANISOU 1008 CZ PHE A 128 3636 4711 3781 679 198 -179 C ATOM 1009 N TRP A 129 12.230 16.274 7.897 1.00 31.68 N ANISOU 1009 N TRP A 129 4152 4325 3559 417 409 -659 N ATOM 1010 CA TRP A 129 12.582 15.002 7.304 1.00 33.52 C ANISOU 1010 CA TRP A 129 4482 4441 3814 488 592 -766 C ATOM 1011 C TRP A 129 14.103 14.883 7.259 1.00 34.70 C ANISOU 1011 C TRP A 129 4507 4651 4025 650 714 -724 C ATOM 1012 O TRP A 129 14.779 15.730 6.687 1.00 34.81 O ANISOU 1012 O TRP A 129 4427 4829 3972 610 707 -705 O ATOM 1013 CB TRP A 129 11.980 14.909 5.898 1.00 34.29 C ANISOU 1013 CB TRP A 129 4713 4550 3765 316 641 -909 C ATOM 1014 CG TRP A 129 12.114 13.575 5.286 1.00 36.82 C ANISOU 1014 CG TRP A 129 5183 4717 4090 346 842 -1054 C ATOM 1015 CD1 TRP A 129 12.825 13.256 4.169 1.00 38.96 C ANISOU 1015 CD1 TRP A 129 5503 5008 4292 339 1017 -1170 C ATOM 1016 CD2 TRP A 129 11.533 12.354 5.762 1.00 38.73 C ANISOU 1016 CD2 TRP A 129 5563 4743 4408 381 910 -1108 C ATOM 1017 NE1 TRP A 129 12.724 11.905 3.910 1.00 41.92 N ANISOU 1017 NE1 TRP A 129 6051 5177 4701 373 1204 -1306 N ATOM 1018 CE2 TRP A 129 11.939 11.326 4.874 1.00 41.82 C ANISOU 1018 CE2 TRP A 129 6099 5011 4780 397 1139 -1265 C ATOM 1019 CE3 TRP A 129 10.711 12.027 6.854 1.00 37.93 C ANISOU 1019 CE3 TRP A 129 5487 4537 4386 392 812 -1041 C ATOM 1020 CZ2 TRP A 129 11.547 9.985 5.042 1.00 44.23 C ANISOU 1020 CZ2 TRP A 129 6587 5069 5151 423 1273 -1358 C ATOM 1021 CZ3 TRP A 129 10.320 10.691 7.028 1.00 40.88 C ANISOU 1021 CZ3 TRP A 129 6028 4686 4820 413 931 -1119 C ATOM 1022 CH2 TRP A 129 10.739 9.685 6.121 1.00 43.62 C ANISOU 1022 CH2 TRP A 129 6530 4891 5153 427 1159 -1276 C ATOM 1023 N GLY A 130 14.638 13.841 7.880 1.00 35.87 N ANISOU 1023 N GLY A 130 4645 4675 4308 833 823 -690 N ATOM 1024 CA GLY A 130 16.074 13.619 7.895 1.00 37.40 C ANISOU 1024 CA GLY A 130 4693 4931 4586 1015 948 -624 C ATOM 1025 C GLY A 130 16.756 14.526 8.894 1.00 36.80 C ANISOU 1025 C GLY A 130 4407 5033 4543 1055 803 -441 C ATOM 1026 O GLY A 130 16.710 14.273 10.099 1.00 36.33 O ANISOU 1026 O GLY A 130 4296 4935 4571 1133 727 -320 O ATOM 1027 N THR A 131 17.394 15.580 8.387 1.00 36.91 N ANISOU 1027 N THR A 131 4305 5248 4471 980 768 -419 N ATOM 1028 CA THR A 131 18.131 16.525 9.226 1.00 36.62 C ANISOU 1028 CA THR A 131 4075 5399 4439 976 640 -260 C ATOM 1029 C THR A 131 17.722 17.965 8.968 1.00 35.20 C ANISOU 1029 C THR A 131 3902 5342 4129 767 495 -268 C ATOM 1030 O THR A 131 18.317 18.891 9.527 1.00 34.92 O ANISOU 1030 O THR A 131 3735 5462 4072 717 396 -160 O ATOM 1031 CB THR A 131 19.657 16.449 9.014 1.00 38.35 C ANISOU 1031 CB THR A 131 4094 5773 4704 1106 751 -178 C ATOM 1032 OG1 THR A 131 20.013 17.185 7.841 1.00 38.93 O ANISOU 1032 OG1 THR A 131 4154 5978 4661 992 797 -255 O ATOM 1033 CG2 THR A 131 20.131 15.018 8.882 1.00 41.10 C ANISOU 1033 CG2 THR A 131 4446 5980 5189 1334 955 -192 C ATOM 1034 N SER A 132 16.721 18.164 8.121 1.00 34.58 N ANISOU 1034 N SER A 132 3978 5196 3964 638 482 -385 N ATOM 1035 CA SER A 132 16.287 19.518 7.817 1.00 33.64 C ANISOU 1035 CA SER A 132 3870 5172 3740 459 354 -373 C ATOM 1036 C SER A 132 14.781 19.621 7.604 1.00 32.67 C ANISOU 1036 C SER A 132 3900 4938 3575 348 275 -436 C ATOM 1037 O SER A 132 14.117 18.608 7.380 1.00 33.19 O ANISOU 1037 O SER A 132 4078 4875 3658 373 337 -521 O ATOM 1038 CB SER A 132 17.022 20.034 6.584 1.00 34.30 C ANISOU 1038 CB SER A 132 3913 5396 3725 389 425 -406 C ATOM 1039 OG SER A 132 16.578 19.337 5.447 1.00 35.24 O ANISOU 1039 OG SER A 132 4160 5445 3783 360 535 -540 O ATOM 1040 N TRP A 133 14.264 20.849 7.699 1.00 31.41 N ANISOU 1040 N TRP A 133 3740 4829 3367 225 145 -386 N ATOM 1041 CA TRP A 133 12.926 21.192 7.235 1.00 30.67 C ANISOU 1041 CA TRP A 133 3752 4680 3222 111 69 -418 C ATOM 1042 C TRP A 133 12.870 21.227 5.702 1.00 31.41 C ANISOU 1042 C TRP A 133 3900 4839 3194 9 119 -484 C ATOM 1043 O TRP A 133 13.814 21.656 5.034 1.00 31.60 O ANISOU 1043 O TRP A 133 3870 4981 3157 -17 168 -476 O ATOM 1044 CB TRP A 133 12.518 22.561 7.771 1.00 29.92 C ANISOU 1044 CB TRP A 133 3629 4610 3130 35 -58 -329 C ATOM 1045 CG TRP A 133 12.587 22.690 9.263 1.00 30.19 C ANISOU 1045 CG TRP A 133 3620 4600 3249 93 -105 -273 C ATOM 1046 CD1 TRP A 133 13.626 23.190 10.000 1.00 31.01 C ANISOU 1046 CD1 TRP A 133 3631 4786 3366 105 -118 -208 C ATOM 1047 CD2 TRP A 133 11.575 22.307 10.203 1.00 28.65 C ANISOU 1047 CD2 TRP A 133 3474 4294 3119 122 -146 -276 C ATOM 1048 NE1 TRP A 133 13.319 23.142 11.342 1.00 29.56 N ANISOU 1048 NE1 TRP A 133 3445 4547 3240 132 -166 -174 N ATOM 1049 CE2 TRP A 133 12.069 22.602 11.493 1.00 28.11 C ANISOU 1049 CE2 TRP A 133 3348 4241 3093 150 -178 -216 C ATOM 1050 CE3 TRP A 133 10.306 21.733 10.080 1.00 27.84 C ANISOU 1050 CE3 TRP A 133 3452 4095 3030 109 -159 -320 C ATOM 1051 CZ2 TRP A 133 11.332 22.362 12.648 1.00 27.52 C ANISOU 1051 CZ2 TRP A 133 3304 4083 3070 169 -214 -206 C ATOM 1052 CZ3 TRP A 133 9.572 21.489 11.234 1.00 27.96 C ANISOU 1052 CZ3 TRP A 133 3486 4027 3111 137 -194 -305 C ATOM 1053 CH2 TRP A 133 10.087 21.806 12.499 1.00 27.81 C ANISOU 1053 CH2 TRP A 133 3417 4019 3129 170 -216 -251 C ATOM 1054 N GLN A 134 11.751 20.772 5.158 1.00 31.45 N ANISOU 1054 N GLN A 134 4011 4786 3152 -65 103 -545 N ATOM 1055 CA GLN A 134 11.520 20.776 3.725 1.00 33.05 C ANISOU 1055 CA GLN A 134 4281 5065 3210 -200 132 -604 C ATOM 1056 C GLN A 134 10.043 21.023 3.474 1.00 32.47 C ANISOU 1056 C GLN A 134 4266 4979 3093 -321 11 -576 C ATOM 1057 O GLN A 134 9.200 20.578 4.268 1.00 31.98 O ANISOU 1057 O GLN A 134 4227 4814 3109 -284 -29 -576 O ATOM 1058 CB GLN A 134 11.936 19.434 3.098 1.00 34.90 C ANISOU 1058 CB GLN A 134 4600 5253 3409 -172 306 -751 C ATOM 1059 CG GLN A 134 11.059 18.237 3.500 1.00 36.42 C ANISOU 1059 CG GLN A 134 4902 5286 3651 -151 337 -831 C ATOM 1060 CD GLN A 134 11.157 17.059 2.534 1.00 40.68 C ANISOU 1060 CD GLN A 134 5580 5769 4107 -201 508 -998 C ATOM 1061 OE1 GLN A 134 10.151 16.390 2.240 1.00 41.77 O ANISOU 1061 OE1 GLN A 134 5845 5839 4187 -314 504 -1077 O ATOM 1062 NE2 GLN A 134 12.365 16.794 2.039 1.00 41.16 N ANISOU 1062 NE2 GLN A 134 5620 5861 4157 -126 671 -1058 N ATOM 1063 N THR A 135 9.718 21.724 2.385 1.00 32.62 N ANISOU 1063 N THR A 135 4295 5114 2984 -467 -48 -537 N ATOM 1064 CA THR A 135 8.311 21.838 1.988 1.00 32.50 C ANISOU 1064 CA THR A 135 4315 5121 2913 -590 -160 -494 C ATOM 1065 C THR A 135 7.864 20.569 1.292 1.00 33.34 C ANISOU 1065 C THR A 135 4537 5215 2915 -691 -86 -633 C ATOM 1066 O THR A 135 8.674 19.848 0.733 1.00 34.50 O ANISOU 1066 O THR A 135 4750 5362 2996 -696 59 -759 O ATOM 1067 CB THR A 135 8.030 23.017 1.062 1.00 32.84 C ANISOU 1067 CB THR A 135 4322 5301 2854 -719 -266 -369 C ATOM 1068 OG1 THR A 135 8.877 22.927 -0.086 1.00 34.81 O ANISOU 1068 OG1 THR A 135 4608 5665 2952 -814 -183 -430 O ATOM 1069 CG2 THR A 135 8.265 24.321 1.779 1.00 31.90 C ANISOU 1069 CG2 THR A 135 4117 5157 2847 -638 -339 -231 C ATOM 1070 N VAL A 136 6.568 20.308 1.337 1.00 33.24 N ANISOU 1070 N VAL A 136 4549 5193 2887 -777 -175 -612 N ATOM 1071 CA VAL A 136 5.979 19.152 0.663 1.00 34.64 C ANISOU 1071 CA VAL A 136 4851 5368 2944 -923 -122 -741 C ATOM 1072 C VAL A 136 5.388 19.570 -0.693 1.00 35.93 C ANISOU 1072 C VAL A 136 5027 5722 2901 -1157 -209 -696 C ATOM 1073 O VAL A 136 5.215 20.760 -0.945 1.00 35.53 O ANISOU 1073 O VAL A 136 4876 5785 2840 -1178 -333 -532 O ATOM 1074 CB VAL A 136 4.917 18.477 1.565 1.00 34.14 C ANISOU 1074 CB VAL A 136 4804 5194 2974 -905 -164 -747 C ATOM 1075 CG1 VAL A 136 5.550 18.039 2.882 1.00 32.71 C ANISOU 1075 CG1 VAL A 136 4614 4839 2976 -690 -81 -777 C ATOM 1076 CG2 VAL A 136 3.747 19.416 1.828 1.00 33.09 C ANISOU 1076 CG2 VAL A 136 4552 5144 2876 -942 -345 -572 C ATOM 1077 N PRO A 137 5.097 18.604 -1.578 1.00 37.82 N ANISOU 1077 N PRO A 137 5400 5998 2971 -1344 -141 -836 N ATOM 1078 CA PRO A 137 4.512 18.955 -2.885 1.00 39.56 C ANISOU 1078 CA PRO A 137 5634 6433 2963 -1602 -236 -785 C ATOM 1079 C PRO A 137 3.241 19.800 -2.787 1.00 39.32 C ANISOU 1079 C PRO A 137 5468 6523 2949 -1664 -460 -564 C ATOM 1080 O PRO A 137 2.398 19.563 -1.916 1.00 38.53 O ANISOU 1080 O PRO A 137 5321 6345 2973 -1604 -519 -524 O ATOM 1081 CB PRO A 137 4.201 17.595 -3.505 1.00 41.15 C ANISOU 1081 CB PRO A 137 6018 6611 3005 -1796 -124 -991 C ATOM 1082 CG PRO A 137 5.244 16.709 -2.960 1.00 41.14 C ANISOU 1082 CG PRO A 137 6114 6394 3122 -1615 96 -1170 C ATOM 1083 CD PRO A 137 5.490 17.184 -1.531 1.00 38.95 C ANISOU 1083 CD PRO A 137 5702 5989 3107 -1335 50 -1053 C ATOM 1084 N GLY A 138 3.138 20.799 -3.662 1.00 40.18 N ANISOU 1084 N GLY A 138 5504 6819 2942 -1773 -574 -409 N ATOM 1085 CA GLY A 138 1.980 21.686 -3.696 1.00 40.30 C ANISOU 1085 CA GLY A 138 5372 6960 2979 -1817 -781 -164 C ATOM 1086 C GLY A 138 2.088 22.952 -2.861 1.00 38.62 C ANISOU 1086 C GLY A 138 5020 6668 2985 -1590 -848 20 C ATOM 1087 O GLY A 138 1.232 23.833 -2.966 1.00 39.34 O ANISOU 1087 O GLY A 138 4984 6851 3112 -1598 -999 243 O ATOM 1088 N ALA A 139 3.125 23.036 -2.029 1.00 36.69 N ANISOU 1088 N ALA A 139 4798 6255 2886 -1392 -731 -65 N ATOM 1089 CA ALA A 139 3.360 24.191 -1.165 1.00 34.87 C ANISOU 1089 CA ALA A 139 4470 5928 2850 -1198 -767 72 C ATOM 1090 C ALA A 139 3.739 25.392 -2.004 1.00 35.52 C ANISOU 1090 C ALA A 139 4511 6123 2862 -1254 -832 230 C ATOM 1091 O ALA A 139 4.216 25.225 -3.131 1.00 37.10 O ANISOU 1091 O ALA A 139 4771 6459 2866 -1414 -808 189 O ATOM 1092 CB ALA A 139 4.464 23.883 -0.185 1.00 33.44 C ANISOU 1092 CB ALA A 139 4330 5581 2794 -1026 -629 -65 C ATOM 1093 N PRO A 140 3.535 26.610 -1.474 1.00 34.78 N ANISOU 1093 N PRO A 140 4328 5964 2922 -1132 -902 409 N ATOM 1094 CA PRO A 140 3.894 27.775 -2.271 1.00 35.55 C ANISOU 1094 CA PRO A 140 4400 6147 2961 -1189 -961 576 C ATOM 1095 C PRO A 140 5.381 28.113 -2.172 1.00 34.45 C ANISOU 1095 C PRO A 140 4314 5954 2821 -1145 -851 491 C ATOM 1096 O PRO A 140 5.983 27.984 -1.114 1.00 33.15 O ANISOU 1096 O PRO A 140 4161 5646 2790 -1003 -764 388 O ATOM 1097 CB PRO A 140 3.034 28.903 -1.666 1.00 35.43 C ANISOU 1097 CB PRO A 140 4281 6044 3135 -1061 -1056 796 C ATOM 1098 CG PRO A 140 2.176 28.278 -0.633 1.00 34.31 C ANISOU 1098 CG PRO A 140 4101 5807 3129 -957 -1047 736 C ATOM 1099 CD PRO A 140 2.852 27.009 -0.238 1.00 33.84 C ANISOU 1099 CD PRO A 140 4136 5699 3023 -961 -928 480 C ATOM 1100 N SER A 141 5.951 28.579 -3.270 1.00 35.22 N ANISOU 1100 N SER A 141 4434 6186 2761 -1280 -862 550 N ATOM 1101 CA SER A 141 7.379 28.844 -3.339 1.00 34.69 C ANISOU 1101 CA SER A 141 4404 6113 2663 -1272 -754 472 C ATOM 1102 C SER A 141 7.889 29.795 -2.278 1.00 33.33 C ANISOU 1102 C SER A 141 4202 5780 2682 -1122 -736 530 C ATOM 1103 O SER A 141 9.051 29.708 -1.880 1.00 32.86 O ANISOU 1103 O SER A 141 4156 5691 2640 -1078 -632 421 O ATOM 1104 CB SER A 141 7.720 29.399 -4.702 1.00 36.12 C ANISOU 1104 CB SER A 141 4603 6475 2645 -1457 -790 574 C ATOM 1105 OG SER A 141 7.192 28.539 -5.690 1.00 38.25 O ANISOU 1105 OG SER A 141 4913 6907 2713 -1629 -809 517 O ATOM 1106 N TRP A 142 7.023 30.696 -1.818 1.00 32.95 N ANISOU 1106 N TRP A 142 4111 5634 2774 -1049 -830 701 N ATOM 1107 CA TRP A 142 7.455 31.768 -0.931 1.00 31.69 C ANISOU 1107 CA TRP A 142 3951 5314 2775 -945 -808 764 C ATOM 1108 C TRP A 142 7.989 31.215 0.375 1.00 29.59 C ANISOU 1108 C TRP A 142 3695 4927 2621 -822 -712 591 C ATOM 1109 O TRP A 142 8.846 31.832 1.004 1.00 28.42 O ANISOU 1109 O TRP A 142 3562 4702 2535 -791 -661 576 O ATOM 1110 CB TRP A 142 6.356 32.817 -0.717 1.00 32.30 C ANISOU 1110 CB TRP A 142 3992 5286 2995 -877 -899 977 C ATOM 1111 CG TRP A 142 5.124 32.318 -0.064 1.00 32.62 C ANISOU 1111 CG TRP A 142 3979 5267 3149 -774 -932 976 C ATOM 1112 CD1 TRP A 142 3.962 31.964 -0.680 1.00 34.24 C ANISOU 1112 CD1 TRP A 142 4118 5585 3308 -819 -1030 1079 C ATOM 1113 CD2 TRP A 142 4.911 32.128 1.342 1.00 32.59 C ANISOU 1113 CD2 TRP A 142 3974 5096 3314 -627 -869 877 C ATOM 1114 NE1 TRP A 142 3.036 31.556 0.253 1.00 33.72 N ANISOU 1114 NE1 TRP A 142 4002 5431 3380 -702 -1027 1048 N ATOM 1115 CE2 TRP A 142 3.593 31.645 1.502 1.00 32.70 C ANISOU 1115 CE2 TRP A 142 3917 5124 3382 -581 -925 921 C ATOM 1116 CE3 TRP A 142 5.710 32.308 2.483 1.00 32.64 C ANISOU 1116 CE3 TRP A 142 4027 4962 3413 -549 -775 759 C ATOM 1117 CZ2 TRP A 142 3.049 31.339 2.756 1.00 32.27 C ANISOU 1117 CZ2 TRP A 142 3844 4940 3477 -453 -878 846 C ATOM 1118 CZ3 TRP A 142 5.164 32.009 3.736 1.00 32.53 C ANISOU 1118 CZ3 TRP A 142 4002 4821 3537 -429 -736 687 C ATOM 1119 CH2 TRP A 142 3.843 31.530 3.857 1.00 31.54 C ANISOU 1119 CH2 TRP A 142 3812 4704 3467 -378 -782 728 C ATOM 1120 N LEU A 143 7.504 30.024 0.734 1.00 28.73 N ANISOU 1120 N LEU A 143 3579 4817 2519 -776 -691 468 N ATOM 1121 CA LEU A 143 7.926 29.314 1.941 1.00 27.53 C ANISOU 1121 CA LEU A 143 3432 4566 2461 -663 -609 317 C ATOM 1122 C LEU A 143 9.412 28.918 1.929 1.00 27.62 C ANISOU 1122 C LEU A 143 3453 4634 2409 -673 -507 199 C ATOM 1123 O LEU A 143 9.973 28.541 2.962 1.00 26.55 O ANISOU 1123 O LEU A 143 3304 4431 2352 -582 -447 114 O ATOM 1124 CB LEU A 143 7.070 28.070 2.145 1.00 27.02 C ANISOU 1124 CB LEU A 143 3371 4496 2401 -636 -609 226 C ATOM 1125 CG LEU A 143 5.683 28.180 2.779 1.00 27.39 C ANISOU 1125 CG LEU A 143 3381 4461 2566 -572 -677 300 C ATOM 1126 CD1 LEU A 143 4.945 26.852 2.642 1.00 26.70 C ANISOU 1126 CD1 LEU A 143 3304 4414 2425 -607 -678 206 C ATOM 1127 CD2 LEU A 143 5.769 28.584 4.247 1.00 26.70 C ANISOU 1127 CD2 LEU A 143 3286 4214 2643 -440 -638 282 C ATOM 1128 N ASP A 144 10.049 29.017 0.766 1.00 28.89 N ANISOU 1128 N ASP A 144 3623 4932 2421 -788 -486 207 N ATOM 1129 CA ASP A 144 11.448 28.658 0.640 1.00 29.44 C ANISOU 1129 CA ASP A 144 3678 5079 2430 -795 -377 108 C ATOM 1130 C ASP A 144 12.350 29.528 1.494 1.00 28.75 C ANISOU 1130 C ASP A 144 3552 4946 2425 -760 -363 149 C ATOM 1131 O ASP A 144 13.391 29.063 1.952 1.00 28.77 O ANISOU 1131 O ASP A 144 3509 4984 2438 -711 -279 67 O ATOM 1132 CB ASP A 144 11.904 28.703 -0.819 1.00 31.33 C ANISOU 1132 CB ASP A 144 3936 5486 2482 -943 -349 114 C ATOM 1133 CG ASP A 144 11.466 27.481 -1.612 1.00 33.88 C ANISOU 1133 CG ASP A 144 4309 5877 2686 -996 -302 -3 C ATOM 1134 OD1 ASP A 144 11.281 26.387 -1.028 1.00 36.06 O ANISOU 1134 OD1 ASP A 144 4603 6074 3026 -901 -242 -128 O ATOM 1135 OD2 ASP A 144 11.309 27.613 -2.841 1.00 38.14 O ANISOU 1135 OD2 ASP A 144 4883 6551 3057 -1152 -322 30 O ATOM 1136 N LEU A 145 11.959 30.785 1.702 1.00 28.63 N ANISOU 1136 N LEU A 145 3556 4853 2468 -790 -439 281 N ATOM 1137 CA LEU A 145 12.725 31.686 2.571 1.00 28.00 C ANISOU 1137 CA LEU A 145 3468 4711 2458 -791 -425 312 C ATOM 1138 C LEU A 145 12.558 31.345 4.060 1.00 26.64 C ANISOU 1138 C LEU A 145 3286 4419 2416 -676 -411 243 C ATOM 1139 O LEU A 145 13.546 31.264 4.777 1.00 26.31 O ANISOU 1139 O LEU A 145 3205 4409 2383 -669 -366 194 O ATOM 1140 CB LEU A 145 12.410 33.151 2.276 1.00 28.56 C ANISOU 1140 CB LEU A 145 3591 4710 2551 -870 -486 467 C ATOM 1141 CG LEU A 145 13.120 34.235 3.086 1.00 28.80 C ANISOU 1141 CG LEU A 145 3651 4654 2639 -915 -466 499 C ATOM 1142 CD1 LEU A 145 14.636 34.046 3.148 1.00 29.34 C ANISOU 1142 CD1 LEU A 145 3659 4869 2621 -987 -403 432 C ATOM 1143 CD2 LEU A 145 12.778 35.590 2.517 1.00 29.98 C ANISOU 1143 CD2 LEU A 145 3871 4719 2800 -997 -511 661 C ATOM 1144 N PRO A 146 11.315 31.132 4.528 1.00 26.07 N ANISOU 1144 N PRO A 146 3240 4230 2435 -595 -450 249 N ATOM 1145 CA PRO A 146 11.129 30.548 5.856 1.00 25.40 C ANISOU 1145 CA PRO A 146 3146 4058 2445 -494 -427 169 C ATOM 1146 C PRO A 146 11.966 29.286 6.095 1.00 25.66 C ANISOU 1146 C PRO A 146 3128 4178 2444 -443 -364 59 C ATOM 1147 O PRO A 146 12.608 29.155 7.151 1.00 25.49 O ANISOU 1147 O PRO A 146 3075 4147 2463 -407 -338 26 O ATOM 1148 CB PRO A 146 9.652 30.198 5.861 1.00 24.69 C ANISOU 1148 CB PRO A 146 3073 3891 2417 -433 -471 187 C ATOM 1149 CG PRO A 146 9.038 31.248 5.039 1.00 25.79 C ANISOU 1149 CG PRO A 146 3232 4014 2554 -488 -529 324 C ATOM 1150 CD PRO A 146 10.057 31.697 4.022 1.00 26.38 C ANISOU 1150 CD PRO A 146 3308 4206 2508 -600 -522 362 C ATOM 1151 N ILE A 147 11.965 28.380 5.117 1.00 26.35 N ANISOU 1151 N ILE A 147 3210 4349 2453 -446 -334 10 N ATOM 1152 CA ILE A 147 12.712 27.129 5.220 1.00 26.57 C ANISOU 1152 CA ILE A 147 3199 4430 2465 -376 -247 -91 C ATOM 1153 C ILE A 147 14.220 27.371 5.219 1.00 27.55 C ANISOU 1153 C ILE A 147 3246 4672 2551 -395 -188 -84 C ATOM 1154 O ILE A 147 14.945 26.706 5.958 1.00 27.72 O ANISOU 1154 O ILE A 147 3201 4713 2617 -308 -137 -118 O ATOM 1155 CB ILE A 147 12.288 26.095 4.137 1.00 26.94 C ANISOU 1155 CB ILE A 147 3290 4515 2432 -392 -202 -167 C ATOM 1156 CG1 ILE A 147 11.145 25.206 4.639 1.00 26.30 C ANISOU 1156 CG1 ILE A 147 3256 4323 2414 -331 -222 -216 C ATOM 1157 CG2 ILE A 147 13.410 25.157 3.829 1.00 27.51 C ANISOU 1157 CG2 ILE A 147 3327 4661 2466 -343 -75 -257 C ATOM 1158 CD1 ILE A 147 10.098 25.890 5.522 1.00 24.83 C ANISOU 1158 CD1 ILE A 147 3074 4034 2325 -311 -316 -140 C ATOM 1159 N LYS A 148 14.691 28.331 4.424 1.00 28.62 N ANISOU 1159 N LYS A 148 3377 4894 2605 -511 -200 -24 N ATOM 1160 CA LYS A 148 16.125 28.653 4.402 1.00 30.14 C ANISOU 1160 CA LYS A 148 3479 5220 2752 -553 -148 -6 C ATOM 1161 C LYS A 148 16.600 29.165 5.765 1.00 30.07 C ANISOU 1161 C LYS A 148 3425 5185 2815 -548 -183 31 C ATOM 1162 O LYS A 148 17.751 28.943 6.163 1.00 30.78 O ANISOU 1162 O LYS A 148 3405 5393 2897 -535 -141 35 O ATOM 1163 CB LYS A 148 16.461 29.668 3.305 1.00 31.16 C ANISOU 1163 CB LYS A 148 3625 5442 2772 -705 -161 62 C ATOM 1164 CG LYS A 148 17.887 30.220 3.402 1.00 33.56 C ANISOU 1164 CG LYS A 148 3833 5888 3031 -782 -122 99 C ATOM 1165 CD LYS A 148 18.362 30.894 2.132 1.00 36.54 C ANISOU 1165 CD LYS A 148 4216 6391 3278 -929 -102 149 C ATOM 1166 CE LYS A 148 18.849 29.877 1.133 1.00 39.29 C ANISOU 1166 CE LYS A 148 4516 6876 3538 -898 14 65 C ATOM 1167 NZ LYS A 148 18.566 30.357 -0.254 1.00 42.23 N ANISOU 1167 NZ LYS A 148 4960 7317 3769 -1042 5 102 N ATOM 1168 N VAL A 149 15.693 29.828 6.475 1.00 29.45 N ANISOU 1168 N VAL A 149 3426 4960 2802 -562 -256 62 N ATOM 1169 CA VAL A 149 16.001 30.449 7.742 1.00 29.35 C ANISOU 1169 CA VAL A 149 3408 4908 2834 -597 -285 84 C ATOM 1170 C VAL A 149 15.991 29.392 8.826 1.00 29.31 C ANISOU 1170 C VAL A 149 3355 4889 2891 -478 -273 37 C ATOM 1171 O VAL A 149 16.915 29.308 9.640 1.00 30.04 O ANISOU 1171 O VAL A 149 3364 5074 2977 -492 -270 54 O ATOM 1172 CB VAL A 149 14.989 31.565 8.071 1.00 28.84 C ANISOU 1172 CB VAL A 149 3465 4671 2823 -649 -335 123 C ATOM 1173 CG1 VAL A 149 15.214 32.102 9.458 1.00 28.32 C ANISOU 1173 CG1 VAL A 149 3422 4547 2792 -696 -344 114 C ATOM 1174 CG2 VAL A 149 15.110 32.695 7.070 1.00 29.27 C ANISOU 1174 CG2 VAL A 149 3568 4730 2823 -770 -349 201 C ATOM 1175 N LEU A 150 14.938 28.581 8.839 1.00 28.98 N ANISOU 1175 N LEU A 150 3362 4744 2905 -373 -273 -7 N ATOM 1176 CA LEU A 150 14.800 27.546 9.864 1.00 28.09 C ANISOU 1176 CA LEU A 150 3222 4596 2855 -263 -263 -42 C ATOM 1177 C LEU A 150 15.940 26.537 9.762 1.00 28.81 C ANISOU 1177 C LEU A 150 3197 4814 2934 -183 -198 -48 C ATOM 1178 O LEU A 150 16.414 26.025 10.784 1.00 29.43 O ANISOU 1178 O LEU A 150 3207 4925 3051 -124 -200 -24 O ATOM 1179 CB LEU A 150 13.441 26.858 9.784 1.00 27.10 C ANISOU 1179 CB LEU A 150 3173 4341 2783 -187 -270 -87 C ATOM 1180 CG LEU A 150 12.210 27.735 10.019 1.00 25.76 C ANISOU 1180 CG LEU A 150 3088 4045 2655 -228 -323 -66 C ATOM 1181 CD1 LEU A 150 10.959 27.017 9.521 1.00 24.75 C ANISOU 1181 CD1 LEU A 150 3002 3848 2552 -176 -332 -94 C ATOM 1182 CD2 LEU A 150 12.074 28.124 11.489 1.00 24.54 C ANISOU 1182 CD2 LEU A 150 2952 3821 2550 -234 -339 -64 C ATOM 1183 N ASN A 151 16.408 26.277 8.545 1.00 28.92 N ANISOU 1183 N ASN A 151 3183 4909 2895 -181 -135 -69 N ATOM 1184 CA ASN A 151 17.502 25.338 8.392 1.00 29.68 C ANISOU 1184 CA ASN A 151 3163 5116 2998 -83 -43 -74 C ATOM 1185 C ASN A 151 18.821 25.980 8.704 1.00 30.47 C ANISOU 1185 C ASN A 151 3126 5391 3062 -147 -50 5 C ATOM 1186 O ASN A 151 19.800 25.276 8.879 1.00 31.98 O ANISOU 1186 O ASN A 151 3179 5692 3279 -52 13 36 O ATOM 1187 CB ASN A 151 17.527 24.681 7.011 1.00 30.30 C ANISOU 1187 CB ASN A 151 3270 5213 3030 -53 59 -149 C ATOM 1188 CG ASN A 151 16.353 23.753 6.789 1.00 29.68 C ANISOU 1188 CG ASN A 151 3313 4981 2982 6 78 -234 C ATOM 1189 OD1 ASN A 151 15.817 23.149 7.732 1.00 30.37 O ANISOU 1189 OD1 ASN A 151 3427 4960 3154 88 53 -237 O ATOM 1190 ND2 ASN A 151 15.926 23.651 5.545 1.00 28.88 N ANISOU 1190 ND2 ASN A 151 3291 4883 2799 -57 117 -298 N ATOM 1191 N ALA A 152 18.846 27.310 8.789 1.00 30.19 N ANISOU 1191 N ALA A 152 3122 5377 2970 -310 -122 46 N ATOM 1192 CA ALA A 152 20.056 28.033 9.205 1.00 30.68 C ANISOU 1192 CA ALA A 152 3065 5611 2981 -420 -144 123 C ATOM 1193 C ALA A 152 20.418 27.624 10.617 1.00 30.96 C ANISOU 1193 C ALA A 152 3015 5688 3060 -375 -185 173 C ATOM 1194 O ALA A 152 21.590 27.555 10.977 1.00 31.81 O ANISOU 1194 O ALA A 152 2957 5986 3144 -393 -182 250 O ATOM 1195 CB ALA A 152 19.841 29.532 9.140 1.00 30.02 C ANISOU 1195 CB ALA A 152 3080 5488 2837 -615 -208 147 C ATOM 1196 N ASP A 153 19.382 27.313 11.392 1.00 30.44 N ANISOU 1196 N ASP A 153 3053 5459 3054 -320 -225 138 N ATOM 1197 CA ASP A 153 19.481 27.098 12.819 1.00 30.76 C ANISOU 1197 CA ASP A 153 3054 5518 3115 -318 -281 183 C ATOM 1198 C ASP A 153 19.904 25.673 13.175 1.00 31.54 C ANISOU 1198 C ASP A 153 3031 5668 3285 -130 -241 228 C ATOM 1199 O ASP A 153 19.063 24.823 13.446 1.00 31.05 O ANISOU 1199 O ASP A 153 3043 5461 3294 -11 -228 190 O ATOM 1200 CB ASP A 153 18.134 27.432 13.442 1.00 29.64 C ANISOU 1200 CB ASP A 153 3083 5177 3003 -346 -324 124 C ATOM 1201 CG ASP A 153 18.155 27.384 14.947 1.00 30.72 C ANISOU 1201 CG ASP A 153 3208 5332 3131 -389 -380 158 C ATOM 1202 OD1 ASP A 153 19.206 27.038 15.524 1.00 31.29 O ANISOU 1202 OD1 ASP A 153 3133 5583 3174 -395 -404 245 O ATOM 1203 OD2 ASP A 153 17.101 27.688 15.551 1.00 32.11 O ANISOU 1203 OD2 ASP A 153 3518 5356 3327 -419 -399 105 O ATOM 1204 N GLN A 154 21.214 25.438 13.200 1.00 33.37 N ANISOU 1204 N GLN A 154 3070 6107 3503 -106 -221 322 N ATOM 1205 CA GLN A 154 21.785 24.135 13.517 1.00 34.94 C ANISOU 1205 CA GLN A 154 3125 6364 3787 91 -170 399 C ATOM 1206 C GLN A 154 21.273 23.573 14.851 1.00 34.70 C ANISOU 1206 C GLN A 154 3124 6261 3800 138 -239 447 C ATOM 1207 O GLN A 154 20.784 22.449 14.894 1.00 34.68 O ANISOU 1207 O GLN A 154 3161 6123 3891 312 -187 432 O ATOM 1208 CB GLN A 154 23.313 24.206 13.514 1.00 37.10 C ANISOU 1208 CB GLN A 154 3153 6910 4035 84 -157 529 C ATOM 1209 CG GLN A 154 23.938 24.659 12.188 1.00 40.27 C ANISOU 1209 CG GLN A 154 3502 7410 4389 42 -70 491 C ATOM 1210 CD GLN A 154 25.231 25.481 12.382 1.00 45.27 C ANISOU 1210 CD GLN A 154 3938 8330 4933 -116 -117 609 C ATOM 1211 OE1 GLN A 154 25.210 26.632 12.864 1.00 44.98 O ANISOU 1211 OE1 GLN A 154 3957 8341 4793 -353 -222 617 O ATOM 1212 NE2 GLN A 154 26.358 24.889 11.999 1.00 48.48 N ANISOU 1212 NE2 GLN A 154 4115 8926 5380 7 -28 699 N ATOM 1213 N GLY A 155 21.372 24.354 15.929 1.00 34.85 N ANISOU 1213 N GLY A 155 3137 6366 3738 -33 -350 500 N ATOM 1214 CA GLY A 155 20.898 23.928 17.249 1.00 34.61 C ANISOU 1214 CA GLY A 155 3140 6293 3717 -27 -419 547 C ATOM 1215 C GLY A 155 19.485 23.343 17.280 1.00 33.48 C ANISOU 1215 C GLY A 155 3182 5891 3646 66 -390 443 C ATOM 1216 O GLY A 155 19.231 22.335 17.957 1.00 33.62 O ANISOU 1216 O GLY A 155 3192 5855 3726 184 -393 497 O ATOM 1217 N THR A 156 18.557 23.968 16.554 1.00 32.20 N ANISOU 1217 N THR A 156 3181 5578 3477 10 -364 310 N ATOM 1218 CA THR A 156 17.194 23.475 16.520 1.00 30.95 C ANISOU 1218 CA THR A 156 3177 5203 3379 80 -341 220 C ATOM 1219 C THR A 156 17.189 22.128 15.827 1.00 31.79 C ANISOU 1219 C THR A 156 3263 5238 3578 276 -254 211 C ATOM 1220 O THR A 156 16.533 21.199 16.282 1.00 31.82 O ANISOU 1220 O THR A 156 3326 5122 3644 367 -241 207 O ATOM 1221 CB THR A 156 16.233 24.469 15.845 1.00 29.82 C ANISOU 1221 CB THR A 156 3178 4939 3212 -17 -339 112 C ATOM 1222 OG1 THR A 156 16.106 25.619 16.683 1.00 29.22 O ANISOU 1222 OG1 THR A 156 3155 4877 3072 -184 -395 109 O ATOM 1223 CG2 THR A 156 14.830 23.856 15.632 1.00 27.69 C ANISOU 1223 CG2 THR A 156 3035 4478 3008 61 -313 33 C ATOM 1224 N SER A 157 17.953 22.019 14.746 1.00 32.82 N ANISOU 1224 N SER A 157 3319 5440 3713 330 -181 206 N ATOM 1225 CA SER A 157 18.031 20.776 13.994 1.00 33.75 C ANISOU 1225 CA SER A 157 3434 5477 3912 507 -65 175 C ATOM 1226 C SER A 157 18.459 19.607 14.889 1.00 34.57 C ANISOU 1226 C SER A 157 3454 5575 4107 665 -46 286 C ATOM 1227 O SER A 157 17.759 18.599 14.963 1.00 34.69 O ANISOU 1227 O SER A 157 3568 5416 4195 768 2 249 O ATOM 1228 CB SER A 157 18.964 20.924 12.784 1.00 34.78 C ANISOU 1228 CB SER A 157 3478 5719 4019 528 26 157 C ATOM 1229 OG SER A 157 18.738 19.881 11.848 1.00 36.65 O ANISOU 1229 OG SER A 157 3782 5832 4311 657 160 68 O ATOM 1230 N ALA A 158 19.588 19.756 15.577 1.00 35.44 N ANISOU 1230 N ALA A 158 3379 5878 4208 673 -90 435 N ATOM 1231 CA ALA A 158 20.105 18.708 16.448 1.00 36.68 C ANISOU 1231 CA ALA A 158 3423 6061 4454 828 -86 587 C ATOM 1232 C ALA A 158 19.059 18.283 17.452 1.00 35.88 C ANISOU 1232 C ALA A 158 3452 5814 4367 812 -150 588 C ATOM 1233 O ALA A 158 18.865 17.095 17.674 1.00 36.76 O ANISOU 1233 O ALA A 158 3591 5795 4581 970 -93 631 O ATOM 1234 CB ALA A 158 21.362 19.170 17.160 1.00 38.04 C ANISOU 1234 CB ALA A 158 3365 6509 4578 778 -168 768 C ATOM 1235 N THR A 159 18.377 19.264 18.034 1.00 34.68 N ANISOU 1235 N THR A 159 3388 5674 4113 618 -254 537 N ATOM 1236 CA THR A 159 17.349 19.034 19.046 1.00 34.00 C ANISOU 1236 CA THR A 159 3422 5477 4019 570 -313 529 C ATOM 1237 C THR A 159 16.150 18.276 18.482 1.00 33.14 C ANISOU 1237 C THR A 159 3485 5125 3983 647 -236 404 C ATOM 1238 O THR A 159 15.645 17.361 19.112 1.00 33.64 O ANISOU 1238 O THR A 159 3603 5079 4099 714 -232 443 O ATOM 1239 CB THR A 159 16.871 20.374 19.665 1.00 33.03 C ANISOU 1239 CB THR A 159 3368 5408 3773 342 -405 473 C ATOM 1240 OG1 THR A 159 18.000 21.211 19.929 1.00 34.72 O ANISOU 1240 OG1 THR A 159 3445 5848 3899 227 -465 557 O ATOM 1241 CG2 THR A 159 16.108 20.153 20.962 1.00 32.43 C ANISOU 1241 CG2 THR A 159 3369 5283 3669 281 -464 499 C ATOM 1242 N VAL A 160 15.694 18.664 17.299 1.00 32.62 N ANISOU 1242 N VAL A 160 3501 4986 3906 618 -183 266 N ATOM 1243 CA VAL A 160 14.538 18.028 16.673 1.00 32.31 C ANISOU 1243 CA VAL A 160 3618 4749 3910 650 -122 145 C ATOM 1244 C VAL A 160 14.848 16.584 16.225 1.00 34.51 C ANISOU 1244 C VAL A 160 3908 4915 4290 828 -3 154 C ATOM 1245 O VAL A 160 13.998 15.686 16.366 1.00 34.66 O ANISOU 1245 O VAL A 160 4047 4764 4357 863 31 114 O ATOM 1246 CB VAL A 160 13.999 18.873 15.507 1.00 31.01 C ANISOU 1246 CB VAL A 160 3524 4568 3689 553 -111 19 C ATOM 1247 CG1 VAL A 160 12.883 18.157 14.784 1.00 29.67 C ANISOU 1247 CG1 VAL A 160 3495 4233 3545 565 -55 -91 C ATOM 1248 CG2 VAL A 160 13.511 20.203 16.029 1.00 29.69 C ANISOU 1248 CG2 VAL A 160 3377 4450 3452 400 -206 11 C ATOM 1249 N GLN A 161 16.056 16.366 15.702 1.00 36.28 N ANISOU 1249 N GLN A 161 4010 5226 4549 937 71 205 N ATOM 1250 CA GLN A 161 16.490 15.024 15.332 1.00 38.59 C ANISOU 1250 CA GLN A 161 4307 5400 4957 1130 213 222 C ATOM 1251 C GLN A 161 16.510 14.128 16.555 1.00 40.18 C ANISOU 1251 C GLN A 161 4486 5537 5243 1233 187 368 C ATOM 1252 O GLN A 161 16.086 12.976 16.481 1.00 41.34 O ANISOU 1252 O GLN A 161 4748 5480 5479 1335 281 343 O ATOM 1253 CB GLN A 161 17.871 15.026 14.689 1.00 40.04 C ANISOU 1253 CB GLN A 161 4326 5715 5173 1244 306 275 C ATOM 1254 CG GLN A 161 17.927 15.603 13.304 1.00 39.21 C ANISOU 1254 CG GLN A 161 4258 5647 4994 1169 377 128 C ATOM 1255 CD GLN A 161 19.345 15.678 12.793 1.00 40.11 C ANISOU 1255 CD GLN A 161 4185 5923 5132 1269 468 195 C ATOM 1256 OE1 GLN A 161 20.032 14.659 12.688 1.00 41.28 O ANISOU 1256 OE1 GLN A 161 4268 6016 5399 1472 608 248 O ATOM 1257 NE2 GLN A 161 19.797 16.890 12.474 1.00 38.77 N ANISOU 1257 NE2 GLN A 161 3924 5950 4857 1131 399 199 N ATOM 1258 N MET A 162 16.994 14.647 17.679 1.00 40.84 N ANISOU 1258 N MET A 162 4435 5793 5288 1188 60 524 N ATOM 1259 CA MET A 162 16.954 13.869 18.909 1.00 42.56 C ANISOU 1259 CA MET A 162 4634 5975 5561 1255 12 682 C ATOM 1260 C MET A 162 15.522 13.528 19.318 1.00 40.94 C ANISOU 1260 C MET A 162 4628 5586 5341 1169 -12 593 C ATOM 1261 O MET A 162 15.244 12.368 19.612 1.00 41.94 O ANISOU 1261 O MET A 162 4829 5545 5561 1278 45 643 O ATOM 1262 CB MET A 162 17.698 14.553 20.053 1.00 43.67 C ANISOU 1262 CB MET A 162 4600 6369 5625 1174 -132 862 C ATOM 1263 CG MET A 162 17.889 13.639 21.263 1.00 47.77 C ANISOU 1263 CG MET A 162 5063 6885 6201 1264 -179 1072 C ATOM 1264 SD MET A 162 19.118 14.231 22.437 1.00 54.44 S ANISOU 1264 SD MET A 162 5649 8079 6955 1191 -337 1329 S ATOM 1265 CE MET A 162 18.252 15.654 23.130 1.00 51.21 C ANISOU 1265 CE MET A 162 5357 7763 6338 862 -473 1195 C ATOM 1266 N LEU A 163 14.625 14.519 19.309 1.00 38.76 N ANISOU 1266 N LEU A 163 4434 5335 4957 982 -86 469 N ATOM 1267 CA LEU A 163 13.204 14.310 19.655 1.00 37.64 C ANISOU 1267 CA LEU A 163 4457 5047 4796 889 -106 383 C ATOM 1268 C LEU A 163 12.558 13.168 18.887 1.00 37.81 C ANISOU 1268 C LEU A 163 4624 4841 4900 966 11 287 C ATOM 1269 O LEU A 163 12.000 12.252 19.476 1.00 38.20 O ANISOU 1269 O LEU A 163 4761 4756 4996 990 25 326 O ATOM 1270 CB LEU A 163 12.379 15.577 19.426 1.00 35.90 C ANISOU 1270 CB LEU A 163 4288 4875 4476 713 -166 254 C ATOM 1271 CG LEU A 163 12.512 16.743 20.414 1.00 36.43 C ANISOU 1271 CG LEU A 163 4293 5104 4446 576 -273 303 C ATOM 1272 CD1 LEU A 163 11.271 17.609 20.336 1.00 34.72 C ANISOU 1272 CD1 LEU A 163 4178 4837 4177 441 -295 174 C ATOM 1273 CD2 LEU A 163 12.740 16.279 21.865 1.00 37.79 C ANISOU 1273 CD2 LEU A 163 4423 5334 4601 571 -335 452 C ATOM 1274 N LEU A 164 12.669 13.233 17.565 1.00 37.74 N ANISOU 1274 N LEU A 164 4649 4796 4894 984 97 163 N ATOM 1275 CA LEU A 164 12.070 12.266 16.667 1.00 37.75 C ANISOU 1275 CA LEU A 164 4807 4597 4940 1012 218 38 C ATOM 1276 C LEU A 164 12.806 10.921 16.679 1.00 40.42 C ANISOU 1276 C LEU A 164 5159 4790 5409 1208 352 111 C ATOM 1277 O LEU A 164 12.174 9.881 16.851 1.00 41.59 O ANISOU 1277 O LEU A 164 5450 4738 5614 1227 413 91 O ATOM 1278 CB LEU A 164 12.008 12.847 15.250 1.00 36.97 C ANISOU 1278 CB LEU A 164 4736 4536 4774 942 264 -112 C ATOM 1279 CG LEU A 164 11.390 14.231 15.005 1.00 33.37 C ANISOU 1279 CG LEU A 164 4260 4212 4208 774 151 -170 C ATOM 1280 CD1 LEU A 164 11.283 14.508 13.527 1.00 32.29 C ANISOU 1280 CD1 LEU A 164 4173 4087 4009 713 210 -301 C ATOM 1281 CD2 LEU A 164 10.021 14.340 15.613 1.00 32.52 C ANISOU 1281 CD2 LEU A 164 4234 4049 4072 657 72 -194 C ATOM 1282 N ASN A 165 14.129 10.931 16.510 1.00 41.70 N ANISOU 1282 N ASN A 165 5172 5045 5628 1357 407 203 N ATOM 1283 CA ASN A 165 14.890 9.675 16.438 1.00 44.24 C ANISOU 1283 CA ASN A 165 5492 5218 6101 1580 562 282 C ATOM 1284 C ASN A 165 14.960 8.906 17.760 1.00 44.84 C ANISOU 1284 C ASN A 165 5541 5228 6267 1678 516 486 C ATOM 1285 O ASN A 165 14.813 7.689 17.773 1.00 46.72 O ANISOU 1285 O ASN A 165 5901 5229 6622 1795 638 503 O ATOM 1286 CB ASN A 165 16.322 9.891 15.906 1.00 46.15 C ANISOU 1286 CB ASN A 165 5546 5598 6390 1731 644 347 C ATOM 1287 CG ASN A 165 16.362 10.387 14.470 1.00 47.14 C ANISOU 1287 CG ASN A 165 5717 5754 6439 1659 735 148 C ATOM 1288 OD1 ASN A 165 15.333 10.699 13.881 1.00 47.07 O ANISOU 1288 OD1 ASN A 165 5863 5693 6330 1485 710 -21 O ATOM 1289 ND2 ASN A 165 17.569 10.462 13.905 1.00 51.54 N ANISOU 1289 ND2 ASN A 165 6126 6417 7041 1791 839 186 N ATOM 1290 N ASP A 166 15.194 9.606 18.865 1.00 43.44 N ANISOU 1290 N ASP A 166 5219 5257 6029 1617 347 643 N ATOM 1291 CA ASP A 166 15.463 8.931 20.130 1.00 44.02 C ANISOU 1291 CA ASP A 166 5231 5321 6172 1709 291 875 C ATOM 1292 C ASP A 166 14.380 9.095 21.188 1.00 42.21 C ANISOU 1292 C ASP A 166 5095 5092 5850 1532 157 890 C ATOM 1293 O ASP A 166 13.912 8.106 21.751 1.00 43.13 O ANISOU 1293 O ASP A 166 5318 5035 6034 1573 184 963 O ATOM 1294 CB ASP A 166 16.811 9.373 20.687 1.00 45.13 C ANISOU 1294 CB ASP A 166 5105 5724 6320 1796 215 1096 C ATOM 1295 CG ASP A 166 17.938 9.086 19.741 1.00 47.80 C ANISOU 1295 CG ASP A 166 5324 6069 6770 1999 365 1113 C ATOM 1296 OD1 ASP A 166 17.790 8.154 18.923 1.00 50.27 O ANISOU 1296 OD1 ASP A 166 5774 6128 7198 2132 552 1009 O ATOM 1297 OD2 ASP A 166 18.968 9.794 19.801 1.00 49.21 O ANISOU 1297 OD2 ASP A 166 5278 6507 6914 2013 306 1220 O ATOM 1298 N THR A 167 13.994 10.339 21.459 1.00 39.58 N ANISOU 1298 N THR A 167 4727 4943 5369 1336 29 823 N ATOM 1299 CA THR A 167 13.121 10.647 22.580 1.00 38.00 C ANISOU 1299 CA THR A 167 4579 4787 5071 1170 -89 850 C ATOM 1300 C THR A 167 11.732 10.059 22.382 1.00 37.21 C ANISOU 1300 C THR A 167 4688 4468 4981 1095 -37 710 C ATOM 1301 O THR A 167 11.218 9.385 23.273 1.00 38.17 O ANISOU 1301 O THR A 167 4879 4511 5114 1072 -60 799 O ATOM 1302 CB THR A 167 13.018 12.157 22.834 1.00 36.11 C ANISOU 1302 CB THR A 167 4273 4765 4682 983 -203 785 C ATOM 1303 OG1 THR A 167 14.329 12.709 22.987 1.00 37.26 O ANISOU 1303 OG1 THR A 167 4226 5129 4804 1020 -255 911 O ATOM 1304 CG2 THR A 167 12.245 12.417 24.098 1.00 35.54 C ANISOU 1304 CG2 THR A 167 4247 4744 4511 826 -301 823 C ATOM 1305 N CYS A 168 11.140 10.290 21.213 1.00 35.60 N ANISOU 1305 N CYS A 168 4579 4181 4766 1045 29 506 N ATOM 1306 CA CYS A 168 9.802 9.795 20.930 1.00 34.54 C ANISOU 1306 CA CYS A 168 4625 3874 4625 944 70 372 C ATOM 1307 C CYS A 168 9.675 8.300 21.202 1.00 36.14 C ANISOU 1307 C CYS A 168 4947 3849 4934 1037 158 444 C ATOM 1308 O CYS A 168 8.995 7.911 22.149 1.00 36.04 O ANISOU 1308 O CYS A 168 4994 3793 4905 965 112 513 O ATOM 1309 CB CYS A 168 9.376 10.114 19.497 1.00 33.57 C ANISOU 1309 CB CYS A 168 4571 3709 4474 888 134 170 C ATOM 1310 SG CYS A 168 7.591 10.240 19.335 1.00 33.01 S ANISOU 1310 SG CYS A 168 4636 3579 4327 680 102 23 S ATOM 1311 N PRO A 169 10.341 7.460 20.384 1.00 37.69 N ANISOU 1311 N PRO A 169 5188 3891 5243 1197 301 429 N ATOM 1312 CA PRO A 169 10.203 6.023 20.527 1.00 39.75 C ANISOU 1312 CA PRO A 169 5595 3888 5621 1289 415 480 C ATOM 1313 C PRO A 169 10.386 5.570 21.970 1.00 41.04 C ANISOU 1313 C PRO A 169 5708 4063 5821 1339 336 722 C ATOM 1314 O PRO A 169 9.522 4.869 22.501 1.00 41.79 O ANISOU 1314 O PRO A 169 5943 4015 5920 1258 338 739 O ATOM 1315 CB PRO A 169 11.332 5.488 19.658 1.00 41.62 C ANISOU 1315 CB PRO A 169 5808 4025 5982 1504 575 482 C ATOM 1316 CG PRO A 169 11.518 6.511 18.644 1.00 39.93 C ANISOU 1316 CG PRO A 169 5525 3967 5678 1440 568 326 C ATOM 1317 CD PRO A 169 11.320 7.797 19.337 1.00 37.84 C ANISOU 1317 CD PRO A 169 5121 3967 5289 1305 378 372 C ATOM 1318 N LEU A 170 11.482 5.989 22.601 1.00 41.60 N ANISOU 1318 N LEU A 170 5576 4326 5904 1448 259 914 N ATOM 1319 CA LEU A 170 11.756 5.649 23.995 1.00 42.88 C ANISOU 1319 CA LEU A 170 5663 4554 6075 1478 162 1172 C ATOM 1320 C LEU A 170 10.609 6.054 24.917 1.00 41.35 C ANISOU 1320 C LEU A 170 5536 4436 5740 1245 41 1145 C ATOM 1321 O LEU A 170 10.177 5.270 25.763 1.00 42.81 O ANISOU 1321 O LEU A 170 5803 4520 5943 1223 27 1268 O ATOM 1322 CB LEU A 170 13.062 6.294 24.468 1.00 43.57 C ANISOU 1322 CB LEU A 170 5497 4911 6148 1569 68 1364 C ATOM 1323 CG LEU A 170 13.229 6.447 25.987 1.00 44.89 C ANISOU 1323 CG LEU A 170 5558 5268 6231 1495 -93 1604 C ATOM 1324 CD1 LEU A 170 13.595 5.115 26.668 1.00 48.24 C ANISOU 1324 CD1 LEU A 170 5993 5542 6794 1666 -60 1870 C ATOM 1325 CD2 LEU A 170 14.243 7.526 26.319 1.00 45.14 C ANISOU 1325 CD2 LEU A 170 5353 5631 6166 1464 -215 1704 C ATOM 1326 N PHE A 171 10.114 7.274 24.748 1.00 38.98 N ANISOU 1326 N PHE A 171 5201 4306 5305 1077 -32 989 N ATOM 1327 CA PHE A 171 9.068 7.787 25.620 1.00 37.61 C ANISOU 1327 CA PHE A 171 5069 4222 5000 868 -125 954 C ATOM 1328 C PHE A 171 7.822 6.940 25.556 1.00 37.63 C ANISOU 1328 C PHE A 171 5261 4012 5025 785 -62 870 C ATOM 1329 O PHE A 171 7.241 6.612 26.588 1.00 38.31 O ANISOU 1329 O PHE A 171 5394 4099 5064 689 -108 959 O ATOM 1330 CB PHE A 171 8.712 9.237 25.289 1.00 35.33 C ANISOU 1330 CB PHE A 171 4724 4106 4593 729 -180 787 C ATOM 1331 CG PHE A 171 7.613 9.794 26.151 1.00 34.84 C ANISOU 1331 CG PHE A 171 4703 4123 4413 533 -243 738 C ATOM 1332 CD1 PHE A 171 7.738 9.804 27.541 1.00 35.17 C ANISOU 1332 CD1 PHE A 171 4705 4284 4374 462 -324 894 C ATOM 1333 CD2 PHE A 171 6.448 10.302 25.575 1.00 34.17 C ANISOU 1333 CD2 PHE A 171 4688 4004 4292 417 -217 545 C ATOM 1334 CE1 PHE A 171 6.724 10.313 28.338 1.00 35.38 C ANISOU 1334 CE1 PHE A 171 4775 4380 4286 280 -355 833 C ATOM 1335 CE2 PHE A 171 5.418 10.818 26.367 1.00 33.22 C ANISOU 1335 CE2 PHE A 171 4591 3954 4078 256 -251 501 C ATOM 1336 CZ PHE A 171 5.554 10.825 27.748 1.00 34.73 C ANISOU 1336 CZ PHE A 171 4756 4250 4190 188 -309 632 C ATOM 1337 N VAL A 172 7.428 6.588 24.338 1.00 37.35 N ANISOU 1337 N VAL A 172 5335 3810 5046 800 43 698 N ATOM 1338 CA VAL A 172 6.197 5.850 24.097 1.00 37.16 C ANISOU 1338 CA VAL A 172 5492 3601 5025 683 103 589 C ATOM 1339 C VAL A 172 6.316 4.387 24.517 1.00 39.72 C ANISOU 1339 C VAL A 172 5945 3688 5460 768 181 725 C ATOM 1340 O VAL A 172 5.380 3.839 25.113 1.00 40.22 O ANISOU 1340 O VAL A 172 6119 3668 5494 640 174 744 O ATOM 1341 CB VAL A 172 5.772 5.940 22.633 1.00 36.27 C ANISOU 1341 CB VAL A 172 5459 3407 4914 641 185 367 C ATOM 1342 CG1 VAL A 172 4.478 5.181 22.408 1.00 35.58 C ANISOU 1342 CG1 VAL A 172 5551 3159 4810 482 235 262 C ATOM 1343 CG2 VAL A 172 5.639 7.388 22.234 1.00 33.93 C ANISOU 1343 CG2 VAL A 172 5039 3333 4521 564 106 262 C ATOM 1344 N ARG A 173 7.452 3.754 24.224 1.00 41.35 N ANISOU 1344 N ARG A 173 6133 3780 5797 986 263 829 N ATOM 1345 CA ARG A 173 7.637 2.382 24.674 1.00 44.22 C ANISOU 1345 CA ARG A 173 6616 3897 6289 1096 346 988 C ATOM 1346 C ARG A 173 7.445 2.361 26.183 1.00 44.36 C ANISOU 1346 C ARG A 173 6579 4031 6244 1025 217 1203 C ATOM 1347 O ARG A 173 6.883 1.414 26.728 1.00 46.21 O ANISOU 1347 O ARG A 173 6957 4091 6510 976 247 1286 O ATOM 1348 CB ARG A 173 8.983 1.781 24.237 1.00 46.35 C ANISOU 1348 CB ARG A 173 6837 4044 6729 1378 461 1103 C ATOM 1349 CG ARG A 173 8.869 0.899 22.986 1.00 49.00 C ANISOU 1349 CG ARG A 173 7375 4069 7173 1440 671 922 C ATOM 1350 CD ARG A 173 10.177 0.190 22.632 1.00 55.01 C ANISOU 1350 CD ARG A 173 8098 4675 8130 1746 822 1046 C ATOM 1351 NE ARG A 173 10.910 0.802 21.512 1.00 57.43 N ANISOU 1351 NE ARG A 173 8305 5075 8441 1837 895 904 N ATOM 1352 CZ ARG A 173 11.809 1.790 21.620 1.00 57.85 C ANISOU 1352 CZ ARG A 173 8103 5421 8457 1915 795 990 C ATOM 1353 NH1 ARG A 173 12.108 2.326 22.801 1.00 57.94 N ANISOU 1353 NH1 ARG A 173 7929 5673 8413 1902 612 1210 N ATOM 1354 NH2 ARG A 173 12.412 2.258 20.534 1.00 57.54 N ANISOU 1354 NH2 ARG A 173 7998 5444 8420 1982 880 851 N ATOM 1355 N GLY A 174 7.865 3.442 26.834 1.00 42.81 N ANISOU 1355 N GLY A 174 6191 4134 5940 990 78 1279 N ATOM 1356 CA GLY A 174 7.651 3.628 28.259 1.00 42.61 C ANISOU 1356 CA GLY A 174 6109 4273 5807 875 -50 1451 C ATOM 1357 C GLY A 174 6.192 3.815 28.606 1.00 41.08 C ANISOU 1357 C GLY A 174 6027 4088 5493 631 -72 1315 C ATOM 1358 O GLY A 174 5.710 3.250 29.582 1.00 41.89 O ANISOU 1358 O GLY A 174 6196 4160 5559 541 -102 1443 O ATOM 1359 N LEU A 175 5.490 4.610 27.804 1.00 39.16 N ANISOU 1359 N LEU A 175 5793 3895 5190 523 -56 1070 N ATOM 1360 CA LEU A 175 4.070 4.870 28.020 1.00 38.17 C ANISOU 1360 CA LEU A 175 5740 3799 4964 304 -67 936 C ATOM 1361 C LEU A 175 3.247 3.595 27.928 1.00 40.13 C ANISOU 1361 C LEU A 175 6179 3798 5269 241 15 930 C ATOM 1362 O LEU A 175 2.392 3.344 28.775 1.00 40.45 O ANISOU 1362 O LEU A 175 6272 3857 5239 87 -10 974 O ATOM 1363 CB LEU A 175 3.536 5.869 27.001 1.00 35.92 C ANISOU 1363 CB LEU A 175 5418 3594 4636 236 -57 701 C ATOM 1364 CG LEU A 175 3.634 7.378 27.241 1.00 33.78 C ANISOU 1364 CG LEU A 175 4997 3576 4260 183 -137 645 C ATOM 1365 CD1 LEU A 175 2.866 8.109 26.134 1.00 29.69 C ANISOU 1365 CD1 LEU A 175 4476 3078 3727 116 -110 432 C ATOM 1366 CD2 LEU A 175 3.109 7.774 28.622 1.00 32.48 C ANISOU 1366 CD2 LEU A 175 4803 3561 3978 40 -199 715 C ATOM 1367 N LEU A 176 3.517 2.786 26.904 1.00 41.54 N ANISOU 1367 N LEU A 176 6471 3744 5570 346 125 869 N ATOM 1368 CA LEU A 176 2.751 1.570 26.668 1.00 43.38 C ANISOU 1368 CA LEU A 176 6915 3711 5855 264 223 833 C ATOM 1369 C LEU A 176 2.837 0.595 27.839 1.00 46.06 C ANISOU 1369 C LEU A 176 7329 3937 6233 278 216 1070 C ATOM 1370 O LEU A 176 1.904 -0.168 28.084 1.00 46.88 O ANISOU 1370 O LEU A 176 7587 3902 6322 126 255 1061 O ATOM 1371 CB LEU A 176 3.201 0.894 25.376 1.00 44.36 C ANISOU 1371 CB LEU A 176 7162 3594 6100 382 364 722 C ATOM 1372 CG LEU A 176 3.030 1.673 24.067 1.00 42.35 C ANISOU 1372 CG LEU A 176 6871 3423 5798 339 385 483 C ATOM 1373 CD1 LEU A 176 3.601 0.897 22.902 1.00 43.57 C ANISOU 1373 CD1 LEU A 176 7162 3331 6062 457 544 387 C ATOM 1374 CD2 LEU A 176 1.585 1.996 23.800 1.00 40.80 C ANISOU 1374 CD2 LEU A 176 6714 3305 5482 80 349 321 C ATOM 1375 N GLU A 177 3.957 0.619 28.558 1.00 47.80 N ANISOU 1375 N GLU A 177 7435 4231 6496 449 162 1296 N ATOM 1376 CA GLU A 177 4.101 -0.188 29.773 1.00 50.77 C ANISOU 1376 CA GLU A 177 7851 4549 6891 460 127 1565 C ATOM 1377 C GLU A 177 3.196 0.376 30.857 1.00 49.82 C ANISOU 1377 C GLU A 177 7688 4654 6588 223 18 1581 C ATOM 1378 O GLU A 177 2.350 -0.333 31.399 1.00 51.14 O ANISOU 1378 O GLU A 177 7987 4719 6725 77 37 1627 O ATOM 1379 CB GLU A 177 5.542 -0.201 30.289 1.00 52.19 C ANISOU 1379 CB GLU A 177 7878 4808 7144 690 73 1828 C ATOM 1380 CG GLU A 177 6.527 -1.024 29.481 1.00 55.97 C ANISOU 1380 CG GLU A 177 8398 5032 7837 964 204 1890 C ATOM 1381 CD GLU A 177 7.902 -1.086 30.152 1.00 60.73 C ANISOU 1381 CD GLU A 177 8814 5748 8514 1188 136 2206 C ATOM 1382 OE1 GLU A 177 8.016 -1.677 31.263 1.00 63.09 O ANISOU 1382 OE1 GLU A 177 9113 6045 8815 1192 71 2486 O ATOM 1383 OE2 GLU A 177 8.864 -0.541 29.562 1.00 60.85 O ANISOU 1383 OE2 GLU A 177 8671 5870 8578 1350 143 2186 O ATOM 1384 N ALA A 178 3.371 1.658 31.157 1.00 47.93 N ANISOU 1384 N ALA A 178 7272 4714 6224 178 -79 1534 N ATOM 1385 CA ALA A 178 2.666 2.281 32.262 1.00 47.31 C ANISOU 1385 CA ALA A 178 7143 4863 5969 -28 -163 1551 C ATOM 1386 C ALA A 178 1.182 2.334 31.977 1.00 46.45 C ANISOU 1386 C ALA A 178 7126 4721 5803 -232 -110 1345 C ATOM 1387 O ALA A 178 0.371 2.175 32.881 1.00 47.04 O ANISOU 1387 O ALA A 178 7239 4857 5776 -408 -126 1392 O ATOM 1388 CB ALA A 178 3.221 3.673 32.529 1.00 45.61 C ANISOU 1388 CB ALA A 178 6743 4944 5644 -32 -253 1516 C ATOM 1389 N GLY A 179 0.839 2.526 30.707 1.00 45.76 N ANISOU 1389 N GLY A 179 7065 4548 5773 -215 -46 1131 N ATOM 1390 CA GLY A 179 -0.542 2.712 30.287 1.00 45.17 C ANISOU 1390 CA GLY A 179 7034 4485 5642 -405 -8 938 C ATOM 1391 C GLY A 179 -1.275 1.444 29.919 1.00 47.15 C ANISOU 1391 C GLY A 179 7477 4486 5951 -499 75 917 C ATOM 1392 O GLY A 179 -2.457 1.492 29.582 1.00 46.86 O ANISOU 1392 O GLY A 179 7470 4472 5862 -679 100 777 O ATOM 1393 N LYS A 180 -0.581 0.307 29.998 1.00 49.56 N ANISOU 1393 N LYS A 180 7911 4553 6367 -381 122 1067 N ATOM 1394 CA LYS A 180 -1.118 -0.991 29.572 1.00 51.66 C ANISOU 1394 CA LYS A 180 8400 4522 6707 -459 226 1045 C ATOM 1395 C LYS A 180 -2.570 -1.167 30.018 1.00 51.79 C ANISOU 1395 C LYS A 180 8471 4596 6612 -741 222 991 C ATOM 1396 O LYS A 180 -3.445 -1.505 29.212 1.00 52.05 O ANISOU 1396 O LYS A 180 8603 4538 6637 -893 282 828 O ATOM 1397 CB LYS A 180 -0.234 -2.130 30.102 1.00 54.29 C ANISOU 1397 CB LYS A 180 8848 4616 7164 -300 267 1287 C ATOM 1398 CG LYS A 180 -0.576 -3.527 29.592 1.00 57.20 C ANISOU 1398 CG LYS A 180 9481 4612 7639 -344 404 1267 C ATOM 1399 CD LYS A 180 0.472 -4.547 30.046 1.00 61.44 C ANISOU 1399 CD LYS A 180 10110 4897 8337 -122 458 1527 C ATOM 1400 CE LYS A 180 -0.072 -5.978 30.050 1.00 64.83 C ANISOU 1400 CE LYS A 180 10825 4961 8845 -223 582 1569 C ATOM 1401 NZ LYS A 180 -0.513 -6.422 28.694 1.00 65.44 N ANISOU 1401 NZ LYS A 180 11090 4805 8968 -302 727 1300 N ATOM 1402 N SER A 181 -2.810 -0.892 31.297 1.00 51.79 N ANISOU 1402 N SER A 181 8394 4773 6512 -824 151 1128 N ATOM 1403 CA SER A 181 -4.109 -1.091 31.932 1.00 52.17 C ANISOU 1403 CA SER A 181 8478 4896 6450 -1084 154 1115 C ATOM 1404 C SER A 181 -5.263 -0.390 31.212 1.00 50.56 C ANISOU 1404 C SER A 181 8191 4841 6178 -1246 165 883 C ATOM 1405 O SER A 181 -6.214 -1.040 30.791 1.00 51.57 O ANISOU 1405 O SER A 181 8426 4871 6296 -1428 218 804 O ATOM 1406 CB SER A 181 -4.045 -0.641 33.390 1.00 52.24 C ANISOU 1406 CB SER A 181 8383 5127 6340 -1132 79 1277 C ATOM 1407 OG SER A 181 -5.025 -1.317 34.140 1.00 53.62 O ANISOU 1407 OG SER A 181 8652 5284 6439 -1354 102 1344 O ATOM 1408 N ASP A 182 -5.174 0.930 31.072 1.00 48.37 N ANISOU 1408 N ASP A 182 7723 4802 5855 -1184 117 787 N ATOM 1409 CA ASP A 182 -6.198 1.699 30.370 1.00 47.00 C ANISOU 1409 CA ASP A 182 7441 4782 5634 -1299 122 598 C ATOM 1410 C ASP A 182 -6.264 1.358 28.886 1.00 46.80 C ANISOU 1410 C ASP A 182 7492 4611 5679 -1293 160 456 C ATOM 1411 O ASP A 182 -7.336 1.372 28.292 1.00 46.97 O ANISOU 1411 O ASP A 182 7496 4690 5661 -1465 174 340 O ATOM 1412 CB ASP A 182 -5.955 3.203 30.533 1.00 45.27 C ANISOU 1412 CB ASP A 182 7019 4810 5372 -1205 75 542 C ATOM 1413 CG ASP A 182 -6.168 3.680 31.958 1.00 46.18 C ANISOU 1413 CG ASP A 182 7058 5108 5381 -1274 58 631 C ATOM 1414 OD1 ASP A 182 -7.133 3.214 32.598 1.00 48.62 O ANISOU 1414 OD1 ASP A 182 7399 5449 5625 -1457 90 663 O ATOM 1415 OD2 ASP A 182 -5.383 4.530 32.437 1.00 45.59 O ANISOU 1415 OD2 ASP A 182 6895 5153 5274 -1165 19 662 O ATOM 1416 N LEU A 183 -5.119 1.053 28.283 1.00 46.54 N ANISOU 1416 N LEU A 183 7536 4406 5741 -1106 179 468 N ATOM 1417 CA LEU A 183 -5.074 0.828 26.844 1.00 46.18 C ANISOU 1417 CA LEU A 183 7567 4237 5744 -1099 226 315 C ATOM 1418 C LEU A 183 -5.759 -0.470 26.444 1.00 48.38 C ANISOU 1418 C LEU A 183 8062 4289 6030 -1286 306 273 C ATOM 1419 O LEU A 183 -6.323 -0.569 25.361 1.00 48.74 O ANISOU 1419 O LEU A 183 8153 4319 6048 -1415 332 118 O ATOM 1420 CB LEU A 183 -3.631 0.868 26.327 1.00 45.64 C ANISOU 1420 CB LEU A 183 7514 4052 5774 -842 248 333 C ATOM 1421 CG LEU A 183 -2.932 2.227 26.252 1.00 42.86 C ANISOU 1421 CG LEU A 183 6959 3917 5410 -685 177 317 C ATOM 1422 CD1 LEU A 183 -1.528 2.037 25.761 1.00 42.98 C ANISOU 1422 CD1 LEU A 183 7002 3802 5527 -452 214 353 C ATOM 1423 CD2 LEU A 183 -3.667 3.233 25.367 1.00 40.09 C ANISOU 1423 CD2 LEU A 183 6487 3749 4997 -774 145 150 C ATOM 1424 N GLU A 184 -5.702 -1.462 27.322 1.00 50.20 N ANISOU 1424 N GLU A 184 8435 4350 6289 -1316 342 419 N ATOM 1425 CA GLU A 184 -6.282 -2.753 27.039 1.00 52.84 C ANISOU 1425 CA GLU A 184 9007 4432 6637 -1500 430 393 C ATOM 1426 C GLU A 184 -7.655 -2.892 27.678 1.00 53.32 C ANISOU 1426 C GLU A 184 9045 4629 6585 -1786 402 407 C ATOM 1427 O GLU A 184 -8.207 -3.995 27.738 1.00 55.47 O ANISOU 1427 O GLU A 184 9515 4708 6852 -1975 466 422 O ATOM 1428 CB GLU A 184 -5.333 -3.867 27.502 1.00 55.21 C ANISOU 1428 CB GLU A 184 9504 4412 7062 -1347 506 557 C ATOM 1429 CG GLU A 184 -4.449 -4.445 26.380 1.00 57.39 C ANISOU 1429 CG GLU A 184 9942 4401 7461 -1189 622 469 C ATOM 1430 CD GLU A 184 -3.075 -4.928 26.861 1.00 59.43 C ANISOU 1430 CD GLU A 184 10248 4459 7875 -886 667 666 C ATOM 1431 OE1 GLU A 184 -3.008 -5.838 27.727 1.00 60.27 O ANISOU 1431 OE1 GLU A 184 10484 4380 8037 -884 699 856 O ATOM 1432 OE2 GLU A 184 -2.059 -4.396 26.349 1.00 58.85 O ANISOU 1432 OE2 GLU A 184 10073 4420 7868 -650 672 643 O ATOM 1433 N LYS A 185 -8.211 -1.770 28.137 1.00 51.63 N ANISOU 1433 N LYS A 185 8592 4741 6285 -1822 321 398 N ATOM 1434 CA LYS A 185 -9.490 -1.766 28.856 1.00 52.30 C ANISOU 1434 CA LYS A 185 8608 4999 6265 -2068 305 423 C ATOM 1435 C LYS A 185 -10.626 -2.318 28.000 1.00 53.37 C ANISOU 1435 C LYS A 185 8817 5114 6349 -2346 336 297 C ATOM 1436 O LYS A 185 -10.635 -2.156 26.775 1.00 53.24 O ANISOU 1436 O LYS A 185 8804 5085 6339 -2357 338 153 O ATOM 1437 CB LYS A 185 -9.846 -0.365 29.363 1.00 50.33 C ANISOU 1437 CB LYS A 185 8083 5090 5949 -2026 242 410 C ATOM 1438 CG LYS A 185 -10.505 0.539 28.312 1.00 50.43 C ANISOU 1438 CG LYS A 185 7926 5297 5940 -2069 213 251 C ATOM 1439 CD LYS A 185 -10.669 1.985 28.806 1.00 51.04 C ANISOU 1439 CD LYS A 185 7748 5659 5986 -1970 175 245 C ATOM 1440 CE LYS A 185 -11.709 2.746 27.987 1.00 50.61 C ANISOU 1440 CE LYS A 185 7507 5818 5905 -2064 155 136 C ATOM 1441 NZ LYS A 185 -12.058 4.055 28.602 1.00 49.60 N ANISOU 1441 NZ LYS A 185 7147 5939 5760 -1986 152 139 N ATOM 1442 N GLN A 186 -11.576 -2.975 28.659 1.00 52.95 N ANISOU 1442 N GLN A 186 5920 4253 9944 741 729 -24 N ATOM 1443 CA GLN A 186 -12.735 -3.523 27.981 1.00 52.38 C ANISOU 1443 CA GLN A 186 5839 4007 10055 595 895 -12 C ATOM 1444 C GLN A 186 -14.023 -2.989 28.601 1.00 52.23 C ANISOU 1444 C GLN A 186 5931 4159 9755 460 1074 180 C ATOM 1445 O GLN A 186 -14.377 -3.345 29.729 1.00 54.38 O ANISOU 1445 O GLN A 186 6327 4453 9881 456 1085 524 O ATOM 1446 CB GLN A 186 -12.703 -5.055 28.007 1.00 55.48 C ANISOU 1446 CB GLN A 186 6218 4001 10862 636 804 155 C ATOM 1447 CG GLN A 186 -11.630 -5.683 27.119 1.00 54.86 C ANISOU 1447 CG GLN A 186 5965 3714 11166 769 668 -154 C ATOM 1448 CD GLN A 186 -11.946 -5.586 25.637 1.00 51.29 C ANISOU 1448 CD GLN A 186 5362 3285 10842 669 799 -578 C ATOM 1449 OE1 GLN A 186 -13.105 -5.542 25.237 1.00 49.10 O ANISOU 1449 OE1 GLN A 186 5100 3018 10536 507 941 -592 O ATOM 1450 NE2 GLN A 186 -10.907 -5.561 24.815 1.00 51.11 N ANISOU 1450 NE2 GLN A 186 5171 3308 10941 770 750 -936 N ATOM 1451 N GLU A 187 -14.703 -2.119 27.855 1.00 50.01 N ANISOU 1451 N GLU A 187 5591 4023 9389 359 1216 -35 N ATOM 1452 CA GLU A 187 -15.962 -1.531 28.302 1.00 50.28 C ANISOU 1452 CA GLU A 187 5668 4219 9219 251 1392 65 C ATOM 1453 C GLU A 187 -17.129 -1.935 27.401 1.00 49.82 C ANISOU 1453 C GLU A 187 5503 4042 9385 110 1513 -7 C ATOM 1454 O GLU A 187 -17.068 -1.814 26.175 1.00 48.36 O ANISOU 1454 O GLU A 187 5213 3834 9327 95 1484 -267 O ATOM 1455 CB GLU A 187 -15.850 -0.005 28.423 1.00 48.68 C ANISOU 1455 CB GLU A 187 5469 4287 8741 283 1420 -108 C ATOM 1456 CG GLU A 187 -14.934 0.478 29.568 1.00 51.52 C ANISOU 1456 CG GLU A 187 5916 4819 8841 398 1306 -68 C ATOM 1457 CD GLU A 187 -15.550 0.332 30.967 1.00 56.44 C ANISOU 1457 CD GLU A 187 6657 5619 9167 394 1382 185 C ATOM 1458 OE1 GLU A 187 -16.682 -0.195 31.097 1.00 58.38 O ANISOU 1458 OE1 GLU A 187 6909 5829 9445 284 1555 369 O ATOM 1459 OE2 GLU A 187 -14.892 0.750 31.947 1.00 58.65 O ANISOU 1459 OE2 GLU A 187 7009 6111 9165 493 1273 187 O ATOM 1460 N LYS A 188 -18.188 -2.427 28.028 1.00 51.57 N ANISOU 1460 N LYS A 188 5737 4225 9634 -1 1649 221 N ATOM 1461 CA LYS A 188 -19.287 -3.047 27.302 1.00 52.18 C ANISOU 1461 CA LYS A 188 5676 4147 10003 -153 1738 161 C ATOM 1462 C LYS A 188 -20.191 -2.026 26.605 1.00 50.32 C ANISOU 1462 C LYS A 188 5321 4124 9673 -195 1814 -65 C ATOM 1463 O LYS A 188 -20.480 -0.959 27.154 1.00 49.93 O ANISOU 1463 O LYS A 188 5302 4312 9359 -155 1895 -51 O ATOM 1464 CB LYS A 188 -20.101 -3.929 28.246 1.00 55.35 C ANISOU 1464 CB LYS A 188 6096 4421 10512 -290 1883 516 C ATOM 1465 CG LYS A 188 -19.279 -4.989 28.955 1.00 57.78 C ANISOU 1465 CG LYS A 188 6532 4477 10945 -239 1781 834 C ATOM 1466 CD LYS A 188 -20.080 -5.652 30.059 1.00 60.93 C ANISOU 1466 CD LYS A 188 6985 4826 11339 -388 1964 1296 C ATOM 1467 CE LYS A 188 -19.539 -7.034 30.378 1.00 64.13 C ANISOU 1467 CE LYS A 188 7464 4803 12101 -384 1846 1637 C ATOM 1468 NZ LYS A 188 -20.572 -7.900 31.002 1.00 67.60 N ANISOU 1468 NZ LYS A 188 7883 5057 12744 -619 2060 2064 N ATOM 1469 N PRO A 189 -20.642 -2.348 25.384 1.00 49.93 N ANISOU 1469 N PRO A 189 5125 3995 9852 -259 1765 -295 N ATOM 1470 CA PRO A 189 -21.641 -1.483 24.764 1.00 48.74 C ANISOU 1470 CA PRO A 189 4845 4042 9633 -288 1802 -449 C ATOM 1471 C PRO A 189 -23.031 -1.741 25.340 1.00 50.70 C ANISOU 1471 C PRO A 189 4966 4295 10003 -426 1970 -330 C ATOM 1472 O PRO A 189 -23.338 -2.852 25.793 1.00 53.14 O ANISOU 1472 O PRO A 189 5247 4396 10547 -558 2048 -171 O ATOM 1473 CB PRO A 189 -21.609 -1.916 23.299 1.00 48.85 C ANISOU 1473 CB PRO A 189 4739 4012 9811 -309 1665 -735 C ATOM 1474 CG PRO A 189 -21.207 -3.364 23.351 1.00 50.58 C ANISOU 1474 CG PRO A 189 4951 3917 10350 -368 1630 -736 C ATOM 1475 CD PRO A 189 -20.273 -3.488 24.521 1.00 50.89 C ANISOU 1475 CD PRO A 189 5174 3863 10300 -288 1653 -460 C ATOM 1476 N VAL A 190 -23.862 -0.710 25.324 1.00 49.99 N ANISOU 1476 N VAL A 190 4778 4422 9795 -399 2031 -400 N ATOM 1477 CA VAL A 190 -25.275 -0.862 25.629 1.00 51.85 C ANISOU 1477 CA VAL A 190 4807 4706 10186 -526 2190 -374 C ATOM 1478 C VAL A 190 -26.023 -0.354 24.404 1.00 51.41 C ANISOU 1478 C VAL A 190 4547 4753 10233 -497 2051 -633 C ATOM 1479 O VAL A 190 -25.614 0.644 23.795 1.00 49.63 O ANISOU 1479 O VAL A 190 4380 4650 9829 -346 1914 -730 O ATOM 1480 CB VAL A 190 -25.686 -0.085 26.894 1.00 52.46 C ANISOU 1480 CB VAL A 190 4906 4992 10033 -490 2403 -243 C ATOM 1481 CG1 VAL A 190 -26.986 -0.626 27.429 1.00 56.23 C ANISOU 1481 CG1 VAL A 190 5168 5501 10696 -671 2639 -151 C ATOM 1482 CG2 VAL A 190 -24.610 -0.184 27.978 1.00 52.37 C ANISOU 1482 CG2 VAL A 190 5153 4993 9751 -433 2443 -28 C ATOM 1483 N ALA A 191 -27.092 -1.049 24.027 1.00 53.59 N ANISOU 1483 N ALA A 191 4576 4976 10809 -646 2068 -728 N ATOM 1484 CA ALA A 191 -27.826 -0.718 22.804 1.00 54.09 C ANISOU 1484 CA ALA A 191 4420 5165 10966 -615 1878 -987 C ATOM 1485 C ALA A 191 -29.289 -0.384 23.048 1.00 56.46 C ANISOU 1485 C ALA A 191 4415 5596 11443 -665 1976 -1037 C ATOM 1486 O ALA A 191 -29.891 -0.889 23.996 1.00 58.86 O ANISOU 1486 O ALA A 191 4613 5844 11909 -819 2225 -911 O ATOM 1487 CB ALA A 191 -27.715 -1.841 21.807 1.00 55.36 C ANISOU 1487 CB ALA A 191 4499 5184 11350 -723 1715 -1197 C ATOM 1488 N TRP A 192 -29.853 0.468 22.192 1.00 56.42 N ANISOU 1488 N TRP A 192 4254 5776 11407 -531 1784 -1200 N ATOM 1489 CA TRP A 192 -31.285 0.761 22.226 1.00 59.11 C ANISOU 1489 CA TRP A 192 4233 6247 11980 -548 1815 -1311 C ATOM 1490 C TRP A 192 -31.841 1.089 20.843 1.00 60.40 C ANISOU 1490 C TRP A 192 4194 6570 12187 -447 1472 -1531 C ATOM 1491 O TRP A 192 -31.087 1.415 19.921 1.00 59.04 O ANISOU 1491 O TRP A 192 4205 6463 11764 -326 1239 -1546 O ATOM 1492 CB TRP A 192 -31.609 1.864 23.236 1.00 58.96 C ANISOU 1492 CB TRP A 192 4198 6340 11865 -414 2012 -1216 C ATOM 1493 CG TRP A 192 -31.155 3.244 22.861 1.00 57.37 C ANISOU 1493 CG TRP A 192 4134 6213 11452 -146 1835 -1209 C ATOM 1494 CD1 TRP A 192 -31.872 4.192 22.187 1.00 58.79 C ANISOU 1494 CD1 TRP A 192 4114 6502 11722 38 1629 -1304 C ATOM 1495 CD2 TRP A 192 -29.896 3.842 23.170 1.00 54.95 C ANISOU 1495 CD2 TRP A 192 4173 5842 10862 -38 1843 -1079 C ATOM 1496 NE1 TRP A 192 -31.133 5.339 22.049 1.00 56.81 N ANISOU 1496 NE1 TRP A 192 4082 6217 11285 242 1522 -1206 N ATOM 1497 CE2 TRP A 192 -29.916 5.153 22.647 1.00 54.64 C ANISOU 1497 CE2 TRP A 192 4132 5842 10787 184 1660 -1091 C ATOM 1498 CE3 TRP A 192 -28.748 3.396 23.836 1.00 53.14 C ANISOU 1498 CE3 TRP A 192 4235 5514 10441 -106 1966 -948 C ATOM 1499 CZ2 TRP A 192 -28.832 6.021 22.766 1.00 52.94 C ANISOU 1499 CZ2 TRP A 192 4184 5548 10381 303 1626 -992 C ATOM 1500 CZ3 TRP A 192 -27.677 4.261 23.960 1.00 51.17 C ANISOU 1500 CZ3 TRP A 192 4233 5236 9975 30 1913 -887 C ATOM 1501 CH2 TRP A 192 -27.724 5.558 23.422 1.00 50.84 C ANISOU 1501 CH2 TRP A 192 4173 5213 9931 215 1757 -917 C ATOM 1502 N LEU A 193 -33.161 0.994 20.701 1.00 63.64 N ANISOU 1502 N LEU A 193 4209 7077 12896 -501 1441 -1692 N ATOM 1503 CA LEU A 193 -33.790 1.127 19.394 1.00 65.79 C ANISOU 1503 CA LEU A 193 4245 7535 13219 -419 1073 -1919 C ATOM 1504 C LEU A 193 -34.790 2.268 19.351 1.00 67.73 C ANISOU 1504 C LEU A 193 4219 7960 13555 -208 966 -1939 C ATOM 1505 O LEU A 193 -35.353 2.625 20.378 1.00 68.68 O ANISOU 1505 O LEU A 193 4192 8056 13847 -205 1233 -1894 O ATOM 1506 CB LEU A 193 -34.486 -0.177 19.008 1.00 68.84 C ANISOU 1506 CB LEU A 193 4325 7867 13965 -675 1024 -2187 C ATOM 1507 CG LEU A 193 -33.721 -1.491 19.159 1.00 68.39 C ANISOU 1507 CG LEU A 193 4442 7535 14007 -908 1147 -2206 C ATOM 1508 CD1 LEU A 193 -34.670 -2.653 18.912 1.00 72.52 C ANISOU 1508 CD1 LEU A 193 4574 7949 15032 -1179 1122 -2489 C ATOM 1509 CD2 LEU A 193 -32.514 -1.556 18.229 1.00 65.46 C ANISOU 1509 CD2 LEU A 193 4383 7202 13287 -800 925 -2269 C ATOM 1510 N SER A 194 -34.993 2.831 18.158 1.00 69.10 N ANISOU 1510 N SER A 194 4323 8331 13601 -20 571 -2005 N ATOM 1511 CA SER A 194 -36.024 3.848 17.887 1.00 71.90 C ANISOU 1511 CA SER A 194 4371 8845 14104 215 361 -2032 C ATOM 1512 C SER A 194 -36.255 3.982 16.375 1.00 74.49 C ANISOU 1512 C SER A 194 4607 9435 14260 349 -134 -2117 C ATOM 1513 O SER A 194 -35.516 3.390 15.580 1.00 73.81 O ANISOU 1513 O SER A 194 4731 9431 13881 264 -271 -2164 O ATOM 1514 CB SER A 194 -35.648 5.206 18.501 1.00 70.21 C ANISOU 1514 CB SER A 194 4351 8532 13793 461 462 -1790 C ATOM 1515 OG SER A 194 -34.389 5.664 18.039 1.00 67.08 O ANISOU 1515 OG SER A 194 4388 8088 13010 548 363 -1563 O ATOM 1516 N SER A 195 -37.267 4.758 15.982 1.00 77.93 N ANISOU 1516 N SER A 195 4718 10030 14860 573 -410 -2145 N ATOM 1517 CA SER A 195 -37.605 4.930 14.566 1.00 81.36 C ANISOU 1517 CA SER A 195 5037 10780 15097 727 -927 -2195 C ATOM 1518 C SER A 195 -38.092 6.339 14.207 1.00 84.08 C ANISOU 1518 C SER A 195 5288 11200 15457 1100 -1235 -1955 C ATOM 1519 O SER A 195 -38.822 6.971 14.974 1.00 85.26 O ANISOU 1519 O SER A 195 5181 11212 16002 1234 -1119 -1963 O ATOM 1520 CB SER A 195 -38.650 3.891 14.143 1.00 85.28 C ANISOU 1520 CB SER A 195 5063 11459 15881 553 -1099 -2620 C ATOM 1521 OG SER A 195 -39.864 4.065 14.853 1.00 87.53 O ANISOU 1521 OG SER A 195 4872 11694 16690 571 -992 -2761 O ATOM 1522 N VAL A 196 -37.683 6.815 13.029 1.00 85.73 N ANISOU 1522 N VAL A 196 5697 11634 15241 1270 -1621 -1737 N ATOM 1523 CA VAL A 196 -38.147 8.100 12.477 1.00 89.40 C ANISOU 1523 CA VAL A 196 6084 12174 15711 1637 -2003 -1436 C ATOM 1524 C VAL A 196 -38.697 7.923 11.046 1.00 94.58 C ANISOU 1524 C VAL A 196 6554 13302 16081 1750 -2571 -1491 C ATOM 1525 O VAL A 196 -38.354 6.949 10.368 1.00 94.70 O ANISOU 1525 O VAL A 196 6641 13593 15747 1550 -2646 -1718 O ATOM 1526 CB VAL A 196 -37.023 9.193 12.496 1.00 87.13 C ANISOU 1526 CB VAL A 196 6280 11668 15159 1780 -1924 -940 C ATOM 1527 CG1 VAL A 196 -36.624 9.558 13.927 1.00 83.02 C ANISOU 1527 CG1 VAL A 196 5878 10715 14951 1730 -1443 -929 C ATOM 1528 CG2 VAL A 196 -35.799 8.751 11.695 1.00 85.42 C ANISOU 1528 CG2 VAL A 196 6484 11644 14327 1622 -1925 -799 C ATOM 1529 N PRO A 197 -39.568 8.845 10.587 1.00 99.45 N ANISOU 1529 N PRO A 197 6910 14026 16852 2087 -2993 -1316 N ATOM 1530 CA PRO A 197 -39.997 8.785 9.180 1.00104.87 C ANISOU 1530 CA PRO A 197 7469 15222 17155 2231 -3587 -1295 C ATOM 1531 C PRO A 197 -38.904 9.257 8.212 1.00104.97 C ANISOU 1531 C PRO A 197 7994 15439 16450 2300 -3744 -816 C ATOM 1532 O PRO A 197 -38.665 8.622 7.180 1.00106.88 O ANISOU 1532 O PRO A 197 8311 16158 16139 2209 -3981 -940 O ATOM 1533 CB PRO A 197 -41.204 9.738 9.131 1.00110.09 C ANISOU 1533 CB PRO A 197 7705 15865 18260 2608 -3975 -1180 C ATOM 1534 CG PRO A 197 -41.636 9.913 10.558 1.00107.57 C ANISOU 1534 CG PRO A 197 7147 15091 18632 2579 -3530 -1374 C ATOM 1535 CD PRO A 197 -40.372 9.809 11.362 1.00101.09 C ANISOU 1535 CD PRO A 197 6826 13935 17648 2346 -2969 -1244 C ATOM 1536 N GLN A 205 -37.380 5.053 8.775 1.00 92.34 N ANISOU 1536 N GLN A 205 6560 13896 14630 1184 -2821 -2225 N ATOM 1537 CA GLN A 205 -36.148 4.306 9.021 1.00 88.21 C ANISOU 1537 CA GLN A 205 6393 13219 13904 934 -2438 -2313 C ATOM 1538 C GLN A 205 -35.913 3.982 10.508 1.00 83.32 C ANISOU 1538 C GLN A 205 5817 12052 13787 748 -1911 -2334 C ATOM 1539 O GLN A 205 -35.931 4.871 11.370 1.00 81.15 O ANISOU 1539 O GLN A 205 5613 11488 13733 868 -1716 -2017 O ATOM 1540 CB GLN A 205 -34.920 5.011 8.399 1.00 87.06 C ANISOU 1540 CB GLN A 205 6728 13227 13123 1038 -2430 -1876 C ATOM 1541 CG GLN A 205 -34.553 6.393 8.967 1.00 85.28 C ANISOU 1541 CG GLN A 205 6744 12690 12967 1229 -2293 -1283 C ATOM 1542 CD GLN A 205 -33.046 6.706 8.894 1.00 83.33 C ANISOU 1542 CD GLN A 205 6978 12372 12310 1163 -2025 -960 C ATOM 1543 OE1 GLN A 205 -32.332 6.216 8.013 1.00 84.96 O ANISOU 1543 OE1 GLN A 205 7351 12932 11998 1072 -2065 -1048 O ATOM 1544 NE2 GLN A 205 -32.565 7.534 9.825 1.00 79.18 N ANISOU 1544 NE2 GLN A 205 6643 11409 12034 1209 -1746 -628 N ATOM 1545 N LEU A 206 -35.701 2.697 10.791 1.00 82.10 N ANISOU 1545 N LEU A 206 5615 11769 13812 462 -1697 -2718 N ATOM 1546 CA LEU A 206 -35.390 2.229 12.142 1.00 78.04 C ANISOU 1546 CA LEU A 206 5176 10784 13693 264 -1210 -2703 C ATOM 1547 C LEU A 206 -33.916 2.469 12.484 1.00 73.42 C ANISOU 1547 C LEU A 206 5087 10017 12792 257 -927 -2409 C ATOM 1548 O LEU A 206 -33.046 2.387 11.615 1.00 73.38 O ANISOU 1548 O LEU A 206 5322 10228 12330 277 -1037 -2405 O ATOM 1549 CB LEU A 206 -35.761 0.750 12.299 1.00 79.40 C ANISOU 1549 CB LEU A 206 5091 10830 14248 -39 -1117 -3168 C ATOM 1550 N VAL A 207 -33.652 2.777 13.754 1.00 70.06 N ANISOU 1550 N VAL A 207 4786 9235 12597 229 -564 -2188 N ATOM 1551 CA VAL A 207 -32.318 3.173 14.215 1.00 66.02 C ANISOU 1551 CA VAL A 207 4701 8542 11842 246 -316 -1902 C ATOM 1552 C VAL A 207 -31.857 2.307 15.386 1.00 63.41 C ANISOU 1552 C VAL A 207 4461 7871 11762 34 67 -1957 C ATOM 1553 O VAL A 207 -32.608 2.087 16.336 1.00 63.90 O ANISOU 1553 O VAL A 207 4320 7765 12194 -51 258 -1991 O ATOM 1554 CB VAL A 207 -32.291 4.661 14.657 1.00 64.94 C ANISOU 1554 CB VAL A 207 4677 8314 11682 473 -290 -1526 C ATOM 1555 CG1 VAL A 207 -30.896 5.065 15.127 1.00 61.13 C ANISOU 1555 CG1 VAL A 207 4596 7643 10987 466 -51 -1279 C ATOM 1556 CG2 VAL A 207 -32.755 5.573 13.532 1.00 68.02 C ANISOU 1556 CG2 VAL A 207 4992 8991 11863 705 -691 -1370 C ATOM 1557 N CYS A 208 -30.621 1.825 15.311 1.00 61.24 N ANISOU 1557 N CYS A 208 4475 7516 11276 -41 180 -1947 N ATOM 1558 CA CYS A 208 -30.034 1.040 16.390 1.00 59.14 C ANISOU 1558 CA CYS A 208 4336 6924 11210 -204 498 -1929 C ATOM 1559 C CYS A 208 -28.863 1.776 17.043 1.00 55.93 C ANISOU 1559 C CYS A 208 4272 6395 10585 -115 681 -1631 C ATOM 1560 O CYS A 208 -27.769 1.876 16.464 1.00 54.97 O ANISOU 1560 O CYS A 208 4370 6346 10170 -75 637 -1597 O ATOM 1561 CB CYS A 208 -29.576 -0.323 15.880 1.00 60.09 C ANISOU 1561 CB CYS A 208 4451 6982 11400 -368 467 -2230 C ATOM 1562 SG CYS A 208 -28.837 -1.329 17.178 1.00 58.37 S ANISOU 1562 SG CYS A 208 4391 6318 11468 -539 805 -2131 S ATOM 1563 N HIS A 209 -29.096 2.292 18.248 1.00 54.68 N ANISOU 1563 N HIS A 209 4128 6080 10568 -90 892 -1453 N ATOM 1564 CA HIS A 209 -28.089 3.078 18.958 1.00 51.65 C ANISOU 1564 CA HIS A 209 4024 5589 10012 -2 1040 -1224 C ATOM 1565 C HIS A 209 -27.176 2.151 19.763 1.00 49.98 C ANISOU 1565 C HIS A 209 3988 5179 9822 -133 1244 -1201 C ATOM 1566 O HIS A 209 -27.662 1.326 20.531 1.00 50.98 O ANISOU 1566 O HIS A 209 4015 5178 10176 -269 1400 -1220 O ATOM 1567 CB HIS A 209 -28.754 4.082 19.900 1.00 51.73 C ANISOU 1567 CB HIS A 209 3951 5558 10145 104 1158 -1118 C ATOM 1568 CG HIS A 209 -29.811 4.934 19.261 1.00 54.07 C ANISOU 1568 CG HIS A 209 4016 5993 10536 259 949 -1139 C ATOM 1569 ND1 HIS A 209 -29.610 6.261 18.948 1.00 54.62 N ANISOU 1569 ND1 HIS A 209 4171 6063 10519 461 818 -974 N ATOM 1570 CD2 HIS A 209 -31.090 4.660 18.915 1.00 57.20 C ANISOU 1570 CD2 HIS A 209 4074 6506 11155 250 833 -1295 C ATOM 1571 CE1 HIS A 209 -30.710 6.764 18.417 1.00 56.34 C ANISOU 1571 CE1 HIS A 209 4130 6390 10888 596 610 -1001 C ATOM 1572 NE2 HIS A 209 -31.624 5.812 18.387 1.00 58.64 N ANISOU 1572 NE2 HIS A 209 4148 6777 11356 474 610 -1216 N ATOM 1573 N VAL A 210 -25.864 2.288 19.577 1.00 47.94 N ANISOU 1573 N VAL A 210 3971 4897 9348 -93 1238 -1136 N ATOM 1574 CA VAL A 210 -24.869 1.516 20.317 1.00 46.69 C ANISOU 1574 CA VAL A 210 3978 4553 9209 -165 1379 -1096 C ATOM 1575 C VAL A 210 -23.918 2.472 21.026 1.00 45.22 C ANISOU 1575 C VAL A 210 3997 4338 8845 -65 1459 -925 C ATOM 1576 O VAL A 210 -23.289 3.323 20.387 1.00 44.43 O ANISOU 1576 O VAL A 210 3984 4327 8572 18 1373 -888 O ATOM 1577 CB VAL A 210 -24.034 0.630 19.377 1.00 46.88 C ANISOU 1577 CB VAL A 210 4044 4576 9193 -208 1279 -1273 C ATOM 1578 CG1 VAL A 210 -23.197 -0.399 20.171 1.00 45.67 C ANISOU 1578 CG1 VAL A 210 3998 4165 9188 -270 1390 -1243 C ATOM 1579 CG2 VAL A 210 -24.927 -0.057 18.366 1.00 49.57 C ANISOU 1579 CG2 VAL A 210 4164 5018 9653 -280 1130 -1532 C ATOM 1580 N SER A 211 -23.784 2.319 22.339 1.00 45.24 N ANISOU 1580 N SER A 211 4074 4232 8885 -87 1622 -818 N ATOM 1581 CA SER A 211 -23.037 3.298 23.113 1.00 44.40 C ANISOU 1581 CA SER A 211 4119 4128 8624 8 1677 -724 C ATOM 1582 C SER A 211 -22.279 2.690 24.276 1.00 44.37 C ANISOU 1582 C SER A 211 4254 4039 8567 -20 1779 -631 C ATOM 1583 O SER A 211 -22.779 1.783 24.942 1.00 46.04 O ANISOU 1583 O SER A 211 4431 4195 8866 -111 1886 -550 O ATOM 1584 CB SER A 211 -23.995 4.374 23.637 1.00 45.27 C ANISOU 1584 CB SER A 211 4130 4306 8766 87 1741 -723 C ATOM 1585 OG SER A 211 -23.296 5.458 24.232 1.00 45.43 O ANISOU 1585 OG SER A 211 4269 4309 8683 188 1760 -710 O ATOM 1586 N GLY A 212 -21.076 3.209 24.517 1.00 43.30 N ANISOU 1586 N GLY A 212 4260 3896 8295 51 1738 -618 N ATOM 1587 CA GLY A 212 -20.292 2.867 25.704 1.00 43.60 C ANISOU 1587 CA GLY A 212 4426 3908 8231 67 1782 -529 C ATOM 1588 C GLY A 212 -19.159 1.873 25.500 1.00 43.51 C ANISOU 1588 C GLY A 212 4485 3778 8268 61 1692 -508 C ATOM 1589 O GLY A 212 -18.395 1.595 26.429 1.00 44.26 O ANISOU 1589 O GLY A 212 4681 3856 8280 104 1673 -415 O ATOM 1590 N PHE A 213 -19.037 1.336 24.293 1.00 43.17 N ANISOU 1590 N PHE A 213 4371 3676 8354 27 1621 -620 N ATOM 1591 CA PHE A 213 -18.052 0.293 24.048 1.00 43.69 C ANISOU 1591 CA PHE A 213 4456 3607 8539 38 1546 -665 C ATOM 1592 C PHE A 213 -16.643 0.855 23.969 1.00 42.84 C ANISOU 1592 C PHE A 213 4394 3554 8330 124 1480 -731 C ATOM 1593 O PHE A 213 -16.448 2.022 23.622 1.00 41.77 O ANISOU 1593 O PHE A 213 4257 3547 8068 137 1489 -773 O ATOM 1594 CB PHE A 213 -18.387 -0.529 22.795 1.00 44.28 C ANISOU 1594 CB PHE A 213 4408 3627 8788 -22 1501 -855 C ATOM 1595 CG PHE A 213 -18.568 0.293 21.553 1.00 43.62 C ANISOU 1595 CG PHE A 213 4259 3757 8559 -21 1468 -1002 C ATOM 1596 CD1 PHE A 213 -19.755 0.980 21.320 1.00 43.22 C ANISOU 1596 CD1 PHE A 213 4148 3823 8450 -47 1479 -965 C ATOM 1597 CD2 PHE A 213 -17.555 0.373 20.605 1.00 43.74 C ANISOU 1597 CD2 PHE A 213 4256 3876 8487 10 1428 -1159 C ATOM 1598 CE1 PHE A 213 -19.923 1.737 20.172 1.00 42.63 C ANISOU 1598 CE1 PHE A 213 4026 3948 8223 -28 1412 -1029 C ATOM 1599 CE2 PHE A 213 -17.715 1.132 19.457 1.00 43.10 C ANISOU 1599 CE2 PHE A 213 4134 4034 8209 0 1408 -1220 C ATOM 1600 CZ PHE A 213 -18.905 1.808 19.240 1.00 43.20 C ANISOU 1600 CZ PHE A 213 4116 4144 8155 -13 1381 -1129 C ATOM 1601 N TYR A 214 -15.682 0.010 24.344 1.00 43.91 N ANISOU 1601 N TYR A 214 4549 3564 8569 180 1408 -722 N ATOM 1602 CA TYR A 214 -14.257 0.234 24.125 1.00 43.86 C ANISOU 1602 CA TYR A 214 4514 3593 8558 257 1334 -842 C ATOM 1603 C TYR A 214 -13.549 -1.118 24.108 1.00 45.86 C ANISOU 1603 C TYR A 214 4718 3647 9060 326 1242 -894 C ATOM 1604 O TYR A 214 -13.734 -1.912 25.031 1.00 47.33 O ANISOU 1604 O TYR A 214 4973 3662 9348 358 1192 -695 O ATOM 1605 CB TYR A 214 -13.649 1.117 25.207 1.00 43.37 C ANISOU 1605 CB TYR A 214 4523 3619 8338 316 1294 -759 C ATOM 1606 CG TYR A 214 -12.332 1.673 24.771 1.00 43.53 C ANISOU 1606 CG TYR A 214 4454 3709 8376 348 1248 -921 C ATOM 1607 CD1 TYR A 214 -11.154 0.974 25.004 1.00 45.64 C ANISOU 1607 CD1 TYR A 214 4653 3912 8778 445 1131 -987 C ATOM 1608 CD2 TYR A 214 -12.260 2.886 24.086 1.00 43.39 C ANISOU 1608 CD2 TYR A 214 4396 3806 8285 276 1324 -991 C ATOM 1609 CE1 TYR A 214 -9.931 1.466 24.579 1.00 46.53 C ANISOU 1609 CE1 TYR A 214 4628 4107 8944 457 1113 -1163 C ATOM 1610 CE2 TYR A 214 -11.037 3.400 23.663 1.00 44.05 C ANISOU 1610 CE2 TYR A 214 4370 3951 8417 263 1322 -1115 C ATOM 1611 CZ TYR A 214 -9.878 2.680 23.913 1.00 45.90 C ANISOU 1611 CZ TYR A 214 4507 4155 8779 346 1228 -1223 C ATOM 1612 OH TYR A 214 -8.660 3.159 23.503 1.00 47.09 O ANISOU 1612 OH TYR A 214 4496 4385 9011 320 1247 -1371 O ATOM 1613 N PRO A 215 -12.689 -1.366 23.103 1.00 46.63 N ANISOU 1613 N PRO A 215 4686 3767 9264 359 1225 -1149 N ATOM 1614 CA PRO A 215 -12.154 -0.434 22.105 1.00 46.21 C ANISOU 1614 CA PRO A 215 4549 3952 9055 320 1300 -1325 C ATOM 1615 C PRO A 215 -13.075 -0.135 20.930 1.00 46.11 C ANISOU 1615 C PRO A 215 4512 4097 8910 217 1387 -1409 C ATOM 1616 O PRO A 215 -14.197 -0.634 20.869 1.00 46.23 O ANISOU 1616 O PRO A 215 4548 4036 8980 173 1380 -1382 O ATOM 1617 CB PRO A 215 -10.871 -1.136 21.604 1.00 47.92 C ANISOU 1617 CB PRO A 215 4605 4142 9460 408 1264 -1576 C ATOM 1618 CG PRO A 215 -10.722 -2.393 22.440 1.00 49.50 C ANISOU 1618 CG PRO A 215 4819 4034 9956 525 1122 -1508 C ATOM 1619 CD PRO A 215 -12.088 -2.702 22.958 1.00 49.00 C ANISOU 1619 CD PRO A 215 4896 3837 9886 449 1134 -1275 C ATOM 1620 N LYS A 216 -12.557 0.665 20.001 1.00 46.52 N ANISOU 1620 N LYS A 216 4502 4382 8790 175 1464 -1496 N ATOM 1621 CA LYS A 216 -13.298 1.149 18.839 1.00 46.88 C ANISOU 1621 CA LYS A 216 4536 4653 8623 93 1520 -1516 C ATOM 1622 C LYS A 216 -13.801 0.054 17.891 1.00 48.44 C ANISOU 1622 C LYS A 216 4642 4908 8854 84 1495 -1781 C ATOM 1623 O LYS A 216 -14.953 0.126 17.476 1.00 49.04 O ANISOU 1623 O LYS A 216 4732 5060 8842 37 1458 -1756 O ATOM 1624 CB LYS A 216 -12.481 2.213 18.088 1.00 47.70 C ANISOU 1624 CB LYS A 216 4600 4997 8526 36 1624 -1482 C ATOM 1625 CG LYS A 216 -13.289 3.144 17.192 1.00 48.50 C ANISOU 1625 CG LYS A 216 4748 5310 8369 -36 1653 -1317 C ATOM 1626 CD LYS A 216 -12.452 4.344 16.768 1.00 50.05 C ANISOU 1626 CD LYS A 216 4933 5644 8439 -115 1767 -1152 C ATOM 1627 CE LYS A 216 -12.987 4.928 15.474 1.00 52.86 C ANISOU 1627 CE LYS A 216 5308 6295 8483 -180 1801 -1005 C ATOM 1628 NZ LYS A 216 -12.367 6.231 15.111 1.00 55.27 N ANISOU 1628 NZ LYS A 216 5627 6668 8705 -284 1916 -718 N ATOM 1629 N PRO A 217 -12.962 -0.953 17.540 1.00 50.15 N ANISOU 1629 N PRO A 217 4735 5087 9232 139 1497 -2080 N ATOM 1630 CA PRO A 217 -13.501 -2.046 16.693 1.00 52.21 C ANISOU 1630 CA PRO A 217 4889 5362 9585 132 1455 -2414 C ATOM 1631 C PRO A 217 -14.825 -2.645 17.203 1.00 51.92 C ANISOU 1631 C PRO A 217 4895 5070 9762 89 1358 -2333 C ATOM 1632 O PRO A 217 -14.903 -3.112 18.344 1.00 51.47 O ANISOU 1632 O PRO A 217 4901 4675 9982 115 1320 -2149 O ATOM 1633 CB PRO A 217 -12.377 -3.082 16.711 1.00 53.89 C ANISOU 1633 CB PRO A 217 4965 5413 10099 237 1449 -2718 C ATOM 1634 CG PRO A 217 -11.134 -2.244 16.820 1.00 53.37 C ANISOU 1634 CG PRO A 217 4872 5514 9891 264 1546 -2632 C ATOM 1635 CD PRO A 217 -11.497 -1.077 17.707 1.00 50.69 C ANISOU 1635 CD PRO A 217 4708 5142 9410 211 1538 -2198 C ATOM 1636 N VAL A 218 -15.854 -2.604 16.352 1.00 52.67 N ANISOU 1636 N VAL A 218 4942 5361 9709 18 1320 -2453 N ATOM 1637 CA VAL A 218 -17.207 -3.073 16.698 1.00 52.60 C ANISOU 1637 CA VAL A 218 4915 5162 9908 -53 1244 -2406 C ATOM 1638 C VAL A 218 -18.022 -3.468 15.439 1.00 55.03 C ANISOU 1638 C VAL A 218 5073 5707 10127 -110 1151 -2763 C ATOM 1639 O VAL A 218 -17.747 -2.998 14.331 1.00 56.14 O ANISOU 1639 O VAL A 218 5181 6261 9887 -93 1149 -2921 O ATOM 1640 CB VAL A 218 -17.957 -2.010 17.565 1.00 50.05 C ANISOU 1640 CB VAL A 218 4713 4836 9468 -79 1273 -1986 C ATOM 1641 CG1 VAL A 218 -18.440 -0.857 16.720 1.00 49.83 C ANISOU 1641 CG1 VAL A 218 4689 5172 9071 -85 1249 -1916 C ATOM 1642 CG2 VAL A 218 -19.112 -2.628 18.332 1.00 50.21 C ANISOU 1642 CG2 VAL A 218 4699 4592 9788 -156 1259 -1888 C ATOM 1643 N TRP A 219 -19.014 -4.332 15.619 1.00 56.25 N ANISOU 1643 N TRP A 219 5126 5622 10624 -189 1074 -2886 N ATOM 1644 CA TRP A 219 -19.866 -4.786 14.520 1.00 59.10 C ANISOU 1644 CA TRP A 219 5308 6187 10961 -252 944 -3281 C ATOM 1645 C TRP A 219 -21.369 -4.658 14.859 1.00 59.18 C ANISOU 1645 C TRP A 219 5241 6131 11112 -356 874 -3133 C ATOM 1646 O TRP A 219 -21.834 -5.141 15.900 1.00 58.77 O ANISOU 1646 O TRP A 219 5184 5685 11461 -434 933 -2942 O ATOM 1647 CB TRP A 219 -19.498 -6.226 14.167 1.00 62.26 C ANISOU 1647 CB TRP A 219 5555 6331 11771 -261 898 -3775 C ATOM 1648 CG TRP A 219 -20.191 -6.794 12.962 1.00 66.11 C ANISOU 1648 CG TRP A 219 5829 7054 12236 -318 746 -4321 C ATOM 1649 CD1 TRP A 219 -19.722 -6.804 11.676 1.00 68.65 C ANISOU 1649 CD1 TRP A 219 6064 7844 12176 -259 703 -4773 C ATOM 1650 CD2 TRP A 219 -21.458 -7.468 12.931 1.00 68.45 C ANISOU 1650 CD2 TRP A 219 5942 7161 12904 -455 616 -4515 C ATOM 1651 NE1 TRP A 219 -20.622 -7.435 10.846 1.00 71.95 N ANISOU 1651 NE1 TRP A 219 6270 8399 12670 -333 523 -5265 N ATOM 1652 CE2 TRP A 219 -21.696 -7.852 11.589 1.00 72.30 C ANISOU 1652 CE2 TRP A 219 6238 8020 13213 -459 457 -5126 C ATOM 1653 CE3 TRP A 219 -22.418 -7.783 13.904 1.00 67.91 C ANISOU 1653 CE3 TRP A 219 5833 6678 13293 -588 631 -4244 C ATOM 1654 CZ2 TRP A 219 -22.857 -8.531 11.195 1.00 75.56 C ANISOU 1654 CZ2 TRP A 219 6405 8371 13933 -589 277 -5504 C ATOM 1655 CZ3 TRP A 219 -23.575 -8.459 13.509 1.00 71.36 C ANISOU 1655 CZ3 TRP A 219 6016 7035 14062 -737 491 -4583 C ATOM 1656 CH2 TRP A 219 -23.779 -8.826 12.167 1.00 74.89 C ANISOU 1656 CH2 TRP A 219 6262 7827 14367 -735 297 -5223 C ATOM 1657 N VAL A 220 -22.118 -4.001 13.974 1.00 59.98 N ANISOU 1657 N VAL A 220 5268 6645 10877 -353 751 -3204 N ATOM 1658 CA VAL A 220 -23.546 -3.746 14.189 1.00 60.41 C ANISOU 1658 CA VAL A 220 5198 6704 11051 -423 664 -3093 C ATOM 1659 C VAL A 220 -24.335 -3.969 12.898 1.00 64.18 C ANISOU 1659 C VAL A 220 5459 7548 11378 -446 429 -3506 C ATOM 1660 O VAL A 220 -24.053 -3.345 11.869 1.00 65.01 O ANISOU 1660 O VAL A 220 5604 8126 10971 -355 330 -3569 O ATOM 1661 CB VAL A 220 -23.786 -2.307 14.705 1.00 57.50 C ANISOU 1661 CB VAL A 220 4964 6466 10417 -343 718 -2612 C ATOM 1662 CG1 VAL A 220 -25.262 -1.995 14.796 1.00 58.66 C ANISOU 1662 CG1 VAL A 220 4929 6671 10687 -380 617 -2558 C ATOM 1663 CG2 VAL A 220 -23.143 -2.113 16.059 1.00 54.65 C ANISOU 1663 CG2 VAL A 220 4784 5779 10200 -330 923 -2268 C ATOM 1664 N MET A 221 -25.322 -4.861 12.959 1.00 66.89 N ANISOU 1664 N MET A 221 5564 7690 12163 -579 338 -3778 N ATOM 1665 CA MET A 221 -26.157 -5.162 11.799 1.00 71.12 C ANISOU 1665 CA MET A 221 5845 8566 12610 -612 73 -4239 C ATOM 1666 C MET A 221 -27.628 -5.346 12.170 1.00 73.21 C ANISOU 1666 C MET A 221 5844 8691 13283 -740 -17 -4251 C ATOM 1667 O MET A 221 -27.956 -5.827 13.262 1.00 72.46 O ANISOU 1667 O MET A 221 5706 8123 13701 -873 157 -4071 O ATOM 1668 CB MET A 221 -25.648 -6.413 11.090 1.00 74.32 C ANISOU 1668 CB MET A 221 6131 8907 13201 -662 8 -4860 C ATOM 1669 CG MET A 221 -25.922 -6.443 9.600 1.00 77.95 C ANISOU 1669 CG MET A 221 6429 9960 13227 -617 -259 -5376 C ATOM 1670 SD MET A 221 -24.691 -5.515 8.673 1.00 75.57 S ANISOU 1670 SD MET A 221 6378 10285 12052 -432 -206 -5266 S ATOM 1671 CE MET A 221 -25.346 -5.633 7.005 1.00 81.68 C ANISOU 1671 CE MET A 221 6926 11814 12293 -402 -558 -5852 C ATOM 1672 N TRP A 222 -28.507 -4.945 11.255 1.00 76.45 N ANISOU 1672 N TRP A 222 6060 9545 13442 -699 -290 -4445 N ATOM 1673 CA TRP A 222 -29.926 -5.269 11.359 1.00 79.86 C ANISOU 1673 CA TRP A 222 6140 9909 14294 -828 -430 -4616 C ATOM 1674 C TRP A 222 -30.153 -6.692 10.847 1.00 84.76 C ANISOU 1674 C TRP A 222 6491 10357 15356 -1006 -555 -5274 C ATOM 1675 O TRP A 222 -29.595 -7.097 9.817 1.00 87.41 O ANISOU 1675 O TRP A 222 6828 10966 15417 -953 -710 -5737 O ATOM 1676 CB TRP A 222 -30.777 -4.272 10.569 1.00 81.68 C ANISOU 1676 CB TRP A 222 6237 10687 14110 -684 -729 -4574 C ATOM 1677 CG TRP A 222 -30.946 -2.932 11.245 1.00 78.53 C ANISOU 1677 CG TRP A 222 5989 10312 13535 -537 -624 -3963 C ATOM 1678 CD1 TRP A 222 -30.216 -1.796 11.017 1.00 76.34 C ANISOU 1678 CD1 TRP A 222 6010 10276 12720 -342 -610 -3573 C ATOM 1679 CD2 TRP A 222 -31.909 -2.593 12.250 1.00 77.81 C ANISOU 1679 CD2 TRP A 222 5731 9984 13849 -580 -507 -3710 C ATOM 1680 NE1 TRP A 222 -30.661 -0.775 11.821 1.00 74.00 N ANISOU 1680 NE1 TRP A 222 5745 9860 12512 -248 -518 -3126 N ATOM 1681 CE2 TRP A 222 -31.700 -1.236 12.588 1.00 75.24 C ANISOU 1681 CE2 TRP A 222 5617 9756 13216 -380 -446 -3220 C ATOM 1682 CE3 TRP A 222 -32.923 -3.306 12.904 1.00 79.56 C ANISOU 1682 CE3 TRP A 222 5624 9919 14686 -783 -424 -3861 C ATOM 1683 CZ2 TRP A 222 -32.473 -0.576 13.550 1.00 74.45 C ANISOU 1683 CZ2 TRP A 222 5403 9500 13386 -346 -315 -2942 C ATOM 1684 CZ3 TRP A 222 -33.692 -2.649 13.857 1.00 78.75 C ANISOU 1684 CZ3 TRP A 222 5407 9708 14806 -767 -263 -3542 C ATOM 1685 CH2 TRP A 222 -33.462 -1.297 14.170 1.00 76.36 C ANISOU 1685 CH2 TRP A 222 5314 9530 14168 -535 -215 -3118 C ATOM 1686 N MET A 223 -30.956 -7.455 11.580 1.00 86.63 N ANISOU 1686 N MET A 223 6485 10135 16297 -1228 -467 -5328 N ATOM 1687 CA MET A 223 -31.174 -8.860 11.260 1.00 91.44 C ANISOU 1687 CA MET A 223 6824 10423 17496 -1435 -555 -5922 C ATOM 1688 C MET A 223 -32.636 -9.231 11.350 1.00 95.09 C ANISOU 1688 C MET A 223 6843 10788 18497 -1648 -673 -6130 C ATOM 1689 O MET A 223 -33.371 -8.702 12.184 1.00 93.57 O ANISOU 1689 O MET A 223 6578 10519 18457 -1701 -523 -5695 O ATOM 1690 CB MET A 223 -30.387 -9.776 12.206 1.00 90.71 C ANISOU 1690 CB MET A 223 6892 9640 17934 -1553 -261 -5760 C ATOM 1691 CG MET A 223 -28.868 -9.647 12.159 1.00 88.76 C ANISOU 1691 CG MET A 223 7014 9403 17308 -1361 -146 -5646 C ATOM 1692 SD MET A 223 -28.035 -11.257 12.049 1.00 96.76 S ANISOU 1692 SD MET A 223 7973 9822 18968 -1449 -123 -6152 S ATOM 1693 CE MET A 223 -28.918 -12.266 13.251 1.00 98.12 C ANISOU 1693 CE MET A 223 7947 9184 20151 -1773 41 -5908 C ATOM 1694 N ARG A 224 -33.042 -10.144 10.474 1.00100.31 N ANISOU 1694 N ARG A 224 7179 11475 19459 -1772 -939 -6847 N ATOM 1695 CA ARG A 224 -34.305 -10.852 10.597 1.00104.80 C ANISOU 1695 CA ARG A 224 7270 11790 20758 -2052 -1028 -7160 C ATOM 1696 C ARG A 224 -33.923 -12.323 10.727 1.00107.94 C ANISOU 1696 C ARG A 224 7576 11523 21915 -2282 -942 -7557 C ATOM 1697 O ARG A 224 -33.569 -12.969 9.741 1.00111.66 O ANISOU 1697 O ARG A 224 7950 12096 22380 -2256 -1183 -8255 O ATOM 1698 CB ARG A 224 -35.197 -10.588 9.373 1.00109.37 C ANISOU 1698 CB ARG A 224 7491 13008 21056 -1988 -1493 -7722 C ATOM 1699 CG ARG A 224 -36.453 -11.461 9.268 1.00115.93 C ANISOU 1699 CG ARG A 224 7746 13614 22687 -2294 -1660 -8245 C ATOM 1700 CD ARG A 224 -37.310 -11.094 8.054 1.00120.49 C ANISOU 1700 CD ARG A 224 7970 14914 22898 -2186 -2178 -8787 C ATOM 1701 NE ARG A 224 -38.197 -9.955 8.315 1.00118.85 N ANISOU 1701 NE ARG A 224 7639 15067 22450 -2059 -2244 -8333 N ATOM 1702 CZ ARG A 224 -37.988 -8.709 7.889 1.00115.70 C ANISOU 1702 CZ ARG A 224 7487 15266 21206 -1719 -2403 -7979 C ATOM 1703 NH1 ARG A 224 -36.918 -8.410 7.165 1.00114.11 N ANISOU 1703 NH1 ARG A 224 7677 15428 20253 -1495 -2487 -7993 N ATOM 1704 NH2 ARG A 224 -38.860 -7.754 8.188 1.00114.61 N ANISOU 1704 NH2 ARG A 224 7185 15351 21011 -1604 -2468 -7605 N ATOM 1705 N GLY A 225 -33.949 -12.830 11.957 1.00106.82 N ANISOU 1705 N GLY A 225 7478 10704 22406 -2492 -592 -7096 N ATOM 1706 CA GLY A 225 -33.545 -14.207 12.243 1.00110.07 C ANISOU 1706 CA GLY A 225 7838 10358 23625 -2704 -485 -7317 C ATOM 1707 C GLY A 225 -32.042 -14.421 12.178 1.00107.39 C ANISOU 1707 C GLY A 225 7897 9868 23039 -2488 -414 -7293 C ATOM 1708 O GLY A 225 -31.324 -14.117 13.132 1.00103.10 O ANISOU 1708 O GLY A 225 7710 9106 22356 -2402 -133 -6624 O ATOM 1709 N ASP A 226 -31.574 -14.948 11.047 1.00110.49 N ANISOU 1709 N ASP A 226 8197 10410 23374 -2396 -676 -8068 N ATOM 1710 CA ASP A 226 -30.150 -15.217 10.817 1.00108.94 C ANISOU 1710 CA ASP A 226 8293 10121 22977 -2179 -627 -8201 C ATOM 1711 C ASP A 226 -29.643 -14.573 9.520 1.00108.51 C ANISOU 1711 C ASP A 226 8308 10915 22006 -1908 -857 -8683 C ATOM 1712 O ASP A 226 -28.511 -14.829 9.086 1.00108.49 O ANISOU 1712 O ASP A 226 8462 10957 21804 -1731 -839 -8972 O ATOM 1713 CB ASP A 226 -29.876 -16.730 10.814 1.00114.60 C ANISOU 1713 CB ASP A 226 8822 10046 24674 -2336 -649 -8706 C ATOM 1714 CG ASP A 226 -30.523 -17.452 9.631 1.00121.26 C ANISOU 1714 CG ASP A 226 9221 11020 25834 -2455 -992 -9750 C ATOM 1715 OD1 ASP A 226 -29.786 -18.098 8.858 1.00124.11 O ANISOU 1715 OD1 ASP A 226 9534 11349 26272 -2336 -1125 -10466 O ATOM 1716 OD2 ASP A 226 -31.761 -17.380 9.474 1.00123.78 O ANISOU 1716 OD2 ASP A 226 9210 11489 26333 -2660 -1136 -9902 O ATOM 1717 N GLN A 227 -30.493 -13.746 8.909 1.00108.47 N ANISOU 1717 N GLN A 227 8169 11592 21453 -1874 -1069 -8750 N ATOM 1718 CA GLN A 227 -30.145 -13.008 7.695 1.00108.46 C ANISOU 1718 CA GLN A 227 8248 12476 20487 -1630 -1291 -9067 C ATOM 1719 C GLN A 227 -29.792 -11.555 8.009 1.00101.94 C ANISOU 1719 C GLN A 227 7786 12092 18855 -1422 -1151 -8270 C ATOM 1720 O GLN A 227 -30.469 -10.897 8.802 1.00 98.90 O ANISOU 1720 O GLN A 227 7423 11617 18538 -1470 -1055 -7672 O ATOM 1721 CB GLN A 227 -31.289 -13.059 6.674 1.00113.90 C ANISOU 1721 CB GLN A 227 8537 13678 21063 -1697 -1696 -9699 C ATOM 1722 CG GLN A 227 -31.492 -14.427 6.023 1.00121.64 C ANISOU 1722 CG GLN A 227 9139 14389 22689 -1862 -1907 -10703 C ATOM 1723 CD GLN A 227 -30.523 -14.695 4.870 1.00124.68 C ANISOU 1723 CD GLN A 227 9589 15258 22527 -1666 -2031 -11418 C ATOM 1724 OE1 GLN A 227 -30.638 -14.096 3.800 1.00126.58 O ANISOU 1724 OE1 GLN A 227 9806 16393 21896 -1509 -2289 -11710 O ATOM 1725 NE2 GLN A 227 -29.574 -15.613 5.082 1.00125.41 N ANISOU 1725 NE2 GLN A 227 9744 14774 23132 -1667 -1849 -11703 N ATOM 1726 N GLU A 228 -28.721 -11.072 7.383 1.00100.27 N ANISOU 1726 N GLU A 228 7834 12345 17919 -1200 -1123 -8295 N ATOM 1727 CA GLU A 228 -28.332 -9.666 7.451 1.00 95.19 C ANISOU 1727 CA GLU A 228 7511 12171 16486 -1007 -1030 -7625 C ATOM 1728 C GLU A 228 -29.269 -8.826 6.586 1.00 97.21 C ANISOU 1728 C GLU A 228 7632 13148 16155 -931 -1352 -7657 C ATOM 1729 O GLU A 228 -29.861 -9.332 5.630 1.00102.92 O ANISOU 1729 O GLU A 228 8061 14212 16833 -971 -1666 -8328 O ATOM 1730 CB GLU A 228 -26.885 -9.483 6.969 1.00 93.96 C ANISOU 1730 CB GLU A 228 7621 12295 15784 -831 -887 -7680 C ATOM 1731 CG GLU A 228 -25.820 -10.051 7.908 1.00 91.19 C ANISOU 1731 CG GLU A 228 7445 11280 15924 -837 -579 -7496 C ATOM 1732 CD GLU A 228 -24.383 -9.830 7.416 1.00 90.63 C ANISOU 1732 CD GLU A 228 7578 11521 15336 -660 -430 -7579 C ATOM 1733 OE1 GLU A 228 -23.505 -10.640 7.786 1.00 90.29 O ANISOU 1733 OE1 GLU A 228 7552 11009 15746 -642 -279 -7767 O ATOM 1734 OE2 GLU A 228 -24.124 -8.856 6.671 1.00 90.25 O ANISOU 1734 OE2 GLU A 228 7656 12173 14461 -539 -457 -7436 O ATOM 1735 N GLN A 229 -29.412 -7.550 6.928 1.00 93.02 N ANISOU 1735 N GLN A 229 7302 12838 15202 -809 -1300 -6951 N ATOM 1736 CA GLN A 229 -30.123 -6.613 6.070 1.00 95.12 C ANISOU 1736 CA GLN A 229 7495 13804 14841 -674 -1618 -6870 C ATOM 1737 C GLN A 229 -29.104 -5.689 5.417 1.00 93.95 C ANISOU 1737 C GLN A 229 7685 14201 13811 -474 -1563 -6562 C ATOM 1738 O GLN A 229 -28.489 -4.859 6.085 1.00 89.04 O ANISOU 1738 O GLN A 229 7361 13411 13061 -399 -1308 -5916 O ATOM 1739 CB GLN A 229 -31.175 -5.828 6.859 1.00 92.85 C ANISOU 1739 CB GLN A 229 7122 13351 14805 -674 -1639 -6331 C ATOM 1740 CG GLN A 229 -32.128 -6.693 7.690 1.00 93.66 C ANISOU 1740 CG GLN A 229 6895 12874 15818 -913 -1586 -6520 C ATOM 1741 CD GLN A 229 -32.803 -7.791 6.880 1.00100.15 C ANISOU 1741 CD GLN A 229 7305 13793 16955 -1063 -1893 -7355 C ATOM 1742 OE1 GLN A 229 -32.695 -8.974 7.206 1.00101.88 O ANISOU 1742 OE1 GLN A 229 7387 13485 17839 -1271 -1775 -7741 O ATOM 1743 NE2 GLN A 229 -33.493 -7.403 5.815 1.00104.21 N ANISOU 1743 NE2 GLN A 229 7612 14972 17012 -953 -2313 -7639 N ATOM 1744 N GLN A 230 -28.925 -5.851 4.107 1.00 99.17 N ANISOU 1744 N GLN A 230 8282 15532 13865 -403 -1794 -7047 N ATOM 1745 CA GLN A 230 -27.831 -5.206 3.365 1.00 99.53 C ANISOU 1745 CA GLN A 230 8616 16137 13065 -260 -1687 -6858 C ATOM 1746 C GLN A 230 -27.867 -3.673 3.331 1.00 97.53 C ANISOU 1746 C GLN A 230 8610 16201 12245 -107 -1706 -6017 C ATOM 1747 O GLN A 230 -26.821 -3.034 3.193 1.00 95.80 O ANISOU 1747 O GLN A 230 8679 16164 11557 -40 -1474 -5634 O ATOM 1748 CB GLN A 230 -27.740 -5.764 1.940 1.00106.46 C ANISOU 1748 CB GLN A 230 9336 17750 13364 -227 -1932 -7612 C ATOM 1749 CG GLN A 230 -29.016 -5.603 1.112 1.00112.15 C ANISOU 1749 CG GLN A 230 9790 19034 13786 -183 -2431 -7854 C ATOM 1750 CD GLN A 230 -28.958 -6.358 -0.199 1.00119.64 C ANISOU 1750 CD GLN A 230 10540 20679 14240 -173 -2684 -8751 C ATOM 1751 OE1 GLN A 230 -28.065 -6.135 -1.017 1.00122.10 O ANISOU 1751 OE1 GLN A 230 11030 21608 13755 -82 -2582 -8815 O ATOM 1752 NE2 GLN A 230 -29.912 -7.259 -0.407 1.00123.75 N ANISOU 1752 NE2 GLN A 230 10664 21124 15231 -278 -3002 -9482 N ATOM 1753 N GLY A 231 -29.062 -3.097 3.455 1.00 98.32 N ANISOU 1753 N GLY A 231 8569 16338 12450 -57 -1981 -5747 N ATOM 1754 CA GLY A 231 -29.244 -1.642 3.448 1.00 97.33 C ANISOU 1754 CA GLY A 231 8636 16425 11921 109 -2051 -4961 C ATOM 1755 C GLY A 231 -28.675 -0.910 4.657 1.00 91.05 C ANISOU 1755 C GLY A 231 8105 15042 11448 114 -1681 -4298 C ATOM 1756 O GLY A 231 -28.429 0.301 4.592 1.00 90.04 O ANISOU 1756 O GLY A 231 8199 15055 10957 242 -1660 -3662 O ATOM 1757 N THR A 232 -28.474 -1.644 5.756 1.00 87.42 N ANISOU 1757 N THR A 232 7615 13923 11676 -26 -1405 -4444 N ATOM 1758 CA THR A 232 -27.876 -1.116 6.992 1.00 81.82 C ANISOU 1758 CA THR A 232 7140 12667 11281 -35 -1053 -3918 C ATOM 1759 C THR A 232 -26.766 -0.089 6.721 1.00 80.69 C ANISOU 1759 C THR A 232 7327 12745 10587 63 -889 -3426 C ATOM 1760 O THR A 232 -25.685 -0.449 6.248 1.00 81.32 O ANISOU 1760 O THR A 232 7523 13012 10364 31 -730 -3617 O ATOM 1761 CB THR A 232 -27.316 -2.268 7.881 1.00 79.09 C ANISOU 1761 CB THR A 232 6785 11746 11521 -195 -768 -4214 C ATOM 1762 OG1 THR A 232 -28.357 -3.207 8.175 1.00 80.63 O ANISOU 1762 OG1 THR A 232 6665 11673 12296 -326 -888 -4608 O ATOM 1763 CG2 THR A 232 -26.754 -1.735 9.183 1.00 73.14 C ANISOU 1763 CG2 THR A 232 6257 10497 11037 -193 -450 -3692 C ATOM 1764 N HIS A 233 -27.052 1.184 6.999 1.00 79.76 N ANISOU 1764 N HIS A 233 7325 12594 10385 180 -925 -2820 N ATOM 1765 CA HIS A 233 -26.052 2.246 6.899 1.00 78.88 C ANISOU 1765 CA HIS A 233 7510 12565 9894 242 -749 -2287 C ATOM 1766 C HIS A 233 -25.461 2.555 8.277 1.00 73.39 C ANISOU 1766 C HIS A 233 6965 11254 9664 200 -423 -2003 C ATOM 1767 O HIS A 233 -26.131 3.100 9.161 1.00 71.28 O ANISOU 1767 O HIS A 233 6664 10639 9782 250 -430 -1750 O ATOM 1768 CB HIS A 233 -26.624 3.505 6.214 1.00 82.29 C ANISOU 1768 CB HIS A 233 7989 13344 9932 405 -1019 -1779 C ATOM 1769 CG HIS A 233 -25.644 4.642 6.089 1.00 83.00 C ANISOU 1769 CG HIS A 233 8369 13465 9703 439 -837 -1181 C ATOM 1770 ND1 HIS A 233 -24.503 4.569 5.314 1.00 85.80 N ANISOU 1770 ND1 HIS A 233 8876 14202 9521 367 -661 -1179 N ATOM 1771 CD2 HIS A 233 -25.646 5.886 6.631 1.00 82.15 C ANISOU 1771 CD2 HIS A 233 8395 13037 9780 524 -794 -587 C ATOM 1772 CE1 HIS A 233 -23.840 5.711 5.395 1.00 85.04 C ANISOU 1772 CE1 HIS A 233 8995 14009 9306 380 -507 -572 C ATOM 1773 NE2 HIS A 233 -24.513 6.527 6.187 1.00 83.11 N ANISOU 1773 NE2 HIS A 233 8749 13315 9513 478 -599 -213 N ATOM 1774 N ARG A 234 -24.202 2.166 8.441 1.00 71.74 N ANISOU 1774 N ARG A 234 6895 10954 9409 119 -147 -2101 N ATOM 1775 CA ARG A 234 -23.395 2.473 9.616 1.00 67.59 C ANISOU 1775 CA ARG A 234 6528 9947 9206 86 141 -1849 C ATOM 1776 C ARG A 234 -23.037 3.974 9.624 1.00 66.65 C ANISOU 1776 C ARG A 234 6596 9843 8886 159 188 -1255 C ATOM 1777 O ARG A 234 -22.683 4.538 8.587 1.00 69.65 O ANISOU 1777 O ARG A 234 7056 10638 8770 182 138 -1051 O ATOM 1778 CB ARG A 234 -22.120 1.612 9.566 1.00 67.50 C ANISOU 1778 CB ARG A 234 6563 9917 9166 3 365 -2162 C ATOM 1779 CG ARG A 234 -21.359 1.434 10.883 1.00 65.18 C ANISOU 1779 CG ARG A 234 6361 9101 9302 -34 609 -2078 C ATOM 1780 CD ARG A 234 -19.955 0.809 10.674 1.00 68.15 C ANISOU 1780 CD ARG A 234 6768 9521 9603 -72 804 -2329 C ATOM 1781 NE ARG A 234 -19.045 1.627 9.852 1.00 72.24 N ANISOU 1781 NE ARG A 234 7384 10430 9634 -71 915 -2125 N ATOM 1782 CZ ARG A 234 -18.434 2.750 10.251 1.00 71.75 C ANISOU 1782 CZ ARG A 234 7466 10262 9534 -76 1049 -1667 C ATOM 1783 NH1 ARG A 234 -18.633 3.239 11.469 1.00 69.18 N ANISOU 1783 NH1 ARG A 234 7211 9486 9590 -57 1071 -1407 N ATOM 1784 NH2 ARG A 234 -17.625 3.404 9.423 1.00 73.95 N ANISOU 1784 NH2 ARG A 234 7804 10903 9392 -114 1173 -1479 N ATOM 1785 N GLY A 235 -23.137 4.618 10.785 1.00 63.12 N ANISOU 1785 N GLY A 235 6210 8947 8826 187 288 -982 N ATOM 1786 CA GLY A 235 -22.730 6.023 10.921 1.00 62.50 C ANISOU 1786 CA GLY A 235 6291 8763 8693 243 345 -472 C ATOM 1787 C GLY A 235 -21.228 6.166 11.130 1.00 60.77 C ANISOU 1787 C GLY A 235 6224 8458 8407 148 620 -394 C ATOM 1788 O GLY A 235 -20.456 5.243 10.827 1.00 60.94 O ANISOU 1788 O GLY A 235 6228 8637 8291 66 740 -711 O ATOM 1789 N ASP A 236 -20.804 7.323 11.641 1.00 59.31 N ANISOU 1789 N ASP A 236 6156 8012 8368 162 713 -11 N ATOM 1790 CA ASP A 236 -19.415 7.513 12.066 1.00 57.04 C ANISOU 1790 CA ASP A 236 5965 7572 8136 62 967 35 C ATOM 1791 C ASP A 236 -19.290 7.170 13.534 1.00 52.70 C ANISOU 1791 C ASP A 236 5405 6599 8018 64 1065 -152 C ATOM 1792 O ASP A 236 -20.274 7.203 14.275 1.00 51.53 O ANISOU 1792 O ASP A 236 5207 6242 8129 139 976 -183 O ATOM 1793 CB ASP A 236 -18.972 8.958 11.873 1.00 58.75 C ANISOU 1793 CB ASP A 236 6291 7693 8339 48 1012 527 C ATOM 1794 CG ASP A 236 -19.438 9.535 10.573 1.00 63.83 C ANISOU 1794 CG ASP A 236 6965 8700 8588 84 854 872 C ATOM 1795 OD1 ASP A 236 -18.985 9.045 9.514 1.00 67.34 O ANISOU 1795 OD1 ASP A 236 7409 9621 8556 13 903 802 O ATOM 1796 OD2 ASP A 236 -20.258 10.479 10.614 1.00 65.52 O ANISOU 1796 OD2 ASP A 236 7194 8740 8962 200 674 1206 O ATOM 1797 N PHE A 237 -18.080 6.844 13.964 1.00 50.65 N ANISOU 1797 N PHE A 237 5178 6249 7819 -12 1248 -275 N ATOM 1798 CA PHE A 237 -17.833 6.724 15.384 1.00 47.38 C ANISOU 1798 CA PHE A 237 4781 5471 7750 0 1321 -368 C ATOM 1799 C PHE A 237 -17.891 8.108 16.025 1.00 47.21 C ANISOU 1799 C PHE A 237 4822 5190 7926 33 1324 -90 C ATOM 1800 O PHE A 237 -17.271 9.068 15.551 1.00 48.65 O ANISOU 1800 O PHE A 237 5050 5377 8056 -16 1373 159 O ATOM 1801 CB PHE A 237 -16.508 6.023 15.659 1.00 46.24 C ANISOU 1801 CB PHE A 237 4627 5308 7633 -60 1463 -574 C ATOM 1802 CG PHE A 237 -16.533 4.547 15.353 1.00 46.63 C ANISOU 1802 CG PHE A 237 4595 5471 7653 -60 1446 -921 C ATOM 1803 CD1 PHE A 237 -17.012 3.632 16.296 1.00 44.92 C ANISOU 1803 CD1 PHE A 237 4355 5013 7698 -28 1406 -1081 C ATOM 1804 CD2 PHE A 237 -16.089 4.069 14.122 1.00 48.51 C ANISOU 1804 CD2 PHE A 237 4768 6052 7613 -99 1480 -1094 C ATOM 1805 CE1 PHE A 237 -17.047 2.275 16.024 1.00 44.21 C ANISOU 1805 CE1 PHE A 237 4178 4937 7683 -36 1379 -1392 C ATOM 1806 CE2 PHE A 237 -16.116 2.708 13.840 1.00 48.92 C ANISOU 1806 CE2 PHE A 237 4718 6160 7709 -88 1452 -1489 C ATOM 1807 CZ PHE A 237 -16.603 1.811 14.795 1.00 47.67 C ANISOU 1807 CZ PHE A 237 4537 5673 7904 -58 1390 -1630 C ATOM 1808 N LEU A 238 -18.690 8.213 17.081 1.00 45.81 N ANISOU 1808 N LEU A 238 4627 4784 7994 111 1282 -143 N ATOM 1809 CA LEU A 238 -18.798 9.445 17.841 1.00 45.58 C ANISOU 1809 CA LEU A 238 4628 4483 8209 165 1284 0 C ATOM 1810 C LEU A 238 -18.337 9.201 19.281 1.00 43.44 C ANISOU 1810 C LEU A 238 4375 4026 8106 164 1376 -200 C ATOM 1811 O LEU A 238 -18.671 8.169 19.877 1.00 41.96 O ANISOU 1811 O LEU A 238 4165 3872 7906 173 1397 -375 O ATOM 1812 CB LEU A 238 -20.232 9.976 17.791 1.00 46.86 C ANISOU 1812 CB LEU A 238 4718 4595 8490 291 1147 91 C ATOM 1813 CG LEU A 238 -20.916 10.111 16.419 1.00 49.27 C ANISOU 1813 CG LEU A 238 4986 5137 8599 331 983 287 C ATOM 1814 CD1 LEU A 238 -22.306 10.724 16.572 1.00 50.24 C ANISOU 1814 CD1 LEU A 238 4994 5156 8938 492 824 355 C ATOM 1815 CD2 LEU A 238 -20.094 10.904 15.407 1.00 51.02 C ANISOU 1815 CD2 LEU A 238 5301 5438 8646 270 987 617 C ATOM 1816 N PRO A 239 -17.553 10.144 19.844 1.00 43.47 N ANISOU 1816 N PRO A 239 4414 3837 8267 146 1421 -167 N ATOM 1817 CA PRO A 239 -16.987 9.914 21.170 1.00 41.96 C ANISOU 1817 CA PRO A 239 4238 3546 8159 151 1474 -375 C ATOM 1818 C PRO A 239 -17.950 10.282 22.280 1.00 42.09 C ANISOU 1818 C PRO A 239 4233 3455 8306 256 1466 -485 C ATOM 1819 O PRO A 239 -18.763 11.188 22.112 1.00 43.48 O ANISOU 1819 O PRO A 239 4364 3518 8639 331 1421 -412 O ATOM 1820 CB PRO A 239 -15.781 10.847 21.205 1.00 42.43 C ANISOU 1820 CB PRO A 239 4300 3467 8353 74 1506 -341 C ATOM 1821 CG PRO A 239 -16.089 11.924 20.216 1.00 44.98 C ANISOU 1821 CG PRO A 239 4621 3697 8771 55 1479 -65 C ATOM 1822 CD PRO A 239 -17.210 11.478 19.323 1.00 45.44 C ANISOU 1822 CD PRO A 239 4678 3938 8651 117 1408 67 C ATOM 1823 N ASN A 240 -17.866 9.558 23.391 1.00 41.25 N ANISOU 1823 N ASN A 240 4146 3401 8127 271 1511 -650 N ATOM 1824 CA ASN A 240 -18.468 9.991 24.645 1.00 42.11 C ANISOU 1824 CA ASN A 240 4234 3472 8293 355 1549 -802 C ATOM 1825 C ASN A 240 -17.452 10.799 25.467 1.00 43.05 C ANISOU 1825 C ASN A 240 4377 3491 8488 357 1530 -962 C ATOM 1826 O ASN A 240 -16.270 10.846 25.118 1.00 43.06 O ANISOU 1826 O ASN A 240 4397 3455 8509 279 1496 -938 O ATOM 1827 CB ASN A 240 -18.983 8.785 25.426 1.00 41.55 C ANISOU 1827 CB ASN A 240 4175 3559 8053 354 1621 -844 C ATOM 1828 CG ASN A 240 -20.126 8.084 24.720 1.00 41.59 C ANISOU 1828 CG ASN A 240 4105 3628 8070 336 1636 -752 C ATOM 1829 OD1 ASN A 240 -21.077 8.722 24.277 1.00 42.63 O ANISOU 1829 OD1 ASN A 240 4138 3732 8327 393 1611 -736 O ATOM 1830 ND2 ASN A 240 -20.045 6.763 24.623 1.00 41.62 N ANISOU 1830 ND2 ASN A 240 4129 3696 7987 263 1654 -709 N ATOM 1831 N ALA A 241 -17.908 11.447 26.540 1.00 44.68 N ANISOU 1831 N ALA A 241 4551 3676 8750 442 1556 -1169 N ATOM 1832 CA ALA A 241 -17.013 12.205 27.421 1.00 46.03 C ANISOU 1832 CA ALA A 241 4719 3781 8991 450 1513 -1412 C ATOM 1833 C ALA A 241 -16.169 11.289 28.306 1.00 45.92 C ANISOU 1833 C ALA A 241 4772 3987 8690 430 1488 -1492 C ATOM 1834 O ALA A 241 -15.098 11.677 28.755 1.00 46.95 O ANISOU 1834 O ALA A 241 4887 4095 8857 407 1401 -1658 O ATOM 1835 CB ALA A 241 -17.793 13.182 28.268 1.00 48.01 C ANISOU 1835 CB ALA A 241 4892 3970 9381 565 1543 -1684 C ATOM 1836 N ASP A 242 -16.647 10.069 28.539 1.00 45.54 N ANISOU 1836 N ASP A 242 4780 4130 8392 437 1545 -1359 N ATOM 1837 CA ASP A 242 -15.968 9.125 29.424 1.00 46.28 C ANISOU 1837 CA ASP A 242 4950 4415 8218 444 1501 -1355 C ATOM 1838 C ASP A 242 -15.012 8.191 28.685 1.00 44.87 C ANISOU 1838 C ASP A 242 4793 4192 8062 388 1424 -1192 C ATOM 1839 O ASP A 242 -14.620 7.157 29.218 1.00 45.25 O ANISOU 1839 O ASP A 242 4900 4346 7946 411 1376 -1105 O ATOM 1840 CB ASP A 242 -16.987 8.312 30.219 1.00 47.31 C ANISOU 1840 CB ASP A 242 5126 4749 8101 472 1622 -1263 C ATOM 1841 CG ASP A 242 -17.780 7.357 29.347 1.00 46.93 C ANISOU 1841 CG ASP A 242 5066 4638 8127 408 1701 -1021 C ATOM 1842 OD1 ASP A 242 -17.602 7.377 28.107 1.00 46.63 O ANISOU 1842 OD1 ASP A 242 4993 4446 8280 365 1652 -957 O ATOM 1843 OD2 ASP A 242 -18.585 6.587 29.910 1.00 48.77 O ANISOU 1843 OD2 ASP A 242 5313 4998 8220 389 1817 -905 O ATOM 1844 N GLU A 243 -14.647 8.566 27.463 1.00 44.11 N ANISOU 1844 N GLU A 243 4642 3945 8173 322 1418 -1146 N ATOM 1845 CA GLU A 243 -13.618 7.865 26.676 1.00 43.73 C ANISOU 1845 CA GLU A 243 4566 3882 8167 270 1373 -1078 C ATOM 1846 C GLU A 243 -14.048 6.473 26.226 1.00 42.82 C ANISOU 1846 C GLU A 243 4483 3805 7981 270 1402 -936 C ATOM 1847 O GLU A 243 -13.258 5.524 26.191 1.00 42.67 O ANISOU 1847 O GLU A 243 4453 3793 7965 287 1341 -929 O ATOM 1848 CB GLU A 243 -12.257 7.864 27.391 1.00 44.77 C ANISOU 1848 CB GLU A 243 4659 4058 8295 292 1249 -1221 C ATOM 1849 CG GLU A 243 -11.599 9.256 27.424 1.00 47.17 C ANISOU 1849 CG GLU A 243 4870 4260 8793 236 1218 -1397 C ATOM 1850 CD GLU A 243 -10.082 9.205 27.559 1.00 49.59 C ANISOU 1850 CD GLU A 243 5055 4591 9196 207 1106 -1534 C ATOM 1851 OE1 GLU A 243 -9.375 9.830 26.717 1.00 49.18 O ANISOU 1851 OE1 GLU A 243 4882 4431 9375 86 1158 -1546 O ATOM 1852 OE2 GLU A 243 -9.607 8.535 28.508 1.00 50.60 O ANISOU 1852 OE2 GLU A 243 5195 4861 9169 305 966 -1608 O ATOM 1853 N THR A 244 -15.333 6.372 25.898 1.00 42.58 N ANISOU 1853 N THR A 244 4464 3774 7942 258 1481 -852 N ATOM 1854 CA THR A 244 -15.894 5.202 25.247 1.00 41.83 C ANISOU 1854 CA THR A 244 4359 3677 7859 226 1508 -765 C ATOM 1855 C THR A 244 -16.520 5.700 23.961 1.00 41.82 C ANISOU 1855 C THR A 244 4298 3682 7911 184 1530 -744 C ATOM 1856 O THR A 244 -16.600 6.913 23.729 1.00 42.12 O ANISOU 1856 O THR A 244 4321 3693 7990 191 1530 -732 O ATOM 1857 CB THR A 244 -16.980 4.547 26.091 1.00 42.23 C ANISOU 1857 CB THR A 244 4438 3752 7854 231 1574 -681 C ATOM 1858 OG1 THR A 244 -18.037 5.486 26.305 1.00 42.02 O ANISOU 1858 OG1 THR A 244 4374 3770 7823 247 1648 -710 O ATOM 1859 CG2 THR A 244 -16.428 4.070 27.424 1.00 42.85 C ANISOU 1859 CG2 THR A 244 4602 3878 7800 279 1544 -627 C ATOM 1860 N TRP A 245 -16.982 4.770 23.133 1.00 42.12 N ANISOU 1860 N TRP A 245 4294 3747 7961 147 1528 -738 N ATOM 1861 CA TRP A 245 -17.509 5.123 21.816 1.00 42.40 C ANISOU 1861 CA TRP A 245 4270 3866 7974 118 1507 -722 C ATOM 1862 C TRP A 245 -19.041 5.066 21.661 1.00 42.77 C ANISOU 1862 C TRP A 245 4247 3943 8061 124 1497 -696 C ATOM 1863 O TRP A 245 -19.744 4.480 22.480 1.00 42.79 O ANISOU 1863 O TRP A 245 4228 3900 8132 116 1547 -703 O ATOM 1864 CB TRP A 245 -16.787 4.318 20.726 1.00 42.82 C ANISOU 1864 CB TRP A 245 4283 4009 7976 75 1489 -821 C ATOM 1865 CG TRP A 245 -15.367 4.770 20.506 1.00 42.20 C ANISOU 1865 CG TRP A 245 4208 3962 7863 60 1519 -841 C ATOM 1866 CD1 TRP A 245 -14.236 4.119 20.889 1.00 42.22 C ANISOU 1866 CD1 TRP A 245 4189 3920 7931 78 1519 -952 C ATOM 1867 CD2 TRP A 245 -14.938 5.971 19.857 1.00 42.43 C ANISOU 1867 CD2 TRP A 245 4234 4058 7828 17 1553 -730 C ATOM 1868 NE1 TRP A 245 -13.127 4.833 20.516 1.00 42.53 N ANISOU 1868 NE1 TRP A 245 4183 4024 7953 38 1566 -962 N ATOM 1869 CE2 TRP A 245 -13.529 5.979 19.884 1.00 42.96 C ANISOU 1869 CE2 TRP A 245 4257 4137 7929 -17 1603 -807 C ATOM 1870 CE3 TRP A 245 -15.607 7.042 19.254 1.00 43.10 C ANISOU 1870 CE3 TRP A 245 4335 4173 7867 5 1539 -546 C ATOM 1871 CZ2 TRP A 245 -12.772 7.021 19.337 1.00 43.74 C ANISOU 1871 CZ2 TRP A 245 4321 4278 8020 -103 1677 -703 C ATOM 1872 CZ3 TRP A 245 -14.851 8.074 18.705 1.00 44.73 C ANISOU 1872 CZ3 TRP A 245 4540 4392 8063 -63 1593 -397 C ATOM 1873 CH2 TRP A 245 -13.448 8.054 18.752 1.00 44.30 C ANISOU 1873 CH2 TRP A 245 4436 4350 8046 -136 1680 -476 C ATOM 1874 N TYR A 246 -19.527 5.710 20.604 1.00 43.63 N ANISOU 1874 N TYR A 246 4307 4146 8126 136 1432 -643 N ATOM 1875 CA TYR A 246 -20.933 5.706 20.228 1.00 45.09 C ANISOU 1875 CA TYR A 246 4377 4394 8361 159 1370 -639 C ATOM 1876 C TYR A 246 -21.041 5.582 18.713 1.00 46.34 C ANISOU 1876 C TYR A 246 4487 4752 8369 142 1251 -643 C ATOM 1877 O TYR A 246 -20.327 6.260 17.974 1.00 47.05 O ANISOU 1877 O TYR A 246 4640 4927 8310 145 1230 -526 O ATOM 1878 CB TYR A 246 -21.619 7.000 20.695 1.00 45.99 C ANISOU 1878 CB TYR A 246 4460 4432 8584 256 1363 -546 C ATOM 1879 CG TYR A 246 -23.074 7.153 20.269 1.00 48.19 C ANISOU 1879 CG TYR A 246 4573 4781 8957 315 1271 -545 C ATOM 1880 CD1 TYR A 246 -24.105 7.047 21.197 1.00 48.96 C ANISOU 1880 CD1 TYR A 246 4544 4842 9217 341 1354 -632 C ATOM 1881 CD2 TYR A 246 -23.411 7.422 18.937 1.00 50.27 C ANISOU 1881 CD2 TYR A 246 4784 5190 9127 348 1099 -455 C ATOM 1882 CE1 TYR A 246 -25.434 7.187 20.811 1.00 51.69 C ANISOU 1882 CE1 TYR A 246 4680 5261 9697 400 1265 -663 C ATOM 1883 CE2 TYR A 246 -24.728 7.560 18.541 1.00 52.62 C ANISOU 1883 CE2 TYR A 246 4898 5571 9523 424 966 -466 C ATOM 1884 CZ TYR A 246 -25.740 7.442 19.479 1.00 53.32 C ANISOU 1884 CZ TYR A 246 4828 5589 9841 451 1047 -586 C ATOM 1885 OH TYR A 246 -27.053 7.589 19.081 1.00 55.13 O ANISOU 1885 OH TYR A 246 4820 5910 10215 532 908 -627 O ATOM 1886 N LEU A 247 -21.948 4.723 18.261 1.00 47.30 N ANISOU 1886 N LEU A 247 4483 4970 8520 113 1178 -779 N ATOM 1887 CA LEU A 247 -22.234 4.556 16.842 1.00 49.07 C ANISOU 1887 CA LEU A 247 4635 5456 8555 109 1028 -841 C ATOM 1888 C LEU A 247 -23.688 4.153 16.668 1.00 50.58 C ANISOU 1888 C LEU A 247 4629 5709 8879 114 906 -958 C ATOM 1889 O LEU A 247 -24.268 3.521 17.553 1.00 50.26 O ANISOU 1889 O LEU A 247 4503 5503 9091 61 989 -1050 O ATOM 1890 CB LEU A 247 -21.336 3.473 16.253 1.00 49.28 C ANISOU 1890 CB LEU A 247 4676 5580 8468 32 1058 -1065 C ATOM 1891 CG LEU A 247 -21.768 2.857 14.923 1.00 52.24 C ANISOU 1891 CG LEU A 247 4933 6259 8657 10 908 -1290 C ATOM 1892 CD1 LEU A 247 -21.458 3.805 13.772 1.00 54.56 C ANISOU 1892 CD1 LEU A 247 5287 6887 8557 54 833 -1107 C ATOM 1893 CD2 LEU A 247 -21.088 1.515 14.720 1.00 52.99 C ANISOU 1893 CD2 LEU A 247 4989 6328 8816 -58 960 -1633 C ATOM 1894 N GLN A 248 -24.276 4.508 15.528 1.00 52.82 N ANISOU 1894 N GLN A 248 4827 6255 8987 169 706 -940 N ATOM 1895 CA GLN A 248 -25.630 4.044 15.204 1.00 54.62 C ANISOU 1895 CA GLN A 248 4817 6593 9345 171 542 -1113 C ATOM 1896 C GLN A 248 -25.795 3.462 13.791 1.00 57.61 C ANISOU 1896 C GLN A 248 5102 7331 9458 150 327 -1332 C ATOM 1897 O GLN A 248 -25.095 3.870 12.855 1.00 58.66 O ANISOU 1897 O GLN A 248 5356 7725 9207 186 268 -1230 O ATOM 1898 CB GLN A 248 -26.654 5.149 15.458 1.00 55.40 C ANISOU 1898 CB GLN A 248 4806 6659 9584 310 443 -917 C ATOM 1899 CG GLN A 248 -26.478 6.389 14.605 1.00 55.49 C ANISOU 1899 CG GLN A 248 4910 6819 9353 451 273 -612 C ATOM 1900 CD GLN A 248 -27.519 7.439 14.903 1.00 54.44 C ANISOU 1900 CD GLN A 248 4638 6581 9465 622 152 -445 C ATOM 1901 OE1 GLN A 248 -28.081 8.036 13.991 1.00 57.21 O ANISOU 1901 OE1 GLN A 248 4913 7120 9703 754 -115 -284 O ATOM 1902 NE2 GLN A 248 -27.789 7.665 16.182 1.00 51.10 N ANISOU 1902 NE2 GLN A 248 4167 5879 9369 637 339 -492 N ATOM 1903 N ALA A 249 -26.728 2.512 13.664 1.00 59.36 N ANISOU 1903 N ALA A 249 5088 7583 9884 77 225 -1645 N ATOM 1904 CA ALA A 249 -27.084 1.894 12.379 1.00 62.98 C ANISOU 1904 CA ALA A 249 5397 8404 10127 57 -20 -1960 C ATOM 1905 C ALA A 249 -28.512 2.233 11.962 1.00 66.32 C ANISOU 1905 C ALA A 249 5557 9022 10621 137 -301 -1991 C ATOM 1906 O ALA A 249 -29.445 2.161 12.771 1.00 66.24 O ANISOU 1906 O ALA A 249 5354 8789 11026 111 -260 -2011 O ATOM 1907 CB ALA A 249 -26.911 0.401 12.447 1.00 63.25 C ANISOU 1907 CB ALA A 249 5333 8299 10401 -103 48 -2395 C ATOM 1908 N THR A 250 -28.671 2.605 10.693 1.00 69.93 N ANISOU 1908 N THR A 250 5989 9931 10650 237 -586 -1989 N ATOM 1909 CA THR A 250 -29.979 2.956 10.131 1.00 73.74 C ANISOU 1909 CA THR A 250 6205 10670 11142 350 -934 -2016 C ATOM 1910 C THR A 250 -30.333 2.030 8.975 1.00 78.16 C ANISOU 1910 C THR A 250 6571 11656 11471 294 -1212 -2496 C ATOM 1911 O THR A 250 -29.474 1.691 8.154 1.00 79.28 O ANISOU 1911 O THR A 250 6860 12096 11167 263 -1213 -2642 O ATOM 1912 CB THR A 250 -30.023 4.418 9.626 1.00 75.15 C ANISOU 1912 CB THR A 250 6510 11043 11000 572 -1118 -1507 C ATOM 1913 OG1 THR A 250 -28.937 4.650 8.722 1.00 75.89 O ANISOU 1913 OG1 THR A 250 6868 11451 10516 576 -1106 -1345 O ATOM 1914 CG2 THR A 250 -29.926 5.397 10.786 1.00 71.85 C ANISOU 1914 CG2 THR A 250 6203 10178 10920 648 -899 -1126 C ATOM 1915 N LEU A 251 -31.598 1.623 8.920 1.00 81.06 N ANISOU 1915 N LEU A 251 6575 12071 12152 276 -1441 -2785 N ATOM 1916 CA LEU A 251 -32.104 0.793 7.831 1.00 86.13 C ANISOU 1916 CA LEU A 251 6968 13133 12623 229 -1769 -3308 C ATOM 1917 C LEU A 251 -33.487 1.269 7.428 1.00 90.33 C ANISOU 1917 C LEU A 251 7162 13929 13230 370 -2175 -3313 C ATOM 1918 O LEU A 251 -34.367 1.399 8.277 1.00 89.77 O ANISOU 1918 O LEU A 251 6853 13546 13710 359 -2121 -3267 O ATOM 1919 CB LEU A 251 -32.159 -0.682 8.248 1.00 86.03 C ANISOU 1919 CB LEU A 251 6771 12807 13110 -24 -1614 -3864 C ATOM 1920 CG LEU A 251 -32.978 -1.663 7.391 1.00 91.74 C ANISOU 1920 CG LEU A 251 7114 13815 13928 -120 -1952 -4527 C ATOM 1921 CD1 LEU A 251 -32.232 -2.091 6.126 1.00 95.04 C ANISOU 1921 CD1 LEU A 251 7639 14738 13735 -97 -2114 -4905 C ATOM 1922 CD2 LEU A 251 -33.395 -2.884 8.202 1.00 91.17 C ANISOU 1922 CD2 LEU A 251 6789 13217 14636 -386 -1765 -4909 C ATOM 1923 N ASP A 252 -33.677 1.524 6.135 1.00 95.24 N ANISOU 1923 N ASP A 252 7746 15161 13281 509 -2582 -3373 N ATOM 1924 CA ASP A 252 -34.976 1.954 5.622 1.00100.11 C ANISOU 1924 CA ASP A 252 8017 16097 13923 677 -3053 -3393 C ATOM 1925 C ASP A 252 -35.973 0.808 5.574 1.00103.27 C ANISOU 1925 C ASP A 252 7939 16508 14789 507 -3231 -4086 C ATOM 1926 O ASP A 252 -35.652 -0.285 5.104 1.00104.77 O ANISOU 1926 O ASP A 252 8077 16826 14903 329 -3238 -4642 O ATOM 1927 CB ASP A 252 -34.843 2.614 4.248 1.00105.09 C ANISOU 1927 CB ASP A 252 8776 17425 13729 892 -3462 -3174 C ATOM 1928 CG ASP A 252 -34.912 4.129 4.322 1.00105.18 C ANISOU 1928 CG ASP A 252 8967 17395 13603 1161 -3556 -2395 C ATOM 1929 OD1 ASP A 252 -35.813 4.712 3.680 1.00110.54 O ANISOU 1929 OD1 ASP A 252 9441 18426 14132 1389 -4034 -2242 O ATOM 1930 OD2 ASP A 252 -34.082 4.742 5.032 1.00100.71 O ANISOU 1930 OD2 ASP A 252 8724 16419 13122 1154 -3177 -1949 O ATOM 1931 N VAL A 253 -37.175 1.074 6.086 1.00104.57 N ANISOU 1931 N VAL A 253 7728 16512 15490 558 -3360 -4073 N ATOM 1932 CA VAL A 253 -38.252 0.084 6.156 1.00107.96 C ANISOU 1932 CA VAL A 253 7631 16898 16489 373 -3508 -4689 C ATOM 1933 C VAL A 253 -39.587 0.689 5.708 1.00113.21 C ANISOU 1933 C VAL A 253 7857 17907 17250 590 -4011 -4702 C ATOM 1934 O VAL A 253 -39.941 1.802 6.110 1.00112.25 O ANISOU 1934 O VAL A 253 7743 17687 17219 825 -4033 -4200 O ATOM 1935 CB VAL A 253 -38.425 -0.490 7.597 1.00104.06 C ANISOU 1935 CB VAL A 253 7019 15718 16801 113 -3005 -4732 C ATOM 1936 CG1 VAL A 253 -39.233 -1.781 7.569 1.00108.01 C ANISOU 1936 CG1 VAL A 253 7036 16124 17880 -174 -3083 -5408 C ATOM 1937 CG2 VAL A 253 -37.078 -0.735 8.276 1.00 98.09 C ANISOU 1937 CG2 VAL A 253 6744 14564 15963 -11 -2506 -4503 C ATOM 1938 N GLU A 254 -40.315 -0.047 4.868 1.00119.15 N ANISOU 1938 N GLU A 254 8206 19056 18011 524 -4436 -5310 N ATOM 1939 CA GLU A 254 -41.701 0.289 4.548 1.00124.85 C ANISOU 1939 CA GLU A 254 8389 20062 18988 684 -4923 -5456 C ATOM 1940 C GLU A 254 -42.541 0.009 5.790 1.00123.30 C ANISOU 1940 C GLU A 254 7787 19308 19753 496 -4593 -5564 C ATOM 1941 O GLU A 254 -42.322 -0.998 6.473 1.00120.98 O ANISOU 1941 O GLU A 254 7459 18579 19927 147 -4179 -5854 O ATOM 1942 CB GLU A 254 -42.211 -0.527 3.354 1.00132.01 C ANISOU 1942 CB GLU A 254 8941 21549 19666 627 -5463 -6170 C ATOM 1943 N ALA A 255 -43.482 0.906 6.085 1.00124.97 N ANISOU 1943 N ALA A 255 7689 19534 20259 732 -4764 -5307 N ATOM 1944 CA ALA A 255 -44.253 0.852 7.328 1.00123.53 C ANISOU 1944 CA ALA A 255 7135 18878 20921 593 -4388 -5327 C ATOM 1945 C ALA A 255 -45.066 -0.437 7.458 1.00127.14 C ANISOU 1945 C ALA A 255 7029 19241 22039 216 -4366 -6017 C ATOM 1946 O ALA A 255 -45.778 -0.829 6.534 1.00133.29 O ANISOU 1946 O ALA A 255 7387 20437 22820 225 -4892 -6510 O ATOM 1947 CB ALA A 255 -45.145 2.076 7.451 1.00125.99 C ANISOU 1947 CB ALA A 255 7161 19295 21414 966 -4646 -5009 C ATOM 1948 N GLY A 256 -44.936 -1.092 8.609 1.00123.73 N ANISOU 1948 N GLY A 256 6592 18260 22161 -122 -3760 -6034 N ATOM 1949 CA GLY A 256 -45.593 -2.373 8.865 1.00127.12 C ANISOU 1949 CA GLY A 256 6530 18469 23299 -546 -3635 -6604 C ATOM 1950 C GLY A 256 -44.635 -3.552 8.918 1.00124.90 C ANISOU 1950 C GLY A 256 6574 17863 23018 -885 -3348 -6816 C ATOM 1951 O GLY A 256 -44.961 -4.594 9.489 1.00126.34 O ANISOU 1951 O GLY A 256 6474 17644 23884 -1280 -3054 -7103 O ATOM 1952 N GLU A 257 -43.449 -3.382 8.334 1.00121.84 N ANISOU 1952 N GLU A 257 6764 17628 21902 -730 -3421 -6655 N ATOM 1953 CA GLU A 257 -42.462 -4.463 8.202 1.00120.36 C ANISOU 1953 CA GLU A 257 6878 17192 21663 -981 -3227 -6917 C ATOM 1954 C GLU A 257 -41.494 -4.569 9.381 1.00113.67 C ANISOU 1954 C GLU A 257 6496 15772 20922 -1109 -2590 -6438 C ATOM 1955 O GLU A 257 -40.525 -5.329 9.322 1.00111.89 O ANISOU 1955 O GLU A 257 6581 15316 20617 -1251 -2422 -6560 O ATOM 1956 CB GLU A 257 -41.649 -4.293 6.912 1.00121.32 C ANISOU 1956 CB GLU A 257 7337 17838 20921 -758 -3618 -7059 C ATOM 1957 CG GLU A 257 -42.420 -4.498 5.609 1.00129.14 C ANISOU 1957 CG GLU A 257 7908 19453 21707 -676 -4284 -7666 C ATOM 1958 CD GLU A 257 -41.628 -4.049 4.385 1.00130.49 C ANISOU 1958 CD GLU A 257 8461 20266 20853 -397 -4639 -7641 C ATOM 1959 OE1 GLU A 257 -40.629 -3.314 4.546 1.00125.42 O ANISOU 1959 OE1 GLU A 257 8368 19606 19680 -223 -4398 -7049 O ATOM 1960 OE2 GLU A 257 -42.008 -4.426 3.257 1.00136.94 O ANISOU 1960 OE2 GLU A 257 9014 21637 21381 -361 -5157 -8222 O ATOM 1961 N GLU A 258 -41.762 -3.817 10.447 1.00110.49 N ANISOU 1961 N GLU A 258 6117 15161 20704 -1044 -2256 -5931 N ATOM 1962 CA GLU A 258 -40.878 -3.762 11.617 1.00104.46 C ANISOU 1962 CA GLU A 258 5795 13938 19957 -1122 -1686 -5442 C ATOM 1963 C GLU A 258 -40.910 -5.048 12.456 1.00105.03 C ANISOU 1963 C GLU A 258 5742 13463 20702 -1549 -1278 -5580 C ATOM 1964 O GLU A 258 -40.088 -5.227 13.360 1.00100.76 O ANISOU 1964 O GLU A 258 5579 12543 20161 -1638 -847 -5213 O ATOM 1965 CB GLU A 258 -41.215 -2.554 12.503 1.00101.95 C ANISOU 1965 CB GLU A 258 5502 13610 19625 -916 -1467 -4936 C ATOM 1966 CG GLU A 258 -41.546 -1.257 11.767 1.00103.06 C ANISOU 1966 CG GLU A 258 5613 14208 19337 -503 -1898 -4786 C ATOM 1967 CD GLU A 258 -43.022 -1.137 11.406 1.00109.65 C ANISOU 1967 CD GLU A 258 5781 15309 20572 -454 -2247 -5108 C ATOM 1968 OE1 GLU A 258 -43.830 -1.989 11.840 1.00112.58 O ANISOU 1968 OE1 GLU A 258 5686 15498 21590 -764 -2090 -5435 O ATOM 1969 OE2 GLU A 258 -43.379 -0.184 10.683 1.00112.14 O ANISOU 1969 OE2 GLU A 258 6019 16010 20580 -105 -2689 -5013 O ATOM 1970 N ALA A 259 -41.860 -5.933 12.147 1.00110.73 N ANISOU 1970 N ALA A 259 5921 14140 22010 -1812 -1438 -6094 N ATOM 1971 CA ALA A 259 -42.037 -7.208 12.851 1.00112.77 C ANISOU 1971 CA ALA A 259 5985 13841 23021 -2255 -1087 -6232 C ATOM 1972 C ALA A 259 -40.890 -8.196 12.600 1.00111.68 C ANISOU 1972 C ALA A 259 6213 13366 22853 -2382 -1036 -6390 C ATOM 1973 O ALA A 259 -40.378 -8.304 11.478 1.00112.50 O ANISOU 1973 O ALA A 259 6442 13756 22548 -2232 -1416 -6775 O ATOM 1974 CB ALA A 259 -43.373 -7.838 12.473 1.00119.81 C ANISOU 1974 CB ALA A 259 6150 14780 24591 -2506 -1317 -6790 C ATOM 1975 N GLY A 260 -40.493 -8.907 13.657 1.00110.27 N ANISOU 1975 N GLY A 260 6194 12602 23100 -2646 -562 -6086 N ATOM 1976 CA GLY A 260 -39.454 -9.938 13.580 1.00109.54 C ANISOU 1976 CA GLY A 260 6400 12073 23149 -2776 -482 -6207 C ATOM 1977 C GLY A 260 -38.051 -9.398 13.383 1.00103.79 C ANISOU 1977 C GLY A 260 6281 11489 21666 -2461 -486 -5952 C ATOM 1978 O GLY A 260 -37.124 -10.152 13.081 1.00103.78 O ANISOU 1978 O GLY A 260 6504 11235 21694 -2489 -504 -6154 O ATOM 1979 N LEU A 261 -37.891 -8.091 13.549 1.00 99.30 N ANISOU 1979 N LEU A 261 5950 11304 20474 -2160 -467 -5531 N ATOM 1980 CA LEU A 261 -36.588 -7.459 13.386 1.00 94.20 C ANISOU 1980 CA LEU A 261 5850 10811 19131 -1878 -454 -5256 C ATOM 1981 C LEU A 261 -35.846 -7.262 14.712 1.00 89.53 C ANISOU 1981 C LEU A 261 5642 9859 18515 -1887 6 -4632 C ATOM 1982 O LEU A 261 -36.456 -7.019 15.759 1.00 89.38 O ANISOU 1982 O LEU A 261 5514 9702 18744 -1989 300 -4284 O ATOM 1983 CB LEU A 261 -36.720 -6.131 12.631 1.00 92.92 C ANISOU 1983 CB LEU A 261 5747 11269 18288 -1535 -760 -5180 C ATOM 1984 CG LEU A 261 -36.545 -6.187 11.112 1.00 95.54 C ANISOU 1984 CG LEU A 261 6038 12080 18183 -1393 -1231 -5675 C ATOM 1985 CD1 LEU A 261 -37.312 -5.072 10.424 1.00 96.88 C ANISOU 1985 CD1 LEU A 261 6036 12827 17946 -1138 -1598 -5629 C ATOM 1986 CD2 LEU A 261 -35.071 -6.129 10.751 1.00 92.00 C ANISOU 1986 CD2 LEU A 261 6077 11687 17191 -1249 -1172 -5589 C ATOM 1987 N ALA A 262 -34.524 -7.379 14.648 1.00 86.20 N ANISOU 1987 N ALA A 262 5645 9330 17776 -1775 62 -4527 N ATOM 1988 CA ALA A 262 -33.663 -7.176 15.802 1.00 81.81 C ANISOU 1988 CA ALA A 262 5475 8493 17116 -1744 425 -3977 C ATOM 1989 C ALA A 262 -32.378 -6.471 15.374 1.00 77.66 C ANISOU 1989 C ALA A 262 5371 8204 15933 -1462 349 -3858 C ATOM 1990 O ALA A 262 -32.114 -6.326 14.178 1.00 78.62 O ANISOU 1990 O ALA A 262 5492 8668 15711 -1330 55 -4202 O ATOM 1991 CB ALA A 262 -33.358 -8.508 16.477 1.00 83.67 C ANISOU 1991 CB ALA A 262 5724 8123 17944 -2008 649 -3941 C ATOM 1992 N CYS A 263 -31.593 -6.018 16.349 1.00 73.56 N ANISOU 1992 N CYS A 263 5190 7538 15221 -1380 617 -3376 N ATOM 1993 CA CYS A 263 -30.283 -5.418 16.082 1.00 69.67 C ANISOU 1993 CA CYS A 263 5076 7199 14196 -1156 593 -3243 C ATOM 1994 C CYS A 263 -29.178 -6.178 16.825 1.00 68.10 C ANISOU 1994 C CYS A 263 5130 6577 14169 -1208 801 -3073 C ATOM 1995 O CYS A 263 -29.131 -6.163 18.057 1.00 66.88 O ANISOU 1995 O CYS A 263 5090 6178 14144 -1267 1058 -2664 O ATOM 1996 CB CYS A 263 -30.278 -3.932 16.468 1.00 66.39 C ANISOU 1996 CB CYS A 263 4822 7056 13348 -955 653 -2852 C ATOM 1997 SG CYS A 263 -28.650 -3.182 16.356 1.00 61.89 S ANISOU 1997 SG CYS A 263 4690 6594 12232 -740 688 -2626 S ATOM 1998 N ARG A 264 -28.300 -6.841 16.074 1.00 68.59 N ANISOU 1998 N ARG A 264 5263 6581 14218 -1171 680 -3398 N ATOM 1999 CA ARG A 264 -27.262 -7.681 16.670 1.00 68.23 C ANISOU 1999 CA ARG A 264 5401 6097 14425 -1194 819 -3296 C ATOM 2000 C ARG A 264 -25.942 -6.951 16.711 1.00 64.42 C ANISOU 2000 C ARG A 264 5239 5789 13450 -975 863 -3099 C ATOM 2001 O ARG A 264 -25.497 -6.396 15.702 1.00 64.01 O ANISOU 2001 O ARG A 264 5227 6132 12963 -837 726 -3318 O ATOM 2002 CB ARG A 264 -27.103 -8.987 15.891 1.00 72.59 C ANISOU 2002 CB ARG A 264 5776 6395 15411 -1288 672 -3846 C ATOM 2003 CG ARG A 264 -26.283 -10.073 16.596 1.00 73.89 C ANISOU 2003 CG ARG A 264 6051 5960 16064 -1335 792 -3735 C ATOM 2004 CD ARG A 264 -26.457 -11.409 15.877 1.00 79.70 C ANISOU 2004 CD ARG A 264 6524 6352 17407 -1466 640 -4330 C ATOM 2005 NE ARG A 264 -25.653 -12.491 16.446 1.00 81.79 N ANISOU 2005 NE ARG A 264 6873 5982 18223 -1480 710 -4250 N ATOM 2006 CZ ARG A 264 -26.133 -13.473 17.205 1.00 85.11 C ANISOU 2006 CZ ARG A 264 7190 5779 19369 -1701 803 -4045 C ATOM 2007 NH1 ARG A 264 -27.427 -13.523 17.504 1.00 87.23 N ANISOU 2007 NH1 ARG A 264 7243 5999 19901 -1955 874 -3928 N ATOM 2008 NH2 ARG A 264 -25.313 -14.407 17.669 1.00 86.42 N ANISOU 2008 NH2 ARG A 264 7451 5361 20024 -1669 828 -3934 N ATOM 2009 N VAL A 265 -25.311 -6.952 17.880 1.00 62.25 N ANISOU 2009 N VAL A 265 5177 5243 13231 -953 1053 -2676 N ATOM 2010 CA VAL A 265 -24.043 -6.252 18.048 1.00 58.74 C ANISOU 2010 CA VAL A 265 5003 4937 12380 -762 1095 -2488 C ATOM 2011 C VAL A 265 -22.985 -7.182 18.608 1.00 59.38 C ANISOU 2011 C VAL A 265 5200 4608 12753 -736 1146 -2423 C ATOM 2012 O VAL A 265 -23.173 -7.766 19.676 1.00 60.52 O ANISOU 2012 O VAL A 265 5382 4386 13228 -830 1258 -2109 O ATOM 2013 CB VAL A 265 -24.179 -5.017 18.971 1.00 55.61 C ANISOU 2013 CB VAL A 265 4763 4712 11655 -696 1230 -2034 C ATOM 2014 CG1 VAL A 265 -22.839 -4.323 19.132 1.00 52.46 C ANISOU 2014 CG1 VAL A 265 4605 4424 10905 -526 1256 -1887 C ATOM 2015 CG2 VAL A 265 -25.212 -4.049 18.429 1.00 54.72 C ANISOU 2015 CG2 VAL A 265 4517 4958 11315 -680 1154 -2083 C ATOM 2016 N LYS A 266 -21.885 -7.318 17.871 1.00 59.24 N ANISOU 2016 N LYS A 266 5223 4674 12610 -603 1064 -2707 N ATOM 2017 CA LYS A 266 -20.714 -8.060 18.332 1.00 59.95 C ANISOU 2017 CA LYS A 266 5406 4415 12956 -514 1080 -2669 C ATOM 2018 C LYS A 266 -19.643 -7.064 18.774 1.00 56.50 C ANISOU 2018 C LYS A 266 5180 4202 12087 -351 1142 -2392 C ATOM 2019 O LYS A 266 -19.437 -6.035 18.123 1.00 54.71 O ANISOU 2019 O LYS A 266 4984 4404 11399 -288 1141 -2463 O ATOM 2020 CB LYS A 266 -20.148 -8.940 17.218 1.00 62.92 C ANISOU 2020 CB LYS A 266 5626 4730 13552 -462 962 -3261 C ATOM 2021 CG LYS A 266 -21.132 -9.905 16.561 1.00 67.42 C ANISOU 2021 CG LYS A 266 5943 5115 14557 -620 858 -3694 C ATOM 2022 CD LYS A 266 -20.376 -11.018 15.818 1.00 71.70 C ANISOU 2022 CD LYS A 266 6338 5420 15483 -545 758 -4274 C ATOM 2023 CE LYS A 266 -21.262 -11.760 14.829 1.00 75.96 C ANISOU 2023 CE LYS A 266 6596 5949 16317 -680 617 -4890 C ATOM 2024 NZ LYS A 266 -22.314 -12.574 15.496 1.00 78.46 N ANISOU 2024 NZ LYS A 266 6790 5722 17300 -907 616 -4736 N ATOM 2025 N HIS A 267 -18.967 -7.368 19.881 1.00 56.14 N ANISOU 2025 N HIS A 267 5267 3862 12202 -290 1182 -2062 N ATOM 2026 CA HIS A 267 -17.866 -6.538 20.382 1.00 53.18 C ANISOU 2026 CA HIS A 267 5054 3660 11491 -140 1208 -1848 C ATOM 2027 C HIS A 267 -16.975 -7.355 21.313 1.00 54.72 C ANISOU 2027 C HIS A 267 5322 3471 11999 -41 1161 -1641 C ATOM 2028 O HIS A 267 -17.448 -8.262 22.003 1.00 57.51 O ANISOU 2028 O HIS A 267 5684 3439 12729 -117 1159 -1418 O ATOM 2029 CB HIS A 267 -18.401 -5.293 21.100 1.00 50.31 C ANISOU 2029 CB HIS A 267 4820 3555 10741 -169 1303 -1492 C ATOM 2030 CG HIS A 267 -17.329 -4.351 21.554 1.00 47.61 C ANISOU 2030 CG HIS A 267 4612 3394 10082 -39 1314 -1342 C ATOM 2031 ND1 HIS A 267 -16.903 -4.286 22.862 1.00 46.93 N ANISOU 2031 ND1 HIS A 267 4664 3199 9968 17 1325 -1007 N ATOM 2032 CD2 HIS A 267 -16.587 -3.449 20.871 1.00 45.57 C ANISOU 2032 CD2 HIS A 267 4355 3427 9534 30 1312 -1487 C ATOM 2033 CE1 HIS A 267 -15.945 -3.383 22.965 1.00 45.21 C ANISOU 2033 CE1 HIS A 267 4505 3183 9489 119 1308 -1006 C ATOM 2034 NE2 HIS A 267 -15.736 -2.859 21.771 1.00 43.88 N ANISOU 2034 NE2 HIS A 267 4253 3234 9187 116 1317 -1276 N ATOM 2035 N SER A 268 -15.690 -7.024 21.335 1.00 53.57 N ANISOU 2035 N SER A 268 5214 3430 11712 123 1118 -1687 N ATOM 2036 CA SER A 268 -14.705 -7.775 22.116 1.00 55.47 C ANISOU 2036 CA SER A 268 5489 3338 12249 268 1016 -1527 C ATOM 2037 C SER A 268 -15.034 -7.906 23.609 1.00 56.26 C ANISOU 2037 C SER A 268 5765 3253 12357 244 1016 -958 C ATOM 2038 O SER A 268 -14.591 -8.847 24.260 1.00 59.15 O ANISOU 2038 O SER A 268 6158 3242 13074 328 908 -746 O ATOM 2039 CB SER A 268 -13.299 -7.179 21.924 1.00 54.20 C ANISOU 2039 CB SER A 268 5299 3409 11885 440 975 -1678 C ATOM 2040 OG SER A 268 -13.313 -5.762 21.985 1.00 50.24 O ANISOU 2040 OG SER A 268 4885 3326 10878 400 1064 -1570 O ATOM 2041 N SER A 269 -15.819 -6.971 24.137 1.00 54.30 N ANISOU 2041 N SER A 269 5628 3283 11722 139 1137 -711 N ATOM 2042 CA SER A 269 -16.044 -6.863 25.581 1.00 55.35 C ANISOU 2042 CA SER A 269 5932 3403 11694 127 1172 -205 C ATOM 2043 C SER A 269 -16.958 -7.946 26.129 1.00 59.08 C ANISOU 2043 C SER A 269 6413 3516 12518 -19 1233 104 C ATOM 2044 O SER A 269 -16.826 -8.367 27.282 1.00 61.39 O ANISOU 2044 O SER A 269 6841 3673 12811 2 1217 564 O ATOM 2045 CB SER A 269 -16.626 -5.489 25.918 1.00 52.38 C ANISOU 2045 CB SER A 269 5630 3450 10821 70 1305 -132 C ATOM 2046 OG SER A 269 -17.819 -5.272 25.194 1.00 51.48 O ANISOU 2046 OG SER A 269 5409 3419 10733 -83 1420 -299 O ATOM 2047 N LEU A 270 -17.881 -8.386 25.283 1.00 60.22 N ANISOU 2047 N LEU A 270 6402 3524 12954 -180 1297 -142 N ATOM 2048 CA LEU A 270 -18.948 -9.290 25.675 1.00 64.11 C ANISOU 2048 CA LEU A 270 6846 3690 13821 -388 1398 105 C ATOM 2049 C LEU A 270 -18.463 -10.734 25.754 1.00 68.90 C ANISOU 2049 C LEU A 270 7421 3701 15055 -358 1268 195 C ATOM 2050 O LEU A 270 -18.933 -11.509 26.589 1.00 72.65 O ANISOU 2050 O LEU A 270 7948 3844 15811 -484 1333 655 O ATOM 2051 CB LEU A 270 -20.109 -9.164 24.682 1.00 63.71 C ANISOU 2051 CB LEU A 270 6592 3737 13879 -569 1478 -263 C ATOM 2052 CG LEU A 270 -20.508 -7.732 24.270 1.00 59.74 C ANISOU 2052 CG LEU A 270 6078 3776 12843 -549 1542 -444 C ATOM 2053 CD1 LEU A 270 -21.081 -7.697 22.860 1.00 59.70 C ANISOU 2053 CD1 LEU A 270 5862 3879 12941 -612 1478 -949 C ATOM 2054 CD2 LEU A 270 -21.470 -7.076 25.268 1.00 59.21 C ANISOU 2054 CD2 LEU A 270 6061 3932 12505 -659 1742 -89 C ATOM 2055 N GLY A 271 -17.514 -11.083 24.888 1.00 69.30 N ANISOU 2055 N GLY A 271 7376 3613 15342 -188 1095 -234 N ATOM 2056 CA GLY A 271 -16.984 -12.438 24.822 1.00 74.14 C ANISOU 2056 CA GLY A 271 7915 3616 16639 -113 941 -261 C ATOM 2057 C GLY A 271 -18.005 -13.375 24.215 1.00 77.82 C ANISOU 2057 C GLY A 271 8188 3679 17700 -341 984 -491 C ATOM 2058 O GLY A 271 -18.431 -14.336 24.855 1.00 82.45 O ANISOU 2058 O GLY A 271 8785 3751 18790 -470 1002 -102 O ATOM 2059 N GLY A 272 -18.412 -13.074 22.984 1.00 76.43 N ANISOU 2059 N GLY A 272 7830 3753 17458 -403 996 -1107 N ATOM 2060 CA GLY A 272 -19.347 -13.909 22.229 1.00 80.24 C ANISOU 2060 CA GLY A 272 8075 3919 18492 -611 992 -1487 C ATOM 2061 C GLY A 272 -20.797 -13.839 22.677 1.00 81.29 C ANISOU 2061 C GLY A 272 8166 4062 18660 -916 1167 -1187 C ATOM 2062 O GLY A 272 -21.657 -14.536 22.131 1.00 84.64 O ANISOU 2062 O GLY A 272 8362 4211 19587 -1124 1162 -1485 O ATOM 2063 N GLN A 273 -21.070 -13.012 23.678 1.00 78.95 N ANISOU 2063 N GLN A 273 8057 4088 17853 -947 1325 -640 N ATOM 2064 CA GLN A 273 -22.429 -12.823 24.149 1.00 79.96 C ANISOU 2064 CA GLN A 273 8115 4313 17952 -1221 1535 -370 C ATOM 2065 C GLN A 273 -23.018 -11.640 23.390 1.00 75.92 C ANISOU 2065 C GLN A 273 7506 4410 16929 -1219 1562 -747 C ATOM 2066 O GLN A 273 -23.155 -10.536 23.944 1.00 72.70 O ANISOU 2066 O GLN A 273 7227 4447 15947 -1168 1679 -496 O ATOM 2067 CB GLN A 273 -22.454 -12.593 25.667 1.00 80.46 C ANISOU 2067 CB GLN A 273 8410 4436 17724 -1250 1712 391 C ATOM 2068 N ASP A 274 -23.350 -11.875 22.115 1.00 76.52 N ANISOU 2068 N ASP A 274 7349 4504 17221 -1260 1432 -1364 N ATOM 2069 CA ASP A 274 -23.876 -10.824 21.232 1.00 73.36 C ANISOU 2069 CA ASP A 274 6846 4673 16356 -1232 1395 -1726 C ATOM 2070 C ASP A 274 -25.086 -10.152 21.844 1.00 72.68 C ANISOU 2070 C ASP A 274 6699 4833 16083 -1390 1578 -1428 C ATOM 2071 O ASP A 274 -25.900 -10.796 22.501 1.00 76.20 O ANISOU 2071 O ASP A 274 7035 4987 16930 -1621 1726 -1170 O ATOM 2072 CB ASP A 274 -24.248 -11.376 19.851 1.00 75.70 C ANISOU 2072 CB ASP A 274 6867 4946 16949 -1293 1215 -2412 C ATOM 2073 CG ASP A 274 -23.036 -11.699 18.996 1.00 76.15 C ANISOU 2073 CG ASP A 274 6953 4984 16995 -1087 1049 -2855 C ATOM 2074 OD1 ASP A 274 -21.895 -11.471 19.443 1.00 75.16 O ANISOU 2074 OD1 ASP A 274 7041 4853 16665 -896 1067 -2627 O ATOM 2075 OD2 ASP A 274 -23.219 -12.187 17.864 1.00 78.71 O ANISOU 2075 OD2 ASP A 274 7059 5332 17514 -1114 901 -3474 O ATOM 2076 N ILE A 275 -25.196 -8.848 21.646 1.00 68.92 N ANISOU 2076 N ILE A 275 6277 4880 15030 -1265 1582 -1454 N ATOM 2077 CA ILE A 275 -26.387 -8.148 22.083 1.00 68.65 C ANISOU 2077 CA ILE A 275 6126 5104 14855 -1377 1734 -1284 C ATOM 2078 C ILE A 275 -27.487 -8.417 21.064 1.00 71.17 C ANISOU 2078 C ILE A 275 6101 5481 15461 -1520 1615 -1729 C ATOM 2079 O ILE A 275 -27.270 -8.348 19.850 1.00 70.54 O ANISOU 2079 O ILE A 275 5944 5571 15286 -1425 1387 -2186 O ATOM 2080 CB ILE A 275 -26.114 -6.645 22.365 1.00 64.39 C ANISOU 2080 CB ILE A 275 5759 5024 13681 -1177 1774 -1130 C ATOM 2081 CG1 ILE A 275 -25.601 -6.486 23.806 1.00 63.43 C ANISOU 2081 CG1 ILE A 275 5882 4848 13370 -1141 1966 -630 C ATOM 2082 CG2 ILE A 275 -27.367 -5.801 22.149 1.00 63.97 C ANISOU 2082 CG2 ILE A 275 5491 5299 13517 -1217 1810 -1224 C ATOM 2083 CD1 ILE A 275 -24.726 -5.276 24.056 1.00 58.69 C ANISOU 2083 CD1 ILE A 275 5509 4556 12233 -910 1938 -550 C ATOM 2084 N ILE A 276 -28.650 -8.785 21.583 1.00 74.59 N ANISOU 2084 N ILE A 276 6308 5786 16246 -1761 1777 -1595 N ATOM 2085 CA ILE A 276 -29.781 -9.166 20.757 1.00 78.20 C ANISOU 2085 CA ILE A 276 6379 6254 17078 -1936 1663 -2014 C ATOM 2086 C ILE A 276 -31.017 -8.403 21.205 1.00 78.60 C ANISOU 2086 C ILE A 276 6216 6608 17042 -2019 1822 -1873 C ATOM 2087 O ILE A 276 -31.714 -8.810 22.134 1.00 81.38 O ANISOU 2087 O ILE A 276 6441 6780 17701 -2249 2094 -1572 O ATOM 2088 CB ILE A 276 -30.012 -10.713 20.757 1.00 83.67 C ANISOU 2088 CB ILE A 276 6887 6354 18550 -2209 1674 -2126 C ATOM 2089 CG1 ILE A 276 -29.887 -11.311 22.173 1.00 86.04 C ANISOU 2089 CG1 ILE A 276 7337 6248 19106 -2369 1978 -1489 C ATOM 2090 CG2 ILE A 276 -29.043 -11.409 19.795 1.00 84.04 C ANISOU 2090 CG2 ILE A 276 6993 6187 18750 -2094 1414 -2574 C ATOM 2091 CD1 ILE A 276 -31.228 -11.699 22.826 1.00 90.45 C ANISOU 2091 CD1 ILE A 276 7591 6673 20102 -2717 2244 -1266 C ATOM 2092 N LEU A 277 -31.265 -7.270 20.558 1.00 76.39 N ANISOU 2092 N LEU A 277 5889 6796 16340 -1821 1663 -2069 N ATOM 2093 CA LEU A 277 -32.454 -6.477 20.855 1.00 77.28 C ANISOU 2093 CA LEU A 277 5747 7204 16410 -1845 1765 -2017 C ATOM 2094 C LEU A 277 -33.530 -6.615 19.786 1.00 80.48 C ANISOU 2094 C LEU A 277 5726 7765 17088 -1921 1514 -2492 C ATOM 2095 O LEU A 277 -33.346 -6.194 18.645 1.00 79.54 O ANISOU 2095 O LEU A 277 5604 7919 16699 -1739 1187 -2814 O ATOM 2096 CB LEU A 277 -32.106 -5.001 21.088 1.00 73.10 C ANISOU 2096 CB LEU A 277 5435 7047 15291 -1556 1774 -1833 C ATOM 2097 CG LEU A 277 -32.151 -4.506 22.537 1.00 72.21 C ANISOU 2097 CG LEU A 277 5451 6968 15019 -1558 2128 -1403 C ATOM 2098 CD1 LEU A 277 -31.623 -3.097 22.613 1.00 67.72 C ANISOU 2098 CD1 LEU A 277 5105 6693 13933 -1260 2075 -1324 C ATOM 2099 CD2 LEU A 277 -33.566 -4.580 23.126 1.00 76.43 C ANISOU 2099 CD2 LEU A 277 5598 7569 15872 -1757 2369 -1373 C ATOM 2100 N TYR A 278 -34.653 -7.204 20.177 1.00 84.79 N ANISOU 2100 N TYR A 278 5899 8164 18153 -2200 1671 -2518 N ATOM 2101 CA TYR A 278 -35.789 -7.376 19.288 1.00 88.82 C ANISOU 2101 CA TYR A 278 5930 8821 18995 -2301 1435 -2984 C ATOM 2102 C TYR A 278 -36.705 -6.157 19.342 1.00 88.21 C ANISOU 2102 C TYR A 278 5627 9188 18702 -2139 1417 -2967 C ATOM 2103 O TYR A 278 -36.802 -5.485 20.373 1.00 86.64 O ANISOU 2103 O TYR A 278 5519 9070 18329 -2085 1722 -2598 O ATOM 2104 CB TYR A 278 -36.565 -8.636 19.665 1.00 94.47 C ANISOU 2104 CB TYR A 278 6294 9123 20476 -2711 1616 -3046 C ATOM 2105 CG TYR A 278 -35.749 -9.905 19.598 1.00 97.10 C ANISOU 2105 CG TYR A 278 6802 8925 21168 -2869 1608 -3082 C ATOM 2106 CD1 TYR A 278 -35.013 -10.342 20.704 1.00 97.39 C ANISOU 2106 CD1 TYR A 278 7170 8593 21242 -2945 1925 -2544 C ATOM 2107 CD2 TYR A 278 -35.718 -10.677 18.431 1.00100.98 C ANISOU 2107 CD2 TYR A 278 7110 9285 21974 -2925 1263 -3677 C ATOM 2108 CE1 TYR A 278 -34.260 -11.513 20.646 1.00100.19 C ANISOU 2108 CE1 TYR A 278 7666 8404 21998 -3056 1887 -2560 C ATOM 2109 CE2 TYR A 278 -34.975 -11.853 18.364 1.00103.48 C ANISOU 2109 CE2 TYR A 278 7552 9061 22704 -3047 1248 -3769 C ATOM 2110 CZ TYR A 278 -34.248 -12.262 19.474 1.00103.28 C ANISOU 2110 CZ TYR A 278 7853 8620 22770 -3105 1557 -3190 C ATOM 2111 OH TYR A 278 -33.508 -13.419 19.416 1.00106.45 O ANISOU 2111 OH TYR A 278 8364 8440 23643 -3191 1515 -3260 O ATOM 2112 N TRP A 279 -37.373 -5.884 18.225 1.00 89.98 N ANISOU 2112 N TRP A 279 5542 9707 18940 -2047 1038 -3393 N ATOM 2113 CA TRP A 279 -38.272 -4.742 18.108 1.00 90.41 C ANISOU 2113 CA TRP A 279 5336 10162 18853 -1849 930 -3419 C ATOM 2114 C TRP A 279 -39.624 -5.005 18.773 1.00 94.88 C ANISOU 2114 C TRP A 279 5377 10692 19981 -2096 1173 -3460 C ATOM 2115 O TRP A 279 -40.264 -6.031 18.537 1.00 99.34 O ANISOU 2115 O TRP A 279 5572 11073 21101 -2402 1147 -3745 O ATOM 2116 CB TRP A 279 -38.460 -4.383 16.633 1.00 91.57 C ANISOU 2116 CB TRP A 279 5349 10669 18773 -1640 390 -3818 C ATOM 2117 CG TRP A 279 -39.277 -3.150 16.388 1.00 92.43 C ANISOU 2117 CG TRP A 279 5225 11171 18724 -1370 192 -3806 C ATOM 2118 CD1 TRP A 279 -40.493 -3.087 15.778 1.00 97.25 C ANISOU 2118 CD1 TRP A 279 5303 12029 19619 -1364 -101 -4148 C ATOM 2119 CD2 TRP A 279 -38.934 -1.802 16.739 1.00 89.30 C ANISOU 2119 CD2 TRP A 279 5093 10930 17906 -1050 243 -3449 C ATOM 2120 NE1 TRP A 279 -40.931 -1.786 15.724 1.00 97.06 N ANISOU 2120 NE1 TRP A 279 5200 12297 19380 -1036 -246 -3998 N ATOM 2121 CE2 TRP A 279 -39.993 -0.977 16.307 1.00 92.46 C ANISOU 2121 CE2 TRP A 279 5106 11639 18386 -846 -31 -3575 C ATOM 2122 CE3 TRP A 279 -37.835 -1.211 17.381 1.00 84.71 C ANISOU 2122 CE3 TRP A 279 5014 10237 16935 -915 475 -3059 C ATOM 2123 CZ2 TRP A 279 -39.989 0.412 16.495 1.00 91.39 C ANISOU 2123 CZ2 TRP A 279 5081 11649 17994 -506 -72 -3310 C ATOM 2124 CZ3 TRP A 279 -37.831 0.171 17.567 1.00 83.11 C ANISOU 2124 CZ3 TRP A 279 4914 10196 16468 -606 442 -2832 C ATOM 2125 CH2 TRP A 279 -38.900 0.964 17.124 1.00 86.55 C ANISOU 2125 CH2 TRP A 279 4969 10886 17031 -402 175 -2951 C TER 2126 TRP A 279 ATOM 2127 N GLN B 2 -11.966 28.424 4.694 1.00 56.31 N ANISOU 2127 N GLN B 2 6739 8455 6202 515 -308 2235 N ATOM 2128 CA GLN B 2 -13.057 28.130 5.669 1.00 54.49 C ANISOU 2128 CA GLN B 2 6495 8066 6143 451 -457 1960 C ATOM 2129 C GLN B 2 -13.750 26.810 5.371 1.00 54.46 C ANISOU 2129 C GLN B 2 6609 8358 5724 350 -602 1626 C ATOM 2130 O GLN B 2 -13.841 26.391 4.220 1.00 57.21 O ANISOU 2130 O GLN B 2 7004 9116 5618 327 -654 1673 O ATOM 2131 CB GLN B 2 -14.096 29.254 5.684 1.00 56.22 C ANISOU 2131 CB GLN B 2 6493 8215 6653 543 -532 2301 C ATOM 2132 CG GLN B 2 -13.939 30.248 6.833 1.00 55.40 C ANISOU 2132 CG GLN B 2 6313 7591 7144 566 -398 2314 C ATOM 2133 CD GLN B 2 -14.670 31.572 6.593 1.00 58.89 C ANISOU 2133 CD GLN B 2 6512 7906 7957 702 -354 2769 C ATOM 2134 OE1 GLN B 2 -15.657 31.633 5.853 1.00 61.19 O ANISOU 2134 OE1 GLN B 2 6656 8503 8092 779 -489 3049 O ATOM 2135 NE2 GLN B 2 -14.181 32.640 7.224 1.00 58.83 N ANISOU 2135 NE2 GLN B 2 6442 7443 8469 722 -155 2852 N ATOM 2136 N LYS B 3 -14.239 26.164 6.426 1.00 51.97 N ANISOU 2136 N LYS B 3 6341 7836 5568 273 -652 1279 N ATOM 2137 CA LYS B 3 -15.008 24.918 6.316 1.00 51.84 C ANISOU 2137 CA LYS B 3 6407 8010 5279 156 -775 941 C ATOM 2138 C LYS B 3 -16.099 24.838 7.413 1.00 49.93 C ANISOU 2138 C LYS B 3 6077 7556 5337 128 -875 798 C ATOM 2139 O LYS B 3 -15.851 25.126 8.595 1.00 47.23 O ANISOU 2139 O LYS B 3 5738 6866 5340 156 -778 725 O ATOM 2140 CB LYS B 3 -14.079 23.687 6.333 1.00 50.58 C ANISOU 2140 CB LYS B 3 6454 7824 4941 84 -620 597 C ATOM 2141 N THR B 4 -17.302 24.451 6.990 1.00 51.48 N ANISOU 2141 N THR B 4 6186 7997 5377 61 -1070 764 N ATOM 2142 CA THR B 4 -18.508 24.453 7.826 1.00 50.61 C ANISOU 2142 CA THR B 4 5940 7743 5547 51 -1166 714 C ATOM 2143 C THR B 4 -18.500 23.363 8.919 1.00 47.71 C ANISOU 2143 C THR B 4 5691 7132 5303 -29 -1084 307 C ATOM 2144 O THR B 4 -18.085 22.229 8.666 1.00 47.74 O ANISOU 2144 O THR B 4 5842 7208 5088 -133 -1045 23 O ATOM 2145 CB THR B 4 -19.766 24.354 6.922 1.00 54.02 C ANISOU 2145 CB THR B 4 6189 8570 5766 -15 -1425 855 C ATOM 2146 OG1 THR B 4 -19.843 25.531 6.114 1.00 56.93 O ANISOU 2146 OG1 THR B 4 6387 9135 6108 104 -1481 1345 O ATOM 2147 CG2 THR B 4 -21.063 24.218 7.725 1.00 53.79 C ANISOU 2147 CG2 THR B 4 5988 8410 6040 -32 -1516 811 C ATOM 2148 N PRO B 5 -18.957 23.711 10.138 1.00 45.51 N ANISOU 2148 N PRO B 5 5346 6557 5388 26 -1024 294 N ATOM 2149 CA PRO B 5 -19.084 22.767 11.241 1.00 43.15 C ANISOU 2149 CA PRO B 5 5118 6061 5215 -28 -944 -5 C ATOM 2150 C PRO B 5 -20.235 21.771 11.065 1.00 44.19 C ANISOU 2150 C PRO B 5 5171 6325 5296 -139 -1074 -168 C ATOM 2151 O PRO B 5 -21.339 22.172 10.678 1.00 46.42 O ANISOU 2151 O PRO B 5 5263 6751 5624 -140 -1233 2 O ATOM 2152 CB PRO B 5 -19.407 23.673 12.433 1.00 42.21 C ANISOU 2152 CB PRO B 5 4931 5659 5449 67 -845 78 C ATOM 2153 CG PRO B 5 -19.172 25.059 11.970 1.00 43.62 C ANISOU 2153 CG PRO B 5 5034 5808 5730 164 -828 381 C ATOM 2154 CD PRO B 5 -19.400 25.057 10.529 1.00 45.97 C ANISOU 2154 CD PRO B 5 5252 6444 5769 153 -989 580 C ATOM 2155 N GLN B 6 -19.981 20.490 11.341 1.00 42.97 N ANISOU 2155 N GLN B 6 5129 6109 5090 -236 -998 -465 N ATOM 2156 CA GLN B 6 -21.057 19.502 11.477 1.00 43.80 C ANISOU 2156 CA GLN B 6 5146 6230 5266 -356 -1071 -652 C ATOM 2157 C GLN B 6 -21.369 19.368 12.959 1.00 41.73 C ANISOU 2157 C GLN B 6 4844 5679 5331 -282 -930 -675 C ATOM 2158 O GLN B 6 -20.468 19.497 13.801 1.00 40.12 O ANISOU 2158 O GLN B 6 4749 5302 5192 -200 -763 -677 O ATOM 2159 CB GLN B 6 -20.678 18.137 10.892 1.00 44.64 C ANISOU 2159 CB GLN B 6 5387 6390 5186 -514 -1021 -973 C ATOM 2160 CG GLN B 6 -20.470 18.079 9.364 1.00 48.53 C ANISOU 2160 CG GLN B 6 5947 7222 5270 -631 -1144 -1034 C ATOM 2161 CD GLN B 6 -21.638 18.642 8.547 1.00 53.66 C ANISOU 2161 CD GLN B 6 6396 8220 5771 -712 -1450 -864 C ATOM 2162 OE1 GLN B 6 -22.546 17.904 8.136 1.00 56.95 O ANISOU 2162 OE1 GLN B 6 6726 8797 6117 -913 -1609 -1057 O ATOM 2163 NE2 GLN B 6 -21.613 19.957 8.303 1.00 54.14 N ANISOU 2163 NE2 GLN B 6 6356 8402 5814 -564 -1530 -477 N ATOM 2164 N ILE B 7 -22.640 19.135 13.286 1.00 42.14 N ANISOU 2164 N ILE B 7 4723 5715 5573 -318 -999 -671 N ATOM 2165 CA ILE B 7 -23.076 19.070 14.686 1.00 39.83 C ANISOU 2165 CA ILE B 7 4378 5184 5571 -234 -842 -662 C ATOM 2166 C ILE B 7 -23.971 17.860 14.904 1.00 40.60 C ANISOU 2166 C ILE B 7 4366 5238 5823 -350 -842 -811 C ATOM 2167 O ILE B 7 -24.905 17.634 14.134 1.00 43.06 O ANISOU 2167 O ILE B 7 4518 5708 6134 -474 -1031 -821 O ATOM 2168 CB ILE B 7 -23.843 20.332 15.110 1.00 40.19 C ANISOU 2168 CB ILE B 7 4279 5174 5819 -102 -842 -422 C ATOM 2169 CG1 ILE B 7 -23.097 21.597 14.676 1.00 39.69 C ANISOU 2169 CG1 ILE B 7 4280 5135 5667 -12 -849 -252 C ATOM 2170 CG2 ILE B 7 -24.058 20.331 16.610 1.00 39.02 C ANISOU 2170 CG2 ILE B 7 4142 4792 5890 -10 -621 -453 C ATOM 2171 CD1 ILE B 7 -23.867 22.864 14.878 1.00 40.59 C ANISOU 2171 CD1 ILE B 7 4231 5158 6034 119 -815 0 C ATOM 2172 N GLN B 8 -23.683 17.090 15.954 1.00 38.68 N ANISOU 2172 N GLN B 8 4182 4795 5719 -319 -635 -902 N ATOM 2173 CA GLN B 8 -24.405 15.849 16.226 1.00 39.01 C ANISOU 2173 CA GLN B 8 4118 4736 5969 -424 -577 -1028 C ATOM 2174 C GLN B 8 -24.772 15.721 17.697 1.00 37.58 C ANISOU 2174 C GLN B 8 3872 4373 6032 -301 -367 -922 C ATOM 2175 O GLN B 8 -23.900 15.698 18.567 1.00 35.99 O ANISOU 2175 O GLN B 8 3797 4096 5782 -200 -194 -884 O ATOM 2176 CB GLN B 8 -23.588 14.637 15.773 1.00 39.17 C ANISOU 2176 CB GLN B 8 4270 4693 5919 -538 -483 -1257 C ATOM 2177 CG GLN B 8 -23.263 14.644 14.293 1.00 41.29 C ANISOU 2177 CG GLN B 8 4626 5165 5898 -679 -651 -1413 C ATOM 2178 CD GLN B 8 -22.967 13.264 13.737 1.00 44.44 C ANISOU 2178 CD GLN B 8 5108 5467 6311 -853 -538 -1726 C ATOM 2179 OE1 GLN B 8 -21.920 13.048 13.130 1.00 44.10 O ANISOU 2179 OE1 GLN B 8 5245 5441 6069 -862 -446 -1844 O ATOM 2180 NE2 GLN B 8 -23.893 12.321 13.937 1.00 46.90 N ANISOU 2180 NE2 GLN B 8 5279 5643 6896 -996 -511 -1868 N ATOM 2181 N VAL B 9 -26.069 15.627 17.968 1.00 38.22 N ANISOU 2181 N VAL B 9 3739 4420 6362 -318 -385 -852 N ATOM 2182 CA VAL B 9 -26.549 15.527 19.343 1.00 37.08 C ANISOU 2182 CA VAL B 9 3522 4130 6438 -193 -158 -732 C ATOM 2183 C VAL B 9 -26.977 14.106 19.664 1.00 37.99 C ANISOU 2183 C VAL B 9 3524 4103 6809 -283 -33 -793 C ATOM 2184 O VAL B 9 -27.738 13.506 18.916 1.00 40.16 O ANISOU 2184 O VAL B 9 3641 4380 7239 -455 -164 -891 O ATOM 2185 CB VAL B 9 -27.720 16.488 19.594 1.00 38.15 C ANISOU 2185 CB VAL B 9 3472 4277 6748 -102 -177 -555 C ATOM 2186 CG1 VAL B 9 -27.991 16.605 21.082 1.00 37.52 C ANISOU 2186 CG1 VAL B 9 3390 4069 6798 57 114 -452 C ATOM 2187 CG2 VAL B 9 -27.426 17.858 18.979 1.00 37.19 C ANISOU 2187 CG2 VAL B 9 3410 4261 6460 -37 -309 -476 C ATOM 2188 N TYR B 10 -26.486 13.575 20.781 1.00 36.88 N ANISOU 2188 N TYR B 10 3444 3851 6718 -179 219 -720 N ATOM 2189 CA TYR B 10 -26.739 12.182 21.176 1.00 37.84 C ANISOU 2189 CA TYR B 10 3453 3794 7132 -234 403 -719 C ATOM 2190 C TYR B 10 -26.528 11.974 22.670 1.00 36.97 C ANISOU 2190 C TYR B 10 3344 3641 7063 -56 687 -497 C ATOM 2191 O TYR B 10 -25.708 12.650 23.278 1.00 35.63 O ANISOU 2191 O TYR B 10 3332 3597 6610 62 727 -422 O ATOM 2192 CB TYR B 10 -25.871 11.205 20.365 1.00 38.25 C ANISOU 2192 CB TYR B 10 3606 3760 7169 -366 408 -915 C ATOM 2193 CG TYR B 10 -24.369 11.469 20.390 1.00 37.19 C ANISOU 2193 CG TYR B 10 3695 3697 6740 -273 450 -899 C ATOM 2194 CD1 TYR B 10 -23.789 12.425 19.554 1.00 36.24 C ANISOU 2194 CD1 TYR B 10 3722 3747 6301 -291 246 -987 C ATOM 2195 CD2 TYR B 10 -23.528 10.742 21.236 1.00 38.15 C ANISOU 2195 CD2 TYR B 10 3841 3724 6929 -167 698 -747 C ATOM 2196 CE1 TYR B 10 -22.421 12.658 19.575 1.00 35.57 C ANISOU 2196 CE1 TYR B 10 3805 3719 5992 -217 288 -951 C ATOM 2197 CE2 TYR B 10 -22.155 10.964 21.265 1.00 36.28 C ANISOU 2197 CE2 TYR B 10 3755 3574 6456 -91 722 -689 C ATOM 2198 CZ TYR B 10 -21.606 11.920 20.431 1.00 35.98 C ANISOU 2198 CZ TYR B 10 3864 3686 6122 -124 517 -807 C ATOM 2199 OH TYR B 10 -20.238 12.136 20.444 1.00 34.91 O ANISOU 2199 OH TYR B 10 3846 3628 5792 -60 544 -732 O ATOM 2200 N SER B 11 -27.280 11.049 23.257 1.00 38.36 N ANISOU 2200 N SER B 11 3329 3664 7581 -54 878 -383 N ATOM 2201 CA SER B 11 -27.173 10.766 24.681 1.00 38.49 C ANISOU 2201 CA SER B 11 3319 3686 7621 116 1164 -120 C ATOM 2202 C SER B 11 -26.223 9.594 24.979 1.00 38.97 C ANISOU 2202 C SER B 11 3392 3646 7769 139 1354 -12 C ATOM 2203 O SER B 11 -26.050 8.691 24.151 1.00 39.65 O ANISOU 2203 O SER B 11 3441 3534 8090 5 1354 -157 O ATOM 2204 CB SER B 11 -28.551 10.502 25.269 1.00 40.62 C ANISOU 2204 CB SER B 11 3343 3855 8234 149 1318 30 C ATOM 2205 OG SER B 11 -29.237 9.521 24.516 1.00 42.93 O ANISOU 2205 OG SER B 11 3436 3934 8943 -33 1281 -70 O ATOM 2206 N ARG B 12 -25.611 9.628 26.166 1.00 38.75 N ANISOU 2206 N ARG B 12 3408 3768 7549 303 1530 248 N ATOM 2207 CA ARG B 12 -24.604 8.645 26.579 1.00 39.07 C ANISOU 2207 CA ARG B 12 3424 3772 7647 370 1716 465 C ATOM 2208 C ARG B 12 -25.277 7.325 26.858 1.00 42.21 C ANISOU 2208 C ARG B 12 3581 3891 8565 374 1989 642 C ATOM 2209 O ARG B 12 -24.706 6.259 26.609 1.00 43.07 O ANISOU 2209 O ARG B 12 3624 3785 8957 361 2149 712 O ATOM 2210 CB ARG B 12 -23.854 9.136 27.829 1.00 38.49 C ANISOU 2210 CB ARG B 12 3426 4030 7168 523 1783 734 C ATOM 2211 CG ARG B 12 -22.867 8.152 28.485 1.00 37.71 C ANISOU 2211 CG ARG B 12 3230 3979 7118 630 1985 1102 C ATOM 2212 CD ARG B 12 -21.824 7.651 27.518 1.00 34.04 C ANISOU 2212 CD ARG B 12 2805 3355 6774 573 1940 1012 C ATOM 2213 NE ARG B 12 -20.892 6.674 28.089 1.00 33.85 N ANISOU 2213 NE ARG B 12 2638 3336 6889 699 2167 1421 N ATOM 2214 CZ ARG B 12 -21.191 5.403 28.362 1.00 35.13 C ANISOU 2214 CZ ARG B 12 2579 3225 7542 769 2482 1687 C ATOM 2215 NH1 ARG B 12 -22.408 4.934 28.155 1.00 35.12 N ANISOU 2215 NH1 ARG B 12 2479 2932 7934 701 2595 1559 N ATOM 2216 NH2 ARG B 12 -20.270 4.594 28.858 1.00 36.78 N ANISOU 2216 NH2 ARG B 12 2633 3448 7892 908 2696 2118 N ATOM 2217 N HIS B 13 -26.500 7.419 27.370 1.00 43.95 N ANISOU 2217 N HIS B 13 3657 4088 8954 398 2073 725 N ATOM 2218 CA HIS B 13 -27.290 6.255 27.754 1.00 47.56 C ANISOU 2218 CA HIS B 13 3848 4278 9943 405 2353 933 C ATOM 2219 C HIS B 13 -28.633 6.249 27.026 1.00 48.74 C ANISOU 2219 C HIS B 13 3844 4229 10445 228 2243 701 C ATOM 2220 O HIS B 13 -29.026 7.268 26.452 1.00 47.21 O ANISOU 2220 O HIS B 13 3735 4173 10030 158 1971 471 O ATOM 2221 CB HIS B 13 -27.512 6.257 29.276 1.00 49.24 C ANISOU 2221 CB HIS B 13 3968 4692 10049 623 2621 1367 C ATOM 2222 CG HIS B 13 -26.244 6.264 30.074 1.00 49.05 C ANISOU 2222 CG HIS B 13 4048 4953 9636 773 2693 1645 C ATOM 2223 ND1 HIS B 13 -25.295 5.268 29.974 1.00 49.84 N ANISOU 2223 ND1 HIS B 13 4078 4922 9936 804 2825 1841 N ATOM 2224 CD2 HIS B 13 -25.775 7.137 30.997 1.00 48.78 C ANISOU 2224 CD2 HIS B 13 4159 5340 9034 884 2654 1767 C ATOM 2225 CE1 HIS B 13 -24.292 5.531 30.792 1.00 49.98 C ANISOU 2225 CE1 HIS B 13 4162 5305 9522 936 2831 2123 C ATOM 2226 NE2 HIS B 13 -24.557 6.661 31.424 1.00 49.65 N ANISOU 2226 NE2 HIS B 13 4263 5619 8984 965 2712 2056 N ATOM 2227 N PRO B 14 -29.340 5.105 27.047 1.00 52.00 N ANISOU 2227 N PRO B 14 4000 4320 11436 150 2454 790 N ATOM 2228 CA PRO B 14 -30.698 5.069 26.516 1.00 53.93 C ANISOU 2228 CA PRO B 14 4034 4416 12042 -30 2349 630 C ATOM 2229 C PRO B 14 -31.547 6.109 27.231 1.00 53.64 C ANISOU 2229 C PRO B 14 3943 4616 11820 117 2338 804 C ATOM 2230 O PRO B 14 -31.586 6.119 28.462 1.00 54.03 O ANISOU 2230 O PRO B 14 3958 4770 11800 339 2618 1154 O ATOM 2231 CB PRO B 14 -31.192 3.662 26.885 1.00 57.67 C ANISOU 2231 CB PRO B 14 4220 4517 13175 -73 2687 830 C ATOM 2232 CG PRO B 14 -29.976 2.859 27.130 1.00 57.80 C ANISOU 2232 CG PRO B 14 4327 4411 13225 24 2919 973 C ATOM 2233 CD PRO B 14 -28.943 3.812 27.638 1.00 54.71 C ANISOU 2233 CD PRO B 14 4197 4424 12165 234 2821 1096 C ATOM 2234 N PRO B 15 -32.208 6.998 26.468 1.00 53.32 N ANISOU 2234 N PRO B 15 3893 4675 11691 4 2037 579 N ATOM 2235 CA PRO B 15 -32.963 8.067 27.111 1.00 53.37 C ANISOU 2235 CA PRO B 15 3857 4865 11556 169 2075 739 C ATOM 2236 C PRO B 15 -34.214 7.520 27.775 1.00 57.10 C ANISOU 2236 C PRO B 15 3986 5179 12530 209 2340 1017 C ATOM 2237 O PRO B 15 -34.896 6.649 27.221 1.00 59.83 O ANISOU 2237 O PRO B 15 4065 5285 13382 2 2304 966 O ATOM 2238 CB PRO B 15 -33.302 9.016 25.956 1.00 52.14 C ANISOU 2238 CB PRO B 15 3724 4816 11272 28 1689 477 C ATOM 2239 CG PRO B 15 -33.272 8.188 24.740 1.00 53.30 C ANISOU 2239 CG PRO B 15 3795 4818 11637 -268 1462 205 C ATOM 2240 CD PRO B 15 -32.339 7.024 24.999 1.00 53.58 C ANISOU 2240 CD PRO B 15 3927 4666 11766 -276 1681 201 C ATOM 2241 N GLU B 16 -34.489 8.004 28.977 1.00 57.97 N ANISOU 2241 N GLU B 16 4105 5424 12497 461 2625 1297 N ATOM 2242 CA GLU B 16 -35.619 7.517 29.755 1.00 61.69 C ANISOU 2242 CA GLU B 16 4257 5768 13416 548 2948 1622 C ATOM 2243 C GLU B 16 -36.204 8.675 30.567 1.00 62.19 C ANISOU 2243 C GLU B 16 4359 6024 13248 778 3126 1761 C ATOM 2244 O GLU B 16 -35.513 9.301 31.374 1.00 61.07 O ANISOU 2244 O GLU B 16 4501 6116 12587 959 3264 1785 O ATOM 2245 CB GLU B 16 -35.186 6.328 30.630 1.00 63.07 C ANISOU 2245 CB GLU B 16 4372 5844 13749 642 3297 1925 C ATOM 2246 CG GLU B 16 -36.101 6.037 31.798 1.00 67.04 C ANISOU 2246 CG GLU B 16 4628 6326 14519 834 3723 2353 C ATOM 2247 CD GLU B 16 -36.341 4.553 32.013 1.00 71.01 C ANISOU 2247 CD GLU B 16 4832 6517 15633 780 3987 2628 C ATOM 2248 OE1 GLU B 16 -35.458 3.738 31.648 1.00 71.59 O ANISOU 2248 OE1 GLU B 16 4972 6445 15784 684 3948 2560 O ATOM 2249 OE2 GLU B 16 -37.420 4.207 32.549 1.00 72.88 O ANISOU 2249 OE2 GLU B 16 4749 6624 16317 841 4266 2928 O ATOM 2250 N ASN B 17 -37.474 8.975 30.336 1.00 64.50 N ANISOU 2250 N ASN B 17 4357 6217 13934 757 3130 1838 N ATOM 2251 CA ASN B 17 -38.074 10.137 30.970 1.00 65.68 C ANISOU 2251 CA ASN B 17 4532 6490 13933 978 3330 1940 C ATOM 2252 C ASN B 17 -37.852 10.180 32.485 1.00 67.03 C ANISOU 2252 C ASN B 17 4860 6813 13794 1244 3798 2170 C ATOM 2253 O ASN B 17 -37.931 9.151 33.165 1.00 68.93 O ANISOU 2253 O ASN B 17 4960 7004 14226 1293 4066 2451 O ATOM 2254 CB ASN B 17 -39.547 10.273 30.584 1.00 68.53 C ANISOU 2254 CB ASN B 17 4464 6702 14874 938 3326 2094 C ATOM 2255 CG ASN B 17 -39.728 10.818 29.170 1.00 67.93 C ANISOU 2255 CG ASN B 17 4304 6637 14871 728 2837 1864 C ATOM 2256 OD1 ASN B 17 -38.768 11.249 28.530 1.00 65.27 O ANISOU 2256 OD1 ASN B 17 4265 6415 14119 649 2547 1584 O ATOM 2257 ND2 ASN B 17 -40.964 10.812 28.683 1.00 71.41 N ANISOU 2257 ND2 ASN B 17 4312 6989 15833 637 2745 2021 N ATOM 2258 N GLY B 18 -37.512 11.367 32.988 1.00 66.34 N ANISOU 2258 N GLY B 18 5073 6925 13209 1397 3894 2041 N ATOM 2259 CA GLY B 18 -37.278 11.582 34.417 1.00 68.21 C ANISOU 2259 CA GLY B 18 5509 7386 13021 1618 4317 2183 C ATOM 2260 C GLY B 18 -36.054 10.914 35.036 1.00 67.51 C ANISOU 2260 C GLY B 18 5639 7529 12481 1619 4336 2249 C ATOM 2261 O GLY B 18 -35.952 10.834 36.258 1.00 69.82 O ANISOU 2261 O GLY B 18 6021 8059 12448 1782 4688 2455 O ATOM 2262 N LYS B 19 -35.120 10.447 34.208 1.00 64.77 N ANISOU 2262 N LYS B 19 5367 7145 12099 1444 3975 2099 N ATOM 2263 CA LYS B 19 -33.910 9.783 34.707 1.00 64.43 C ANISOU 2263 CA LYS B 19 5477 7307 11695 1452 3980 2216 C ATOM 2264 C LYS B 19 -32.629 10.478 34.230 1.00 61.23 C ANISOU 2264 C LYS B 19 5408 7076 10779 1351 3638 1885 C ATOM 2265 O LYS B 19 -32.416 10.614 33.028 1.00 58.90 O ANISOU 2265 O LYS B 19 5127 6607 10644 1193 3301 1628 O ATOM 2266 CB LYS B 19 -33.896 8.297 34.309 1.00 65.06 C ANISOU 2266 CB LYS B 19 5281 7131 12306 1364 3980 2443 C ATOM 2267 N PRO B 20 -31.774 10.931 35.174 1.00 61.76 N ANISOU 2267 N PRO B 20 5738 7516 10213 1427 3721 1894 N ATOM 2268 CA PRO B 20 -30.486 11.565 34.850 1.00 59.00 C ANISOU 2268 CA PRO B 20 5681 7358 9380 1322 3414 1618 C ATOM 2269 C PRO B 20 -29.697 10.838 33.758 1.00 56.33 C ANISOU 2269 C PRO B 20 5288 6847 9267 1183 3108 1576 C ATOM 2270 O PRO B 20 -29.649 9.604 33.731 1.00 57.18 O ANISOU 2270 O PRO B 20 5189 6825 9711 1192 3200 1849 O ATOM 2271 CB PRO B 20 -29.734 11.502 36.178 1.00 61.27 C ANISOU 2271 CB PRO B 20 6109 8097 9074 1406 3587 1819 C ATOM 2272 CG PRO B 20 -30.813 11.648 37.200 1.00 65.06 C ANISOU 2272 CG PRO B 20 6524 8657 9538 1565 4000 1983 C ATOM 2273 CD PRO B 20 -32.059 11.001 36.622 1.00 65.34 C ANISOU 2273 CD PRO B 20 6226 8266 10335 1602 4117 2139 C ATOM 2274 N ASN B 21 -29.092 11.619 32.869 1.00 53.37 N ANISOU 2274 N ASN B 21 5099 6449 8729 1061 2789 1235 N ATOM 2275 CA ASN B 21 -28.357 11.112 31.713 1.00 51.02 C ANISOU 2275 CA ASN B 21 4792 5993 8602 925 2509 1124 C ATOM 2276 C ASN B 21 -27.354 12.203 31.338 1.00 48.89 C ANISOU 2276 C ASN B 21 4799 5889 7888 849 2246 838 C ATOM 2277 O ASN B 21 -27.351 13.269 31.957 1.00 49.62 O ANISOU 2277 O ASN B 21 5064 6165 7623 884 2292 713 O ATOM 2278 CB ASN B 21 -29.341 10.826 30.558 1.00 50.53 C ANISOU 2278 CB ASN B 21 4536 5582 9082 820 2397 995 C ATOM 2279 CG ASN B 21 -28.747 9.960 29.439 1.00 48.99 C ANISOU 2279 CG ASN B 21 4298 5194 9123 668 2204 892 C ATOM 2280 OD1 ASN B 21 -27.530 9.799 29.323 1.00 49.41 O ANISOU 2280 OD1 ASN B 21 4493 5344 8938 652 2119 878 O ATOM 2281 ND2 ASN B 21 -29.618 9.410 28.600 1.00 47.91 N ANISOU 2281 ND2 ASN B 21 3957 4788 9459 542 2144 808 N ATOM 2282 N ILE B 22 -26.497 11.932 30.356 1.00 46.86 N ANISOU 2282 N ILE B 22 4585 5551 7670 741 2005 726 N ATOM 2283 CA ILE B 22 -25.612 12.942 29.785 1.00 44.56 C ANISOU 2283 CA ILE B 22 4515 5359 7057 657 1747 467 C ATOM 2284 C ILE B 22 -25.951 13.180 28.316 1.00 43.10 C ANISOU 2284 C ILE B 22 4306 4940 7130 548 1518 235 C ATOM 2285 O ILE B 22 -26.153 12.227 27.550 1.00 43.18 O ANISOU 2285 O ILE B 22 4178 4757 7470 478 1480 244 O ATOM 2286 CB ILE B 22 -24.149 12.520 29.884 1.00 43.89 C ANISOU 2286 CB ILE B 22 4500 5447 6730 631 1662 572 C ATOM 2287 CG1 ILE B 22 -23.721 12.464 31.352 1.00 46.55 C ANISOU 2287 CG1 ILE B 22 4858 6134 6693 714 1825 817 C ATOM 2288 CG2 ILE B 22 -23.264 13.472 29.082 1.00 40.83 C ANISOU 2288 CG2 ILE B 22 4299 5102 6112 528 1391 312 C ATOM 2289 CD1 ILE B 22 -22.438 11.684 31.577 1.00 48.32 C ANISOU 2289 CD1 ILE B 22 5025 6537 6798 723 1792 1090 C ATOM 2290 N LEU B 23 -26.006 14.453 27.930 1.00 42.09 N ANISOU 2290 N LEU B 23 4309 4836 6846 523 1379 29 N ATOM 2291 CA LEU B 23 -26.240 14.828 26.540 1.00 40.86 C ANISOU 2291 CA LEU B 23 4131 4546 6849 428 1139 -138 C ATOM 2292 C LEU B 23 -24.950 15.322 25.890 1.00 39.14 C ANISOU 2292 C LEU B 23 4100 4416 6357 357 932 -271 C ATOM 2293 O LEU B 23 -24.338 16.273 26.375 1.00 38.90 O ANISOU 2293 O LEU B 23 4231 4509 6042 375 928 -334 O ATOM 2294 CB LEU B 23 -27.320 15.905 26.458 1.00 41.50 C ANISOU 2294 CB LEU B 23 4160 4560 7050 478 1158 -186 C ATOM 2295 CG LEU B 23 -27.871 16.279 25.083 1.00 41.23 C ANISOU 2295 CG LEU B 23 4015 4435 7216 398 916 -257 C ATOM 2296 CD1 LEU B 23 -28.721 15.176 24.501 1.00 41.99 C ANISOU 2296 CD1 LEU B 23 3865 4432 7656 306 858 -202 C ATOM 2297 CD2 LEU B 23 -28.681 17.543 25.196 1.00 42.37 C ANISOU 2297 CD2 LEU B 23 4118 4527 7454 495 985 -236 C ATOM 2298 N ASN B 24 -24.547 14.673 24.798 1.00 38.36 N ANISOU 2298 N ASN B 24 3976 4246 6352 262 782 -330 N ATOM 2299 CA ASN B 24 -23.333 15.043 24.072 1.00 36.93 C ANISOU 2299 CA ASN B 24 3947 4136 5948 204 615 -427 C ATOM 2300 C ASN B 24 -23.624 15.893 22.830 1.00 36.37 C ANISOU 2300 C ASN B 24 3897 4044 5879 140 400 -563 C ATOM 2301 O ASN B 24 -24.628 15.674 22.141 1.00 37.32 O ANISOU 2301 O ASN B 24 3878 4096 6207 88 323 -593 O ATOM 2302 CB ASN B 24 -22.554 13.792 23.659 1.00 37.14 C ANISOU 2302 CB ASN B 24 3954 4106 6053 159 647 -397 C ATOM 2303 CG ASN B 24 -22.209 12.888 24.833 1.00 38.97 C ANISOU 2303 CG ASN B 24 4115 4367 6323 244 870 -168 C ATOM 2304 OD1 ASN B 24 -21.934 13.358 25.931 1.00 40.35 O ANISOU 2304 OD1 ASN B 24 4335 4725 6272 315 935 -48 O ATOM 2305 ND2 ASN B 24 -22.209 11.577 24.594 1.00 40.51 N ANISOU 2305 ND2 ASN B 24 4196 4389 6806 228 1002 -103 N ATOM 2306 N CYS B 25 -22.753 16.864 22.557 1.00 35.06 N ANISOU 2306 N CYS B 25 3875 3957 5488 136 298 -612 N ATOM 2307 CA CYS B 25 -22.790 17.614 21.304 1.00 35.03 C ANISOU 2307 CA CYS B 25 3886 3963 5460 89 104 -674 C ATOM 2308 C CYS B 25 -21.405 17.664 20.661 1.00 34.17 C ANISOU 2308 C CYS B 25 3911 3925 5146 43 17 -710 C ATOM 2309 O CYS B 25 -20.454 18.230 21.230 1.00 33.66 O ANISOU 2309 O CYS B 25 3952 3913 4926 62 47 -689 O ATOM 2310 CB CYS B 25 -23.310 19.024 21.508 1.00 35.53 C ANISOU 2310 CB CYS B 25 3951 3997 5553 155 110 -649 C ATOM 2311 SG CYS B 25 -23.151 20.028 20.013 1.00 36.45 S ANISOU 2311 SG CYS B 25 4064 4153 5633 126 -105 -619 S ATOM 2312 N TYR B 26 -21.311 17.084 19.468 1.00 34.19 N ANISOU 2312 N TYR B 26 3901 3942 5146 -33 -85 -775 N ATOM 2313 CA TYR B 26 -20.041 16.835 18.833 1.00 33.61 C ANISOU 2313 CA TYR B 26 3939 3916 4917 -64 -101 -804 C ATOM 2314 C TYR B 26 -19.941 17.631 17.543 1.00 34.16 C ANISOU 2314 C TYR B 26 4046 4081 4851 -102 -271 -823 C ATOM 2315 O TYR B 26 -20.649 17.355 16.559 1.00 35.75 O ANISOU 2315 O TYR B 26 4191 4344 5050 -180 -385 -894 O ATOM 2316 CB TYR B 26 -19.898 15.348 18.574 1.00 34.28 C ANISOU 2316 CB TYR B 26 4001 3917 5106 -117 6 -882 C ATOM 2317 CG TYR B 26 -18.577 14.875 17.972 1.00 35.11 C ANISOU 2317 CG TYR B 26 4206 4024 5112 -127 76 -905 C ATOM 2318 CD1 TYR B 26 -17.340 15.199 18.552 1.00 34.53 C ANISOU 2318 CD1 TYR B 26 4176 3999 4944 -53 135 -754 C ATOM 2319 CD2 TYR B 26 -18.576 14.035 16.857 1.00 36.25 C ANISOU 2319 CD2 TYR B 26 4384 4119 5269 -222 105 -1086 C ATOM 2320 CE1 TYR B 26 -16.142 14.713 18.007 1.00 35.10 C ANISOU 2320 CE1 TYR B 26 4297 4056 4982 -41 234 -729 C ATOM 2321 CE2 TYR B 26 -17.404 13.554 16.316 1.00 36.97 C ANISOU 2321 CE2 TYR B 26 4566 4177 5303 -212 238 -1113 C ATOM 2322 CZ TYR B 26 -16.194 13.885 16.887 1.00 36.98 C ANISOU 2322 CZ TYR B 26 4582 4209 5258 -104 312 -908 C ATOM 2323 OH TYR B 26 -15.049 13.381 16.304 1.00 38.52 O ANISOU 2323 OH TYR B 26 4834 4358 5443 -78 473 -899 O ATOM 2324 N VAL B 27 -19.055 18.627 17.570 1.00 33.11 N ANISOU 2324 N VAL B 27 3993 3986 4602 -61 -291 -744 N ATOM 2325 CA VAL B 27 -18.858 19.543 16.462 1.00 33.16 C ANISOU 2325 CA VAL B 27 4020 4080 4498 -66 -416 -684 C ATOM 2326 C VAL B 27 -17.537 19.234 15.758 1.00 33.11 C ANISOU 2326 C VAL B 27 4115 4135 4329 -87 -386 -688 C ATOM 2327 O VAL B 27 -16.479 19.121 16.400 1.00 31.94 O ANISOU 2327 O VAL B 27 4012 3948 4175 -66 -289 -650 O ATOM 2328 CB VAL B 27 -18.891 20.989 16.942 1.00 32.84 C ANISOU 2328 CB VAL B 27 3971 3977 4528 -5 -417 -578 C ATOM 2329 CG1 VAL B 27 -19.041 21.922 15.763 1.00 34.15 C ANISOU 2329 CG1 VAL B 27 4094 4220 4663 13 -533 -440 C ATOM 2330 CG2 VAL B 27 -20.042 21.185 17.898 1.00 33.39 C ANISOU 2330 CG2 VAL B 27 3959 3946 4780 37 -353 -591 C ATOM 2331 N THR B 28 -17.613 19.098 14.433 1.00 34.32 N ANISOU 2331 N THR B 28 4288 4417 4336 -133 -468 -718 N ATOM 2332 CA THR B 28 -16.503 18.592 13.635 1.00 34.81 C ANISOU 2332 CA THR B 28 4453 4536 4238 -152 -386 -757 C ATOM 2333 C THR B 28 -16.380 19.315 12.312 1.00 36.73 C ANISOU 2333 C THR B 28 4721 4973 4262 -160 -490 -670 C ATOM 2334 O THR B 28 -17.268 20.067 11.922 1.00 37.98 O ANISOU 2334 O THR B 28 4792 5240 4398 -160 -649 -567 O ATOM 2335 CB THR B 28 -16.696 17.109 13.296 1.00 35.74 C ANISOU 2335 CB THR B 28 4607 4616 4355 -234 -287 -983 C ATOM 2336 OG1 THR B 28 -18.031 16.907 12.837 1.00 36.70 O ANISOU 2336 OG1 THR B 28 4658 4824 4461 -335 -437 -1100 O ATOM 2337 CG2 THR B 28 -16.452 16.238 14.502 1.00 34.28 C ANISOU 2337 CG2 THR B 28 4390 4237 4396 -196 -114 -993 C ATOM 2338 N GLN B 29 -15.264 19.067 11.627 1.00 37.74 N ANISOU 2338 N GLN B 29 4947 5153 4239 -151 -378 -668 N ATOM 2339 CA GLN B 29 -15.062 19.479 10.228 1.00 40.03 C ANISOU 2339 CA GLN B 29 5284 5677 4248 -164 -429 -600 C ATOM 2340 C GLN B 29 -14.896 20.993 10.001 1.00 39.49 C ANISOU 2340 C GLN B 29 5141 5673 4190 -80 -519 -287 C ATOM 2341 O GLN B 29 -14.883 21.452 8.844 1.00 41.56 O ANISOU 2341 O GLN B 29 5405 6169 4217 -74 -579 -151 O ATOM 2342 CB GLN B 29 -16.174 18.919 9.310 1.00 42.94 C ANISOU 2342 CB GLN B 29 5652 6264 4399 -293 -571 -781 C ATOM 2343 CG GLN B 29 -16.356 17.396 9.314 1.00 45.98 C ANISOU 2343 CG GLN B 29 6119 6558 4795 -415 -452 -1138 C ATOM 2344 CD GLN B 29 -15.072 16.632 9.008 1.00 50.13 C ANISOU 2344 CD GLN B 29 6795 6983 5268 -388 -164 -1256 C ATOM 2345 OE1 GLN B 29 -14.286 17.020 8.132 1.00 52.47 O ANISOU 2345 OE1 GLN B 29 7175 7433 5327 -349 -96 -1169 O ATOM 2346 NE2 GLN B 29 -14.860 15.530 9.726 1.00 50.92 N ANISOU 2346 NE2 GLN B 29 6911 6815 5621 -393 39 -1417 N ATOM 2347 N PHE B 30 -14.742 21.763 11.081 1.00 36.85 N ANISOU 2347 N PHE B 30 4741 5136 4123 -25 -508 -174 N ATOM 2348 CA PHE B 30 -14.608 23.218 10.941 1.00 36.62 C ANISOU 2348 CA PHE B 30 4633 5081 4199 41 -545 95 C ATOM 2349 C PHE B 30 -13.177 23.749 10.883 1.00 36.19 C ANISOU 2349 C PHE B 30 4603 4958 4190 71 -424 241 C ATOM 2350 O PHE B 30 -12.251 23.155 11.440 1.00 35.29 O ANISOU 2350 O PHE B 30 4536 4762 4112 49 -320 150 O ATOM 2351 CB PHE B 30 -15.394 23.952 12.018 1.00 35.59 C ANISOU 2351 CB PHE B 30 4415 4753 4355 61 -579 110 C ATOM 2352 CG PHE B 30 -15.017 23.574 13.404 1.00 32.55 C ANISOU 2352 CG PHE B 30 4076 4185 4106 25 -496 -64 C ATOM 2353 CD1 PHE B 30 -15.620 22.481 14.028 1.00 31.06 C ANISOU 2353 CD1 PHE B 30 3904 3988 3910 -6 -492 -256 C ATOM 2354 CD2 PHE B 30 -14.078 24.320 14.106 1.00 30.89 C ANISOU 2354 CD2 PHE B 30 3873 3832 4030 7 -428 -21 C ATOM 2355 CE1 PHE B 30 -15.271 22.121 15.343 1.00 29.27 C ANISOU 2355 CE1 PHE B 30 3700 3649 3772 -28 -413 -357 C ATOM 2356 CE2 PHE B 30 -13.731 23.975 15.414 1.00 29.31 C ANISOU 2356 CE2 PHE B 30 3701 3549 3886 -48 -384 -165 C ATOM 2357 CZ PHE B 30 -14.334 22.875 16.036 1.00 27.57 C ANISOU 2357 CZ PHE B 30 3496 3358 3622 -52 -374 -310 C ATOM 2358 N HIS B 31 -13.026 24.871 10.186 1.00 37.03 N ANISOU 2358 N HIS B 31 4641 5105 4325 127 -434 513 N ATOM 2359 CA HIS B 31 -11.784 25.616 10.112 0.50 36.79 C ANISOU 2359 CA HIS B 31 4585 4979 4416 149 -323 702 C ATOM 2360 C HIS B 31 -12.177 27.058 9.801 1.00 38.98 C ANISOU 2360 C HIS B 31 4737 5176 4898 210 -342 992 C ATOM 2361 O HIS B 31 -13.001 27.286 8.904 1.00 40.52 O ANISOU 2361 O HIS B 31 4870 5564 4960 273 -419 1170 O ATOM 2362 CB HIS B 31 -10.883 25.052 9.014 0.50 37.43 C ANISOU 2362 CB HIS B 31 4731 5262 4227 178 -218 777 C ATOM 2363 CG HIS B 31 -9.437 25.368 9.207 0.50 35.19 C ANISOU 2363 CG HIS B 31 4413 4858 4098 181 -76 911 C ATOM 2364 ND1 HIS B 31 -8.917 26.625 8.996 0.50 34.84 N ANISOU 2364 ND1 HIS B 31 4259 4716 4263 206 -36 1198 N ATOM 2365 CD2 HIS B 31 -8.403 24.592 9.601 0.50 32.66 C ANISOU 2365 CD2 HIS B 31 4117 4492 3800 159 39 830 C ATOM 2366 CE1 HIS B 31 -7.623 26.611 9.255 0.50 34.21 C ANISOU 2366 CE1 HIS B 31 4137 4549 4312 176 75 1265 C ATOM 2367 NE2 HIS B 31 -7.286 25.389 9.623 0.50 32.73 N ANISOU 2367 NE2 HIS B 31 4020 4407 4008 156 118 1064 N ATOM 2368 N PRO B 32 -11.612 28.044 10.534 1.00 39.44 N ANISOU 2368 N PRO B 32 4735 4953 5297 180 -266 1051 N ATOM 2369 CA PRO B 32 -10.594 28.003 11.592 1.00 38.67 C ANISOU 2369 CA PRO B 32 4663 4676 5354 69 -214 888 C ATOM 2370 C PRO B 32 -11.117 27.442 12.919 1.00 37.34 C ANISOU 2370 C PRO B 32 4557 4427 5205 -9 -269 568 C ATOM 2371 O PRO B 32 -12.291 27.101 13.009 1.00 37.14 O ANISOU 2371 O PRO B 32 4550 4440 5121 32 -326 473 O ATOM 2372 CB PRO B 32 -10.197 29.476 11.734 1.00 40.34 C ANISOU 2372 CB PRO B 32 4769 4625 5933 41 -133 1063 C ATOM 2373 CG PRO B 32 -11.388 30.214 11.341 1.00 41.37 C ANISOU 2373 CG PRO B 32 4830 4692 6196 145 -131 1218 C ATOM 2374 CD PRO B 32 -12.023 29.430 10.251 1.00 41.56 C ANISOU 2374 CD PRO B 32 4870 5066 5854 248 -223 1333 C ATOM 2375 N PRO B 33 -10.251 27.337 13.945 1.00 37.30 N ANISOU 2375 N PRO B 33 4559 4343 5271 -127 -259 433 N ATOM 2376 CA PRO B 33 -10.673 26.667 15.176 1.00 36.57 C ANISOU 2376 CA PRO B 33 4522 4253 5121 -192 -303 174 C ATOM 2377 C PRO B 33 -11.491 27.511 16.152 1.00 37.94 C ANISOU 2377 C PRO B 33 4711 4231 5475 -247 -289 7 C ATOM 2378 O PRO B 33 -11.838 27.021 17.220 1.00 37.66 O ANISOU 2378 O PRO B 33 4724 4220 5364 -299 -305 -195 O ATOM 2379 CB PRO B 33 -9.342 26.282 15.829 1.00 36.29 C ANISOU 2379 CB PRO B 33 4451 4281 5058 -302 -311 163 C ATOM 2380 CG PRO B 33 -8.401 27.327 15.383 1.00 37.45 C ANISOU 2380 CG PRO B 33 4514 4328 5388 -358 -278 334 C ATOM 2381 CD PRO B 33 -8.822 27.703 13.990 1.00 38.03 C ANISOU 2381 CD PRO B 33 4583 4400 5467 -212 -219 545 C ATOM 2382 N HIS B 34 -11.785 28.762 15.820 1.00 40.55 N ANISOU 2382 N HIS B 34 4994 4356 6056 -226 -223 103 N ATOM 2383 CA HIS B 34 -12.501 29.614 16.762 1.00 42.49 C ANISOU 2383 CA HIS B 34 5264 4356 6525 -277 -137 -83 C ATOM 2384 C HIS B 34 -13.997 29.384 16.660 1.00 42.29 C ANISOU 2384 C HIS B 34 5230 4328 6512 -134 -118 -76 C ATOM 2385 O HIS B 34 -14.564 29.443 15.567 1.00 42.95 O ANISOU 2385 O HIS B 34 5228 4477 6613 0 -145 173 O ATOM 2386 CB HIS B 34 -12.173 31.085 16.555 1.00 45.36 C ANISOU 2386 CB HIS B 34 5562 4418 7253 -320 -12 8 C ATOM 2387 CG HIS B 34 -12.875 31.988 17.521 1.00 49.22 C ANISOU 2387 CG HIS B 34 6094 4595 8012 -379 143 -231 C ATOM 2388 ND1 HIS B 34 -12.656 31.934 18.882 1.00 51.28 N ANISOU 2388 ND1 HIS B 34 6469 4835 8181 -569 155 -609 N ATOM 2389 CD2 HIS B 34 -13.799 32.961 17.328 1.00 52.99 C ANISOU 2389 CD2 HIS B 34 6511 4774 8849 -267 325 -141 C ATOM 2390 CE1 HIS B 34 -13.410 32.838 19.485 1.00 54.32 C ANISOU 2390 CE1 HIS B 34 6896 4905 8840 -583 359 -799 C ATOM 2391 NE2 HIS B 34 -14.113 33.475 18.564 1.00 55.34 N ANISOU 2391 NE2 HIS B 34 6911 4830 9287 -389 481 -508 N ATOM 2392 N ILE B 35 -14.637 29.142 17.803 1.00 41.99 N ANISOU 2392 N ILE B 35 5259 4242 6453 -172 -73 -328 N ATOM 2393 CA ILE B 35 -16.012 28.644 17.801 1.00 41.45 C ANISOU 2393 CA ILE B 35 5160 4214 6377 -47 -66 -318 C ATOM 2394 C ILE B 35 -16.794 28.989 19.082 1.00 42.38 C ANISOU 2394 C ILE B 35 5333 4152 6618 -67 91 -560 C ATOM 2395 O ILE B 35 -16.250 28.914 20.172 1.00 42.44 O ANISOU 2395 O ILE B 35 5450 4173 6502 -206 124 -810 O ATOM 2396 CB ILE B 35 -16.000 27.112 17.511 1.00 39.11 C ANISOU 2396 CB ILE B 35 4877 4210 5772 -31 -207 -315 C ATOM 2397 CG1 ILE B 35 -17.298 26.659 16.828 1.00 39.32 C ANISOU 2397 CG1 ILE B 35 4809 4321 5809 83 -263 -199 C ATOM 2398 CG2 ILE B 35 -15.664 26.325 18.764 1.00 38.20 C ANISOU 2398 CG2 ILE B 35 4848 4173 5493 -123 -196 -536 C ATOM 2399 CD1 ILE B 35 -17.111 25.497 15.840 1.00 36.47 C ANISOU 2399 CD1 ILE B 35 4445 4219 5193 81 -400 -141 C ATOM 2400 N GLU B 36 -18.055 29.394 18.943 1.00 43.78 N ANISOU 2400 N GLU B 36 5420 4185 7029 68 199 -467 N ATOM 2401 CA GLU B 36 -18.914 29.611 20.108 1.00 45.53 C ANISOU 2401 CA GLU B 36 5691 4242 7367 82 398 -683 C ATOM 2402 C GLU B 36 -19.990 28.525 20.170 1.00 43.93 C ANISOU 2402 C GLU B 36 5415 4212 7064 181 341 -627 C ATOM 2403 O GLU B 36 -20.934 28.527 19.373 1.00 44.54 O ANISOU 2403 O GLU B 36 5322 4296 7304 312 303 -382 O ATOM 2404 CB GLU B 36 -19.553 31.012 20.106 1.00 49.31 C ANISOU 2404 CB GLU B 36 6102 4337 8298 170 657 -629 C ATOM 2405 CG GLU B 36 -18.625 32.187 20.528 1.00 54.23 C ANISOU 2405 CG GLU B 36 6831 4673 9101 22 817 -830 C ATOM 2406 CD GLU B 36 -18.216 33.139 19.370 1.00 59.03 C ANISOU 2406 CD GLU B 36 7302 5099 10026 80 831 -511 C ATOM 2407 OE1 GLU B 36 -18.244 32.745 18.176 1.00 59.98 O ANISOU 2407 OE1 GLU B 36 7285 5440 10064 192 640 -146 O ATOM 2408 OE2 GLU B 36 -17.856 34.300 19.660 1.00 62.23 O ANISOU 2408 OE2 GLU B 36 7738 5141 10766 2 1052 -630 O ATOM 2409 N ILE B 37 -19.831 27.589 21.106 1.00 42.16 N ANISOU 2409 N ILE B 37 5292 4145 6582 107 328 -823 N ATOM 2410 CA ILE B 37 -20.764 26.470 21.254 1.00 40.68 C ANISOU 2410 CA ILE B 37 5028 4097 6331 179 296 -777 C ATOM 2411 C ILE B 37 -21.601 26.605 22.522 1.00 41.79 C ANISOU 2411 C ILE B 37 5208 4126 6546 218 539 -937 C ATOM 2412 O ILE B 37 -21.062 26.681 23.626 1.00 42.01 O ANISOU 2412 O ILE B 37 5391 4185 6387 118 640 -1167 O ATOM 2413 CB ILE B 37 -20.050 25.103 21.300 1.00 38.44 C ANISOU 2413 CB ILE B 37 4790 4072 5744 103 141 -803 C ATOM 2414 CG1 ILE B 37 -19.118 24.927 20.114 1.00 37.72 C ANISOU 2414 CG1 ILE B 37 4689 4088 5553 66 -41 -681 C ATOM 2415 CG2 ILE B 37 -21.061 23.970 21.295 1.00 37.99 C ANISOU 2415 CG2 ILE B 37 4626 4100 5709 166 124 -742 C ATOM 2416 CD1 ILE B 37 -18.410 23.598 20.111 1.00 35.61 C ANISOU 2416 CD1 ILE B 37 4453 4014 5063 14 -128 -695 C ATOM 2417 N GLN B 38 -22.920 26.607 22.346 1.00 42.40 N ANISOU 2417 N GLN B 38 5126 4110 6873 356 628 -797 N ATOM 2418 CA GLN B 38 -23.849 26.660 23.455 1.00 43.78 C ANISOU 2418 CA GLN B 38 5307 4176 7151 427 898 -903 C ATOM 2419 C GLN B 38 -24.688 25.395 23.504 1.00 42.43 C ANISOU 2419 C GLN B 38 4996 4163 6962 479 837 -782 C ATOM 2420 O GLN B 38 -25.022 24.819 22.472 1.00 41.50 O ANISOU 2420 O GLN B 38 4713 4146 6908 491 621 -589 O ATOM 2421 CB GLN B 38 -24.768 27.857 23.294 1.00 46.93 C ANISOU 2421 CB GLN B 38 5591 4264 7976 567 1132 -803 C ATOM 2422 CG GLN B 38 -24.084 29.220 23.345 1.00 50.11 C ANISOU 2422 CG GLN B 38 6117 4405 8516 520 1285 -939 C ATOM 2423 CD GLN B 38 -25.100 30.349 23.304 1.00 55.98 C ANISOU 2423 CD GLN B 38 6725 4778 9768 693 1607 -817 C ATOM 2424 OE1 GLN B 38 -25.976 30.380 22.435 1.00 57.44 O ANISOU 2424 OE1 GLN B 38 6638 4948 10239 849 1547 -447 O ATOM 2425 NE2 GLN B 38 -25.000 31.277 24.254 1.00 60.09 N ANISOU 2425 NE2 GLN B 38 7419 5002 10409 658 1965 -1126 N ATOM 2426 N MET B 39 -25.025 24.956 24.708 1.00 42.66 N ANISOU 2426 N MET B 39 5089 4224 6894 492 1034 -902 N ATOM 2427 CA MET B 39 -26.017 23.899 24.857 1.00 42.32 C ANISOU 2427 CA MET B 39 4877 4254 6948 561 1054 -761 C ATOM 2428 C MET B 39 -27.292 24.519 25.407 1.00 44.50 C ANISOU 2428 C MET B 39 5044 4325 7539 712 1367 -712 C ATOM 2429 O MET B 39 -27.246 25.387 26.275 1.00 46.29 O ANISOU 2429 O MET B 39 5425 4411 7751 739 1653 -899 O ATOM 2430 CB MET B 39 -25.504 22.752 25.731 1.00 41.50 C ANISOU 2430 CB MET B 39 4868 4359 6540 495 1061 -830 C ATOM 2431 CG MET B 39 -24.284 22.042 25.128 1.00 40.40 C ANISOU 2431 CG MET B 39 4790 4393 6169 375 790 -825 C ATOM 2432 SD MET B 39 -24.066 20.298 25.563 1.00 42.02 S ANISOU 2432 SD MET B 39 4938 4779 6247 350 766 -725 S ATOM 2433 CE MET B 39 -25.398 19.522 24.639 1.00 40.56 C ANISOU 2433 CE MET B 39 4490 4487 6435 387 698 -577 C ATOM 2434 N LEU B 40 -28.429 24.096 24.873 1.00 44.63 N ANISOU 2434 N LEU B 40 4783 4318 7857 797 1325 -470 N ATOM 2435 CA LEU B 40 -29.684 24.777 25.150 1.00 47.06 C ANISOU 2435 CA LEU B 40 4911 4408 8560 966 1611 -335 C ATOM 2436 C LEU B 40 -30.744 23.847 25.709 1.00 48.10 C ANISOU 2436 C LEU B 40 4856 4581 8840 1032 1742 -206 C ATOM 2437 O LEU B 40 -30.846 22.691 25.310 1.00 47.06 O ANISOU 2437 O LEU B 40 4598 4613 8670 946 1509 -114 O ATOM 2438 CB LEU B 40 -30.218 25.447 23.883 1.00 47.81 C ANISOU 2438 CB LEU B 40 4748 4421 8995 1031 1453 -55 C ATOM 2439 CG LEU B 40 -29.479 26.643 23.276 1.00 47.44 C ANISOU 2439 CG LEU B 40 4801 4249 8976 1031 1420 -69 C ATOM 2440 CD1 LEU B 40 -30.106 26.972 21.961 1.00 47.86 C ANISOU 2440 CD1 LEU B 40 4532 4338 9314 1096 1206 313 C ATOM 2441 CD2 LEU B 40 -29.497 27.868 24.179 1.00 50.08 C ANISOU 2441 CD2 LEU B 40 5287 4251 9489 1127 1858 -243 C ATOM 2442 N LYS B 41 -31.527 24.363 26.646 1.00 50.62 N ANISOU 2442 N LYS B 41 5157 4723 9353 1181 2153 -213 N ATOM 2443 CA LYS B 41 -32.716 23.689 27.116 1.00 51.96 C ANISOU 2443 CA LYS B 41 5086 4881 9776 1284 2336 -20 C ATOM 2444 C LYS B 41 -33.829 24.674 26.871 1.00 55.17 C ANISOU 2444 C LYS B 41 5238 5031 10694 1471 2568 202 C ATOM 2445 O LYS B 41 -33.899 25.719 27.524 1.00 57.41 O ANISOU 2445 O LYS B 41 5664 5083 11068 1590 2962 69 O ATOM 2446 CB LYS B 41 -32.602 23.371 28.603 1.00 52.93 C ANISOU 2446 CB LYS B 41 5427 5056 9629 1317 2690 -203 C ATOM 2447 CG LYS B 41 -33.710 22.509 29.150 1.00 54.21 C ANISOU 2447 CG LYS B 41 5346 5231 10021 1417 2891 19 C ATOM 2448 CD LYS B 41 -33.449 22.192 30.605 1.00 55.21 C ANISOU 2448 CD LYS B 41 5712 5482 9783 1446 3228 -138 C ATOM 2449 CE LYS B 41 -34.680 21.610 31.274 1.00 57.64 C ANISOU 2449 CE LYS B 41 5775 5747 10379 1597 3559 108 C ATOM 2450 NZ LYS B 41 -34.458 21.412 32.729 1.00 59.48 N ANISOU 2450 NZ LYS B 41 6251 6142 10205 1644 3931 -21 N ATOM 2451 N ASN B 42 -34.672 24.351 25.897 1.00 55.76 N ANISOU 2451 N ASN B 42 4924 5151 11113 1481 2324 542 N ATOM 2452 CA ASN B 42 -35.821 25.186 25.533 1.00 59.25 C ANISOU 2452 CA ASN B 42 5013 5394 12104 1669 2494 880 C ATOM 2453 C ASN B 42 -35.407 26.568 25.070 1.00 60.19 C ANISOU 2453 C ASN B 42 5213 5316 12339 1750 2569 884 C ATOM 2454 O ASN B 42 -36.141 27.540 25.275 1.00 63.94 O ANISOU 2454 O ASN B 42 5532 5501 13262 1961 2943 1060 O ATOM 2455 CB ASN B 42 -36.815 25.298 26.691 1.00 62.32 C ANISOU 2455 CB ASN B 42 5313 5580 12784 1868 3030 939 C ATOM 2456 CG ASN B 42 -37.278 23.958 27.182 1.00 61.49 C ANISOU 2456 CG ASN B 42 5091 5642 12630 1806 3004 993 C ATOM 2457 OD1 ASN B 42 -37.731 23.124 26.400 1.00 61.07 O ANISOU 2457 OD1 ASN B 42 4727 5750 12725 1692 2642 1215 O ATOM 2458 ND2 ASN B 42 -37.166 23.736 28.486 1.00 61.96 N ANISOU 2458 ND2 ASN B 42 5394 5673 12475 1866 3395 788 N ATOM 2459 N GLY B 43 -34.228 26.640 24.453 1.00 57.24 N ANISOU 2459 N GLY B 43 5068 5073 11607 1591 2249 712 N ATOM 2460 CA GLY B 43 -33.690 27.886 23.926 1.00 58.08 C ANISOU 2460 CA GLY B 43 5250 5000 11816 1640 2285 730 C ATOM 2461 C GLY B 43 -33.021 28.730 24.988 1.00 59.06 C ANISOU 2461 C GLY B 43 5757 4848 11834 1662 2706 332 C ATOM 2462 O GLY B 43 -32.688 29.887 24.746 1.00 60.55 O ANISOU 2462 O GLY B 43 6005 4778 12222 1717 2861 319 O ATOM 2463 N LYS B 44 -32.841 28.153 26.172 1.00 58.87 N ANISOU 2463 N LYS B 44 5981 4888 11500 1606 2899 13 N ATOM 2464 CA LYS B 44 -32.113 28.807 27.254 1.00 60.41 C ANISOU 2464 CA LYS B 44 6574 4929 11451 1554 3241 -437 C ATOM 2465 C LYS B 44 -30.776 28.110 27.480 1.00 57.27 C ANISOU 2465 C LYS B 44 6481 4846 10434 1312 2928 -733 C ATOM 2466 O LYS B 44 -30.708 26.880 27.552 1.00 54.87 O ANISOU 2466 O LYS B 44 6141 4839 9868 1241 2694 -671 O ATOM 2467 CB LYS B 44 -32.947 28.829 28.538 1.00 63.69 C ANISOU 2467 CB LYS B 44 7040 5212 11949 1687 3765 -561 C ATOM 2468 CG LYS B 44 -33.930 30.009 28.630 1.00 68.67 C ANISOU 2468 CG LYS B 44 7507 5389 13197 1929 4274 -431 C ATOM 2469 CD LYS B 44 -35.236 29.646 29.361 1.00 70.94 C ANISOU 2469 CD LYS B 44 7591 5608 13754 2131 4672 -255 C ATOM 2470 CE LYS B 44 -35.118 29.767 30.872 1.00 73.01 C ANISOU 2470 CE LYS B 44 8225 5830 13687 2120 5174 -710 C ATOM 2471 NZ LYS B 44 -36.435 29.537 31.526 1.00 76.73 N ANISOU 2471 NZ LYS B 44 8477 6192 14486 2354 5630 -496 N ATOM 2472 N LYS B 45 -29.718 28.915 27.565 1.00 57.83 N ANISOU 2472 N LYS B 45 6818 4826 10329 1186 2940 -1025 N ATOM 2473 CA LYS B 45 -28.351 28.440 27.769 1.00 55.64 C ANISOU 2473 CA LYS B 45 6802 4831 9507 954 2656 -1279 C ATOM 2474 C LYS B 45 -28.197 27.686 29.093 1.00 56.05 C ANISOU 2474 C LYS B 45 7049 5136 9112 881 2787 -1508 C ATOM 2475 O LYS B 45 -28.519 28.195 30.163 1.00 59.20 O ANISOU 2475 O LYS B 45 7608 5426 9460 908 3194 -1760 O ATOM 2476 CB LYS B 45 -27.387 29.630 27.697 1.00 57.07 C ANISOU 2476 CB LYS B 45 7191 4810 9683 831 2711 -1547 C ATOM 2477 CG LYS B 45 -25.893 29.305 27.708 1.00 55.50 C ANISOU 2477 CG LYS B 45 7199 4886 9004 584 2381 -1747 C ATOM 2478 CD LYS B 45 -25.101 30.605 27.839 1.00 59.35 C ANISOU 2478 CD LYS B 45 7878 5112 9560 446 2524 -2054 C ATOM 2479 CE LYS B 45 -23.600 30.382 28.011 1.00 58.98 C ANISOU 2479 CE LYS B 45 8018 5341 9052 176 2226 -2269 C ATOM 2480 NZ LYS B 45 -22.900 31.702 28.231 1.00 62.53 N ANISOU 2480 NZ LYS B 45 8640 5501 9617 5 2397 -2612 N ATOM 2481 N ILE B 46 -27.719 26.454 28.989 1.00 53.45 N ANISOU 2481 N ILE B 46 6692 5147 8469 796 2464 -1398 N ATOM 2482 CA ILE B 46 -27.454 25.599 30.141 1.00 54.21 C ANISOU 2482 CA ILE B 46 6924 5547 8127 732 2532 -1505 C ATOM 2483 C ILE B 46 -26.159 26.079 30.811 1.00 55.63 C ANISOU 2483 C ILE B 46 7408 5889 7839 517 2492 -1857 C ATOM 2484 O ILE B 46 -25.193 26.408 30.107 1.00 54.10 O ANISOU 2484 O ILE B 46 7257 5689 7608 390 2219 -1904 O ATOM 2485 CB ILE B 46 -27.338 24.109 29.700 1.00 50.89 C ANISOU 2485 CB ILE B 46 6332 5379 7624 721 2218 -1222 C ATOM 2486 CG1 ILE B 46 -28.582 23.707 28.892 1.00 49.90 C ANISOU 2486 CG1 ILE B 46 5884 5097 7977 868 2196 -913 C ATOM 2487 CG2 ILE B 46 -27.075 23.180 30.907 1.00 51.31 C ANISOU 2487 CG2 ILE B 46 6477 5749 7268 686 2314 -1234 C ATOM 2488 CD1 ILE B 46 -28.550 22.313 28.297 1.00 46.51 C ANISOU 2488 CD1 ILE B 46 5279 4836 7557 824 1906 -694 C ATOM 2489 N PRO B 47 -26.130 26.125 32.163 1.00 59.09 N ANISOU 2489 N PRO B 47 8045 6503 7905 462 2758 -2099 N ATOM 2490 CA PRO B 47 -24.954 26.673 32.850 1.00 61.10 C ANISOU 2490 CA PRO B 47 8574 6948 7692 211 2708 -2470 C ATOM 2491 C PRO B 47 -23.757 25.707 32.977 1.00 59.20 C ANISOU 2491 C PRO B 47 8337 7167 6990 51 2320 -2352 C ATOM 2492 O PRO B 47 -22.639 26.065 32.599 1.00 58.39 O ANISOU 2492 O PRO B 47 8298 7118 6769 -131 2058 -2461 O ATOM 2493 CB PRO B 47 -25.501 27.079 34.236 1.00 66.12 C ANISOU 2493 CB PRO B 47 9413 7638 8070 209 3162 -2776 C ATOM 2494 CG PRO B 47 -26.986 26.736 34.233 1.00 66.34 C ANISOU 2494 CG PRO B 47 9247 7464 8494 499 3475 -2512 C ATOM 2495 CD PRO B 47 -27.198 25.767 33.117 1.00 61.71 C ANISOU 2495 CD PRO B 47 8352 6874 8220 614 3133 -2052 C ATOM 2496 N LYS B 48 -23.979 24.503 33.496 1.00 58.99 N ANISOU 2496 N LYS B 48 8213 7446 6754 131 2308 -2093 N ATOM 2497 CA LYS B 48 -22.871 23.577 33.749 1.00 58.29 C ANISOU 2497 CA LYS B 48 8099 7791 6259 8 2006 -1927 C ATOM 2498 C LYS B 48 -22.497 22.751 32.501 1.00 54.37 C ANISOU 2498 C LYS B 48 7390 7218 6050 64 1684 -1601 C ATOM 2499 O LYS B 48 -22.774 21.540 32.429 1.00 53.37 O ANISOU 2499 O LYS B 48 7090 7189 6001 178 1651 -1278 O ATOM 2500 CB LYS B 48 -23.223 22.638 34.904 1.00 20.00 C ATOM 2501 N VAL B 49 -21.876 23.397 31.514 1.00 52.56 N ANISOU 2501 N VAL B 49 7176 6800 5993 -19 1477 -1692 N ATOM 2502 CA VAL B 49 -21.517 22.684 30.285 1.00 48.74 C ANISOU 2502 CA VAL B 49 6525 6252 5743 24 1208 -1432 C ATOM 2503 C VAL B 49 -20.017 22.501 30.192 1.00 48.07 C ANISOU 2503 C VAL B 49 6467 6411 5387 -138 938 -1404 C ATOM 2504 O VAL B 49 -19.264 23.474 30.234 1.00 48.97 O ANISOU 2504 O VAL B 49 6703 6521 5383 -301 865 -1630 O ATOM 2505 CB VAL B 49 -22.069 23.375 29.016 1.00 47.37 C ANISOU 2505 CB VAL B 49 6284 5704 6012 100 1177 -1438 C ATOM 2506 CG1 VAL B 49 -21.475 22.767 27.751 1.00 43.56 C ANISOU 2506 CG1 VAL B 49 5683 5220 5646 93 889 -1243 C ATOM 2507 CG2 VAL B 49 -23.583 23.271 28.985 1.00 47.90 C ANISOU 2507 CG2 VAL B 49 6226 5570 6404 280 1398 -1341 C ATOM 2508 N GLU B 50 -19.597 21.243 30.061 1.00 46.84 N ANISOU 2508 N GLU B 50 6173 6438 5187 -94 816 -1111 N ATOM 2509 CA GLU B 50 -18.178 20.892 29.966 1.00 46.46 C ANISOU 2509 CA GLU B 50 6089 6627 4935 -211 587 -991 C ATOM 2510 C GLU B 50 -17.687 20.707 28.529 1.00 43.29 C ANISOU 2510 C GLU B 50 5608 6029 4811 -186 415 -890 C ATOM 2511 O GLU B 50 -18.436 20.272 27.648 1.00 41.25 O ANISOU 2511 O GLU B 50 5273 5544 4856 -65 444 -816 O ATOM 2512 CB GLU B 50 -17.882 19.645 30.788 1.00 47.55 C ANISOU 2512 CB GLU B 50 6105 7095 4865 -165 607 -686 C ATOM 2513 CG GLU B 50 -18.045 19.829 32.276 1.00 52.64 C ANISOU 2513 CG GLU B 50 6833 8076 5092 -226 736 -751 C ATOM 2514 CD GLU B 50 -17.568 18.617 33.057 1.00 57.26 C ANISOU 2514 CD GLU B 50 7255 9050 5450 -180 727 -352 C ATOM 2515 OE1 GLU B 50 -16.400 18.200 32.846 1.00 57.66 O ANISOU 2515 OE1 GLU B 50 7188 9282 5439 -239 528 -134 O ATOM 2516 OE2 GLU B 50 -18.356 18.085 33.882 1.00 59.38 O ANISOU 2516 OE2 GLU B 50 7489 9442 5632 -69 942 -213 O ATOM 2517 N MET B 51 -16.414 21.035 28.322 1.00 43.29 N ANISOU 2517 N MET B 51 5618 6148 4682 -319 236 -890 N ATOM 2518 CA MET B 51 -15.785 21.023 26.999 1.00 41.36 C ANISOU 2518 CA MET B 51 5322 5749 4644 -309 98 -811 C ATOM 2519 C MET B 51 -14.490 20.225 27.004 1.00 40.69 C ANISOU 2519 C MET B 51 5119 5891 4450 -344 -20 -562 C ATOM 2520 O MET B 51 -13.598 20.475 27.816 1.00 42.37 O ANISOU 2520 O MET B 51 5317 6381 4401 -485 -115 -540 O ATOM 2521 CB MET B 51 -15.466 22.453 26.573 1.00 42.06 C ANISOU 2521 CB MET B 51 5513 5682 4786 -425 38 -1032 C ATOM 2522 CG MET B 51 -15.929 22.822 25.186 1.00 42.41 C ANISOU 2522 CG MET B 51 5544 5434 5137 -331 28 -1021 C ATOM 2523 SD MET B 51 -17.723 23.004 25.085 1.00 46.35 S ANISOU 2523 SD MET B 51 6042 5700 5870 -181 201 -1088 S ATOM 2524 CE MET B 51 -17.799 24.579 24.228 1.00 47.28 C ANISOU 2524 CE MET B 51 6200 5537 6229 -200 206 -1185 C ATOM 2525 N SER B 52 -14.389 19.265 26.092 1.00 38.66 N ANISOU 2525 N SER B 52 4765 5520 4403 -228 -5 -377 N ATOM 2526 CA SER B 52 -13.153 18.510 25.918 1.00 38.27 C ANISOU 2526 CA SER B 52 4585 5609 4347 -225 -59 -116 C ATOM 2527 C SER B 52 -12.175 19.475 25.321 1.00 37.58 C ANISOU 2527 C SER B 52 4528 5511 4239 -342 -203 -187 C ATOM 2528 O SER B 52 -12.581 20.522 24.819 1.00 37.27 O ANISOU 2528 O SER B 52 4606 5295 4260 -387 -230 -410 O ATOM 2529 CB SER B 52 -13.352 17.353 24.944 1.00 37.13 C ANISOU 2529 CB SER B 52 4369 5262 4477 -83 53 9 C ATOM 2530 OG SER B 52 -13.433 17.825 23.606 1.00 36.08 O ANISOU 2530 OG SER B 52 4316 4919 4474 -84 9 -140 O ATOM 2531 N ASP B 53 -10.896 19.139 25.358 1.00 37.74 N ANISOU 2531 N ASP B 53 4415 5704 4219 -381 -275 42 N ATOM 2532 CA ASP B 53 -9.925 19.953 24.663 1.00 37.38 C ANISOU 2532 CA ASP B 53 4364 5621 4219 -480 -388 22 C ATOM 2533 C ASP B 53 -10.161 19.854 23.165 1.00 35.68 C ANISOU 2533 C ASP B 53 4203 5121 4233 -361 -309 -8 C ATOM 2534 O ASP B 53 -10.584 18.816 22.649 1.00 35.29 O ANISOU 2534 O ASP B 53 4137 4963 4308 -221 -180 60 O ATOM 2535 CB ASP B 53 -8.526 19.505 25.000 1.00 38.71 C ANISOU 2535 CB ASP B 53 4327 6045 4336 -530 -467 334 C ATOM 2536 CG ASP B 53 -8.300 19.422 26.470 1.00 40.95 C ANISOU 2536 CG ASP B 53 4523 6707 4331 -650 -568 424 C ATOM 2537 OD1 ASP B 53 -8.732 20.349 27.184 1.00 41.35 O ANISOU 2537 OD1 ASP B 53 4707 6838 4165 -813 -645 135 O ATOM 2538 OD2 ASP B 53 -7.697 18.425 26.912 1.00 43.31 O ANISOU 2538 OD2 ASP B 53 4613 7227 4616 -579 -550 794 O ATOM 2539 N MET B 54 -9.920 20.954 22.475 1.00 35.45 N ANISOU 2539 N MET B 54 4238 4976 4255 -432 -376 -122 N ATOM 2540 CA MET B 54 -10.029 20.995 21.040 1.00 34.43 C ANISOU 2540 CA MET B 54 4153 4658 4269 -337 -321 -118 C ATOM 2541 C MET B 54 -8.921 20.134 20.469 1.00 34.60 C ANISOU 2541 C MET B 54 4063 4731 4354 -271 -252 119 C ATOM 2542 O MET B 54 -7.807 20.115 21.004 1.00 36.10 O ANISOU 2542 O MET B 54 4115 5078 4524 -338 -303 302 O ATOM 2543 CB MET B 54 -9.885 22.440 20.585 1.00 35.06 C ANISOU 2543 CB MET B 54 4288 4629 4406 -427 -391 -215 C ATOM 2544 CG MET B 54 -9.716 22.657 19.102 1.00 36.04 C ANISOU 2544 CG MET B 54 4427 4637 4628 -345 -351 -132 C ATOM 2545 SD MET B 54 -10.999 23.783 18.561 1.00 39.66 S ANISOU 2545 SD MET B 54 4981 4909 5180 -315 -356 -271 S ATOM 2546 CE MET B 54 -12.296 22.572 18.412 1.00 38.44 C ANISOU 2546 CE MET B 54 4861 4773 4970 -197 -313 -342 C ATOM 2547 N SER B 55 -9.236 19.412 19.401 1.00 33.56 N ANISOU 2547 N SER B 55 3978 4475 4300 -149 -125 112 N ATOM 2548 CA SER B 55 -8.270 18.576 18.712 1.00 34.47 C ANISOU 2548 CA SER B 55 4016 4577 4504 -64 21 293 C ATOM 2549 C SER B 55 -8.527 18.627 17.203 1.00 34.37 C ANISOU 2549 C SER B 55 4125 4450 4485 -7 103 185 C ATOM 2550 O SER B 55 -9.466 19.287 16.764 1.00 34.14 O ANISOU 2550 O SER B 55 4202 4385 4386 -33 11 22 O ATOM 2551 CB SER B 55 -8.380 17.146 19.228 1.00 35.12 C ANISOU 2551 CB SER B 55 4019 4644 4682 26 178 391 C ATOM 2552 OG SER B 55 -7.359 16.325 18.694 1.00 36.91 O ANISOU 2552 OG SER B 55 4147 4822 5056 122 377 592 O ATOM 2553 N PHE B 56 -7.699 17.954 16.405 1.00 35.24 N ANISOU 2553 N PHE B 56 4210 4524 4656 72 288 294 N ATOM 2554 CA PHE B 56 -7.974 17.839 14.970 1.00 35.53 C ANISOU 2554 CA PHE B 56 4383 4506 4609 113 391 158 C ATOM 2555 C PHE B 56 -7.613 16.478 14.388 1.00 37.24 C ANISOU 2555 C PHE B 56 4621 4619 4911 201 682 131 C ATOM 2556 O PHE B 56 -6.758 15.772 14.924 1.00 38.19 O ANISOU 2556 O PHE B 56 4602 4691 5217 270 844 331 O ATOM 2557 CB PHE B 56 -7.310 18.968 14.168 1.00 35.99 C ANISOU 2557 CB PHE B 56 4449 4627 4598 101 343 273 C ATOM 2558 CG PHE B 56 -5.834 19.088 14.379 1.00 35.68 C ANISOU 2558 CG PHE B 56 4252 4616 4690 120 423 550 C ATOM 2559 CD1 PHE B 56 -4.959 18.193 13.790 1.00 36.15 C ANISOU 2559 CD1 PHE B 56 4272 4632 4831 227 694 669 C ATOM 2560 CD2 PHE B 56 -5.321 20.116 15.153 1.00 34.93 C ANISOU 2560 CD2 PHE B 56 4034 4578 4658 15 242 681 C ATOM 2561 CE1 PHE B 56 -3.598 18.306 13.988 1.00 37.28 C ANISOU 2561 CE1 PHE B 56 4219 4808 5137 254 772 978 C ATOM 2562 CE2 PHE B 56 -3.959 20.237 15.351 1.00 36.03 C ANISOU 2562 CE2 PHE B 56 3985 4772 4934 0 281 953 C ATOM 2563 CZ PHE B 56 -3.095 19.332 14.765 1.00 37.08 C ANISOU 2563 CZ PHE B 56 4044 4879 5167 132 540 1134 C ATOM 2564 N SER B 57 -8.267 16.138 13.277 1.00 38.34 N ANISOU 2564 N SER B 57 4921 4730 4917 190 758 -113 N ATOM 2565 CA SER B 57 -8.112 14.845 12.599 1.00 40.57 C ANISOU 2565 CA SER B 57 5276 4873 5264 234 1069 -264 C ATOM 2566 C SER B 57 -6.949 14.829 11.612 1.00 42.35 C ANISOU 2566 C SER B 57 5535 5107 5449 313 1314 -168 C ATOM 2567 O SER B 57 -6.194 15.802 11.502 1.00 42.29 O ANISOU 2567 O SER B 57 5460 5216 5394 338 1231 67 O ATOM 2568 CB SER B 57 -9.410 14.496 11.864 1.00 41.51 C ANISOU 2568 CB SER B 57 5558 5001 5213 128 1011 -632 C ATOM 2569 OG SER B 57 -10.539 14.595 12.732 1.00 41.01 O ANISOU 2569 OG SER B 57 5443 4931 5208 65 795 -692 O ATOM 2570 N LYS B 58 -6.819 13.720 10.886 1.00 44.52 N ANISOU 2570 N LYS B 58 5914 5236 5764 344 1646 -365 N ATOM 2571 CA LYS B 58 -5.794 13.558 9.854 1.00 46.42 C ANISOU 2571 CA LYS B 58 6219 5466 5953 429 1964 -327 C ATOM 2572 C LYS B 58 -5.905 14.642 8.777 1.00 46.08 C ANISOU 2572 C LYS B 58 6306 5687 5517 380 1805 -360 C ATOM 2573 O LYS B 58 -4.900 15.208 8.358 1.00 46.66 O ANISOU 2573 O LYS B 58 6327 5833 5570 466 1910 -109 O ATOM 2574 CB LYS B 58 -5.885 12.152 9.240 1.00 49.89 C ANISOU 2574 CB LYS B 58 6799 5673 6485 435 2374 -653 C ATOM 2575 CG LYS B 58 -4.725 11.772 8.306 1.00 54.51 C ANISOU 2575 CG LYS B 58 7444 6176 7091 556 2825 -617 C ATOM 2576 CD LYS B 58 -4.862 10.346 7.770 1.00 59.51 C ANISOU 2576 CD LYS B 58 8234 6513 7863 543 3286 -1008 C ATOM 2577 CE LYS B 58 -3.666 9.960 6.889 1.00 63.56 C ANISOU 2577 CE LYS B 58 8808 6911 8430 689 3809 -970 C ATOM 2578 NZ LYS B 58 -3.533 8.475 6.707 1.00 66.64 N ANISOU 2578 NZ LYS B 58 9274 6879 9168 729 4369 -1254 N ATOM 2579 N ASP B 59 -7.127 14.944 8.355 1.00 45.31 N ANISOU 2579 N ASP B 59 6338 5745 5133 248 1553 -615 N ATOM 2580 CA ASP B 59 -7.365 15.981 7.348 1.00 45.93 C ANISOU 2580 CA ASP B 59 6503 6114 4836 209 1381 -582 C ATOM 2581 C ASP B 59 -7.170 17.426 7.826 1.00 43.36 C ANISOU 2581 C ASP B 59 6023 5882 4568 242 1109 -223 C ATOM 2582 O ASP B 59 -7.372 18.352 7.048 1.00 44.27 O ANISOU 2582 O ASP B 59 6171 6211 4439 232 981 -120 O ATOM 2583 CB ASP B 59 -8.742 15.805 6.674 1.00 47.50 C ANISOU 2583 CB ASP B 59 6846 6495 4708 50 1191 -925 C ATOM 2584 CG ASP B 59 -9.934 16.115 7.605 1.00 46.25 C ANISOU 2584 CG ASP B 59 6583 6315 4676 -28 846 -942 C ATOM 2585 OD1 ASP B 59 -9.765 16.250 8.848 1.00 45.84 O ANISOU 2585 OD1 ASP B 59 6389 6084 4946 28 792 -771 O ATOM 2586 OD2 ASP B 59 -11.064 16.203 7.073 1.00 47.11 O ANISOU 2586 OD2 ASP B 59 6744 6615 4542 -154 634 -1124 O ATOM 2587 N TRP B 60 -6.778 17.609 9.090 1.00 40.70 N ANISOU 2587 N TRP B 60 5515 5393 4555 270 1035 -35 N ATOM 2588 CA TRP B 60 -6.443 18.929 9.676 1.00 38.74 C ANISOU 2588 CA TRP B 60 5120 5177 4421 265 821 250 C ATOM 2589 C TRP B 60 -7.640 19.749 10.161 1.00 37.31 C ANISOU 2589 C TRP B 60 4933 5034 4208 182 506 185 C ATOM 2590 O TRP B 60 -7.480 20.884 10.646 1.00 36.36 O ANISOU 2590 O TRP B 60 4713 4896 4207 159 357 360 O ATOM 2591 CB TRP B 60 -5.597 19.782 8.726 1.00 39.91 C ANISOU 2591 CB TRP B 60 5251 5435 4479 322 909 494 C ATOM 2592 CG TRP B 60 -4.298 19.167 8.369 1.00 40.90 C ANISOU 2592 CG TRP B 60 5335 5504 4701 422 1241 631 C ATOM 2593 CD1 TRP B 60 -3.983 18.534 7.203 1.00 42.82 C ANISOU 2593 CD1 TRP B 60 5721 5808 4741 492 1545 537 C ATOM 2594 CD2 TRP B 60 -3.126 19.114 9.184 1.00 40.15 C ANISOU 2594 CD2 TRP B 60 5027 5293 4937 463 1326 897 C ATOM 2595 NE1 TRP B 60 -2.684 18.096 7.237 1.00 43.78 N ANISOU 2595 NE1 TRP B 60 5729 5812 5093 604 1855 743 N ATOM 2596 CE2 TRP B 60 -2.134 18.435 8.443 1.00 41.78 C ANISOU 2596 CE2 TRP B 60 5233 5463 5180 587 1707 996 C ATOM 2597 CE3 TRP B 60 -2.816 19.572 10.471 1.00 38.22 C ANISOU 2597 CE3 TRP B 60 4581 5000 4941 392 1116 1061 C ATOM 2598 CZ2 TRP B 60 -0.857 18.208 8.942 1.00 41.77 C ANISOU 2598 CZ2 TRP B 60 4996 5369 5505 663 1876 1310 C ATOM 2599 CZ3 TRP B 60 -1.545 19.348 10.962 1.00 38.78 C ANISOU 2599 CZ3 TRP B 60 4426 5030 5277 432 1239 1351 C ATOM 2600 CH2 TRP B 60 -0.581 18.671 10.198 1.00 40.40 C ANISOU 2600 CH2 TRP B 60 4595 5191 5564 577 1612 1503 C ATOM 2601 N SER B 61 -8.835 19.181 10.020 1.00 37.25 N ANISOU 2601 N SER B 61 5020 5058 4076 130 430 -72 N ATOM 2602 CA SER B 61 -10.055 19.844 10.444 1.00 35.98 C ANISOU 2602 CA SER B 61 4830 4922 3917 72 173 -118 C ATOM 2603 C SER B 61 -10.240 19.630 11.936 1.00 33.93 C ANISOU 2603 C SER B 61 4489 4506 3895 51 119 -151 C ATOM 2604 O SER B 61 -9.840 18.606 12.473 1.00 33.77 O ANISOU 2604 O SER B 61 4452 4394 3985 67 259 -199 O ATOM 2605 CB SER B 61 -11.232 19.266 9.688 1.00 37.27 C ANISOU 2605 CB SER B 61 5085 5212 3863 7 104 -355 C ATOM 2606 OG SER B 61 -11.309 17.873 9.930 1.00 38.90 O ANISOU 2606 OG SER B 61 5347 5300 4133 -27 258 -601 O ATOM 2607 N PHE B 62 -10.865 20.593 12.599 1.00 33.05 N ANISOU 2607 N PHE B 62 4323 4368 3868 22 -55 -109 N ATOM 2608 CA PHE B 62 -10.982 20.582 14.046 1.00 31.47 C ANISOU 2608 CA PHE B 62 4060 4068 3831 -8 -99 -135 C ATOM 2609 C PHE B 62 -12.225 19.861 14.498 1.00 31.09 C ANISOU 2609 C PHE B 62 4027 3987 3799 -24 -133 -315 C ATOM 2610 O PHE B 62 -13.171 19.723 13.730 1.00 31.84 O ANISOU 2610 O PHE B 62 4157 4135 3807 -37 -190 -415 O ATOM 2611 CB PHE B 62 -10.963 22.012 14.575 1.00 31.39 C ANISOU 2611 CB PHE B 62 4000 4008 3918 -46 -210 -47 C ATOM 2612 CG PHE B 62 -9.654 22.715 14.345 1.00 32.18 C ANISOU 2612 CG PHE B 62 4046 4107 4075 -63 -175 137 C ATOM 2613 CD1 PHE B 62 -9.483 23.551 13.246 1.00 32.28 C ANISOU 2613 CD1 PHE B 62 4057 4139 4068 -27 -166 285 C ATOM 2614 CD2 PHE B 62 -8.577 22.515 15.216 1.00 32.45 C ANISOU 2614 CD2 PHE B 62 3997 4146 4188 -117 -153 207 C ATOM 2615 CE1 PHE B 62 -8.268 24.188 13.027 1.00 33.55 C ANISOU 2615 CE1 PHE B 62 4142 4278 4327 -44 -111 481 C ATOM 2616 CE2 PHE B 62 -7.358 23.147 15.004 1.00 32.69 C ANISOU 2616 CE2 PHE B 62 3936 4178 4307 -154 -131 394 C ATOM 2617 CZ PHE B 62 -7.204 23.987 13.911 1.00 33.94 C ANISOU 2617 CZ PHE B 62 4102 4309 4485 -117 -98 522 C ATOM 2618 N TYR B 63 -12.191 19.364 15.734 1.00 30.61 N ANISOU 2618 N TYR B 63 3918 3869 3843 -31 -99 -329 N ATOM 2619 CA TYR B 63 -13.334 18.717 16.362 1.00 30.77 C ANISOU 2619 CA TYR B 63 3925 3841 3927 -37 -102 -454 C ATOM 2620 C TYR B 63 -13.318 18.915 17.873 1.00 30.44 C ANISOU 2620 C TYR B 63 3828 3796 3943 -48 -112 -407 C ATOM 2621 O TYR B 63 -12.267 18.894 18.482 1.00 31.00 O ANISOU 2621 O TYR B 63 3851 3923 4003 -58 -86 -283 O ATOM 2622 CB TYR B 63 -13.382 17.225 16.016 1.00 31.59 C ANISOU 2622 CB TYR B 63 4037 3886 4080 -25 49 -543 C ATOM 2623 CG TYR B 63 -12.252 16.378 16.579 1.00 32.35 C ANISOU 2623 CG TYR B 63 4071 3938 4282 27 228 -403 C ATOM 2624 CD1 TYR B 63 -12.260 15.957 17.918 1.00 32.10 C ANISOU 2624 CD1 TYR B 63 3940 3902 4355 51 265 -288 C ATOM 2625 CD2 TYR B 63 -11.199 15.959 15.763 1.00 33.03 C ANISOU 2625 CD2 TYR B 63 4179 4004 4368 66 383 -349 C ATOM 2626 CE1 TYR B 63 -11.238 15.178 18.431 1.00 32.43 C ANISOU 2626 CE1 TYR B 63 3873 3940 4509 114 420 -75 C ATOM 2627 CE2 TYR B 63 -10.178 15.168 16.268 1.00 33.86 C ANISOU 2627 CE2 TYR B 63 4179 4055 4631 138 572 -158 C ATOM 2628 CZ TYR B 63 -10.202 14.782 17.602 1.00 33.72 C ANISOU 2628 CZ TYR B 63 4031 4052 4728 163 576 0 C ATOM 2629 OH TYR B 63 -9.174 14.010 18.101 1.00 35.69 O ANISOU 2629 OH TYR B 63 4127 4287 5148 249 754 273 O ATOM 2630 N ILE B 64 -14.488 19.109 18.472 1.00 30.57 N ANISOU 2630 N ILE B 64 3837 3776 4001 -52 -149 -495 N ATOM 2631 CA ILE B 64 -14.598 19.294 19.921 1.00 30.71 C ANISOU 2631 CA ILE B 64 3829 3826 4014 -67 -130 -483 C ATOM 2632 C ILE B 64 -15.881 18.636 20.435 1.00 30.92 C ANISOU 2632 C ILE B 64 3819 3799 4129 -30 -67 -546 C ATOM 2633 O ILE B 64 -16.886 18.601 19.736 1.00 30.91 O ANISOU 2633 O ILE B 64 3807 3728 4211 -20 -98 -622 O ATOM 2634 CB ILE B 64 -14.511 20.808 20.317 1.00 31.08 C ANISOU 2634 CB ILE B 64 3920 3863 4026 -125 -203 -533 C ATOM 2635 CG1 ILE B 64 -14.448 21.007 21.841 1.00 31.71 C ANISOU 2635 CG1 ILE B 64 4005 4029 4015 -182 -175 -577 C ATOM 2636 CG2 ILE B 64 -15.644 21.611 19.696 1.00 31.26 C ANISOU 2636 CG2 ILE B 64 3958 3767 4154 -91 -231 -599 C ATOM 2637 CD1 ILE B 64 -13.813 22.321 22.263 1.00 30.68 C ANISOU 2637 CD1 ILE B 64 3924 3902 3831 -303 -230 -660 C ATOM 2638 N LEU B 65 -15.827 18.093 21.644 1.00 31.60 N ANISOU 2638 N LEU B 65 3861 3950 4196 -15 16 -478 N ATOM 2639 CA LEU B 65 -16.990 17.456 22.244 1.00 32.58 C ANISOU 2639 CA LEU B 65 3930 4023 4427 28 113 -492 C ATOM 2640 C LEU B 65 -17.548 18.245 23.430 1.00 33.86 C ANISOU 2640 C LEU B 65 4120 4245 4500 26 146 -537 C ATOM 2641 O LEU B 65 -16.823 18.588 24.389 1.00 34.78 O ANISOU 2641 O LEU B 65 4268 4524 4423 -17 145 -503 O ATOM 2642 CB LEU B 65 -16.663 16.025 22.680 1.00 32.90 C ANISOU 2642 CB LEU B 65 3874 4072 4555 75 254 -337 C ATOM 2643 CG LEU B 65 -17.826 15.275 23.327 1.00 33.18 C ANISOU 2643 CG LEU B 65 3822 4035 4749 123 386 -308 C ATOM 2644 CD1 LEU B 65 -18.851 14.856 22.287 1.00 33.24 C ANISOU 2644 CD1 LEU B 65 3800 3857 4973 94 374 -457 C ATOM 2645 CD2 LEU B 65 -17.306 14.081 24.074 1.00 34.21 C ANISOU 2645 CD2 LEU B 65 3838 4204 4958 187 552 -67 C ATOM 2646 N ALA B 66 -18.842 18.530 23.365 1.00 34.26 N ANISOU 2646 N ALA B 66 4151 4181 4684 62 183 -618 N ATOM 2647 CA ALA B 66 -19.492 19.218 24.466 1.00 35.81 C ANISOU 2647 CA ALA B 66 4382 4395 4831 82 288 -679 C ATOM 2648 C ALA B 66 -20.531 18.294 25.044 1.00 36.69 C ANISOU 2648 C ALA B 66 4386 4479 5074 157 436 -599 C ATOM 2649 O ALA B 66 -21.296 17.661 24.312 1.00 36.71 O ANISOU 2649 O ALA B 66 4283 4359 5308 179 424 -574 O ATOM 2650 CB ALA B 66 -20.127 20.535 24.011 1.00 36.20 C ANISOU 2650 CB ALA B 66 4469 4296 4988 89 270 -796 C ATOM 2651 N HIS B 67 -20.538 18.213 26.365 1.00 37.80 N ANISOU 2651 N HIS B 67 4548 4759 5054 177 574 -557 N ATOM 2652 CA HIS B 67 -21.505 17.415 27.064 1.00 38.69 C ANISOU 2652 CA HIS B 67 4553 4861 5288 263 758 -440 C ATOM 2653 C HIS B 67 -22.029 18.189 28.266 1.00 40.55 C ANISOU 2653 C HIS B 67 4870 5184 5353 291 931 -522 C ATOM 2654 O HIS B 67 -21.386 19.120 28.747 1.00 41.07 O ANISOU 2654 O HIS B 67 5087 5370 5147 213 905 -673 O ATOM 2655 CB HIS B 67 -20.879 16.083 27.479 1.00 38.96 C ANISOU 2655 CB HIS B 67 4490 5014 5299 287 813 -206 C ATOM 2656 CG HIS B 67 -19.727 16.221 28.426 1.00 40.46 C ANISOU 2656 CG HIS B 67 4739 5508 5126 247 790 -110 C ATOM 2657 ND1 HIS B 67 -18.475 16.637 28.021 1.00 40.02 N ANISOU 2657 ND1 HIS B 67 4746 5548 4912 156 611 -145 N ATOM 2658 CD2 HIS B 67 -19.639 15.998 29.761 1.00 42.59 C ANISOU 2658 CD2 HIS B 67 4992 6051 5139 271 910 41 C ATOM 2659 CE1 HIS B 67 -17.666 16.663 29.067 1.00 41.80 C ANISOU 2659 CE1 HIS B 67 4972 6096 4814 109 595 -23 C ATOM 2660 NE2 HIS B 67 -18.348 16.285 30.135 1.00 43.33 N ANISOU 2660 NE2 HIS B 67 5127 6426 4910 174 768 87 N ATOM 2661 N THR B 68 -23.215 17.809 28.720 1.00 41.94 N ANISOU 2661 N THR B 68 4945 5285 5707 389 1127 -443 N ATOM 2662 CA THR B 68 -23.801 18.336 29.939 1.00 44.64 C ANISOU 2662 CA THR B 68 5357 5717 5888 442 1370 -499 C ATOM 2663 C THR B 68 -24.750 17.295 30.538 1.00 46.26 C ANISOU 2663 C THR B 68 5389 5920 6267 560 1590 -264 C ATOM 2664 O THR B 68 -25.257 16.424 29.823 1.00 45.12 O ANISOU 2664 O THR B 68 5060 5603 6481 587 1551 -127 O ATOM 2665 CB THR B 68 -24.522 19.702 29.703 1.00 45.39 C ANISOU 2665 CB THR B 68 5531 5599 6118 461 1453 -724 C ATOM 2666 OG1 THR B 68 -24.988 20.235 30.953 1.00 47.84 O ANISOU 2666 OG1 THR B 68 5949 5988 6239 504 1747 -833 O ATOM 2667 CG2 THR B 68 -25.690 19.556 28.738 1.00 44.54 C ANISOU 2667 CG2 THR B 68 5221 5228 6476 545 1440 -626 C ATOM 2668 N GLU B 69 -24.955 17.368 31.851 1.00 49.24 N ANISOU 2668 N GLU B 69 5828 6503 6379 611 1829 -225 N ATOM 2669 CA GLU B 69 -25.923 16.514 32.518 1.00 51.84 C ANISOU 2669 CA GLU B 69 5989 6832 6876 741 2093 23 C ATOM 2670 C GLU B 69 -27.304 17.015 32.188 1.00 52.44 C ANISOU 2670 C GLU B 69 5972 6617 7337 828 2247 -46 C ATOM 2671 O GLU B 69 -27.546 18.223 32.181 1.00 53.47 O ANISOU 2671 O GLU B 69 6236 6658 7423 827 2308 -284 O ATOM 2672 CB GLU B 69 -25.734 16.542 34.029 1.00 55.19 C ANISOU 2672 CB GLU B 69 6519 7620 6832 774 2321 92 C ATOM 2673 CG GLU B 69 -24.605 15.671 34.509 1.00 57.71 C ANISOU 2673 CG GLU B 69 6801 8278 6847 735 2213 351 C ATOM 2674 CD GLU B 69 -24.005 16.182 35.795 1.00 63.31 C ANISOU 2674 CD GLU B 69 7691 9456 6908 668 2281 290 C ATOM 2675 OE1 GLU B 69 -24.753 16.307 36.796 1.00 67.03 O ANISOU 2675 OE1 GLU B 69 8203 10074 7193 749 2583 310 O ATOM 2676 OE2 GLU B 69 -22.782 16.462 35.796 1.00 64.18 O ANISOU 2676 OE2 GLU B 69 7895 9809 6683 520 2031 216 O ATOM 2677 N PHE B 70 -28.211 16.093 31.901 1.00 52.52 N ANISOU 2677 N PHE B 70 5727 6459 7771 896 2322 177 N ATOM 2678 CA PHE B 70 -29.588 16.468 31.672 1.00 53.72 C ANISOU 2678 CA PHE B 70 5720 6371 8321 983 2473 190 C ATOM 2679 C PHE B 70 -30.513 15.332 32.068 1.00 55.81 C ANISOU 2679 C PHE B 70 5714 6570 8921 1068 2685 494 C ATOM 2680 O PHE B 70 -30.160 14.157 31.939 1.00 55.51 O ANISOU 2680 O PHE B 70 5561 6543 8987 1025 2617 669 O ATOM 2681 CB PHE B 70 -29.802 16.908 30.214 1.00 51.52 C ANISOU 2681 CB PHE B 70 5356 5872 8347 904 2182 76 C ATOM 2682 CG PHE B 70 -30.074 15.779 29.250 1.00 50.12 C ANISOU 2682 CG PHE B 70 4941 5575 8527 818 1982 200 C ATOM 2683 CD1 PHE B 70 -29.190 14.705 29.122 1.00 48.03 C ANISOU 2683 CD1 PHE B 70 4695 5377 8178 737 1876 253 C ATOM 2684 CD2 PHE B 70 -31.216 15.806 28.446 1.00 50.47 C ANISOU 2684 CD2 PHE B 70 4729 5439 9008 802 1907 258 C ATOM 2685 CE1 PHE B 70 -29.446 13.672 28.225 1.00 46.86 C ANISOU 2685 CE1 PHE B 70 4353 5073 8379 631 1738 295 C ATOM 2686 CE2 PHE B 70 -31.478 14.779 27.545 1.00 49.51 C ANISOU 2686 CE2 PHE B 70 4400 5227 9186 666 1709 302 C ATOM 2687 CZ PHE B 70 -30.586 13.712 27.432 1.00 47.71 C ANISOU 2687 CZ PHE B 70 4234 5021 8871 574 1641 285 C ATOM 2688 N THR B 71 -31.682 15.698 32.583 1.00 58.38 N ANISOU 2688 N THR B 71 5929 6802 9450 1197 2984 570 N ATOM 2689 CA THR B 71 -32.753 14.752 32.809 1.00 60.42 C ANISOU 2689 CA THR B 71 5874 6939 10145 1274 3188 870 C ATOM 2690 C THR B 71 -33.804 14.975 31.724 1.00 60.37 C ANISOU 2690 C THR B 71 5600 6657 10680 1238 3046 873 C ATOM 2691 O THR B 71 -34.391 16.052 31.637 1.00 61.13 O ANISOU 2691 O THR B 71 5698 6665 10862 1316 3134 794 O ATOM 2692 CB THR B 71 -33.333 14.907 34.215 1.00 63.89 C ANISOU 2692 CB THR B 71 6339 7507 10430 1454 3657 1014 C ATOM 2693 OG1 THR B 71 -32.348 14.487 35.165 1.00 65.21 O ANISOU 2693 OG1 THR B 71 6696 8007 10074 1458 3732 1082 O ATOM 2694 CG2 THR B 71 -34.568 14.052 34.388 1.00 66.45 C ANISOU 2694 CG2 THR B 71 6297 7661 11291 1545 3895 1351 C ATOM 2695 N PRO B 72 -34.017 13.961 30.867 1.00 59.91 N ANISOU 2695 N PRO B 72 5300 6469 10994 1104 2823 964 N ATOM 2696 CA PRO B 72 -34.955 14.101 29.758 1.00 60.59 C ANISOU 2696 CA PRO B 72 5107 6378 11537 1014 2609 968 C ATOM 2697 C PRO B 72 -36.410 13.925 30.197 1.00 64.30 C ANISOU 2697 C PRO B 72 5227 6714 12491 1120 2890 1239 C ATOM 2698 O PRO B 72 -36.751 12.924 30.842 1.00 66.37 O ANISOU 2698 O PRO B 72 5330 6933 12955 1150 3117 1453 O ATOM 2699 CB PRO B 72 -34.528 12.986 28.796 1.00 59.18 C ANISOU 2699 CB PRO B 72 4841 6141 11504 790 2297 901 C ATOM 2700 CG PRO B 72 -33.888 11.969 29.650 1.00 59.07 C ANISOU 2700 CG PRO B 72 4902 6164 11378 829 2507 1023 C ATOM 2701 CD PRO B 72 -33.325 12.659 30.852 1.00 59.03 C ANISOU 2701 CD PRO B 72 5167 6375 10886 1011 2757 1049 C ATOM 2702 N THR B 73 -37.252 14.900 29.868 1.00 65.63 N ANISOU 2702 N THR B 73 5251 6808 12877 1193 2901 1274 N ATOM 2703 CA THR B 73 -38.678 14.796 30.153 1.00 69.25 C ANISOU 2703 CA THR B 73 5320 7131 13862 1293 3148 1567 C ATOM 2704 C THR B 73 -39.464 14.826 28.849 1.00 70.32 C ANISOU 2704 C THR B 73 5085 7198 14437 1130 2774 1638 C ATOM 2705 O THR B 73 -38.899 15.041 27.776 1.00 68.35 O ANISOU 2705 O THR B 73 4923 7025 14020 964 2358 1449 O ATOM 2706 CB THR B 73 -39.184 15.915 31.099 1.00 71.38 C ANISOU 2706 CB THR B 73 5669 7367 14086 1567 3605 1633 C ATOM 2707 OG1 THR B 73 -39.318 17.142 30.370 1.00 71.65 O ANISOU 2707 OG1 THR B 73 5705 7340 14177 1598 3462 1548 O ATOM 2708 CG2 THR B 73 -38.244 16.113 32.294 1.00 70.38 C ANISOU 2708 CG2 THR B 73 5978 7400 13362 1676 3902 1468 C ATOM 2709 N GLU B 74 -40.771 14.614 28.954 1.00 74.11 N ANISOU 2709 N GLU B 74 5133 7566 15461 1174 2923 1935 N ATOM 2710 CA GLU B 74 -41.657 14.569 27.798 1.00 76.22 C ANISOU 2710 CA GLU B 74 4965 7824 16170 996 2558 2065 C ATOM 2711 C GLU B 74 -41.815 15.944 27.126 1.00 76.22 C ANISOU 2711 C GLU B 74 4941 7881 16139 1085 2406 2096 C ATOM 2712 O GLU B 74 -41.950 16.034 25.904 1.00 76.54 O ANISOU 2712 O GLU B 74 4791 8040 16252 888 1945 2094 O ATOM 2713 CB GLU B 74 -43.016 14.019 28.233 1.00 80.47 C ANISOU 2713 CB GLU B 74 5013 8231 17331 1036 2803 2425 C ATOM 2714 CG GLU B 74 -43.885 13.463 27.115 1.00 83.99 C ANISOU 2714 CG GLU B 74 4957 8700 18255 741 2376 2541 C ATOM 2715 CD GLU B 74 -45.228 12.944 27.626 1.00 89.67 C ANISOU 2715 CD GLU B 74 5158 9275 19638 782 2647 2927 C ATOM 2716 OE1 GLU B 74 -45.251 11.885 28.298 1.00 89.97 O ANISOU 2716 OE1 GLU B 74 5166 9182 19837 747 2886 2968 O ATOM 2717 OE2 GLU B 74 -46.263 13.599 27.354 1.00 93.59 O ANISOU 2717 OE2 GLU B 74 5247 9783 20530 859 2636 3233 O ATOM 2718 N THR B 75 -41.770 17.008 27.927 1.00 76.30 N ANISOU 2718 N THR B 75 5150 7811 16031 1375 2811 2121 N ATOM 2719 CA THR B 75 -42.079 18.365 27.450 1.00 77.09 C ANISOU 2719 CA THR B 75 5169 7873 16248 1518 2804 2228 C ATOM 2720 C THR B 75 -40.874 19.277 27.197 1.00 73.52 C ANISOU 2720 C THR B 75 5173 7464 15299 1536 2701 1925 C ATOM 2721 O THR B 75 -41.047 20.383 26.680 1.00 74.58 O ANISOU 2721 O THR B 75 5232 7547 15559 1638 2672 2028 O ATOM 2722 CB THR B 75 -43.009 19.100 28.436 1.00 80.83 C ANISOU 2722 CB THR B 75 5501 8143 17068 1843 3403 2473 C ATOM 2723 OG1 THR B 75 -42.477 18.984 29.762 1.00 80.58 O ANISOU 2723 OG1 THR B 75 5869 8072 16676 1978 3862 2268 O ATOM 2724 CG2 THR B 75 -44.423 18.518 28.401 1.00 85.23 C ANISOU 2724 CG2 THR B 75 5464 8646 18274 1848 3467 2894 C ATOM 2725 N ASP B 76 -39.671 18.833 27.568 1.00 69.53 N ANISOU 2725 N ASP B 76 5099 7042 14276 1445 2662 1597 N ATOM 2726 CA ASP B 76 -38.461 19.659 27.425 1.00 66.03 C ANISOU 2726 CA ASP B 76 5083 6639 13366 1444 2580 1305 C ATOM 2727 C ASP B 76 -37.693 19.361 26.143 1.00 62.92 C ANISOU 2727 C ASP B 76 4740 6411 12757 1202 2028 1176 C ATOM 2728 O ASP B 76 -37.469 18.199 25.803 1.00 61.94 O ANISOU 2728 O ASP B 76 4575 6388 12572 1004 1784 1112 O ATOM 2729 CB ASP B 76 -37.544 19.490 28.639 1.00 64.47 C ANISOU 2729 CB ASP B 76 5316 6478 12700 1493 2874 1046 C ATOM 2730 CG ASP B 76 -38.070 20.201 29.873 1.00 67.27 C ANISOU 2730 CG ASP B 76 5751 6699 13110 1739 3455 1067 C ATOM 2731 OD1 ASP B 76 -38.367 21.415 29.785 1.00 68.56 O ANISOU 2731 OD1 ASP B 76 5917 6694 13440 1878 3640 1065 O ATOM 2732 OD2 ASP B 76 -38.176 19.549 30.936 1.00 67.50 O ANISOU 2732 OD2 ASP B 76 5843 6786 13017 1798 3756 1090 O ATOM 2733 N THR B 77 -37.296 20.413 25.432 1.00 61.79 N ANISOU 2733 N THR B 77 4683 6275 12521 1224 1873 1143 N ATOM 2734 CA THR B 77 -36.496 20.264 24.214 1.00 59.16 C ANISOU 2734 CA THR B 77 4431 6123 11926 1019 1391 1025 C ATOM 2735 C THR B 77 -35.072 20.783 24.424 1.00 55.94 C ANISOU 2735 C THR B 77 4485 5722 11048 1019 1414 728 C ATOM 2736 O THR B 77 -34.860 21.846 25.021 1.00 56.58 O ANISOU 2736 O THR B 77 4744 5657 11095 1177 1705 666 O ATOM 2737 CB THR B 77 -37.120 20.982 22.981 1.00 61.36 C ANISOU 2737 CB THR B 77 4381 6482 12452 1009 1106 1298 C ATOM 2738 OG1 THR B 77 -36.767 22.376 22.987 1.00 61.54 O ANISOU 2738 OG1 THR B 77 4547 6376 12460 1187 1272 1327 O ATOM 2739 CG2 THR B 77 -38.646 20.826 22.942 1.00 65.12 C ANISOU 2739 CG2 THR B 77 4342 6932 13467 1062 1155 1668 C ATOM 2740 N TYR B 78 -34.104 20.031 23.914 1.00 52.65 N ANISOU 2740 N TYR B 78 4245 5458 10302 828 1122 537 N ATOM 2741 CA TYR B 78 -32.696 20.369 24.061 1.00 49.35 C ANISOU 2741 CA TYR B 78 4218 5077 9454 800 1103 286 C ATOM 2742 C TYR B 78 -32.043 20.610 22.714 1.00 47.98 C ANISOU 2742 C TYR B 78 4079 5036 9117 673 722 254 C ATOM 2743 O TYR B 78 -32.491 20.084 21.701 1.00 49.00 O ANISOU 2743 O TYR B 78 3985 5292 9340 543 428 345 O ATOM 2744 CB TYR B 78 -31.977 19.236 24.769 1.00 47.53 C ANISOU 2744 CB TYR B 78 4173 4914 8971 722 1161 131 C ATOM 2745 CG TYR B 78 -32.343 19.088 26.225 1.00 48.26 C ANISOU 2745 CG TYR B 78 4309 4941 9085 858 1564 159 C ATOM 2746 CD1 TYR B 78 -33.501 18.412 26.618 1.00 49.84 C ANISOU 2746 CD1 TYR B 78 4229 5077 9632 909 1729 356 C ATOM 2747 CD2 TYR B 78 -31.519 19.609 27.212 1.00 47.04 C ANISOU 2747 CD2 TYR B 78 4468 4822 8583 917 1778 -9 C ATOM 2748 CE1 TYR B 78 -33.823 18.271 27.962 1.00 51.27 C ANISOU 2748 CE1 TYR B 78 4454 5229 9796 1048 2130 408 C ATOM 2749 CE2 TYR B 78 -31.829 19.476 28.545 1.00 48.84 C ANISOU 2749 CE2 TYR B 78 4755 5061 8742 1027 2148 7 C ATOM 2750 CZ TYR B 78 -32.975 18.809 28.920 1.00 50.78 C ANISOU 2750 CZ TYR B 78 4733 5243 9318 1108 2339 227 C ATOM 2751 OH TYR B 78 -33.249 18.690 30.259 1.00 52.56 O ANISOU 2751 OH TYR B 78 5029 5510 9432 1232 2736 264 O ATOM 2752 N ALA B 79 -30.975 21.398 22.696 1.00 46.39 N ANISOU 2752 N ALA B 79 4151 4822 8652 691 729 115 N ATOM 2753 CA ALA B 79 -30.295 21.709 21.439 1.00 45.39 C ANISOU 2753 CA ALA B 79 4065 4823 8358 595 413 116 C ATOM 2754 C ALA B 79 -28.800 22.012 21.577 1.00 43.08 C ANISOU 2754 C ALA B 79 4112 4545 7711 553 408 -95 C ATOM 2755 O ALA B 79 -28.281 22.262 22.677 1.00 42.73 O ANISOU 2755 O ALA B 79 4276 4414 7545 598 644 -246 O ATOM 2756 CB ALA B 79 -31.003 22.861 20.725 1.00 47.57 C ANISOU 2756 CB ALA B 79 4115 5059 8902 701 372 384 C ATOM 2757 N CYS B 80 -28.119 21.994 20.438 1.00 41.89 N ANISOU 2757 N CYS B 80 4001 4536 7381 452 133 -98 N ATOM 2758 CA CYS B 80 -26.765 22.498 20.351 1.00 40.00 C ANISOU 2758 CA CYS B 80 4016 4304 6879 423 113 -224 C ATOM 2759 C CYS B 80 -26.714 23.573 19.275 1.00 41.21 C ANISOU 2759 C CYS B 80 4091 4473 7094 460 -15 -46 C ATOM 2760 O CYS B 80 -27.085 23.320 18.116 1.00 41.93 O ANISOU 2760 O CYS B 80 4015 4749 7167 404 -263 102 O ATOM 2761 CB CYS B 80 -25.804 21.374 20.029 1.00 38.09 C ANISOU 2761 CB CYS B 80 3907 4209 6356 287 -35 -369 C ATOM 2762 SG CYS B 80 -24.131 21.744 20.472 1.00 35.43 S ANISOU 2762 SG CYS B 80 3858 3871 5734 258 19 -517 S ATOM 2763 N ARG B 81 -26.256 24.760 19.687 1.00 41.61 N ANISOU 2763 N ARG B 81 4257 4340 7214 540 165 -63 N ATOM 2764 CA ARG B 81 -26.269 25.994 18.900 1.00 43.16 C ANISOU 2764 CA ARG B 81 4358 4457 7583 621 151 157 C ATOM 2765 C ARG B 81 -24.841 26.473 18.733 1.00 41.95 C ANISOU 2765 C ARG B 81 4430 4283 7225 553 129 37 C ATOM 2766 O ARG B 81 -24.103 26.575 19.715 1.00 41.04 O ANISOU 2766 O ARG B 81 4530 4059 7006 501 281 -215 O ATOM 2767 CB ARG B 81 -27.062 27.048 19.665 1.00 45.73 C ANISOU 2767 CB ARG B 81 4602 4472 8300 781 484 227 C ATOM 2768 CG ARG B 81 -27.510 28.299 18.902 1.00 48.66 C ANISOU 2768 CG ARG B 81 4759 4702 9027 923 541 573 C ATOM 2769 CD ARG B 81 -28.115 29.259 19.928 1.00 52.00 C ANISOU 2769 CD ARG B 81 5176 4730 9853 1073 981 530 C ATOM 2770 NE ARG B 81 -29.146 30.179 19.433 1.00 56.23 N ANISOU 2770 NE ARG B 81 5381 5092 10891 1274 1122 951 N ATOM 2771 CZ ARG B 81 -30.431 29.879 19.227 1.00 56.93 C ANISOU 2771 CZ ARG B 81 5134 5265 11231 1381 1092 1258 C ATOM 2772 NH1 ARG B 81 -30.901 28.653 19.420 1.00 53.35 N ANISOU 2772 NH1 ARG B 81 4630 5054 10585 1289 917 1174 N ATOM 2773 NH2 ARG B 81 -31.250 30.827 18.789 1.00 61.22 N ANISOU 2773 NH2 ARG B 81 5354 5642 12266 1580 1242 1695 N ATOM 2774 N VAL B 82 -24.460 26.787 17.496 1.00 42.50 N ANISOU 2774 N VAL B 82 4433 4487 7228 543 -61 240 N ATOM 2775 CA VAL B 82 -23.051 27.014 17.147 1.00 41.39 C ANISOU 2775 CA VAL B 82 4475 4380 6871 464 -117 163 C ATOM 2776 C VAL B 82 -22.795 28.229 16.249 1.00 43.61 C ANISOU 2776 C VAL B 82 4662 4591 7316 540 -111 449 C ATOM 2777 O VAL B 82 -23.451 28.403 15.221 1.00 45.68 O ANISOU 2777 O VAL B 82 4708 5013 7634 610 -247 774 O ATOM 2778 CB VAL B 82 -22.463 25.744 16.489 1.00 39.42 C ANISOU 2778 CB VAL B 82 4298 4428 6252 344 -348 77 C ATOM 2779 CG1 VAL B 82 -21.289 26.064 15.574 1.00 38.76 C ANISOU 2779 CG1 VAL B 82 4296 4446 5985 306 -439 157 C ATOM 2780 CG2 VAL B 82 -22.068 24.739 17.553 1.00 37.57 C ANISOU 2780 CG2 VAL B 82 4218 4183 5874 266 -279 -206 C ATOM 2781 N LYS B 83 -21.833 29.061 16.648 1.00 44.00 N ANISOU 2781 N LYS B 83 4853 4419 7445 513 41 347 N ATOM 2782 CA LYS B 83 -21.376 30.198 15.840 1.00 45.99 C ANISOU 2782 CA LYS B 83 5028 4563 7884 573 82 619 C ATOM 2783 C LYS B 83 -19.972 29.929 15.317 1.00 44.50 C ANISOU 2783 C LYS B 83 4977 4533 7398 460 -46 571 C ATOM 2784 O LYS B 83 -19.117 29.415 16.053 1.00 42.73 O ANISOU 2784 O LYS B 83 4939 4313 6984 332 -43 268 O ATOM 2785 CB LYS B 83 -21.340 31.470 16.679 1.00 48.19 C ANISOU 2785 CB LYS B 83 5341 4392 8577 608 407 530 C ATOM 2786 CG LYS B 83 -22.619 32.284 16.729 1.00 52.11 C ANISOU 2786 CG LYS B 83 5619 4639 9540 793 622 773 C ATOM 2787 CD LYS B 83 -22.582 33.212 17.948 1.00 56.04 C ANISOU 2787 CD LYS B 83 6249 4664 10378 777 1008 471 C ATOM 2788 CE LYS B 83 -22.733 34.696 17.567 1.00 61.06 C ANISOU 2788 CE LYS B 83 6726 4886 11587 911 1294 755 C ATOM 2789 NZ LYS B 83 -24.153 35.091 17.303 1.00 63.89 N ANISOU 2789 NZ LYS B 83 6784 5122 12368 1154 1451 1145 N ATOM 2790 N HIS B 84 -19.737 30.286 14.054 1.00 45.61 N ANISOU 2790 N HIS B 84 5002 4825 7501 517 -147 912 N ATOM 2791 CA HIS B 84 -18.444 30.083 13.394 1.00 44.38 C ANISOU 2791 CA HIS B 84 4948 4830 7086 441 -233 933 C ATOM 2792 C HIS B 84 -18.355 30.942 12.144 1.00 46.73 C ANISOU 2792 C HIS B 84 5080 5203 7474 550 -243 1388 C ATOM 2793 O HIS B 84 -19.341 31.095 11.426 1.00 48.63 O ANISOU 2793 O HIS B 84 5123 5610 7745 659 -326 1704 O ATOM 2794 CB HIS B 84 -18.262 28.611 13.025 1.00 42.29 C ANISOU 2794 CB HIS B 84 4778 4918 6373 359 -430 774 C ATOM 2795 CG HIS B 84 -16.881 28.269 12.562 1.00 41.67 C ANISOU 2795 CG HIS B 84 4821 4960 6050 288 -453 740 C ATOM 2796 ND1 HIS B 84 -16.591 27.958 11.250 1.00 42.87 N ANISOU 2796 ND1 HIS B 84 4953 5416 5920 306 -556 932 N ATOM 2797 CD2 HIS B 84 -15.710 28.180 13.237 1.00 40.09 C ANISOU 2797 CD2 HIS B 84 4748 4642 5843 197 -377 554 C ATOM 2798 CE1 HIS B 84 -15.301 27.697 11.137 1.00 42.08 C ANISOU 2798 CE1 HIS B 84 4966 5335 5686 253 -504 867 C ATOM 2799 NE2 HIS B 84 -14.744 27.822 12.329 1.00 40.19 N ANISOU 2799 NE2 HIS B 84 4796 4846 5627 185 -412 659 N ATOM 2800 N ALA B 85 -17.172 31.489 11.881 1.00 47.02 N ANISOU 2800 N ALA B 85 5167 5146 7551 517 -163 1462 N ATOM 2801 CA ALA B 85 -16.973 32.433 10.768 1.00 50.07 C ANISOU 2801 CA ALA B 85 5386 5562 8078 633 -116 1944 C ATOM 2802 C ALA B 85 -17.620 31.957 9.464 1.00 51.54 C ANISOU 2802 C ALA B 85 5439 6231 7912 716 -327 2276 C ATOM 2803 O ALA B 85 -18.287 32.725 8.761 1.00 54.59 O ANISOU 2803 O ALA B 85 5588 6678 8475 860 -317 2741 O ATOM 2804 CB ALA B 85 -15.482 32.726 10.564 1.00 49.83 C ANISOU 2804 CB ALA B 85 5441 5460 8034 557 -38 1952 C ATOM 2805 N SER B 86 -17.442 30.671 9.184 1.00 49.78 N ANISOU 2805 N SER B 86 5359 6355 7199 612 -509 2029 N ATOM 2806 CA SER B 86 -17.986 30.005 8.004 1.00 51.58 C ANISOU 2806 CA SER B 86 5517 7090 6990 612 -732 2195 C ATOM 2807 C SER B 86 -19.498 30.125 7.849 1.00 54.01 C ANISOU 2807 C SER B 86 5591 7536 7396 675 -868 2408 C ATOM 2808 O SER B 86 -20.049 29.644 6.864 1.00 56.15 O ANISOU 2808 O SER B 86 5766 8273 7297 642 -1094 2561 O ATOM 2809 CB SER B 86 -17.666 28.522 8.093 1.00 49.04 C ANISOU 2809 CB SER B 86 5414 6966 6252 459 -837 1748 C ATOM 2810 OG SER B 86 -18.369 27.959 9.184 1.00 46.42 O ANISOU 2810 OG SER B 86 5113 6452 6071 404 -851 1429 O ATOM 2811 N MET B 87 -20.165 30.736 8.825 1.00 54.20 N ANISOU 2811 N MET B 87 5516 7173 7905 750 -728 2404 N ATOM 2812 CA MET B 87 -21.627 30.773 8.858 1.00 56.26 C ANISOU 2812 CA MET B 87 5531 7514 8332 817 -822 2591 C ATOM 2813 C MET B 87 -22.201 32.172 9.078 1.00 59.36 C ANISOU 2813 C MET B 87 5670 7559 9326 1018 -599 3011 C ATOM 2814 O MET B 87 -21.794 32.892 10.002 1.00 58.72 O ANISOU 2814 O MET B 87 5683 6970 9659 1055 -307 2857 O ATOM 2815 CB MET B 87 -22.156 29.805 9.921 1.00 53.46 C ANISOU 2815 CB MET B 87 5292 7046 7974 713 -842 2124 C ATOM 2816 CG MET B 87 -22.808 28.545 9.358 1.00 53.30 C ANISOU 2816 CG MET B 87 5238 7472 7540 576 -1138 1998 C ATOM 2817 SD MET B 87 -22.680 27.071 10.409 1.00 49.93 S ANISOU 2817 SD MET B 87 5067 6935 6970 406 -1129 1372 S ATOM 2818 CE MET B 87 -22.778 27.732 12.077 1.00 47.43 C ANISOU 2818 CE MET B 87 4802 6063 7155 507 -813 1220 C ATOM 2819 N ALA B 88 -23.147 32.546 8.218 1.00 63.25 N ANISOU 2819 N ALA B 88 5829 8335 9869 1136 -729 3543 N ATOM 2820 CA ALA B 88 -23.851 33.809 8.357 1.00 66.88 C ANISOU 2820 CA ALA B 88 5983 8469 10959 1360 -496 4022 C ATOM 2821 C ALA B 88 -24.673 33.799 9.646 1.00 66.03 C ANISOU 2821 C ALA B 88 5872 7942 11273 1392 -298 3739 C ATOM 2822 O ALA B 88 -24.503 34.666 10.502 1.00 66.23 O ANISOU 2822 O ALA B 88 5951 7401 11811 1478 69 3644 O ATOM 2823 CB ALA B 88 -24.731 34.067 7.147 1.00 71.49 C ANISOU 2823 CB ALA B 88 6164 9541 11459 1475 -722 4707 C ATOM 2824 N GLU B 89 -25.545 32.805 9.786 1.00 65.42 N ANISOU 2824 N GLU B 89 5740 8141 10975 1307 -522 3579 N ATOM 2825 CA GLU B 89 -26.362 32.665 10.989 1.00 64.92 C ANISOU 2825 CA GLU B 89 5669 7737 11261 1339 -333 3322 C ATOM 2826 C GLU B 89 -25.940 31.435 11.782 1.00 60.30 C ANISOU 2826 C GLU B 89 5426 7177 10307 1131 -410 2668 C ATOM 2827 O GLU B 89 -25.568 30.426 11.188 1.00 58.74 O ANISOU 2827 O GLU B 89 5342 7383 9595 965 -704 2504 O ATOM 2828 CB GLU B 89 -27.859 32.579 10.638 1.00 68.47 C ANISOU 2828 CB GLU B 89 5699 8425 11892 1435 -477 3746 C ATOM 2829 CG GLU B 89 -28.497 33.893 10.141 1.00 74.42 C ANISOU 2829 CG GLU B 89 6037 9047 13193 1702 -304 4470 C ATOM 2830 CD GLU B 89 -28.744 34.931 11.247 1.00 76.57 C ANISOU 2830 CD GLU B 89 6300 8592 14201 1900 234 4439 C ATOM 2831 OE1 GLU B 89 -27.915 35.045 12.181 1.00 74.25 O ANISOU 2831 OE1 GLU B 89 6382 7881 13948 1823 496 3901 O ATOM 2832 OE2 GLU B 89 -29.766 35.650 11.169 1.00 80.58 O ANISOU 2832 OE2 GLU B 89 6409 8954 15253 2126 409 4961 O ATOM 2833 N PRO B 90 -25.997 31.516 13.126 1.00 58.66 N ANISOU 2833 N PRO B 90 5380 6543 10366 1143 -120 2304 N ATOM 2834 CA PRO B 90 -25.776 30.369 14.019 1.00 55.09 C ANISOU 2834 CA PRO B 90 5191 6111 9630 982 -158 1770 C ATOM 2835 C PRO B 90 -26.627 29.142 13.670 1.00 54.81 C ANISOU 2835 C PRO B 90 5021 6457 9347 887 -451 1759 C ATOM 2836 O PRO B 90 -27.840 29.253 13.502 1.00 57.38 O ANISOU 2836 O PRO B 90 5032 6849 9919 974 -489 2058 O ATOM 2837 CB PRO B 90 -26.192 30.913 15.398 1.00 55.45 C ANISOU 2837 CB PRO B 90 5294 5686 10088 1071 228 1569 C ATOM 2838 CG PRO B 90 -26.939 32.186 15.113 1.00 59.51 C ANISOU 2838 CG PRO B 90 5513 5948 11151 1291 450 2027 C ATOM 2839 CD PRO B 90 -26.276 32.735 13.898 1.00 60.68 C ANISOU 2839 CD PRO B 90 5577 6262 11215 1311 299 2382 C ATOM 2840 N LYS B 91 -25.987 27.983 13.558 1.00 52.38 N ANISOU 2840 N LYS B 91 4928 6378 8596 703 -639 1427 N ATOM 2841 CA LYS B 91 -26.712 26.741 13.297 1.00 52.76 C ANISOU 2841 CA LYS B 91 4881 6725 8442 569 -882 1328 C ATOM 2842 C LYS B 91 -27.153 26.071 14.591 1.00 51.22 C ANISOU 2842 C LYS B 91 4757 6305 8398 552 -711 1029 C ATOM 2843 O LYS B 91 -26.332 25.798 15.474 1.00 48.28 O ANISOU 2843 O LYS B 91 4660 5749 7934 517 -547 705 O ATOM 2844 CB LYS B 91 -25.893 25.760 12.446 1.00 51.48 C ANISOU 2844 CB LYS B 91 4893 6895 7771 379 -1125 1122 C ATOM 2845 CG LYS B 91 -26.688 24.501 12.037 1.00 52.66 C ANISOU 2845 CG LYS B 91 4929 7339 7740 198 -1375 991 C ATOM 2846 CD LYS B 91 -26.077 23.747 10.854 1.00 53.81 C ANISOU 2846 CD LYS B 91 5193 7862 7390 10 -1614 852 C ATOM 2847 CE LYS B 91 -24.749 23.084 11.209 1.00 50.25 C ANISOU 2847 CE LYS B 91 5096 7263 6733 -49 -1466 474 C ATOM 2848 NZ LYS B 91 -24.465 21.912 10.340 1.00 51.54 N ANISOU 2848 NZ LYS B 91 5371 7706 6504 -262 -1625 205 N ATOM 2849 N THR B 92 -28.456 25.807 14.681 1.00 53.46 N ANISOU 2849 N THR B 92 4762 6641 8909 574 -757 1183 N ATOM 2850 CA THR B 92 -29.023 25.069 15.804 1.00 52.79 C ANISOU 2850 CA THR B 92 4694 6391 8972 560 -601 961 C ATOM 2851 C THR B 92 -29.469 23.652 15.405 1.00 53.12 C ANISOU 2851 C THR B 92 4652 6699 8833 357 -859 822 C ATOM 2852 O THR B 92 -30.209 23.468 14.437 1.00 55.70 O ANISOU 2852 O THR B 92 4708 7317 9137 269 -1139 1029 O ATOM 2853 CB THR B 92 -30.187 25.839 16.438 1.00 55.09 C ANISOU 2853 CB THR B 92 4728 6447 9757 754 -356 1218 C ATOM 2854 OG1 THR B 92 -29.872 27.235 16.456 1.00 56.27 O ANISOU 2854 OG1 THR B 92 4895 6358 10126 925 -139 1399 O ATOM 2855 CG2 THR B 92 -30.426 25.358 17.863 1.00 53.75 C ANISOU 2855 CG2 THR B 92 4685 6032 9706 784 -63 949 C ATOM 2856 N VAL B 93 -28.998 22.658 16.151 1.00 51.04 N ANISOU 2856 N VAL B 93 4607 6339 8446 268 -762 479 N ATOM 2857 CA VAL B 93 -29.427 21.277 15.952 1.00 51.97 C ANISOU 2857 CA VAL B 93 4652 6598 8498 77 -919 312 C ATOM 2858 C VAL B 93 -30.134 20.796 17.223 1.00 52.45 C ANISOU 2858 C VAL B 93 4643 6430 8857 139 -672 262 C ATOM 2859 O VAL B 93 -29.604 20.919 18.327 1.00 50.52 O ANISOU 2859 O VAL B 93 4605 5973 8616 244 -395 140 O ATOM 2860 CB VAL B 93 -28.234 20.343 15.554 1.00 49.87 C ANISOU 2860 CB VAL B 93 4669 6420 7859 -84 -999 -5 C ATOM 2861 CG1 VAL B 93 -28.629 18.889 15.617 1.00 49.77 C ANISOU 2861 CG1 VAL B 93 4609 6420 7882 -268 -1044 -226 C ATOM 2862 CG2 VAL B 93 -27.721 20.676 14.154 1.00 50.49 C ANISOU 2862 CG2 VAL B 93 4778 6787 7619 -166 -1249 55 C ATOM 2863 N TYR B 94 -31.343 20.270 17.061 1.00 55.77 N ANISOU 2863 N TYR B 94 4752 6923 9514 63 -778 376 N ATOM 2864 CA TYR B 94 -32.135 19.788 18.194 1.00 57.08 C ANISOU 2864 CA TYR B 94 4800 6886 10000 127 -531 386 C ATOM 2865 C TYR B 94 -31.857 18.323 18.502 1.00 56.91 C ANISOU 2865 C TYR B 94 4882 6829 9914 -38 -512 115 C ATOM 2866 O TYR B 94 -31.524 17.542 17.611 1.00 57.18 O ANISOU 2866 O TYR B 94 4952 7013 9759 -254 -748 -62 O ATOM 2867 CB TYR B 94 -33.634 20.025 17.946 1.00 60.30 C ANISOU 2867 CB TYR B 94 4762 7356 10792 150 -613 709 C ATOM 2868 CG TYR B 94 -33.992 21.492 17.963 1.00 61.35 C ANISOU 2868 CG TYR B 94 4766 7414 11130 387 -487 1037 C ATOM 2869 CD1 TYR B 94 -33.851 22.277 16.815 1.00 61.78 C ANISOU 2869 CD1 TYR B 94 4722 7685 11068 384 -741 1255 C ATOM 2870 CD2 TYR B 94 -34.437 22.110 19.141 1.00 61.40 C ANISOU 2870 CD2 TYR B 94 4757 7119 11454 625 -70 1133 C ATOM 2871 CE1 TYR B 94 -34.155 23.635 16.833 1.00 63.67 C ANISOU 2871 CE1 TYR B 94 4820 7798 11574 622 -575 1596 C ATOM 2872 CE2 TYR B 94 -34.747 23.469 19.172 1.00 62.63 C ANISOU 2872 CE2 TYR B 94 4802 7129 11866 850 117 1408 C ATOM 2873 CZ TYR B 94 -34.603 24.226 18.015 1.00 64.13 C ANISOU 2873 CZ TYR B 94 4867 7493 12005 854 -132 1655 C ATOM 2874 OH TYR B 94 -34.905 25.572 18.029 1.00 66.03 O ANISOU 2874 OH TYR B 94 4970 7542 12576 1093 93 1971 O ATOM 2875 N TRP B 95 -31.977 17.961 19.775 1.00 57.37 N ANISOU 2875 N TRP B 95 4988 6678 10131 68 -197 91 N ATOM 2876 CA TRP B 95 -31.909 16.566 20.169 1.00 58.37 C ANISOU 2876 CA TRP B 95 5133 6728 10318 -54 -123 -64 C ATOM 2877 C TRP B 95 -33.204 15.848 19.797 1.00 62.87 C ANISOU 2877 C TRP B 95 5330 7319 11239 -208 -250 20 C ATOM 2878 O TRP B 95 -34.301 16.375 19.988 1.00 64.79 O ANISOU 2878 O TRP B 95 5287 7552 11778 -118 -212 272 O ATOM 2879 CB TRP B 95 -31.642 16.430 21.666 1.00 56.92 C ANISOU 2879 CB TRP B 95 5090 6372 10164 118 255 -49 C ATOM 2880 CG TRP B 95 -31.574 14.995 22.132 1.00 55.99 C ANISOU 2880 CG TRP B 95 4953 6157 10164 28 377 -121 C ATOM 2881 CD1 TRP B 95 -30.743 14.027 21.664 1.00 54.07 C ANISOU 2881 CD1 TRP B 95 4838 5908 9799 -122 294 -311 C ATOM 2882 CD2 TRP B 95 -32.361 14.382 23.166 1.00 56.61 C ANISOU 2882 CD2 TRP B 95 4859 6100 10550 103 654 27 C ATOM 2883 NE1 TRP B 95 -30.961 12.849 22.333 1.00 55.05 N ANISOU 2883 NE1 TRP B 95 4868 5875 10172 -146 504 -279 N ATOM 2884 CE2 TRP B 95 -31.951 13.037 23.259 1.00 56.13 C ANISOU 2884 CE2 TRP B 95 4817 5946 10562 -12 715 -60 C ATOM 2885 CE3 TRP B 95 -33.373 14.840 24.022 1.00 58.21 C ANISOU 2885 CE3 TRP B 95 4885 6235 10999 269 895 244 C ATOM 2886 CZ2 TRP B 95 -32.514 12.141 24.168 1.00 57.54 C ANISOU 2886 CZ2 TRP B 95 4830 5976 11055 30 991 92 C ATOM 2887 CZ3 TRP B 95 -33.938 13.945 24.924 1.00 59.62 C ANISOU 2887 CZ3 TRP B 95 4911 6293 11447 310 1166 379 C ATOM 2888 CH2 TRP B 95 -33.505 12.611 24.989 1.00 59.22 C ANISOU 2888 CH2 TRP B 95 4871 6163 11468 190 1202 318 C ATOM 2889 N ASP B 96 -33.051 14.641 19.262 1.00 65.36 N ANISOU 2889 N ASP B 96 5640 7645 11549 -452 -381 -197 N ATOM 2890 CA ASP B 96 -34.165 13.800 18.873 1.00 70.45 C ANISOU 2890 CA ASP B 96 5944 8298 12526 -675 -520 -195 C ATOM 2891 C ASP B 96 -33.807 12.347 19.151 1.00 71.93 C ANISOU 2891 C ASP B 96 6211 8278 12841 -827 -369 -433 C ATOM 2892 O ASP B 96 -32.735 11.883 18.763 1.00 70.84 O ANISOU 2892 O ASP B 96 6346 8125 12444 -908 -379 -686 O ATOM 2893 CB ASP B 96 -34.470 13.995 17.388 1.00 72.67 C ANISOU 2893 CB ASP B 96 6084 8890 12638 -919 -962 -259 C ATOM 2894 CG ASP B 96 -35.776 13.350 16.969 1.00 77.39 C ANISOU 2894 CG ASP B 96 6259 9563 13581 -1176 -1167 -218 C ATOM 2895 OD1 ASP B 96 -36.493 12.810 17.838 1.00 78.68 O ANISOU 2895 OD1 ASP B 96 6220 9500 14175 -1140 -942 -107 O ATOM 2896 OD2 ASP B 96 -36.094 13.383 15.764 1.00 80.43 O ANISOU 2896 OD2 ASP B 96 6498 10265 13797 -1429 -1562 -283 O ATOM 2897 N ARG B 97 -34.703 11.633 19.826 1.00 39.70 N ATOM 2898 CA ARG B 97 -34.510 10.188 20.117 1.00 41.35 C ATOM 2899 C ARG B 97 -34.546 9.276 18.859 1.00 41.61 C ATOM 2900 O ARG B 97 -35.513 9.269 18.070 1.00 41.99 O ATOM 2901 CB ARG B 97 -35.534 9.708 21.157 1.00 41.72 C ATOM 2902 CG ARG B 97 -36.159 10.851 21.957 1.00 44.43 C ATOM 2903 CD ARG B 97 -36.594 10.405 23.344 1.00 48.67 C ATOM 2904 NE ARG B 97 -37.213 11.505 24.089 1.00 50.74 N ATOM 2905 CZ ARG B 97 -37.521 11.467 25.385 1.00 51.72 C ATOM 2906 NH1 ARG B 97 -37.267 10.385 26.121 1.00 51.09 N ATOM 2907 NH2 ARG B 97 -38.084 12.528 25.951 1.00 53.09 N TER 2908 ARG B 97 ATOM 2909 N THR C 1 18.272 44.642 33.152 1.00 45.02 N ANISOU 2909 N THR C 1 4845 6449 5810 904 758 -1178 N ATOM 2910 CA THR C 1 18.559 44.122 31.772 1.00 42.47 C ANISOU 2910 CA THR C 1 4639 5939 5557 878 615 -876 C ATOM 2911 C THR C 1 19.014 42.668 31.830 1.00 40.78 C ANISOU 2911 C THR C 1 4537 5868 5089 710 660 -653 C ATOM 2912 O THR C 1 19.234 42.125 32.921 1.00 41.09 O ANISOU 2912 O THR C 1 4587 6120 4906 603 769 -685 O ATOM 2913 CB THR C 1 19.622 44.969 31.045 1.00 41.33 C ANISOU 2913 CB THR C 1 4637 5518 5547 924 447 -806 C ATOM 2914 OG1 THR C 1 20.865 44.878 31.749 1.00 40.19 O ANISOU 2914 OG1 THR C 1 4638 5419 5213 848 478 -808 O ATOM 2915 CG2 THR C 1 19.187 46.425 30.972 1.00 43.27 C ANISOU 2915 CG2 THR C 1 4772 5571 6098 1085 353 -1007 C ATOM 2916 N GLN C 2 19.180 42.053 30.658 1.00 39.13 N ANISOU 2916 N GLN C 2 4404 5541 4923 675 559 -430 N ATOM 2917 CA GLN C 2 19.386 40.597 30.570 1.00 37.81 C ANISOU 2917 CA GLN C 2 4302 5473 4590 536 577 -239 C ATOM 2918 C GLN C 2 20.846 40.130 30.416 1.00 35.78 C ANISOU 2918 C GLN C 2 4222 5137 4236 464 512 -115 C ATOM 2919 O GLN C 2 21.130 38.937 30.466 1.00 35.25 O ANISOU 2919 O GLN C 2 4201 5124 4067 357 508 17 O ATOM 2920 CB GLN C 2 18.505 39.993 29.459 1.00 37.50 C ANISOU 2920 CB GLN C 2 4201 5397 4649 530 525 -110 C ATOM 2921 CG GLN C 2 16.985 40.049 29.722 1.00 39.41 C ANISOU 2921 CG GLN C 2 4247 5770 4956 566 602 -200 C ATOM 2922 CD GLN C 2 16.171 39.598 28.514 1.00 39.84 C ANISOU 2922 CD GLN C 2 4247 5762 5129 563 524 -67 C ATOM 2923 OE1 GLN C 2 16.121 38.411 28.184 1.00 40.04 O ANISOU 2923 OE1 GLN C 2 4310 5834 5068 454 513 83 O ATOM 2924 NE2 GLN C 2 15.541 40.549 27.842 1.00 40.62 N ANISOU 2924 NE2 GLN C 2 4252 5739 5442 677 448 -120 N ATOM 2925 N VAL C 3 21.770 41.058 30.230 1.00 35.01 N ANISOU 2925 N VAL C 3 4209 4902 4193 519 449 -162 N ATOM 2926 CA VAL C 3 23.180 40.697 30.080 1.00 33.41 C ANISOU 2926 CA VAL C 3 4148 4636 3909 456 391 -68 C ATOM 2927 C VAL C 3 24.020 41.646 30.933 1.00 33.77 C ANISOU 2927 C VAL C 3 4253 4662 3916 481 399 -187 C ATOM 2928 O VAL C 3 23.984 42.864 30.724 1.00 34.74 O ANISOU 2928 O VAL C 3 4362 4669 4168 570 353 -287 O ATOM 2929 CB VAL C 3 23.617 40.742 28.592 1.00 32.05 C ANISOU 2929 CB VAL C 3 4024 4321 3833 458 278 38 C ATOM 2930 CG1 VAL C 3 25.121 40.675 28.458 1.00 31.90 C ANISOU 2930 CG1 VAL C 3 4120 4248 3751 411 227 81 C ATOM 2931 CG2 VAL C 3 22.992 39.610 27.828 1.00 31.06 C ANISOU 2931 CG2 VAL C 3 3855 4233 3712 407 271 144 C ATOM 2932 N GLU C 4 24.747 41.091 31.906 1.00 33.28 N ANISOU 2932 N GLU C 4 4251 4703 3691 395 437 -169 N ATOM 2933 CA GLU C 4 25.527 41.905 32.847 1.00 33.55 C ANISOU 2933 CA GLU C 4 4340 4752 3657 396 451 -287 C ATOM 2934 C GLU C 4 27.023 41.560 32.868 1.00 31.95 C ANISOU 2934 C GLU C 4 4263 4493 3385 329 379 -181 C ATOM 2935 O GLU C 4 27.408 40.385 32.962 1.00 31.44 O ANISOU 2935 O GLU C 4 4225 4474 3247 240 359 -45 O ATOM 2936 CB GLU C 4 24.944 41.826 34.254 1.00 35.27 C ANISOU 2936 CB GLU C 4 4485 5198 3718 339 570 -409 C ATOM 2937 CG GLU C 4 23.495 42.319 34.391 1.00 38.83 C ANISOU 2937 CG GLU C 4 4775 5736 4243 416 661 -580 C ATOM 2938 CD GLU C 4 23.367 43.841 34.484 1.00 42.58 C ANISOU 2938 CD GLU C 4 5201 6100 4876 555 652 -824 C ATOM 2939 OE1 GLU C 4 22.858 44.338 35.520 1.00 44.45 O ANISOU 2939 OE1 GLU C 4 5335 6501 5053 565 760 -1062 O ATOM 2940 OE2 GLU C 4 23.765 44.539 33.523 1.00 42.92 O ANISOU 2940 OE2 GLU C 4 5299 5899 5111 643 529 -785 O ATOM 2941 N GLN C 5 27.855 42.600 32.781 1.00 31.00 N ANISOU 2941 N GLN C 5 4206 4259 3313 371 324 -248 N ATOM 2942 CA GLN C 5 29.306 42.448 32.790 1.00 28.95 C ANISOU 2942 CA GLN C 5 4048 3949 3002 314 255 -169 C ATOM 2943 C GLN C 5 29.970 42.930 34.077 1.00 29.22 C ANISOU 2943 C GLN C 5 4132 4055 2915 271 274 -261 C ATOM 2944 O GLN C 5 29.486 43.846 34.758 1.00 30.02 O ANISOU 2944 O GLN C 5 4201 4195 3012 312 324 -437 O ATOM 2945 CB GLN C 5 29.916 43.141 31.581 1.00 28.26 C ANISOU 2945 CB GLN C 5 3998 3701 3039 352 159 -132 C ATOM 2946 CG GLN C 5 29.529 42.483 30.267 1.00 27.83 C ANISOU 2946 CG GLN C 5 3904 3617 3055 349 131 -24 C ATOM 2947 CD GLN C 5 30.280 43.047 29.077 1.00 27.36 C ANISOU 2947 CD GLN C 5 3875 3463 3059 329 36 34 C ATOM 2948 OE1 GLN C 5 29.707 43.745 28.252 1.00 27.82 O ANISOU 2948 OE1 GLN C 5 3903 3451 3216 353 -17 52 O ATOM 2949 NE2 GLN C 5 31.568 42.739 28.982 1.00 27.36 N ANISOU 2949 NE2 GLN C 5 3922 3474 3001 269 5 72 N ATOM 2950 N SER C 6 31.079 42.276 34.403 1.00 28.15 N ANISOU 2950 N SER C 6 4062 3940 2694 185 226 -154 N ATOM 2951 CA SER C 6 31.867 42.577 35.597 1.00 28.94 C ANISOU 2951 CA SER C 6 4217 4119 2660 113 221 -201 C ATOM 2952 C SER C 6 33.352 42.236 35.355 1.00 28.01 C ANISOU 2952 C SER C 6 4170 3920 2554 67 118 -81 C ATOM 2953 O SER C 6 33.653 41.246 34.665 1.00 27.52 O ANISOU 2953 O SER C 6 4091 3811 2556 56 70 45 O ATOM 2954 CB SER C 6 31.335 41.787 36.793 1.00 29.86 C ANISOU 2954 CB SER C 6 4298 4452 2597 -1 283 -175 C ATOM 2955 OG SER C 6 31.792 42.343 38.010 1.00 31.01 O ANISOU 2955 OG SER C 6 4479 4721 2584 -78 301 -273 O ATOM 2956 N PRO C 7 34.285 43.063 35.872 1.00 27.89 N ANISOU 2956 N PRO C 7 4218 3882 2496 46 79 -142 N ATOM 2957 CA PRO C 7 34.091 44.334 36.543 1.00 29.30 C ANISOU 2957 CA PRO C 7 4415 4074 2642 71 112 -329 C ATOM 2958 C PRO C 7 33.590 45.375 35.569 1.00 29.50 C ANISOU 2958 C PRO C 7 4419 3939 2850 189 95 -417 C ATOM 2959 O PRO C 7 33.679 45.190 34.364 1.00 28.35 O ANISOU 2959 O PRO C 7 4266 3690 2816 220 47 -309 O ATOM 2960 CB PRO C 7 35.504 44.721 36.987 1.00 29.60 C ANISOU 2960 CB PRO C 7 4535 4083 2629 8 30 -310 C ATOM 2961 CG PRO C 7 36.346 43.538 36.770 1.00 28.01 C ANISOU 2961 CG PRO C 7 4339 3886 2417 -55 -34 -117 C ATOM 2962 CD PRO C 7 35.708 42.753 35.708 1.00 26.85 C ANISOU 2962 CD PRO C 7 4131 3692 2377 -1 -17 -38 C ATOM 2963 N GLN C 8 33.058 46.465 36.097 1.00 31.59 N ANISOU 2963 N GLN C 8 4663 4188 3151 244 123 -620 N ATOM 2964 CA GLN C 8 32.600 47.569 35.276 1.00 32.40 C ANISOU 2964 CA GLN C 8 4739 4099 3473 352 61 -700 C ATOM 2965 C GLN C 8 33.800 48.167 34.539 1.00 31.61 C ANISOU 2965 C GLN C 8 4720 3835 3455 323 -75 -592 C ATOM 2966 O GLN C 8 33.723 48.432 33.333 1.00 31.09 O ANISOU 2966 O GLN C 8 4644 3640 3528 346 -156 -486 O ATOM 2967 CB GLN C 8 31.937 48.612 36.161 1.00 34.93 C ANISOU 2967 CB GLN C 8 5006 4422 3845 419 101 -981 C ATOM 2968 CG GLN C 8 30.933 49.504 35.458 1.00 38.13 C ANISOU 2968 CG GLN C 8 5325 4648 4516 553 50 -1088 C ATOM 2969 CD GLN C 8 30.763 50.836 36.173 1.00 42.60 C ANISOU 2969 CD GLN C 8 5852 5115 5219 630 17 -1384 C ATOM 2970 OE1 GLN C 8 29.700 51.126 36.727 1.00 45.52 O ANISOU 2970 OE1 GLN C 8 6097 5552 5648 713 104 -1632 O ATOM 2971 NE2 GLN C 8 31.826 51.644 36.186 1.00 43.20 N ANISOU 2971 NE2 GLN C 8 6023 5039 5353 599 -108 -1379 N ATOM 2972 N SER C 9 34.906 48.354 35.268 1.00 31.40 N ANISOU 2972 N SER C 9 4767 3839 3324 251 -104 -607 N ATOM 2973 CA SER C 9 36.181 48.786 34.689 1.00 30.50 C ANISOU 2973 CA SER C 9 4722 3616 3250 194 -225 -493 C ATOM 2974 C SER C 9 37.343 48.299 35.550 1.00 30.45 C ANISOU 2974 C SER C 9 4772 3722 3074 96 -223 -454 C ATOM 2975 O SER C 9 37.175 48.093 36.747 1.00 31.80 O ANISOU 2975 O SER C 9 4949 4023 3110 66 -158 -553 O ATOM 2976 CB SER C 9 36.235 50.301 34.590 1.00 31.36 C ANISOU 2976 CB SER C 9 4854 3535 3527 230 -337 -601 C ATOM 2977 OG SER C 9 36.248 50.863 35.884 1.00 32.89 O ANISOU 2977 OG SER C 9 5065 3763 3667 238 -306 -816 O ATOM 2978 N LEU C 10 38.521 48.134 34.950 1.00 29.44 N ANISOU 2978 N LEU C 10 4673 3563 2948 33 -300 -311 N ATOM 2979 CA LEU C 10 39.710 47.684 35.681 1.00 29.21 C ANISOU 2979 CA LEU C 10 4682 3619 2798 -55 -325 -259 C ATOM 2980 C LEU C 10 41.012 48.261 35.112 1.00 29.14 C ANISOU 2980 C LEU C 10 4702 3534 2836 -117 -434 -182 C ATOM 2981 O LEU C 10 41.068 48.617 33.926 1.00 28.99 O ANISOU 2981 O LEU C 10 4659 3440 2916 -116 -480 -114 O ATOM 2982 CB LEU C 10 39.784 46.156 35.711 1.00 28.35 C ANISOU 2982 CB LEU C 10 4526 3623 2621 -80 -284 -139 C ATOM 2983 CG LEU C 10 40.200 45.384 34.453 1.00 26.65 C ANISOU 2983 CG LEU C 10 4250 3387 2490 -74 -305 -18 C ATOM 2984 CD1 LEU C 10 41.017 44.146 34.800 1.00 26.50 C ANISOU 2984 CD1 LEU C 10 4194 3432 2443 -121 -336 74 C ATOM 2985 CD2 LEU C 10 38.995 44.979 33.671 1.00 26.71 C ANISOU 2985 CD2 LEU C 10 4205 3387 2558 -7 -241 -16 C ATOM 2986 N VAL C 11 42.047 48.347 35.955 1.00 29.23 N ANISOU 2986 N VAL C 11 4757 3588 2762 -192 -481 -182 N ATOM 2987 CA VAL C 11 43.356 48.869 35.535 1.00 29.37 C ANISOU 2987 CA VAL C 11 4790 3558 2810 -267 -583 -110 C ATOM 2988 C VAL C 11 44.458 47.836 35.762 1.00 29.40 C ANISOU 2988 C VAL C 11 4755 3665 2752 -327 -602 -8 C ATOM 2989 O VAL C 11 44.622 47.358 36.883 1.00 30.35 O ANISOU 2989 O VAL C 11 4897 3859 2774 -360 -601 -14 O ATOM 2990 CB VAL C 11 43.729 50.189 36.272 1.00 30.30 C ANISOU 2990 CB VAL C 11 4990 3591 2930 -307 -662 -216 C ATOM 2991 CG1 VAL C 11 45.087 50.667 35.839 1.00 29.40 C ANISOU 2991 CG1 VAL C 11 4886 3445 2841 -404 -773 -119 C ATOM 2992 CG2 VAL C 11 42.709 51.266 35.997 1.00 30.80 C ANISOU 2992 CG2 VAL C 11 5070 3506 3125 -234 -681 -333 C ATOM 2993 N VAL C 12 45.202 47.480 34.711 1.00 28.99 N ANISOU 2993 N VAL C 12 4627 3628 2758 -352 -627 80 N ATOM 2994 CA VAL C 12 46.308 46.522 34.870 1.00 29.11 C ANISOU 2994 CA VAL C 12 4571 3719 2769 -391 -661 147 C ATOM 2995 C VAL C 12 47.622 47.013 34.288 1.00 29.94 C ANISOU 2995 C VAL C 12 4631 3845 2901 -472 -732 185 C ATOM 2996 O VAL C 12 47.643 47.899 33.426 1.00 30.20 O ANISOU 2996 O VAL C 12 4669 3852 2954 -513 -749 195 O ATOM 2997 CB VAL C 12 45.990 45.104 34.305 1.00 28.17 C ANISOU 2997 CB VAL C 12 4345 3645 2715 -331 -610 177 C ATOM 2998 CG1 VAL C 12 44.659 44.581 34.836 1.00 27.39 C ANISOU 2998 CG1 VAL C 12 4282 3541 2584 -272 -545 162 C ATOM 2999 CG2 VAL C 12 46.009 45.095 32.789 1.00 27.80 C ANISOU 2999 CG2 VAL C 12 4209 3623 2731 -325 -575 171 C ATOM 3000 N ARG C 13 48.717 46.437 34.784 1.00 31.03 N ANISOU 3000 N ARG C 13 4715 4033 3043 -511 -788 221 N ATOM 3001 CA ARG C 13 50.058 46.713 34.278 1.00 31.99 C ANISOU 3001 CA ARG C 13 4754 4207 3193 -591 -848 249 C ATOM 3002 C ARG C 13 50.307 45.710 33.169 1.00 31.99 C ANISOU 3002 C ARG C 13 4583 4292 3279 -557 -797 229 C ATOM 3003 O ARG C 13 49.951 44.547 33.302 1.00 31.48 O ANISOU 3003 O ARG C 13 4458 4219 3283 -476 -773 214 O ATOM 3004 CB ARG C 13 51.132 46.526 35.361 1.00 32.66 C ANISOU 3004 CB ARG C 13 4837 4307 3264 -643 -945 285 C ATOM 3005 CG ARG C 13 50.933 47.253 36.684 1.00 34.15 C ANISOU 3005 CG ARG C 13 5181 4449 3345 -687 -994 277 C ATOM 3006 CD ARG C 13 52.246 47.213 37.486 1.00 37.70 C ANISOU 3006 CD ARG C 13 5610 4936 3779 -776 -1111 333 C ATOM 3007 NE ARG C 13 52.109 47.110 38.944 1.00 39.46 N ANISOU 3007 NE ARG C 13 5928 5174 3892 -823 -1164 349 N ATOM 3008 CZ ARG C 13 52.179 45.965 39.626 1.00 41.89 C ANISOU 3008 CZ ARG C 13 6189 5520 4207 -827 -1214 433 C ATOM 3009 NH1 ARG C 13 52.347 44.813 38.996 1.00 43.14 N ANISOU 3009 NH1 ARG C 13 6206 5666 4519 -757 -1221 482 N ATOM 3010 NH2 ARG C 13 52.064 45.958 40.946 1.00 44.99 N ANISOU 3010 NH2 ARG C 13 6669 5966 4458 -915 -1270 465 N ATOM 3011 N GLN C 14 50.934 46.153 32.084 1.00 33.16 N ANISOU 3011 N GLN C 14 4642 4532 3424 -634 -789 223 N ATOM 3012 CA GLN C 14 51.212 45.274 30.954 1.00 34.07 C ANISOU 3012 CA GLN C 14 4570 4775 3599 -620 -724 155 C ATOM 3013 C GLN C 14 51.945 43.996 31.381 1.00 34.67 C ANISOU 3013 C GLN C 14 4504 4859 3811 -548 -755 99 C ATOM 3014 O GLN C 14 52.833 44.036 32.241 1.00 35.34 O ANISOU 3014 O GLN C 14 4586 4917 3924 -573 -847 138 O ATOM 3015 CB GLN C 14 51.980 46.025 29.866 1.00 34.99 C ANISOU 3015 CB GLN C 14 4596 5049 3650 -765 -720 161 C ATOM 3016 CG GLN C 14 53.483 45.793 29.820 1.00 37.52 C ANISOU 3016 CG GLN C 14 4750 5499 4007 -829 -754 119 C ATOM 3017 CD GLN C 14 54.076 46.052 28.434 1.00 40.20 C ANISOU 3017 CD GLN C 14 4920 6082 4271 -973 -698 76 C ATOM 3018 OE1 GLN C 14 53.531 46.829 27.639 1.00 41.56 O ANISOU 3018 OE1 GLN C 14 5151 6310 4331 -1081 -683 148 O ATOM 3019 NE2 GLN C 14 55.194 45.394 28.140 1.00 40.74 N ANISOU 3019 NE2 GLN C 14 4764 6311 4404 -986 -677 -42 N ATOM 3020 N GLY C 15 51.548 42.873 30.784 1.00 34.57 N ANISOU 3020 N GLY C 15 4369 4865 3901 -461 -699 11 N ATOM 3021 CA GLY C 15 52.127 41.573 31.104 1.00 35.24 C ANISOU 3021 CA GLY C 15 4300 4911 4179 -376 -757 -52 C ATOM 3022 C GLY C 15 51.179 40.755 31.954 1.00 35.11 C ANISOU 3022 C GLY C 15 4374 4738 4230 -287 -799 15 C ATOM 3023 O GLY C 15 51.163 39.526 31.879 1.00 35.86 O ANISOU 3023 O GLY C 15 4343 4771 4511 -203 -838 -39 O ATOM 3024 N GLU C 16 50.377 41.440 32.765 1.00 34.51 N ANISOU 3024 N GLU C 16 4502 4601 4008 -314 -798 125 N ATOM 3025 CA GLU C 16 49.467 40.778 33.695 1.00 34.08 C ANISOU 3025 CA GLU C 16 4537 4448 3965 -272 -834 207 C ATOM 3026 C GLU C 16 48.277 40.273 32.927 1.00 33.13 C ANISOU 3026 C GLU C 16 4403 4316 3867 -204 -739 157 C ATOM 3027 O GLU C 16 47.957 40.814 31.872 1.00 32.30 O ANISOU 3027 O GLU C 16 4287 4280 3705 -209 -641 86 O ATOM 3028 CB GLU C 16 49.019 41.741 34.801 1.00 34.03 C ANISOU 3028 CB GLU C 16 4725 4430 3774 -337 -843 291 C ATOM 3029 CG GLU C 16 50.165 42.223 35.688 1.00 35.58 C ANISOU 3029 CG GLU C 16 4947 4639 3932 -420 -951 346 C ATOM 3030 CD GLU C 16 49.779 43.320 36.673 1.00 37.06 C ANISOU 3030 CD GLU C 16 5316 4836 3929 -492 -947 371 C ATOM 3031 OE1 GLU C 16 48.690 43.941 36.526 1.00 35.45 O ANISOU 3031 OE1 GLU C 16 5208 4625 3637 -468 -853 320 O ATOM 3032 OE2 GLU C 16 50.591 43.555 37.603 1.00 38.45 O ANISOU 3032 OE2 GLU C 16 5526 5027 4058 -573 -1048 427 O ATOM 3033 N ASN C 17 47.638 39.229 33.456 1.00 33.38 N ANISOU 3033 N ASN C 17 4433 4266 3982 -161 -786 212 N ATOM 3034 CA ASN C 17 46.421 38.654 32.869 1.00 32.63 C ANISOU 3034 CA ASN C 17 4332 4150 3915 -103 -710 181 C ATOM 3035 C ASN C 17 45.187 39.215 33.537 1.00 32.29 C ANISOU 3035 C ASN C 17 4453 4114 3701 -128 -652 256 C ATOM 3036 O ASN C 17 45.223 39.626 34.708 1.00 32.81 O ANISOU 3036 O ASN C 17 4621 4189 3656 -189 -695 338 O ATOM 3037 CB ASN C 17 46.410 37.137 33.028 1.00 33.05 C ANISOU 3037 CB ASN C 17 4273 4099 4187 -53 -814 201 C ATOM 3038 CG ASN C 17 47.743 36.509 32.703 1.00 34.99 C ANISOU 3038 CG ASN C 17 4333 4310 4652 -18 -911 114 C ATOM 3039 OD1 ASN C 17 48.499 37.012 31.866 1.00 37.64 O ANISOU 3039 OD1 ASN C 17 4579 4745 4976 -18 -846 -18 O ATOM 3040 ND2 ASN C 17 48.048 35.407 33.359 1.00 35.14 N ANISOU 3040 ND2 ASN C 17 4276 4193 4881 0 -1080 189 N ATOM 3041 N CYS C 18 44.085 39.244 32.810 1.00 31.70 N ANISOU 3041 N CYS C 18 4392 4052 3602 -87 -553 213 N ATOM 3042 CA CYS C 18 42.843 39.578 33.468 1.00 32.26 C ANISOU 3042 CA CYS C 18 4578 4132 3549 -96 -500 262 C ATOM 3043 C CYS C 18 41.689 38.691 33.063 1.00 32.03 C ANISOU 3043 C CYS C 18 4510 4081 3578 -51 -459 269 C ATOM 3044 O CYS C 18 41.739 38.025 32.036 1.00 32.02 O ANISOU 3044 O CYS C 18 4407 4059 3701 -6 -452 208 O ATOM 3045 CB CYS C 18 42.498 41.052 33.300 1.00 31.97 C ANISOU 3045 CB CYS C 18 4634 4126 3387 -105 -426 211 C ATOM 3046 SG CYS C 18 42.444 41.582 31.622 1.00 33.61 S ANISOU 3046 SG CYS C 18 4785 4354 3631 -85 -368 141 S ATOM 3047 N VAL C 19 40.668 38.683 33.916 1.00 32.44 N ANISOU 3047 N VAL C 19 4634 4160 3530 -77 -432 330 N ATOM 3048 CA VAL C 19 39.482 37.858 33.766 1.00 32.36 C ANISOU 3048 CA VAL C 19 4597 4144 3553 -60 -402 363 C ATOM 3049 C VAL C 19 38.267 38.772 33.651 1.00 31.83 C ANISOU 3049 C VAL C 19 4589 4136 3370 -35 -279 307 C ATOM 3050 O VAL C 19 38.031 39.606 34.525 1.00 32.27 O ANISOU 3050 O VAL C 19 4716 4253 3293 -68 -245 288 O ATOM 3051 CB VAL C 19 39.318 36.952 34.995 1.00 33.29 C ANISOU 3051 CB VAL C 19 4723 4273 3651 -146 -495 508 C ATOM 3052 CG1 VAL C 19 38.089 36.077 34.862 1.00 33.81 C ANISOU 3052 CG1 VAL C 19 4757 4339 3752 -149 -477 562 C ATOM 3053 CG2 VAL C 19 40.561 36.095 35.174 1.00 35.05 C ANISOU 3053 CG2 VAL C 19 4878 4403 4038 -165 -658 575 C ATOM 3054 N LEU C 20 37.498 38.624 32.579 1.00 31.02 N ANISOU 3054 N LEU C 20 4442 4016 3329 20 -222 264 N ATOM 3055 CA LEU C 20 36.279 39.407 32.428 1.00 30.72 C ANISOU 3055 CA LEU C 20 4435 4013 3226 52 -129 218 C ATOM 3056 C LEU C 20 35.042 38.514 32.444 1.00 31.34 C ANISOU 3056 C LEU C 20 4471 4117 3321 55 -95 261 C ATOM 3057 O LEU C 20 35.027 37.451 31.841 1.00 31.28 O ANISOU 3057 O LEU C 20 4401 4067 3418 60 -133 294 O ATOM 3058 CB LEU C 20 36.339 40.235 31.148 1.00 29.83 C ANISOU 3058 CB LEU C 20 4310 3869 3154 92 -107 157 C ATOM 3059 CG LEU C 20 37.593 41.071 30.886 1.00 28.39 C ANISOU 3059 CG LEU C 20 4153 3672 2963 64 -152 134 C ATOM 3060 CD1 LEU C 20 37.316 42.070 29.799 1.00 27.01 C ANISOU 3060 CD1 LEU C 20 3979 3483 2801 66 -145 114 C ATOM 3061 CD2 LEU C 20 38.053 41.793 32.116 1.00 28.77 C ANISOU 3061 CD2 LEU C 20 4279 3719 2932 38 -174 126 C ATOM 3062 N GLN C 21 33.997 38.937 33.138 1.00 32.65 N ANISOU 3062 N GLN C 21 4656 4358 3393 48 -25 244 N ATOM 3063 CA GLN C 21 32.818 38.079 33.264 1.00 33.89 C ANISOU 3063 CA GLN C 21 4762 4567 3547 27 5 298 C ATOM 3064 C GLN C 21 31.576 38.584 32.551 1.00 33.80 C ANISOU 3064 C GLN C 21 4713 4566 3564 96 89 229 C ATOM 3065 O GLN C 21 31.311 39.791 32.502 1.00 34.03 O ANISOU 3065 O GLN C 21 4759 4591 3580 150 133 130 O ATOM 3066 CB GLN C 21 32.472 37.868 34.723 1.00 35.42 C ANISOU 3066 CB GLN C 21 4968 4897 3592 -74 20 349 C ATOM 3067 CG GLN C 21 33.485 37.092 35.510 1.00 37.79 C ANISOU 3067 CG GLN C 21 5292 5194 3873 -177 -98 477 C ATOM 3068 CD GLN C 21 33.304 37.347 36.979 1.00 42.64 C ANISOU 3068 CD GLN C 21 5935 5990 4278 -304 -74 502 C ATOM 3069 OE1 GLN C 21 34.179 37.925 37.631 1.00 45.14 O ANISOU 3069 OE1 GLN C 21 6306 6334 4511 -342 -103 477 O ATOM 3070 NE2 GLN C 21 32.145 36.947 37.516 1.00 44.14 N ANISOU 3070 NE2 GLN C 21 6079 6331 4360 -386 -16 542 N ATOM 3071 N CYS C 22 30.824 37.632 32.001 1.00 34.04 N ANISOU 3071 N CYS C 22 4684 4590 3658 92 87 286 N ATOM 3072 CA CYS C 22 29.479 37.869 31.485 1.00 34.19 C ANISOU 3072 CA CYS C 22 4651 4639 3701 137 155 250 C ATOM 3073 C CYS C 22 28.489 36.956 32.181 1.00 34.55 C ANISOU 3073 C CYS C 22 4644 4787 3695 67 182 325 C ATOM 3074 O CYS C 22 28.695 35.744 32.256 1.00 34.65 O ANISOU 3074 O CYS C 22 4645 4775 3745 -1 109 437 O ATOM 3075 CB CYS C 22 29.409 37.635 29.986 1.00 33.40 C ANISOU 3075 CB CYS C 22 4518 4458 3714 178 126 250 C ATOM 3076 SG CYS C 22 28.049 38.548 29.233 1.00 35.75 S ANISOU 3076 SG CYS C 22 4766 4762 4055 245 177 200 S ATOM 3077 N ASN C 23 27.432 37.555 32.713 1.00 35.16 N ANISOU 3077 N ASN C 23 4678 4980 3701 77 277 256 N ATOM 3078 CA ASN C 23 26.341 36.813 33.341 1.00 35.91 C ANISOU 3078 CA ASN C 23 4701 5222 3723 -8 322 317 C ATOM 3079 C ASN C 23 25.036 37.265 32.715 1.00 35.27 C ANISOU 3079 C ASN C 23 4531 5162 3707 72 397 236 C ATOM 3080 O ASN C 23 24.743 38.461 32.667 1.00 35.96 O ANISOU 3080 O ASN C 23 4596 5244 3823 167 451 90 O ATOM 3081 CB ASN C 23 26.311 37.041 34.855 1.00 37.69 C ANISOU 3081 CB ASN C 23 4922 5644 3753 -113 379 292 C ATOM 3082 CG ASN C 23 25.988 35.772 35.621 1.00 40.91 C ANISOU 3082 CG ASN C 23 5299 6185 4060 -292 338 474 C ATOM 3083 OD1 ASN C 23 24.890 35.207 35.497 1.00 43.86 O ANISOU 3083 OD1 ASN C 23 5590 6640 4434 -336 370 526 O ATOM 3084 ND2 ASN C 23 26.955 35.298 36.407 1.00 43.04 N ANISOU 3084 ND2 ASN C 23 5631 6471 4253 -411 243 594 N ATOM 3085 N TYR C 24 24.257 36.318 32.215 1.00 34.01 N ANISOU 3085 N TYR C 24 4315 5009 3599 36 380 331 N ATOM 3086 CA TYR C 24 23.050 36.677 31.495 1.00 32.93 C ANISOU 3086 CA TYR C 24 4088 4879 3545 110 429 274 C ATOM 3087 C TYR C 24 21.811 35.908 31.958 1.00 33.26 C ANISOU 3087 C TYR C 24 4024 5083 3530 20 481 335 C ATOM 3088 O TYR C 24 21.922 34.851 32.570 1.00 33.63 O ANISOU 3088 O TYR C 24 4080 5199 3498 -117 443 471 O ATOM 3089 CB TYR C 24 23.293 36.526 29.983 1.00 31.80 C ANISOU 3089 CB TYR C 24 3971 4567 3544 169 349 308 C ATOM 3090 CG TYR C 24 23.653 35.125 29.520 1.00 30.71 C ANISOU 3090 CG TYR C 24 3852 4367 3448 94 265 425 C ATOM 3091 CD1 TYR C 24 22.659 34.233 29.147 1.00 30.12 C ANISOU 3091 CD1 TYR C 24 3707 4318 3419 47 252 496 C ATOM 3092 CD2 TYR C 24 24.983 34.700 29.442 1.00 30.38 C ANISOU 3092 CD2 TYR C 24 3883 4230 3429 75 187 447 C ATOM 3093 CE1 TYR C 24 22.954 32.959 28.725 1.00 30.18 C ANISOU 3093 CE1 TYR C 24 3722 4242 3504 -14 157 576 C ATOM 3094 CE2 TYR C 24 25.298 33.403 29.010 1.00 30.82 C ANISOU 3094 CE2 TYR C 24 3930 4203 3577 25 94 514 C ATOM 3095 CZ TYR C 24 24.261 32.539 28.652 1.00 30.82 C ANISOU 3095 CZ TYR C 24 3865 4213 3633 -19 76 574 C ATOM 3096 OH TYR C 24 24.496 31.248 28.225 1.00 31.07 O ANISOU 3096 OH TYR C 24 3877 4138 3790 -65 -32 619 O ATOM 3097 N SER C 25 20.637 36.452 31.663 1.00 33.02 N ANISOU 3097 N SER C 25 3884 5109 3554 89 551 246 N ATOM 3098 CA SER C 25 19.372 35.735 31.861 1.00 33.61 C ANISOU 3098 CA SER C 25 3838 5336 3598 8 597 305 C ATOM 3099 C SER C 25 18.597 35.435 30.556 1.00 32.68 C ANISOU 3099 C SER C 25 3670 5112 3635 61 548 354 C ATOM 3100 O SER C 25 17.444 35.003 30.611 1.00 33.43 O ANISOU 3100 O SER C 25 3647 5326 3727 11 587 386 O ATOM 3101 CB SER C 25 18.470 36.491 32.839 1.00 35.30 C ANISOU 3101 CB SER C 25 3915 5777 3721 14 740 140 C ATOM 3102 OG SER C 25 18.268 37.823 32.406 1.00 35.12 O ANISOU 3102 OG SER C 25 3848 5656 3839 191 764 -49 O ATOM 3103 N VAL C 26 19.231 35.649 29.402 1.00 30.86 N ANISOU 3103 N VAL C 26 3518 4687 3519 137 461 363 N ATOM 3104 CA VAL C 26 18.576 35.483 28.097 1.00 30.34 C ANISOU 3104 CA VAL C 26 3410 4540 3578 170 405 401 C ATOM 3105 C VAL C 26 18.068 34.055 27.867 1.00 30.70 C ANISOU 3105 C VAL C 26 3427 4613 3626 57 364 530 C ATOM 3106 O VAL C 26 18.658 33.099 28.361 1.00 30.76 O ANISOU 3106 O VAL C 26 3490 4613 3586 -37 323 612 O ATOM 3107 CB VAL C 26 19.509 35.904 26.938 1.00 28.95 C ANISOU 3107 CB VAL C 26 3326 4202 3473 222 317 394 C ATOM 3108 CG1 VAL C 26 18.818 35.738 25.588 1.00 27.75 C ANISOU 3108 CG1 VAL C 26 3125 4005 3412 221 253 440 C ATOM 3109 CG2 VAL C 26 19.961 37.337 27.120 1.00 28.91 C ANISOU 3109 CG2 VAL C 26 3346 4146 3491 318 327 294 C ATOM 3110 N THR C 27 16.965 33.924 27.121 1.00 31.27 N ANISOU 3110 N THR C 27 3406 4701 3774 64 353 552 N ATOM 3111 CA THR C 27 16.332 32.626 26.853 1.00 31.28 C ANISOU 3111 CA THR C 27 3367 4722 3795 -45 306 667 C ATOM 3112 C THR C 27 15.599 32.602 25.519 1.00 30.94 C ANISOU 3112 C THR C 27 3272 4626 3857 -21 251 678 C ATOM 3113 O THR C 27 14.751 33.446 25.271 1.00 31.40 O ANISOU 3113 O THR C 27 3238 4728 3966 47 282 636 O ATOM 3114 CB THR C 27 15.327 32.264 27.952 1.00 32.79 C ANISOU 3114 CB THR C 27 3445 5108 3904 -137 383 716 C ATOM 3115 OG1 THR C 27 15.983 32.326 29.218 1.00 33.16 O ANISOU 3115 OG1 THR C 27 3535 5244 3819 -190 430 714 O ATOM 3116 CG2 THR C 27 14.757 30.862 27.736 1.00 33.02 C ANISOU 3116 CG2 THR C 27 3443 5140 3963 -276 305 865 C ATOM 3117 N PRO C 28 15.927 31.633 24.655 1.00 30.50 N ANISOU 3117 N PRO C 28 3265 4477 3848 -83 157 721 N ATOM 3118 CA PRO C 28 17.031 30.708 24.834 1.00 30.25 C ANISOU 3118 CA PRO C 28 3325 4351 3818 -137 93 737 C ATOM 3119 C PRO C 28 18.343 31.401 24.506 1.00 29.69 C ANISOU 3119 C PRO C 28 3347 4202 3731 -63 88 643 C ATOM 3120 O PRO C 28 18.336 32.522 24.015 1.00 29.64 O ANISOU 3120 O PRO C 28 3341 4206 3713 9 115 591 O ATOM 3121 CB PRO C 28 16.728 29.607 23.824 1.00 30.18 C ANISOU 3121 CB PRO C 28 3296 4271 3901 -205 -2 756 C ATOM 3122 CG PRO C 28 15.922 30.269 22.787 1.00 29.92 C ANISOU 3122 CG PRO C 28 3206 4284 3880 -171 7 730 C ATOM 3123 CD PRO C 28 15.109 31.292 23.479 1.00 30.51 C ANISOU 3123 CD PRO C 28 3208 4465 3920 -111 97 747 C ATOM 3124 N ASP C 29 19.450 30.731 24.797 1.00 30.17 N ANISOU 3124 N ASP C 29 3476 4180 3809 -89 37 634 N ATOM 3125 CA ASP C 29 20.787 31.277 24.646 1.00 29.79 C ANISOU 3125 CA ASP C 29 3504 4073 3741 -34 33 549 C ATOM 3126 C ASP C 29 21.547 30.450 23.630 1.00 29.80 C ANISOU 3126 C ASP C 29 3512 3984 3826 -55 -47 467 C ATOM 3127 O ASP C 29 22.174 29.439 23.971 1.00 30.28 O ANISOU 3127 O ASP C 29 3581 3950 3975 -86 -121 464 O ATOM 3128 CB ASP C 29 21.517 31.268 26.001 1.00 30.27 C ANISOU 3128 CB ASP C 29 3616 4133 3753 -44 44 589 C ATOM 3129 CG ASP C 29 21.430 29.915 26.731 1.00 32.50 C ANISOU 3129 CG ASP C 29 3884 4376 4090 -147 -39 703 C ATOM 3130 OD1 ASP C 29 20.709 29.007 26.267 1.00 34.69 O ANISOU 3130 OD1 ASP C 29 4108 4621 4451 -204 -97 747 O ATOM 3131 OD2 ASP C 29 22.093 29.755 27.782 1.00 35.17 O ANISOU 3131 OD2 ASP C 29 4261 4709 4392 -187 -66 764 O ATOM 3132 N ASN C 30 21.478 30.861 22.371 1.00 29.73 N ANISOU 3132 N ASN C 30 3485 4010 3800 -50 -45 392 N ATOM 3133 CA ASN C 30 22.110 30.084 21.307 1.00 30.25 C ANISOU 3133 CA ASN C 30 3528 4042 3922 -87 -102 265 C ATOM 3134 C ASN C 30 23.629 30.196 21.347 1.00 30.15 C ANISOU 3134 C ASN C 30 3550 3995 3910 -57 -106 156 C ATOM 3135 O ASN C 30 24.334 29.187 21.368 1.00 30.87 O ANISOU 3135 O ASN C 30 3616 3994 4120 -59 -168 64 O ATOM 3136 CB ASN C 30 21.563 30.481 19.929 1.00 30.44 C ANISOU 3136 CB ASN C 30 3513 4168 3886 -133 -101 225 C ATOM 3137 CG ASN C 30 22.279 29.781 18.790 1.00 30.90 C ANISOU 3137 CG ASN C 30 3531 4250 3959 -189 -137 46 C ATOM 3138 OD1 ASN C 30 23.160 30.361 18.153 1.00 32.35 O ANISOU 3138 OD1 ASN C 30 3720 4519 4053 -209 -115 -45 O ATOM 3139 ND2 ASN C 30 21.922 28.532 18.539 1.00 30.00 N ANISOU 3139 ND2 ASN C 30 3365 4073 3961 -224 -195 -19 N ATOM 3140 N HIS C 31 24.124 31.428 21.365 1.00 29.52 N ANISOU 3140 N HIS C 31 3517 3977 3724 -27 -55 163 N ATOM 3141 CA HIS C 31 25.551 31.668 21.291 1.00 29.37 C ANISOU 3141 CA HIS C 31 3520 3955 3686 -12 -53 63 C ATOM 3142 C HIS C 31 25.926 32.947 22.031 1.00 29.02 C ANISOU 3142 C HIS C 31 3547 3924 3556 30 -11 136 C ATOM 3143 O HIS C 31 25.075 33.825 22.230 1.00 29.27 O ANISOU 3143 O HIS C 31 3597 3984 3542 48 15 226 O ATOM 3144 CB HIS C 31 25.965 31.777 19.832 1.00 29.69 C ANISOU 3144 CB HIS C 31 3509 4109 3662 -78 -51 -68 C ATOM 3145 CG HIS C 31 25.491 33.030 19.160 1.00 28.94 C ANISOU 3145 CG HIS C 31 3433 4127 3435 -125 -35 16 C ATOM 3146 ND1 HIS C 31 24.333 33.084 18.416 1.00 29.14 N ANISOU 3146 ND1 HIS C 31 3423 4213 3435 -180 -56 77 N ATOM 3147 CD2 HIS C 31 26.031 34.270 19.106 1.00 27.62 C ANISOU 3147 CD2 HIS C 31 3310 4007 3176 -137 -28 67 C ATOM 3148 CE1 HIS C 31 24.178 34.307 17.938 1.00 28.78 C ANISOU 3148 CE1 HIS C 31 3397 4237 3301 -221 -75 171 C ATOM 3149 NE2 HIS C 31 25.199 35.043 18.334 1.00 27.48 N ANISOU 3149 NE2 HIS C 31 3282 4061 3098 -199 -61 167 N ATOM 3150 N LEU C 32 27.194 33.052 22.424 1.00 28.57 N ANISOU 3150 N LEU C 32 3519 3839 3499 50 -16 81 N ATOM 3151 CA LEU C 32 27.698 34.239 23.099 1.00 28.07 C ANISOU 3151 CA LEU C 32 3525 3780 3359 82 11 130 C ATOM 3152 C LEU C 32 28.935 34.759 22.399 1.00 28.31 C ANISOU 3152 C LEU C 32 3554 3868 3336 50 7 45 C ATOM 3153 O LEU C 32 29.836 33.992 22.055 1.00 29.54 O ANISOU 3153 O LEU C 32 3657 4028 3538 35 -9 -72 O ATOM 3154 CB LEU C 32 28.007 33.925 24.547 1.00 27.95 C ANISOU 3154 CB LEU C 32 3552 3694 3375 115 4 182 C ATOM 3155 CG LEU C 32 28.539 35.065 25.402 1.00 28.13 C ANISOU 3155 CG LEU C 32 3646 3723 3320 144 32 209 C ATOM 3156 CD1 LEU C 32 27.922 35.080 26.787 1.00 27.94 C ANISOU 3156 CD1 LEU C 32 3650 3703 3264 153 58 286 C ATOM 3157 CD2 LEU C 32 30.030 34.912 25.489 1.00 29.54 C ANISOU 3157 CD2 LEU C 32 3836 3873 3515 139 -3 150 C ATOM 3158 N ARG C 33 28.987 36.066 22.190 1.00 27.98 N ANISOU 3158 N ARG C 33 3554 3867 3209 34 12 99 N ATOM 3159 CA ARG C 33 30.061 36.656 21.418 1.00 27.89 C ANISOU 3159 CA ARG C 33 3534 3944 3120 -36 0 51 C ATOM 3160 C ARG C 33 30.716 37.766 22.213 1.00 27.39 C ANISOU 3160 C ARG C 33 3548 3832 3028 -8 -9 106 C ATOM 3161 O ARG C 33 30.027 38.586 22.806 1.00 27.38 O ANISOU 3161 O ARG C 33 3599 3763 3043 38 -16 187 O ATOM 3162 CB ARG C 33 29.489 37.203 20.113 1.00 28.75 C ANISOU 3162 CB ARG C 33 3610 4166 3149 -137 -27 96 C ATOM 3163 CG ARG C 33 30.515 37.760 19.148 1.00 29.57 C ANISOU 3163 CG ARG C 33 3684 4420 3130 -266 -45 66 C ATOM 3164 CD ARG C 33 29.842 38.425 17.992 1.00 30.08 C ANISOU 3164 CD ARG C 33 3728 4595 3105 -397 -104 172 C ATOM 3165 NE ARG C 33 29.184 37.485 17.089 1.00 32.11 N ANISOU 3165 NE ARG C 33 3908 4959 3335 -458 -89 101 N ATOM 3166 CZ ARG C 33 29.813 36.820 16.129 1.00 33.88 C ANISOU 3166 CZ ARG C 33 4041 5375 3458 -572 -55 -55 C ATOM 3167 NH1 ARG C 33 31.120 36.980 15.971 1.00 35.58 N ANISOU 3167 NH1 ARG C 33 4220 5704 3593 -633 -25 -153 N ATOM 3168 NH2 ARG C 33 29.145 35.993 15.333 1.00 33.66 N ANISOU 3168 NH2 ARG C 33 3942 5438 3409 -629 -46 -136 N ATOM 3169 N TRP C 34 32.044 37.776 22.234 1.00 27.26 N ANISOU 3169 N TRP C 34 3525 3850 2984 -36 -11 40 N ATOM 3170 CA TRP C 34 32.803 38.825 22.905 1.00 27.14 C ANISOU 3170 CA TRP C 34 3580 3796 2936 -29 -30 85 C ATOM 3171 C TRP C 34 33.422 39.743 21.872 1.00 27.77 C ANISOU 3171 C TRP C 34 3645 3986 2920 -150 -67 112 C ATOM 3172 O TRP C 34 34.074 39.277 20.935 1.00 28.69 O ANISOU 3172 O TRP C 34 3677 4248 2974 -240 -51 26 O ATOM 3173 CB TRP C 34 33.921 38.229 23.753 1.00 27.13 C ANISOU 3173 CB TRP C 34 3577 3757 2973 9 -25 17 C ATOM 3174 CG TRP C 34 33.483 37.667 25.067 1.00 27.07 C ANISOU 3174 CG TRP C 34 3611 3644 3031 89 -21 52 C ATOM 3175 CD1 TRP C 34 33.091 36.384 25.321 1.00 27.11 C ANISOU 3175 CD1 TRP C 34 3572 3606 3123 116 -29 37 C ATOM 3176 CD2 TRP C 34 33.413 38.364 26.316 1.00 26.55 C ANISOU 3176 CD2 TRP C 34 3630 3520 2936 125 -20 111 C ATOM 3177 NE1 TRP C 34 32.769 36.240 26.649 1.00 27.13 N ANISOU 3177 NE1 TRP C 34 3629 3548 3131 145 -36 114 N ATOM 3178 CE2 TRP C 34 32.961 37.439 27.284 1.00 26.93 C ANISOU 3178 CE2 TRP C 34 3679 3530 3022 151 -19 142 C ATOM 3179 CE3 TRP C 34 33.666 39.682 26.707 1.00 25.78 C ANISOU 3179 CE3 TRP C 34 3602 3405 2787 124 -30 133 C ATOM 3180 CZ2 TRP C 34 32.767 37.788 28.616 1.00 27.14 C ANISOU 3180 CZ2 TRP C 34 3767 3549 2996 160 -7 187 C ATOM 3181 CZ3 TRP C 34 33.473 40.028 28.022 1.00 26.40 C ANISOU 3181 CZ3 TRP C 34 3741 3448 2843 159 -16 144 C ATOM 3182 CH2 TRP C 34 33.028 39.085 28.966 1.00 27.69 C ANISOU 3182 CH2 TRP C 34 3897 3619 3004 170 3 167 C ATOM 3183 N PHE C 35 33.221 41.046 22.037 1.00 27.64 N ANISOU 3183 N PHE C 35 3697 3909 2896 -165 -126 222 N ATOM 3184 CA PHE C 35 33.765 42.025 21.117 1.00 27.91 C ANISOU 3184 CA PHE C 35 3725 4033 2846 -310 -199 301 C ATOM 3185 C PHE C 35 34.802 42.857 21.844 1.00 28.02 C ANISOU 3185 C PHE C 35 3802 3987 2859 -312 -234 319 C ATOM 3186 O PHE C 35 34.711 43.049 23.060 1.00 27.70 O ANISOU 3186 O PHE C 35 3828 3805 2893 -193 -223 299 O ATOM 3187 CB PHE C 35 32.683 43.003 20.699 1.00 28.48 C ANISOU 3187 CB PHE C 35 3824 4033 2964 -338 -296 446 C ATOM 3188 CG PHE C 35 31.770 42.527 19.620 1.00 28.62 C ANISOU 3188 CG PHE C 35 3775 4150 2948 -408 -305 480 C ATOM 3189 CD1 PHE C 35 32.186 42.494 18.301 1.00 29.65 C ANISOU 3189 CD1 PHE C 35 3842 4493 2932 -604 -336 512 C ATOM 3190 CD2 PHE C 35 30.454 42.208 19.909 1.00 28.54 C ANISOU 3190 CD2 PHE C 35 3761 4044 3040 -299 -290 488 C ATOM 3191 CE1 PHE C 35 31.317 42.097 17.280 1.00 29.96 C ANISOU 3191 CE1 PHE C 35 3820 4643 2920 -691 -355 547 C ATOM 3192 CE2 PHE C 35 29.573 41.816 18.893 1.00 29.66 C ANISOU 3192 CE2 PHE C 35 3841 4274 3153 -373 -314 532 C ATOM 3193 CZ PHE C 35 30.009 41.763 17.576 1.00 29.70 C ANISOU 3193 CZ PHE C 35 3792 4486 3007 -570 -350 563 C ATOM 3194 N LYS C 36 35.758 43.386 21.083 1.00 28.81 N ANISOU 3194 N LYS C 36 3872 4216 2858 -467 -280 359 N ATOM 3195 CA LYS C 36 36.671 44.428 21.540 1.00 28.51 C ANISOU 3195 CA LYS C 36 3893 4125 2815 -512 -350 419 C ATOM 3196 C LYS C 36 36.330 45.725 20.808 1.00 29.51 C ANISOU 3196 C LYS C 36 4048 4224 2939 -649 -499 604 C ATOM 3197 O LYS C 36 36.253 45.726 19.582 1.00 30.27 O ANISOU 3197 O LYS C 36 4079 4493 2929 -818 -536 681 O ATOM 3198 CB LYS C 36 38.115 44.029 21.240 1.00 28.48 C ANISOU 3198 CB LYS C 36 3815 4302 2706 -609 -304 335 C ATOM 3199 CG LYS C 36 39.148 45.029 21.733 1.00 29.04 C ANISOU 3199 CG LYS C 36 3939 4331 2765 -666 -375 397 C ATOM 3200 CD LYS C 36 40.518 44.812 21.098 1.00 29.53 C ANISOU 3200 CD LYS C 36 3892 4629 2699 -816 -343 337 C ATOM 3201 CE LYS C 36 41.498 45.914 21.496 1.00 29.67 C ANISOU 3201 CE LYS C 36 3963 4612 2699 -904 -434 431 C ATOM 3202 NZ LYS C 36 42.899 45.576 21.105 1.00 31.10 N ANISOU 3202 NZ LYS C 36 4018 5027 2771 -1021 -382 340 N ATOM 3203 N GLN C 37 36.125 46.811 21.562 1.00 29.65 N ANISOU 3203 N GLN C 37 4155 4028 3084 -586 -599 672 N ATOM 3204 CA GLN C 37 35.887 48.155 20.998 1.00 30.79 C ANISOU 3204 CA GLN C 37 4327 4078 3293 -709 -793 862 C ATOM 3205 C GLN C 37 36.853 49.223 21.530 1.00 32.02 C ANISOU 3205 C GLN C 37 4548 4128 3489 -760 -898 912 C ATOM 3206 O GLN C 37 36.765 49.639 22.685 1.00 31.61 O ANISOU 3206 O GLN C 37 4564 3879 3568 -609 -902 826 O ATOM 3207 CB GLN C 37 34.440 48.605 21.237 1.00 30.60 C ANISOU 3207 CB GLN C 37 4322 3840 3465 -580 -867 895 C ATOM 3208 CG GLN C 37 34.086 49.968 20.636 1.00 31.05 C ANISOU 3208 CG GLN C 37 4392 3748 3657 -694 -1113 1102 C ATOM 3209 CD GLN C 37 32.683 50.457 20.989 1.00 29.99 C ANISOU 3209 CD GLN C 37 4250 3369 3777 -532 -1197 1093 C ATOM 3210 OE1 GLN C 37 32.143 50.143 22.044 1.00 28.99 O ANISOU 3210 OE1 GLN C 37 4130 3146 3739 -321 -1077 907 O ATOM 3211 NE2 GLN C 37 32.095 51.242 20.102 1.00 30.95 N ANISOU 3211 NE2 GLN C 37 4342 3402 4017 -645 -1415 1297 N ATOM 3212 N ASP C 38 37.768 49.665 20.671 1.00 34.05 N ANISOU 3212 N ASP C 38 4776 4541 3620 -993 -984 1045 N ATOM 3213 CA ASP C 38 38.599 50.839 20.936 1.00 35.91 C ANISOU 3213 CA ASP C 38 5069 4673 3904 -1095 -1136 1152 C ATOM 3214 C ASP C 38 37.737 52.091 21.010 1.00 37.74 C ANISOU 3214 C ASP C 38 5358 4608 4374 -1075 -1361 1291 C ATOM 3215 O ASP C 38 36.714 52.224 20.318 1.00 38.08 O ANISOU 3215 O ASP C 38 5371 4608 4490 -1101 -1452 1402 O ATOM 3216 CB ASP C 38 39.663 51.035 19.847 1.00 37.47 C ANISOU 3216 CB ASP C 38 5198 5144 3893 -1395 -1191 1295 C ATOM 3217 CG ASP C 38 40.535 49.811 19.644 1.00 37.79 C ANISOU 3217 CG ASP C 38 5140 5490 3729 -1417 -978 1122 C ATOM 3218 OD1 ASP C 38 40.929 49.181 20.643 1.00 38.26 O ANISOU 3218 OD1 ASP C 38 5215 5494 3828 -1233 -847 935 O ATOM 3219 OD2 ASP C 38 40.827 49.471 18.478 1.00 40.06 O ANISOU 3219 OD2 ASP C 38 5320 6081 3821 -1627 -951 1164 O ATOM 3220 N THR C 39 38.170 53.015 21.854 1.00 39.03 N ANISOU 3220 N THR C 39 5595 4556 4678 -1028 -1464 1275 N ATOM 3221 CA THR C 39 37.460 54.261 22.066 1.00 41.25 C ANISOU 3221 CA THR C 39 5919 4508 5247 -983 -1696 1356 C ATOM 3222 C THR C 39 37.139 54.950 20.734 1.00 43.67 C ANISOU 3222 C THR C 39 6187 4814 5592 -1221 -1942 1660 C ATOM 3223 O THR C 39 38.015 55.121 19.870 1.00 44.37 O ANISOU 3223 O THR C 39 6253 5110 5494 -1499 -2018 1855 O ATOM 3224 CB THR C 39 38.281 55.207 22.927 1.00 42.01 C ANISOU 3224 CB THR C 39 6089 4418 5454 -976 -1801 1318 C ATOM 3225 OG1 THR C 39 39.470 55.545 22.206 1.00 42.39 O ANISOU 3225 OG1 THR C 39 6133 4632 5343 -1253 -1898 1516 O ATOM 3226 CG2 THR C 39 38.631 54.538 24.286 1.00 40.32 C ANISOU 3226 CG2 THR C 39 5913 4229 5176 -772 -1573 1036 C ATOM 3227 N GLY C 40 35.868 55.325 20.594 1.00 44.87 N ANISOU 3227 N GLY C 40 6318 4750 5982 -1121 -2070 1701 N ATOM 3228 CA GLY C 40 35.353 55.953 19.394 1.00 47.32 C ANISOU 3228 CA GLY C 40 6586 5023 6370 -1331 -2334 2005 C ATOM 3229 C GLY C 40 35.647 55.140 18.152 1.00 47.35 C ANISOU 3229 C GLY C 40 6529 5432 6030 -1582 -2249 2151 C ATOM 3230 O GLY C 40 36.244 55.648 17.197 1.00 49.48 O ANISOU 3230 O GLY C 40 6781 5848 6172 -1902 -2424 2421 O ATOM 3231 N LYS C 41 35.235 53.877 18.169 1.00 45.08 N ANISOU 3231 N LYS C 41 6200 5339 5588 -1455 -1986 1964 N ATOM 3232 CA LYS C 41 35.574 52.946 17.112 1.00 44.42 C ANISOU 3232 CA LYS C 41 6045 5659 5174 -1659 -1857 2006 C ATOM 3233 C LYS C 41 34.533 51.836 17.047 1.00 42.82 C ANISOU 3233 C LYS C 41 5795 5523 4950 -1492 -1680 1854 C ATOM 3234 O LYS C 41 33.436 51.952 17.592 1.00 42.58 O ANISOU 3234 O LYS C 41 5778 5242 5160 -1274 -1707 1793 O ATOM 3235 CB LYS C 41 36.960 52.347 17.351 1.00 43.76 C ANISOU 3235 CB LYS C 41 5950 5829 4847 -1712 -1659 1859 C ATOM 3236 CG LYS C 41 38.135 53.272 17.116 1.00 45.98 C ANISOU 3236 CG LYS C 41 6247 6167 5056 -1960 -1813 2034 C ATOM 3237 CD LYS C 41 38.529 53.276 15.649 1.00 49.78 C ANISOU 3237 CD LYS C 41 6637 7022 5257 -2342 -1887 2253 C ATOM 3238 CE LYS C 41 39.874 53.973 15.443 1.00 52.19 C ANISOU 3238 CE LYS C 41 6932 7473 5423 -2611 -1983 2394 C ATOM 3239 NZ LYS C 41 40.314 53.890 14.026 1.00 53.82 N ANISOU 3239 NZ LYS C 41 7025 8128 5298 -3015 -2020 2580 N ATOM 3240 N GLY C 42 34.885 50.752 16.378 1.00 41.73 N ANISOU 3240 N GLY C 42 5589 5732 4533 -1599 -1500 1774 N ATOM 3241 CA GLY C 42 33.900 49.780 15.984 1.00 40.66 C ANISOU 3241 CA GLY C 42 5399 5691 4359 -1525 -1389 1691 C ATOM 3242 C GLY C 42 34.057 48.490 16.723 1.00 38.39 C ANISOU 3242 C GLY C 42 5101 5467 4020 -1308 -1113 1391 C ATOM 3243 O GLY C 42 35.001 48.313 17.488 1.00 38.05 O ANISOU 3243 O GLY C 42 5084 5421 3951 -1230 -1008 1253 O ATOM 3244 N LEU C 43 33.131 47.584 16.458 1.00 37.37 N ANISOU 3244 N LEU C 43 4925 5392 3880 -1229 -1019 1310 N ATOM 3245 CA LEU C 43 33.053 46.323 17.137 1.00 35.25 C ANISOU 3245 CA LEU C 43 4643 5143 3607 -1027 -799 1060 C ATOM 3246 C LEU C 43 33.850 45.259 16.398 1.00 34.97 C ANISOU 3246 C LEU C 43 4517 5429 3342 -1154 -659 922 C ATOM 3247 O LEU C 43 33.412 44.755 15.368 1.00 36.01 O ANISOU 3247 O LEU C 43 4575 5756 3353 -1283 -649 930 O ATOM 3248 CB LEU C 43 31.588 45.909 17.202 1.00 35.17 C ANISOU 3248 CB LEU C 43 4619 5020 3724 -890 -790 1050 C ATOM 3249 CG LEU C 43 30.611 47.005 17.640 1.00 36.65 C ANISOU 3249 CG LEU C 43 4845 4921 4158 -789 -953 1177 C ATOM 3250 CD1 LEU C 43 29.173 46.615 17.298 1.00 36.89 C ANISOU 3250 CD1 LEU C 43 4823 4916 4277 -726 -968 1204 C ATOM 3251 CD2 LEU C 43 30.763 47.300 19.134 1.00 35.86 C ANISOU 3251 CD2 LEU C 43 4809 4601 4214 -565 -892 1038 C ATOM 3252 N VAL C 44 35.017 44.914 16.927 1.00 33.89 N ANISOU 3252 N VAL C 44 4372 5349 3156 -1117 -554 775 N ATOM 3253 CA VAL C 44 35.817 43.811 16.398 1.00 33.22 C ANISOU 3253 CA VAL C 44 4173 5535 2915 -1184 -410 574 C ATOM 3254 C VAL C 44 35.527 42.542 17.197 1.00 31.65 C ANISOU 3254 C VAL C 44 3964 5222 2840 -946 -274 362 C ATOM 3255 O VAL C 44 35.757 42.500 18.406 1.00 30.39 O ANISOU 3255 O VAL C 44 3870 4867 2808 -772 -247 318 O ATOM 3256 CB VAL C 44 37.314 44.140 16.472 1.00 33.81 C ANISOU 3256 CB VAL C 44 4213 5741 2891 -1288 -392 533 C ATOM 3257 CG1 VAL C 44 38.161 42.963 16.017 1.00 33.07 C ANISOU 3257 CG1 VAL C 44 3968 5910 2686 -1321 -238 270 C ATOM 3258 CG2 VAL C 44 37.610 45.388 15.650 1.00 35.42 C ANISOU 3258 CG2 VAL C 44 4422 6072 2963 -1564 -549 776 C ATOM 3259 N SER C 45 35.004 41.520 16.515 1.00 31.57 N ANISOU 3259 N SER C 45 3870 5337 2789 -960 -206 245 N ATOM 3260 CA SER C 45 34.698 40.223 17.143 1.00 29.88 C ANISOU 3260 CA SER C 45 3632 5015 2705 -767 -107 61 C ATOM 3261 C SER C 45 35.959 39.462 17.533 1.00 29.55 C ANISOU 3261 C SER C 45 3516 5020 2692 -711 -25 -147 C ATOM 3262 O SER C 45 36.875 39.296 16.723 1.00 30.20 O ANISOU 3262 O SER C 45 3479 5346 2648 -848 15 -274 O ATOM 3263 CB SER C 45 33.848 39.358 16.207 1.00 30.44 C ANISOU 3263 CB SER C 45 3624 5207 2734 -818 -77 -16 C ATOM 3264 OG SER C 45 33.671 38.047 16.721 1.00 29.35 O ANISOU 3264 OG SER C 45 3450 4967 2736 -658 -4 -195 O ATOM 3265 N LEU C 46 35.990 38.992 18.777 1.00 28.28 N ANISOU 3265 N LEU C 46 3410 4640 2697 -520 -9 -184 N ATOM 3266 CA LEU C 46 37.142 38.245 19.290 1.00 28.05 C ANISOU 3266 CA LEU C 46 3309 4601 2748 -449 31 -355 C ATOM 3267 C LEU C 46 36.928 36.758 19.173 1.00 28.04 C ANISOU 3267 C LEU C 46 3207 4571 2875 -363 68 -547 C ATOM 3268 O LEU C 46 37.833 36.031 18.769 1.00 29.06 O ANISOU 3268 O LEU C 46 3192 4808 3041 -374 103 -765 O ATOM 3269 CB LEU C 46 37.449 38.609 20.749 1.00 26.87 C ANISOU 3269 CB LEU C 46 3272 4240 2699 -325 -3 -264 C ATOM 3270 CG LEU C 46 37.826 40.065 21.033 1.00 26.91 C ANISOU 3270 CG LEU C 46 3373 4231 2620 -391 -56 -108 C ATOM 3271 CD1 LEU C 46 38.112 40.271 22.513 1.00 26.06 C ANISOU 3271 CD1 LEU C 46 3364 3934 2604 -271 -80 -64 C ATOM 3272 CD2 LEU C 46 39.018 40.506 20.174 1.00 27.67 C ANISOU 3272 CD2 LEU C 46 3379 4552 2584 -558 -53 -152 C ATOM 3273 N THR C 47 35.722 36.319 19.519 1.00 27.27 N ANISOU 3273 N THR C 47 3171 4328 2863 -279 52 -477 N ATOM 3274 CA THR C 47 35.391 34.898 19.577 1.00 27.63 C ANISOU 3274 CA THR C 47 3141 4288 3069 -194 54 -620 C ATOM 3275 C THR C 47 33.897 34.704 19.776 1.00 26.72 C ANISOU 3275 C THR C 47 3100 4063 2988 -154 36 -492 C ATOM 3276 O THR C 47 33.198 35.607 20.238 1.00 26.22 O ANISOU 3276 O THR C 47 3148 3943 2871 -144 24 -305 O ATOM 3277 CB THR C 47 36.171 34.164 20.712 1.00 27.56 C ANISOU 3277 CB THR C 47 3117 4099 3254 -70 12 -674 C ATOM 3278 OG1 THR C 47 36.324 32.789 20.371 1.00 29.81 O ANISOU 3278 OG1 THR C 47 3266 4344 3717 -23 -8 -883 O ATOM 3279 CG2 THR C 47 35.467 34.266 22.037 1.00 25.82 C ANISOU 3279 CG2 THR C 47 3033 3681 3095 13 -31 -475 C ATOM 3280 N VAL C 48 33.410 33.523 19.429 1.00 26.86 N ANISOU 3280 N VAL C 48 3042 4050 3114 -128 30 -610 N ATOM 3281 CA VAL C 48 32.005 33.222 19.605 1.00 26.13 C ANISOU 3281 CA VAL C 48 3001 3865 3061 -101 11 -495 C ATOM 3282 C VAL C 48 31.898 31.813 20.172 1.00 26.36 C ANISOU 3282 C VAL C 48 2984 3723 3308 -16 -41 -571 C ATOM 3283 O VAL C 48 32.510 30.889 19.643 1.00 28.07 O ANISOU 3283 O VAL C 48 3079 3947 3638 -12 -58 -787 O ATOM 3284 CB VAL C 48 31.208 33.429 18.280 1.00 26.45 C ANISOU 3284 CB VAL C 48 3002 4076 2970 -216 32 -508 C ATOM 3285 CG1 VAL C 48 31.788 32.620 17.152 1.00 27.40 C ANISOU 3285 CG1 VAL C 48 2976 4355 3078 -291 57 -770 C ATOM 3286 CG2 VAL C 48 29.745 33.094 18.473 1.00 27.02 C ANISOU 3286 CG2 VAL C 48 3114 4054 3100 -184 8 -391 C ATOM 3287 N LEU C 49 31.158 31.650 21.263 1.00 25.18 N ANISOU 3287 N LEU C 49 2916 3423 3227 39 -77 -400 N ATOM 3288 CA LEU C 49 31.037 30.346 21.911 1.00 25.59 C ANISOU 3288 CA LEU C 49 2933 3300 3489 87 -164 -409 C ATOM 3289 C LEU C 49 29.639 29.802 21.697 1.00 25.79 C ANISOU 3289 C LEU C 49 2959 3299 3542 62 -179 -341 C ATOM 3290 O LEU C 49 28.663 30.526 21.884 1.00 25.22 O ANISOU 3290 O LEU C 49 2955 3281 3346 44 -132 -190 O ATOM 3291 CB LEU C 49 31.309 30.498 23.393 1.00 25.26 C ANISOU 3291 CB LEU C 49 2974 3146 3479 124 -208 -244 C ATOM 3292 CG LEU C 49 32.660 31.144 23.672 1.00 25.70 C ANISOU 3292 CG LEU C 49 3039 3230 3496 142 -198 -290 C ATOM 3293 CD1 LEU C 49 32.462 32.431 24.439 1.00 25.13 C ANISOU 3293 CD1 LEU C 49 3088 3209 3251 136 -143 -132 C ATOM 3294 CD2 LEU C 49 33.611 30.192 24.401 1.00 27.08 C ANISOU 3294 CD2 LEU C 49 3160 3248 3882 183 -317 -322 C ATOM 3295 N VAL C 50 29.529 28.530 21.313 1.00 27.13 N ANISOU 3295 N VAL C 50 3039 3375 3894 63 -254 -462 N ATOM 3296 CA VAL C 50 28.240 27.981 20.855 1.00 27.34 C ANISOU 3296 CA VAL C 50 3049 3396 3942 21 -271 -428 C ATOM 3297 C VAL C 50 27.655 26.823 21.656 1.00 29.00 C ANISOU 3297 C VAL C 50 3253 3413 4351 23 -393 -319 C ATOM 3298 O VAL C 50 26.442 26.669 21.684 1.00 29.15 O ANISOU 3298 O VAL C 50 3291 3444 4340 -20 -393 -197 O ATOM 3299 CB VAL C 50 28.246 27.594 19.337 1.00 27.64 C ANISOU 3299 CB VAL C 50 2981 3549 3971 -25 -247 -673 C ATOM 3300 CG1 VAL C 50 28.598 28.780 18.486 1.00 26.77 C ANISOU 3300 CG1 VAL C 50 2878 3673 3621 -83 -142 -718 C ATOM 3301 CG2 VAL C 50 29.173 26.438 19.055 1.00 28.26 C ANISOU 3301 CG2 VAL C 50 2934 3517 4286 13 -327 -934 C ATOM 3302 N ASP C 51 28.502 26.014 22.288 1.00 31.17 N ANISOU 3302 N ASP C 51 3492 3511 4839 59 -513 -348 N ATOM 3303 CA ASP C 51 28.071 24.756 22.907 1.00 33.68 C ANISOU 3303 CA ASP C 51 3784 3618 5394 33 -682 -246 C ATOM 3304 C ASP C 51 27.750 24.896 24.384 1.00 34.13 C ANISOU 3304 C ASP C 51 3932 3637 5400 -15 -730 56 C ATOM 3305 O ASP C 51 28.165 25.865 25.015 1.00 33.69 O ANISOU 3305 O ASP C 51 3948 3680 5174 -2 -648 137 O ATOM 3306 CB ASP C 51 29.144 23.696 22.725 1.00 35.68 C ANISOU 3306 CB ASP C 51 3922 3669 5964 89 -833 -448 C ATOM 3307 CG ASP C 51 29.312 23.281 21.279 1.00 38.08 C ANISOU 3307 CG ASP C 51 4102 4020 6346 115 -799 -790 C ATOM 3308 OD1 ASP C 51 28.342 23.443 20.492 1.00 38.96 O ANISOU 3308 OD1 ASP C 51 4223 4266 6315 61 -716 -814 O ATOM 3309 OD2 ASP C 51 30.416 22.788 20.938 1.00 40.57 O ANISOU 3309 OD2 ASP C 51 4296 4252 6865 183 -857 -1048 O ATOM 3310 N GLN C 52 27.026 23.916 24.930 1.00 35.96 N ANISOU 3310 N GLN C 52 4153 3738 5772 -90 -870 220 N ATOM 3311 CA GLN C 52 26.571 23.934 26.330 1.00 36.80 C ANISOU 3311 CA GLN C 52 4327 3860 5795 -189 -921 525 C ATOM 3312 C GLN C 52 27.700 24.300 27.307 1.00 36.74 C ANISOU 3312 C GLN C 52 4362 3829 5767 -178 -961 598 C ATOM 3313 O GLN C 52 27.569 25.215 28.120 1.00 35.93 O ANISOU 3313 O GLN C 52 4337 3890 5425 -213 -856 725 O ATOM 3314 CB GLN C 52 25.928 22.590 26.694 1.00 38.75 C ANISOU 3314 CB GLN C 52 4531 3932 6259 -298 -1127 686 C ATOM 3315 CG GLN C 52 24.889 22.646 27.827 1.00 41.20 C ANISOU 3315 CG GLN C 52 4891 4370 6395 -454 -1127 999 C ATOM 3316 CD GLN C 52 23.564 23.351 27.447 1.00 43.14 C ANISOU 3316 CD GLN C 52 5145 4845 6403 -470 -931 1003 C ATOM 3317 OE1 GLN C 52 23.125 23.352 26.284 1.00 41.91 O ANISOU 3317 OE1 GLN C 52 4951 4693 6278 -409 -870 836 O ATOM 3318 NE2 GLN C 52 22.922 23.945 28.450 1.00 44.41 N ANISOU 3318 NE2 GLN C 52 5339 5208 6328 -560 -838 1185 N ATOM 3319 N LYS C 53 28.812 23.587 27.209 1.00 38.02 N ANISOU 3319 N LYS C 53 4460 3789 6196 -127 -1118 496 N ATOM 3320 CA LYS C 53 30.022 23.967 27.909 1.00 38.41 C ANISOU 3320 CA LYS C 53 4532 3814 6247 -98 -1156 520 C ATOM 3321 C LYS C 53 31.070 24.090 26.836 1.00 38.26 C ANISOU 3321 C LYS C 53 4428 3762 6346 36 -1111 197 C ATOM 3322 O LYS C 53 31.480 23.092 26.258 1.00 40.31 O ANISOU 3322 O LYS C 53 4570 3833 6913 87 -1247 26 O ATOM 3323 CB LYS C 53 30.421 22.932 28.968 1.00 40.36 C ANISOU 3323 CB LYS C 53 4757 3845 6734 -186 -1431 738 C ATOM 3324 CG LYS C 53 29.329 22.656 29.983 1.00 42.01 C ANISOU 3324 CG LYS C 53 5026 4120 6815 -369 -1493 1069 C ATOM 3325 CD LYS C 53 29.889 22.359 31.356 1.00 46.66 C ANISOU 3325 CD LYS C 53 5646 4652 7432 -501 -1687 1348 C ATOM 3326 CE LYS C 53 28.845 21.669 32.243 1.00 49.49 C ANISOU 3326 CE LYS C 53 6021 5040 7742 -726 -1823 1685 C ATOM 3327 NZ LYS C 53 27.577 22.449 32.347 1.00 48.54 N ANISOU 3327 NZ LYS C 53 5953 5232 7258 -791 -1575 1724 N ATOM 3328 N ASP C 54 31.477 25.319 26.551 1.00 36.78 N ANISOU 3328 N ASP C 54 4288 3769 5919 83 -921 103 N ATOM 3329 CA ASP C 54 32.336 25.599 25.412 1.00 36.68 C ANISOU 3329 CA ASP C 54 4190 3813 5935 173 -837 -198 C ATOM 3330 C ASP C 54 33.579 26.348 25.837 1.00 36.34 C ANISOU 3330 C ASP C 54 4162 3817 5827 209 -808 -220 C ATOM 3331 O ASP C 54 33.559 27.090 26.817 1.00 35.72 O ANISOU 3331 O ASP C 54 4196 3804 5572 168 -778 -21 O ATOM 3332 CB ASP C 54 31.577 26.407 24.351 1.00 35.27 C ANISOU 3332 CB ASP C 54 4036 3849 5515 163 -644 -295 C ATOM 3333 CG ASP C 54 32.119 26.182 22.942 1.00 36.20 C ANISOU 3333 CG ASP C 54 4025 4030 5700 202 -596 -621 C ATOM 3334 OD1 ASP C 54 33.207 25.571 22.800 1.00 38.56 O ANISOU 3334 OD1 ASP C 54 4205 4226 6219 260 -680 -813 O ATOM 3335 OD2 ASP C 54 31.453 26.610 21.972 1.00 34.44 O ANISOU 3335 OD2 ASP C 54 3804 3974 5309 165 -479 -695 O ATOM 3336 N LYS C 55 34.663 26.133 25.094 1.00 37.22 N ANISOU 3336 N LYS C 55 4146 3911 6085 281 -817 -485 N ATOM 3337 CA LYS C 55 35.935 26.835 25.312 1.00 36.93 C ANISOU 3337 CA LYS C 55 4095 3939 5996 314 -783 -544 C ATOM 3338 C LYS C 55 36.504 27.229 23.962 1.00 36.50 C ANISOU 3338 C LYS C 55 3932 4067 5870 341 -644 -850 C ATOM 3339 O LYS C 55 36.499 26.429 23.035 1.00 37.97 O ANISOU 3339 O LYS C 55 3977 4231 6219 369 -661 -1097 O ATOM 3340 CB LYS C 55 36.937 25.956 26.075 1.00 38.63 C ANISOU 3340 CB LYS C 55 4223 3923 6533 357 -998 -529 C ATOM 3341 CG LYS C 55 36.378 25.362 27.360 1.00 41.05 C ANISOU 3341 CG LYS C 55 4615 4054 6927 286 -1179 -207 C ATOM 3342 CD LYS C 55 37.436 24.711 28.235 1.00 45.69 C ANISOU 3342 CD LYS C 55 5134 4428 7798 299 -1416 -125 C ATOM 3343 CE LYS C 55 36.778 23.906 29.363 1.00 48.89 C ANISOU 3343 CE LYS C 55 5602 4662 8313 186 -1635 209 C ATOM 3344 NZ LYS C 55 36.051 22.672 28.861 1.00 51.86 N ANISOU 3344 NZ LYS C 55 5893 4840 8973 189 -1776 162 N ATOM 3345 N THR C 56 36.970 28.464 23.846 1.00 34.93 N ANISOU 3345 N THR C 56 3791 4063 5419 312 -512 -836 N ATOM 3346 CA THR C 56 37.554 28.955 22.605 1.00 35.12 C ANISOU 3346 CA THR C 56 3713 4310 5321 289 -383 -1084 C ATOM 3347 C THR C 56 38.828 29.741 22.905 1.00 35.06 C ANISOU 3347 C THR C 56 3692 4387 5244 287 -357 -1098 C ATOM 3348 O THR C 56 39.023 30.215 24.029 1.00 34.70 O ANISOU 3348 O THR C 56 3764 4260 5162 291 -406 -882 O ATOM 3349 CB THR C 56 36.574 29.889 21.852 1.00 33.92 C ANISOU 3349 CB THR C 56 3654 4364 4869 200 -243 -1014 C ATOM 3350 OG1 THR C 56 36.201 30.995 22.691 1.00 33.42 O ANISOU 3350 OG1 THR C 56 3767 4311 4620 175 -214 -747 O ATOM 3351 CG2 THR C 56 35.318 29.153 21.422 1.00 33.73 C ANISOU 3351 CG2 THR C 56 3629 4288 4899 191 -260 -1016 C ATOM 3352 N SER C 57 39.698 29.879 21.912 1.00 35.86 N ANISOU 3352 N SER C 57 3641 4675 5311 264 -279 -1358 N ATOM 3353 CA SER C 57 40.845 30.777 22.034 1.00 35.73 C ANISOU 3353 CA SER C 57 3609 4791 5177 231 -233 -1365 C ATOM 3354 C SER C 57 41.204 31.489 20.734 1.00 36.20 C ANISOU 3354 C SER C 57 3578 5180 4995 114 -87 -1535 C ATOM 3355 O SER C 57 40.851 31.060 19.650 1.00 37.37 O ANISOU 3355 O SER C 57 3618 5469 5111 69 -24 -1735 O ATOM 3356 CB SER C 57 42.060 30.045 22.591 1.00 36.94 C ANISOU 3356 CB SER C 57 3616 4797 5622 325 -351 -1491 C ATOM 3357 OG SER C 57 42.466 29.035 21.707 1.00 39.09 O ANISOU 3357 OG SER C 57 3651 5090 6112 375 -357 -1843 O ATOM 3358 N ASN C 58 41.912 32.596 20.861 1.00 36.05 N ANISOU 3358 N ASN C 58 3606 5297 4793 41 -43 -1442 N ATOM 3359 CA ASN C 58 42.287 33.408 19.724 1.00 36.86 C ANISOU 3359 CA ASN C 58 3639 5731 4635 -115 71 -1533 C ATOM 3360 C ASN C 58 43.479 34.260 20.133 1.00 36.93 C ANISOU 3360 C ASN C 58 3643 5817 4570 -160 70 -1476 C ATOM 3361 O ASN C 58 43.317 35.281 20.801 1.00 35.55 O ANISOU 3361 O ASN C 58 3653 5580 4275 -192 43 -1212 O ATOM 3362 CB ASN C 58 41.105 34.275 19.293 1.00 35.66 C ANISOU 3362 CB ASN C 58 3650 5661 4237 -224 111 -1319 C ATOM 3363 CG ASN C 58 41.425 35.164 18.116 1.00 37.10 C ANISOU 3363 CG ASN C 58 3772 6187 4136 -430 193 -1349 C ATOM 3364 OD1 ASN C 58 42.548 35.171 17.600 1.00 38.98 O ANISOU 3364 OD1 ASN C 58 3842 6645 4324 -507 244 -1541 O ATOM 3365 ND2 ASN C 58 40.432 35.937 17.684 1.00 37.28 N ANISOU 3365 ND2 ASN C 58 3921 6269 3973 -536 193 -1147 N ATOM 3366 N GLY C 59 44.673 33.815 19.745 1.00 38.77 N ANISOU 3366 N GLY C 59 3651 6183 4896 -158 96 -1746 N ATOM 3367 CA GLY C 59 45.913 34.424 20.216 1.00 39.12 C ANISOU 3367 CA GLY C 59 3658 6280 4925 -183 79 -1717 C ATOM 3368 C GLY C 59 45.941 34.499 21.732 1.00 37.93 C ANISOU 3368 C GLY C 59 3674 5814 4925 -64 -47 -1478 C ATOM 3369 O GLY C 59 45.988 33.483 22.412 1.00 38.47 O ANISOU 3369 O GLY C 59 3698 5644 5276 77 -149 -1524 O ATOM 3370 N ARG C 60 45.874 35.709 22.267 1.00 36.66 N ANISOU 3370 N ARG C 60 3704 5651 4576 -138 -57 -1217 N ATOM 3371 CA ARG C 60 46.060 35.912 23.700 1.00 35.71 C ANISOU 3371 CA ARG C 60 3725 5296 4546 -61 -164 -1016 C ATOM 3372 C ARG C 60 44.730 35.944 24.469 1.00 34.02 C ANISOU 3372 C ARG C 60 3725 4883 4319 -9 -203 -800 C ATOM 3373 O ARG C 60 44.700 36.039 25.709 1.00 33.65 O ANISOU 3373 O ARG C 60 3800 4665 4320 36 -286 -636 O ATOM 3374 CB ARG C 60 46.892 37.173 23.931 1.00 35.56 C ANISOU 3374 CB ARG C 60 3767 5387 4359 -168 -161 -901 C ATOM 3375 CG ARG C 60 48.365 37.028 23.480 1.00 38.24 C ANISOU 3375 CG ARG C 60 3875 5906 4749 -209 -142 -1105 C ATOM 3376 CD ARG C 60 49.110 38.358 23.429 1.00 39.71 C ANISOU 3376 CD ARG C 60 4109 6254 4724 -362 -128 -987 C ATOM 3377 NE ARG C 60 48.500 39.305 24.354 1.00 41.14 N ANISOU 3377 NE ARG C 60 4555 6263 4812 -369 -190 -709 N ATOM 3378 CZ ARG C 60 47.776 40.368 23.999 1.00 42.19 C ANISOU 3378 CZ ARG C 60 4837 6443 4750 -475 -169 -553 C ATOM 3379 NH1 ARG C 60 47.587 40.692 22.717 1.00 41.88 N ANISOU 3379 NH1 ARG C 60 4725 6635 4553 -617 -100 -594 N ATOM 3380 NH2 ARG C 60 47.256 41.131 24.949 1.00 42.41 N ANISOU 3380 NH2 ARG C 60 5076 6289 4749 -450 -232 -357 N ATOM 3381 N TYR C 62 43.634 35.834 23.723 1.00 33.08 N ANISOU 3381 N TYR C 62 3632 4813 4125 -30 -141 -812 N ATOM 3382 CA TYR C 62 42.300 35.799 24.296 1.00 31.36 C ANISOU 3382 CA TYR C 62 3576 4443 3896 13 -160 -643 C ATOM 3383 C TYR C 62 41.835 34.364 24.332 1.00 31.56 C ANISOU 3383 C TYR C 62 3518 4334 4138 105 -209 -736 C ATOM 3384 O TYR C 62 41.847 33.691 23.304 1.00 32.82 O ANISOU 3384 O TYR C 62 3529 4580 4360 103 -170 -942 O ATOM 3385 CB TYR C 62 41.312 36.550 23.409 1.00 30.86 C ANISOU 3385 CB TYR C 62 3580 4504 3641 -71 -84 -585 C ATOM 3386 CG TYR C 62 41.677 37.962 23.020 1.00 31.14 C ANISOU 3386 CG TYR C 62 3672 4681 3477 -194 -59 -496 C ATOM 3387 CD1 TYR C 62 41.843 38.305 21.686 1.00 32.21 C ANISOU 3387 CD1 TYR C 62 3715 5054 3469 -332 -5 -569 C ATOM 3388 CD2 TYR C 62 41.817 38.963 23.979 1.00 31.64 C ANISOU 3388 CD2 TYR C 62 3881 4649 3493 -194 -105 -333 C ATOM 3389 CE1 TYR C 62 42.161 39.605 21.314 1.00 33.73 C ANISOU 3389 CE1 TYR C 62 3958 5368 3488 -477 -18 -446 C ATOM 3390 CE2 TYR C 62 42.135 40.266 23.618 1.00 32.69 C ANISOU 3390 CE2 TYR C 62 4066 4876 3480 -313 -115 -241 C ATOM 3391 CZ TYR C 62 42.298 40.580 22.279 1.00 33.92 C ANISOU 3391 CZ TYR C 62 4130 5251 3508 -459 -82 -278 C ATOM 3392 OH TYR C 62 42.597 41.870 21.903 1.00 35.71 O ANISOU 3392 OH TYR C 62 4407 5562 3599 -608 -125 -147 O ATOM 3393 N SER C 63 41.429 33.885 25.498 1.00 30.49 N ANISOU 3393 N SER C 63 3470 3999 4116 166 -301 -590 N ATOM 3394 CA SER C 63 40.732 32.609 25.567 1.00 30.17 C ANISOU 3394 CA SER C 63 3381 3811 4270 226 -370 -615 C ATOM 3395 C SER C 63 39.438 32.847 26.316 1.00 29.14 C ANISOU 3395 C SER C 63 3419 3615 4036 210 -369 -393 C ATOM 3396 O SER C 63 39.342 33.801 27.090 1.00 28.42 O ANISOU 3396 O SER C 63 3462 3548 3789 178 -347 -242 O ATOM 3397 CB SER C 63 41.590 31.538 26.232 1.00 31.30 C ANISOU 3397 CB SER C 63 3414 3773 4705 294 -527 -656 C ATOM 3398 OG SER C 63 41.945 31.906 27.542 1.00 29.77 O ANISOU 3398 OG SER C 63 3330 3499 4482 275 -612 -448 O ATOM 3399 N ALA C 64 38.431 32.015 26.067 1.00 29.10 N ANISOU 3399 N ALA C 64 3398 3543 4116 227 -386 -393 N ATOM 3400 CA ALA C 64 37.112 32.238 26.657 1.00 28.47 C ANISOU 3400 CA ALA C 64 3449 3443 3925 201 -364 -206 C ATOM 3401 C ALA C 64 36.396 30.943 26.947 1.00 29.43 C ANISOU 3401 C ALA C 64 3535 3421 4227 212 -465 -154 C ATOM 3402 O ALA C 64 36.636 29.940 26.268 1.00 30.83 O ANISOU 3402 O ALA C 64 3583 3521 4610 248 -526 -308 O ATOM 3403 CB ALA C 64 36.252 33.112 25.744 1.00 27.58 C ANISOU 3403 CB ALA C 64 3379 3473 3626 171 -236 -225 C ATOM 3404 N THR C 65 35.513 30.965 27.948 1.00 29.03 N ANISOU 3404 N THR C 65 3585 3343 4101 169 -486 49 N ATOM 3405 CA THR C 65 34.658 29.808 28.234 1.00 29.99 C ANISOU 3405 CA THR C 65 3683 3352 4361 142 -584 144 C ATOM 3406 C THR C 65 33.192 30.178 28.459 1.00 29.53 C ANISOU 3406 C THR C 65 3704 3388 4129 94 -495 268 C ATOM 3407 O THR C 65 32.899 31.232 29.009 1.00 29.31 O ANISOU 3407 O THR C 65 3765 3476 3897 74 -400 337 O ATOM 3408 CB THR C 65 35.154 28.999 29.442 1.00 31.02 C ANISOU 3408 CB THR C 65 3809 3337 4641 97 -773 307 C ATOM 3409 OG1 THR C 65 35.015 29.771 30.637 1.00 30.05 O ANISOU 3409 OG1 THR C 65 3802 3316 4299 21 -741 487 O ATOM 3410 CG2 THR C 65 36.596 28.610 29.255 1.00 32.48 C ANISOU 3410 CG2 THR C 65 3890 3409 5041 158 -880 179 C ATOM 3411 N LEU C 66 32.286 29.298 28.037 1.00 29.94 N ANISOU 3411 N LEU C 66 3709 3385 4283 79 -531 276 N ATOM 3412 CA LEU C 66 30.863 29.481 28.252 1.00 29.66 C ANISOU 3412 CA LEU C 66 3718 3436 4114 29 -461 392 C ATOM 3413 C LEU C 66 30.321 28.277 28.982 1.00 31.00 C ANISOU 3413 C LEU C 66 3865 3504 4409 -56 -605 562 C ATOM 3414 O LEU C 66 30.728 27.159 28.686 1.00 32.11 O ANISOU 3414 O LEU C 66 3931 3470 4799 -47 -756 525 O ATOM 3415 CB LEU C 66 30.152 29.621 26.906 1.00 29.54 C ANISOU 3415 CB LEU C 66 3662 3477 4084 65 -370 260 C ATOM 3416 CG LEU C 66 28.617 29.618 26.775 1.00 29.59 C ANISOU 3416 CG LEU C 66 3674 3554 4014 27 -313 341 C ATOM 3417 CD1 LEU C 66 27.982 30.899 27.315 1.00 28.04 C ANISOU 3417 CD1 LEU C 66 3544 3502 3608 28 -188 410 C ATOM 3418 CD2 LEU C 66 28.226 29.411 25.307 1.00 29.08 C ANISOU 3418 CD2 LEU C 66 3546 3507 3995 49 -282 194 C ATOM 3419 N ASP C 67 29.424 28.519 29.944 1.00 31.35 N ANISOU 3419 N ASP C 67 3961 3662 4287 -148 -568 738 N ATOM 3420 CA ASP C 67 28.621 27.485 30.610 1.00 32.53 C ANISOU 3420 CA ASP C 67 4088 3778 4493 -276 -686 937 C ATOM 3421 C ASP C 67 27.163 27.915 30.534 1.00 32.36 C ANISOU 3421 C ASP C 67 4067 3929 4299 -310 -543 967 C ATOM 3422 O ASP C 67 26.753 28.886 31.177 1.00 32.11 O ANISOU 3422 O ASP C 67 4073 4083 4044 -330 -409 987 O ATOM 3423 CB ASP C 67 29.041 27.341 32.071 1.00 33.78 C ANISOU 3423 CB ASP C 67 4287 3970 4578 -406 -791 1147 C ATOM 3424 CG ASP C 67 28.289 26.230 32.810 1.00 36.23 C ANISOU 3424 CG ASP C 67 4568 4260 4937 -587 -948 1400 C ATOM 3425 OD1 ASP C 67 27.184 25.830 32.388 1.00 37.13 O ANISOU 3425 OD1 ASP C 67 4644 4399 5066 -619 -921 1421 O ATOM 3426 OD2 ASP C 67 28.807 25.757 33.843 1.00 38.23 O ANISOU 3426 OD2 ASP C 67 4834 4481 5209 -720 -1116 1600 O ATOM 3427 N LYS C 68 26.377 27.185 29.754 1.00 32.66 N ANISOU 3427 N LYS C 68 4048 3903 4458 -313 -576 951 N ATOM 3428 CA LYS C 68 24.983 27.541 29.528 1.00 32.50 C ANISOU 3428 CA LYS C 68 4006 4034 4308 -335 -451 967 C ATOM 3429 C LYS C 68 24.014 27.178 30.651 1.00 34.32 C ANISOU 3429 C LYS C 68 4218 4399 4423 -499 -467 1181 C ATOM 3430 O LYS C 68 22.884 27.657 30.652 1.00 34.80 O ANISOU 3430 O LYS C 68 4245 4629 4350 -515 -337 1178 O ATOM 3431 CB LYS C 68 24.494 26.940 28.217 1.00 32.24 C ANISOU 3431 CB LYS C 68 3916 3904 4429 -290 -478 863 C ATOM 3432 CG LYS C 68 25.108 27.577 27.000 1.00 30.67 C ANISOU 3432 CG LYS C 68 3718 3688 4246 -162 -402 640 C ATOM 3433 CD LYS C 68 24.179 27.505 25.824 1.00 29.36 C ANISOU 3433 CD LYS C 68 3504 3557 4095 -147 -356 557 C ATOM 3434 CE LYS C 68 24.957 27.526 24.528 1.00 27.94 C ANISOU 3434 CE LYS C 68 3295 3334 3986 -79 -354 340 C ATOM 3435 NZ LYS C 68 24.035 27.510 23.372 1.00 26.44 N ANISOU 3435 NZ LYS C 68 3060 3210 3775 -92 -315 271 N ATOM 3436 N ASP C 69 24.424 26.322 31.583 1.00 36.34 N ANISOU 3436 N ASP C 69 4480 4593 4734 -637 -635 1371 N ATOM 3437 CA ASP C 69 23.601 26.026 32.761 1.00 38.43 C ANISOU 3437 CA ASP C 69 4723 5044 4834 -844 -654 1600 C ATOM 3438 C ASP C 69 23.711 27.173 33.747 1.00 38.19 C ANISOU 3438 C ASP C 69 4727 5265 4518 -871 -497 1576 C ATOM 3439 O ASP C 69 22.700 27.656 34.263 1.00 38.69 O ANISOU 3439 O ASP C 69 4745 5585 4370 -945 -353 1585 O ATOM 3440 CB ASP C 69 24.044 24.736 33.457 1.00 40.86 C ANISOU 3440 CB ASP C 69 5026 5203 5295 -1020 -926 1853 C ATOM 3441 CG ASP C 69 24.051 23.538 32.532 1.00 43.09 C ANISOU 3441 CG ASP C 69 5265 5191 5918 -986 -1116 1848 C ATOM 3442 OD1 ASP C 69 24.884 22.631 32.764 1.00 46.52 O ANISOU 3442 OD1 ASP C 69 5693 5388 6594 -1031 -1364 1954 O ATOM 3443 OD2 ASP C 69 23.231 23.493 31.582 1.00 44.31 O ANISOU 3443 OD2 ASP C 69 5379 5341 6114 -916 -1034 1731 O ATOM 3444 N ALA C 70 24.951 27.596 33.998 1.00 37.38 N ANISOU 3444 N ALA C 70 4691 5091 4422 -809 -527 1522 N ATOM 3445 CA ALA C 70 25.230 28.722 34.872 1.00 37.27 C ANISOU 3445 CA ALA C 70 4717 5283 4161 -820 -392 1463 C ATOM 3446 C ALA C 70 24.816 30.024 34.203 1.00 35.79 C ANISOU 3446 C ALA C 70 4526 5171 3900 -640 -176 1215 C ATOM 3447 O ALA C 70 24.650 31.046 34.869 1.00 36.04 O ANISOU 3447 O ALA C 70 4562 5395 3735 -639 -37 1124 O ATOM 3448 CB ALA C 70 26.697 28.754 35.229 1.00 36.96 C ANISOU 3448 CB ALA C 70 4745 5120 4180 -804 -508 1482 C ATOM 3449 N LYS C 71 24.630 29.960 32.887 1.00 34.67 N ANISOU 3449 N LYS C 71 4367 4878 3927 -501 -166 1107 N ATOM 3450 CA LYS C 71 24.408 31.136 32.052 1.00 33.45 C ANISOU 3450 CA LYS C 71 4213 4739 3757 -336 -21 906 C ATOM 3451 C LYS C 71 25.473 32.147 32.416 1.00 33.06 C ANISOU 3451 C LYS C 71 4236 4692 3635 -271 17 809 C ATOM 3452 O LYS C 71 25.196 33.172 33.035 1.00 33.64 O ANISOU 3452 O LYS C 71 4310 4911 3560 -257 133 727 O ATOM 3453 CB LYS C 71 22.994 31.693 32.225 1.00 33.99 C ANISOU 3453 CB LYS C 71 4206 4999 3711 -343 120 865 C ATOM 3454 CG LYS C 71 21.911 30.708 31.825 1.00 34.53 C ANISOU 3454 CG LYS C 71 4197 5073 3850 -416 80 967 C ATOM 3455 CD LYS C 71 20.689 31.389 31.254 1.00 34.64 C ANISOU 3455 CD LYS C 71 4128 5181 3854 -337 205 863 C ATOM 3456 CE LYS C 71 20.017 30.466 30.257 1.00 35.79 C ANISOU 3456 CE LYS C 71 4228 5229 4141 -353 131 925 C ATOM 3457 NZ LYS C 71 18.600 30.853 29.922 1.00 37.03 N ANISOU 3457 NZ LYS C 71 4276 5511 4282 -329 229 884 N ATOM 3458 N HIS C 72 26.708 31.810 32.052 1.00 32.78 N ANISOU 3458 N HIS C 72 4245 4491 3718 -235 -89 805 N ATOM 3459 CA HIS C 72 27.895 32.571 32.440 1.00 32.31 C ANISOU 3459 CA HIS C 72 4252 4417 3606 -198 -87 745 C ATOM 3460 C HIS C 72 29.073 32.379 31.464 1.00 30.88 C ANISOU 3460 C HIS C 72 4082 4061 3591 -110 -164 667 C ATOM 3461 O HIS C 72 29.320 31.270 30.994 1.00 31.18 O ANISOU 3461 O HIS C 72 4077 3970 3799 -120 -278 699 O ATOM 3462 CB HIS C 72 28.316 32.171 33.859 1.00 33.75 C ANISOU 3462 CB HIS C 72 4462 4677 3686 -344 -165 893 C ATOM 3463 CG HIS C 72 29.451 32.982 34.399 1.00 34.69 C ANISOU 3463 CG HIS C 72 4647 4806 3726 -325 -162 838 C ATOM 3464 ND1 HIS C 72 30.771 32.617 34.236 1.00 34.66 N ANISOU 3464 ND1 HIS C 72 4667 4649 3854 -303 -289 859 N ATOM 3465 CD2 HIS C 72 29.463 34.156 35.075 1.00 35.30 C ANISOU 3465 CD2 HIS C 72 4762 5025 3626 -321 -52 743 C ATOM 3466 CE1 HIS C 72 31.547 33.525 34.797 1.00 34.51 C ANISOU 3466 CE1 HIS C 72 4706 4684 3724 -297 -259 806 C ATOM 3467 NE2 HIS C 72 30.779 34.466 35.317 1.00 36.24 N ANISOU 3467 NE2 HIS C 72 4940 5076 3755 -310 -119 732 N ATOM 3468 N SER C 73 29.801 33.457 31.182 1.00 29.63 N ANISOU 3468 N SER C 73 3966 3904 3388 -33 -108 553 N ATOM 3469 CA SER C 73 30.997 33.387 30.344 1.00 28.96 C ANISOU 3469 CA SER C 73 3874 3710 3420 25 -163 467 C ATOM 3470 C SER C 73 32.129 34.217 30.921 1.00 28.75 C ANISOU 3470 C SER C 73 3906 3697 3321 30 -166 442 C ATOM 3471 O SER C 73 31.896 35.294 31.458 1.00 28.82 O ANISOU 3471 O SER C 73 3967 3791 3191 33 -88 420 O ATOM 3472 CB SER C 73 30.690 33.864 28.925 1.00 28.44 C ANISOU 3472 CB SER C 73 3779 3649 3379 93 -96 349 C ATOM 3473 OG SER C 73 31.792 33.703 28.042 1.00 28.66 O ANISOU 3473 OG SER C 73 3771 3624 3493 121 -135 247 O ATOM 3474 N THR C 74 33.353 33.703 30.824 1.00 28.73 N ANISOU 3474 N THR C 74 3880 3604 3431 35 -264 428 N ATOM 3475 CA THR C 74 34.539 34.473 31.204 1.00 28.59 C ANISOU 3475 CA THR C 74 3906 3596 3362 40 -275 397 C ATOM 3476 C THR C 74 35.492 34.570 30.029 1.00 27.65 C ANISOU 3476 C THR C 74 3729 3438 3340 97 -279 263 C ATOM 3477 O THR C 74 35.622 33.630 29.251 1.00 28.18 O ANISOU 3477 O THR C 74 3705 3443 3559 121 -324 198 O ATOM 3478 CB THR C 74 35.312 33.868 32.399 1.00 29.69 C ANISOU 3478 CB THR C 74 4057 3695 3530 -31 -404 518 C ATOM 3479 OG1 THR C 74 35.746 32.547 32.071 1.00 31.79 O ANISOU 3479 OG1 THR C 74 4233 3821 4026 -24 -543 538 O ATOM 3480 CG2 THR C 74 34.459 33.810 33.656 1.00 31.42 C ANISOU 3480 CG2 THR C 74 4325 4016 3598 -137 -399 658 C ATOM 3481 N LEU C 75 36.155 35.714 29.920 1.00 26.70 N ANISOU 3481 N LEU C 75 3651 3367 3126 104 -235 212 N ATOM 3482 CA LEU C 75 37.108 35.986 28.872 1.00 26.02 C ANISOU 3482 CA LEU C 75 3507 3302 3079 120 -227 97 C ATOM 3483 C LEU C 75 38.450 36.312 29.507 1.00 26.21 C ANISOU 3483 C LEU C 75 3542 3314 3102 103 -285 102 C ATOM 3484 O LEU C 75 38.557 37.299 30.242 1.00 26.05 O ANISOU 3484 O LEU C 75 3616 3321 2959 78 -269 152 O ATOM 3485 CB LEU C 75 36.629 37.179 28.062 1.00 25.79 C ANISOU 3485 CB LEU C 75 3515 3350 2934 113 -143 67 C ATOM 3486 CG LEU C 75 37.593 37.741 27.016 1.00 26.33 C ANISOU 3486 CG LEU C 75 3534 3495 2977 78 -133 -16 C ATOM 3487 CD1 LEU C 75 37.713 36.791 25.807 1.00 27.48 C ANISOU 3487 CD1 LEU C 75 3547 3694 3201 71 -122 -138 C ATOM 3488 CD2 LEU C 75 37.139 39.115 26.592 1.00 25.82 C ANISOU 3488 CD2 LEU C 75 3537 3473 2802 43 -102 26 C ATOM 3489 N HIS C 76 39.458 35.478 29.236 1.00 26.37 N ANISOU 3489 N HIS C 76 3454 3291 3276 119 -359 33 N ATOM 3490 CA HIS C 76 40.774 35.622 29.824 0.50 26.51 C ANISOU 3490 CA HIS C 76 3455 3290 3329 104 -434 39 C ATOM 3491 C HIS C 76 41.656 36.263 28.789 1.00 26.96 C ANISOU 3491 C HIS C 76 3441 3447 3354 95 -378 -93 C ATOM 3492 O HIS C 76 41.750 35.766 27.668 1.00 28.12 O ANISOU 3492 O HIS C 76 3465 3645 3575 110 -344 -235 O ATOM 3493 CB HIS C 76 41.372 34.263 30.175 0.50 27.21 C ANISOU 3493 CB HIS C 76 3433 3251 3654 131 -577 40 C ATOM 3494 CG HIS C 76 40.562 33.460 31.142 0.50 26.49 C ANISOU 3494 CG HIS C 76 3391 3064 3609 103 -668 205 C ATOM 3495 ND1 HIS C 76 40.911 33.322 32.468 0.50 26.18 N ANISOU 3495 ND1 HIS C 76 3407 2984 3556 36 -787 373 N ATOM 3496 CD2 HIS C 76 39.438 32.726 30.971 0.50 25.26 C ANISOU 3496 CD2 HIS C 76 3230 2866 3501 105 -669 242 C ATOM 3497 CE1 HIS C 76 40.031 32.548 33.075 0.50 25.86 C ANISOU 3497 CE1 HIS C 76 3391 2895 3541 -15 -858 518 C ATOM 3498 NE2 HIS C 76 39.129 32.171 32.188 0.50 26.08 N ANISOU 3498 NE2 HIS C 76 3382 2911 3615 31 -787 440 N ATOM 3499 N ILE C 77 42.312 37.359 29.148 1.00 27.05 N ANISOU 3499 N ILE C 77 3521 3509 3247 50 -372 -56 N ATOM 3500 CA ILE C 77 43.347 37.938 28.301 1.00 27.70 C ANISOU 3500 CA ILE C 77 3524 3705 3297 7 -343 -154 C ATOM 3501 C ILE C 77 44.684 37.581 28.945 1.00 29.00 C ANISOU 3501 C ILE C 77 3615 3831 3572 13 -438 -170 C ATOM 3502 O ILE C 77 44.875 37.827 30.128 1.00 29.73 O ANISOU 3502 O ILE C 77 3804 3855 3638 0 -506 -50 O ATOM 3503 CB ILE C 77 43.182 39.467 28.183 1.00 26.88 C ANISOU 3503 CB ILE C 77 3539 3665 3010 -62 -299 -86 C ATOM 3504 CG1 ILE C 77 41.806 39.803 27.619 1.00 27.07 C ANISOU 3504 CG1 ILE C 77 3623 3696 2965 -58 -237 -55 C ATOM 3505 CG2 ILE C 77 44.226 40.058 27.281 1.00 27.24 C ANISOU 3505 CG2 ILE C 77 3498 3850 3001 -146 -284 -152 C ATOM 3506 CD1 ILE C 77 41.430 41.285 27.686 1.00 26.13 C ANISOU 3506 CD1 ILE C 77 3626 3573 2731 -106 -235 25 C ATOM 3507 N THR C 78 45.600 36.970 28.199 1.00 30.31 N ANISOU 3507 N THR C 78 3595 4053 3869 29 -446 -329 N ATOM 3508 CA THR C 78 46.900 36.596 28.777 1.00 31.85 C ANISOU 3508 CA THR C 78 3688 4202 4210 46 -551 -355 C ATOM 3509 C THR C 78 47.961 37.600 28.360 1.00 32.37 C ANISOU 3509 C THR C 78 3712 4429 4159 -35 -508 -404 C ATOM 3510 O THR C 78 47.967 38.054 27.212 1.00 32.91 O ANISOU 3510 O THR C 78 3718 4670 4115 -97 -405 -503 O ATOM 3511 CB THR C 78 47.359 35.171 28.356 1.00 33.15 C ANISOU 3511 CB THR C 78 3631 4297 4666 135 -617 -533 C ATOM 3512 OG1 THR C 78 46.227 34.295 28.282 1.00 33.90 O ANISOU 3512 OG1 THR C 78 3748 4280 4852 189 -631 -520 O ATOM 3513 CG2 THR C 78 48.359 34.604 29.355 1.00 33.28 C ANISOU 3513 CG2 THR C 78 3577 4172 4896 171 -790 -481 C ATOM 3514 N ALA C 79 48.853 37.947 29.285 1.00 32.64 N ANISOU 3514 N ALA C 79 3775 4420 4206 -58 -598 -319 N ATOM 3515 CA ALA C 79 49.969 38.847 28.988 1.00 33.24 C ANISOU 3515 CA ALA C 79 3799 4641 4190 -146 -580 -352 C ATOM 3516 C ALA C 79 49.492 40.083 28.239 1.00 32.54 C ANISOU 3516 C ALA C 79 3812 4687 3865 -252 -479 -311 C ATOM 3517 O ALA C 79 49.588 40.162 27.014 1.00 33.30 O ANISOU 3517 O ALA C 79 3791 4959 3901 -313 -393 -425 O ATOM 3518 CB ALA C 79 51.049 38.110 28.192 1.00 34.96 C ANISOU 3518 CB ALA C 79 3741 4968 4575 -122 -573 -572 C ATOM 3519 N THR C 80 48.955 41.037 28.982 1.00 31.74 N ANISOU 3519 N THR C 80 3919 4504 3637 -285 -501 -153 N ATOM 3520 CA THR C 80 48.292 42.182 28.377 1.00 31.46 C ANISOU 3520 CA THR C 80 3992 4524 3436 -368 -448 -92 C ATOM 3521 C THR C 80 49.287 43.121 27.716 1.00 32.20 C ANISOU 3521 C THR C 80 4028 4776 3432 -512 -453 -87 C ATOM 3522 O THR C 80 50.407 43.321 28.209 1.00 32.64 O ANISOU 3522 O THR C 80 4043 4850 3507 -549 -511 -82 O ATOM 3523 CB THR C 80 47.453 42.952 29.414 1.00 31.07 C ANISOU 3523 CB THR C 80 4155 4327 3322 -347 -482 31 C ATOM 3524 OG1 THR C 80 48.146 42.961 30.678 1.00 32.36 O ANISOU 3524 OG1 THR C 80 4369 4419 3509 -341 -564 75 O ATOM 3525 CG2 THR C 80 46.089 42.291 29.593 1.00 29.99 C ANISOU 3525 CG2 THR C 80 4071 4107 3218 -252 -440 35 C ATOM 3526 N LEU C 81 48.871 43.673 26.581 1.00 32.43 N ANISOU 3526 N LEU C 81 4044 4928 3349 -612 -405 -73 N ATOM 3527 CA LEU C 81 49.646 44.694 25.885 1.00 33.44 C ANISOU 3527 CA LEU C 81 4133 5220 3352 -797 -427 -18 C ATOM 3528 C LEU C 81 48.861 45.984 25.884 1.00 33.42 C ANISOU 3528 C LEU C 81 4313 5113 3273 -870 -493 151 C ATOM 3529 O LEU C 81 47.627 45.959 25.937 1.00 32.98 O ANISOU 3529 O LEU C 81 4354 4934 3242 -789 -481 182 O ATOM 3530 CB LEU C 81 49.952 44.281 24.453 1.00 34.33 C ANISOU 3530 CB LEU C 81 4043 5614 3387 -909 -341 -133 C ATOM 3531 CG LEU C 81 50.826 43.048 24.227 1.00 34.78 C ANISOU 3531 CG LEU C 81 3862 5804 3549 -846 -276 -363 C ATOM 3532 CD1 LEU C 81 50.832 42.729 22.739 1.00 35.33 C ANISOU 3532 CD1 LEU C 81 3743 6177 3505 -969 -171 -507 C ATOM 3533 CD2 LEU C 81 52.252 43.255 24.766 1.00 35.44 C ANISOU 3533 CD2 LEU C 81 3858 5933 3673 -883 -327 -383 C ATOM 3534 N LEU C 82 49.582 47.107 25.841 1.00 34.38 N ANISOU 3534 N LEU C 82 4469 5268 3327 -1021 -577 257 N ATOM 3535 CA LEU C 82 48.980 48.441 25.833 1.00 34.29 C ANISOU 3535 CA LEU C 82 4615 5121 3294 -1102 -686 420 C ATOM 3536 C LEU C 82 47.758 48.512 24.904 1.00 34.30 C ANISOU 3536 C LEU C 82 4632 5129 3271 -1122 -673 474 C ATOM 3537 O LEU C 82 46.714 49.027 25.302 1.00 33.79 O ANISOU 3537 O LEU C 82 4702 4855 3283 -1041 -727 530 O ATOM 3538 CB LEU C 82 50.038 49.502 25.489 1.00 35.48 C ANISOU 3538 CB LEU C 82 4745 5370 3366 -1320 -788 537 C ATOM 3539 CG LEU C 82 49.670 50.817 24.787 1.00 36.63 C ANISOU 3539 CG LEU C 82 4966 5478 3474 -1507 -928 737 C ATOM 3540 CD1 LEU C 82 48.798 51.718 25.643 1.00 37.11 C ANISOU 3540 CD1 LEU C 82 5222 5204 3675 -1402 -1046 796 C ATOM 3541 CD2 LEU C 82 50.918 51.553 24.361 1.00 37.51 C ANISOU 3541 CD2 LEU C 82 5007 5758 3487 -1753 -1013 846 C ATOM 3542 N ASP C 83 47.885 47.955 23.699 1.00 34.98 N ANISOU 3542 N ASP C 83 4565 5468 3256 -1229 -599 435 N ATOM 3543 CA ASP C 83 46.783 47.904 22.720 1.00 35.26 C ANISOU 3543 CA ASP C 83 4595 5554 3247 -1273 -587 487 C ATOM 3544 C ASP C 83 45.445 47.363 23.214 1.00 33.29 C ANISOU 3544 C ASP C 83 4433 5103 3112 -1062 -545 439 C ATOM 3545 O ASP C 83 44.406 47.770 22.700 1.00 33.69 O ANISOU 3545 O ASP C 83 4536 5097 3169 -1089 -593 537 O ATOM 3546 CB ASP C 83 47.200 47.162 21.437 1.00 36.81 C ANISOU 3546 CB ASP C 83 4590 6100 3297 -1414 -484 389 C ATOM 3547 CG ASP C 83 47.902 48.076 20.428 1.00 40.00 C ANISOU 3547 CG ASP C 83 4922 6758 3520 -1726 -558 535 C ATOM 3548 OD1 ASP C 83 47.710 49.318 20.495 1.00 41.10 O ANISOU 3548 OD1 ASP C 83 5188 6758 3669 -1839 -721 763 O ATOM 3549 OD2 ASP C 83 48.646 47.545 19.573 1.00 42.07 O ANISOU 3549 OD2 ASP C 83 4986 7362 3635 -1867 -460 414 O ATOM 3550 N ASP C 84 45.472 46.458 24.192 1.00 31.73 N ANISOU 3550 N ASP C 84 4242 4807 3006 -872 -472 305 N ATOM 3551 CA ASP C 84 44.255 45.936 24.832 1.00 30.50 C ANISOU 3551 CA ASP C 84 4167 4475 2946 -689 -435 269 C ATOM 3552 C ASP C 84 43.397 46.956 25.589 1.00 30.19 C ANISOU 3552 C ASP C 84 4288 4207 2976 -628 -516 356 C ATOM 3553 O ASP C 84 42.278 46.652 25.997 1.00 29.47 O ANISOU 3553 O ASP C 84 4245 4005 2948 -501 -481 328 O ATOM 3554 CB ASP C 84 44.602 44.813 25.787 1.00 29.95 C ANISOU 3554 CB ASP C 84 4067 4359 2953 -545 -376 148 C ATOM 3555 CG ASP C 84 45.104 43.597 25.074 1.00 31.34 C ANISOU 3555 CG ASP C 84 4066 4701 3139 -545 -299 11 C ATOM 3556 OD1 ASP C 84 44.665 43.381 23.918 1.00 33.11 O ANISOU 3556 OD1 ASP C 84 4213 5063 3304 -612 -254 -17 O ATOM 3557 OD2 ASP C 84 45.930 42.864 25.672 1.00 31.35 O ANISOU 3557 OD2 ASP C 84 3998 4693 3220 -481 -296 -75 O ATOM 3558 N THR C 85 43.925 48.155 25.795 1.00 30.80 N ANISOU 3558 N THR C 85 4432 4215 3054 -719 -627 444 N ATOM 3559 CA THR C 85 43.124 49.246 26.314 1.00 30.89 C ANISOU 3559 CA THR C 85 4566 4005 3166 -673 -726 497 C ATOM 3560 C THR C 85 41.940 49.479 25.379 1.00 31.87 C ANISOU 3560 C THR C 85 4679 4101 3331 -691 -763 577 C ATOM 3561 O THR C 85 42.096 49.918 24.223 1.00 33.11 O ANISOU 3561 O THR C 85 4789 4357 3433 -865 -843 711 O ATOM 3562 CB THR C 85 43.963 50.501 26.479 1.00 31.69 C ANISOU 3562 CB THR C 85 4724 4033 3284 -795 -869 584 C ATOM 3563 OG1 THR C 85 45.035 50.211 27.382 1.00 30.69 O ANISOU 3563 OG1 THR C 85 4602 3941 3117 -775 -834 508 O ATOM 3564 CG2 THR C 85 43.130 51.631 27.025 1.00 31.54 C ANISOU 3564 CG2 THR C 85 4813 3753 3419 -730 -989 596 C ATOM 3565 N ALA C 86 40.760 49.155 25.899 1.00 31.41 N ANISOU 3565 N ALA C 86 4652 3926 3355 -528 -709 503 N ATOM 3566 CA ALA C 86 39.542 49.109 25.120 1.00 31.61 C ANISOU 3566 CA ALA C 86 4651 3932 3429 -513 -722 556 C ATOM 3567 C ALA C 86 38.383 48.766 26.043 1.00 31.55 C ANISOU 3567 C ALA C 86 4673 3801 3514 -319 -647 440 C ATOM 3568 O ALA C 86 38.588 48.426 27.223 1.00 31.29 O ANISOU 3568 O ALA C 86 4677 3743 3469 -223 -574 326 O ATOM 3569 CB ALA C 86 39.668 48.057 24.053 1.00 31.01 C ANISOU 3569 CB ALA C 86 4470 4085 3229 -592 -634 562 C ATOM 3570 N THR C 87 37.169 48.869 25.502 1.00 31.95 N ANISOU 3570 N THR C 87 4699 3796 3645 -283 -673 479 N ATOM 3571 CA THR C 87 35.970 48.369 26.158 1.00 31.64 C ANISOU 3571 CA THR C 87 4651 3700 3671 -122 -582 372 C ATOM 3572 C THR C 87 35.667 46.988 25.578 1.00 31.01 C ANISOU 3572 C THR C 87 4503 3783 3498 -123 -467 368 C ATOM 3573 O THR C 87 35.718 46.797 24.354 1.00 31.29 O ANISOU 3573 O THR C 87 4484 3924 3479 -235 -496 457 O ATOM 3574 CB THR C 87 34.775 49.312 25.937 1.00 32.75 C ANISOU 3574 CB THR C 87 4782 3668 3994 -68 -692 401 C ATOM 3575 OG1 THR C 87 34.900 50.463 26.781 1.00 34.17 O ANISOU 3575 OG1 THR C 87 5014 3663 4306 -15 -783 327 O ATOM 3576 CG2 THR C 87 33.467 48.615 26.252 1.00 32.10 C ANISOU 3576 CG2 THR C 87 4650 3595 3952 64 -584 311 C ATOM 3577 N TYR C 88 35.364 46.029 26.453 1.00 30.45 N ANISOU 3577 N TYR C 88 4427 3740 3402 -19 -348 266 N ATOM 3578 CA TYR C 88 35.067 44.667 26.025 1.00 29.89 C ANISOU 3578 CA TYR C 88 4292 3784 3282 -12 -258 250 C ATOM 3579 C TYR C 88 33.605 44.409 26.220 1.00 29.79 C ANISOU 3579 C TYR C 88 4257 3729 3333 79 -216 230 C ATOM 3580 O TYR C 88 33.079 44.664 27.296 1.00 29.85 O ANISOU 3580 O TYR C 88 4290 3674 3377 165 -184 163 O ATOM 3581 CB TYR C 88 35.945 43.666 26.776 1.00 29.70 C ANISOU 3581 CB TYR C 88 4264 3819 3203 5 -194 187 C ATOM 3582 CG TYR C 88 37.367 43.809 26.327 1.00 30.53 C ANISOU 3582 CG TYR C 88 4351 3994 3254 -91 -231 197 C ATOM 3583 CD1 TYR C 88 38.179 44.835 26.835 1.00 31.17 C ANISOU 3583 CD1 TYR C 88 4495 4023 3325 -127 -294 216 C ATOM 3584 CD2 TYR C 88 37.886 42.973 25.341 1.00 30.95 C ANISOU 3584 CD2 TYR C 88 4308 4181 3271 -154 -203 169 C ATOM 3585 CE1 TYR C 88 39.478 45.002 26.391 1.00 32.64 C ANISOU 3585 CE1 TYR C 88 4650 4295 3456 -231 -329 233 C ATOM 3586 CE2 TYR C 88 39.187 43.131 24.884 1.00 32.75 C ANISOU 3586 CE2 TYR C 88 4488 4513 3442 -253 -224 154 C ATOM 3587 CZ TYR C 88 39.977 44.148 25.409 1.00 33.41 C ANISOU 3587 CZ TYR C 88 4636 4551 3508 -296 -287 200 C ATOM 3588 OH TYR C 88 41.263 44.302 24.949 1.00 35.01 O ANISOU 3588 OH TYR C 88 4776 4877 3649 -407 -306 191 O ATOM 3589 N ILE C 89 32.950 43.938 25.162 1.00 29.95 N ANISOU 3589 N ILE C 89 4217 3806 3358 46 -216 278 N ATOM 3590 CA ILE C 89 31.483 43.871 25.121 1.00 30.65 C ANISOU 3590 CA ILE C 89 4269 3853 3524 117 -200 281 C ATOM 3591 C ILE C 89 30.943 42.462 24.896 1.00 30.51 C ANISOU 3591 C ILE C 89 4195 3924 3473 128 -118 261 C ATOM 3592 O ILE C 89 31.443 41.704 24.053 1.00 30.57 O ANISOU 3592 O ILE C 89 4165 4026 3424 54 -110 264 O ATOM 3593 CB ILE C 89 30.896 44.841 24.085 1.00 31.15 C ANISOU 3593 CB ILE C 89 4310 3861 3666 66 -320 384 C ATOM 3594 CG1 ILE C 89 30.801 46.231 24.698 1.00 32.61 C ANISOU 3594 CG1 ILE C 89 4533 3876 3980 121 -413 372 C ATOM 3595 CG2 ILE C 89 29.511 44.392 23.649 1.00 31.83 C ANISOU 3595 CG2 ILE C 89 4328 3956 3810 106 -304 405 C ATOM 3596 CD1 ILE C 89 30.415 47.328 23.724 1.00 35.36 C ANISOU 3596 CD1 ILE C 89 4862 4122 4451 53 -593 509 C ATOM 3597 N CYS C 90 29.907 42.137 25.657 1.00 30.76 N ANISOU 3597 N CYS C 90 4209 3933 3547 212 -60 225 N ATOM 3598 CA CYS C 90 29.332 40.810 25.673 1.00 30.98 C ANISOU 3598 CA CYS C 90 4189 4022 3559 219 2 219 C ATOM 3599 C CYS C 90 27.976 40.809 24.958 1.00 30.79 C ANISOU 3599 C CYS C 90 4101 4001 3596 232 -7 258 C ATOM 3600 O CYS C 90 27.164 41.722 25.166 1.00 31.71 O ANISOU 3600 O CYS C 90 4199 4057 3791 289 -29 255 O ATOM 3601 CB CYS C 90 29.155 40.389 27.126 1.00 31.61 C ANISOU 3601 CB CYS C 90 4285 4111 3613 265 68 178 C ATOM 3602 SG CYS C 90 28.656 38.709 27.295 1.00 35.11 S ANISOU 3602 SG CYS C 90 4680 4610 4052 241 105 209 S ATOM 3603 N VAL C 91 27.733 39.805 24.111 1.00 29.61 N ANISOU 3603 N VAL C 91 3905 3915 3431 181 -2 278 N ATOM 3604 CA VAL C 91 26.468 39.717 23.375 1.00 29.34 C ANISOU 3604 CA VAL C 91 3807 3896 3446 177 -20 324 C ATOM 3605 C VAL C 91 25.929 38.294 23.354 1.00 28.96 C ANISOU 3605 C VAL C 91 3711 3895 3396 166 26 310 C ATOM 3606 O VAL C 91 26.676 37.351 23.109 1.00 28.76 O ANISOU 3606 O VAL C 91 3685 3899 3344 124 31 267 O ATOM 3607 CB VAL C 91 26.594 40.215 21.913 1.00 29.68 C ANISOU 3607 CB VAL C 91 3831 3980 3466 76 -109 392 C ATOM 3608 CG1 VAL C 91 25.256 40.727 21.409 1.00 29.95 C ANISOU 3608 CG1 VAL C 91 3809 3982 3588 87 -171 472 C ATOM 3609 CG2 VAL C 91 27.611 41.319 21.798 1.00 30.10 C ANISOU 3609 CG2 VAL C 91 3937 4005 3493 32 -175 422 C ATOM 3610 N VAL C 92 24.629 38.145 23.597 1.00 29.18 N ANISOU 3610 N VAL C 92 3687 3925 3476 203 48 336 N ATOM 3611 CA VAL C 92 23.977 36.826 23.569 1.00 29.13 C ANISOU 3611 CA VAL C 92 3632 3955 3481 177 74 345 C ATOM 3612 C VAL C 92 22.886 36.742 22.501 1.00 29.78 C ANISOU 3612 C VAL C 92 3644 4069 3601 145 37 391 C ATOM 3613 O VAL C 92 22.076 37.665 22.357 1.00 30.18 O ANISOU 3613 O VAL C 92 3659 4104 3705 181 12 430 O ATOM 3614 CB VAL C 92 23.394 36.442 24.947 1.00 29.28 C ANISOU 3614 CB VAL C 92 3636 3991 3499 212 138 351 C ATOM 3615 CG1 VAL C 92 22.567 35.174 24.846 1.00 28.36 C ANISOU 3615 CG1 VAL C 92 3460 3904 3410 163 138 396 C ATOM 3616 CG2 VAL C 92 24.516 36.274 25.952 1.00 28.67 C ANISOU 3616 CG2 VAL C 92 3625 3898 3369 208 152 329 C ATOM 3617 N GLY C 93 22.870 35.626 21.772 1.00 29.99 N ANISOU 3617 N GLY C 93 3644 4130 3621 78 20 375 N ATOM 3618 CA GLY C 93 21.962 35.443 20.643 1.00 31.05 C ANISOU 3618 CA GLY C 93 3716 4315 3768 19 -23 412 C ATOM 3619 C GLY C 93 20.823 34.488 20.945 1.00 31.94 C ANISOU 3619 C GLY C 93 3769 4431 3937 19 -5 441 C ATOM 3620 O GLY C 93 21.061 33.315 21.249 1.00 31.77 O ANISOU 3620 O GLY C 93 3748 4386 3936 -3 0 406 O ATOM 3621 N ASP C 94 19.597 35.030 20.885 1.00 32.94 N ANISOU 3621 N ASP C 94 3832 4574 4110 44 -13 509 N ATOM 3622 CA ASP C 94 18.304 34.321 20.919 1.00 33.50 C ANISOU 3622 CA ASP C 94 3820 4677 4232 25 -8 556 C ATOM 3623 C ASP C 94 18.207 33.051 20.085 1.00 33.18 C ANISOU 3623 C ASP C 94 3763 4656 4189 -69 -51 539 C ATOM 3624 O ASP C 94 17.636 32.061 20.525 1.00 33.73 O ANISOU 3624 O ASP C 94 3796 4719 4299 -94 -43 562 O ATOM 3625 CB ASP C 94 17.239 35.243 20.340 1.00 34.88 C ANISOU 3625 CB ASP C 94 3917 4867 4468 45 -56 621 C ATOM 3626 CG ASP C 94 16.656 36.173 21.354 1.00 38.01 C ANISOU 3626 CG ASP C 94 4260 5245 4938 156 -8 609 C ATOM 3627 OD1 ASP C 94 16.831 35.944 22.565 1.00 40.88 O ANISOU 3627 OD1 ASP C 94 4634 5630 5270 193 82 559 O ATOM 3628 OD2 ASP C 94 15.988 37.134 20.931 1.00 42.12 O ANISOU 3628 OD2 ASP C 94 4712 5735 5558 197 -73 644 O ATOM 3629 N ARG C 95 18.696 33.113 18.851 1.00 32.55 N ANISOU 3629 N ARG C 95 3695 4614 4059 -140 -104 499 N ATOM 3630 CA ARG C 95 18.492 32.042 17.886 1.00 32.48 C ANISOU 3630 CA ARG C 95 3649 4647 4045 -238 -148 444 C ATOM 3631 C ARG C 95 19.781 31.756 17.139 1.00 32.30 C ANISOU 3631 C ARG C 95 3655 4666 3953 -296 -156 301 C ATOM 3632 O ARG C 95 20.689 32.588 17.112 1.00 32.14 O ANISOU 3632 O ARG C 95 3679 4670 3864 -286 -141 286 O ATOM 3633 CB ARG C 95 17.441 32.439 16.837 1.00 33.03 C ANISOU 3633 CB ARG C 95 3656 4799 4095 -310 -212 526 C ATOM 3634 CG ARG C 95 16.091 32.854 17.340 1.00 31.98 C ANISOU 3634 CG ARG C 95 3456 4647 4048 -255 -214 649 C ATOM 3635 CD ARG C 95 15.199 31.679 17.651 1.00 31.10 C ANISOU 3635 CD ARG C 95 3289 4530 3999 -280 -205 662 C ATOM 3636 NE ARG C 95 13.836 32.130 17.919 1.00 30.41 N ANISOU 3636 NE ARG C 95 3104 4468 3982 -246 -208 768 N ATOM 3637 CZ ARG C 95 13.431 32.716 19.047 1.00 28.85 C ANISOU 3637 CZ ARG C 95 2866 4260 3834 -145 -140 793 C ATOM 3638 NH1 ARG C 95 12.170 33.085 19.172 1.00 29.97 N ANISOU 3638 NH1 ARG C 95 2887 4442 4057 -115 -143 853 N ATOM 3639 NH2 ARG C 95 14.268 32.940 20.048 1.00 26.55 N ANISOU 3639 NH2 ARG C 95 2640 3935 3512 -80 -67 740 N ATOM 3640 N GLY C 96 19.839 30.588 16.507 1.00 32.22 N ANISOU 3640 N GLY C 96 3604 4671 3967 -363 -182 179 N ATOM 3641 CA GLY C 96 20.925 30.268 15.599 1.00 32.00 C ANISOU 3641 CA GLY C 96 3559 4729 3871 -434 -183 -10 C ATOM 3642 C GLY C 96 20.615 30.675 14.175 1.00 32.44 C ANISOU 3642 C GLY C 96 3572 4978 3776 -580 -216 -19 C ATOM 3643 O GLY C 96 21.106 30.036 13.236 1.00 33.33 O ANISOU 3643 O GLY C 96 3629 5208 3827 -678 -217 -214 O ATOM 3644 N SER C 97 19.802 31.731 14.019 1.00 31.74 N ANISOU 3644 N SER C 97 3494 4928 3638 -603 -253 181 N ATOM 3645 CA SER C 97 19.414 32.265 12.699 1.00 32.38 C ANISOU 3645 CA SER C 97 3537 5193 3574 -770 -323 243 C ATOM 3646 C SER C 97 19.079 33.764 12.728 1.00 32.25 C ANISOU 3646 C SER C 97 3547 5168 3539 -771 -390 472 C ATOM 3647 O SER C 97 19.084 34.384 13.782 1.00 31.52 O ANISOU 3647 O SER C 97 3495 4928 3553 -627 -367 547 O ATOM 3648 CB SER C 97 18.228 31.486 12.122 1.00 33.04 C ANISOU 3648 CB SER C 97 3558 5311 3686 -840 -373 253 C ATOM 3649 OG SER C 97 17.007 31.897 12.719 1.00 32.15 O ANISOU 3649 OG SER C 97 3434 5090 3692 -758 -408 449 O ATOM 3650 N ALA C 98 18.765 34.326 11.562 1.00 33.38 N ANISOU 3650 N ALA C 98 3656 5468 3557 -945 -491 579 N ATOM 3651 CA ALA C 98 18.403 35.738 11.418 1.00 33.70 C ANISOU 3651 CA ALA C 98 3705 5479 3619 -973 -611 817 C ATOM 3652 C ALA C 98 17.229 36.168 12.295 1.00 33.78 C ANISOU 3652 C ALA C 98 3692 5291 3853 -802 -643 948 C ATOM 3653 O ALA C 98 17.072 37.368 12.577 1.00 34.36 O ANISOU 3653 O ALA C 98 3770 5259 4027 -748 -728 1092 O ATOM 3654 CB ALA C 98 18.113 36.058 9.976 1.00 34.83 C ANISOU 3654 CB ALA C 98 3802 5834 3597 -1223 -744 936 C ATOM 3655 N LEU C 99 16.420 35.190 12.719 1.00 33.79 N ANISOU 3655 N LEU C 99 3654 5244 3942 -725 -582 883 N ATOM 3656 CA LEU C 99 15.225 35.414 13.545 1.00 33.89 C ANISOU 3656 CA LEU C 99 3608 5122 4145 -581 -586 970 C ATOM 3657 C LEU C 99 15.536 35.919 14.955 1.00 32.87 C ANISOU 3657 C LEU C 99 3513 4849 4128 -393 -498 932 C ATOM 3658 O LEU C 99 14.641 36.415 15.656 1.00 33.17 O ANISOU 3658 O LEU C 99 3485 4800 4319 -274 -500 984 O ATOM 3659 CB LEU C 99 14.439 34.120 13.680 1.00 34.11 C ANISOU 3659 CB LEU C 99 3587 5165 4207 -580 -534 905 C ATOM 3660 CG LEU C 99 13.808 33.513 12.438 1.00 36.04 C ANISOU 3660 CG LEU C 99 3779 5540 4374 -750 -619 929 C ATOM 3661 CD1 LEU C 99 13.342 32.100 12.755 1.00 36.59 C ANISOU 3661 CD1 LEU C 99 3821 5590 4490 -739 -557 825 C ATOM 3662 CD2 LEU C 99 12.651 34.360 11.970 1.00 39.06 C ANISOU 3662 CD2 LEU C 99 4077 5925 4840 -781 -755 1129 C ATOM 3663 N GLY C 100 16.799 35.789 15.359 1.00 31.60 N ANISOU 3663 N GLY C 100 3438 4680 3887 -373 -420 825 N ATOM 3664 CA GLY C 100 17.235 36.144 16.701 1.00 30.64 C ANISOU 3664 CA GLY C 100 3358 4449 3833 -221 -333 773 C ATOM 3665 C GLY C 100 17.515 37.611 16.930 1.00 30.69 C ANISOU 3665 C GLY C 100 3385 4374 3902 -163 -393 839 C ATOM 3666 O GLY C 100 17.755 38.364 15.999 1.00 31.32 O ANISOU 3666 O GLY C 100 3472 4480 3948 -264 -513 937 O ATOM 3667 N ARG C 103 17.463 38.002 18.198 1.00 30.60 N ANISOU 3667 N ARG C 103 3374 4269 3982 -16 -320 785 N ATOM 3668 CA ARG C 103 17.774 39.348 18.640 1.00 30.77 C ANISOU 3668 CA ARG C 103 3413 4183 4096 65 -368 799 C ATOM 3669 C ARG C 103 19.041 39.223 19.471 1.00 29.82 C ANISOU 3669 C ARG C 103 3394 4053 3885 99 -270 696 C ATOM 3670 O ARG C 103 19.201 38.246 20.221 1.00 29.30 O ANISOU 3670 O ARG C 103 3346 4024 3764 125 -155 615 O ATOM 3671 CB ARG C 103 16.643 39.909 19.505 1.00 31.50 C ANISOU 3671 CB ARG C 103 3398 4197 4373 212 -351 766 C ATOM 3672 CG ARG C 103 15.251 39.822 18.905 1.00 33.68 C ANISOU 3672 CG ARG C 103 3545 4489 4762 200 -426 848 C ATOM 3673 CD ARG C 103 15.094 40.738 17.676 1.00 37.97 C ANISOU 3673 CD ARG C 103 4067 4972 5389 117 -640 1011 C ATOM 3674 NE ARG C 103 14.306 41.940 17.964 1.00 41.06 N ANISOU 3674 NE ARG C 103 4343 5207 6050 243 -752 1027 N ATOM 3675 CZ ARG C 103 13.045 42.130 17.577 1.00 43.68 C ANISOU 3675 CZ ARG C 103 4530 5507 6559 268 -855 1097 C ATOM 3676 NH1 ARG C 103 12.414 41.199 16.874 1.00 44.48 N ANISOU 3676 NH1 ARG C 103 4596 5734 6569 161 -855 1175 N ATOM 3677 NH2 ARG C 103 12.408 43.257 17.890 1.00 46.22 N ANISOU 3677 NH2 ARG C 103 4728 5660 7174 405 -969 1077 N ATOM 3678 N LEU C 104 19.941 40.197 19.324 1.00 29.66 N ANISOU 3678 N LEU C 104 3435 3977 3856 82 -337 721 N ATOM 3679 CA LEU C 104 21.177 40.254 20.089 1.00 28.31 C ANISOU 3679 CA LEU C 104 3354 3789 3612 112 -264 634 C ATOM 3680 C LEU C 104 20.953 41.051 21.359 1.00 28.67 C ANISOU 3680 C LEU C 104 3390 3730 3772 257 -226 561 C ATOM 3681 O LEU C 104 20.241 42.046 21.345 1.00 29.93 O ANISOU 3681 O LEU C 104 3487 3793 4092 321 -311 584 O ATOM 3682 CB LEU C 104 22.276 40.901 19.262 1.00 28.54 C ANISOU 3682 CB LEU C 104 3445 3837 3563 -1 -357 698 C ATOM 3683 CG LEU C 104 22.677 40.257 17.930 1.00 28.51 C ANISOU 3683 CG LEU C 104 3436 3992 3405 -177 -389 735 C ATOM 3684 CD1 LEU C 104 23.864 40.991 17.322 1.00 27.81 C ANISOU 3684 CD1 LEU C 104 3396 3959 3213 -305 -462 787 C ATOM 3685 CD2 LEU C 104 23.007 38.799 18.124 1.00 27.30 C ANISOU 3685 CD2 LEU C 104 3282 3919 3170 -174 -264 600 C ATOM 3686 N HIS C 105 21.557 40.599 22.455 1.00 27.99 N ANISOU 3686 N HIS C 105 3354 3667 3614 303 -109 461 N ATOM 3687 CA HIS C 105 21.354 41.186 23.780 1.00 28.32 C ANISOU 3687 CA HIS C 105 3379 3667 3715 417 -43 354 C ATOM 3688 C HIS C 105 22.701 41.630 24.337 1.00 27.85 C ANISOU 3688 C HIS C 105 3424 3571 3588 415 -35 306 C ATOM 3689 O HIS C 105 23.550 40.798 24.661 1.00 26.95 O ANISOU 3689 O HIS C 105 3373 3517 3350 368 23 295 O ATOM 3690 CB HIS C 105 20.704 40.164 24.708 1.00 28.19 C ANISOU 3690 CB HIS C 105 3312 3757 3641 434 85 299 C ATOM 3691 CG HIS C 105 19.390 39.648 24.213 1.00 28.99 C ANISOU 3691 CG HIS C 105 3305 3907 3802 425 82 347 C ATOM 3692 ND1 HIS C 105 18.183 40.177 24.619 1.00 31.59 N ANISOU 3692 ND1 HIS C 105 3506 4245 4253 510 104 288 N ATOM 3693 CD2 HIS C 105 19.091 38.654 23.344 1.00 28.34 C ANISOU 3693 CD2 HIS C 105 3212 3871 3685 341 56 432 C ATOM 3694 CE1 HIS C 105 17.197 39.526 24.026 1.00 31.22 C ANISOU 3694 CE1 HIS C 105 3378 4250 4236 473 91 359 C ATOM 3695 NE2 HIS C 105 17.721 38.601 23.242 1.00 29.08 N ANISOU 3695 NE2 HIS C 105 3183 3999 3868 367 58 449 N ATOM 3696 N PHE C 106 22.890 42.943 24.447 1.00 28.65 N ANISOU 3696 N PHE C 106 3534 3556 3797 466 -114 281 N ATOM 3697 CA PHE C 106 24.217 43.522 24.668 1.00 27.70 C ANISOU 3697 CA PHE C 106 3514 3385 3625 439 -148 269 C ATOM 3698 C PHE C 106 24.521 43.866 26.118 1.00 28.17 C ANISOU 3698 C PHE C 106 3597 3436 3669 518 -64 120 C ATOM 3699 O PHE C 106 23.684 44.413 26.825 1.00 29.41 O ANISOU 3699 O PHE C 106 3678 3565 3931 615 -34 1 O ATOM 3700 CB PHE C 106 24.372 44.786 23.830 1.00 28.21 C ANISOU 3700 CB PHE C 106 3584 3314 3819 411 -325 359 C ATOM 3701 CG PHE C 106 24.544 44.530 22.361 1.00 27.08 C ANISOU 3701 CG PHE C 106 3446 3229 3614 266 -421 525 C ATOM 3702 CD1 PHE C 106 23.446 44.321 21.543 1.00 26.98 C ANISOU 3702 CD1 PHE C 106 3352 3235 3666 243 -477 610 C ATOM 3703 CD2 PHE C 106 25.808 44.533 21.786 1.00 26.05 C ANISOU 3703 CD2 PHE C 106 3389 3161 3349 137 -456 590 C ATOM 3704 CE1 PHE C 106 23.606 44.099 20.174 1.00 26.95 C ANISOU 3704 CE1 PHE C 106 3346 3321 3571 79 -568 756 C ATOM 3705 CE2 PHE C 106 25.974 44.312 20.419 1.00 25.51 C ANISOU 3705 CE2 PHE C 106 3305 3202 3186 -26 -532 719 C ATOM 3706 CZ PHE C 106 24.873 44.096 19.612 1.00 25.54 C ANISOU 3706 CZ PHE C 106 3235 3234 3234 -61 -589 803 C ATOM 3707 N GLY C 107 25.738 43.555 26.550 1.00 27.47 N ANISOU 3707 N GLY C 107 3601 3386 3449 468 -29 113 N ATOM 3708 CA GLY C 107 26.245 44.053 27.821 1.00 28.09 C ANISOU 3708 CA GLY C 107 3720 3457 3495 511 19 -10 C ATOM 3709 C GLY C 107 26.717 45.484 27.653 1.00 29.09 C ANISOU 3709 C GLY C 107 3880 3428 3746 536 -101 -33 C ATOM 3710 O GLY C 107 26.985 45.931 26.534 1.00 28.96 O ANISOU 3710 O GLY C 107 3880 3332 3793 480 -229 91 O ATOM 3711 N ALA C 108 26.808 46.209 28.762 1.00 30.29 N ANISOU 3711 N ALA C 108 4036 3545 3929 602 -73 -192 N ATOM 3712 CA ALA C 108 27.297 47.582 28.735 1.00 31.60 C ANISOU 3712 CA ALA C 108 4235 3533 4239 629 -204 -234 C ATOM 3713 C ALA C 108 28.831 47.629 28.716 1.00 31.17 C ANISOU 3713 C ALA C 108 4301 3481 4061 530 -244 -157 C ATOM 3714 O ALA C 108 29.431 48.699 28.768 1.00 32.57 O ANISOU 3714 O ALA C 108 4522 3522 4331 525 -357 -175 O ATOM 3715 CB ALA C 108 26.735 48.380 29.903 1.00 32.82 C ANISOU 3715 CB ALA C 108 4325 3647 4499 745 -162 -483 C ATOM 3716 N GLY C 109 29.479 46.479 28.634 1.00 29.85 N ANISOU 3716 N GLY C 109 4175 3456 3710 451 -166 -76 N ATOM 3717 CA GLY C 109 30.929 46.492 28.526 1.00 29.87 C ANISOU 3717 CA GLY C 109 4262 3469 3617 361 -207 -11 C ATOM 3718 C GLY C 109 31.693 46.484 29.834 1.00 30.26 C ANISOU 3718 C GLY C 109 4369 3562 3566 363 -149 -112 C ATOM 3719 O GLY C 109 31.125 46.701 30.902 1.00 31.19 O ANISOU 3719 O GLY C 109 4467 3703 3682 426 -83 -257 O ATOM 3720 N THR C 110 32.979 46.170 29.723 1.00 29.96 N ANISOU 3720 N THR C 110 4387 3564 3434 281 -171 -42 N ATOM 3721 CA THR C 110 33.962 46.299 30.786 1.00 30.97 C ANISOU 3721 CA THR C 110 4578 3717 3474 254 -161 -100 C ATOM 3722 C THR C 110 35.054 47.153 30.164 1.00 31.60 C ANISOU 3722 C THR C 110 4702 3715 3588 185 -278 -33 C ATOM 3723 O THR C 110 35.542 46.831 29.077 1.00 31.49 O ANISOU 3723 O THR C 110 4668 3738 3557 112 -314 79 O ATOM 3724 CB THR C 110 34.564 44.921 31.194 1.00 30.26 C ANISOU 3724 CB THR C 110 4489 3755 3255 206 -98 -50 C ATOM 3725 OG1 THR C 110 33.631 44.202 32.004 1.00 31.05 O ANISOU 3725 OG1 THR C 110 4555 3941 3301 234 -9 -91 O ATOM 3726 CG2 THR C 110 35.860 45.080 31.988 1.00 30.12 C ANISOU 3726 CG2 THR C 110 4532 3752 3159 150 -132 -58 C ATOM 3727 N GLN C 111 35.439 48.230 30.834 1.00 32.91 N ANISOU 3727 N GLN C 111 4921 3788 3796 191 -339 -111 N ATOM 3728 CA GLN C 111 36.484 49.107 30.319 1.00 33.89 C ANISOU 3728 CA GLN C 111 5089 3830 3957 105 -468 -32 C ATOM 3729 C GLN C 111 37.873 48.669 30.824 1.00 33.09 C ANISOU 3729 C GLN C 111 5028 3823 3720 29 -451 -12 C ATOM 3730 O GLN C 111 38.115 48.636 32.027 1.00 33.65 O ANISOU 3730 O GLN C 111 5138 3921 3728 49 -412 -110 O ATOM 3731 CB GLN C 111 36.191 50.529 30.779 1.00 35.88 C ANISOU 3731 CB GLN C 111 5371 3898 4365 151 -572 -136 C ATOM 3732 CG GLN C 111 36.061 51.558 29.677 1.00 39.36 C ANISOU 3732 CG GLN C 111 5802 4173 4979 104 -750 -15 C ATOM 3733 CD GLN C 111 35.851 52.951 30.239 1.00 43.98 C ANISOU 3733 CD GLN C 111 6409 4531 5772 161 -883 -139 C ATOM 3734 OE1 GLN C 111 36.688 53.457 30.999 1.00 46.55 O ANISOU 3734 OE1 GLN C 111 6794 4819 6072 133 -916 -218 O ATOM 3735 NE2 GLN C 111 34.732 53.576 29.884 1.00 44.97 N ANISOU 3735 NE2 GLN C 111 6472 4490 6123 244 -973 -171 N ATOM 3736 N LEU C 112 38.788 48.331 29.924 1.00 32.12 N ANISOU 3736 N LEU C 112 4882 3772 3550 -66 -482 104 N ATOM 3737 CA LEU C 112 40.135 47.965 30.349 1.00 31.53 C ANISOU 3737 CA LEU C 112 4819 3777 3383 -131 -481 115 C ATOM 3738 C LEU C 112 41.162 49.071 30.092 1.00 32.52 C ANISOU 3738 C LEU C 112 4981 3850 3525 -236 -602 171 C ATOM 3739 O LEU C 112 41.182 49.655 29.010 1.00 33.46 O ANISOU 3739 O LEU C 112 5079 3951 3685 -318 -683 271 O ATOM 3740 CB LEU C 112 40.566 46.683 29.645 1.00 30.65 C ANISOU 3740 CB LEU C 112 4622 3805 3218 -160 -421 160 C ATOM 3741 CG LEU C 112 41.917 46.051 29.992 1.00 29.67 C ANISOU 3741 CG LEU C 112 4466 3765 3041 -206 -422 159 C ATOM 3742 CD1 LEU C 112 41.989 45.716 31.460 1.00 29.55 C ANISOU 3742 CD1 LEU C 112 4504 3728 2994 -161 -408 115 C ATOM 3743 CD2 LEU C 112 42.139 44.808 29.170 1.00 28.05 C ANISOU 3743 CD2 LEU C 112 4146 3671 2842 -209 -370 154 C ATOM 3744 N ILE C 113 41.985 49.374 31.096 1.00 32.85 N ANISOU 3744 N ILE C 113 5077 3875 3529 -255 -629 123 N ATOM 3745 CA ILE C 113 43.186 50.198 30.906 1.00 33.65 C ANISOU 3745 CA ILE C 113 5202 3958 3627 -374 -740 187 C ATOM 3746 C ILE C 113 44.416 49.366 31.253 1.00 33.22 C ANISOU 3746 C ILE C 113 5107 4039 3476 -420 -704 198 C ATOM 3747 O ILE C 113 44.511 48.803 32.359 1.00 33.16 O ANISOU 3747 O ILE C 113 5124 4054 3423 -369 -660 133 O ATOM 3748 CB ILE C 113 43.251 51.478 31.817 1.00 35.18 C ANISOU 3748 CB ILE C 113 5490 3988 3888 -372 -840 110 C ATOM 3749 CG1 ILE C 113 41.926 52.271 31.867 1.00 35.88 C ANISOU 3749 CG1 ILE C 113 5602 3905 4125 -277 -877 27 C ATOM 3750 CG2 ILE C 113 44.456 52.337 31.425 1.00 35.52 C ANISOU 3750 CG2 ILE C 113 5551 4005 3941 -520 -977 213 C ATOM 3751 CD1 ILE C 113 41.634 53.148 30.672 1.00 37.53 C ANISOU 3751 CD1 ILE C 113 5796 3988 4476 -340 -1021 156 C ATOM 3752 N VAL C 114 45.355 49.302 30.315 1.00 32.84 N ANISOU 3752 N VAL C 114 4984 4096 3399 -532 -733 280 N ATOM 3753 CA VAL C 114 46.618 48.603 30.521 1.00 32.29 C ANISOU 3753 CA VAL C 114 4841 4149 3277 -575 -718 276 C ATOM 3754 C VAL C 114 47.737 49.632 30.601 1.00 33.05 C ANISOU 3754 C VAL C 114 4964 4237 3356 -705 -827 331 C ATOM 3755 O VAL C 114 48.030 50.307 29.601 1.00 33.86 O ANISOU 3755 O VAL C 114 5034 4383 3448 -833 -888 420 O ATOM 3756 CB VAL C 114 46.922 47.639 29.348 1.00 32.25 C ANISOU 3756 CB VAL C 114 4684 4315 3254 -607 -649 277 C ATOM 3757 CG1 VAL C 114 48.219 46.878 29.587 1.00 32.35 C ANISOU 3757 CG1 VAL C 114 4589 4437 3266 -626 -642 237 C ATOM 3758 CG2 VAL C 114 45.753 46.682 29.091 1.00 31.33 C ANISOU 3758 CG2 VAL C 114 4540 4195 3168 -495 -557 231 C ATOM 3759 N ILE C 115 48.363 49.759 31.775 1.00 32.82 N ANISOU 3759 N ILE C 115 4992 4166 3312 -698 -866 295 N ATOM 3760 CA ILE C 115 49.510 50.676 31.951 1.00 32.98 C ANISOU 3760 CA ILE C 115 5034 4179 3316 -827 -977 345 C ATOM 3761 C ILE C 115 50.743 50.063 31.300 1.00 32.71 C ANISOU 3761 C ILE C 115 4848 4333 3246 -915 -961 384 C ATOM 3762 O ILE C 115 51.135 48.956 31.661 1.00 32.64 O ANISOU 3762 O ILE C 115 4757 4399 3246 -849 -907 333 O ATOM 3763 CB ILE C 115 49.844 50.942 33.448 1.00 33.41 C ANISOU 3763 CB ILE C 115 5188 4156 3349 -805 -1025 283 C ATOM 3764 CG1 ILE C 115 48.602 51.353 34.267 1.00 33.47 C ANISOU 3764 CG1 ILE C 115 5312 4028 3376 -704 -1005 177 C ATOM 3765 CG2 ILE C 115 50.998 51.924 33.584 1.00 33.39 C ANISOU 3765 CG2 ILE C 115 5210 4135 3340 -945 -1151 336 C ATOM 3766 CD1 ILE C 115 48.081 52.758 34.016 1.00 35.60 C ANISOU 3766 CD1 ILE C 115 5660 4123 3742 -726 -1102 158 C ATOM 3767 N PRO C 116 51.358 50.771 30.341 1.00 64.04 N ANISOU 3767 N PRO C 116 9285 7540 7507 -2897 -514 3520 N ATOM 3768 CA PRO C 116 52.552 50.261 29.659 1.00 62.51 C ANISOU 3768 CA PRO C 116 9261 7010 7480 -2660 -853 3309 C ATOM 3769 C PRO C 116 53.802 50.342 30.534 1.00 62.89 C ANISOU 3769 C PRO C 116 9499 7201 7194 -2402 -962 3425 C ATOM 3770 O PRO C 116 53.962 51.299 31.291 1.00 61.59 O ANISOU 3770 O PRO C 116 9326 7473 6602 -2328 -828 3406 O ATOM 3771 CB PRO C 116 52.689 51.206 28.468 1.00 57.76 C ANISOU 3771 CB PRO C 116 8517 6527 6904 -2513 -872 2778 C ATOM 3772 CG PRO C 116 52.073 52.481 28.931 1.00 55.82 C ANISOU 3772 CG PRO C 116 8106 6767 6337 -2561 -588 2717 C ATOM 3773 CD PRO C 116 50.948 52.092 29.828 1.00 60.19 C ANISOU 3773 CD PRO C 116 8584 7404 6883 -2834 -358 3130 C ATOM 3774 N ASP C 117 54.678 49.347 30.435 1.00 65.12 N ANISOU 3774 N ASP C 117 9955 7105 7684 -2245 -1244 3523 N ATOM 3775 CA ASP C 117 55.925 49.371 31.204 1.00 66.60 C ANISOU 3775 CA ASP C 117 10275 7411 7618 -1971 -1427 3625 C ATOM 3776 C ASP C 117 56.965 50.220 30.480 1.00 63.02 C ANISOU 3776 C ASP C 117 9660 7126 7160 -1699 -1521 3160 C ATOM 3777 O ASP C 117 57.430 49.856 29.402 1.00 62.19 O ANISOU 3777 O ASP C 117 9504 6748 7378 -1541 -1626 2904 O ATOM 3778 CB ASP C 117 56.453 47.951 31.482 1.00 71.08 C ANISOU 3778 CB ASP C 117 11074 7499 8433 -1873 -1701 3968 C ATOM 3779 CG ASP C 117 57.570 47.916 32.549 1.00 73.79 C ANISOU 3779 CG ASP C 117 11564 8004 8469 -1610 -1924 4195 C ATOM 3780 OD1 ASP C 117 57.881 48.948 33.195 1.00 71.77 O ANISOU 3780 OD1 ASP C 117 11257 8231 7781 -1544 -1884 4106 O ATOM 3781 OD2 ASP C 117 58.142 46.823 32.750 1.00 78.00 O ANISOU 3781 OD2 ASP C 117 12282 8145 9210 -1455 -2190 4457 O ATOM 3782 N ILE C 118 57.307 51.362 31.079 1.00 61.95 N ANISOU 3782 N ILE C 118 9452 7432 6656 -1646 -1468 3054 N ATOM 3783 CA ILE C 118 58.304 52.284 30.526 1.00 59.37 C ANISOU 3783 CA ILE C 118 8929 7278 6352 -1451 -1542 2676 C ATOM 3784 C ILE C 118 59.705 51.798 30.863 1.00 62.26 C ANISOU 3784 C ILE C 118 9288 7559 6810 -1176 -1863 2756 C ATOM 3785 O ILE C 118 60.163 51.911 32.003 1.00 64.82 O ANISOU 3785 O ILE C 118 9706 8068 6854 -1120 -2052 2947 O ATOM 3786 CB ILE C 118 58.079 53.729 31.022 1.00 57.29 C ANISOU 3786 CB ILE C 118 8595 7445 5729 -1531 -1410 2506 C ATOM 3787 CG1 ILE C 118 56.774 54.292 30.440 1.00 54.71 C ANISOU 3787 CG1 ILE C 118 8198 7188 5402 -1728 -1099 2363 C ATOM 3788 CG2 ILE C 118 59.269 54.625 30.681 1.00 55.85 C ANISOU 3788 CG2 ILE C 118 8209 7397 5616 -1371 -1549 2209 C ATOM 3789 CD1 ILE C 118 56.540 53.975 28.960 1.00 52.02 C ANISOU 3789 CD1 ILE C 118 7750 6577 5439 -1726 -1052 2155 C ATOM 3790 N GLN C 119 60.372 51.251 29.850 1.00 62.69 N ANISOU 3790 N GLN C 119 9232 7342 7244 -971 -1933 2596 N ATOM 3791 CA GLN C 119 61.622 50.509 30.037 1.00 66.34 C ANISOU 3791 CA GLN C 119 9656 7641 7911 -657 -2228 2698 C ATOM 3792 C GLN C 119 62.720 51.401 30.610 1.00 66.66 C ANISOU 3792 C GLN C 119 9459 8030 7837 -538 -2411 2620 C ATOM 3793 O GLN C 119 63.276 51.124 31.676 1.00 69.72 O ANISOU 3793 O GLN C 119 9927 8479 8086 -436 -2721 2860 O ATOM 3794 CB GLN C 119 62.092 49.905 28.696 1.00 66.56 C ANISOU 3794 CB GLN C 119 9582 7361 8347 -407 -2183 2456 C ATOM 3795 CG GLN C 119 61.037 49.104 27.911 1.00 67.20 C ANISOU 3795 CG GLN C 119 9892 7054 8587 -523 -2072 2411 C ATOM 3796 CD GLN C 119 60.913 47.637 28.364 1.00 73.01 C ANISOU 3796 CD GLN C 119 10914 7304 9523 -472 -2307 2731 C ATOM 3797 OE1 GLN C 119 60.407 46.798 27.617 1.00 74.47 O ANISOU 3797 OE1 GLN C 119 11270 7057 9969 -478 -2326 2643 O ATOM 3798 NE2 GLN C 119 61.376 47.330 29.583 1.00 75.66 N ANISOU 3798 NE2 GLN C 119 11331 7680 9735 -417 -2525 3103 N ATOM 3799 N ASN C 120 62.995 52.487 29.889 1.00 63.64 N ANISOU 3799 N ASN C 120 8800 7860 7522 -569 -2243 2296 N ATOM 3800 CA ASN C 120 64.169 53.299 30.120 1.00 64.32 C ANISOU 3800 CA ASN C 120 8562 8192 7686 -471 -2422 2178 C ATOM 3801 C ASN C 120 63.800 54.774 30.236 1.00 61.33 C ANISOU 3801 C ASN C 120 8113 8103 7085 -723 -2294 1973 C ATOM 3802 O ASN C 120 63.930 55.538 29.267 1.00 58.71 O ANISOU 3802 O ASN C 120 7555 7822 6931 -765 -2063 1744 O ATOM 3803 CB ASN C 120 65.204 53.056 29.013 1.00 65.18 C ANISOU 3803 CB ASN C 120 8321 8198 8247 -197 -2348 2025 C ATOM 3804 CG ASN C 120 65.637 51.589 28.920 1.00 68.86 C ANISOU 3804 CG ASN C 120 8872 8333 8957 127 -2506 2184 C ATOM 3805 OD1 ASN C 120 66.223 51.026 29.862 1.00 72.38 O ANISOU 3805 OD1 ASN C 120 9345 8741 9417 277 -2872 2417 O ATOM 3806 ND2 ASN C 120 65.351 50.966 27.777 1.00 67.53 N ANISOU 3806 ND2 ASN C 120 8783 7904 8971 264 -2264 2046 N ATOM 3807 N PRO C 121 63.354 55.179 31.443 1.00 62.00 N ANISOU 3807 N PRO C 121 8427 8370 6759 -862 -2443 2064 N ATOM 3808 CA PRO C 121 62.937 56.549 31.736 1.00 60.00 C ANISOU 3808 CA PRO C 121 8189 8355 6252 -1060 -2366 1849 C ATOM 3809 C PRO C 121 64.050 57.566 31.457 1.00 59.97 C ANISOU 3809 C PRO C 121 7814 8447 6523 -1064 -2524 1617 C ATOM 3810 O PRO C 121 65.225 57.304 31.739 1.00 63.20 O ANISOU 3810 O PRO C 121 7988 8865 7161 -924 -2857 1672 O ATOM 3811 CB PRO C 121 62.633 56.512 33.243 1.00 63.08 C ANISOU 3811 CB PRO C 121 8915 8920 6134 -1076 -2596 2014 C ATOM 3812 CG PRO C 121 62.494 55.083 33.580 1.00 65.63 C ANISOU 3812 CG PRO C 121 9441 9068 6428 -963 -2658 2384 C ATOM 3813 CD PRO C 121 63.418 54.365 32.667 1.00 65.86 C ANISOU 3813 CD PRO C 121 9186 8852 6984 -775 -2741 2380 C ATOM 3814 N ASP C 122 63.671 58.711 30.903 1.00 56.64 N ANISOU 3814 N ASP C 122 7318 8078 6126 -1231 -2298 1386 N ATOM 3815 CA ASP C 122 64.596 59.809 30.663 1.00 56.83 C ANISOU 3815 CA ASP C 122 7004 8151 6436 -1315 -2421 1197 C ATOM 3816 C ASP C 122 63.827 61.126 30.743 1.00 54.56 C ANISOU 3816 C ASP C 122 6873 7914 5943 -1516 -2297 974 C ATOM 3817 O ASP C 122 63.751 61.854 29.749 1.00 52.61 O ANISOU 3817 O ASP C 122 6469 7594 5927 -1608 -2035 867 O ATOM 3818 CB ASP C 122 65.236 59.646 29.283 1.00 56.00 C ANISOU 3818 CB ASP C 122 6528 7943 6807 -1234 -2155 1204 C ATOM 3819 CG ASP C 122 66.569 60.344 29.169 1.00 59.28 C ANISOU 3819 CG ASP C 122 6464 8406 7654 -1281 -2337 1149 C ATOM 3820 OD1 ASP C 122 67.069 60.851 30.198 1.00 63.83 O ANISOU 3820 OD1 ASP C 122 6991 9061 8201 -1375 -2773 1087 O ATOM 3821 OD2 ASP C 122 67.122 60.378 28.050 1.00 58.68 O ANISOU 3821 OD2 ASP C 122 6053 8295 7946 -1221 -2047 1174 O ATOM 3822 N PRO C 123 63.251 61.440 31.924 1.00 55.40 N ANISOU 3822 N PRO C 123 7317 8143 5589 -1548 -2474 911 N ATOM 3823 CA PRO C 123 62.289 62.549 32.052 1.00 53.71 C ANISOU 3823 CA PRO C 123 7323 7966 5119 -1660 -2305 690 C ATOM 3824 C PRO C 123 62.868 63.916 31.681 1.00 54.07 C ANISOU 3824 C PRO C 123 7162 7909 5472 -1810 -2410 439 C ATOM 3825 O PRO C 123 63.894 64.340 32.226 1.00 57.49 O ANISOU 3825 O PRO C 123 7447 8335 6063 -1868 -2830 340 O ATOM 3826 CB PRO C 123 61.887 62.510 33.525 1.00 56.59 C ANISOU 3826 CB PRO C 123 8072 8516 4913 -1590 -2526 675 C ATOM 3827 CG PRO C 123 63.001 61.815 34.207 1.00 60.72 C ANISOU 3827 CG PRO C 123 8525 9080 5465 -1495 -2976 816 C ATOM 3828 CD PRO C 123 63.594 60.854 33.232 1.00 59.29 C ANISOU 3828 CD PRO C 123 8007 8757 5762 -1438 -2870 1032 C ATOM 3829 N ALA C 124 62.209 64.585 30.740 1.00 50.87 N ANISOU 3829 N ALA C 124 6743 7401 5186 -1883 -2060 358 N ATOM 3830 CA ALA C 124 62.695 65.847 30.207 1.00 51.26 C ANISOU 3830 CA ALA C 124 6605 7285 5585 -2045 -2092 197 C ATOM 3831 C ALA C 124 61.545 66.777 29.875 1.00 49.16 C ANISOU 3831 C ALA C 124 6573 6938 5166 -2067 -1832 41 C ATOM 3832 O ALA C 124 60.419 66.327 29.640 1.00 46.18 O ANISOU 3832 O ALA C 124 6370 6640 4535 -1961 -1536 101 O ATOM 3833 CB ALA C 124 63.534 65.601 28.982 1.00 50.56 C ANISOU 3833 CB ALA C 124 6110 7110 5989 -2078 -1905 374 C ATOM 3834 N VAL C 125 61.840 68.076 29.876 1.00 51.06 N ANISOU 3834 N VAL C 125 6797 6994 5610 -2207 -1978 -156 N ATOM 3835 CA VAL C 125 60.880 69.104 29.472 1.00 49.95 C ANISOU 3835 CA VAL C 125 6856 6707 5417 -2206 -1768 -305 C ATOM 3836 C VAL C 125 61.491 69.955 28.364 1.00 50.52 C ANISOU 3836 C VAL C 125 6683 6513 6001 -2383 -1672 -227 C ATOM 3837 O VAL C 125 62.489 70.644 28.584 1.00 53.77 O ANISOU 3837 O VAL C 125 6919 6749 6763 -2581 -1963 -293 O ATOM 3838 CB VAL C 125 60.455 70.005 30.656 1.00 52.76 C ANISOU 3838 CB VAL C 125 7555 7027 5465 -2161 -2034 -652 C ATOM 3839 CG1 VAL C 125 59.685 71.224 30.160 1.00 52.38 C ANISOU 3839 CG1 VAL C 125 7663 6739 5501 -2148 -1871 -820 C ATOM 3840 CG2 VAL C 125 59.624 69.221 31.651 1.00 52.25 C ANISOU 3840 CG2 VAL C 125 7770 7267 4814 -1951 -1979 -671 C ATOM 3841 N TYR C 126 60.888 69.911 27.179 1.00 47.98 N ANISOU 3841 N TYR C 126 6352 6156 5724 -2322 -1281 -68 N ATOM 3842 CA TYR C 126 61.418 70.651 26.034 1.00 49.22 C ANISOU 3842 CA TYR C 126 6318 6091 6294 -2462 -1111 88 C ATOM 3843 C TYR C 126 60.558 71.830 25.593 1.00 49.35 C ANISOU 3843 C TYR C 126 6577 5865 6308 -2451 -999 3 C ATOM 3844 O TYR C 126 59.351 71.870 25.853 1.00 47.77 O ANISOU 3844 O TYR C 126 6650 5727 5773 -2268 -938 -144 O ATOM 3845 CB TYR C 126 61.648 69.709 24.856 1.00 47.23 C ANISOU 3845 CB TYR C 126 5873 5973 6101 -2369 -764 372 C ATOM 3846 CG TYR C 126 62.572 68.563 25.180 1.00 48.22 C ANISOU 3846 CG TYR C 126 5736 6285 6300 -2335 -863 467 C ATOM 3847 CD1 TYR C 126 63.952 68.758 25.314 1.00 51.45 C ANISOU 3847 CD1 TYR C 126 5758 6652 7137 -2498 -1027 551 C ATOM 3848 CD2 TYR C 126 62.069 67.280 25.358 1.00 46.01 C ANISOU 3848 CD2 TYR C 126 5567 6196 5717 -2141 -816 490 C ATOM 3849 CE1 TYR C 126 64.796 67.691 25.619 1.00 52.24 C ANISOU 3849 CE1 TYR C 126 5592 6925 7332 -2412 -1143 639 C ATOM 3850 CE2 TYR C 126 62.905 66.215 25.656 1.00 46.25 C ANISOU 3850 CE2 TYR C 126 5389 6349 5833 -2070 -930 588 C ATOM 3851 CZ TYR C 126 64.256 66.421 25.782 1.00 48.97 C ANISOU 3851 CZ TYR C 126 5355 6675 6575 -2177 -1093 656 C ATOM 3852 OH TYR C 126 65.050 65.344 26.077 1.00 50.09 O ANISOU 3852 OH TYR C 126 5276 6939 6817 -2051 -1224 753 O ATOM 3853 N GLN C 127 61.197 72.786 24.925 1.00 52.07 N ANISOU 3853 N GLN C 127 6794 5926 7065 -2642 -964 129 N ATOM 3854 CA GLN C 127 60.483 73.872 24.262 1.00 52.90 C ANISOU 3854 CA GLN C 127 7123 5751 7225 -2618 -829 146 C ATOM 3855 C GLN C 127 60.472 73.659 22.735 1.00 52.04 C ANISOU 3855 C GLN C 127 6934 5674 7163 -2561 -417 508 C ATOM 3856 O GLN C 127 61.529 73.524 22.101 1.00 53.74 O ANISOU 3856 O GLN C 127 6856 5894 7668 -2708 -258 780 O ATOM 3857 CB GLN C 127 61.100 75.219 24.631 1.00 57.26 C ANISOU 3857 CB GLN C 127 7680 5879 8199 -2877 -1111 43 C ATOM 3858 CG GLN C 127 60.117 76.375 24.564 1.00 58.41 C ANISOU 3858 CG GLN C 127 8195 5694 8305 -2770 -1140 -115 C ATOM 3859 CD GLN C 127 60.713 77.687 25.060 1.00 63.67 C ANISOU 3859 CD GLN C 127 8921 5859 9411 -3030 -1499 -280 C ATOM 3860 OE1 GLN C 127 60.859 78.641 24.291 1.00 65.53 O ANISOU 3860 OE1 GLN C 127 9186 5696 10016 -3175 -1416 -71 O ATOM 3861 NE2 GLN C 127 61.074 77.735 26.346 1.00 65.37 N ANISOU 3861 NE2 GLN C 127 9182 6068 9587 -3093 -1928 -649 N ATOM 3862 N LEU C 128 59.266 73.604 22.168 1.00 50.05 N ANISOU 3862 N LEU C 128 6938 5474 6605 -2322 -249 505 N ATOM 3863 CA LEU C 128 59.057 73.440 20.724 1.00 49.63 C ANISOU 3863 CA LEU C 128 6926 5460 6473 -2202 80 799 C ATOM 3864 C LEU C 128 58.418 74.702 20.159 1.00 51.67 C ANISOU 3864 C LEU C 128 7438 5395 6798 -2159 104 869 C ATOM 3865 O LEU C 128 57.546 75.290 20.797 1.00 51.87 O ANISOU 3865 O LEU C 128 7664 5288 6756 -2061 -86 616 O ATOM 3866 CB LEU C 128 58.141 72.250 20.452 1.00 45.96 C ANISOU 3866 CB LEU C 128 6549 5305 5608 -1945 169 738 C ATOM 3867 CG LEU C 128 58.527 70.853 20.942 1.00 44.48 C ANISOU 3867 CG LEU C 128 6188 5401 5312 -1925 140 683 C ATOM 3868 CD1 LEU C 128 58.529 70.758 22.457 1.00 44.22 C ANISOU 3868 CD1 LEU C 128 6127 5414 5259 -2004 -139 442 C ATOM 3869 CD2 LEU C 128 57.550 69.853 20.379 1.00 41.72 C ANISOU 3869 CD2 LEU C 128 5964 5239 4650 -1705 228 666 C ATOM 3870 N ARG C 129 58.835 75.115 18.967 1.00 54.10 N ANISOU 3870 N ARG C 129 7755 5581 7219 -2197 358 1226 N ATOM 3871 CA ARG C 129 58.370 76.392 18.404 1.00 57.22 C ANISOU 3871 CA ARG C 129 8410 5603 7727 -2175 366 1370 C ATOM 3872 C ARG C 129 57.418 76.228 17.216 1.00 56.33 C ANISOU 3872 C ARG C 129 8559 5600 7244 -1863 536 1538 C ATOM 3873 O ARG C 129 57.548 75.276 16.444 1.00 55.24 O ANISOU 3873 O ARG C 129 8382 5768 6837 -1740 749 1675 O ATOM 3874 CB ARG C 129 59.561 77.266 18.009 1.00 61.99 C ANISOU 3874 CB ARG C 129 8868 5889 8797 -2499 490 1714 C ATOM 3875 CG ARG C 129 60.435 77.705 19.176 1.00 65.42 C ANISOU 3875 CG ARG C 129 9066 6104 9686 -2837 195 1520 C ATOM 3876 CD ARG C 129 61.126 79.026 18.842 1.00 73.96 C ANISOU 3876 CD ARG C 129 10124 6666 11312 -3160 199 1812 C ATOM 3877 NE ARG C 129 61.643 79.746 20.012 1.00 78.42 N ANISOU 3877 NE ARG C 129 10598 6871 12327 -3460 -236 1521 N ATOM 3878 CZ ARG C 129 60.893 80.362 20.927 1.00 79.32 C ANISOU 3878 CZ ARG C 129 11025 6724 12389 -3354 -620 1081 C ATOM 3879 NH1 ARG C 129 59.563 80.339 20.851 1.00 76.31 N ANISOU 3879 NH1 ARG C 129 10999 6426 11571 -2958 -595 901 N ATOM 3880 NH2 ARG C 129 61.480 80.997 21.936 1.00 83.52 N ANISOU 3880 NH2 ARG C 129 11503 6919 13312 -3626 -1045 799 N ATOM 3881 N ASP C 130 56.464 77.158 17.086 1.00 57.46 N ANISOU 3881 N ASP C 130 8980 5476 7375 -1706 400 1500 N ATOM 3882 CA ASP C 130 55.501 77.186 15.970 1.00 57.33 C ANISOU 3882 CA ASP C 130 9231 5514 7038 -1391 464 1662 C ATOM 3883 C ASP C 130 56.226 77.440 14.646 1.00 60.28 C ANISOU 3883 C ASP C 130 9709 5826 7367 -1431 776 2163 C ATOM 3884 O ASP C 130 56.959 78.418 14.511 1.00 64.10 O ANISOU 3884 O ASP C 130 10204 5957 8195 -1660 873 2444 O ATOM 3885 CB ASP C 130 54.422 78.259 16.230 1.00 58.98 C ANISOU 3885 CB ASP C 130 9675 5401 7333 -1200 221 1520 C ATOM 3886 CG ASP C 130 53.312 78.301 15.151 1.00 60.00 C ANISOU 3886 CG ASP C 130 10054 5595 7150 -835 186 1660 C ATOM 3887 OD1 ASP C 130 53.572 77.997 13.966 1.00 61.33 O ANISOU 3887 OD1 ASP C 130 10346 5886 7069 -769 370 1991 O ATOM 3888 OD2 ASP C 130 52.164 78.676 15.495 1.00 59.92 O ANISOU 3888 OD2 ASP C 130 10116 5515 7135 -583 -37 1431 O ATOM 3889 N SER C 131 56.012 76.547 13.681 1.00 58.96 N ANISOU 3889 N SER C 131 9633 5998 6771 -1207 934 2273 N ATOM 3890 CA SER C 131 56.654 76.621 12.363 1.00 62.43 C ANISOU 3890 CA SER C 131 10220 6485 7016 -1160 1293 2738 C ATOM 3891 C SER C 131 56.405 77.941 11.625 1.00 67.00 C ANISOU 3891 C SER C 131 11132 6684 7642 -1108 1325 3125 C ATOM 3892 O SER C 131 57.309 78.509 11.032 1.00 71.22 O ANISOU 3892 O SER C 131 11681 7063 8315 -1279 1650 3583 O ATOM 3893 CB SER C 131 56.192 75.458 11.494 1.00 61.00 C ANISOU 3893 CB SER C 131 10195 6707 6274 -835 1346 2672 C ATOM 3894 OG SER C 131 54.783 75.460 11.385 1.00 59.74 O ANISOU 3894 OG SER C 131 10257 6553 5887 -561 995 2457 O ATOM 3895 N LYS C 132 55.169 78.414 11.664 1.00 66.66 N ANISOU 3895 N LYS C 132 11333 6487 7509 -863 996 2969 N ATOM 3896 CA LYS C 132 54.816 79.675 11.057 1.00 71.31 C ANISOU 3896 CA LYS C 132 12264 6664 8166 -764 948 3310 C ATOM 3897 C LYS C 132 55.124 80.855 11.994 1.00 73.59 C ANISOU 3897 C LYS C 132 12477 6412 9072 -1048 811 3270 C ATOM 3898 O LYS C 132 55.048 82.016 11.582 1.00 78.30 O ANISOU 3898 O LYS C 132 13347 6544 9861 -1044 785 3597 O ATOM 3899 CB LYS C 132 53.338 79.654 10.653 1.00 70.55 C ANISOU 3899 CB LYS C 132 12434 6640 7732 -325 611 3151 C ATOM 3900 N SER C 133 55.488 80.562 13.242 1.00 71.09 N ANISOU 3900 N SER C 133 11831 6126 9054 -1285 696 2873 N ATOM 3901 CA SER C 133 55.666 81.616 14.253 1.00 73.66 C ANISOU 3901 CA SER C 133 12132 5943 9913 -1506 464 2696 C ATOM 3902 C SER C 133 56.854 81.454 15.200 1.00 73.67 C ANISOU 3902 C SER C 133 11769 5915 10308 -1938 477 2553 C ATOM 3903 O SER C 133 56.816 80.640 16.132 1.00 69.44 O ANISOU 3903 O SER C 133 11009 5692 9684 -1945 350 2134 O ATOM 3904 CB SER C 133 54.388 81.802 15.077 1.00 71.60 C ANISOU 3904 CB SER C 133 11971 5632 9600 -1200 104 2195 C ATOM 3905 OG SER C 133 53.494 82.672 14.417 1.00 75.12 O ANISOU 3905 OG SER C 133 12766 5769 10009 -889 -20 2367 O ATOM 3906 N SER C 134 57.889 82.262 14.964 1.00 78.96 N ANISOU 3906 N SER C 134 12377 6190 11436 -2304 603 2930 N ATOM 3907 CA SER C 134 59.025 82.386 15.880 1.00 80.73 C ANISOU 3907 CA SER C 134 12244 6257 12174 -2753 505 2806 C ATOM 3908 C SER C 134 58.569 82.408 17.345 1.00 78.58 C ANISOU 3908 C SER C 134 11971 5919 11968 -2709 54 2143 C ATOM 3909 O SER C 134 59.063 81.629 18.166 1.00 76.14 O ANISOU 3909 O SER C 134 11364 5918 11646 -2834 -32 1860 O ATOM 3910 CB SER C 134 59.820 83.670 15.581 1.00 87.86 C ANISOU 3910 CB SER C 134 13168 6515 13701 -3145 538 3233 C ATOM 3911 OG SER C 134 60.634 83.552 14.426 1.00 90.84 O ANISOU 3911 OG SER C 134 13401 7020 14095 -3303 1040 3887 O ATOM 3912 N ASP C 135 57.597 83.279 17.634 1.00 79.94 N ANISOU 3912 N ASP C 135 12500 5711 12163 -2478 -212 1914 N ATOM 3913 CA ASP C 135 57.173 83.647 18.997 1.00 79.89 C ANISOU 3913 CA ASP C 135 12588 5513 12254 -2406 -620 1303 C ATOM 3914 C ASP C 135 56.344 82.636 19.827 1.00 74.43 C ANISOU 3914 C ASP C 135 11836 5374 11070 -2087 -691 815 C ATOM 3915 O ASP C 135 56.549 82.522 21.038 1.00 74.23 O ANISOU 3915 O ASP C 135 11746 5386 11072 -2161 -931 382 O ATOM 3916 CB ASP C 135 56.455 85.007 18.962 1.00 84.52 C ANISOU 3916 CB ASP C 135 13589 5450 13075 -2222 -846 1241 C ATOM 3917 CG ASP C 135 55.570 85.184 17.719 1.00 85.03 C ANISOU 3917 CG ASP C 135 13902 5522 12885 -1870 -649 1629 C ATOM 3918 OD1 ASP C 135 55.934 86.005 16.847 1.00 89.84 O ANISOU 3918 OD1 ASP C 135 14681 5679 13775 -2014 -554 2130 O ATOM 3919 OD2 ASP C 135 54.519 84.510 17.609 1.00 81.27 O ANISOU 3919 OD2 ASP C 135 13446 5493 11940 -1459 -609 1458 O ATOM 3920 N LYS C 136 55.419 81.914 19.194 1.00 70.51 N ANISOU 3920 N LYS C 136 11367 5293 10131 -1746 -501 896 N ATOM 3921 CA LYS C 136 54.521 81.012 19.927 1.00 66.03 C ANISOU 3921 CA LYS C 136 10723 5203 9164 -1465 -543 500 C ATOM 3922 C LYS C 136 55.171 79.654 20.186 1.00 61.93 C ANISOU 3922 C LYS C 136 9888 5192 8450 -1640 -417 498 C ATOM 3923 O LYS C 136 55.826 79.103 19.301 1.00 61.45 O ANISOU 3923 O LYS C 136 9688 5294 8368 -1776 -191 856 O ATOM 3924 CB LYS C 136 53.207 80.837 19.163 1.00 64.82 C ANISOU 3924 CB LYS C 136 10686 5233 8711 -1051 -466 574 C ATOM 3925 CG LYS C 136 52.505 82.153 18.854 1.00 69.97 C ANISOU 3925 CG LYS C 136 11649 5381 9557 -805 -611 600 C ATOM 3926 CD LYS C 136 51.198 81.973 18.095 1.00 70.51 C ANISOU 3926 CD LYS C 136 11783 5650 9358 -373 -600 676 C ATOM 3927 CE LYS C 136 50.482 83.316 17.977 1.00 75.95 C ANISOU 3927 CE LYS C 136 12770 5810 10278 -72 -792 649 C ATOM 3928 NZ LYS C 136 49.373 83.288 16.989 1.00 76.91 N ANISOU 3928 NZ LYS C 136 12964 6055 10203 330 -832 841 N ATOM 3929 N SER C 137 54.983 79.104 21.386 1.00 59.59 N ANISOU 3929 N SER C 137 9505 5148 7987 -1600 -545 110 N ATOM 3930 CA SER C 137 55.600 77.814 21.729 1.00 55.91 C ANISOU 3930 CA SER C 137 8769 5117 7358 -1746 -470 115 C ATOM 3931 C SER C 137 54.785 76.898 22.647 1.00 52.70 C ANISOU 3931 C SER C 137 8319 5123 6581 -1544 -493 -182 C ATOM 3932 O SER C 137 53.772 77.297 23.213 1.00 53.59 O ANISOU 3932 O SER C 137 8577 5224 6560 -1294 -554 -447 O ATOM 3933 CB SER C 137 56.975 78.044 22.345 1.00 58.27 C ANISOU 3933 CB SER C 137 8917 5242 7980 -2108 -635 89 C ATOM 3934 OG SER C 137 56.850 78.654 23.614 1.00 61.07 O ANISOU 3934 OG SER C 137 9427 5414 8363 -2094 -950 -334 O ATOM 3935 N VAL C 138 55.250 75.662 22.785 1.00 49.66 N ANISOU 3935 N VAL C 138 7724 5094 6049 -1645 -417 -109 N ATOM 3936 CA VAL C 138 54.654 74.680 23.694 1.00 47.27 C ANISOU 3936 CA VAL C 138 7366 5168 5427 -1524 -420 -304 C ATOM 3937 C VAL C 138 55.749 74.072 24.571 1.00 47.35 C ANISOU 3937 C VAL C 138 7245 5303 5442 -1735 -555 -355 C ATOM 3938 O VAL C 138 56.935 74.123 24.221 1.00 48.07 O ANISOU 3938 O VAL C 138 7189 5273 5802 -1963 -594 -190 O ATOM 3939 CB VAL C 138 53.892 73.540 22.928 1.00 44.20 C ANISOU 3939 CB VAL C 138 6871 5091 4833 -1389 -229 -136 C ATOM 3940 CG1 VAL C 138 52.639 74.074 22.245 1.00 44.14 C ANISOU 3940 CG1 VAL C 138 6965 5017 4791 -1138 -180 -134 C ATOM 3941 CG2 VAL C 138 54.797 72.837 21.903 1.00 42.88 C ANISOU 3941 CG2 VAL C 138 6581 4972 4741 -1523 -113 151 C ATOM 3942 N CYS C 139 55.365 73.506 25.710 1.00 47.02 N ANISOU 3942 N CYS C 139 7239 5515 5111 -1646 -620 -555 N ATOM 3943 CA CYS C 139 56.327 72.772 26.515 1.00 47.61 C ANISOU 3943 CA CYS C 139 7209 5748 5134 -1798 -777 -564 C ATOM 3944 C CYS C 139 55.927 71.309 26.623 1.00 44.51 C ANISOU 3944 C CYS C 139 6715 5716 4481 -1724 -630 -425 C ATOM 3945 O CYS C 139 54.855 70.980 27.127 1.00 44.09 O ANISOU 3945 O CYS C 139 6744 5861 4146 -1561 -521 -501 O ATOM 3946 CB CYS C 139 56.528 73.409 27.890 1.00 51.32 C ANISOU 3946 CB CYS C 139 7873 6153 5472 -1789 -1068 -901 C ATOM 3947 SG CYS C 139 56.914 75.174 27.831 1.00 58.03 S ANISOU 3947 SG CYS C 139 8894 6464 6689 -1887 -1316 -1122 S ATOM 3948 N LEU C 140 56.803 70.444 26.126 1.00 42.92 N ANISOU 3948 N LEU C 140 6317 5575 4414 -1843 -613 -207 N ATOM 3949 CA LEU C 140 56.576 69.018 26.122 1.00 41.04 C ANISOU 3949 CA LEU C 140 6000 5583 4012 -1791 -514 -60 C ATOM 3950 C LEU C 140 57.311 68.374 27.278 1.00 42.73 C ANISOU 3950 C LEU C 140 6192 5933 4110 -1846 -725 -76 C ATOM 3951 O LEU C 140 58.538 68.407 27.321 1.00 44.56 O ANISOU 3951 O LEU C 140 6276 6092 4561 -1964 -899 -36 O ATOM 3952 CB LEU C 140 57.094 68.437 24.811 1.00 39.76 C ANISOU 3952 CB LEU C 140 5681 5380 4046 -1814 -370 160 C ATOM 3953 CG LEU C 140 57.266 66.930 24.615 1.00 38.05 C ANISOU 3953 CG LEU C 140 5374 5309 3775 -1771 -322 306 C ATOM 3954 CD1 LEU C 140 55.976 66.355 24.121 1.00 37.37 C ANISOU 3954 CD1 LEU C 140 5373 5286 3539 -1666 -194 323 C ATOM 3955 CD2 LEU C 140 58.362 66.660 23.608 1.00 37.35 C ANISOU 3955 CD2 LEU C 140 5119 5157 3916 -1780 -230 456 C ATOM 3956 N PHE C 141 56.561 67.814 28.221 1.00 43.07 N ANISOU 3956 N PHE C 141 6368 6182 3816 -1754 -708 -108 N ATOM 3957 CA PHE C 141 57.120 67.037 29.320 1.00 44.75 C ANISOU 3957 CA PHE C 141 6621 6553 3830 -1764 -899 -59 C ATOM 3958 C PHE C 141 57.077 65.620 28.810 1.00 43.20 C ANISOU 3958 C PHE C 141 6303 6421 3689 -1761 -777 207 C ATOM 3959 O PHE C 141 56.007 65.126 28.460 1.00 42.51 O ANISOU 3959 O PHE C 141 6232 6390 3530 -1717 -557 292 O ATOM 3960 CB PHE C 141 56.251 67.201 30.575 1.00 46.69 C ANISOU 3960 CB PHE C 141 7120 6995 3625 -1641 -875 -189 C ATOM 3961 CG PHE C 141 56.701 66.395 31.771 1.00 49.26 C ANISOU 3961 CG PHE C 141 7569 7512 3634 -1616 -1061 -97 C ATOM 3962 CD1 PHE C 141 58.049 66.110 31.995 1.00 51.49 C ANISOU 3962 CD1 PHE C 141 7764 7737 4061 -1695 -1409 -54 C ATOM 3963 CD2 PHE C 141 55.766 65.955 32.704 1.00 50.81 C ANISOU 3963 CD2 PHE C 141 7961 7964 3382 -1496 -884 -27 C ATOM 3964 CE1 PHE C 141 58.455 65.371 33.115 1.00 54.22 C ANISOU 3964 CE1 PHE C 141 8258 8258 4087 -1635 -1635 50 C ATOM 3965 CE2 PHE C 141 56.156 65.220 33.825 1.00 53.95 C ANISOU 3965 CE2 PHE C 141 8535 8545 3420 -1451 -1048 109 C ATOM 3966 CZ PHE C 141 57.504 64.924 34.033 1.00 55.49 C ANISOU 3966 CZ PHE C 141 8686 8661 3737 -1511 -1456 144 C ATOM 3967 N THR C 142 58.225 64.965 28.724 1.00 43.70 N ANISOU 3967 N THR C 142 6225 6450 3930 -1798 -938 329 N ATOM 3968 CA THR C 142 58.260 63.661 28.060 1.00 42.41 C ANISOU 3968 CA THR C 142 5968 6267 3880 -1756 -833 541 C ATOM 3969 C THR C 142 59.175 62.655 28.746 1.00 44.44 C ANISOU 3969 C THR C 142 6184 6564 4138 -1720 -1060 692 C ATOM 3970 O THR C 142 59.981 63.015 29.599 1.00 47.06 O ANISOU 3970 O THR C 142 6502 6948 4430 -1737 -1336 636 O ATOM 3971 CB THR C 142 58.585 63.801 26.528 1.00 40.74 C ANISOU 3971 CB THR C 142 5595 5911 3972 -1742 -665 556 C ATOM 3972 OG1 THR C 142 58.488 62.528 25.881 1.00 39.42 O ANISOU 3972 OG1 THR C 142 5412 5702 3863 -1656 -581 688 O ATOM 3973 CG2 THR C 142 59.976 64.388 26.291 1.00 42.12 C ANISOU 3973 CG2 THR C 142 5548 6020 4437 -1794 -769 546 C ATOM 3974 N ASP C 143 59.009 61.390 28.381 1.00 44.13 N ANISOU 3974 N ASP C 143 6145 6470 4154 -1658 -988 873 N ATOM 3975 CA ASP C 143 59.861 60.290 28.844 1.00 46.45 C ANISOU 3975 CA ASP C 143 6403 6736 4510 -1573 -1197 1050 C ATOM 3976 C ASP C 143 59.840 60.034 30.370 1.00 49.27 C ANISOU 3976 C ASP C 143 6957 7236 4527 -1568 -1423 1162 C ATOM 3977 O ASP C 143 60.809 59.536 30.948 1.00 51.81 O ANISOU 3977 O ASP C 143 7238 7564 4882 -1486 -1713 1268 O ATOM 3978 CB ASP C 143 61.291 60.435 28.285 1.00 47.38 C ANISOU 3978 CB ASP C 143 6225 6796 4983 -1507 -1310 1016 C ATOM 3979 CG ASP C 143 61.335 60.443 26.748 1.00 46.25 C ANISOU 3979 CG ASP C 143 5945 6540 5088 -1449 -1026 970 C ATOM 3980 OD1 ASP C 143 60.265 60.519 26.098 1.00 43.98 O ANISOU 3980 OD1 ASP C 143 5806 6210 4696 -1476 -812 920 O ATOM 3981 OD2 ASP C 143 62.450 60.378 26.180 1.00 48.74 O ANISOU 3981 OD2 ASP C 143 5996 6830 5694 -1356 -1015 990 O ATOM 3982 N PHE C 144 58.723 60.360 31.010 1.00 49.41 N ANISOU 3982 N PHE C 144 7188 7387 4197 -1623 -1280 1151 N ATOM 3983 CA PHE C 144 58.498 59.961 32.395 1.00 52.90 C ANISOU 3983 CA PHE C 144 7884 7997 4219 -1587 -1391 1317 C ATOM 3984 C PHE C 144 57.874 58.557 32.486 1.00 54.02 C ANISOU 3984 C PHE C 144 8123 8061 4343 -1601 -1257 1671 C ATOM 3985 O PHE C 144 57.203 58.115 31.558 1.00 52.07 O ANISOU 3985 O PHE C 144 7777 7659 4347 -1671 -1041 1711 O ATOM 3986 CB PHE C 144 57.660 61.009 33.144 1.00 53.65 C ANISOU 3986 CB PHE C 144 8171 8307 3908 -1590 -1261 1137 C ATOM 3987 CG PHE C 144 56.379 61.400 32.450 1.00 50.81 C ANISOU 3987 CG PHE C 144 7745 7946 3614 -1647 -876 1062 C ATOM 3988 CD1 PHE C 144 55.187 60.742 32.734 1.00 51.57 C ANISOU 3988 CD1 PHE C 144 7901 8143 3552 -1680 -584 1292 C ATOM 3989 CD2 PHE C 144 56.353 62.452 31.541 1.00 48.08 C ANISOU 3989 CD2 PHE C 144 7259 7499 3509 -1669 -819 790 C ATOM 3990 CE1 PHE C 144 53.997 61.113 32.107 1.00 49.26 C ANISOU 3990 CE1 PHE C 144 7478 7865 3372 -1723 -277 1219 C ATOM 3991 CE2 PHE C 144 55.166 62.826 30.912 1.00 45.68 C ANISOU 3991 CE2 PHE C 144 6894 7198 3266 -1682 -523 727 C ATOM 3992 CZ PHE C 144 53.990 62.154 31.197 1.00 46.14 C ANISOU 3992 CZ PHE C 144 6964 7375 3193 -1703 -270 924 C ATOM 3993 N ASP C 145 58.115 57.851 33.589 1.00 58.05 N ANISOU 3993 N ASP C 145 8843 8646 4569 -1539 -1425 1938 N ATOM 3994 CA ASP C 145 57.524 56.529 33.787 1.00 60.30 C ANISOU 3994 CA ASP C 145 9248 8808 4854 -1584 -1307 2337 C ATOM 3995 C ASP C 145 56.078 56.653 34.260 1.00 61.69 C ANISOU 3995 C ASP C 145 9534 9169 4738 -1705 -920 2473 C ATOM 3996 O ASP C 145 55.605 57.746 34.577 1.00 61.46 O ANISOU 3996 O ASP C 145 9532 9389 4431 -1685 -767 2244 O ATOM 3997 CB ASP C 145 58.357 55.679 34.759 1.00 64.61 C ANISOU 3997 CB ASP C 145 9993 9336 5219 -1454 -1636 2643 C ATOM 3998 CG ASP C 145 58.210 56.119 36.211 1.00 69.08 C ANISOU 3998 CG ASP C 145 10876 10241 5132 -1386 -1694 2732 C ATOM 3999 OD1 ASP C 145 57.857 57.291 36.467 1.00 69.23 O ANISOU 3999 OD1 ASP C 145 10930 10502 4874 -1388 -1586 2431 O ATOM 4000 OD2 ASP C 145 58.457 55.285 37.106 1.00 73.79 O ANISOU 4000 OD2 ASP C 145 11726 10850 5462 -1300 -1862 3103 O ATOM 4001 N SER C 146 55.383 55.528 34.324 1.00 64.01 N ANISOU 4001 N SER C 146 9872 9320 5127 -1823 -760 2855 N ATOM 4002 CA SER C 146 53.947 55.553 34.539 1.00 65.79 C ANISOU 4002 CA SER C 146 10062 9692 5244 -1980 -342 3016 C ATOM 4003 C SER C 146 53.569 55.634 36.018 1.00 71.03 C ANISOU 4003 C SER C 146 10997 10706 5284 -1921 -160 3294 C ATOM 4004 O SER C 146 52.518 55.139 36.440 1.00 74.51 O ANISOU 4004 O SER C 146 11434 11236 5640 -2058 199 3656 O ATOM 4005 CB SER C 146 53.315 54.340 33.862 1.00 66.41 C ANISOU 4005 CB SER C 146 10017 9422 5795 -2189 -260 3297 C ATOM 4006 OG SER C 146 53.605 54.330 32.472 1.00 62.92 O ANISOU 4006 OG SER C 146 9385 8694 5829 -2190 -415 2985 O ATOM 4007 N GLN C 147 54.430 56.273 36.802 1.00 72.55 N ANISOU 4007 N GLN C 147 11422 11109 5036 -1713 -412 3124 N ATOM 4008 CA GLN C 147 54.180 56.486 38.227 1.00 77.77 C ANISOU 4008 CA GLN C 147 12430 12146 4973 -1579 -285 3303 C ATOM 4009 C GLN C 147 54.204 57.983 38.522 1.00 77.08 C ANISOU 4009 C GLN C 147 12417 12343 4528 -1410 -292 2790 C ATOM 4010 O GLN C 147 54.178 58.405 39.680 1.00 81.49 O ANISOU 4010 O GLN C 147 13321 13227 4414 -1222 -274 2773 O ATOM 4011 CB GLN C 147 55.216 55.728 39.062 1.00 81.80 C ANISOU 4011 CB GLN C 147 13258 12614 5207 -1449 -691 3600 C ATOM 4012 CG GLN C 147 55.019 54.210 39.025 1.00 84.63 C ANISOU 4012 CG GLN C 147 13646 12682 5829 -1592 -633 4192 C ATOM 4013 CD GLN C 147 56.291 53.449 38.682 1.00 84.53 C ANISOU 4013 CD GLN C 147 13631 12310 6175 -1502 -1160 4246 C ATOM 4014 OE1 GLN C 147 57.169 53.265 39.527 1.00 88.23 O ANISOU 4014 OE1 GLN C 147 14372 12861 6291 -1300 -1536 4379 O ATOM 4015 NE2 GLN C 147 56.388 52.991 37.433 1.00 80.07 N ANISOU 4015 NE2 GLN C 147 12764 11355 6303 -1615 -1200 4136 N ATOM 4016 N THR C 148 54.239 58.770 37.447 1.00 71.86 N ANISOU 4016 N THR C 148 11464 11530 4309 -1463 -326 2373 N ATOM 4017 CA THR C 148 54.248 60.219 37.517 1.00 71.00 C ANISOU 4017 CA THR C 148 11394 11566 4016 -1332 -357 1870 C ATOM 4018 C THR C 148 52.871 60.773 37.176 1.00 70.39 C ANISOU 4018 C THR C 148 11141 11616 3988 -1348 141 1773 C ATOM 4019 O THR C 148 52.362 60.570 36.074 1.00 67.03 O ANISOU 4019 O THR C 148 10385 10998 4086 -1503 287 1796 O ATOM 4020 CB THR C 148 55.305 60.803 36.559 1.00 66.75 C ANISOU 4020 CB THR C 148 10652 10750 3959 -1374 -745 1513 C ATOM 4021 OG1 THR C 148 56.615 60.474 37.035 1.00 68.83 O ANISOU 4021 OG1 THR C 148 11036 10960 4158 -1315 -1234 1553 O ATOM 4022 CG2 THR C 148 55.186 62.314 36.454 1.00 65.69 C ANISOU 4022 CG2 THR C 148 10531 10661 3768 -1294 -753 1023 C ATOM 4023 N ASN C 149 52.268 61.468 38.134 1.00 74.62 N ANISOU 4023 N ASN C 149 11904 12486 3961 -1150 385 1651 N ATOM 4024 CA ASN C 149 51.000 62.151 37.904 1.00 74.86 C ANISOU 4024 CA ASN C 149 11747 12672 4024 -1084 849 1506 C ATOM 4025 C ASN C 149 51.231 63.503 37.255 1.00 72.02 C ANISOU 4025 C ASN C 149 11327 12153 3883 -989 658 952 C ATOM 4026 O ASN C 149 52.030 64.301 37.751 1.00 73.66 O ANISOU 4026 O ASN C 149 11822 12347 3819 -846 322 605 O ATOM 4027 CB ASN C 149 50.246 62.352 39.223 1.00 81.25 C ANISOU 4027 CB ASN C 149 12833 13930 4107 -842 1254 1595 C ATOM 4028 CG ASN C 149 49.711 61.057 39.799 1.00 84.52 C ANISOU 4028 CG ASN C 149 13244 14517 4351 -966 1601 2242 C ATOM 4029 OD1 ASN C 149 49.083 60.260 39.100 1.00 82.33 O ANISOU 4029 OD1 ASN C 149 12588 14093 4601 -1230 1813 2579 O ATOM 4030 ND2 ASN C 149 49.948 60.847 41.088 1.00 89.82 N ANISOU 4030 ND2 ASN C 149 14364 15486 4278 -780 1640 2428 N ATOM 4031 N VAL C 150 50.538 63.761 36.150 1.00 68.61 N ANISOU 4031 N VAL C 150 10538 11574 3955 -1075 833 880 N ATOM 4032 CA VAL C 150 50.564 65.084 35.533 1.00 66.54 C ANISOU 4032 CA VAL C 150 10235 11154 3893 -965 720 417 C ATOM 4033 C VAL C 150 49.289 65.837 35.904 1.00 69.81 C ANISOU 4033 C VAL C 150 10612 11818 4095 -719 1148 261 C ATOM 4034 O VAL C 150 48.199 65.522 35.421 1.00 69.59 O ANISOU 4034 O VAL C 150 10239 11871 4332 -764 1493 450 O ATOM 4035 CB VAL C 150 50.727 65.016 34.005 1.00 61.22 C ANISOU 4035 CB VAL C 150 9243 10145 3873 -1158 582 413 C ATOM 4036 CG1 VAL C 150 50.750 66.415 33.418 1.00 60.16 C ANISOU 4036 CG1 VAL C 150 9111 9830 3918 -1040 480 4 C ATOM 4037 CG2 VAL C 150 52.004 64.284 33.637 1.00 58.63 C ANISOU 4037 CG2 VAL C 150 8928 9597 3752 -1337 218 548 C ATOM 4038 N SER C 151 49.443 66.830 36.775 1.00 73.58 N ANISOU 4038 N SER C 151 11438 12408 4111 -440 1096 -107 N ATOM 4039 CA SER C 151 48.319 67.588 37.309 1.00 77.99 C ANISOU 4039 CA SER C 151 12029 13231 4371 -107 1517 -308 C ATOM 4040 C SER C 151 48.149 68.892 36.535 1.00 76.50 C ANISOU 4040 C SER C 151 11774 12756 4538 32 1392 -749 C ATOM 4041 O SER C 151 49.087 69.344 35.875 1.00 73.07 O ANISOU 4041 O SER C 151 11396 11942 4424 -115 948 -933 O ATOM 4042 CB SER C 151 48.560 67.888 38.789 1.00 84.08 C ANISOU 4042 CB SER C 151 13316 14295 4337 187 1534 -490 C ATOM 4043 OG SER C 151 49.202 66.801 39.435 1.00 85.01 O ANISOU 4043 OG SER C 151 13616 14548 4135 34 1413 -119 O ATOM 4044 N GLN C 152 46.957 69.489 36.613 1.00 79.65 N ANISOU 4044 N GLN C 152 12033 13330 4902 325 1796 -884 N ATOM 4045 CA GLN C 152 46.707 70.811 36.014 1.00 79.74 C ANISOU 4045 CA GLN C 152 12042 13057 5199 541 1685 -1309 C ATOM 4046 C GLN C 152 47.453 71.928 36.779 1.00 83.17 C ANISOU 4046 C GLN C 152 13023 13319 5259 779 1357 -1837 C ATOM 4047 O GLN C 152 47.777 71.771 37.968 1.00 87.28 O ANISOU 4047 O GLN C 152 13922 14086 5155 916 1353 -1924 O ATOM 4048 CB GLN C 152 45.199 71.115 35.937 1.00 82.74 C ANISOU 4048 CB GLN C 152 12085 13684 5669 845 2198 -1308 C ATOM 4049 CG GLN C 152 44.354 70.083 35.167 1.00 81.31 C ANISOU 4049 CG GLN C 152 11314 13645 5935 595 2462 -826 C ATOM 4050 CD GLN C 152 44.656 70.033 33.659 1.00 76.90 C ANISOU 4050 CD GLN C 152 10521 12677 6021 312 2090 -756 C ATOM 4051 OE1 GLN C 152 44.791 71.069 32.994 1.00 75.67 O ANISOU 4051 OE1 GLN C 152 10444 12201 6106 444 1853 -1052 O ATOM 4052 NE2 GLN C 152 44.745 68.816 33.116 1.00 73.87 N ANISOU 4052 NE2 GLN C 152 9881 12289 5896 -57 2045 -356 N ATOM 4053 N SER C 153 47.735 73.042 36.096 1.00 81.92 N ANISOU 4053 N SER C 153 12933 12713 5478 822 1049 -2176 N ATOM 4054 CA SER C 153 48.442 74.172 36.722 1.00 85.46 C ANISOU 4054 CA SER C 153 13887 12884 5699 1002 661 -2709 C ATOM 4055 C SER C 153 47.500 75.122 37.448 1.00 91.63 C ANISOU 4055 C SER C 153 14911 13785 6119 1554 944 -3140 C ATOM 4056 O SER C 153 46.290 75.124 37.204 1.00 92.55 O ANISOU 4056 O SER C 153 14712 14122 6332 1798 1424 -3036 O ATOM 4057 CB SER C 153 49.267 74.961 35.699 1.00 82.38 C ANISOU 4057 CB SER C 153 13486 11893 5921 759 186 -2845 C ATOM 4058 OG SER C 153 49.895 76.087 36.299 1.00 86.22 O ANISOU 4058 OG SER C 153 14438 12044 6278 897 -222 -3367 O ATOM 4059 N LYS C 154 48.084 75.937 38.326 1.00 96.36 N ANISOU 4059 N LYS C 154 16063 14222 6329 1763 610 -3648 N ATOM 4060 CA LYS C 154 47.355 76.921 39.128 1.00103.21 C ANISOU 4060 CA LYS C 154 17292 15151 6771 2352 808 -4173 C ATOM 4061 C LYS C 154 46.740 78.048 38.285 1.00103.08 C ANISOU 4061 C LYS C 154 17150 14701 7315 2576 817 -4426 C ATOM 4062 O LYS C 154 45.634 78.498 38.577 1.00107.53 O ANISOU 4062 O LYS C 154 17688 15462 7706 3088 1253 -4623 O ATOM 4063 CB LYS C 154 48.266 77.498 40.218 1.00108.74 C ANISOU 4063 CB LYS C 154 18677 15704 6936 2485 309 -4704 C ATOM 4064 N ASP C 155 47.447 78.495 37.245 1.00 98.47 N ANISOU 4064 N ASP C 155 16478 13540 7397 2219 361 -4388 N ATOM 4065 CA ASP C 155 46.927 79.544 36.362 1.00 98.23 C ANISOU 4065 CA ASP C 155 16356 13045 7921 2404 325 -4546 C ATOM 4066 C ASP C 155 45.813 79.029 35.446 1.00 94.50 C ANISOU 4066 C ASP C 155 15283 12835 7789 2448 788 -4107 C ATOM 4067 O ASP C 155 45.928 77.970 34.821 1.00 88.82 O ANISOU 4067 O ASP C 155 14166 12324 7258 2052 873 -3600 O ATOM 4068 CB ASP C 155 48.051 80.206 35.544 1.00 95.73 C ANISOU 4068 CB ASP C 155 16155 12026 8193 1995 -275 -4581 C ATOM 4069 CG ASP C 155 47.608 81.512 34.861 1.00 97.85 C ANISOU 4069 CG ASP C 155 16517 11713 8950 2251 -391 -4823 C ATOM 4070 OD1 ASP C 155 46.637 82.150 35.326 1.00102.33 O ANISOU 4070 OD1 ASP C 155 17233 12329 9318 2826 -146 -5178 O ATOM 4071 OD2 ASP C 155 48.245 81.905 33.858 1.00 94.66 O ANISOU 4071 OD2 ASP C 155 16042 10795 9130 1896 -713 -4637 O ATOM 4072 N SER C 156 44.736 79.808 35.394 1.00 98.21 N ANISOU 4072 N SER C 156 15699 13270 8345 2961 1045 -4342 N ATOM 4073 CA SER C 156 43.565 79.528 34.568 1.00 96.31 C ANISOU 4073 CA SER C 156 14878 13244 8470 3092 1418 -4013 C ATOM 4074 C SER C 156 43.875 79.690 33.079 1.00 90.56 C ANISOU 4074 C SER C 156 13939 12054 8415 2749 1079 -3722 C ATOM 4075 O SER C 156 43.179 79.127 32.233 1.00 87.60 O ANISOU 4075 O SER C 156 13066 11873 8346 2672 1257 -3342 O ATOM 4076 CB SER C 156 42.414 80.460 34.984 1.00103.33 C ANISOU 4076 CB SER C 156 15796 14180 9286 3808 1731 -4406 C ATOM 4077 OG SER C 156 41.273 80.305 34.158 1.00102.59 O ANISOU 4077 OG SER C 156 15100 14257 9624 3966 2014 -4115 O ATOM 4078 N ASP C 157 44.923 80.460 32.777 1.00 89.52 N ANISOU 4078 N ASP C 157 14195 11317 8503 2541 585 -3896 N ATOM 4079 CA ASP C 157 45.335 80.747 31.399 1.00 85.03 C ANISOU 4079 CA ASP C 157 13517 10276 8514 2235 284 -3613 C ATOM 4080 C ASP C 157 46.445 79.822 30.893 1.00 78.73 C ANISOU 4080 C ASP C 157 12605 9507 7803 1613 100 -3221 C ATOM 4081 O ASP C 157 46.822 79.878 29.722 1.00 75.41 O ANISOU 4081 O ASP C 157 12071 8794 7788 1345 -72 -2923 O ATOM 4082 CB ASP C 157 45.746 82.220 31.250 1.00 88.85 C ANISOU 4082 CB ASP C 157 14444 10022 9292 2379 -100 -3964 C ATOM 4083 CG ASP C 157 44.552 83.166 31.227 1.00 94.08 C ANISOU 4083 CG ASP C 157 15131 10538 10078 3015 48 -4236 C ATOM 4084 OD1 ASP C 157 44.747 84.363 31.515 1.00 99.58 O ANISOU 4084 OD1 ASP C 157 16275 10672 10887 3263 -217 -4657 O ATOM 4085 OD2 ASP C 157 43.420 82.727 30.924 1.00 93.47 O ANISOU 4085 OD2 ASP C 157 14611 10876 10026 3276 404 -4039 O ATOM 4086 N VAL C 158 46.969 78.979 31.777 1.00 77.57 N ANISOU 4086 N VAL C 158 12505 9716 7251 1426 148 -3215 N ATOM 4087 CA VAL C 158 47.885 77.921 31.363 1.00 71.92 C ANISOU 4087 CA VAL C 158 11612 9115 6599 914 39 -2829 C ATOM 4088 C VAL C 158 47.071 76.656 31.084 1.00 68.62 C ANISOU 4088 C VAL C 158 10752 9214 6107 872 411 -2443 C ATOM 4089 O VAL C 158 46.066 76.391 31.758 1.00 71.42 O ANISOU 4089 O VAL C 158 10981 9969 6185 1168 768 -2495 O ATOM 4090 CB VAL C 158 48.984 77.647 32.421 1.00 73.24 C ANISOU 4090 CB VAL C 158 12065 9342 6422 719 -196 -2994 C ATOM 4091 CG1 VAL C 158 49.921 76.539 31.968 1.00 68.06 C ANISOU 4091 CG1 VAL C 158 11185 8795 5879 245 -302 -2588 C ATOM 4092 CG2 VAL C 158 49.785 78.906 32.692 1.00 77.14 C ANISOU 4092 CG2 VAL C 158 12970 9275 7063 715 -639 -3402 C ATOM 4093 N TYR C 159 47.500 75.895 30.080 1.00 63.13 N ANISOU 4093 N TYR C 159 9817 8491 5679 511 332 -2060 N ATOM 4094 CA TYR C 159 46.821 74.674 29.671 1.00 59.86 C ANISOU 4094 CA TYR C 159 9003 8456 5286 409 581 -1704 C ATOM 4095 C TYR C 159 47.773 73.509 29.746 1.00 56.57 C ANISOU 4095 C TYR C 159 8555 8163 4776 23 496 -1451 C ATOM 4096 O TYR C 159 48.890 73.597 29.236 1.00 54.26 O ANISOU 4096 O TYR C 159 8369 7592 4657 -227 227 -1395 O ATOM 4097 CB TYR C 159 46.296 74.817 28.244 1.00 57.46 C ANISOU 4097 CB TYR C 159 8465 7978 5391 413 530 -1511 C ATOM 4098 CG TYR C 159 45.323 75.956 28.093 1.00 60.34 C ANISOU 4098 CG TYR C 159 8833 8194 5899 833 577 -1727 C ATOM 4099 CD1 TYR C 159 44.006 75.835 28.538 1.00 62.88 C ANISOU 4099 CD1 TYR C 159 8867 8870 6156 1159 889 -1777 C ATOM 4100 CD2 TYR C 159 45.719 77.167 27.529 1.00 60.76 C ANISOU 4100 CD2 TYR C 159 9159 7740 6187 919 321 -1860 C ATOM 4101 CE1 TYR C 159 43.107 76.885 28.414 1.00 66.26 C ANISOU 4101 CE1 TYR C 159 9265 9166 6744 1607 932 -1988 C ATOM 4102 CE2 TYR C 159 44.822 78.225 27.394 1.00 64.23 C ANISOU 4102 CE2 TYR C 159 9628 7993 6783 1351 335 -2055 C ATOM 4103 CZ TYR C 159 43.519 78.074 27.840 1.00 66.72 C ANISOU 4103 CZ TYR C 159 9643 8684 7024 1717 634 -2137 C ATOM 4104 OH TYR C 159 42.627 79.109 27.713 1.00 70.81 O ANISOU 4104 OH TYR C 159 10153 9026 7724 2199 648 -2339 O ATOM 4105 N ILE C 160 47.335 72.430 30.391 1.00 56.88 N ANISOU 4105 N ILE C 160 8433 8610 4569 -13 741 -1274 N ATOM 4106 CA ILE C 160 48.109 71.190 30.449 1.00 54.44 C ANISOU 4106 CA ILE C 160 8077 8409 4197 -341 668 -994 C ATOM 4107 C ILE C 160 47.251 69.989 30.078 1.00 53.75 C ANISOU 4107 C ILE C 160 7627 8572 4225 -451 897 -656 C ATOM 4108 O ILE C 160 46.221 69.728 30.707 1.00 56.96 O ANISOU 4108 O ILE C 160 7865 9291 4485 -309 1218 -596 O ATOM 4109 CB ILE C 160 48.714 70.937 31.846 1.00 56.83 C ANISOU 4109 CB ILE C 160 8654 8904 4035 -334 646 -1078 C ATOM 4110 CG1 ILE C 160 49.488 72.159 32.333 1.00 59.02 C ANISOU 4110 CG1 ILE C 160 9303 8918 4205 -223 354 -1478 C ATOM 4111 CG2 ILE C 160 49.616 69.706 31.821 1.00 54.02 C ANISOU 4111 CG2 ILE C 160 8256 8591 3679 -646 506 -776 C ATOM 4112 CD1 ILE C 160 49.942 72.058 33.764 1.00 63.70 C ANISOU 4112 CD1 ILE C 160 10224 9716 4262 -134 280 -1641 C ATOM 4113 N THR C 161 47.682 69.250 29.065 1.00 50.53 N ANISOU 4113 N THR C 161 7092 8018 4089 -702 737 -439 N ATOM 4114 CA THR C 161 46.980 68.035 28.671 1.00 50.51 C ANISOU 4114 CA THR C 161 6782 8165 4243 -854 856 -146 C ATOM 4115 C THR C 161 47.434 66.902 29.573 1.00 51.59 C ANISOU 4115 C THR C 161 6980 8469 4152 -1031 920 71 C ATOM 4116 O THR C 161 48.572 66.904 30.034 1.00 51.20 O ANISOU 4116 O THR C 161 7188 8347 3918 -1088 749 24 O ATOM 4117 CB THR C 161 47.272 67.644 27.211 1.00 47.00 C ANISOU 4117 CB THR C 161 6253 7478 4128 -1007 629 -44 C ATOM 4118 OG1 THR C 161 48.504 66.923 27.148 1.00 45.04 O ANISOU 4118 OG1 THR C 161 6151 7117 3845 -1208 471 61 O ATOM 4119 CG2 THR C 161 47.360 68.874 26.314 1.00 46.53 C ANISOU 4119 CG2 THR C 161 6292 7174 4215 -851 488 -227 C ATOM 4120 N ASP C 162 46.558 65.931 29.818 1.00 54.00 N ANISOU 4120 N ASP C 162 7033 8978 4506 -1128 1141 336 N ATOM 4121 CA ASP C 162 46.943 64.750 30.583 1.00 55.63 C ANISOU 4121 CA ASP C 162 7310 9289 4537 -1314 1194 625 C ATOM 4122 C ASP C 162 47.921 63.898 29.770 1.00 52.24 C ANISOU 4122 C ASP C 162 6941 8574 4335 -1534 879 737 C ATOM 4123 O ASP C 162 48.087 64.120 28.562 1.00 49.63 O ANISOU 4123 O ASP C 162 6552 8020 4287 -1550 690 622 O ATOM 4124 CB ASP C 162 45.721 63.925 31.010 1.00 59.42 C ANISOU 4124 CB ASP C 162 7475 10014 5088 -1406 1534 940 C ATOM 4125 CG ASP C 162 46.016 63.018 32.211 1.00 63.52 C ANISOU 4125 CG ASP C 162 8161 10710 5263 -1508 1694 1256 C ATOM 4126 OD1 ASP C 162 47.097 63.162 32.841 1.00 63.73 O ANISOU 4126 OD1 ASP C 162 8563 10721 4930 -1441 1528 1174 O ATOM 4127 OD2 ASP C 162 45.162 62.160 32.529 1.00 68.19 O ANISOU 4127 OD2 ASP C 162 8500 11447 5963 -1662 1969 1613 O ATOM 4128 N LYS C 163 48.573 62.939 30.433 1.00 52.87 N ANISOU 4128 N LYS C 163 7160 8666 4262 -1659 832 963 N ATOM 4129 CA LYS C 163 49.574 62.094 29.777 1.00 50.13 C ANISOU 4129 CA LYS C 163 6879 8052 4116 -1802 551 1054 C ATOM 4130 C LYS C 163 48.983 61.220 28.684 1.00 48.87 C ANISOU 4130 C LYS C 163 6504 7704 4362 -1956 497 1174 C ATOM 4131 O LYS C 163 47.794 60.914 28.712 1.00 51.34 O ANISOU 4131 O LYS C 163 6580 8108 4818 -2040 670 1307 O ATOM 4132 CB LYS C 163 50.340 61.234 30.795 1.00 51.98 C ANISOU 4132 CB LYS C 163 7311 8329 4110 -1858 486 1291 C ATOM 4133 CG LYS C 163 49.509 60.380 31.741 1.00 56.25 C ANISOU 4133 CG LYS C 163 7819 9056 4498 -1951 749 1654 C ATOM 4134 CD LYS C 163 50.444 59.520 32.617 1.00 59.30 C ANISOU 4134 CD LYS C 163 8466 9422 4643 -1978 601 1912 C ATOM 4135 CE LYS C 163 49.737 58.890 33.817 1.00 64.53 C ANISOU 4135 CE LYS C 163 9196 10329 4993 -2026 909 2313 C ATOM 4136 NZ LYS C 163 49.682 59.796 34.999 1.00 67.78 N ANISOU 4136 NZ LYS C 163 9839 11115 4799 -1795 1083 2190 N ATOM 4137 N CYS C 164 49.806 60.846 27.713 1.00 45.85 N ANISOU 4137 N CYS C 164 6189 7061 4172 -1981 252 1108 N ATOM 4138 CA CYS C 164 49.461 59.747 26.825 1.00 46.13 C ANISOU 4138 CA CYS C 164 6129 6870 4529 -2117 127 1210 C ATOM 4139 C CYS C 164 50.694 59.032 26.250 1.00 44.07 C ANISOU 4139 C CYS C 164 6038 6355 4353 -2091 -97 1194 C ATOM 4140 O CYS C 164 51.760 59.635 26.099 1.00 42.66 O ANISOU 4140 O CYS C 164 5964 6175 4068 -1962 -156 1056 O ATOM 4141 CB CYS C 164 48.507 60.203 25.729 1.00 45.69 C ANISOU 4141 CB CYS C 164 5895 6779 4686 -2091 91 1046 C ATOM 4142 SG CYS C 164 49.348 60.828 24.312 1.00 46.58 S ANISOU 4142 SG CYS C 164 6169 6716 4815 -1920 -101 780 S ATOM 4143 N VAL C 165 50.543 57.747 25.938 1.00 44.74 N ANISOU 4143 N VAL C 165 6128 6207 4666 -2211 -220 1335 N ATOM 4144 CA VAL C 165 51.655 56.947 25.428 1.00 43.80 C ANISOU 4144 CA VAL C 165 6172 5830 4641 -2130 -415 1311 C ATOM 4145 C VAL C 165 51.633 56.725 23.929 1.00 42.82 C ANISOU 4145 C VAL C 165 6089 5486 4693 -2045 -569 1083 C ATOM 4146 O VAL C 165 50.639 56.269 23.367 1.00 43.61 O ANISOU 4146 O VAL C 165 6125 5455 4991 -2158 -671 1054 O ATOM 4147 CB VAL C 165 51.783 55.565 26.120 1.00 46.64 C ANISOU 4147 CB VAL C 165 6614 5991 5115 -2250 -500 1607 C ATOM 4148 CG1 VAL C 165 52.874 55.602 27.183 1.00 46.72 C ANISOU 4148 CG1 VAL C 165 6744 6116 4890 -2151 -504 1748 C ATOM 4149 CG2 VAL C 165 50.435 55.083 26.678 1.00 49.32 C ANISOU 4149 CG2 VAL C 165 6807 6350 5583 -2512 -384 1865 C ATOM 4150 N LEU C 166 52.754 57.048 23.295 1.00 41.50 N ANISOU 4150 N LEU C 166 6026 5294 4449 -1839 -591 927 N ATOM 4151 CA LEU C 166 52.964 56.734 21.892 1.00 41.88 C ANISOU 4151 CA LEU C 166 6193 5154 4565 -1683 -702 720 C ATOM 4152 C LEU C 166 53.844 55.487 21.760 1.00 44.27 C ANISOU 4152 C LEU C 166 6637 5192 4991 -1569 -828 740 C ATOM 4153 O LEU C 166 54.625 55.163 22.663 1.00 44.68 O ANISOU 4153 O LEU C 166 6672 5253 5052 -1557 -817 909 O ATOM 4154 CB LEU C 166 53.582 57.922 21.150 1.00 39.69 C ANISOU 4154 CB LEU C 166 5931 5031 4117 -1500 -570 568 C ATOM 4155 CG LEU C 166 54.977 58.451 21.502 1.00 37.95 C ANISOU 4155 CG LEU C 166 5663 4921 3834 -1394 -445 611 C ATOM 4156 CD1 LEU C 166 56.082 57.557 20.967 1.00 38.07 C ANISOU 4156 CD1 LEU C 166 5748 4787 3931 -1192 -471 582 C ATOM 4157 CD2 LEU C 166 55.125 59.856 20.936 1.00 35.58 C ANISOU 4157 CD2 LEU C 166 5333 4762 3423 -1335 -297 531 C ATOM 4158 N ASP C 167 53.717 54.808 20.621 1.00 46.24 N ANISOU 4158 N ASP C 167 7051 5199 5320 -1448 -979 545 N ATOM 4159 CA ASP C 167 54.448 53.576 20.365 1.00 48.80 C ANISOU 4159 CA ASP C 167 7551 5211 5781 -1282 -1118 501 C ATOM 4160 C ASP C 167 55.129 53.640 18.987 1.00 49.79 C ANISOU 4160 C ASP C 167 7853 5304 5760 -930 -1077 210 C ATOM 4161 O ASP C 167 54.474 53.598 17.937 1.00 50.72 O ANISOU 4161 O ASP C 167 8137 5333 5801 -870 -1202 -18 O ATOM 4162 CB ASP C 167 53.491 52.385 20.491 1.00 51.66 C ANISOU 4162 CB ASP C 167 7997 5209 6422 -1496 -1388 552 C ATOM 4163 CG ASP C 167 54.176 51.037 20.333 1.00 54.86 C ANISOU 4163 CG ASP C 167 8626 5197 7021 -1325 -1577 512 C ATOM 4164 OD1 ASP C 167 55.388 50.976 20.046 1.00 55.58 O ANISOU 4164 OD1 ASP C 167 8789 5307 7020 -989 -1485 417 O ATOM 4165 OD2 ASP C 167 53.479 50.017 20.499 1.00 57.86 O ANISOU 4165 OD2 ASP C 167 9090 5202 7692 -1529 -1821 586 O ATOM 4166 N MET C 168 56.452 53.762 19.011 1.00 50.14 N ANISOU 4166 N MET C 168 7849 5449 5754 -686 -899 233 N ATOM 4167 CA MET C 168 57.264 53.748 17.799 1.00 52.14 C ANISOU 4167 CA MET C 168 8238 5713 5859 -307 -759 13 C ATOM 4168 C MET C 168 57.497 52.292 17.417 1.00 56.20 C ANISOU 4168 C MET C 168 9002 5837 6515 -76 -963 -152 C ATOM 4169 O MET C 168 58.583 51.732 17.607 1.00 58.05 O ANISOU 4169 O MET C 168 9195 5997 6864 177 -897 -123 O ATOM 4170 CB MET C 168 58.577 54.501 18.024 1.00 51.30 C ANISOU 4170 CB MET C 168 7878 5887 5725 -166 -459 141 C ATOM 4171 CG MET C 168 58.368 55.912 18.535 1.00 48.19 C ANISOU 4171 CG MET C 168 7269 5788 5253 -420 -324 292 C ATOM 4172 SD MET C 168 59.860 56.902 18.663 1.00 49.57 S ANISOU 4172 SD MET C 168 7119 6236 5478 -326 -26 428 S ATOM 4173 CE MET C 168 60.311 57.113 16.941 1.00 51.48 C ANISOU 4173 CE MET C 168 7503 6552 5504 25 293 286 C ATOM 4174 N ARG C 169 56.445 51.698 16.868 1.00 58.14 N ANISOU 4174 N ARG C 169 9497 5807 6785 -159 -1247 -343 N ATOM 4175 CA ARG C 169 56.317 50.252 16.745 1.00 62.45 C ANISOU 4175 CA ARG C 169 10301 5858 7568 -78 -1564 -486 C ATOM 4176 C ARG C 169 57.574 49.554 16.227 1.00 65.79 C ANISOU 4176 C ARG C 169 10890 6139 7968 424 -1467 -667 C ATOM 4177 O ARG C 169 58.036 48.587 16.839 1.00 68.06 O ANISOU 4177 O ARG C 169 11202 6119 8540 493 -1601 -572 O ATOM 4178 CB ARG C 169 55.077 49.904 15.915 1.00 64.55 C ANISOU 4178 CB ARG C 169 10817 5874 7834 -200 -1910 -757 C ATOM 4179 CG ARG C 169 53.835 50.670 16.382 1.00 62.84 C ANISOU 4179 CG ARG C 169 10350 5853 7673 -650 -1967 -573 C ATOM 4180 CD ARG C 169 52.525 50.031 15.943 1.00 67.49 C ANISOU 4180 CD ARG C 169 11057 6104 8483 -889 -2414 -745 C ATOM 4181 NE ARG C 169 51.546 50.053 17.031 1.00 67.53 N ANISOU 4181 NE ARG C 169 10727 6113 8820 -1382 -2465 -405 N ATOM 4182 CZ ARG C 169 51.398 49.076 17.931 1.00 69.93 C ANISOU 4182 CZ ARG C 169 10977 6085 9507 -1637 -2582 -154 C ATOM 4183 NH1 ARG C 169 52.161 47.986 17.884 1.00 72.06 N ANISOU 4183 NH1 ARG C 169 11519 5942 9920 -1441 -2718 -224 N ATOM 4184 NH2 ARG C 169 50.484 49.188 18.886 1.00 69.40 N ANISOU 4184 NH2 ARG C 169 10590 6097 9681 -2066 -2539 191 N ATOM 4185 N SER C 170 58.146 50.068 15.137 1.00 66.64 N ANISOU 4185 N SER C 170 11098 6487 7736 797 -1203 -890 N ATOM 4186 CA SER C 170 59.312 49.439 14.491 1.00 70.60 C ANISOU 4186 CA SER C 170 11746 6907 8173 1352 -1033 -1098 C ATOM 4187 C SER C 170 60.538 49.337 15.402 1.00 70.29 C ANISOU 4187 C SER C 170 11348 6969 8390 1471 -835 -826 C ATOM 4188 O SER C 170 61.408 48.490 15.193 1.00 74.23 O ANISOU 4188 O SER C 170 11923 7276 9005 1902 -803 -957 O ATOM 4189 CB SER C 170 59.677 50.171 13.191 1.00 71.78 C ANISOU 4189 CB SER C 170 12031 7395 7848 1712 -682 -1304 C ATOM 4190 OG SER C 170 60.077 51.504 13.452 1.00 68.40 O ANISOU 4190 OG SER C 170 11223 7445 7320 1557 -302 -1003 O ATOM 4191 N MET C 171 60.590 50.197 16.412 1.00 66.18 N ANISOU 4191 N MET C 171 10445 6740 7960 1116 -740 -474 N ATOM 4192 CA MET C 171 61.711 50.240 17.337 1.00 66.31 C ANISOU 4192 CA MET C 171 10094 6894 8207 1185 -631 -210 C ATOM 4193 C MET C 171 61.420 49.627 18.706 1.00 65.25 C ANISOU 4193 C MET C 171 9915 6523 8355 897 -962 61 C ATOM 4194 O MET C 171 62.294 49.625 19.569 1.00 65.51 O ANISOU 4194 O MET C 171 9675 6658 8558 949 -963 289 O ATOM 4195 CB MET C 171 62.154 51.683 17.531 1.00 63.72 C ANISOU 4195 CB MET C 171 9383 7059 7769 1024 -318 -19 C ATOM 4196 CG MET C 171 63.197 52.167 16.554 1.00 68.17 C ANISOU 4196 CG MET C 171 9789 7901 8213 1401 111 -103 C ATOM 4197 SD MET C 171 63.562 53.907 16.908 1.00 70.63 S ANISOU 4197 SD MET C 171 9655 8679 8503 1074 394 173 S ATOM 4198 CE MET C 171 65.215 54.030 16.201 1.00 74.76 C ANISOU 4198 CE MET C 171 9800 9462 9145 1528 874 212 C ATOM 4199 N ASP C 172 60.199 49.125 18.908 1.00 64.54 N ANISOU 4199 N ASP C 172 10077 6131 8314 589 -1246 63 N ATOM 4200 CA ASP C 172 59.766 48.551 20.194 1.00 64.14 C ANISOU 4200 CA ASP C 172 10019 5862 8488 274 -1505 389 C ATOM 4201 C ASP C 172 59.828 49.604 21.321 1.00 60.18 C ANISOU 4201 C ASP C 172 9200 5789 7876 -20 -1384 705 C ATOM 4202 O ASP C 172 60.020 49.283 22.493 1.00 60.84 O ANISOU 4202 O ASP C 172 9223 5834 8058 -133 -1520 1012 O ATOM 4203 CB ASP C 172 60.604 47.302 20.528 1.00 68.68 C ANISOU 4203 CB ASP C 172 10698 6047 9350 590 -1696 452 C ATOM 4204 CG ASP C 172 60.000 46.455 21.638 1.00 70.55 C ANISOU 4204 CG ASP C 172 11064 5923 9818 284 -1996 797 C ATOM 4205 OD1 ASP C 172 58.942 45.824 21.411 1.00 72.46 O ANISOU 4205 OD1 ASP C 172 11555 5781 10196 44 -2198 751 O ATOM 4206 OD2 ASP C 172 60.601 46.400 22.734 1.00 70.56 O ANISOU 4206 OD2 ASP C 172 10919 6017 9875 284 -2047 1132 O ATOM 4207 N PHE C 173 59.642 50.866 20.950 1.00 56.37 N ANISOU 4207 N PHE C 173 8563 5692 7162 -126 -1152 621 N ATOM 4208 CA PHE C 173 59.837 51.971 21.876 1.00 53.17 C ANISOU 4208 CA PHE C 173 7887 5671 6646 -338 -1045 827 C ATOM 4209 C PHE C 173 58.543 52.706 22.245 1.00 50.14 C ANISOU 4209 C PHE C 173 7514 5432 6105 -723 -1023 891 C ATOM 4210 O PHE C 173 57.763 53.081 21.378 1.00 49.05 O ANISOU 4210 O PHE C 173 7455 5307 5873 -777 -959 709 O ATOM 4211 CB PHE C 173 60.864 52.946 21.301 1.00 52.30 C ANISOU 4211 CB PHE C 173 7531 5873 6469 -140 -784 725 C ATOM 4212 CG PHE C 173 61.073 54.166 22.139 1.00 49.98 C ANISOU 4212 CG PHE C 173 6982 5910 6097 -369 -725 871 C ATOM 4213 CD1 PHE C 173 61.969 54.144 23.206 1.00 50.94 C ANISOU 4213 CD1 PHE C 173 6900 6123 6333 -356 -868 1053 C ATOM 4214 CD2 PHE C 173 60.363 55.341 21.870 1.00 46.89 C ANISOU 4214 CD2 PHE C 173 6581 5713 5523 -579 -578 808 C ATOM 4215 CE1 PHE C 173 62.162 55.276 23.997 1.00 49.53 C ANISOU 4215 CE1 PHE C 173 6531 6215 6073 -565 -885 1130 C ATOM 4216 CE2 PHE C 173 60.545 56.477 22.651 1.00 45.32 C ANISOU 4216 CE2 PHE C 173 6194 5757 5268 -773 -559 896 C ATOM 4217 CZ PHE C 173 61.450 56.444 23.719 1.00 47.07 C ANISOU 4217 CZ PHE C 173 6235 6058 5592 -775 -722 1038 C ATOM 4218 N LYS C 174 58.346 52.926 23.541 1.00 49.28 N ANISOU 4218 N LYS C 174 7327 5453 5944 -946 -1076 1147 N ATOM 4219 CA LYS C 174 57.172 53.626 24.048 1.00 47.27 C ANISOU 4219 CA LYS C 174 7048 5376 5535 -1257 -1005 1223 C ATOM 4220 C LYS C 174 57.568 54.791 24.953 1.00 45.77 C ANISOU 4220 C LYS C 174 6703 5541 5145 -1324 -920 1294 C ATOM 4221 O LYS C 174 58.508 54.680 25.745 1.00 47.07 O ANISOU 4221 O LYS C 174 6814 5766 5303 -1241 -1028 1422 O ATOM 4222 CB LYS C 174 56.270 52.663 24.827 1.00 49.38 C ANISOU 4222 CB LYS C 174 7432 5439 5893 -1481 -1125 1480 C ATOM 4223 CG LYS C 174 55.535 51.648 23.973 1.00 51.45 C ANISOU 4223 CG LYS C 174 7841 5306 6401 -1528 -1262 1386 C ATOM 4224 CD LYS C 174 55.064 50.447 24.794 1.00 55.29 C ANISOU 4224 CD LYS C 174 8440 5476 7092 -1724 -1413 1718 C ATOM 4225 CE LYS C 174 54.160 49.515 23.969 1.00 57.98 C ANISOU 4225 CE LYS C 174 8900 5378 7752 -1860 -1606 1607 C ATOM 4226 NZ LYS C 174 54.806 49.028 22.714 1.00 58.94 N ANISOU 4226 NZ LYS C 174 9210 5214 7971 -1530 -1765 1231 N ATOM 4227 N SER C 175 56.845 55.905 24.835 1.00 43.53 N ANISOU 4227 N SER C 175 6361 5466 4714 -1456 -775 1193 N ATOM 4228 CA SER C 175 57.058 57.068 25.701 1.00 42.32 C ANISOU 4228 CA SER C 175 6117 5595 4369 -1526 -725 1204 C ATOM 4229 C SER C 175 55.756 57.779 26.118 1.00 41.49 C ANISOU 4229 C SER C 175 6025 5650 4089 -1699 -596 1198 C ATOM 4230 O SER C 175 54.824 57.960 25.313 1.00 40.38 O ANISOU 4230 O SER C 175 5868 5469 4004 -1743 -510 1095 O ATOM 4231 CB SER C 175 58.041 58.055 25.059 1.00 41.17 C ANISOU 4231 CB SER C 175 5828 5540 4274 -1414 -662 1038 C ATOM 4232 OG SER C 175 57.514 58.645 23.884 1.00 39.40 O ANISOU 4232 OG SER C 175 5615 5303 4054 -1396 -504 879 O ATOM 4233 N ASN C 176 55.701 58.149 27.396 1.00 42.37 N ANISOU 4233 N ASN C 176 6171 5953 3975 -1761 -600 1302 N ATOM 4234 CA ASN C 176 54.655 59.016 27.920 1.00 42.14 C ANISOU 4234 CA ASN C 176 6141 6131 3738 -1844 -437 1258 C ATOM 4235 C ASN C 176 55.035 60.458 27.607 1.00 40.40 C ANISOU 4235 C ASN C 176 5874 5999 3477 -1781 -417 1001 C ATOM 4236 O ASN C 176 56.215 60.779 27.462 1.00 39.90 O ANISOU 4236 O ASN C 176 5771 5897 3494 -1723 -543 930 O ATOM 4237 CB ASN C 176 54.518 58.842 29.445 1.00 44.96 C ANISOU 4237 CB ASN C 176 6622 6676 3783 -1876 -429 1454 C ATOM 4238 CG ASN C 176 53.453 57.817 29.849 1.00 47.38 C ANISOU 4238 CG ASN C 176 6947 6962 4095 -2011 -289 1755 C ATOM 4239 OD1 ASN C 176 52.263 57.959 29.530 1.00 46.95 O ANISOU 4239 OD1 ASN C 176 6764 6950 4123 -2107 -95 1749 O ATOM 4240 ND2 ASN C 176 53.878 56.792 30.586 1.00 49.88 N ANISOU 4240 ND2 ASN C 176 7398 7204 4349 -2026 -398 2050 N ATOM 4241 N SER C 177 54.040 61.328 27.508 1.00 39.92 N ANISOU 4241 N SER C 177 5791 6035 3341 -1793 -264 882 N ATOM 4242 CA SER C 177 54.300 62.757 27.365 1.00 39.47 C ANISOU 4242 CA SER C 177 5737 6009 3250 -1737 -260 658 C ATOM 4243 C SER C 177 53.096 63.577 27.812 1.00 40.36 C ANISOU 4243 C SER C 177 5869 6267 3199 -1699 -98 556 C ATOM 4244 O SER C 177 51.982 63.052 27.898 1.00 41.49 O ANISOU 4244 O SER C 177 5939 6496 3331 -1728 48 666 O ATOM 4245 CB SER C 177 54.624 63.101 25.912 1.00 37.69 C ANISOU 4245 CB SER C 177 5442 5618 3259 -1700 -248 574 C ATOM 4246 OG SER C 177 53.432 63.174 25.156 1.00 36.74 O ANISOU 4246 OG SER C 177 5295 5483 3182 -1680 -143 541 O ATOM 4247 N ALA C 178 53.323 64.861 28.088 1.00 40.40 N ANISOU 4247 N ALA C 178 5950 6279 3123 -1632 -130 345 N ATOM 4248 CA ALA C 178 52.234 65.822 28.257 1.00 40.85 C ANISOU 4248 CA ALA C 178 6022 6415 3084 -1521 22 188 C ATOM 4249 C ALA C 178 52.614 67.167 27.628 1.00 39.94 C ANISOU 4249 C ALA C 178 5958 6101 3118 -1467 -60 -19 C ATOM 4250 O ALA C 178 53.774 67.564 27.661 1.00 39.99 O ANISOU 4250 O ALA C 178 6016 5974 3204 -1535 -237 -76 O ATOM 4251 CB ALA C 178 51.873 65.971 29.735 1.00 43.71 C ANISOU 4251 CB ALA C 178 6522 7012 3073 -1436 105 140 C ATOM 4252 N VAL C 179 51.644 67.855 27.036 1.00 39.77 N ANISOU 4252 N VAL C 179 5895 6038 3178 -1352 49 -103 N ATOM 4253 CA VAL C 179 51.891 69.192 26.471 1.00 40.13 C ANISOU 4253 CA VAL C 179 6030 5847 3370 -1287 -24 -260 C ATOM 4254 C VAL C 179 51.342 70.283 27.392 1.00 43.18 C ANISOU 4254 C VAL C 179 6559 6246 3602 -1111 0 -518 C ATOM 4255 O VAL C 179 50.281 70.126 28.010 1.00 44.91 O ANISOU 4255 O VAL C 179 6733 6692 3640 -962 179 -560 O ATOM 4256 CB VAL C 179 51.284 69.365 25.043 1.00 38.69 C ANISOU 4256 CB VAL C 179 5769 5548 3383 -1223 22 -178 C ATOM 4257 CG1 VAL C 179 51.702 70.690 24.429 1.00 38.70 C ANISOU 4257 CG1 VAL C 179 5899 5262 3542 -1180 -50 -250 C ATOM 4258 CG2 VAL C 179 51.705 68.230 24.130 1.00 36.72 C ANISOU 4258 CG2 VAL C 179 5436 5301 3216 -1333 6 17 C ATOM 4259 N ALA C 180 52.078 71.381 27.494 1.00 44.63 N ANISOU 4259 N ALA C 180 6908 6174 3876 -1123 -172 -694 N ATOM 4260 CA ALA C 180 51.599 72.541 28.210 1.00 48.04 C ANISOU 4260 CA ALA C 180 7535 6517 4200 -918 -195 -1000 C ATOM 4261 C ALA C 180 51.900 73.800 27.413 1.00 49.44 C ANISOU 4261 C ALA C 180 7814 6273 4697 -917 -329 -1077 C ATOM 4262 O ALA C 180 52.984 73.936 26.835 1.00 48.71 O ANISOU 4262 O ALA C 180 7698 5957 4851 -1147 -470 -950 O ATOM 4263 CB ALA C 180 52.219 72.606 29.559 1.00 50.23 C ANISOU 4263 CB ALA C 180 8011 6875 4201 -929 -352 -1204 C ATOM 4264 N TRP C 181 50.920 74.702 27.365 1.00 52.22 N ANISOU 4264 N TRP C 181 8257 6516 5068 -646 -261 -1248 N ATOM 4265 CA TRP C 181 51.080 76.031 26.754 1.00 54.69 C ANISOU 4265 CA TRP C 181 8735 6365 5678 -598 -404 -1329 C ATOM 4266 C TRP C 181 50.261 77.089 27.511 1.00 59.41 C ANISOU 4266 C TRP C 181 9550 6838 6184 -247 -414 -1704 C ATOM 4267 O TRP C 181 49.411 76.749 28.338 1.00 60.54 O ANISOU 4267 O TRP C 181 9658 7325 6020 -4 -228 -1858 O ATOM 4268 CB TRP C 181 50.700 76.007 25.266 1.00 52.41 C ANISOU 4268 CB TRP C 181 8322 5982 5609 -586 -321 -1029 C ATOM 4269 CG TRP C 181 49.233 75.804 25.018 1.00 52.01 C ANISOU 4269 CG TRP C 181 8128 6157 5478 -284 -159 -1027 C ATOM 4270 CD1 TRP C 181 48.299 76.773 24.776 1.00 54.17 C ANISOU 4270 CD1 TRP C 181 8466 6253 5863 37 -165 -1145 C ATOM 4271 CD2 TRP C 181 48.527 74.555 25.002 1.00 49.98 C ANISOU 4271 CD2 TRP C 181 7597 6321 5074 -283 3 -895 C ATOM 4272 NE1 TRP C 181 47.057 76.208 24.612 1.00 54.19 N ANISOU 4272 NE1 TRP C 181 8200 6582 5807 244 -16 -1096 N ATOM 4273 CE2 TRP C 181 47.166 74.847 24.743 1.00 51.79 C ANISOU 4273 CE2 TRP C 181 7682 6636 5361 24 87 -938 C ATOM 4274 CE3 TRP C 181 48.912 73.215 25.179 1.00 47.02 C ANISOU 4274 CE3 TRP C 181 7072 6223 4572 -512 64 -735 C ATOM 4275 CZ2 TRP C 181 46.187 73.849 24.651 1.00 51.08 C ANISOU 4275 CZ2 TRP C 181 7262 6905 5240 57 221 -820 C ATOM 4276 CZ3 TRP C 181 47.939 72.223 25.092 1.00 46.42 C ANISOU 4276 CZ3 TRP C 181 6732 6456 4448 -477 199 -619 C ATOM 4277 CH2 TRP C 181 46.593 72.547 24.830 1.00 48.97 C ANISOU 4277 CH2 TRP C 181 6876 6864 4865 -218 273 -659 C ATOM 4278 N SER C 182 50.533 78.362 27.230 1.00 63.01 N ANISOU 4278 N SER C 182 10234 6790 6918 -210 -610 -1836 N ATOM 4279 CA SER C 182 49.724 79.458 27.752 1.00 68.52 C ANISOU 4279 CA SER C 182 11167 7274 7593 184 -636 -2203 C ATOM 4280 C SER C 182 49.717 80.658 26.815 1.00 71.34 C ANISOU 4280 C SER C 182 11684 7051 8372 239 -790 -2138 C ATOM 4281 O SER C 182 50.746 81.015 26.237 1.00 71.49 O ANISOU 4281 O SER C 182 11769 6696 8698 -99 -973 -1946 O ATOM 4282 CB SER C 182 50.207 79.892 29.134 1.00 72.52 C ANISOU 4282 CB SER C 182 11979 7702 7872 230 -829 -2650 C ATOM 4283 OG SER C 182 49.318 80.839 29.703 1.00 77.20 O ANISOU 4283 OG SER C 182 12816 8148 8367 699 -799 -3055 O ATOM 4284 N ASN C 183 48.550 81.286 26.696 1.00 74.76 N ANISOU 4284 N ASN C 183 12162 7409 8834 680 -703 -2275 N ATOM 4285 CA ASN C 183 48.352 82.463 25.840 1.00 78.33 C ANISOU 4285 CA ASN C 183 12804 7291 9668 826 -856 -2201 C ATOM 4286 C ASN C 183 49.031 83.742 26.369 1.00 83.81 C ANISOU 4286 C ASN C 183 13916 7324 10603 794 -1172 -2524 C ATOM 4287 O ASN C 183 48.595 84.858 26.072 1.00 88.02 O ANISOU 4287 O ASN C 183 14686 7352 11405 1070 -1299 -2620 O ATOM 4288 CB ASN C 183 46.848 82.693 25.577 1.00 80.12 C ANISOU 4288 CB ASN C 183 12905 7658 9879 1360 -699 -2253 C ATOM 4289 CG ASN C 183 46.004 82.692 26.867 1.00 83.58 C ANISOU 4289 CG ASN C 183 13329 8418 10010 1781 -516 -2711 C ATOM 4290 OD1 ASN C 183 45.669 83.753 27.412 1.00 88.92 O ANISOU 4290 OD1 ASN C 183 14292 8751 10743 2160 -603 -3102 O ATOM 4291 ND2 ASN C 183 45.662 81.500 27.352 1.00 80.34 N ANISOU 4291 ND2 ASN C 183 12603 8653 9270 1732 -242 -2652 N ATOM 4292 N LYS C 184 50.088 83.566 27.162 1.00 84.49 N ANISOU 4292 N LYS C 184 14097 7389 10618 463 -1344 -2698 N ATOM 4293 CA LYS C 184 50.942 84.669 27.607 1.00 89.97 C ANISOU 4293 CA LYS C 184 15148 7421 11614 298 -1736 -2980 C ATOM 4294 C LYS C 184 52.260 84.638 26.829 1.00 88.99 C ANISOU 4294 C LYS C 184 14898 7011 11902 -299 -1883 -2553 C ATOM 4295 O LYS C 184 52.709 83.563 26.402 1.00 84.30 O ANISOU 4295 O LYS C 184 13972 6857 11201 -574 -1699 -2193 O ATOM 4296 CB LYS C 184 51.223 84.577 29.117 1.00 92.57 C ANISOU 4296 CB LYS C 184 15684 7910 11579 367 -1906 -3526 C ATOM 4297 CG LYS C 184 50.029 84.860 30.016 1.00 95.87 C ANISOU 4297 CG LYS C 184 16310 8525 11592 999 -1751 -4014 C ATOM 4298 CD LYS C 184 49.574 86.311 29.889 1.00102.13 C ANISOU 4298 CD LYS C 184 17473 8612 12719 1351 -1949 -4316 C ATOM 4299 CE LYS C 184 48.238 86.544 30.585 1.00105.30 C ANISOU 4299 CE LYS C 184 17987 9273 12748 2072 -1686 -4739 C ATOM 4300 NZ LYS C 184 47.627 87.844 30.200 1.00109.29 N ANISOU 4300 NZ LYS C 184 18768 9118 13638 2487 -1820 -4929 N ATOM 4301 N SER C 185 52.872 85.808 26.639 1.00 94.11 N ANISOU 4301 N SER C 185 15797 6913 13049 -492 -2195 -2582 N ATOM 4302 CA SER C 185 54.206 85.885 26.034 1.00 94.58 C ANISOU 4302 CA SER C 185 15696 6673 13566 -1091 -2322 -2183 C ATOM 4303 C SER C 185 55.304 85.436 27.019 1.00 95.27 C ANISOU 4303 C SER C 185 15672 6906 13619 -1452 -2591 -2425 C ATOM 4304 O SER C 185 56.158 84.622 26.654 1.00 92.25 O ANISOU 4304 O SER C 185 14925 6823 13301 -1826 -2486 -2066 O ATOM 4305 CB SER C 185 54.495 87.286 25.460 1.00100.41 C ANISOU 4305 CB SER C 185 16704 6522 14926 -1232 -2555 -2051 C ATOM 4306 OG SER C 185 54.845 88.222 26.469 1.00106.42 O ANISOU 4306 OG SER C 185 17801 6711 15921 -1271 -3025 -2594 O ATOM 4307 N ASP C 186 55.244 85.938 28.261 1.00 99.69 N ANISOU 4307 N ASP C 186 16557 7281 14038 -1285 -2943 -3050 N ATOM 4308 CA ASP C 186 56.285 85.728 29.297 1.00101.84 C ANISOU 4308 CA ASP C 186 16821 7586 14287 -1591 -3348 -3363 C ATOM 4309 C ASP C 186 56.176 84.430 30.132 1.00 97.91 C ANISOU 4309 C ASP C 186 16181 7899 13121 -1449 -3210 -3494 C ATOM 4310 O ASP C 186 56.525 84.412 31.320 1.00101.05 O ANISOU 4310 O ASP C 186 16785 8363 13247 -1418 -3564 -3957 O ATOM 4311 CB ASP C 186 56.336 86.944 30.234 1.00109.66 C ANISOU 4311 CB ASP C 186 18316 7930 15421 -1474 -3877 -4012 C ATOM 4312 CG ASP C 186 55.121 87.040 31.159 1.00111.00 C ANISOU 4312 CG ASP C 186 18884 8348 14943 -792 -3778 -4584 C ATOM 4313 OD1 ASP C 186 55.186 87.828 32.124 1.00117.41 O ANISOU 4313 OD1 ASP C 186 20150 8766 15694 -625 -4210 -5213 O ATOM 4314 OD2 ASP C 186 54.109 86.337 30.939 1.00106.11 O ANISOU 4314 OD2 ASP C 186 18118 8313 13886 -418 -3275 -4419 O ATOM 4315 N PHE C 187 55.705 83.357 29.499 1.00 91.47 N ANISOU 4315 N PHE C 187 15045 7665 12043 -1365 -2731 -3077 N ATOM 4316 CA PHE C 187 55.504 82.059 30.147 1.00 87.64 C ANISOU 4316 CA PHE C 187 14411 7913 10974 -1241 -2541 -3093 C ATOM 4317 C PHE C 187 56.682 81.126 29.829 1.00 84.43 C ANISOU 4317 C PHE C 187 13599 7738 10743 -1692 -2578 -2708 C ATOM 4318 O PHE C 187 57.156 81.089 28.690 1.00 82.55 O ANISOU 4318 O PHE C 187 13080 7357 10927 -1966 -2429 -2255 O ATOM 4319 CB PHE C 187 54.147 81.491 29.692 1.00 83.71 C ANISOU 4319 CB PHE C 187 13820 7848 10139 -849 -2032 -2919 C ATOM 4320 CG PHE C 187 53.975 80.002 29.890 1.00 79.24 C ANISOU 4320 CG PHE C 187 12980 7980 9147 -842 -1749 -2702 C ATOM 4321 CD1 PHE C 187 54.101 79.125 28.809 1.00 74.26 C ANISOU 4321 CD1 PHE C 187 11990 7571 8655 -1034 -1491 -2198 C ATOM 4322 CD2 PHE C 187 53.630 79.479 31.135 1.00 80.64 C ANISOU 4322 CD2 PHE C 187 13301 8574 8763 -614 -1727 -2991 C ATOM 4323 CE1 PHE C 187 53.916 77.738 28.968 1.00 70.25 C ANISOU 4323 CE1 PHE C 187 11257 7627 7809 -1030 -1263 -2005 C ATOM 4324 CE2 PHE C 187 53.445 78.093 31.303 1.00 77.17 C ANISOU 4324 CE2 PHE C 187 12623 8723 7976 -629 -1462 -2730 C ATOM 4325 CZ PHE C 187 53.586 77.223 30.212 1.00 71.07 C ANISOU 4325 CZ PHE C 187 11481 8101 7422 -848 -1250 -2246 C ATOM 4326 N ALA C 188 57.158 80.393 30.839 1.00 84.45 N ANISOU 4326 N ALA C 188 13587 8099 10402 -1730 -2769 -2882 N ATOM 4327 CA ALA C 188 58.345 79.532 30.695 1.00 82.42 C ANISOU 4327 CA ALA C 188 12942 8042 10332 -2108 -2877 -2575 C ATOM 4328 C ALA C 188 58.120 78.063 31.081 1.00 78.16 C ANISOU 4328 C ALA C 188 12260 8167 9271 -1968 -2645 -2422 C ATOM 4329 O ALA C 188 57.243 77.748 31.890 1.00 78.15 O ANISOU 4329 O ALA C 188 12509 8486 8698 -1628 -2527 -2646 O ATOM 4330 CB ALA C 188 59.513 80.112 31.475 1.00 88.04 C ANISOU 4330 CB ALA C 188 13706 8419 11326 -2400 -3499 -2869 C ATOM 4331 N CYS C 189 58.938 77.178 30.511 1.00 75.13 N ANISOU 4331 N CYS C 189 11473 7967 9106 -2224 -2568 -2026 N ATOM 4332 CA CYS C 189 58.778 75.730 30.689 1.00 71.33 C ANISOU 4332 CA CYS C 189 10839 8027 8235 -2119 -2346 -1811 C ATOM 4333 C CYS C 189 59.231 75.190 32.055 1.00 73.82 C ANISOU 4333 C CYS C 189 11286 8605 8157 -2073 -2697 -2028 C ATOM 4334 O CYS C 189 58.601 74.283 32.610 1.00 72.18 O ANISOU 4334 O CYS C 189 11187 8812 7428 -1849 -2507 -1986 O ATOM 4335 CB CYS C 189 59.482 74.955 29.566 1.00 67.81 C ANISOU 4335 CB CYS C 189 9954 7664 8147 -2338 -2133 -1342 C ATOM 4336 SG CYS C 189 58.964 75.338 27.868 1.00 65.02 S ANISOU 4336 SG CYS C 189 9487 7111 8106 -2344 -1687 -1009 S ATOM 4337 N ALA C 190 60.326 75.725 32.588 1.00 78.17 N ANISOU 4337 N ALA C 190 11822 8911 8967 -2296 -3228 -2229 N ATOM 4338 CA ALA C 190 60.777 75.315 33.913 1.00 81.79 C ANISOU 4338 CA ALA C 190 12465 9599 9013 -2224 -3659 -2467 C ATOM 4339 C ALA C 190 59.703 75.638 34.952 1.00 84.32 C ANISOU 4339 C ALA C 190 13340 10065 8631 -1835 -3624 -2869 C ATOM 4340 O ALA C 190 59.700 75.084 36.056 1.00 86.69 O ANISOU 4340 O ALA C 190 13889 10700 8350 -1652 -3797 -2998 O ATOM 4341 CB ALA C 190 62.092 75.985 34.265 1.00 87.25 C ANISOU 4341 CB ALA C 190 13034 9946 10171 -2542 -4318 -2666 C ATOM 4342 N ASN C 191 58.794 76.535 34.570 1.00 84.31 N ANISOU 4342 N ASN C 191 13531 9824 8680 -1678 -3377 -3040 N ATOM 4343 CA ASN C 191 57.652 76.929 35.387 1.00 86.83 C ANISOU 4343 CA ASN C 191 14320 10277 8393 -1246 -3221 -3412 C ATOM 4344 C ASN C 191 56.391 76.150 35.031 1.00 82.29 C ANISOU 4344 C ASN C 191 13644 10120 7502 -989 -2554 -3119 C ATOM 4345 O ASN C 191 55.415 76.176 35.779 1.00 84.48 O ANISOU 4345 O ASN C 191 14215 10664 7221 -613 -2317 -3326 O ATOM 4346 CB ASN C 191 57.383 78.434 35.239 1.00 90.58 C ANISOU 4346 CB ASN C 191 15064 10196 9157 -1173 -3388 -3815 C ATOM 4347 CG ASN C 191 58.348 79.293 36.051 1.00 97.85 C ANISOU 4347 CG ASN C 191 16267 10718 10194 -1317 -4119 -4293 C ATOM 4348 OD1 ASN C 191 58.298 80.523 35.993 1.00102.22 O ANISOU 4348 OD1 ASN C 191 17065 10723 11051 -1308 -4364 -4646 O ATOM 4349 ND2 ASN C 191 59.224 78.648 36.818 1.00100.07 N ANISOU 4349 ND2 ASN C 191 16527 11239 10256 -1445 -4519 -4315 N ATOM 4350 N ALA C 192 56.420 75.452 33.896 1.00 76.71 N ANISOU 4350 N ALA C 192 12513 9473 7159 -1186 -2259 -2644 N ATOM 4351 CA ALA C 192 55.220 74.830 33.327 1.00 72.66 C ANISOU 4351 CA ALA C 192 11849 9247 6513 -1005 -1698 -2372 C ATOM 4352 C ALA C 192 54.614 73.718 34.176 1.00 72.69 C ANISOU 4352 C ALA C 192 11912 9782 5924 -816 -1443 -2248 C ATOM 4353 O ALA C 192 53.395 73.602 34.266 1.00 72.60 O ANISOU 4353 O ALA C 192 11919 10005 5661 -557 -1033 -2230 O ATOM 4354 CB ALA C 192 55.494 74.331 31.923 1.00 67.43 C ANISOU 4354 CB ALA C 192 10783 8498 6340 -1254 -1525 -1942 C ATOM 4355 N PHE C 193 55.460 72.905 34.797 1.00 73.53 N ANISOU 4355 N PHE C 193 12025 10073 5839 -946 -1682 -2131 N ATOM 4356 CA PHE C 193 54.972 71.763 35.563 1.00 74.19 C ANISOU 4356 CA PHE C 193 12175 10627 5387 -806 -1441 -1913 C ATOM 4357 C PHE C 193 55.280 71.890 37.060 1.00 80.33 C ANISOU 4357 C PHE C 193 13395 11596 5531 -618 -1732 -2195 C ATOM 4358 O PHE C 193 55.619 70.917 37.737 1.00 81.42 O ANISOU 4358 O PHE C 193 13603 12020 5312 -624 -1806 -1972 O ATOM 4359 CB PHE C 193 55.482 70.453 34.953 1.00 69.91 C ANISOU 4359 CB PHE C 193 11291 10179 5092 -1048 -1394 -1438 C ATOM 4360 CG PHE C 193 55.110 70.277 33.497 1.00 65.13 C ANISOU 4360 CG PHE C 193 10327 9422 4996 -1177 -1110 -1196 C ATOM 4361 CD1 PHE C 193 56.004 70.624 32.482 1.00 63.35 C ANISOU 4361 CD1 PHE C 193 9880 8875 5316 -1402 -1296 -1151 C ATOM 4362 CD2 PHE C 193 53.862 69.772 33.134 1.00 63.47 C ANISOU 4362 CD2 PHE C 193 9997 9403 4717 -1071 -663 -1005 C ATOM 4363 CE1 PHE C 193 55.656 70.470 31.125 1.00 58.53 C ANISOU 4363 CE1 PHE C 193 9014 8152 5074 -1474 -1036 -934 C ATOM 4364 CE2 PHE C 193 53.508 69.610 31.776 1.00 58.38 C ANISOU 4364 CE2 PHE C 193 9066 8618 4498 -1167 -481 -819 C ATOM 4365 CZ PHE C 193 54.404 69.963 30.781 1.00 56.39 C ANISOU 4365 CZ PHE C 193 8678 8062 4685 -1346 -666 -793 C ATOM 4366 N ASN C 194 55.142 73.120 37.551 1.00 85.06 N ANISOU 4366 N ASN C 194 14334 12007 5978 -425 -1918 -2698 N ATOM 4367 CA ASN C 194 55.252 73.448 38.969 1.00 92.16 C ANISOU 4367 CA ASN C 194 15759 13074 6182 -154 -2186 -3085 C ATOM 4368 C ASN C 194 54.264 72.670 39.841 1.00 94.71 C ANISOU 4368 C ASN C 194 16281 13962 5742 169 -1686 -2904 C ATOM 4369 O ASN C 194 54.642 72.144 40.891 1.00 98.69 O ANISOU 4369 O ASN C 194 17097 14754 5645 271 -1877 -2880 O ATOM 4370 CB ASN C 194 55.043 74.959 39.186 1.00 96.58 C ANISOU 4370 CB ASN C 194 16663 13276 6757 53 -2391 -3696 C ATOM 4371 CG ASN C 194 56.338 75.764 39.093 1.00 98.75 C ANISOU 4371 CG ASN C 194 16983 13034 7504 -239 -3133 -4001 C ATOM 4372 OD1 ASN C 194 57.321 75.327 38.488 1.00 95.93 O ANISOU 4372 OD1 ASN C 194 16244 12539 7667 -633 -3386 -3703 O ATOM 4373 ND2 ASN C 194 56.338 76.952 39.696 1.00103.88 N ANISOU 4373 ND2 ASN C 194 18086 13381 8004 -40 -3481 -4607 N ATOM 4374 N ASN C 195 53.004 72.598 39.404 1.00 93.19 N ANISOU 4374 N ASN C 195 15892 13930 5587 327 -1054 -2747 N ATOM 4375 CA ASN C 195 51.942 71.955 40.194 1.00 96.39 C ANISOU 4375 CA ASN C 195 16409 14872 5341 625 -481 -2544 C ATOM 4376 C ASN C 195 51.869 70.431 40.009 1.00 93.14 C ANISOU 4376 C ASN C 195 15685 14739 4966 386 -216 -1883 C ATOM 4377 O ASN C 195 50.974 69.773 40.545 1.00 95.34 O ANISOU 4377 O ASN C 195 15965 15437 4822 546 304 -1590 O ATOM 4378 CB ASN C 195 50.576 72.621 39.938 1.00 97.45 C ANISOU 4378 CB ASN C 195 16436 15077 5514 942 67 -2701 C ATOM 4379 CG ASN C 195 49.756 72.819 41.227 1.00105.28 C ANISOU 4379 CG ASN C 195 17832 16525 5643 1448 462 -2911 C ATOM 4380 OD1 ASN C 195 50.307 73.048 42.309 1.00110.55 O ANISOU 4380 OD1 ASN C 195 19044 17295 5664 1643 156 -3216 O ATOM 4381 ND2 ASN C 195 48.433 72.746 41.102 1.00106.53 N ANISOU 4381 ND2 ASN C 195 17717 16972 5787 1683 1141 -2757 N ATOM 4382 N SER C 196 52.815 69.880 39.247 1.00 88.46 N ANISOU 4382 N SER C 196 14819 13891 4902 10 -561 -1642 N ATOM 4383 CA SER C 196 52.993 68.436 39.161 1.00 86.31 C ANISOU 4383 CA SER C 196 14341 13788 4664 -200 -457 -1078 C ATOM 4384 C SER C 196 54.142 67.989 40.052 1.00 89.75 C ANISOU 4384 C SER C 196 15081 14290 4729 -223 -963 -1045 C ATOM 4385 O SER C 196 55.160 68.683 40.169 1.00 90.92 O ANISOU 4385 O SER C 196 15365 14197 4982 -268 -1537 -1400 O ATOM 4386 CB SER C 196 53.254 68.003 37.722 1.00 79.38 C ANISOU 4386 CB SER C 196 12973 12609 4579 -529 -480 -830 C ATOM 4387 OG SER C 196 52.042 67.846 37.014 1.00 76.73 O ANISOU 4387 OG SER C 196 12335 12335 4485 -521 25 -658 O ATOM 4388 N ILE C 197 53.966 66.837 40.695 1.00 92.16 N ANISOU 4388 N ILE C 197 15485 14907 4625 -196 -773 -598 N ATOM 4389 CA ILE C 197 55.062 66.185 41.400 1.00 95.31 C ANISOU 4389 CA ILE C 197 16112 15354 4746 -228 -1270 -445 C ATOM 4390 C ILE C 197 55.863 65.408 40.353 1.00 90.27 C ANISOU 4390 C ILE C 197 15026 14416 4858 -555 -1496 -148 C ATOM 4391 O ILE C 197 55.473 64.312 39.922 1.00 87.79 O ANISOU 4391 O ILE C 197 14480 14124 4751 -683 -1181 327 O ATOM 4392 CB ILE C 197 54.572 65.270 42.551 1.00100.38 C ANISOU 4392 CB ILE C 197 17103 16431 4605 -39 -979 -37 C ATOM 4393 N ILE C 198 56.967 66.017 39.922 1.00 89.51 N ANISOU 4393 N ILE C 198 14796 14018 5195 -684 -2030 -446 N ATOM 4394 CA ILE C 198 57.819 65.459 38.869 1.00 85.48 C ANISOU 4394 CA ILE C 198 13836 13231 5410 -944 -2221 -234 C ATOM 4395 C ILE C 198 59.163 64.974 39.435 1.00 88.94 C ANISOU 4395 C ILE C 198 14319 13656 5818 -958 -2842 -158 C ATOM 4396 O ILE C 198 59.630 65.500 40.457 1.00 94.08 O ANISOU 4396 O ILE C 198 15316 14407 6022 -824 -3287 -436 O ATOM 4397 CB ILE C 198 58.023 66.457 37.667 1.00 81.45 C ANISOU 4397 CB ILE C 198 12993 12377 5576 -1116 -2239 -522 C ATOM 4398 CG1 ILE C 198 58.865 67.681 38.070 1.00 85.25 C ANISOU 4398 CG1 ILE C 198 13613 12680 6098 -1128 -2780 -1000 C ATOM 4399 CG2 ILE C 198 56.676 66.879 37.089 1.00 78.64 C ANISOU 4399 CG2 ILE C 198 12585 12035 5260 -1063 -1677 -568 C ATOM 4400 CD1 ILE C 198 59.417 68.490 36.893 1.00 81.55 C ANISOU 4400 CD1 ILE C 198 12770 11826 6388 -1366 -2881 -1150 C ATOM 4401 N PRO C 199 59.777 63.962 38.779 1.00 86.68 N ANISOU 4401 N PRO C 199 13692 13243 5999 -1087 -2902 196 N ATOM 4402 CA PRO C 199 61.075 63.389 39.158 1.00 89.85 C ANISOU 4402 CA PRO C 199 14021 13612 6505 -1076 -3477 319 C ATOM 4403 C PRO C 199 62.181 64.418 39.400 1.00 93.24 C ANISOU 4403 C PRO C 199 14377 13921 7130 -1134 -4111 -101 C ATOM 4404 O PRO C 199 62.175 65.498 38.805 1.00 91.62 O ANISOU 4404 O PRO C 199 14009 13520 7281 -1274 -4079 -432 O ATOM 4405 CB PRO C 199 61.441 62.540 37.941 1.00 85.13 C ANISOU 4405 CB PRO C 199 12947 12799 6599 -1210 -3312 614 C ATOM 4406 CG PRO C 199 60.143 62.105 37.398 1.00 81.45 C ANISOU 4406 CG PRO C 199 12500 12351 6095 -1239 -2676 817 C ATOM 4407 CD PRO C 199 59.166 63.212 37.665 1.00 81.58 C ANISOU 4407 CD PRO C 199 12735 12485 5777 -1205 -2413 505 C ATOM 4408 N GLU C 200 63.128 64.074 40.265 1.00 98.64 N ANISOU 4408 N GLU C 200 15170 14693 7614 -1038 -4718 -67 N ATOM 4409 CA GLU C 200 64.297 64.915 40.461 1.00102.70 C ANISOU 4409 CA GLU C 200 15515 15065 8443 -1139 -5412 -430 C ATOM 4410 C GLU C 200 65.239 64.853 39.245 1.00 99.89 C ANISOU 4410 C GLU C 200 14449 14445 9059 -1371 -5456 -333 C ATOM 4411 O GLU C 200 66.064 65.753 39.056 1.00101.92 O ANISOU 4411 O GLU C 200 14417 14514 9793 -1558 -5860 -623 O ATOM 4412 CB GLU C 200 65.025 64.537 41.750 1.00109.67 C ANISOU 4412 CB GLU C 200 16709 16140 8819 -945 -6112 -420 C ATOM 4413 CG GLU C 200 65.820 65.680 42.357 1.00115.42 C ANISOU 4413 CG GLU C 200 17516 16774 9565 -1007 -6874 -948 C ATOM 4414 CD GLU C 200 66.161 65.447 43.815 1.00123.66 C ANISOU 4414 CD GLU C 200 19102 18076 9806 -736 -7526 -1022 C ATOM 4415 OE1 GLU C 200 66.283 64.272 44.224 1.00125.31 O ANISOU 4415 OE1 GLU C 200 19421 18483 9709 -547 -7561 -570 O ATOM 4416 OE2 GLU C 200 66.309 66.442 44.555 1.00128.91 O ANISOU 4416 OE2 GLU C 200 20125 18725 10129 -695 -8034 -1537 O ATOM 4417 N ASP C 201 65.099 63.805 38.423 1.00 96.02 N ANISOU 4417 N ASP C 201 13689 13934 8862 -1358 -5027 69 N ATOM 4418 CA ASP C 201 65.915 63.633 37.209 1.00 93.66 C ANISOU 4418 CA ASP C 201 12751 13433 9402 -1502 -4946 187 C ATOM 4419 C ASP C 201 65.671 64.742 36.188 1.00 90.58 C ANISOU 4419 C ASP C 201 12131 12841 9445 -1732 -4619 -40 C ATOM 4420 O ASP C 201 66.620 65.273 35.609 1.00 91.55 O ANISOU 4420 O ASP C 201 11783 12801 10201 -1911 -4802 -116 O ATOM 4421 CB ASP C 201 65.636 62.293 36.507 1.00 90.07 C ANISOU 4421 CB ASP C 201 12170 12968 9083 -1390 -4508 602 C ATOM 4422 CG ASP C 201 65.685 61.098 37.437 1.00 92.96 C ANISOU 4422 CG ASP C 201 12825 13475 9020 -1160 -4734 916 C ATOM 4423 OD1 ASP C 201 66.729 60.863 38.079 1.00 97.00 O ANISOU 4423 OD1 ASP C 201 13235 14034 9588 -1058 -5329 950 O ATOM 4424 OD2 ASP C 201 64.674 60.366 37.486 1.00 91.13 O ANISOU 4424 OD2 ASP C 201 12898 13288 8440 -1089 -4320 1163 O ATOM 4425 N THR C 202 64.394 65.077 35.986 1.00 87.62 N ANISOU 4425 N THR C 202 12071 12478 8743 -1719 -4133 -112 N ATOM 4426 CA THR C 202 63.937 65.924 34.869 1.00 84.32 C ANISOU 4426 CA THR C 202 11485 11863 8688 -1879 -3723 -231 C ATOM 4427 C THR C 202 65.025 66.776 34.213 1.00 85.99 C ANISOU 4427 C THR C 202 11239 11839 9594 -2115 -3947 -347 C ATOM 4428 O THR C 202 65.648 67.632 34.858 1.00 90.26 O ANISOU 4428 O THR C 202 11789 12283 10224 -2232 -4456 -621 O ATOM 4429 CB THR C 202 62.703 66.805 35.236 1.00 83.85 C ANISOU 4429 CB THR C 202 11866 11822 8173 -1829 -3501 -500 C ATOM 4430 OG1 THR C 202 61.658 65.980 35.767 1.00 83.18 O ANISOU 4430 OG1 THR C 202 12115 11983 7506 -1633 -3196 -323 O ATOM 4431 CG2 THR C 202 62.173 67.526 34.009 1.00 79.51 C ANISOU 4431 CG2 THR C 202 11149 11062 7999 -1948 -3077 -547 C ATOM 4432 N PHE C 203 65.240 66.518 32.925 1.00 83.20 N ANISOU 4432 N PHE C 203 10494 11390 9729 -2185 -3560 -129 N ATOM 4433 CA PHE C 203 66.122 67.332 32.103 1.00 84.91 C ANISOU 4433 CA PHE C 203 10252 11394 10615 -2422 -3584 -146 C ATOM 4434 C PHE C 203 65.432 68.654 31.731 1.00 84.00 C ANISOU 4434 C PHE C 203 10332 11053 10531 -2573 -3405 -361 C ATOM 4435 O PHE C 203 64.474 68.672 30.947 1.00 79.97 O ANISOU 4435 O PHE C 203 9968 10522 9896 -2506 -2909 -286 O ATOM 4436 CB PHE C 203 66.569 66.552 30.854 1.00 82.70 C ANISOU 4436 CB PHE C 203 9542 11135 10745 -2376 -3170 176 C ATOM 4437 CG PHE C 203 67.555 67.297 29.974 1.00 85.75 C ANISOU 4437 CG PHE C 203 9398 11357 11825 -2607 -3102 250 C ATOM 4438 CD1 PHE C 203 68.712 67.876 30.515 1.00 91.81 C ANISOU 4438 CD1 PHE C 203 9798 12044 13041 -2817 -3620 165 C ATOM 4439 CD2 PHE C 203 67.339 67.398 28.598 1.00 83.24 C ANISOU 4439 CD2 PHE C 203 8939 10974 11715 -2618 -2526 431 C ATOM 4440 CE1 PHE C 203 69.624 68.559 29.699 1.00 94.90 C ANISOU 4440 CE1 PHE C 203 9634 12281 14142 -3075 -3512 296 C ATOM 4441 CE2 PHE C 203 68.245 68.076 27.775 1.00 86.39 C ANISOU 4441 CE2 PHE C 203 8852 11246 12726 -2831 -2383 573 C ATOM 4442 CZ PHE C 203 69.390 68.658 28.326 1.00 92.15 C ANISOU 4442 CZ PHE C 203 9160 11886 13965 -3078 -2850 527 C ATOM 4443 N PHE C 204 65.903 69.739 32.347 1.00 88.34 N ANISOU 4443 N PHE C 204 10910 11411 11246 -2757 -3870 -645 N ATOM 4444 CA PHE C 204 65.533 71.099 31.977 1.00 88.84 C ANISOU 4444 CA PHE C 204 11096 11151 11507 -2932 -3801 -845 C ATOM 4445 C PHE C 204 66.738 71.709 31.260 1.00 91.91 C ANISOU 4445 C PHE C 204 10922 11285 12715 -3268 -3910 -707 C ATOM 4446 O PHE C 204 67.700 72.130 31.917 1.00 97.26 O ANISOU 4446 O PHE C 204 11393 11842 13719 -3468 -4492 -863 O ATOM 4447 CB PHE C 204 65.209 71.943 33.216 1.00 92.89 C ANISOU 4447 CB PHE C 204 12084 11558 11652 -2900 -4284 -1304 C ATOM 4448 CG PHE C 204 63.919 71.578 33.903 1.00 90.83 C ANISOU 4448 CG PHE C 204 12380 11545 10586 -2568 -4076 -1438 C ATOM 4449 CD1 PHE C 204 63.933 71.021 35.181 1.00 94.06 C ANISOU 4449 CD1 PHE C 204 13096 12224 10419 -2374 -4424 -1566 C ATOM 4450 CD2 PHE C 204 62.690 71.827 33.295 1.00 86.77 C ANISOU 4450 CD2 PHE C 204 12072 11006 9891 -2441 -3539 -1417 C ATOM 4451 CE1 PHE C 204 62.741 70.695 35.836 1.00 93.07 C ANISOU 4451 CE1 PHE C 204 13456 12358 9547 -2073 -4157 -1636 C ATOM 4452 CE2 PHE C 204 61.493 71.507 33.941 1.00 85.58 C ANISOU 4452 CE2 PHE C 204 12345 11109 9063 -2145 -3311 -1515 C ATOM 4453 CZ PHE C 204 61.520 70.940 35.212 1.00 88.82 C ANISOU 4453 CZ PHE C 204 13041 11802 8903 -1970 -3582 -1609 C ATOM 4454 N PRO C 205 66.699 71.750 29.913 1.00 89.07 N ANISOU 4454 N PRO C 205 10302 10854 12688 -3334 -3358 -401 N ATOM 4455 CA PRO C 205 67.829 72.201 29.087 1.00 92.19 C ANISOU 4455 CA PRO C 205 10108 11069 13851 -3636 -3294 -152 C ATOM 4456 C PRO C 205 68.102 73.716 29.139 1.00 96.66 C ANISOU 4456 C PRO C 205 10663 11174 14888 -3996 -3574 -310 C ATOM 4457 O PRO C 205 67.871 74.357 30.169 1.00 99.27 O ANISOU 4457 O PRO C 205 11350 11327 15040 -4034 -4089 -712 O ATOM 4458 CB PRO C 205 67.424 71.757 27.676 1.00 87.89 C ANISOU 4458 CB PRO C 205 9480 10626 13288 -3503 -2562 197 C ATOM 4459 CG PRO C 205 65.941 71.744 27.702 1.00 83.26 C ANISOU 4459 CG PRO C 205 9486 10069 12080 -3267 -2343 44 C ATOM 4460 CD PRO C 205 65.559 71.313 29.087 1.00 83.32 C ANISOU 4460 CD PRO C 205 9824 10240 11592 -3107 -2756 -252 C ATOM 4461 N SER C 206 68.602 74.269 28.034 1.00 98.11 N ANISOU 4461 N SER C 206 10465 11153 15661 -4246 -3230 12 N ATOM 4462 CA SER C 206 69.024 75.669 27.979 1.00103.38 C ANISOU 4462 CA SER C 206 11033 11316 16930 -4656 -3485 -38 C ATOM 4463 C SER C 206 68.965 76.212 26.550 1.00103.05 C ANISOU 4463 C SER C 206 10841 11082 17232 -4796 -2853 392 C ATOM 4464 O SER C 206 69.766 77.065 26.158 1.00108.39 O ANISOU 4464 O SER C 206 11134 11419 18632 -5202 -2892 605 O ATOM 4465 CB SER C 206 70.438 75.817 28.553 1.00110.07 C ANISOU 4465 CB SER C 206 11285 12079 18457 -5002 -4057 -57 C ATOM 4466 OG SER C 206 70.775 77.179 28.698 1.00115.74 O ANISOU 4466 OG SER C 206 11974 12243 19759 -5428 -4436 -186 O TER 4467 SER C 206 ATOM 4468 N ALA D 2 33.229 40.784 4.077 1.00 37.69 N ATOM 4469 CA ALA D 2 31.786 41.168 4.254 1.00 37.63 C ATOM 4470 C ALA D 2 31.589 42.552 4.959 1.00 37.25 C ATOM 4471 O ALA D 2 31.257 42.629 6.156 1.00 37.10 O ATOM 4472 CB ALA D 2 30.989 40.024 4.952 1.00 37.36 C ATOM 4473 N ALA D 3 31.771 43.627 4.176 1.00 57.14 N ANISOU 4473 N ALA D 3 6423 7913 7373 -256 1521 -259 N ATOM 4474 CA ALA D 3 31.840 45.009 4.686 1.00 55.50 C ANISOU 4474 CA ALA D 3 6181 7701 7204 -350 1434 -147 C ATOM 4475 C ALA D 3 30.518 45.788 4.715 1.00 52.84 C ANISOU 4475 C ALA D 3 6105 7333 6637 -398 1252 33 C ATOM 4476 O ALA D 3 29.640 45.587 3.863 1.00 52.91 O ANISOU 4476 O ALA D 3 6364 7332 6408 -444 1263 90 O ATOM 4477 CB ALA D 3 32.890 45.797 3.913 1.00 58.05 C ANISOU 4477 CB ALA D 3 6427 8053 7577 -535 1719 -197 C ATOM 4478 N VAL D 4 30.408 46.689 5.699 1.00 50.36 N ANISOU 4478 N VAL D 4 5728 6991 6414 -386 1077 115 N ATOM 4479 CA VAL D 4 29.247 47.573 5.887 1.00 47.34 C ANISOU 4479 CA VAL D 4 5540 6562 5884 -415 904 270 C ATOM 4480 C VAL D 4 29.682 49.039 6.062 1.00 47.05 C ANISOU 4480 C VAL D 4 5487 6497 5894 -541 906 338 C ATOM 4481 O VAL D 4 30.439 49.374 6.972 1.00 46.85 O ANISOU 4481 O VAL D 4 5273 6463 6064 -516 854 302 O ATOM 4482 CB VAL D 4 28.381 47.124 7.095 1.00 45.22 C ANISOU 4482 CB VAL D 4 5258 6260 5662 -249 666 302 C ATOM 4483 CG1 VAL D 4 27.224 48.095 7.348 1.00 43.49 C ANISOU 4483 CG1 VAL D 4 5194 5984 5348 -266 517 439 C ATOM 4484 CG2 VAL D 4 27.854 45.718 6.875 1.00 44.54 C ANISOU 4484 CG2 VAL D 4 5219 6189 5514 -146 652 252 C ATOM 4485 N THR D 5 29.184 49.905 5.183 1.00 46.62 N ANISOU 4485 N THR D 5 5649 6409 5654 -681 937 442 N ATOM 4486 CA THR D 5 29.551 51.323 5.175 1.00 46.43 C ANISOU 4486 CA THR D 5 5658 6341 5643 -825 942 517 C ATOM 4487 C THR D 5 28.445 52.176 5.772 1.00 44.42 C ANISOU 4487 C THR D 5 5531 6000 5348 -774 703 642 C ATOM 4488 O THR D 5 27.260 51.902 5.569 1.00 43.49 O ANISOU 4488 O THR D 5 5557 5849 5118 -706 585 704 O ATOM 4489 CB THR D 5 29.873 51.836 3.739 1.00 48.65 C ANISOU 4489 CB THR D 5 6128 6617 5740 -1050 1150 550 C ATOM 4490 OG1 THR D 5 28.885 51.363 2.812 1.00 48.10 O ANISOU 4490 OG1 THR D 5 6318 6524 5434 -1059 1122 603 O ATOM 4491 CG2 THR D 5 31.243 51.349 3.286 1.00 50.29 C ANISOU 4491 CG2 THR D 5 6156 6900 6052 -1134 1448 407 C ATOM 4492 N GLN D 6 28.839 53.211 6.508 1.00 43.73 N ANISOU 4492 N GLN D 6 5379 5865 5372 -808 633 672 N ATOM 4493 CA GLN D 6 27.894 54.139 7.131 1.00 41.95 C ANISOU 4493 CA GLN D 6 5266 5539 5135 -759 432 770 C ATOM 4494 C GLN D 6 28.270 55.553 6.762 1.00 42.94 C ANISOU 4494 C GLN D 6 5495 5591 5231 -930 441 850 C ATOM 4495 O GLN D 6 29.439 55.917 6.843 1.00 44.20 O ANISOU 4495 O GLN D 6 5535 5773 5485 -1041 547 807 O ATOM 4496 CB GLN D 6 27.976 54.029 8.652 1.00 40.88 C ANISOU 4496 CB GLN D 6 4985 5387 5160 -618 308 718 C ATOM 4497 CG GLN D 6 26.935 53.176 9.301 1.00 39.12 C ANISOU 4497 CG GLN D 6 4772 5163 4928 -443 204 703 C ATOM 4498 CD GLN D 6 27.258 52.920 10.746 1.00 38.58 C ANISOU 4498 CD GLN D 6 4595 5078 4987 -340 114 637 C ATOM 4499 OE1 GLN D 6 28.052 52.043 11.062 1.00 38.84 O ANISOU 4499 OE1 GLN D 6 4489 5163 5104 -303 140 552 O ATOM 4500 NE2 GLN D 6 26.640 53.685 11.639 1.00 38.50 N ANISOU 4500 NE2 GLN D 6 4664 4975 4990 -293 1 672 N ATOM 4501 N SER D 7 27.293 56.365 6.382 1.00 42.54 N ANISOU 4501 N SER D 7 5655 5436 5073 -955 316 964 N ATOM 4502 CA SER D 7 27.565 57.783 6.190 1.00 43.74 C ANISOU 4502 CA SER D 7 5928 5486 5206 -1104 280 1048 C ATOM 4503 C SER D 7 26.447 58.647 6.771 1.00 42.86 C ANISOU 4503 C SER D 7 5925 5234 5125 -1001 54 1126 C ATOM 4504 O SER D 7 25.287 58.243 6.745 1.00 41.83 O ANISOU 4504 O SER D 7 5844 5076 4975 -871 -52 1151 O ATOM 4505 CB SER D 7 27.776 58.100 4.714 1.00 45.50 C ANISOU 4505 CB SER D 7 6361 5690 5236 -1319 394 1118 C ATOM 4506 OG SER D 7 26.582 58.579 4.142 1.00 46.15 O ANISOU 4506 OG SER D 7 6692 5650 5192 -1313 214 1238 O ATOM 4507 N PRO D 8 26.796 59.824 7.327 1.00 43.40 N ANISOU 4507 N PRO D 8 6017 5208 5266 -1055 -13 1156 N ATOM 4508 CA PRO D 8 28.153 60.314 7.556 1.00 44.59 C ANISOU 4508 CA PRO D 8 6072 5382 5487 -1202 86 1122 C ATOM 4509 C PRO D 8 28.755 59.632 8.766 1.00 43.73 C ANISOU 4509 C PRO D 8 5724 5350 5542 -1085 94 1004 C ATOM 4510 O PRO D 8 28.074 58.880 9.454 1.00 42.23 O ANISOU 4510 O PRO D 8 5482 5182 5380 -901 28 958 O ATOM 4511 CB PRO D 8 27.941 61.794 7.871 1.00 45.43 C ANISOU 4511 CB PRO D 8 6327 5321 5612 -1256 -62 1204 C ATOM 4512 CG PRO D 8 26.597 61.848 8.479 1.00 44.12 C ANISOU 4512 CG PRO D 8 6219 5066 5477 -1049 -232 1216 C ATOM 4513 CD PRO D 8 25.782 60.788 7.793 1.00 43.09 C ANISOU 4513 CD PRO D 8 6098 5008 5266 -966 -209 1221 C ATOM 4514 N ARG D 9 30.022 59.899 9.035 1.00 45.08 N ANISOU 4514 N ARG D 9 5757 5547 5825 -1202 161 959 N ATOM 4515 CA ARG D 9 30.679 59.265 10.167 1.00 44.64 C ANISOU 4515 CA ARG D 9 5486 5538 5937 -1104 122 854 C ATOM 4516 C ARG D 9 30.554 60.132 11.409 1.00 43.53 C ANISOU 4516 C ARG D 9 5403 5271 5865 -1055 -67 863 C ATOM 4517 O ARG D 9 30.795 59.685 12.528 1.00 43.25 O ANISOU 4517 O ARG D 9 5275 5232 5926 -953 -162 791 O ATOM 4518 CB ARG D 9 32.135 58.935 9.813 1.00 46.64 C ANISOU 4518 CB ARG D 9 5515 5881 6326 -1241 281 783 C ATOM 4519 CG ARG D 9 32.244 57.913 8.659 1.00 49.42 C ANISOU 4519 CG ARG D 9 5817 6354 6606 -1266 502 742 C ATOM 4520 CD ARG D 9 32.059 56.448 9.123 1.00 51.02 C ANISOU 4520 CD ARG D 9 5881 6637 6866 -1066 484 644 C ATOM 4521 NE ARG D 9 33.354 55.849 9.447 1.00 56.09 N ANISOU 4521 NE ARG D 9 6233 7338 7741 -1075 551 527 N ATOM 4522 CZ ARG D 9 33.924 55.854 10.657 1.00 58.27 C ANISOU 4522 CZ ARG D 9 6359 7570 8212 -1011 378 480 C ATOM 4523 NH1 ARG D 9 33.312 56.407 11.711 1.00 57.67 N ANISOU 4523 NH1 ARG D 9 6421 7395 8095 -936 155 531 N ATOM 4524 NH2 ARG D 9 35.119 55.293 10.819 1.00 59.90 N ANISOU 4524 NH2 ARG D 9 6280 7816 8664 -1022 424 374 N ATOM 4525 N ASN D 10 30.123 61.366 11.197 1.00 43.20 N ANISOU 4525 N ASN D 10 5550 5108 5756 -1129 -133 952 N ATOM 4526 CA ASN D 10 30.045 62.350 12.248 1.00 42.55 C ANISOU 4526 CA ASN D 10 5559 4882 5725 -1108 -294 958 C ATOM 4527 C ASN D 10 29.117 63.483 11.805 1.00 42.72 C ANISOU 4527 C ASN D 10 5817 4762 5652 -1126 -366 1058 C ATOM 4528 O ASN D 10 29.244 63.992 10.691 1.00 43.90 O ANISOU 4528 O ASN D 10 6057 4896 5727 -1280 -310 1141 O ATOM 4529 CB ASN D 10 31.451 62.875 12.547 1.00 44.16 C ANISOU 4529 CB ASN D 10 5647 5070 6060 -1277 -307 937 C ATOM 4530 CG ASN D 10 31.606 63.358 13.964 1.00 42.96 C ANISOU 4530 CG ASN D 10 5538 4800 5985 -1221 -493 896 C ATOM 4531 OD1 ASN D 10 30.670 63.866 14.560 1.00 41.93 O ANISOU 4531 OD1 ASN D 10 5595 4552 5785 -1112 -591 908 O ATOM 4532 ND2 ASN D 10 32.793 63.196 14.513 1.00 42.34 N ANISOU 4532 ND2 ASN D 10 5288 4739 6060 -1296 -544 841 N ATOM 4533 N LYS D 11 28.173 63.860 12.666 1.00 41.63 N ANISOU 4533 N LYS D 11 5790 4506 5520 -972 -486 1044 N ATOM 4534 CA LYS D 11 27.181 64.890 12.334 1.00 41.45 C ANISOU 4534 CA LYS D 11 5968 4324 5456 -945 -577 1122 C ATOM 4535 C LYS D 11 26.832 65.795 13.515 1.00 41.43 C ANISOU 4535 C LYS D 11 6080 4149 5513 -859 -697 1083 C ATOM 4536 O LYS D 11 26.569 65.321 14.629 1.00 40.32 O ANISOU 4536 O LYS D 11 5907 4010 5404 -721 -701 990 O ATOM 4537 CB LYS D 11 25.906 64.260 11.764 1.00 40.38 C ANISOU 4537 CB LYS D 11 5851 4215 5278 -805 -567 1144 C ATOM 4538 CG LYS D 11 24.807 65.258 11.373 1.00 41.20 C ANISOU 4538 CG LYS D 11 6131 4135 5387 -755 -696 1222 C ATOM 4539 CD LYS D 11 25.233 66.154 10.215 1.00 42.55 C ANISOU 4539 CD LYS D 11 6461 4230 5475 -963 -740 1344 C ATOM 4540 CE LYS D 11 24.073 66.958 9.644 1.00 42.74 C ANISOU 4540 CE LYS D 11 6665 4065 5510 -905 -908 1434 C ATOM 4541 NZ LYS D 11 24.565 67.934 8.629 1.00 43.72 N ANISOU 4541 NZ LYS D 11 6999 4083 5531 -1132 -974 1560 N ATOM 4542 N VAL D 12 26.846 67.101 13.244 1.00 42.52 N ANISOU 4542 N VAL D 12 6383 4124 5650 -954 -790 1154 N ATOM 4543 CA VAL D 12 26.378 68.128 14.179 1.00 42.49 C ANISOU 4543 CA VAL D 12 6533 3917 5696 -871 -906 1122 C ATOM 4544 C VAL D 12 25.060 68.705 13.660 1.00 42.72 C ANISOU 4544 C VAL D 12 6685 3801 5745 -755 -978 1174 C ATOM 4545 O VAL D 12 25.005 69.253 12.553 1.00 43.62 O ANISOU 4545 O VAL D 12 6896 3857 5819 -866 -1038 1287 O ATOM 4546 CB VAL D 12 27.435 69.239 14.391 1.00 43.87 C ANISOU 4546 CB VAL D 12 6804 3980 5883 -1061 -990 1153 C ATOM 4547 CG1 VAL D 12 26.830 70.441 15.083 1.00 44.10 C ANISOU 4547 CG1 VAL D 12 7044 3765 5948 -983 -1116 1134 C ATOM 4548 CG2 VAL D 12 28.596 68.700 15.201 1.00 43.20 C ANISOU 4548 CG2 VAL D 12 6583 3995 5836 -1131 -970 1078 C ATOM 4549 N ALA D 13 24.007 68.559 14.465 1.00 41.76 N ANISOU 4549 N ALA D 13 6562 3611 5694 -540 -973 1088 N ATOM 4550 CA ALA D 13 22.663 68.973 14.073 1.00 41.94 C ANISOU 4550 CA ALA D 13 6638 3493 5803 -393 -1042 1114 C ATOM 4551 C ALA D 13 21.994 69.801 15.146 1.00 42.65 C ANISOU 4551 C ALA D 13 6828 3376 6000 -242 -1072 1018 C ATOM 4552 O ALA D 13 22.340 69.698 16.317 1.00 42.52 O ANISOU 4552 O ALA D 13 6833 3361 5962 -215 -1002 912 O ATOM 4553 CB ALA D 13 21.831 67.773 13.774 1.00 40.59 C ANISOU 4553 CB ALA D 13 6310 3458 5655 -267 -963 1094 C ATOM 4554 N VAL D 14 21.025 70.609 14.730 1.00 43.71 N ANISOU 4554 N VAL D 14 7036 3318 6254 -145 -1183 1052 N ATOM 4555 CA VAL D 14 20.252 71.447 15.636 1.00 44.79 C ANISOU 4555 CA VAL D 14 7257 3231 6530 22 -1196 948 C ATOM 4556 C VAL D 14 18.911 70.779 15.960 1.00 44.71 C ANISOU 4556 C VAL D 14 7085 3228 6676 251 -1089 852 C ATOM 4557 O VAL D 14 18.419 69.955 15.182 1.00 43.96 O ANISOU 4557 O VAL D 14 6842 3253 6608 279 -1091 908 O ATOM 4558 CB VAL D 14 20.039 72.869 15.036 1.00 46.78 C ANISOU 4558 CB VAL D 14 7688 3224 6864 -2 -1403 1033 C ATOM 4559 CG1 VAL D 14 19.097 72.833 13.841 1.00 47.13 C ANISOU 4559 CG1 VAL D 14 7679 3212 7015 60 -1541 1136 C ATOM 4560 CG2 VAL D 14 19.537 73.841 16.090 1.00 48.20 C ANISOU 4560 CG2 VAL D 14 7985 3157 7172 144 -1403 906 C ATOM 4561 N THR D 15 18.338 71.135 17.111 1.00 45.68 N ANISOU 4561 N THR D 15 7245 3214 6898 402 -983 702 N ATOM 4562 CA THR D 15 17.005 70.681 17.522 1.00 46.04 C ANISOU 4562 CA THR D 15 7135 3227 7133 618 -847 588 C ATOM 4563 C THR D 15 15.962 71.027 16.464 1.00 47.33 C ANISOU 4563 C THR D 15 7190 3268 7525 725 -1010 666 C ATOM 4564 O THR D 15 15.948 72.141 15.945 1.00 48.79 O ANISOU 4564 O THR D 15 7500 3253 7785 713 -1209 736 O ATOM 4565 CB THR D 15 16.565 71.330 18.861 1.00 47.47 C ANISOU 4565 CB THR D 15 7426 3217 7395 749 -700 406 C ATOM 4566 OG1 THR D 15 17.653 71.314 19.788 1.00 47.05 O ANISOU 4566 OG1 THR D 15 7554 3210 7112 621 -637 357 O ATOM 4567 CG2 THR D 15 15.380 70.592 19.471 1.00 47.73 C ANISOU 4567 CG2 THR D 15 7283 3272 7582 929 -468 265 C ATOM 4568 N GLY D 16 15.098 70.063 16.156 1.00 46.90 N ANISOU 4568 N GLY D 16 6915 3319 7584 820 -948 657 N ATOM 4569 CA GLY D 16 13.989 70.277 15.240 1.00 48.64 C ANISOU 4569 CA GLY D 16 7006 3412 8062 937 -1123 717 C ATOM 4570 C GLY D 16 14.360 70.140 13.773 1.00 48.59 C ANISOU 4570 C GLY D 16 7052 3467 7943 787 -1366 918 C ATOM 4571 O GLY D 16 13.489 70.215 12.905 1.00 50.03 O ANISOU 4571 O GLY D 16 7155 3546 8309 859 -1561 992 O ATOM 4572 N GLY D 17 15.646 69.945 13.489 1.00 47.26 N ANISOU 4572 N GLY D 17 7023 3453 7482 574 -1359 1002 N ATOM 4573 CA GLY D 17 16.113 69.759 12.116 1.00 47.14 C ANISOU 4573 CA GLY D 17 7090 3509 7312 398 -1529 1178 C ATOM 4574 C GLY D 17 16.135 68.298 11.701 1.00 45.34 C ANISOU 4574 C GLY D 17 6716 3534 6977 357 -1428 1197 C ATOM 4575 O GLY D 17 16.178 67.404 12.549 1.00 43.82 O ANISOU 4575 O GLY D 17 6387 3498 6763 413 -1215 1087 O ATOM 4576 N LYS D 18 16.112 68.061 10.391 1.00 45.81 N ANISOU 4576 N LYS D 18 6837 3615 6952 249 -1590 1339 N ATOM 4577 CA LYS D 18 16.065 66.703 9.840 1.00 44.46 C ANISOU 4577 CA LYS D 18 6557 3656 6678 208 -1524 1364 C ATOM 4578 C LYS D 18 17.452 66.112 9.685 1.00 42.57 C ANISOU 4578 C LYS D 18 6381 3635 6160 12 -1370 1382 C ATOM 4579 O LYS D 18 18.304 66.678 9.013 1.00 43.36 O ANISOU 4579 O LYS D 18 6662 3712 6101 -172 -1427 1476 O ATOM 4580 CB LYS D 18 15.323 66.676 8.496 1.00 45.92 C ANISOU 4580 CB LYS D 18 6807 3743 6899 183 -1782 1499 C ATOM 4581 CG LYS D 18 15.666 65.460 7.620 1.00 46.36 C ANISOU 4581 CG LYS D 18 6873 4002 6740 52 -1738 1560 C ATOM 4582 CD LYS D 18 14.680 65.253 6.471 1.00 49.91 C ANISOU 4582 CD LYS D 18 7366 4342 7255 62 -2005 1670 C ATOM 4583 CE LYS D 18 13.502 64.388 6.898 1.00 49.68 C ANISOU 4583 CE LYS D 18 7059 4345 7472 256 -1989 1587 C ATOM 4584 NZ LYS D 18 12.430 64.351 5.860 1.00 53.20 N ANISOU 4584 NZ LYS D 18 7527 4633 8052 283 -2310 1693 N ATOM 4585 N VAL D 19 17.677 64.964 10.311 1.00 40.68 N ANISOU 4585 N VAL D 19 5984 3596 5875 49 -1171 1289 N ATOM 4586 CA VAL D 19 18.951 64.263 10.156 1.00 39.02 C ANISOU 4586 CA VAL D 19 5786 3590 5450 -111 -1031 1291 C ATOM 4587 C VAL D 19 18.708 62.880 9.583 1.00 37.89 C ANISOU 4587 C VAL D 19 5543 3614 5241 -108 -976 1296 C ATOM 4588 O VAL D 19 17.861 62.125 10.085 1.00 37.06 O ANISOU 4588 O VAL D 19 5288 3546 5248 37 -931 1228 O ATOM 4589 CB VAL D 19 19.717 64.116 11.482 1.00 37.89 C ANISOU 4589 CB VAL D 19 5577 3525 5293 -91 -866 1172 C ATOM 4590 CG1 VAL D 19 21.083 63.511 11.229 1.00 36.74 C ANISOU 4590 CG1 VAL D 19 5419 3559 4982 -257 -760 1179 C ATOM 4591 CG2 VAL D 19 19.846 65.453 12.177 1.00 38.59 C ANISOU 4591 CG2 VAL D 19 5778 3431 5454 -78 -923 1150 C ATOM 4592 N THR D 20 19.456 62.557 8.533 1.00 37.79 N ANISOU 4592 N THR D 20 5625 3691 5042 -281 -964 1371 N ATOM 4593 CA THR D 20 19.366 61.253 7.914 1.00 36.85 C ANISOU 4593 CA THR D 20 5448 3723 4830 -298 -906 1371 C ATOM 4594 C THR D 20 20.701 60.550 7.957 1.00 35.82 C ANISOU 4594 C THR D 20 5276 3779 4556 -414 -710 1320 C ATOM 4595 O THR D 20 21.656 60.974 7.308 1.00 36.55 O ANISOU 4595 O THR D 20 5481 3883 4522 -592 -667 1367 O ATOM 4596 CB THR D 20 18.895 61.349 6.477 1.00 38.19 C ANISOU 4596 CB THR D 20 5789 3813 4907 -393 -1071 1497 C ATOM 4597 OG1 THR D 20 17.612 61.986 6.448 1.00 40.09 O ANISOU 4597 OG1 THR D 20 6036 3860 5336 -267 -1293 1543 O ATOM 4598 CG2 THR D 20 18.782 59.968 5.876 1.00 37.98 C ANISOU 4598 CG2 THR D 20 5723 3932 4775 -409 -1009 1485 C ATOM 4599 N LEU D 21 20.749 59.479 8.745 1.00 34.19 N ANISOU 4599 N LEU D 21 4902 3701 4386 -313 -593 1218 N ATOM 4600 CA LEU D 21 21.892 58.589 8.786 1.00 33.26 C ANISOU 4600 CA LEU D 21 4707 3752 4178 -386 -433 1157 C ATOM 4601 C LEU D 21 21.666 57.478 7.788 1.00 33.75 C ANISOU 4601 C LEU D 21 4781 3908 4135 -413 -402 1174 C ATOM 4602 O LEU D 21 20.549 56.994 7.632 1.00 33.84 O ANISOU 4602 O LEU D 21 4780 3893 4186 -316 -487 1191 O ATOM 4603 CB LEU D 21 22.056 58.004 10.174 1.00 31.46 C ANISOU 4603 CB LEU D 21 4333 3584 4035 -267 -360 1045 C ATOM 4604 CG LEU D 21 22.068 59.021 11.301 1.00 30.20 C ANISOU 4604 CG LEU D 21 4195 3310 3968 -219 -399 1013 C ATOM 4605 CD1 LEU D 21 22.192 58.284 12.620 1.00 27.40 C ANISOU 4605 CD1 LEU D 21 3751 3008 3651 -121 -334 906 C ATOM 4606 CD2 LEU D 21 23.189 60.036 11.098 1.00 29.27 C ANISOU 4606 CD2 LEU D 21 4151 3154 3818 -373 -407 1048 C ATOM 4607 N SER D 22 22.726 57.074 7.108 1.00 34.88 N ANISOU 4607 N SER D 22 4944 4151 4157 -549 -273 1161 N ATOM 4608 CA SER D 22 22.604 56.127 6.013 1.00 35.81 C ANISOU 4608 CA SER D 22 5130 4337 4140 -602 -229 1175 C ATOM 4609 C SER D 22 23.567 54.966 6.192 1.00 35.78 C ANISOU 4609 C SER D 22 4985 4490 4121 -600 -44 1063 C ATOM 4610 O SER D 22 24.644 55.109 6.783 1.00 36.44 O ANISOU 4610 O SER D 22 4950 4624 4273 -629 56 999 O ATOM 4611 CB SER D 22 22.848 56.836 4.678 1.00 37.63 C ANISOU 4611 CB SER D 22 5598 4498 4203 -800 -242 1275 C ATOM 4612 OG SER D 22 22.239 58.123 4.677 1.00 38.40 O ANISOU 4612 OG SER D 22 5818 4428 4345 -810 -426 1373 O ATOM 4613 N CYS D 23 23.175 53.810 5.676 1.00 35.84 N ANISOU 4613 N CYS D 23 5002 4557 4057 -564 -22 1040 N ATOM 4614 CA CYS D 23 23.993 52.618 5.775 1.00 35.43 C ANISOU 4614 CA CYS D 23 4825 4633 4003 -542 135 928 C ATOM 4615 C CYS D 23 23.928 51.845 4.480 1.00 36.34 C ANISOU 4615 C CYS D 23 5081 4780 3947 -624 206 931 C ATOM 4616 O CYS D 23 22.854 51.707 3.886 1.00 36.68 O ANISOU 4616 O CYS D 23 5268 4761 3907 -617 70 1005 O ATOM 4617 CB CYS D 23 23.473 51.750 6.895 1.00 33.86 C ANISOU 4617 CB CYS D 23 4480 4464 3920 -365 77 867 C ATOM 4618 SG CYS D 23 24.405 50.288 7.104 1.00 34.24 S ANISOU 4618 SG CYS D 23 4385 4632 3992 -316 214 735 S ATOM 4619 N ASN D 24 25.069 51.324 4.051 1.00 37.11 N ANISOU 4619 N ASN D 24 5134 4963 4004 -701 415 843 N ATOM 4620 CA ASN D 24 25.159 50.664 2.754 1.00 38.36 C ANISOU 4620 CA ASN D 24 5464 5141 3969 -805 532 827 C ATOM 4621 C ASN D 24 25.966 49.366 2.784 1.00 38.12 C ANISOU 4621 C ASN D 24 5289 5215 3981 -749 718 677 C ATOM 4622 O ASN D 24 27.063 49.335 3.350 1.00 38.26 O ANISOU 4622 O ASN D 24 5093 5290 4153 -733 849 583 O ATOM 4623 CB ASN D 24 25.746 51.638 1.728 1.00 40.58 C ANISOU 4623 CB ASN D 24 5942 5379 4097 -1031 651 882 C ATOM 4624 CG ASN D 24 25.992 50.984 0.393 1.00 43.14 C ANISOU 4624 CG ASN D 24 6482 5717 4192 -1167 823 848 C ATOM 4625 OD1 ASN D 24 27.107 50.528 0.106 1.00 44.68 O ANISOU 4625 OD1 ASN D 24 6591 5991 4393 -1231 1100 726 O ATOM 4626 ND2 ASN D 24 24.943 50.897 -0.426 1.00 43.78 N ANISOU 4626 ND2 ASN D 24 6843 5710 4083 -1209 657 945 N ATOM 4627 N GLN D 25 25.427 48.310 2.166 1.00 37.96 N ANISOU 4627 N GLN D 25 5383 5200 3839 -718 711 653 N ATOM 4628 CA GLN D 25 26.092 46.994 2.123 1.00 38.27 C ANISOU 4628 CA GLN D 25 5311 5315 3916 -650 873 505 C ATOM 4629 C GLN D 25 25.919 46.257 0.799 1.00 40.03 C ANISOU 4629 C GLN D 25 5782 5523 3906 -741 976 477 C ATOM 4630 O GLN D 25 24.790 46.027 0.347 1.00 40.23 O ANISOU 4630 O GLN D 25 6009 5486 3791 -743 797 563 O ATOM 4631 CB GLN D 25 25.660 46.102 3.296 1.00 36.21 C ANISOU 4631 CB GLN D 25 4868 5075 3817 -447 727 464 C ATOM 4632 CG GLN D 25 24.155 45.791 3.390 1.00 34.36 C ANISOU 4632 CG GLN D 25 4748 4787 3522 -379 498 558 C ATOM 4633 CD GLN D 25 23.714 44.579 2.578 1.00 34.34 C ANISOU 4633 CD GLN D 25 4889 4778 3379 -375 502 522 C ATOM 4634 OE1 GLN D 25 24.532 43.751 2.161 1.00 35.36 O ANISOU 4634 OE1 GLN D 25 5009 4949 3479 -377 679 402 O ATOM 4635 NE2 GLN D 25 22.409 44.467 2.359 1.00 33.23 N ANISOU 4635 NE2 GLN D 25 4876 4575 3173 -367 301 620 N ATOM 4636 N THR D 26 27.044 45.875 0.193 1.00 41.83 N ANISOU 4636 N THR D 26 5991 5797 4107 -817 1266 348 N ATOM 4637 CA THR D 26 27.043 45.212 -1.116 1.00 43.67 C ANISOU 4637 CA THR D 26 6494 6006 4092 -926 1424 296 C ATOM 4638 C THR D 26 27.181 43.690 -1.008 1.00 43.47 C ANISOU 4638 C THR D 26 6378 6013 4125 -780 1484 151 C ATOM 4639 O THR D 26 27.597 43.022 -1.959 1.00 45.33 O ANISOU 4639 O THR D 26 6766 6241 4215 -849 1705 42 O ATOM 4640 CB THR D 26 28.170 45.749 -1.996 1.00 46.35 C ANISOU 4640 CB THR D 26 6914 6360 4338 -1128 1763 228 C ATOM 4641 OG1 THR D 26 29.406 45.645 -1.285 1.00 47.06 O ANISOU 4641 OG1 THR D 26 6635 6529 4716 -1057 1956 90 O ATOM 4642 CG2 THR D 26 27.924 47.194 -2.348 1.00 47.01 C ANISOU 4642 CG2 THR D 26 7190 6381 4291 -1310 1689 387 C ATOM 4643 N ASN D 27 26.814 43.159 0.155 1.00 41.34 N ANISOU 4643 N ASN D 27 5889 5763 4057 -585 1289 148 N ATOM 4644 CA ASN D 27 26.919 41.734 0.464 1.00 41.32 C ANISOU 4644 CA ASN D 27 5784 5773 4141 -430 1295 23 C ATOM 4645 C ASN D 27 25.750 40.911 -0.061 1.00 40.96 C ANISOU 4645 C ASN D 27 5988 5671 3905 -418 1132 73 C ATOM 4646 O ASN D 27 25.765 39.676 -0.008 1.00 40.54 O ANISOU 4646 O ASN D 27 5918 5609 3876 -315 1138 -26 O ATOM 4647 CB ASN D 27 26.960 41.553 1.977 1.00 39.46 C ANISOU 4647 CB ASN D 27 5259 5561 4172 -253 1126 19 C ATOM 4648 CG ASN D 27 28.192 42.140 2.602 1.00 40.41 C ANISOU 4648 CG ASN D 27 5110 5723 4521 -243 1246 -49 C ATOM 4649 OD1 ASN D 27 29.294 42.013 2.069 1.00 41.30 O ANISOU 4649 OD1 ASN D 27 5137 5862 4695 -291 1502 -177 O ATOM 4650 ND2 ASN D 27 28.018 42.778 3.760 1.00 40.14 N ANISOU 4650 ND2 ASN D 27 4936 5687 4628 -184 1066 26 N ATOM 4651 N ASN D 28 24.732 41.620 -0.539 1.00 41.00 N ANISOU 4651 N ASN D 28 6216 5620 3741 -524 961 230 N ATOM 4652 CA ASN D 28 23.432 41.049 -0.869 1.00 40.60 C ANISOU 4652 CA ASN D 28 6362 5501 3563 -516 723 314 C ATOM 4653 C ASN D 28 22.713 40.436 0.334 1.00 38.33 C ANISOU 4653 C ASN D 28 5871 5223 3470 -344 515 336 C ATOM 4654 O ASN D 28 21.934 39.500 0.180 1.00 38.27 O ANISOU 4654 O ASN D 28 5959 5174 3408 -309 382 343 O ATOM 4655 CB ASN D 28 23.531 40.048 -2.027 1.00 42.58 C ANISOU 4655 CB ASN D 28 6880 5710 3590 -583 839 224 C ATOM 4656 CG ASN D 28 22.187 39.769 -2.674 1.00 43.01 C ANISOU 4656 CG ASN D 28 7213 5665 3463 -646 569 342 C ATOM 4657 OD1 ASN D 28 21.240 40.555 -2.551 1.00 43.12 O ANISOU 4657 OD1 ASN D 28 7257 5631 3494 -679 324 500 O ATOM 4658 ND2 ASN D 28 22.096 38.649 -3.372 1.00 44.30 N ANISOU 4658 ND2 ASN D 28 7577 5783 3471 -660 603 260 N ATOM 4659 N HIS D 29 22.970 40.968 1.529 1.00 36.83 N ANISOU 4659 N HIS D 29 5425 5078 3492 -254 489 348 N ATOM 4660 CA HIS D 29 22.213 40.564 2.706 1.00 35.02 C ANISOU 4660 CA HIS D 29 5047 4844 3416 -124 306 383 C ATOM 4661 C HIS D 29 20.780 41.081 2.665 1.00 34.63 C ANISOU 4661 C HIS D 29 5079 4733 3345 -158 81 533 C ATOM 4662 O HIS D 29 20.527 42.255 2.357 1.00 35.33 O ANISOU 4662 O HIS D 29 5224 4790 3408 -236 33 627 O ATOM 4663 CB HIS D 29 22.895 41.020 3.985 1.00 33.84 C ANISOU 4663 CB HIS D 29 4651 4737 3469 -37 338 351 C ATOM 4664 CG HIS D 29 24.202 40.339 4.243 1.00 35.29 C ANISOU 4664 CG HIS D 29 4696 4960 3752 29 492 201 C ATOM 4665 ND1 HIS D 29 25.030 40.692 5.288 1.00 34.88 N ANISOU 4665 ND1 HIS D 29 4433 4931 3887 94 508 159 N ATOM 4666 CD2 HIS D 29 24.839 39.347 3.575 1.00 36.35 C ANISOU 4666 CD2 HIS D 29 4869 5097 3845 44 629 77 C ATOM 4667 CE1 HIS D 29 26.114 39.938 5.258 1.00 36.33 C ANISOU 4667 CE1 HIS D 29 4506 5129 4169 152 627 19 C ATOM 4668 NE2 HIS D 29 26.022 39.113 4.230 1.00 36.93 N ANISOU 4668 NE2 HIS D 29 4723 5195 4115 130 719 -39 N ATOM 4669 N ASN D 30 19.837 40.196 2.959 1.00 33.73 N ANISOU 4669 N ASN D 30 4965 4589 3263 -100 -61 552 N ATOM 4670 CA ASN D 30 18.440 40.594 3.024 1.00 33.30 C ANISOU 4670 CA ASN D 30 4925 4470 3257 -117 -274 678 C ATOM 4671 C ASN D 30 18.138 41.522 4.208 1.00 32.01 C ANISOU 4671 C ASN D 30 4565 4313 3283 -52 -306 724 C ATOM 4672 O ASN D 30 17.293 42.397 4.112 1.00 32.18 O ANISOU 4672 O ASN D 30 4587 4276 3364 -79 -432 822 O ATOM 4673 CB ASN D 30 17.533 39.351 3.062 1.00 32.99 C ANISOU 4673 CB ASN D 30 4914 4395 3225 -88 -401 678 C ATOM 4674 CG ASN D 30 17.258 38.770 1.683 1.00 33.89 C ANISOU 4674 CG ASN D 30 5286 4450 3142 -187 -472 689 C ATOM 4675 OD1 ASN D 30 17.867 39.145 0.676 1.00 33.94 O ANISOU 4675 OD1 ASN D 30 5476 4446 2974 -280 -388 676 O ATOM 4676 ND2 ASN D 30 16.327 37.845 1.636 1.00 34.35 N ANISOU 4676 ND2 ASN D 30 5379 4458 3216 -184 -625 712 N ATOM 4677 N ASN D 31 18.863 41.340 5.306 1.00 31.16 N ANISOU 4677 N ASN D 31 4309 4260 3271 31 -200 647 N ATOM 4678 CA ASN D 31 18.448 41.860 6.600 1.00 30.54 C ANISOU 4678 CA ASN D 31 4081 4174 3350 98 -230 671 C ATOM 4679 C ASN D 31 19.384 42.938 7.146 1.00 30.57 C ANISOU 4679 C ASN D 31 4009 4202 3405 104 -140 652 C ATOM 4680 O ASN D 31 20.597 42.753 7.147 1.00 31.15 O ANISOU 4680 O ASN D 31 4056 4321 3457 107 -32 574 O ATOM 4681 CB ASN D 31 18.346 40.701 7.595 1.00 29.84 C ANISOU 4681 CB ASN D 31 3928 4095 3315 175 -228 611 C ATOM 4682 CG ASN D 31 17.710 39.444 6.987 1.00 30.77 C ANISOU 4682 CG ASN D 31 4136 4190 3365 159 -301 608 C ATOM 4683 OD1 ASN D 31 16.562 39.471 6.530 1.00 33.57 O ANISOU 4683 OD1 ASN D 31 4522 4498 3734 116 -417 685 O ATOM 4684 ND2 ASN D 31 18.453 38.336 6.988 1.00 29.58 N ANISOU 4684 ND2 ASN D 31 4020 4058 3160 195 -251 518 N ATOM 4685 N MET D 32 18.831 44.056 7.613 1.00 30.28 N ANISOU 4685 N MET D 32 3927 4123 3456 107 -189 716 N ATOM 4686 CA MET D 32 19.656 45.135 8.161 1.00 30.59 C ANISOU 4686 CA MET D 32 3913 4167 3542 104 -125 704 C ATOM 4687 C MET D 32 19.065 45.714 9.455 1.00 30.34 C ANISOU 4687 C MET D 32 3802 4090 3637 168 -151 715 C ATOM 4688 O MET D 32 17.861 45.577 9.706 1.00 30.41 O ANISOU 4688 O MET D 32 3787 4053 3713 200 -209 749 O ATOM 4689 CB MET D 32 19.899 46.229 7.122 1.00 31.52 C ANISOU 4689 CB MET D 32 4122 4261 3593 5 -127 768 C ATOM 4690 CG MET D 32 20.562 45.733 5.847 1.00 32.87 C ANISOU 4690 CG MET D 32 4412 4469 3609 -83 -52 745 C ATOM 4691 SD MET D 32 20.885 47.011 4.605 1.00 34.88 S ANISOU 4691 SD MET D 32 4839 4678 3737 -241 -37 826 S ATOM 4692 CE MET D 32 22.319 47.836 5.310 1.00 33.32 C ANISOU 4692 CE MET D 32 4509 4528 3624 -261 114 766 C ATOM 4693 N TYR D 33 19.911 46.333 10.284 1.00 30.10 N ANISOU 4693 N TYR D 33 3731 4061 3644 181 -101 677 N ATOM 4694 CA TYR D 33 19.513 46.684 11.646 1.00 30.05 C ANISOU 4694 CA TYR D 33 3693 4005 3719 237 -101 660 C ATOM 4695 C TYR D 33 20.197 47.956 12.108 1.00 30.35 C ANISOU 4695 C TYR D 33 3732 4008 3792 216 -88 659 C ATOM 4696 O TYR D 33 21.414 48.105 11.919 1.00 31.16 O ANISOU 4696 O TYR D 33 3819 4148 3872 175 -64 632 O ATOM 4697 CB TYR D 33 19.869 45.558 12.629 1.00 29.92 C ANISOU 4697 CB TYR D 33 3674 4007 3688 283 -84 588 C ATOM 4698 CG TYR D 33 19.585 44.149 12.138 1.00 31.21 C ANISOU 4698 CG TYR D 33 3850 4207 3802 294 -99 573 C ATOM 4699 CD1 TYR D 33 20.465 43.504 11.268 1.00 31.72 C ANISOU 4699 CD1 TYR D 33 3915 4326 3811 279 -86 537 C ATOM 4700 CD2 TYR D 33 18.441 43.461 12.543 1.00 31.39 C ANISOU 4700 CD2 TYR D 33 3884 4202 3842 313 -112 585 C ATOM 4701 CE1 TYR D 33 20.202 42.227 10.801 1.00 31.91 C ANISOU 4701 CE1 TYR D 33 3972 4367 3784 292 -104 516 C ATOM 4702 CE2 TYR D 33 18.176 42.171 12.081 1.00 31.49 C ANISOU 4702 CE2 TYR D 33 3923 4236 3807 312 -142 575 C ATOM 4703 CZ TYR D 33 19.062 41.560 11.209 1.00 31.40 C ANISOU 4703 CZ TYR D 33 3933 4270 3727 307 -147 541 C ATOM 4704 OH TYR D 33 18.830 40.273 10.749 1.00 31.19 O ANISOU 4704 OH TYR D 33 3954 4250 3648 310 -179 521 O ATOM 4705 N TRP D 34 19.426 48.850 12.736 1.00 29.96 N ANISOU 4705 N TRP D 34 3691 3879 3814 244 -96 680 N ATOM 4706 CA TRP D 34 19.959 50.107 13.265 1.00 29.89 C ANISOU 4706 CA TRP D 34 3707 3812 3836 227 -96 678 C ATOM 4707 C TRP D 34 19.974 50.113 14.776 1.00 29.71 C ANISOU 4707 C TRP D 34 3723 3739 3828 269 -65 615 C ATOM 4708 O TRP D 34 18.932 49.963 15.424 1.00 29.80 O ANISOU 4708 O TRP D 34 3747 3700 3876 317 -20 597 O ATOM 4709 CB TRP D 34 19.154 51.313 12.776 1.00 30.58 C ANISOU 4709 CB TRP D 34 3811 3815 3993 223 -139 744 C ATOM 4710 CG TRP D 34 19.628 51.899 11.477 1.00 30.79 C ANISOU 4710 CG TRP D 34 3878 3850 3969 136 -187 814 C ATOM 4711 CD1 TRP D 34 18.965 51.885 10.286 1.00 30.44 C ANISOU 4711 CD1 TRP D 34 3870 3790 3906 105 -259 888 C ATOM 4712 CD2 TRP D 34 20.860 52.597 11.241 1.00 31.35 C ANISOU 4712 CD2 TRP D 34 3982 3935 3994 46 -168 819 C ATOM 4713 NE1 TRP D 34 19.706 52.521 9.319 1.00 31.62 N ANISOU 4713 NE1 TRP D 34 4107 3938 3969 -5 -274 940 N ATOM 4714 CE2 TRP D 34 20.874 52.972 9.880 1.00 32.31 C ANISOU 4714 CE2 TRP D 34 4177 4050 4048 -45 -201 896 C ATOM 4715 CE3 TRP D 34 21.954 52.947 12.047 1.00 31.16 C ANISOU 4715 CE3 TRP D 34 3939 3916 3983 22 -136 768 C ATOM 4716 CZ2 TRP D 34 21.944 53.678 9.306 1.00 32.82 C ANISOU 4716 CZ2 TRP D 34 4294 4123 4054 -170 -164 920 C ATOM 4717 CZ3 TRP D 34 23.017 53.649 11.472 1.00 30.52 C ANISOU 4717 CZ3 TRP D 34 3873 3846 3879 -91 -119 791 C ATOM 4718 CH2 TRP D 34 23.003 54.000 10.119 1.00 31.59 C ANISOU 4718 CH2 TRP D 34 4076 3983 3942 -190 -113 864 C ATOM 4719 N TYR D 35 21.168 50.320 15.324 1.00 29.75 N ANISOU 4719 N TYR D 35 3753 3743 3808 239 -88 579 N ATOM 4720 CA TYR D 35 21.399 50.369 16.769 1.00 29.74 C ANISOU 4720 CA TYR D 35 3843 3672 3786 255 -96 521 C ATOM 4721 C TYR D 35 21.909 51.740 17.239 1.00 30.35 C ANISOU 4721 C TYR D 35 3981 3665 3886 220 -128 520 C ATOM 4722 O TYR D 35 22.465 52.505 16.437 1.00 30.56 O ANISOU 4722 O TYR D 35 3958 3708 3947 167 -155 561 O ATOM 4723 CB TYR D 35 22.447 49.331 17.155 1.00 29.46 C ANISOU 4723 CB TYR D 35 3802 3676 3715 248 -160 477 C ATOM 4724 CG TYR D 35 22.057 47.894 16.942 1.00 29.07 C ANISOU 4724 CG TYR D 35 3732 3682 3630 284 -146 464 C ATOM 4725 CD1 TYR D 35 22.420 47.217 15.779 1.00 28.65 C ANISOU 4725 CD1 TYR D 35 3576 3720 3589 281 -144 473 C ATOM 4726 CD2 TYR D 35 21.351 47.192 17.920 1.00 29.41 C ANISOU 4726 CD2 TYR D 35 3883 3676 3616 308 -126 438 C ATOM 4727 CE1 TYR D 35 22.077 45.871 15.588 1.00 28.02 C ANISOU 4727 CE1 TYR D 35 3495 3678 3475 314 -144 457 C ATOM 4728 CE2 TYR D 35 21.006 45.856 17.734 1.00 29.21 C ANISOU 4728 CE2 TYR D 35 3852 3691 3557 328 -126 432 C ATOM 4729 CZ TYR D 35 21.375 45.202 16.567 1.00 28.16 C ANISOU 4729 CZ TYR D 35 3610 3644 3446 337 -147 441 C ATOM 4730 OH TYR D 35 21.042 43.880 16.393 1.00 29.39 O ANISOU 4730 OH TYR D 35 3778 3823 3565 358 -158 431 O ATOM 4731 N ARG D 36 21.733 52.031 18.535 1.00 30.59 N ANISOU 4731 N ARG D 36 4145 3596 3882 233 -120 472 N ATOM 4732 CA ARG D 36 22.438 53.146 19.188 1.00 31.16 C ANISOU 4732 CA ARG D 36 4312 3574 3953 189 -182 456 C ATOM 4733 C ARG D 36 23.181 52.711 20.446 1.00 31.72 C ANISOU 4733 C ARG D 36 4521 3585 3948 164 -269 401 C ATOM 4734 O ARG D 36 22.744 51.789 21.146 1.00 32.01 O ANISOU 4734 O ARG D 36 4652 3606 3906 189 -240 366 O ATOM 4735 CB ARG D 36 21.519 54.343 19.477 1.00 31.78 C ANISOU 4735 CB ARG D 36 4472 3540 4064 218 -111 451 C ATOM 4736 CG ARG D 36 20.498 54.173 20.585 1.00 31.93 C ANISOU 4736 CG ARG D 36 4622 3471 4040 267 7 383 C ATOM 4737 CD ARG D 36 19.728 55.484 20.830 1.00 34.25 C ANISOU 4737 CD ARG D 36 4974 3635 4405 306 84 359 C ATOM 4738 NE ARG D 36 20.446 56.408 21.720 1.00 35.42 N ANISOU 4738 NE ARG D 36 5307 3662 4488 259 27 319 N ATOM 4739 CZ ARG D 36 20.033 57.630 22.059 1.00 35.08 C ANISOU 4739 CZ ARG D 36 5357 3480 4490 285 72 284 C ATOM 4740 NH1 ARG D 36 18.896 58.123 21.589 1.00 35.29 N ANISOU 4740 NH1 ARG D 36 5287 3465 4656 369 170 282 N ATOM 4741 NH2 ARG D 36 20.770 58.369 22.871 1.00 34.94 N ANISOU 4741 NH2 ARG D 36 5531 3350 4393 228 -1 249 N ATOM 4742 N GLN D 37 24.306 53.377 20.716 1.00 32.22 N ANISOU 4742 N GLN D 37 4608 3600 4035 102 -393 398 N ATOM 4743 CA GLN D 37 25.156 53.085 21.866 1.00 32.60 C ANISOU 4743 CA GLN D 37 4793 3563 4030 65 -543 356 C ATOM 4744 C GLN D 37 25.353 54.322 22.768 1.00 34.01 C ANISOU 4744 C GLN D 37 5167 3589 4166 13 -603 334 C ATOM 4745 O GLN D 37 25.907 55.337 22.343 1.00 34.07 O ANISOU 4745 O GLN D 37 5109 3581 4254 -36 -650 362 O ATOM 4746 CB GLN D 37 26.495 52.546 21.382 1.00 32.45 C ANISOU 4746 CB GLN D 37 4593 3615 4121 33 -682 363 C ATOM 4747 CG GLN D 37 27.385 51.998 22.485 1.00 33.27 C ANISOU 4747 CG GLN D 37 4808 3624 4210 9 -893 324 C ATOM 4748 CD GLN D 37 28.787 51.684 22.001 1.00 32.71 C ANISOU 4748 CD GLN D 37 4505 3602 4323 -17 -1038 318 C ATOM 4749 OE1 GLN D 37 29.411 52.484 21.311 1.00 32.37 O ANISOU 4749 OE1 GLN D 37 4300 3598 4402 -73 -1021 337 O ATOM 4750 NE2 GLN D 37 29.289 50.514 22.370 1.00 33.40 N ANISOU 4750 NE2 GLN D 37 4572 3673 4444 19 -1177 287 N ATOM 4751 N ASP D 38 24.880 54.223 24.010 1.00 35.13 N ANISOU 4751 N ASP D 38 5574 3609 4166 13 -590 283 N ATOM 4752 CA ASP D 38 25.024 55.285 25.007 1.00 36.93 C ANISOU 4752 CA ASP D 38 6052 3667 4314 -39 -643 245 C ATOM 4753 C ASP D 38 25.686 54.737 26.253 1.00 38.07 C ANISOU 4753 C ASP D 38 6445 3692 4326 -100 -828 211 C ATOM 4754 O ASP D 38 25.416 53.604 26.655 1.00 37.77 O ANISOU 4754 O ASP D 38 6490 3666 4196 -85 -820 197 O ATOM 4755 CB ASP D 38 23.666 55.863 25.384 1.00 37.50 C ANISOU 4755 CB ASP D 38 6270 3662 4317 9 -413 198 C ATOM 4756 CG ASP D 38 22.946 56.447 24.207 1.00 37.89 C ANISOU 4756 CG ASP D 38 6093 3790 4512 74 -279 236 C ATOM 4757 OD1 ASP D 38 23.296 57.581 23.790 1.00 39.30 O ANISOU 4757 OD1 ASP D 38 6235 3928 4769 51 -335 264 O ATOM 4758 OD2 ASP D 38 22.026 55.766 23.704 1.00 38.45 O ANISOU 4758 OD2 ASP D 38 6040 3951 4620 140 -138 244 O ATOM 4759 N THR D 39 26.538 55.544 26.877 1.00 39.44 N ANISOU 4759 N THR D 39 6764 3735 4485 -179 -1016 201 N ATOM 4760 CA THR D 39 27.342 55.038 27.982 1.00 41.13 C ANISOU 4760 CA THR D 39 7213 3818 4597 -250 -1272 183 C ATOM 4761 C THR D 39 26.450 54.457 29.075 1.00 41.66 C ANISOU 4761 C THR D 39 7640 3779 4411 -258 -1164 131 C ATOM 4762 O THR D 39 25.421 55.040 29.429 1.00 41.82 O ANISOU 4762 O THR D 39 7834 3738 4316 -245 -922 81 O ATOM 4763 CB THR D 39 28.311 56.099 28.555 1.00 42.96 C ANISOU 4763 CB THR D 39 7582 3895 4844 -349 -1508 179 C ATOM 4764 OG1 THR D 39 27.564 57.142 29.181 1.00 43.74 O ANISOU 4764 OG1 THR D 39 7970 3860 4791 -368 -1365 130 O ATOM 4765 CG2 THR D 39 29.194 56.689 27.442 1.00 42.95 C ANISOU 4765 CG2 THR D 39 7216 4001 5102 -368 -1582 231 C ATOM 4766 N GLY D 40 26.832 53.279 29.562 1.00 41.94 N ANISOU 4766 N GLY D 40 7775 3786 4374 -278 -1329 139 N ATOM 4767 CA GLY D 40 26.089 52.609 30.622 1.00 42.72 C ANISOU 4767 CA GLY D 40 8252 3772 4208 -318 -1243 99 C ATOM 4768 C GLY D 40 24.882 51.813 30.157 1.00 41.51 C ANISOU 4768 C GLY D 40 7988 3749 4036 -249 -938 93 C ATOM 4769 O GLY D 40 24.130 51.305 30.987 1.00 42.46 O ANISOU 4769 O GLY D 40 8408 3783 3941 -296 -801 56 O ATOM 4770 N HIS D 41 24.686 51.728 28.837 1.00 39.55 N ANISOU 4770 N HIS D 41 7328 3695 4004 -156 -829 130 N ATOM 4771 CA HIS D 41 23.715 50.822 28.221 1.00 38.24 C ANISOU 4771 CA HIS D 41 7002 3663 3864 -92 -615 140 C ATOM 4772 C HIS D 41 24.441 50.070 27.143 1.00 36.49 C ANISOU 4772 C HIS D 41 6448 3591 3827 -36 -759 194 C ATOM 4773 O HIS D 41 25.320 50.620 26.496 1.00 36.23 O ANISOU 4773 O HIS D 41 6205 3607 3955 -25 -883 218 O ATOM 4774 CB HIS D 41 22.589 51.578 27.526 1.00 37.91 C ANISOU 4774 CB HIS D 41 6786 3699 3918 -27 -321 126 C ATOM 4775 CG HIS D 41 21.715 52.368 28.446 1.00 41.56 C ANISOU 4775 CG HIS D 41 7517 4022 4252 -57 -109 50 C ATOM 4776 ND1 HIS D 41 21.958 53.694 28.748 1.00 44.57 N ANISOU 4776 ND1 HIS D 41 8003 4296 4636 -72 -127 17 N ATOM 4777 CD2 HIS D 41 20.584 52.029 29.108 1.00 43.67 C ANISOU 4777 CD2 HIS D 41 7963 4234 4397 -76 150 -10 C ATOM 4778 CE1 HIS D 41 21.020 54.135 29.568 1.00 46.95 C ANISOU 4778 CE1 HIS D 41 8543 4476 4818 -87 115 -68 C ATOM 4779 NE2 HIS D 41 20.174 53.144 29.801 1.00 47.32 N ANISOU 4779 NE2 HIS D 41 8630 4555 4793 -94 300 -90 N ATOM 4780 N GLY D 42 24.062 48.818 26.924 1.00 35.59 N ANISOU 4780 N GLY D 42 6289 3543 3691 -8 -722 206 N ATOM 4781 CA GLY D 42 24.556 48.075 25.768 1.00 34.09 C ANISOU 4781 CA GLY D 42 5776 3500 3675 58 -794 241 C ATOM 4782 C GLY D 42 23.853 48.599 24.537 1.00 32.28 C ANISOU 4782 C GLY D 42 5279 3416 3569 114 -580 262 C ATOM 4783 O GLY D 42 22.980 49.466 24.650 1.00 32.60 O ANISOU 4783 O GLY D 42 5372 3431 3582 112 -403 250 O ATOM 4784 N LEU D 43 24.230 48.095 23.365 1.00 30.79 N ANISOU 4784 N LEU D 43 4818 3361 3519 162 -603 289 N ATOM 4785 CA LEU D 43 23.549 48.474 22.127 1.00 29.25 C ANISOU 4785 CA LEU D 43 4410 3289 3415 201 -434 320 C ATOM 4786 C LEU D 43 22.044 48.229 22.187 1.00 28.83 C ANISOU 4786 C LEU D 43 4409 3242 3303 221 -237 320 C ATOM 4787 O LEU D 43 21.596 47.230 22.723 1.00 28.66 O ANISOU 4787 O LEU D 43 4502 3196 3191 213 -214 305 O ATOM 4788 CB LEU D 43 24.157 47.761 20.919 1.00 28.48 C ANISOU 4788 CB LEU D 43 4074 3317 3429 233 -475 338 C ATOM 4789 CG LEU D 43 25.135 48.561 20.054 1.00 28.09 C ANISOU 4789 CG LEU D 43 3839 3323 3510 211 -512 351 C ATOM 4790 CD1 LEU D 43 26.433 48.831 20.798 1.00 29.37 C ANISOU 4790 CD1 LEU D 43 4027 3404 3730 172 -702 323 C ATOM 4791 CD2 LEU D 43 25.404 47.832 18.753 1.00 26.26 C ANISOU 4791 CD2 LEU D 43 3406 3218 3355 237 -465 357 C ATOM 4792 N ARG D 44 21.270 49.165 21.650 1.00 28.95 N ANISOU 4792 N ARG D 44 4337 3275 3387 242 -106 336 N ATOM 4793 CA ARG D 44 19.810 49.048 21.636 1.00 29.27 C ANISOU 4793 CA ARG D 44 4367 3313 3440 268 76 330 C ATOM 4794 C ARG D 44 19.257 49.148 20.215 1.00 28.64 C ANISOU 4794 C ARG D 44 4058 3331 3492 310 108 384 C ATOM 4795 O ARG D 44 19.570 50.090 19.471 1.00 28.90 O ANISOU 4795 O ARG D 44 4001 3380 3600 314 67 418 O ATOM 4796 CB ARG D 44 19.163 50.083 22.565 1.00 30.06 C ANISOU 4796 CB ARG D 44 4615 3289 3519 261 206 279 C ATOM 4797 CG ARG D 44 19.292 49.717 24.042 1.00 32.42 C ANISOU 4797 CG ARG D 44 5208 3472 3637 201 225 220 C ATOM 4798 CD ARG D 44 18.698 50.764 24.967 1.00 35.44 C ANISOU 4798 CD ARG D 44 5768 3718 3978 187 384 151 C ATOM 4799 NE ARG D 44 19.315 52.070 24.757 1.00 37.13 N ANISOU 4799 NE ARG D 44 5962 3890 4255 201 292 157 N ATOM 4800 CZ ARG D 44 19.020 53.172 25.438 1.00 37.51 C ANISOU 4800 CZ ARG D 44 6163 3807 4283 199 389 96 C ATOM 4801 NH1 ARG D 44 18.111 53.136 26.397 1.00 38.92 N ANISOU 4801 NH1 ARG D 44 6524 3885 4377 184 610 12 N ATOM 4802 NH2 ARG D 44 19.643 54.312 25.152 1.00 37.37 N ANISOU 4802 NH2 ARG D 44 6122 3750 4327 203 277 114 N ATOM 4803 N LEU D 45 18.454 48.159 19.836 1.00 28.06 N ANISOU 4803 N LEU D 45 3915 3312 3434 325 164 396 N ATOM 4804 CA LEU D 45 17.862 48.119 18.506 1.00 27.41 C ANISOU 4804 CA LEU D 45 3653 3304 3459 352 162 451 C ATOM 4805 C LEU D 45 16.760 49.196 18.331 1.00 28.37 C ANISOU 4805 C LEU D 45 3701 3362 3716 387 245 460 C ATOM 4806 O LEU D 45 15.908 49.359 19.207 1.00 29.33 O ANISOU 4806 O LEU D 45 3865 3407 3872 400 381 408 O ATOM 4807 CB LEU D 45 17.309 46.718 18.262 1.00 26.73 C ANISOU 4807 CB LEU D 45 3534 3271 3352 348 176 459 C ATOM 4808 CG LEU D 45 16.806 46.378 16.868 1.00 25.42 C ANISOU 4808 CG LEU D 45 3222 3175 3260 360 131 517 C ATOM 4809 CD1 LEU D 45 17.967 46.183 15.911 1.00 24.20 C ANISOU 4809 CD1 LEU D 45 3043 3098 3055 348 26 539 C ATOM 4810 CD2 LEU D 45 15.933 45.157 16.943 1.00 22.85 C ANISOU 4810 CD2 LEU D 45 2884 2864 2935 348 170 514 C ATOM 4811 N ILE D 46 16.780 49.931 17.215 1.00 28.22 N ANISOU 4811 N ILE D 46 3583 3360 3781 399 167 519 N ATOM 4812 CA ILE D 46 15.763 50.962 16.975 1.00 29.07 C ANISOU 4812 CA ILE D 46 3614 3383 4049 445 197 532 C ATOM 4813 C ILE D 46 14.758 50.506 15.934 1.00 29.35 C ANISOU 4813 C ILE D 46 3506 3443 4202 464 147 587 C ATOM 4814 O ILE D 46 13.554 50.471 16.191 1.00 30.92 O ANISOU 4814 O ILE D 46 3609 3585 4553 506 223 563 O ATOM 4815 CB ILE D 46 16.352 52.293 16.472 1.00 29.25 C ANISOU 4815 CB ILE D 46 3660 3359 4096 437 106 572 C ATOM 4816 CG1 ILE D 46 17.398 52.856 17.434 1.00 29.23 C ANISOU 4816 CG1 ILE D 46 3795 3317 3993 406 119 524 C ATOM 4817 CG2 ILE D 46 15.235 53.295 16.272 1.00 30.52 C ANISOU 4817 CG2 ILE D 46 3746 3405 4447 502 112 581 C ATOM 4818 CD1 ILE D 46 18.237 53.994 16.858 1.00 27.62 C ANISOU 4818 CD1 ILE D 46 3618 3087 3790 365 17 572 C ATOM 4819 N HIS D 47 15.263 50.208 14.742 1.00 28.36 N ANISOU 4819 N HIS D 47 3368 3390 4016 426 21 657 N ATOM 4820 CA HIS D 47 14.457 49.732 13.635 1.00 28.04 C ANISOU 4820 CA HIS D 47 3242 3365 4048 423 -72 720 C ATOM 4821 C HIS D 47 15.259 48.649 12.938 1.00 27.02 C ANISOU 4821 C HIS D 47 3165 3346 3756 368 -119 739 C ATOM 4822 O HIS D 47 16.463 48.523 13.166 1.00 26.69 O ANISOU 4822 O HIS D 47 3193 3358 3590 340 -93 710 O ATOM 4823 CB HIS D 47 14.188 50.862 12.637 1.00 28.79 C ANISOU 4823 CB HIS D 47 3323 3384 4232 425 -208 797 C ATOM 4824 CG HIS D 47 13.198 51.886 13.104 1.00 29.71 C ANISOU 4824 CG HIS D 47 3354 3366 4567 501 -193 778 C ATOM 4825 ND1 HIS D 47 11.902 51.573 13.447 1.00 30.39 N ANISOU 4825 ND1 HIS D 47 3291 3399 4857 560 -142 745 N ATOM 4826 CD2 HIS D 47 13.305 53.231 13.234 1.00 30.27 C ANISOU 4826 CD2 HIS D 47 3460 3334 4709 530 -221 782 C ATOM 4827 CE1 HIS D 47 11.260 52.677 13.787 1.00 31.11 C ANISOU 4827 CE1 HIS D 47 3313 3359 5150 634 -127 718 C ATOM 4828 NE2 HIS D 47 12.088 53.696 13.668 1.00 30.30 N ANISOU 4828 NE2 HIS D 47 3333 3219 4961 621 -183 741 N ATOM 4829 N TYR D 48 14.601 47.875 12.084 1.00 26.82 N ANISOU 4829 N TYR D 48 3101 3340 3748 352 -195 781 N ATOM 4830 CA TYR D 48 15.293 46.890 11.267 1.00 26.10 C ANISOU 4830 CA TYR D 48 3077 3335 3504 302 -237 792 C ATOM 4831 C TYR D 48 14.521 46.581 9.995 1.00 27.07 C ANISOU 4831 C TYR D 48 3203 3437 3645 267 -375 865 C ATOM 4832 O TYR D 48 13.426 47.093 9.799 1.00 27.62 O ANISOU 4832 O TYR D 48 3198 3422 3875 288 -461 911 O ATOM 4833 CB TYR D 48 15.604 45.626 12.071 1.00 25.20 C ANISOU 4833 CB TYR D 48 2978 3278 3320 313 -157 725 C ATOM 4834 CG TYR D 48 14.418 44.847 12.614 1.00 24.39 C ANISOU 4834 CG TYR D 48 2814 3147 3305 327 -126 713 C ATOM 4835 CD1 TYR D 48 13.731 45.275 13.750 1.00 23.13 C ANISOU 4835 CD1 TYR D 48 2604 2927 3256 356 -17 676 C ATOM 4836 CD2 TYR D 48 14.020 43.653 12.013 1.00 23.76 C ANISOU 4836 CD2 TYR D 48 2738 3096 3193 298 -186 730 C ATOM 4837 CE1 TYR D 48 12.668 44.551 14.266 1.00 23.19 C ANISOU 4837 CE1 TYR D 48 2550 2910 3351 346 51 658 C ATOM 4838 CE2 TYR D 48 12.957 42.915 12.518 1.00 24.57 C ANISOU 4838 CE2 TYR D 48 2780 3171 3386 290 -151 721 C ATOM 4839 CZ TYR D 48 12.282 43.366 13.652 1.00 24.60 C ANISOU 4839 CZ TYR D 48 2716 3121 3510 309 -20 685 C ATOM 4840 OH TYR D 48 11.232 42.616 14.159 1.00 24.46 O ANISOU 4840 OH TYR D 48 2630 3075 3587 279 51 670 O ATOM 4841 N SER D 49 15.098 45.755 9.128 1.00 27.43 N ANISOU 4841 N SER D 49 3342 3544 3538 215 -405 870 N ATOM 4842 CA SER D 49 14.489 45.472 7.833 1.00 29.31 C ANISOU 4842 CA SER D 49 3646 3747 3743 160 -554 940 C ATOM 4843 C SER D 49 14.765 44.053 7.337 1.00 29.78 C ANISOU 4843 C SER D 49 3785 3866 3664 127 -550 908 C ATOM 4844 O SER D 49 15.828 43.477 7.585 1.00 29.27 O ANISOU 4844 O SER D 49 3755 3875 3490 134 -435 836 O ATOM 4845 CB SER D 49 14.954 46.493 6.786 1.00 30.03 C ANISOU 4845 CB SER D 49 3865 3800 3745 91 -627 1005 C ATOM 4846 OG SER D 49 14.393 46.212 5.515 1.00 31.04 O ANISOU 4846 OG SER D 49 4116 3874 3805 20 -795 1077 O ATOM 4847 N TYR D 50 13.797 43.500 6.620 1.00 31.21 N ANISOU 4847 N TYR D 50 3991 3998 3869 94 -694 959 N ATOM 4848 CA TYR D 50 13.958 42.187 6.032 1.00 31.72 C ANISOU 4848 CA TYR D 50 4162 4095 3795 56 -713 932 C ATOM 4849 C TYR D 50 14.036 42.256 4.506 1.00 33.48 C ANISOU 4849 C TYR D 50 4589 4276 3856 -39 -836 988 C ATOM 4850 O TYR D 50 13.994 41.231 3.819 1.00 34.44 O ANISOU 4850 O TYR D 50 4837 4395 3855 -84 -884 973 O ATOM 4851 CB TYR D 50 12.808 41.284 6.459 1.00 31.96 C ANISOU 4851 CB TYR D 50 4093 4095 3956 70 -781 939 C ATOM 4852 CG TYR D 50 12.875 40.791 7.879 1.00 29.95 C ANISOU 4852 CG TYR D 50 3725 3882 3773 129 -632 869 C ATOM 4853 CD1 TYR D 50 14.064 40.303 8.417 1.00 29.97 C ANISOU 4853 CD1 TYR D 50 3783 3953 3652 160 -502 789 C ATOM 4854 CD2 TYR D 50 11.744 40.778 8.671 1.00 29.34 C ANISOU 4854 CD2 TYR D 50 3493 3761 3892 145 -625 880 C ATOM 4855 CE1 TYR D 50 14.121 39.825 9.725 1.00 29.37 C ANISOU 4855 CE1 TYR D 50 3656 3889 3616 198 -403 736 C ATOM 4856 CE2 TYR D 50 11.782 40.304 9.966 1.00 30.05 C ANISOU 4856 CE2 TYR D 50 3534 3874 4008 171 -476 819 C ATOM 4857 CZ TYR D 50 12.969 39.824 10.490 1.00 29.51 C ANISOU 4857 CZ TYR D 50 3568 3862 3783 194 -382 754 C ATOM 4858 OH TYR D 50 12.995 39.360 11.778 1.00 28.83 O ANISOU 4858 OH TYR D 50 3482 3773 3700 205 -270 705 O ATOM 4859 N GLY D 51 14.157 43.462 3.968 1.00 34.39 N ANISOU 4859 N GLY D 51 4772 4342 3952 -81 -891 1050 N ATOM 4860 CA GLY D 51 14.312 43.606 2.530 1.00 35.96 C ANISOU 4860 CA GLY D 51 5225 4486 3954 -199 -996 1107 C ATOM 4861 C GLY D 51 13.827 44.941 2.039 1.00 37.25 C ANISOU 4861 C GLY D 51 5446 4537 4172 -242 -1167 1216 C ATOM 4862 O GLY D 51 13.251 45.724 2.807 1.00 37.13 O ANISOU 4862 O GLY D 51 5243 4480 4383 -164 -1213 1242 O ATOM 4863 N ALA D 52 14.069 45.205 0.756 1.00 38.78 N ANISOU 4863 N ALA D 52 5922 4665 4148 -373 -1258 1275 N ATOM 4864 CA ALA D 52 13.564 46.412 0.127 1.00 40.38 C ANISOU 4864 CA ALA D 52 6244 4725 4375 -435 -1477 1397 C ATOM 4865 C ALA D 52 12.085 46.587 0.484 1.00 41.06 C ANISOU 4865 C ALA D 52 6135 4699 4768 -350 -1740 1464 C ATOM 4866 O ALA D 52 11.288 45.647 0.362 1.00 41.28 O ANISOU 4866 O ALA D 52 6115 4704 4864 -341 -1866 1467 O ATOM 4867 CB ALA D 52 13.764 46.356 -1.384 1.00 42.19 C ANISOU 4867 CB ALA D 52 6863 4868 4300 -611 -1591 1460 C ATOM 4868 N GLY D 53 11.737 47.775 0.976 1.00 41.57 N ANISOU 4868 N GLY D 53 6064 4691 5041 -285 -1806 1506 N ATOM 4869 CA GLY D 53 10.336 48.140 1.201 1.00 42.96 C ANISOU 4869 CA GLY D 53 6043 4729 5549 -204 -2060 1566 C ATOM 4870 C GLY D 53 9.816 47.818 2.586 1.00 42.01 C ANISOU 4870 C GLY D 53 5565 4678 5718 -59 -1903 1477 C ATOM 4871 O GLY D 53 8.811 48.385 3.007 1.00 43.03 O ANISOU 4871 O GLY D 53 5479 4702 6167 27 -2023 1496 O ATOM 4872 N SER D 54 10.488 46.897 3.280 1.00 40.23 N ANISOU 4872 N SER D 54 5289 4615 5383 -39 -1635 1375 N ATOM 4873 CA SER D 54 10.161 46.555 4.654 1.00 39.16 C ANISOU 4873 CA SER D 54 4882 4546 5451 69 -1449 1286 C ATOM 4874 C SER D 54 10.915 47.464 5.609 1.00 38.25 C ANISOU 4874 C SER D 54 4709 4476 5348 132 -1242 1229 C ATOM 4875 O SER D 54 12.129 47.632 5.466 1.00 37.69 O ANISOU 4875 O SER D 54 4786 4480 5054 86 -1123 1208 O ATOM 4876 CB SER D 54 10.544 45.095 4.948 1.00 38.15 C ANISOU 4876 CB SER D 54 4769 4542 5183 51 -1300 1213 C ATOM 4877 OG SER D 54 11.017 44.914 6.295 1.00 36.72 O ANISOU 4877 OG SER D 54 4461 4458 5034 123 -1044 1115 O ATOM 4878 N THR D 55 10.202 48.044 6.576 1.00 38.24 N ANISOU 4878 N THR D 55 4493 4421 5615 230 -1192 1197 N ATOM 4879 CA THR D 55 10.839 48.552 7.795 1.00 36.98 C ANISOU 4879 CA THR D 55 4274 4316 5460 292 -955 1113 C ATOM 4880 C THR D 55 10.082 48.031 8.988 1.00 36.30 C ANISOU 4880 C THR D 55 3986 4244 5564 361 -802 1032 C ATOM 4881 O THR D 55 8.881 47.830 8.905 1.00 37.43 O ANISOU 4881 O THR D 55 3969 4312 5940 385 -892 1048 O ATOM 4882 CB THR D 55 10.886 50.070 7.866 1.00 37.93 C ANISOU 4882 CB THR D 55 4398 4332 5680 331 -1003 1139 C ATOM 4883 OG1 THR D 55 9.611 50.601 7.485 1.00 41.66 O ANISOU 4883 OG1 THR D 55 4747 4649 6432 379 -1210 1194 O ATOM 4884 CG2 THR D 55 11.957 50.608 6.934 1.00 37.96 C ANISOU 4884 CG2 THR D 55 4637 4346 5441 235 -1069 1202 C ATOM 4885 N GLU D 56 10.800 47.801 10.085 1.00 34.92 N ANISOU 4885 N GLU D 56 3829 4152 5286 379 -577 947 N ATOM 4886 CA GLU D 56 10.247 47.190 11.290 1.00 34.66 C ANISOU 4886 CA GLU D 56 3678 4136 5356 412 -394 865 C ATOM 4887 C GLU D 56 10.676 47.916 12.552 1.00 34.31 C ANISOU 4887 C GLU D 56 3649 4080 5308 459 -198 785 C ATOM 4888 O GLU D 56 11.859 48.162 12.753 1.00 33.33 O ANISOU 4888 O GLU D 56 3663 4007 4995 442 -160 770 O ATOM 4889 CB GLU D 56 10.706 45.739 11.426 1.00 33.58 C ANISOU 4889 CB GLU D 56 3622 4104 5032 358 -335 840 C ATOM 4890 CG GLU D 56 10.077 44.744 10.484 1.00 34.40 C ANISOU 4890 CG GLU D 56 3709 4211 5152 307 -486 893 C ATOM 4891 CD GLU D 56 8.574 44.834 10.417 1.00 37.18 C ANISOU 4891 CD GLU D 56 3854 4467 5804 322 -559 916 C ATOM 4892 OE1 GLU D 56 7.925 45.262 11.403 1.00 37.43 O ANISOU 4892 OE1 GLU D 56 3732 4453 6037 369 -405 858 O ATOM 4893 OE2 GLU D 56 8.046 44.457 9.351 1.00 39.85 O ANISOU 4893 OE2 GLU D 56 4188 4768 6185 279 -774 988 O ATOM 4894 N LYS D 57 9.715 48.220 13.418 1.00 35.39 N ANISOU 4894 N LYS D 57 3645 4142 5659 509 -66 725 N ATOM 4895 CA LYS D 57 10.023 48.757 14.734 1.00 35.41 C ANISOU 4895 CA LYS D 57 3702 4120 5631 539 146 633 C ATOM 4896 C LYS D 57 10.883 47.784 15.540 1.00 34.26 C ANISOU 4896 C LYS D 57 3718 4065 5234 481 265 588 C ATOM 4897 O LYS D 57 10.654 46.567 15.516 1.00 34.12 O ANISOU 4897 O LYS D 57 3696 4102 5166 433 276 592 O ATOM 4898 CB LYS D 57 8.739 49.070 15.487 1.00 37.12 C ANISOU 4898 CB LYS D 57 3741 4237 6125 590 310 558 C ATOM 4899 CG LYS D 57 8.046 50.309 14.978 1.00 39.48 C ANISOU 4899 CG LYS D 57 3891 4408 6703 677 202 577 C ATOM 4900 CD LYS D 57 6.750 50.539 15.704 1.00 43.43 C ANISOU 4900 CD LYS D 57 4170 4805 7527 738 389 482 C ATOM 4901 CE LYS D 57 6.239 51.938 15.456 1.00 45.84 C ANISOU 4901 CE LYS D 57 4351 4955 8111 850 305 472 C ATOM 4902 NZ LYS D 57 4.899 52.109 16.083 1.00 50.13 N ANISOU 4902 NZ LYS D 57 4625 5388 9035 920 500 364 N ATOM 4903 N GLY D 58 11.878 48.336 16.234 1.00 33.57 N ANISOU 4903 N GLY D 58 3780 3977 4999 482 323 549 N ATOM 4904 CA GLY D 58 12.737 47.584 17.133 1.00 32.58 C ANISOU 4904 CA GLY D 58 3823 3899 4657 435 399 504 C ATOM 4905 C GLY D 58 12.286 47.731 18.573 1.00 33.75 C ANISOU 4905 C GLY D 58 4047 3970 4806 427 616 412 C ATOM 4906 O GLY D 58 11.115 47.531 18.877 1.00 34.98 O ANISOU 4906 O GLY D 58 4096 4083 5113 428 756 377 O ATOM 4907 N ASP D 59 13.218 48.085 19.456 1.00 33.53 N ANISOU 4907 N ASP D 59 4212 3915 4614 409 646 369 N ATOM 4908 CA ASP D 59 12.963 48.145 20.899 1.00 34.54 C ANISOU 4908 CA ASP D 59 4502 3955 4665 375 847 279 C ATOM 4909 C ASP D 59 12.725 49.556 21.398 1.00 35.45 C ANISOU 4909 C ASP D 59 4639 3962 4870 423 952 218 C ATOM 4910 O ASP D 59 11.972 49.766 22.345 1.00 36.81 O ANISOU 4910 O ASP D 59 4866 4043 5076 414 1181 129 O ATOM 4911 CB ASP D 59 14.117 47.513 21.678 1.00 33.99 C ANISOU 4911 CB ASP D 59 4684 3893 4337 310 782 268 C ATOM 4912 CG ASP D 59 14.011 45.999 21.750 1.00 34.75 C ANISOU 4912 CG ASP D 59 4826 4039 4339 251 770 286 C ATOM 4913 OD1 ASP D 59 12.876 45.482 21.841 1.00 35.67 O ANISOU 4913 OD1 ASP D 59 4864 4147 4541 224 918 271 O ATOM 4914 OD2 ASP D 59 15.064 45.320 21.722 1.00 35.81 O ANISOU 4914 OD2 ASP D 59 5066 4210 4332 231 608 313 O ATOM 4915 N ILE D 60 13.386 50.517 20.763 1.00 34.73 N ANISOU 4915 N ILE D 60 4518 3868 4809 466 797 261 N ATOM 4916 CA ILE D 60 13.197 51.925 21.075 1.00 35.71 C ANISOU 4916 CA ILE D 60 4660 3876 5033 520 856 213 C ATOM 4917 C ILE D 60 12.976 52.747 19.790 1.00 35.78 C ANISOU 4917 C ILE D 60 4478 3881 5236 587 698 289 C ATOM 4918 O ILE D 60 13.724 53.680 19.489 1.00 35.52 O ANISOU 4918 O ILE D 60 4505 3819 5173 592 576 321 O ATOM 4919 CB ILE D 60 14.353 52.484 21.948 1.00 35.61 C ANISOU 4919 CB ILE D 60 4904 3808 4818 477 822 179 C ATOM 4920 CG1 ILE D 60 15.720 52.050 21.408 1.00 33.64 C ANISOU 4920 CG1 ILE D 60 4693 3661 4429 428 597 257 C ATOM 4921 CG2 ILE D 60 14.180 52.061 23.400 1.00 36.41 C ANISOU 4921 CG2 ILE D 60 5238 3835 4760 417 1015 81 C ATOM 4922 CD1 ILE D 60 16.855 52.964 21.833 1.00 32.92 C ANISOU 4922 CD1 ILE D 60 4758 3508 4241 398 494 249 C ATOM 4923 N PRO D 61 11.926 52.405 19.027 1.00 36.47 N ANISOU 4923 N PRO D 61 4350 3983 5524 626 684 322 N ATOM 4924 CA PRO D 61 11.714 53.053 17.733 1.00 36.34 C ANISOU 4924 CA PRO D 61 4194 3948 5665 671 485 411 C ATOM 4925 C PRO D 61 11.354 54.524 17.831 1.00 37.54 C ANISOU 4925 C PRO D 61 4321 3948 5994 752 484 379 C ATOM 4926 O PRO D 61 11.605 55.261 16.883 1.00 37.58 O ANISOU 4926 O PRO D 61 4313 3921 6045 764 286 463 O ATOM 4927 CB PRO D 61 10.535 52.273 17.146 1.00 36.96 C ANISOU 4927 CB PRO D 61 4062 4046 5936 689 473 436 C ATOM 4928 CG PRO D 61 9.786 51.772 18.337 1.00 38.29 C ANISOU 4928 CG PRO D 61 4206 4185 6158 686 744 324 C ATOM 4929 CD PRO D 61 10.874 51.407 19.309 1.00 37.37 C ANISOU 4929 CD PRO D 61 4350 4116 5733 614 832 284 C ATOM 4930 N ASP D 62 10.777 54.938 18.963 1.00 38.98 N ANISOU 4930 N ASP D 62 4520 4027 6264 799 709 257 N ATOM 4931 CA ASP D 62 10.240 56.299 19.134 1.00 40.52 C ANISOU 4931 CA ASP D 62 4669 4050 6677 900 740 199 C ATOM 4932 C ASP D 62 11.247 57.397 18.809 1.00 39.81 C ANISOU 4932 C ASP D 62 4736 3911 6480 889 562 255 C ATOM 4933 O ASP D 62 12.345 57.436 19.358 1.00 38.90 O ANISOU 4933 O ASP D 62 4831 3833 6115 814 572 246 O ATOM 4934 CB ASP D 62 9.679 56.490 20.547 1.00 42.31 C ANISOU 4934 CB ASP D 62 4954 4177 6945 930 1062 35 C ATOM 4935 CG ASP D 62 8.308 55.831 20.737 1.00 44.61 C ANISOU 4935 CG ASP D 62 5007 4454 7488 966 1263 -35 C ATOM 4936 OD1 ASP D 62 7.755 55.922 21.856 1.00 45.81 O ANISOU 4936 OD1 ASP D 62 5198 4523 7684 976 1575 -181 O ATOM 4937 OD2 ASP D 62 7.776 55.226 19.777 1.00 45.27 O ANISOU 4937 OD2 ASP D 62 4875 4600 7727 972 1118 49 O ATOM 4938 N GLY D 63 10.867 58.275 17.889 1.00 40.55 N ANISOU 4938 N GLY D 63 4727 3906 6774 954 378 319 N ATOM 4939 CA GLY D 63 11.700 59.409 17.509 1.00 40.22 C ANISOU 4939 CA GLY D 63 4833 3792 6657 934 207 378 C ATOM 4940 C GLY D 63 12.382 59.164 16.189 1.00 39.01 C ANISOU 4940 C GLY D 63 4701 3739 6381 843 -36 533 C ATOM 4941 O GLY D 63 13.021 60.058 15.643 1.00 39.16 O ANISOU 4941 O GLY D 63 4832 3701 6346 802 -194 605 O ATOM 4942 N TYR D 64 12.226 57.947 15.672 1.00 38.20 N ANISOU 4942 N TYR D 64 4508 3776 6230 802 -55 580 N ATOM 4943 CA TYR D 64 12.954 57.495 14.485 1.00 37.09 C ANISOU 4943 CA TYR D 64 4419 3748 5925 699 -232 704 C ATOM 4944 C TYR D 64 12.036 56.895 13.444 1.00 37.70 C ANISOU 4944 C TYR D 64 4357 3833 6133 714 -370 778 C ATOM 4945 O TYR D 64 11.101 56.170 13.780 1.00 38.15 O ANISOU 4945 O TYR D 64 4258 3902 6334 769 -281 726 O ATOM 4946 CB TYR D 64 13.978 56.432 14.867 1.00 35.18 C ANISOU 4946 CB TYR D 64 4257 3679 5431 610 -133 685 C ATOM 4947 CG TYR D 64 14.997 56.893 15.861 1.00 34.24 C ANISOU 4947 CG TYR D 64 4286 3553 5171 574 -46 624 C ATOM 4948 CD1 TYR D 64 16.137 57.575 15.444 1.00 34.44 C ANISOU 4948 CD1 TYR D 64 4423 3582 5079 490 -149 680 C ATOM 4949 CD2 TYR D 64 14.826 56.657 17.221 1.00 33.54 C ANISOU 4949 CD2 TYR D 64 4242 3440 5062 608 135 510 C ATOM 4950 CE1 TYR D 64 17.091 58.010 16.357 1.00 33.24 C ANISOU 4950 CE1 TYR D 64 4399 3411 4820 448 -103 628 C ATOM 4951 CE2 TYR D 64 15.775 57.088 18.142 1.00 33.54 C ANISOU 4951 CE2 TYR D 64 4413 3411 4920 564 174 459 C ATOM 4952 CZ TYR D 64 16.903 57.761 17.699 1.00 32.57 C ANISOU 4952 CZ TYR D 64 4372 3293 4710 488 39 520 C ATOM 4953 OH TYR D 64 17.842 58.189 18.594 1.00 32.75 O ANISOU 4953 OH TYR D 64 4551 3275 4617 437 45 474 O ATOM 4954 N LYS D 65 12.328 57.200 12.184 1.00 38.17 N ANISOU 4954 N LYS D 65 4495 3877 6132 648 -590 899 N ATOM 4955 CA LYS D 65 11.676 56.586 11.035 1.00 39.14 C ANISOU 4955 CA LYS D 65 4560 4006 6307 625 -770 989 C ATOM 4956 C LYS D 65 12.756 55.836 10.234 1.00 37.73 C ANISOU 4956 C LYS D 65 4533 3980 5824 484 -796 1054 C ATOM 4957 O LYS D 65 13.916 56.263 10.216 1.00 37.37 O ANISOU 4957 O LYS D 65 4629 3976 5593 404 -756 1065 O ATOM 4958 CB LYS D 65 10.977 57.663 10.194 1.00 41.21 C ANISOU 4958 CB LYS D 65 4825 4070 6762 663 -1031 1074 C ATOM 4959 CG LYS D 65 10.048 57.124 9.103 1.00 44.12 C ANISOU 4959 CG LYS D 65 5124 4392 7248 655 -1267 1163 C ATOM 4960 CD LYS D 65 8.699 57.867 9.043 1.00 49.13 C ANISOU 4960 CD LYS D 65 5575 4807 8284 790 -1443 1164 C ATOM 4961 CE LYS D 65 8.687 59.034 8.039 1.00 52.19 C ANISOU 4961 CE LYS D 65 6127 5000 8704 766 -1767 1288 C ATOM 4962 NZ LYS D 65 8.735 58.619 6.598 1.00 52.55 N ANISOU 4962 NZ LYS D 65 6350 5036 8580 634 -2049 1437 N ATOM 4963 N ALA D 66 12.399 54.707 9.616 1.00 37.02 N ANISOU 4963 N ALA D 66 4405 3967 5695 451 -847 1085 N ATOM 4964 CA ALA D 66 13.361 53.970 8.788 1.00 35.78 C ANISOU 4964 CA ALA D 66 4395 3937 5264 326 -855 1131 C ATOM 4965 C ALA D 66 12.948 53.907 7.328 1.00 36.88 C ANISOU 4965 C ALA D 66 4641 4012 5360 252 -1092 1246 C ATOM 4966 O ALA D 66 11.810 54.188 6.980 1.00 38.45 O ANISOU 4966 O ALA D 66 4766 4078 5766 305 -1281 1295 O ATOM 4967 CB ALA D 66 13.607 52.590 9.328 1.00 34.34 C ANISOU 4967 CB ALA D 66 4150 3905 4993 328 -695 1056 C ATOM 4968 N SER D 67 13.897 53.551 6.472 1.00 36.43 N ANISOU 4968 N SER D 67 4767 4037 5039 122 -1083 1286 N ATOM 4969 CA SER D 67 13.660 53.468 5.044 1.00 37.42 C ANISOU 4969 CA SER D 67 5074 4097 5047 17 -1291 1394 C ATOM 4970 C SER D 67 14.611 52.455 4.418 1.00 36.55 C ANISOU 4970 C SER D 67 5103 4129 4655 -98 -1168 1374 C ATOM 4971 O SER D 67 15.832 52.535 4.599 1.00 35.96 O ANISOU 4971 O SER D 67 5078 4152 4433 -156 -979 1326 O ATOM 4972 CB SER D 67 13.849 54.834 4.399 1.00 39.03 C ANISOU 4972 CB SER D 67 5459 4154 5215 -55 -1444 1490 C ATOM 4973 OG SER D 67 13.540 54.795 3.014 1.00 41.59 O ANISOU 4973 OG SER D 67 6010 4383 5408 -172 -1675 1604 O ATOM 4974 N ARG D 68 14.041 51.492 3.701 1.00 36.42 N ANISOU 4974 N ARG D 68 5136 4115 4588 -127 -1276 1400 N ATOM 4975 CA ARG D 68 14.826 50.523 2.961 1.00 35.85 C ANISOU 4975 CA ARG D 68 5224 4147 4250 -235 -1174 1376 C ATOM 4976 C ARG D 68 14.456 50.629 1.479 1.00 37.73 C ANISOU 4976 C ARG D 68 5743 4266 4326 -370 -1401 1488 C ATOM 4977 O ARG D 68 13.662 49.832 0.972 1.00 38.40 O ANISOU 4977 O ARG D 68 5863 4312 4415 -376 -1559 1516 O ATOM 4978 CB ARG D 68 14.580 49.108 3.503 1.00 34.46 C ANISOU 4978 CB ARG D 68 4901 4078 4116 -160 -1082 1292 C ATOM 4979 CG ARG D 68 15.517 48.051 2.952 1.00 34.06 C ANISOU 4979 CG ARG D 68 4981 4139 3823 -238 -933 1232 C ATOM 4980 CD ARG D 68 16.780 47.915 3.781 1.00 33.42 C ANISOU 4980 CD ARG D 68 4799 4187 3712 -207 -672 1124 C ATOM 4981 NE ARG D 68 17.737 47.006 3.150 1.00 34.71 N ANISOU 4981 NE ARG D 68 5075 4436 3676 -276 -524 1056 N ATOM 4982 CZ ARG D 68 17.786 45.689 3.342 1.00 34.62 C ANISOU 4982 CZ ARG D 68 5015 4492 3646 -226 -463 979 C ATOM 4983 NH1 ARG D 68 16.928 45.082 4.156 1.00 33.63 N ANISOU 4983 NH1 ARG D 68 4743 4364 3669 -125 -534 968 N ATOM 4984 NH2 ARG D 68 18.702 44.972 2.710 1.00 36.45 N ANISOU 4984 NH2 ARG D 68 5352 4783 3714 -283 -318 905 N ATOM 4985 N PRO D 69 15.014 51.630 0.776 1.00 38.84 N ANISOU 4985 N PRO D 69 6112 4332 4314 -494 -1434 1559 N ATOM 4986 CA PRO D 69 14.634 51.828 -0.624 1.00 41.22 C ANISOU 4986 CA PRO D 69 6740 4486 4434 -643 -1677 1678 C ATOM 4987 C PRO D 69 15.213 50.783 -1.569 1.00 41.80 C ANISOU 4987 C PRO D 69 7055 4632 4195 -780 -1563 1646 C ATOM 4988 O PRO D 69 14.692 50.595 -2.660 1.00 43.66 O ANISOU 4988 O PRO D 69 7565 4746 4277 -890 -1785 1731 O ATOM 4989 CB PRO D 69 15.204 53.209 -0.949 1.00 42.16 C ANISOU 4989 CB PRO D 69 7043 4512 4463 -749 -1694 1752 C ATOM 4990 CG PRO D 69 16.306 53.384 -0.018 1.00 40.52 C ANISOU 4990 CG PRO D 69 6660 4457 4277 -713 -1373 1647 C ATOM 4991 CD PRO D 69 15.905 52.698 1.247 1.00 38.40 C ANISOU 4991 CD PRO D 69 6042 4293 4256 -515 -1289 1546 C ATOM 4992 N SER D 70 16.285 50.119 -1.150 1.00 40.75 N ANISOU 4992 N SER D 70 6829 4678 3977 -771 -1231 1519 N ATOM 4993 CA SER D 70 16.913 49.081 -1.954 1.00 41.63 C ANISOU 4993 CA SER D 70 7136 4860 3821 -877 -1072 1455 C ATOM 4994 C SER D 70 17.513 48.030 -1.041 1.00 39.87 C ANISOU 4994 C SER D 70 6648 4813 3687 -754 -816 1304 C ATOM 4995 O SER D 70 17.559 48.219 0.183 1.00 38.18 O ANISOU 4995 O SER D 70 6142 4665 3700 -615 -754 1259 O ATOM 4996 CB SER D 70 17.989 49.679 -2.869 1.00 43.47 C ANISOU 4996 CB SER D 70 7666 5080 3771 -1081 -899 1466 C ATOM 4997 OG SER D 70 19.106 50.157 -2.135 1.00 43.01 O ANISOU 4997 OG SER D 70 7419 5137 3787 -1062 -624 1387 O ATOM 4998 N GLN D 71 17.958 46.923 -1.640 1.00 40.67 N ANISOU 4998 N GLN D 71 6878 4972 3603 -807 -681 1224 N ATOM 4999 CA GLN D 71 18.619 45.833 -0.917 1.00 39.58 C ANISOU 4999 CA GLN D 71 6530 4977 3531 -698 -455 1077 C ATOM 5000 C GLN D 71 19.847 46.376 -0.224 1.00 39.30 C ANISOU 5000 C GLN D 71 6320 5041 3572 -678 -204 1000 C ATOM 5001 O GLN D 71 20.144 45.995 0.909 1.00 37.73 O ANISOU 5001 O GLN D 71 5853 4927 3554 -541 -123 920 O ATOM 5002 CB GLN D 71 19.018 44.712 -1.889 1.00 40.82 C ANISOU 5002 CB GLN D 71 6909 5149 3450 -780 -337 998 C ATOM 5003 CG GLN D 71 19.790 43.529 -1.279 1.00 40.18 C ANISOU 5003 CG GLN D 71 6640 5192 3436 -668 -112 836 C ATOM 5004 CD GLN D 71 18.923 42.586 -0.440 1.00 39.18 C ANISOU 5004 CD GLN D 71 6329 5076 3481 -519 -263 825 C ATOM 5005 OE1 GLN D 71 17.763 42.872 -0.151 1.00 39.44 O ANISOU 5005 OE1 GLN D 71 6308 5044 3632 -484 -502 928 O ATOM 5006 NE2 GLN D 71 19.492 41.452 -0.054 1.00 38.04 N ANISOU 5006 NE2 GLN D 71 6086 5003 3364 -434 -118 697 N ATOM 5007 N GLU D 72 20.528 47.294 -0.916 1.00 41.31 N ANISOU 5007 N GLU D 72 6746 5266 3684 -831 -105 1033 N ATOM 5008 CA GLU D 72 21.814 47.854 -0.498 1.00 41.69 C ANISOU 5008 CA GLU D 72 6660 5396 3786 -860 144 961 C ATOM 5009 C GLU D 72 21.741 48.937 0.584 1.00 40.47 C ANISOU 5009 C GLU D 72 6302 5230 3844 -784 61 1010 C ATOM 5010 O GLU D 72 22.609 48.988 1.454 1.00 39.68 O ANISOU 5010 O GLU D 72 5978 5215 3885 -723 210 926 O ATOM 5011 CB GLU D 72 22.563 48.393 -1.717 1.00 44.36 C ANISOU 5011 CB GLU D 72 7282 5699 3874 -1086 310 976 C ATOM 5012 CG GLU D 72 23.162 47.311 -2.625 1.00 47.71 C ANISOU 5012 CG GLU D 72 7864 6165 4100 -1165 540 860 C ATOM 5013 CD GLU D 72 22.108 46.485 -3.387 1.00 50.00 C ANISOU 5013 CD GLU D 72 8406 6371 4219 -1176 341 904 C ATOM 5014 OE1 GLU D 72 21.175 47.074 -3.981 1.00 50.37 O ANISOU 5014 OE1 GLU D 72 8700 6285 4152 -1262 74 1052 O ATOM 5015 OE2 GLU D 72 22.230 45.238 -3.396 1.00 51.04 O ANISOU 5015 OE2 GLU D 72 8494 6556 4342 -1099 433 790 O ATOM 5016 N ASN D 73 20.727 49.801 0.535 1.00 40.55 N ANISOU 5016 N ASN D 73 6395 5122 3891 -785 -186 1141 N ATOM 5017 CA ASN D 73 20.644 50.906 1.492 1.00 39.88 C ANISOU 5017 CA ASN D 73 6155 5003 3994 -719 -254 1179 C ATOM 5018 C ASN D 73 19.598 50.744 2.586 1.00 38.05 C ANISOU 5018 C ASN D 73 5713 4751 3992 -531 -411 1182 C ATOM 5019 O ASN D 73 18.482 50.318 2.319 1.00 38.24 O ANISOU 5019 O ASN D 73 5771 4714 4045 -486 -590 1230 O ATOM 5020 CB ASN D 73 20.461 52.247 0.775 1.00 41.65 C ANISOU 5020 CB ASN D 73 6607 5089 4131 -857 -384 1309 C ATOM 5021 CG ASN D 73 21.658 52.608 -0.129 1.00 45.19 C ANISOU 5021 CG ASN D 73 7254 5557 4359 -1072 -169 1300 C ATOM 5022 OD1 ASN D 73 22.817 52.601 0.309 1.00 46.01 O ANISOU 5022 OD1 ASN D 73 7204 5767 4509 -1092 73 1204 O ATOM 5023 ND2 ASN D 73 21.371 52.942 -1.397 1.00 47.50 N ANISOU 5023 ND2 ASN D 73 7897 5733 4416 -1246 -265 1400 N ATOM 5024 N PHE D 74 19.992 51.077 3.816 1.00 36.63 N ANISOU 5024 N PHE D 74 5326 4616 3975 -436 -333 1125 N ATOM 5025 CA PHE D 74 19.100 51.183 4.970 1.00 35.16 C ANISOU 5025 CA PHE D 74 4966 4396 3999 -281 -430 1119 C ATOM 5026 C PHE D 74 19.364 52.522 5.670 1.00 35.55 C ANISOU 5026 C PHE D 74 4973 4383 4151 -271 -436 1137 C ATOM 5027 O PHE D 74 20.459 52.753 6.180 1.00 35.27 O ANISOU 5027 O PHE D 74 4880 4408 4112 -298 -300 1079 O ATOM 5028 CB PHE D 74 19.355 50.021 5.937 1.00 33.59 C ANISOU 5028 CB PHE D 74 4595 4306 3862 -175 -315 1008 C ATOM 5029 CG PHE D 74 18.289 49.841 7.001 1.00 31.67 C ANISOU 5029 CG PHE D 74 4214 4028 3793 -40 -384 995 C ATOM 5030 CD1 PHE D 74 16.972 50.271 6.794 1.00 31.78 C ANISOU 5030 CD1 PHE D 74 4226 3933 3917 -5 -548 1069 C ATOM 5031 CD2 PHE D 74 18.594 49.197 8.187 1.00 28.45 C ANISOU 5031 CD2 PHE D 74 3682 3684 3445 42 -285 905 C ATOM 5032 CE1 PHE D 74 15.997 50.087 7.765 1.00 29.48 C ANISOU 5032 CE1 PHE D 74 3785 3609 3806 107 -563 1040 C ATOM 5033 CE2 PHE D 74 17.629 49.012 9.154 1.00 27.68 C ANISOU 5033 CE2 PHE D 74 3489 3550 3480 138 -307 887 C ATOM 5034 CZ PHE D 74 16.330 49.462 8.947 1.00 27.95 C ANISOU 5034 CZ PHE D 74 3496 3488 3637 169 -422 948 C ATOM 5035 N SER D 75 18.361 53.397 5.689 1.00 36.38 N ANISOU 5035 N SER D 75 5102 4353 4366 -230 -609 1213 N ATOM 5036 CA SER D 75 18.492 54.731 6.283 1.00 37.06 C ANISOU 5036 CA SER D 75 5180 4350 4553 -217 -637 1232 C ATOM 5037 C SER D 75 17.664 54.967 7.546 1.00 36.43 C ANISOU 5037 C SER D 75 4936 4213 4691 -54 -658 1183 C ATOM 5038 O SER D 75 16.480 54.631 7.605 1.00 36.60 O ANISOU 5038 O SER D 75 4881 4184 4843 37 -750 1192 O ATOM 5039 CB SER D 75 18.115 55.806 5.266 1.00 39.07 C ANISOU 5039 CB SER D 75 5628 4449 4766 -309 -820 1356 C ATOM 5040 OG SER D 75 19.254 56.302 4.598 1.00 40.85 O ANISOU 5040 OG SER D 75 6016 4694 4811 -484 -734 1388 O ATOM 5041 N LEU D 76 18.300 55.581 8.541 1.00 36.01 N ANISOU 5041 N LEU D 76 4841 4161 4682 -32 -566 1128 N ATOM 5042 CA LEU D 76 17.622 56.048 9.743 1.00 35.52 C ANISOU 5042 CA LEU D 76 4682 4018 4796 98 -558 1073 C ATOM 5043 C LEU D 76 17.347 57.552 9.633 1.00 37.13 C ANISOU 5043 C LEU D 76 4965 4052 5089 97 -676 1129 C ATOM 5044 O LEU D 76 18.275 58.358 9.482 1.00 37.72 O ANISOU 5044 O LEU D 76 5146 4104 5080 -2 -673 1157 O ATOM 5045 CB LEU D 76 18.464 55.743 10.980 1.00 33.99 C ANISOU 5045 CB LEU D 76 4434 3903 4576 120 -407 972 C ATOM 5046 CG LEU D 76 17.724 55.877 12.306 1.00 33.43 C ANISOU 5046 CG LEU D 76 4298 3766 4639 244 -349 893 C ATOM 5047 CD1 LEU D 76 16.813 54.702 12.516 1.00 32.86 C ANISOU 5047 CD1 LEU D 76 4123 3745 4617 316 -303 857 C ATOM 5048 CD2 LEU D 76 18.694 55.992 13.453 1.00 33.68 C ANISOU 5048 CD2 LEU D 76 4363 3820 4613 230 -259 816 C ATOM 5049 N ILE D 77 16.073 57.923 9.705 1.00 38.14 N ANISOU 5049 N ILE D 77 5032 4049 5409 207 -783 1142 N ATOM 5050 CA ILE D 77 15.676 59.317 9.590 1.00 40.02 C ANISOU 5050 CA ILE D 77 5338 4096 5772 234 -922 1190 C ATOM 5051 C ILE D 77 15.133 59.819 10.908 1.00 40.58 C ANISOU 5051 C ILE D 77 5304 4078 6035 378 -831 1084 C ATOM 5052 O ILE D 77 14.288 59.182 11.529 1.00 40.64 O ANISOU 5052 O ILE D 77 5158 4103 6180 488 -744 1009 O ATOM 5053 CB ILE D 77 14.602 59.532 8.498 1.00 41.60 C ANISOU 5053 CB ILE D 77 5560 4161 6084 252 -1167 1292 C ATOM 5054 CG1 ILE D 77 15.125 59.104 7.126 1.00 41.79 C ANISOU 5054 CG1 ILE D 77 5759 4246 5874 84 -1259 1399 C ATOM 5055 CG2 ILE D 77 14.163 60.989 8.451 1.00 43.18 C ANISOU 5055 CG2 ILE D 77 5826 4134 6447 300 -1336 1335 C ATOM 5056 CD1 ILE D 77 14.047 58.520 6.204 1.00 42.42 C ANISOU 5056 CD1 ILE D 77 5829 4268 6021 102 -1462 1469 C ATOM 5057 N LEU D 78 15.643 60.969 11.323 1.00 41.70 N ANISOU 5057 N LEU D 78 5548 4118 6177 362 -837 1075 N ATOM 5058 CA LEU D 78 15.124 61.712 12.453 1.00 42.77 C ANISOU 5058 CA LEU D 78 5642 4121 6487 491 -767 976 C ATOM 5059 C LEU D 78 14.443 62.938 11.848 1.00 45.55 C ANISOU 5059 C LEU D 78 6042 4248 7016 540 -978 1043 C ATOM 5060 O LEU D 78 15.124 63.823 11.301 1.00 46.42 O ANISOU 5060 O LEU D 78 6327 4284 7027 434 -1101 1128 O ATOM 5061 CB LEU D 78 16.283 62.136 13.360 1.00 41.70 C ANISOU 5061 CB LEU D 78 5621 4012 6210 426 -653 917 C ATOM 5062 CG LEU D 78 17.046 61.096 14.199 1.00 39.80 C ANISOU 5062 CG LEU D 78 5358 3946 5819 388 -479 839 C ATOM 5063 CD1 LEU D 78 17.722 60.010 13.377 1.00 37.82 C ANISOU 5063 CD1 LEU D 78 5077 3880 5413 283 -483 898 C ATOM 5064 CD2 LEU D 78 18.081 61.778 15.065 1.00 39.66 C ANISOU 5064 CD2 LEU D 78 5468 3892 5710 328 -440 792 C ATOM 5065 N GLU D 79 13.109 62.977 11.906 1.00 47.34 N ANISOU 5065 N GLU D 79 6112 4356 7518 692 -1030 1009 N ATOM 5066 CA GLU D 79 12.333 64.099 11.349 1.00 49.86 C ANISOU 5066 CA GLU D 79 6447 4430 8067 769 -1268 1066 C ATOM 5067 C GLU D 79 12.573 65.374 12.156 1.00 51.04 C ANISOU 5067 C GLU D 79 6695 4415 8284 825 -1227 996 C ATOM 5068 O GLU D 79 12.954 66.402 11.602 1.00 52.24 O ANISOU 5068 O GLU D 79 7024 4426 8397 761 -1415 1086 O ATOM 5069 CB GLU D 79 10.834 63.780 11.318 1.00 51.30 C ANISOU 5069 CB GLU D 79 6379 4519 8592 934 -1324 1024 C ATOM 5070 CG GLU D 79 10.435 62.568 10.467 1.00 51.88 C ANISOU 5070 CG GLU D 79 6360 4718 8635 883 -1412 1099 C ATOM 5071 CD GLU D 79 10.326 62.878 8.972 1.00 54.61 C ANISOU 5071 CD GLU D 79 6849 4957 8942 796 -1768 1272 C ATOM 5072 OE1 GLU D 79 10.685 64.004 8.553 1.00 57.09 O ANISOU 5072 OE1 GLU D 79 7357 5116 9217 751 -1940 1348 O ATOM 5073 OE2 GLU D 79 9.874 61.992 8.211 1.00 53.81 O ANISOU 5073 OE2 GLU D 79 6696 4913 8837 759 -1887 1336 O ATOM 5074 N LEU D 80 12.354 65.294 13.469 1.00 51.15 N ANISOU 5074 N LEU D 80 6621 4434 8380 930 -978 836 N ATOM 5075 CA LEU D 80 12.575 66.422 14.385 1.00 52.24 C ANISOU 5075 CA LEU D 80 6874 4413 8562 984 -904 742 C ATOM 5076 C LEU D 80 13.570 66.018 15.470 1.00 50.57 C ANISOU 5076 C LEU D 80 6768 4347 8100 902 -669 655 C ATOM 5077 O LEU D 80 13.180 65.510 16.527 1.00 50.81 O ANISOU 5077 O LEU D 80 6725 4412 8167 978 -433 517 O ATOM 5078 CB LEU D 80 11.256 66.887 15.023 1.00 54.35 C ANISOU 5078 CB LEU D 80 6972 4484 9194 1201 -825 606 C ATOM 5079 CG LEU D 80 10.082 67.296 14.120 1.00 56.88 C ANISOU 5079 CG LEU D 80 7132 4618 9863 1325 -1076 664 C ATOM 5080 CD1 LEU D 80 8.763 67.365 14.902 1.00 58.98 C ANISOU 5080 CD1 LEU D 80 7137 4748 10523 1542 -904 491 C ATOM 5081 CD2 LEU D 80 10.355 68.616 13.388 1.00 58.70 C ANISOU 5081 CD2 LEU D 80 7558 4629 10118 1301 -1381 776 C ATOM 5082 N ALA D 81 14.853 66.242 15.197 1.00 49.16 N ANISOU 5082 N ALA D 81 6767 4239 7674 735 -741 737 N ATOM 5083 CA ALA D 81 15.923 65.831 16.099 1.00 47.60 C ANISOU 5083 CA ALA D 81 6664 4172 7250 639 -586 676 C ATOM 5084 C ALA D 81 15.868 66.520 17.467 1.00 48.54 C ANISOU 5084 C ALA D 81 6895 4149 7399 711 -449 530 C ATOM 5085 O ALA D 81 15.621 67.729 17.564 1.00 50.25 O ANISOU 5085 O ALA D 81 7205 4153 7733 768 -525 510 O ATOM 5086 CB ALA D 81 17.277 66.063 15.445 1.00 47.04 C ANISOU 5086 CB ALA D 81 6723 4178 6973 444 -705 792 C ATOM 5087 N THR D 82 16.096 65.735 18.518 1.00 47.23 N ANISOU 5087 N THR D 82 6749 4084 7113 703 -256 428 N ATOM 5088 CA THR D 82 16.192 66.261 19.877 1.00 47.89 C ANISOU 5088 CA THR D 82 7004 4041 7150 734 -117 287 C ATOM 5089 C THR D 82 17.540 65.883 20.509 1.00 46.52 C ANISOU 5089 C THR D 82 6991 3972 6711 581 -124 289 C ATOM 5090 O THR D 82 18.182 64.929 20.065 1.00 44.65 O ANISOU 5090 O THR D 82 6675 3927 6362 489 -165 363 O ATOM 5091 CB THR D 82 15.049 65.754 20.770 1.00 48.59 C ANISOU 5091 CB THR D 82 7017 4095 7349 868 139 136 C ATOM 5092 OG1 THR D 82 15.218 64.353 21.013 1.00 47.94 O ANISOU 5092 OG1 THR D 82 6877 4214 7125 811 245 134 O ATOM 5093 CG2 THR D 82 13.692 66.023 20.132 1.00 49.50 C ANISOU 5093 CG2 THR D 82 6910 4109 7787 1026 133 128 C ATOM 5094 N PRO D 83 17.973 66.632 21.546 1.00 47.42 N ANISOU 5094 N PRO D 83 7334 3943 6740 556 -97 201 N ATOM 5095 CA PRO D 83 19.260 66.362 22.194 1.00 46.66 C ANISOU 5095 CA PRO D 83 7396 3909 6422 408 -155 204 C ATOM 5096 C PRO D 83 19.426 64.938 22.757 1.00 45.32 C ANISOU 5096 C PRO D 83 7200 3903 6117 380 -52 168 C ATOM 5097 O PRO D 83 20.549 64.437 22.830 1.00 44.28 O ANISOU 5097 O PRO D 83 7096 3874 5854 259 -162 216 O ATOM 5098 CB PRO D 83 19.302 67.402 23.319 1.00 48.40 C ANISOU 5098 CB PRO D 83 7890 3903 6596 420 -120 88 C ATOM 5099 CG PRO D 83 18.503 68.529 22.793 1.00 49.96 C ANISOU 5099 CG PRO D 83 8055 3928 6999 530 -144 86 C ATOM 5100 CD PRO D 83 17.371 67.879 22.056 1.00 49.55 C ANISOU 5100 CD PRO D 83 7735 3963 7130 655 -57 105 C ATOM 5101 N SER D 84 18.323 64.300 23.143 1.00 45.37 N ANISOU 5101 N SER D 84 7145 3919 6174 488 151 84 N ATOM 5102 CA SER D 84 18.366 62.952 23.683 1.00 44.26 C ANISOU 5102 CA SER D 84 7005 3910 5902 457 251 54 C ATOM 5103 C SER D 84 18.765 61.952 22.599 1.00 42.46 C ANISOU 5103 C SER D 84 6554 3896 5683 414 144 175 C ATOM 5104 O SER D 84 18.967 60.763 22.873 1.00 41.57 O ANISOU 5104 O SER D 84 6426 3903 5466 381 179 171 O ATOM 5105 CB SER D 84 17.002 62.578 24.257 1.00 45.50 C ANISOU 5105 CB SER D 84 7133 4017 6138 567 519 -62 C ATOM 5106 OG SER D 84 16.020 62.532 23.234 1.00 45.07 O ANISOU 5106 OG SER D 84 6800 4002 6324 672 540 -18 O ATOM 5107 N GLN D 85 18.868 62.440 21.364 1.00 41.93 N ANISOU 5107 N GLN D 85 6343 3860 5730 410 14 281 N ATOM 5108 CA GLN D 85 19.253 61.597 20.239 1.00 40.06 C ANISOU 5108 CA GLN D 85 5926 3808 5488 361 -71 389 C ATOM 5109 C GLN D 85 20.737 61.706 19.928 1.00 39.59 C ANISOU 5109 C GLN D 85 5896 3814 5331 220 -221 457 C ATOM 5110 O GLN D 85 21.223 61.085 18.986 1.00 39.41 O ANISOU 5110 O GLN D 85 5740 3936 5299 163 -273 534 O ATOM 5111 CB GLN D 85 18.401 61.899 19.011 1.00 40.01 C ANISOU 5111 CB GLN D 85 5763 3794 5645 423 -113 464 C ATOM 5112 CG GLN D 85 16.960 61.432 19.171 1.00 40.48 C ANISOU 5112 CG GLN D 85 5704 3830 5846 555 25 404 C ATOM 5113 CD GLN D 85 16.112 61.710 17.956 1.00 40.32 C ANISOU 5113 CD GLN D 85 5528 3780 6012 617 -73 485 C ATOM 5114 OE1 GLN D 85 16.040 62.843 17.478 1.00 41.65 O ANISOU 5114 OE1 GLN D 85 5738 3815 6274 630 -195 529 O ATOM 5115 NE2 GLN D 85 15.455 60.675 17.450 1.00 38.77 N ANISOU 5115 NE2 GLN D 85 5171 3689 5869 647 -47 509 N ATOM 5116 N THR D 86 21.457 62.490 20.723 1.00 40.12 N ANISOU 5116 N THR D 86 6137 3768 5340 158 -283 420 N ATOM 5117 CA THR D 86 22.910 62.456 20.722 1.00 39.54 C ANISOU 5117 CA THR D 86 6077 3749 5198 20 -419 460 C ATOM 5118 C THR D 86 23.323 61.034 21.077 1.00 38.58 C ANISOU 5118 C THR D 86 5894 3764 5002 10 -404 435 C ATOM 5119 O THR D 86 22.987 60.547 22.163 1.00 39.00 O ANISOU 5119 O THR D 86 6078 3769 4970 51 -345 354 O ATOM 5120 CB THR D 86 23.485 63.408 21.786 1.00 40.75 C ANISOU 5120 CB THR D 86 6457 3731 5295 -38 -500 405 C ATOM 5121 OG1 THR D 86 23.015 64.738 21.549 1.00 41.93 O ANISOU 5121 OG1 THR D 86 6689 3726 5518 -13 -512 415 O ATOM 5122 CG2 THR D 86 24.998 63.392 21.769 1.00 40.40 C ANISOU 5122 CG2 THR D 86 6388 3732 5231 -188 -665 448 C ATOM 5123 N SER D 87 24.024 60.363 20.166 1.00 37.44 N ANISOU 5123 N SER D 87 5570 3774 4883 -47 -450 499 N ATOM 5124 CA SER D 87 24.522 59.010 20.431 1.00 36.62 C ANISOU 5124 CA SER D 87 5394 3786 4734 -50 -463 475 C ATOM 5125 C SER D 87 25.566 58.611 19.402 1.00 35.90 C ANISOU 5125 C SER D 87 5106 3830 4703 -133 -515 532 C ATOM 5126 O SER D 87 25.920 59.404 18.533 1.00 36.59 O ANISOU 5126 O SER D 87 5138 3922 4844 -209 -528 592 O ATOM 5127 CB SER D 87 23.362 57.995 20.421 1.00 35.99 C ANISOU 5127 CB SER D 87 5278 3769 4628 56 -330 451 C ATOM 5128 OG SER D 87 23.655 56.842 21.203 1.00 35.10 O ANISOU 5128 OG SER D 87 5210 3691 4436 61 -349 403 O ATOM 5129 N VAL D 88 26.075 57.392 19.518 1.00 34.63 N ANISOU 5129 N VAL D 88 4855 3766 4538 -124 -537 506 N ATOM 5130 CA VAL D 88 26.816 56.784 18.427 1.00 34.10 C ANISOU 5130 CA VAL D 88 4578 3839 4538 -171 -521 537 C ATOM 5131 C VAL D 88 25.875 55.751 17.826 1.00 33.02 C ANISOU 5131 C VAL D 88 4383 3802 4361 -82 -411 543 C ATOM 5132 O VAL D 88 25.323 54.927 18.549 1.00 32.65 O ANISOU 5132 O VAL D 88 4398 3747 4260 -6 -400 501 O ATOM 5133 CB VAL D 88 28.127 56.129 18.912 1.00 34.68 C ANISOU 5133 CB VAL D 88 4560 3935 4683 -214 -642 493 C ATOM 5134 CG1 VAL D 88 28.808 55.355 17.788 1.00 33.78 C ANISOU 5134 CG1 VAL D 88 4212 3965 4657 -241 -576 497 C ATOM 5135 CG2 VAL D 88 29.066 57.189 19.470 1.00 35.57 C ANISOU 5135 CG2 VAL D 88 4719 3939 4858 -319 -778 493 C ATOM 5136 N TYR D 89 25.658 55.815 16.517 1.00 32.69 N ANISOU 5136 N TYR D 89 4251 3838 4333 -108 -336 600 N ATOM 5137 CA TYR D 89 24.692 54.927 15.880 1.00 31.75 C ANISOU 5137 CA TYR D 89 4095 3793 4175 -35 -258 614 C ATOM 5138 C TYR D 89 25.427 53.895 15.071 1.00 31.96 C ANISOU 5138 C TYR D 89 3987 3947 4209 -64 -222 602 C ATOM 5139 O TYR D 89 26.355 54.231 14.326 1.00 32.96 O ANISOU 5139 O TYR D 89 4037 4114 4371 -162 -197 618 O ATOM 5140 CB TYR D 89 23.736 55.703 14.979 1.00 31.74 C ANISOU 5140 CB TYR D 89 4132 3755 4171 -36 -231 687 C ATOM 5141 CG TYR D 89 22.808 56.624 15.725 1.00 31.96 C ANISOU 5141 CG TYR D 89 4270 3646 4228 26 -247 680 C ATOM 5142 CD1 TYR D 89 23.234 57.892 16.138 1.00 32.67 C ANISOU 5142 CD1 TYR D 89 4449 3624 4341 -24 -301 686 C ATOM 5143 CD2 TYR D 89 21.499 56.232 16.021 1.00 31.18 C ANISOU 5143 CD2 TYR D 89 4177 3519 4151 133 -196 660 C ATOM 5144 CE1 TYR D 89 22.383 58.742 16.840 1.00 33.54 C ANISOU 5144 CE1 TYR D 89 4668 3591 4486 45 -299 661 C ATOM 5145 CE2 TYR D 89 20.643 57.068 16.717 1.00 31.69 C ANISOU 5145 CE2 TYR D 89 4319 3449 4273 199 -174 631 C ATOM 5146 CZ TYR D 89 21.091 58.320 17.125 1.00 33.02 C ANISOU 5146 CZ TYR D 89 4591 3501 4454 162 -223 627 C ATOM 5147 OH TYR D 89 20.250 59.148 17.816 1.00 33.69 O ANISOU 5147 OH TYR D 89 4760 3438 4602 237 -185 581 O ATOM 5148 N PHE D 90 25.018 52.638 15.226 1.00 31.29 N ANISOU 5148 N PHE D 90 3878 3916 4095 13 -203 568 N ATOM 5149 CA PHE D 90 25.621 51.537 14.484 1.00 31.20 C ANISOU 5149 CA PHE D 90 3751 4011 4094 8 -162 540 C ATOM 5150 C PHE D 90 24.617 50.853 13.585 1.00 30.50 C ANISOU 5150 C PHE D 90 3677 3976 3937 44 -99 572 C ATOM 5151 O PHE D 90 23.487 50.609 13.967 1.00 30.03 O ANISOU 5151 O PHE D 90 3678 3883 3848 111 -109 584 O ATOM 5152 CB PHE D 90 26.243 50.505 15.424 1.00 31.21 C ANISOU 5152 CB PHE D 90 3715 4010 4133 62 -236 466 C ATOM 5153 CG PHE D 90 27.516 50.960 16.083 1.00 32.09 C ANISOU 5153 CG PHE D 90 3771 4074 4346 13 -334 430 C ATOM 5154 CD1 PHE D 90 27.495 51.502 17.358 1.00 32.14 C ANISOU 5154 CD1 PHE D 90 3907 3968 4337 15 -449 422 C ATOM 5155 CD2 PHE D 90 28.736 50.814 15.441 1.00 33.46 C ANISOU 5155 CD2 PHE D 90 3765 4305 4642 -41 -309 396 C ATOM 5156 CE1 PHE D 90 28.667 51.917 17.983 1.00 33.49 C ANISOU 5156 CE1 PHE D 90 4038 4077 4609 -39 -582 394 C ATOM 5157 CE2 PHE D 90 29.914 51.230 16.056 1.00 35.45 C ANISOU 5157 CE2 PHE D 90 3931 4504 5034 -92 -421 362 C ATOM 5158 CZ PHE D 90 29.875 51.787 17.333 1.00 34.80 C ANISOU 5158 CZ PHE D 90 3990 4302 4932 -91 -581 368 C ATOM 5159 N CYS D 91 25.056 50.545 12.379 1.00 31.21 N ANISOU 5159 N CYS D 91 3713 4140 4004 -12 -28 578 N ATOM 5160 CA CYS D 91 24.252 49.826 11.424 1.00 31.24 C ANISOU 5160 CA CYS D 91 3752 4187 3929 3 9 605 C ATOM 5161 C CYS D 91 24.800 48.423 11.296 1.00 31.06 C ANISOU 5161 C CYS D 91 3657 4235 3910 43 47 528 C ATOM 5162 O CYS D 91 26.011 48.221 11.398 1.00 31.79 O ANISOU 5162 O CYS D 91 3645 4356 4078 25 79 462 O ATOM 5163 CB CYS D 91 24.353 50.515 10.077 1.00 32.19 C ANISOU 5163 CB CYS D 91 3931 4318 3983 -109 65 667 C ATOM 5164 SG CYS D 91 23.594 49.563 8.795 1.00 35.23 S ANISOU 5164 SG CYS D 91 4396 4742 4246 -118 90 693 S ATOM 5165 N ALA D 92 23.924 47.451 11.059 1.00 30.62 N ANISOU 5165 N ALA D 92 3643 4195 3795 99 36 532 N ATOM 5166 CA ALA D 92 24.373 46.073 10.824 1.00 30.86 C ANISOU 5166 CA ALA D 92 3629 4277 3821 141 66 458 C ATOM 5167 C ALA D 92 23.632 45.425 9.678 1.00 30.91 C ANISOU 5167 C ALA D 92 3715 4310 3720 123 97 484 C ATOM 5168 O ALA D 92 22.525 45.852 9.340 1.00 31.12 O ANISOU 5168 O ALA D 92 3824 4304 3698 104 49 566 O ATOM 5169 CB ALA D 92 24.200 45.243 12.066 1.00 30.45 C ANISOU 5169 CB ALA D 92 3572 4191 3807 232 -20 417 C ATOM 5170 N SER D 93 24.241 44.395 9.088 1.00 31.18 N ANISOU 5170 N SER D 93 3725 4387 3734 133 165 410 N ATOM 5171 CA SER D 93 23.570 43.570 8.074 1.00 31.03 C ANISOU 5171 CA SER D 93 3813 4379 3597 120 179 420 C ATOM 5172 C SER D 93 23.809 42.073 8.283 1.00 31.15 C ANISOU 5172 C SER D 93 3801 4403 3630 204 173 330 C ATOM 5173 O SER D 93 24.759 41.679 8.968 1.00 31.53 O ANISOU 5173 O SER D 93 3737 4452 3791 266 178 247 O ATOM 5174 CB SER D 93 24.004 43.980 6.670 1.00 31.96 C ANISOU 5174 CB SER D 93 4014 4521 3608 4 301 424 C ATOM 5175 OG SER D 93 25.137 43.251 6.263 1.00 32.53 O ANISOU 5175 OG SER D 93 4022 4634 3703 8 446 305 O ATOM 5176 N GLY D 94 22.942 41.247 7.698 1.00 31.26 N ANISOU 5176 N GLY D 94 3925 4405 3546 206 135 349 N ATOM 5177 CA GLY D 94 23.079 39.785 7.776 1.00 31.58 C ANISOU 5177 CA GLY D 94 3975 4437 3586 278 119 268 C ATOM 5178 C GLY D 94 22.220 38.986 6.809 1.00 31.94 C ANISOU 5178 C GLY D 94 4172 4466 3499 246 91 289 C ATOM 5179 O GLY D 94 21.161 39.448 6.377 1.00 31.95 O ANISOU 5179 O GLY D 94 4259 4447 3432 183 19 389 O ATOM 5180 N ASP D 95 22.675 37.782 6.460 1.00 32.58 N ANISOU 5180 N ASP D 95 4285 4538 3557 291 128 191 N ATOM 5181 CA ASP D 95 21.824 36.834 5.721 1.00 32.59 C ANISOU 5181 CA ASP D 95 4446 4502 3434 267 67 205 C ATOM 5182 C ASP D 95 20.966 36.041 6.700 1.00 30.99 C ANISOU 5182 C ASP D 95 4235 4257 3282 322 -81 239 C ATOM 5183 O ASP D 95 20.588 36.554 7.738 1.00 30.01 O ANISOU 5183 O ASP D 95 4029 4131 3241 338 -137 296 O ATOM 5184 CB ASP D 95 22.630 35.916 4.782 1.00 34.28 C ANISOU 5184 CB ASP D 95 4738 4708 3578 279 192 76 C ATOM 5185 CG ASP D 95 23.720 35.125 5.496 1.00 36.03 C ANISOU 5185 CG ASP D 95 4817 4918 3954 404 232 -55 C ATOM 5186 OD1 ASP D 95 23.495 34.595 6.609 1.00 37.05 O ANISOU 5186 OD1 ASP D 95 4891 5011 4176 483 93 -43 O ATOM 5187 OD2 ASP D 95 24.819 35.011 4.918 1.00 39.44 O ANISOU 5187 OD2 ASP D 95 5199 5363 4422 419 404 -177 O ATOM 5188 N GLU D 96 20.668 34.793 6.374 1.00 31.14 N ANISOU 5188 N GLU D 96 4356 4232 3242 340 -131 201 N ATOM 5189 CA GLU D 96 19.811 33.973 7.223 1.00 30.30 C ANISOU 5189 CA GLU D 96 4268 4077 3169 363 -263 238 C ATOM 5190 C GLU D 96 20.482 33.584 8.544 1.00 29.86 C ANISOU 5190 C GLU D 96 4128 3997 3221 453 -287 186 C ATOM 5191 O GLU D 96 19.808 33.142 9.469 1.00 29.42 O ANISOU 5191 O GLU D 96 4096 3897 3185 452 -376 229 O ATOM 5192 CB GLU D 96 19.290 32.734 6.465 1.00 31.01 C ANISOU 5192 CB GLU D 96 4514 4110 3157 341 -331 217 C ATOM 5193 CG GLU D 96 20.347 31.801 5.859 1.00 32.18 C ANISOU 5193 CG GLU D 96 4729 4232 3267 404 -252 76 C ATOM 5194 CD GLU D 96 20.947 32.291 4.544 1.00 34.59 C ANISOU 5194 CD GLU D 96 5104 4570 3468 355 -101 23 C ATOM 5195 OE1 GLU D 96 21.781 31.556 3.978 1.00 36.86 O ANISOU 5195 OE1 GLU D 96 5444 4831 3729 402 4 -109 O ATOM 5196 OE2 GLU D 96 20.608 33.401 4.069 1.00 35.49 O ANISOU 5196 OE2 GLU D 96 5233 4724 3527 265 -78 107 O ATOM 5197 N GLY D 97 21.796 33.776 8.627 1.00 30.16 N ANISOU 5197 N GLY D 97 4074 4052 3333 519 -212 94 N ATOM 5198 CA GLY D 97 22.576 33.358 9.782 1.00 30.33 C ANISOU 5198 CA GLY D 97 4029 4024 3470 608 -280 38 C ATOM 5199 C GLY D 97 22.442 34.264 10.986 1.00 29.68 C ANISOU 5199 C GLY D 97 3892 3944 3440 592 -325 106 C ATOM 5200 O GLY D 97 21.789 35.302 10.925 1.00 29.00 O ANISOU 5200 O GLY D 97 3791 3904 3323 524 -281 188 O ATOM 5201 N TYR D 98 23.067 33.874 12.093 1.00 30.05 N ANISOU 5201 N TYR D 98 3929 3922 3566 654 -428 69 N ATOM 5202 CA TYR D 98 23.005 34.692 13.302 1.00 29.40 C ANISOU 5202 CA TYR D 98 3844 3819 3506 630 -477 123 C ATOM 5203 C TYR D 98 23.964 35.885 13.303 1.00 29.97 C ANISOU 5203 C TYR D 98 3774 3937 3677 635 -424 101 C ATOM 5204 O TYR D 98 23.686 36.888 13.961 1.00 30.31 O ANISOU 5204 O TYR D 98 3823 3984 3708 589 -420 160 O ATOM 5205 CB TYR D 98 23.164 33.854 14.574 1.00 29.31 C ANISOU 5205 CB TYR D 98 3946 3690 3500 663 -640 114 C ATOM 5206 CG TYR D 98 24.451 33.072 14.705 1.00 30.12 C ANISOU 5206 CG TYR D 98 3998 3716 3731 769 -761 12 C ATOM 5207 CD1 TYR D 98 24.476 31.697 14.473 1.00 30.63 C ANISOU 5207 CD1 TYR D 98 4139 3706 3793 826 -842 -37 C ATOM 5208 CD2 TYR D 98 25.635 33.695 15.088 1.00 30.11 C ANISOU 5208 CD2 TYR D 98 3863 3700 3878 815 -811 -35 C ATOM 5209 CE1 TYR D 98 25.648 30.968 14.601 1.00 32.11 C ANISOU 5209 CE1 TYR D 98 4263 3801 4138 942 -967 -140 C ATOM 5210 CE2 TYR D 98 26.808 32.983 15.220 1.00 31.56 C ANISOU 5210 CE2 TYR D 98 3960 3796 4234 922 -941 -135 C ATOM 5211 CZ TYR D 98 26.818 31.615 14.980 1.00 33.97 C ANISOU 5211 CZ TYR D 98 4334 4022 4551 994 -1019 -191 C ATOM 5212 OH TYR D 98 28.006 30.894 15.117 1.00 36.69 O ANISOU 5212 OH TYR D 98 4572 4257 5110 1121 -1164 -302 O ATOM 5213 N THR D 99 25.075 35.789 12.571 1.00 30.74 N ANISOU 5213 N THR D 99 3743 4059 3876 683 -369 10 N ATOM 5214 CA THR D 99 26.083 36.854 12.554 1.00 30.80 C ANISOU 5214 CA THR D 99 3595 4103 4003 673 -313 -17 C ATOM 5215 C THR D 99 25.536 38.148 11.979 1.00 29.91 C ANISOU 5215 C THR D 99 3483 4072 3809 575 -187 61 C ATOM 5216 O THR D 99 24.924 38.163 10.913 1.00 29.59 O ANISOU 5216 O THR D 99 3496 4081 3665 527 -87 88 O ATOM 5217 CB THR D 99 27.334 36.460 11.748 1.00 32.29 C ANISOU 5217 CB THR D 99 3622 4306 4340 729 -226 -145 C ATOM 5218 OG1 THR D 99 27.836 35.210 12.223 1.00 33.73 O ANISOU 5218 OG1 THR D 99 3796 4391 4628 840 -365 -227 O ATOM 5219 CG2 THR D 99 28.417 37.503 11.901 1.00 32.92 C ANISOU 5219 CG2 THR D 99 3518 4409 4580 707 -186 -175 C ATOM 5220 N GLN D 100 25.750 39.233 12.713 1.00 29.88 N ANISOU 5220 N GLN D 100 3443 4061 3850 543 -219 101 N ATOM 5221 CA GLN D 100 25.521 40.580 12.184 1.00 29.32 C ANISOU 5221 CA GLN D 100 3352 4046 3742 458 -115 163 C ATOM 5222 C GLN D 100 26.853 41.303 12.017 1.00 29.88 C ANISOU 5222 C GLN D 100 3266 4137 3950 435 -61 110 C ATOM 5223 O GLN D 100 27.693 41.344 12.913 1.00 30.38 O ANISOU 5223 O GLN D 100 3248 4150 4146 471 -166 69 O ATOM 5224 CB GLN D 100 24.522 41.352 13.034 1.00 28.18 C ANISOU 5224 CB GLN D 100 3303 3868 3535 427 -167 254 C ATOM 5225 CG GLN D 100 23.127 40.738 12.917 1.00 28.76 C ANISOU 5225 CG GLN D 100 3488 3934 3504 426 -173 306 C ATOM 5226 CD GLN D 100 22.072 41.408 13.777 1.00 29.81 C ANISOU 5226 CD GLN D 100 3690 4026 3609 402 -186 373 C ATOM 5227 OE1 GLN D 100 22.312 42.443 14.408 1.00 30.40 O ANISOU 5227 OE1 GLN D 100 3760 4075 3716 385 -187 385 O ATOM 5228 NE2 GLN D 100 20.884 40.816 13.801 1.00 30.09 N ANISOU 5228 NE2 GLN D 100 3789 4047 3596 396 -185 408 N ATOM 5229 N TYR D 101 27.052 41.812 10.816 1.00 29.75 N ANISOU 5229 N TYR D 101 3218 4185 3899 362 98 109 N ATOM 5230 CA TYR D 101 28.257 42.509 10.464 1.00 30.12 C ANISOU 5230 CA TYR D 101 3114 4260 4071 309 199 58 C ATOM 5231 C TYR D 101 27.955 43.984 10.650 1.00 29.71 C ANISOU 5231 C TYR D 101 3106 4206 3976 216 193 156 C ATOM 5232 O TYR D 101 26.955 44.498 10.122 1.00 29.33 O ANISOU 5232 O TYR D 101 3194 4168 3781 162 220 244 O ATOM 5233 CB TYR D 101 28.613 42.168 9.028 1.00 30.90 C ANISOU 5233 CB TYR D 101 3202 4416 4124 260 407 -3 C ATOM 5234 CG TYR D 101 28.677 40.666 8.790 1.00 30.26 C ANISOU 5234 CG TYR D 101 3122 4319 4057 360 411 -99 C ATOM 5235 CD1 TYR D 101 29.895 39.976 8.877 1.00 29.09 C ANISOU 5235 CD1 TYR D 101 2781 4151 4120 437 450 -240 C ATOM 5236 CD2 TYR D 101 27.513 39.931 8.497 1.00 26.72 C ANISOU 5236 CD2 TYR D 101 2857 3861 3435 381 360 -52 C ATOM 5237 CE1 TYR D 101 29.955 38.602 8.666 1.00 29.26 C ANISOU 5237 CE1 TYR D 101 2814 4138 4166 541 443 -335 C ATOM 5238 CE2 TYR D 101 27.563 38.565 8.284 1.00 26.18 C ANISOU 5238 CE2 TYR D 101 2811 3764 3372 466 352 -138 C ATOM 5239 CZ TYR D 101 28.787 37.894 8.365 1.00 29.00 C ANISOU 5239 CZ TYR D 101 2996 4095 3926 552 396 -282 C ATOM 5240 OH TYR D 101 28.843 36.516 8.146 1.00 29.57 O ANISOU 5240 OH TYR D 101 3100 4119 4015 649 380 -377 O ATOM 5241 N PHE D 102 28.793 44.651 11.440 1.00 29.66 N ANISOU 5241 N PHE D 102 2991 4168 4112 204 127 140 N ATOM 5242 CA PHE D 102 28.510 46.005 11.877 1.00 28.87 C ANISOU 5242 CA PHE D 102 2951 4037 3981 133 83 225 C ATOM 5243 C PHE D 102 29.322 47.013 11.097 1.00 30.22 C ANISOU 5243 C PHE D 102 3038 4242 4204 9 215 227 C ATOM 5244 O PHE D 102 30.405 46.701 10.618 1.00 31.89 O ANISOU 5244 O PHE D 102 3085 4488 4542 -15 322 140 O ATOM 5245 CB PHE D 102 28.778 46.139 13.369 1.00 28.43 C ANISOU 5245 CB PHE D 102 2892 3899 4013 182 -103 217 C ATOM 5246 CG PHE D 102 27.763 45.437 14.236 1.00 27.01 C ANISOU 5246 CG PHE D 102 2863 3668 3730 263 -213 241 C ATOM 5247 CD1 PHE D 102 27.939 44.096 14.598 1.00 25.23 C ANISOU 5247 CD1 PHE D 102 2630 3420 3538 350 -294 181 C ATOM 5248 CD2 PHE D 102 26.615 46.124 14.698 1.00 24.93 C ANISOU 5248 CD2 PHE D 102 2754 3369 3350 248 -225 317 C ATOM 5249 CE1 PHE D 102 26.992 43.450 15.399 1.00 23.29 C ANISOU 5249 CE1 PHE D 102 2547 3121 3182 397 -379 208 C ATOM 5250 CE2 PHE D 102 25.671 45.491 15.510 1.00 21.68 C ANISOU 5250 CE2 PHE D 102 2475 2909 2852 302 -282 329 C ATOM 5251 CZ PHE D 102 25.860 44.154 15.866 1.00 21.99 C ANISOU 5251 CZ PHE D 102 2526 2930 2898 364 -357 280 C ATOM 5252 N GLY D 103 28.774 48.212 10.938 1.00 29.87 N ANISOU 5252 N GLY D 103 3105 4177 4067 -73 219 322 N ATOM 5253 CA GLY D 103 29.501 49.295 10.309 1.00 31.61 C ANISOU 5253 CA GLY D 103 3283 4408 4320 -215 326 342 C ATOM 5254 C GLY D 103 30.372 49.992 11.342 1.00 32.93 C ANISOU 5254 C GLY D 103 3337 4521 4654 -236 217 324 C ATOM 5255 O GLY D 103 30.369 49.614 12.524 1.00 32.55 O ANISOU 5255 O GLY D 103 3276 4420 4672 -139 50 298 O ATOM 5256 N PRO D 104 31.106 51.034 10.916 1.00 34.48 N ANISOU 5256 N PRO D 104 3480 4716 4906 -379 299 343 N ATOM 5257 CA PRO D 104 32.058 51.707 11.794 1.00 35.73 C ANISOU 5257 CA PRO D 104 3514 4816 5246 -422 189 322 C ATOM 5258 C PRO D 104 31.414 52.656 12.818 1.00 35.15 C ANISOU 5258 C PRO D 104 3606 4641 5107 -409 7 399 C ATOM 5259 O PRO D 104 32.121 53.238 13.652 1.00 36.20 O ANISOU 5259 O PRO D 104 3683 4705 5367 -446 -120 387 O ATOM 5260 CB PRO D 104 32.934 52.488 10.814 1.00 37.49 C ANISOU 5260 CB PRO D 104 3644 5073 5527 -605 376 323 C ATOM 5261 CG PRO D 104 32.051 52.763 9.656 1.00 37.01 C ANISOU 5261 CG PRO D 104 3791 5041 5229 -673 515 401 C ATOM 5262 CD PRO D 104 31.024 51.673 9.590 1.00 35.28 C ANISOU 5262 CD PRO D 104 3671 4850 4884 -526 481 396 C ATOM 5263 N GLY D 105 30.098 52.811 12.757 1.00 33.77 N ANISOU 5263 N GLY D 105 3630 4447 4754 -358 -5 467 N ATOM 5264 CA GLY D 105 29.408 53.715 13.657 1.00 33.96 C ANISOU 5264 CA GLY D 105 3813 4367 4724 -336 -134 521 C ATOM 5265 C GLY D 105 29.429 55.158 13.194 1.00 35.51 C ANISOU 5265 C GLY D 105 4091 4509 4893 -464 -110 596 C ATOM 5266 O GLY D 105 30.360 55.591 12.513 1.00 36.96 O ANISOU 5266 O GLY D 105 4183 4722 5140 -599 -26 599 O ATOM 5267 N THR D 106 28.387 55.898 13.575 1.00 35.60 N ANISOU 5267 N THR D 106 4275 4430 4821 -422 -177 652 N ATOM 5268 CA THR D 106 28.233 57.311 13.249 1.00 37.07 C ANISOU 5268 CA THR D 106 4576 4529 4981 -519 -194 728 C ATOM 5269 C THR D 106 27.952 58.093 14.523 1.00 37.46 C ANISOU 5269 C THR D 106 4739 4444 5049 -471 -324 718 C ATOM 5270 O THR D 106 26.977 57.808 15.225 1.00 36.60 O ANISOU 5270 O THR D 106 4716 4294 4898 -344 -353 696 O ATOM 5271 CB THR D 106 27.040 57.501 12.296 1.00 36.80 C ANISOU 5271 CB THR D 106 4663 4482 4836 -500 -157 805 C ATOM 5272 OG1 THR D 106 27.340 56.895 11.032 1.00 37.99 O ANISOU 5272 OG1 THR D 106 4768 4736 4929 -576 -36 818 O ATOM 5273 CG2 THR D 106 26.725 58.972 12.097 1.00 37.46 C ANISOU 5273 CG2 THR D 106 4895 4437 4902 -572 -221 885 C ATOM 5274 N ARG D 107 28.796 59.070 14.838 1.00 39.14 N ANISOU 5274 N ARG D 107 4963 4583 5324 -582 -389 726 N ATOM 5275 CA ARG D 107 28.500 59.920 15.991 1.00 40.22 C ANISOU 5275 CA ARG D 107 5255 4570 5455 -548 -510 714 C ATOM 5276 C ARG D 107 27.644 61.103 15.577 1.00 40.36 C ANISOU 5276 C ARG D 107 5431 4479 5425 -558 -512 784 C ATOM 5277 O ARG D 107 27.973 61.818 14.625 1.00 41.18 O ANISOU 5277 O ARG D 107 5544 4575 5528 -685 -490 855 O ATOM 5278 CB ARG D 107 29.756 60.459 16.663 1.00 41.98 C ANISOU 5278 CB ARG D 107 5445 4731 5774 -660 -625 689 C ATOM 5279 CG ARG D 107 30.975 59.577 16.612 1.00 44.92 C ANISOU 5279 CG ARG D 107 5591 5203 6272 -709 -633 640 C ATOM 5280 CD ARG D 107 32.146 60.402 17.109 1.00 50.75 C ANISOU 5280 CD ARG D 107 6289 5854 7138 -848 -765 635 C ATOM 5281 NE ARG D 107 33.432 59.748 16.906 1.00 54.46 N ANISOU 5281 NE ARG D 107 6487 6408 7799 -918 -769 588 N ATOM 5282 CZ ARG D 107 34.013 58.940 17.788 1.00 55.65 C ANISOU 5282 CZ ARG D 107 6545 6541 8057 -856 -920 519 C ATOM 5283 NH1 ARG D 107 33.414 58.662 18.947 1.00 54.32 N ANISOU 5283 NH1 ARG D 107 6578 6281 7779 -743 -1067 495 N ATOM 5284 NH2 ARG D 107 35.197 58.409 17.499 1.00 57.32 N ANISOU 5284 NH2 ARG D 107 6469 6816 8494 -914 -921 470 N ATOM 5285 N LEU D 108 26.556 61.307 16.315 1.00 39.68 N ANISOU 5285 N LEU D 108 5476 4295 5305 -428 -536 758 N ATOM 5286 CA LEU D 108 25.689 62.470 16.148 1.00 39.83 C ANISOU 5286 CA LEU D 108 5639 4170 5323 -402 -564 801 C ATOM 5287 C LEU D 108 25.630 63.280 17.435 1.00 40.20 C ANISOU 5287 C LEU D 108 5845 4052 5376 -369 -634 741 C ATOM 5288 O LEU D 108 25.575 62.713 18.529 1.00 40.08 O ANISOU 5288 O LEU D 108 5869 4028 5330 -300 -629 658 O ATOM 5289 CB LEU D 108 24.276 62.039 15.738 1.00 39.02 C ANISOU 5289 CB LEU D 108 5530 4078 5219 -263 -505 812 C ATOM 5290 CG LEU D 108 23.132 63.054 15.886 1.00 40.31 C ANISOU 5290 CG LEU D 108 5812 4067 5438 -169 -541 819 C ATOM 5291 CD1 LEU D 108 23.262 64.229 14.893 1.00 41.54 C ANISOU 5291 CD1 LEU D 108 6050 4125 5608 -272 -633 923 C ATOM 5292 CD2 LEU D 108 21.769 62.361 15.762 1.00 39.97 C ANISOU 5292 CD2 LEU D 108 5700 4044 5442 -17 -479 799 C ATOM 5293 N LEU D 109 25.657 64.603 17.292 1.00 40.88 N ANISOU 5293 N LEU D 109 6054 3994 5486 -430 -704 782 N ATOM 5294 CA LEU D 109 25.397 65.515 18.396 1.00 41.26 C ANISOU 5294 CA LEU D 109 6292 3852 5534 -385 -761 722 C ATOM 5295 C LEU D 109 24.295 66.480 17.998 1.00 42.03 C ANISOU 5295 C LEU D 109 6487 3800 5683 -302 -765 749 C ATOM 5296 O LEU D 109 24.392 67.154 16.963 1.00 42.79 O ANISOU 5296 O LEU D 109 6590 3864 5803 -386 -825 848 O ATOM 5297 CB LEU D 109 26.657 66.299 18.751 1.00 42.41 C ANISOU 5297 CB LEU D 109 6506 3923 5683 -550 -885 734 C ATOM 5298 CG LEU D 109 26.602 67.343 19.870 1.00 42.83 C ANISOU 5298 CG LEU D 109 6797 3759 5717 -541 -971 673 C ATOM 5299 CD1 LEU D 109 26.807 66.705 21.234 1.00 42.54 C ANISOU 5299 CD1 LEU D 109 6849 3704 5609 -499 -989 569 C ATOM 5300 CD2 LEU D 109 27.669 68.379 19.624 1.00 43.38 C ANISOU 5300 CD2 LEU D 109 6914 3746 5821 -731 -1105 736 C ATOM 5301 N VAL D 110 23.251 66.546 18.817 1.00 41.93 N ANISOU 5301 N VAL D 110 6554 3684 5695 -143 -699 659 N ATOM 5302 CA VAL D 110 22.173 67.491 18.591 1.00 43.07 C ANISOU 5302 CA VAL D 110 6769 3654 5941 -36 -710 660 C ATOM 5303 C VAL D 110 22.228 68.592 19.651 1.00 45.01 C ANISOU 5303 C VAL D 110 7234 3681 6185 -20 -742 577 C ATOM 5304 O VAL D 110 22.197 68.317 20.855 1.00 45.42 O ANISOU 5304 O VAL D 110 7387 3698 6172 23 -662 462 O ATOM 5305 CB VAL D 110 20.817 66.784 18.570 1.00 42.47 C ANISOU 5305 CB VAL D 110 6577 3608 5950 142 -587 610 C ATOM 5306 CG1 VAL D 110 19.718 67.727 18.121 1.00 44.33 C ANISOU 5306 CG1 VAL D 110 6829 3662 6354 258 -634 622 C ATOM 5307 CG2 VAL D 110 20.874 65.599 17.634 1.00 40.89 C ANISOU 5307 CG2 VAL D 110 6193 3622 5722 111 -567 683 C ATOM 5308 N LEU D 111 22.343 69.835 19.194 1.00 46.58 N ANISOU 5308 N LEU D 111 7541 3721 6437 -72 -866 637 N ATOM 5309 CA LEU D 111 22.463 70.989 20.082 1.00 48.64 C ANISOU 5309 CA LEU D 111 8033 3752 6695 -72 -920 565 C ATOM 5310 C LEU D 111 21.210 71.849 20.049 1.00 50.64 C ANISOU 5310 C LEU D 111 8348 3790 7101 102 -904 517 C ATOM 5311 O LEU D 111 20.492 71.874 19.040 1.00 50.69 O ANISOU 5311 O LEU D 111 8233 3798 7228 169 -944 591 O ATOM 5312 CB LEU D 111 23.648 71.855 19.665 1.00 49.43 C ANISOU 5312 CB LEU D 111 8227 3799 6754 -280 -1093 666 C ATOM 5313 CG LEU D 111 25.066 71.290 19.750 1.00 48.49 C ANISOU 5313 CG LEU D 111 8040 3842 6542 -473 -1138 704 C ATOM 5314 CD1 LEU D 111 26.017 72.182 18.950 1.00 47.77 C ANISOU 5314 CD1 LEU D 111 7983 3705 6461 -686 -1275 825 C ATOM 5315 CD2 LEU D 111 25.518 71.134 21.210 1.00 48.19 C ANISOU 5315 CD2 LEU D 111 8141 3747 6422 -477 -1146 586 C ATOM 5316 N GLU D 112 20.952 72.558 21.149 1.00 52.60 N ANISOU 5316 N GLU D 112 8795 3837 7353 175 -859 386 N ATOM 5317 CA GLU D 112 19.835 73.513 21.203 1.00 55.01 C ANISOU 5317 CA GLU D 112 9164 3899 7839 351 -842 316 C ATOM 5318 C GLU D 112 19.989 74.521 20.072 1.00 55.50 C ANISOU 5318 C GLU D 112 9257 3842 7987 285 -1068 460 C ATOM 5319 O GLU D 112 19.053 74.762 19.326 1.00 56.16 O ANISOU 5319 O GLU D 112 9242 3845 8251 408 -1119 496 O ATOM 5320 CB GLU D 112 19.771 74.247 22.558 1.00 57.30 C ANISOU 5320 CB GLU D 112 9719 3968 8085 402 -761 149 C ATOM 5321 CG GLU D 112 20.158 73.402 23.791 1.00 58.50 C ANISOU 5321 CG GLU D 112 9973 4213 8040 360 -607 37 C ATOM 5322 CD GLU D 112 19.028 72.502 24.307 1.00 60.97 C ANISOU 5322 CD GLU D 112 10174 4586 8406 526 -332 -91 C ATOM 5323 OE1 GLU D 112 17.869 72.622 23.837 1.00 62.66 O ANISOU 5323 OE1 GLU D 112 10217 4745 8846 697 -245 -120 O ATOM 5324 OE2 GLU D 112 19.301 71.668 25.200 1.00 61.65 O ANISOU 5324 OE2 GLU D 112 10348 4763 8315 477 -212 -162 O ATOM 5325 N ASP D 113 21.191 75.079 19.942 1.00 55.58 N ANISOU 5325 N ASP D 113 9410 3836 7873 76 -1217 546 N ATOM 5326 CA ASP D 113 21.480 76.119 18.955 1.00 56.63 C ANISOU 5326 CA ASP D 113 9636 3835 8047 -33 -1429 687 C ATOM 5327 C ASP D 113 22.888 75.972 18.363 1.00 55.32 C ANISOU 5327 C ASP D 113 9462 3825 7731 -314 -1519 826 C ATOM 5328 O ASP D 113 23.755 75.335 18.967 1.00 54.45 O ANISOU 5328 O ASP D 113 9313 3866 7511 -414 -1456 790 O ATOM 5329 CB ASP D 113 21.319 77.506 19.587 1.00 59.18 C ANISOU 5329 CB ASP D 113 10216 3837 8431 15 -1519 612 C ATOM 5330 CG ASP D 113 21.109 78.593 18.554 1.00 61.85 C ANISOU 5330 CG ASP D 113 10652 3977 8873 -16 -1738 740 C ATOM 5331 OD1 ASP D 113 21.107 79.789 18.928 1.00 65.21 O ANISOU 5331 OD1 ASP D 113 11305 4127 9344 -4 -1848 702 O ATOM 5332 OD2 ASP D 113 20.943 78.251 17.359 1.00 62.35 O ANISOU 5332 OD2 ASP D 113 10591 4141 8958 -60 -1811 880 O ATOM 5333 N LEU D 114 23.106 76.569 17.192 1.00 62.69 N ANISOU 5333 N LEU D 114 5623 7757 10439 1495 1540 -763 N ATOM 5334 CA LEU D 114 24.373 76.452 16.475 1.00 58.35 C ANISOU 5334 CA LEU D 114 5412 7062 9695 1354 1294 -663 C ATOM 5335 C LEU D 114 25.248 77.696 16.550 1.00 57.90 C ANISOU 5335 C LEU D 114 5623 6777 9598 1477 1234 -800 C ATOM 5336 O LEU D 114 26.319 77.737 15.944 1.00 55.34 O ANISOU 5336 O LEU D 114 5560 6321 9144 1372 1046 -711 O ATOM 5337 CB LEU D 114 24.120 76.113 15.005 1.00 57.19 C ANISOU 5337 CB LEU D 114 5180 6844 9704 1301 965 -470 C ATOM 5338 CG LEU D 114 23.436 74.792 14.668 1.00 56.74 C ANISOU 5338 CG LEU D 114 4881 6957 9722 1129 930 -349 C ATOM 5339 CD1 LEU D 114 23.259 74.688 13.175 1.00 56.19 C ANISOU 5339 CD1 LEU D 114 4755 6825 9768 1125 560 -229 C ATOM 5340 CD2 LEU D 114 24.208 73.596 15.195 1.00 53.96 C ANISOU 5340 CD2 LEU D 114 4692 6706 9103 879 1051 -288 C ATOM 5341 N ARG D 115 24.793 78.702 17.291 1.00 60.74 N ANISOU 5341 N ARG D 115 5902 7082 10096 1697 1401 -1028 N ATOM 5342 CA ARG D 115 25.474 79.996 17.375 1.00 61.37 C ANISOU 5342 CA ARG D 115 6186 6883 10250 1831 1343 -1200 C ATOM 5343 C ARG D 115 26.966 79.879 17.724 1.00 58.96 C ANISOU 5343 C ARG D 115 6229 6547 9626 1656 1317 -1252 C ATOM 5344 O ARG D 115 27.787 80.673 17.254 1.00 58.51 O ANISOU 5344 O ARG D 115 6364 6215 9654 1661 1155 -1257 O ATOM 5345 CB ARG D 115 24.758 80.919 18.374 1.00 65.25 C ANISOU 5345 CB ARG D 115 6527 7362 10904 2087 1580 -1518 C ATOM 5346 CG ARG D 115 24.955 80.532 19.839 1.00 66.10 C ANISOU 5346 CG ARG D 115 6686 7761 10668 2054 1890 -1752 C ATOM 5347 CD ARG D 115 23.996 81.236 20.803 1.00 70.74 C ANISOU 5347 CD ARG D 115 7054 8437 11386 2325 2169 -2067 C ATOM 5348 NE ARG D 115 24.249 80.813 22.184 1.00 71.35 N ANISOU 5348 NE ARG D 115 7205 8859 11045 2297 2464 -2266 N ATOM 5349 CZ ARG D 115 23.775 79.698 22.745 1.00 70.96 C ANISOU 5349 CZ ARG D 115 7014 9188 10759 2196 2697 -2117 C ATOM 5350 NH1 ARG D 115 22.993 78.865 22.063 1.00 69.71 N ANISOU 5350 NH1 ARG D 115 6610 9092 10786 2095 2668 -1807 N ATOM 5351 NH2 ARG D 115 24.086 79.414 24.001 1.00 71.93 N ANISOU 5351 NH2 ARG D 115 7234 9633 10463 2197 2957 -2273 N ATOM 5352 N ASN D 116 27.314 78.879 18.528 1.00 57.74 N ANISOU 5352 N ASN D 116 6136 6671 9131 1500 1473 -1262 N ATOM 5353 CA ASN D 116 28.663 78.769 19.058 1.00 56.17 C ANISOU 5353 CA ASN D 116 6228 6494 8621 1366 1465 -1346 C ATOM 5354 C ASN D 116 29.650 78.017 18.176 1.00 52.46 C ANISOU 5354 C ASN D 116 5934 5980 8018 1143 1254 -1092 C ATOM 5355 O ASN D 116 30.853 78.081 18.419 1.00 51.42 O ANISOU 5355 O ASN D 116 6031 5812 7696 1042 1201 -1149 O ATOM 5356 CB ASN D 116 28.636 78.161 20.463 1.00 57.64 C ANISOU 5356 CB ASN D 116 6412 7020 8468 1348 1738 -1481 C ATOM 5357 CG ASN D 116 28.585 79.222 21.563 1.00 62.01 C ANISOU 5357 CG ASN D 116 6988 7588 8984 1548 1902 -1877 C ATOM 5358 OD1 ASN D 116 27.526 79.484 22.152 1.00 65.32 O ANISOU 5358 OD1 ASN D 116 7196 8139 9484 1727 2122 -2023 O ATOM 5359 ND2 ASN D 116 29.737 79.840 21.844 1.00 62.66 N ANISOU 5359 ND2 ASN D 116 7310 7540 8957 1518 1794 -2079 N ATOM 5360 N VAL D 117 29.150 77.319 17.155 1.00 51.00 N ANISOU 5360 N VAL D 117 5628 5809 7939 1074 1129 -841 N ATOM 5361 CA VAL D 117 29.992 76.488 16.292 1.00 47.27 C ANISOU 5361 CA VAL D 117 5300 5331 7329 879 947 -627 C ATOM 5362 C VAL D 117 31.139 77.306 15.700 1.00 46.07 C ANISOU 5362 C VAL D 117 5375 4944 7184 862 778 -618 C ATOM 5363 O VAL D 117 30.931 78.390 15.150 1.00 47.46 O ANISOU 5363 O VAL D 117 5533 4895 7604 996 685 -619 O ATOM 5364 CB VAL D 117 29.174 75.809 15.172 1.00 46.96 C ANISOU 5364 CB VAL D 117 5077 5326 7441 847 800 -426 C ATOM 5365 CG1 VAL D 117 30.091 75.066 14.215 1.00 44.47 C ANISOU 5365 CG1 VAL D 117 4923 4997 6975 678 607 -259 C ATOM 5366 CG2 VAL D 117 28.149 74.852 15.759 1.00 47.48 C ANISOU 5366 CG2 VAL D 117 4897 5606 7536 808 974 -413 C ATOM 5367 N THR D 118 32.353 76.786 15.852 1.00 43.65 N ANISOU 5367 N THR D 118 5266 4684 6634 701 751 -593 N ATOM 5368 CA THR D 118 33.563 77.441 15.373 1.00 42.41 C ANISOU 5368 CA THR D 118 5304 4331 6478 647 621 -574 C ATOM 5369 C THR D 118 34.534 76.370 14.893 1.00 39.67 C ANISOU 5369 C THR D 118 5078 4089 5906 461 537 -413 C ATOM 5370 O THR D 118 34.734 75.369 15.578 1.00 38.83 O ANISOU 5370 O THR D 118 4986 4177 5590 371 624 -428 O ATOM 5371 CB THR D 118 34.259 78.255 16.493 1.00 43.54 C ANISOU 5371 CB THR D 118 5557 4405 6582 673 709 -848 C ATOM 5372 OG1 THR D 118 33.306 79.090 17.159 1.00 46.15 O ANISOU 5372 OG1 THR D 118 5764 4683 7088 861 829 -1064 O ATOM 5373 CG2 THR D 118 35.385 79.124 15.920 1.00 43.38 C ANISOU 5373 CG2 THR D 118 5683 4115 6685 617 574 -826 C ATOM 5374 N PRO D 119 35.148 76.577 13.717 1.00 38.69 N ANISOU 5374 N PRO D 119 5036 3840 5823 417 380 -246 N ATOM 5375 CA PRO D 119 36.180 75.648 13.284 1.00 36.35 C ANISOU 5375 CA PRO D 119 4854 3637 5319 261 317 -134 C ATOM 5376 C PRO D 119 37.471 75.915 14.048 1.00 36.02 C ANISOU 5376 C PRO D 119 4954 3563 5170 177 356 -253 C ATOM 5377 O PRO D 119 37.647 77.001 14.594 1.00 37.57 O ANISOU 5377 O PRO D 119 5175 3610 5490 232 387 -408 O ATOM 5378 CB PRO D 119 36.359 75.999 11.813 1.00 36.47 C ANISOU 5378 CB PRO D 119 4899 3553 5406 277 164 69 C ATOM 5379 CG PRO D 119 36.006 77.436 11.723 1.00 38.30 C ANISOU 5379 CG PRO D 119 5107 3554 5893 411 155 62 C ATOM 5380 CD PRO D 119 34.961 77.688 12.762 1.00 39.87 C ANISOU 5380 CD PRO D 119 5178 3765 6206 523 270 -135 C ATOM 5381 N PRO D 120 38.375 74.932 14.094 1.00 34.48 N ANISOU 5381 N PRO D 120 4834 3495 4770 51 342 -202 N ATOM 5382 CA PRO D 120 39.608 75.111 14.855 1.00 34.61 C ANISOU 5382 CA PRO D 120 4954 3516 4680 -23 354 -320 C ATOM 5383 C PRO D 120 40.704 75.891 14.117 1.00 34.98 C ANISOU 5383 C PRO D 120 5073 3382 4836 -85 267 -262 C ATOM 5384 O PRO D 120 40.645 76.054 12.894 1.00 34.97 O ANISOU 5384 O PRO D 120 5070 3298 4919 -80 206 -71 O ATOM 5385 CB PRO D 120 40.059 73.670 15.094 1.00 32.91 C ANISOU 5385 CB PRO D 120 4762 3503 4239 -111 366 -244 C ATOM 5386 CG PRO D 120 39.561 72.939 13.908 1.00 31.69 C ANISOU 5386 CG PRO D 120 4560 3358 4122 -124 307 -69 C ATOM 5387 CD PRO D 120 38.242 73.559 13.578 1.00 32.79 C ANISOU 5387 CD PRO D 120 4593 3429 4436 -15 312 -68 C ATOM 5388 N LYS D 121 41.686 76.373 14.875 1.00 35.86 N ANISOU 5388 N LYS D 121 5234 3450 4940 -143 264 -423 N ATOM 5389 CA LYS D 121 42.918 76.917 14.314 1.00 36.43 C ANISOU 5389 CA LYS D 121 5347 3376 5119 -245 200 -364 C ATOM 5390 C LYS D 121 44.064 75.947 14.632 1.00 35.08 C ANISOU 5390 C LYS D 121 5205 3390 4732 -352 174 -364 C ATOM 5391 O LYS D 121 44.220 75.513 15.772 1.00 35.96 O ANISOU 5391 O LYS D 121 5325 3662 4675 -348 186 -524 O ATOM 5392 CB LYS D 121 43.179 78.329 14.852 1.00 38.67 C ANISOU 5392 CB LYS D 121 5625 3414 5655 -240 190 -569 C ATOM 5393 CG LYS D 121 42.437 79.414 14.052 1.00 42.14 C ANISOU 5393 CG LYS D 121 6035 3572 6405 -152 193 -454 C ATOM 5394 CD LYS D 121 42.243 80.722 14.833 1.00 48.05 C ANISOU 5394 CD LYS D 121 6759 4058 7438 -92 202 -731 C ATOM 5395 CE LYS D 121 41.106 80.597 15.884 1.00 50.10 C ANISOU 5395 CE LYS D 121 6984 4460 7593 56 275 -985 C ATOM 5396 NZ LYS D 121 41.282 81.508 17.070 1.00 51.99 N ANISOU 5396 NZ LYS D 121 7220 4584 7951 93 284 -1393 N ATOM 5397 N VAL D 122 44.853 75.586 13.630 1.00 33.68 N ANISOU 5397 N VAL D 122 5037 3215 4545 -427 144 -175 N ATOM 5398 CA VAL D 122 45.820 74.512 13.808 1.00 32.24 C ANISOU 5398 CA VAL D 122 4861 3212 4175 -496 124 -154 C ATOM 5399 C VAL D 122 47.244 75.032 13.699 1.00 33.25 C ANISOU 5399 C VAL D 122 4963 3264 4405 -606 87 -171 C ATOM 5400 O VAL D 122 47.559 75.812 12.799 1.00 34.32 O ANISOU 5400 O VAL D 122 5081 3235 4724 -650 101 -47 O ATOM 5401 CB VAL D 122 45.568 73.358 12.802 1.00 30.52 C ANISOU 5401 CB VAL D 122 4649 3109 3837 -479 131 34 C ATOM 5402 CG1 VAL D 122 46.541 72.218 13.007 1.00 29.44 C ANISOU 5402 CG1 VAL D 122 4511 3122 3552 -526 114 46 C ATOM 5403 CG2 VAL D 122 44.161 72.846 12.943 1.00 29.88 C ANISOU 5403 CG2 VAL D 122 4555 3086 3713 -396 156 35 C ATOM 5404 N SER D 123 48.097 74.609 14.631 1.00 33.45 N ANISOU 5404 N SER D 123 4970 3420 4321 -649 39 -305 N ATOM 5405 CA SER D 123 49.509 74.993 14.627 1.00 34.45 C ANISOU 5405 CA SER D 123 5027 3504 4558 -762 -12 -345 C ATOM 5406 C SER D 123 50.362 73.759 14.780 1.00 33.54 C ANISOU 5406 C SER D 123 4883 3604 4255 -772 -45 -295 C ATOM 5407 O SER D 123 49.986 72.830 15.488 1.00 32.94 O ANISOU 5407 O SER D 123 4846 3699 3970 -698 -58 -319 O ATOM 5408 CB SER D 123 49.826 75.978 15.750 1.00 36.45 C ANISOU 5408 CB SER D 123 5248 3677 4925 -800 -88 -633 C ATOM 5409 OG SER D 123 49.064 77.161 15.614 1.00 37.77 O ANISOU 5409 OG SER D 123 5432 3595 5324 -778 -55 -698 O ATOM 5410 N LEU D 124 51.507 73.751 14.106 1.00 33.89 N ANISOU 5410 N LEU D 124 4846 3634 4397 -855 -45 -204 N ATOM 5411 CA LEU D 124 52.444 72.651 14.208 1.00 33.28 C ANISOU 5411 CA LEU D 124 4712 3738 4194 -850 -79 -166 C ATOM 5412 C LEU D 124 53.701 73.165 14.853 1.00 35.40 C ANISOU 5412 C LEU D 124 4853 4018 4580 -944 -176 -310 C ATOM 5413 O LEU D 124 54.229 74.206 14.460 1.00 37.33 O ANISOU 5413 O LEU D 124 5015 4096 5074 -1057 -162 -325 O ATOM 5414 CB LEU D 124 52.755 72.067 12.834 1.00 32.34 C ANISOU 5414 CB LEU D 124 4573 3641 4075 -845 12 38 C ATOM 5415 CG LEU D 124 53.724 70.880 12.793 1.00 31.52 C ANISOU 5415 CG LEU D 124 4396 3698 3881 -814 -4 73 C ATOM 5416 CD1 LEU D 124 53.117 69.671 13.452 1.00 29.35 C ANISOU 5416 CD1 LEU D 124 4196 3531 3426 -708 -44 62 C ATOM 5417 CD2 LEU D 124 54.101 70.557 11.364 1.00 31.53 C ANISOU 5417 CD2 LEU D 124 4364 3720 3895 -807 106 225 C ATOM 5418 N PHE D 125 54.179 72.438 15.854 1.00 36.00 N ANISOU 5418 N PHE D 125 4900 4286 4492 -898 -284 -405 N ATOM 5419 CA PHE D 125 55.337 72.875 16.622 1.00 38.15 C ANISOU 5419 CA PHE D 125 5033 4615 4847 -972 -426 -585 C ATOM 5420 C PHE D 125 56.539 71.983 16.329 1.00 38.31 C ANISOU 5420 C PHE D 125 4917 4772 4867 -968 -456 -478 C ATOM 5421 O PHE D 125 56.487 70.773 16.533 1.00 37.60 O ANISOU 5421 O PHE D 125 4866 4837 4582 -851 -467 -378 O ATOM 5422 CB PHE D 125 54.988 72.943 18.115 1.00 39.23 C ANISOU 5422 CB PHE D 125 5225 4903 4778 -903 -558 -811 C ATOM 5423 CG PHE D 125 53.975 74.003 18.438 1.00 39.60 C ANISOU 5423 CG PHE D 125 5363 4803 4879 -906 -526 -981 C ATOM 5424 CD1 PHE D 125 52.611 73.726 18.383 1.00 36.93 C ANISOU 5424 CD1 PHE D 125 5167 4460 4403 -804 -409 -896 C ATOM 5425 CD2 PHE D 125 54.380 75.295 18.758 1.00 42.21 C ANISOU 5425 CD2 PHE D 125 5613 4973 5450 -1012 -612 -1239 C ATOM 5426 CE1 PHE D 125 51.665 74.716 18.659 1.00 36.49 C ANISOU 5426 CE1 PHE D 125 5173 4265 4426 -784 -370 -1059 C ATOM 5427 CE2 PHE D 125 53.438 76.286 19.033 1.00 42.70 C ANISOU 5427 CE2 PHE D 125 5753 4864 5606 -994 -577 -1417 C ATOM 5428 CZ PHE D 125 52.075 75.986 18.983 1.00 39.50 C ANISOU 5428 CZ PHE D 125 5490 4479 5038 -868 -451 -1321 C ATOM 5429 N GLU D 126 57.604 72.600 15.828 1.00 39.69 N ANISOU 5429 N GLU D 126 4916 4866 5298 -1096 -455 -488 N ATOM 5430 CA GLU D 126 58.799 71.895 15.381 1.00 40.18 C ANISOU 5430 CA GLU D 126 4806 5042 5419 -1097 -449 -387 C ATOM 5431 C GLU D 126 59.614 71.337 16.563 1.00 40.89 C ANISOU 5431 C GLU D 126 4784 5349 5404 -1039 -660 -521 C ATOM 5432 O GLU D 126 59.819 72.033 17.565 1.00 43.02 O ANISOU 5432 O GLU D 126 5004 5651 5691 -1091 -831 -750 O ATOM 5433 CB GLU D 126 59.667 72.825 14.516 1.00 42.42 C ANISOU 5433 CB GLU D 126 4905 5179 6034 -1266 -357 -339 C ATOM 5434 CG GLU D 126 59.073 73.200 13.137 1.00 43.53 C ANISOU 5434 CG GLU D 126 5134 5164 6241 -1293 -130 -116 C ATOM 5435 CD GLU D 126 59.937 74.217 12.363 1.00 49.43 C ANISOU 5435 CD GLU D 126 5690 5762 7328 -1470 -16 -17 C ATOM 5436 OE1 GLU D 126 61.154 74.351 12.653 1.00 52.20 O ANISOU 5436 OE1 GLU D 126 5799 6158 7878 -1569 -79 -94 O ATOM 5437 OE2 GLU D 126 59.399 74.884 11.449 1.00 51.09 O ANISOU 5437 OE2 GLU D 126 5976 5813 7621 -1510 138 160 O ATOM 5438 N PRO D 127 60.087 70.082 16.442 1.00 39.49 N ANISOU 5438 N PRO D 127 4559 5323 5121 -915 -663 -388 N ATOM 5439 CA PRO D 127 60.825 69.400 17.501 1.00 40.39 C ANISOU 5439 CA PRO D 127 4571 5658 5117 -817 -867 -447 C ATOM 5440 C PRO D 127 62.029 70.152 18.042 1.00 42.65 C ANISOU 5440 C PRO D 127 4604 6013 5587 -929 -1052 -643 C ATOM 5441 O PRO D 127 62.731 70.822 17.296 1.00 43.24 O ANISOU 5441 O PRO D 127 4499 5969 5962 -1077 -977 -655 O ATOM 5442 CB PRO D 127 61.285 68.098 16.832 1.00 39.55 C ANISOU 5442 CB PRO D 127 4409 5606 5013 -689 -784 -248 C ATOM 5443 CG PRO D 127 60.996 68.258 15.393 1.00 38.34 C ANISOU 5443 CG PRO D 127 4291 5293 4985 -748 -545 -141 C ATOM 5444 CD PRO D 127 59.853 69.184 15.302 1.00 37.53 C ANISOU 5444 CD PRO D 127 4368 5042 4848 -835 -479 -182 C ATOM 5445 N SER D 128 62.248 70.009 19.346 1.00 43.99 N ANISOU 5445 N SER D 128 4753 6393 5567 -853 -1295 -787 N ATOM 5446 CA SER D 128 63.339 70.663 20.058 1.00 46.75 C ANISOU 5446 CA SER D 128 4856 6856 6052 -942 -1539 -1031 C ATOM 5447 C SER D 128 64.697 70.117 19.680 1.00 47.77 C ANISOU 5447 C SER D 128 4689 7078 6384 -930 -1588 -946 C ATOM 5448 O SER D 128 64.907 68.914 19.696 1.00 47.19 O ANISOU 5448 O SER D 128 4616 7140 6175 -748 -1594 -757 O ATOM 5449 CB SER D 128 63.148 70.513 21.561 1.00 48.61 C ANISOU 5449 CB SER D 128 5168 7365 5938 -817 -1797 -1196 C ATOM 5450 OG SER D 128 64.374 70.701 22.239 1.00 52.02 O ANISOU 5450 OG SER D 128 5328 7992 6447 -840 -2080 -1387 O ATOM 5451 N LYS D 129 65.617 71.029 19.374 1.00 49.87 N ANISOU 5451 N LYS D 129 4684 7254 7009 -1125 -1623 -1089 N ATOM 5452 CA LYS D 129 67.001 70.697 19.021 1.00 51.59 C ANISOU 5452 CA LYS D 129 4552 7564 7485 -1143 -1664 -1043 C ATOM 5453 C LYS D 129 67.712 69.996 20.186 1.00 53.76 C ANISOU 5453 C LYS D 129 4687 8160 7580 -978 -1994 -1126 C ATOM 5454 O LYS D 129 68.585 69.140 19.985 1.00 54.35 O ANISOU 5454 O LYS D 129 4554 8364 7732 -860 -2020 -992 O ATOM 5455 CB LYS D 129 67.756 71.967 18.601 1.00 53.94 C ANISOU 5455 CB LYS D 129 4571 7686 8238 -1421 -1642 -1194 C ATOM 5456 N ALA D 130 67.310 70.374 21.399 1.00 54.99 N ANISOU 5456 N ALA D 130 4957 8456 7482 -952 -2242 -1349 N ATOM 5457 CA ALA D 130 67.786 69.753 22.628 1.00 57.38 C ANISOU 5457 CA ALA D 130 5186 9113 7502 -766 -2575 -1413 C ATOM 5458 C ALA D 130 67.289 68.316 22.754 1.00 55.30 C ANISOU 5458 C ALA D 130 5130 8972 6910 -490 -2505 -1078 C ATOM 5459 O ALA D 130 68.044 67.439 23.160 1.00 57.41 O ANISOU 5459 O ALA D 130 5243 9455 7115 -312 -2677 -958 O ATOM 5460 CB ALA D 130 67.374 70.582 23.837 1.00 59.44 C ANISOU 5460 CB ALA D 130 5548 9516 7522 -800 -2825 -1754 C ATOM 5461 N GLU D 131 66.032 68.068 22.397 1.00 51.72 N ANISOU 5461 N GLU D 131 5005 8361 6287 -455 -2259 -919 N ATOM 5462 CA GLU D 131 65.534 66.698 22.356 1.00 50.16 C ANISOU 5462 CA GLU D 131 4983 8197 5880 -230 -2155 -591 C ATOM 5463 C GLU D 131 66.333 65.870 21.355 1.00 49.71 C ANISOU 5463 C GLU D 131 4737 8043 6108 -167 -2031 -400 C ATOM 5464 O GLU D 131 66.955 64.875 21.732 1.00 51.59 O ANISOU 5464 O GLU D 131 4862 8432 6306 30 -2164 -247 O ATOM 5465 CB GLU D 131 64.046 66.642 22.027 1.00 46.85 C ANISOU 5465 CB GLU D 131 4901 7595 5303 -238 -1904 -482 C ATOM 5466 CG GLU D 131 63.475 65.239 22.096 1.00 46.04 C ANISOU 5466 CG GLU D 131 4968 7503 5021 -28 -1813 -159 C ATOM 5467 CD GLU D 131 62.197 65.066 21.282 1.00 44.67 C ANISOU 5467 CD GLU D 131 5038 7076 4857 -69 -1522 -41 C ATOM 5468 OE1 GLU D 131 61.723 66.044 20.650 1.00 43.53 O ANISOU 5468 OE1 GLU D 131 4947 6766 4827 -241 -1390 -187 O ATOM 5469 OE2 GLU D 131 61.660 63.934 21.273 1.00 44.57 O ANISOU 5469 OE2 GLU D 131 5154 7021 4761 73 -1435 206 O ATOM 5470 N ILE D 132 66.330 66.294 20.091 1.00 47.74 N ANISOU 5470 N ILE D 132 4445 7555 6138 -320 -1776 -407 N ATOM 5471 CA ILE D 132 67.104 65.625 19.047 1.00 47.55 C ANISOU 5471 CA ILE D 132 4229 7462 6375 -265 -1621 -274 C ATOM 5472 C ILE D 132 68.435 65.085 19.582 1.00 51.11 C ANISOU 5472 C ILE D 132 4356 8130 6935 -133 -1858 -272 C ATOM 5473 O ILE D 132 68.740 63.899 19.425 1.00 51.39 O ANISOU 5473 O ILE D 132 4347 8187 6991 80 -1837 -89 O ATOM 5474 CB ILE D 132 67.330 66.541 17.813 1.00 46.62 C ANISOU 5474 CB ILE D 132 3997 7163 6552 -486 -1380 -339 C ATOM 5475 CG1 ILE D 132 66.087 66.541 16.927 1.00 43.77 C ANISOU 5475 CG1 ILE D 132 3943 6596 6093 -516 -1104 -235 C ATOM 5476 CG2 ILE D 132 68.480 66.049 16.956 1.00 47.43 C ANISOU 5476 CG2 ILE D 132 3796 7294 6931 -439 -1266 -266 C ATOM 5477 CD1 ILE D 132 65.382 67.869 16.828 1.00 43.46 C ANISOU 5477 CD1 ILE D 132 4027 6412 6075 -728 -1043 -351 C ATOM 5478 N SER D 133 69.196 65.950 20.249 1.00 54.08 N ANISOU 5478 N SER D 133 4497 8655 7397 -252 -2101 -491 N ATOM 5479 CA SER D 133 70.568 65.635 20.625 1.00 57.98 C ANISOU 5479 CA SER D 133 4608 9357 8065 -165 -2334 -526 C ATOM 5480 C SER D 133 70.698 64.873 21.942 1.00 60.24 C ANISOU 5480 C SER D 133 4919 9926 8045 81 -2670 -455 C ATOM 5481 O SER D 133 71.795 64.446 22.301 1.00 63.26 O ANISOU 5481 O SER D 133 4990 10502 8543 209 -2892 -442 O ATOM 5482 CB SER D 133 71.421 66.909 20.648 1.00 60.72 C ANISOU 5482 CB SER D 133 4629 9725 8715 -426 -2451 -806 C ATOM 5483 OG SER D 133 70.940 67.826 21.613 1.00 61.85 O ANISOU 5483 OG SER D 133 4898 9933 8670 -542 -2670 -1053 O ATOM 5484 N HIS D 134 69.587 64.693 22.652 1.00 59.07 N ANISOU 5484 N HIS D 134 5126 9816 7503 160 -2699 -385 N ATOM 5485 CA HIS D 134 69.607 63.949 23.917 1.00 61.98 C ANISOU 5485 CA HIS D 134 5554 10477 7519 409 -2986 -252 C ATOM 5486 C HIS D 134 69.060 62.526 23.782 1.00 60.65 C ANISOU 5486 C HIS D 134 5590 10210 7244 657 -2837 133 C ATOM 5487 O HIS D 134 69.479 61.615 24.504 1.00 62.95 O ANISOU 5487 O HIS D 134 5819 10689 7410 908 -3039 346 O ATOM 5488 CB HIS D 134 68.837 64.707 25.001 1.00 62.80 C ANISOU 5488 CB HIS D 134 5877 10761 7223 353 -3144 -435 C ATOM 5489 CG HIS D 134 68.947 64.094 26.365 1.00 67.02 C ANISOU 5489 CG HIS D 134 6451 11677 7336 605 -3456 -313 C ATOM 5490 ND1 HIS D 134 70.122 64.087 27.087 1.00 72.61 N ANISOU 5490 ND1 HIS D 134 6849 12708 8033 705 -3837 -415 N ATOM 5491 CD2 HIS D 134 68.026 63.474 27.140 1.00 67.34 C ANISOU 5491 CD2 HIS D 134 6794 11850 6941 784 -3443 -74 C ATOM 5492 CE1 HIS D 134 69.921 63.485 28.246 1.00 75.76 C ANISOU 5492 CE1 HIS D 134 7375 13439 7971 951 -4055 -234 C ATOM 5493 NE2 HIS D 134 68.657 63.103 28.303 1.00 73.05 N ANISOU 5493 NE2 HIS D 134 7405 12984 7365 999 -3804 -11 N ATOM 5494 N THR D 135 68.135 62.353 22.843 1.00 57.16 N ANISOU 5494 N THR D 135 5377 9463 6878 584 -2496 222 N ATOM 5495 CA THR D 135 67.363 61.126 22.703 1.00 56.07 C ANISOU 5495 CA THR D 135 5471 9172 6662 765 -2335 539 C ATOM 5496 C THR D 135 67.612 60.458 21.365 1.00 55.00 C ANISOU 5496 C THR D 135 5254 8758 6885 794 -2082 609 C ATOM 5497 O THR D 135 67.434 59.242 21.228 1.00 55.22 O ANISOU 5497 O THR D 135 5352 8653 6976 991 -2012 849 O ATOM 5498 CB THR D 135 65.865 61.437 22.732 1.00 53.03 C ANISOU 5498 CB THR D 135 5441 8663 6045 657 -2148 552 C ATOM 5499 OG1 THR D 135 65.551 62.313 21.637 1.00 50.21 O ANISOU 5499 OG1 THR D 135 5105 8092 5879 423 -1924 349 O ATOM 5500 CG2 THR D 135 65.466 62.085 24.055 1.00 54.22 C ANISOU 5500 CG2 THR D 135 5707 9101 5794 648 -2353 460 C ATOM 5501 N GLN D 136 68.002 61.275 20.384 1.00 54.38 N ANISOU 5501 N GLN D 136 5029 8590 7043 599 -1938 395 N ATOM 5502 CA GLN D 136 68.054 60.896 18.966 1.00 53.01 C ANISOU 5502 CA GLN D 136 4821 8184 7136 588 -1641 405 C ATOM 5503 C GLN D 136 66.653 60.698 18.410 1.00 49.79 C ANISOU 5503 C GLN D 136 4758 7549 6610 538 -1404 468 C ATOM 5504 O GLN D 136 66.454 59.925 17.469 1.00 48.98 O ANISOU 5504 O GLN D 136 4702 7261 6648 618 -1204 525 O ATOM 5505 CB GLN D 136 68.948 59.671 18.713 1.00 55.18 C ANISOU 5505 CB GLN D 136 4886 8441 7639 840 -1657 537 C ATOM 5506 CG GLN D 136 70.388 59.811 19.237 1.00 60.16 C ANISOU 5506 CG GLN D 136 5123 9313 8421 911 -1908 480 C ATOM 5507 CD GLN D 136 71.135 61.045 18.699 1.00 62.34 C ANISOU 5507 CD GLN D 136 5130 9665 8893 665 -1858 239 C ATOM 5508 OE1 GLN D 136 70.573 61.894 17.989 1.00 60.29 O ANISOU 5508 OE1 GLN D 136 4995 9282 8632 437 -1644 132 O ATOM 5509 NE2 GLN D 136 72.415 61.141 19.045 1.00 66.10 N ANISOU 5509 NE2 GLN D 136 5215 10337 9564 711 -2062 173 N ATOM 5510 N LYS D 137 65.685 61.398 19.005 1.00 48.44 N ANISOU 5510 N LYS D 137 4812 7404 6189 415 -1437 430 N ATOM 5511 CA LYS D 137 64.292 61.346 18.553 1.00 45.55 C ANISOU 5511 CA LYS D 137 4747 6845 5715 350 -1234 475 C ATOM 5512 C LYS D 137 63.701 62.759 18.466 1.00 44.26 C ANISOU 5512 C LYS D 137 4679 6676 5463 118 -1183 293 C ATOM 5513 O LYS D 137 64.073 63.641 19.240 1.00 45.96 O ANISOU 5513 O LYS D 137 4810 7048 5605 34 -1357 153 O ATOM 5514 CB LYS D 137 63.447 60.449 19.466 1.00 45.42 C ANISOU 5514 CB LYS D 137 4939 6827 5492 497 -1293 694 C ATOM 5515 CG LYS D 137 63.761 58.964 19.350 1.00 46.73 C ANISOU 5515 CG LYS D 137 5060 6879 5818 723 -1286 911 C ATOM 5516 CD LYS D 137 63.090 58.163 20.455 1.00 48.54 C ANISOU 5516 CD LYS D 137 5455 7135 5854 862 -1369 1187 C ATOM 5517 CE LYS D 137 64.108 57.380 21.314 1.00 52.49 C ANISOU 5517 CE LYS D 137 5786 7790 6369 1097 -1598 1388 C ATOM 5518 NZ LYS D 137 64.504 56.054 20.755 1.00 53.86 N ANISOU 5518 NZ LYS D 137 5876 7720 6870 1291 -1535 1549 N ATOM 5519 N ALA D 138 62.799 62.971 17.512 1.00 41.76 N ANISOU 5519 N ALA D 138 4524 6171 5171 24 -959 280 N ATOM 5520 CA ALA D 138 62.175 64.272 17.325 1.00 40.70 C ANISOU 5520 CA ALA D 138 4484 5986 4996 -172 -895 142 C ATOM 5521 C ALA D 138 60.671 64.186 17.507 1.00 39.13 C ANISOU 5521 C ALA D 138 4564 5694 4611 -172 -812 199 C ATOM 5522 O ALA D 138 60.002 63.415 16.822 1.00 37.78 O ANISOU 5522 O ALA D 138 4506 5387 4463 -116 -670 303 O ATOM 5523 CB ALA D 138 62.501 64.815 15.961 1.00 40.02 C ANISOU 5523 CB ALA D 138 4303 5787 5115 -290 -704 91 C ATOM 5524 N THR D 139 60.140 64.977 18.436 1.00 39.85 N ANISOU 5524 N THR D 139 4746 5865 4531 -233 -903 106 N ATOM 5525 CA THR D 139 58.704 64.993 18.680 1.00 38.68 C ANISOU 5525 CA THR D 139 4829 5653 4215 -233 -812 149 C ATOM 5526 C THR D 139 58.094 66.265 18.138 1.00 37.72 C ANISOU 5526 C THR D 139 4768 5405 4159 -392 -715 1 C ATOM 5527 O THR D 139 58.403 67.351 18.619 1.00 39.17 O ANISOU 5527 O THR D 139 4893 5635 4355 -486 -811 -182 O ATOM 5528 CB THR D 139 58.354 64.909 20.180 1.00 40.30 C ANISOU 5528 CB THR D 139 5116 6063 4135 -149 -950 165 C ATOM 5529 OG1 THR D 139 58.968 63.754 20.767 1.00 42.01 O ANISOU 5529 OG1 THR D 139 5271 6407 4284 16 -1060 352 O ATOM 5530 CG2 THR D 139 56.829 64.845 20.363 1.00 38.36 C ANISOU 5530 CG2 THR D 139 5080 5753 3743 -145 -808 234 C ATOM 5531 N LEU D 140 57.238 66.118 17.134 1.00 35.86 N ANISOU 5531 N LEU D 140 4639 5003 3984 -415 -541 73 N ATOM 5532 CA LEU D 140 56.407 67.209 16.644 1.00 35.07 C ANISOU 5532 CA LEU D 140 4625 4774 3927 -527 -447 -9 C ATOM 5533 C LEU D 140 55.153 67.322 17.523 1.00 35.28 C ANISOU 5533 C LEU D 140 4807 4828 3769 -491 -444 -28 C ATOM 5534 O LEU D 140 54.638 66.313 18.019 1.00 35.66 O ANISOU 5534 O LEU D 140 4927 4937 3685 -389 -432 99 O ATOM 5535 CB LEU D 140 55.982 66.948 15.199 1.00 33.20 C ANISOU 5535 CB LEU D 140 4428 4396 3789 -538 -285 83 C ATOM 5536 CG LEU D 140 57.008 66.900 14.069 1.00 33.23 C ANISOU 5536 CG LEU D 140 4295 4386 3944 -565 -214 112 C ATOM 5537 CD1 LEU D 140 57.782 65.589 14.043 1.00 33.63 C ANISOU 5537 CD1 LEU D 140 4257 4511 4010 -442 -239 173 C ATOM 5538 CD2 LEU D 140 56.272 67.063 12.774 1.00 31.61 C ANISOU 5538 CD2 LEU D 140 4175 4082 3752 -585 -65 168 C ATOM 5539 N VAL D 141 54.659 68.539 17.725 1.00 35.53 N ANISOU 5539 N VAL D 141 4878 4803 3818 -569 -439 -179 N ATOM 5540 CA VAL D 141 53.410 68.706 18.448 1.00 35.44 C ANISOU 5540 CA VAL D 141 4997 4822 3648 -523 -399 -214 C ATOM 5541 C VAL D 141 52.441 69.555 17.647 1.00 34.88 C ANISOU 5541 C VAL D 141 4987 4556 3710 -582 -284 -247 C ATOM 5542 O VAL D 141 52.829 70.545 17.016 1.00 35.26 O ANISOU 5542 O VAL D 141 4983 4467 3949 -677 -282 -320 O ATOM 5543 CB VAL D 141 53.610 69.262 19.881 1.00 37.55 C ANISOU 5543 CB VAL D 141 5261 5275 3733 -495 -529 -406 C ATOM 5544 CG1 VAL D 141 52.278 69.701 20.496 1.00 36.88 C ANISOU 5544 CG1 VAL D 141 5294 5212 3507 -451 -445 -486 C ATOM 5545 CG2 VAL D 141 54.258 68.216 20.757 1.00 38.49 C ANISOU 5545 CG2 VAL D 141 5349 5631 3646 -388 -639 -299 C ATOM 5546 N CYS D 142 51.178 69.138 17.682 1.00 34.25 N ANISOU 5546 N CYS D 142 5000 4464 3549 -524 -189 -166 N ATOM 5547 CA CYS D 142 50.118 69.799 16.968 1.00 33.68 C ANISOU 5547 CA CYS D 142 4975 4234 3589 -547 -95 -174 C ATOM 5548 C CYS D 142 49.045 70.320 17.914 1.00 34.34 C ANISOU 5548 C CYS D 142 5113 4361 3574 -496 -56 -288 C ATOM 5549 O CYS D 142 48.737 69.687 18.922 1.00 35.56 O ANISOU 5549 O CYS D 142 5295 4690 3528 -426 -43 -264 O ATOM 5550 CB CYS D 142 49.497 68.809 16.021 1.00 32.45 C ANISOU 5550 CB CYS D 142 4842 4026 3462 -519 -19 0 C ATOM 5551 SG CYS D 142 48.171 69.509 15.085 1.00 33.91 S ANISOU 5551 SG CYS D 142 5061 4060 3763 -524 56 10 S ATOM 5552 N LEU D 143 48.454 71.457 17.566 1.00 34.02 N ANISOU 5552 N LEU D 143 5081 4167 3679 -517 -22 -390 N ATOM 5553 CA LEU D 143 47.470 72.102 18.418 1.00 34.70 C ANISOU 5553 CA LEU D 143 5198 4278 3707 -453 25 -544 C ATOM 5554 C LEU D 143 46.267 72.611 17.657 1.00 33.86 C ANISOU 5554 C LEU D 143 5097 4002 3766 -427 113 -502 C ATOM 5555 O LEU D 143 46.357 73.586 16.912 1.00 34.28 O ANISOU 5555 O LEU D 143 5136 3851 4036 -465 95 -528 O ATOM 5556 CB LEU D 143 48.101 73.285 19.142 1.00 36.77 C ANISOU 5556 CB LEU D 143 5442 4515 4015 -480 -64 -824 C ATOM 5557 CG LEU D 143 48.535 73.120 20.588 1.00 39.05 C ANISOU 5557 CG LEU D 143 5738 5066 4032 -427 -140 -1002 C ATOM 5558 CD1 LEU D 143 48.728 74.491 21.189 1.00 41.68 C ANISOU 5558 CD1 LEU D 143 6053 5322 4463 -442 -217 -1357 C ATOM 5559 CD2 LEU D 143 47.501 72.354 21.368 1.00 40.39 C ANISOU 5559 CD2 LEU D 143 5961 5454 3931 -309 -24 -919 C ATOM 5560 N ALA D 144 45.133 71.964 17.866 1.00 33.10 N ANISOU 5560 N ALA D 144 5003 3988 3584 -359 207 -420 N ATOM 5561 CA ALA D 144 43.859 72.484 17.397 1.00 32.83 C ANISOU 5561 CA ALA D 144 4943 3836 3694 -307 280 -417 C ATOM 5562 C ALA D 144 43.228 73.285 18.544 1.00 34.90 C ANISOU 5562 C ALA D 144 5200 4155 3905 -221 345 -640 C ATOM 5563 O ALA D 144 43.072 72.771 19.664 1.00 36.11 O ANISOU 5563 O ALA D 144 5363 4533 3825 -171 407 -684 O ATOM 5564 CB ALA D 144 42.963 71.340 16.974 1.00 31.46 C ANISOU 5564 CB ALA D 144 4734 3719 3502 -292 343 -230 C ATOM 5565 N THR D 145 42.877 74.541 18.288 1.00 35.55 N ANISOU 5565 N THR D 145 5266 4041 4200 -188 339 -779 N ATOM 5566 CA THR D 145 42.383 75.400 19.363 1.00 37.89 C ANISOU 5566 CA THR D 145 5554 4368 4473 -90 396 -1059 C ATOM 5567 C THR D 145 41.223 76.282 18.933 1.00 38.66 C ANISOU 5567 C THR D 145 5593 4270 4825 5 459 -1104 C ATOM 5568 O THR D 145 41.146 76.700 17.782 1.00 38.18 O ANISOU 5568 O THR D 145 5516 3981 5008 -18 406 -961 O ATOM 5569 CB THR D 145 43.488 76.328 19.890 1.00 39.47 C ANISOU 5569 CB THR D 145 5786 4493 4717 -136 284 -1326 C ATOM 5570 OG1 THR D 145 44.029 77.064 18.796 1.00 39.70 O ANISOU 5570 OG1 THR D 145 5804 4217 5064 -224 204 -1251 O ATOM 5571 CG2 THR D 145 44.614 75.548 20.561 1.00 39.27 C ANISOU 5571 CG2 THR D 145 5794 4710 4418 -197 202 -1332 C ATOM 5572 N GLY D 146 40.329 76.569 19.872 1.00 40.55 N ANISOU 5572 N GLY D 146 5794 4621 4994 131 577 -1294 N ATOM 5573 CA GLY D 146 39.260 77.545 19.657 1.00 41.81 C ANISOU 5573 CA GLY D 146 5876 4590 5419 256 638 -1398 C ATOM 5574 C GLY D 146 38.064 77.041 18.881 1.00 40.63 C ANISOU 5574 C GLY D 146 5623 4439 5375 305 702 -1157 C ATOM 5575 O GLY D 146 37.315 77.830 18.320 1.00 41.86 O ANISOU 5575 O GLY D 146 5706 4392 5808 398 698 -1161 O ATOM 5576 N PHE D 147 37.872 75.726 18.858 1.00 38.80 N ANISOU 5576 N PHE D 147 5369 4422 4951 245 748 -951 N ATOM 5577 CA PHE D 147 36.789 75.132 18.096 1.00 37.70 C ANISOU 5577 CA PHE D 147 5108 4286 4931 262 779 -745 C ATOM 5578 C PHE D 147 35.682 74.670 19.008 1.00 39.44 C ANISOU 5578 C PHE D 147 5203 4722 5062 342 974 -778 C ATOM 5579 O PHE D 147 35.908 74.432 20.201 1.00 40.56 O ANISOU 5579 O PHE D 147 5385 5077 4949 361 1093 -883 O ATOM 5580 CB PHE D 147 37.285 73.954 17.251 1.00 35.28 C ANISOU 5580 CB PHE D 147 4834 4014 4557 126 686 -497 C ATOM 5581 CG PHE D 147 37.887 72.838 18.047 1.00 34.25 C ANISOU 5581 CG PHE D 147 4759 4091 4163 48 741 -442 C ATOM 5582 CD1 PHE D 147 39.237 72.866 18.404 1.00 33.44 C ANISOU 5582 CD1 PHE D 147 4784 4016 3904 -12 667 -497 C ATOM 5583 CD2 PHE D 147 37.110 71.750 18.438 1.00 33.61 C ANISOU 5583 CD2 PHE D 147 4583 4167 4020 36 865 -311 C ATOM 5584 CE1 PHE D 147 39.802 71.827 19.143 1.00 32.65 C ANISOU 5584 CE1 PHE D 147 4728 4113 3563 -57 700 -416 C ATOM 5585 CE2 PHE D 147 37.669 70.711 19.175 1.00 33.58 C ANISOU 5585 CE2 PHE D 147 4632 4332 3794 -22 919 -206 C ATOM 5586 CZ PHE D 147 39.013 70.747 19.525 1.00 32.77 C ANISOU 5586 CZ PHE D 147 4668 4270 3512 -56 829 -253 C ATOM 5587 N TYR D 148 34.492 74.532 18.423 1.00 39.74 N ANISOU 5587 N TYR D 148 5075 4724 5301 391 1006 -676 N ATOM 5588 CA TYR D 148 33.300 74.069 19.115 1.00 41.50 C ANISOU 5588 CA TYR D 148 5120 5136 5513 455 1210 -666 C ATOM 5589 C TYR D 148 32.391 73.484 18.055 1.00 41.18 C ANISOU 5589 C TYR D 148 4906 5034 5705 418 1142 -474 C ATOM 5590 O TYR D 148 32.324 74.029 16.954 1.00 40.74 O ANISOU 5590 O TYR D 148 4843 4794 5844 446 966 -443 O ATOM 5591 CB TYR D 148 32.591 75.236 19.835 1.00 44.40 C ANISOU 5591 CB TYR D 148 5405 5500 5964 647 1344 -926 C ATOM 5592 CG TYR D 148 31.409 74.799 20.674 1.00 46.48 C ANISOU 5592 CG TYR D 148 5468 6006 6186 725 1604 -926 C ATOM 5593 CD1 TYR D 148 31.596 74.317 21.968 1.00 47.71 C ANISOU 5593 CD1 TYR D 148 5668 6457 6001 730 1807 -966 C ATOM 5594 CD2 TYR D 148 30.108 74.836 20.167 1.00 47.25 C ANISOU 5594 CD2 TYR D 148 5315 6062 6574 797 1650 -861 C ATOM 5595 CE1 TYR D 148 30.531 73.888 22.737 1.00 49.25 C ANISOU 5595 CE1 TYR D 148 5670 6899 6143 796 2084 -920 C ATOM 5596 CE2 TYR D 148 29.031 74.413 20.935 1.00 49.03 C ANISOU 5596 CE2 TYR D 148 5323 6518 6790 854 1915 -843 C ATOM 5597 CZ TYR D 148 29.257 73.938 22.216 1.00 50.25 C ANISOU 5597 CZ TYR D 148 5532 6962 6598 849 2148 -861 C ATOM 5598 OH TYR D 148 28.215 73.513 22.993 1.00 53.69 O ANISOU 5598 OH TYR D 148 5746 7650 7005 905 2449 -804 O ATOM 5599 N PRO D 149 31.711 72.362 18.352 1.00 41.98 N ANISOU 5599 N PRO D 149 4862 5293 5794 349 1270 -335 N ATOM 5600 CA PRO D 149 31.817 71.443 19.492 1.00 43.08 C ANISOU 5600 CA PRO D 149 5009 5657 5703 289 1475 -254 C ATOM 5601 C PRO D 149 32.956 70.421 19.322 1.00 41.15 C ANISOU 5601 C PRO D 149 4931 5407 5296 134 1372 -97 C ATOM 5602 O PRO D 149 33.641 70.448 18.304 1.00 38.94 O ANISOU 5602 O PRO D 149 4752 4965 5080 74 1156 -80 O ATOM 5603 CB PRO D 149 30.469 70.732 19.470 1.00 44.83 C ANISOU 5603 CB PRO D 149 4950 5952 6133 265 1617 -121 C ATOM 5604 CG PRO D 149 30.094 70.725 18.029 1.00 43.38 C ANISOU 5604 CG PRO D 149 4671 5575 6238 227 1379 -83 C ATOM 5605 CD PRO D 149 30.540 72.045 17.514 1.00 42.52 C ANISOU 5605 CD PRO D 149 4691 5315 6149 348 1220 -239 C ATOM 5606 N ASP D 150 33.120 69.514 20.289 1.00 42.41 N ANISOU 5606 N ASP D 150 5107 5750 5257 84 1535 36 N ATOM 5607 CA ASP D 150 34.313 68.654 20.368 1.00 41.66 C ANISOU 5607 CA ASP D 150 5181 5663 4985 -19 1451 171 C ATOM 5608 C ASP D 150 34.382 67.503 19.344 1.00 40.50 C ANISOU 5608 C ASP D 150 4990 5351 5047 -164 1323 352 C ATOM 5609 O ASP D 150 34.928 66.423 19.628 1.00 40.47 O ANISOU 5609 O ASP D 150 5039 5366 4972 -246 1344 530 O ATOM 5610 CB ASP D 150 34.562 68.151 21.805 1.00 43.65 C ANISOU 5610 CB ASP D 150 5485 6181 4920 9 1652 275 C ATOM 5611 CG ASP D 150 33.456 67.228 22.326 1.00 47.19 C ANISOU 5611 CG ASP D 150 5734 6745 5451 -26 1902 510 C ATOM 5612 OD1 ASP D 150 32.264 67.554 22.139 1.00 49.97 O ANISOU 5612 OD1 ASP D 150 5882 7083 6021 6 2008 460 O ATOM 5613 OD2 ASP D 150 33.783 66.186 22.950 1.00 48.46 O ANISOU 5613 OD2 ASP D 150 5928 7007 5477 -83 2001 764 O ATOM 5614 N HIS D 151 33.870 67.766 18.143 1.00 39.81 N ANISOU 5614 N HIS D 151 4811 5102 5212 -178 1176 290 N ATOM 5615 CA HIS D 151 33.801 66.770 17.089 1.00 38.87 C ANISOU 5615 CA HIS D 151 4631 4843 5295 -296 1035 383 C ATOM 5616 C HIS D 151 34.855 67.006 16.034 1.00 36.93 C ANISOU 5616 C HIS D 151 4551 4483 4997 -309 803 313 C ATOM 5617 O HIS D 151 34.591 67.572 14.971 1.00 36.93 O ANISOU 5617 O HIS D 151 4522 4406 5104 -275 651 235 O ATOM 5618 CB HIS D 151 32.402 66.740 16.497 1.00 40.00 C ANISOU 5618 CB HIS D 151 4521 4944 5735 -302 1025 366 C ATOM 5619 CG HIS D 151 31.431 65.980 17.336 1.00 42.43 C ANISOU 5619 CG HIS D 151 4618 5331 6172 -358 1257 503 C ATOM 5620 ND1 HIS D 151 30.137 65.732 16.941 1.00 45.03 N ANISOU 5620 ND1 HIS D 151 4662 5630 6818 -395 1272 509 N ATOM 5621 CD2 HIS D 151 31.575 65.387 18.545 1.00 44.59 C ANISOU 5621 CD2 HIS D 151 4911 5727 6305 -385 1490 667 C ATOM 5622 CE1 HIS D 151 29.521 65.026 17.873 1.00 47.70 C ANISOU 5622 CE1 HIS D 151 4840 6049 7234 -458 1528 676 C ATOM 5623 NE2 HIS D 151 30.372 64.804 18.858 1.00 47.55 N ANISOU 5623 NE2 HIS D 151 5013 6131 6923 -447 1671 791 N ATOM 5624 N VAL D 152 36.065 66.573 16.354 1.00 36.35 N ANISOU 5624 N VAL D 152 4642 4423 4747 -346 786 362 N ATOM 5625 CA VAL D 152 37.196 66.677 15.447 1.00 34.70 C ANISOU 5625 CA VAL D 152 4575 4131 4477 -363 607 316 C ATOM 5626 C VAL D 152 37.931 65.354 15.366 1.00 34.36 C ANISOU 5626 C VAL D 152 4577 4046 4432 -446 577 420 C ATOM 5627 O VAL D 152 37.916 64.567 16.318 1.00 35.20 O ANISOU 5627 O VAL D 152 4664 4199 4511 -473 702 553 O ATOM 5628 CB VAL D 152 38.193 67.752 15.898 1.00 34.24 C ANISOU 5628 CB VAL D 152 4668 4115 4226 -304 594 225 C ATOM 5629 CG1 VAL D 152 37.533 69.127 15.907 1.00 35.52 C ANISOU 5629 CG1 VAL D 152 4792 4256 4447 -211 612 100 C ATOM 5630 CG2 VAL D 152 38.777 67.420 17.267 1.00 34.90 C ANISOU 5630 CG2 VAL D 152 4819 4338 4104 -298 707 269 C ATOM 5631 N GLU D 153 38.563 65.126 14.215 1.00 33.23 N ANISOU 5631 N GLU D 153 4487 3819 4318 -469 420 370 N ATOM 5632 CA GLU D 153 39.414 63.976 13.999 1.00 32.95 C ANISOU 5632 CA GLU D 153 4502 3721 4297 -519 374 421 C ATOM 5633 C GLU D 153 40.782 64.470 13.590 1.00 31.28 C ANISOU 5633 C GLU D 153 4429 3533 3924 -487 290 366 C ATOM 5634 O GLU D 153 40.935 65.052 12.520 1.00 30.83 O ANISOU 5634 O GLU D 153 4396 3465 3853 -467 192 284 O ATOM 5635 CB GLU D 153 38.838 63.086 12.909 1.00 33.59 C ANISOU 5635 CB GLU D 153 4483 3689 4592 -573 273 366 C ATOM 5636 CG GLU D 153 37.622 62.302 13.327 1.00 37.70 C ANISOU 5636 CG GLU D 153 4829 4145 5352 -643 356 436 C ATOM 5637 CD GLU D 153 36.932 61.621 12.147 1.00 42.22 C ANISOU 5637 CD GLU D 153 5272 4608 6163 -701 209 307 C ATOM 5638 OE1 GLU D 153 37.307 61.911 10.981 1.00 42.29 O ANISOU 5638 OE1 GLU D 153 5342 4643 6085 -658 44 158 O ATOM 5639 OE2 GLU D 153 36.006 60.805 12.390 1.00 44.86 O ANISOU 5639 OE2 GLU D 153 5433 4843 6769 -790 260 352 O ATOM 5640 N LEU D 154 41.774 64.259 14.450 1.00 31.16 N ANISOU 5640 N LEU D 154 4489 3568 3783 -477 330 431 N ATOM 5641 CA LEU D 154 43.145 64.692 14.169 1.00 30.26 C ANISOU 5641 CA LEU D 154 4467 3482 3548 -458 257 382 C ATOM 5642 C LEU D 154 43.892 63.536 13.526 1.00 29.70 C ANISOU 5642 C LEU D 154 4399 3341 3545 -468 200 401 C ATOM 5643 O LEU D 154 43.786 62.407 13.993 1.00 30.29 O ANISOU 5643 O LEU D 154 4442 3358 3710 -479 234 497 O ATOM 5644 CB LEU D 154 43.848 65.113 15.467 1.00 31.09 C ANISOU 5644 CB LEU D 154 4625 3703 3484 -430 298 406 C ATOM 5645 CG LEU D 154 45.104 65.990 15.380 1.00 31.77 C ANISOU 5645 CG LEU D 154 4767 3828 3476 -426 226 318 C ATOM 5646 CD1 LEU D 154 45.119 66.992 16.517 1.00 33.08 C ANISOU 5646 CD1 LEU D 154 4958 4096 3513 -401 252 233 C ATOM 5647 CD2 LEU D 154 46.407 65.166 15.341 1.00 31.76 C ANISOU 5647 CD2 LEU D 154 4774 3844 3451 -422 168 370 C ATOM 5648 N SER D 155 44.622 63.810 12.446 1.00 28.50 N ANISOU 5648 N SER D 155 4276 3187 3365 -457 127 318 N ATOM 5649 CA SER D 155 45.393 62.772 11.762 1.00 28.64 C ANISOU 5649 CA SER D 155 4290 3155 3438 -442 84 289 C ATOM 5650 C SER D 155 46.747 63.315 11.368 1.00 28.21 C ANISOU 5650 C SER D 155 4270 3175 3273 -417 65 259 C ATOM 5651 O SER D 155 46.888 64.511 11.113 1.00 28.07 O ANISOU 5651 O SER D 155 4276 3215 3176 -429 67 244 O ATOM 5652 CB SER D 155 44.652 62.212 10.534 1.00 29.07 C ANISOU 5652 CB SER D 155 4303 3147 3597 -446 23 179 C ATOM 5653 OG SER D 155 44.028 63.234 9.766 1.00 28.95 O ANISOU 5653 OG SER D 155 4290 3201 3507 -439 -15 129 O ATOM 5654 N TRP D 156 47.748 62.439 11.339 1.00 28.47 N ANISOU 5654 N TRP D 156 4287 3190 3339 -381 55 261 N ATOM 5655 CA TRP D 156 49.090 62.839 10.946 1.00 27.97 C ANISOU 5655 CA TRP D 156 4215 3208 3205 -358 53 235 C ATOM 5656 C TRP D 156 49.449 62.253 9.598 1.00 28.35 C ANISOU 5656 C TRP D 156 4243 3259 3268 -310 50 129 C ATOM 5657 O TRP D 156 49.227 61.063 9.337 1.00 29.10 O ANISOU 5657 O TRP D 156 4319 3259 3477 -271 29 65 O ATOM 5658 CB TRP D 156 50.104 62.365 11.960 1.00 28.58 C ANISOU 5658 CB TRP D 156 4261 3305 3294 -325 39 307 C ATOM 5659 CG TRP D 156 50.130 63.124 13.230 1.00 29.01 C ANISOU 5659 CG TRP D 156 4331 3436 3255 -353 27 368 C ATOM 5660 CD1 TRP D 156 49.451 62.826 14.373 1.00 29.86 C ANISOU 5660 CD1 TRP D 156 4465 3552 3329 -345 39 459 C ATOM 5661 CD2 TRP D 156 50.917 64.275 13.517 1.00 29.04 C ANISOU 5661 CD2 TRP D 156 4315 3531 3186 -388 2 325 C ATOM 5662 NE1 TRP D 156 49.754 63.735 15.348 1.00 30.51 N ANISOU 5662 NE1 TRP D 156 4559 3757 3275 -355 15 445 N ATOM 5663 CE2 TRP D 156 50.654 64.636 14.848 1.00 30.16 C ANISOU 5663 CE2 TRP D 156 4482 3744 3232 -390 -21 345 C ATOM 5664 CE3 TRP D 156 51.810 65.047 12.774 1.00 30.40 C ANISOU 5664 CE3 TRP D 156 4440 3733 3378 -424 7 271 C ATOM 5665 CZ2 TRP D 156 51.253 65.738 15.456 1.00 31.81 C ANISOU 5665 CZ2 TRP D 156 4673 4036 3379 -427 -71 259 C ATOM 5666 CZ3 TRP D 156 52.406 66.143 13.375 1.00 31.34 C ANISOU 5666 CZ3 TRP D 156 4525 3901 3483 -482 -28 227 C ATOM 5667 CH2 TRP D 156 52.124 66.478 14.703 1.00 31.78 C ANISOU 5667 CH2 TRP D 156 4608 4010 3457 -483 -83 195 C ATOM 5668 N TRP D 157 50.020 63.096 8.745 1.00 28.18 N ANISOU 5668 N TRP D 157 4221 3346 3140 -310 81 109 N ATOM 5669 CA TRP D 157 50.345 62.696 7.381 1.00 28.65 C ANISOU 5669 CA TRP D 157 4269 3480 3138 -247 101 4 C ATOM 5670 C TRP D 157 51.787 62.997 7.065 1.00 29.02 C ANISOU 5670 C TRP D 157 4255 3636 3137 -223 177 26 C ATOM 5671 O TRP D 157 52.250 64.118 7.247 1.00 29.28 O ANISOU 5671 O TRP D 157 4270 3719 3136 -285 217 128 O ATOM 5672 CB TRP D 157 49.431 63.414 6.399 1.00 28.60 C ANISOU 5672 CB TRP D 157 4310 3549 3009 -253 84 -7 C ATOM 5673 CG TRP D 157 47.989 63.063 6.580 1.00 27.91 C ANISOU 5673 CG TRP D 157 4239 3369 2997 -273 2 -52 C ATOM 5674 CD1 TRP D 157 47.140 63.524 7.557 1.00 27.21 C ANISOU 5674 CD1 TRP D 157 4156 3197 2984 -331 -10 31 C ATOM 5675 CD2 TRP D 157 47.224 62.174 5.775 1.00 27.22 C ANISOU 5675 CD2 TRP D 157 4138 3271 2933 -235 -76 -215 C ATOM 5676 NE1 TRP D 157 45.894 62.973 7.398 1.00 26.73 N ANISOU 5676 NE1 TRP D 157 4070 3076 3012 -339 -76 -38 N ATOM 5677 CE2 TRP D 157 45.918 62.144 6.307 1.00 27.31 C ANISOU 5677 CE2 TRP D 157 4128 3180 3067 -290 -134 -198 C ATOM 5678 CE3 TRP D 157 47.509 61.413 4.648 1.00 28.82 C ANISOU 5678 CE3 TRP D 157 4333 3551 3068 -156 -105 -402 C ATOM 5679 CZ2 TRP D 157 44.900 61.380 5.747 1.00 28.74 C ANISOU 5679 CZ2 TRP D 157 4260 3316 3342 -289 -235 -353 C ATOM 5680 CZ3 TRP D 157 46.499 60.649 4.091 1.00 31.84 C ANISOU 5680 CZ3 TRP D 157 4688 3891 3517 -145 -221 -591 C ATOM 5681 CH2 TRP D 157 45.206 60.639 4.642 1.00 30.97 C ANISOU 5681 CH2 TRP D 157 4539 3660 3568 -222 -293 -560 C ATOM 5682 N VAL D 158 52.505 61.978 6.627 1.00 29.82 N ANISOU 5682 N VAL D 158 4303 3753 3276 -134 201 -78 N ATOM 5683 CA VAL D 158 53.873 62.161 6.161 1.00 30.57 C ANISOU 5683 CA VAL D 158 4305 3979 3333 -94 298 -74 C ATOM 5684 C VAL D 158 53.953 61.792 4.678 1.00 32.21 C ANISOU 5684 C VAL D 158 4515 4330 3395 2 368 -213 C ATOM 5685 O VAL D 158 53.575 60.681 4.266 1.00 33.08 O ANISOU 5685 O VAL D 158 4643 4386 3540 89 323 -401 O ATOM 5686 CB VAL D 158 54.883 61.382 7.019 1.00 30.93 C ANISOU 5686 CB VAL D 158 4249 3960 3543 -42 279 -73 C ATOM 5687 CG1 VAL D 158 56.261 61.428 6.400 1.00 32.25 C ANISOU 5687 CG1 VAL D 158 4280 4273 3700 18 390 -100 C ATOM 5688 CG2 VAL D 158 54.914 61.955 8.418 1.00 28.86 C ANISOU 5688 CG2 VAL D 158 3984 3645 3338 -128 207 62 C ATOM 5689 N ASN D 159 54.411 62.764 3.893 1.00 32.73 N ANISOU 5689 N ASN D 159 4561 4577 3298 -15 481 -120 N ATOM 5690 CA ASN D 159 54.472 62.680 2.443 1.00 34.61 C ANISOU 5690 CA ASN D 159 4814 5033 3305 81 570 -204 C ATOM 5691 C ASN D 159 53.195 62.170 1.809 1.00 34.98 C ANISOU 5691 C ASN D 159 4968 5086 3236 135 453 -367 C ATOM 5692 O ASN D 159 53.228 61.279 0.969 1.00 37.14 O ANISOU 5692 O ASN D 159 5240 5458 3415 256 454 -599 O ATOM 5693 CB ASN D 159 55.678 61.862 2.011 1.00 36.47 C ANISOU 5693 CB ASN D 159 4931 5373 3554 201 685 -342 C ATOM 5694 CG ASN D 159 56.975 62.431 2.538 1.00 37.40 C ANISOU 5694 CG ASN D 159 4898 5517 3795 143 796 -181 C ATOM 5695 OD1 ASN D 159 57.214 63.646 2.486 1.00 37.28 O ANISOU 5695 OD1 ASN D 159 4858 5567 3741 35 874 29 O ATOM 5696 ND2 ASN D 159 57.823 61.556 3.055 1.00 38.78 N ANISOU 5696 ND2 ASN D 159 4955 5624 4157 216 792 -278 N ATOM 5697 N GLY D 160 52.067 62.731 2.232 1.00 33.63 N ANISOU 5697 N GLY D 160 4873 4812 3093 49 345 -273 N ATOM 5698 CA GLY D 160 50.769 62.398 1.659 1.00 34.05 C ANISOU 5698 CA GLY D 160 4995 4880 3061 82 212 -409 C ATOM 5699 C GLY D 160 50.252 61.040 2.080 1.00 34.27 C ANISOU 5699 C GLY D 160 5006 4712 3304 98 97 -638 C ATOM 5700 O GLY D 160 49.279 60.533 1.514 1.00 35.07 O ANISOU 5700 O GLY D 160 5128 4817 3380 126 -23 -821 O ATOM 5701 N LYS D 161 50.901 60.433 3.069 1.00 33.89 N ANISOU 5701 N LYS D 161 4906 4482 3489 79 126 -620 N ATOM 5702 CA LYS D 161 50.379 59.184 3.634 1.00 34.41 C ANISOU 5702 CA LYS D 161 4951 4301 3821 78 32 -757 C ATOM 5703 C LYS D 161 50.228 59.277 5.147 1.00 32.76 C ANISOU 5703 C LYS D 161 4735 3902 3812 -16 22 -547 C ATOM 5704 O LYS D 161 51.030 59.919 5.827 1.00 31.87 O ANISOU 5704 O LYS D 161 4606 3832 3673 -41 86 -376 O ATOM 5705 CB LYS D 161 51.213 57.982 3.188 1.00 36.20 C ANISOU 5705 CB LYS D 161 5121 4486 4147 203 61 -983 C ATOM 5706 CG LYS D 161 51.210 57.858 1.671 1.00 38.65 C ANISOU 5706 CG LYS D 161 5448 5029 4209 312 67 -1241 C ATOM 5707 CD LYS D 161 51.771 56.558 1.155 1.00 42.33 C ANISOU 5707 CD LYS D 161 5859 5427 4798 452 74 -1559 C ATOM 5708 CE LYS D 161 51.348 56.364 -0.290 1.00 45.59 C ANISOU 5708 CE LYS D 161 6305 6072 4945 552 24 -1879 C ATOM 5709 NZ LYS D 161 52.378 55.641 -1.085 1.00 49.21 N ANISOU 5709 NZ LYS D 161 6711 6652 5335 734 127 -2159 N ATOM 5710 N GLU D 162 49.160 58.678 5.656 1.00 32.86 N ANISOU 5710 N GLU D 162 4748 3726 4012 -70 -58 -565 N ATOM 5711 CA GLU D 162 48.842 58.764 7.069 1.00 31.87 C ANISOU 5711 CA GLU D 162 4621 3466 4023 -149 -50 -354 C ATOM 5712 C GLU D 162 49.778 57.873 7.874 1.00 32.60 C ANISOU 5712 C GLU D 162 4671 3427 4288 -95 -23 -282 C ATOM 5713 O GLU D 162 50.025 56.721 7.501 1.00 33.99 O ANISOU 5713 O GLU D 162 4808 3462 4644 -24 -42 -422 O ATOM 5714 CB GLU D 162 47.383 58.379 7.312 1.00 32.22 C ANISOU 5714 CB GLU D 162 4650 3367 4225 -225 -113 -368 C ATOM 5715 CG GLU D 162 46.910 58.599 8.747 1.00 32.42 C ANISOU 5715 CG GLU D 162 4674 3315 4331 -300 -71 -133 C ATOM 5716 CD GLU D 162 45.402 58.492 8.915 1.00 33.47 C ANISOU 5716 CD GLU D 162 4763 3359 4596 -384 -99 -128 C ATOM 5717 OE1 GLU D 162 44.708 58.022 7.991 1.00 33.65 O ANISOU 5717 OE1 GLU D 162 4739 3330 4715 -396 -183 -319 O ATOM 5718 OE2 GLU D 162 44.911 58.889 9.990 1.00 35.03 O ANISOU 5718 OE2 GLU D 162 4957 3556 4796 -435 -38 53 O ATOM 5719 N VAL D 163 50.305 58.429 8.966 1.00 31.81 N ANISOU 5719 N VAL D 163 4575 3377 4136 -118 7 -78 N ATOM 5720 CA VAL D 163 51.162 57.690 9.900 1.00 32.66 C ANISOU 5720 CA VAL D 163 4638 3396 4376 -54 7 44 C ATOM 5721 C VAL D 163 50.396 57.401 11.184 1.00 32.91 C ANISOU 5721 C VAL D 163 4691 3320 4494 -106 0 251 C ATOM 5722 O VAL D 163 49.600 58.225 11.635 1.00 32.07 O ANISOU 5722 O VAL D 163 4626 3291 4267 -189 16 321 O ATOM 5723 CB VAL D 163 52.492 58.446 10.238 1.00 32.16 C ANISOU 5723 CB VAL D 163 4533 3512 4175 -23 24 114 C ATOM 5724 CG1 VAL D 163 53.412 58.494 9.039 1.00 32.41 C ANISOU 5724 CG1 VAL D 163 4508 3646 4162 45 72 -48 C ATOM 5725 CG2 VAL D 163 52.218 59.845 10.739 1.00 30.50 C ANISOU 5725 CG2 VAL D 163 4365 3442 3780 -123 28 197 C ATOM 5726 N HIS D 164 50.627 56.227 11.759 1.00 34.72 N ANISOU 5726 N HIS D 164 4884 3370 4937 -43 -8 360 N ATOM 5727 CA HIS D 164 49.969 55.832 13.002 1.00 35.41 C ANISOU 5727 CA HIS D 164 4984 3369 5100 -77 13 616 C ATOM 5728 C HIS D 164 51.010 55.494 14.047 1.00 36.00 C ANISOU 5728 C HIS D 164 5038 3488 5152 26 -10 833 C ATOM 5729 O HIS D 164 50.813 55.730 15.229 1.00 36.24 O ANISOU 5729 O HIS D 164 5097 3621 5050 18 2 1058 O ATOM 5730 CB HIS D 164 49.058 54.624 12.777 1.00 37.51 C ANISOU 5730 CB HIS D 164 5216 3336 5701 -110 26 614 C ATOM 5731 CG HIS D 164 47.855 54.914 11.928 1.00 38.72 C ANISOU 5731 CG HIS D 164 5364 3463 5884 -218 21 419 C ATOM 5732 ND1 HIS D 164 46.757 55.609 12.400 1.00 38.80 N ANISOU 5732 ND1 HIS D 164 5385 3560 5797 -321 64 511 N ATOM 5733 CD2 HIS D 164 47.568 54.578 10.645 1.00 39.49 C ANISOU 5733 CD2 HIS D 164 5435 3476 6094 -224 -35 124 C ATOM 5734 CE1 HIS D 164 45.851 55.696 11.440 1.00 39.20 C ANISOU 5734 CE1 HIS D 164 5404 3573 5919 -387 22 302 C ATOM 5735 NE2 HIS D 164 46.317 55.077 10.367 1.00 39.80 N ANISOU 5735 NE2 HIS D 164 5462 3556 6104 -332 -47 61 N ATOM 5736 N SER D 165 52.121 54.931 13.594 1.00 36.71 N ANISOU 5736 N SER D 165 5067 3522 5358 141 -49 756 N ATOM 5737 CA SER D 165 53.237 54.638 14.464 1.00 37.85 C ANISOU 5737 CA SER D 165 5161 3731 5490 265 -103 942 C ATOM 5738 C SER D 165 53.799 55.937 15.014 1.00 36.45 C ANISOU 5738 C SER D 165 4988 3872 4989 234 -144 952 C ATOM 5739 O SER D 165 54.066 56.862 14.258 1.00 35.12 O ANISOU 5739 O SER D 165 4809 3830 4704 177 -131 753 O ATOM 5740 CB SER D 165 54.318 53.872 13.706 1.00 39.04 C ANISOU 5740 CB SER D 165 5214 3768 5850 405 -128 805 C ATOM 5741 OG SER D 165 55.372 53.504 14.578 1.00 41.39 O ANISOU 5741 OG SER D 165 5439 4116 6173 544 -200 1007 O ATOM 5742 N GLY D 166 53.956 55.998 16.334 1.00 37.49 N ANISOU 5742 N GLY D 166 5133 4131 4982 273 -193 1188 N ATOM 5743 CA GLY D 166 54.560 57.136 17.006 1.00 36.90 C ANISOU 5743 CA GLY D 166 5045 4351 4625 256 -267 1167 C ATOM 5744 C GLY D 166 53.602 58.283 17.193 1.00 35.59 C ANISOU 5744 C GLY D 166 4970 4303 4251 120 -217 1086 C ATOM 5745 O GLY D 166 54.014 59.407 17.469 1.00 34.98 O ANISOU 5745 O GLY D 166 4881 4420 3989 75 -270 976 O ATOM 5746 N VAL D 167 52.316 58.002 17.036 1.00 35.73 N ANISOU 5746 N VAL D 167 5057 4183 4337 54 -118 1126 N ATOM 5747 CA VAL D 167 51.291 59.022 17.188 1.00 34.91 C ANISOU 5747 CA VAL D 167 5021 4170 4074 -52 -58 1052 C ATOM 5748 C VAL D 167 50.631 58.877 18.542 1.00 37.00 C ANISOU 5748 C VAL D 167 5332 4543 4182 -31 -14 1271 C ATOM 5749 O VAL D 167 50.466 57.762 19.043 1.00 38.81 O ANISOU 5749 O VAL D 167 5554 4676 4515 28 18 1517 O ATOM 5750 CB VAL D 167 50.249 58.963 16.045 1.00 33.42 C ANISOU 5750 CB VAL D 167 4847 3803 4047 -139 17 923 C ATOM 5751 CG1 VAL D 167 49.057 59.837 16.353 1.00 32.75 C ANISOU 5751 CG1 VAL D 167 4810 3792 3843 -222 83 899 C ATOM 5752 CG2 VAL D 167 50.880 59.435 14.745 1.00 31.93 C ANISOU 5752 CG2 VAL D 167 4630 3608 3893 -153 -12 702 C ATOM 5753 N CYS D 168 50.299 60.013 19.153 1.00 37.55 N ANISOU 5753 N CYS D 168 5444 4816 4006 -68 -5 1188 N ATOM 5754 CA CYS D 168 49.429 60.016 20.332 1.00 39.83 C ANISOU 5754 CA CYS D 168 5781 5247 4107 -50 82 1354 C ATOM 5755 C CYS D 168 48.575 61.277 20.478 1.00 38.92 C ANISOU 5755 C CYS D 168 5702 5244 3842 -116 146 1169 C ATOM 5756 O CYS D 168 49.107 62.378 20.603 1.00 38.73 O ANISOU 5756 O CYS D 168 5689 5352 3674 -124 63 961 O ATOM 5757 CB CYS D 168 50.206 59.776 21.617 1.00 41.86 C ANISOU 5757 CB CYS D 168 6047 5745 4111 71 2 1530 C ATOM 5758 SG CYS D 168 49.011 59.408 22.892 1.00 47.39 S ANISOU 5758 SG CYS D 168 6800 6602 4604 108 174 1819 S ATOM 5759 N THR D 169 47.256 61.098 20.492 1.00 39.20 N ANISOU 5759 N THR D 169 5737 5210 3947 -161 294 1243 N ATOM 5760 CA THR D 169 46.316 62.221 20.557 1.00 38.87 C ANISOU 5760 CA THR D 169 5707 5242 3818 -204 370 1072 C ATOM 5761 C THR D 169 45.481 62.203 21.828 1.00 41.40 C ANISOU 5761 C THR D 169 6040 5769 3922 -155 517 1215 C ATOM 5762 O THR D 169 44.881 61.180 22.158 1.00 42.70 O ANISOU 5762 O THR D 169 6170 5886 4167 -155 639 1486 O ATOM 5763 CB THR D 169 45.346 62.190 19.374 1.00 37.21 C ANISOU 5763 CB THR D 169 5450 4807 3882 -292 424 996 C ATOM 5764 OG1 THR D 169 46.084 62.133 18.149 1.00 35.42 O ANISOU 5764 OG1 THR D 169 5217 4429 3813 -321 309 876 O ATOM 5765 CG2 THR D 169 44.452 63.410 19.386 1.00 36.65 C ANISOU 5765 CG2 THR D 169 5375 4797 3752 -311 483 822 C ATOM 5766 N ASP D 170 45.418 63.348 22.512 1.00 42.43 N ANISOU 5766 N ASP D 170 6207 6117 3798 -115 518 1025 N ATOM 5767 CA ASP D 170 44.658 63.479 23.757 1.00 45.22 C ANISOU 5767 CA ASP D 170 6573 6732 3876 -42 673 1108 C ATOM 5768 C ASP D 170 43.348 62.711 23.657 1.00 46.39 C ANISOU 5768 C ASP D 170 6645 6770 4210 -88 885 1339 C ATOM 5769 O ASP D 170 42.632 62.855 22.668 1.00 44.80 O ANISOU 5769 O ASP D 170 6379 6345 4299 -175 910 1243 O ATOM 5770 CB ASP D 170 44.358 64.945 24.067 1.00 45.17 C ANISOU 5770 CB ASP D 170 6589 6860 3713 -15 676 771 C ATOM 5771 CG ASP D 170 45.607 65.781 24.262 1.00 44.55 C ANISOU 5771 CG ASP D 170 6560 6879 3489 9 466 514 C ATOM 5772 OD1 ASP D 170 46.730 65.279 24.097 1.00 44.18 O ANISOU 5772 OD1 ASP D 170 6515 6812 3458 6 315 591 O ATOM 5773 OD2 ASP D 170 45.464 66.971 24.576 1.00 44.96 O ANISOU 5773 OD2 ASP D 170 6628 7011 3445 31 450 214 O ATOM 5774 N PRO D 171 43.031 61.890 24.676 1.00 49.77 N ANISOU 5774 N PRO D 171 7066 7365 4479 -32 1034 1660 N ATOM 5775 CA PRO D 171 41.813 61.080 24.634 1.00 51.29 C ANISOU 5775 CA PRO D 171 7152 7435 4902 -98 1254 1918 C ATOM 5776 C PRO D 171 40.581 61.961 24.465 1.00 51.44 C ANISOU 5776 C PRO D 171 7089 7478 4978 -130 1392 1714 C ATOM 5777 O PRO D 171 39.738 61.676 23.624 1.00 50.68 O ANISOU 5777 O PRO D 171 6876 7138 5241 -233 1440 1717 O ATOM 5778 CB PRO D 171 41.806 60.377 25.990 1.00 55.28 C ANISOU 5778 CB PRO D 171 7680 8210 5113 -2 1408 2293 C ATOM 5779 CG PRO D 171 42.694 61.211 26.868 1.00 56.25 C ANISOU 5779 CG PRO D 171 7922 8699 4750 136 1287 2117 C ATOM 5780 CD PRO D 171 43.735 61.776 25.966 1.00 52.60 C ANISOU 5780 CD PRO D 171 7503 8068 4414 101 1013 1797 C ATOM 5781 N GLN D 172 40.499 63.032 25.250 1.00 53.07 N ANISOU 5781 N GLN D 172 7343 7976 4845 -29 1437 1510 N ATOM 5782 CA GLN D 172 39.456 64.048 25.092 1.00 53.39 C ANISOU 5782 CA GLN D 172 7307 8033 4944 -22 1544 1259 C ATOM 5783 C GLN D 172 40.069 65.440 24.912 1.00 51.73 C ANISOU 5783 C GLN D 172 7185 7850 4619 29 1369 846 C ATOM 5784 O GLN D 172 41.180 65.687 25.374 1.00 51.99 O ANISOU 5784 O GLN D 172 7329 8022 4403 82 1221 754 O ATOM 5785 CB GLN D 172 38.465 64.040 26.277 1.00 57.29 C ANISOU 5785 CB GLN D 172 7733 8837 5197 61 1841 1393 C ATOM 5786 CG GLN D 172 39.086 63.936 27.673 1.00 61.64 C ANISOU 5786 CG GLN D 172 8397 9795 5227 201 1893 1508 C ATOM 5787 CD GLN D 172 39.022 62.515 28.237 1.00 66.39 C ANISOU 5787 CD GLN D 172 8972 10459 5794 187 2045 2032 C ATOM 5788 OE1 GLN D 172 38.336 61.646 27.687 1.00 67.25 O ANISOU 5788 OE1 GLN D 172 8953 10302 6297 63 2158 2287 O ATOM 5789 NE2 GLN D 172 39.734 62.276 29.341 1.00 68.78 N ANISOU 5789 NE2 GLN D 172 9386 11108 5638 318 2039 2198 N ATOM 5790 N PRO D 173 39.354 66.349 24.225 1.00 50.55 N ANISOU 5790 N PRO D 173 6970 7550 4686 12 1373 607 N ATOM 5791 CA PRO D 173 39.799 67.746 24.153 1.00 49.89 C ANISOU 5791 CA PRO D 173 6954 7460 4542 66 1243 233 C ATOM 5792 C PRO D 173 39.562 68.449 25.479 1.00 52.79 C ANISOU 5792 C PRO D 173 7349 8155 4554 207 1368 48 C ATOM 5793 O PRO D 173 38.714 68.013 26.252 1.00 55.40 O ANISOU 5793 O PRO D 173 7615 8704 4732 268 1603 204 O ATOM 5794 CB PRO D 173 38.889 68.357 23.081 1.00 48.47 C ANISOU 5794 CB PRO D 173 6673 7024 4718 30 1248 117 C ATOM 5795 CG PRO D 173 38.325 67.170 22.322 1.00 47.99 C ANISOU 5795 CG PRO D 173 6512 6807 4915 -74 1287 397 C ATOM 5796 CD PRO D 173 38.180 66.108 23.369 1.00 49.90 C ANISOU 5796 CD PRO D 173 6737 7258 4965 -61 1461 676 C ATOM 5797 N LEU D 174 40.312 69.513 25.747 1.00 52.73 N ANISOU 5797 N LEU D 174 7426 8188 4421 259 1219 -289 N ATOM 5798 CA LEU D 174 40.119 70.284 26.974 1.00 55.90 C ANISOU 5798 CA LEU D 174 7857 8901 4480 407 1309 -561 C ATOM 5799 C LEU D 174 39.393 71.606 26.707 1.00 56.00 C ANISOU 5799 C LEU D 174 7814 8754 4709 465 1349 -919 C ATOM 5800 O LEU D 174 39.612 72.247 25.683 1.00 53.78 O ANISOU 5800 O LEU D 174 7526 8131 4776 392 1201 -1037 O ATOM 5801 CB LEU D 174 41.458 70.516 27.705 1.00 57.33 C ANISOU 5801 CB LEU D 174 8155 9288 4338 445 1102 -737 C ATOM 5802 CG LEU D 174 42.586 71.353 27.076 1.00 55.68 C ANISOU 5802 CG LEU D 174 7988 8832 4335 363 820 -1015 C ATOM 5803 CD1 LEU D 174 42.400 72.831 27.364 1.00 57.65 C ANISOU 5803 CD1 LEU D 174 8237 9033 4635 431 791 -1498 C ATOM 5804 CD2 LEU D 174 43.938 70.911 27.592 1.00 56.45 C ANISOU 5804 CD2 LEU D 174 8150 9126 4173 356 616 -981 C ATOM 5805 N LYS D 175 38.522 71.994 27.629 1.00 58.92 N ANISOU 5805 N LYS D 175 8137 9378 4873 612 1563 -1070 N ATOM 5806 CA LYS D 175 37.847 73.278 27.564 1.00 60.00 C ANISOU 5806 CA LYS D 175 8216 9386 5196 710 1612 -1447 C ATOM 5807 C LYS D 175 38.859 74.381 27.857 1.00 61.01 C ANISOU 5807 C LYS D 175 8450 9462 5268 740 1390 -1885 C ATOM 5808 O LYS D 175 39.619 74.285 28.824 1.00 63.05 O ANISOU 5808 O LYS D 175 8800 10032 5124 790 1320 -2011 O ATOM 5809 CB LYS D 175 36.696 73.320 28.575 1.00 63.73 C ANISOU 5809 CB LYS D 175 8596 10194 5424 879 1928 -1507 C ATOM 5810 CG LYS D 175 35.429 72.610 28.108 1.00 63.30 C ANISOU 5810 CG LYS D 175 8362 10083 5608 845 2160 -1168 C ATOM 5811 CD LYS D 175 34.402 72.456 29.224 1.00 67.33 C ANISOU 5811 CD LYS D 175 8763 10994 5826 1000 2514 -1151 C ATOM 5812 CE LYS D 175 34.531 71.109 29.920 1.00 68.85 C ANISOU 5812 CE LYS D 175 8976 11512 5670 957 2666 -711 C ATOM 5813 NZ LYS D 175 33.652 71.021 31.128 1.00 73.78 N ANISOU 5813 NZ LYS D 175 9510 12598 5926 1123 3036 -685 N ATOM 5814 N GLU D 176 38.889 75.411 27.013 1.00 59.83 N ANISOU 5814 N GLU D 176 8279 8917 5538 706 1266 -2101 N ATOM 5815 CA GLU D 176 39.779 76.551 27.253 1.00 61.38 C ANISOU 5815 CA GLU D 176 8544 8991 5786 714 1064 -2536 C ATOM 5816 C GLU D 176 39.169 77.602 28.183 1.00 65.99 C ANISOU 5816 C GLU D 176 9105 9691 6278 908 1176 -3016 C ATOM 5817 O GLU D 176 39.882 78.436 28.753 1.00 68.55 O ANISOU 5817 O GLU D 176 9486 10023 6537 941 1024 -3447 O ATOM 5818 CB GLU D 176 40.319 77.178 25.959 1.00 58.46 C ANISOU 5818 CB GLU D 176 8171 8129 5914 573 869 -2520 C ATOM 5819 CG GLU D 176 39.511 76.961 24.695 1.00 55.48 C ANISOU 5819 CG GLU D 176 7713 7468 5900 526 936 -2200 C ATOM 5820 CD GLU D 176 40.283 77.349 23.436 1.00 52.19 C ANISOU 5820 CD GLU D 176 7318 6662 5851 379 740 -2095 C ATOM 5821 OE1 GLU D 176 39.787 78.181 22.657 1.00 52.31 O ANISOU 5821 OE1 GLU D 176 7282 6353 6241 404 732 -2121 O ATOM 5822 OE2 GLU D 176 41.395 76.839 23.229 1.00 50.24 O ANISOU 5822 OE2 GLU D 176 7129 6442 5518 250 601 -1972 O ATOM 5823 N GLN D 177 37.853 77.539 28.354 1.00 67.39 N ANISOU 5823 N GLN D 177 9179 9966 6460 1039 1441 -2963 N ATOM 5824 CA GLN D 177 37.168 78.421 29.279 1.00 71.99 C ANISOU 5824 CA GLN D 177 9721 10709 6923 1255 1597 -3411 C ATOM 5825 C GLN D 177 36.176 77.619 30.143 1.00 74.50 C ANISOU 5825 C GLN D 177 9966 11508 6834 1389 1929 -3231 C ATOM 5826 O GLN D 177 34.963 77.818 30.039 1.00 75.56 O ANISOU 5826 O GLN D 177 9951 11609 7148 1500 2160 -3224 O ATOM 5827 CB GLN D 177 36.475 79.545 28.498 1.00 72.05 C ANISOU 5827 CB GLN D 177 9628 10249 7498 1313 1600 -3606 C ATOM 5828 CG GLN D 177 36.515 80.913 29.180 1.00 76.55 C ANISOU 5828 CG GLN D 177 10210 10734 8141 1477 1567 -4240 C ATOM 5829 CD GLN D 177 37.909 81.537 29.203 1.00 76.24 C ANISOU 5829 CD GLN D 177 10289 10498 8180 1357 1254 -4536 C ATOM 5830 OE1 GLN D 177 38.635 81.504 28.209 1.00 72.57 O ANISOU 5830 OE1 GLN D 177 9852 9689 8032 1161 1057 -4299 O ATOM 5831 NE2 GLN D 177 38.279 82.116 30.342 1.00 79.62 N ANISOU 5831 NE2 GLN D 177 10770 11161 8320 1476 1210 -5072 N ATOM 5832 N PRO D 178 36.694 76.717 31.012 1.00 75.89 N ANISOU 5832 N PRO D 178 10230 12137 6467 1387 1958 -3064 N ATOM 5833 CA PRO D 178 35.874 75.783 31.792 1.00 78.39 C ANISOU 5833 CA PRO D 178 10482 12914 6388 1481 2285 -2766 C ATOM 5834 C PRO D 178 34.643 76.390 32.469 1.00 82.94 C ANISOU 5834 C PRO D 178 10929 13705 6880 1709 2606 -3042 C ATOM 5835 O PRO D 178 33.648 75.687 32.655 1.00 84.03 O ANISOU 5835 O PRO D 178 10929 14052 6946 1746 2919 -2714 O ATOM 5836 CB PRO D 178 36.854 75.259 32.847 1.00 80.54 C ANISOU 5836 CB PRO D 178 10907 13652 6044 1514 2197 -2753 C ATOM 5837 CG PRO D 178 38.156 75.297 32.180 1.00 77.01 C ANISOU 5837 CG PRO D 178 10564 12904 5792 1339 1824 -2758 C ATOM 5838 CD PRO D 178 38.126 76.546 31.329 1.00 75.78 C ANISOU 5838 CD PRO D 178 10369 12233 6190 1302 1677 -3131 C ATOM 5839 N ALA D 179 34.703 77.675 32.816 1.00 86.00 N ANISOU 5839 N ALA D 179 11340 14021 7316 1858 2538 -3643 N ATOM 5840 CA ALA D 179 33.569 78.367 33.446 1.00 90.88 C ANISOU 5840 CA ALA D 179 11826 14817 7886 2106 2838 -3986 C ATOM 5841 C ALA D 179 32.368 78.629 32.507 1.00 89.61 C ANISOU 5841 C ALA D 179 11448 14276 8325 2117 2988 -3853 C ATOM 5842 O ALA D 179 31.459 79.391 32.849 1.00 93.17 O ANISOU 5842 O ALA D 179 11765 14760 8874 2332 3196 -4188 O ATOM 5843 CB ALA D 179 34.045 79.676 34.095 1.00 94.65 C ANISOU 5843 CB ALA D 179 12393 15293 8278 2270 2693 -4725 C ATOM 5844 N LEU D 180 32.358 77.983 31.340 1.00 85.14 N ANISOU 5844 N LEU D 180 10835 13373 8141 1904 2876 -3380 N ATOM 5845 CA LEU D 180 31.353 78.263 30.305 1.00 83.85 C ANISOU 5845 CA LEU D 180 10471 12824 8565 1902 2928 -3257 C ATOM 5846 C LEU D 180 30.553 77.057 29.782 1.00 81.67 C ANISOU 5846 C LEU D 180 10022 12600 8407 1777 3094 -2688 C ATOM 5847 O LEU D 180 31.114 76.036 29.352 1.00 78.38 O ANISOU 5847 O LEU D 180 9681 12159 7940 1569 2976 -2284 O ATOM 5848 CB LEU D 180 31.981 79.025 29.125 1.00 80.86 C ANISOU 5848 CB LEU D 180 10165 11862 8696 1792 2579 -3348 C ATOM 5849 CG LEU D 180 31.685 80.519 28.915 1.00 83.60 C ANISOU 5849 CG LEU D 180 10462 11843 9459 1958 2515 -3815 C ATOM 5850 CD1 LEU D 180 32.439 81.419 29.904 1.00 86.52 C ANISOU 5850 CD1 LEU D 180 10979 12308 9588 2074 2436 -4400 C ATOM 5851 CD2 LEU D 180 32.008 80.899 27.458 1.00 80.15 C ANISOU 5851 CD2 LEU D 180 10038 10837 9578 1814 2235 -3629 C ATOM 5852 N ASN D 181 29.231 77.224 29.817 1.00 83.72 N ANISOU 5852 N ASN D 181 10030 12911 8870 1912 3363 -2694 N ATOM 5853 CA ASN D 181 28.246 76.305 29.230 1.00 82.13 C ANISOU 5853 CA ASN D 181 9587 12691 8928 1809 3517 -2239 C ATOM 5854 C ASN D 181 28.369 76.143 27.707 1.00 76.96 C ANISOU 5854 C ASN D 181 8910 11557 8775 1623 3213 -2000 C ATOM 5855 O ASN D 181 27.862 75.176 27.129 1.00 75.34 O ANISOU 5855 O ASN D 181 8555 11321 8751 1475 3248 -1607 O ATOM 5856 CB ASN D 181 26.816 76.756 29.603 1.00 86.46 C ANISOU 5856 CB ASN D 181 9834 13383 9634 2026 3852 -2388 C ATOM 5857 CG ASN D 181 26.658 78.298 29.682 1.00 89.32 C ANISOU 5857 CG ASN D 181 10193 13544 10202 2274 3798 -2953 C ATOM 5858 OD1 ASN D 181 25.840 78.810 30.456 1.00 93.54 O ANISOU 5858 OD1 ASN D 181 10567 14316 10658 2515 4094 -3233 O ATOM 5859 ND2 ASN D 181 27.437 79.029 28.884 1.00 87.23 N ANISOU 5859 ND2 ASN D 181 10093 12830 10220 2218 3437 -3111 N ATOM 5860 N ASP D 182 29.046 77.095 27.070 1.00 74.41 N ANISOU 5860 N ASP D 182 8730 10870 8674 1632 2918 -2242 N ATOM 5861 CA ASP D 182 29.225 77.084 25.629 1.00 69.70 C ANISOU 5861 CA ASP D 182 8132 9853 8496 1490 2632 -2037 C ATOM 5862 C ASP D 182 30.719 77.161 25.231 1.00 65.94 C ANISOU 5862 C ASP D 182 7937 9187 7932 1338 2325 -2046 C ATOM 5863 O ASP D 182 31.056 77.430 24.069 1.00 63.08 O ANISOU 5863 O ASP D 182 7613 8470 7883 1250 2079 -1947 O ATOM 5864 CB ASP D 182 28.402 78.220 25.009 1.00 71.10 C ANISOU 5864 CB ASP D 182 8146 9724 9146 1661 2591 -2234 C ATOM 5865 N SER D 183 31.603 76.894 26.196 1.00 65.74 N ANISOU 5865 N SER D 183 8088 9429 7463 1314 2346 -2143 N ATOM 5866 CA SER D 183 33.060 76.989 25.999 1.00 62.67 C ANISOU 5866 CA SER D 183 7932 8909 6970 1184 2073 -2192 C ATOM 5867 C SER D 183 33.590 76.302 24.746 1.00 58.00 C ANISOU 5867 C SER D 183 7384 8069 6583 973 1857 -1830 C ATOM 5868 O SER D 183 33.055 75.292 24.308 1.00 56.62 O ANISOU 5868 O SER D 183 7106 7945 6463 885 1924 -1491 O ATOM 5869 CB SER D 183 33.809 76.425 27.205 1.00 63.96 C ANISOU 5869 CB SER D 183 8234 9483 6585 1180 2132 -2232 C ATOM 5870 OG SER D 183 35.184 76.264 26.897 1.00 60.32 O ANISOU 5870 OG SER D 183 7951 8909 6059 1028 1861 -2192 O ATOM 5871 N ARG D 184 34.665 76.856 24.200 1.00 55.91 N ANISOU 5871 N ARG D 184 7263 7545 6435 891 1607 -1926 N ATOM 5872 CA ARG D 184 35.368 76.270 23.067 1.00 51.87 C ANISOU 5872 CA ARG D 184 6815 6837 6055 705 1407 -1628 C ATOM 5873 C ARG D 184 36.421 75.267 23.542 1.00 50.14 C ANISOU 5873 C ARG D 184 6725 6844 5483 584 1357 -1487 C ATOM 5874 O ARG D 184 36.768 75.250 24.720 1.00 52.22 O ANISOU 5874 O ARG D 184 7053 7388 5401 647 1425 -1651 O ATOM 5875 CB ARG D 184 35.981 77.380 22.212 1.00 51.30 C ANISOU 5875 CB ARG D 184 6808 6379 6305 681 1197 -1756 C ATOM 5876 CG ARG D 184 34.989 77.945 21.213 1.00 52.90 C ANISOU 5876 CG ARG D 184 6878 6314 6909 757 1187 -1673 C ATOM 5877 CD ARG D 184 35.092 79.449 21.032 1.00 57.96 C ANISOU 5877 CD ARG D 184 7533 6619 7869 858 1106 -1934 C ATOM 5878 NE ARG D 184 33.766 80.027 20.776 1.00 62.37 N ANISOU 5878 NE ARG D 184 7919 7060 8719 1037 1198 -1965 N ATOM 5879 CZ ARG D 184 33.521 81.057 19.962 1.00 64.55 C ANISOU 5879 CZ ARG D 184 8154 6969 9402 1120 1096 -1962 C ATOM 5880 NH1 ARG D 184 34.511 81.641 19.284 1.00 63.56 N ANISOU 5880 NH1 ARG D 184 8152 6546 9451 1021 916 -1908 N ATOM 5881 NH2 ARG D 184 32.273 81.497 19.814 1.00 66.41 N ANISOU 5881 NH2 ARG D 184 8208 7134 9889 1307 1180 -1985 N ATOM 5882 N TYR D 185 36.915 74.429 22.628 1.00 46.70 N ANISOU 5882 N TYR D 185 6319 6301 5124 431 1233 -1189 N ATOM 5883 CA TYR D 185 37.857 73.352 22.967 1.00 44.98 C ANISOU 5883 CA TYR D 185 6197 6262 4630 330 1185 -1008 C ATOM 5884 C TYR D 185 39.246 73.493 22.359 1.00 42.86 C ANISOU 5884 C TYR D 185 6044 5828 4413 216 951 -1016 C ATOM 5885 O TYR D 185 39.448 74.198 21.363 1.00 41.84 O ANISOU 5885 O TYR D 185 5917 5413 4569 176 830 -1054 O ATOM 5886 CB TYR D 185 37.296 72.004 22.542 1.00 43.37 C ANISOU 5886 CB TYR D 185 5911 6100 4469 250 1266 -648 C ATOM 5887 CG TYR D 185 36.029 71.591 23.255 1.00 45.68 C ANISOU 5887 CG TYR D 185 6062 6600 4696 326 1527 -564 C ATOM 5888 CD1 TYR D 185 36.084 70.839 24.433 1.00 47.30 C ANISOU 5888 CD1 TYR D 185 6288 7130 4555 356 1692 -441 C ATOM 5889 CD2 TYR D 185 34.773 71.928 22.740 1.00 45.92 C ANISOU 5889 CD2 TYR D 185 5917 6516 5014 374 1616 -577 C ATOM 5890 CE1 TYR D 185 34.926 70.443 25.088 1.00 50.09 C ANISOU 5890 CE1 TYR D 185 6493 7689 4851 418 1971 -323 C ATOM 5891 CE2 TYR D 185 33.603 71.535 23.387 1.00 48.78 C ANISOU 5891 CE2 TYR D 185 6109 7077 5349 435 1877 -490 C ATOM 5892 CZ TYR D 185 33.692 70.793 24.559 1.00 51.14 C ANISOU 5892 CZ TYR D 185 6433 7696 5303 449 2070 -357 C ATOM 5893 OH TYR D 185 32.549 70.399 25.201 1.00 54.24 O ANISOU 5893 OH TYR D 185 6641 8297 5671 501 2364 -234 O ATOM 5894 N SER D 186 40.198 72.802 22.976 1.00 42.51 N ANISOU 5894 N SER D 186 6080 5980 4090 175 898 -952 N ATOM 5895 CA SER D 186 41.555 72.680 22.455 1.00 40.51 C ANISOU 5895 CA SER D 186 5901 5619 3871 64 697 -915 C ATOM 5896 C SER D 186 42.002 71.231 22.554 1.00 39.41 C ANISOU 5896 C SER D 186 5782 5629 3562 11 696 -616 C ATOM 5897 O SER D 186 41.640 70.533 23.504 1.00 41.49 O ANISOU 5897 O SER D 186 6043 6151 3571 72 822 -504 O ATOM 5898 CB SER D 186 42.515 73.567 23.237 1.00 42.26 C ANISOU 5898 CB SER D 186 6184 5911 3963 87 575 -1237 C ATOM 5899 OG SER D 186 42.451 74.888 22.763 1.00 42.51 O ANISOU 5899 OG SER D 186 6199 5663 4291 86 518 -1478 O ATOM 5900 N LEU D 187 42.791 70.780 21.589 1.00 36.54 N ANISOU 5900 N LEU D 187 5434 5105 3346 -90 568 -475 N ATOM 5901 CA LEU D 187 43.190 69.392 21.545 1.00 35.59 C ANISOU 5901 CA LEU D 187 5320 5058 3144 -129 562 -202 C ATOM 5902 C LEU D 187 44.616 69.289 21.029 1.00 34.59 C ANISOU 5902 C LEU D 187 5227 4855 3060 -198 384 -201 C ATOM 5903 O LEU D 187 44.959 69.933 20.024 1.00 33.71 O ANISOU 5903 O LEU D 187 5107 4539 3163 -260 305 -277 O ATOM 5904 CB LEU D 187 42.236 68.621 20.636 1.00 34.16 C ANISOU 5904 CB LEU D 187 5068 4730 3180 -173 645 3 C ATOM 5905 CG LEU D 187 42.627 67.198 20.235 1.00 33.60 C ANISOU 5905 CG LEU D 187 4991 4618 3157 -231 619 256 C ATOM 5906 CD1 LEU D 187 42.216 66.178 21.284 1.00 35.70 C ANISOU 5906 CD1 LEU D 187 5239 5060 3267 -194 758 473 C ATOM 5907 CD2 LEU D 187 42.017 66.851 18.905 1.00 32.40 C ANISOU 5907 CD2 LEU D 187 4775 4251 3283 -295 602 316 C ATOM 5908 N SER D 188 45.443 68.481 21.702 1.00 34.89 N ANISOU 5908 N SER D 188 5289 5066 2900 -178 329 -90 N ATOM 5909 CA SER D 188 46.858 68.349 21.338 1.00 33.81 C ANISOU 5909 CA SER D 188 5151 4892 2803 -225 162 -97 C ATOM 5910 C SER D 188 47.208 66.962 20.841 1.00 32.64 C ANISOU 5910 C SER D 188 4986 4692 2722 -239 157 171 C ATOM 5911 O SER D 188 46.539 65.978 21.172 1.00 33.38 O ANISOU 5911 O SER D 188 5080 4829 2773 -204 263 382 O ATOM 5912 CB SER D 188 47.754 68.682 22.526 1.00 36.06 C ANISOU 5912 CB SER D 188 5453 5423 2827 -172 44 -244 C ATOM 5913 OG SER D 188 47.960 67.540 23.354 1.00 38.05 O ANISOU 5913 OG SER D 188 5721 5898 2838 -91 51 -16 O ATOM 5914 N SER D 189 48.288 66.878 20.073 1.00 31.29 N ANISOU 5914 N SER D 189 4786 4420 2681 -287 44 161 N ATOM 5915 CA SER D 189 48.760 65.594 19.574 1.00 30.14 C ANISOU 5915 CA SER D 189 4615 4210 2625 -279 28 364 C ATOM 5916 C SER D 189 50.258 65.577 19.403 1.00 30.20 C ANISOU 5916 C SER D 189 4572 4247 2657 -283 -110 323 C ATOM 5917 O SER D 189 50.857 66.602 19.092 1.00 30.35 O ANISOU 5917 O SER D 189 4557 4239 2734 -342 -177 144 O ATOM 5918 CB SER D 189 48.122 65.277 18.234 1.00 28.12 C ANISOU 5918 CB SER D 189 4347 3738 2601 -332 93 404 C ATOM 5919 OG SER D 189 48.402 63.948 17.873 1.00 27.38 O ANISOU 5919 OG SER D 189 4230 3569 2605 -310 90 565 O ATOM 5920 N ARG D 190 50.842 64.392 19.564 1.00 30.48 N ANISOU 5920 N ARG D 190 4581 4310 2691 -220 -146 501 N ATOM 5921 CA ARG D 190 52.278 64.189 19.433 1.00 30.56 C ANISOU 5921 CA ARG D 190 4508 4359 2744 -198 -276 487 C ATOM 5922 C ARG D 190 52.626 63.214 18.320 1.00 29.11 C ANISOU 5922 C ARG D 190 4278 3999 2782 -186 -245 582 C ATOM 5923 O ARG D 190 51.956 62.197 18.135 1.00 28.66 O ANISOU 5923 O ARG D 190 4254 3828 2807 -153 -169 729 O ATOM 5924 CB ARG D 190 52.840 63.713 20.766 1.00 32.92 C ANISOU 5924 CB ARG D 190 4796 4889 2823 -89 -381 595 C ATOM 5925 CG ARG D 190 52.737 64.794 21.842 1.00 36.54 C ANISOU 5925 CG ARG D 190 5285 5573 3026 -88 -447 413 C ATOM 5926 CD ARG D 190 52.347 64.251 23.204 1.00 41.28 C ANISOU 5926 CD ARG D 190 5948 6427 3309 34 -441 579 C ATOM 5927 NE ARG D 190 50.978 63.739 23.226 1.00 43.05 N ANISOU 5927 NE ARG D 190 6249 6575 3532 39 -236 759 N ATOM 5928 CZ ARG D 190 49.981 64.260 23.934 1.00 45.15 C ANISOU 5928 CZ ARG D 190 6578 6980 3597 54 -126 703 C ATOM 5929 NH1 ARG D 190 48.779 63.717 23.865 1.00 46.88 N ANISOU 5929 NH1 ARG D 190 6824 7113 3874 46 68 888 N ATOM 5930 NH2 ARG D 190 50.172 65.311 24.712 1.00 47.53 N ANISOU 5930 NH2 ARG D 190 6897 7504 3660 80 -207 444 N ATOM 5931 N LEU D 191 53.671 63.553 17.569 1.00 28.78 N ANISOU 5931 N LEU D 191 4147 3933 2854 -217 -295 478 N ATOM 5932 CA LEU D 191 54.285 62.643 16.589 1.00 28.61 C ANISOU 5932 CA LEU D 191 4058 3800 3012 -174 -273 525 C ATOM 5933 C LEU D 191 55.803 62.582 16.761 1.00 30.16 C ANISOU 5933 C LEU D 191 4111 4102 3248 -126 -382 504 C ATOM 5934 O LEU D 191 56.520 63.541 16.432 1.00 30.41 O ANISOU 5934 O LEU D 191 4054 4184 3318 -204 -408 373 O ATOM 5935 CB LEU D 191 53.941 63.043 15.147 1.00 27.00 C ANISOU 5935 CB LEU D 191 3867 3473 2919 -247 -174 424 C ATOM 5936 CG LEU D 191 54.585 62.187 14.049 1.00 26.43 C ANISOU 5936 CG LEU D 191 3725 3326 2991 -188 -136 413 C ATOM 5937 CD1 LEU D 191 54.343 60.690 14.292 1.00 25.46 C ANISOU 5937 CD1 LEU D 191 3616 3093 2964 -82 -142 522 C ATOM 5938 CD2 LEU D 191 54.091 62.626 12.673 1.00 24.09 C ANISOU 5938 CD2 LEU D 191 3464 2972 2718 -244 -41 322 C ATOM 5939 N ARG D 192 56.290 61.452 17.268 1.00 31.65 N ANISOU 5939 N ARG D 192 4255 4309 3462 3 -445 650 N ATOM 5940 CA ARG D 192 57.721 61.285 17.488 1.00 33.39 C ANISOU 5940 CA ARG D 192 4309 4641 3738 77 -566 645 C ATOM 5941 C ARG D 192 58.320 60.385 16.431 1.00 33.68 C ANISOU 5941 C ARG D 192 4251 4541 4003 155 -501 651 C ATOM 5942 O ARG D 192 57.813 59.293 16.172 1.00 33.71 O ANISOU 5942 O ARG D 192 4316 4381 4111 235 -440 748 O ATOM 5943 CB ARG D 192 58.017 60.735 18.883 1.00 35.66 C ANISOU 5943 CB ARG D 192 4585 5086 3877 204 -715 812 C ATOM 5944 CG ARG D 192 59.465 60.922 19.306 1.00 37.16 C ANISOU 5944 CG ARG D 192 4580 5460 4079 263 -895 762 C ATOM 5945 CD ARG D 192 59.705 60.311 20.657 1.00 39.45 C ANISOU 5945 CD ARG D 192 4869 5938 4182 418 -1060 958 C ATOM 5946 NE ARG D 192 60.547 61.160 21.493 1.00 41.13 N ANISOU 5946 NE ARG D 192 4961 6431 4234 406 -1274 816 N ATOM 5947 CZ ARG D 192 60.804 60.935 22.779 1.00 44.08 C ANISOU 5947 CZ ARG D 192 5330 7068 4349 536 -1463 931 C ATOM 5948 NH1 ARG D 192 61.581 61.775 23.447 1.00 46.42 N ANISOU 5948 NH1 ARG D 192 5500 7625 4513 511 -1682 731 N ATOM 5949 NH2 ARG D 192 60.292 59.877 23.403 1.00 44.52 N ANISOU 5949 NH2 ARG D 192 5498 7134 4282 690 -1439 1250 N ATOM 5950 N VAL D 193 59.394 60.862 15.818 1.00 34.39 N ANISOU 5950 N VAL D 193 4180 4696 4192 129 -503 531 N ATOM 5951 CA VAL D 193 60.107 60.105 14.798 1.00 35.66 C ANISOU 5951 CA VAL D 193 4222 4779 4550 221 -422 498 C ATOM 5952 C VAL D 193 61.598 60.068 15.135 1.00 38.44 C ANISOU 5952 C VAL D 193 4331 5274 5001 299 -533 493 C ATOM 5953 O VAL D 193 62.042 60.746 16.072 1.00 39.39 O ANISOU 5953 O VAL D 193 4379 5557 5032 254 -685 489 O ATOM 5954 CB VAL D 193 59.883 60.680 13.366 1.00 34.11 C ANISOU 5954 CB VAL D 193 4043 4536 4381 122 -247 360 C ATOM 5955 CG1 VAL D 193 58.419 60.611 12.984 1.00 32.37 C ANISOU 5955 CG1 VAL D 193 4032 4185 4082 69 -169 356 C ATOM 5956 CG2 VAL D 193 60.391 62.108 13.255 1.00 33.66 C ANISOU 5956 CG2 VAL D 193 3895 4600 4294 -31 -238 286 C ATOM 5957 N SER D 194 62.363 59.282 14.375 1.00 40.15 N ANISOU 5957 N SER D 194 4406 5440 5409 424 -465 466 N ATOM 5958 CA SER D 194 63.807 59.240 14.542 1.00 42.97 C ANISOU 5958 CA SER D 194 4487 5935 5904 506 -549 450 C ATOM 5959 C SER D 194 64.395 60.566 14.071 1.00 43.48 C ANISOU 5959 C SER D 194 4409 6132 5979 325 -490 322 C ATOM 5960 O SER D 194 63.871 61.196 13.136 1.00 41.98 O ANISOU 5960 O SER D 194 4312 5894 5746 197 -316 254 O ATOM 5961 CB SER D 194 64.403 58.087 13.748 1.00 44.37 C ANISOU 5961 CB SER D 194 4544 6012 6302 698 -453 425 C ATOM 5962 OG SER D 194 64.736 58.500 12.440 1.00 44.68 O ANISOU 5962 OG SER D 194 4497 6086 6392 639 -248 269 O ATOM 5963 N ALA D 195 65.474 60.997 14.722 1.00 45.91 N ANISOU 5963 N ALA D 195 4480 6604 6360 311 -643 302 N ATOM 5964 CA ALA D 195 66.123 62.258 14.363 1.00 46.62 C ANISOU 5964 CA ALA D 195 4389 6788 6537 118 -597 192 C ATOM 5965 C ALA D 195 66.485 62.296 12.868 1.00 46.80 C ANISOU 5965 C ALA D 195 4311 6782 6689 98 -318 154 C ATOM 5966 O ALA D 195 66.290 63.308 12.205 1.00 45.97 O ANISOU 5966 O ALA D 195 4226 6664 6578 -81 -172 127 O ATOM 5967 CB ALA D 195 67.339 62.483 15.224 1.00 49.41 C ANISOU 5967 CB ALA D 195 4447 7319 7009 132 -820 155 C ATOM 5968 N THR D 196 66.967 61.172 12.342 1.00 48.23 N ANISOU 5968 N THR D 196 4395 6955 6976 300 -236 160 N ATOM 5969 CA THR D 196 67.310 61.057 10.921 1.00 49.14 C ANISOU 5969 CA THR D 196 4419 7091 7160 329 42 101 C ATOM 5970 C THR D 196 66.114 61.307 10.016 1.00 47.00 C ANISOU 5970 C THR D 196 4433 6729 6696 252 216 85 C ATOM 5971 O THR D 196 66.267 61.798 8.897 1.00 47.88 O ANISOU 5971 O THR D 196 4499 6915 6779 189 443 64 O ATOM 5972 CB THR D 196 67.871 59.672 10.582 1.00 50.82 C ANISOU 5972 CB THR D 196 4515 7280 7513 599 86 62 C ATOM 5973 OG1 THR D 196 68.831 59.301 11.573 1.00 53.09 O ANISOU 5973 OG1 THR D 196 4564 7637 7970 711 -127 111 O ATOM 5974 CG2 THR D 196 68.531 59.676 9.194 1.00 52.45 C ANISOU 5974 CG2 THR D 196 4548 7596 7786 641 381 -32 C ATOM 5975 N PHE D 197 64.927 60.958 10.495 1.00 44.80 N ANISOU 5975 N PHE D 197 4432 6311 6280 264 114 113 N ATOM 5976 CA PHE D 197 63.732 61.156 9.706 1.00 42.60 C ANISOU 5976 CA PHE D 197 4404 5952 5830 201 238 89 C ATOM 5977 C PHE D 197 63.375 62.633 9.640 1.00 41.49 C ANISOU 5977 C PHE D 197 4317 5844 5604 -23 273 135 C ATOM 5978 O PHE D 197 63.182 63.173 8.545 1.00 41.77 O ANISOU 5978 O PHE D 197 4385 5920 5565 -86 457 140 O ATOM 5979 CB PHE D 197 62.571 60.321 10.240 1.00 41.20 C ANISOU 5979 CB PHE D 197 4464 5604 5585 271 128 110 C ATOM 5980 CG PHE D 197 61.542 60.003 9.201 1.00 40.28 C ANISOU 5980 CG PHE D 197 4535 5405 5364 285 251 30 C ATOM 5981 CD1 PHE D 197 60.286 60.598 9.244 1.00 38.68 C ANISOU 5981 CD1 PHE D 197 4540 5142 5013 160 234 60 C ATOM 5982 CD2 PHE D 197 61.839 59.132 8.164 1.00 41.59 C ANISOU 5982 CD2 PHE D 197 4651 5571 5580 435 376 -104 C ATOM 5983 CE1 PHE D 197 59.336 60.316 8.277 1.00 38.84 C ANISOU 5983 CE1 PHE D 197 4708 5112 4938 177 314 -25 C ATOM 5984 CE2 PHE D 197 60.906 58.854 7.192 1.00 42.62 C ANISOU 5984 CE2 PHE D 197 4943 5659 5592 451 457 -221 C ATOM 5985 CZ PHE D 197 59.645 59.445 7.245 1.00 40.62 C ANISOU 5985 CZ PHE D 197 4888 5354 5192 318 415 -175 C ATOM 5986 N TRP D 198 63.320 63.285 10.803 1.00 40.79 N ANISOU 5986 N TRP D 198 4230 5742 5526 -129 95 165 N ATOM 5987 CA TRP D 198 63.025 64.708 10.879 1.00 39.78 C ANISOU 5987 CA TRP D 198 4137 5595 5381 -336 104 179 C ATOM 5988 C TRP D 198 64.077 65.577 10.193 1.00 41.80 C ANISOU 5988 C TRP D 198 4150 5929 5802 -456 243 199 C ATOM 5989 O TRP D 198 63.737 66.604 9.619 1.00 41.59 O ANISOU 5989 O TRP D 198 4174 5855 5775 -601 361 256 O ATOM 5990 CB TRP D 198 62.854 65.155 12.328 1.00 39.57 C ANISOU 5990 CB TRP D 198 4140 5560 5336 -399 -127 145 C ATOM 5991 CG TRP D 198 62.928 66.661 12.498 1.00 40.12 C ANISOU 5991 CG TRP D 198 4160 5595 5490 -610 -142 102 C ATOM 5992 CD1 TRP D 198 63.949 67.362 13.052 1.00 42.04 C ANISOU 5992 CD1 TRP D 198 4166 5894 5913 -719 -253 27 C ATOM 5993 CD2 TRP D 198 61.953 67.638 12.074 1.00 38.92 C ANISOU 5993 CD2 TRP D 198 4179 5314 5295 -734 -49 123 C ATOM 5994 NE1 TRP D 198 63.672 68.705 13.023 1.00 43.04 N ANISOU 5994 NE1 TRP D 198 4312 5904 6136 -912 -231 -12 N ATOM 5995 CE2 TRP D 198 62.456 68.904 12.424 1.00 40.18 C ANISOU 5995 CE2 TRP D 198 4202 5424 5639 -914 -101 61 C ATOM 5996 CE3 TRP D 198 60.697 67.560 11.445 1.00 36.89 C ANISOU 5996 CE3 TRP D 198 4161 4971 4886 -703 55 182 C ATOM 5997 CZ2 TRP D 198 61.754 70.088 12.171 1.00 40.10 C ANISOU 5997 CZ2 TRP D 198 4299 5253 5685 -1053 -39 73 C ATOM 5998 CZ3 TRP D 198 60.000 68.733 11.193 1.00 35.89 C ANISOU 5998 CZ3 TRP D 198 4131 4722 4782 -829 107 206 C ATOM 5999 CH2 TRP D 198 60.531 69.982 11.557 1.00 38.20 C ANISOU 5999 CH2 TRP D 198 4297 4941 5278 -996 66 161 C ATOM 6000 N GLN D 199 65.345 65.176 10.248 1.00 43.88 N ANISOU 6000 N GLN D 199 4136 6307 6231 -394 239 177 N ATOM 6001 CA GLN D 199 66.421 65.988 9.659 1.00 46.38 C ANISOU 6001 CA GLN D 199 4168 6705 6750 -523 387 213 C ATOM 6002 C GLN D 199 66.442 65.929 8.137 1.00 46.82 C ANISOU 6002 C GLN D 199 4225 6831 6733 -488 703 293 C ATOM 6003 O GLN D 199 67.183 66.679 7.490 1.00 48.76 O ANISOU 6003 O GLN D 199 4261 7147 7117 -608 890 381 O ATOM 6004 CB GLN D 199 67.792 65.592 10.212 1.00 49.07 C ANISOU 6004 CB GLN D 199 4165 7169 7312 -464 279 158 C ATOM 6005 CG GLN D 199 67.998 65.921 11.686 1.00 49.91 C ANISOU 6005 CG GLN D 199 4205 7272 7486 -527 -44 75 C ATOM 6006 CD GLN D 199 69.254 65.291 12.247 1.00 52.68 C ANISOU 6006 CD GLN D 199 4231 7771 8014 -407 -195 29 C ATOM 6007 OE1 GLN D 199 69.551 64.118 11.993 1.00 52.59 O ANISOU 6007 OE1 GLN D 199 4175 7811 7997 -182 -154 54 O ATOM 6008 NE2 GLN D 199 70.004 66.070 13.016 1.00 55.13 N ANISOU 6008 NE2 GLN D 199 4296 8141 8510 -551 -385 -54 N ATOM 6009 N ASN D 200 65.636 65.028 7.578 1.00 45.22 N ANISOU 6009 N ASN D 200 4247 6621 6312 -324 762 260 N ATOM 6010 CA ASN D 200 65.505 64.895 6.132 1.00 46.01 C ANISOU 6010 CA ASN D 200 4393 6831 6258 -258 1033 295 C ATOM 6011 C ASN D 200 64.652 66.036 5.574 1.00 45.07 C ANISOU 6011 C ASN D 200 4450 6664 6009 -415 1126 433 C ATOM 6012 O ASN D 200 63.455 66.123 5.869 1.00 42.95 O ANISOU 6012 O ASN D 200 4442 6267 5609 -431 1002 420 O ATOM 6013 CB ASN D 200 64.904 63.529 5.766 1.00 45.14 C ANISOU 6013 CB ASN D 200 4453 6713 5985 -31 1021 156 C ATOM 6014 CG ASN D 200 65.149 63.134 4.304 1.00 46.96 C ANISOU 6014 CG ASN D 200 4649 7130 6062 99 1291 107 C ATOM 6015 OD1 ASN D 200 65.587 63.939 3.480 1.00 48.65 O ANISOU 6015 OD1 ASN D 200 4757 7501 6225 17 1514 231 O ATOM 6016 ND2 ASN D 200 64.858 61.880 3.985 1.00 46.47 N ANISOU 6016 ND2 ASN D 200 4675 7052 5928 307 1276 -74 N ATOM 6017 N PRO D 201 65.266 66.921 4.772 1.00 46.95 N ANISOU 6017 N PRO D 201 4533 7001 6304 -526 1354 590 N ATOM 6018 CA PRO D 201 64.561 68.070 4.211 1.00 46.90 C ANISOU 6018 CA PRO D 201 4668 6934 6216 -667 1454 779 C ATOM 6019 C PRO D 201 63.501 67.707 3.173 1.00 46.06 C ANISOU 6019 C PRO D 201 4826 6919 5755 -533 1543 799 C ATOM 6020 O PRO D 201 62.783 68.586 2.704 1.00 45.64 O ANISOU 6020 O PRO D 201 4915 6821 5606 -613 1596 970 O ATOM 6021 CB PRO D 201 65.687 68.877 3.552 1.00 50.27 C ANISOU 6021 CB PRO D 201 4811 7470 6819 -791 1713 974 C ATOM 6022 CG PRO D 201 66.704 67.878 3.226 1.00 52.04 C ANISOU 6022 CG PRO D 201 4814 7909 7050 -633 1832 866 C ATOM 6023 CD PRO D 201 66.675 66.902 4.361 1.00 49.94 C ANISOU 6023 CD PRO D 201 4568 7550 6857 -524 1544 629 C ATOM 6024 N ARG D 202 63.413 66.428 2.822 1.00 46.22 N ANISOU 6024 N ARG D 202 4899 7056 5605 -324 1543 614 N ATOM 6025 CA ARG D 202 62.495 65.985 1.781 1.00 46.70 C ANISOU 6025 CA ARG D 202 5178 7237 5330 -186 1607 568 C ATOM 6026 C ARG D 202 61.296 65.253 2.353 1.00 44.22 C ANISOU 6026 C ARG D 202 5094 6754 4953 -120 1362 394 C ATOM 6027 O ARG D 202 60.498 64.685 1.608 1.00 44.17 O ANISOU 6027 O ARG D 202 5249 6824 4709 0 1359 286 O ATOM 6028 CB ARG D 202 63.210 65.127 0.739 1.00 49.47 C ANISOU 6028 CB ARG D 202 5416 7858 5521 4 1819 453 C ATOM 6029 CG ARG D 202 64.426 65.808 0.118 1.00 53.44 C ANISOU 6029 CG ARG D 202 5657 8566 6082 -55 2111 649 C ATOM 6030 CD ARG D 202 64.600 65.442 -1.341 1.00 57.23 C ANISOU 6030 CD ARG D 202 6139 9393 6214 120 2384 629 C ATOM 6031 NE ARG D 202 64.237 64.053 -1.609 1.00 57.96 N ANISOU 6031 NE ARG D 202 6341 9540 6142 357 2300 279 N ATOM 6032 CZ ARG D 202 64.486 63.418 -2.750 1.00 61.05 C ANISOU 6032 CZ ARG D 202 6714 10236 6246 563 2500 124 C ATOM 6033 NH1 ARG D 202 65.118 64.035 -3.740 1.00 65.05 N ANISOU 6033 NH1 ARG D 202 7098 11066 6552 571 2823 327 N ATOM 6034 NH2 ARG D 202 64.108 62.158 -2.897 1.00 61.41 N ANISOU 6034 NH2 ARG D 202 6858 10262 6213 764 2386 -237 N ATOM 6035 N ASN D 203 61.171 65.282 3.677 1.00 42.70 N ANISOU 6035 N ASN D 203 4903 6350 4971 -202 1157 366 N ATOM 6036 CA ASN D 203 60.000 64.755 4.352 1.00 40.72 C ANISOU 6036 CA ASN D 203 4853 5930 4689 -173 950 264 C ATOM 6037 C ASN D 203 59.036 65.859 4.783 1.00 39.48 C ANISOU 6037 C ASN D 203 4835 5639 4525 -319 862 386 C ATOM 6038 O ASN D 203 59.370 66.703 5.617 1.00 39.21 O ANISOU 6038 O ASN D 203 4728 5508 4661 -455 807 460 O ATOM 6039 CB ASN D 203 60.419 63.906 5.544 1.00 40.33 C ANISOU 6039 CB ASN D 203 4727 5768 4827 -125 793 163 C ATOM 6040 CG ASN D 203 61.018 62.587 5.127 1.00 42.69 C ANISOU 6040 CG ASN D 203 4937 6129 5153 65 843 10 C ATOM 6041 OD1 ASN D 203 60.769 62.102 4.021 1.00 43.98 O ANISOU 6041 OD1 ASN D 203 5158 6392 5159 175 954 -95 O ATOM 6042 ND2 ASN D 203 61.815 61.992 6.011 1.00 43.77 N ANISOU 6042 ND2 ASN D 203 4928 6213 5488 123 751 -17 N ATOM 6043 N HIS D 204 57.837 65.838 4.203 1.00 39.07 N ANISOU 6043 N HIS D 204 4969 5585 4291 -281 838 379 N ATOM 6044 CA HIS D 204 56.810 66.831 4.469 1.00 38.20 C ANISOU 6044 CA HIS D 204 4987 5353 4174 -381 765 487 C ATOM 6045 C HIS D 204 55.938 66.300 5.586 1.00 36.07 C ANISOU 6045 C HIS D 204 4814 4922 3969 -376 581 374 C ATOM 6046 O HIS D 204 55.391 65.205 5.484 1.00 35.78 O ANISOU 6046 O HIS D 204 4842 4879 3873 -277 521 246 O ATOM 6047 CB HIS D 204 55.991 67.075 3.194 1.00 39.22 C ANISOU 6047 CB HIS D 204 5237 5603 4063 -319 830 556 C ATOM 6048 CG HIS D 204 55.225 68.367 3.181 1.00 40.36 C ANISOU 6048 CG HIS D 204 5462 5647 4225 -409 810 743 C ATOM 6049 ND1 HIS D 204 54.010 68.501 2.541 1.00 41.67 N ANISOU 6049 ND1 HIS D 204 5767 5848 4218 -346 752 775 N ATOM 6050 CD2 HIS D 204 55.501 69.582 3.715 1.00 41.88 C ANISOU 6050 CD2 HIS D 204 5603 5690 4619 -549 830 893 C ATOM 6051 CE1 HIS D 204 53.571 69.741 2.682 1.00 41.78 C ANISOU 6051 CE1 HIS D 204 5815 5734 4327 -427 747 961 C ATOM 6052 NE2 HIS D 204 54.460 70.419 3.385 1.00 41.92 N ANISOU 6052 NE2 HIS D 204 5724 5622 4583 -554 799 1027 N ATOM 6053 N PHE D 205 55.834 67.061 6.669 1.00 35.34 N ANISOU 6053 N PHE D 205 4718 4699 4009 -484 498 414 N ATOM 6054 CA PHE D 205 55.002 66.668 7.810 1.00 33.58 C ANISOU 6054 CA PHE D 205 4581 4361 3815 -479 354 337 C ATOM 6055 C PHE D 205 53.729 67.488 7.838 1.00 32.81 C ANISOU 6055 C PHE D 205 4605 4174 3686 -521 321 380 C ATOM 6056 O PHE D 205 53.747 68.700 7.566 1.00 33.47 O ANISOU 6056 O PHE D 205 4684 4215 3818 -597 367 478 O ATOM 6057 CB PHE D 205 55.757 66.856 9.120 1.00 33.50 C ANISOU 6057 CB PHE D 205 4479 4319 3930 -535 269 308 C ATOM 6058 CG PHE D 205 56.938 65.953 9.259 1.00 35.07 C ANISOU 6058 CG PHE D 205 4540 4600 4185 -467 266 270 C ATOM 6059 CD1 PHE D 205 58.201 66.368 8.855 1.00 37.33 C ANISOU 6059 CD1 PHE D 205 4649 4968 4565 -508 348 299 C ATOM 6060 CD2 PHE D 205 56.793 64.677 9.781 1.00 34.98 C ANISOU 6060 CD2 PHE D 205 4553 4570 4166 -357 191 224 C ATOM 6061 CE1 PHE D 205 59.293 65.524 8.976 1.00 38.40 C ANISOU 6061 CE1 PHE D 205 4628 5187 4775 -425 344 258 C ATOM 6062 CE2 PHE D 205 57.883 63.830 9.902 1.00 36.18 C ANISOU 6062 CE2 PHE D 205 4568 4778 4401 -267 181 200 C ATOM 6063 CZ PHE D 205 59.132 64.253 9.499 1.00 37.59 C ANISOU 6063 CZ PHE D 205 4563 5058 4661 -292 252 205 C ATOM 6064 N ARG D 206 52.619 66.834 8.162 1.00 31.54 N ANISOU 6064 N ARG D 206 4537 3965 3482 -472 247 320 N ATOM 6065 CA ARG D 206 51.353 67.550 8.186 1.00 31.05 C ANISOU 6065 CA ARG D 206 4561 3829 3407 -493 216 351 C ATOM 6066 C ARG D 206 50.359 67.049 9.224 1.00 30.32 C ANISOU 6066 C ARG D 206 4516 3667 3339 -480 143 291 C ATOM 6067 O ARG D 206 49.922 65.883 9.180 1.00 30.04 O ANISOU 6067 O ARG D 206 4491 3629 3292 -429 117 243 O ATOM 6068 CB ARG D 206 50.711 67.604 6.790 1.00 31.37 C ANISOU 6068 CB ARG D 206 4650 3939 3330 -437 244 393 C ATOM 6069 CG ARG D 206 49.517 68.521 6.733 1.00 30.36 C ANISOU 6069 CG ARG D 206 4581 3738 3216 -445 206 457 C ATOM 6070 CD ARG D 206 48.865 68.471 5.391 1.00 30.87 C ANISOU 6070 CD ARG D 206 4685 3912 3133 -368 194 500 C ATOM 6071 NE ARG D 206 49.616 69.217 4.393 1.00 33.68 N ANISOU 6071 NE ARG D 206 5030 4365 3400 -363 293 661 N ATOM 6072 CZ ARG D 206 49.525 70.534 4.214 1.00 34.84 C ANISOU 6072 CZ ARG D 206 5187 4435 3616 -397 332 849 C ATOM 6073 NH1 ARG D 206 50.245 71.129 3.273 1.00 35.46 N ANISOU 6073 NH1 ARG D 206 5247 4607 3621 -397 448 1042 N ATOM 6074 NH2 ARG D 206 48.716 71.259 4.983 1.00 35.18 N ANISOU 6074 NH2 ARG D 206 5250 4299 3817 -424 270 853 N ATOM 6075 N CYS D 207 50.015 67.955 10.143 1.00 30.07 N ANISOU 6075 N CYS D 207 4500 3570 3357 -528 123 289 N ATOM 6076 CA CYS D 207 48.942 67.741 11.091 1.00 29.92 C ANISOU 6076 CA CYS D 207 4518 3514 3336 -512 93 253 C ATOM 6077 C CYS D 207 47.644 68.219 10.464 1.00 28.91 C ANISOU 6077 C CYS D 207 4423 3337 3223 -490 96 273 C ATOM 6078 O CYS D 207 47.585 69.331 9.939 1.00 29.68 O ANISOU 6078 O CYS D 207 4530 3390 3357 -502 109 317 O ATOM 6079 CB CYS D 207 49.191 68.506 12.386 1.00 30.62 C ANISOU 6079 CB CYS D 207 4602 3595 3438 -547 73 196 C ATOM 6080 SG CYS D 207 47.923 68.112 13.635 1.00 35.69 S ANISOU 6080 SG CYS D 207 5280 4260 4020 -504 83 168 S ATOM 6081 N GLN D 208 46.609 67.385 10.535 1.00 27.51 N ANISOU 6081 N GLN D 208 4246 3157 3049 -458 81 255 N ATOM 6082 CA GLN D 208 45.341 67.654 9.871 1.00 26.86 C ANISOU 6082 CA GLN D 208 4158 3052 2994 -428 56 261 C ATOM 6083 C GLN D 208 44.152 67.449 10.774 1.00 26.73 C ANISOU 6083 C GLN D 208 4108 3005 3045 -423 72 238 C ATOM 6084 O GLN D 208 43.909 66.325 11.236 1.00 27.07 O ANISOU 6084 O GLN D 208 4122 3047 3117 -435 85 236 O ATOM 6085 CB GLN D 208 45.165 66.726 8.680 1.00 27.01 C ANISOU 6085 CB GLN D 208 4165 3123 2976 -396 6 231 C ATOM 6086 CG GLN D 208 43.793 66.843 8.062 1.00 27.75 C ANISOU 6086 CG GLN D 208 4224 3220 3099 -361 -59 215 C ATOM 6087 CD GLN D 208 43.432 65.699 7.153 1.00 27.82 C ANISOU 6087 CD GLN D 208 4199 3275 3097 -339 -140 112 C ATOM 6088 OE1 GLN D 208 43.770 65.710 5.974 1.00 29.63 O ANISOU 6088 OE1 GLN D 208 4454 3612 3193 -289 -185 86 O ATOM 6089 NE2 GLN D 208 42.714 64.723 7.684 1.00 26.75 N ANISOU 6089 NE2 GLN D 208 3997 3062 3105 -374 -156 48 N ATOM 6090 N VAL D 209 43.382 68.515 10.995 1.00 26.86 N ANISOU 6090 N VAL D 209 4114 2983 3110 -399 86 236 N ATOM 6091 CA VAL D 209 42.136 68.415 11.772 1.00 26.85 C ANISOU 6091 CA VAL D 209 4051 2975 3176 -379 128 212 C ATOM 6092 C VAL D 209 40.912 68.450 10.882 1.00 27.22 C ANISOU 6092 C VAL D 209 4022 3009 3313 -340 70 218 C ATOM 6093 O VAL D 209 40.718 69.380 10.098 1.00 27.45 O ANISOU 6093 O VAL D 209 4058 3014 3357 -290 17 247 O ATOM 6094 CB VAL D 209 42.009 69.507 12.843 1.00 27.34 C ANISOU 6094 CB VAL D 209 4125 3018 3245 -354 194 155 C ATOM 6095 CG1 VAL D 209 40.805 69.228 13.712 1.00 27.41 C ANISOU 6095 CG1 VAL D 209 4055 3069 3289 -324 279 136 C ATOM 6096 CG2 VAL D 209 43.263 69.551 13.700 1.00 27.78 C ANISOU 6096 CG2 VAL D 209 4242 3115 3197 -390 209 116 C ATOM 6097 N GLN D 210 40.103 67.407 10.997 1.00 27.62 N ANISOU 6097 N GLN D 210 3984 3071 3438 -363 72 206 N ATOM 6098 CA GLN D 210 38.840 67.336 10.289 1.00 28.70 C ANISOU 6098 CA GLN D 210 4003 3210 3690 -335 -2 184 C ATOM 6099 C GLN D 210 37.763 67.775 11.267 1.00 29.88 C ANISOU 6099 C GLN D 210 4050 3353 3951 -309 98 185 C ATOM 6100 O GLN D 210 37.424 67.057 12.217 1.00 30.47 O ANISOU 6100 O GLN D 210 4062 3438 4076 -356 209 206 O ATOM 6101 CB GLN D 210 38.595 65.921 9.772 1.00 28.65 C ANISOU 6101 CB GLN D 210 3928 3197 3760 -393 -70 135 C ATOM 6102 CG GLN D 210 37.198 65.658 9.283 1.00 30.30 C ANISOU 6102 CG GLN D 210 3967 3409 4135 -391 -155 81 C ATOM 6103 CD GLN D 210 36.948 66.177 7.886 1.00 31.71 C ANISOU 6103 CD GLN D 210 4141 3669 4237 -313 -333 36 C ATOM 6104 OE1 GLN D 210 36.165 67.101 7.693 1.00 32.94 O ANISOU 6104 OE1 GLN D 210 4230 3854 4430 -235 -375 71 O ATOM 6105 NE2 GLN D 210 37.604 65.576 6.899 1.00 32.52 N ANISOU 6105 NE2 GLN D 210 4310 3824 4222 -314 -437 -39 N ATOM 6106 N PHE D 211 37.261 68.985 11.052 1.00 30.57 N ANISOU 6106 N PHE D 211 4114 3421 4079 -222 76 180 N ATOM 6107 CA PHE D 211 36.201 69.535 11.880 1.00 31.96 C ANISOU 6107 CA PHE D 211 4175 3596 4373 -164 178 151 C ATOM 6108 C PHE D 211 34.819 69.140 11.333 1.00 33.58 C ANISOU 6108 C PHE D 211 4176 3825 4757 -146 110 146 C ATOM 6109 O PHE D 211 34.627 69.055 10.112 1.00 33.69 O ANISOU 6109 O PHE D 211 4162 3853 4787 -125 -64 151 O ATOM 6110 CB PHE D 211 36.362 71.049 11.935 1.00 32.07 C ANISOU 6110 CB PHE D 211 4249 3534 4401 -65 182 128 C ATOM 6111 CG PHE D 211 35.267 71.767 12.667 1.00 33.11 C ANISOU 6111 CG PHE D 211 4256 3652 4672 33 281 61 C ATOM 6112 CD1 PHE D 211 35.125 71.638 14.043 1.00 33.73 C ANISOU 6112 CD1 PHE D 211 4313 3801 4700 30 461 -15 C ATOM 6113 CD2 PHE D 211 34.405 72.609 11.982 1.00 33.09 C ANISOU 6113 CD2 PHE D 211 4154 3584 4834 151 199 79 C ATOM 6114 CE1 PHE D 211 34.121 72.328 14.722 1.00 35.49 C ANISOU 6114 CE1 PHE D 211 4411 4036 5037 143 579 -105 C ATOM 6115 CE2 PHE D 211 33.408 73.301 12.641 1.00 34.95 C ANISOU 6115 CE2 PHE D 211 4255 3798 5227 266 298 0 C ATOM 6116 CZ PHE D 211 33.264 73.167 14.013 1.00 36.54 C ANISOU 6116 CZ PHE D 211 4431 4075 5378 262 499 -108 C ATOM 6117 N TYR D 212 33.871 68.880 12.233 1.00 34.75 N ANISOU 6117 N TYR D 212 4168 4005 5029 -151 248 135 N ATOM 6118 CA TYR D 212 32.488 68.677 11.819 1.00 36.70 C ANISOU 6118 CA TYR D 212 4172 4273 5498 -130 195 120 C ATOM 6119 C TYR D 212 31.616 69.816 12.329 1.00 38.62 C ANISOU 6119 C TYR D 212 4300 4523 5850 7 287 87 C ATOM 6120 O TYR D 212 31.496 70.017 13.547 1.00 39.34 O ANISOU 6120 O TYR D 212 4378 4653 5915 28 501 64 O ATOM 6121 CB TYR D 212 31.972 67.318 12.283 1.00 37.34 C ANISOU 6121 CB TYR D 212 4102 4369 5715 -263 284 148 C ATOM 6122 CG TYR D 212 32.684 66.184 11.589 1.00 36.61 C ANISOU 6122 CG TYR D 212 4090 4226 5593 -377 157 143 C ATOM 6123 CD1 TYR D 212 33.841 65.633 12.138 1.00 35.22 C ANISOU 6123 CD1 TYR D 212 4093 4023 5265 -439 241 198 C ATOM 6124 CD2 TYR D 212 32.227 65.682 10.366 1.00 36.53 C ANISOU 6124 CD2 TYR D 212 3972 4206 5700 -404 -62 57 C ATOM 6125 CE1 TYR D 212 34.517 64.613 11.503 1.00 34.30 C ANISOU 6125 CE1 TYR D 212 4043 3843 5148 -518 134 173 C ATOM 6126 CE2 TYR D 212 32.902 64.650 9.720 1.00 35.56 C ANISOU 6126 CE2 TYR D 212 3926 4035 5552 -490 -175 -2 C ATOM 6127 CZ TYR D 212 34.049 64.126 10.295 1.00 34.76 C ANISOU 6127 CZ TYR D 212 3999 3878 5330 -543 -65 59 C ATOM 6128 OH TYR D 212 34.748 63.108 9.684 1.00 34.71 O ANISOU 6128 OH TYR D 212 4060 3805 5324 -604 -163 -13 O ATOM 6129 N GLY D 213 31.035 70.566 11.390 1.00 39.69 N ANISOU 6129 N GLY D 213 4356 4634 6092 121 122 84 N ATOM 6130 CA GLY D 213 30.177 71.703 11.713 1.00 41.76 C ANISOU 6130 CA GLY D 213 4490 4868 6510 285 181 50 C ATOM 6131 C GLY D 213 28.901 71.739 10.894 1.00 44.24 C ANISOU 6131 C GLY D 213 4540 5222 7049 366 22 60 C ATOM 6132 O GLY D 213 28.269 70.714 10.677 1.00 44.81 O ANISOU 6132 O GLY D 213 4428 5368 7229 266 -25 46 O ATOM 6133 N LEU D 214 28.522 72.928 10.445 1.00 46.26 N ANISOU 6133 N LEU D 214 4762 5412 7402 550 -69 85 N ATOM 6134 CA LEU D 214 27.305 73.111 9.664 1.00 49.70 C ANISOU 6134 CA LEU D 214 4933 5900 8051 668 -249 107 C ATOM 6135 C LEU D 214 27.463 72.596 8.241 1.00 50.50 C ANISOU 6135 C LEU D 214 5063 6088 8038 634 -550 168 C ATOM 6136 O LEU D 214 28.563 72.598 7.697 1.00 49.19 O ANISOU 6136 O LEU D 214 5153 5906 7632 592 -619 230 O ATOM 6137 CB LEU D 214 26.929 74.592 9.624 1.00 51.44 C ANISOU 6137 CB LEU D 214 5124 6000 8420 905 -261 143 C ATOM 6138 CG LEU D 214 26.137 75.183 10.794 1.00 52.98 C ANISOU 6138 CG LEU D 214 5142 6155 8834 1022 -21 26 C ATOM 6139 CD1 LEU D 214 26.958 75.218 12.067 1.00 51.67 C ANISOU 6139 CD1 LEU D 214 5168 5952 8512 943 252 -82 C ATOM 6140 CD2 LEU D 214 25.656 76.574 10.454 1.00 54.92 C ANISOU 6140 CD2 LEU D 214 5323 6251 9293 1281 -102 65 C ATOM 6141 N SER D 215 26.368 72.143 7.642 1.00 53.61 N ANISOU 6141 N SER D 215 5177 6595 8598 655 -729 131 N ATOM 6142 CA SER D 215 26.379 71.811 6.225 1.00 55.66 C ANISOU 6142 CA SER D 215 5441 6981 8726 673 -1054 153 C ATOM 6143 C SER D 215 26.008 73.070 5.445 1.00 58.52 C ANISOU 6143 C SER D 215 5783 7351 9102 925 -1236 303 C ATOM 6144 O SER D 215 25.567 74.051 6.037 1.00 59.88 O ANISOU 6144 O SER D 215 5879 7402 9470 1071 -1114 350 O ATOM 6145 CB SER D 215 25.398 70.676 5.925 1.00 57.44 C ANISOU 6145 CB SER D 215 5359 7328 9136 564 -1200 9 C ATOM 6146 OG SER D 215 24.087 71.179 5.731 1.00 61.04 O ANISOU 6146 OG SER D 215 5488 7848 9858 715 -1323 8 O ATOM 6147 N GLU D 216 26.176 73.051 4.125 1.00 60.57 N ANISOU 6147 N GLU D 216 6107 7755 9150 994 -1523 380 N ATOM 6148 CA GLU D 216 25.750 74.182 3.291 1.00 64.28 C ANISOU 6148 CA GLU D 216 6540 8258 9624 1252 -1723 578 C ATOM 6149 C GLU D 216 24.231 74.372 3.312 1.00 67.56 C ANISOU 6149 C GLU D 216 6565 8735 10368 1392 -1855 530 C ATOM 6150 O GLU D 216 23.724 75.415 2.898 1.00 70.21 O ANISOU 6150 O GLU D 216 6823 9049 10805 1636 -1980 703 O ATOM 6151 CB GLU D 216 26.235 74.035 1.844 1.00 65.66 C ANISOU 6151 CB GLU D 216 6863 8648 9435 1307 -2003 687 C ATOM 6152 CG GLU D 216 27.751 73.934 1.690 1.00 64.97 C ANISOU 6152 CG GLU D 216 7135 8524 9025 1197 -1871 761 C ATOM 6153 CD GLU D 216 28.245 72.489 1.581 1.00 65.71 C ANISOU 6153 CD GLU D 216 7279 8741 8946 979 -1883 525 C ATOM 6154 OE1 GLU D 216 27.635 71.576 2.203 1.00 65.89 O ANISOU 6154 OE1 GLU D 216 7104 8743 9188 839 -1846 303 O ATOM 6155 OE2 GLU D 216 29.252 72.273 0.863 1.00 65.17 O ANISOU 6155 OE2 GLU D 216 7439 8780 8544 953 -1916 573 O ATOM 6156 N ASN D 217 23.512 73.364 3.796 1.00 67.89 N ANISOU 6156 N ASN D 217 6346 8841 10608 1238 -1821 315 N ATOM 6157 CA ASN D 217 22.053 73.437 3.895 1.00 71.34 C ANISOU 6157 CA ASN D 217 6357 9346 11402 1341 -1920 248 C ATOM 6158 C ASN D 217 21.561 73.938 5.265 1.00 71.14 C ANISOU 6158 C ASN D 217 6184 9149 11696 1376 -1575 216 C ATOM 6159 O ASN D 217 20.358 73.926 5.551 1.00 73.81 O ANISOU 6159 O ASN D 217 6138 9538 12369 1440 -1577 144 O ATOM 6160 CB ASN D 217 21.425 72.087 3.512 1.00 72.89 C ANISOU 6160 CB ASN D 217 6289 9718 11688 1158 -2109 33 C ATOM 6161 CG ASN D 217 21.709 71.698 2.055 1.00 74.41 C ANISOU 6161 CG ASN D 217 6577 10133 11561 1184 -2502 9 C ATOM 6162 OD1 ASN D 217 21.347 72.425 1.124 1.00 77.77 O ANISOU 6162 OD1 ASN D 217 6958 10706 11885 1420 -2784 142 O ATOM 6163 ND2 ASN D 217 22.353 70.548 1.858 1.00 71.75 N ANISOU 6163 ND2 ASN D 217 6371 9834 11058 960 -2519 -159 N ATOM 6164 N ASP D 218 22.506 74.389 6.092 1.00 68.05 N ANISOU 6164 N ASP D 218 6087 8577 11191 1343 -1284 254 N ATOM 6165 CA ASP D 218 22.212 74.972 7.400 1.00 67.67 C ANISOU 6165 CA ASP D 218 5962 8388 11361 1404 -948 196 C ATOM 6166 C ASP D 218 22.216 76.502 7.324 1.00 68.91 C ANISOU 6166 C ASP D 218 6195 8369 11618 1683 -956 315 C ATOM 6167 O ASP D 218 23.011 77.087 6.591 1.00 68.14 O ANISOU 6167 O ASP D 218 6364 8191 11336 1750 -1095 479 O ATOM 6168 CB ASP D 218 23.231 74.492 8.445 1.00 64.27 C ANISOU 6168 CB ASP D 218 5792 7883 10745 1198 -639 123 C ATOM 6169 CG ASP D 218 22.987 73.060 8.904 1.00 63.11 C ANISOU 6169 CG ASP D 218 5498 7851 10631 949 -534 20 C ATOM 6170 OD1 ASP D 218 21.814 72.644 8.973 1.00 65.97 O ANISOU 6170 OD1 ASP D 218 5486 8307 11273 942 -550 -37 O ATOM 6171 OD2 ASP D 218 23.967 72.353 9.219 1.00 59.28 O ANISOU 6171 OD2 ASP D 218 5254 7345 9925 760 -429 10 O ATOM 6172 N GLU D 219 21.334 77.134 8.098 1.00 70.93 N ANISOU 6172 N GLU D 219 6206 8554 12189 1846 -787 236 N ATOM 6173 CA GLU D 219 21.159 78.592 8.106 1.00 72.83 C ANISOU 6173 CA GLU D 219 6459 8583 12631 2138 -785 315 C ATOM 6174 C GLU D 219 22.272 79.297 8.883 1.00 70.35 C ANISOU 6174 C GLU D 219 6490 8027 12214 2118 -543 269 C ATOM 6175 O GLU D 219 22.809 78.729 9.831 1.00 68.27 O ANISOU 6175 O GLU D 219 6346 7799 11796 1928 -296 115 O ATOM 6176 CB GLU D 219 19.811 78.933 8.742 1.00 76.51 C ANISOU 6176 CB GLU D 219 6513 9068 13490 2323 -660 190 C ATOM 6177 CG GLU D 219 19.061 80.073 8.063 1.00 81.41 C ANISOU 6177 CG GLU D 219 6952 9577 14404 2665 -876 329 C ATOM 6178 CD GLU D 219 18.361 79.639 6.784 1.00 84.49 C ANISOU 6178 CD GLU D 219 7112 10189 14801 2716 -1280 477 C ATOM 6179 OE1 GLU D 219 17.853 78.495 6.734 1.00 84.36 O ANISOU 6179 OE1 GLU D 219 6867 10414 14771 2531 -1332 365 O ATOM 6180 OE2 GLU D 219 18.311 80.448 5.833 1.00 87.61 O ANISOU 6180 OE2 GLU D 219 7546 10515 15225 2945 -1552 708 O ATOM 6181 N TRP D 220 22.611 80.530 8.501 1.00 70.87 N ANISOU 6181 N TRP D 220 6701 7842 12384 2314 -621 406 N ATOM 6182 CA TRP D 220 23.684 81.263 9.186 1.00 68.71 C ANISOU 6182 CA TRP D 220 6732 7304 12069 2285 -424 338 C ATOM 6183 C TRP D 220 23.471 82.766 9.220 1.00 71.86 C ANISOU 6183 C TRP D 220 7117 7365 12822 2567 -420 380 C ATOM 6184 O TRP D 220 23.829 83.477 8.277 1.00 73.05 O ANISOU 6184 O TRP D 220 7393 7341 13021 2671 -613 654 O ATOM 6185 CB TRP D 220 25.051 80.943 8.567 1.00 65.50 C ANISOU 6185 CB TRP D 220 6674 6892 11320 2083 -516 494 C ATOM 6186 CG TRP D 220 26.217 81.442 9.380 1.00 62.41 C ANISOU 6186 CG TRP D 220 6562 6279 10871 1987 -312 377 C ATOM 6187 CD1 TRP D 220 27.153 82.354 8.997 1.00 61.42 C ANISOU 6187 CD1 TRP D 220 6671 5884 10783 2009 -354 527 C ATOM 6188 CD2 TRP D 220 26.557 81.056 10.716 1.00 59.81 C ANISOU 6188 CD2 TRP D 220 6287 5995 10444 1853 -44 89 C ATOM 6189 NE1 TRP D 220 28.063 82.554 10.005 1.00 58.89 N ANISOU 6189 NE1 TRP D 220 6531 5427 10417 1884 -151 311 N ATOM 6190 CE2 TRP D 220 27.718 81.772 11.073 1.00 58.21 C ANISOU 6190 CE2 TRP D 220 6349 5551 10218 1801 31 38 C ATOM 6191 CE3 TRP D 220 25.994 80.169 11.646 1.00 59.10 C ANISOU 6191 CE3 TRP D 220 6036 6139 10280 1771 139 -110 C ATOM 6192 CZ2 TRP D 220 28.328 81.631 12.322 1.00 57.02 C ANISOU 6192 CZ2 TRP D 220 6311 5415 9940 1686 250 -236 C ATOM 6193 CZ3 TRP D 220 26.604 80.029 12.888 1.00 57.37 C ANISOU 6193 CZ3 TRP D 220 5947 5941 9909 1667 385 -336 C ATOM 6194 CH2 TRP D 220 27.756 80.760 13.214 1.00 56.16 C ANISOU 6194 CH2 TRP D 220 6063 5573 9702 1634 422 -413 C ATOM 6195 N THR D 221 22.915 83.248 10.329 1.00 73.44 N ANISOU 6195 N THR D 221 7167 7467 13271 2696 -183 110 N ATOM 6196 CA THR D 221 22.579 84.669 10.482 1.00 76.83 C ANISOU 6196 CA THR D 221 7539 7541 14113 2993 -158 81 C ATOM 6197 C THR D 221 23.791 85.530 10.842 1.00 75.99 C ANISOU 6197 C THR D 221 7761 7079 14031 2945 -66 19 C ATOM 6198 O THR D 221 23.927 86.652 10.359 1.00 78.54 O ANISOU 6198 O THR D 221 8143 7044 14655 3122 -168 180 O ATOM 6199 CB THR D 221 21.488 84.877 11.548 1.00 79.61 C ANISOU 6199 CB THR D 221 7581 7935 14733 3175 77 -235 C ATOM 6200 OG1 THR D 221 21.984 84.466 12.828 1.00 77.63 O ANISOU 6200 OG1 THR D 221 7447 7788 14260 3008 382 -557 O ATOM 6201 CG2 THR D 221 20.229 84.074 11.201 1.00 81.06 C ANISOU 6201 CG2 THR D 221 7378 8449 14972 3217 -9 -173 C ATOM 6202 N GLN D 222 24.660 84.988 11.692 1.00 72.74 N ANISOU 6202 N GLN D 222 7546 6764 13329 2704 118 -202 N ATOM 6203 CA GLN D 222 25.849 85.682 12.179 1.00 71.72 C ANISOU 6203 CA GLN D 222 7699 6342 13208 2621 206 -331 C ATOM 6204 C GLN D 222 26.712 86.255 11.067 1.00 71.57 C ANISOU 6204 C GLN D 222 7889 6059 13247 2582 6 23 C ATOM 6205 O GLN D 222 26.748 85.733 9.945 1.00 70.30 O ANISOU 6205 O GLN D 222 7746 6066 12900 2525 -188 366 O ATOM 6206 CB GLN D 222 26.695 84.756 13.049 1.00 68.04 C ANISOU 6206 CB GLN D 222 7402 6118 12332 2344 367 -545 C ATOM 6207 CG GLN D 222 26.243 84.665 14.485 1.00 68.79 C ANISOU 6207 CG GLN D 222 7388 6352 12397 2399 640 -955 C ATOM 6208 CD GLN D 222 27.211 83.881 15.353 1.00 65.89 C ANISOU 6208 CD GLN D 222 7220 6202 11614 2150 777 -1128 C ATOM 6209 OE1 GLN D 222 28.406 84.184 15.416 1.00 64.76 O ANISOU 6209 OE1 GLN D 222 7324 5896 11387 2019 734 -1163 O ATOM 6210 NE2 GLN D 222 26.698 82.866 16.031 1.00 65.26 N ANISOU 6210 NE2 GLN D 222 7015 6489 11291 2085 942 -1216 N ATOM 6211 N ASP D 223 27.414 87.330 11.419 1.00 73.12 N ANISOU 6211 N ASP D 223 8233 5848 13701 2611 66 -79 N ATOM 6212 CA ASP D 223 28.225 88.111 10.501 1.00 73.73 C ANISOU 6212 CA ASP D 223 8483 5586 13944 2592 -70 259 C ATOM 6213 C ASP D 223 29.446 87.328 10.032 1.00 69.43 C ANISOU 6213 C ASP D 223 8168 5230 12982 2286 -114 439 C ATOM 6214 O ASP D 223 29.706 87.238 8.833 1.00 69.19 O ANISOU 6214 O ASP D 223 8203 5242 12845 2264 -272 857 O ATOM 6215 CB ASP D 223 28.647 89.407 11.191 1.00 77.05 C ANISOU 6215 CB ASP D 223 8971 5495 14809 2672 32 20 C ATOM 6216 CG ASP D 223 29.029 90.494 10.213 1.00 80.48 C ANISOU 6216 CG ASP D 223 9483 5473 15624 2757 -97 423 C ATOM 6217 OD1 ASP D 223 30.023 90.320 9.472 1.00 78.80 O ANISOU 6217 OD1 ASP D 223 9450 5264 15226 2557 -167 744 O ATOM 6218 OD2 ASP D 223 28.339 91.535 10.200 1.00 85.33 O ANISOU 6218 OD2 ASP D 223 9968 5715 16739 3032 -115 431 O ATOM 6219 N ARG D 224 30.175 86.749 10.982 1.00 66.24 N ANISOU 6219 N ARG D 224 7876 4968 12325 2072 27 123 N ATOM 6220 CA ARG D 224 31.399 85.988 10.697 1.00 62.28 C ANISOU 6220 CA ARG D 224 7574 4637 11451 1789 7 237 C ATOM 6221 C ARG D 224 31.227 84.831 9.704 1.00 59.56 C ANISOU 6221 C ARG D 224 7215 4680 10734 1712 -121 525 C ATOM 6222 O ARG D 224 30.114 84.330 9.504 1.00 59.88 O ANISOU 6222 O ARG D 224 7072 4944 10737 1829 -178 543 O ATOM 6223 CB ARG D 224 32.000 85.447 11.996 1.00 60.24 C ANISOU 6223 CB ARG D 224 7392 4529 10966 1617 167 -168 C ATOM 6224 CG ARG D 224 31.038 84.629 12.850 1.00 59.54 C ANISOU 6224 CG ARG D 224 7147 4776 10698 1671 284 -423 C ATOM 6225 CD ARG D 224 31.730 83.430 13.468 1.00 56.16 C ANISOU 6225 CD ARG D 224 6821 4681 9835 1439 364 -546 C ATOM 6226 NE ARG D 224 31.084 83.021 14.713 1.00 56.66 N ANISOU 6226 NE ARG D 224 6775 4969 9785 1490 549 -866 N ATOM 6227 CZ ARG D 224 30.972 81.760 15.123 1.00 55.10 C ANISOU 6227 CZ ARG D 224 6549 5133 9252 1368 628 -877 C ATOM 6228 NH1 ARG D 224 31.445 80.759 14.381 1.00 50.90 N ANISOU 6228 NH1 ARG D 224 6088 4760 8490 1194 522 -631 N ATOM 6229 NH2 ARG D 224 30.365 81.497 16.273 1.00 56.41 N ANISOU 6229 NH2 ARG D 224 6608 5499 9325 1432 827 -1130 N ATOM 6230 N ALA D 225 32.348 84.410 9.108 1.00 56.95 N ANISOU 6230 N ALA D 225 7063 4427 10149 1513 -164 716 N ATOM 6231 CA ALA D 225 32.401 83.276 8.176 1.00 54.09 C ANISOU 6231 CA ALA D 225 6719 4428 9405 1422 -281 930 C ATOM 6232 C ALA D 225 31.706 82.032 8.725 1.00 51.66 C ANISOU 6232 C ALA D 225 6287 4464 8876 1370 -248 702 C ATOM 6233 O ALA D 225 32.001 81.594 9.846 1.00 49.91 O ANISOU 6233 O ALA D 225 6093 4305 8566 1254 -95 417 O ATOM 6234 CB ALA D 225 33.849 82.956 7.811 1.00 52.02 C ANISOU 6234 CB ALA D 225 6661 4200 8904 1201 -262 1050 C ATOM 6235 N LYS D 226 30.786 81.487 7.922 1.00 51.70 N ANISOU 6235 N LYS D 226 6147 4693 8805 1459 -399 842 N ATOM 6236 CA LYS D 226 29.990 80.287 8.250 1.00 49.97 C ANISOU 6236 CA LYS D 226 5762 4777 8448 1406 -393 675 C ATOM 6237 C LYS D 226 30.838 79.054 8.561 1.00 46.02 C ANISOU 6237 C LYS D 226 5387 4475 7622 1155 -323 570 C ATOM 6238 O LYS D 226 31.608 78.624 7.704 1.00 45.04 O ANISOU 6238 O LYS D 226 5400 4444 7271 1057 -423 726 O ATOM 6239 CB LYS D 226 29.046 79.963 7.092 1.00 51.65 C ANISOU 6239 CB LYS D 226 5806 5181 8638 1524 -628 861 C ATOM 6240 CG LYS D 226 28.128 78.775 7.341 1.00 51.82 C ANISOU 6240 CG LYS D 226 5607 5473 8609 1461 -644 693 C ATOM 6241 CD LYS D 226 27.080 78.667 6.245 1.00 55.71 C ANISOU 6241 CD LYS D 226 5886 6130 9152 1610 -911 834 C ATOM 6242 CE LYS D 226 26.243 77.408 6.386 1.00 55.90 C ANISOU 6242 CE LYS D 226 5672 6405 9162 1504 -950 662 C ATOM 6243 NZ LYS D 226 25.374 77.197 5.184 1.00 58.44 N ANISOU 6243 NZ LYS D 226 5795 6926 9484 1622 -1269 769 N ATOM 6244 N PRO D 227 30.677 78.469 9.773 1.00 44.23 N ANISOU 6244 N PRO D 227 5106 4331 7370 1070 -144 322 N ATOM 6245 CA PRO D 227 31.527 77.404 10.302 1.00 40.94 C ANISOU 6245 CA PRO D 227 4811 4055 6688 855 -50 229 C ATOM 6246 C PRO D 227 31.136 76.022 9.780 1.00 39.62 C ANISOU 6246 C PRO D 227 4548 4129 6376 752 -141 267 C ATOM 6247 O PRO D 227 30.680 75.160 10.546 1.00 39.12 O ANISOU 6247 O PRO D 227 4372 4189 6303 674 -25 148 O ATOM 6248 CB PRO D 227 31.288 77.482 11.818 1.00 41.12 C ANISOU 6248 CB PRO D 227 4783 4078 6761 861 177 -15 C ATOM 6249 CG PRO D 227 30.238 78.491 12.027 1.00 44.12 C ANISOU 6249 CG PRO D 227 4993 4332 7437 1077 209 -81 C ATOM 6250 CD PRO D 227 29.593 78.763 10.717 1.00 45.98 C ANISOU 6250 CD PRO D 227 5122 4539 7809 1196 -8 137 C ATOM 6251 N VAL D 228 31.326 75.826 8.479 1.00 39.18 N ANISOU 6251 N VAL D 228 4535 4138 6214 754 -344 431 N ATOM 6252 CA VAL D 228 31.014 74.564 7.817 1.00 38.32 C ANISOU 6252 CA VAL D 228 4341 4237 5980 664 -474 424 C ATOM 6253 C VAL D 228 31.956 73.427 8.229 1.00 35.81 C ANISOU 6253 C VAL D 228 4154 3986 5468 461 -382 343 C ATOM 6254 O VAL D 228 33.067 73.664 8.704 1.00 34.20 O ANISOU 6254 O VAL D 228 4138 3701 5157 396 -270 343 O ATOM 6255 CB VAL D 228 31.024 74.719 6.275 1.00 39.19 C ANISOU 6255 CB VAL D 228 4480 4441 5969 749 -727 595 C ATOM 6256 CG1 VAL D 228 29.892 75.627 5.834 1.00 42.38 C ANISOU 6256 CG1 VAL D 228 4704 4817 6582 967 -857 695 C ATOM 6257 CG2 VAL D 228 32.366 75.247 5.778 1.00 37.58 C ANISOU 6257 CG2 VAL D 228 4533 4167 5577 726 -712 750 C ATOM 6258 N THR D 229 31.496 72.193 8.059 1.00 35.84 N ANISOU 6258 N THR D 229 4035 4119 5463 365 -439 271 N ATOM 6259 CA THR D 229 32.381 71.034 8.124 1.00 34.21 C ANISOU 6259 CA THR D 229 3945 3958 5094 198 -408 222 C ATOM 6260 C THR D 229 33.539 71.323 7.183 1.00 33.55 C ANISOU 6260 C THR D 229 4076 3889 4783 209 -501 313 C ATOM 6261 O THR D 229 33.306 71.764 6.057 1.00 35.14 O ANISOU 6261 O THR D 229 4269 4159 4924 313 -674 401 O ATOM 6262 CB THR D 229 31.662 69.758 7.643 1.00 34.86 C ANISOU 6262 CB THR D 229 3853 4141 5251 114 -531 132 C ATOM 6263 OG1 THR D 229 30.490 69.548 8.437 1.00 36.09 O ANISOU 6263 OG1 THR D 229 3764 4289 5659 101 -432 83 O ATOM 6264 CG2 THR D 229 32.575 68.553 7.725 1.00 32.07 C ANISOU 6264 CG2 THR D 229 3616 3787 4784 -40 -494 77 C ATOM 6265 N GLN D 230 34.767 71.081 7.641 1.00 31.83 N ANISOU 6265 N GLN D 230 4032 3630 4433 111 -385 307 N ATOM 6266 CA GLN D 230 35.961 71.435 6.881 1.00 31.46 C ANISOU 6266 CA GLN D 230 4166 3592 4195 113 -421 405 C ATOM 6267 C GLN D 230 37.239 70.880 7.480 1.00 30.15 C ANISOU 6267 C GLN D 230 4132 3402 3920 -8 -301 363 C ATOM 6268 O GLN D 230 37.258 70.408 8.616 1.00 29.81 O ANISOU 6268 O GLN D 230 4069 3324 3934 -78 -184 283 O ATOM 6269 CB GLN D 230 36.102 72.939 6.861 1.00 32.14 C ANISOU 6269 CB GLN D 230 4308 3549 4353 213 -392 536 C ATOM 6270 CG GLN D 230 36.351 73.514 8.237 1.00 31.21 C ANISOU 6270 CG GLN D 230 4217 3278 4362 184 -220 455 C ATOM 6271 CD GLN D 230 36.325 74.993 8.214 1.00 32.22 C ANISOU 6271 CD GLN D 230 4370 3226 4645 289 -206 542 C ATOM 6272 OE1 GLN D 230 37.279 75.633 7.762 1.00 32.16 O ANISOU 6272 OE1 GLN D 230 4482 3132 4607 271 -204 665 O ATOM 6273 NE2 GLN D 230 35.216 75.568 8.671 1.00 33.68 N ANISOU 6273 NE2 GLN D 230 4425 3337 5033 404 -189 487 N ATOM 6274 N ILE D 231 38.319 70.980 6.720 1.00 30.32 N ANISOU 6274 N ILE D 231 4280 3464 3778 -20 -324 438 N ATOM 6275 CA ILE D 231 39.629 70.600 7.214 1.00 29.36 C ANISOU 6275 CA ILE D 231 4262 3322 3571 -116 -222 412 C ATOM 6276 C ILE D 231 40.481 71.839 7.484 1.00 30.20 C ANISOU 6276 C ILE D 231 4453 3312 3708 -118 -143 506 C ATOM 6277 O ILE D 231 40.606 72.720 6.628 1.00 31.61 O ANISOU 6277 O ILE D 231 4664 3469 3877 -59 -177 656 O ATOM 6278 CB ILE D 231 40.362 69.693 6.216 1.00 28.81 C ANISOU 6278 CB ILE D 231 4242 3383 3320 -138 -279 397 C ATOM 6279 CG1 ILE D 231 39.677 68.327 6.145 1.00 28.60 C ANISOU 6279 CG1 ILE D 231 4127 3411 3328 -169 -353 247 C ATOM 6280 CG2 ILE D 231 41.827 69.555 6.608 1.00 27.60 C ANISOU 6280 CG2 ILE D 231 4178 3208 3099 -211 -174 404 C ATOM 6281 CD1 ILE D 231 40.278 67.366 5.116 1.00 28.10 C ANISOU 6281 CD1 ILE D 231 4100 3469 3106 -168 -426 160 C ATOM 6282 N VAL D 232 41.050 71.913 8.682 1.00 30.02 N ANISOU 6282 N VAL D 232 4458 3216 3734 -185 -44 423 N ATOM 6283 CA VAL D 232 42.121 72.865 8.939 1.00 31.12 C ANISOU 6283 CA VAL D 232 4663 3247 3916 -226 11 459 C ATOM 6284 C VAL D 232 43.392 72.067 9.186 1.00 30.64 C ANISOU 6284 C VAL D 232 4642 3262 3739 -318 45 419 C ATOM 6285 O VAL D 232 43.379 71.062 9.897 1.00 30.07 O ANISOU 6285 O VAL D 232 4556 3258 3610 -347 60 327 O ATOM 6286 CB VAL D 232 41.826 73.807 10.133 1.00 31.80 C ANISOU 6286 CB VAL D 232 4733 3188 4161 -211 68 348 C ATOM 6287 CG1 VAL D 232 42.788 74.976 10.128 1.00 32.27 C ANISOU 6287 CG1 VAL D 232 4835 3082 4344 -254 91 383 C ATOM 6288 CG2 VAL D 232 40.385 74.314 10.088 1.00 33.14 C ANISOU 6288 CG2 VAL D 232 4826 3303 4462 -95 47 347 C ATOM 6289 N SER D 233 44.488 72.512 8.585 1.00 32.01 N ANISOU 6289 N SER D 233 4849 3419 3895 -359 67 515 N ATOM 6290 CA SER D 233 45.745 71.768 8.632 1.00 31.67 C ANISOU 6290 CA SER D 233 4814 3463 3757 -428 96 489 C ATOM 6291 C SER D 233 46.959 72.677 8.798 1.00 32.10 C ANISOU 6291 C SER D 233 4858 3427 3910 -508 146 530 C ATOM 6292 O SER D 233 46.926 73.846 8.422 1.00 33.20 O ANISOU 6292 O SER D 233 4998 3433 4184 -513 167 637 O ATOM 6293 CB SER D 233 45.889 70.937 7.361 1.00 31.95 C ANISOU 6293 CB SER D 233 4857 3649 3632 -390 77 553 C ATOM 6294 OG SER D 233 47.179 70.370 7.287 1.00 34.25 O ANISOU 6294 OG SER D 233 5139 4014 3861 -436 125 537 O ATOM 6295 N ALA D 234 48.010 72.119 9.389 1.00 31.55 N ANISOU 6295 N ALA D 234 4762 3416 3810 -570 157 449 N ATOM 6296 CA ALA D 234 49.312 72.773 9.513 1.00 32.66 C ANISOU 6296 CA ALA D 234 4849 3500 4059 -664 191 466 C ATOM 6297 C ALA D 234 50.400 71.805 9.064 1.00 32.64 C ANISOU 6297 C ALA D 234 4801 3652 3950 -677 222 492 C ATOM 6298 O ALA D 234 50.235 70.579 9.140 1.00 31.68 O ANISOU 6298 O ALA D 234 4695 3644 3699 -621 196 433 O ATOM 6299 CB ALA D 234 49.562 73.238 10.935 1.00 32.67 C ANISOU 6299 CB ALA D 234 4827 3424 4163 -715 144 285 C ATOM 6300 N GLU D 235 51.520 72.375 8.633 1.00 34.19 N ANISOU 6300 N GLU D 235 4920 3830 4241 -754 286 578 N ATOM 6301 CA GLU D 235 52.479 71.706 7.772 1.00 34.71 C ANISOU 6301 CA GLU D 235 4925 4049 4213 -744 364 654 C ATOM 6302 C GLU D 235 53.880 72.198 8.098 1.00 36.30 C ANISOU 6302 C GLU D 235 4984 4220 4587 -859 404 657 C ATOM 6303 O GLU D 235 54.052 73.362 8.443 1.00 37.78 O ANISOU 6303 O GLU D 235 5129 4237 4988 -960 401 674 O ATOM 6304 CB GLU D 235 52.099 72.023 6.307 1.00 35.60 C ANISOU 6304 CB GLU D 235 5083 4224 4219 -691 451 853 C ATOM 6305 CG GLU D 235 53.232 72.358 5.326 1.00 38.03 C ANISOU 6305 CG GLU D 235 5300 4623 4525 -731 603 1034 C ATOM 6306 CD GLU D 235 53.654 73.830 5.334 1.00 41.06 C ANISOU 6306 CD GLU D 235 5619 4811 5172 -856 675 1209 C ATOM 6307 OE1 GLU D 235 52.783 74.710 5.497 1.00 41.49 O ANISOU 6307 OE1 GLU D 235 5742 4681 5342 -857 626 1265 O ATOM 6308 OE2 GLU D 235 54.866 74.113 5.167 1.00 43.79 O ANISOU 6308 OE2 GLU D 235 5824 5169 5645 -953 785 1291 O ATOM 6309 N ALA D 236 54.874 71.313 7.992 1.00 36.85 N ANISOU 6309 N ALA D 236 4961 4439 4603 -842 433 622 N ATOM 6310 CA ALA D 236 56.304 71.697 8.031 1.00 38.39 C ANISOU 6310 CA ALA D 236 4970 4645 4970 -946 491 650 C ATOM 6311 C ALA D 236 57.213 70.669 7.357 1.00 38.79 C ANISOU 6311 C ALA D 236 4921 4898 4919 -874 584 668 C ATOM 6312 O ALA D 236 56.937 69.469 7.366 1.00 37.60 O ANISOU 6312 O ALA D 236 4831 4846 4610 -750 541 575 O ATOM 6313 CB ALA D 236 56.767 71.937 9.459 1.00 38.49 C ANISOU 6313 CB ALA D 236 4903 4586 5136 -1022 345 470 C ATOM 6314 N TRP D 237 58.307 71.148 6.783 1.00 40.94 N ANISOU 6314 N TRP D 237 5024 5215 5316 -952 721 785 N ATOM 6315 CA TRP D 237 59.302 70.263 6.188 1.00 41.89 C ANISOU 6315 CA TRP D 237 5009 5538 5371 -878 833 784 C ATOM 6316 C TRP D 237 60.402 69.879 7.179 1.00 42.58 C ANISOU 6316 C TRP D 237 4901 5644 5634 -909 735 646 C ATOM 6317 O TRP D 237 60.804 70.674 8.028 1.00 43.77 O ANISOU 6317 O TRP D 237 4948 5679 6005 -1047 638 602 O ATOM 6318 CB TRP D 237 59.926 70.925 4.961 1.00 44.27 C ANISOU 6318 CB TRP D 237 5202 5928 5691 -929 1074 1013 C ATOM 6319 CG TRP D 237 59.010 71.019 3.792 1.00 43.83 C ANISOU 6319 CG TRP D 237 5322 5958 5373 -838 1176 1162 C ATOM 6320 CD1 TRP D 237 58.137 72.029 3.515 1.00 43.66 C ANISOU 6320 CD1 TRP D 237 5425 5804 5359 -886 1175 1333 C ATOM 6321 CD2 TRP D 237 58.875 70.068 2.733 1.00 44.06 C ANISOU 6321 CD2 TRP D 237 5413 6238 5090 -665 1273 1137 C ATOM 6322 NE1 TRP D 237 57.463 71.769 2.347 1.00 44.20 N ANISOU 6322 NE1 TRP D 237 5627 6052 5116 -751 1252 1441 N ATOM 6323 CE2 TRP D 237 57.898 70.573 1.841 1.00 44.32 C ANISOU 6323 CE2 TRP D 237 5609 6314 4917 -619 1311 1302 C ATOM 6324 CE3 TRP D 237 59.485 68.838 2.446 1.00 44.11 C ANISOU 6324 CE3 TRP D 237 5345 6434 4979 -531 1322 970 C ATOM 6325 CZ2 TRP D 237 57.509 69.890 0.684 1.00 44.46 C ANISOU 6325 CZ2 TRP D 237 5721 6592 4579 -450 1378 1284 C ATOM 6326 CZ3 TRP D 237 59.103 68.159 1.287 1.00 44.59 C ANISOU 6326 CZ3 TRP D 237 5503 6721 4717 -365 1408 929 C ATOM 6327 CH2 TRP D 237 58.119 68.689 0.424 1.00 44.92 C ANISOU 6327 CH2 TRP D 237 5712 6835 4522 -330 1427 1075 C ATOM 6328 N GLY D 238 60.903 68.660 7.058 1.00 42.68 N ANISOU 6328 N GLY D 238 4851 5804 5562 -772 744 563 N ATOM 6329 CA GLY D 238 62.094 68.269 7.788 1.00 44.15 C ANISOU 6329 CA GLY D 238 4809 6047 5919 -772 669 474 C ATOM 6330 C GLY D 238 63.257 69.184 7.456 1.00 47.16 C ANISOU 6330 C GLY D 238 4924 6455 6538 -922 798 571 C ATOM 6331 O GLY D 238 63.328 69.720 6.349 1.00 48.38 O ANISOU 6331 O GLY D 238 5059 6651 6672 -967 1021 741 O ATOM 6332 N ARG D 239 64.164 69.361 8.420 1.00 48.76 N ANISOU 6332 N ARG D 239 4912 6647 6968 -1001 656 476 N ATOM 6333 CA ARG D 239 65.294 70.295 8.296 1.00 51.86 C ANISOU 6333 CA ARG D 239 5004 7029 7673 -1184 741 540 C ATOM 6334 C ARG D 239 66.488 69.854 9.136 1.00 53.33 C ANISOU 6334 C ARG D 239 4898 7316 8048 -1171 585 400 C ATOM 6335 O ARG D 239 66.338 69.532 10.314 1.00 52.55 O ANISOU 6335 O ARG D 239 4846 7209 7913 -1124 315 242 O ATOM 6336 CB ARG D 239 64.863 71.718 8.675 1.00 52.32 C ANISOU 6336 CB ARG D 239 5109 6854 7917 -1397 681 562 C ATOM 6337 CG ARG D 239 63.902 71.792 9.866 1.00 51.90 C ANISOU 6337 CG ARG D 239 5275 6684 7762 -1377 416 379 C ATOM 6338 CD ARG D 239 63.089 73.083 9.864 1.00 54.41 C ANISOU 6338 CD ARG D 239 5726 6755 8191 -1519 426 419 C ATOM 6339 NE ARG D 239 63.974 74.229 9.653 1.00 60.10 N ANISOU 6339 NE ARG D 239 6194 7335 9305 -1742 507 487 N ATOM 6340 CZ ARG D 239 64.548 74.955 10.615 1.00 62.69 C ANISOU 6340 CZ ARG D 239 6343 7541 9936 -1902 323 290 C ATOM 6341 NH1 ARG D 239 64.329 74.689 11.899 1.00 61.77 N ANISOU 6341 NH1 ARG D 239 6288 7467 9715 -1846 42 9 N ATOM 6342 NH2 ARG D 239 65.345 75.965 10.283 1.00 66.38 N ANISOU 6342 NH2 ARG D 239 6558 7848 10814 -2122 424 375 N ATOM 6343 N ALA D 240 67.668 69.860 8.514 1.00 56.01 N ANISOU 6343 N ALA D 240 4925 7777 8581 -1204 760 475 N ATOM 6344 CA ALA D 240 68.927 69.418 9.132 1.00 58.06 C ANISOU 6344 CA ALA D 240 4842 8164 9055 -1176 635 362 C ATOM 6345 C ALA D 240 69.145 69.920 10.564 1.00 58.50 C ANISOU 6345 C ALA D 240 4806 8145 9277 -1291 291 178 C ATOM 6346 O ALA D 240 69.266 71.120 10.801 1.00 59.75 O ANISOU 6346 O ALA D 240 4870 8156 9678 -1525 253 153 O ATOM 6347 CB ALA D 240 70.114 69.802 8.243 1.00 61.47 C ANISOU 6347 CB ALA D 240 4906 8696 9752 -1276 907 492 C TER 6348 ALA D 240 HETATM 6349 C1 NAG E 1 17.858 10.919 12.563 1.00 55.66 C ANISOU 6349 C1 NAG E 1 6659 7002 7489 1739 940 26 C HETATM 6350 C2 NAG E 1 19.374 11.012 12.392 1.00 59.06 C ANISOU 6350 C2 NAG E 1 6852 7600 7990 1911 1027 149 C HETATM 6351 C3 NAG E 1 19.710 11.561 11.009 1.00 60.56 C ANISOU 6351 C3 NAG E 1 7045 7882 8084 1837 1132 -11 C HETATM 6352 C4 NAG E 1 19.040 10.760 9.894 1.00 63.21 C ANISOU 6352 C4 NAG E 1 7634 7980 8404 1812 1320 -243 C HETATM 6353 C5 NAG E 1 17.557 10.516 10.220 1.00 61.92 C ANISOU 6353 C5 NAG E 1 7694 7642 8190 1658 1218 -329 C HETATM 6354 C6 NAG E 1 16.889 9.545 9.235 1.00 64.59 C ANISOU 6354 C6 NAG E 1 8294 7734 8514 1618 1406 -547 C HETATM 6355 C7 NAG E 1 20.407 11.330 14.588 1.00 58.70 C ANISOU 6355 C7 NAG E 1 6456 7824 8022 2019 786 573 C HETATM 6356 C8 NAG E 1 21.016 12.295 15.562 1.00 58.33 C ANISOU 6356 C8 NAG E 1 6187 8073 7902 1931 587 763 C HETATM 6357 N2 NAG E 1 19.984 11.832 13.425 1.00 57.71 N ANISOU 6357 N2 NAG E 1 6453 7679 7794 1887 842 355 N HETATM 6358 O3 NAG E 1 21.104 11.529 10.823 1.00 63.04 O ANISOU 6358 O3 NAG E 1 7134 8343 8474 2008 1240 97 O HETATM 6359 O4 NAG E 1 19.124 11.519 8.705 1.00 64.88 O ANISOU 6359 O4 NAG E 1 7862 8320 8471 1667 1353 -386 O HETATM 6360 O5 NAG E 1 17.356 10.063 11.556 1.00 59.43 O ANISOU 6360 O5 NAG E 1 7351 7253 7978 1743 1123 -166 O HETATM 6361 O6 NAG E 1 15.619 9.169 9.735 1.00 66.60 O ANISOU 6361 O6 NAG E 1 8722 7834 8750 1500 1313 -583 O HETATM 6362 O7 NAG E 1 20.312 10.143 14.893 1.00 60.14 O ANISOU 6362 O7 NAG E 1 6708 7797 8345 2190 887 630 O HETATM 6363 C1 NAG E 2 20.040 10.977 7.741 1.00 69.58 C ANISOU 6363 C1 NAG E 2 8431 8894 9112 1803 1606 -464 C HETATM 6364 C2 NAG E 2 19.576 11.346 6.324 1.00 70.38 C ANISOU 6364 C2 NAG E 2 8691 9016 9033 1597 1676 -691 C HETATM 6365 C3 NAG E 2 20.657 11.105 5.269 1.00 73.15 C ANISOU 6365 C3 NAG E 2 8980 9423 9389 1699 1929 -773 C HETATM 6366 C4 NAG E 2 22.052 11.553 5.708 1.00 74.24 C ANISOU 6366 C4 NAG E 2 8801 9790 9618 1867 1929 -574 C HETATM 6367 C5 NAG E 2 22.356 11.067 7.131 1.00 74.73 C ANISOU 6367 C5 NAG E 2 8721 9803 9869 2074 1851 -346 C HETATM 6368 C6 NAG E 2 23.683 11.604 7.672 1.00 75.87 C ANISOU 6368 C6 NAG E 2 8524 10224 10080 2199 1803 -117 C HETATM 6369 C7 NAG E 2 17.256 11.151 5.476 1.00 70.17 C ANISOU 6369 C7 NAG E 2 9091 8781 8791 1226 1594 -974 C HETATM 6370 C8 NAG E 2 16.131 10.218 5.127 1.00 70.62 C ANISOU 6370 C8 NAG E 2 9421 8602 8810 1116 1664 -1139 C HETATM 6371 N2 NAG E 2 18.388 10.596 5.934 1.00 71.28 N ANISOU 6371 N2 NAG E 2 9090 8893 9102 1486 1729 -867 N HETATM 6372 O3 NAG E 2 20.297 11.813 4.109 1.00 72.64 O ANISOU 6372 O3 NAG E 2 9011 9471 9116 1461 1920 -930 O HETATM 6373 O4 NAG E 2 22.997 11.077 4.771 1.00 76.86 O ANISOU 6373 O4 NAG E 2 9086 10130 9989 2001 2211 -657 O HETATM 6374 O5 NAG E 2 21.325 11.499 8.003 1.00 71.63 O ANISOU 6374 O5 NAG E 2 8407 9388 9420 1920 1598 -297 O HETATM 6375 O6 NAG E 2 23.486 12.834 8.348 1.00 73.25 O ANISOU 6375 O6 NAG E 2 8093 10108 9631 2003 1519 -8 O HETATM 6376 O7 NAG E 2 17.087 12.362 5.334 1.00 69.04 O ANISOU 6376 O7 NAG E 2 8864 8844 8525 1070 1419 -933 O HETATM 6377 C1 FUC E 3 14.507 9.857 9.088 1.00 66.88 C ANISOU 6377 C1 FUC E 3 8872 7934 8606 1233 1202 -723 C HETATM 6378 C2 FUC E 3 13.197 9.076 9.293 1.00 67.38 C ANISOU 6378 C2 FUC E 3 9153 7791 8658 1116 1189 -806 C HETATM 6379 C3 FUC E 3 12.768 9.195 10.773 1.00 65.98 C ANISOU 6379 C3 FUC E 3 8903 7617 8548 1143 1015 -634 C HETATM 6380 C4 FUC E 3 12.546 10.676 11.128 1.00 63.67 C ANISOU 6380 C4 FUC E 3 8460 7575 8158 1024 798 -560 C HETATM 6381 C5 FUC E 3 13.848 11.436 10.822 1.00 63.96 C ANISOU 6381 C5 FUC E 3 8307 7802 8191 1115 815 -496 C HETATM 6382 C6 FUC E 3 13.707 12.931 11.091 1.00 61.95 C ANISOU 6382 C6 FUC E 3 7929 7769 7840 986 623 -435 C HETATM 6383 O2 FUC E 3 13.351 7.736 8.858 1.00 70.14 O ANISOU 6383 O2 FUC E 3 9677 7885 9088 1206 1422 -912 O HETATM 6384 O3 FUC E 3 11.660 8.386 11.127 1.00 65.03 O ANISOU 6384 O3 FUC E 3 8963 7308 8439 1057 1011 -681 O HETATM 6385 O4 FUC E 3 11.444 11.245 10.439 1.00 61.28 O ANISOU 6385 O4 FUC E 3 8247 7321 7716 803 717 -678 O HETATM 6386 O5 FUC E 3 14.304 11.217 9.485 1.00 65.23 O ANISOU 6386 O5 FUC E 3 8524 7952 8309 1115 981 -635 O HETATM 6387 C1 NAG A 500 -6.427 41.672 17.530 1.00 58.82 C ANISOU 6387 C1 NAG A 500 7519 5309 9522 1534 1370 677 C HETATM 6388 C2 NAG A 500 -7.376 42.864 17.787 1.00 63.96 C ANISOU 6388 C2 NAG A 500 8168 5660 10474 1788 1635 775 C HETATM 6389 C3 NAG A 500 -8.117 42.644 19.108 1.00 64.81 C ANISOU 6389 C3 NAG A 500 8272 5715 10637 1850 1865 594 C HETATM 6390 C4 NAG A 500 -8.969 41.391 18.962 1.00 63.23 C ANISOU 6390 C4 NAG A 500 7783 5849 10394 1884 1710 678 C HETATM 6391 C5 NAG A 500 -8.004 40.218 18.737 1.00 59.60 C ANISOU 6391 C5 NAG A 500 7354 5657 9636 1625 1447 578 C HETATM 6392 C6 NAG A 500 -8.756 38.893 18.571 1.00 58.48 C ANISOU 6392 C6 NAG A 500 6961 5832 9425 1617 1287 642 C HETATM 6393 C7 NAG A 500 -6.022 44.786 16.896 1.00 68.85 C ANISOU 6393 C7 NAG A 500 9129 5867 11165 1730 1692 870 C HETATM 6394 C8 NAG A 500 -5.513 46.148 17.273 1.00 71.80 C ANISOU 6394 C8 NAG A 500 9799 5842 11639 1716 1929 785 C HETATM 6395 N2 NAG A 500 -6.743 44.174 17.843 1.00 67.12 N ANISOU 6395 N2 NAG A 500 8825 5719 10957 1782 1799 739 N HETATM 6396 O3 NAG A 500 -8.899 43.765 19.468 1.00 68.84 O ANISOU 6396 O3 NAG A 500 8813 5918 11426 2083 2158 642 O HETATM 6397 O4 NAG A 500 -9.818 41.196 20.080 1.00 64.06 O ANISOU 6397 O4 NAG A 500 7841 5927 10571 1963 1922 554 O HETATM 6398 O5 NAG A 500 -7.155 40.445 17.610 1.00 57.88 O ANISOU 6398 O5 NAG A 500 7179 5468 9346 1546 1258 695 O HETATM 6399 O6 NAG A 500 -9.424 38.845 17.328 1.00 59.40 O ANISOU 6399 O6 NAG A 500 6840 6092 9636 1731 1125 928 O HETATM 6400 O7 NAG A 500 -5.744 44.323 15.785 1.00 67.92 O ANISOU 6400 O7 NAG A 500 8881 5977 10950 1676 1431 1040 O HETATM 6401 C1 NAG A 501 -1.161 33.017 25.486 1.00 42.08 C ANISOU 6401 C1 NAG A 501 5906 4529 5552 -55 905 -760 C HETATM 6402 C2 NAG A 501 -1.838 34.373 25.651 1.00 45.57 C ANISOU 6402 C2 NAG A 501 6430 4743 6143 26 1125 -810 C HETATM 6403 C3 NAG A 501 -0.870 35.546 25.484 1.00 47.63 C ANISOU 6403 C3 NAG A 501 6856 4863 6377 -66 1169 -858 C HETATM 6404 C4 NAG A 501 0.315 35.398 26.453 1.00 48.00 C ANISOU 6404 C4 NAG A 501 7046 5003 6188 -321 1139 -983 C HETATM 6405 C5 NAG A 501 0.945 34.012 26.234 1.00 45.12 C ANISOU 6405 C5 NAG A 501 6556 4892 5697 -367 908 -902 C HETATM 6406 C6 NAG A 501 1.979 33.724 27.310 1.00 45.07 C ANISOU 6406 C6 NAG A 501 6648 5015 5462 -604 870 -990 C HETATM 6407 C7 NAG A 501 -4.201 34.599 25.145 1.00 46.81 C ANISOU 6407 C7 NAG A 501 6357 4796 6632 365 1289 -677 C HETATM 6408 C8 NAG A 501 -5.223 34.748 24.066 1.00 46.86 C ANISOU 6408 C8 NAG A 501 6172 4789 6842 578 1264 -498 C HETATM 6409 N2 NAG A 501 -2.940 34.517 24.727 1.00 45.91 N ANISOU 6409 N2 NAG A 501 6317 4735 6391 243 1137 -675 N HETATM 6410 O3 NAG A 501 -1.593 36.742 25.713 1.00 50.61 O ANISOU 6410 O3 NAG A 501 7325 4996 6910 24 1403 -908 O HETATM 6411 O4 NAG A 501 1.269 36.465 26.383 1.00 48.68 O ANISOU 6411 O4 NAG A 501 7294 4980 6221 -455 1178 -1038 O HETATM 6412 O5 NAG A 501 -0.027 32.968 26.329 1.00 43.86 O ANISOU 6412 O5 NAG A 501 6260 4819 5585 -258 881 -855 O HETATM 6413 O6 NAG A 501 1.464 32.691 28.124 1.00 45.32 O ANISOU 6413 O6 NAG A 501 6624 5164 5431 -614 861 -1002 O HETATM 6414 O7 NAG A 501 -4.552 34.548 26.324 1.00 47.71 O ANISOU 6414 O7 NAG A 501 6538 4892 6698 306 1441 -806 O HETATM 6415 C1A QUX A 286 16.911 28.276 19.885 1.00 40.97 C ANISOU 6415 C1A QUX A 286 4735 6551 4282 -746 -526 131 C HETATM 6416 C2A QUX A 286 18.112 28.309 18.941 1.00 41.77 C ANISOU 6416 C2A QUX A 286 4689 6815 4366 -739 -534 203 C HETATM 6417 O2A QUX A 286 17.716 28.926 17.709 1.00 39.57 O ANISOU 6417 O2A QUX A 286 4489 6415 4129 -722 -483 139 O HETATM 6418 C3A QUX A 286 18.684 26.888 18.708 1.00 42.47 C ANISOU 6418 C3A QUX A 286 4605 7012 4519 -538 -534 301 C HETATM 6419 O3A QUX A 286 19.852 26.929 17.876 1.00 44.23 O ANISOU 6419 O3A QUX A 286 4674 7405 4726 -529 -521 368 O HETATM 6420 C4A QUX A 286 19.035 26.163 20.015 1.00 43.53 C ANISOU 6420 C4A QUX A 286 4650 7269 4622 -537 -596 405 C HETATM 6421 O4A QUX A 286 20.303 26.613 20.500 1.00 44.43 O ANISOU 6421 O4A QUX A 286 4617 7640 4624 -695 -663 513 O HETATM 6422 C5M QUX A 286 17.932 26.337 21.078 1.00 44.09 C ANISOU 6422 C5M QUX A 286 4883 7202 4666 -612 -610 333 C HETATM 6423 O5M QUX A 286 17.369 25.991 23.405 1.00 47.85 O ANISOU 6423 O5M QUX A 286 5431 7721 5027 -756 -683 371 O HETATM 6424 C6A QUX A 286 18.476 26.063 22.496 1.00 46.85 C ANISOU 6424 C6A QUX A 286 5155 7731 4915 -721 -692 443 C HETATM 6425 O6A QUX A 286 17.312 27.663 21.119 1.00 42.88 O ANISOU 6425 O6A QUX A 286 4903 6928 4463 -782 -583 209 O HETATM 6426 CAG QUX A 286 15.740 27.514 19.288 1.00 39.98 C ANISOU 6426 CAG QUX A 286 4670 6240 4280 -548 -478 79 C HETATM 6427 CAL QUX A 286 14.398 28.197 19.548 1.00 39.41 C ANISOU 6427 CAL QUX A 286 4771 5963 4240 -584 -437 -23 C HETATM 6428 CAM QUX A 286 13.239 27.446 18.862 1.00 38.13 C ANISOU 6428 CAM QUX A 286 4644 5652 4190 -409 -403 -58 C HETATM 6429 CAN QUX A 286 12.921 28.098 17.519 1.00 37.88 C ANISOU 6429 CAN QUX A 286 4650 5542 4200 -389 -376 -85 C HETATM 6430 CAO QUX A 286 12.410 27.132 16.470 1.00 37.25 C ANISOU 6430 CAO QUX A 286 4544 5423 4188 -240 -363 -88 C HETATM 6431 CAP QUX A 286 10.872 27.020 16.465 1.00 34.07 C ANISOU 6431 CAP QUX A 286 4223 4865 3858 -183 -344 -133 C HETATM 6432 CAQ QUX A 286 10.434 25.737 15.740 1.00 33.40 C ANISOU 6432 CAQ QUX A 286 4112 4765 3813 -65 -337 -141 C HETATM 6433 CAR QUX A 286 8.991 25.840 15.221 1.00 33.31 C ANISOU 6433 CAR QUX A 286 4157 4644 3857 -39 -332 -167 C HETATM 6434 CAS QUX A 286 8.685 24.810 14.122 1.00 32.36 C ANISOU 6434 CAS QUX A 286 4025 4530 3740 19 -328 -182 C HETATM 6435 CAT QUX A 286 8.733 25.466 12.732 1.00 32.11 C ANISOU 6435 CAT QUX A 286 3991 4532 3676 -19 -339 -165 C HETATM 6436 CAU QUX A 286 7.784 24.818 11.720 1.00 30.20 C ANISOU 6436 CAU QUX A 286 3768 4276 3429 -10 -347 -183 C HETATM 6437 CAV QUX A 286 7.794 25.608 10.412 1.00 29.16 C ANISOU 6437 CAV QUX A 286 3634 4198 3248 -71 -373 -142 C HETATM 6438 CAW QUX A 286 6.620 26.587 10.332 1.00 29.20 C ANISOU 6438 CAW QUX A 286 3643 4147 3304 -89 -416 -73 C HETATM 6439 CAX QUX A 286 6.813 27.561 9.161 1.00 30.18 C ANISOU 6439 CAX QUX A 286 3763 4322 3382 -151 -448 1 C HETATM 6440 CAY QUX A 286 5.516 28.306 8.841 1.00 31.34 C ANISOU 6440 CAY QUX A 286 3894 4425 3588 -148 -495 100 C HETATM 6441 CAZ QUX A 286 5.784 29.579 8.030 1.00 32.65 C ANISOU 6441 CAZ QUX A 286 4066 4601 3740 -197 -522 208 C HETATM 6442 CBA QUX A 286 4.767 30.680 8.342 1.00 32.88 C ANISOU 6442 CBA QUX A 286 4087 4515 3891 -146 -530 317 C HETATM 6443 CBB QUX A 286 5.383 32.040 8.031 1.00 34.17 C ANISOU 6443 CBB QUX A 286 4294 4623 4065 -185 -520 399 C HETATM 6444 CBC QUX A 286 4.338 33.028 7.511 1.00 36.09 C ANISOU 6444 CBC QUX A 286 4512 4798 4401 -143 -552 569 C HETATM 6445 OBD QUX A 286 11.901 29.057 17.704 1.00 40.38 O ANISOU 6445 OBD QUX A 286 5088 5704 4552 -435 -341 -138 O HETATM 6446 OBE QUX A 286 12.897 27.627 15.212 1.00 39.26 O ANISOU 6446 OBE QUX A 286 4775 5719 4422 -260 -357 -74 O HETATM 6447 NBF QUX A 286 13.560 26.015 18.704 1.00 37.54 N ANISOU 6447 NBF QUX A 286 4470 5640 4152 -265 -415 -3 N HETATM 6448 CBG QUX A 286 13.354 25.106 19.664 1.00 37.44 C ANISOU 6448 CBG QUX A 286 4444 5634 4148 -219 -430 27 C HETATM 6449 OBH QUX A 286 12.883 25.336 20.787 1.00 37.93 O ANISOU 6449 OBH QUX A 286 4567 5672 4172 -301 -440 10 O HETATM 6450 CBI QUX A 286 13.788 23.703 19.266 1.00 36.81 C ANISOU 6450 CBI QUX A 286 4273 5587 4128 -57 -421 91 C HETATM 6451 CBK QUX A 286 13.012 22.658 20.059 1.00 36.54 C ANISOU 6451 CBK QUX A 286 4280 5468 4135 13 -419 103 C HETATM 6452 CBL QUX A 286 12.328 21.676 19.126 1.00 35.38 C ANISOU 6452 CBL QUX A 286 4174 5189 4078 150 -365 58 C HETATM 6453 CBM QUX A 286 10.980 22.197 18.663 1.00 34.29 C ANISOU 6453 CBM QUX A 286 4144 4923 3960 111 -346 -43 C HETATM 6454 CBN QUX A 286 10.247 21.093 17.914 1.00 34.91 C ANISOU 6454 CBN QUX A 286 4268 4894 4104 207 -305 -82 C HETATM 6455 CBO QUX A 286 8.762 21.124 18.232 1.00 34.71 C ANISOU 6455 CBO QUX A 286 4324 4763 4101 171 -305 -134 C HETATM 6456 CBP QUX A 286 8.178 19.736 18.036 1.00 35.73 C ANISOU 6456 CBP QUX A 286 4497 4803 4277 238 -274 -149 C HETATM 6457 CBQ QUX A 286 6.661 19.802 17.864 1.00 36.81 C ANISOU 6457 CBQ QUX A 286 4692 4861 4432 191 -273 -205 C HETATM 6458 CBR QUX A 286 5.947 19.667 19.212 1.00 37.29 C ANISOU 6458 CBR QUX A 286 4777 4895 4498 156 -279 -188 C HETATM 6459 CBS QUX A 286 4.470 20.013 19.082 1.00 36.70 C ANISOU 6459 CBS QUX A 286 4724 4774 4446 109 -272 -231 C HETATM 6460 CBT QUX A 286 3.976 20.611 20.388 1.00 36.65 C ANISOU 6460 CBT QUX A 286 4724 4773 4430 59 -259 -228 C HETATM 6461 CBU QUX A 286 3.400 19.516 21.274 1.00 36.27 C ANISOU 6461 CBU QUX A 286 4708 4690 4382 46 -247 -212 C HETATM 6462 CBV QUX A 286 3.732 19.802 22.735 1.00 36.44 C ANISOU 6462 CBV QUX A 286 4740 4757 4350 -4 -242 -185 C HETATM 6463 CBW QUX A 286 3.080 18.743 23.615 1.00 36.23 C ANISOU 6463 CBW QUX A 286 4748 4700 4316 -30 -230 -157 C HETATM 6464 CBX QUX A 286 3.906 18.505 24.856 1.00 36.28 C ANISOU 6464 CBX QUX A 286 4763 4772 4250 -67 -253 -85 C HETATM 6465 CBY QUX A 286 3.725 17.079 25.340 1.00 37.12 C ANISOU 6465 CBY QUX A 286 4904 4833 4366 -52 -260 -12 C HETATM 6466 CBZ QUX A 286 4.881 16.223 24.828 1.00 37.86 C ANISOU 6466 CBZ QUX A 286 4979 4909 4497 51 -289 69 C HETATM 6467 CCA QUX A 286 5.140 15.025 25.749 1.00 38.51 C ANISOU 6467 CCA QUX A 286 5088 4971 4574 66 -305 194 C HETATM 6468 CCB QUX A 286 5.798 13.869 24.984 1.00 38.80 C ANISOU 6468 CCB QUX A 286 5136 4905 4700 201 -286 253 C HETATM 6469 CCC QUX A 286 7.236 14.184 24.559 1.00 39.38 C ANISOU 6469 CCC QUX A 286 5116 5060 4786 296 -308 311 C HETATM 6470 CCD QUX A 286 7.628 13.397 23.298 1.00 41.11 C ANISOU 6470 CCD QUX A 286 5356 5159 5105 429 -244 284 C HETATM 6471 CCE QUX A 286 7.499 14.263 22.045 1.00 40.28 C ANISOU 6471 CCE QUX A 286 5240 5072 4994 413 -224 147 C HETATM 6472 CCF QUX A 286 8.212 13.634 20.844 1.00 41.77 C ANISOU 6472 CCF QUX A 286 5433 5188 5251 534 -154 124 C HETATM 6473 CCG QUX A 286 7.563 14.062 19.504 1.00 41.69 C ANISOU 6473 CCG QUX A 286 5470 5145 5226 481 -122 -26 C HETATM 6474 CCH QUX A 286 7.848 15.536 19.139 1.00 40.09 C ANISOU 6474 CCH QUX A 286 5184 5083 4965 429 -171 -59 C CONECT 116 6387 CONECT 306 6401 CONECT 812 1310 CONECT 1289 6349 CONECT 1310 812 CONECT 1562 1997 CONECT 1997 1562 CONECT 2311 2762 CONECT 2762 2311 CONECT 3076 3602 CONECT 3602 3076 CONECT 3947 4336 CONECT 4142 5758 CONECT 4336 3947 CONECT 4618 5164 CONECT 5164 4618 CONECT 5551 6080 CONECT 5758 4142 CONECT 6080 5551 CONECT 6349 1289 6350 6360 CONECT 6350 6349 6351 6357 CONECT 6351 6350 6352 6358 CONECT 6352 6351 6353 6359 CONECT 6353 6352 6354 6360 CONECT 6354 6353 6361 CONECT 6355 6356 6357 6362 CONECT 6356 6355 CONECT 6357 6350 6355 CONECT 6358 6351 CONECT 6359 6352 6363 CONECT 6360 6349 6353 CONECT 6361 6354 6377 CONECT 6362 6355 CONECT 6363 6359 6364 6374 CONECT 6364 6363 6365 6371 CONECT 6365 6364 6366 6372 CONECT 6366 6365 6367 6373 CONECT 6367 6366 6368 6374 CONECT 6368 6367 6375 CONECT 6369 6370 6371 6376 CONECT 6370 6369 CONECT 6371 6364 6369 CONECT 6372 6365 CONECT 6373 6366 CONECT 6374 6363 6367 CONECT 6375 6368 CONECT 6376 6369 CONECT 6377 6361 6378 6386 CONECT 6378 6377 6379 6383 CONECT 6379 6378 6380 6384 CONECT 6380 6379 6381 6385 CONECT 6381 6380 6382 6386 CONECT 6382 6381 CONECT 6383 6378 CONECT 6384 6379 CONECT 6385 6380 CONECT 6386 6377 6381 CONECT 6387 116 6388 6398 CONECT 6388 6387 6389 6395 CONECT 6389 6388 6390 6396 CONECT 6390 6389 6391 6397 CONECT 6391 6390 6392 6398 CONECT 6392 6391 6399 CONECT 6393 6394 6395 6400 CONECT 6394 6393 CONECT 6395 6388 6393 CONECT 6396 6389 CONECT 6397 6390 CONECT 6398 6387 6391 CONECT 6399 6392 CONECT 6400 6393 CONECT 6401 306 6402 6412 CONECT 6402 6401 6403 6409 CONECT 6403 6402 6404 6410 CONECT 6404 6403 6405 6411 CONECT 6405 6404 6406 6412 CONECT 6406 6405 6413 CONECT 6407 6408 6409 6414 CONECT 6408 6407 CONECT 6409 6402 6407 CONECT 6410 6403 CONECT 6411 6404 CONECT 6412 6401 6405 CONECT 6413 6406 CONECT 6414 6407 CONECT 6415 6416 6425 6426 CONECT 6416 6415 6417 6418 CONECT 6417 6416 CONECT 6418 6416 6419 6420 CONECT 6419 6418 CONECT 6420 6418 6421 6422 CONECT 6421 6420 CONECT 6422 6420 6424 6425 CONECT 6423 6424 CONECT 6424 6422 6423 CONECT 6425 6415 6422 CONECT 6426 6415 6427 CONECT 6427 6426 6428 CONECT 6428 6427 6429 6447 CONECT 6429 6428 6430 6445 CONECT 6430 6429 6431 6446 CONECT 6431 6430 6432 CONECT 6432 6431 6433 CONECT 6433 6432 6434 CONECT 6434 6433 6435 CONECT 6435 6434 6436 CONECT 6436 6435 6437 CONECT 6437 6436 6438 CONECT 6438 6437 6439 CONECT 6439 6438 6440 CONECT 6440 6439 6441 CONECT 6441 6440 6442 CONECT 6442 6441 6443 CONECT 6443 6442 6444 CONECT 6444 6443 CONECT 6445 6429 CONECT 6446 6430 CONECT 6447 6428 6448 CONECT 6448 6447 6449 6450 CONECT 6449 6448 CONECT 6450 6448 6451 CONECT 6451 6450 6452 CONECT 6452 6451 6453 CONECT 6453 6452 6454 CONECT 6454 6453 6455 CONECT 6455 6454 6456 CONECT 6456 6455 6457 CONECT 6457 6456 6458 CONECT 6458 6457 6459 CONECT 6459 6458 6460 CONECT 6460 6459 6461 CONECT 6461 6460 6462 CONECT 6462 6461 6463 CONECT 6463 6462 6464 CONECT 6464 6463 6465 CONECT 6465 6464 6466 CONECT 6466 6465 6467 CONECT 6467 6466 6468 CONECT 6468 6467 6469 CONECT 6469 6468 6470 CONECT 6470 6469 6471 CONECT 6471 6470 6472 CONECT 6472 6471 6473 CONECT 6473 6472 6474 CONECT 6474 6473 MASTER 477 0 6 11 80 0 0 6 6470 4 145 66 END
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PDBbind
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1g7p
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PDBbind
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PDBbind
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RCSB PDB
PDBbind
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PDBbind
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PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >1NEZ_2|Chain... at 98%
1p1z
RCSB PDB
PDBbind
99aa, >1P1Z_2|Chain... at 98%
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >2CLV_2|Chains... at 98%
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RCSB PDB
PDBbind
99aa, >2FO4_2|Chain... at 98%
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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3ard
RCSB PDB
PDBbind
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3are
RCSB PDB
PDBbind
99aa, >3ARE_2|Chain... at 100%
3arf
RCSB PDB
PDBbind
99aa, >3ARF_2|Chain... at 100%
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RCSB PDB
PDBbind
99aa, >3ARG_2|Chain... at 100%
3c8k
RCSB PDB
PDBbind
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3dmm
RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >3HE6_2|Chain... at 100%
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RCSB PDB
PDBbind
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3ilq
RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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3rtq
RCSB PDB
PDBbind
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RCSB PDB
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3rzc
RCSB PDB
PDBbind
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3scm
RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
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RCSB PDB
PDBbind
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PDBbind
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RCSB PDB
PDBbind
100aa, >4PGD_2|Chain... at 99%
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RCSB PDB
PDBbind
100aa, >4PGE_2|Chain... at 99%
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >5TW2_2|Chain... at 100%
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PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >6MJJ_4|Chain... at 100%
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >6MJ4_4|Chain... at 100%
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RCSB PDB
PDBbind
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RCSB PDB
PDBbind
99aa, >6MIV_4|Chain... at 100%
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RCSB PDB
PDBbind
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PDBbind
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3tn0
RCSB PDB
PDBbind
QUX
Entry Information
PDB ID
3qux
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
refolded Va14Vb8.2 TCR
Ligand Name
QUX
EC.Number
E.C.-.-.-.-
Resolution
2.91(Å)
Affinity (Kd/Ki/IC50)
Kd=247nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2011) Embo J. Vol. 30: pp. 2294-2305
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):
P01848
A0A5B9
P01887
P11609
Entrez Gene ID
NCBI Entrez Gene ID:
12010
12479
ASD
Information of known allosteric effects of PDB entries
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