Browse entries in the PDBbind-CN Database
HEADER VIRAL PROTEIN/APOPTOSIS 30-AUG-13 4MI8 TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF MURINE GAMMA-HERPESVIRUS 68 BCL-2 TITLE 2 HOMOLOG M11 AND A BECLIN 1 BH3 DOMAIN-DERIVED PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCL-2 HOMOLOG (GENE 16?); COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 2-136; COMPND 5 SYNONYM: M11, M11 PROTEIN, V-BCL-2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BECLIN-1; COMPND 9 CHAIN: C, D; COMPND 10 FRAGMENT: UNP RESIDUES 107-130; COMPND 11 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN, PROTEIN COMPND 12 GT197; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MURID HERPESVIRUS 4; SOURCE 3 ORGANISM_COMMON: MUHV-4; SOURCE 4 ORGANISM_TAXID: 33708; SOURCE 5 GENE: GAMMAHV.M11, M11, V-BCL-2, V-BCL-2 GAMMAHV.M11; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21(D+); SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS BH3D, BCL-2 FAMILY, ANTI-APOPTOTIC AND ANTI-AUTOPHAGIC ACTIVITIES, KEYWDS 2 VIRAL PROTEIN-APOPTOSIS COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.SU,Y.MEI,S.SINHA REVDAT 3 17-FEB-16 4MI8 1 AUTHOR REVDAT 2 08-OCT-14 4MI8 1 JRNL REVDAT 1 29-JAN-14 4MI8 0 JRNL AUTH M.SU,Y.MEI,R.SANISHVILI,B.LEVINE,C.L.COLBERT,S.SINHA JRNL TITL TARGETING GAMMA-HERPESVIRUS 68 BCL-2-MEDIATED JRNL TITL 2 DOWN-REGULATION OF AUTOPHAGY. JRNL REF J.BIOL.CHEM. V. 289 8029 2014 JRNL REFN ISSN 0021-9258 JRNL PMID 24443581 JRNL DOI 10.1074/JBC.M113.515361 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.16 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 24082 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) : 0.160 REMARK 3 R VALUE (WORKING SET) : 0.156 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 989 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16 REMARK 3 REFLECTION IN BIN (WORKING SET) : 458 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 27.03 REMARK 3 BIN R VALUE (WORKING SET) : 0.1550 REMARK 3 BIN FREE R VALUE SET COUNT : 21 REMARK 3 BIN FREE R VALUE : 0.2610 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2542 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 20 REMARK 3 SOLVENT ATOMS : 133 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.77 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.05000 REMARK 3 B22 (A**2) : -0.04000 REMARK 3 B33 (A**2) : 0.01000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.06000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.221 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.124 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.664 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2614 ; 0.019 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3539 ; 1.970 ; 1.951 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 309 ; 5.889 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;31.320 ;23.680 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 455 ;18.995 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;18.919 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 401 ; 0.120 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1942 ; 0.011 ; 0.020 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 4 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 2 A 136 REMARK 3 ORIGIN FOR THE GROUP (A): -5.6313 41.3706 13.2718 REMARK 3 T TENSOR REMARK 3 T11: 0.1386 T22: 0.1162 REMARK 3 T33: 0.0859 T12: -0.0203 REMARK 3 T13: 0.0881 T23: 0.0081 REMARK 3 L TENSOR REMARK 3 L11: 2.9062 L22: 7.5447 REMARK 3 L33: 1.3266 L12: 0.3261 REMARK 3 L13: -0.2465 L23: -2.0376 REMARK 3 S TENSOR REMARK 3 S11: -0.0064 S12: 0.3130 S13: 0.0936 REMARK 3 S21: -0.1901 S22: -0.0546 S23: -0.5255 REMARK 3 S31: -0.0073 S32: 0.0455 S33: 0.0610 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 2 B 137 REMARK 3 ORIGIN FOR THE GROUP (A): 8.2406 70.9044 12.7799 REMARK 3 T TENSOR REMARK 3 T11: 0.0959 T22: 0.0819 REMARK 3 T33: 0.0737 T12: -0.0378 REMARK 3 T13: -0.0599 T23: -0.0076 REMARK 3 L TENSOR REMARK 3 L11: 2.1173 L22: 2.4018 REMARK 3 L33: 1.4249 L12: -0.4776 REMARK 3 L13: 0.4413 L23: 0.6981 REMARK 3 S TENSOR REMARK 3 S11: 0.0928 S12: 0.1702 S13: -0.1338 REMARK 3 S21: 0.1979 S22: -0.0260 S23: 0.0158 REMARK 3 S31: 0.1699 S32: -0.0555 S33: -0.0668 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 108 C 127 REMARK 3 ORIGIN FOR THE GROUP (A): -6.4562 26.1554 14.9517 REMARK 3 T TENSOR REMARK 3 T11: 0.1276 T22: 0.0250 REMARK 3 T33: 0.1315 T12: 0.0066 REMARK 3 T13: 0.0980 T23: -0.0277 REMARK 3 L TENSOR REMARK 3 L11: 8.8079 L22: 8.4085 REMARK 3 L33: 3.1155 L12: -2.1041 REMARK 3 L13: -2.5972 L23: -2.0796 REMARK 3 S TENSOR REMARK 3 S11: -0.0921 S12: 0.4181 S13: -0.6039 REMARK 3 S21: -0.3665 S22: -0.1888 S23: -0.3024 REMARK 3 S31: 0.2909 S32: -0.0181 S33: 0.2809 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 106 D 127 REMARK 3 ORIGIN FOR THE GROUP (A): 8.3757 86.1927 13.9477 REMARK 3 T TENSOR REMARK 3 T11: 0.1459 T22: 0.0105 REMARK 3 T33: 0.1144 T12: -0.0121 REMARK 3 T13: -0.0463 T23: 0.0067 REMARK 3 L TENSOR REMARK 3 L11: 11.0520 L22: 4.2450 REMARK 3 L33: 3.7665 L12: -0.9635 REMARK 3 L13: 3.4848 L23: -0.3841 REMARK 3 S TENSOR REMARK 3 S11: -0.1786 S12: -0.0878 S13: 0.6392 REMARK 3 S21: -0.1178 S22: 0.1311 S23: 0.0338 REMARK 3 S31: -0.2871 S32: -0.0227 S33: 0.0475 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4MI8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-13. REMARK 100 THE RCSB ID CODE IS RCSB081942. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24082 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE, 8% 2-PROPANOL, REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.29900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.42200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.29900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 70.42200 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8290 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 15740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 37.47028 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 42.69262 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 35.29900 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 70.42200 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 2.17128 REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 70.42200 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 42.69262 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 363 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 330 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 213 LIES ON A SPECIAL POSITION. REMARK 375 HOH C 206 LIES ON A SPECIAL POSITION. REMARK 375 HOH D 214 LIES ON A SPECIAL POSITION. REMARK 375 HOH B 364 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 ALA A 1 REMARK 465 HIS A 137 REMARK 465 HIS A 138 REMARK 465 HIS A 139 REMARK 465 HIS A 140 REMARK 465 HIS A 141 REMARK 465 HIS A 142 REMARK 465 MET B 0 REMARK 465 ALA B 1 REMARK 465 HIS B 138 REMARK 465 HIS B 139 REMARK 465 HIS B 140 REMARK 465 HIS B 141 REMARK 465 HIS B 142 REMARK 465 GLY C 105 REMARK 465 SER C 106 REMARK 465 GLY C 107 REMARK 465 GLY C 128 REMARK 465 GLN C 129 REMARK 465 THR C 130 REMARK 465 GLY D 105 REMARK 465 GLY D 128 REMARK 465 GLN D 129 REMARK 465 THR D 130 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 GLU A 101 -19.73 -142.56 REMARK 500 VAL A 102 -65.11 -96.84 REMARK 500 TRP A 108 72.19 -100.16 REMARK 500 PHE A 132 84.42 -167.54 REMARK 500 PHE B 132 81.07 -155.39 REMARK 500 MET D 126 71.13 55.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 203 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3DVU RELATED DB: PDB REMARK 900 STRUCTURE OF GAMMA-HERPESVIRUS M11 BOUND TO THE BECLIN 1 REMARK 900 BH3D DBREF 4MI8 A 2 136 UNP P89884 P89884_MHV68 2 136 DBREF 4MI8 B 2 136 UNP P89884 P89884_MHV68 2 136 DBREF 4MI8 C 107 130 UNP Q14457 BECN1_HUMAN 107 130 DBREF 4MI8 D 107 130 UNP Q14457 BECN1_HUMAN 107 130 SEQADV 4MI8 MET A 0 UNP P89884 EXPRESSION TAG SEQADV 4MI8 ALA A 1 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 137 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 138 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 139 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 140 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 141 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS A 142 UNP P89884 EXPRESSION TAG SEQADV 4MI8 MET B 0 UNP P89884 EXPRESSION TAG SEQADV 4MI8 ALA B 1 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 137 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 138 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 139 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 140 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 141 UNP P89884 EXPRESSION TAG SEQADV 4MI8 HIS B 142 UNP P89884 EXPRESSION TAG SEQADV 4MI8 GLY C 105 UNP Q14457 EXPRESSION TAG SEQADV 4MI8 SER C 106 UNP Q14457 EXPRESSION TAG SEQADV 4MI8 GLU C 120 UNP Q14457 GLY 120 ENGINEERED MUTATION SEQADV 4MI8 ALA C 121 UNP Q14457 ASP 121 ENGINEERED MUTATION SEQADV 4MI8 GLY D 105 UNP Q14457 EXPRESSION TAG SEQADV 4MI8 SER D 106 UNP Q14457 EXPRESSION TAG SEQADV 4MI8 GLU D 120 UNP Q14457 GLY 120 ENGINEERED MUTATION SEQADV 4MI8 ALA D 121 UNP Q14457 ASP 121 ENGINEERED MUTATION SEQRES 1 A 143 MET ALA SER HIS LYS LYS SER GLY THR TYR TRP ALA THR SEQRES 2 A 143 LEU ILE THR ALA PHE LEU LYS THR VAL SER LYS VAL GLU SEQRES 3 A 143 GLU LEU ASP CYS VAL ASP SER ALA VAL LEU VAL ASP VAL SEQRES 4 A 143 SER LYS ILE ILE THR LEU THR GLN GLU PHE ARG ARG HIS SEQRES 5 A 143 TYR ASP SER VAL TYR ARG ALA ASP TYR GLY PRO ALA LEU SEQRES 6 A 143 LYS ASN TRP LYS ARG ASP LEU SER LYS LEU PHE THR SER SEQRES 7 A 143 LEU PHE VAL ASP VAL ILE ASN SER GLY ARG ILE VAL GLY SEQRES 8 A 143 PHE PHE ASP VAL GLY ARG TYR VAL CYS GLU GLU VAL LEU SEQRES 9 A 143 CYS PRO GLY SER TRP THR GLU ASP HIS GLU LEU LEU ASN SEQRES 10 A 143 ASP CYS MET THR HIS PHE PHE ILE GLU ASN ASN LEU MET SEQRES 11 A 143 ASN HIS PHE PRO LEU GLU ASP HIS HIS HIS HIS HIS HIS SEQRES 1 B 143 MET ALA SER HIS LYS LYS SER GLY THR TYR TRP ALA THR SEQRES 2 B 143 LEU ILE THR ALA PHE LEU LYS THR VAL SER LYS VAL GLU SEQRES 3 B 143 GLU LEU ASP CYS VAL ASP SER ALA VAL LEU VAL ASP VAL SEQRES 4 B 143 SER LYS ILE ILE THR LEU THR GLN GLU PHE ARG ARG HIS SEQRES 5 B 143 TYR ASP SER VAL TYR ARG ALA ASP TYR GLY PRO ALA LEU SEQRES 6 B 143 LYS ASN TRP LYS ARG ASP LEU SER LYS LEU PHE THR SER SEQRES 7 B 143 LEU PHE VAL ASP VAL ILE ASN SER GLY ARG ILE VAL GLY SEQRES 8 B 143 PHE PHE ASP VAL GLY ARG TYR VAL CYS GLU GLU VAL LEU SEQRES 9 B 143 CYS PRO GLY SER TRP THR GLU ASP HIS GLU LEU LEU ASN SEQRES 10 B 143 ASP CYS MET THR HIS PHE PHE ILE GLU ASN ASN LEU MET SEQRES 11 B 143 ASN HIS PHE PRO LEU GLU ASP HIS HIS HIS HIS HIS HIS SEQRES 1 C 26 GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS SEQRES 2 C 26 VAL THR GLU ALA LEU PHE ASP ILE MET SER GLY GLN THR SEQRES 1 D 26 GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS SEQRES 2 D 26 VAL THR GLU ALA LEU PHE ASP ILE MET SER GLY GLN THR HET SO4 A 201 5 HET SO4 B 201 5 HET SO4 B 202 5 HET SO4 B 203 5 HETNAM SO4 SULFATE ION FORMUL 5 SO4 4(O4 S 2-) FORMUL 9 HOH *133(H2 O) HELIX 1 1 SER A 6 LYS A 23 1 18 HELIX 2 2 GLU A 26 VAL A 30 5 5 HELIX 3 3 ASP A 31 TYR A 56 1 26 HELIX 4 4 ALA A 63 LYS A 65 5 3 HELIX 5 5 ASN A 66 ASP A 81 1 16 HELIX 6 6 ASN A 84 VAL A 102 1 19 HELIX 7 7 THR A 109 ASN A 126 1 18 HELIX 8 8 ASN A 127 PHE A 132 5 6 HELIX 9 9 SER B 6 LYS B 23 1 18 HELIX 10 10 GLU B 26 VAL B 30 5 5 HELIX 11 11 ASP B 31 TYR B 56 1 26 HELIX 12 12 TYR B 60 LYS B 65 1 6 HELIX 13 13 ASN B 66 PHE B 79 1 14 HELIX 14 14 ASN B 84 VAL B 102 1 19 HELIX 15 15 THR B 109 ASN B 126 1 18 HELIX 16 16 ASN B 127 PHE B 132 5 6 HELIX 17 17 MET C 109 ASP C 124 1 16 HELIX 18 18 GLY D 107 ASP D 124 1 18 SSBOND 1 CYS A 29 CYS B 104 1555 1555 1.99 SITE 1 AC1 6 ARG A 57 ALA A 58 HOH A 325 SO4 B 201 SITE 2 AC1 6 ARG C 115 ARG D 115 SITE 1 AC2 5 SO4 A 201 ARG B 57 ALA B 58 ARG C 115 SITE 2 AC2 5 ARG D 115 SITE 1 AC3 2 HIS B 3 LYS B 4 SITE 1 AC4 3 ASN B 127 ASN B 130 HIS B 131 CRYST1 70.598 140.844 54.038 90.00 127.81 90.00 C 1 2 1 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 0.014165 0.000000 0.010992 0.00000 SCALE2 0.000000 0.007100 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023424 0.00000 ATOM 1 N SER A 2 -26.601 43.656 10.158 1.00 94.69 N ANISOU 1 N SER A 2 9674 11050 15254 -384 -762 2727 N ATOM 2 CA SER A 2 -25.166 43.441 9.821 1.00100.73 C ANISOU 2 CA SER A 2 10903 12058 15313 -427 -777 2386 C ATOM 3 C SER A 2 -24.973 42.932 8.386 1.00102.82 C ANISOU 3 C SER A 2 11375 12451 15239 -632 -1321 2362 C ATOM 4 O SER A 2 -25.752 42.099 7.918 1.00104.64 O ANISOU 4 O SER A 2 11487 12610 15662 -773 -1692 2468 O ATOM 5 CB SER A 2 -24.566 42.409 10.761 1.00 99.26 C ANISOU 5 CB SER A 2 10880 11919 14916 -386 -502 2107 C ATOM 6 OG SER A 2 -24.432 41.192 10.062 1.00105.23 O ANISOU 6 OG SER A 2 11773 12755 15452 -549 -853 1991 O ATOM 7 N HIS A 3 -23.919 43.415 7.715 1.00100.59 N ANISOU 7 N HIS A 3 11429 12340 14452 -651 -1352 2220 N ATOM 8 CA HIS A 3 -23.594 43.029 6.323 1.00 98.03 C ANISOU 8 CA HIS A 3 11411 12137 13699 -828 -1790 2174 C ATOM 9 C HIS A 3 -22.135 43.248 5.991 1.00 89.75 C ANISOU 9 C HIS A 3 10761 11270 12070 -799 -1601 1924 C ATOM 10 O HIS A 3 -21.379 43.848 6.764 1.00 81.16 O ANISOU 10 O HIS A 3 9682 10213 10942 -656 -1198 1818 O ATOM 11 CB HIS A 3 -24.410 43.830 5.299 1.00109.50 C ANISOU 11 CB HIS A 3 12747 13531 15328 -923 -2209 2513 C ATOM 12 CG HIS A 3 -25.777 44.283 5.786 1.00119.02 C ANISOU 12 CG HIS A 3 13435 14516 17271 -876 -2252 2862 C ATOM 13 ND1 HIS A 3 -26.844 44.360 4.966 1.00119.99 N ANISOU 13 ND1 HIS A 3 13356 14524 17710 -1017 -2770 3187 N ATOM 14 CD2 HIS A 3 -26.220 44.697 7.047 1.00119.16 C ANISOU 14 CD2 HIS A 3 13105 14383 17787 -692 -1803 2942 C ATOM 15 CE1 HIS A 3 -27.914 44.802 5.662 1.00121.76 C ANISOU 15 CE1 HIS A 3 13068 14528 18665 -919 -2640 3482 C ATOM 16 NE2 HIS A 3 -27.528 45.001 6.937 1.00119.93 N ANISOU 16 NE2 HIS A 3 12772 14274 18521 -713 -2015 3318 N ATOM 17 N LYS A 4 -21.749 42.838 4.789 1.00 85.39 N ANISOU 17 N LYS A 4 10552 10816 11078 -938 -1899 1851 N ATOM 18 CA LYS A 4 -20.409 43.016 4.268 1.00 80.36 C ANISOU 18 CA LYS A 4 10295 10329 9911 -919 -1723 1657 C ATOM 19 C LYS A 4 -20.007 44.477 4.206 1.00 80.26 C ANISOU 19 C LYS A 4 10238 10347 9912 -822 -1540 1804 C ATOM 20 O LYS A 4 -20.789 45.308 3.807 1.00 79.32 O ANISOU 20 O LYS A 4 9956 10165 10016 -846 -1752 2088 O ATOM 21 CB LYS A 4 -20.314 42.356 2.885 1.00 85.31 C ANISOU 21 CB LYS A 4 11324 11009 10080 -1092 -2090 1599 C ATOM 22 CG LYS A 4 -19.454 43.046 1.812 1.00 94.10 C ANISOU 22 CG LYS A 4 12810 12235 10708 -1108 -2060 1611 C ATOM 23 CD LYS A 4 -18.505 42.104 1.092 1.00 95.16 C ANISOU 23 CD LYS A 4 13430 12440 10287 -1166 -1991 1331 C ATOM 24 CE LYS A 4 -18.380 42.463 -0.376 1.00 97.24 C ANISOU 24 CE LYS A 4 14130 12752 10064 -1278 -2229 1430 C ATOM 25 NZ LYS A 4 -17.071 43.048 -0.766 1.00 94.54 N ANISOU 25 NZ LYS A 4 14049 12507 9365 -1181 -1824 1366 N ATOM 26 N LYS A 5 -18.770 44.780 4.562 1.00 74.25 N ANISOU 26 N LYS A 5 9612 9663 8937 -722 -1169 1626 N ATOM 27 CA LYS A 5 -18.275 46.136 4.423 1.00 69.96 C ANISOU 27 CA LYS A 5 9054 9136 8391 -647 -1005 1753 C ATOM 28 C LYS A 5 -17.160 46.220 3.403 1.00 65.33 C ANISOU 28 C LYS A 5 8834 8669 7319 -685 -951 1678 C ATOM 29 O LYS A 5 -16.608 45.235 2.987 1.00 64.45 O ANISOU 29 O LYS A 5 8993 8621 6874 -738 -945 1482 O ATOM 30 CB LYS A 5 -17.834 46.713 5.760 1.00 66.58 C ANISOU 30 CB LYS A 5 8432 8647 8219 -498 -618 1669 C ATOM 31 CG LYS A 5 -18.915 46.737 6.811 1.00 67.37 C ANISOU 31 CG LYS A 5 8208 8603 8784 -434 -573 1753 C ATOM 32 CD LYS A 5 -19.844 47.911 6.652 1.00 70.03 C ANISOU 32 CD LYS A 5 8300 8821 9487 -400 -657 2060 C ATOM 33 CE LYS A 5 -20.977 47.819 7.644 1.00 74.73 C ANISOU 33 CE LYS A 5 8570 9244 10581 -328 -563 2159 C ATOM 34 NZ LYS A 5 -22.290 48.329 7.171 1.00 83.45 N ANISOU 34 NZ LYS A 5 9380 10214 12114 -353 -816 2511 N ATOM 35 N SER A 6 -16.846 47.429 2.998 1.00 64.45 N ANISOU 35 N SER A 6 8728 8565 7193 -649 -881 1851 N ATOM 36 CA SER A 6 -15.929 47.654 1.912 1.00 62.83 C ANISOU 36 CA SER A 6 8862 8453 6558 -683 -821 1857 C ATOM 37 C SER A 6 -14.502 47.508 2.326 1.00 58.86 C ANISOU 37 C SER A 6 8446 7988 5929 -600 -414 1637 C ATOM 38 O SER A 6 -14.189 47.623 3.471 1.00 54.16 O ANISOU 38 O SER A 6 7631 7343 5603 -513 -205 1531 O ATOM 39 CB SER A 6 -16.137 49.043 1.351 1.00 60.28 C ANISOU 39 CB SER A 6 8481 8106 6316 -674 -889 2163 C ATOM 40 OG SER A 6 -15.536 50.000 2.159 1.00 56.26 O ANISOU 40 OG SER A 6 7761 7540 6074 -554 -568 2166 O ATOM 41 N GLY A 7 -13.648 47.273 1.346 1.00 58.84 N ANISOU 41 N GLY A 7 8783 8055 5516 -630 -308 1589 N ATOM 42 CA GLY A 7 -12.232 47.252 1.551 1.00 56.49 C ANISOU 42 CA GLY A 7 8544 7770 5149 -551 88 1447 C ATOM 43 C GLY A 7 -11.759 48.561 2.097 1.00 56.61 C ANISOU 43 C GLY A 7 8313 7731 5464 -469 277 1578 C ATOM 44 O GLY A 7 -10.837 48.606 2.872 1.00 57.55 O ANISOU 44 O GLY A 7 8306 7812 5750 -401 531 1458 O ATOM 45 N THR A 8 -12.401 49.632 1.682 1.00 55.52 N ANISOU 45 N THR A 8 8109 7572 5415 -485 122 1837 N ATOM 46 CA THR A 8 -12.042 50.949 2.147 1.00 54.15 C ANISOU 46 CA THR A 8 7713 7316 5546 -415 281 1972 C ATOM 47 C THR A 8 -12.288 51.065 3.630 1.00 50.64 C ANISOU 47 C THR A 8 6970 6772 5497 -350 334 1849 C ATOM 48 O THR A 8 -11.473 51.542 4.365 1.00 51.35 O ANISOU 48 O THR A 8 6951 6792 5769 -295 545 1774 O ATOM 49 CB THR A 8 -12.875 52.030 1.446 1.00 56.68 C ANISOU 49 CB THR A 8 7996 7607 5933 -443 71 2295 C ATOM 50 OG1 THR A 8 -12.802 51.862 0.034 1.00 63.09 O ANISOU 50 OG1 THR A 8 9154 8511 6307 -521 -36 2425 O ATOM 51 CG2 THR A 8 -12.379 53.358 1.794 1.00 55.41 C ANISOU 51 CG2 THR A 8 7648 7344 6061 -374 262 2426 C ATOM 52 N TYR A 9 -13.452 50.656 4.054 1.00 48.83 N ANISOU 52 N TYR A 9 6626 6519 5407 -363 131 1845 N ATOM 53 CA TYR A 9 -13.796 50.656 5.470 1.00 45.15 C ANISOU 53 CA TYR A 9 5935 5949 5271 -296 216 1726 C ATOM 54 C TYR A 9 -12.857 49.754 6.296 1.00 42.06 C ANISOU 54 C TYR A 9 5599 5579 4802 -274 395 1444 C ATOM 55 O TYR A 9 -12.408 50.125 7.404 1.00 38.48 O ANISOU 55 O TYR A 9 5047 5032 4540 -217 552 1342 O ATOM 56 CB TYR A 9 -15.243 50.246 5.677 1.00 49.69 C ANISOU 56 CB TYR A 9 6370 6483 6026 -312 -2 1803 C ATOM 57 CG TYR A 9 -15.596 50.360 7.113 1.00 50.80 C ANISOU 57 CG TYR A 9 6318 6495 6490 -225 161 1706 C ATOM 58 CD1 TYR A 9 -15.583 51.605 7.750 1.00 52.35 C ANISOU 58 CD1 TYR A 9 6387 6546 6959 -142 329 1776 C ATOM 59 CD2 TYR A 9 -15.832 49.229 7.868 1.00 48.62 C ANISOU 59 CD2 TYR A 9 6032 6226 6216 -222 181 1530 C ATOM 60 CE1 TYR A 9 -15.840 51.717 9.106 1.00 54.34 C ANISOU 60 CE1 TYR A 9 6548 6657 7440 -59 518 1658 C ATOM 61 CE2 TYR A 9 -16.112 49.328 9.215 1.00 53.12 C ANISOU 61 CE2 TYR A 9 6487 6671 7026 -138 368 1443 C ATOM 62 CZ TYR A 9 -16.110 50.564 9.832 1.00 52.08 C ANISOU 62 CZ TYR A 9 6277 6393 7119 -56 542 1498 C ATOM 63 OH TYR A 9 -16.381 50.654 11.173 1.00 50.34 O ANISOU 63 OH TYR A 9 6023 6027 7074 28 754 1393 O ATOM 64 N TRP A 10 -12.532 48.595 5.737 1.00 40.19 N ANISOU 64 N TRP A 10 5542 5446 4282 -325 358 1326 N ATOM 65 CA TRP A 10 -11.749 47.625 6.422 1.00 37.71 C ANISOU 65 CA TRP A 10 5261 5143 3924 -307 494 1093 C ATOM 66 C TRP A 10 -10.334 48.049 6.592 1.00 37.60 C ANISOU 66 C TRP A 10 5252 5102 3933 -273 721 1047 C ATOM 67 O TRP A 10 -9.755 47.743 7.636 1.00 34.50 O ANISOU 67 O TRP A 10 4783 4655 3672 -244 810 904 O ATOM 68 CB TRP A 10 -11.816 46.305 5.692 1.00 42.05 C ANISOU 68 CB TRP A 10 6007 5777 4192 -367 406 988 C ATOM 69 CG TRP A 10 -12.941 45.429 6.201 1.00 41.43 C ANISOU 69 CG TRP A 10 5851 5680 4209 -395 219 930 C ATOM 70 CD1 TRP A 10 -14.178 45.205 5.605 1.00 44.47 C ANISOU 70 CD1 TRP A 10 6243 6071 4584 -469 -65 1047 C ATOM 71 CD2 TRP A 10 -12.962 44.658 7.468 1.00 39.52 C ANISOU 71 CD2 TRP A 10 5493 5391 4132 -357 292 770 C ATOM 72 NE1 TRP A 10 -14.954 44.356 6.391 1.00 46.11 N ANISOU 72 NE1 TRP A 10 6316 6229 4975 -474 -148 974 N ATOM 73 CE2 TRP A 10 -14.270 43.972 7.511 1.00 41.82 C ANISOU 73 CE2 TRP A 10 5715 5660 4515 -404 78 805 C ATOM 74 CE3 TRP A 10 -12.030 44.430 8.511 1.00 35.31 C ANISOU 74 CE3 TRP A 10 4917 4822 3677 -301 483 625 C ATOM 75 CZ2 TRP A 10 -14.620 43.117 8.567 1.00 38.96 C ANISOU 75 CZ2 TRP A 10 5249 5246 4309 -381 113 700 C ATOM 76 CZ3 TRP A 10 -12.402 43.586 9.575 1.00 35.82 C ANISOU 76 CZ3 TRP A 10 4910 4843 3857 -283 483 519 C ATOM 77 CH2 TRP A 10 -13.664 42.948 9.603 1.00 35.77 C ANISOU 77 CH2 TRP A 10 4842 4821 3928 -315 330 556 C ATOM 78 N ALA A 11 -9.768 48.780 5.610 1.00 37.84 N ANISOU 78 N ALA A 11 5362 5152 3865 -281 806 1191 N ATOM 79 CA ALA A 11 -8.435 49.367 5.745 1.00 35.36 C ANISOU 79 CA ALA A 11 4990 4776 3668 -251 1027 1204 C ATOM 80 C ALA A 11 -8.396 50.305 6.941 1.00 35.23 C ANISOU 80 C ALA A 11 4777 4628 3982 -223 1020 1201 C ATOM 81 O ALA A 11 -7.440 50.321 7.706 1.00 35.41 O ANISOU 81 O ALA A 11 4722 4571 4163 -215 1106 1108 O ATOM 82 CB ALA A 11 -8.034 50.152 4.458 1.00 37.17 C ANISOU 82 CB ALA A 11 5329 5030 3762 -261 1132 1414 C ATOM 83 N THR A 12 -9.416 51.132 7.076 1.00 34.11 N ANISOU 83 N THR A 12 4565 4438 3956 -213 911 1314 N ATOM 84 CA THR A 12 -9.543 52.017 8.247 1.00 36.01 C ANISOU 84 CA THR A 12 4678 4521 4484 -179 926 1285 C ATOM 85 C THR A 12 -9.609 51.223 9.572 1.00 31.55 C ANISOU 85 C THR A 12 4116 3915 3957 -164 914 1064 C ATOM 86 O THR A 12 -8.926 51.538 10.579 1.00 29.84 O ANISOU 86 O THR A 12 3888 3578 3871 -163 954 958 O ATOM 87 CB THR A 12 -10.821 52.879 8.093 1.00 36.18 C ANISOU 87 CB THR A 12 4621 4483 4644 -152 842 1456 C ATOM 88 OG1 THR A 12 -10.568 53.794 7.037 1.00 38.57 O ANISOU 88 OG1 THR A 12 4922 4789 4943 -167 855 1676 O ATOM 89 CG2 THR A 12 -11.164 53.686 9.345 1.00 36.08 C ANISOU 89 CG2 THR A 12 4525 4276 4908 -99 902 1397 C ATOM 90 N LEU A 13 -10.433 50.181 9.541 1.00 31.50 N ANISOU 90 N LEU A 13 4142 3997 3828 -165 837 1010 N ATOM 91 CA LEU A 13 -10.751 49.410 10.721 1.00 29.63 C ANISOU 91 CA LEU A 13 3914 3725 3621 -145 834 847 C ATOM 92 C LEU A 13 -9.494 48.645 11.156 1.00 29.22 C ANISOU 92 C LEU A 13 3915 3688 3500 -168 872 693 C ATOM 93 O LEU A 13 -9.154 48.584 12.363 1.00 29.60 O ANISOU 93 O LEU A 13 3986 3641 3618 -161 879 576 O ATOM 94 CB LEU A 13 -11.873 48.426 10.320 1.00 30.21 C ANISOU 94 CB LEU A 13 3983 3888 3609 -156 728 866 C ATOM 95 CG LEU A 13 -12.320 47.544 11.456 1.00 30.79 C ANISOU 95 CG LEU A 13 4053 3923 3722 -132 748 733 C ATOM 96 CD1 LEU A 13 -12.466 48.391 12.755 1.00 30.83 C ANISOU 96 CD1 LEU A 13 4055 3763 3897 -71 869 697 C ATOM 97 CD2 LEU A 13 -13.609 46.770 11.029 1.00 31.44 C ANISOU 97 CD2 LEU A 13 4074 4051 3820 -150 625 804 C ATOM 98 N ILE A 14 -8.753 48.095 10.190 1.00 29.08 N ANISOU 98 N ILE A 14 3931 3767 3352 -195 904 705 N ATOM 99 CA ILE A 14 -7.523 47.389 10.551 1.00 27.82 C ANISOU 99 CA ILE A 14 3770 3592 3209 -206 960 597 C ATOM 100 C ILE A 14 -6.475 48.280 11.244 1.00 28.48 C ANISOU 100 C ILE A 14 3777 3537 3506 -220 977 609 C ATOM 101 O ILE A 14 -5.764 47.884 12.257 1.00 26.65 O ANISOU 101 O ILE A 14 3528 3226 3371 -239 921 510 O ATOM 102 CB ILE A 14 -6.950 46.645 9.316 1.00 29.61 C ANISOU 102 CB ILE A 14 4061 3913 3276 -214 1061 613 C ATOM 103 CG1 ILE A 14 -7.866 45.442 8.942 1.00 30.21 C ANISOU 103 CG1 ILE A 14 4247 4085 3146 -225 985 533 C ATOM 104 CG2 ILE A 14 -5.565 46.093 9.657 1.00 28.73 C ANISOU 104 CG2 ILE A 14 3885 3742 3291 -210 1163 550 C ATOM 105 CD1 ILE A 14 -7.859 45.053 7.487 1.00 33.59 C ANISOU 105 CD1 ILE A 14 4841 4597 3324 -245 1038 570 C ATOM 106 N THR A 15 -6.314 49.493 10.686 1.00 29.66 N ANISOU 106 N THR A 15 3881 3640 3748 -224 1022 748 N ATOM 107 CA THR A 15 -5.337 50.397 11.260 1.00 30.29 C ANISOU 107 CA THR A 15 3880 3562 4066 -256 1009 772 C ATOM 108 C THR A 15 -5.814 50.812 12.668 1.00 30.81 C ANISOU 108 C THR A 15 4015 3496 4194 -262 889 655 C ATOM 109 O THR A 15 -5.012 50.903 13.592 1.00 31.92 O ANISOU 109 O THR A 15 4165 3508 4454 -310 790 580 O ATOM 110 CB THR A 15 -5.258 51.671 10.422 1.00 33.29 C ANISOU 110 CB THR A 15 4202 3900 4548 -256 1085 955 C ATOM 111 OG1 THR A 15 -4.965 51.341 9.059 1.00 32.63 O ANISOU 111 OG1 THR A 15 4128 3937 4333 -243 1228 1075 O ATOM 112 CG2 THR A 15 -4.165 52.665 11.010 1.00 34.29 C ANISOU 112 CG2 THR A 15 4223 3823 4985 -308 1048 988 C ATOM 113 N ALA A 16 -7.113 51.091 12.835 1.00 30.04 N ANISOU 113 N ALA A 16 3981 3405 4028 -217 899 652 N ATOM 114 CA ALA A 16 -7.612 51.517 14.153 1.00 29.93 C ANISOU 114 CA ALA A 16 4082 3238 4052 -204 866 539 C ATOM 115 C ALA A 16 -7.468 50.334 15.109 1.00 28.70 C ANISOU 115 C ALA A 16 4028 3105 3771 -216 803 388 C ATOM 116 O ALA A 16 -7.081 50.534 16.266 1.00 29.62 O ANISOU 116 O ALA A 16 4281 3078 3895 -248 723 279 O ATOM 117 CB ALA A 16 -9.033 51.971 14.027 1.00 30.09 C ANISOU 117 CB ALA A 16 4102 3245 4086 -134 949 605 C ATOM 118 N PHE A 17 -7.611 49.095 14.583 1.00 27.49 N ANISOU 118 N PHE A 17 3827 3117 3499 -204 814 385 N ATOM 119 CA PHE A 17 -7.457 47.879 15.414 1.00 25.71 C ANISOU 119 CA PHE A 17 3677 2914 3179 -213 757 267 C ATOM 120 C PHE A 17 -6.029 47.813 15.900 1.00 26.68 C ANISOU 120 C PHE A 17 3789 2953 3397 -278 639 234 C ATOM 121 O PHE A 17 -5.825 47.665 17.103 1.00 27.41 O ANISOU 121 O PHE A 17 4017 2941 3455 -308 527 145 O ATOM 122 CB PHE A 17 -7.784 46.612 14.667 1.00 24.46 C ANISOU 122 CB PHE A 17 3462 2915 2916 -197 787 271 C ATOM 123 CG PHE A 17 -7.413 45.337 15.412 1.00 25.41 C ANISOU 123 CG PHE A 17 3626 3045 2985 -209 731 173 C ATOM 124 CD1 PHE A 17 -8.233 44.816 16.433 1.00 24.95 C ANISOU 124 CD1 PHE A 17 3675 2956 2850 -184 729 109 C ATOM 125 CD2 PHE A 17 -6.206 44.652 15.113 1.00 26.24 C ANISOU 125 CD2 PHE A 17 3653 3166 3152 -238 705 168 C ATOM 126 CE1 PHE A 17 -7.876 43.608 17.074 1.00 26.65 C ANISOU 126 CE1 PHE A 17 3928 3177 3021 -197 671 47 C ATOM 127 CE2 PHE A 17 -5.863 43.464 15.745 1.00 25.63 C ANISOU 127 CE2 PHE A 17 3590 3082 3066 -245 646 105 C ATOM 128 CZ PHE A 17 -6.688 42.936 16.733 1.00 25.24 C ANISOU 128 CZ PHE A 17 3658 3018 2912 -230 612 45 C ATOM 129 N LEU A 18 -5.059 47.918 14.988 1.00 26.72 N ANISOU 129 N LEU A 18 3640 2983 3528 -303 663 323 N ATOM 130 CA LEU A 18 -3.617 47.843 15.365 1.00 29.59 C ANISOU 130 CA LEU A 18 3914 3239 4091 -368 547 341 C ATOM 131 C LEU A 18 -3.170 49.013 16.291 1.00 31.78 C ANISOU 131 C LEU A 18 4261 3312 4503 -441 375 325 C ATOM 132 O LEU A 18 -2.366 48.809 17.229 1.00 35.34 O ANISOU 132 O LEU A 18 4747 3639 5043 -516 162 289 O ATOM 133 CB LEU A 18 -2.728 47.783 14.141 1.00 27.56 C ANISOU 133 CB LEU A 18 3462 3022 3986 -361 685 467 C ATOM 134 CG LEU A 18 -2.989 46.573 13.218 1.00 28.12 C ANISOU 134 CG LEU A 18 3526 3255 3904 -302 850 455 C ATOM 135 CD1 LEU A 18 -2.186 46.742 11.905 1.00 31.15 C ANISOU 135 CD1 LEU A 18 3790 3655 4390 -280 1065 586 C ATOM 136 CD2 LEU A 18 -2.508 45.298 13.878 1.00 27.49 C ANISOU 136 CD2 LEU A 18 3423 3158 3864 -307 777 381 C ATOM 137 N LYS A 19 -3.664 50.214 16.032 1.00 31.91 N ANISOU 137 N LYS A 19 4308 3272 4544 -429 439 359 N ATOM 138 CA LYS A 19 -3.261 51.382 16.850 1.00 35.98 C ANISOU 138 CA LYS A 19 4919 3559 5192 -504 282 326 C ATOM 139 C LYS A 19 -3.828 51.183 18.242 1.00 40.90 C ANISOU 139 C LYS A 19 5844 4093 5603 -513 174 156 C ATOM 140 O LYS A 19 -3.119 51.429 19.246 1.00 45.63 O ANISOU 140 O LYS A 19 6588 4511 6237 -612 -68 87 O ATOM 141 CB LYS A 19 -3.733 52.725 16.263 1.00 36.04 C ANISOU 141 CB LYS A 19 4899 3502 5294 -477 402 402 C ATOM 142 CG LYS A 19 -3.132 53.061 14.907 1.00 36.33 C ANISOU 142 CG LYS A 19 4682 3602 5519 -473 523 595 C ATOM 143 CD LYS A 19 -3.511 54.463 14.386 1.00 37.24 C ANISOU 143 CD LYS A 19 4766 3624 5759 -458 612 701 C ATOM 144 CE LYS A 19 -2.677 54.749 13.132 1.00 39.68 C ANISOU 144 CE LYS A 19 4844 3973 6259 -468 731 914 C ATOM 145 NZ LYS A 19 -2.977 56.003 12.304 1.00 43.93 N ANISOU 145 NZ LYS A 19 5314 4458 6920 -446 850 1087 N ATOM 146 N THR A 20 -5.079 50.695 18.316 1.00 38.74 N ANISOU 146 N THR A 20 5676 3932 5113 -419 343 104 N ATOM 147 CA THR A 20 -5.724 50.459 19.625 1.00 39.47 C ANISOU 147 CA THR A 20 6078 3935 4984 -405 326 -39 C ATOM 148 C THR A 20 -4.953 49.430 20.423 1.00 40.37 C ANISOU 148 C THR A 20 6278 4046 5014 -474 113 -89 C ATOM 149 O THR A 20 -4.685 49.682 21.570 1.00 44.19 O ANISOU 149 O THR A 20 7041 4362 5387 -541 -55 -185 O ATOM 150 CB THR A 20 -7.226 50.045 19.533 1.00 40.51 C ANISOU 150 CB THR A 20 6246 4169 4976 -284 578 -44 C ATOM 151 OG1 THR A 20 -8.027 51.072 18.925 1.00 37.14 O ANISOU 151 OG1 THR A 20 5744 3705 4661 -219 750 24 O ATOM 152 CG2 THR A 20 -7.804 49.800 20.896 1.00 41.74 C ANISOU 152 CG2 THR A 20 6731 4211 4918 -260 622 -169 C ATOM 153 N VAL A 21 -4.609 48.268 19.853 1.00 38.48 N ANISOU 153 N VAL A 21 5832 3971 4817 -462 113 -23 N ATOM 154 CA VAL A 21 -3.942 47.227 20.624 1.00 33.98 C ANISOU 154 CA VAL A 21 5321 3387 4202 -517 -84 -44 C ATOM 155 C VAL A 21 -2.482 47.613 20.872 1.00 41.63 C ANISOU 155 C VAL A 21 6206 4204 5409 -642 -381 12 C ATOM 156 O VAL A 21 -1.836 47.126 21.825 1.00 41.55 O ANISOU 156 O VAL A 21 6313 4096 5378 -725 -653 2 O ATOM 157 CB VAL A 21 -4.031 45.800 19.995 1.00 33.61 C ANISOU 157 CB VAL A 21 5085 3525 4161 -459 18 3 C ATOM 158 CG1 VAL A 21 -5.488 45.376 19.752 1.00 29.03 C ANISOU 158 CG1 VAL A 21 4560 3071 3399 -359 257 -32 C ATOM 159 CG2 VAL A 21 -3.202 45.685 18.714 1.00 30.19 C ANISOU 159 CG2 VAL A 21 4334 3162 3976 -458 80 111 C ATOM 160 N SER A 22 -1.944 48.496 20.023 1.00 44.80 N ANISOU 160 N SER A 22 6393 4566 6065 -663 -349 98 N ATOM 161 CA SER A 22 -0.633 49.109 20.302 1.00 47.13 C ANISOU 161 CA SER A 22 6591 4663 6654 -794 -638 169 C ATOM 162 C SER A 22 -0.673 50.293 21.285 1.00 50.96 C ANISOU 162 C SER A 22 7384 4915 7064 -890 -851 63 C ATOM 163 O SER A 22 0.366 50.765 21.747 1.00 54.04 O ANISOU 163 O SER A 22 7756 5101 7674 -1031 -1180 103 O ATOM 164 CB SER A 22 0.040 49.522 19.008 1.00 45.65 C ANISOU 164 CB SER A 22 6037 4501 6807 -780 -491 330 C ATOM 165 OG SER A 22 0.321 48.352 18.290 1.00 44.49 O ANISOU 165 OG SER A 22 5668 4506 6729 -713 -337 409 O ATOM 166 N LYS A 23 -1.873 50.761 21.611 1.00 52.02 N ANISOU 166 N LYS A 23 7803 5050 6910 -818 -665 -67 N ATOM 167 CA LYS A 23 -2.031 51.885 22.540 1.00 58.27 C ANISOU 167 CA LYS A 23 8954 5595 7590 -888 -795 -201 C ATOM 168 C LYS A 23 -1.417 53.166 21.967 1.00 58.71 C ANISOU 168 C LYS A 23 8832 5495 7979 -956 -860 -130 C ATOM 169 O LYS A 23 -0.703 53.862 22.674 1.00 62.76 O ANISOU 169 O LYS A 23 9508 5757 8582 -1100 -1178 -180 O ATOM 170 CB LYS A 23 -1.409 51.568 23.907 1.00 60.51 C ANISOU 170 CB LYS A 23 9572 5708 7711 -1025 -1188 -288 C ATOM 171 CG LYS A 23 -2.069 50.414 24.626 1.00 63.12 C ANISOU 171 CG LYS A 23 10147 6154 7683 -961 -1115 -353 C ATOM 172 CD LYS A 23 -1.042 49.802 25.569 1.00 74.08 C ANISOU 172 CD LYS A 23 11672 7431 9044 -1114 -1575 -327 C ATOM 173 CE LYS A 23 -1.655 49.156 26.824 1.00 78.56 C ANISOU 173 CE LYS A 23 12739 7972 9138 -1105 -1602 -440 C ATOM 174 NZ LYS A 23 -1.532 50.019 28.051 1.00 78.22 N ANISOU 174 NZ LYS A 23 13272 7641 8808 -1233 -1870 -599 N ATOM 175 N VAL A 24 -1.676 53.449 20.687 1.00 56.00 N ANISOU 175 N VAL A 24 8171 5290 7816 -863 -582 -3 N ATOM 176 CA VAL A 24 -1.312 54.712 20.069 1.00 54.90 C ANISOU 176 CA VAL A 24 7873 5014 7974 -901 -565 85 C ATOM 177 C VAL A 24 -2.537 55.432 19.453 1.00 60.20 C ANISOU 177 C VAL A 24 8565 5739 8568 -768 -223 87 C ATOM 178 O VAL A 24 -2.438 56.158 18.445 1.00 58.55 O ANISOU 178 O VAL A 24 8116 5538 8592 -745 -94 236 O ATOM 179 CB VAL A 24 -0.166 54.566 19.052 1.00 54.13 C ANISOU 179 CB VAL A 24 7339 4966 8262 -941 -590 305 C ATOM 180 CG1 VAL A 24 1.055 54.048 19.745 1.00 56.40 C ANISOU 180 CG1 VAL A 24 7570 5128 8732 -1081 -959 333 C ATOM 181 CG2 VAL A 24 -0.539 53.671 17.877 1.00 49.07 C ANISOU 181 CG2 VAL A 24 6466 4620 7559 -808 -275 416 C ATOM 182 N GLU A 25 -3.700 55.240 20.067 1.00 61.43 N ANISOU 182 N GLU A 25 9001 5916 8424 -679 -71 -52 N ATOM 183 CA GLU A 25 -4.870 56.045 19.738 1.00 64.42 C ANISOU 183 CA GLU A 25 9420 6264 8792 -563 214 -48 C ATOM 184 C GLU A 25 -5.810 56.078 20.937 1.00 69.71 C ANISOU 184 C GLU A 25 10499 6800 9188 -508 321 -242 C ATOM 185 O GLU A 25 -6.330 55.033 21.347 1.00 67.90 O ANISOU 185 O GLU A 25 10371 6703 8724 -453 395 -291 O ATOM 186 CB GLU A 25 -5.599 55.505 18.498 1.00 61.00 C ANISOU 186 CB GLU A 25 8701 6107 8368 -445 453 114 C ATOM 187 CG GLU A 25 -6.083 56.620 17.582 1.00 64.64 C ANISOU 187 CG GLU A 25 9002 6527 9032 -388 619 257 C ATOM 188 CD GLU A 25 -6.576 56.121 16.205 1.00 70.31 C ANISOU 188 CD GLU A 25 9452 7511 9751 -311 764 450 C ATOM 189 OE1 GLU A 25 -6.857 54.900 16.081 1.00 65.27 O ANISOU 189 OE1 GLU A 25 8795 7074 8932 -281 781 431 O ATOM 190 OE2 GLU A 25 -6.693 56.950 15.231 1.00 72.10 O ANISOU 190 OE2 GLU A 25 9512 7735 10149 -289 846 626 O ATOM 191 N GLU A 26 -6.002 57.286 21.486 1.00 76.36 N ANISOU 191 N GLU A 26 11583 7357 10073 -520 355 -346 N ATOM 192 CA GLU A 26 -7.009 57.583 22.521 1.00 75.40 C ANISOU 192 CA GLU A 26 11876 7048 9724 -436 574 -524 C ATOM 193 C GLU A 26 -8.406 57.209 22.063 1.00 75.71 C ANISOU 193 C GLU A 26 11767 7242 9759 -252 956 -429 C ATOM 194 O GLU A 26 -8.825 57.502 20.916 1.00 72.28 O ANISOU 194 O GLU A 26 10971 6924 9567 -182 1083 -241 O ATOM 195 CB GLU A 26 -7.021 59.065 22.858 1.00 80.47 C ANISOU 195 CB GLU A 26 12729 7346 10499 -459 610 -621 C ATOM 196 CG GLU A 26 -6.862 59.407 24.325 1.00 86.65 C ANISOU 196 CG GLU A 26 14111 7817 10996 -535 507 -891 C ATOM 197 CD GLU A 26 -5.411 59.316 24.767 1.00 90.11 C ANISOU 197 CD GLU A 26 14653 8168 11415 -760 -13 -948 C ATOM 198 OE1 GLU A 26 -4.698 58.382 24.286 1.00 83.32 O ANISOU 198 OE1 GLU A 26 13473 7557 10627 -821 -230 -806 O ATOM 199 OE2 GLU A 26 -4.996 60.177 25.586 1.00 89.86 O ANISOU 199 OE2 GLU A 26 15022 7799 11323 -878 -207 -1129 O ATOM 200 N LEU A 27 -9.125 56.572 22.984 1.00 74.55 N ANISOU 200 N LEU A 27 11910 7075 9342 -180 1125 -543 N ATOM 201 CA LEU A 27 -10.453 56.026 22.696 1.00 72.17 C ANISOU 201 CA LEU A 27 11455 6901 9063 -17 1466 -440 C ATOM 202 C LEU A 27 -11.340 57.164 22.175 1.00 68.46 C ANISOU 202 C LEU A 27 10838 6283 8891 99 1744 -342 C ATOM 203 O LEU A 27 -12.033 57.033 21.164 1.00 63.78 O ANISOU 203 O LEU A 27 9869 5848 8518 178 1851 -136 O ATOM 204 CB LEU A 27 -11.028 55.364 23.968 1.00 71.10 C ANISOU 204 CB LEU A 27 11722 6682 8610 40 1647 -583 C ATOM 205 CG LEU A 27 -10.300 54.132 24.515 1.00 71.16 C ANISOU 205 CG LEU A 27 11868 6839 8332 -60 1386 -642 C ATOM 206 CD1 LEU A 27 -11.133 53.463 25.601 1.00 72.79 C ANISOU 206 CD1 LEU A 27 12421 6980 8254 31 1655 -720 C ATOM 207 CD2 LEU A 27 -9.984 53.137 23.396 1.00 68.52 C ANISOU 207 CD2 LEU A 27 11067 6833 8136 -87 1223 -472 C ATOM 208 N ASP A 28 -11.269 58.285 22.882 1.00 71.96 N ANISOU 208 N ASP A 28 11600 6399 9342 97 1827 -490 N ATOM 209 CA ASP A 28 -11.740 59.581 22.405 1.00 75.64 C ANISOU 209 CA ASP A 28 11939 6663 10138 171 2013 -409 C ATOM 210 C ASP A 28 -11.514 59.901 20.959 1.00 75.71 C ANISOU 210 C ASP A 28 11459 6846 10459 148 1878 -160 C ATOM 211 O ASP A 28 -12.383 60.497 20.324 1.00 81.44 O ANISOU 211 O ASP A 28 11947 7522 11473 261 2090 13 O ATOM 212 CB ASP A 28 -11.090 60.695 23.193 1.00 75.92 C ANISOU 212 CB ASP A 28 12370 6344 10132 88 1933 -622 C ATOM 213 CG ASP A 28 -12.048 61.315 24.118 1.00 88.55 C ANISOU 213 CG ASP A 28 14346 7611 11688 225 2346 -769 C ATOM 214 OD1 ASP A 28 -13.048 60.631 24.422 1.00 93.54 O ANISOU 214 OD1 ASP A 28 14997 8305 12240 365 2665 -733 O ATOM 215 OD2 ASP A 28 -11.846 62.475 24.529 1.00102.05 O ANISOU 215 OD2 ASP A 28 16326 8978 13471 203 2386 -910 O ATOM 216 N CYS A 29 -10.346 59.535 20.442 1.00 72.56 N ANISOU 216 N CYS A 29 10919 6629 10021 5 1539 -123 N ATOM 217 CA CYS A 29 -9.871 60.102 19.189 1.00 70.34 C ANISOU 217 CA CYS A 29 10281 6434 10011 -37 1420 87 C ATOM 218 C CYS A 29 -10.431 59.297 18.056 1.00 67.00 C ANISOU 218 C CYS A 29 9510 6331 9616 24 1460 311 C ATOM 219 O CYS A 29 -10.418 59.748 16.910 1.00 67.29 O ANISOU 219 O CYS A 29 9268 6450 9850 27 1439 528 O ATOM 220 CB CYS A 29 -8.335 60.116 19.145 1.00 73.96 C ANISOU 220 CB CYS A 29 10734 6899 10466 -211 1085 48 C ATOM 221 SG CYS A 29 -7.581 60.999 20.553 1.00 83.86 S ANISOU 221 SG CYS A 29 12450 7747 11665 -335 913 -232 S ATOM 222 N VAL A 30 -10.922 58.095 18.360 1.00 59.50 N ANISOU 222 N VAL A 30 8599 5551 8457 63 1505 265 N ATOM 223 CA VAL A 30 -11.436 57.216 17.310 1.00 55.79 C ANISOU 223 CA VAL A 30 7838 5370 7988 98 1493 452 C ATOM 224 C VAL A 30 -12.892 57.600 16.982 1.00 51.98 C ANISOU 224 C VAL A 30 7199 4825 7724 231 1717 616 C ATOM 225 O VAL A 30 -13.659 57.920 17.876 1.00 51.79 O ANISOU 225 O VAL A 30 7328 4589 7762 325 1953 536 O ATOM 226 CB VAL A 30 -11.405 55.753 17.809 1.00 56.19 C ANISOU 226 CB VAL A 30 7983 5594 7774 81 1442 342 C ATOM 227 CG1 VAL A 30 -11.541 54.791 16.656 1.00 52.22 C ANISOU 227 CG1 VAL A 30 7221 5382 7239 69 1349 494 C ATOM 228 CG2 VAL A 30 -10.145 55.472 18.628 1.00 60.12 C ANISOU 228 CG2 VAL A 30 8708 6046 8088 -32 1249 154 C ATOM 229 N ASP A 31 -13.282 57.539 15.719 1.00 48.20 N ANISOU 229 N ASP A 31 6430 4515 7370 238 1646 857 N ATOM 230 CA ASP A 31 -14.677 57.601 15.381 1.00 49.17 C ANISOU 230 CA ASP A 31 6360 4610 7715 343 1778 1047 C ATOM 231 C ASP A 31 -15.470 56.508 16.172 1.00 49.41 C ANISOU 231 C ASP A 31 6453 4668 7654 403 1906 958 C ATOM 232 O ASP A 31 -15.104 55.329 16.139 1.00 48.44 O ANISOU 232 O ASP A 31 6365 4753 7287 339 1770 881 O ATOM 233 CB ASP A 31 -14.823 57.428 13.873 1.00 52.08 C ANISOU 233 CB ASP A 31 6467 5196 8125 299 1578 1307 C ATOM 234 CG ASP A 31 -16.193 56.856 13.456 1.00 63.44 C ANISOU 234 CG ASP A 31 7693 6697 9714 357 1574 1499 C ATOM 235 OD1 ASP A 31 -16.981 56.387 14.317 1.00 77.39 O ANISOU 235 OD1 ASP A 31 9479 8372 11555 433 1747 1432 O ATOM 236 OD2 ASP A 31 -16.513 56.829 12.251 1.00 68.23 O ANISOU 236 OD2 ASP A 31 8118 7436 10370 318 1384 1735 O ATOM 237 N SER A 32 -16.565 56.899 16.846 1.00 50.36 N ANISOU 237 N SER A 32 6570 4560 8005 532 2196 990 N ATOM 238 CA SER A 32 -17.406 55.949 17.640 1.00 51.51 C ANISOU 238 CA SER A 32 6760 4688 8123 606 2389 943 C ATOM 239 C SER A 32 -17.691 54.594 17.029 1.00 46.57 C ANISOU 239 C SER A 32 5946 4333 7414 550 2193 1036 C ATOM 240 O SER A 32 -17.432 53.585 17.633 1.00 46.88 O ANISOU 240 O SER A 32 6140 4463 7212 521 2188 889 O ATOM 241 CB SER A 32 -18.743 56.607 17.964 1.00 52.71 C ANISOU 241 CB SER A 32 6775 4568 8684 767 2736 1095 C ATOM 242 OG SER A 32 -18.561 57.238 19.176 1.00 53.22 O ANISOU 242 OG SER A 32 7196 4361 8665 836 3034 877 O ATOM 243 N ALA A 33 -18.241 54.594 15.818 1.00 49.12 N ANISOU 243 N ALA A 33 5955 4766 7943 528 2011 1290 N ATOM 244 CA ALA A 33 -18.631 53.373 15.085 1.00 50.09 C ANISOU 244 CA ALA A 33 5903 5113 8015 460 1782 1395 C ATOM 245 C ALA A 33 -17.422 52.517 14.788 1.00 47.53 C ANISOU 245 C ALA A 33 5745 5031 7283 338 1556 1221 C ATOM 246 O ALA A 33 -17.508 51.292 14.801 1.00 46.88 O ANISOU 246 O ALA A 33 5663 5083 7065 296 1468 1170 O ATOM 247 CB ALA A 33 -19.274 53.761 13.776 1.00 52.22 C ANISOU 247 CB ALA A 33 5882 5429 8528 433 1565 1694 C ATOM 248 N VAL A 34 -16.298 53.170 14.489 1.00 44.08 N ANISOU 248 N VAL A 34 5423 4626 6699 284 1475 1151 N ATOM 249 CA VAL A 34 -15.088 52.433 14.276 1.00 39.92 C ANISOU 249 CA VAL A 34 5028 4283 5857 185 1316 1004 C ATOM 250 C VAL A 34 -14.655 51.853 15.642 1.00 38.72 C ANISOU 250 C VAL A 34 5101 4070 5542 196 1427 768 C ATOM 251 O VAL A 34 -14.184 50.731 15.726 1.00 34.11 O ANISOU 251 O VAL A 34 4574 3625 4761 143 1330 670 O ATOM 252 CB VAL A 34 -13.984 53.343 13.727 1.00 39.88 C ANISOU 252 CB VAL A 34 5061 4281 5812 132 1242 1015 C ATOM 253 CG1 VAL A 34 -12.622 52.683 13.915 1.00 35.22 C ANISOU 253 CG1 VAL A 34 4608 3794 4979 52 1154 841 C ATOM 254 CG2 VAL A 34 -14.261 53.714 12.248 1.00 40.14 C ANISOU 254 CG2 VAL A 34 4926 4418 5909 103 1103 1261 C ATOM 255 N LEU A 35 -14.770 52.642 16.706 1.00 37.51 N ANISOU 255 N LEU A 35 5106 3691 5454 261 1625 678 N ATOM 256 CA LEU A 35 -14.356 52.126 17.998 1.00 37.47 C ANISOU 256 CA LEU A 35 5380 3619 5238 258 1699 467 C ATOM 257 C LEU A 35 -15.225 50.874 18.389 1.00 35.39 C ANISOU 257 C LEU A 35 5080 3420 4945 301 1792 483 C ATOM 258 O LEU A 35 -14.778 49.930 19.065 1.00 32.60 O ANISOU 258 O LEU A 35 4891 3124 4372 267 1754 356 O ATOM 259 CB LEU A 35 -14.524 53.225 19.037 1.00 40.38 C ANISOU 259 CB LEU A 35 5985 3699 5657 326 1924 369 C ATOM 260 CG LEU A 35 -14.101 52.811 20.438 1.00 44.23 C ANISOU 260 CG LEU A 35 6854 4086 5867 312 1984 150 C ATOM 261 CD1 LEU A 35 -12.643 52.320 20.361 1.00 44.40 C ANISOU 261 CD1 LEU A 35 6948 4247 5676 170 1655 48 C ATOM 262 CD2 LEU A 35 -14.286 53.954 21.444 1.00 46.92 C ANISOU 262 CD2 LEU A 35 7514 4106 6209 375 2219 26 C ATOM 263 N VAL A 36 -16.465 50.870 17.933 1.00 35.03 N ANISOU 263 N VAL A 36 4794 3351 5163 371 1893 669 N ATOM 264 CA VAL A 36 -17.331 49.702 18.170 1.00 34.63 C ANISOU 264 CA VAL A 36 4646 3346 5164 400 1960 725 C ATOM 265 C VAL A 36 -16.744 48.429 17.503 1.00 32.04 C ANISOU 265 C VAL A 36 4264 3267 4643 288 1676 688 C ATOM 266 O VAL A 36 -16.656 47.372 18.154 1.00 29.99 O ANISOU 266 O VAL A 36 4104 3044 4246 278 1701 598 O ATOM 267 CB VAL A 36 -18.819 49.986 17.839 1.00 34.40 C ANISOU 267 CB VAL A 36 4322 3200 5550 490 2107 968 C ATOM 268 CG1 VAL A 36 -19.655 48.688 17.855 1.00 35.16 C ANISOU 268 CG1 VAL A 36 4249 3355 5756 486 2097 1060 C ATOM 269 CG2 VAL A 36 -19.350 50.911 18.899 1.00 37.09 C ANISOU 269 CG2 VAL A 36 4797 3253 6044 628 2506 948 C ATOM 270 N ASP A 37 -16.365 48.556 16.247 1.00 31.74 N ANISOU 270 N ASP A 37 4094 3373 4593 214 1440 760 N ATOM 271 CA ASP A 37 -15.918 47.424 15.437 1.00 31.89 C ANISOU 271 CA ASP A 37 4074 3595 4447 119 1209 734 C ATOM 272 C ASP A 37 -14.587 46.964 15.919 1.00 27.44 C ANISOU 272 C ASP A 37 3706 3091 3629 73 1169 543 C ATOM 273 O ASP A 37 -14.333 45.765 15.992 1.00 27.71 O ANISOU 273 O ASP A 37 3766 3216 3547 35 1099 470 O ATOM 274 CB ASP A 37 -15.884 47.820 13.969 1.00 34.98 C ANISOU 274 CB ASP A 37 4342 4092 4855 61 1011 870 C ATOM 275 CG ASP A 37 -17.287 47.925 13.386 1.00 43.13 C ANISOU 275 CG ASP A 37 5147 5081 6159 75 944 1095 C ATOM 276 OD1 ASP A 37 -18.244 47.292 13.911 1.00 52.43 O ANISOU 276 OD1 ASP A 37 6219 6188 7516 109 1013 1142 O ATOM 277 OD2 ASP A 37 -17.478 48.644 12.410 1.00 49.29 O ANISOU 277 OD2 ASP A 37 5837 5880 7011 50 815 1255 O ATOM 278 N VAL A 38 -13.742 47.929 16.286 1.00 28.07 N ANISOU 278 N VAL A 38 3910 3093 3663 73 1202 475 N ATOM 279 CA VAL A 38 -12.445 47.620 16.870 1.00 25.97 C ANISOU 279 CA VAL A 38 3809 2837 3222 20 1131 323 C ATOM 280 C VAL A 38 -12.626 46.742 18.100 1.00 25.60 C ANISOU 280 C VAL A 38 3917 2740 3069 41 1200 223 C ATOM 281 O VAL A 38 -12.028 45.673 18.174 1.00 25.22 O ANISOU 281 O VAL A 38 3887 2782 2912 -4 1095 164 O ATOM 282 CB VAL A 38 -11.648 48.872 17.183 1.00 27.76 C ANISOU 282 CB VAL A 38 4139 2936 3471 3 1127 281 C ATOM 283 CG1 VAL A 38 -10.536 48.505 18.155 1.00 28.41 C ANISOU 283 CG1 VAL A 38 4413 2970 3412 -54 1027 135 C ATOM 284 CG2 VAL A 38 -11.060 49.478 15.893 1.00 26.58 C ANISOU 284 CG2 VAL A 38 3839 2867 3393 -39 1036 385 C ATOM 285 N SER A 39 -13.493 47.150 19.039 1.00 27.10 N ANISOU 285 N SER A 39 4221 2773 3302 120 1405 222 N ATOM 286 CA SER A 39 -13.711 46.434 20.279 1.00 27.30 C ANISOU 286 CA SER A 39 4450 2726 3195 149 1520 146 C ATOM 287 C SER A 39 -14.300 45.055 19.977 1.00 26.22 C ANISOU 287 C SER A 39 4149 2710 3103 149 1504 212 C ATOM 288 O SER A 39 -14.003 44.024 20.654 1.00 25.81 O ANISOU 288 O SER A 39 4213 2681 2913 129 1478 153 O ATOM 289 CB SER A 39 -14.652 47.281 21.175 1.00 32.30 C ANISOU 289 CB SER A 39 5242 3139 3892 256 1829 154 C ATOM 290 OG SER A 39 -14.980 46.460 22.345 1.00 35.34 O ANISOU 290 OG SER A 39 5847 3457 4123 294 1989 107 O ATOM 291 N LYS A 40 -15.132 44.995 18.938 1.00 25.28 N ANISOU 291 N LYS A 40 3761 2656 3190 159 1485 346 N ATOM 292 CA LYS A 40 -15.699 43.733 18.615 1.00 26.42 C ANISOU 292 CA LYS A 40 3756 2883 3399 138 1430 401 C ATOM 293 C LYS A 40 -14.561 42.739 18.196 1.00 24.36 C ANISOU 293 C LYS A 40 3529 2770 2957 49 1212 296 C ATOM 294 O LYS A 40 -14.498 41.589 18.650 1.00 24.77 O ANISOU 294 O LYS A 40 3614 2841 2956 36 1200 258 O ATOM 295 CB LYS A 40 -16.672 43.882 17.497 1.00 27.96 C ANISOU 295 CB LYS A 40 3683 3109 3832 131 1357 564 C ATOM 296 CG LYS A 40 -16.882 42.572 16.769 1.00 31.58 C ANISOU 296 CG LYS A 40 4015 3681 4302 56 1166 582 C ATOM 297 CD LYS A 40 -17.966 42.833 15.739 1.00 39.85 C ANISOU 297 CD LYS A 40 4821 4721 5597 33 1045 767 C ATOM 298 CE LYS A 40 -18.317 41.511 15.074 1.00 45.27 C ANISOU 298 CE LYS A 40 5414 5478 6308 -57 830 779 C ATOM 299 NZ LYS A 40 -19.666 41.513 14.466 1.00 48.85 N ANISOU 299 NZ LYS A 40 5610 5860 7088 -86 702 992 N ATOM 300 N ILE A 41 -13.627 43.207 17.378 1.00 23.71 N ANISOU 300 N ILE A 41 3437 2768 2804 -1 1073 261 N ATOM 301 CA ILE A 41 -12.567 42.333 16.911 1.00 21.55 C ANISOU 301 CA ILE A 41 3170 2600 2417 -65 931 182 C ATOM 302 C ILE A 41 -11.607 42.024 18.051 1.00 21.40 C ANISOU 302 C ILE A 41 3313 2525 2293 -73 921 87 C ATOM 303 O ILE A 41 -11.206 40.889 18.185 1.00 21.48 O ANISOU 303 O ILE A 41 3321 2571 2268 -96 862 47 O ATOM 304 CB ILE A 41 -11.838 42.970 15.747 1.00 22.27 C ANISOU 304 CB ILE A 41 3211 2764 2485 -102 850 199 C ATOM 305 CG1 ILE A 41 -12.824 43.024 14.557 1.00 22.81 C ANISOU 305 CG1 ILE A 41 3160 2897 2610 -116 795 307 C ATOM 306 CG2 ILE A 41 -10.573 42.114 15.346 1.00 22.35 C ANISOU 306 CG2 ILE A 41 3235 2843 2415 -147 778 119 C ATOM 307 CD1 ILE A 41 -12.258 44.022 13.556 1.00 24.50 C ANISOU 307 CD1 ILE A 41 3366 3154 2789 -136 762 365 C ATOM 308 N ILE A 42 -11.270 42.987 18.916 1.00 21.35 N ANISOU 308 N ILE A 42 3462 2409 2240 -60 956 55 N ATOM 309 CA ILE A 42 -10.359 42.645 20.007 1.00 22.23 C ANISOU 309 CA ILE A 42 3758 2456 2234 -93 870 -19 C ATOM 310 C ILE A 42 -11.041 41.592 20.893 1.00 22.44 C ANISOU 310 C ILE A 42 3878 2455 2191 -60 957 -14 C ATOM 311 O ILE A 42 -10.402 40.603 21.262 1.00 24.25 O ANISOU 311 O ILE A 42 4138 2704 2371 -95 847 -33 O ATOM 312 CB ILE A 42 -10.036 43.830 20.912 1.00 23.96 C ANISOU 312 CB ILE A 42 4206 2523 2374 -101 869 -70 C ATOM 313 CG1 ILE A 42 -9.235 44.878 20.159 1.00 23.75 C ANISOU 313 CG1 ILE A 42 4082 2492 2450 -144 771 -61 C ATOM 314 CG2 ILE A 42 -9.332 43.315 22.187 1.00 24.98 C ANISOU 314 CG2 ILE A 42 4587 2569 2336 -147 741 -129 C ATOM 315 CD1 ILE A 42 -9.062 46.212 20.878 1.00 26.49 C ANISOU 315 CD1 ILE A 42 4639 2661 2763 -157 770 -114 C ATOM 316 N THR A 43 -12.331 41.754 21.187 1.00 23.10 N ANISOU 316 N THR A 43 3976 2484 2317 11 1166 38 N ATOM 317 CA THR A 43 -13.073 40.752 22.042 1.00 23.61 C ANISOU 317 CA THR A 43 4115 2503 2352 52 1303 77 C ATOM 318 C THR A 43 -13.058 39.343 21.368 1.00 23.28 C ANISOU 318 C THR A 43 3865 2575 2407 14 1191 105 C ATOM 319 O THR A 43 -12.788 38.357 22.018 1.00 24.37 O ANISOU 319 O THR A 43 4082 2699 2479 2 1162 102 O ATOM 320 CB THR A 43 -14.508 41.188 22.216 1.00 23.45 C ANISOU 320 CB THR A 43 4049 2390 2472 143 1581 169 C ATOM 321 OG1 THR A 43 -14.506 42.446 22.835 1.00 25.37 O ANISOU 321 OG1 THR A 43 4511 2499 2628 186 1718 125 O ATOM 322 CG2 THR A 43 -15.262 40.259 22.974 1.00 24.31 C ANISOU 322 CG2 THR A 43 4196 2439 2600 188 1756 238 C ATOM 323 N LEU A 44 -13.317 39.238 20.055 1.00 23.33 N ANISOU 323 N LEU A 44 3635 2675 2553 -11 1114 129 N ATOM 324 CA LEU A 44 -13.245 37.915 19.393 1.00 21.44 C ANISOU 324 CA LEU A 44 3259 2510 2377 -56 1003 120 C ATOM 325 C LEU A 44 -11.825 37.354 19.559 1.00 22.21 C ANISOU 325 C LEU A 44 3429 2633 2377 -95 874 38 C ATOM 326 O LEU A 44 -11.627 36.181 19.906 1.00 22.52 O ANISOU 326 O LEU A 44 3466 2657 2433 -107 842 33 O ATOM 327 CB LEU A 44 -13.654 37.990 17.905 1.00 22.29 C ANISOU 327 CB LEU A 44 3191 2698 2579 -93 909 140 C ATOM 328 CG LEU A 44 -15.124 38.477 17.768 1.00 24.82 C ANISOU 328 CG LEU A 44 3384 2966 3081 -62 991 269 C ATOM 329 CD1 LEU A 44 -15.545 38.848 16.342 1.00 25.50 C ANISOU 329 CD1 LEU A 44 3335 3116 3236 -112 842 323 C ATOM 330 CD2 LEU A 44 -16.037 37.455 18.387 1.00 26.26 C ANISOU 330 CD2 LEU A 44 3495 3071 3410 -47 1075 340 C ATOM 331 N THR A 45 -10.798 38.195 19.340 1.00 23.07 N ANISOU 331 N THR A 45 3577 2758 2432 -116 798 -3 N ATOM 332 CA THR A 45 -9.421 37.676 19.485 1.00 21.19 C ANISOU 332 CA THR A 45 3347 2512 2191 -153 671 -40 C ATOM 333 C THR A 45 -9.136 37.193 20.883 1.00 21.63 C ANISOU 333 C THR A 45 3563 2483 2173 -157 619 -22 C ATOM 334 O THR A 45 -8.429 36.211 21.064 1.00 23.50 O ANISOU 334 O THR A 45 3761 2704 2465 -177 526 -13 O ATOM 335 CB THR A 45 -8.290 38.639 18.989 1.00 21.33 C ANISOU 335 CB THR A 45 3331 2534 2240 -182 595 -54 C ATOM 336 OG1 THR A 45 -8.213 39.818 19.799 1.00 20.84 O ANISOU 336 OG1 THR A 45 3418 2393 2107 -189 569 -51 O ATOM 337 CG2 THR A 45 -8.446 39.072 17.479 1.00 20.67 C ANISOU 337 CG2 THR A 45 3120 2540 2195 -180 655 -52 C ATOM 338 N GLN A 46 -9.671 37.864 21.892 1.00 23.69 N ANISOU 338 N GLN A 46 4030 2670 2302 -135 689 -9 N ATOM 339 CA GLN A 46 -9.445 37.425 23.256 1.00 25.35 C ANISOU 339 CA GLN A 46 4474 2791 2369 -145 639 15 C ATOM 340 C GLN A 46 -10.118 36.102 23.503 1.00 25.12 C ANISOU 340 C GLN A 46 4398 2767 2381 -116 731 74 C ATOM 341 O GLN A 46 -9.562 35.245 24.181 1.00 27.78 O ANISOU 341 O GLN A 46 4809 3064 2682 -140 620 116 O ATOM 342 CB GLN A 46 -9.901 38.505 24.232 1.00 26.50 C ANISOU 342 CB GLN A 46 4922 2830 2316 -122 742 -5 C ATOM 343 CG GLN A 46 -8.926 39.706 24.276 1.00 28.76 C ANISOU 343 CG GLN A 46 5311 3061 2556 -182 565 -67 C ATOM 344 CD GLN A 46 -9.500 40.896 25.019 1.00 32.55 C ANISOU 344 CD GLN A 46 6092 3415 2860 -151 709 -119 C ATOM 345 OE1 GLN A 46 -10.715 41.121 24.967 1.00 35.30 O ANISOU 345 OE1 GLN A 46 6436 3749 3230 -63 998 -100 O ATOM 346 NE2 GLN A 46 -8.636 41.702 25.693 1.00 34.90 N ANISOU 346 NE2 GLN A 46 6649 3592 3018 -227 506 -181 N ATOM 347 N GLU A 47 -11.277 35.907 22.933 1.00 25.57 N ANISOU 347 N GLU A 47 4310 2858 2549 -73 904 99 N ATOM 348 CA GLU A 47 -11.978 34.630 23.069 1.00 28.80 C ANISOU 348 CA GLU A 47 4630 3252 3059 -56 983 165 C ATOM 349 C GLU A 47 -11.205 33.517 22.354 1.00 28.18 C ANISOU 349 C GLU A 47 4380 3218 3110 -101 823 132 C ATOM 350 O GLU A 47 -11.031 32.391 22.872 1.00 27.70 O ANISOU 350 O GLU A 47 4326 3110 3089 -107 792 181 O ATOM 351 CB GLU A 47 -13.329 34.707 22.395 1.00 32.03 C ANISOU 351 CB GLU A 47 4858 3671 3639 -25 1136 210 C ATOM 352 CG GLU A 47 -14.411 35.260 23.235 1.00 43.67 C ANISOU 352 CG GLU A 47 6442 5050 5101 46 1393 298 C ATOM 353 CD GLU A 47 -14.574 34.455 24.538 1.00 54.42 C ANISOU 353 CD GLU A 47 7996 6317 6363 76 1522 378 C ATOM 354 OE1 GLU A 47 -14.954 33.269 24.467 1.00 62.40 O ANISOU 354 OE1 GLU A 47 8862 7315 7533 65 1529 449 O ATOM 355 OE2 GLU A 47 -14.313 35.004 25.648 1.00 61.86 O ANISOU 355 OE2 GLU A 47 9268 7185 7053 105 1611 373 O ATOM 356 N PHE A 48 -10.723 33.843 21.153 1.00 25.00 N ANISOU 356 N PHE A 48 3837 2888 2774 -126 746 56 N ATOM 357 CA PHE A 48 -9.950 32.863 20.361 1.00 23.16 C ANISOU 357 CA PHE A 48 3468 2669 2661 -153 658 5 C ATOM 358 C PHE A 48 -8.643 32.502 21.139 1.00 24.33 C ANISOU 358 C PHE A 48 3667 2755 2820 -165 532 38 C ATOM 359 O PHE A 48 -8.276 31.348 21.266 1.00 25.21 O ANISOU 359 O PHE A 48 3715 2814 3049 -166 495 61 O ATOM 360 CB PHE A 48 -9.612 33.512 19.052 1.00 21.11 C ANISOU 360 CB PHE A 48 3127 2483 2412 -167 647 -69 C ATOM 361 CG PHE A 48 -8.765 32.665 18.137 1.00 22.46 C ANISOU 361 CG PHE A 48 3206 2647 2682 -178 629 -137 C ATOM 362 CD1 PHE A 48 -7.354 32.618 18.302 1.00 20.69 C ANISOU 362 CD1 PHE A 48 2942 2376 2541 -173 585 -126 C ATOM 363 CD2 PHE A 48 -9.368 31.988 17.012 1.00 20.80 C ANISOU 363 CD2 PHE A 48 2954 2452 2496 -198 659 -211 C ATOM 364 CE1 PHE A 48 -6.584 31.859 17.401 1.00 21.92 C ANISOU 364 CE1 PHE A 48 3008 2495 2828 -161 646 -183 C ATOM 365 CE2 PHE A 48 -8.566 31.244 16.131 1.00 22.53 C ANISOU 365 CE2 PHE A 48 3151 2635 2774 -197 697 -299 C ATOM 366 CZ PHE A 48 -7.177 31.160 16.325 1.00 20.93 C ANISOU 366 CZ PHE A 48 2895 2378 2678 -166 728 -284 C ATOM 367 N ARG A 49 -7.956 33.481 21.679 1.00 24.72 N ANISOU 367 N ARG A 49 3825 2789 2778 -181 442 53 N ATOM 368 CA ARG A 49 -6.749 33.231 22.523 1.00 25.82 C ANISOU 368 CA ARG A 49 4016 2845 2950 -216 247 120 C ATOM 369 C ARG A 49 -7.006 32.389 23.770 1.00 29.05 C ANISOU 369 C ARG A 49 4583 3183 3274 -217 200 214 C ATOM 370 O ARG A 49 -6.169 31.562 24.116 1.00 30.55 O ANISOU 370 O ARG A 49 4714 3303 3589 -238 52 291 O ATOM 371 CB ARG A 49 -6.110 34.567 22.934 1.00 26.00 C ANISOU 371 CB ARG A 49 4163 2838 2876 -257 115 118 C ATOM 372 CG ARG A 49 -4.740 34.376 23.587 1.00 27.45 C ANISOU 372 CG ARG A 49 4342 2919 3169 -319 -161 206 C ATOM 373 CD ARG A 49 -3.653 34.095 22.522 1.00 27.32 C ANISOU 373 CD ARG A 49 4007 2892 3480 -315 -175 221 C ATOM 374 NE ARG A 49 -3.452 35.279 21.633 1.00 26.02 N ANISOU 374 NE ARG A 49 3765 2774 3349 -318 -101 164 N ATOM 375 CZ ARG A 49 -2.705 36.331 21.951 1.00 29.62 C ANISOU 375 CZ ARG A 49 4250 3162 3844 -380 -275 200 C ATOM 376 NH1 ARG A 49 -1.993 36.284 23.103 1.00 32.34 N ANISOU 376 NH1 ARG A 49 4700 3383 4205 -456 -578 290 N ATOM 377 NH2 ARG A 49 -2.569 37.398 21.125 1.00 28.09 N ANISOU 377 NH2 ARG A 49 3976 3000 3698 -379 -187 165 N ATOM 378 N ARG A 50 -8.177 32.529 24.414 1.00 30.65 N ANISOU 378 N ARG A 50 4967 3383 3296 -188 352 232 N ATOM 379 CA ARG A 50 -8.494 31.697 25.576 1.00 35.61 C ANISOU 379 CA ARG A 50 5769 3937 3824 -180 361 343 C ATOM 380 C ARG A 50 -8.600 30.222 25.168 1.00 32.93 C ANISOU 380 C ARG A 50 5210 3584 3720 -166 390 387 C ATOM 381 O ARG A 50 -8.164 29.343 25.877 1.00 31.57 O ANISOU 381 O ARG A 50 5081 3337 3577 -179 285 494 O ATOM 382 CB ARG A 50 -9.824 32.057 26.196 1.00 42.22 C ANISOU 382 CB ARG A 50 6803 4755 4483 -129 615 368 C ATOM 383 CG ARG A 50 -9.822 33.221 27.143 1.00 59.67 C ANISOU 383 CG ARG A 50 9374 6909 6390 -133 627 351 C ATOM 384 CD ARG A 50 -11.237 33.444 27.694 1.00 72.30 C ANISOU 384 CD ARG A 50 11138 8458 7876 -53 981 393 C ATOM 385 NE ARG A 50 -11.650 32.414 28.667 1.00 86.48 N ANISOU 385 NE ARG A 50 13091 10179 9588 -28 1093 532 N ATOM 386 CZ ARG A 50 -11.337 32.437 29.964 1.00 95.89 C ANISOU 386 CZ ARG A 50 14707 11279 10450 -45 1050 594 C ATOM 387 NH1 ARG A 50 -10.597 33.435 30.441 1.00 99.95 N ANISOU 387 NH1 ARG A 50 15527 11751 10697 -99 862 512 N ATOM 388 NH2 ARG A 50 -11.757 31.467 30.783 1.00 96.94 N ANISOU 388 NH2 ARG A 50 14978 11345 10511 -18 1178 746 N ATOM 389 N HIS A 51 -9.159 29.949 24.006 1.00 32.18 N ANISOU 389 N HIS A 51 4892 3540 3793 -148 510 305 N ATOM 390 CA HIS A 51 -9.185 28.526 23.568 1.00 31.42 C ANISOU 390 CA HIS A 51 4613 3396 3929 -146 520 318 C ATOM 391 C HIS A 51 -7.804 28.027 23.229 1.00 31.33 C ANISOU 391 C HIS A 51 4476 3339 4087 -160 372 308 C ATOM 392 O HIS A 51 -7.457 26.914 23.558 1.00 31.07 O ANISOU 392 O HIS A 51 4380 3215 4210 -156 324 385 O ATOM 393 CB HIS A 51 -10.059 28.363 22.325 1.00 32.09 C ANISOU 393 CB HIS A 51 4535 3525 4133 -147 631 214 C ATOM 394 CG HIS A 51 -11.511 28.654 22.557 1.00 30.88 C ANISOU 394 CG HIS A 51 4409 3378 3945 -133 779 265 C ATOM 395 ND1 HIS A 51 -12.324 27.806 23.234 1.00 31.62 N ANISOU 395 ND1 HIS A 51 4498 3388 4127 -121 878 382 N ATOM 396 CD2 HIS A 51 -12.302 29.682 22.121 1.00 30.37 C ANISOU 396 CD2 HIS A 51 4336 3372 3830 -125 858 238 C ATOM 397 CE1 HIS A 51 -13.562 28.307 23.287 1.00 31.22 C ANISOU 397 CE1 HIS A 51 4429 3334 4098 -100 1034 436 C ATOM 398 NE2 HIS A 51 -13.557 29.463 22.620 1.00 30.63 N ANISOU 398 NE2 HIS A 51 4350 3346 3943 -102 1014 349 N ATOM 399 N TYR A 52 -7.009 28.840 22.525 1.00 28.61 N ANISOU 399 N TYR A 52 4069 3041 3762 -168 323 230 N ATOM 400 CA TYR A 52 -5.664 28.425 22.248 1.00 29.23 C ANISOU 400 CA TYR A 52 3996 3045 4065 -168 223 255 C ATOM 401 C TYR A 52 -4.941 28.090 23.558 1.00 30.65 C ANISOU 401 C TYR A 52 4247 3127 4271 -195 7 428 C ATOM 402 O TYR A 52 -4.335 27.024 23.664 1.00 31.68 O ANISOU 402 O TYR A 52 4242 3149 4645 -182 -48 511 O ATOM 403 CB TYR A 52 -4.910 29.505 21.473 1.00 29.76 C ANISOU 403 CB TYR A 52 3994 3160 4155 -175 219 190 C ATOM 404 CG TYR A 52 -3.438 29.158 21.220 1.00 30.77 C ANISOU 404 CG TYR A 52 3921 3178 4591 -166 150 255 C ATOM 405 CD1 TYR A 52 -2.479 29.467 22.183 1.00 34.07 C ANISOU 405 CD1 TYR A 52 4335 3514 5096 -209 -103 406 C ATOM 406 CD2 TYR A 52 -3.002 28.635 19.990 1.00 30.62 C ANISOU 406 CD2 TYR A 52 3733 3119 4781 -117 341 172 C ATOM 407 CE1 TYR A 52 -1.134 29.135 21.980 1.00 36.81 C ANISOU 407 CE1 TYR A 52 4438 3729 5819 -201 -176 510 C ATOM 408 CE2 TYR A 52 -1.622 28.341 19.742 1.00 32.34 C ANISOU 408 CE2 TYR A 52 3733 3201 5352 -87 346 255 C ATOM 409 CZ TYR A 52 -0.721 28.598 20.753 1.00 34.52 C ANISOU 409 CZ TYR A 52 3938 3392 5787 -129 81 439 C ATOM 410 OH TYR A 52 0.614 28.349 20.615 1.00 39.05 O ANISOU 410 OH TYR A 52 4248 3807 6783 -107 51 571 O ATOM 411 N ASP A 53 -4.982 29.002 24.514 1.00 31.94 N ANISOU 411 N ASP A 53 4639 3310 4188 -234 -124 482 N ATOM 412 CA ASP A 53 -4.271 28.889 25.769 1.00 33.54 C ANISOU 412 CA ASP A 53 4990 3416 4338 -286 -397 644 C ATOM 413 C ASP A 53 -4.748 27.730 26.612 1.00 35.73 C ANISOU 413 C ASP A 53 5365 3631 4581 -273 -390 772 C ATOM 414 O ASP A 53 -4.043 27.301 27.456 1.00 36.34 O ANISOU 414 O ASP A 53 5503 3611 4693 -312 -630 934 O ATOM 415 CB ASP A 53 -4.407 30.146 26.612 1.00 33.80 C ANISOU 415 CB ASP A 53 5348 3465 4029 -338 -514 636 C ATOM 416 CG ASP A 53 -3.546 31.287 26.133 1.00 34.90 C ANISOU 416 CG ASP A 53 5404 3607 4249 -382 -649 580 C ATOM 417 OD1 ASP A 53 -2.693 31.119 25.302 1.00 35.54 O ANISOU 417 OD1 ASP A 53 5184 3666 4654 -375 -673 587 O ATOM 418 OD2 ASP A 53 -3.738 32.379 26.605 1.00 36.71 O ANISOU 418 OD2 ASP A 53 5882 3841 4224 -421 -706 532 O ATOM 419 N SER A 54 -5.956 27.265 26.384 1.00 34.36 N ANISOU 419 N SER A 54 5200 3501 4354 -225 -131 720 N ATOM 420 CA SER A 54 -6.480 26.179 27.178 1.00 39.27 C ANISOU 420 CA SER A 54 5903 4051 4965 -211 -89 860 C ATOM 421 C SER A 54 -6.022 24.820 26.683 1.00 38.22 C ANISOU 421 C SER A 54 5487 3824 5210 -189 -102 906 C ATOM 422 O SER A 54 -6.194 23.858 27.340 1.00 41.10 O ANISOU 422 O SER A 54 5882 4102 5631 -184 -116 1051 O ATOM 423 CB SER A 54 -7.983 26.269 27.316 1.00 38.93 C ANISOU 423 CB SER A 54 5982 4054 4754 -173 192 832 C ATOM 424 OG SER A 54 -8.631 25.841 26.177 1.00 44.82 O ANISOU 424 OG SER A 54 6477 4830 5724 -147 363 718 O ATOM 425 N VAL A 55 -5.410 24.788 25.524 1.00 35.16 N ANISOU 425 N VAL A 55 4846 3436 5077 -173 -75 784 N ATOM 426 CA VAL A 55 -5.017 23.582 24.845 1.00 34.30 C ANISOU 426 CA VAL A 55 4484 3215 5332 -138 -13 773 C ATOM 427 C VAL A 55 -3.520 23.551 24.754 1.00 35.06 C ANISOU 427 C VAL A 55 4404 3214 5704 -137 -181 854 C ATOM 428 O VAL A 55 -2.940 22.534 24.892 1.00 35.51 O ANISOU 428 O VAL A 55 4304 3124 6063 -114 -229 968 O ATOM 429 CB VAL A 55 -5.611 23.558 23.430 1.00 34.07 C ANISOU 429 CB VAL A 55 4345 3237 5361 -113 216 545 C ATOM 430 CG1 VAL A 55 -4.977 22.543 22.523 1.00 37.93 C ANISOU 430 CG1 VAL A 55 4622 3591 6197 -74 306 474 C ATOM 431 CG2 VAL A 55 -7.066 23.261 23.517 1.00 35.97 C ANISOU 431 CG2 VAL A 55 4673 3514 5482 -122 345 517 C ATOM 432 N TYR A 56 -2.900 24.691 24.514 1.00 34.88 N ANISOU 432 N TYR A 56 4380 3253 5621 -160 -264 812 N ATOM 433 CA TYR A 56 -1.487 24.728 24.268 1.00 36.95 C ANISOU 433 CA TYR A 56 4409 3403 6227 -155 -387 900 C ATOM 434 C TYR A 56 -0.756 25.557 25.287 1.00 41.45 C ANISOU 434 C TYR A 56 5083 3953 6715 -237 -742 1065 C ATOM 435 O TYR A 56 -1.201 26.585 25.702 1.00 42.06 O ANISOU 435 O TYR A 56 5408 4136 6437 -288 -816 1012 O ATOM 436 CB TYR A 56 -1.180 25.194 22.858 1.00 34.97 C ANISOU 436 CB TYR A 56 3996 3186 6105 -110 -152 723 C ATOM 437 CG TYR A 56 -1.775 24.377 21.747 1.00 32.46 C ANISOU 437 CG TYR A 56 3624 2856 5853 -46 161 541 C ATOM 438 CD1 TYR A 56 -1.371 23.091 21.506 1.00 33.17 C ANISOU 438 CD1 TYR A 56 3547 2770 6287 10 261 572 C ATOM 439 CD2 TYR A 56 -2.714 24.906 20.917 1.00 30.38 C ANISOU 439 CD2 TYR A 56 3487 2733 5321 -48 334 341 C ATOM 440 CE1 TYR A 56 -1.904 22.360 20.496 1.00 32.63 C ANISOU 440 CE1 TYR A 56 3484 2661 6252 53 522 382 C ATOM 441 CE2 TYR A 56 -3.244 24.176 19.906 1.00 30.11 C ANISOU 441 CE2 TYR A 56 3449 2668 5322 -16 553 173 C ATOM 442 CZ TYR A 56 -2.836 22.899 19.712 1.00 31.37 C ANISOU 442 CZ TYR A 56 3484 2646 5788 31 645 181 C ATOM 443 OH TYR A 56 -3.365 22.193 18.704 1.00 32.93 O ANISOU 443 OH TYR A 56 3731 2788 5992 49 843 -11 O ATOM 444 N ARG A 57 0.379 25.071 25.715 1.00 45.07 N ANISOU 444 N ARG A 57 5352 4246 7525 -256 -982 1276 N ATOM 445 CA ARG A 57 1.165 25.777 26.699 1.00 49.59 C ANISOU 445 CA ARG A 57 6021 4761 8059 -361 -1406 1457 C ATOM 446 C ARG A 57 2.021 26.905 26.113 1.00 49.01 C ANISOU 446 C ARG A 57 5780 4678 8162 -393 -1471 1424 C ATOM 447 O ARG A 57 2.080 27.983 26.695 1.00 46.86 O ANISOU 447 O ARG A 57 5731 4444 7630 -489 -1719 1426 O ATOM 448 CB ARG A 57 2.013 24.793 27.519 1.00 57.85 C ANISOU 448 CB ARG A 57 6931 5613 9437 -389 -1722 1754 C ATOM 449 CG ARG A 57 2.048 25.197 28.972 1.00 65.76 C ANISOU 449 CG ARG A 57 8302 6599 10086 -517 -2170 1923 C ATOM 450 CD ARG A 57 2.089 23.993 29.899 1.00 75.81 C ANISOU 450 CD ARG A 57 9630 7753 11421 -527 -2361 2172 C ATOM 451 NE ARG A 57 3.220 23.087 29.621 1.00 87.77 N ANISOU 451 NE ARG A 57 10681 9059 13610 -492 -2477 2392 N ATOM 452 CZ ARG A 57 4.523 23.389 29.741 1.00 93.72 C ANISOU 452 CZ ARG A 57 11170 9651 14787 -559 -2843 2599 C ATOM 453 NH1 ARG A 57 4.929 24.605 30.129 1.00 90.40 N ANISOU 453 NH1 ARG A 57 10913 9252 14182 -685 -3180 2607 N ATOM 454 NH2 ARG A 57 5.435 22.456 29.457 1.00 96.90 N ANISOU 454 NH2 ARG A 57 11118 9841 15857 -499 -2866 2812 N ATOM 455 N ALA A 58 2.706 26.682 24.998 1.00 47.94 N ANISOU 455 N ALA A 58 5276 4470 8471 -315 -1241 1401 N ATOM 456 CA ALA A 58 3.482 27.769 24.428 1.00 48.68 C ANISOU 456 CA ALA A 58 5203 4545 8746 -340 -1259 1392 C ATOM 457 C ALA A 58 2.591 28.798 23.767 1.00 47.63 C ANISOU 457 C ALA A 58 5279 4613 8204 -330 -1015 1140 C ATOM 458 O ALA A 58 1.510 28.490 23.248 1.00 44.33 O ANISOU 458 O ALA A 58 5000 4326 7518 -267 -715 952 O ATOM 459 CB ALA A 58 4.544 27.285 23.454 1.00 50.49 C ANISOU 459 CB ALA A 58 4984 4608 9591 -249 -1035 1473 C ATOM 460 N ASP A 59 3.086 30.030 23.801 1.00 48.21 N ANISOU 460 N ASP A 59 5353 4686 8278 -403 -1180 1160 N ATOM 461 CA ASP A 59 2.471 31.137 23.151 1.00 48.05 C ANISOU 461 CA ASP A 59 5472 4817 7968 -398 -983 968 C ATOM 462 C ASP A 59 2.985 31.183 21.719 1.00 44.81 C ANISOU 462 C ASP A 59 4762 4388 7877 -307 -623 921 C ATOM 463 O ASP A 59 3.719 30.298 21.279 1.00 42.26 O ANISOU 463 O ASP A 59 4154 3929 7972 -238 -487 1014 O ATOM 464 CB ASP A 59 2.704 32.402 23.970 1.00 52.83 C ANISOU 464 CB ASP A 59 6268 5404 8403 -525 -1338 1010 C ATOM 465 CG ASP A 59 4.110 32.959 23.854 1.00 58.80 C ANISOU 465 CG ASP A 59 6714 5987 9638 -591 -1563 1186 C ATOM 466 OD1 ASP A 59 4.920 32.614 22.955 1.00 59.58 O ANISOU 466 OD1 ASP A 59 6423 5995 10219 -519 -1355 1270 O ATOM 467 OD2 ASP A 59 4.382 33.854 24.673 1.00 69.50 O ANISOU 467 OD2 ASP A 59 8241 7282 10883 -721 -1943 1237 O ATOM 468 N TYR A 60 2.528 32.177 20.980 1.00 42.14 N ANISOU 468 N TYR A 60 4515 4176 7320 -298 -434 777 N ATOM 469 CA TYR A 60 2.844 32.276 19.541 1.00 43.87 C ANISOU 469 CA TYR A 60 4547 4400 7723 -209 -43 714 C ATOM 470 C TYR A 60 4.295 32.743 19.301 1.00 47.77 C ANISOU 470 C TYR A 60 4699 4716 8736 -220 -81 907 C ATOM 471 O TYR A 60 4.785 32.750 18.164 1.00 51.16 O ANISOU 471 O TYR A 60 4944 5098 9396 -135 279 905 O ATOM 472 CB TYR A 60 1.973 33.382 18.911 1.00 40.02 C ANISOU 472 CB TYR A 60 4264 4090 6851 -215 105 552 C ATOM 473 CG TYR A 60 0.465 33.233 18.975 1.00 38.50 C ANISOU 473 CG TYR A 60 4368 4068 6192 -207 168 380 C ATOM 474 CD1 TYR A 60 -0.142 31.974 19.220 1.00 36.44 C ANISOU 474 CD1 TYR A 60 4172 3811 5864 -173 209 334 C ATOM 475 CD2 TYR A 60 -0.375 34.351 18.733 1.00 33.21 C ANISOU 475 CD2 TYR A 60 3880 3533 5204 -230 205 281 C ATOM 476 CE1 TYR A 60 -1.523 31.826 19.210 1.00 33.49 C ANISOU 476 CE1 TYR A 60 4014 3566 5144 -168 280 206 C ATOM 477 CE2 TYR A 60 -1.763 34.209 18.743 1.00 31.67 C ANISOU 477 CE2 TYR A 60 3897 3467 4671 -217 277 160 C ATOM 478 CZ TYR A 60 -2.336 32.964 18.988 1.00 31.53 C ANISOU 478 CZ TYR A 60 3920 3446 4614 -190 309 127 C ATOM 479 OH TYR A 60 -3.718 32.807 19.009 1.00 27.59 O ANISOU 479 OH TYR A 60 3583 3045 3853 -183 375 39 O ATOM 480 N GLY A 61 4.937 33.197 20.376 1.00 50.51 N ANISOU 480 N GLY A 61 4991 4952 9248 -335 -521 1078 N ATOM 481 CA GLY A 61 6.204 33.902 20.317 1.00 55.43 C ANISOU 481 CA GLY A 61 5301 5399 10363 -388 -663 1281 C ATOM 482 C GLY A 61 7.442 33.179 19.855 1.00 59.98 C ANISOU 482 C GLY A 61 5421 5748 11619 -314 -509 1494 C ATOM 483 O GLY A 61 8.450 33.813 19.649 1.00 66.91 O ANISOU 483 O GLY A 61 5997 6471 12955 -346 -556 1675 O ATOM 484 N PRO A 62 7.420 31.844 19.749 1.00 62.94 N ANISOU 484 N PRO A 62 5718 6070 12128 -216 -332 1499 N ATOM 485 CA PRO A 62 8.582 31.323 19.033 1.00 65.07 C ANISOU 485 CA PRO A 62 5545 6106 13073 -110 -35 1680 C ATOM 486 C PRO A 62 8.432 31.256 17.501 1.00 65.14 C ANISOU 486 C PRO A 62 5561 6159 13030 44 629 1515 C ATOM 487 O PRO A 62 9.437 31.212 16.830 1.00 70.82 O ANISOU 487 O PRO A 62 5941 6681 14285 129 934 1669 O ATOM 488 CB PRO A 62 8.780 29.932 19.648 1.00 66.45 C ANISOU 488 CB PRO A 62 5604 6144 13500 -74 -154 1793 C ATOM 489 CG PRO A 62 8.131 30.004 20.991 1.00 64.90 C ANISOU 489 CG PRO A 62 5715 6058 12888 -216 -697 1787 C ATOM 490 CD PRO A 62 6.909 30.857 20.715 1.00 63.27 C ANISOU 490 CD PRO A 62 5928 6128 11984 -241 -584 1499 C ATOM 491 N ALA A 63 7.225 31.266 16.939 1.00 60.82 N ANISOU 491 N ALA A 63 5399 5843 11868 77 853 1227 N ATOM 492 CA ALA A 63 7.081 31.304 15.470 1.00 63.58 C ANISOU 492 CA ALA A 63 5830 6231 12097 198 1426 1074 C ATOM 493 C ALA A 63 7.075 32.746 14.889 1.00 70.13 C ANISOU 493 C ALA A 63 6715 7165 12766 159 1506 1068 C ATOM 494 O ALA A 63 7.616 33.018 13.816 1.00 75.07 O ANISOU 494 O ALA A 63 7241 7716 13567 247 1938 1103 O ATOM 495 CB ALA A 63 5.837 30.529 15.053 1.00 61.87 C ANISOU 495 CB ALA A 63 5982 6174 11353 241 1597 792 C ATOM 496 N LEU A 64 6.477 33.665 15.644 1.00 68.48 N ANISOU 496 N LEU A 64 6677 7106 12234 30 1101 1036 N ATOM 497 CA LEU A 64 6.202 35.033 15.238 1.00 67.91 C ANISOU 497 CA LEU A 64 6720 7154 11929 -20 1116 1000 C ATOM 498 C LEU A 64 7.345 36.009 15.510 1.00 74.09 C ANISOU 498 C LEU A 64 7182 7767 13202 -91 943 1246 C ATOM 499 O LEU A 64 7.311 37.136 15.033 1.00 72.28 O ANISOU 499 O LEU A 64 6986 7590 12888 -118 1021 1252 O ATOM 500 CB LEU A 64 4.989 35.551 16.009 1.00 60.91 C ANISOU 500 CB LEU A 64 6172 6468 10503 -119 776 849 C ATOM 501 CG LEU A 64 3.625 35.637 15.341 1.00 57.75 C ANISOU 501 CG LEU A 64 6116 6293 9533 -86 968 616 C ATOM 502 CD1 LEU A 64 3.460 34.775 14.096 1.00 55.06 C ANISOU 502 CD1 LEU A 64 5838 5967 9115 30 1412 504 C ATOM 503 CD2 LEU A 64 2.646 35.288 16.428 1.00 53.15 C ANISOU 503 CD2 LEU A 64 5754 5806 8634 -146 659 523 C ATOM 504 N LYS A 65 8.319 35.619 16.323 1.00 77.25 N ANISOU 504 N LYS A 65 7270 7955 14127 -137 659 1464 N ATOM 505 CA LYS A 65 9.530 36.406 16.408 1.00 78.91 C ANISOU 505 CA LYS A 65 7101 7951 14932 -198 532 1733 C ATOM 506 C LYS A 65 10.046 36.676 14.996 1.00 79.61 C ANISOU 506 C LYS A 65 7010 7976 15264 -67 1142 1792 C ATOM 507 O LYS A 65 10.674 37.678 14.787 1.00 82.66 O ANISOU 507 O LYS A 65 7190 8263 15955 -115 1137 1953 O ATOM 508 CB LYS A 65 10.605 35.709 17.246 1.00 84.65 C ANISOU 508 CB LYS A 65 7447 8414 16303 -240 211 2003 C ATOM 509 CG LYS A 65 11.113 34.378 16.688 1.00 83.95 C ANISOU 509 CG LYS A 65 7110 8176 16611 -73 631 2077 C ATOM 510 CD LYS A 65 12.307 33.818 17.470 1.00 87.01 C ANISOU 510 CD LYS A 65 7029 8257 17772 -115 301 2416 C ATOM 511 CE LYS A 65 11.903 33.370 18.875 1.00 87.38 C ANISOU 511 CE LYS A 65 7271 8350 17579 -249 -341 2414 C ATOM 512 NZ LYS A 65 12.481 32.048 19.291 1.00 86.38 N ANISOU 512 NZ LYS A 65 6866 8018 17937 -191 -408 2607 N ATOM 513 N ASN A 66 9.760 35.805 14.029 1.00 79.88 N ANISOU 513 N ASN A 66 7158 8054 15139 92 1671 1659 N ATOM 514 CA ASN A 66 10.227 36.019 12.654 1.00 82.39 C ANISOU 514 CA ASN A 66 7393 8301 15610 225 2303 1704 C ATOM 515 C ASN A 66 9.146 36.452 11.687 1.00 76.20 C ANISOU 515 C ASN A 66 7063 7771 14118 261 2590 1454 C ATOM 516 O ASN A 66 9.242 36.198 10.490 1.00 75.14 O ANISOU 516 O ASN A 66 7034 7614 13904 392 3153 1406 O ATOM 517 CB ASN A 66 10.888 34.766 12.105 1.00 93.42 C ANISOU 517 CB ASN A 66 8603 9491 17401 392 2774 1761 C ATOM 518 CG ASN A 66 11.618 33.976 13.173 1.00106.80 C ANISOU 518 CG ASN A 66 9928 10970 19681 360 2422 1961 C ATOM 519 OD1 ASN A 66 12.194 34.557 14.098 1.00113.43 O ANISOU 519 OD1 ASN A 66 10489 11709 20903 224 1921 2183 O ATOM 520 ND2 ASN A 66 11.601 32.641 13.053 1.00112.33 N ANISOU 520 ND2 ASN A 66 10639 11582 20461 476 2655 1891 N ATOM 521 N TRP A 67 8.117 37.105 12.217 1.00 74.16 N ANISOU 521 N TRP A 67 7089 7737 13352 145 2199 1306 N ATOM 522 CA TRP A 67 6.987 37.591 11.435 1.00 67.77 C ANISOU 522 CA TRP A 67 6686 7168 11897 154 2359 1099 C ATOM 523 C TRP A 67 7.454 38.364 10.250 1.00 69.81 C ANISOU 523 C TRP A 67 6910 7386 12227 218 2796 1203 C ATOM 524 O TRP A 67 6.852 38.313 9.176 1.00 72.01 O ANISOU 524 O TRP A 67 7506 7787 12067 285 3138 1067 O ATOM 525 CB TRP A 67 6.113 38.481 12.291 1.00 60.75 C ANISOU 525 CB TRP A 67 5973 6442 10668 19 1879 1021 C ATOM 526 CG TRP A 67 6.678 39.864 12.549 1.00 58.13 C ANISOU 526 CG TRP A 67 5457 6032 10599 -72 1696 1195 C ATOM 527 CD1 TRP A 67 7.510 40.252 13.593 1.00 55.81 C ANISOU 527 CD1 TRP A 67 4884 5560 10762 -180 1296 1370 C ATOM 528 CD2 TRP A 67 6.412 41.105 11.783 1.00 54.28 C ANISOU 528 CD2 TRP A 67 5070 5625 9930 -82 1853 1215 C ATOM 529 NE1 TRP A 67 7.772 41.590 13.521 1.00 57.39 N ANISOU 529 NE1 TRP A 67 5007 5714 11083 -257 1205 1475 N ATOM 530 CE2 TRP A 67 7.144 42.167 12.469 1.00 54.92 C ANISOU 530 CE2 TRP A 67 4901 5552 10415 -196 1542 1396 C ATOM 531 CE3 TRP A 67 5.669 41.416 10.661 1.00 52.80 C ANISOU 531 CE3 TRP A 67 5154 5599 9307 -21 2170 1118 C ATOM 532 CZ2 TRP A 67 7.146 43.477 12.014 1.00 53.94 C ANISOU 532 CZ2 TRP A 67 4775 5431 10289 -234 1599 1475 C ATOM 533 CZ3 TRP A 67 5.658 42.735 10.216 1.00 50.88 C ANISOU 533 CZ3 TRP A 67 4916 5375 9043 -57 2214 1215 C ATOM 534 CH2 TRP A 67 6.378 43.748 10.879 1.00 53.76 C ANISOU 534 CH2 TRP A 67 5015 5585 9828 -155 1953 1388 C ATOM 535 N LYS A 68 8.535 39.106 10.442 1.00 75.11 N ANISOU 535 N LYS A 68 7207 7873 13460 186 2768 1462 N ATOM 536 CA LYS A 68 9.180 39.841 9.351 1.00 78.58 C ANISOU 536 CA LYS A 68 7541 8222 14095 255 3233 1628 C ATOM 537 C LYS A 68 9.126 39.212 7.928 1.00 82.39 C ANISOU 537 C LYS A 68 8270 8712 14322 421 3911 1543 C ATOM 538 O LYS A 68 8.535 39.818 7.013 1.00 83.77 O ANISOU 538 O LYS A 68 8768 9035 14024 437 4129 1472 O ATOM 539 CB LYS A 68 10.607 40.205 9.746 1.00 83.04 C ANISOU 539 CB LYS A 68 7555 8490 15505 232 3195 1960 C ATOM 540 CG LYS A 68 10.713 41.354 10.758 1.00 82.87 C ANISOU 540 CG LYS A 68 7373 8444 15671 47 2600 2068 C ATOM 541 CD LYS A 68 10.233 42.721 10.268 1.00 83.29 C ANISOU 541 CD LYS A 68 7604 8619 15422 -5 2627 2059 C ATOM 542 CE LYS A 68 10.156 42.891 8.746 1.00 87.13 C ANISOU 542 CE LYS A 68 8260 9164 15681 134 3290 2075 C ATOM 543 NZ LYS A 68 8.766 42.561 8.282 1.00 86.19 N ANISOU 543 NZ LYS A 68 8676 9338 14733 168 3342 1773 N ATOM 544 N ARG A 69 9.705 38.010 7.764 1.00 80.32 N ANISOU 544 N ARG A 69 7893 8277 14348 539 4223 1548 N ATOM 545 CA ARG A 69 9.716 37.289 6.480 1.00 83.69 C ANISOU 545 CA ARG A 69 8606 8659 14534 700 4886 1439 C ATOM 546 C ARG A 69 8.608 36.243 6.340 1.00 83.08 C ANISOU 546 C ARG A 69 8984 8741 13840 711 4826 1102 C ATOM 547 O ARG A 69 8.212 35.910 5.231 1.00 83.77 O ANISOU 547 O ARG A 69 9488 8871 13469 790 5235 940 O ATOM 548 CB ARG A 69 11.100 36.652 6.250 1.00 94.49 C ANISOU 548 CB ARG A 69 9568 9679 16655 847 5375 1662 C ATOM 549 CG ARG A 69 11.363 36.117 4.826 1.00102.47 C ANISOU 549 CG ARG A 69 10868 10570 17497 1036 6199 1599 C ATOM 550 CD ARG A 69 12.854 35.964 4.434 1.00104.41 C ANISOU 550 CD ARG A 69 10656 10439 18575 1195 6813 1914 C ATOM 551 NE ARG A 69 13.055 35.075 3.271 1.00107.39 N ANISOU 551 NE ARG A 69 11365 10658 18781 1396 7610 1790 N ATOM 552 CZ ARG A 69 14.202 34.875 2.612 1.00110.13 C ANISOU 552 CZ ARG A 69 11468 10670 19705 1581 8352 2016 C ATOM 553 NH1 ARG A 69 15.316 35.495 2.957 1.00115.31 N ANISOU 553 NH1 ARG A 69 11481 11100 21232 1591 8407 2416 N ATOM 554 NH2 ARG A 69 14.240 34.049 1.579 1.00114.64 N ANISOU 554 NH2 ARG A 69 12458 11105 19997 1758 9067 1844 N ATOM 555 N ASP A 70 8.093 35.758 7.476 1.00 81.32 N ANISOU 555 N ASP A 70 8703 8596 13598 620 4296 1006 N ATOM 556 CA ASP A 70 7.150 34.632 7.528 1.00 76.25 C ANISOU 556 CA ASP A 70 8390 8053 12529 624 4205 728 C ATOM 557 C ASP A 70 5.678 34.975 7.689 1.00 68.23 C ANISOU 557 C ASP A 70 7745 7329 10850 507 3810 520 C ATOM 558 O ASP A 70 4.822 34.073 7.569 1.00 59.24 O ANISOU 558 O ASP A 70 6898 6264 9345 504 3762 294 O ATOM 559 CB ASP A 70 7.502 33.710 8.699 1.00 84.43 C ANISOU 559 CB ASP A 70 9121 8961 14000 612 3910 779 C ATOM 560 CG ASP A 70 8.944 33.206 8.651 1.00 97.75 C ANISOU 560 CG ASP A 70 10374 10318 16448 732 4258 1012 C ATOM 561 OD1 ASP A 70 9.649 33.409 7.629 1.00102.48 O ANISOU 561 OD1 ASP A 70 10941 10772 17226 850 4828 1104 O ATOM 562 OD2 ASP A 70 9.373 32.601 9.661 1.00101.67 O ANISOU 562 OD2 ASP A 70 10554 10686 17388 709 3964 1126 O ATOM 563 N LEU A 71 5.362 36.238 8.005 1.00 62.53 N ANISOU 563 N LEU A 71 6990 6747 10019 408 3517 604 N ATOM 564 CA LEU A 71 3.989 36.556 8.356 1.00 55.43 C ANISOU 564 CA LEU A 71 6363 6089 8610 303 3123 445 C ATOM 565 C LEU A 71 3.077 36.178 7.221 1.00 56.06 C ANISOU 565 C LEU A 71 6886 6285 8130 328 3329 246 C ATOM 566 O LEU A 71 2.051 35.553 7.445 1.00 53.80 O ANISOU 566 O LEU A 71 6805 6102 7533 282 3104 69 O ATOM 567 CB LEU A 71 3.766 38.020 8.795 1.00 53.54 C ANISOU 567 CB LEU A 71 6047 5952 8345 206 2828 558 C ATOM 568 CG LEU A 71 2.505 38.232 9.678 1.00 49.46 C ANISOU 568 CG LEU A 71 5682 5611 7498 105 2367 434 C ATOM 569 CD1 LEU A 71 2.272 37.108 10.700 1.00 44.90 C ANISOU 569 CD1 LEU A 71 5065 5006 6990 90 2130 345 C ATOM 570 CD2 LEU A 71 2.547 39.551 10.409 1.00 45.14 C ANISOU 570 CD2 LEU A 71 5007 5081 7065 19 2074 550 C ATOM 571 N SER A 72 3.461 36.507 5.998 1.00 60.00 N ANISOU 571 N SER A 72 7547 6744 8505 395 3754 285 N ATOM 572 CA SER A 72 2.563 36.269 4.862 1.00 64.66 C ANISOU 572 CA SER A 72 8633 7444 8491 392 3890 105 C ATOM 573 C SER A 72 2.396 34.762 4.568 1.00 62.51 C ANISOU 573 C SER A 72 8584 7073 8095 442 4048 -115 C ATOM 574 O SER A 72 1.386 34.306 3.977 1.00 60.59 O ANISOU 574 O SER A 72 8751 6919 7352 392 3959 -315 O ATOM 575 CB SER A 72 3.022 37.046 3.625 1.00 70.20 C ANISOU 575 CB SER A 72 9516 8123 9034 447 4310 218 C ATOM 576 OG SER A 72 4.439 37.017 3.492 1.00 75.78 O ANISOU 576 OG SER A 72 9932 8604 10255 562 4755 394 O ATOM 577 N LYS A 73 3.372 33.993 5.037 1.00 63.04 N ANISOU 577 N LYS A 73 8359 6934 8658 529 4239 -64 N ATOM 578 CA LYS A 73 3.376 32.531 4.866 1.00 65.57 C ANISOU 578 CA LYS A 73 8827 7107 8981 592 4422 -252 C ATOM 579 C LYS A 73 2.358 31.967 5.904 1.00 58.46 C ANISOU 579 C LYS A 73 7895 6323 7995 486 3887 -370 C ATOM 580 O LYS A 73 1.378 31.293 5.521 1.00 57.22 O ANISOU 580 O LYS A 73 8087 6220 7435 438 3784 -589 O ATOM 581 CB LYS A 73 4.810 31.997 5.048 1.00 69.63 C ANISOU 581 CB LYS A 73 8974 7336 10146 731 4815 -104 C ATOM 582 CG LYS A 73 5.297 30.922 4.074 1.00 73.89 C ANISOU 582 CG LYS A 73 9763 7636 10675 873 5406 -243 C ATOM 583 CD LYS A 73 5.658 31.484 2.710 1.00 78.01 C ANISOU 583 CD LYS A 73 10610 8112 10916 952 5951 -227 C ATOM 584 CE LYS A 73 6.670 30.554 2.017 1.00 84.49 C ANISOU 584 CE LYS A 73 11484 8595 12023 1142 6665 -254 C ATOM 585 NZ LYS A 73 6.842 30.629 0.519 1.00 92.98 N ANISOU 585 NZ LYS A 73 13102 9576 12652 1238 7301 -350 N ATOM 586 N LEU A 74 2.530 32.327 7.186 1.00 53.03 N ANISOU 586 N LEU A 74 6823 5671 7654 438 3532 -217 N ATOM 587 CA LEU A 74 1.506 32.015 8.177 1.00 48.10 C ANISOU 587 CA LEU A 74 6202 5173 6901 339 3058 -295 C ATOM 588 C LEU A 74 0.125 32.353 7.651 1.00 46.93 C ANISOU 588 C LEU A 74 6411 5224 6196 250 2871 -440 C ATOM 589 O LEU A 74 -0.748 31.481 7.669 1.00 43.68 O ANISOU 589 O LEU A 74 6182 4829 5586 209 2730 -603 O ATOM 590 CB LEU A 74 1.722 32.706 9.521 1.00 46.73 C ANISOU 590 CB LEU A 74 5698 5045 7013 278 2689 -114 C ATOM 591 CG LEU A 74 0.638 32.362 10.603 1.00 41.15 C ANISOU 591 CG LEU A 74 5033 4453 6151 190 2260 -184 C ATOM 592 CD1 LEU A 74 0.504 30.858 10.877 1.00 41.90 C ANISOU 592 CD1 LEU A 74 5141 4434 6344 220 2274 -286 C ATOM 593 CD2 LEU A 74 1.049 33.083 11.847 1.00 40.25 C ANISOU 593 CD2 LEU A 74 4663 4341 6290 138 1957 -9 C ATOM 594 N PHE A 75 -0.059 33.580 7.112 1.00 47.08 N ANISOU 594 N PHE A 75 6522 5368 5998 218 2874 -365 N ATOM 595 CA PHE A 75 -1.426 34.024 6.734 1.00 45.14 C ANISOU 595 CA PHE A 75 6553 5306 5291 122 2618 -448 C ATOM 596 C PHE A 75 -1.955 33.130 5.652 1.00 48.63 C ANISOU 596 C PHE A 75 7394 5714 5371 113 2744 -648 C ATOM 597 O PHE A 75 -3.112 32.698 5.707 1.00 49.80 O ANISOU 597 O PHE A 75 7699 5931 5292 27 2456 -762 O ATOM 598 CB PHE A 75 -1.538 35.503 6.306 1.00 43.63 C ANISOU 598 CB PHE A 75 6390 5238 4951 92 2596 -311 C ATOM 599 CG PHE A 75 -1.394 36.515 7.439 1.00 41.30 C ANISOU 599 CG PHE A 75 5776 4990 4926 61 2355 -152 C ATOM 600 CD1 PHE A 75 -1.755 36.206 8.794 1.00 40.15 C ANISOU 600 CD1 PHE A 75 5453 4852 4949 22 2047 -163 C ATOM 601 CD2 PHE A 75 -0.946 37.788 7.159 1.00 39.85 C ANISOU 601 CD2 PHE A 75 5512 4828 4800 63 2433 6 C ATOM 602 CE1 PHE A 75 -1.651 37.195 9.816 1.00 35.80 C ANISOU 602 CE1 PHE A 75 4701 4324 4576 -16 1826 -41 C ATOM 603 CE2 PHE A 75 -0.811 38.747 8.163 1.00 39.87 C ANISOU 603 CE2 PHE A 75 5271 4843 5036 23 2203 129 C ATOM 604 CZ PHE A 75 -1.179 38.463 9.489 1.00 38.27 C ANISOU 604 CZ PHE A 75 4945 4643 4952 -19 1895 92 C ATOM 605 N THR A 76 -1.118 32.842 4.648 1.00 53.53 N ANISOU 605 N THR A 76 8196 6202 5940 200 3183 -687 N ATOM 606 CA THR A 76 -1.582 31.978 3.562 1.00 56.17 C ANISOU 606 CA THR A 76 9003 6470 5869 184 3313 -908 C ATOM 607 C THR A 76 -1.956 30.534 4.029 1.00 54.81 C ANISOU 607 C THR A 76 8845 6182 5800 168 3194 -1093 C ATOM 608 O THR A 76 -2.997 30.016 3.593 1.00 54.53 O ANISOU 608 O THR A 76 9128 6171 5422 69 2967 -1261 O ATOM 609 CB THR A 76 -0.651 32.040 2.293 1.00 66.60 C ANISOU 609 CB THR A 76 10616 7657 7032 288 3875 -921 C ATOM 610 OG1 THR A 76 0.720 31.962 2.702 1.00 69.17 O ANISOU 610 OG1 THR A 76 10571 7817 7894 425 4251 -784 O ATOM 611 CG2 THR A 76 -0.864 33.387 1.486 1.00 62.37 C ANISOU 611 CG2 THR A 76 10278 7275 6147 247 3883 -786 C ATOM 612 N SER A 77 -1.169 29.903 4.918 1.00 53.04 N ANISOU 612 N SER A 77 8270 5822 6061 250 3298 -1042 N ATOM 613 CA SER A 77 -1.585 28.559 5.436 1.00 55.92 C ANISOU 613 CA SER A 77 8625 6075 6546 229 3158 -1189 C ATOM 614 C SER A 77 -2.878 28.622 6.192 1.00 55.31 C ANISOU 614 C SER A 77 8489 6161 6367 100 2649 -1189 C ATOM 615 O SER A 77 -3.793 27.822 5.962 1.00 55.95 O ANISOU 615 O SER A 77 8790 6210 6260 20 2471 -1353 O ATOM 616 CB SER A 77 -0.506 27.764 6.222 1.00 61.34 C ANISOU 616 CB SER A 77 8956 6561 7791 343 3355 -1113 C ATOM 617 OG SER A 77 0.100 28.484 7.289 1.00 65.41 O ANISOU 617 OG SER A 77 9030 7134 8690 360 3219 -867 O ATOM 618 N LEU A 78 -3.005 29.667 7.008 1.00 52.78 N ANISOU 618 N LEU A 78 7900 6001 6153 72 2425 -1002 N ATOM 619 CA LEU A 78 -4.215 29.872 7.762 1.00 47.15 C ANISOU 619 CA LEU A 78 7117 5428 5369 -31 2011 -973 C ATOM 620 C LEU A 78 -5.499 29.931 6.870 1.00 48.96 C ANISOU 620 C LEU A 78 7676 5740 5186 -143 1807 -1085 C ATOM 621 O LEU A 78 -6.613 29.636 7.360 1.00 48.38 O ANISOU 621 O LEU A 78 7564 5709 5108 -228 1496 -1094 O ATOM 622 CB LEU A 78 -3.986 31.125 8.621 1.00 44.93 C ANISOU 622 CB LEU A 78 6565 5271 5235 -26 1889 -770 C ATOM 623 CG LEU A 78 -4.986 31.689 9.571 1.00 44.58 C ANISOU 623 CG LEU A 78 6407 5357 5174 -96 1555 -687 C ATOM 624 CD1 LEU A 78 -5.239 30.607 10.610 1.00 42.81 C ANISOU 624 CD1 LEU A 78 6057 5056 5152 -101 1430 -706 C ATOM 625 CD2 LEU A 78 -4.414 32.987 10.188 1.00 43.50 C ANISOU 625 CD2 LEU A 78 6076 5286 5168 -76 1531 -518 C ATOM 626 N PHE A 79 -5.385 30.264 5.563 1.00 51.04 N ANISOU 626 N PHE A 79 8272 6007 5115 -151 1965 -1152 N ATOM 627 CA PHE A 79 -6.620 30.295 4.725 1.00 52.10 C ANISOU 627 CA PHE A 79 8733 6202 4861 -282 1686 -1236 C ATOM 628 C PHE A 79 -6.658 29.253 3.574 1.00 60.32 C ANISOU 628 C PHE A 79 10237 7082 5599 -318 1800 -1476 C ATOM 629 O PHE A 79 -7.635 29.192 2.757 1.00 60.31 O ANISOU 629 O PHE A 79 10575 7098 5242 -451 1525 -1559 O ATOM 630 CB PHE A 79 -6.921 31.712 4.247 1.00 51.97 C ANISOU 630 CB PHE A 79 8770 6352 4625 -318 1591 -1084 C ATOM 631 CG PHE A 79 -7.266 32.691 5.391 1.00 48.71 C ANISOU 631 CG PHE A 79 7963 6073 4471 -316 1392 -884 C ATOM 632 CD1 PHE A 79 -8.543 32.749 5.912 1.00 47.13 C ANISOU 632 CD1 PHE A 79 7656 5936 4316 -405 1031 -835 C ATOM 633 CD2 PHE A 79 -6.304 33.537 5.930 1.00 48.03 C ANISOU 633 CD2 PHE A 79 7632 6018 4601 -227 1581 -746 C ATOM 634 CE1 PHE A 79 -8.872 33.625 6.941 1.00 45.31 C ANISOU 634 CE1 PHE A 79 7123 5794 4298 -390 912 -671 C ATOM 635 CE2 PHE A 79 -6.628 34.449 6.951 1.00 47.47 C ANISOU 635 CE2 PHE A 79 7278 6039 4718 -233 1401 -594 C ATOM 636 CZ PHE A 79 -7.911 34.483 7.468 1.00 42.68 C ANISOU 636 CZ PHE A 79 6609 5492 4117 -306 1092 -567 C ATOM 637 N VAL A 80 -5.611 28.412 3.531 1.00 62.91 N ANISOU 637 N VAL A 80 10587 7228 6088 -205 2185 -1585 N ATOM 638 CA VAL A 80 -5.458 27.439 2.413 1.00 70.37 C ANISOU 638 CA VAL A 80 12024 7973 6740 -211 2401 -1838 C ATOM 639 C VAL A 80 -6.683 26.583 2.326 1.00 72.05 C ANISOU 639 C VAL A 80 12428 8130 6820 -367 1988 -1996 C ATOM 640 O VAL A 80 -7.472 26.703 1.375 1.00 79.13 O ANISOU 640 O VAL A 80 13738 9044 7283 -501 1748 -2085 O ATOM 641 CB VAL A 80 -4.323 26.437 2.581 1.00 71.25 C ANISOU 641 CB VAL A 80 12065 7846 7161 -64 2849 -1936 C ATOM 642 CG1 VAL A 80 -3.918 25.908 1.207 1.00 78.83 C ANISOU 642 CG1 VAL A 80 13606 8609 7737 -30 3231 -2166 C ATOM 643 CG2 VAL A 80 -3.126 27.059 3.247 1.00 71.19 C ANISOU 643 CG2 VAL A 80 11620 7862 7567 85 3148 -1716 C ATOM 644 N ASP A 81 -6.845 25.748 3.348 1.00 66.80 N ANISOU 644 N ASP A 81 11445 7388 6548 -360 1877 -2000 N ATOM 645 CA ASP A 81 -7.947 24.804 3.403 1.00 67.46 C ANISOU 645 CA ASP A 81 11631 7377 6625 -502 1509 -2130 C ATOM 646 C ASP A 81 -9.367 25.421 3.517 1.00 65.64 C ANISOU 646 C ASP A 81 11330 7313 6298 -668 978 -2006 C ATOM 647 O ASP A 81 -10.307 24.823 3.024 1.00 67.92 O ANISOU 647 O ASP A 81 11858 7506 6442 -821 653 -2126 O ATOM 648 CB ASP A 81 -7.679 23.766 4.502 1.00 63.96 C ANISOU 648 CB ASP A 81 10844 6797 6661 -436 1574 -2129 C ATOM 649 CG ASP A 81 -7.616 24.391 5.885 1.00 61.56 C ANISOU 649 CG ASP A 81 10011 6661 6718 -379 1487 -1863 C ATOM 650 OD1 ASP A 81 -6.788 25.321 6.139 1.00 57.13 O ANISOU 650 OD1 ASP A 81 9273 6215 6220 -277 1688 -1713 O ATOM 651 OD2 ASP A 81 -8.428 23.927 6.706 1.00 57.52 O ANISOU 651 OD2 ASP A 81 9289 6145 6422 -446 1213 -1805 O ATOM 652 N VAL A 82 -9.536 26.594 4.143 1.00 62.60 N ANISOU 652 N VAL A 82 10620 7144 6022 -642 883 -1763 N ATOM 653 CA VAL A 82 -10.879 27.234 4.248 1.00 57.73 C ANISOU 653 CA VAL A 82 9901 6657 5379 -779 429 -1617 C ATOM 654 C VAL A 82 -10.821 28.723 4.658 1.00 55.94 C ANISOU 654 C VAL A 82 9420 6644 5189 -722 441 -1376 C ATOM 655 O VAL A 82 -9.861 29.166 5.334 1.00 50.09 O ANISOU 655 O VAL A 82 8449 5957 4626 -586 728 -1293 O ATOM 656 CB VAL A 82 -11.813 26.452 5.220 1.00 56.54 C ANISOU 656 CB VAL A 82 9453 6437 5594 -845 160 -1573 C ATOM 657 CG1 VAL A 82 -11.285 26.478 6.642 1.00 51.46 C ANISOU 657 CG1 VAL A 82 8385 5836 5331 -712 357 -1440 C ATOM 658 CG2 VAL A 82 -13.248 26.963 5.160 1.00 56.22 C ANISOU 658 CG2 VAL A 82 9319 6467 5574 -991 -287 -1423 C ATOM 659 N ILE A 83 -11.840 29.480 4.228 1.00 56.34 N ANISOU 659 N ILE A 83 9517 6791 5098 -833 109 -1258 N ATOM 660 CA ILE A 83 -12.087 30.841 4.729 1.00 55.08 C ANISOU 660 CA ILE A 83 9079 6801 5046 -796 57 -1019 C ATOM 661 C ILE A 83 -13.388 30.885 5.517 1.00 51.80 C ANISOU 661 C ILE A 83 8353 6396 4932 -867 -266 -869 C ATOM 662 O ILE A 83 -14.486 30.632 4.981 1.00 55.36 O ANISOU 662 O ILE A 83 8891 6794 5349 -1012 -628 -849 O ATOM 663 CB ILE A 83 -12.236 31.904 3.634 1.00 58.90 C ANISOU 663 CB ILE A 83 9809 7383 5188 -847 -36 -933 C ATOM 664 CG1 ILE A 83 -11.309 31.632 2.448 1.00 66.76 C ANISOU 664 CG1 ILE A 83 11270 8321 5776 -828 220 -1102 C ATOM 665 CG2 ILE A 83 -12.066 33.288 4.248 1.00 58.82 C ANISOU 665 CG2 ILE A 83 9499 7515 5335 -761 54 -713 C ATOM 666 CD1 ILE A 83 -9.922 32.228 2.550 1.00 69.63 C ANISOU 666 CD1 ILE A 83 11571 8727 6159 -667 689 -1067 C ATOM 667 N ASN A 84 -13.258 31.199 6.797 1.00 45.08 N ANISOU 667 N ASN A 84 7150 5590 4388 -769 -132 -754 N ATOM 668 CA ASN A 84 -14.437 31.465 7.595 1.00 42.35 C ANISOU 668 CA ASN A 84 6507 5251 4332 -802 -335 -577 C ATOM 669 C ASN A 84 -14.106 32.530 8.622 1.00 38.11 C ANISOU 669 C ASN A 84 5728 4809 3942 -683 -141 -432 C ATOM 670 O ASN A 84 -12.969 33.011 8.685 1.00 35.20 O ANISOU 670 O ASN A 84 5407 4497 3470 -595 93 -467 O ATOM 671 CB ASN A 84 -15.016 30.178 8.188 1.00 40.36 C ANISOU 671 CB ASN A 84 6138 4862 4333 -848 -430 -625 C ATOM 672 CG ASN A 84 -14.100 29.532 9.229 1.00 39.97 C ANISOU 672 CG ASN A 84 5981 4776 4429 -734 -146 -690 C ATOM 673 OD1 ASN A 84 -13.342 30.198 9.920 1.00 35.80 O ANISOU 673 OD1 ASN A 84 5351 4327 3923 -624 66 -632 O ATOM 674 ND2 ASN A 84 -14.183 28.213 9.347 1.00 38.96 N ANISOU 674 ND2 ASN A 84 5877 4507 4420 -772 -176 -801 N ATOM 675 N SER A 85 -15.077 32.938 9.422 1.00 36.70 N ANISOU 675 N SER A 85 5298 4626 4020 -678 -225 -265 N ATOM 676 CA SER A 85 -14.798 34.081 10.270 1.00 33.86 C ANISOU 676 CA SER A 85 4791 4336 3739 -574 -48 -148 C ATOM 677 C SER A 85 -13.887 33.730 11.424 1.00 30.87 C ANISOU 677 C SER A 85 4357 3940 3431 -480 182 -207 C ATOM 678 O SER A 85 -13.223 34.583 11.935 1.00 30.77 O ANISOU 678 O SER A 85 4320 3974 3398 -408 322 -172 O ATOM 679 CB SER A 85 -16.093 34.712 10.743 1.00 36.74 C ANISOU 679 CB SER A 85 4933 4672 4353 -580 -146 52 C ATOM 680 OG SER A 85 -16.836 33.727 11.430 1.00 37.15 O ANISOU 680 OG SER A 85 4844 4620 4652 -601 -180 78 O ATOM 681 N GLY A 86 -13.839 32.470 11.814 1.00 30.07 N ANISOU 681 N GLY A 86 4246 3756 3423 -491 191 -287 N ATOM 682 CA GLY A 86 -12.957 32.002 12.847 1.00 26.50 C ANISOU 682 CA GLY A 86 3755 3272 3040 -416 359 -322 C ATOM 683 C GLY A 86 -11.515 32.058 12.400 1.00 27.73 C ANISOU 683 C GLY A 86 4022 3451 3063 -374 491 -425 C ATOM 684 O GLY A 86 -10.607 32.344 13.230 1.00 24.03 O ANISOU 684 O GLY A 86 3497 2985 2650 -308 604 -395 O ATOM 685 N ARG A 87 -11.252 31.761 11.104 1.00 28.90 N ANISOU 685 N ARG A 87 4341 3593 3046 -415 481 -539 N ATOM 686 CA ARG A 87 -9.875 31.932 10.569 1.00 27.74 C ANISOU 686 CA ARG A 87 4291 3449 2800 -359 679 -609 C ATOM 687 C ARG A 87 -9.526 33.405 10.534 1.00 26.81 C ANISOU 687 C ARG A 87 4135 3431 2621 -327 728 -500 C ATOM 688 O ARG A 87 -8.408 33.867 10.901 1.00 25.54 O ANISOU 688 O ARG A 87 3900 3266 2537 -264 874 -465 O ATOM 689 CB ARG A 87 -9.719 31.285 9.184 1.00 31.02 C ANISOU 689 CB ARG A 87 4966 3812 3010 -401 716 -761 C ATOM 690 CG ARG A 87 -9.952 29.778 9.098 1.00 31.22 C ANISOU 690 CG ARG A 87 5068 3697 3098 -438 680 -903 C ATOM 691 CD ARG A 87 -8.989 29.001 10.008 1.00 32.09 C ANISOU 691 CD ARG A 87 5024 3710 3459 -350 860 -917 C ATOM 692 NE ARG A 87 -9.331 27.571 9.968 1.00 34.06 N ANISOU 692 NE ARG A 87 5330 3808 3802 -388 814 -1038 N ATOM 693 CZ ARG A 87 -8.848 26.722 9.044 1.00 38.45 C ANISOU 693 CZ ARG A 87 6111 4229 4270 -386 952 -1221 C ATOM 694 NH1 ARG A 87 -7.989 27.152 8.102 1.00 39.78 N ANISOU 694 NH1 ARG A 87 6470 4400 4246 -336 1181 -1288 N ATOM 695 NH2 ARG A 87 -9.217 25.439 9.055 1.00 39.46 N ANISOU 695 NH2 ARG A 87 6291 4195 4507 -429 891 -1336 N ATOM 696 N ILE A 88 -10.466 34.205 10.078 1.00 27.11 N ANISOU 696 N ILE A 88 4203 3539 2558 -376 589 -424 N ATOM 697 CA ILE A 88 -10.252 35.641 10.221 1.00 27.57 C ANISOU 697 CA ILE A 88 4195 3670 2611 -343 629 -303 C ATOM 698 C ILE A 88 -9.951 36.126 11.672 1.00 25.25 C ANISOU 698 C ILE A 88 3734 3357 2503 -286 676 -235 C ATOM 699 O ILE A 88 -9.042 36.983 11.892 1.00 24.78 O ANISOU 699 O ILE A 88 3638 3304 2473 -248 765 -193 O ATOM 700 CB ILE A 88 -11.436 36.395 9.659 1.00 29.47 C ANISOU 700 CB ILE A 88 4451 3963 2783 -399 454 -200 C ATOM 701 CG1 ILE A 88 -11.533 35.956 8.164 1.00 33.54 C ANISOU 701 CG1 ILE A 88 5217 4488 3040 -472 376 -273 C ATOM 702 CG2 ILE A 88 -11.215 37.916 9.896 1.00 28.97 C ANISOU 702 CG2 ILE A 88 4305 3947 2755 -355 514 -71 C ATOM 703 CD1 ILE A 88 -12.653 36.581 7.373 1.00 37.47 C ANISOU 703 CD1 ILE A 88 5768 5024 3444 -555 130 -154 C ATOM 704 N VAL A 89 -10.674 35.620 12.672 1.00 22.10 N ANISOU 704 N VAL A 89 3255 2917 2225 -285 615 -217 N ATOM 705 CA VAL A 89 -10.384 36.096 13.989 1.00 20.85 C ANISOU 705 CA VAL A 89 3032 2729 2160 -239 659 -163 C ATOM 706 C VAL A 89 -8.951 35.680 14.379 1.00 19.63 C ANISOU 706 C VAL A 89 2871 2530 2059 -213 722 -209 C ATOM 707 O VAL A 89 -8.234 36.424 14.966 1.00 20.94 O ANISOU 707 O VAL A 89 3018 2678 2263 -196 729 -167 O ATOM 708 CB VAL A 89 -11.356 35.457 14.995 1.00 21.46 C ANISOU 708 CB VAL A 89 3065 2752 2336 -234 635 -127 C ATOM 709 CG1 VAL A 89 -10.884 35.720 16.442 1.00 19.84 C ANISOU 709 CG1 VAL A 89 2887 2496 2157 -191 687 -94 C ATOM 710 CG2 VAL A 89 -12.777 35.930 14.708 1.00 20.61 C ANISOU 710 CG2 VAL A 89 2898 2652 2280 -252 585 -37 C ATOM 711 N GLY A 90 -8.530 34.482 14.019 1.00 20.64 N ANISOU 711 N GLY A 90 3005 2615 2221 -215 754 -285 N ATOM 712 CA GLY A 90 -7.141 34.029 14.245 1.00 22.21 C ANISOU 712 CA GLY A 90 3149 2743 2546 -182 826 -299 C ATOM 713 C GLY A 90 -6.100 34.965 13.586 1.00 24.57 C ANISOU 713 C GLY A 90 3423 3053 2858 -164 926 -267 C ATOM 714 O GLY A 90 -5.030 35.254 14.184 1.00 24.32 O ANISOU 714 O GLY A 90 3288 2959 2993 -148 922 -201 O ATOM 715 N PHE A 91 -6.389 35.391 12.337 1.00 25.54 N ANISOU 715 N PHE A 91 3643 3239 2821 -174 1000 -294 N ATOM 716 CA PHE A 91 -5.579 36.362 11.600 1.00 27.14 C ANISOU 716 CA PHE A 91 3841 3457 3015 -157 1126 -238 C ATOM 717 C PHE A 91 -5.405 37.648 12.462 1.00 27.86 C ANISOU 717 C PHE A 91 3832 3553 3198 -165 1029 -130 C ATOM 718 O PHE A 91 -4.287 38.228 12.635 1.00 29.55 O ANISOU 718 O PHE A 91 3937 3706 3583 -154 1076 -57 O ATOM 719 CB PHE A 91 -6.297 36.590 10.257 1.00 27.59 C ANISOU 719 CB PHE A 91 4079 3591 2812 -184 1157 -270 C ATOM 720 CG PHE A 91 -5.934 37.879 9.525 1.00 29.58 C ANISOU 720 CG PHE A 91 4356 3889 2993 -178 1245 -170 C ATOM 721 CD1 PHE A 91 -6.620 39.038 9.787 1.00 26.96 C ANISOU 721 CD1 PHE A 91 3987 3617 2641 -203 1114 -74 C ATOM 722 CD2 PHE A 91 -5.047 37.855 8.416 1.00 31.89 C ANISOU 722 CD2 PHE A 91 4747 4152 3217 -145 1491 -170 C ATOM 723 CE1 PHE A 91 -6.392 40.187 9.015 1.00 29.98 C ANISOU 723 CE1 PHE A 91 4401 4033 2955 -202 1186 32 C ATOM 724 CE2 PHE A 91 -4.790 39.011 7.663 1.00 32.32 C ANISOU 724 CE2 PHE A 91 4845 4246 3189 -142 1589 -55 C ATOM 725 CZ PHE A 91 -5.477 40.188 7.965 1.00 31.60 C ANISOU 725 CZ PHE A 91 4695 4222 3091 -176 1414 50 C ATOM 726 N PHE A 92 -6.510 38.125 12.993 1.00 24.29 N ANISOU 726 N PHE A 92 3417 3148 2663 -188 901 -115 N ATOM 727 CA PHE A 92 -6.383 39.334 13.788 1.00 22.52 C ANISOU 727 CA PHE A 92 3157 2899 2502 -193 834 -43 C ATOM 728 C PHE A 92 -5.643 39.058 15.059 1.00 22.87 C ANISOU 728 C PHE A 92 3159 2849 2683 -200 744 -38 C ATOM 729 O PHE A 92 -5.003 39.968 15.579 1.00 23.67 O ANISOU 729 O PHE A 92 3234 2886 2872 -220 677 13 O ATOM 730 CB PHE A 92 -7.768 39.956 14.079 1.00 21.57 C ANISOU 730 CB PHE A 92 3091 2814 2290 -197 774 -18 C ATOM 731 CG PHE A 92 -8.281 40.832 12.945 1.00 22.20 C ANISOU 731 CG PHE A 92 3185 2959 2290 -204 801 45 C ATOM 732 CD1 PHE A 92 -7.684 42.087 12.696 1.00 21.99 C ANISOU 732 CD1 PHE A 92 3130 2914 2310 -203 839 120 C ATOM 733 CD2 PHE A 92 -9.335 40.383 12.080 1.00 21.63 C ANISOU 733 CD2 PHE A 92 3158 2952 2108 -225 757 48 C ATOM 734 CE1 PHE A 92 -8.133 42.867 11.632 1.00 24.44 C ANISOU 734 CE1 PHE A 92 3463 3281 2544 -209 859 207 C ATOM 735 CE2 PHE A 92 -9.769 41.193 10.962 1.00 23.10 C ANISOU 735 CE2 PHE A 92 3382 3194 2201 -245 734 137 C ATOM 736 CZ PHE A 92 -9.184 42.404 10.743 1.00 23.75 C ANISOU 736 CZ PHE A 92 3441 3268 2313 -231 797 220 C ATOM 737 N ASP A 93 -5.763 37.855 15.633 1.00 23.18 N ANISOU 737 N ASP A 93 3207 2862 2740 -194 707 -79 N ATOM 738 CA ASP A 93 -5.088 37.619 16.957 1.00 22.64 C ANISOU 738 CA ASP A 93 3133 2696 2775 -212 569 -45 C ATOM 739 C ASP A 93 -3.631 37.481 16.715 1.00 24.37 C ANISOU 739 C ASP A 93 3200 2834 3225 -217 565 9 C ATOM 740 O ASP A 93 -2.795 37.774 17.603 1.00 25.31 O ANISOU 740 O ASP A 93 3280 2852 3482 -256 395 79 O ATOM 741 CB ASP A 93 -5.549 36.296 17.581 1.00 22.97 C ANISOU 741 CB ASP A 93 3208 2719 2799 -202 540 -71 C ATOM 742 CG ASP A 93 -5.132 36.162 19.027 1.00 25.31 C ANISOU 742 CG ASP A 93 3574 2924 3116 -228 372 -16 C ATOM 743 OD1 ASP A 93 -5.028 37.213 19.724 1.00 27.30 O ANISOU 743 OD1 ASP A 93 3937 3139 3296 -260 271 6 O ATOM 744 OD2 ASP A 93 -4.944 35.010 19.530 1.00 25.45 O ANISOU 744 OD2 ASP A 93 3573 2893 3204 -224 324 8 O ATOM 745 N VAL A 94 -3.269 36.921 15.546 1.00 24.81 N ANISOU 745 N VAL A 94 3174 2904 3348 -178 750 -14 N ATOM 746 CA VAL A 94 -1.814 36.957 15.209 1.00 27.37 C ANISOU 746 CA VAL A 94 3314 3123 3965 -164 823 71 C ATOM 747 C VAL A 94 -1.283 38.387 15.146 1.00 28.40 C ANISOU 747 C VAL A 94 3383 3228 4180 -198 783 160 C ATOM 748 O VAL A 94 -0.214 38.717 15.758 1.00 30.86 O ANISOU 748 O VAL A 94 3543 3410 4772 -236 642 269 O ATOM 749 CB VAL A 94 -1.503 36.196 13.922 1.00 28.32 C ANISOU 749 CB VAL A 94 3407 3234 4119 -101 1107 25 C ATOM 750 CG1 VAL A 94 -0.089 36.541 13.463 1.00 30.94 C ANISOU 750 CG1 VAL A 94 3536 3446 4774 -71 1263 146 C ATOM 751 CG2 VAL A 94 -1.823 34.680 14.151 1.00 27.29 C ANISOU 751 CG2 VAL A 94 3308 3069 3991 -76 1114 -57 C ATOM 752 N GLY A 95 -2.021 39.266 14.451 1.00 27.08 N ANISOU 752 N GLY A 95 3321 3162 3806 -196 868 132 N ATOM 753 CA GLY A 95 -1.601 40.698 14.373 1.00 26.78 C ANISOU 753 CA GLY A 95 3230 3087 3858 -229 836 221 C ATOM 754 C GLY A 95 -1.604 41.340 15.772 1.00 28.90 C ANISOU 754 C GLY A 95 3549 3275 4156 -297 555 231 C ATOM 755 O GLY A 95 -0.753 42.188 16.064 1.00 32.66 O ANISOU 755 O GLY A 95 3930 3637 4842 -349 442 317 O ATOM 756 N ARG A 96 -2.556 40.969 16.640 1.00 26.27 N ANISOU 756 N ARG A 96 3388 2979 3613 -302 447 148 N ATOM 757 CA ARG A 96 -2.577 41.513 17.984 1.00 28.83 C ANISOU 757 CA ARG A 96 3849 3208 3895 -361 216 139 C ATOM 758 C ARG A 96 -1.376 41.062 18.785 1.00 32.32 C ANISOU 758 C ARG A 96 4207 3515 4559 -422 -12 212 C ATOM 759 O ARG A 96 -0.830 41.852 19.549 1.00 35.89 O ANISOU 759 O ARG A 96 4715 3840 5083 -504 -245 246 O ATOM 760 CB ARG A 96 -3.834 41.099 18.734 1.00 26.27 C ANISOU 760 CB ARG A 96 3741 2936 3306 -337 219 56 C ATOM 761 CG ARG A 96 -3.892 41.653 20.147 1.00 28.01 C ANISOU 761 CG ARG A 96 4194 3040 3410 -390 29 32 C ATOM 762 CD ARG A 96 -5.229 41.374 20.903 1.00 26.09 C ANISOU 762 CD ARG A 96 4186 2824 2905 -345 124 -32 C ATOM 763 NE ARG A 96 -5.443 39.941 21.133 1.00 26.66 N ANISOU 763 NE ARG A 96 4236 2941 2952 -319 141 -20 N ATOM 764 CZ ARG A 96 -5.407 39.366 22.353 1.00 29.02 C ANISOU 764 CZ ARG A 96 4725 3167 3133 -343 20 -9 C ATOM 765 NH1 ARG A 96 -5.215 40.080 23.451 1.00 28.72 N ANISOU 765 NH1 ARG A 96 4961 3010 2942 -396 -129 -25 N ATOM 766 NH2 ARG A 96 -5.646 38.081 22.511 1.00 27.53 N ANISOU 766 NH2 ARG A 96 4498 3013 2949 -316 53 19 N ATOM 767 N TYR A 97 -0.990 39.775 18.625 1.00 34.82 N ANISOU 767 N TYR A 97 4396 3835 4997 -388 31 240 N ATOM 768 CA TYR A 97 0.187 39.234 19.294 1.00 36.11 C ANISOU 768 CA TYR A 97 4420 3854 5447 -438 -191 351 C ATOM 769 C TYR A 97 1.404 40.060 18.852 1.00 37.45 C ANISOU 769 C TYR A 97 4347 3901 5980 -480 -233 478 C ATOM 770 O TYR A 97 2.123 40.562 19.707 1.00 42.09 O ANISOU 770 O TYR A 97 4922 4342 6730 -582 -555 562 O ATOM 771 CB TYR A 97 0.460 37.760 18.930 1.00 35.86 C ANISOU 771 CB TYR A 97 4234 3823 5568 -371 -59 376 C ATOM 772 CG TYR A 97 1.643 37.197 19.748 1.00 40.15 C ANISOU 772 CG TYR A 97 4611 4192 6454 -425 -331 531 C ATOM 773 CD1 TYR A 97 1.428 36.690 21.042 1.00 41.86 C ANISOU 773 CD1 TYR A 97 5008 4368 6530 -480 -618 551 C ATOM 774 CD2 TYR A 97 2.975 37.203 19.256 1.00 42.96 C ANISOU 774 CD2 TYR A 97 4627 4404 7294 -423 -306 688 C ATOM 775 CE1 TYR A 97 2.478 36.202 21.830 1.00 44.49 C ANISOU 775 CE1 TYR A 97 5206 4533 7167 -545 -933 723 C ATOM 776 CE2 TYR A 97 4.037 36.702 20.037 1.00 47.16 C ANISOU 776 CE2 TYR A 97 4966 4750 8204 -480 -602 869 C ATOM 777 CZ TYR A 97 3.767 36.199 21.327 1.00 48.96 C ANISOU 777 CZ TYR A 97 5397 4953 8254 -548 -945 885 C ATOM 778 OH TYR A 97 4.743 35.693 22.175 1.00 53.67 O ANISOU 778 OH TYR A 97 5840 5364 9187 -622 -1308 1086 O ATOM 779 N VAL A 98 1.658 40.153 17.542 1.00 36.47 N ANISOU 779 N VAL A 98 4045 3819 5993 -410 81 505 N ATOM 780 CA VAL A 98 2.808 40.903 17.046 1.00 38.25 C ANISOU 780 CA VAL A 98 4010 3915 6608 -436 111 656 C ATOM 781 C VAL A 98 2.865 42.315 17.699 1.00 40.68 C ANISOU 781 C VAL A 98 4407 4142 6906 -547 -164 674 C ATOM 782 O VAL A 98 3.857 42.651 18.370 1.00 44.33 O ANISOU 782 O VAL A 98 4731 4418 7696 -648 -466 799 O ATOM 783 CB VAL A 98 2.829 41.050 15.525 1.00 37.18 C ANISOU 783 CB VAL A 98 3783 3852 6491 -342 537 669 C ATOM 784 CG1 VAL A 98 4.012 41.939 15.122 1.00 37.17 C ANISOU 784 CG1 VAL A 98 3506 3694 6924 -372 582 858 C ATOM 785 CG2 VAL A 98 2.938 39.690 14.875 1.00 35.82 C ANISOU 785 CG2 VAL A 98 3552 3702 6356 -242 811 640 C ATOM 786 N CYS A 99 1.799 43.102 17.578 1.00 38.40 N ANISOU 786 N CYS A 99 4356 3965 6269 -537 -93 554 N ATOM 787 CA CYS A 99 1.758 44.403 18.264 1.00 39.26 C ANISOU 787 CA CYS A 99 4601 3971 6346 -634 -332 539 C ATOM 788 C CYS A 99 2.086 44.299 19.728 1.00 42.76 C ANISOU 788 C CYS A 99 5199 4270 6777 -747 -750 526 C ATOM 789 O CYS A 99 2.788 45.148 20.239 1.00 43.46 O ANISOU 789 O CYS A 99 5274 4180 7060 -863 -1032 585 O ATOM 790 CB CYS A 99 0.413 45.077 18.185 1.00 36.80 C ANISOU 790 CB CYS A 99 4554 3775 5654 -594 -206 403 C ATOM 791 SG CYS A 99 -0.001 45.557 16.510 1.00 37.11 S ANISOU 791 SG CYS A 99 4471 3955 5675 -500 183 448 S ATOM 792 N GLU A 100 1.534 43.342 20.432 1.00 40.57 N ANISOU 792 N GLU A 100 5109 4056 6248 -725 -811 450 N ATOM 793 CA GLU A 100 1.537 43.426 21.866 1.00 43.80 C ANISOU 793 CA GLU A 100 5810 4346 6485 -829 -1180 410 C ATOM 794 C GLU A 100 2.764 42.795 22.504 1.00 49.80 C ANISOU 794 C GLU A 100 6412 4947 7564 -927 -1545 566 C ATOM 795 O GLU A 100 2.986 42.956 23.680 1.00 50.21 O ANISOU 795 O GLU A 100 6712 4864 7501 -1046 -1934 565 O ATOM 796 CB GLU A 100 0.257 42.825 22.457 1.00 44.18 C ANISOU 796 CB GLU A 100 6189 4516 6081 -763 -1064 273 C ATOM 797 CG GLU A 100 -0.988 43.674 22.375 1.00 42.42 C ANISOU 797 CG GLU A 100 6211 4363 5544 -707 -840 134 C ATOM 798 CD GLU A 100 -2.200 43.054 23.033 1.00 44.36 C ANISOU 798 CD GLU A 100 6743 4687 5423 -641 -707 39 C ATOM 799 OE1 GLU A 100 -2.234 41.867 23.289 1.00 44.66 O ANISOU 799 OE1 GLU A 100 6761 4777 5432 -617 -718 73 O ATOM 800 OE2 GLU A 100 -3.145 43.755 23.304 1.00 40.94 O ANISOU 800 OE2 GLU A 100 6547 4247 4761 -606 -567 -56 O ATOM 801 N GLU A 101 3.550 42.070 21.732 1.00 51.57 N ANISOU 801 N GLU A 101 6240 5168 8188 -875 -1417 709 N ATOM 802 CA GLU A 101 4.691 41.382 22.299 1.00 55.10 C ANISOU 802 CA GLU A 101 6475 5445 9015 -952 -1747 895 C ATOM 803 C GLU A 101 5.929 41.325 21.480 1.00 58.23 C ANISOU 803 C GLU A 101 6372 5715 10038 -940 -1666 1105 C ATOM 804 O GLU A 101 6.968 41.072 22.014 1.00 66.61 O ANISOU 804 O GLU A 101 7221 6582 11508 -1033 -2010 1297 O ATOM 805 CB GLU A 101 4.352 39.969 22.672 1.00 56.61 C ANISOU 805 CB GLU A 101 6726 5712 9072 -887 -1715 891 C ATOM 806 CG GLU A 101 4.167 39.805 24.157 1.00 61.82 C ANISOU 806 CG GLU A 101 7755 6299 9437 -1000 -2145 880 C ATOM 807 CD GLU A 101 2.741 39.666 24.524 1.00 58.53 C ANISOU 807 CD GLU A 101 7754 6047 8439 -933 -1947 682 C ATOM 808 OE1 GLU A 101 1.988 39.171 23.689 1.00 60.33 O ANISOU 808 OE1 GLU A 101 7902 6443 8579 -798 -1535 599 O ATOM 809 OE2 GLU A 101 2.369 40.045 25.629 1.00 60.28 O ANISOU 809 OE2 GLU A 101 8388 6210 8303 -1017 -2193 617 O ATOM 810 N VAL A 102 5.822 41.528 20.189 1.00 54.24 N ANISOU 810 N VAL A 102 5684 5305 9620 -824 -1206 1090 N ATOM 811 CA VAL A 102 6.984 41.553 19.358 1.00 53.27 C ANISOU 811 CA VAL A 102 5107 5042 10091 -795 -1039 1299 C ATOM 812 C VAL A 102 7.440 42.984 19.121 1.00 56.57 C ANISOU 812 C VAL A 102 5423 5346 10724 -883 -1117 1374 C ATOM 813 O VAL A 102 8.496 43.349 19.583 1.00 59.88 O ANISOU 813 O VAL A 102 5600 5531 11622 -1005 -1460 1567 O ATOM 814 CB VAL A 102 6.742 40.807 18.077 1.00 52.05 C ANISOU 814 CB VAL A 102 4838 5020 9919 -616 -468 1260 C ATOM 815 CG1 VAL A 102 7.902 40.969 17.137 1.00 51.32 C ANISOU 815 CG1 VAL A 102 4317 4769 10413 -566 -190 1476 C ATOM 816 CG2 VAL A 102 6.500 39.357 18.393 1.00 49.66 C ANISOU 816 CG2 VAL A 102 4577 4760 9530 -551 -446 1217 C ATOM 817 N LEU A 103 6.621 43.783 18.433 1.00 55.10 N ANISOU 817 N LEU A 103 5419 5309 10207 -829 -834 1238 N ATOM 818 CA LEU A 103 6.878 45.194 18.199 1.00 52.93 C ANISOU 818 CA LEU A 103 5094 4936 10083 -905 -885 1292 C ATOM 819 C LEU A 103 7.057 46.001 19.486 1.00 56.34 C ANISOU 819 C LEU A 103 5711 5190 10505 -1095 -1455 1267 C ATOM 820 O LEU A 103 6.527 45.701 20.542 1.00 56.45 O ANISOU 820 O LEU A 103 6064 5227 10157 -1152 -1746 1131 O ATOM 821 CB LEU A 103 5.762 45.820 17.359 1.00 47.54 C ANISOU 821 CB LEU A 103 4635 4458 8971 -811 -520 1140 C ATOM 822 CG LEU A 103 5.457 45.171 16.013 1.00 47.22 C ANISOU 822 CG LEU A 103 4519 4592 8832 -645 14 1137 C ATOM 823 CD1 LEU A 103 4.631 46.117 15.153 1.00 44.06 C ANISOU 823 CD1 LEU A 103 4276 4325 8139 -596 273 1074 C ATOM 824 CD2 LEU A 103 6.735 44.780 15.286 1.00 50.67 C ANISOU 824 CD2 LEU A 103 4541 4884 9827 -597 248 1365 C ATOM 825 N CYS A 104 7.805 47.070 19.354 1.00 61.39 N ANISOU 825 N CYS A 104 6153 5634 11538 -1196 -1593 1401 N ATOM 826 CA CYS A 104 8.017 48.034 20.393 1.00 66.36 C ANISOU 826 CA CYS A 104 6973 6057 12182 -1390 -2115 1368 C ATOM 827 C CYS A 104 6.667 48.553 20.928 1.00 61.93 C ANISOU 827 C CYS A 104 6967 5625 10939 -1381 -2117 1076 C ATOM 828 O CYS A 104 5.780 48.969 20.152 1.00 55.30 O ANISOU 828 O CYS A 104 6221 4957 9834 -1260 -1708 972 O ATOM 829 CB CYS A 104 8.831 49.111 19.708 1.00 76.64 C ANISOU 829 CB CYS A 104 7927 7176 14015 -1446 -2060 1556 C ATOM 830 SG CYS A 104 8.514 48.840 17.924 1.00 87.95 S ANISOU 830 SG CYS A 104 9120 8847 15450 -1202 -1256 1619 S ATOM 831 N PRO A 105 6.512 48.564 22.263 1.00 64.72 N ANISOU 831 N PRO A 105 7701 5872 11019 -1511 -2574 958 N ATOM 832 CA PRO A 105 5.212 48.834 22.888 1.00 63.68 C ANISOU 832 CA PRO A 105 8117 5843 10235 -1477 -2515 688 C ATOM 833 C PRO A 105 4.800 50.322 22.887 1.00 66.46 C ANISOU 833 C PRO A 105 8684 6082 10486 -1525 -2499 566 C ATOM 834 O PRO A 105 5.655 51.196 22.691 1.00 74.61 O ANISOU 834 O PRO A 105 9497 6905 11945 -1640 -2691 685 O ATOM 835 CB PRO A 105 5.414 48.326 24.325 1.00 65.87 C ANISOU 835 CB PRO A 105 8735 5995 10299 -1613 -3018 643 C ATOM 836 CG PRO A 105 6.917 48.269 24.541 1.00 71.25 C ANISOU 836 CG PRO A 105 9059 6431 11582 -1781 -3492 892 C ATOM 837 CD PRO A 105 7.607 48.643 23.251 1.00 71.11 C ANISOU 837 CD PRO A 105 8470 6394 12154 -1724 -3203 1087 C ATOM 838 N GLY A 106 3.506 50.587 23.107 1.00 61.86 N ANISOU 838 N GLY A 106 8500 5613 9391 -1433 -2261 350 N ATOM 839 CA GLY A 106 2.910 51.927 23.143 1.00 59.07 C ANISOU 839 CA GLY A 106 8390 5152 8904 -1443 -2175 215 C ATOM 840 C GLY A 106 3.386 52.885 22.063 1.00 58.45 C ANISOU 840 C GLY A 106 7935 5011 9260 -1444 -2028 358 C ATOM 841 O GLY A 106 3.372 54.080 22.267 1.00 63.41 O ANISOU 841 O GLY A 106 8707 5442 9945 -1522 -2131 296 O ATOM 842 N SER A 107 3.806 52.357 20.918 1.00 58.28 N ANISOU 842 N SER A 107 7461 5143 9539 -1355 -1764 550 N ATOM 843 CA SER A 107 4.331 53.209 19.854 1.00 59.40 C ANISOU 843 CA SER A 107 7248 5223 10099 -1350 -1588 724 C ATOM 844 C SER A 107 3.859 52.805 18.459 1.00 54.89 C ANISOU 844 C SER A 107 6452 4920 9483 -1165 -1062 814 C ATOM 845 O SER A 107 3.650 51.626 18.177 1.00 54.04 O ANISOU 845 O SER A 107 6296 5010 9225 -1066 -890 811 O ATOM 846 CB SER A 107 5.861 53.233 19.899 1.00 62.60 C ANISOU 846 CB SER A 107 7274 5401 11109 -1494 -1898 950 C ATOM 847 OG SER A 107 6.331 53.286 21.235 1.00 71.14 O ANISOU 847 OG SER A 107 8584 6252 12192 -1681 -2466 879 O ATOM 848 N TRP A 108 3.701 53.801 17.591 1.00 52.88 N ANISOU 848 N TRP A 108 6087 4652 9352 -1128 -829 896 N ATOM 849 CA TRP A 108 3.334 53.570 16.207 1.00 50.85 C ANISOU 849 CA TRP A 108 5659 4617 9042 -977 -371 1006 C ATOM 850 C TRP A 108 4.558 53.651 15.345 1.00 53.72 C ANISOU 850 C TRP A 108 5610 4892 9907 -991 -239 1270 C ATOM 851 O TRP A 108 4.751 54.626 14.588 1.00 55.59 O ANISOU 851 O TRP A 108 5703 5059 10360 -988 -70 1418 O ATOM 852 CB TRP A 108 2.299 54.590 15.750 1.00 48.90 C ANISOU 852 CB TRP A 108 5572 4418 8592 -915 -177 964 C ATOM 853 CG TRP A 108 1.553 54.177 14.504 1.00 48.65 C ANISOU 853 CG TRP A 108 5506 4652 8326 -764 220 1026 C ATOM 854 CD1 TRP A 108 1.389 54.907 13.330 1.00 51.18 C ANISOU 854 CD1 TRP A 108 5720 5020 8708 -707 488 1189 C ATOM 855 CD2 TRP A 108 0.841 52.912 14.266 1.00 46.45 C ANISOU 855 CD2 TRP A 108 5332 4623 7696 -663 369 935 C ATOM 856 NE1 TRP A 108 0.649 54.203 12.414 1.00 49.78 N ANISOU 856 NE1 TRP A 108 5603 5095 8216 -590 753 1199 N ATOM 857 CE2 TRP A 108 0.289 53.001 12.912 1.00 46.37 C ANISOU 857 CE2 TRP A 108 5288 4786 7542 -562 693 1042 C ATOM 858 CE3 TRP A 108 0.615 51.764 15.010 1.00 44.63 C ANISOU 858 CE3 TRP A 108 5224 4469 7265 -654 253 791 C ATOM 859 CZ2 TRP A 108 -0.450 51.974 12.353 1.00 43.43 C ANISOU 859 CZ2 TRP A 108 5015 4641 6847 -472 856 987 C ATOM 860 CZ3 TRP A 108 -0.133 50.735 14.433 1.00 40.27 C ANISOU 860 CZ3 TRP A 108 4733 4146 6422 -551 457 744 C ATOM 861 CH2 TRP A 108 -0.651 50.840 13.137 1.00 41.97 C ANISOU 861 CH2 TRP A 108 4923 4513 6510 -469 736 830 C ATOM 862 N THR A 109 5.405 52.633 15.451 1.00 53.02 N ANISOU 862 N THR A 109 5313 4786 10044 -1000 -290 1353 N ATOM 863 CA THR A 109 6.693 52.600 14.751 1.00 57.08 C ANISOU 863 CA THR A 109 5392 5166 11128 -1007 -145 1629 C ATOM 864 C THR A 109 6.462 52.239 13.318 1.00 57.60 C ANISOU 864 C THR A 109 5385 5431 11069 -840 411 1723 C ATOM 865 O THR A 109 5.329 51.904 12.928 1.00 54.26 O ANISOU 865 O THR A 109 5240 5253 10125 -738 602 1570 O ATOM 866 CB THR A 109 7.658 51.566 15.344 1.00 57.99 C ANISOU 866 CB THR A 109 5289 5173 11573 -1057 -363 1707 C ATOM 867 OG1 THR A 109 7.203 50.271 14.982 1.00 55.06 O ANISOU 867 OG1 THR A 109 4999 5031 10891 -917 -94 1622 O ATOM 868 CG2 THR A 109 7.691 51.670 16.871 1.00 60.18 C ANISOU 868 CG2 THR A 109 5772 5296 11797 -1225 -965 1572 C ATOM 869 N GLU A 110 7.548 52.261 12.564 1.00 61.69 N ANISOU 869 N GLU A 110 5540 5825 12073 -817 660 1983 N ATOM 870 CA GLU A 110 7.528 51.980 11.143 1.00 65.26 C ANISOU 870 CA GLU A 110 5948 6416 12433 -664 1227 2103 C ATOM 871 C GLU A 110 7.200 50.533 10.838 1.00 62.33 C ANISOU 871 C GLU A 110 5704 6238 11741 -542 1451 1980 C ATOM 872 O GLU A 110 6.653 50.263 9.785 1.00 60.74 O ANISOU 872 O GLU A 110 5680 6217 11180 -424 1839 1958 O ATOM 873 CB GLU A 110 8.876 52.333 10.525 1.00 73.38 C ANISOU 873 CB GLU A 110 6543 7212 14125 -666 1474 2431 C ATOM 874 CG GLU A 110 9.319 53.778 10.811 1.00 83.00 C ANISOU 874 CG GLU A 110 7585 8192 15760 -804 1236 2582 C ATOM 875 CD GLU A 110 8.449 54.845 10.109 1.00 88.96 C ANISOU 875 CD GLU A 110 8570 9059 16174 -770 1420 2574 C ATOM 876 OE1 GLU A 110 8.436 54.843 8.849 1.00 97.36 O ANISOU 876 OE1 GLU A 110 9633 10224 17134 -645 1926 2725 O ATOM 877 OE2 GLU A 110 7.793 55.692 10.796 1.00 82.58 O ANISOU 877 OE2 GLU A 110 7955 8217 15204 -863 1074 2430 O ATOM 878 N ASP A 111 7.584 49.623 11.737 1.00 60.42 N ANISOU 878 N ASP A 111 5377 5931 11648 -580 1191 1918 N ATOM 879 CA ASP A 111 7.218 48.212 11.672 1.00 60.31 C ANISOU 879 CA ASP A 111 5495 6073 11347 -482 1325 1775 C ATOM 880 C ASP A 111 5.730 47.978 11.911 1.00 55.68 C ANISOU 880 C ASP A 111 5329 5735 10091 -461 1218 1502 C ATOM 881 O ASP A 111 5.156 47.076 11.296 1.00 51.61 O ANISOU 881 O ASP A 111 4983 5392 9235 -357 1474 1397 O ATOM 882 CB ASP A 111 7.951 47.400 12.718 1.00 63.71 C ANISOU 882 CB ASP A 111 5729 6353 12125 -546 1000 1799 C ATOM 883 CG ASP A 111 9.352 47.082 12.319 1.00 72.23 C ANISOU 883 CG ASP A 111 6357 7206 13880 -513 1214 2074 C ATOM 884 OD1 ASP A 111 9.699 47.307 11.136 1.00 76.87 O ANISOU 884 OD1 ASP A 111 6832 7779 14597 -411 1717 2220 O ATOM 885 OD2 ASP A 111 10.105 46.607 13.198 1.00 73.10 O ANISOU 885 OD2 ASP A 111 6229 7138 14406 -590 884 2163 O ATOM 886 N HIS A 112 5.127 48.753 12.816 1.00 50.65 N ANISOU 886 N HIS A 112 4859 5086 9299 -560 850 1392 N ATOM 887 CA HIS A 112 3.672 48.768 12.897 1.00 47.95 C ANISOU 887 CA HIS A 112 4872 4949 8397 -525 828 1186 C ATOM 888 C HIS A 112 3.022 49.051 11.587 1.00 49.50 C ANISOU 888 C HIS A 112 5177 5306 8325 -432 1186 1218 C ATOM 889 O HIS A 112 2.035 48.393 11.225 1.00 46.76 O ANISOU 889 O HIS A 112 5049 5150 7567 -365 1290 1089 O ATOM 890 CB HIS A 112 3.194 49.790 13.865 1.00 45.95 C ANISOU 890 CB HIS A 112 4774 4613 8073 -623 497 1098 C ATOM 891 CG HIS A 112 3.442 49.428 15.292 1.00 45.63 C ANISOU 891 CG HIS A 112 4803 4454 8081 -721 92 1001 C ATOM 892 ND1 HIS A 112 4.641 49.588 15.873 1.00 48.02 N ANISOU 892 ND1 HIS A 112 4889 4529 8828 -833 -180 1124 N ATOM 893 CD2 HIS A 112 2.572 48.959 16.278 1.00 42.17 C ANISOU 893 CD2 HIS A 112 4661 4085 7276 -730 -99 805 C ATOM 894 CE1 HIS A 112 4.550 49.209 17.174 1.00 49.59 C ANISOU 894 CE1 HIS A 112 5277 4663 8903 -918 -563 1003 C ATOM 895 NE2 HIS A 112 3.274 48.840 17.415 1.00 44.35 N ANISOU 895 NE2 HIS A 112 4940 4184 7726 -847 -480 806 N ATOM 896 N GLU A 113 3.576 50.014 10.851 1.00 51.93 N ANISOU 896 N GLU A 113 5336 5524 8872 -436 1360 1408 N ATOM 897 CA GLU A 113 3.054 50.418 9.541 1.00 53.19 C ANISOU 897 CA GLU A 113 5617 5816 8779 -359 1690 1487 C ATOM 898 C GLU A 113 3.198 49.305 8.550 1.00 50.28 C ANISOU 898 C GLU A 113 5310 5557 8237 -256 2047 1491 C ATOM 899 O GLU A 113 2.357 49.116 7.725 1.00 51.02 O ANISOU 899 O GLU A 113 5651 5820 7914 -201 2200 1442 O ATOM 900 CB GLU A 113 3.713 51.721 9.044 1.00 57.59 C ANISOU 900 CB GLU A 113 5991 6221 9671 -392 1802 1722 C ATOM 901 CG GLU A 113 3.037 52.968 9.652 1.00 68.64 C ANISOU 901 CG GLU A 113 7475 7563 11041 -469 1521 1680 C ATOM 902 CD GLU A 113 3.839 54.286 9.522 1.00 80.23 C ANISOU 902 CD GLU A 113 8714 8806 12964 -538 1521 1897 C ATOM 903 OE1 GLU A 113 5.055 54.265 9.164 1.00 87.63 O ANISOU 903 OE1 GLU A 113 9365 9597 14334 -546 1686 2099 O ATOM 904 OE2 GLU A 113 3.252 55.370 9.790 1.00 81.18 O ANISOU 904 OE2 GLU A 113 8923 8868 13052 -582 1368 1879 O ATOM 905 N LEU A 114 4.261 48.536 8.687 1.00 52.94 N ANISOU 905 N LEU A 114 5431 5773 8910 -235 2154 1547 N ATOM 906 CA LEU A 114 4.549 47.362 7.852 1.00 54.31 C ANISOU 906 CA LEU A 114 5660 5993 8982 -127 2530 1532 C ATOM 907 C LEU A 114 3.604 46.192 8.175 1.00 49.70 C ANISOU 907 C LEU A 114 5324 5571 7990 -105 2397 1281 C ATOM 908 O LEU A 114 3.022 45.530 7.288 1.00 49.22 O ANISOU 908 O LEU A 114 5526 5644 7533 -38 2623 1187 O ATOM 909 CB LEU A 114 5.967 46.942 8.186 1.00 56.86 C ANISOU 909 CB LEU A 114 5608 6088 9909 -119 2616 1681 C ATOM 910 CG LEU A 114 6.778 46.361 7.071 1.00 62.61 C ANISOU 910 CG LEU A 114 6263 6736 10788 6 3175 1812 C ATOM 911 CD1 LEU A 114 7.148 47.493 6.089 1.00 64.68 C ANISOU 911 CD1 LEU A 114 6484 6943 11148 28 3500 2044 C ATOM 912 CD2 LEU A 114 7.975 45.714 7.768 1.00 66.59 C ANISOU 912 CD2 LEU A 114 6364 7010 11927 5 3131 1925 C ATOM 913 N LEU A 115 3.435 45.949 9.467 1.00 45.87 N ANISOU 913 N LEU A 115 4779 5058 7592 -174 2010 1175 N ATOM 914 CA LEU A 115 2.380 45.023 9.948 1.00 43.58 C ANISOU 914 CA LEU A 115 4718 4914 6928 -169 1837 954 C ATOM 915 C LEU A 115 0.995 45.404 9.371 1.00 39.84 C ANISOU 915 C LEU A 115 4539 4630 5970 -162 1836 865 C ATOM 916 O LEU A 115 0.278 44.555 8.814 1.00 41.44 O ANISOU 916 O LEU A 115 4948 4957 5839 -120 1931 749 O ATOM 917 CB LEU A 115 2.365 44.991 11.480 1.00 40.73 C ANISOU 917 CB LEU A 115 4291 4481 6703 -253 1421 888 C ATOM 918 CG LEU A 115 1.347 43.992 12.040 1.00 38.96 C ANISOU 918 CG LEU A 115 4274 4382 6146 -242 1281 694 C ATOM 919 CD1 LEU A 115 1.634 42.556 11.576 1.00 38.67 C ANISOU 919 CD1 LEU A 115 4222 4357 6112 -167 1492 647 C ATOM 920 CD2 LEU A 115 1.328 44.162 13.556 1.00 38.22 C ANISOU 920 CD2 LEU A 115 4182 4206 6135 -328 894 650 C ATOM 921 N ASN A 116 0.659 46.694 9.479 1.00 41.40 N ANISOU 921 N ASN A 116 4737 4819 6172 -208 1717 936 N ATOM 922 CA ASN A 116 -0.585 47.237 8.927 1.00 41.09 C ANISOU 922 CA ASN A 116 4914 4923 5776 -203 1699 914 C ATOM 923 C ASN A 116 -0.776 46.875 7.470 1.00 43.99 C ANISOU 923 C ASN A 116 5457 5397 5859 -147 1982 955 C ATOM 924 O ASN A 116 -1.795 46.276 7.131 1.00 43.11 O ANISOU 924 O ASN A 116 5561 5417 5402 -140 1927 847 O ATOM 925 CB ASN A 116 -0.635 48.727 9.143 1.00 42.94 C ANISOU 925 CB ASN A 116 5077 5078 6161 -248 1595 1027 C ATOM 926 CG ASN A 116 -2.056 49.340 8.935 1.00 43.97 C ANISOU 926 CG ASN A 116 5384 5317 6004 -246 1496 1008 C ATOM 927 OD1 ASN A 116 -2.996 48.711 8.498 1.00 46.91 O ANISOU 927 OD1 ASN A 116 5921 5830 6074 -221 1495 939 O ATOM 928 ND2 ASN A 116 -2.170 50.591 9.228 1.00 47.74 N ANISOU 928 ND2 ASN A 116 5806 5703 6631 -277 1409 1087 N ATOM 929 N ASP A 117 0.237 47.200 6.631 1.00 48.95 N ANISOU 929 N ASP A 117 6007 5947 6646 -112 2287 1118 N ATOM 930 CA ASP A 117 0.214 47.023 5.190 1.00 49.11 C ANISOU 930 CA ASP A 117 6252 6036 6371 -58 2609 1184 C ATOM 931 C ASP A 117 -0.003 45.605 4.813 1.00 46.07 C ANISOU 931 C ASP A 117 6076 5711 5715 -18 2718 1013 C ATOM 932 O ASP A 117 -0.898 45.279 4.013 1.00 46.38 O ANISOU 932 O ASP A 117 6436 5876 5312 -23 2709 943 O ATOM 933 CB ASP A 117 1.546 47.478 4.546 1.00 55.54 C ANISOU 933 CB ASP A 117 6908 6706 7490 -11 2990 1398 C ATOM 934 CG ASP A 117 1.699 48.977 4.524 1.00 62.87 C ANISOU 934 CG ASP A 117 7690 7570 8626 -53 2942 1604 C ATOM 935 OD1 ASP A 117 0.758 49.658 4.999 1.00 65.08 O ANISOU 935 OD1 ASP A 117 8013 7916 8800 -110 2624 1566 O ATOM 936 OD2 ASP A 117 2.750 49.476 4.033 1.00 67.52 O ANISOU 936 OD2 ASP A 117 8114 8024 9519 -23 3244 1815 O ATOM 937 N CYS A 118 0.875 44.766 5.352 1.00 44.52 N ANISOU 937 N CYS A 118 5697 5403 5817 17 2812 960 N ATOM 938 CA CYS A 118 0.797 43.324 5.180 1.00 47.76 C ANISOU 938 CA CYS A 118 6257 5822 6066 60 2918 785 C ATOM 939 C CYS A 118 -0.630 42.813 5.520 1.00 45.77 C ANISOU 939 C CYS A 118 6211 5719 5459 5 2578 598 C ATOM 940 O CYS A 118 -1.309 42.181 4.624 1.00 44.75 O ANISOU 940 O CYS A 118 6410 5671 4921 7 2639 492 O ATOM 941 CB CYS A 118 1.835 42.628 6.072 1.00 50.84 C ANISOU 941 CB CYS A 118 6335 6054 6929 89 2944 784 C ATOM 942 SG CYS A 118 1.636 40.818 6.144 1.00 60.30 S ANISOU 942 SG CYS A 118 7674 7240 7997 136 3002 558 S ATOM 943 N MET A 119 -1.119 43.142 6.743 1.00 38.68 N ANISOU 943 N MET A 119 5151 4841 4703 -51 2227 569 N ATOM 944 CA MET A 119 -2.473 42.642 7.121 1.00 36.85 C ANISOU 944 CA MET A 119 5069 4723 4208 -93 1950 423 C ATOM 945 C MET A 119 -3.512 43.224 6.203 1.00 36.91 C ANISOU 945 C MET A 119 5301 4848 3876 -124 1887 467 C ATOM 946 O MET A 119 -4.414 42.504 5.771 1.00 38.17 O ANISOU 946 O MET A 119 5669 5081 3752 -149 1790 364 O ATOM 947 CB MET A 119 -2.840 42.916 8.585 1.00 33.43 C ANISOU 947 CB MET A 119 4471 4270 3959 -132 1654 395 C ATOM 948 CG MET A 119 -2.069 42.046 9.557 1.00 33.04 C ANISOU 948 CG MET A 119 4265 4121 4168 -121 1619 336 C ATOM 949 SD MET A 119 -2.494 42.484 11.273 1.00 33.58 S ANISOU 949 SD MET A 119 4248 4153 4358 -177 1276 310 S ATOM 950 CE MET A 119 -4.166 41.813 11.312 1.00 29.94 C ANISOU 950 CE MET A 119 3979 3821 3576 -180 1165 184 C ATOM 951 N THR A 120 -3.396 44.513 5.901 1.00 37.70 N ANISOU 951 N THR A 120 5351 4946 4027 -131 1914 633 N ATOM 952 CA THR A 120 -4.356 45.188 5.035 1.00 39.52 C ANISOU 952 CA THR A 120 5769 5272 3973 -164 1825 724 C ATOM 953 C THR A 120 -4.291 44.666 3.603 1.00 45.16 C ANISOU 953 C THR A 120 6809 6031 4317 -156 2020 723 C ATOM 954 O THR A 120 -5.311 44.577 2.919 1.00 47.20 O ANISOU 954 O THR A 120 7309 6377 4248 -207 1848 722 O ATOM 955 CB THR A 120 -4.132 46.712 5.025 1.00 40.13 C ANISOU 955 CB THR A 120 5709 5310 4227 -168 1836 923 C ATOM 956 OG1 THR A 120 -4.204 47.217 6.364 1.00 40.91 O ANISOU 956 OG1 THR A 120 5577 5339 4629 -183 1653 896 O ATOM 957 CG2 THR A 120 -5.186 47.399 4.171 1.00 39.45 C ANISOU 957 CG2 THR A 120 5796 5313 3880 -202 1709 1049 C ATOM 958 N HIS A 121 -3.088 44.324 3.154 1.00 49.48 N ANISOU 958 N HIS A 121 7376 6496 4927 -94 2380 732 N ATOM 959 CA HIS A 121 -2.889 43.833 1.804 1.00 56.42 C ANISOU 959 CA HIS A 121 8625 7381 5431 -71 2652 719 C ATOM 960 C HIS A 121 -3.369 42.419 1.653 1.00 57.07 C ANISOU 960 C HIS A 121 8947 7475 5262 -88 2587 485 C ATOM 961 O HIS A 121 -3.750 41.988 0.543 1.00 58.91 O ANISOU 961 O HIS A 121 9600 7735 5047 -114 2639 428 O ATOM 962 CB HIS A 121 -1.420 43.932 1.411 1.00 61.71 C ANISOU 962 CB HIS A 121 9215 7920 6312 21 3134 821 C ATOM 963 CG HIS A 121 -0.911 45.350 1.308 1.00 70.70 C ANISOU 963 CG HIS A 121 10160 9024 7678 28 3234 1079 C ATOM 964 ND1 HIS A 121 0.393 45.660 1.423 1.00 72.17 N ANISOU 964 ND1 HIS A 121 10081 9063 8278 92 3561 1215 N ATOM 965 CD2 HIS A 121 -1.584 46.551 1.094 1.00 74.39 C ANISOU 965 CD2 HIS A 121 10648 9569 8050 -26 3031 1240 C ATOM 966 CE1 HIS A 121 0.550 46.991 1.290 1.00 54.71 C ANISOU 966 CE1 HIS A 121 7738 6834 6216 73 3562 1442 C ATOM 967 NE2 HIS A 121 -0.661 47.535 1.088 1.00 77.60 N ANISOU 967 NE2 HIS A 121 10820 9872 8792 5 3246 1452 N ATOM 968 N PHE A 122 -3.359 41.674 2.753 1.00 50.44 N ANISOU 968 N PHE A 122 7875 6598 4690 -82 2460 351 N ATOM 969 CA PHE A 122 -3.775 40.322 2.740 1.00 48.07 C ANISOU 969 CA PHE A 122 7748 6284 4233 -98 2394 139 C ATOM 970 C PHE A 122 -5.278 40.267 2.892 1.00 47.81 C ANISOU 970 C PHE A 122 7801 6356 4008 -199 1957 93 C ATOM 971 O PHE A 122 -5.933 39.528 2.168 1.00 49.63 O ANISOU 971 O PHE A 122 8352 6599 3907 -255 1854 -22 O ATOM 972 CB PHE A 122 -3.056 39.522 3.833 1.00 47.73 C ANISOU 972 CB PHE A 122 7410 6138 4588 -44 2462 52 C ATOM 973 CG PHE A 122 -3.347 38.065 3.765 1.00 50.42 C ANISOU 973 CG PHE A 122 7923 6429 4805 -48 2453 -160 C ATOM 974 CD1 PHE A 122 -4.604 37.589 4.154 1.00 48.51 C ANISOU 974 CD1 PHE A 122 7734 6257 4439 -132 2080 -261 C ATOM 975 CD2 PHE A 122 -2.402 37.161 3.222 1.00 52.90 C ANISOU 975 CD2 PHE A 122 8361 6599 5138 35 2845 -251 C ATOM 976 CE1 PHE A 122 -4.938 36.234 4.051 1.00 50.69 C ANISOU 976 CE1 PHE A 122 8177 6469 4614 -151 2046 -455 C ATOM 977 CE2 PHE A 122 -2.713 35.801 3.155 1.00 53.84 C ANISOU 977 CE2 PHE A 122 8658 6647 5152 28 2830 -462 C ATOM 978 CZ PHE A 122 -3.979 35.326 3.576 1.00 53.73 C ANISOU 978 CZ PHE A 122 8692 6709 5013 -73 2412 -568 C ATOM 979 N PHE A 123 -5.831 41.030 3.856 1.00 43.54 N ANISOU 979 N PHE A 123 6977 5864 3702 -223 1702 186 N ATOM 980 CA PHE A 123 -7.277 41.004 4.078 1.00 42.36 C ANISOU 980 CA PHE A 123 6841 5783 3468 -303 1326 180 C ATOM 981 C PHE A 123 -7.960 41.336 2.730 1.00 46.36 C ANISOU 981 C PHE A 123 7676 6351 3587 -374 1207 259 C ATOM 982 O PHE A 123 -8.870 40.625 2.284 1.00 46.23 O ANISOU 982 O PHE A 123 7864 6348 3354 -457 966 181 O ATOM 983 CB PHE A 123 -7.635 42.054 5.126 1.00 38.10 C ANISOU 983 CB PHE A 123 5996 5259 3223 -295 1182 302 C ATOM 984 CG PHE A 123 -9.038 41.990 5.608 1.00 35.24 C ANISOU 984 CG PHE A 123 5562 4925 2902 -347 872 313 C ATOM 985 CD1 PHE A 123 -10.072 42.586 4.912 1.00 36.66 C ANISOU 985 CD1 PHE A 123 5822 5151 2954 -407 657 448 C ATOM 986 CD2 PHE A 123 -9.316 41.338 6.825 1.00 33.77 C ANISOU 986 CD2 PHE A 123 5204 4699 2927 -333 804 216 C ATOM 987 CE1 PHE A 123 -11.372 42.551 5.395 1.00 37.91 C ANISOU 987 CE1 PHE A 123 5850 5303 3249 -447 394 495 C ATOM 988 CE2 PHE A 123 -10.590 41.273 7.317 1.00 32.54 C ANISOU 988 CE2 PHE A 123 4956 4545 2864 -367 583 249 C ATOM 989 CZ PHE A 123 -11.616 41.892 6.627 1.00 35.99 C ANISOU 989 CZ PHE A 123 5427 5014 3235 -419 388 392 C ATOM 990 N ILE A 124 -7.536 42.427 2.105 1.00 47.91 N ANISOU 990 N ILE A 124 7922 6571 3710 -354 1342 432 N ATOM 991 CA ILE A 124 -8.155 42.825 0.836 1.00 55.37 C ANISOU 991 CA ILE A 124 9202 7571 4265 -427 1206 546 C ATOM 992 C ILE A 124 -7.847 41.882 -0.336 1.00 57.12 C ANISOU 992 C ILE A 124 9907 7764 4033 -451 1357 409 C ATOM 993 O ILE A 124 -8.786 41.356 -0.922 1.00 58.14 O ANISOU 993 O ILE A 124 10317 7910 3865 -558 1049 353 O ATOM 994 CB ILE A 124 -7.916 44.295 0.478 1.00 58.45 C ANISOU 994 CB ILE A 124 9525 7988 4695 -405 1283 801 C ATOM 995 CG1 ILE A 124 -8.437 45.182 1.632 1.00 59.58 C ANISOU 995 CG1 ILE A 124 9249 8129 5259 -393 1093 905 C ATOM 996 CG2 ILE A 124 -8.636 44.615 -0.824 1.00 63.03 C ANISOU 996 CG2 ILE A 124 10481 8623 4844 -493 1086 938 C ATOM 997 CD1 ILE A 124 -8.204 46.665 1.480 1.00 57.80 C ANISOU 997 CD1 ILE A 124 8898 7895 5169 -367 1161 1145 C ATOM 998 N GLU A 125 -6.572 41.623 -0.629 1.00 57.99 N ANISOU 998 N GLU A 125 10110 7803 4119 -356 1819 353 N ATOM 999 CA GLU A 125 -6.223 40.763 -1.766 1.00 65.24 C ANISOU 999 CA GLU A 125 11541 8659 4588 -359 2050 211 C ATOM 1000 C GLU A 125 -6.941 39.426 -1.661 1.00 66.21 C ANISOU 1000 C GLU A 125 11832 8742 4582 -435 1796 -37 C ATOM 1001 O GLU A 125 -7.359 38.893 -2.678 1.00 66.80 O ANISOU 1001 O GLU A 125 12407 8790 4183 -518 1700 -136 O ATOM 1002 CB GLU A 125 -4.712 40.592 -1.936 1.00 69.03 C ANISOU 1002 CB GLU A 125 12016 9026 5186 -219 2653 193 C ATOM 1003 CG GLU A 125 -4.085 41.680 -2.814 1.00 77.47 C ANISOU 1003 CG GLU A 125 13233 10101 6101 -173 2968 426 C ATOM 1004 CD GLU A 125 -2.864 42.391 -2.182 1.00 78.41 C ANISOU 1004 CD GLU A 125 12886 10150 6755 -56 3329 588 C ATOM 1005 OE1 GLU A 125 -1.950 41.681 -1.694 1.00 83.22 O ANISOU 1005 OE1 GLU A 125 13299 10639 7683 34 3627 486 O ATOM 1006 OE2 GLU A 125 -2.791 43.667 -2.173 1.00 75.70 O ANISOU 1006 OE2 GLU A 125 12359 9852 6553 -59 3301 832 O ATOM 1007 N ASN A 126 -7.161 38.926 -0.439 1.00 62.10 N ANISOU 1007 N ASN A 126 10919 8210 4467 -423 1649 -124 N ATOM 1008 CA ASN A 126 -7.887 37.666 -0.255 1.00 59.80 C ANISOU 1008 CA ASN A 126 10734 7867 4123 -499 1397 -334 C ATOM 1009 C ASN A 126 -9.378 37.815 -0.109 1.00 57.78 C ANISOU 1009 C ASN A 126 10417 7677 3859 -636 848 -264 C ATOM 1010 O ASN A 126 -10.080 36.848 0.139 1.00 59.24 O ANISOU 1010 O ASN A 126 10619 7810 4080 -711 598 -401 O ATOM 1011 CB ASN A 126 -7.305 36.814 0.889 1.00 60.17 C ANISOU 1011 CB ASN A 126 10448 7832 4580 -415 1563 -467 C ATOM 1012 CG ASN A 126 -5.970 36.197 0.510 1.00 67.54 C ANISOU 1012 CG ASN A 126 11526 8635 5499 -299 2077 -581 C ATOM 1013 OD1 ASN A 126 -5.910 35.021 0.081 1.00 70.08 O ANISOU 1013 OD1 ASN A 126 12140 8839 5649 -307 2174 -795 O ATOM 1014 ND2 ASN A 126 -4.896 37.008 0.565 1.00 66.45 N ANISOU 1014 ND2 ASN A 126 11205 8491 5550 -193 2426 -429 N ATOM 1015 N ASN A 127 -9.882 39.021 -0.262 1.00 58.32 N ANISOU 1015 N ASN A 127 10389 7838 3931 -668 660 -32 N ATOM 1016 CA ASN A 127 -11.308 39.247 -0.053 1.00 57.23 C ANISOU 1016 CA ASN A 127 10109 7738 3899 -783 158 84 C ATOM 1017 C ASN A 127 -11.823 38.693 1.276 1.00 53.25 C ANISOU 1017 C ASN A 127 9197 7201 3834 -768 35 21 C ATOM 1018 O ASN A 127 -12.878 38.099 1.334 1.00 55.53 O ANISOU 1018 O ASN A 127 9471 7453 4176 -871 -315 -1 O ATOM 1019 CB ASN A 127 -12.093 38.697 -1.247 1.00 64.31 C ANISOU 1019 CB ASN A 127 11479 8602 4355 -942 -190 37 C ATOM 1020 CG ASN A 127 -13.528 39.203 -1.305 1.00 66.89 C ANISOU 1020 CG ASN A 127 11661 8954 4799 -1072 -735 250 C ATOM 1021 OD1 ASN A 127 -13.855 40.283 -0.808 1.00 68.80 O ANISOU 1021 OD1 ASN A 127 11548 9252 5342 -1029 -788 478 O ATOM 1022 ND2 ASN A 127 -14.393 38.409 -1.914 1.00 69.40 N ANISOU 1022 ND2 ASN A 127 12250 9204 4916 -1234 -1150 182 N ATOM 1023 N LEU A 128 -11.073 38.873 2.356 1.00 49.50 N ANISOU 1023 N LEU A 128 8400 6726 3682 -647 313 4 N ATOM 1024 CA LEU A 128 -11.591 38.481 3.707 1.00 47.67 C ANISOU 1024 CA LEU A 128 7806 6465 3841 -627 211 -21 C ATOM 1025 C LEU A 128 -12.879 39.188 4.134 1.00 47.65 C ANISOU 1025 C LEU A 128 7559 6483 4063 -672 -93 168 C ATOM 1026 O LEU A 128 -13.612 38.680 4.976 1.00 46.94 O ANISOU 1026 O LEU A 128 7256 6346 4231 -685 -219 156 O ATOM 1027 CB LEU A 128 -10.522 38.614 4.800 1.00 41.02 C ANISOU 1027 CB LEU A 128 6714 5607 3265 -504 521 -57 C ATOM 1028 CG LEU A 128 -9.422 37.586 4.513 1.00 44.59 C ANISOU 1028 CG LEU A 128 7336 5992 3615 -460 795 -241 C ATOM 1029 CD1 LEU A 128 -8.533 37.472 5.725 1.00 42.92 C ANISOU 1029 CD1 LEU A 128 6838 5737 3731 -365 990 -262 C ATOM 1030 CD2 LEU A 128 -9.940 36.188 4.096 1.00 45.37 C ANISOU 1030 CD2 LEU A 128 7658 6018 3562 -534 661 -422 C ATOM 1031 N MET A 129 -13.143 40.366 3.563 1.00 51.21 N ANISOU 1031 N MET A 129 8028 6984 4447 -688 -178 364 N ATOM 1032 CA MET A 129 -14.369 41.130 3.885 1.00 56.16 C ANISOU 1032 CA MET A 129 8401 7600 5338 -718 -441 579 C ATOM 1033 C MET A 129 -15.558 40.291 3.554 1.00 61.19 C ANISOU 1033 C MET A 129 9071 8183 5995 -844 -817 587 C ATOM 1034 O MET A 129 -16.590 40.412 4.216 1.00 61.24 O ANISOU 1034 O MET A 129 8776 8133 6360 -852 -977 715 O ATOM 1035 CB MET A 129 -14.485 42.430 3.096 1.00 58.92 C ANISOU 1035 CB MET A 129 8804 7992 5589 -731 -514 805 C ATOM 1036 CG MET A 129 -13.932 42.333 1.697 1.00 67.19 C ANISOU 1036 CG MET A 129 10284 9086 6158 -791 -513 783 C ATOM 1037 SD MET A 129 -12.454 43.342 1.607 1.00 77.48 S ANISOU 1037 SD MET A 129 11613 10431 7394 -669 -64 823 S ATOM 1038 CE MET A 129 -11.058 42.226 1.539 1.00 64.13 C ANISOU 1038 CE MET A 129 10137 8719 5512 -610 323 548 C ATOM 1039 N ASN A 130 -15.377 39.417 2.550 1.00 64.95 N ANISOU 1039 N ASN A 130 9925 8652 6102 -940 -932 446 N ATOM 1040 CA ASN A 130 -16.384 38.435 2.131 1.00 71.65 C ANISOU 1040 CA ASN A 130 10876 9419 6927 -1091 -1330 409 C ATOM 1041 C ASN A 130 -16.945 37.493 3.219 1.00 71.59 C ANISOU 1041 C ASN A 130 10572 9325 7306 -1086 -1363 335 C ATOM 1042 O ASN A 130 -18.066 37.016 3.068 1.00 76.88 O ANISOU 1042 O ASN A 130 11164 9907 8140 -1210 -1738 411 O ATOM 1043 CB ASN A 130 -15.813 37.565 1.015 1.00 75.70 C ANISOU 1043 CB ASN A 130 11916 9912 6937 -1172 -1339 193 C ATOM 1044 CG ASN A 130 -16.757 37.426 -0.158 1.00 83.39 C ANISOU 1044 CG ASN A 130 13197 10838 7649 -1368 -1852 275 C ATOM 1045 OD1 ASN A 130 -17.072 36.306 -0.647 1.00 85.98 O ANISOU 1045 OD1 ASN A 130 13808 11065 7796 -1499 -2093 104 O ATOM 1046 ND2 ASN A 130 -17.208 38.573 -0.643 1.00 86.75 N ANISOU 1046 ND2 ASN A 130 13589 11318 8052 -1401 -2053 545 N ATOM 1047 N HIS A 131 -16.192 37.233 4.274 1.00 69.03 N ANISOU 1047 N HIS A 131 10085 9008 7135 -956 -1001 213 N ATOM 1048 CA HIS A 131 -16.574 36.256 5.271 1.00 68.38 C ANISOU 1048 CA HIS A 131 9786 8841 7354 -945 -987 137 C ATOM 1049 C HIS A 131 -16.681 36.790 6.674 1.00 63.71 C ANISOU 1049 C HIS A 131 8827 8251 7129 -820 -770 240 C ATOM 1050 O HIS A 131 -16.365 36.101 7.636 1.00 62.49 O ANISOU 1050 O HIS A 131 8572 8059 7114 -758 -587 138 O ATOM 1051 CB HIS A 131 -15.564 35.147 5.243 1.00 68.82 C ANISOU 1051 CB HIS A 131 10059 8869 7219 -920 -777 -125 C ATOM 1052 CG HIS A 131 -15.702 34.226 4.082 1.00 76.71 C ANISOU 1052 CG HIS A 131 11435 9797 7913 -1055 -996 -276 C ATOM 1053 ND1 HIS A 131 -15.000 34.375 2.969 1.00 81.65 N ANISOU 1053 ND1 HIS A 131 12460 10454 8108 -1072 -919 -368 N ATOM 1054 CD2 HIS A 131 -16.485 33.106 3.903 1.00 80.29 C ANISOU 1054 CD2 HIS A 131 11946 10124 8437 -1184 -1288 -357 C ATOM 1055 CE1 HIS A 131 -15.314 33.409 2.114 1.00 81.83 C ANISOU 1055 CE1 HIS A 131 12830 10374 7889 -1206 -1149 -522 C ATOM 1056 NE2 HIS A 131 -16.216 32.627 2.692 1.00 84.97 N ANISOU 1056 NE2 HIS A 131 13004 10670 8608 -1281 -1396 -519 N ATOM 1057 N PHE A 132 -17.125 38.018 6.825 1.00 62.60 N ANISOU 1057 N PHE A 132 8513 8135 7139 -781 -782 445 N ATOM 1058 CA PHE A 132 -17.074 38.668 8.109 1.00 60.71 C ANISOU 1058 CA PHE A 132 8020 7881 7167 -652 -524 511 C ATOM 1059 C PHE A 132 -17.901 39.917 8.087 1.00 61.94 C ANISOU 1059 C PHE A 132 7982 8011 7540 -631 -597 756 C ATOM 1060 O PHE A 132 -17.383 40.983 7.868 1.00 60.73 O ANISOU 1060 O PHE A 132 7875 7911 7290 -583 -494 809 O ATOM 1061 CB PHE A 132 -15.616 39.025 8.439 1.00 55.93 C ANISOU 1061 CB PHE A 132 7531 7344 6375 -557 -218 379 C ATOM 1062 CG PHE A 132 -15.372 39.274 9.888 1.00 51.72 C ANISOU 1062 CG PHE A 132 6835 6772 6044 -449 19 369 C ATOM 1063 CD1 PHE A 132 -15.915 40.361 10.509 1.00 50.75 C ANISOU 1063 CD1 PHE A 132 6549 6607 6127 -387 91 516 C ATOM 1064 CD2 PHE A 132 -14.623 38.404 10.628 1.00 50.96 C ANISOU 1064 CD2 PHE A 132 6777 6662 5925 -414 163 217 C ATOM 1065 CE1 PHE A 132 -15.709 40.581 11.834 1.00 49.48 C ANISOU 1065 CE1 PHE A 132 6323 6389 6088 -297 307 487 C ATOM 1066 CE2 PHE A 132 -14.414 38.615 11.961 1.00 50.57 C ANISOU 1066 CE2 PHE A 132 6639 6568 6008 -333 337 215 C ATOM 1067 CZ PHE A 132 -14.958 39.705 12.567 1.00 48.77 C ANISOU 1067 CZ PHE A 132 6306 6297 5927 -277 412 338 C ATOM 1068 N PRO A 133 -19.195 39.812 8.313 1.00 65.53 N ANISOU 1068 N PRO A 133 8195 8364 8341 -665 -763 928 N ATOM 1069 CA PRO A 133 -19.982 41.042 8.190 1.00 63.85 C ANISOU 1069 CA PRO A 133 7778 8101 8381 -638 -829 1189 C ATOM 1070 C PRO A 133 -19.921 41.847 9.446 1.00 62.83 C ANISOU 1070 C PRO A 133 7478 7912 8484 -481 -464 1224 C ATOM 1071 O PRO A 133 -19.541 41.318 10.453 1.00 61.82 O ANISOU 1071 O PRO A 133 7364 7767 8358 -415 -227 1082 O ATOM 1072 CB PRO A 133 -21.412 40.547 7.999 1.00 63.32 C ANISOU 1072 CB PRO A 133 7470 7906 8682 -732 -1137 1384 C ATOM 1073 CG PRO A 133 -21.368 39.079 7.948 1.00 66.24 C ANISOU 1073 CG PRO A 133 7949 8263 8955 -823 -1259 1211 C ATOM 1074 CD PRO A 133 -20.192 38.728 8.751 1.00 63.43 C ANISOU 1074 CD PRO A 133 7744 7979 8378 -719 -891 963 C ATOM 1075 N LEU A 134 -20.318 43.106 9.380 1.00 64.60 N ANISOU 1075 N LEU A 134 7565 8085 8896 -427 -430 1418 N ATOM 1076 CA LEU A 134 -20.285 44.007 10.558 1.00 66.58 C ANISOU 1076 CA LEU A 134 7704 8241 9353 -275 -63 1438 C ATOM 1077 C LEU A 134 -21.625 44.736 10.745 1.00 70.61 C ANISOU 1077 C LEU A 134 7891 8576 10363 -221 -52 1727 C ATOM 1078 O LEU A 134 -22.431 44.776 9.819 1.00 71.75 O ANISOU 1078 O LEU A 134 7887 8694 10679 -311 -381 1941 O ATOM 1079 CB LEU A 134 -19.143 45.017 10.417 1.00 59.06 C ANISOU 1079 CB LEU A 134 6931 7362 8146 -231 71 1355 C ATOM 1080 CG LEU A 134 -17.732 44.441 10.404 1.00 55.16 C ANISOU 1080 CG LEU A 134 6700 6997 7260 -255 138 1101 C ATOM 1081 CD1 LEU A 134 -16.774 45.510 9.917 1.00 45.91 C ANISOU 1081 CD1 LEU A 134 5645 5880 5918 -240 197 1102 C ATOM 1082 CD2 LEU A 134 -17.388 43.960 11.805 1.00 50.71 C ANISOU 1082 CD2 LEU A 134 6161 6381 6725 -180 389 941 C ATOM 1083 N GLU A 135 -21.788 45.319 11.908 1.00 77.69 N ANISOU 1083 N GLU A 135 8708 9341 11471 -79 319 1731 N ATOM 1084 CA GLU A 135 -23.014 45.946 12.319 1.00 85.76 C ANISOU 1084 CA GLU A 135 9419 10151 13014 12 462 1986 C ATOM 1085 C GLU A 135 -23.432 47.108 11.472 1.00 88.90 C ANISOU 1085 C GLU A 135 9662 10496 13620 8 300 2231 C ATOM 1086 O GLU A 135 -22.642 47.929 11.064 1.00 88.98 O ANISOU 1086 O GLU A 135 9837 10584 13387 9 289 2177 O ATOM 1087 CB GLU A 135 -22.909 46.402 13.767 1.00 91.45 C ANISOU 1087 CB GLU A 135 10206 10730 13813 177 961 1887 C ATOM 1088 CG GLU A 135 -24.206 46.269 14.550 1.00105.93 C ANISOU 1088 CG GLU A 135 11756 12330 16164 280 1224 2084 C ATOM 1089 CD GLU A 135 -24.291 45.007 15.397 1.00110.24 C ANISOU 1089 CD GLU A 135 12358 12871 16659 284 1374 1973 C ATOM 1090 OE1 GLU A 135 -24.612 45.124 16.587 1.00106.76 O ANISOU 1090 OE1 GLU A 135 11946 12264 16353 422 1814 1966 O ATOM 1091 OE2 GLU A 135 -24.053 43.899 14.881 1.00107.63 O ANISOU 1091 OE2 GLU A 135 12062 12683 16151 153 1072 1897 O ATOM 1092 N ASP A 136 -24.729 47.157 11.250 1.00 95.97 N ANISOU 1092 N ASP A 136 10203 11232 15027 4 177 2534 N ATOM 1093 CA ASP A 136 -25.378 48.208 10.511 1.00103.79 C ANISOU 1093 CA ASP A 136 10963 12122 16351 5 0 2844 C ATOM 1094 C ASP A 136 -24.879 48.200 9.076 1.00105.11 C ANISOU 1094 C ASP A 136 11315 12485 16136 -163 -487 2866 C ATOM 1095 O ASP A 136 -25.720 48.456 8.159 1.00105.81 O ANISOU 1095 O ASP A 136 11191 12512 16501 -252 -875 3181 O ATOM 1096 CB ASP A 136 -25.327 49.549 11.288 1.00105.33 C ANISOU 1096 CB ASP A 136 11116 12145 16759 191 449 2874 C ATOM 1097 CG ASP A 136 -24.195 50.445 10.892 1.00103.36 C ANISOU 1097 CG ASP A 136 11142 12016 16114 186 447 2742 C ATOM 1098 OD1 ASP A 136 -23.975 50.667 9.703 1.00105.63 O ANISOU 1098 OD1 ASP A 136 11474 12429 16233 72 76 2852 O ATOM 1099 OD2 ASP A 136 -23.543 51.000 11.782 1.00 99.85 O ANISOU 1099 OD2 ASP A 136 10877 11517 15545 296 823 2544 O TER 1100 ASP A 136 ATOM 1101 N SER B 2 29.150 68.350 10.728 1.00 66.80 N ANISOU 1101 N SER B 2 6996 8567 9817 414 -1214 -1322 N ATOM 1102 CA SER B 2 27.722 68.590 10.239 1.00 67.02 C ANISOU 1102 CA SER B 2 7189 8637 9640 338 -1093 -1176 C ATOM 1103 C SER B 2 27.546 69.054 8.773 1.00 65.23 C ANISOU 1103 C SER B 2 6866 8585 9335 284 -854 -1138 C ATOM 1104 O SER B 2 28.312 69.895 8.308 1.00 62.49 O ANISOU 1104 O SER B 2 6348 8322 9075 232 -727 -1136 O ATOM 1105 CB SER B 2 26.956 69.550 11.148 1.00 60.86 C ANISOU 1105 CB SER B 2 6548 7776 8801 250 -1124 -1036 C ATOM 1106 OG SER B 2 27.014 70.828 10.558 1.00 63.72 O ANISOU 1106 OG SER B 2 6809 8225 9175 149 -954 -956 O ATOM 1107 N HIS B 3 26.519 68.513 8.081 1.00 58.73 N ANISOU 1107 N HIS B 3 6158 7811 8345 293 -799 -1104 N ATOM 1108 CA HIS B 3 26.331 68.702 6.645 1.00 57.72 C ANISOU 1108 CA HIS B 3 5966 7856 8111 274 -601 -1089 C ATOM 1109 C HIS B 3 24.889 68.674 6.297 1.00 54.60 C ANISOU 1109 C HIS B 3 5740 7475 7530 241 -571 -988 C ATOM 1110 O HIS B 3 24.068 68.213 7.094 1.00 51.80 O ANISOU 1110 O HIS B 3 5540 6999 7142 244 -701 -959 O ATOM 1111 CB HIS B 3 26.984 67.567 5.851 1.00 65.56 C ANISOU 1111 CB HIS B 3 6856 8928 9126 385 -590 -1262 C ATOM 1112 CG HIS B 3 28.484 67.423 6.081 1.00 78.97 C ANISOU 1112 CG HIS B 3 8352 10625 11027 442 -622 -1399 C ATOM 1113 ND1 HIS B 3 29.410 67.948 5.240 1.00 83.79 N ANISOU 1113 ND1 HIS B 3 8758 11383 11697 422 -443 -1439 N ATOM 1114 CD2 HIS B 3 29.204 66.779 7.102 1.00 81.06 C ANISOU 1114 CD2 HIS B 3 8590 10754 11456 522 -824 -1509 C ATOM 1115 CE1 HIS B 3 30.650 67.664 5.699 1.00 84.15 C ANISOU 1115 CE1 HIS B 3 8632 11390 11950 483 -524 -1580 C ATOM 1116 NE2 HIS B 3 30.521 66.952 6.842 1.00 84.34 N ANISOU 1116 NE2 HIS B 3 8770 11239 12036 551 -770 -1624 N ATOM 1117 N LYS B 4 24.574 69.118 5.079 1.00 50.48 N ANISOU 1117 N LYS B 4 5189 7106 6885 213 -400 -937 N ATOM 1118 CA LYS B 4 23.208 69.060 4.546 1.00 52.06 C ANISOU 1118 CA LYS B 4 5531 7344 6906 195 -374 -862 C ATOM 1119 C LYS B 4 22.802 67.589 4.292 1.00 50.49 C ANISOU 1119 C LYS B 4 5394 7128 6663 287 -472 -994 C ATOM 1120 O LYS B 4 23.619 66.780 3.814 1.00 52.87 O ANISOU 1120 O LYS B 4 5599 7479 7010 373 -473 -1143 O ATOM 1121 CB LYS B 4 23.058 69.937 3.296 1.00 55.59 C ANISOU 1121 CB LYS B 4 5938 7960 7224 155 -181 -773 C ATOM 1122 CG LYS B 4 22.655 69.194 2.033 1.00 64.52 C ANISOU 1122 CG LYS B 4 7088 9232 8195 226 -124 -849 C ATOM 1123 CD LYS B 4 22.273 70.166 0.922 1.00 72.16 C ANISOU 1123 CD LYS B 4 8067 10350 8998 184 45 -722 C ATOM 1124 CE LYS B 4 21.911 69.456 -0.369 1.00 77.23 C ANISOU 1124 CE LYS B 4 8735 11150 9458 267 95 -809 C ATOM 1125 NZ LYS B 4 20.679 68.628 -0.177 1.00 83.25 N ANISOU 1125 NZ LYS B 4 9629 11840 10162 302 -59 -858 N ATOM 1126 N LYS B 5 21.578 67.234 4.655 1.00 42.66 N ANISOU 1126 N LYS B 5 4552 6055 5603 269 -557 -949 N ATOM 1127 CA LYS B 5 21.110 65.867 4.469 1.00 41.06 C ANISOU 1127 CA LYS B 5 4413 5807 5380 338 -657 -1065 C ATOM 1128 C LYS B 5 20.032 65.815 3.361 1.00 42.95 C ANISOU 1128 C LYS B 5 4704 6161 5455 335 -594 -1055 C ATOM 1129 O LYS B 5 19.433 66.860 2.991 1.00 41.21 O ANISOU 1129 O LYS B 5 4505 6019 5134 274 -500 -928 O ATOM 1130 CB LYS B 5 20.534 65.349 5.779 1.00 38.44 C ANISOU 1130 CB LYS B 5 4211 5279 5114 315 -811 -1031 C ATOM 1131 CG LYS B 5 21.489 65.373 6.933 1.00 43.84 C ANISOU 1131 CG LYS B 5 4875 5847 5937 329 -904 -1039 C ATOM 1132 CD LYS B 5 22.708 64.504 6.674 1.00 44.30 C ANISOU 1132 CD LYS B 5 4821 5908 6102 436 -956 -1205 C ATOM 1133 CE LYS B 5 23.588 64.425 7.898 1.00 50.06 C ANISOU 1133 CE LYS B 5 5543 6504 6975 465 -1089 -1221 C ATOM 1134 NZ LYS B 5 24.975 64.040 7.475 1.00 52.62 N ANISOU 1134 NZ LYS B 5 5692 6882 7420 561 -1094 -1379 N ATOM 1135 N SER B 6 19.749 64.594 2.877 1.00 40.37 N ANISOU 1135 N SER B 6 4402 5826 5111 407 -665 -1193 N ATOM 1136 CA SER B 6 18.839 64.375 1.771 1.00 39.61 C ANISOU 1136 CA SER B 6 4341 5840 4868 426 -633 -1228 C ATOM 1137 C SER B 6 17.366 64.551 2.165 1.00 40.61 C ANISOU 1137 C SER B 6 4585 5892 4954 351 -687 -1127 C ATOM 1138 O SER B 6 16.975 64.447 3.377 1.00 40.24 O ANISOU 1138 O SER B 6 4609 5678 5001 294 -770 -1060 O ATOM 1139 CB SER B 6 19.051 62.977 1.206 1.00 38.08 C ANISOU 1139 CB SER B 6 4130 5643 4697 530 -710 -1432 C ATOM 1140 OG SER B 6 18.582 62.049 2.145 1.00 37.49 O ANISOU 1140 OG SER B 6 4141 5364 4740 518 -865 -1459 O ATOM 1141 N GLY B 7 16.538 64.811 1.135 1.00 39.78 N ANISOU 1141 N GLY B 7 4498 5914 4703 357 -641 -1119 N ATOM 1142 CA GLY B 7 15.091 64.904 1.342 1.00 36.90 C ANISOU 1142 CA GLY B 7 4217 5495 4307 299 -697 -1054 C ATOM 1143 C GLY B 7 14.522 63.667 2.039 1.00 37.88 C ANISOU 1143 C GLY B 7 4400 5445 4548 287 -834 -1135 C ATOM 1144 O GLY B 7 13.695 63.728 2.960 1.00 37.06 O ANISOU 1144 O GLY B 7 4361 5218 4504 209 -877 -1050 O ATOM 1145 N THR B 8 15.004 62.527 1.585 1.00 41.26 N ANISOU 1145 N THR B 8 4803 5862 5011 367 -894 -1303 N ATOM 1146 CA THR B 8 14.612 61.236 2.083 1.00 40.64 C ANISOU 1146 CA THR B 8 4777 5609 5054 367 -1026 -1395 C ATOM 1147 C THR B 8 14.790 61.145 3.586 1.00 39.83 C ANISOU 1147 C THR B 8 4737 5316 5083 305 -1076 -1295 C ATOM 1148 O THR B 8 13.863 60.711 4.316 1.00 40.52 O ANISOU 1148 O THR B 8 4904 5257 5234 233 -1139 -1248 O ATOM 1149 CB THR B 8 15.496 60.218 1.339 1.00 44.80 C ANISOU 1149 CB THR B 8 5249 6167 5605 486 -1068 -1596 C ATOM 1150 OG1 THR B 8 15.181 60.367 -0.045 1.00 50.66 O ANISOU 1150 OG1 THR B 8 5954 7101 6192 541 -1018 -1681 O ATOM 1151 CG2 THR B 8 15.265 58.760 1.784 1.00 44.03 C ANISOU 1151 CG2 THR B 8 5205 5866 5658 502 -1219 -1712 C ATOM 1152 N TYR B 9 15.981 61.538 4.041 1.00 36.47 N ANISOU 1152 N TYR B 9 4271 4891 4694 334 -1048 -1268 N ATOM 1153 CA TYR B 9 16.323 61.488 5.453 1.00 36.48 C ANISOU 1153 CA TYR B 9 4335 4726 4800 298 -1109 -1184 C ATOM 1154 C TYR B 9 15.454 62.519 6.165 1.00 34.97 C ANISOU 1154 C TYR B 9 4203 4523 4561 191 -1055 -1011 C ATOM 1155 O TYR B 9 14.938 62.243 7.257 1.00 35.41 O ANISOU 1155 O TYR B 9 4357 4429 4668 133 -1110 -938 O ATOM 1156 CB TYR B 9 17.806 61.861 5.686 1.00 38.49 C ANISOU 1156 CB TYR B 9 4508 5012 5104 356 -1092 -1204 C ATOM 1157 CG TYR B 9 18.129 61.819 7.136 1.00 40.58 C ANISOU 1157 CG TYR B 9 4849 5110 5461 331 -1177 -1126 C ATOM 1158 CD1 TYR B 9 18.073 60.608 7.803 1.00 41.39 C ANISOU 1158 CD1 TYR B 9 5044 5029 5654 357 -1313 -1169 C ATOM 1159 CD2 TYR B 9 18.343 63.002 7.885 1.00 41.15 C ANISOU 1159 CD2 TYR B 9 4921 5195 5518 275 -1130 -999 C ATOM 1160 CE1 TYR B 9 18.281 60.529 9.156 1.00 44.20 C ANISOU 1160 CE1 TYR B 9 5498 5230 6065 339 -1400 -1084 C ATOM 1161 CE2 TYR B 9 18.576 62.932 9.241 1.00 41.55 C ANISOU 1161 CE2 TYR B 9 5061 5098 5630 261 -1222 -936 C ATOM 1162 CZ TYR B 9 18.546 61.684 9.876 1.00 44.44 C ANISOU 1162 CZ TYR B 9 5527 5292 6064 296 -1356 -974 C ATOM 1163 OH TYR B 9 18.776 61.528 11.235 1.00 42.75 O ANISOU 1163 OH TYR B 9 5426 4928 5889 293 -1459 -904 O ATOM 1164 N TRP B 10 15.303 63.712 5.579 1.00 32.46 N ANISOU 1164 N TRP B 10 3831 4357 4144 168 -944 -943 N ATOM 1165 CA TRP B 10 14.466 64.661 6.240 1.00 30.27 C ANISOU 1165 CA TRP B 10 3605 4060 3835 81 -903 -797 C ATOM 1166 C TRP B 10 13.033 64.188 6.370 1.00 32.23 C ANISOU 1166 C TRP B 10 3919 4246 4081 24 -936 -784 C ATOM 1167 O TRP B 10 12.426 64.413 7.447 1.00 30.14 O ANISOU 1167 O TRP B 10 3726 3881 3844 -48 -941 -688 O ATOM 1168 CB TRP B 10 14.523 65.957 5.508 1.00 33.54 C ANISOU 1168 CB TRP B 10 3956 4631 4156 74 -791 -729 C ATOM 1169 CG TRP B 10 15.617 66.854 6.064 1.00 31.67 C ANISOU 1169 CG TRP B 10 3679 4394 3961 67 -748 -665 C ATOM 1170 CD1 TRP B 10 16.868 67.074 5.524 1.00 33.46 C ANISOU 1170 CD1 TRP B 10 3807 4705 4203 115 -696 -712 C ATOM 1171 CD2 TRP B 10 15.615 67.602 7.318 1.00 32.05 C ANISOU 1171 CD2 TRP B 10 3776 4347 4057 10 -759 -560 C ATOM 1172 NE1 TRP B 10 17.607 67.921 6.286 1.00 33.66 N ANISOU 1172 NE1 TRP B 10 3804 4692 4295 85 -678 -644 N ATOM 1173 CE2 TRP B 10 16.935 68.268 7.394 1.00 31.80 C ANISOU 1173 CE2 TRP B 10 3660 4346 4078 27 -724 -557 C ATOM 1174 CE3 TRP B 10 14.678 67.809 8.352 1.00 31.39 C ANISOU 1174 CE3 TRP B 10 3786 4163 3976 -52 -786 -479 C ATOM 1175 CZ2 TRP B 10 17.266 69.129 8.403 1.00 28.96 C ANISOU 1175 CZ2 TRP B 10 3314 3919 3772 -13 -733 -483 C ATOM 1176 CZ3 TRP B 10 15.043 68.679 9.415 1.00 29.89 C ANISOU 1176 CZ3 TRP B 10 3622 3914 3821 -85 -788 -403 C ATOM 1177 CH2 TRP B 10 16.303 69.315 9.429 1.00 29.84 C ANISOU 1177 CH2 TRP B 10 3537 3934 3866 -63 -772 -409 C ATOM 1178 N ALA B 11 12.491 63.475 5.343 1.00 30.41 N ANISOU 1178 N ALA B 11 3663 4067 3825 55 -964 -892 N ATOM 1179 CA ALA B 11 11.190 62.817 5.473 1.00 30.57 C ANISOU 1179 CA ALA B 11 3727 4006 3884 -3 -1013 -908 C ATOM 1180 C ALA B 11 11.095 61.963 6.706 1.00 34.32 C ANISOU 1180 C ALA B 11 4289 4278 4473 -53 -1077 -880 C ATOM 1181 O ALA B 11 10.111 62.063 7.475 1.00 33.46 O ANISOU 1181 O ALA B 11 4232 4091 4391 -144 -1060 -794 O ATOM 1182 CB ALA B 11 10.856 61.943 4.243 1.00 31.60 C ANISOU 1182 CB ALA B 11 3815 4194 3999 53 -1068 -1067 C ATOM 1183 N THR B 12 12.110 61.106 6.916 1.00 34.72 N ANISOU 1183 N THR B 12 4359 4240 4592 7 -1149 -952 N ATOM 1184 CA THR B 12 12.126 60.223 8.112 1.00 35.01 C ANISOU 1184 CA THR B 12 4504 4067 4731 -29 -1225 -913 C ATOM 1185 C THR B 12 12.201 61.066 9.385 1.00 33.75 C ANISOU 1185 C THR B 12 4414 3866 4544 -83 -1182 -757 C ATOM 1186 O THR B 12 11.600 60.757 10.437 1.00 34.74 O ANISOU 1186 O THR B 12 4643 3857 4698 -157 -1192 -668 O ATOM 1187 CB THR B 12 13.398 59.398 8.026 1.00 36.45 C ANISOU 1187 CB THR B 12 4680 4188 4982 74 -1315 -1019 C ATOM 1188 OG1 THR B 12 13.267 58.528 6.907 1.00 37.65 O ANISOU 1188 OG1 THR B 12 4778 4365 5162 128 -1362 -1180 O ATOM 1189 CG2 THR B 12 13.735 58.644 9.322 1.00 36.18 C ANISOU 1189 CG2 THR B 12 4770 3941 5037 64 -1408 -961 C ATOM 1190 N LEU B 13 12.983 62.128 9.300 1.00 32.25 N ANISOU 1190 N LEU B 13 4168 3790 4297 -46 -1133 -728 N ATOM 1191 CA LEU B 13 13.243 62.929 10.464 1.00 31.22 C ANISOU 1191 CA LEU B 13 4095 3620 4145 -78 -1113 -612 C ATOM 1192 C LEU B 13 11.953 63.682 10.936 1.00 30.16 C ANISOU 1192 C LEU B 13 3999 3501 3958 -175 -1030 -501 C ATOM 1193 O LEU B 13 11.611 63.768 12.162 1.00 28.74 O ANISOU 1193 O LEU B 13 3923 3226 3772 -228 -1027 -408 O ATOM 1194 CB LEU B 13 14.432 63.872 10.123 1.00 31.07 C ANISOU 1194 CB LEU B 13 3982 3716 4107 -18 -1082 -628 C ATOM 1195 CG LEU B 13 14.876 64.760 11.290 1.00 34.03 C ANISOU 1195 CG LEU B 13 4403 4052 4475 -38 -1082 -534 C ATOM 1196 CD1 LEU B 13 14.951 63.969 12.607 1.00 35.12 C ANISOU 1196 CD1 LEU B 13 4680 4016 4646 -41 -1181 -498 C ATOM 1197 CD2 LEU B 13 16.175 65.531 10.985 1.00 30.31 C ANISOU 1197 CD2 LEU B 13 3822 3665 4028 15 -1067 -567 C ATOM 1198 N ILE B 14 11.220 64.217 9.955 1.00 28.43 N ANISOU 1198 N ILE B 14 3698 3408 3694 -190 -964 -517 N ATOM 1199 CA ILE B 14 9.979 64.928 10.241 1.00 28.47 C ANISOU 1199 CA ILE B 14 3712 3439 3666 -266 -892 -437 C ATOM 1200 C ILE B 14 8.901 63.984 10.886 1.00 30.81 C ANISOU 1200 C ILE B 14 4079 3609 4018 -346 -904 -420 C ATOM 1201 O ILE B 14 8.178 64.378 11.841 1.00 30.24 O ANISOU 1201 O ILE B 14 4061 3496 3932 -416 -847 -330 O ATOM 1202 CB ILE B 14 9.427 65.630 8.951 1.00 28.88 C ANISOU 1202 CB ILE B 14 3662 3649 3661 -249 -844 -466 C ATOM 1203 CG1 ILE B 14 10.343 66.814 8.522 1.00 25.77 C ANISOU 1203 CG1 ILE B 14 3216 3369 3209 -199 -798 -432 C ATOM 1204 CG2 ILE B 14 8.051 66.163 9.200 1.00 25.83 C ANISOU 1204 CG2 ILE B 14 3271 3276 3267 -316 -792 -408 C ATOM 1205 CD1 ILE B 14 10.190 67.186 7.069 1.00 26.21 C ANISOU 1205 CD1 ILE B 14 3191 3575 3193 -154 -769 -472 C ATOM 1206 N THR B 15 8.765 62.755 10.365 1.00 29.37 N ANISOU 1206 N THR B 15 3892 3364 3902 -341 -969 -510 N ATOM 1207 CA THR B 15 7.794 61.816 10.893 1.00 29.26 C ANISOU 1207 CA THR B 15 3935 3217 3966 -428 -975 -494 C ATOM 1208 C THR B 15 8.149 61.483 12.362 1.00 30.72 C ANISOU 1208 C THR B 15 4264 3252 4158 -461 -983 -389 C ATOM 1209 O THR B 15 7.291 61.548 13.291 1.00 31.73 O ANISOU 1209 O THR B 15 4457 3319 4281 -553 -914 -294 O ATOM 1210 CB THR B 15 7.827 60.541 10.067 1.00 32.16 C ANISOU 1210 CB THR B 15 4277 3523 4420 -402 -1065 -622 C ATOM 1211 OG1 THR B 15 7.373 60.860 8.736 1.00 36.51 O ANISOU 1211 OG1 THR B 15 4709 4224 4941 -369 -1062 -720 O ATOM 1212 CG2 THR B 15 6.857 59.437 10.714 1.00 33.64 C ANISOU 1212 CG2 THR B 15 4531 3530 4722 -512 -1075 -595 C ATOM 1213 N ALA B 16 9.420 61.162 12.588 1.00 29.75 N ANISOU 1213 N ALA B 16 4190 3076 4036 -381 -1065 -408 N ATOM 1214 CA ALA B 16 9.902 60.884 13.944 1.00 31.02 C ANISOU 1214 CA ALA B 16 4499 3103 4185 -387 -1100 -314 C ATOM 1215 C ALA B 16 9.659 62.114 14.875 1.00 31.13 C ANISOU 1215 C ALA B 16 4552 3177 4098 -422 -1012 -205 C ATOM 1216 O ALA B 16 9.084 61.956 16.000 1.00 32.34 O ANISOU 1216 O ALA B 16 4827 3243 4218 -492 -970 -102 O ATOM 1217 CB ALA B 16 11.366 60.484 13.875 1.00 31.14 C ANISOU 1217 CB ALA B 16 4526 3079 4228 -274 -1218 -378 C ATOM 1218 N PHE B 17 9.958 63.327 14.369 1.00 29.52 N ANISOU 1218 N PHE B 17 4247 3123 3846 -384 -972 -226 N ATOM 1219 CA PHE B 17 9.676 64.535 15.146 1.00 27.94 C ANISOU 1219 CA PHE B 17 4071 2976 3567 -411 -896 -145 C ATOM 1220 C PHE B 17 8.216 64.570 15.542 1.00 27.53 C ANISOU 1220 C PHE B 17 4041 2916 3504 -511 -795 -86 C ATOM 1221 O PHE B 17 7.870 64.777 16.710 1.00 27.99 O ANISOU 1221 O PHE B 17 4203 2927 3505 -553 -746 -3 O ATOM 1222 CB PHE B 17 10.004 65.759 14.313 1.00 28.88 C ANISOU 1222 CB PHE B 17 4065 3244 3664 -369 -862 -177 C ATOM 1223 CG PHE B 17 9.658 67.053 15.000 1.00 29.06 C ANISOU 1223 CG PHE B 17 4101 3315 3626 -393 -791 -110 C ATOM 1224 CD1 PHE B 17 10.552 67.631 15.933 1.00 29.53 C ANISOU 1224 CD1 PHE B 17 4223 3343 3652 -358 -830 -82 C ATOM 1225 CD2 PHE B 17 8.454 67.700 14.719 1.00 28.91 C ANISOU 1225 CD2 PHE B 17 4025 3366 3593 -442 -700 -89 C ATOM 1226 CE1 PHE B 17 10.227 68.848 16.534 1.00 32.47 C ANISOU 1226 CE1 PHE B 17 4605 3756 3977 -373 -772 -39 C ATOM 1227 CE2 PHE B 17 8.116 68.895 15.337 1.00 29.29 C ANISOU 1227 CE2 PHE B 17 4080 3451 3597 -453 -639 -41 C ATOM 1228 CZ PHE B 17 9.001 69.484 16.241 1.00 28.67 C ANISOU 1228 CZ PHE B 17 4069 3341 3483 -420 -672 -18 C ATOM 1229 N LEU B 18 7.328 64.399 14.555 1.00 28.09 N ANISOU 1229 N LEU B 18 4006 3042 3624 -545 -759 -138 N ATOM 1230 CA LEU B 18 5.899 64.569 14.827 1.00 27.71 C ANISOU 1230 CA LEU B 18 3936 3006 3588 -637 -657 -101 C ATOM 1231 C LEU B 18 5.391 63.461 15.791 1.00 31.67 C ANISOU 1231 C LEU B 18 4555 3357 4123 -724 -634 -38 C ATOM 1232 O LEU B 18 4.500 63.732 16.629 1.00 32.84 O ANISOU 1232 O LEU B 18 4738 3496 4243 -801 -526 33 O ATOM 1233 CB LEU B 18 5.093 64.599 13.508 1.00 26.94 C ANISOU 1233 CB LEU B 18 3689 2999 3546 -644 -652 -185 C ATOM 1234 CG LEU B 18 5.417 65.806 12.592 1.00 25.37 C ANISOU 1234 CG LEU B 18 3393 2954 3294 -567 -654 -216 C ATOM 1235 CD1 LEU B 18 4.702 65.708 11.250 1.00 26.91 C ANISOU 1235 CD1 LEU B 18 3466 3237 3522 -556 -674 -302 C ATOM 1236 CD2 LEU B 18 5.058 67.114 13.233 1.00 22.79 C ANISOU 1236 CD2 LEU B 18 3066 2682 2913 -576 -574 -148 C ATOM 1237 N LYS B 19 5.923 62.231 15.659 1.00 30.62 N ANISOU 1237 N LYS B 19 4480 3101 4052 -713 -726 -64 N ATOM 1238 CA LYS B 19 5.460 61.115 16.466 1.00 33.40 C ANISOU 1238 CA LYS B 19 4950 3290 4451 -800 -709 7 C ATOM 1239 C LYS B 19 5.985 61.309 17.888 1.00 36.91 C ANISOU 1239 C LYS B 19 5570 3671 4782 -790 -696 125 C ATOM 1240 O LYS B 19 5.274 61.097 18.872 1.00 39.42 O ANISOU 1240 O LYS B 19 5989 3925 5065 -878 -601 228 O ATOM 1241 CB LYS B 19 5.984 59.804 15.878 1.00 33.03 C ANISOU 1241 CB LYS B 19 4921 3119 4511 -773 -833 -63 C ATOM 1242 CG LYS B 19 5.257 59.360 14.629 1.00 32.84 C ANISOU 1242 CG LYS B 19 4749 3126 4601 -802 -847 -181 C ATOM 1243 CD LYS B 19 5.647 57.919 14.177 1.00 32.49 C ANISOU 1243 CD LYS B 19 4737 2926 4681 -785 -969 -257 C ATOM 1244 CE LYS B 19 4.856 57.576 12.909 1.00 33.07 C ANISOU 1244 CE LYS B 19 4657 3048 4859 -809 -990 -397 C ATOM 1245 NZ LYS B 19 5.211 56.235 12.337 1.00 36.99 N ANISOU 1245 NZ LYS B 19 5167 3402 5484 -782 -1118 -504 N ATOM 1246 N THR B 20 7.213 61.793 17.998 1.00 36.99 N ANISOU 1246 N THR B 20 5612 3714 4729 -681 -786 107 N ATOM 1247 CA THR B 20 7.771 61.998 19.317 1.00 39.10 C ANISOU 1247 CA THR B 20 6046 3928 4884 -655 -803 201 C ATOM 1248 C THR B 20 6.993 63.074 20.070 1.00 42.49 C ANISOU 1248 C THR B 20 6489 4448 5209 -703 -666 262 C ATOM 1249 O THR B 20 6.575 62.840 21.211 1.00 40.09 O ANISOU 1249 O THR B 20 6332 4079 4822 -756 -600 364 O ATOM 1250 CB THR B 20 9.216 62.448 19.223 1.00 42.34 C ANISOU 1250 CB THR B 20 6448 4369 5268 -528 -931 145 C ATOM 1251 OG1 THR B 20 9.967 61.378 18.651 1.00 43.19 O ANISOU 1251 OG1 THR B 20 6554 4385 5472 -473 -1058 83 O ATOM 1252 CG2 THR B 20 9.802 62.743 20.620 1.00 42.71 C ANISOU 1252 CG2 THR B 20 6667 4369 5192 -489 -972 226 C ATOM 1253 N VAL B 21 6.811 64.258 19.452 1.00 40.26 N ANISOU 1253 N VAL B 21 6061 4313 4924 -679 -621 201 N ATOM 1254 CA VAL B 21 6.020 65.296 20.127 1.00 36.65 C ANISOU 1254 CA VAL B 21 5604 3937 4384 -716 -495 241 C ATOM 1255 C VAL B 21 4.558 64.881 20.329 1.00 38.40 C ANISOU 1255 C VAL B 21 5807 4145 4638 -836 -351 282 C ATOM 1256 O VAL B 21 3.862 65.402 21.196 1.00 40.31 O ANISOU 1256 O VAL B 21 6092 4422 4803 -878 -230 332 O ATOM 1257 CB VAL B 21 6.121 66.692 19.477 1.00 31.47 C ANISOU 1257 CB VAL B 21 4807 3419 3729 -662 -485 175 C ATOM 1258 CG1 VAL B 21 7.565 67.178 19.518 1.00 28.88 C ANISOU 1258 CG1 VAL B 21 4503 3097 3373 -562 -604 146 C ATOM 1259 CG2 VAL B 21 5.546 66.705 18.106 1.00 28.66 C ANISOU 1259 CG2 VAL B 21 4282 3134 3474 -677 -470 108 C ATOM 1260 N SER B 22 4.075 63.966 19.502 1.00 42.87 N ANISOU 1260 N SER B 22 6295 4665 5328 -890 -360 248 N ATOM 1261 CA SER B 22 2.737 63.390 19.727 1.00 43.60 C ANISOU 1261 CA SER B 22 6364 4717 5483 -1019 -231 286 C ATOM 1262 C SER B 22 2.674 62.292 20.842 1.00 47.37 C ANISOU 1262 C SER B 22 7033 5036 5928 -1096 -193 408 C ATOM 1263 O SER B 22 1.592 61.851 21.176 1.00 50.15 O ANISOU 1263 O SER B 22 7376 5350 6328 -1217 -62 457 O ATOM 1264 CB SER B 22 2.168 62.884 18.422 1.00 43.50 C ANISOU 1264 CB SER B 22 6185 4715 5628 -1052 -263 190 C ATOM 1265 OG SER B 22 2.266 63.904 17.437 1.00 41.85 O ANISOU 1265 OG SER B 22 5829 4651 5419 -973 -301 98 O ATOM 1266 N LYS B 23 3.820 61.876 21.376 1.00 46.12 N ANISOU 1266 N LYS B 23 7041 4786 5697 -1026 -308 456 N ATOM 1267 CA LYS B 23 3.937 60.918 22.485 1.00 54.31 C ANISOU 1267 CA LYS B 23 8296 5666 6671 -1072 -298 589 C ATOM 1268 C LYS B 23 3.451 59.592 21.983 1.00 60.87 C ANISOU 1268 C LYS B 23 9108 6354 7667 -1166 -306 597 C ATOM 1269 O LYS B 23 2.793 58.839 22.700 1.00 59.26 O ANISOU 1269 O LYS B 23 9012 6035 7469 -1280 -206 712 O ATOM 1270 CB LYS B 23 3.137 61.335 23.729 1.00 58.03 C ANISOU 1270 CB LYS B 23 8872 6172 7004 -1146 -117 699 C ATOM 1271 CG LYS B 23 3.765 62.500 24.495 1.00 58.69 C ANISOU 1271 CG LYS B 23 9034 6361 6904 -1042 -134 699 C ATOM 1272 CD LYS B 23 2.977 62.912 25.744 1.00 67.59 C ANISOU 1272 CD LYS B 23 10273 7535 7873 -1103 50 792 C ATOM 1273 CE LYS B 23 3.187 61.947 26.923 1.00 71.62 C ANISOU 1273 CE LYS B 23 11053 7905 8254 -1136 61 952 C ATOM 1274 NZ LYS B 23 3.063 62.596 28.260 1.00 73.98 N ANISOU 1274 NZ LYS B 23 11518 8274 8317 -1114 163 1023 N ATOM 1275 N VAL B 24 3.755 59.328 20.721 1.00 56.44 N ANISOU 1275 N VAL B 24 8404 5800 7241 -1121 -420 469 N ATOM 1276 CA VAL B 24 3.222 58.168 20.078 1.00 55.87 C ANISOU 1276 CA VAL B 24 8277 5604 7346 -1204 -439 437 C ATOM 1277 C VAL B 24 4.436 57.331 19.641 1.00 58.57 C ANISOU 1277 C VAL B 24 8685 5828 7743 -1101 -638 385 C ATOM 1278 O VAL B 24 4.422 56.540 18.681 1.00 57.88 O ANISOU 1278 O VAL B 24 8512 5673 7808 -1102 -724 285 O ATOM 1279 CB VAL B 24 2.244 58.645 19.016 1.00 51.92 C ANISOU 1279 CB VAL B 24 7542 5235 6952 -1249 -377 318 C ATOM 1280 CG1 VAL B 24 2.794 58.538 17.589 1.00 44.63 C ANISOU 1280 CG1 VAL B 24 6482 4359 6115 -1153 -526 157 C ATOM 1281 CG2 VAL B 24 0.968 57.930 19.255 1.00 51.96 C ANISOU 1281 CG2 VAL B 24 7517 5148 7077 -1415 -250 366 C ATOM 1282 N GLU B 25 5.504 57.542 20.402 1.00 58.25 N ANISOU 1282 N GLU B 25 8795 5766 7573 -1002 -717 445 N ATOM 1283 CA GLU B 25 6.706 56.809 20.262 1.00 63.50 C ANISOU 1283 CA GLU B 25 9540 6314 8273 -894 -902 412 C ATOM 1284 C GLU B 25 7.470 56.888 21.567 1.00 75.68 C ANISOU 1284 C GLU B 25 11301 7793 9661 -833 -951 536 C ATOM 1285 O GLU B 25 7.532 57.960 22.195 1.00 74.36 O ANISOU 1285 O GLU B 25 11159 7753 9344 -808 -889 571 O ATOM 1286 CB GLU B 25 7.519 57.339 19.113 1.00 58.62 C ANISOU 1286 CB GLU B 25 8755 5826 7690 -771 -1003 247 C ATOM 1287 CG GLU B 25 8.198 56.195 18.409 1.00 63.09 C ANISOU 1287 CG GLU B 25 9315 6262 8393 -707 -1159 154 C ATOM 1288 CD GLU B 25 8.347 56.439 16.950 1.00 56.94 C ANISOU 1288 CD GLU B 25 8330 5613 7690 -650 -1194 -23 C ATOM 1289 OE1 GLU B 25 8.351 57.611 16.561 1.00 57.62 O ANISOU 1289 OE1 GLU B 25 8302 5891 7701 -621 -1133 -62 O ATOM 1290 OE2 GLU B 25 8.469 55.459 16.199 1.00 58.58 O ANISOU 1290 OE2 GLU B 25 8500 5728 8029 -629 -1285 -122 O ATOM 1291 N GLU B 26 7.972 55.715 21.986 1.00 86.70 N ANISOU 1291 N GLU B 26 12862 8981 11098 -812 -1067 601 N ATOM 1292 CA GLU B 26 8.883 55.560 23.118 1.00 89.08 C ANISOU 1292 CA GLU B 26 13387 9190 11268 -723 -1175 704 C ATOM 1293 C GLU B 26 10.282 55.799 22.573 1.00 88.16 C ANISOU 1293 C GLU B 26 13193 9121 11184 -550 -1367 564 C ATOM 1294 O GLU B 26 10.606 55.327 21.457 1.00 82.95 O ANISOU 1294 O GLU B 26 12392 8443 10681 -507 -1449 428 O ATOM 1295 CB GLU B 26 8.783 54.155 23.696 1.00 94.97 C ANISOU 1295 CB GLU B 26 14339 9679 12067 -771 -1228 835 C ATOM 1296 CG GLU B 26 9.230 54.068 25.155 1.00109.83 C ANISOU 1296 CG GLU B 26 16501 11475 13756 -727 -1271 1007 C ATOM 1297 CD GLU B 26 8.308 53.211 25.994 1.00121.95 C ANISOU 1297 CD GLU B 26 18234 12839 15261 -875 -1147 1212 C ATOM 1298 OE1 GLU B 26 8.427 53.239 27.248 1.00122.97 O ANISOU 1298 OE1 GLU B 26 18606 12925 15191 -863 -1132 1376 O ATOM 1299 OE2 GLU B 26 7.460 52.519 25.388 1.00119.18 O ANISOU 1299 OE2 GLU B 26 17797 12400 15087 -1004 -1064 1205 O ATOM 1300 N LEU B 27 11.099 56.522 23.349 1.00 81.31 N ANISOU 1300 N LEU B 27 12408 8315 10171 -451 -1435 587 N ATOM 1301 CA LEU B 27 12.454 56.899 22.934 1.00 75.99 C ANISOU 1301 CA LEU B 27 11641 7700 9530 -293 -1602 453 C ATOM 1302 C LEU B 27 13.221 55.655 22.517 1.00 73.12 C ANISOU 1302 C LEU B 27 11303 7165 9315 -209 -1782 395 C ATOM 1303 O LEU B 27 14.019 55.627 21.559 1.00 62.41 O ANISOU 1303 O LEU B 27 9782 5855 8075 -114 -1877 236 O ATOM 1304 CB LEU B 27 13.175 57.602 24.103 1.00 71.94 C ANISOU 1304 CB LEU B 27 11265 7221 8848 -208 -1676 508 C ATOM 1305 CG LEU B 27 12.740 59.054 24.324 1.00 72.03 C ANISOU 1305 CG LEU B 27 11200 7428 8739 -247 -1536 502 C ATOM 1306 CD1 LEU B 27 12.319 59.698 22.982 1.00 64.04 C ANISOU 1306 CD1 LEU B 27 9924 6569 7840 -293 -1428 380 C ATOM 1307 CD2 LEU B 27 11.651 59.086 25.395 1.00 73.17 C ANISOU 1307 CD2 LEU B 27 11523 7552 8726 -355 -1383 663 C ATOM 1308 N ASP B 28 12.937 54.606 23.264 1.00 76.35 N ANISOU 1308 N ASP B 28 11925 7368 9715 -247 -1818 532 N ATOM 1309 CA ASP B 28 13.569 53.341 23.040 1.00 87.28 C ANISOU 1309 CA ASP B 28 13373 8549 11241 -169 -1995 500 C ATOM 1310 C ASP B 28 13.356 52.718 21.667 1.00 81.94 C ANISOU 1310 C ASP B 28 12511 7851 10770 -189 -1998 350 C ATOM 1311 O ASP B 28 14.100 51.818 21.296 1.00 77.02 O ANISOU 1311 O ASP B 28 11892 7092 10281 -87 -2166 267 O ATOM 1312 CB ASP B 28 13.165 52.378 24.146 1.00 98.28 C ANISOU 1312 CB ASP B 28 15050 9713 12578 -227 -2012 707 C ATOM 1313 CG ASP B 28 14.231 52.273 25.189 1.00112.66 C ANISOU 1313 CG ASP B 28 17071 11448 14284 -82 -2202 774 C ATOM 1314 OD1 ASP B 28 15.316 51.798 24.796 1.00121.11 O ANISOU 1314 OD1 ASP B 28 18096 12445 15475 67 -2409 656 O ATOM 1315 OD2 ASP B 28 14.020 52.689 26.362 1.00115.79 O ANISOU 1315 OD2 ASP B 28 17658 11863 14473 -105 -2153 928 O ATOM 1316 N CYS B 29 12.380 53.235 20.914 1.00 78.28 N ANISOU 1316 N CYS B 29 11884 7531 10330 -303 -1824 303 N ATOM 1317 CA CYS B 29 11.856 52.564 19.732 1.00 75.05 C ANISOU 1317 CA CYS B 29 11333 7087 10096 -352 -1807 185 C ATOM 1318 C CYS B 29 12.356 53.257 18.446 1.00 70.94 C ANISOU 1318 C CYS B 29 10564 6776 9615 -267 -1815 -20 C ATOM 1319 O CYS B 29 12.258 52.702 17.357 1.00 63.00 O ANISOU 1319 O CYS B 29 9435 5759 8742 -255 -1846 -160 O ATOM 1320 CB CYS B 29 10.310 52.396 19.840 1.00 73.41 C ANISOU 1320 CB CYS B 29 11139 6847 9906 -548 -1625 285 C ATOM 1321 SG CYS B 29 9.732 51.086 21.012 1.00 80.29 S ANISOU 1321 SG CYS B 29 12290 7407 10810 -663 -1623 507 S ATOM 1322 N VAL B 30 12.951 54.445 18.588 1.00 61.62 N ANISOU 1322 N VAL B 30 9319 5776 8317 -203 -1794 -37 N ATOM 1323 CA VAL B 30 13.494 55.186 17.433 1.00 56.42 C ANISOU 1323 CA VAL B 30 8438 5318 7681 -127 -1786 -205 C ATOM 1324 C VAL B 30 15.013 54.864 17.170 1.00 52.45 C ANISOU 1324 C VAL B 30 7891 4790 7248 45 -1960 -331 C ATOM 1325 O VAL B 30 15.770 54.584 18.095 1.00 52.72 O ANISOU 1325 O VAL B 30 8057 4709 7264 120 -2085 -275 O ATOM 1326 CB VAL B 30 13.117 56.698 17.594 1.00 54.15 C ANISOU 1326 CB VAL B 30 8079 5237 7257 -178 -1641 -157 C ATOM 1327 CG1 VAL B 30 13.279 57.097 19.040 1.00 58.56 C ANISOU 1327 CG1 VAL B 30 8813 5748 7688 -182 -1650 -12 C ATOM 1328 CG2 VAL B 30 13.862 57.629 16.664 1.00 47.01 C ANISOU 1328 CG2 VAL B 30 6982 4528 6350 -97 -1633 -286 C ATOM 1329 N ASP B 31 15.420 54.834 15.907 1.00 47.41 N ANISOU 1329 N ASP B 31 7069 4255 6690 110 -1970 -505 N ATOM 1330 CA ASP B 31 16.804 54.793 15.527 1.00 47.63 C ANISOU 1330 CA ASP B 31 7000 4320 6777 263 -2086 -642 C ATOM 1331 C ASP B 31 17.646 55.920 16.192 1.00 48.89 C ANISOU 1331 C ASP B 31 7140 4586 6850 313 -2094 -603 C ATOM 1332 O ASP B 31 17.275 57.104 16.155 1.00 43.38 O ANISOU 1332 O ASP B 31 6379 4049 6054 246 -1963 -557 O ATOM 1333 CB ASP B 31 16.921 54.963 14.020 1.00 51.51 C ANISOU 1333 CB ASP B 31 7281 4977 7313 298 -2025 -817 C ATOM 1334 CG ASP B 31 18.368 55.052 13.591 1.00 59.27 C ANISOU 1334 CG ASP B 31 8135 6031 8355 450 -2109 -963 C ATOM 1335 OD1 ASP B 31 19.082 54.081 13.846 1.00 70.94 O ANISOU 1335 OD1 ASP B 31 9663 7352 9938 552 -2266 -1024 O ATOM 1336 OD2 ASP B 31 18.858 56.081 13.079 1.00 64.19 O ANISOU 1336 OD2 ASP B 31 8607 6852 8930 471 -2025 -1012 O ATOM 1337 N SER B 32 18.772 55.553 16.804 1.00 48.75 N ANISOU 1337 N SER B 32 7174 4470 6879 435 -2260 -629 N ATOM 1338 CA SER B 32 19.519 56.483 17.666 1.00 46.05 C ANISOU 1338 CA SER B 32 6846 4185 6464 479 -2303 -585 C ATOM 1339 C SER B 32 19.915 57.787 17.048 1.00 42.99 C ANISOU 1339 C SER B 32 6258 4022 6055 475 -2196 -656 C ATOM 1340 O SER B 32 19.721 58.842 17.663 1.00 41.65 O ANISOU 1340 O SER B 32 6114 3928 5783 420 -2133 -570 O ATOM 1341 CB SER B 32 20.782 55.811 18.152 1.00 48.16 C ANISOU 1341 CB SER B 32 7150 4325 6822 634 -2522 -652 C ATOM 1342 OG SER B 32 20.386 54.910 19.132 1.00 49.80 O ANISOU 1342 OG SER B 32 7604 4319 7001 625 -2620 -521 O ATOM 1343 N ALA B 33 20.505 57.702 15.858 1.00 43.02 N ANISOU 1343 N ALA B 33 6068 4125 6154 536 -2178 -814 N ATOM 1344 CA ALA B 33 20.890 58.850 15.043 1.00 43.00 C ANISOU 1344 CA ALA B 33 5861 4336 6140 527 -2055 -882 C ATOM 1345 C ALA B 33 19.669 59.725 14.709 1.00 43.79 C ANISOU 1345 C ALA B 33 5957 4555 6126 390 -1869 -787 C ATOM 1346 O ALA B 33 19.752 60.964 14.737 1.00 40.63 O ANISOU 1346 O ALA B 33 5485 4280 5673 350 -1781 -750 O ATOM 1347 CB ALA B 33 21.565 58.358 13.770 1.00 44.29 C ANISOU 1347 CB ALA B 33 5846 4574 6408 613 -2052 -1062 C ATOM 1348 N VAL B 34 18.516 59.089 14.433 1.00 41.91 N ANISOU 1348 N VAL B 34 5795 4264 5864 319 -1820 -748 N ATOM 1349 CA VAL B 34 17.279 59.885 14.230 1.00 37.30 C ANISOU 1349 CA VAL B 34 5212 3780 5182 195 -1662 -657 C ATOM 1350 C VAL B 34 16.900 60.544 15.592 1.00 37.68 C ANISOU 1350 C VAL B 34 5399 3779 5137 134 -1650 -507 C ATOM 1351 O VAL B 34 16.563 61.735 15.644 1.00 35.23 O ANISOU 1351 O VAL B 34 5045 3585 4754 79 -1545 -456 O ATOM 1352 CB VAL B 34 16.124 59.013 13.682 1.00 37.95 C ANISOU 1352 CB VAL B 34 5330 3807 5281 131 -1626 -664 C ATOM 1353 CG1 VAL B 34 14.853 59.790 13.675 1.00 34.82 C ANISOU 1353 CG1 VAL B 34 4939 3492 4797 11 -1486 -569 C ATOM 1354 CG2 VAL B 34 16.380 58.603 12.230 1.00 38.23 C ANISOU 1354 CG2 VAL B 34 5219 3934 5374 190 -1618 -825 C ATOM 1355 N LEU B 35 16.976 59.767 16.682 1.00 35.43 N ANISOU 1355 N LEU B 35 5290 3322 4850 151 -1760 -440 N ATOM 1356 CA LEU B 35 16.606 60.264 17.963 1.00 36.99 C ANISOU 1356 CA LEU B 35 5638 3477 4938 103 -1749 -306 C ATOM 1357 C LEU B 35 17.485 61.531 18.344 1.00 36.18 C ANISOU 1357 C LEU B 35 5466 3479 4801 150 -1767 -327 C ATOM 1358 O LEU B 35 17.031 62.461 18.999 1.00 34.04 O ANISOU 1358 O LEU B 35 5244 3256 4431 96 -1698 -249 O ATOM 1359 CB LEU B 35 16.773 59.117 18.993 1.00 39.48 C ANISOU 1359 CB LEU B 35 6162 3585 5254 139 -1887 -237 C ATOM 1360 CG LEU B 35 16.236 59.467 20.400 1.00 42.92 C ANISOU 1360 CG LEU B 35 6797 3970 5543 84 -1862 -80 C ATOM 1361 CD1 LEU B 35 14.799 60.028 20.258 1.00 44.37 C ANISOU 1361 CD1 LEU B 35 6965 4239 5654 -58 -1659 -5 C ATOM 1362 CD2 LEU B 35 16.251 58.285 21.352 1.00 41.04 C ANISOU 1362 CD2 LEU B 35 6787 3521 5284 106 -1978 18 C ATOM 1363 N VAL B 36 18.741 61.559 17.910 1.00 35.48 N ANISOU 1363 N VAL B 36 5251 3422 4808 251 -1858 -444 N ATOM 1364 CA VAL B 36 19.587 62.734 18.212 1.00 35.61 C ANISOU 1364 CA VAL B 36 5179 3526 4825 283 -1877 -474 C ATOM 1365 C VAL B 36 19.045 63.979 17.534 1.00 34.53 C ANISOU 1365 C VAL B 36 4918 3548 4653 199 -1703 -459 C ATOM 1366 O VAL B 36 18.872 65.078 18.179 1.00 33.31 O ANISOU 1366 O VAL B 36 4789 3433 4433 160 -1665 -403 O ATOM 1367 CB VAL B 36 21.115 62.440 17.934 1.00 36.09 C ANISOU 1367 CB VAL B 36 5111 3578 5022 409 -2015 -613 C ATOM 1368 CG1 VAL B 36 21.978 63.712 17.979 1.00 36.65 C ANISOU 1368 CG1 VAL B 36 5036 3756 5134 422 -2007 -663 C ATOM 1369 CG2 VAL B 36 21.615 61.449 18.968 1.00 36.17 C ANISOU 1369 CG2 VAL B 36 5286 3415 5044 501 -2217 -601 C ATOM 1370 N ASP B 37 18.736 63.807 16.252 1.00 34.24 N ANISOU 1370 N ASP B 37 4761 3597 4654 178 -1607 -509 N ATOM 1371 CA ASP B 37 18.322 64.890 15.398 1.00 32.42 C ANISOU 1371 CA ASP B 37 4405 3517 4397 117 -1455 -500 C ATOM 1372 C ASP B 37 16.962 65.387 15.815 1.00 30.71 C ANISOU 1372 C ASP B 37 4284 3306 4077 20 -1358 -388 C ATOM 1373 O ASP B 37 16.732 66.579 15.917 1.00 29.55 O ANISOU 1373 O ASP B 37 4103 3233 3893 -21 -1283 -346 O ATOM 1374 CB ASP B 37 18.351 64.420 13.955 1.00 37.86 C ANISOU 1374 CB ASP B 37 4965 4290 5128 136 -1397 -587 C ATOM 1375 CG ASP B 37 19.791 64.258 13.419 1.00 42.09 C ANISOU 1375 CG ASP B 37 5358 4867 5769 231 -1452 -711 C ATOM 1376 OD1 ASP B 37 20.710 64.809 14.033 1.00 49.83 O ANISOU 1376 OD1 ASP B 37 6301 5835 6798 262 -1511 -723 O ATOM 1377 OD2 ASP B 37 20.029 63.599 12.383 1.00 47.91 O ANISOU 1377 OD2 ASP B 37 6007 5652 6545 277 -1436 -809 O ATOM 1378 N VAL B 38 16.073 64.478 16.136 1.00 30.17 N ANISOU 1378 N VAL B 38 4338 3149 3975 -16 -1363 -342 N ATOM 1379 CA VAL B 38 14.796 64.889 16.655 1.00 30.73 C ANISOU 1379 CA VAL B 38 4494 3221 3959 -107 -1267 -242 C ATOM 1380 C VAL B 38 14.917 65.747 17.950 1.00 30.98 C ANISOU 1380 C VAL B 38 4624 3233 3916 -111 -1282 -175 C ATOM 1381 O VAL B 38 14.316 66.832 18.062 1.00 32.09 O ANISOU 1381 O VAL B 38 4740 3448 4005 -160 -1186 -137 O ATOM 1382 CB VAL B 38 13.910 63.629 16.877 1.00 32.00 C ANISOU 1382 CB VAL B 38 4771 3269 4120 -153 -1272 -202 C ATOM 1383 CG1 VAL B 38 12.813 63.879 17.927 1.00 28.82 C ANISOU 1383 CG1 VAL B 38 4498 2828 3623 -238 -1193 -86 C ATOM 1384 CG2 VAL B 38 13.389 63.205 15.526 1.00 30.72 C ANISOU 1384 CG2 VAL B 38 4493 3167 4014 -172 -1220 -271 C ATOM 1385 N SER B 39 15.692 65.285 18.903 1.00 29.91 N ANISOU 1385 N SER B 39 4597 2995 3770 -51 -1411 -172 N ATOM 1386 CA SER B 39 15.894 65.996 20.147 1.00 29.84 C ANISOU 1386 CA SER B 39 4694 2965 3678 -38 -1452 -128 C ATOM 1387 C SER B 39 16.506 67.384 19.932 1.00 28.35 C ANISOU 1387 C SER B 39 4372 2876 3526 -23 -1437 -180 C ATOM 1388 O SER B 39 16.164 68.385 20.594 1.00 26.73 O ANISOU 1388 O SER B 39 4205 2700 3252 -49 -1397 -148 O ATOM 1389 CB SER B 39 16.752 65.122 21.026 1.00 34.01 C ANISOU 1389 CB SER B 39 5355 3367 4201 45 -1625 -131 C ATOM 1390 OG SER B 39 17.129 65.891 22.202 1.00 37.26 O ANISOU 1390 OG SER B 39 5861 3771 4527 79 -1692 -113 O ATOM 1391 N LYS B 40 17.387 67.464 18.954 1.00 29.87 N ANISOU 1391 N LYS B 40 4398 3120 3831 15 -1459 -265 N ATOM 1392 CA LYS B 40 17.967 68.726 18.549 1.00 28.97 C ANISOU 1392 CA LYS B 40 4136 3094 3778 13 -1423 -305 C ATOM 1393 C LYS B 40 16.910 69.692 18.089 1.00 26.91 C ANISOU 1393 C LYS B 40 3835 2917 3472 -67 -1269 -249 C ATOM 1394 O LYS B 40 16.778 70.819 18.582 1.00 25.91 O ANISOU 1394 O LYS B 40 3712 2808 3324 -89 -1244 -229 O ATOM 1395 CB LYS B 40 18.941 68.480 17.403 1.00 31.97 C ANISOU 1395 CB LYS B 40 4341 3528 4280 54 -1432 -394 C ATOM 1396 CG LYS B 40 19.401 69.821 16.785 1.00 33.63 C ANISOU 1396 CG LYS B 40 4387 3835 4556 24 -1352 -412 C ATOM 1397 CD LYS B 40 20.385 69.582 15.667 1.00 34.00 C ANISOU 1397 CD LYS B 40 4259 3949 4712 61 -1335 -496 C ATOM 1398 CE LYS B 40 20.654 70.906 14.966 1.00 38.88 C ANISOU 1398 CE LYS B 40 4730 4661 5381 9 -1220 -480 C ATOM 1399 NZ LYS B 40 22.112 71.061 14.544 1.00 44.48 N ANISOU 1399 NZ LYS B 40 5261 5403 6236 46 -1244 -573 N ATOM 1400 N ILE B 41 16.118 69.251 17.127 1.00 28.30 N ANISOU 1400 N ILE B 41 3972 3142 3639 -103 -1177 -233 N ATOM 1401 CA ILE B 41 14.983 70.063 16.661 1.00 26.24 C ANISOU 1401 CA ILE B 41 3679 2957 3334 -169 -1044 -180 C ATOM 1402 C ILE B 41 14.020 70.406 17.784 1.00 25.12 C ANISOU 1402 C ILE B 41 3666 2775 3103 -208 -1013 -116 C ATOM 1403 O ILE B 41 13.700 71.575 17.925 1.00 24.78 O ANISOU 1403 O ILE B 41 3596 2773 3048 -229 -958 -96 O ATOM 1404 CB ILE B 41 14.257 69.380 15.503 1.00 27.68 C ANISOU 1404 CB ILE B 41 3808 3190 3517 -191 -978 -187 C ATOM 1405 CG1 ILE B 41 15.240 69.341 14.323 1.00 28.63 C ANISOU 1405 CG1 ILE B 41 3789 3383 3706 -147 -982 -255 C ATOM 1406 CG2 ILE B 41 13.000 70.172 15.080 1.00 25.50 C ANISOU 1406 CG2 ILE B 41 3503 2987 3198 -248 -863 -136 C ATOM 1407 CD1 ILE B 41 14.840 68.296 13.320 1.00 28.72 C ANISOU 1407 CD1 ILE B 41 3771 3423 3717 -138 -968 -300 C ATOM 1408 N ILE B 42 13.513 69.434 18.545 1.00 23.62 N ANISOU 1408 N ILE B 42 3614 2508 2852 -220 -1036 -82 N ATOM 1409 CA ILE B 42 12.629 69.746 19.678 1.00 23.97 C ANISOU 1409 CA ILE B 42 3786 2527 2795 -257 -986 -21 C ATOM 1410 C ILE B 42 13.213 70.849 20.555 1.00 25.30 C ANISOU 1410 C ILE B 42 3985 2696 2934 -222 -1034 -38 C ATOM 1411 O ILE B 42 12.543 71.851 20.800 1.00 28.32 O ANISOU 1411 O ILE B 42 4359 3121 3282 -248 -955 -24 O ATOM 1412 CB ILE B 42 12.311 68.504 20.506 1.00 26.15 C ANISOU 1412 CB ILE B 42 4226 2704 3007 -270 -1017 30 C ATOM 1413 CG1 ILE B 42 11.378 67.608 19.660 1.00 26.16 C ANISOU 1413 CG1 ILE B 42 4184 2704 3050 -330 -942 44 C ATOM 1414 CG2 ILE B 42 11.663 68.904 21.825 1.00 26.27 C ANISOU 1414 CG2 ILE B 42 4386 2702 2894 -293 -968 89 C ATOM 1415 CD1 ILE B 42 11.176 66.173 20.227 1.00 29.00 C ANISOU 1415 CD1 ILE B 42 4689 2938 3391 -351 -980 95 C ATOM 1416 N THR B 43 14.472 70.720 20.958 1.00 25.02 N ANISOU 1416 N THR B 43 3967 2612 2929 -156 -1170 -83 N ATOM 1417 CA THR B 43 15.164 71.709 21.808 1.00 25.66 C ANISOU 1417 CA THR B 43 4070 2681 2999 -115 -1248 -123 C ATOM 1418 C THR B 43 15.185 73.095 21.151 1.00 26.09 C ANISOU 1418 C THR B 43 3974 2803 3136 -140 -1181 -150 C ATOM 1419 O THR B 43 14.844 74.101 21.803 1.00 24.92 O ANISOU 1419 O THR B 43 3861 2660 2948 -146 -1160 -154 O ATOM 1420 CB THR B 43 16.616 71.246 22.013 1.00 26.61 C ANISOU 1420 CB THR B 43 4178 2746 3188 -37 -1418 -188 C ATOM 1421 OG1 THR B 43 16.603 69.905 22.485 1.00 27.55 O ANISOU 1421 OG1 THR B 43 4437 2787 3245 -8 -1488 -154 O ATOM 1422 CG2 THR B 43 17.426 72.142 22.902 1.00 27.18 C ANISOU 1422 CG2 THR B 43 4266 2795 3267 11 -1530 -248 C ATOM 1423 N LEU B 44 15.534 73.140 19.856 1.00 24.86 N ANISOU 1423 N LEU B 44 3661 2698 3086 -154 -1142 -165 N ATOM 1424 CA LEU B 44 15.526 74.436 19.164 1.00 25.39 C ANISOU 1424 CA LEU B 44 3600 2820 3229 -183 -1070 -165 C ATOM 1425 C LEU B 44 14.071 75.059 19.189 1.00 24.59 C ANISOU 1425 C LEU B 44 3533 2752 3056 -228 -951 -110 C ATOM 1426 O LEU B 44 13.892 76.248 19.448 1.00 25.49 O ANISOU 1426 O LEU B 44 3628 2865 3190 -235 -929 -114 O ATOM 1427 CB LEU B 44 16.061 74.297 17.729 1.00 25.61 C ANISOU 1427 CB LEU B 44 3473 2908 3349 -191 -1028 -174 C ATOM 1428 CG LEU B 44 17.543 73.879 17.636 1.00 27.32 C ANISOU 1428 CG LEU B 44 3614 3103 3664 -144 -1129 -246 C ATOM 1429 CD1 LEU B 44 17.910 73.756 16.156 1.00 26.96 C ANISOU 1429 CD1 LEU B 44 3419 3140 3685 -154 -1049 -253 C ATOM 1430 CD2 LEU B 44 18.386 74.965 18.283 1.00 28.90 C ANISOU 1430 CD2 LEU B 44 3771 3262 3945 -138 -1197 -288 C ATOM 1431 N THR B 45 13.034 74.255 18.998 1.00 24.22 N ANISOU 1431 N THR B 45 3534 2727 2942 -254 -883 -70 N ATOM 1432 CA THR B 45 11.651 74.806 19.020 1.00 23.58 C ANISOU 1432 CA THR B 45 3463 2683 2815 -292 -774 -33 C ATOM 1433 C THR B 45 11.248 75.300 20.399 1.00 24.23 C ANISOU 1433 C THR B 45 3662 2731 2815 -283 -774 -40 C ATOM 1434 O THR B 45 10.548 76.313 20.522 1.00 26.13 O ANISOU 1434 O THR B 45 3879 2995 3055 -290 -711 -42 O ATOM 1435 CB THR B 45 10.586 73.789 18.494 1.00 23.30 C ANISOU 1435 CB THR B 45 3430 2675 2746 -330 -703 -2 C ATOM 1436 OG1 THR B 45 10.397 72.719 19.441 1.00 22.26 O ANISOU 1436 OG1 THR B 45 3433 2483 2541 -340 -723 15 O ATOM 1437 CG2 THR B 45 11.009 73.243 17.083 1.00 21.12 C ANISOU 1437 CG2 THR B 45 3046 2443 2535 -325 -713 -16 C ATOM 1438 N GLN B 46 11.636 74.586 21.448 1.00 24.95 N ANISOU 1438 N GLN B 46 3886 2767 2828 -261 -843 -45 N ATOM 1439 CA GLN B 46 11.503 75.097 22.859 1.00 27.42 C ANISOU 1439 CA GLN B 46 4329 3052 3036 -234 -864 -64 C ATOM 1440 C GLN B 46 12.247 76.375 23.141 1.00 26.02 C ANISOU 1440 C GLN B 46 4108 2860 2917 -196 -936 -131 C ATOM 1441 O GLN B 46 11.737 77.255 23.846 1.00 26.53 O ANISOU 1441 O GLN B 46 4216 2930 2933 -184 -905 -160 O ATOM 1442 CB GLN B 46 11.842 74.018 23.928 1.00 26.82 C ANISOU 1442 CB GLN B 46 4429 2918 2843 -208 -939 -44 C ATOM 1443 CG GLN B 46 10.964 72.796 23.799 1.00 28.95 C ANISOU 1443 CG GLN B 46 4757 3180 3060 -261 -854 31 C ATOM 1444 CD GLN B 46 11.557 71.628 24.551 1.00 33.99 C ANISOU 1444 CD GLN B 46 5555 3738 3622 -231 -955 65 C ATOM 1445 OE1 GLN B 46 12.779 71.469 24.596 1.00 35.18 O ANISOU 1445 OE1 GLN B 46 5706 3845 3816 -168 -1104 23 O ATOM 1446 NE2 GLN B 46 10.708 70.818 25.164 1.00 36.05 N ANISOU 1446 NE2 GLN B 46 5950 3973 3776 -275 -875 142 N ATOM 1447 N GLU B 47 13.415 76.529 22.553 1.00 27.46 N ANISOU 1447 N GLU B 47 4191 3023 3219 -179 -1025 -163 N ATOM 1448 CA GLU B 47 14.158 77.821 22.679 1.00 31.26 C ANISOU 1448 CA GLU B 47 4600 3477 3800 -159 -1089 -228 C ATOM 1449 C GLU B 47 13.350 78.900 21.959 1.00 32.14 C ANISOU 1449 C GLU B 47 4616 3621 3973 -196 -976 -203 C ATOM 1450 O GLU B 47 13.079 80.002 22.522 1.00 31.47 O ANISOU 1450 O GLU B 47 4548 3512 3897 -182 -977 -244 O ATOM 1451 CB GLU B 47 15.544 77.732 22.024 1.00 36.28 C ANISOU 1451 CB GLU B 47 5114 4092 4576 -151 -1178 -261 C ATOM 1452 CG GLU B 47 16.602 77.069 22.873 1.00 41.29 C ANISOU 1452 CG GLU B 47 5821 4675 5194 -92 -1338 -320 C ATOM 1453 CD GLU B 47 16.845 77.899 24.144 1.00 57.76 C ANISOU 1453 CD GLU B 47 7993 6714 7240 -49 -1439 -396 C ATOM 1454 OE1 GLU B 47 17.284 79.098 24.047 1.00 63.75 O ANISOU 1454 OE1 GLU B 47 8651 7446 8123 -60 -1465 -452 O ATOM 1455 OE2 GLU B 47 16.564 77.364 25.252 1.00 57.32 O ANISOU 1455 OE2 GLU B 47 8115 6642 7022 -5 -1491 -398 O ATOM 1456 N PHE B 48 12.899 78.556 20.732 1.00 29.85 N ANISOU 1456 N PHE B 48 4238 3384 3720 -233 -887 -141 N ATOM 1457 CA PHE B 48 12.152 79.515 19.915 1.00 27.66 C ANISOU 1457 CA PHE B 48 3873 3138 3500 -257 -796 -106 C ATOM 1458 C PHE B 48 10.850 79.918 20.622 1.00 27.09 C ANISOU 1458 C PHE B 48 3871 3076 3346 -250 -728 -112 C ATOM 1459 O PHE B 48 10.531 81.125 20.694 1.00 27.32 O ANISOU 1459 O PHE B 48 3869 3084 3429 -238 -713 -132 O ATOM 1460 CB PHE B 48 11.829 78.846 18.601 1.00 26.91 C ANISOU 1460 CB PHE B 48 3701 3108 3416 -283 -730 -47 C ATOM 1461 CG PHE B 48 11.122 79.724 17.620 1.00 24.37 C ANISOU 1461 CG PHE B 48 3295 2823 3143 -297 -654 -1 C ATOM 1462 CD1 PHE B 48 9.713 79.782 17.635 1.00 23.11 C ANISOU 1462 CD1 PHE B 48 3152 2697 2929 -298 -582 15 C ATOM 1463 CD2 PHE B 48 11.835 80.387 16.625 1.00 22.54 C ANISOU 1463 CD2 PHE B 48 2964 2593 3006 -307 -651 33 C ATOM 1464 CE1 PHE B 48 9.029 80.517 16.716 1.00 22.58 C ANISOU 1464 CE1 PHE B 48 3013 2663 2905 -296 -533 56 C ATOM 1465 CE2 PHE B 48 11.140 81.122 15.668 1.00 24.87 C ANISOU 1465 CE2 PHE B 48 3203 2921 3327 -312 -588 94 C ATOM 1466 CZ PHE B 48 9.740 81.227 15.729 1.00 22.15 C ANISOU 1466 CZ PHE B 48 2882 2604 2931 -299 -542 102 C ATOM 1467 N ARG B 49 10.109 78.937 21.124 1.00 24.21 N ANISOU 1467 N ARG B 49 3594 2740 2867 -258 -683 -98 N ATOM 1468 CA ARG B 49 8.867 79.198 21.888 1.00 25.83 C ANISOU 1468 CA ARG B 49 3860 2967 2987 -256 -598 -111 C ATOM 1469 C ARG B 49 9.054 80.091 23.107 1.00 27.93 C ANISOU 1469 C ARG B 49 4207 3195 3211 -211 -640 -183 C ATOM 1470 O ARG B 49 8.185 80.968 23.374 1.00 30.68 O ANISOU 1470 O ARG B 49 4542 3557 3560 -194 -576 -217 O ATOM 1471 CB ARG B 49 8.151 77.915 22.330 1.00 25.13 C ANISOU 1471 CB ARG B 49 3859 2905 2786 -287 -533 -76 C ATOM 1472 CG ARG B 49 6.756 78.154 22.927 1.00 26.07 C ANISOU 1472 CG ARG B 49 4005 3065 2837 -299 -408 -85 C ATOM 1473 CD ARG B 49 5.673 78.372 21.843 1.00 26.68 C ANISOU 1473 CD ARG B 49 3942 3196 2999 -326 -321 -67 C ATOM 1474 NE ARG B 49 5.598 77.211 20.970 1.00 25.06 N ANISOU 1474 NE ARG B 49 3697 3007 2819 -372 -315 -17 N ATOM 1475 CZ ARG B 49 4.856 76.123 21.243 1.00 27.09 C ANISOU 1475 CZ ARG B 49 3994 3276 3025 -424 -242 9 C ATOM 1476 NH1 ARG B 49 4.085 76.101 22.336 1.00 26.18 N ANISOU 1476 NH1 ARG B 49 3953 3171 2823 -440 -148 3 N ATOM 1477 NH2 ARG B 49 4.869 75.053 20.430 1.00 26.51 N ANISOU 1477 NH2 ARG B 49 3883 3199 2989 -463 -256 40 N ATOM 1478 N ARG B 50 10.158 79.908 23.845 1.00 29.72 N ANISOU 1478 N ARG B 50 4513 3373 3406 -181 -756 -222 N ATOM 1479 CA ARG B 50 10.459 80.742 25.009 1.00 33.90 C ANISOU 1479 CA ARG B 50 5125 3864 3891 -128 -825 -311 C ATOM 1480 C ARG B 50 10.560 82.207 24.624 1.00 30.62 C ANISOU 1480 C ARG B 50 4603 3410 3621 -117 -843 -360 C ATOM 1481 O ARG B 50 10.142 83.061 25.368 1.00 31.24 O ANISOU 1481 O ARG B 50 4723 3474 3672 -78 -839 -433 O ATOM 1482 CB ARG B 50 11.769 80.341 25.651 1.00 42.07 C ANISOU 1482 CB ARG B 50 6233 4849 4902 -92 -980 -351 C ATOM 1483 CG ARG B 50 11.589 79.312 26.724 1.00 57.45 C ANISOU 1483 CG ARG B 50 8363 6811 6654 -69 -989 -335 C ATOM 1484 CD ARG B 50 12.870 79.108 27.522 1.00 73.84 C ANISOU 1484 CD ARG B 50 10526 8832 8697 -8 -1175 -395 C ATOM 1485 NE ARG B 50 13.190 80.253 28.383 1.00 85.84 N ANISOU 1485 NE ARG B 50 12082 10324 10210 49 -1263 -512 N ATOM 1486 CZ ARG B 50 12.644 80.479 29.580 1.00 87.96 C ANISOU 1486 CZ ARG B 50 12506 10617 10297 98 -1247 -560 C ATOM 1487 NH1 ARG B 50 11.727 79.646 30.068 1.00 87.94 N ANISOU 1487 NH1 ARG B 50 12637 10669 10106 85 -1127 -485 N ATOM 1488 NH2 ARG B 50 13.016 81.546 30.285 1.00 90.55 N ANISOU 1488 NH2 ARG B 50 12856 10914 10636 157 -1346 -688 N ATOM 1489 N HIS B 51 11.152 82.497 23.477 1.00 29.11 N ANISOU 1489 N HIS B 51 4281 3195 3584 -148 -864 -320 N ATOM 1490 CA HIS B 51 11.225 83.892 23.026 1.00 28.95 C ANISOU 1490 CA HIS B 51 4165 3120 3714 -148 -874 -342 C ATOM 1491 C HIS B 51 9.854 84.360 22.637 1.00 28.90 C ANISOU 1491 C HIS B 51 4128 3151 3703 -145 -759 -313 C ATOM 1492 O HIS B 51 9.521 85.475 22.895 1.00 28.88 O ANISOU 1492 O HIS B 51 4112 3100 3760 -115 -764 -364 O ATOM 1493 CB HIS B 51 12.152 84.026 21.793 1.00 29.58 C ANISOU 1493 CB HIS B 51 4116 3177 3948 -192 -896 -281 C ATOM 1494 CG HIS B 51 13.595 83.749 22.100 1.00 31.67 C ANISOU 1494 CG HIS B 51 4369 3397 4267 -193 -1015 -328 C ATOM 1495 ND1 HIS B 51 14.373 84.627 22.772 1.00 32.80 N ANISOU 1495 ND1 HIS B 51 4505 3454 4502 -176 -1123 -419 N ATOM 1496 CD2 HIS B 51 14.383 82.675 21.822 1.00 30.39 C ANISOU 1496 CD2 HIS B 51 4191 3263 4092 -203 -1052 -309 C ATOM 1497 CE1 HIS B 51 15.584 84.120 22.915 1.00 33.50 C ANISOU 1497 CE1 HIS B 51 4569 3524 4636 -176 -1224 -455 C ATOM 1498 NE2 HIS B 51 15.596 82.926 22.338 1.00 33.22 N ANISOU 1498 NE2 HIS B 51 4529 3559 4536 -189 -1180 -388 N ATOM 1499 N TYR B 52 9.069 83.554 21.929 1.00 27.27 N ANISOU 1499 N TYR B 52 3893 3020 3447 -173 -667 -237 N ATOM 1500 CA TYR B 52 7.736 84.017 21.503 1.00 27.97 C ANISOU 1500 CA TYR B 52 3932 3146 3551 -163 -572 -220 C ATOM 1501 C TYR B 52 6.955 84.358 22.777 1.00 30.37 C ANISOU 1501 C TYR B 52 4317 3457 3765 -119 -534 -309 C ATOM 1502 O TYR B 52 6.356 85.426 22.879 1.00 31.03 O ANISOU 1502 O TYR B 52 4367 3514 3910 -79 -517 -358 O ATOM 1503 CB TYR B 52 6.986 82.921 20.727 1.00 25.74 C ANISOU 1503 CB TYR B 52 3615 2949 3218 -199 -491 -150 C ATOM 1504 CG TYR B 52 5.548 83.246 20.407 1.00 28.15 C ANISOU 1504 CG TYR B 52 3861 3300 3534 -185 -403 -149 C ATOM 1505 CD1 TYR B 52 4.557 82.930 21.330 1.00 28.70 C ANISOU 1505 CD1 TYR B 52 3977 3413 3514 -178 -321 -199 C ATOM 1506 CD2 TYR B 52 5.162 83.864 19.173 1.00 27.11 C ANISOU 1506 CD2 TYR B 52 3624 3173 3502 -174 -401 -99 C ATOM 1507 CE1 TYR B 52 3.268 83.225 21.071 1.00 29.33 C ANISOU 1507 CE1 TYR B 52 3982 3538 3624 -162 -243 -215 C ATOM 1508 CE2 TYR B 52 3.821 84.155 18.884 1.00 25.30 C ANISOU 1508 CE2 TYR B 52 3332 2986 3294 -148 -341 -111 C ATOM 1509 CZ TYR B 52 2.898 83.829 19.872 1.00 30.36 C ANISOU 1509 CZ TYR B 52 4002 3668 3865 -143 -262 -178 C ATOM 1510 OH TYR B 52 1.524 84.048 19.779 1.00 32.61 O ANISOU 1510 OH TYR B 52 4211 4002 4178 -117 -191 -214 O ATOM 1511 N ASP B 53 6.961 83.438 23.744 1.00 32.05 N ANISOU 1511 N ASP B 53 4643 3705 3830 -122 -518 -329 N ATOM 1512 CA ASP B 53 6.201 83.611 24.957 1.00 32.19 C ANISOU 1512 CA ASP B 53 4750 3752 3727 -84 -457 -405 C ATOM 1513 C ASP B 53 6.657 84.799 25.753 1.00 35.26 C ANISOU 1513 C ASP B 53 5180 4076 4142 -20 -540 -517 C ATOM 1514 O ASP B 53 5.879 85.260 26.545 1.00 35.64 O ANISOU 1514 O ASP B 53 5269 4150 4121 25 -478 -596 O ATOM 1515 CB ASP B 53 6.283 82.396 25.875 1.00 31.82 C ANISOU 1515 CB ASP B 53 4845 3745 3500 -101 -432 -387 C ATOM 1516 CG ASP B 53 5.512 81.230 25.337 1.00 34.62 C ANISOU 1516 CG ASP B 53 5172 4160 3823 -166 -324 -297 C ATOM 1517 OD1 ASP B 53 4.716 81.396 24.403 1.00 33.89 O ANISOU 1517 OD1 ASP B 53 4953 4098 3826 -188 -257 -271 O ATOM 1518 OD2 ASP B 53 5.717 80.103 25.825 1.00 38.81 O ANISOU 1518 OD2 ASP B 53 5808 4698 4238 -195 -316 -251 O ATOM 1519 N SER B 54 7.900 85.268 25.604 1.00 32.79 N ANISOU 1519 N SER B 54 4852 3680 3928 -16 -676 -536 N ATOM 1520 CA SER B 54 8.325 86.465 26.336 1.00 36.08 C ANISOU 1520 CA SER B 54 5294 4017 4398 42 -769 -658 C ATOM 1521 C SER B 54 7.718 87.741 25.769 1.00 36.26 C ANISOU 1521 C SER B 54 5213 3986 4579 63 -744 -682 C ATOM 1522 O SER B 54 7.588 88.745 26.444 1.00 38.32 O ANISOU 1522 O SER B 54 5498 4192 4872 123 -784 -798 O ATOM 1523 CB SER B 54 9.851 86.592 26.347 1.00 35.03 C ANISOU 1523 CB SER B 54 5154 3800 4354 31 -927 -681 C ATOM 1524 OG SER B 54 10.272 85.457 27.037 1.00 39.75 O ANISOU 1524 OG SER B 54 5867 4446 4791 35 -960 -675 O ATOM 1525 N VAL B 55 7.346 87.707 24.515 1.00 34.61 N ANISOU 1525 N VAL B 55 4896 3787 4468 23 -689 -575 N ATOM 1526 CA VAL B 55 6.958 88.932 23.862 1.00 33.82 C ANISOU 1526 CA VAL B 55 4705 3613 4533 46 -695 -575 C ATOM 1527 C VAL B 55 5.440 88.998 23.744 1.00 34.04 C ANISOU 1527 C VAL B 55 4696 3710 4525 83 -580 -582 C ATOM 1528 O VAL B 55 4.884 90.092 23.833 1.00 33.60 O ANISOU 1528 O VAL B 55 4607 3597 4562 143 -587 -648 O ATOM 1529 CB VAL B 55 7.635 88.940 22.480 1.00 33.23 C ANISOU 1529 CB VAL B 55 4537 3500 4589 -15 -721 -445 C ATOM 1530 CG1 VAL B 55 7.050 89.981 21.571 1.00 34.14 C ANISOU 1530 CG1 VAL B 55 4569 3555 4847 3 -707 -396 C ATOM 1531 CG2 VAL B 55 9.098 89.233 22.685 1.00 35.35 C ANISOU 1531 CG2 VAL B 55 4810 3677 4944 -44 -835 -470 C ATOM 1532 N TYR B 56 4.792 87.845 23.459 1.00 31.65 N ANISOU 1532 N TYR B 56 4386 3521 4116 47 -482 -516 N ATOM 1533 CA TYR B 56 3.356 87.761 23.222 1.00 32.99 C ANISOU 1533 CA TYR B 56 4494 3768 4275 68 -372 -519 C ATOM 1534 C TYR B 56 2.687 86.882 24.258 1.00 35.81 C ANISOU 1534 C TYR B 56 4921 4224 4460 62 -263 -569 C ATOM 1535 O TYR B 56 3.227 85.820 24.583 1.00 33.73 O ANISOU 1535 O TYR B 56 4739 3994 4082 11 -259 -525 O ATOM 1536 CB TYR B 56 3.100 87.197 21.847 1.00 30.94 C ANISOU 1536 CB TYR B 56 4143 3549 4065 22 -351 -397 C ATOM 1537 CG TYR B 56 3.803 87.982 20.771 1.00 29.06 C ANISOU 1537 CG TYR B 56 3851 3223 3968 20 -440 -323 C ATOM 1538 CD1 TYR B 56 3.412 89.313 20.507 1.00 30.00 C ANISOU 1538 CD1 TYR B 56 3921 3258 4219 81 -477 -347 C ATOM 1539 CD2 TYR B 56 4.851 87.404 20.014 1.00 26.03 C ANISOU 1539 CD2 TYR B 56 3465 2836 3590 -41 -482 -227 C ATOM 1540 CE1 TYR B 56 4.076 90.097 19.541 1.00 29.08 C ANISOU 1540 CE1 TYR B 56 3770 3045 4235 72 -550 -259 C ATOM 1541 CE2 TYR B 56 5.517 88.204 19.045 1.00 28.28 C ANISOU 1541 CE2 TYR B 56 3701 3041 4002 -50 -541 -150 C ATOM 1542 CZ TYR B 56 5.119 89.528 18.806 1.00 28.26 C ANISOU 1542 CZ TYR B 56 3664 2948 4123 1 -571 -155 C ATOM 1543 OH TYR B 56 5.754 90.323 17.844 1.00 31.79 O ANISOU 1543 OH TYR B 56 4077 3306 4695 -16 -619 -57 O ATOM 1544 N ARG B 57 1.554 87.348 24.779 1.00 39.79 N ANISOU 1544 N ARG B 57 5396 4769 4952 116 -174 -658 N ATOM 1545 CA ARG B 57 0.619 86.596 25.646 1.00 43.84 C ANISOU 1545 CA ARG B 57 5945 5393 5318 104 -25 -699 C ATOM 1546 C ARG B 57 -0.219 85.510 24.899 1.00 42.69 C ANISOU 1546 C ARG B 57 5712 5331 5176 31 77 -610 C ATOM 1547 O ARG B 57 -0.261 84.381 25.339 1.00 42.58 O ANISOU 1547 O ARG B 57 5767 5373 5038 -33 152 -566 O ATOM 1548 CB ARG B 57 -0.318 87.563 26.381 1.00 48.99 C ANISOU 1548 CB ARG B 57 6569 6065 5981 193 44 -842 C ATOM 1549 CG ARG B 57 -0.185 87.542 27.892 1.00 62.21 C ANISOU 1549 CG ARG B 57 8388 7777 7472 228 93 -945 C ATOM 1550 CD ARG B 57 -0.412 88.925 28.452 1.00 82.06 C ANISOU 1550 CD ARG B 57 10891 10242 10045 340 58 -1106 C ATOM 1551 NE ARG B 57 -0.977 88.955 29.811 1.00103.63 N ANISOU 1551 NE ARG B 57 13711 13064 12601 394 179 -1235 N ATOM 1552 CZ ARG B 57 -2.042 89.684 30.159 1.00118.52 C ANISOU 1552 CZ ARG B 57 15518 14992 14522 475 275 -1369 C ATOM 1553 NH1 ARG B 57 -2.659 90.433 29.250 1.00124.92 N ANISOU 1553 NH1 ARG B 57 16163 15752 15547 516 247 -1386 N ATOM 1554 NH2 ARG B 57 -2.489 89.683 31.413 1.00122.56 N ANISOU 1554 NH2 ARG B 57 16117 15598 14851 524 397 -1488 N ATOM 1555 N ALA B 58 -0.893 85.810 23.792 1.00 40.93 N ANISOU 1555 N ALA B 58 5345 5113 5095 41 71 -584 N ATOM 1556 CA ALA B 58 -1.622 84.767 23.095 1.00 39.23 C ANISOU 1556 CA ALA B 58 5045 4971 4889 -26 143 -518 C ATOM 1557 C ALA B 58 -0.648 83.686 22.621 1.00 40.04 C ANISOU 1557 C ALA B 58 5213 5059 4940 -105 87 -408 C ATOM 1558 O ALA B 58 0.476 83.991 22.173 1.00 37.59 O ANISOU 1558 O ALA B 58 4940 4680 4661 -97 -32 -364 O ATOM 1559 CB ALA B 58 -2.312 85.351 21.891 1.00 38.86 C ANISOU 1559 CB ALA B 58 4846 4921 4999 15 100 -510 C ATOM 1560 N ASP B 59 -1.100 82.426 22.664 1.00 41.74 N ANISOU 1560 N ASP B 59 5429 5334 5096 -182 174 -367 N ATOM 1561 CA ASP B 59 -0.374 81.298 22.097 1.00 41.30 C ANISOU 1561 CA ASP B 59 5413 5265 5013 -252 124 -274 C ATOM 1562 C ASP B 59 -0.765 81.213 20.597 1.00 38.80 C ANISOU 1562 C ASP B 59 4956 4968 4817 -257 78 -238 C ATOM 1563 O ASP B 59 -1.545 82.063 20.128 1.00 38.40 O ANISOU 1563 O ASP B 59 4796 4934 4860 -203 77 -278 O ATOM 1564 CB ASP B 59 -0.696 80.017 22.902 1.00 43.41 C ANISOU 1564 CB ASP B 59 5760 5566 5169 -330 234 -248 C ATOM 1565 CG ASP B 59 -2.121 79.562 22.733 1.00 46.48 C ANISOU 1565 CG ASP B 59 6028 6022 5609 -378 365 -267 C ATOM 1566 OD1 ASP B 59 -2.835 80.048 21.801 1.00 47.31 O ANISOU 1566 OD1 ASP B 59 5978 6154 5843 -349 346 -298 O ATOM 1567 OD2 ASP B 59 -2.536 78.685 23.540 1.00 55.18 O ANISOU 1567 OD2 ASP B 59 7191 7148 6626 -447 487 -248 O ATOM 1568 N TYR B 60 -0.267 80.222 19.844 1.00 34.09 N ANISOU 1568 N TYR B 60 4366 4371 4217 -309 33 -171 N ATOM 1569 CA TYR B 60 -0.657 80.110 18.406 1.00 32.71 C ANISOU 1569 CA TYR B 60 4068 4227 4131 -305 -17 -147 C ATOM 1570 C TYR B 60 -2.120 79.701 18.041 1.00 35.49 C ANISOU 1570 C TYR B 60 4290 4645 4550 -327 52 -188 C ATOM 1571 O TYR B 60 -2.530 79.714 16.831 1.00 34.97 O ANISOU 1571 O TYR B 60 4119 4612 4556 -305 -9 -184 O ATOM 1572 CB TYR B 60 0.258 79.126 17.661 1.00 30.96 C ANISOU 1572 CB TYR B 60 3883 3996 3886 -346 -85 -87 C ATOM 1573 CG TYR B 60 1.753 79.278 17.837 1.00 30.52 C ANISOU 1573 CG TYR B 60 3926 3883 3787 -334 -159 -51 C ATOM 1574 CD1 TYR B 60 2.345 80.524 18.112 1.00 29.35 C ANISOU 1574 CD1 TYR B 60 3802 3689 3660 -281 -202 -59 C ATOM 1575 CD2 TYR B 60 2.585 78.189 17.631 1.00 28.24 C ANISOU 1575 CD2 TYR B 60 3690 3581 3460 -374 -197 -17 C ATOM 1576 CE1 TYR B 60 3.740 80.650 18.262 1.00 30.38 C ANISOU 1576 CE1 TYR B 60 4002 3766 3777 -277 -275 -37 C ATOM 1577 CE2 TYR B 60 3.964 78.307 17.795 1.00 28.90 C ANISOU 1577 CE2 TYR B 60 3843 3616 3523 -359 -269 2 C ATOM 1578 CZ TYR B 60 4.539 79.534 18.087 1.00 29.45 C ANISOU 1578 CZ TYR B 60 3925 3646 3618 -315 -307 -8 C ATOM 1579 OH TYR B 60 5.913 79.626 18.221 1.00 27.60 O ANISOU 1579 OH TYR B 60 3736 3363 3387 -307 -382 0 O ATOM 1580 N GLY B 61 -2.878 79.257 19.039 1.00 36.91 N ANISOU 1580 N GLY B 61 4472 4848 4702 -374 177 -226 N ATOM 1581 CA GLY B 61 -4.152 78.550 18.788 1.00 36.84 C ANISOU 1581 CA GLY B 61 4336 4895 4766 -429 256 -262 C ATOM 1582 C GLY B 61 -5.145 79.291 17.918 1.00 40.60 C ANISOU 1582 C GLY B 61 4643 5417 5368 -363 218 -321 C ATOM 1583 O GLY B 61 -5.714 78.724 16.950 1.00 40.42 O ANISOU 1583 O GLY B 61 4509 5427 5422 -383 176 -333 O ATOM 1584 N PRO B 62 -5.394 80.566 18.229 1.00 43.66 N ANISOU 1584 N PRO B 62 5005 5801 5784 -274 217 -369 N ATOM 1585 CA PRO B 62 -6.450 81.240 17.430 1.00 45.11 C ANISOU 1585 CA PRO B 62 5020 6022 6097 -200 173 -429 C ATOM 1586 C PRO B 62 -6.213 81.200 15.913 1.00 46.08 C ANISOU 1586 C PRO B 62 5102 6147 6258 -165 21 -381 C ATOM 1587 O PRO B 62 -7.178 80.963 15.185 1.00 53.19 O ANISOU 1587 O PRO B 62 5863 7100 7249 -152 -9 -427 O ATOM 1588 CB PRO B 62 -6.468 82.684 17.965 1.00 47.98 C ANISOU 1588 CB PRO B 62 5397 6352 6481 -96 166 -476 C ATOM 1589 CG PRO B 62 -5.567 82.705 19.182 1.00 50.42 C ANISOU 1589 CG PRO B 62 5870 6622 6667 -125 227 -461 C ATOM 1590 CD PRO B 62 -5.042 81.305 19.453 1.00 48.61 C ANISOU 1590 CD PRO B 62 5731 6399 6339 -240 276 -396 C ATOM 1591 N ALA B 63 -4.960 81.368 15.454 1.00 40.33 N ANISOU 1591 N ALA B 63 4491 5372 5459 -151 -68 -294 N ATOM 1592 CA ALA B 63 -4.617 81.310 14.021 1.00 43.07 C ANISOU 1592 CA ALA B 63 4822 5733 5808 -118 -194 -238 C ATOM 1593 C ALA B 63 -4.671 79.924 13.429 1.00 44.47 C ANISOU 1593 C ALA B 63 4975 5954 5967 -191 -204 -238 C ATOM 1594 O ALA B 63 -4.828 79.765 12.230 1.00 50.19 O ANISOU 1594 O ALA B 63 5648 6718 6703 -157 -300 -230 O ATOM 1595 CB ALA B 63 -3.237 81.916 13.750 1.00 40.52 C ANISOU 1595 CB ALA B 63 4621 5352 5424 -91 -259 -147 C ATOM 1596 N LEU B 64 -4.476 78.921 14.262 1.00 46.16 N ANISOU 1596 N LEU B 64 5240 6154 6144 -287 -115 -243 N ATOM 1597 CA LEU B 64 -4.339 77.560 13.782 1.00 47.86 C ANISOU 1597 CA LEU B 64 5457 6382 6347 -360 -131 -239 C ATOM 1598 C LEU B 64 -5.667 76.790 13.815 1.00 50.24 C ANISOU 1598 C LEU B 64 5621 6720 6747 -420 -76 -318 C ATOM 1599 O LEU B 64 -5.711 75.618 13.463 1.00 48.45 O ANISOU 1599 O LEU B 64 5381 6491 6538 -490 -89 -330 O ATOM 1600 CB LEU B 64 -3.206 76.843 14.530 1.00 42.11 C ANISOU 1600 CB LEU B 64 4876 5596 5528 -425 -94 -185 C ATOM 1601 CG LEU B 64 -1.808 77.387 14.240 1.00 40.75 C ANISOU 1601 CG LEU B 64 4807 5393 5284 -376 -169 -120 C ATOM 1602 CD1 LEU B 64 -0.848 76.587 15.050 1.00 35.30 C ANISOU 1602 CD1 LEU B 64 4242 4647 4524 -434 -142 -88 C ATOM 1603 CD2 LEU B 64 -1.409 77.279 12.752 1.00 43.28 C ANISOU 1603 CD2 LEU B 64 5097 5751 5597 -334 -275 -99 C ATOM 1604 N LYS B 65 -6.751 77.467 14.194 1.00 56.79 N ANISOU 1604 N LYS B 65 6339 7580 7658 -391 -20 -380 N ATOM 1605 CA LYS B 65 -8.104 76.880 14.146 1.00 61.67 C ANISOU 1605 CA LYS B 65 6788 8241 8404 -443 32 -470 C ATOM 1606 C LYS B 65 -8.375 76.197 12.811 1.00 61.63 C ANISOU 1606 C LYS B 65 6695 8266 8453 -439 -99 -505 C ATOM 1607 O LYS B 65 -9.075 75.190 12.755 1.00 61.11 O ANISOU 1607 O LYS B 65 6533 8206 8478 -527 -67 -563 O ATOM 1608 CB LYS B 65 -9.185 77.930 14.421 1.00 66.37 C ANISOU 1608 CB LYS B 65 7247 8877 9095 -371 69 -548 C ATOM 1609 CG LYS B 65 -9.108 78.459 15.854 1.00 73.64 C ANISOU 1609 CG LYS B 65 8237 9778 9964 -383 220 -545 C ATOM 1610 CD LYS B 65 -10.366 79.173 16.325 1.00 77.93 C ANISOU 1610 CD LYS B 65 8618 10371 10621 -338 305 -651 C ATOM 1611 CE LYS B 65 -10.316 79.247 17.850 1.00 83.01 C ANISOU 1611 CE LYS B 65 9343 11009 11186 -386 492 -654 C ATOM 1612 NZ LYS B 65 -11.104 80.387 18.386 1.00 87.52 N ANISOU 1612 NZ LYS B 65 9816 11617 11822 -293 554 -753 N ATOM 1613 N ASN B 66 -7.780 76.724 11.747 1.00 57.97 N ANISOU 1613 N ASN B 66 6275 7820 7931 -342 -243 -470 N ATOM 1614 CA ASN B 66 -8.063 76.276 10.392 1.00 56.03 C ANISOU 1614 CA ASN B 66 5956 7621 7711 -306 -384 -513 C ATOM 1615 C ASN B 66 -6.792 75.759 9.702 1.00 49.31 C ANISOU 1615 C ASN B 66 5242 6759 6734 -304 -457 -446 C ATOM 1616 O ASN B 66 -6.614 75.901 8.463 1.00 45.55 O ANISOU 1616 O ASN B 66 4765 6333 6209 -224 -588 -446 O ATOM 1617 CB ASN B 66 -8.657 77.460 9.613 1.00 64.14 C ANISOU 1617 CB ASN B 66 6902 8697 8770 -169 -496 -535 C ATOM 1618 CG ASN B 66 -10.166 77.491 9.637 1.00 70.71 C ANISOU 1618 CG ASN B 66 7529 9570 9766 -159 -498 -657 C ATOM 1619 OD1 ASN B 66 -10.842 76.632 9.047 1.00 72.93 O ANISOU 1619 OD1 ASN B 66 7694 9887 10130 -194 -557 -744 O ATOM 1620 ND2 ASN B 66 -10.705 78.503 10.292 1.00 70.77 N ANISOU 1620 ND2 ASN B 66 7481 9573 9834 -106 -441 -677 N ATOM 1621 N TRP B 67 -5.907 75.165 10.499 1.00 40.98 N ANISOU 1621 N TRP B 67 4306 5644 5622 -384 -372 -393 N ATOM 1622 CA TRP B 67 -4.676 74.679 9.982 1.00 36.26 C ANISOU 1622 CA TRP B 67 3824 5031 4921 -381 -427 -342 C ATOM 1623 C TRP B 67 -4.912 73.725 8.797 1.00 35.83 C ANISOU 1623 C TRP B 67 3712 5019 4883 -378 -534 -413 C ATOM 1624 O TRP B 67 -4.139 73.689 7.794 1.00 32.18 O ANISOU 1624 O TRP B 67 3305 4596 4327 -316 -623 -394 O ATOM 1625 CB TRP B 67 -3.893 74.020 11.109 1.00 32.22 C ANISOU 1625 CB TRP B 67 3429 4441 4373 -469 -332 -296 C ATOM 1626 CG TRP B 67 -4.427 72.683 11.512 1.00 31.07 C ANISOU 1626 CG TRP B 67 3250 4253 4302 -579 -282 -343 C ATOM 1627 CD1 TRP B 67 -5.373 72.420 12.495 1.00 32.20 C ANISOU 1627 CD1 TRP B 67 3338 4370 4528 -664 -162 -365 C ATOM 1628 CD2 TRP B 67 -4.060 71.382 10.966 1.00 30.02 C ANISOU 1628 CD2 TRP B 67 3139 4088 4179 -624 -341 -373 C ATOM 1629 NE1 TRP B 67 -5.616 71.090 12.568 1.00 33.49 N ANISOU 1629 NE1 TRP B 67 3489 4480 4757 -765 -143 -393 N ATOM 1630 CE2 TRP B 67 -4.846 70.405 11.701 1.00 32.80 C ANISOU 1630 CE2 TRP B 67 3449 4377 4634 -744 -254 -402 C ATOM 1631 CE3 TRP B 67 -3.209 70.949 9.958 1.00 29.31 C ANISOU 1631 CE3 TRP B 67 3094 4015 4029 -576 -447 -385 C ATOM 1632 CZ2 TRP B 67 -4.810 69.058 11.398 1.00 35.85 C ANISOU 1632 CZ2 TRP B 67 3838 4704 5081 -814 -292 -443 C ATOM 1633 CZ3 TRP B 67 -3.119 69.608 9.691 1.00 29.51 C ANISOU 1633 CZ3 TRP B 67 3123 3990 4098 -633 -485 -437 C ATOM 1634 CH2 TRP B 67 -3.903 68.662 10.381 1.00 35.98 C ANISOU 1634 CH2 TRP B 67 3903 4731 5035 -751 -418 -466 C ATOM 1635 N LYS B 68 -5.990 72.952 8.881 1.00 37.31 N ANISOU 1635 N LYS B 68 3780 5203 5192 -443 -523 -504 N ATOM 1636 CA LYS B 68 -6.218 71.941 7.884 1.00 41.75 C ANISOU 1636 CA LYS B 68 4287 5788 5787 -452 -628 -592 C ATOM 1637 C LYS B 68 -6.304 72.581 6.501 1.00 39.93 C ANISOU 1637 C LYS B 68 4026 5656 5489 -320 -776 -617 C ATOM 1638 O LYS B 68 -5.849 71.998 5.531 1.00 41.14 O ANISOU 1638 O LYS B 68 4212 5844 5574 -285 -872 -653 O ATOM 1639 CB LYS B 68 -7.459 71.118 8.178 1.00 43.76 C ANISOU 1639 CB LYS B 68 4395 6016 6214 -548 -598 -693 C ATOM 1640 CG LYS B 68 -7.220 69.671 7.795 1.00 49.43 C ANISOU 1640 CG LYS B 68 5127 6682 6971 -620 -647 -753 C ATOM 1641 CD LYS B 68 -8.418 68.791 8.110 1.00 55.16 C ANISOU 1641 CD LYS B 68 5704 7360 7894 -738 -610 -849 C ATOM 1642 CE LYS B 68 -8.809 68.885 9.579 1.00 60.08 C ANISOU 1642 CE LYS B 68 6325 7922 8580 -847 -416 -782 C ATOM 1643 NZ LYS B 68 -9.376 67.552 9.979 1.00 72.34 N ANISOU 1643 NZ LYS B 68 7817 9378 10292 -1002 -356 -828 N ATOM 1644 N ARG B 69 -6.823 73.793 6.473 1.00 36.40 N ANISOU 1644 N ARG B 69 3533 5248 5049 -242 -788 -592 N ATOM 1645 CA ARG B 69 -6.974 74.581 5.271 1.00 38.48 C ANISOU 1645 CA ARG B 69 3785 5595 5241 -107 -925 -589 C ATOM 1646 C ARG B 69 -5.795 75.516 5.097 1.00 38.46 C ANISOU 1646 C ARG B 69 3930 5594 5090 -42 -911 -453 C ATOM 1647 O ARG B 69 -5.341 75.685 4.001 1.00 39.22 O ANISOU 1647 O ARG B 69 4082 5752 5068 39 -1001 -425 O ATOM 1648 CB ARG B 69 -8.231 75.444 5.363 1.00 40.04 C ANISOU 1648 CB ARG B 69 3847 5817 5551 -50 -956 -635 C ATOM 1649 CG ARG B 69 -8.770 75.864 4.014 1.00 45.01 C ANISOU 1649 CG ARG B 69 4426 6533 6143 84 -1138 -678 C ATOM 1650 CD ARG B 69 -9.450 77.224 3.976 1.00 47.95 C ANISOU 1650 CD ARG B 69 4746 6918 6555 196 -1186 -651 C ATOM 1651 NE ARG B 69 -10.480 77.479 4.970 1.00 55.67 N ANISOU 1651 NE ARG B 69 5577 7862 7713 157 -1106 -722 N ATOM 1652 CZ ARG B 69 -10.431 78.456 5.880 1.00 59.59 C ANISOU 1652 CZ ARG B 69 6095 8308 8239 170 -1006 -662 C ATOM 1653 NH1 ARG B 69 -9.397 79.266 5.985 1.00 61.77 N ANISOU 1653 NH1 ARG B 69 6530 8544 8395 207 -977 -528 N ATOM 1654 NH2 ARG B 69 -11.412 78.616 6.734 1.00 64.65 N ANISOU 1654 NH2 ARG B 69 6592 8936 9038 140 -926 -745 N ATOM 1655 N ASP B 70 -5.295 76.115 6.171 1.00 35.12 N ANISOU 1655 N ASP B 70 3570 5103 4671 -78 -795 -372 N ATOM 1656 CA ASP B 70 -4.445 77.315 6.050 1.00 33.30 C ANISOU 1656 CA ASP B 70 3443 4861 4349 -10 -791 -250 C ATOM 1657 C ASP B 70 -2.941 77.176 6.347 1.00 30.21 C ANISOU 1657 C ASP B 70 3183 4429 3865 -52 -725 -165 C ATOM 1658 O ASP B 70 -2.165 78.144 6.177 1.00 27.90 O ANISOU 1658 O ASP B 70 2968 4124 3512 -7 -720 -64 O ATOM 1659 CB ASP B 70 -4.989 78.367 6.994 1.00 35.78 C ANISOU 1659 CB ASP B 70 3722 5123 4748 4 -732 -233 C ATOM 1660 CG ASP B 70 -6.290 78.916 6.559 1.00 37.74 C ANISOU 1660 CG ASP B 70 3846 5411 5081 85 -814 -295 C ATOM 1661 OD1 ASP B 70 -6.731 78.785 5.397 1.00 42.32 O ANISOU 1661 OD1 ASP B 70 4384 6062 5635 156 -941 -329 O ATOM 1662 OD2 ASP B 70 -6.914 79.538 7.414 1.00 42.35 O ANISOU 1662 OD2 ASP B 70 4371 5959 5762 88 -756 -321 O ATOM 1663 N LEU B 71 -2.503 75.980 6.732 1.00 29.59 N ANISOU 1663 N LEU B 71 3127 4326 3788 -135 -685 -205 N ATOM 1664 CA LEU B 71 -1.149 75.826 7.252 1.00 29.48 C ANISOU 1664 CA LEU B 71 3222 4262 3718 -175 -624 -142 C ATOM 1665 C LEU B 71 -0.138 76.141 6.149 1.00 31.77 C ANISOU 1665 C LEU B 71 3571 4607 3894 -112 -668 -81 C ATOM 1666 O LEU B 71 0.831 76.824 6.404 1.00 29.88 O ANISOU 1666 O LEU B 71 3397 4334 3621 -109 -627 3 O ATOM 1667 CB LEU B 71 -0.897 74.416 7.797 1.00 28.42 C ANISOU 1667 CB LEU B 71 3106 4082 3610 -263 -592 -197 C ATOM 1668 CG LEU B 71 0.298 74.350 8.764 1.00 28.78 C ANISOU 1668 CG LEU B 71 3255 4053 3628 -305 -527 -139 C ATOM 1669 CD1 LEU B 71 0.149 75.279 9.969 1.00 25.73 C ANISOU 1669 CD1 LEU B 71 2893 3612 3272 -320 -455 -95 C ATOM 1670 CD2 LEU B 71 0.383 72.914 9.193 1.00 27.37 C ANISOU 1670 CD2 LEU B 71 3096 3822 3480 -380 -516 -191 C ATOM 1671 N SER B 72 -0.361 75.691 4.911 1.00 33.93 N ANISOU 1671 N SER B 72 3819 4967 4105 -61 -749 -125 N ATOM 1672 CA SER B 72 0.657 75.896 3.883 1.00 34.00 C ANISOU 1672 CA SER B 72 3892 5041 3984 -7 -766 -66 C ATOM 1673 C SER B 72 0.783 77.399 3.496 1.00 33.90 C ANISOU 1673 C SER B 72 3916 5039 3926 58 -765 58 C ATOM 1674 O SER B 72 1.860 77.928 3.087 1.00 37.88 O ANISOU 1674 O SER B 72 4485 5556 4351 73 -725 154 O ATOM 1675 CB SER B 72 0.389 74.971 2.713 1.00 36.62 C ANISOU 1675 CB SER B 72 4200 5468 4246 36 -851 -159 C ATOM 1676 OG SER B 72 -0.092 75.678 1.610 1.00 45.64 O ANISOU 1676 OG SER B 72 5343 6700 5299 133 -928 -128 O ATOM 1677 N LYS B 73 -0.285 78.122 3.736 1.00 33.24 N ANISOU 1677 N LYS B 73 3785 4933 3912 89 -798 59 N ATOM 1678 CA LYS B 73 -0.310 79.555 3.591 1.00 35.16 C ANISOU 1678 CA LYS B 73 4059 5149 4150 147 -805 171 C ATOM 1679 C LYS B 73 0.586 80.208 4.630 1.00 33.02 C ANISOU 1679 C LYS B 73 3838 4776 3934 91 -712 242 C ATOM 1680 O LYS B 73 1.273 81.190 4.332 1.00 35.28 O ANISOU 1680 O LYS B 73 4181 5034 4189 113 -694 357 O ATOM 1681 CB LYS B 73 -1.739 80.026 3.816 1.00 39.00 C ANISOU 1681 CB LYS B 73 4463 5623 4734 193 -866 120 C ATOM 1682 CG LYS B 73 -2.114 81.245 3.028 1.00 47.13 C ANISOU 1682 CG LYS B 73 5516 6662 5729 300 -944 209 C ATOM 1683 CD LYS B 73 -3.609 81.548 3.154 1.00 47.69 C ANISOU 1683 CD LYS B 73 5479 6732 5907 360 -1026 126 C ATOM 1684 CE LYS B 73 -4.137 81.430 4.565 1.00 50.94 C ANISOU 1684 CE LYS B 73 5810 7074 6470 291 -945 42 C ATOM 1685 NZ LYS B 73 -5.412 82.213 4.633 1.00 60.57 N ANISOU 1685 NZ LYS B 73 6933 8281 7799 375 -1015 -5 N ATOM 1686 N LEU B 74 0.533 79.691 5.861 1.00 30.65 N ANISOU 1686 N LEU B 74 3515 4414 3716 17 -657 175 N ATOM 1687 CA LEU B 74 1.394 80.164 6.975 1.00 29.03 C ANISOU 1687 CA LEU B 74 3359 4113 3556 -35 -583 216 C ATOM 1688 C LEU B 74 2.829 79.886 6.588 1.00 27.35 C ANISOU 1688 C LEU B 74 3202 3913 3277 -60 -555 267 C ATOM 1689 O LEU B 74 3.658 80.748 6.645 1.00 27.36 O ANISOU 1689 O LEU B 74 3241 3867 3287 -62 -527 349 O ATOM 1690 CB LEU B 74 1.058 79.473 8.308 1.00 27.19 C ANISOU 1690 CB LEU B 74 3110 3831 3389 -102 -533 133 C ATOM 1691 CG LEU B 74 1.962 79.920 9.498 1.00 29.37 C ANISOU 1691 CG LEU B 74 3450 4016 3694 -143 -477 161 C ATOM 1692 CD1 LEU B 74 1.936 81.438 9.734 1.00 26.81 C ANISOU 1692 CD1 LEU B 74 3136 3629 3420 -100 -480 216 C ATOM 1693 CD2 LEU B 74 1.568 79.182 10.769 1.00 26.64 C ANISOU 1693 CD2 LEU B 74 3111 3635 3378 -202 -427 89 C ATOM 1694 N PHE B 75 3.097 78.694 6.098 1.00 26.48 N ANISOU 1694 N PHE B 75 3086 3865 3109 -75 -565 212 N ATOM 1695 CA PHE B 75 4.454 78.299 5.788 1.00 25.77 C ANISOU 1695 CA PHE B 75 3031 3793 2967 -94 -533 234 C ATOM 1696 C PHE B 75 5.045 79.137 4.684 1.00 26.67 C ANISOU 1696 C PHE B 75 3169 3959 3005 -50 -521 337 C ATOM 1697 O PHE B 75 6.214 79.585 4.775 1.00 27.17 O ANISOU 1697 O PHE B 75 3253 3992 3078 -77 -466 402 O ATOM 1698 CB PHE B 75 4.488 76.797 5.430 1.00 27.06 C ANISOU 1698 CB PHE B 75 3179 4011 3092 -105 -558 134 C ATOM 1699 CG PHE B 75 4.249 75.879 6.628 1.00 26.62 C ANISOU 1699 CG PHE B 75 3122 3877 3113 -168 -550 58 C ATOM 1700 CD1 PHE B 75 4.480 76.357 7.959 1.00 25.66 C ANISOU 1700 CD1 PHE B 75 3032 3660 3058 -211 -508 86 C ATOM 1701 CD2 PHE B 75 3.905 74.558 6.443 1.00 23.66 C ANISOU 1701 CD2 PHE B 75 2728 3519 2741 -185 -584 -36 C ATOM 1702 CE1 PHE B 75 4.311 75.509 9.061 1.00 25.74 C ANISOU 1702 CE1 PHE B 75 3066 3604 3112 -266 -494 34 C ATOM 1703 CE2 PHE B 75 3.769 73.704 7.554 1.00 27.27 C ANISOU 1703 CE2 PHE B 75 3203 3891 3266 -251 -568 -82 C ATOM 1704 CZ PHE B 75 3.987 74.168 8.873 1.00 24.47 C ANISOU 1704 CZ PHE B 75 2892 3451 2953 -291 -519 -39 C ATOM 1705 N THR B 76 4.257 79.358 3.632 1.00 28.57 N ANISOU 1705 N THR B 76 3405 4278 3171 17 -573 357 N ATOM 1706 CA THR B 76 4.714 80.083 2.481 1.00 29.43 C ANISOU 1706 CA THR B 76 3556 4448 3177 65 -560 468 C ATOM 1707 C THR B 76 5.115 81.502 2.972 1.00 31.45 C ANISOU 1707 C THR B 76 3841 4597 3513 45 -517 593 C ATOM 1708 O THR B 76 6.137 82.065 2.569 1.00 33.16 O ANISOU 1708 O THR B 76 4088 4808 3703 26 -452 695 O ATOM 1709 CB THR B 76 3.542 80.215 1.463 1.00 33.63 C ANISOU 1709 CB THR B 76 4089 5064 3624 155 -654 466 C ATOM 1710 OG1 THR B 76 3.240 78.940 0.897 1.00 33.37 O ANISOU 1710 OG1 THR B 76 4029 5130 3520 176 -703 343 O ATOM 1711 CG2 THR B 76 3.882 81.149 0.352 1.00 32.24 C ANISOU 1711 CG2 THR B 76 3982 4937 3331 212 -644 611 C ATOM 1712 N SER B 77 4.286 82.093 3.819 1.00 29.80 N ANISOU 1712 N SER B 77 3613 4298 3409 48 -551 578 N ATOM 1713 CA SER B 77 4.515 83.431 4.291 1.00 31.96 C ANISOU 1713 CA SER B 77 3913 4458 3773 41 -532 672 C ATOM 1714 C SER B 77 5.773 83.496 5.155 1.00 31.77 C ANISOU 1714 C SER B 77 3892 4356 3824 -41 -461 675 C ATOM 1715 O SER B 77 6.511 84.453 5.144 1.00 31.77 O ANISOU 1715 O SER B 77 3914 4283 3874 -64 -426 771 O ATOM 1716 CB SER B 77 3.307 83.845 5.166 1.00 33.47 C ANISOU 1716 CB SER B 77 4070 4580 4067 68 -581 609 C ATOM 1717 OG SER B 77 3.497 85.148 5.653 1.00 41.13 O ANISOU 1717 OG SER B 77 5065 5428 5133 70 -574 681 O ATOM 1718 N LEU B 78 6.021 82.435 5.904 1.00 29.60 N ANISOU 1718 N LEU B 78 3593 4089 3563 -84 -450 566 N ATOM 1719 CA LEU B 78 7.140 82.387 6.812 1.00 29.82 C ANISOU 1719 CA LEU B 78 3623 4045 3662 -147 -410 546 C ATOM 1720 C LEU B 78 8.485 82.397 6.076 1.00 29.47 C ANISOU 1720 C LEU B 78 3573 4036 3589 -174 -353 610 C ATOM 1721 O LEU B 78 9.541 82.752 6.629 1.00 30.65 O ANISOU 1721 O LEU B 78 3710 4115 3821 -224 -322 622 O ATOM 1722 CB LEU B 78 6.965 81.128 7.634 1.00 29.80 C ANISOU 1722 CB LEU B 78 3612 4053 3658 -172 -424 425 C ATOM 1723 CG LEU B 78 7.772 80.799 8.835 1.00 34.41 C ANISOU 1723 CG LEU B 78 4209 4563 4301 -220 -416 371 C ATOM 1724 CD1 LEU B 78 7.705 82.020 9.745 1.00 36.47 C ANISOU 1724 CD1 LEU B 78 4487 4716 4653 -226 -421 394 C ATOM 1725 CD2 LEU B 78 7.103 79.547 9.472 1.00 29.46 C ANISOU 1725 CD2 LEU B 78 3592 3952 3651 -231 -435 275 C ATOM 1726 N PHE B 79 8.470 81.998 4.827 1.00 28.10 N ANISOU 1726 N PHE B 79 3402 3979 3298 -140 -338 641 N ATOM 1727 CA PHE B 79 9.715 81.907 4.083 1.00 29.20 C ANISOU 1727 CA PHE B 79 3527 4174 3394 -164 -263 690 C ATOM 1728 C PHE B 79 9.685 82.913 2.948 1.00 32.52 C ANISOU 1728 C PHE B 79 3984 4627 3745 -139 -223 842 C ATOM 1729 O PHE B 79 10.535 82.897 2.051 1.00 35.31 O ANISOU 1729 O PHE B 79 4334 5058 4025 -149 -141 905 O ATOM 1730 CB PHE B 79 9.900 80.484 3.580 1.00 27.02 C ANISOU 1730 CB PHE B 79 3230 4014 3021 -142 -264 588 C ATOM 1731 CG PHE B 79 10.198 79.505 4.724 1.00 26.68 C ANISOU 1731 CG PHE B 79 3163 3917 3058 -175 -297 462 C ATOM 1732 CD1 PHE B 79 11.394 79.554 5.397 1.00 26.68 C ANISOU 1732 CD1 PHE B 79 3132 3855 3151 -222 -267 447 C ATOM 1733 CD2 PHE B 79 9.252 78.604 5.156 1.00 25.90 C ANISOU 1733 CD2 PHE B 79 3074 3818 2950 -160 -362 366 C ATOM 1734 CE1 PHE B 79 11.695 78.691 6.447 1.00 27.30 C ANISOU 1734 CE1 PHE B 79 3206 3877 3291 -240 -311 343 C ATOM 1735 CE2 PHE B 79 9.517 77.730 6.206 1.00 23.96 C ANISOU 1735 CE2 PHE B 79 2827 3511 2766 -191 -389 274 C ATOM 1736 CZ PHE B 79 10.762 77.766 6.860 1.00 25.64 C ANISOU 1736 CZ PHE B 79 3026 3665 3052 -224 -369 265 C ATOM 1737 N VAL B 80 8.697 83.785 2.952 1.00 31.55 N ANISOU 1737 N VAL B 80 3899 4448 3639 -101 -277 904 N ATOM 1738 CA VAL B 80 8.554 84.577 1.734 1.00 36.41 C ANISOU 1738 CA VAL B 80 4572 5107 4156 -59 -257 1055 C ATOM 1739 C VAL B 80 9.679 85.593 1.595 1.00 37.21 C ANISOU 1739 C VAL B 80 4681 5130 4327 -126 -159 1196 C ATOM 1740 O VAL B 80 10.166 85.782 0.510 1.00 38.89 O ANISOU 1740 O VAL B 80 4927 5421 4429 -123 -83 1308 O ATOM 1741 CB VAL B 80 7.157 85.218 1.580 1.00 34.60 C ANISOU 1741 CB VAL B 80 4384 4845 3918 21 -358 1088 C ATOM 1742 CG1 VAL B 80 6.944 86.278 2.668 1.00 36.65 C ANISOU 1742 CG1 VAL B 80 4637 4930 4358 -4 -384 1107 C ATOM 1743 CG2 VAL B 80 7.023 85.803 0.192 1.00 34.94 C ANISOU 1743 CG2 VAL B 80 4505 4956 3816 81 -353 1241 C ATOM 1744 N ASP B 81 10.134 86.175 2.704 1.00 38.10 N ANISOU 1744 N ASP B 81 4759 5095 4620 -190 -155 1180 N ATOM 1745 CA ASP B 81 11.169 87.229 2.665 1.00 41.15 C ANISOU 1745 CA ASP B 81 5138 5378 5118 -267 -73 1306 C ATOM 1746 C ASP B 81 12.551 86.686 2.894 1.00 43.23 C ANISOU 1746 C ASP B 81 5321 5669 5437 -346 13 1251 C ATOM 1747 O ASP B 81 13.505 87.268 2.417 1.00 45.37 O ANISOU 1747 O ASP B 81 5569 5920 5751 -410 115 1361 O ATOM 1748 CB ASP B 81 10.902 88.308 3.735 1.00 41.80 C ANISOU 1748 CB ASP B 81 5225 5268 5389 -288 -135 1308 C ATOM 1749 CG ASP B 81 10.656 87.711 5.117 1.00 41.40 C ANISOU 1749 CG ASP B 81 5133 5178 5418 -288 -206 1127 C ATOM 1750 OD1 ASP B 81 9.895 86.729 5.235 1.00 39.74 O ANISOU 1750 OD1 ASP B 81 4924 5061 5113 -237 -252 1024 O ATOM 1751 OD2 ASP B 81 11.248 88.198 6.095 1.00 40.99 O ANISOU 1751 OD2 ASP B 81 5051 5002 5522 -342 -216 1086 O ATOM 1752 N VAL B 82 12.683 85.606 3.675 1.00 40.10 N ANISOU 1752 N VAL B 82 4874 5305 5056 -344 -29 1084 N ATOM 1753 CA VAL B 82 13.988 85.016 3.872 1.00 38.02 C ANISOU 1753 CA VAL B 82 4527 5071 4849 -401 33 1018 C ATOM 1754 C VAL B 82 13.868 83.527 4.186 1.00 37.26 C ANISOU 1754 C VAL B 82 4410 5065 4683 -360 -17 856 C ATOM 1755 O VAL B 82 12.867 83.077 4.845 1.00 36.39 O ANISOU 1755 O VAL B 82 4338 4933 4554 -319 -112 774 O ATOM 1756 CB VAL B 82 14.803 85.765 4.956 1.00 39.40 C ANISOU 1756 CB VAL B 82 4646 5085 5238 -477 22 1000 C ATOM 1757 CG1 VAL B 82 14.185 85.634 6.345 1.00 36.68 C ANISOU 1757 CG1 VAL B 82 4326 4647 4966 -454 -99 878 C ATOM 1758 CG2 VAL B 82 16.216 85.237 4.944 1.00 42.69 C ANISOU 1758 CG2 VAL B 82 4959 5543 5719 -531 91 944 C ATOM 1759 N ILE B 83 14.840 82.744 3.717 1.00 36.27 N ANISOU 1759 N ILE B 83 4222 5035 4523 -371 49 809 N ATOM 1760 CA ILE B 83 14.965 81.383 4.249 1.00 34.55 C ANISOU 1760 CA ILE B 83 3977 4855 4294 -342 -11 647 C ATOM 1761 C ILE B 83 16.187 81.282 5.136 1.00 34.61 C ANISOU 1761 C ILE B 83 3903 4788 4460 -392 -15 574 C ATOM 1762 O ILE B 83 17.266 81.455 4.641 1.00 36.63 O ANISOU 1762 O ILE B 83 4078 5080 4759 -428 76 599 O ATOM 1763 CB ILE B 83 15.061 80.351 3.142 1.00 35.69 C ANISOU 1763 CB ILE B 83 4112 5162 4286 -291 32 602 C ATOM 1764 CG1 ILE B 83 13.993 80.664 2.105 1.00 39.65 C ANISOU 1764 CG1 ILE B 83 4692 5744 4628 -240 37 690 C ATOM 1765 CG2 ILE B 83 14.906 78.944 3.693 1.00 33.45 C ANISOU 1765 CG2 ILE B 83 3822 4890 3995 -254 -54 440 C ATOM 1766 CD1 ILE B 83 13.687 79.514 1.172 1.00 39.32 C ANISOU 1766 CD1 ILE B 83 4663 5855 4420 -169 29 606 C ATOM 1767 N ASN B 84 16.052 80.994 6.433 1.00 34.08 N ANISOU 1767 N ASN B 84 3852 4623 4476 -392 -119 481 N ATOM 1768 CA ASN B 84 17.275 80.744 7.259 1.00 32.55 C ANISOU 1768 CA ASN B 84 3580 4369 4419 -421 -149 392 C ATOM 1769 C ASN B 84 16.897 79.698 8.307 1.00 31.96 C ANISOU 1769 C ASN B 84 3559 4257 4328 -380 -267 272 C ATOM 1770 O ASN B 84 15.737 79.267 8.297 1.00 28.38 O ANISOU 1770 O ASN B 84 3185 3826 3771 -346 -298 270 O ATOM 1771 CB ASN B 84 17.789 82.049 7.861 1.00 32.37 C ANISOU 1771 CB ASN B 84 3523 4220 4557 -485 -149 443 C ATOM 1772 CG ASN B 84 16.806 82.672 8.812 1.00 33.04 C ANISOU 1772 CG ASN B 84 3698 4197 4660 -477 -233 450 C ATOM 1773 OD1 ASN B 84 15.933 81.981 9.384 1.00 29.21 O ANISOU 1773 OD1 ASN B 84 3289 3718 4094 -431 -303 388 O ATOM 1774 ND2 ASN B 84 16.931 84.013 9.021 1.00 32.39 N ANISOU 1774 ND2 ASN B 84 3606 4006 4695 -525 -222 522 N ATOM 1775 N SER B 85 17.824 79.260 9.182 1.00 29.15 N ANISOU 1775 N SER B 85 3162 3844 4071 -381 -335 176 N ATOM 1776 CA SER B 85 17.491 78.111 9.988 1.00 27.79 C ANISOU 1776 CA SER B 85 3057 3647 3855 -336 -435 82 C ATOM 1777 C SER B 85 16.559 78.506 11.125 1.00 25.75 C ANISOU 1777 C SER B 85 2903 3296 3584 -340 -503 91 C ATOM 1778 O SER B 85 15.853 77.643 11.667 1.00 29.66 O ANISOU 1778 O SER B 85 3482 3781 4007 -313 -556 50 O ATOM 1779 CB SER B 85 18.739 77.407 10.483 1.00 29.65 C ANISOU 1779 CB SER B 85 3228 3857 4181 -316 -500 -22 C ATOM 1780 OG SER B 85 19.523 78.379 11.156 1.00 34.60 O ANISOU 1780 OG SER B 85 3801 4400 4947 -355 -529 -25 O ATOM 1781 N GLY B 86 16.487 79.781 11.445 1.00 24.20 N ANISOU 1781 N GLY B 86 2705 3034 3455 -374 -493 144 N ATOM 1782 CA GLY B 86 15.590 80.242 12.519 1.00 23.03 C ANISOU 1782 CA GLY B 86 2651 2807 3292 -369 -547 139 C ATOM 1783 C GLY B 86 14.147 80.149 12.033 1.00 22.40 C ANISOU 1783 C GLY B 86 2628 2780 3102 -353 -504 189 C ATOM 1784 O GLY B 86 13.224 79.842 12.820 1.00 23.20 O ANISOU 1784 O GLY B 86 2807 2858 3149 -337 -537 159 O ATOM 1785 N ARG B 87 13.925 80.392 10.745 1.00 21.92 N ANISOU 1785 N ARG B 87 2527 2796 3004 -354 -430 263 N ATOM 1786 CA ARG B 87 12.547 80.300 10.170 1.00 22.10 C ANISOU 1786 CA ARG B 87 2590 2877 2929 -328 -408 301 C ATOM 1787 C ARG B 87 12.134 78.826 10.072 1.00 20.94 C ANISOU 1787 C ARG B 87 2466 2792 2697 -304 -431 231 C ATOM 1788 O ARG B 87 11.002 78.480 10.356 1.00 23.07 O ANISOU 1788 O ARG B 87 2779 3065 2922 -294 -447 213 O ATOM 1789 CB ARG B 87 12.465 80.975 8.777 1.00 23.10 C ANISOU 1789 CB ARG B 87 2683 3071 3021 -324 -339 403 C ATOM 1790 CG ARG B 87 12.735 82.488 8.736 1.00 23.56 C ANISOU 1790 CG ARG B 87 2730 3051 3172 -352 -311 497 C ATOM 1791 CD ARG B 87 11.652 83.316 9.421 1.00 24.19 C ANISOU 1791 CD ARG B 87 2861 3048 3282 -335 -353 508 C ATOM 1792 NE ARG B 87 11.939 84.792 9.369 1.00 25.94 N ANISOU 1792 NE ARG B 87 3074 3169 3612 -360 -338 594 N ATOM 1793 CZ ARG B 87 11.487 85.629 8.447 1.00 27.97 C ANISOU 1793 CZ ARG B 87 3345 3427 3855 -345 -307 711 C ATOM 1794 NH1 ARG B 87 10.714 85.175 7.401 1.00 27.28 N ANISOU 1794 NH1 ARG B 87 3278 3455 3633 -297 -291 754 N ATOM 1795 NH2 ARG B 87 11.820 86.933 8.549 1.00 26.39 N ANISOU 1795 NH2 ARG B 87 3143 3105 3779 -375 -302 785 N ATOM 1796 N ILE B 88 13.060 77.934 9.783 1.00 21.43 N ANISOU 1796 N ILE B 88 2494 2891 2759 -298 -436 182 N ATOM 1797 CA ILE B 88 12.751 76.494 9.784 1.00 21.10 C ANISOU 1797 CA ILE B 88 2479 2878 2661 -276 -473 106 C ATOM 1798 C ILE B 88 12.460 76.042 11.208 1.00 22.83 C ANISOU 1798 C ILE B 88 2773 3002 2898 -286 -535 63 C ATOM 1799 O ILE B 88 11.619 75.175 11.436 1.00 21.36 O ANISOU 1799 O ILE B 88 2636 2813 2668 -286 -553 34 O ATOM 1800 CB ILE B 88 13.915 75.724 9.194 1.00 22.75 C ANISOU 1800 CB ILE B 88 2629 3135 2881 -255 -470 52 C ATOM 1801 CG1 ILE B 88 14.234 76.247 7.767 1.00 23.08 C ANISOU 1801 CG1 ILE B 88 2603 3285 2880 -247 -383 106 C ATOM 1802 CG2 ILE B 88 13.697 74.228 9.345 1.00 23.05 C ANISOU 1802 CG2 ILE B 88 2702 3168 2888 -230 -527 -34 C ATOM 1803 CD1 ILE B 88 15.465 75.631 7.066 1.00 26.10 C ANISOU 1803 CD1 ILE B 88 2905 3737 3273 -224 -349 49 C ATOM 1804 N VAL B 89 13.129 76.613 12.212 1.00 23.11 N ANISOU 1804 N VAL B 89 2826 2959 2997 -297 -570 57 N ATOM 1805 CA VAL B 89 12.788 76.198 13.602 1.00 21.19 C ANISOU 1805 CA VAL B 89 2679 2636 2736 -299 -627 23 C ATOM 1806 C VAL B 89 11.379 76.639 13.917 1.00 20.45 C ANISOU 1806 C VAL B 89 2631 2541 2597 -313 -586 55 C ATOM 1807 O VAL B 89 10.635 75.894 14.483 1.00 23.29 O ANISOU 1807 O VAL B 89 3055 2885 2909 -322 -588 38 O ATOM 1808 CB VAL B 89 13.732 76.904 14.622 1.00 20.56 C ANISOU 1808 CB VAL B 89 2612 2477 2723 -297 -685 0 C ATOM 1809 CG1 VAL B 89 13.193 76.661 16.025 1.00 20.16 C ANISOU 1809 CG1 VAL B 89 2683 2361 2617 -292 -729 -22 C ATOM 1810 CG2 VAL B 89 15.113 76.385 14.433 1.00 19.96 C ANISOU 1810 CG2 VAL B 89 2477 2397 2709 -279 -736 -48 C ATOM 1811 N GLY B 90 11.005 77.864 13.501 1.00 22.82 N ANISOU 1811 N GLY B 90 2891 2856 2923 -315 -545 102 N ATOM 1812 CA GLY B 90 9.606 78.362 13.594 1.00 22.66 C ANISOU 1812 CA GLY B 90 2887 2847 2877 -315 -506 124 C ATOM 1813 C GLY B 90 8.579 77.408 12.984 1.00 22.01 C ANISOU 1813 C GLY B 90 2793 2829 2739 -317 -484 114 C ATOM 1814 O GLY B 90 7.518 77.120 13.576 1.00 24.80 O ANISOU 1814 O GLY B 90 3178 3175 3072 -330 -463 94 O ATOM 1815 N PHE B 91 8.904 76.953 11.783 1.00 21.77 N ANISOU 1815 N PHE B 91 2714 2866 2693 -305 -483 120 N ATOM 1816 CA PHE B 91 8.188 75.910 11.023 1.00 20.51 C ANISOU 1816 CA PHE B 91 2535 2769 2489 -301 -485 88 C ATOM 1817 C PHE B 91 7.955 74.633 11.844 1.00 21.44 C ANISOU 1817 C PHE B 91 2707 2837 2603 -329 -506 35 C ATOM 1818 O PHE B 91 6.837 74.124 11.921 1.00 22.37 O ANISOU 1818 O PHE B 91 2824 2960 2716 -351 -492 15 O ATOM 1819 CB PHE B 91 8.999 75.649 9.742 1.00 20.75 C ANISOU 1819 CB PHE B 91 2517 2876 2494 -273 -486 89 C ATOM 1820 CG PHE B 91 8.680 74.337 9.016 1.00 22.25 C ANISOU 1820 CG PHE B 91 2692 3118 2643 -260 -511 22 C ATOM 1821 CD1 PHE B 91 7.740 74.311 7.958 1.00 21.79 C ANISOU 1821 CD1 PHE B 91 2599 3144 2537 -236 -513 16 C ATOM 1822 CD2 PHE B 91 9.385 73.201 9.265 1.00 19.36 C ANISOU 1822 CD2 PHE B 91 2345 2719 2292 -262 -545 -39 C ATOM 1823 CE1 PHE B 91 7.491 73.104 7.262 1.00 21.88 C ANISOU 1823 CE1 PHE B 91 2593 3199 2519 -221 -550 -65 C ATOM 1824 CE2 PHE B 91 9.113 72.027 8.548 1.00 22.14 C ANISOU 1824 CE2 PHE B 91 2682 3107 2621 -246 -575 -112 C ATOM 1825 CZ PHE B 91 8.181 71.951 7.570 1.00 19.90 C ANISOU 1825 CZ PHE B 91 2363 2904 2295 -229 -578 -132 C ATOM 1826 N PHE B 92 8.968 74.171 12.561 1.00 21.87 N ANISOU 1826 N PHE B 92 2810 2831 2670 -332 -541 18 N ATOM 1827 CA PHE B 92 8.800 72.943 13.322 1.00 19.71 C ANISOU 1827 CA PHE B 92 2607 2495 2387 -355 -567 -13 C ATOM 1828 C PHE B 92 8.028 73.270 14.594 1.00 20.22 C ANISOU 1828 C PHE B 92 2743 2507 2432 -387 -533 10 C ATOM 1829 O PHE B 92 7.348 72.404 15.173 1.00 20.56 O ANISOU 1829 O PHE B 92 2842 2511 2459 -425 -515 7 O ATOM 1830 CB PHE B 92 10.192 72.357 13.654 1.00 20.24 C ANISOU 1830 CB PHE B 92 2707 2510 2472 -330 -635 -41 C ATOM 1831 CG PHE B 92 10.759 71.508 12.559 1.00 21.14 C ANISOU 1831 CG PHE B 92 2765 2667 2602 -301 -663 -91 C ATOM 1832 CD1 PHE B 92 10.259 70.260 12.339 1.00 22.57 C ANISOU 1832 CD1 PHE B 92 2967 2826 2783 -311 -685 -131 C ATOM 1833 CD2 PHE B 92 11.729 72.000 11.702 1.00 23.16 C ANISOU 1833 CD2 PHE B 92 2938 2986 2874 -266 -656 -101 C ATOM 1834 CE1 PHE B 92 10.698 69.481 11.286 1.00 24.21 C ANISOU 1834 CE1 PHE B 92 3121 3075 3001 -274 -714 -197 C ATOM 1835 CE2 PHE B 92 12.207 71.218 10.651 1.00 24.83 C ANISOU 1835 CE2 PHE B 92 3096 3255 3086 -231 -668 -160 C ATOM 1836 CZ PHE B 92 11.687 69.960 10.452 1.00 24.42 C ANISOU 1836 CZ PHE B 92 3071 3181 3027 -229 -703 -215 C ATOM 1837 N ASP B 93 8.124 74.510 15.056 1.00 20.92 N ANISOU 1837 N ASP B 93 2834 2592 2524 -374 -517 32 N ATOM 1838 CA ASP B 93 7.533 74.814 16.358 1.00 21.55 C ANISOU 1838 CA ASP B 93 2991 2628 2569 -391 -484 37 C ATOM 1839 C ASP B 93 6.052 74.919 16.173 1.00 22.59 C ANISOU 1839 C ASP B 93 3079 2803 2703 -417 -408 39 C ATOM 1840 O ASP B 93 5.259 74.560 17.072 1.00 23.22 O ANISOU 1840 O ASP B 93 3213 2862 2750 -452 -353 38 O ATOM 1841 CB ASP B 93 8.045 76.134 16.962 1.00 20.21 C ANISOU 1841 CB ASP B 93 2835 2433 2412 -362 -500 37 C ATOM 1842 CG ASP B 93 7.478 76.305 18.370 1.00 23.36 C ANISOU 1842 CG ASP B 93 3331 2797 2749 -369 -468 25 C ATOM 1843 OD1 ASP B 93 7.329 75.229 19.018 1.00 22.70 O ANISOU 1843 OD1 ASP B 93 3334 2685 2604 -395 -461 32 O ATOM 1844 OD2 ASP B 93 7.077 77.416 18.826 1.00 25.35 O ANISOU 1844 OD2 ASP B 93 3580 3048 3006 -351 -440 10 O ATOM 1845 N VAL B 94 5.660 75.388 14.972 1.00 23.69 N ANISOU 1845 N VAL B 94 3117 3006 2879 -398 -403 42 N ATOM 1846 CA VAL B 94 4.228 75.403 14.599 1.00 23.30 C ANISOU 1846 CA VAL B 94 3000 3004 2850 -412 -354 28 C ATOM 1847 C VAL B 94 3.680 73.972 14.502 1.00 25.27 C ANISOU 1847 C VAL B 94 3249 3248 3104 -464 -344 2 C ATOM 1848 O VAL B 94 2.585 73.675 15.010 1.00 26.20 O ANISOU 1848 O VAL B 94 3354 3363 3239 -508 -281 -12 O ATOM 1849 CB VAL B 94 3.968 76.173 13.271 1.00 22.79 C ANISOU 1849 CB VAL B 94 2841 3008 2811 -367 -377 40 C ATOM 1850 CG1 VAL B 94 2.606 75.789 12.712 1.00 22.98 C ANISOU 1850 CG1 VAL B 94 2785 3084 2861 -377 -361 5 C ATOM 1851 CG2 VAL B 94 4.045 77.693 13.480 1.00 20.73 C ANISOU 1851 CG2 VAL B 94 2574 2732 2572 -327 -371 70 C ATOM 1852 N GLY B 95 4.416 73.078 13.847 1.00 24.82 N ANISOU 1852 N GLY B 95 3199 3187 3046 -460 -401 -11 N ATOM 1853 CA GLY B 95 3.936 71.665 13.701 1.00 25.11 C ANISOU 1853 CA GLY B 95 3236 3197 3108 -509 -406 -44 C ATOM 1854 C GLY B 95 3.858 71.039 15.074 1.00 26.27 C ANISOU 1854 C GLY B 95 3490 3255 3237 -565 -366 -16 C ATOM 1855 O GLY B 95 2.945 70.259 15.354 1.00 30.11 O ANISOU 1855 O GLY B 95 3973 3711 3755 -631 -318 -22 O ATOM 1856 N ARG B 96 4.797 71.381 15.957 1.00 26.51 N ANISOU 1856 N ARG B 96 3616 3240 3215 -541 -384 16 N ATOM 1857 CA ARG B 96 4.805 70.893 17.354 1.00 26.17 C ANISOU 1857 CA ARG B 96 3705 3118 3119 -578 -353 53 C ATOM 1858 C ARG B 96 3.592 71.361 18.102 1.00 28.26 C ANISOU 1858 C ARG B 96 3967 3406 3364 -621 -238 66 C ATOM 1859 O ARG B 96 2.950 70.597 18.830 1.00 29.30 O ANISOU 1859 O ARG B 96 4160 3494 3479 -688 -168 95 O ATOM 1860 CB ARG B 96 6.070 71.371 18.119 1.00 25.43 C ANISOU 1860 CB ARG B 96 3707 2987 2968 -524 -418 67 C ATOM 1861 CG ARG B 96 6.021 70.963 19.593 1.00 27.17 C ANISOU 1861 CG ARG B 96 4083 3138 3101 -548 -392 109 C ATOM 1862 CD ARG B 96 7.347 71.199 20.270 1.00 28.23 C ANISOU 1862 CD ARG B 96 4312 3227 3186 -485 -494 107 C ATOM 1863 NE ARG B 96 7.614 72.645 20.529 1.00 27.26 N ANISOU 1863 NE ARG B 96 4160 3146 3052 -440 -498 79 N ATOM 1864 CZ ARG B 96 7.526 73.230 21.719 1.00 26.02 C ANISOU 1864 CZ ARG B 96 4100 2978 2808 -424 -479 79 C ATOM 1865 NH1 ARG B 96 7.115 72.505 22.751 1.00 27.30 N ANISOU 1865 NH1 ARG B 96 4402 3104 2867 -453 -436 121 N ATOM 1866 NH2 ARG B 96 7.793 74.515 21.880 1.00 23.31 N ANISOU 1866 NH2 ARG B 96 3721 2658 2477 -382 -497 38 N ATOM 1867 N TYR B 97 3.256 72.637 17.908 1.00 30.25 N ANISOU 1867 N TYR B 97 4144 3723 3626 -582 -213 46 N ATOM 1868 CA TYR B 97 2.014 73.213 18.518 1.00 29.52 C ANISOU 1868 CA TYR B 97 4017 3667 3531 -607 -99 36 C ATOM 1869 C TYR B 97 0.781 72.429 18.035 1.00 29.50 C ANISOU 1869 C TYR B 97 3919 3685 3605 -676 -37 17 C ATOM 1870 O TYR B 97 -0.134 72.067 18.842 1.00 29.70 O ANISOU 1870 O TYR B 97 3957 3703 3626 -744 78 26 O ATOM 1871 CB TYR B 97 1.859 74.755 18.201 1.00 27.21 C ANISOU 1871 CB TYR B 97 3645 3429 3264 -538 -106 6 C ATOM 1872 CG TYR B 97 0.663 75.337 18.904 1.00 29.59 C ANISOU 1872 CG TYR B 97 3910 3765 3568 -549 5 -22 C ATOM 1873 CD1 TYR B 97 0.790 75.844 20.211 1.00 31.58 C ANISOU 1873 CD1 TYR B 97 4265 4000 3736 -533 57 -26 C ATOM 1874 CD2 TYR B 97 -0.627 75.308 18.322 1.00 30.75 C ANISOU 1874 CD2 TYR B 97 3919 3966 3800 -571 60 -58 C ATOM 1875 CE1 TYR B 97 -0.292 76.334 20.910 1.00 32.95 C ANISOU 1875 CE1 TYR B 97 4405 4213 3901 -538 175 -65 C ATOM 1876 CE2 TYR B 97 -1.744 75.780 19.042 1.00 33.06 C ANISOU 1876 CE2 TYR B 97 4163 4294 4106 -580 177 -97 C ATOM 1877 CZ TYR B 97 -1.552 76.293 20.335 1.00 34.47 C ANISOU 1877 CZ TYR B 97 4447 4459 4190 -563 241 -100 C ATOM 1878 OH TYR B 97 -2.566 76.809 21.088 1.00 37.64 O ANISOU 1878 OH TYR B 97 4807 4905 4591 -561 365 -150 O ATOM 1879 N VAL B 98 0.680 72.233 16.716 1.00 26.57 N ANISOU 1879 N VAL B 98 3441 3349 3307 -661 -104 -16 N ATOM 1880 CA VAL B 98 -0.535 71.560 16.208 1.00 27.51 C ANISOU 1880 CA VAL B 98 3448 3489 3517 -722 -64 -56 C ATOM 1881 C VAL B 98 -0.607 70.148 16.888 1.00 30.61 C ANISOU 1881 C VAL B 98 3924 3790 3915 -819 -19 -24 C ATOM 1882 O VAL B 98 -1.654 69.729 17.373 1.00 33.32 O ANISOU 1882 O VAL B 98 4231 4122 4307 -902 86 -25 O ATOM 1883 CB VAL B 98 -0.563 71.479 14.677 1.00 26.35 C ANISOU 1883 CB VAL B 98 3192 3394 3426 -680 -164 -106 C ATOM 1884 CG1 VAL B 98 -1.616 70.489 14.124 1.00 26.79 C ANISOU 1884 CG1 VAL B 98 3143 3450 3585 -746 -160 -165 C ATOM 1885 CG2 VAL B 98 -0.702 72.865 14.065 1.00 26.27 C ANISOU 1885 CG2 VAL B 98 3108 3463 3412 -593 -194 -117 C ATOM 1886 N CYS B 99 0.510 69.449 16.983 1.00 30.34 N ANISOU 1886 N CYS B 99 4005 3685 3836 -809 -93 9 N ATOM 1887 CA CYS B 99 0.476 68.128 17.549 1.00 33.89 C ANISOU 1887 CA CYS B 99 4546 4031 4300 -891 -69 48 C ATOM 1888 C CYS B 99 0.083 68.222 18.995 1.00 36.51 C ANISOU 1888 C CYS B 99 4983 4333 4555 -944 57 117 C ATOM 1889 O CYS B 99 -0.672 67.428 19.457 1.00 40.06 O ANISOU 1889 O CYS B 99 5447 4731 5041 -1042 149 149 O ATOM 1890 CB CYS B 99 1.823 67.442 17.488 1.00 33.33 C ANISOU 1890 CB CYS B 99 4589 3882 4193 -850 -185 68 C ATOM 1891 SG CYS B 99 2.282 66.862 15.840 1.00 33.17 S ANISOU 1891 SG CYS B 99 4466 3880 4257 -804 -317 -19 S ATOM 1892 N GLU B 100 0.613 69.163 19.729 1.00 36.03 N ANISOU 1892 N GLU B 100 5002 4303 4386 -882 65 138 N ATOM 1893 CA GLU B 100 0.503 69.105 21.174 1.00 37.58 C ANISOU 1893 CA GLU B 100 5345 4465 4469 -915 164 205 C ATOM 1894 C GLU B 100 -0.730 69.825 21.696 1.00 39.96 C ANISOU 1894 C GLU B 100 5572 4846 4767 -949 324 184 C ATOM 1895 O GLU B 100 -1.147 69.596 22.840 1.00 40.17 O ANISOU 1895 O GLU B 100 5700 4857 4706 -1002 450 238 O ATOM 1896 CB GLU B 100 1.743 69.740 21.812 1.00 34.94 C ANISOU 1896 CB GLU B 100 5144 4120 4011 -822 77 220 C ATOM 1897 CG GLU B 100 2.949 68.836 21.649 1.00 36.16 C ANISOU 1897 CG GLU B 100 5398 4182 4159 -796 -62 249 C ATOM 1898 CD GLU B 100 4.186 69.420 22.316 1.00 39.80 C ANISOU 1898 CD GLU B 100 5977 4629 4517 -705 -161 252 C ATOM 1899 OE1 GLU B 100 4.238 70.665 22.536 1.00 39.30 O ANISOU 1899 OE1 GLU B 100 5881 4633 4418 -653 -149 212 O ATOM 1900 OE2 GLU B 100 5.142 68.643 22.581 1.00 40.02 O ANISOU 1900 OE2 GLU B 100 6120 4571 4514 -680 -265 284 O ATOM 1901 N GLU B 101 -1.303 70.715 20.897 1.00 37.42 N ANISOU 1901 N GLU B 101 5078 4609 4529 -910 321 107 N ATOM 1902 CA GLU B 101 -2.353 71.554 21.468 1.00 41.14 C ANISOU 1902 CA GLU B 101 5478 5157 4996 -914 459 71 C ATOM 1903 C GLU B 101 -3.564 71.525 20.617 1.00 41.79 C ANISOU 1903 C GLU B 101 5354 5292 5234 -954 501 7 C ATOM 1904 O GLU B 101 -4.598 71.935 21.077 1.00 47.09 O ANISOU 1904 O GLU B 101 5941 6019 5932 -978 633 -29 O ATOM 1905 CB GLU B 101 -1.926 73.007 21.643 1.00 41.42 C ANISOU 1905 CB GLU B 101 5519 5245 4975 -802 416 28 C ATOM 1906 CG GLU B 101 -0.536 73.179 22.250 1.00 45.39 C ANISOU 1906 CG GLU B 101 6199 5697 5352 -743 321 67 C ATOM 1907 CD GLU B 101 -0.462 72.871 23.729 1.00 54.58 C ANISOU 1907 CD GLU B 101 7541 6835 6362 -769 411 116 C ATOM 1908 OE1 GLU B 101 -1.509 72.705 24.427 1.00 55.65 O ANISOU 1908 OE1 GLU B 101 7671 7005 6468 -831 579 123 O ATOM 1909 OE2 GLU B 101 0.689 72.804 24.201 1.00 65.16 O ANISOU 1909 OE2 GLU B 101 9029 8124 7605 -723 310 146 O ATOM 1910 N VAL B 102 -3.453 71.047 19.379 1.00 39.36 N ANISOU 1910 N VAL B 102 4957 4971 5026 -952 387 -21 N ATOM 1911 CA VAL B 102 -4.628 71.011 18.521 1.00 38.17 C ANISOU 1911 CA VAL B 102 4603 4873 5026 -980 401 -98 C ATOM 1912 C VAL B 102 -5.167 69.604 18.355 1.00 40.96 C ANISOU 1912 C VAL B 102 4920 5163 5482 -1103 435 -92 C ATOM 1913 O VAL B 102 -6.337 69.357 18.487 1.00 43.20 O ANISOU 1913 O VAL B 102 5077 5465 5872 -1183 543 -128 O ATOM 1914 CB VAL B 102 -4.338 71.629 17.148 1.00 37.78 C ANISOU 1914 CB VAL B 102 4459 4874 5020 -880 245 -152 C ATOM 1915 CG1 VAL B 102 -5.624 71.645 16.326 1.00 35.16 C ANISOU 1915 CG1 VAL B 102 3921 4602 4836 -894 244 -240 C ATOM 1916 CG2 VAL B 102 -3.817 73.062 17.326 1.00 34.42 C ANISOU 1916 CG2 VAL B 102 4071 4491 4517 -769 215 -148 C ATOM 1917 N LEU B 103 -4.285 68.657 18.115 1.00 40.96 N ANISOU 1917 N LEU B 103 5029 5076 5460 -1121 345 -50 N ATOM 1918 CA LEU B 103 -4.685 67.360 17.709 1.00 40.04 C ANISOU 1918 CA LEU B 103 4869 4882 5463 -1220 334 -62 C ATOM 1919 C LEU B 103 -4.813 66.466 18.929 1.00 45.56 C ANISOU 1919 C LEU B 103 5699 5480 6133 -1339 469 37 C ATOM 1920 O LEU B 103 -4.355 66.750 20.043 1.00 43.60 O ANISOU 1920 O LEU B 103 5610 5220 5738 -1328 542 121 O ATOM 1921 CB LEU B 103 -3.642 66.766 16.764 1.00 35.78 C ANISOU 1921 CB LEU B 103 4380 4294 4922 -1166 159 -80 C ATOM 1922 CG LEU B 103 -3.315 67.468 15.448 1.00 35.65 C ANISOU 1922 CG LEU B 103 4267 4370 4907 -1049 19 -160 C ATOM 1923 CD1 LEU B 103 -2.355 66.612 14.646 1.00 35.01 C ANISOU 1923 CD1 LEU B 103 4240 4235 4827 -1018 -119 -182 C ATOM 1924 CD2 LEU B 103 -4.576 67.670 14.635 1.00 37.02 C ANISOU 1924 CD2 LEU B 103 4237 4619 5211 -1061 15 -258 C ATOM 1925 N CYS B 104 -5.385 65.315 18.669 1.00 49.73 N ANISOU 1925 N CYS B 104 6172 5924 6800 -1453 487 29 N ATOM 1926 CA CYS B 104 -5.591 64.323 19.699 1.00 54.43 C ANISOU 1926 CA CYS B 104 6887 6400 7392 -1586 616 137 C ATOM 1927 C CYS B 104 -4.293 63.918 20.324 1.00 50.34 C ANISOU 1927 C CYS B 104 6617 5787 6722 -1543 549 243 C ATOM 1928 O CYS B 104 -3.369 63.570 19.620 1.00 50.73 O ANISOU 1928 O CYS B 104 6709 5791 6777 -1473 379 215 O ATOM 1929 CB CYS B 104 -6.274 63.131 19.089 1.00 60.62 C ANISOU 1929 CB CYS B 104 7562 7087 8384 -1707 603 97 C ATOM 1930 SG CYS B 104 -7.764 62.917 20.043 1.00 83.21 S ANISOU 1930 SG CYS B 104 10329 9947 11341 -1884 872 141 S ATOM 1931 N PRO B 105 -4.204 63.986 21.655 1.00 53.02 N ANISOU 1931 N PRO B 105 7123 6106 6917 -1575 679 357 N ATOM 1932 CA PRO B 105 -2.952 63.745 22.353 1.00 51.77 C ANISOU 1932 CA PRO B 105 7209 5869 6593 -1512 600 454 C ATOM 1933 C PRO B 105 -2.593 62.239 22.422 1.00 54.80 C ANISOU 1933 C PRO B 105 7719 6065 7036 -1590 545 536 C ATOM 1934 O PRO B 105 -3.484 61.376 22.354 1.00 56.87 O ANISOU 1934 O PRO B 105 7918 6247 7443 -1729 636 558 O ATOM 1935 CB PRO B 105 -3.295 64.258 23.741 1.00 57.41 C ANISOU 1935 CB PRO B 105 8039 6632 7141 -1537 779 539 C ATOM 1936 CG PRO B 105 -4.729 63.777 23.938 1.00 58.80 C ANISOU 1936 CG PRO B 105 8095 6803 7442 -1698 984 555 C ATOM 1937 CD PRO B 105 -5.345 64.084 22.596 1.00 57.95 C ANISOU 1937 CD PRO B 105 7718 6765 7535 -1686 915 405 C ATOM 1938 N GLY B 106 -1.318 61.899 22.540 1.00 52.81 N ANISOU 1938 N GLY B 106 7635 5731 6698 -1503 392 577 N ATOM 1939 CA GLY B 106 -0.920 60.473 22.557 1.00 54.10 C ANISOU 1939 CA GLY B 106 7923 5701 6933 -1557 314 646 C ATOM 1940 C GLY B 106 -1.549 59.586 21.478 1.00 54.64 C ANISOU 1940 C GLY B 106 7829 5694 7239 -1643 277 565 C ATOM 1941 O GLY B 106 -1.966 58.456 21.774 1.00 62.11 O ANISOU 1941 O GLY B 106 8837 6480 8283 -1767 328 642 O ATOM 1942 N SER B 107 -1.612 60.075 20.235 1.00 49.87 N ANISOU 1942 N SER B 107 7027 5196 6726 -1577 184 411 N ATOM 1943 CA SER B 107 -2.337 59.401 19.153 1.00 51.43 C ANISOU 1943 CA SER B 107 7045 5355 7139 -1646 144 303 C ATOM 1944 C SER B 107 -1.792 59.765 17.800 1.00 48.37 C ANISOU 1944 C SER B 107 6536 5058 6783 -1518 -28 152 C ATOM 1945 O SER B 107 -1.440 60.905 17.547 1.00 48.66 O ANISOU 1945 O SER B 107 6529 5246 6715 -1410 -52 113 O ATOM 1946 CB SER B 107 -3.815 59.779 19.173 1.00 52.54 C ANISOU 1946 CB SER B 107 7004 5579 7380 -1758 311 271 C ATOM 1947 OG SER B 107 -4.345 59.579 20.468 1.00 58.59 O ANISOU 1947 OG SER B 107 7878 6292 8093 -1876 507 414 O ATOM 1948 N TRP B 108 -1.721 58.801 16.914 1.00 43.89 N ANISOU 1948 N TRP B 108 5917 4399 6360 -1530 -147 66 N ATOM 1949 CA TRP B 108 -1.293 59.092 15.594 1.00 43.35 C ANISOU 1949 CA TRP B 108 5734 4429 6309 -1412 -294 -82 C ATOM 1950 C TRP B 108 -2.507 58.871 14.804 1.00 48.58 C ANISOU 1950 C TRP B 108 6201 5119 7140 -1490 -282 -193 C ATOM 1951 O TRP B 108 -2.831 57.698 14.407 1.00 49.85 O ANISOU 1951 O TRP B 108 6329 5141 7469 -1566 -340 -251 O ATOM 1952 CB TRP B 108 -0.156 58.158 15.192 1.00 45.13 C ANISOU 1952 CB TRP B 108 6059 4536 6553 -1341 -455 -117 C ATOM 1953 CG TRP B 108 0.511 58.589 13.920 1.00 45.75 C ANISOU 1953 CG TRP B 108 6044 4741 6596 -1199 -588 -256 C ATOM 1954 CD1 TRP B 108 0.422 57.985 12.650 1.00 47.93 C ANISOU 1954 CD1 TRP B 108 6212 5019 6979 -1166 -709 -414 C ATOM 1955 CD2 TRP B 108 1.318 59.806 13.715 1.00 42.14 C ANISOU 1955 CD2 TRP B 108 5585 4447 5980 -1070 -606 -257 C ATOM 1956 NE1 TRP B 108 1.141 58.696 11.713 1.00 48.13 N ANISOU 1956 NE1 TRP B 108 6184 5200 6903 -1026 -787 -499 N ATOM 1957 CE2 TRP B 108 1.706 59.810 12.289 1.00 42.25 C ANISOU 1957 CE2 TRP B 108 5494 4551 6006 -969 -726 -404 C ATOM 1958 CE3 TRP B 108 1.773 60.825 14.540 1.00 40.59 C ANISOU 1958 CE3 TRP B 108 5464 4318 5640 -1030 -540 -159 C ATOM 1959 CZ2 TRP B 108 2.531 60.797 11.751 1.00 39.46 C ANISOU 1959 CZ2 TRP B 108 5118 4347 5529 -846 -759 -427 C ATOM 1960 CZ3 TRP B 108 2.595 61.806 13.982 1.00 37.45 C ANISOU 1960 CZ3 TRP B 108 5031 4056 5143 -908 -591 -196 C ATOM 1961 CH2 TRP B 108 2.941 61.807 12.616 1.00 36.70 C ANISOU 1961 CH2 TRP B 108 4834 4045 5065 -825 -687 -318 C ATOM 1962 N THR B 109 -3.261 59.949 14.615 1.00 45.60 N ANISOU 1962 N THR B 109 5685 4904 6739 -1477 -212 -228 N ATOM 1963 CA THR B 109 -4.505 59.856 13.861 1.00 48.46 C ANISOU 1963 CA THR B 109 5836 5309 7267 -1540 -210 -347 C ATOM 1964 C THR B 109 -4.267 60.187 12.411 1.00 49.43 C ANISOU 1964 C THR B 109 5850 5549 7380 -1412 -375 -499 C ATOM 1965 O THR B 109 -3.150 60.440 11.993 1.00 49.85 O ANISOU 1965 O THR B 109 5987 5647 7308 -1287 -471 -506 O ATOM 1966 CB THR B 109 -5.560 60.855 14.359 1.00 48.02 C ANISOU 1966 CB THR B 109 5666 5372 7209 -1583 -56 -324 C ATOM 1967 OG1 THR B 109 -5.184 62.162 13.896 1.00 50.54 O ANISOU 1967 OG1 THR B 109 5954 5861 7390 -1436 -105 -355 O ATOM 1968 CG2 THR B 109 -5.703 60.840 15.910 1.00 48.69 C ANISOU 1968 CG2 THR B 109 5880 5390 7231 -1684 138 -161 C ATOM 1969 N GLU B 110 -5.351 60.241 11.664 1.00 51.54 N ANISOU 1969 N GLU B 110 5927 5878 7777 -1440 -403 -619 N ATOM 1970 CA GLU B 110 -5.338 60.698 10.307 1.00 54.70 C ANISOU 1970 CA GLU B 110 6220 6415 8149 -1316 -549 -758 C ATOM 1971 C GLU B 110 -4.843 62.156 10.102 1.00 48.84 C ANISOU 1971 C GLU B 110 5496 5845 7215 -1176 -548 -717 C ATOM 1972 O GLU B 110 -4.179 62.467 9.119 1.00 46.29 O ANISOU 1972 O GLU B 110 5183 5612 6793 -1049 -666 -776 O ATOM 1973 CB GLU B 110 -6.764 60.588 9.779 1.00 63.57 C ANISOU 1973 CB GLU B 110 7128 7571 9454 -1382 -565 -882 C ATOM 1974 CG GLU B 110 -6.935 61.066 8.356 1.00 73.96 C ANISOU 1974 CG GLU B 110 8329 9035 10738 -1250 -728 -1031 C ATOM 1975 CD GLU B 110 -6.853 59.937 7.333 1.00 89.12 C ANISOU 1975 CD GLU B 110 10215 10891 12754 -1239 -896 -1188 C ATOM 1976 OE1 GLU B 110 -7.933 59.502 6.850 1.00 93.15 O ANISOU 1976 OE1 GLU B 110 10558 11387 13446 -1300 -957 -1322 O ATOM 1977 OE2 GLU B 110 -5.722 59.486 7.000 1.00 91.76 O ANISOU 1977 OE2 GLU B 110 10680 11191 12992 -1166 -973 -1194 O ATOM 1978 N ASP B 111 -5.267 63.055 10.967 1.00 43.80 N ANISOU 1978 N ASP B 111 4850 5255 6538 -1201 -413 -628 N ATOM 1979 CA ASP B 111 -4.869 64.446 10.845 1.00 43.51 C ANISOU 1979 CA ASP B 111 4829 5355 6349 -1080 -411 -589 C ATOM 1980 C ASP B 111 -3.338 64.580 11.017 1.00 38.67 C ANISOU 1980 C ASP B 111 4391 4725 5578 -1001 -444 -511 C ATOM 1981 O ASP B 111 -2.720 65.424 10.359 1.00 38.59 O ANISOU 1981 O ASP B 111 4388 4818 5456 -884 -506 -516 O ATOM 1982 CB ASP B 111 -5.616 65.301 11.874 1.00 44.65 C ANISOU 1982 CB ASP B 111 4936 5533 6495 -1127 -255 -520 C ATOM 1983 CG ASP B 111 -7.075 65.629 11.455 1.00 49.81 C ANISOU 1983 CG ASP B 111 5375 6260 7289 -1151 -245 -619 C ATOM 1984 OD1 ASP B 111 -7.443 65.559 10.242 1.00 45.78 O ANISOU 1984 OD1 ASP B 111 4749 5811 6836 -1094 -384 -738 O ATOM 1985 OD2 ASP B 111 -7.849 65.975 12.382 1.00 51.30 O ANISOU 1985 OD2 ASP B 111 5512 6451 7527 -1222 -95 -583 O ATOM 1986 N HIS B 112 -2.757 63.749 11.877 1.00 37.12 N ANISOU 1986 N HIS B 112 4327 4395 5381 -1065 -404 -439 N ATOM 1987 CA HIS B 112 -1.322 63.738 12.073 1.00 39.80 C ANISOU 1987 CA HIS B 112 4817 4705 5601 -992 -450 -382 C ATOM 1988 C HIS B 112 -0.631 63.466 10.771 1.00 40.85 C ANISOU 1988 C HIS B 112 4923 4885 5713 -894 -591 -482 C ATOM 1989 O HIS B 112 0.291 64.207 10.368 1.00 38.89 O ANISOU 1989 O HIS B 112 4706 4724 5348 -789 -628 -470 O ATOM 1990 CB HIS B 112 -0.931 62.689 13.106 1.00 37.53 C ANISOU 1990 CB HIS B 112 4672 4249 5339 -1073 -415 -303 C ATOM 1991 CG HIS B 112 -1.260 63.080 14.527 1.00 40.17 C ANISOU 1991 CG HIS B 112 5087 4552 5623 -1144 -267 -180 C ATOM 1992 ND1 HIS B 112 -2.509 63.017 15.023 1.00 42.00 N ANISOU 1992 ND1 HIS B 112 5245 4774 5940 -1255 -142 -164 N ATOM 1993 CD2 HIS B 112 -0.450 63.548 15.559 1.00 39.07 C ANISOU 1993 CD2 HIS B 112 5099 4398 5350 -1110 -226 -75 C ATOM 1994 CE1 HIS B 112 -2.502 63.423 16.306 1.00 41.55 C ANISOU 1994 CE1 HIS B 112 5295 4704 5788 -1289 -15 -52 C ATOM 1995 NE2 HIS B 112 -1.241 63.748 16.633 1.00 41.38 N ANISOU 1995 NE2 HIS B 112 5417 4677 5629 -1196 -77 0 N ATOM 1996 N GLU B 113 -1.062 62.409 10.089 1.00 40.40 N ANISOU 1996 N GLU B 113 4805 4773 5772 -929 -667 -587 N ATOM 1997 CA GLU B 113 -0.515 62.070 8.782 1.00 42.84 C ANISOU 1997 CA GLU B 113 5083 5138 6058 -831 -802 -707 C ATOM 1998 C GLU B 113 -0.554 63.297 7.881 1.00 43.22 C ANISOU 1998 C GLU B 113 5057 5372 5992 -725 -826 -731 C ATOM 1999 O GLU B 113 0.469 63.719 7.344 1.00 43.79 O ANISOU 1999 O GLU B 113 5173 5521 5942 -622 -862 -728 O ATOM 2000 CB GLU B 113 -1.304 60.923 8.149 1.00 51.02 C ANISOU 2000 CB GLU B 113 6033 6103 7251 -888 -882 -841 C ATOM 2001 CG GLU B 113 -0.810 59.540 8.540 1.00 59.60 C ANISOU 2001 CG GLU B 113 7212 7000 8434 -942 -920 -851 C ATOM 2002 CD GLU B 113 -1.937 58.535 8.674 1.00 72.17 C ANISOU 2002 CD GLU B 113 8731 8457 10232 -1079 -921 -906 C ATOM 2003 OE1 GLU B 113 -3.059 58.834 8.214 1.00 82.32 O ANISOU 2003 OE1 GLU B 113 9869 9818 11593 -1113 -921 -979 O ATOM 2004 OE2 GLU B 113 -1.702 57.447 9.240 1.00 68.83 O ANISOU 2004 OE2 GLU B 113 8396 7846 9909 -1153 -926 -876 O ATOM 2005 N LEU B 114 -1.744 63.869 7.727 1.00 41.57 N ANISOU 2005 N LEU B 114 4734 5231 5830 -750 -802 -752 N ATOM 2006 CA LEU B 114 -1.909 65.100 6.960 1.00 41.13 C ANISOU 2006 CA LEU B 114 4619 5336 5674 -650 -827 -756 C ATOM 2007 C LEU B 114 -0.913 66.279 7.321 1.00 38.86 C ANISOU 2007 C LEU B 114 4421 5104 5239 -581 -768 -633 C ATOM 2008 O LEU B 114 -0.345 66.915 6.422 1.00 36.50 O ANISOU 2008 O LEU B 114 4129 4913 4828 -479 -816 -636 O ATOM 2009 CB LEU B 114 -3.325 65.562 7.211 1.00 43.86 C ANISOU 2009 CB LEU B 114 4840 5706 6118 -703 -785 -769 C ATOM 2010 CG LEU B 114 -4.030 66.443 6.223 1.00 48.59 C ANISOU 2010 CG LEU B 114 5331 6444 6686 -614 -859 -827 C ATOM 2011 CD1 LEU B 114 -4.236 65.619 4.950 1.00 50.35 C ANISOU 2011 CD1 LEU B 114 5495 6704 6933 -570 -1009 -978 C ATOM 2012 CD2 LEU B 114 -5.370 66.784 6.879 1.00 52.54 C ANISOU 2012 CD2 LEU B 114 5708 6933 7320 -688 -786 -831 C ATOM 2013 N LEU B 115 -0.721 66.537 8.625 1.00 36.15 N ANISOU 2013 N LEU B 115 4149 4686 4901 -641 -664 -528 N ATOM 2014 CA LEU B 115 0.344 67.450 9.117 1.00 33.05 C ANISOU 2014 CA LEU B 115 3849 4311 4397 -590 -621 -428 C ATOM 2015 C LEU B 115 1.697 66.962 8.572 1.00 32.33 C ANISOU 2015 C LEU B 115 3825 4218 4242 -528 -686 -448 C ATOM 2016 O LEU B 115 2.433 67.736 7.951 1.00 32.42 O ANISOU 2016 O LEU B 115 3840 4317 4160 -447 -702 -428 O ATOM 2017 CB LEU B 115 0.355 67.454 10.639 1.00 30.19 C ANISOU 2017 CB LEU B 115 3568 3852 4051 -666 -521 -340 C ATOM 2018 CG LEU B 115 1.301 68.468 11.312 1.00 30.28 C ANISOU 2018 CG LEU B 115 3665 3873 3966 -621 -483 -251 C ATOM 2019 CD1 LEU B 115 1.089 69.861 10.743 1.00 26.50 C ANISOU 2019 CD1 LEU B 115 3121 3503 3443 -550 -482 -237 C ATOM 2020 CD2 LEU B 115 1.064 68.391 12.806 1.00 27.76 C ANISOU 2020 CD2 LEU B 115 3426 3469 3653 -694 -390 -184 C ATOM 2021 N ASN B 116 1.994 65.668 8.773 1.00 32.04 N ANISOU 2021 N ASN B 116 3833 4076 4266 -568 -721 -491 N ATOM 2022 CA ASN B 116 3.237 65.067 8.284 1.00 31.08 C ANISOU 2022 CA ASN B 116 3760 3943 4106 -504 -788 -535 C ATOM 2023 C ASN B 116 3.435 65.331 6.810 1.00 31.50 C ANISOU 2023 C ASN B 116 3747 4135 4086 -409 -848 -616 C ATOM 2024 O ASN B 116 4.476 65.783 6.411 1.00 30.44 O ANISOU 2024 O ASN B 116 3634 4068 3865 -337 -846 -600 O ATOM 2025 CB ASN B 116 3.224 63.574 8.586 1.00 32.59 C ANISOU 2025 CB ASN B 116 3992 3989 4402 -559 -834 -589 C ATOM 2026 CG ASN B 116 4.633 62.922 8.554 1.00 37.39 C ANISOU 2026 CG ASN B 116 4674 4541 4990 -496 -893 -615 C ATOM 2027 OD1 ASN B 116 5.612 63.558 8.235 1.00 40.44 O ANISOU 2027 OD1 ASN B 116 5064 5011 5289 -416 -893 -603 O ATOM 2028 ND2 ASN B 116 4.722 61.642 8.900 1.00 41.33 N ANISOU 2028 ND2 ASN B 116 5228 4889 5585 -534 -944 -651 N ATOM 2029 N ASP B 117 2.412 65.013 5.991 1.00 33.94 N ANISOU 2029 N ASP B 117 3973 4489 4432 -411 -902 -710 N ATOM 2030 CA ASP B 117 2.543 65.186 4.546 1.00 35.99 C ANISOU 2030 CA ASP B 117 4186 4890 4598 -311 -971 -795 C ATOM 2031 C ASP B 117 2.663 66.647 4.155 1.00 33.54 C ANISOU 2031 C ASP B 117 3868 4710 4165 -249 -928 -705 C ATOM 2032 O ASP B 117 3.441 66.992 3.240 1.00 34.88 O ANISOU 2032 O ASP B 117 4051 4989 4214 -162 -938 -712 O ATOM 2033 CB ASP B 117 1.362 64.581 3.773 1.00 37.31 C ANISOU 2033 CB ASP B 117 4266 5079 4830 -319 -1060 -925 C ATOM 2034 CG ASP B 117 1.363 63.060 3.797 1.00 42.83 C ANISOU 2034 CG ASP B 117 4970 5654 5650 -362 -1127 -1042 C ATOM 2035 OD1 ASP B 117 2.331 62.432 4.317 1.00 43.17 O ANISOU 2035 OD1 ASP B 117 5090 5598 5712 -370 -1114 -1025 O ATOM 2036 OD2 ASP B 117 0.337 62.499 3.321 1.00 49.81 O ANISOU 2036 OD2 ASP B 117 5773 6527 6625 -390 -1203 -1155 O ATOM 2037 N CYS B 118 1.832 67.503 4.756 1.00 31.25 N ANISOU 2037 N CYS B 118 3551 4414 3909 -290 -880 -628 N ATOM 2038 CA CYS B 118 2.016 68.937 4.510 1.00 31.64 C ANISOU 2038 CA CYS B 118 3606 4555 3861 -232 -841 -529 C ATOM 2039 C CYS B 118 3.476 69.428 4.871 1.00 31.74 C ANISOU 2039 C CYS B 118 3694 4558 3809 -213 -778 -440 C ATOM 2040 O CYS B 118 4.164 70.093 4.059 1.00 32.31 O ANISOU 2040 O CYS B 118 3776 4725 3775 -145 -769 -403 O ATOM 2041 CB CYS B 118 0.944 69.715 5.290 1.00 32.49 C ANISOU 2041 CB CYS B 118 3673 4634 4039 -278 -797 -473 C ATOM 2042 SG CYS B 118 1.230 71.511 5.270 1.00 37.32 S ANISOU 2042 SG CYS B 118 4307 5306 4566 -218 -749 -341 S ATOM 2043 N MET B 119 3.977 69.086 6.068 1.00 27.91 N ANISOU 2043 N MET B 119 3260 3957 3387 -274 -736 -405 N ATOM 2044 CA MET B 119 5.267 69.635 6.429 1.00 25.18 C ANISOU 2044 CA MET B 119 2965 3603 3000 -253 -693 -334 C ATOM 2045 C MET B 119 6.336 69.076 5.542 1.00 25.39 C ANISOU 2045 C MET B 119 2990 3683 2972 -194 -721 -394 C ATOM 2046 O MET B 119 7.222 69.808 5.097 1.00 25.77 O ANISOU 2046 O MET B 119 3036 3801 2954 -151 -684 -347 O ATOM 2047 CB MET B 119 5.539 69.384 7.917 1.00 26.55 C ANISOU 2047 CB MET B 119 3202 3646 3240 -318 -663 -292 C ATOM 2048 CG MET B 119 4.652 70.269 8.825 1.00 24.94 C ANISOU 2048 CG MET B 119 3001 3414 3062 -362 -607 -223 C ATOM 2049 SD MET B 119 4.940 69.829 10.524 1.00 27.93 S ANISOU 2049 SD MET B 119 3476 3654 3480 -428 -573 -182 S ATOM 2050 CE MET B 119 6.624 70.433 10.820 1.00 23.41 C ANISOU 2050 CE MET B 119 2954 3071 2868 -380 -585 -139 C ATOM 2051 N THR B 120 6.273 67.783 5.259 1.00 26.64 N ANISOU 2051 N THR B 120 3145 3810 3167 -192 -781 -503 N ATOM 2052 CA THR B 120 7.358 67.117 4.568 1.00 27.48 C ANISOU 2052 CA THR B 120 3250 3953 3237 -130 -807 -582 C ATOM 2053 C THR B 120 7.411 67.634 3.169 1.00 29.36 C ANISOU 2053 C THR B 120 3450 4356 3348 -53 -801 -604 C ATOM 2054 O THR B 120 8.442 67.873 2.583 1.00 29.40 O ANISOU 2054 O THR B 120 3448 4442 3280 1 -762 -603 O ATOM 2055 CB THR B 120 7.092 65.591 4.482 1.00 28.81 C ANISOU 2055 CB THR B 120 3422 4041 3483 -138 -889 -712 C ATOM 2056 OG1 THR B 120 7.169 65.035 5.793 1.00 32.01 O ANISOU 2056 OG1 THR B 120 3885 4283 3994 -207 -892 -675 O ATOM 2057 CG2 THR B 120 8.138 64.886 3.609 1.00 26.54 C ANISOU 2057 CG2 THR B 120 3121 3807 3155 -53 -923 -825 C ATOM 2058 N HIS B 121 6.244 67.776 2.591 1.00 33.84 N ANISOU 2058 N HIS B 121 3991 4979 3888 -46 -840 -628 N ATOM 2059 CA HIS B 121 6.170 68.198 1.251 1.00 35.03 C ANISOU 2059 CA HIS B 121 4124 5285 3899 35 -853 -648 C ATOM 2060 C HIS B 121 6.588 69.636 1.057 1.00 33.34 C ANISOU 2060 C HIS B 121 3927 5147 3595 56 -771 -503 C ATOM 2061 O HIS B 121 7.228 69.963 0.050 1.00 34.23 O ANISOU 2061 O HIS B 121 4048 5384 3576 122 -736 -491 O ATOM 2062 CB HIS B 121 4.757 68.110 0.937 1.00 42.11 C ANISOU 2062 CB HIS B 121 4987 6198 4816 31 -929 -697 C ATOM 2063 CG HIS B 121 4.550 68.072 -0.463 1.00 50.37 C ANISOU 2063 CG HIS B 121 6024 7389 5725 124 -988 -771 C ATOM 2064 ND1 HIS B 121 3.916 69.083 -1.172 1.00 60.50 N ANISOU 2064 ND1 HIS B 121 7307 8779 6900 177 -1005 -706 N ATOM 2065 CD2 HIS B 121 5.056 67.194 -1.376 1.00 58.81 C ANISOU 2065 CD2 HIS B 121 7097 8530 6718 192 -1031 -904 C ATOM 2066 CE1 HIS B 121 3.956 68.786 -2.483 1.00 64.23 C ANISOU 2066 CE1 HIS B 121 7791 9389 7223 273 -1064 -795 C ATOM 2067 NE2 HIS B 121 4.654 67.621 -2.612 1.00 74.46 N ANISOU 2067 NE2 HIS B 121 9085 10668 8537 282 -1076 -925 N ATOM 2068 N PHE B 122 6.203 70.520 1.992 1.00 29.02 N ANISOU 2068 N PHE B 122 3386 4524 3115 0 -734 -391 N ATOM 2069 CA PHE B 122 6.727 71.901 1.999 1.00 27.44 C ANISOU 2069 CA PHE B 122 3205 4354 2867 6 -657 -249 C ATOM 2070 C PHE B 122 8.257 71.959 2.180 1.00 28.19 C ANISOU 2070 C PHE B 122 3307 4442 2963 0 -583 -220 C ATOM 2071 O PHE B 122 8.980 72.688 1.470 1.00 28.04 O ANISOU 2071 O PHE B 122 3288 4507 2859 31 -517 -150 O ATOM 2072 CB PHE B 122 6.107 72.702 3.144 1.00 27.00 C ANISOU 2072 CB PHE B 122 3154 4196 2908 -52 -640 -165 C ATOM 2073 CG PHE B 122 6.452 74.178 3.065 1.00 27.70 C ANISOU 2073 CG PHE B 122 3260 4300 2963 -41 -581 -28 C ATOM 2074 CD1 PHE B 122 5.664 75.035 2.275 1.00 29.54 C ANISOU 2074 CD1 PHE B 122 3495 4601 3127 9 -604 32 C ATOM 2075 CD2 PHE B 122 7.589 74.669 3.675 1.00 27.08 C ANISOU 2075 CD2 PHE B 122 3195 4168 2927 -74 -515 36 C ATOM 2076 CE1 PHE B 122 5.970 76.384 2.141 1.00 28.98 C ANISOU 2076 CE1 PHE B 122 3450 4527 3033 20 -556 168 C ATOM 2077 CE2 PHE B 122 7.914 76.015 3.549 1.00 26.41 C ANISOU 2077 CE2 PHE B 122 3121 4081 2830 -73 -463 160 C ATOM 2078 CZ PHE B 122 7.106 76.866 2.789 1.00 29.69 C ANISOU 2078 CZ PHE B 122 3549 4550 3180 -28 -480 232 C ATOM 2079 N PHE B 123 8.758 71.157 3.130 1.00 25.93 N ANISOU 2079 N PHE B 123 3022 4050 2778 -39 -596 -275 N ATOM 2080 CA PHE B 123 10.173 71.168 3.423 1.00 26.40 C ANISOU 2080 CA PHE B 123 3072 4091 2867 -41 -547 -265 C ATOM 2081 C PHE B 123 10.969 70.803 2.154 1.00 27.31 C ANISOU 2081 C PHE B 123 3155 4338 2883 28 -515 -328 C ATOM 2082 O PHE B 123 11.908 71.458 1.814 1.00 30.07 O ANISOU 2082 O PHE B 123 3479 4745 3201 36 -434 -270 O ATOM 2083 CB PHE B 123 10.456 70.179 4.536 1.00 25.15 C ANISOU 2083 CB PHE B 123 2934 3802 2821 -73 -598 -330 C ATOM 2084 CG PHE B 123 11.794 70.346 5.163 1.00 25.92 C ANISOU 2084 CG PHE B 123 3019 3850 2978 -79 -571 -313 C ATOM 2085 CD1 PHE B 123 12.939 69.740 4.564 1.00 27.46 C ANISOU 2085 CD1 PHE B 123 3168 4099 3168 -27 -561 -396 C ATOM 2086 CD2 PHE B 123 11.929 71.027 6.342 1.00 23.95 C ANISOU 2086 CD2 PHE B 123 2798 3505 2797 -127 -565 -238 C ATOM 2087 CE1 PHE B 123 14.198 69.854 5.157 1.00 27.54 C ANISOU 2087 CE1 PHE B 123 3145 4062 3256 -28 -549 -397 C ATOM 2088 CE2 PHE B 123 13.199 71.152 6.952 1.00 27.41 C ANISOU 2088 CE2 PHE B 123 3218 3894 3304 -127 -563 -239 C ATOM 2089 CZ PHE B 123 14.323 70.566 6.361 1.00 27.47 C ANISOU 2089 CZ PHE B 123 3165 3951 3321 -79 -558 -318 C ATOM 2090 N ILE B 124 10.534 69.813 1.420 1.00 28.00 N ANISOU 2090 N ILE B 124 3241 4480 2919 75 -574 -447 N ATOM 2091 CA ILE B 124 11.296 69.320 0.325 1.00 30.41 C ANISOU 2091 CA ILE B 124 3519 4908 3129 148 -547 -534 C ATOM 2092 C ILE B 124 11.171 70.213 -0.884 1.00 32.19 C ANISOU 2092 C ILE B 124 3754 5293 3183 193 -483 -460 C ATOM 2093 O ILE B 124 12.206 70.538 -1.493 1.00 34.77 O ANISOU 2093 O ILE B 124 4056 5717 3436 221 -382 -435 O ATOM 2094 CB ILE B 124 10.885 67.878 0.000 1.00 31.91 C ANISOU 2094 CB ILE B 124 3708 5084 3333 189 -648 -709 C ATOM 2095 CG1 ILE B 124 11.359 66.925 1.106 1.00 33.96 C ANISOU 2095 CG1 ILE B 124 3967 5182 3753 155 -699 -773 C ATOM 2096 CG2 ILE B 124 11.440 67.452 -1.350 1.00 34.16 C ANISOU 2096 CG2 ILE B 124 3971 5529 3479 284 -624 -817 C ATOM 2097 CD1 ILE B 124 10.732 65.552 0.929 1.00 37.62 C ANISOU 2097 CD1 ILE B 124 4440 5587 4265 174 -810 -927 C ATOM 2098 N GLU B 125 9.944 70.615 -1.258 1.00 31.63 N ANISOU 2098 N GLU B 125 3717 5254 3048 204 -537 -423 N ATOM 2099 CA GLU B 125 9.792 71.524 -2.402 1.00 32.48 C ANISOU 2099 CA GLU B 125 3857 5507 2978 257 -490 -332 C ATOM 2100 C GLU B 125 10.455 72.898 -2.198 1.00 32.75 C ANISOU 2100 C GLU B 125 3899 5531 3014 214 -371 -146 C ATOM 2101 O GLU B 125 10.872 73.554 -3.159 1.00 34.01 O ANISOU 2101 O GLU B 125 4084 5810 3029 250 -286 -60 O ATOM 2102 CB GLU B 125 8.355 71.638 -2.864 1.00 32.19 C ANISOU 2102 CB GLU B 125 3850 5503 2879 293 -596 -344 C ATOM 2103 CG GLU B 125 7.692 70.292 -2.980 1.00 33.29 C ANISOU 2103 CG GLU B 125 3965 5627 3055 318 -718 -533 C ATOM 2104 CD GLU B 125 8.338 69.379 -4.046 1.00 38.90 C ANISOU 2104 CD GLU B 125 4676 6464 3639 403 -720 -678 C ATOM 2105 OE1 GLU B 125 9.236 69.870 -4.827 1.00 35.57 O ANISOU 2105 OE1 GLU B 125 4275 6173 3067 449 -613 -620 O ATOM 2106 OE2 GLU B 125 7.970 68.148 -4.042 1.00 41.69 O ANISOU 2106 OE2 GLU B 125 5006 6777 4059 417 -822 -854 O ATOM 2107 N ASN B 126 10.580 73.339 -0.949 1.00 32.11 N ANISOU 2107 N ASN B 126 3802 5304 3094 136 -362 -83 N ATOM 2108 CA ASN B 126 11.281 74.603 -0.719 1.00 33.57 C ANISOU 2108 CA ASN B 126 3986 5461 3310 90 -260 74 C ATOM 2109 C ASN B 126 12.762 74.416 -0.427 1.00 34.67 C ANISOU 2109 C ASN B 126 4063 5588 3521 59 -172 52 C ATOM 2110 O ASN B 126 13.484 75.375 -0.079 1.00 34.44 O ANISOU 2110 O ASN B 126 4011 5513 3562 6 -91 161 O ATOM 2111 CB ASN B 126 10.607 75.410 0.376 1.00 31.70 C ANISOU 2111 CB ASN B 126 3765 5084 3195 33 -298 157 C ATOM 2112 CG ASN B 126 9.254 75.901 -0.064 1.00 31.39 C ANISOU 2112 CG ASN B 126 3769 5071 3086 71 -364 203 C ATOM 2113 OD1 ASN B 126 9.152 76.940 -0.663 1.00 31.57 O ANISOU 2113 OD1 ASN B 126 3827 5131 3036 90 -329 330 O ATOM 2114 ND2 ASN B 126 8.218 75.094 0.158 1.00 30.06 N ANISOU 2114 ND2 ASN B 126 3594 4885 2943 85 -465 94 N ATOM 2115 N ASN B 127 13.194 73.172 -0.525 1.00 35.19 N ANISOU 2115 N ASN B 127 4094 5682 3592 95 -201 -101 N ATOM 2116 CA ASN B 127 14.577 72.847 -0.403 1.00 37.31 C ANISOU 2116 CA ASN B 127 4291 5960 3926 89 -131 -153 C ATOM 2117 C ASN B 127 15.128 73.320 0.921 1.00 34.71 C ANISOU 2117 C ASN B 127 3931 5481 3778 16 -136 -105 C ATOM 2118 O ASN B 127 16.294 73.742 1.014 1.00 38.01 O ANISOU 2118 O ASN B 127 4278 5902 4264 -12 -51 -78 O ATOM 2119 CB ASN B 127 15.334 73.470 -1.576 1.00 43.99 C ANISOU 2119 CB ASN B 127 5111 6959 4645 110 16 -82 C ATOM 2120 CG ASN B 127 16.786 73.015 -1.633 1.00 50.79 C ANISOU 2120 CG ASN B 127 5869 7860 5569 116 103 -166 C ATOM 2121 OD1 ASN B 127 17.141 71.916 -1.174 1.00 52.19 O ANISOU 2121 OD1 ASN B 127 6005 7990 5834 146 30 -320 O ATOM 2122 ND2 ASN B 127 17.639 73.870 -2.169 1.00 53.71 N ANISOU 2122 ND2 ASN B 127 6191 8306 5909 85 258 -64 N ATOM 2123 N LEU B 128 14.324 73.209 1.974 1.00 31.23 N ANISOU 2123 N LEU B 128 3536 4911 3419 -15 -235 -107 N ATOM 2124 CA LEU B 128 14.783 73.684 3.278 1.00 29.64 C ANISOU 2124 CA LEU B 128 3324 4572 3367 -75 -252 -68 C ATOM 2125 C LEU B 128 15.972 72.820 3.780 1.00 32.57 C ANISOU 2125 C LEU B 128 3635 4902 3838 -61 -277 -179 C ATOM 2126 O LEU B 128 16.759 73.232 4.680 1.00 31.86 O ANISOU 2126 O LEU B 128 3511 4725 3871 -98 -284 -162 O ATOM 2127 CB LEU B 128 13.653 73.673 4.274 1.00 27.04 C ANISOU 2127 CB LEU B 128 3064 4131 3079 -104 -340 -54 C ATOM 2128 CG LEU B 128 12.395 74.452 3.824 1.00 28.74 C ANISOU 2128 CG LEU B 128 3324 4381 3217 -104 -336 33 C ATOM 2129 CD1 LEU B 128 11.380 74.575 4.980 1.00 25.19 C ANISOU 2129 CD1 LEU B 128 2921 3816 2834 -140 -399 43 C ATOM 2130 CD2 LEU B 128 12.845 75.828 3.383 1.00 28.95 C ANISOU 2130 CD2 LEU B 128 3336 4436 3229 -123 -247 165 C ATOM 2131 N MET B 129 16.150 71.646 3.196 1.00 33.57 N ANISOU 2131 N MET B 129 3744 5089 3923 0 -301 -303 N ATOM 2132 CA MET B 129 17.349 70.841 3.601 1.00 37.26 C ANISOU 2132 CA MET B 129 4143 5517 4496 30 -331 -416 C ATOM 2133 C MET B 129 18.651 71.596 3.325 1.00 39.00 C ANISOU 2133 C MET B 129 4253 5795 4769 14 -221 -386 C ATOM 2134 O MET B 129 19.692 71.329 3.918 1.00 39.90 O ANISOU 2134 O MET B 129 4295 5854 5010 22 -249 -452 O ATOM 2135 CB MET B 129 17.372 69.434 2.972 1.00 39.45 C ANISOU 2135 CB MET B 129 4414 5841 4733 109 -380 -572 C ATOM 2136 CG MET B 129 17.115 69.323 1.507 1.00 45.84 C ANISOU 2136 CG MET B 129 5212 6820 5387 161 -308 -605 C ATOM 2137 SD MET B 129 15.373 69.343 0.951 1.00 48.46 S ANISOU 2137 SD MET B 129 5645 7188 5580 161 -358 -569 S ATOM 2138 CE MET B 129 14.516 68.684 2.328 1.00 45.50 C ANISOU 2138 CE MET B 129 5337 6617 5332 114 -497 -587 C ATOM 2139 N ASN B 130 18.578 72.574 2.438 1.00 39.83 N ANISOU 2139 N ASN B 130 4345 6005 4783 -11 -98 -279 N ATOM 2140 CA ASN B 130 19.769 73.316 2.110 1.00 44.30 C ANISOU 2140 CA ASN B 130 4800 6625 5406 -43 29 -236 C ATOM 2141 C ASN B 130 20.067 74.528 3.039 1.00 41.82 C ANISOU 2141 C ASN B 130 4467 6192 5230 -131 34 -125 C ATOM 2142 O ASN B 130 21.012 75.270 2.812 1.00 45.06 O ANISOU 2142 O ASN B 130 4779 6628 5714 -177 142 -76 O ATOM 2143 CB ASN B 130 19.686 73.702 0.644 1.00 49.36 C ANISOU 2143 CB ASN B 130 5440 7439 5874 -26 173 -172 C ATOM 2144 CG ASN B 130 20.972 74.220 0.134 1.00 57.60 C ANISOU 2144 CG ASN B 130 6357 8564 6964 -55 333 -147 C ATOM 2145 OD1 ASN B 130 21.005 75.300 -0.434 1.00 60.42 O ANISOU 2145 OD1 ASN B 130 6720 8969 7267 -109 458 4 O ATOM 2146 ND2 ASN B 130 22.071 73.482 0.366 1.00 65.88 N ANISOU 2146 ND2 ASN B 130 7285 9618 8130 -24 330 -290 N ATOM 2147 N HIS B 131 19.314 74.660 4.116 1.00 38.45 N ANISOU 2147 N HIS B 131 4126 5633 4849 -153 -82 -101 N ATOM 2148 CA HIS B 131 19.522 75.674 5.114 1.00 36.85 C ANISOU 2148 CA HIS B 131 3919 5308 4774 -219 -107 -30 C ATOM 2149 C HIS B 131 19.410 75.155 6.525 1.00 35.50 C ANISOU 2149 C HIS B 131 3797 5001 4689 -209 -257 -104 C ATOM 2150 O HIS B 131 19.074 75.886 7.429 1.00 33.36 O ANISOU 2150 O HIS B 131 3575 4628 4471 -249 -305 -51 O ATOM 2151 CB HIS B 131 18.517 76.789 4.946 1.00 41.98 C ANISOU 2151 CB HIS B 131 4649 5940 5362 -260 -74 114 C ATOM 2152 CG HIS B 131 18.434 77.357 3.578 1.00 43.27 C ANISOU 2152 CG HIS B 131 4803 6227 5409 -264 60 215 C ATOM 2153 ND1 HIS B 131 19.051 78.468 3.243 1.00 44.51 N ANISOU 2153 ND1 HIS B 131 4907 6382 5621 -325 168 326 N ATOM 2154 CD2 HIS B 131 17.733 76.948 2.468 1.00 45.40 C ANISOU 2154 CD2 HIS B 131 5126 6624 5501 -210 93 225 C ATOM 2155 CE1 HIS B 131 18.778 78.754 1.985 1.00 47.26 C ANISOU 2155 CE1 HIS B 131 5285 6852 5819 -311 274 417 C ATOM 2156 NE2 HIS B 131 17.969 77.824 1.513 1.00 45.68 N ANISOU 2156 NE2 HIS B 131 5151 6736 5470 -234 221 349 N ATOM 2157 N PHE B 132 19.678 73.887 6.738 1.00 36.08 N ANISOU 2157 N PHE B 132 3870 5069 4772 -151 -335 -226 N ATOM 2158 CA PHE B 132 19.644 73.320 8.063 1.00 38.39 C ANISOU 2158 CA PHE B 132 4226 5230 5130 -136 -478 -283 C ATOM 2159 C PHE B 132 20.531 72.099 8.126 1.00 40.43 C ANISOU 2159 C PHE B 132 4432 5483 5447 -67 -547 -419 C ATOM 2160 O PHE B 132 20.059 71.006 8.051 1.00 39.64 O ANISOU 2160 O PHE B 132 4394 5374 5295 -21 -605 -479 O ATOM 2161 CB PHE B 132 18.223 72.969 8.458 1.00 35.48 C ANISOU 2161 CB PHE B 132 3996 4816 4667 -138 -531 -251 C ATOM 2162 CG PHE B 132 17.992 72.893 9.928 1.00 33.92 C ANISOU 2162 CG PHE B 132 3890 4484 4513 -150 -641 -252 C ATOM 2163 CD1 PHE B 132 18.466 71.846 10.665 1.00 32.86 C ANISOU 2163 CD1 PHE B 132 3789 4274 4422 -106 -751 -335 C ATOM 2164 CD2 PHE B 132 17.277 73.864 10.566 1.00 34.33 C ANISOU 2164 CD2 PHE B 132 4004 4487 4552 -196 -634 -170 C ATOM 2165 CE1 PHE B 132 18.238 71.776 12.006 1.00 34.99 C ANISOU 2165 CE1 PHE B 132 4164 4429 4702 -111 -847 -325 C ATOM 2166 CE2 PHE B 132 17.043 73.795 11.909 1.00 35.73 C ANISOU 2166 CE2 PHE B 132 4276 4558 4744 -200 -722 -176 C ATOM 2167 CZ PHE B 132 17.534 72.754 12.636 1.00 35.28 C ANISOU 2167 CZ PHE B 132 4262 4433 4710 -159 -827 -247 C ATOM 2168 N PRO B 133 21.899 72.368 8.295 1.00 44.04 N ANISOU 2168 N PRO B 133 4758 5936 6041 -62 -545 -473 N ATOM 2169 CA PRO B 133 22.737 71.159 8.316 1.00 44.10 C ANISOU 2169 CA PRO B 133 4706 5938 6114 21 -622 -616 C ATOM 2170 C PRO B 133 22.696 70.392 9.617 1.00 42.32 C ANISOU 2170 C PRO B 133 4582 5565 5934 63 -805 -666 C ATOM 2171 O PRO B 133 22.361 70.906 10.646 1.00 41.03 O ANISOU 2171 O PRO B 133 4505 5308 5778 27 -872 -606 O ATOM 2172 CB PRO B 133 24.123 71.678 8.011 1.00 43.00 C ANISOU 2172 CB PRO B 133 4379 5851 6109 13 -554 -663 C ATOM 2173 CG PRO B 133 24.169 72.967 8.664 1.00 43.51 C ANISOU 2173 CG PRO B 133 4440 5851 6242 -69 -547 -570 C ATOM 2174 CD PRO B 133 22.846 73.577 8.483 1.00 43.03 C ANISOU 2174 CD PRO B 133 4509 5796 6043 -121 -492 -437 C ATOM 2175 N LEU B 134 23.040 69.129 9.541 1.00 41.86 N ANISOU 2175 N LEU B 134 4520 5485 5898 146 -886 -778 N ATOM 2176 CA LEU B 134 22.964 68.261 10.683 1.00 44.95 C ANISOU 2176 CA LEU B 134 5030 5731 6317 194 -1061 -812 C ATOM 2177 C LEU B 134 24.242 67.463 10.872 1.00 46.16 C ANISOU 2177 C LEU B 134 5087 5845 6605 291 -1172 -953 C ATOM 2178 O LEU B 134 24.990 67.280 9.952 1.00 46.66 O ANISOU 2178 O LEU B 134 4998 6007 6722 330 -1101 -1044 O ATOM 2179 CB LEU B 134 21.792 67.313 10.518 1.00 41.41 C ANISOU 2179 CB LEU B 134 4722 5251 5763 200 -1082 -796 C ATOM 2180 CG LEU B 134 20.376 67.835 10.597 1.00 37.65 C ANISOU 2180 CG LEU B 134 4361 4778 5167 119 -1017 -672 C ATOM 2181 CD1 LEU B 134 19.497 66.678 10.242 1.00 36.41 C ANISOU 2181 CD1 LEU B 134 4289 4595 4951 137 -1044 -702 C ATOM 2182 CD2 LEU B 134 20.047 68.372 11.969 1.00 34.84 C ANISOU 2182 CD2 LEU B 134 4118 4314 4805 78 -1085 -590 C ATOM 2183 N GLU B 135 24.481 66.986 12.075 1.00 46.91 N ANISOU 2183 N GLU B 135 5276 5799 6748 337 -1347 -972 N ATOM 2184 CA GLU B 135 25.718 66.243 12.328 1.00 55.96 C ANISOU 2184 CA GLU B 135 6331 6895 8036 444 -1481 -1111 C ATOM 2185 C GLU B 135 25.749 64.907 11.600 1.00 57.35 C ANISOU 2185 C GLU B 135 6498 7073 8218 531 -1505 -1215 C ATOM 2186 O GLU B 135 24.749 64.167 11.595 1.00 51.60 O ANISOU 2186 O GLU B 135 5922 6286 7396 525 -1526 -1173 O ATOM 2187 CB GLU B 135 25.925 65.960 13.808 1.00 61.03 C ANISOU 2187 CB GLU B 135 7105 7377 8708 490 -1689 -1101 C ATOM 2188 CG GLU B 135 27.360 66.243 14.255 1.00 77.83 C ANISOU 2188 CG GLU B 135 9078 9487 11006 554 -1800 -1210 C ATOM 2189 CD GLU B 135 27.519 67.662 14.823 1.00 83.83 C ANISOU 2189 CD GLU B 135 9800 10262 11791 472 -1775 -1151 C ATOM 2190 OE1 GLU B 135 26.492 68.390 14.869 1.00 82.94 O ANISOU 2190 OE1 GLU B 135 9791 10169 11555 375 -1671 -1024 O ATOM 2191 OE2 GLU B 135 28.648 68.055 15.237 1.00 85.14 O ANISOU 2191 OE2 GLU B 135 9829 10412 12110 507 -1868 -1240 O ATOM 2192 N ASP B 136 26.886 64.594 10.988 1.00 63.05 N ANISOU 2192 N ASP B 136 7034 7860 9063 610 -1499 -1360 N ATOM 2193 CA ASP B 136 27.044 63.343 10.257 1.00 69.96 C ANISOU 2193 CA ASP B 136 7879 8740 9961 710 -1526 -1490 C ATOM 2194 C ASP B 136 27.001 62.145 11.200 1.00 70.36 C ANISOU 2194 C ASP B 136 8083 8594 10056 799 -1751 -1522 C ATOM 2195 O ASP B 136 27.819 62.031 12.112 1.00 68.94 O ANISOU 2195 O ASP B 136 7894 8316 9985 865 -1912 -1562 O ATOM 2196 CB ASP B 136 28.355 63.344 9.468 1.00 73.80 C ANISOU 2196 CB ASP B 136 8114 9346 10579 782 -1463 -1651 C ATOM 2197 CG ASP B 136 28.320 64.286 8.281 1.00 76.32 C ANISOU 2197 CG ASP B 136 8300 9869 10829 701 -1213 -1617 C ATOM 2198 OD1 ASP B 136 27.268 64.921 8.055 1.00 73.45 O ANISOU 2198 OD1 ASP B 136 8044 9546 10318 600 -1110 -1474 O ATOM 2199 OD2 ASP B 136 29.344 64.391 7.573 1.00 85.59 O ANISOU 2199 OD2 ASP B 136 9262 11161 12095 741 -1118 -1732 O ATOM 2200 N HIS B 137 26.042 61.254 10.972 1.00 67.07 N ANISOU 2200 N HIS B 137 7811 8115 9559 799 -1768 -1502 N ATOM 2201 CA HIS B 137 25.891 60.070 11.796 1.00 73.23 C ANISOU 2201 CA HIS B 137 8755 8691 10376 870 -1966 -1510 C ATOM 2202 C HIS B 137 26.343 58.840 11.066 1.00 81.63 C ANISOU 2202 C HIS B 137 9755 9728 11535 992 -2028 -1682 C ATOM 2203 O HIS B 137 27.127 58.029 11.697 1.00 88.52 O ANISOU 2203 O HIS B 137 10644 10456 12533 1112 -2224 -1764 O ATOM 2204 CB HIS B 137 24.443 59.911 12.243 1.00 66.61 C ANISOU 2204 CB HIS B 137 8138 7765 9406 770 -1953 -1354 C ATOM 2205 CG HIS B 137 23.977 60.987 13.194 1.00 63.93 C ANISOU 2205 CG HIS B 137 7893 7420 8977 670 -1923 -1192 C ATOM 2206 ND1 HIS B 137 24.667 61.324 14.299 1.00 64.70 N ANISOU 2206 ND1 HIS B 137 8024 7444 9117 705 -2048 -1170 N ATOM 2207 CD2 HIS B 137 22.849 61.805 13.171 1.00 56.81 C ANISOU 2207 CD2 HIS B 137 7057 6581 7946 543 -1787 -1059 C ATOM 2208 CE1 HIS B 137 24.017 62.307 14.951 1.00 63.02 C ANISOU 2208 CE1 HIS B 137 7899 7248 8800 605 -1989 -1034 C ATOM 2209 NE2 HIS B 137 22.905 62.600 14.259 1.00 55.63 N ANISOU 2209 NE2 HIS B 137 6978 6393 7765 507 -1825 -966 N TER 2210 HIS B 137 ATOM 2211 N THR C 108 8.229 25.396 13.078 1.00 76.34 N ANISOU 2211 N THR C 108 7287 7716 14002 1132 2839 2267 N ATOM 2212 CA THR C 108 7.773 26.372 14.111 1.00 74.37 C ANISOU 2212 CA THR C 108 6994 7650 13614 856 2209 2156 C ATOM 2213 C THR C 108 6.583 27.152 13.574 1.00 76.83 C ANISOU 2213 C THR C 108 7732 8089 13370 768 2216 1846 C ATOM 2214 O THR C 108 5.503 27.204 14.221 1.00 73.60 O ANISOU 2214 O THR C 108 7599 7836 12531 635 1873 1586 O ATOM 2215 CB THR C 108 8.848 27.387 14.513 1.00 77.03 C ANISOU 2215 CB THR C 108 6805 7924 14538 723 1970 2413 C ATOM 2216 OG1 THR C 108 10.105 26.725 14.626 1.00 84.85 O ANISOU 2216 OG1 THR C 108 7318 8769 16153 861 2102 2790 O ATOM 2217 CG2 THR C 108 8.527 27.991 15.846 1.00 74.37 C ANISOU 2217 CG2 THR C 108 6421 7761 14075 464 1270 2254 C ATOM 2218 N MET C 109 6.758 27.742 12.396 1.00 71.90 N ANISOU 2218 N MET C 109 7153 7409 12756 874 2635 1918 N ATOM 2219 CA MET C 109 5.674 28.500 11.815 1.00 68.96 C ANISOU 2219 CA MET C 109 7143 7182 11875 835 2654 1706 C ATOM 2220 C MET C 109 4.517 27.625 11.337 1.00 63.19 C ANISOU 2220 C MET C 109 6892 6589 10528 913 2742 1381 C ATOM 2221 O MET C 109 3.369 27.910 11.640 1.00 63.95 O ANISOU 2221 O MET C 109 7229 6838 10230 785 2455 1147 O ATOM 2222 CB MET C 109 6.198 29.417 10.729 1.00 77.30 C ANISOU 2222 CB MET C 109 8096 8166 13107 960 3080 1953 C ATOM 2223 CG MET C 109 5.171 30.381 10.174 1.00 80.91 C ANISOU 2223 CG MET C 109 8848 8781 13114 942 3083 1846 C ATOM 2224 SD MET C 109 4.884 29.963 8.443 1.00102.62 S ANISOU 2224 SD MET C 109 11997 11683 15312 1289 3692 1856 S ATOM 2225 CE MET C 109 3.396 28.964 8.476 1.00 84.77 C ANISOU 2225 CE MET C 109 10233 9665 12311 1239 3407 1346 C ATOM 2226 N GLU C 110 4.811 26.571 10.599 1.00 62.71 N ANISOU 2226 N GLU C 110 6951 6447 10429 1115 3143 1348 N ATOM 2227 CA GLU C 110 3.824 25.585 10.164 1.00 60.90 C ANISOU 2227 CA GLU C 110 7133 6285 9723 1160 3210 978 C ATOM 2228 C GLU C 110 3.090 24.926 11.334 1.00 54.86 C ANISOU 2228 C GLU C 110 6397 5515 8934 987 2804 807 C ATOM 2229 O GLU C 110 1.914 24.600 11.251 1.00 50.61 O ANISOU 2229 O GLU C 110 6146 5071 8011 911 2670 497 O ATOM 2230 CB GLU C 110 4.512 24.490 9.299 1.00 71.63 C ANISOU 2230 CB GLU C 110 8571 7462 11184 1409 3754 956 C ATOM 2231 CG GLU C 110 3.577 23.872 8.256 1.00 79.78 C ANISOU 2231 CG GLU C 110 10095 8598 11619 1491 3933 512 C ATOM 2232 CD GLU C 110 2.357 24.761 7.902 1.00 82.24 C ANISOU 2232 CD GLU C 110 10662 9237 11350 1379 3628 324 C ATOM 2233 OE1 GLU C 110 2.386 26.003 8.128 1.00 80.11 O ANISOU 2233 OE1 GLU C 110 10229 9085 11125 1315 3463 582 O ATOM 2234 OE2 GLU C 110 1.350 24.216 7.390 1.00 83.16 O ANISOU 2234 OE2 GLU C 110 11118 9474 11007 1352 3548 -85 O ATOM 2235 N ASN C 111 3.835 24.710 12.401 1.00 51.97 N ANISOU 2235 N ASN C 111 5702 5041 9004 947 2626 1050 N ATOM 2236 CA ASN C 111 3.292 24.318 13.645 1.00 51.29 C ANISOU 2236 CA ASN C 111 5603 4992 8893 820 2243 1011 C ATOM 2237 C ASN C 111 2.303 25.361 14.261 1.00 46.10 C ANISOU 2237 C ASN C 111 5072 4543 7902 623 1829 875 C ATOM 2238 O ASN C 111 1.255 24.976 14.778 1.00 41.13 O ANISOU 2238 O ASN C 111 4635 3971 7022 550 1661 703 O ATOM 2239 CB ASN C 111 4.432 24.038 14.605 1.00 57.90 C ANISOU 2239 CB ASN C 111 6036 5746 10217 856 2106 1362 C ATOM 2240 CG ASN C 111 4.012 23.166 15.794 1.00 62.22 C ANISOU 2240 CG ASN C 111 6590 6307 10743 839 1859 1405 C ATOM 2241 OD1 ASN C 111 3.077 22.329 15.714 1.00 61.67 O ANISOU 2241 OD1 ASN C 111 6783 6171 10480 852 1978 1202 O ATOM 2242 ND2 ASN C 111 4.735 23.340 16.910 1.00 68.85 N ANISOU 2242 ND2 ASN C 111 7117 7234 11808 821 1512 1692 N ATOM 2243 N LEU C 112 2.643 26.652 14.216 1.00 43.70 N ANISOU 2243 N LEU C 112 4638 4301 7663 548 1716 969 N ATOM 2244 CA LEU C 112 1.754 27.699 14.699 1.00 41.05 C ANISOU 2244 CA LEU C 112 4428 4101 7067 388 1412 833 C ATOM 2245 C LEU C 112 0.430 27.603 13.949 1.00 39.91 C ANISOU 2245 C LEU C 112 4626 4062 6476 404 1519 592 C ATOM 2246 O LEU C 112 -0.629 27.535 14.558 1.00 36.06 O ANISOU 2246 O LEU C 112 4293 3652 5755 316 1310 441 O ATOM 2247 CB LEU C 112 2.349 29.108 14.547 1.00 41.15 C ANISOU 2247 CB LEU C 112 4241 4078 7316 316 1376 958 C ATOM 2248 CG LEU C 112 1.461 30.243 15.110 1.00 38.63 C ANISOU 2248 CG LEU C 112 4048 3832 6797 158 1103 803 C ATOM 2249 CD1 LEU C 112 1.011 29.861 16.513 1.00 36.47 C ANISOU 2249 CD1 LEU C 112 3854 3642 6361 64 732 674 C ATOM 2250 CD2 LEU C 112 2.138 31.632 15.079 1.00 37.28 C ANISOU 2250 CD2 LEU C 112 3632 3530 7002 58 1073 910 C ATOM 2251 N SER C 113 0.537 27.618 12.626 1.00 42.47 N ANISOU 2251 N SER C 113 5045 4402 6690 532 1845 582 N ATOM 2252 CA SER C 113 -0.565 27.455 11.706 1.00 42.41 C ANISOU 2252 CA SER C 113 5335 4540 6239 573 1925 354 C ATOM 2253 C SER C 113 -1.513 26.305 12.089 1.00 41.74 C ANISOU 2253 C SER C 113 5406 4439 6015 504 1798 89 C ATOM 2254 O SER C 113 -2.742 26.537 12.231 1.00 38.03 O ANISOU 2254 O SER C 113 5060 4090 5299 408 1594 -63 O ATOM 2255 CB SER C 113 -0.017 27.234 10.296 1.00 47.38 C ANISOU 2255 CB SER C 113 6064 5189 6749 778 2333 373 C ATOM 2256 OG SER C 113 -1.083 27.353 9.388 1.00 48.97 O ANISOU 2256 OG SER C 113 6545 5616 6447 816 2318 167 O ATOM 2257 N ARG C 114 -0.944 25.090 12.245 1.00 40.99 N ANISOU 2257 N ARG C 114 5263 4157 6153 563 1955 69 N ATOM 2258 CA ARG C 114 -1.695 23.968 12.705 1.00 41.18 C ANISOU 2258 CA ARG C 114 5370 4077 6202 499 1892 -120 C ATOM 2259 C ARG C 114 -2.439 24.278 14.037 1.00 38.44 C ANISOU 2259 C ARG C 114 4968 3784 5854 366 1566 -42 C ATOM 2260 O ARG C 114 -3.617 23.969 14.190 1.00 40.02 O ANISOU 2260 O ARG C 114 5276 4001 5930 279 1466 -215 O ATOM 2261 CB ARG C 114 -0.739 22.802 12.917 1.00 48.18 C ANISOU 2261 CB ARG C 114 6130 4702 7473 608 2136 -17 C ATOM 2262 CG ARG C 114 -1.430 21.616 13.555 1.00 55.59 C ANISOU 2262 CG ARG C 114 7097 5459 8566 554 2117 -128 C ATOM 2263 CD ARG C 114 -0.488 20.451 13.860 1.00 66.69 C ANISOU 2263 CD ARG C 114 8343 6568 10426 692 2391 51 C ATOM 2264 NE ARG C 114 -1.210 19.166 13.768 1.00 79.42 N ANISOU 2264 NE ARG C 114 10061 7909 12207 661 2558 -199 N ATOM 2265 CZ ARG C 114 -2.093 18.695 14.660 1.00 75.03 C ANISOU 2265 CZ ARG C 114 9476 7275 11759 569 2425 -167 C ATOM 2266 NH1 ARG C 114 -2.371 19.401 15.730 1.00 73.38 N ANISOU 2266 NH1 ARG C 114 9188 7280 11412 526 2128 92 N ATOM 2267 NH2 ARG C 114 -2.683 17.506 14.490 1.00 71.85 N ANISOU 2267 NH2 ARG C 114 9121 6548 11631 529 2626 -395 N ATOM 2268 N ARG C 115 -1.755 24.865 15.007 1.00 33.91 N ANISOU 2268 N ARG C 115 4224 3235 5425 356 1407 208 N ATOM 2269 CA ARG C 115 -2.374 25.137 16.294 1.00 33.01 C ANISOU 2269 CA ARG C 115 4118 3193 5233 274 1140 265 C ATOM 2270 C ARG C 115 -3.534 26.189 16.154 1.00 32.78 C ANISOU 2270 C ARG C 115 4233 3308 4913 180 1010 121 C ATOM 2271 O ARG C 115 -4.595 26.096 16.872 1.00 31.74 O ANISOU 2271 O ARG C 115 4187 3204 4669 131 911 77 O ATOM 2272 CB ARG C 115 -1.286 25.582 17.281 1.00 31.08 C ANISOU 2272 CB ARG C 115 3675 2981 5151 285 947 502 C ATOM 2273 CG ARG C 115 -0.359 24.403 17.625 1.00 33.46 C ANISOU 2273 CG ARG C 115 3798 3157 5759 406 1048 718 C ATOM 2274 CD ARG C 115 0.673 24.810 18.673 1.00 35.80 C ANISOU 2274 CD ARG C 115 3859 3550 6193 412 755 964 C ATOM 2275 NE ARG C 115 1.276 23.603 19.206 1.00 39.70 N ANISOU 2275 NE ARG C 115 4188 3963 6932 560 820 1234 N ATOM 2276 CZ ARG C 115 1.927 23.527 20.360 1.00 40.27 C ANISOU 2276 CZ ARG C 115 4079 4171 7051 614 526 1499 C ATOM 2277 NH1 ARG C 115 2.154 24.623 21.088 1.00 41.70 N ANISOU 2277 NH1 ARG C 115 4227 4563 7053 501 116 1451 N ATOM 2278 NH2 ARG C 115 2.337 22.361 20.782 1.00 42.00 N ANISOU 2278 NH2 ARG C 115 4154 4312 7494 787 636 1800 N ATOM 2279 N LEU C 116 -3.364 27.150 15.248 1.00 27.62 N ANISOU 2279 N LEU C 116 3587 2729 4177 184 1060 103 N ATOM 2280 CA LEU C 116 -4.370 28.190 15.061 1.00 28.04 C ANISOU 2280 CA LEU C 116 3733 2902 4019 133 974 41 C ATOM 2281 C LEU C 116 -5.615 27.572 14.435 1.00 29.85 C ANISOU 2281 C LEU C 116 4084 3196 4061 121 993 -142 C ATOM 2282 O LEU C 116 -6.752 27.987 14.731 1.00 30.00 O ANISOU 2282 O LEU C 116 4140 3281 3977 69 884 -176 O ATOM 2283 CB LEU C 116 -3.815 29.310 14.118 1.00 30.93 C ANISOU 2283 CB LEU C 116 4049 3313 4389 184 1087 145 C ATOM 2284 CG LEU C 116 -2.636 30.183 14.641 1.00 30.64 C ANISOU 2284 CG LEU C 116 3822 3168 4650 150 1048 309 C ATOM 2285 CD1 LEU C 116 -2.063 31.126 13.519 1.00 31.49 C ANISOU 2285 CD1 LEU C 116 3843 3261 4859 231 1277 476 C ATOM 2286 CD2 LEU C 116 -3.055 30.983 15.877 1.00 28.95 C ANISOU 2286 CD2 LEU C 116 3623 2932 4444 33 806 255 C ATOM 2287 N LYS C 117 -5.437 26.576 13.580 1.00 30.87 N ANISOU 2287 N LYS C 117 4259 3290 4179 164 1128 -280 N ATOM 2288 CA LYS C 117 -6.587 25.909 12.959 1.00 30.78 C ANISOU 2288 CA LYS C 117 4338 3326 4029 112 1083 -531 C ATOM 2289 C LYS C 117 -7.338 25.032 13.932 1.00 28.73 C ANISOU 2289 C LYS C 117 4028 2908 3980 17 1024 -578 C ATOM 2290 O LYS C 117 -8.544 24.923 13.877 1.00 29.93 O ANISOU 2290 O LYS C 117 4168 3096 4108 -67 913 -694 O ATOM 2291 CB LYS C 117 -6.134 25.069 11.783 1.00 33.81 C ANISOU 2291 CB LYS C 117 4827 3688 4331 179 1254 -746 C ATOM 2292 CG LYS C 117 -5.380 25.860 10.749 1.00 37.09 C ANISOU 2292 CG LYS C 117 5309 4266 4515 326 1400 -648 C ATOM 2293 CD LYS C 117 -5.066 25.037 9.498 1.00 39.99 C ANISOU 2293 CD LYS C 117 5859 4654 4681 430 1604 -910 C ATOM 2294 CE LYS C 117 -4.476 25.981 8.482 1.00 44.36 C ANISOU 2294 CE LYS C 117 6491 5422 4940 619 1783 -730 C ATOM 2295 NZ LYS C 117 -4.182 25.322 7.190 1.00 51.06 N ANISOU 2295 NZ LYS C 117 7586 6355 5458 775 2018 -982 N ATOM 2296 N VAL C 118 -6.608 24.333 14.796 1.00 28.31 N ANISOU 2296 N VAL C 118 3913 2671 4173 50 1119 -449 N ATOM 2297 CA VAL C 118 -7.226 23.687 15.930 1.00 25.97 C ANISOU 2297 CA VAL C 118 3562 2240 4066 15 1111 -359 C ATOM 2298 C VAL C 118 -8.035 24.677 16.772 1.00 25.54 C ANISOU 2298 C VAL C 118 3520 2317 3868 -11 973 -235 C ATOM 2299 O VAL C 118 -9.181 24.393 17.127 1.00 28.84 O ANISOU 2299 O VAL C 118 3909 2684 4365 -62 976 -250 O ATOM 2300 CB VAL C 118 -6.179 22.978 16.805 1.00 27.12 C ANISOU 2300 CB VAL C 118 3630 2238 4435 112 1217 -129 C ATOM 2301 CG1 VAL C 118 -6.771 22.635 18.170 1.00 29.07 C ANISOU 2301 CG1 VAL C 118 3850 2434 4762 137 1209 82 C ATOM 2302 CG2 VAL C 118 -5.644 21.735 16.092 1.00 26.52 C ANISOU 2302 CG2 VAL C 118 3527 1928 4621 150 1445 -251 C ATOM 2303 N THR C 119 -7.464 25.846 17.089 1.00 25.61 N ANISOU 2303 N THR C 119 3556 2455 3719 23 881 -121 N ATOM 2304 CA THR C 119 -8.130 26.811 17.880 1.00 24.30 C ANISOU 2304 CA THR C 119 3439 2368 3425 15 799 -51 C ATOM 2305 C THR C 119 -9.382 27.313 17.115 1.00 27.68 C ANISOU 2305 C THR C 119 3859 2872 3787 -33 781 -150 C ATOM 2306 O THR C 119 -10.501 27.478 17.727 1.00 26.62 O ANISOU 2306 O THR C 119 3716 2723 3675 -40 800 -100 O ATOM 2307 CB THR C 119 -7.152 27.952 18.177 1.00 24.32 C ANISOU 2307 CB THR C 119 3455 2436 3350 29 702 9 C ATOM 2308 OG1 THR C 119 -6.049 27.373 18.855 1.00 24.29 O ANISOU 2308 OG1 THR C 119 3400 2396 3434 70 658 116 O ATOM 2309 CG2 THR C 119 -7.817 28.993 19.082 1.00 24.90 C ANISOU 2309 CG2 THR C 119 3625 2546 3291 25 647 18 C ATOM 2310 N GLU C 120 -9.227 27.574 15.806 1.00 25.88 N ANISOU 2310 N GLU C 120 3621 2744 3469 -37 759 -248 N ATOM 2311 CA GLU C 120 -10.399 27.994 14.998 1.00 25.45 C ANISOU 2311 CA GLU C 120 3528 2824 3319 -60 682 -306 C ATOM 2312 C GLU C 120 -11.503 26.961 15.105 1.00 27.26 C ANISOU 2312 C GLU C 120 3668 2975 3715 -148 647 -421 C ATOM 2313 O GLU C 120 -12.662 27.329 15.341 1.00 28.07 O ANISOU 2313 O GLU C 120 3673 3107 3886 -170 602 -354 O ATOM 2314 CB GLU C 120 -10.066 28.323 13.515 1.00 26.62 C ANISOU 2314 CB GLU C 120 3710 3156 3249 -7 658 -371 C ATOM 2315 CG GLU C 120 -11.300 28.722 12.692 1.00 27.60 C ANISOU 2315 CG GLU C 120 3770 3489 3227 -6 510 -393 C ATOM 2316 CD GLU C 120 -11.968 27.503 12.124 1.00 31.78 C ANISOU 2316 CD GLU C 120 4266 4038 3772 -109 376 -675 C ATOM 2317 OE1 GLU C 120 -11.281 26.666 11.529 1.00 35.14 O ANISOU 2317 OE1 GLU C 120 4797 4431 4124 -112 425 -888 O ATOM 2318 OE2 GLU C 120 -13.171 27.369 12.234 1.00 37.86 O ANISOU 2318 OE2 GLU C 120 4888 4830 4666 -190 232 -704 O ATOM 2319 N ALA C 121 -11.155 25.658 14.999 1.00 28.02 N ANISOU 2319 N ALA C 121 3762 2918 3965 -196 702 -570 N ATOM 2320 CA ALA C 121 -12.193 24.619 15.152 1.00 28.88 C ANISOU 2320 CA ALA C 121 3740 2866 4367 -307 697 -684 C ATOM 2321 C ALA C 121 -12.901 24.636 16.536 1.00 29.57 C ANISOU 2321 C ALA C 121 3745 2822 4668 -286 816 -434 C ATOM 2322 O ALA C 121 -14.076 24.382 16.644 1.00 30.36 O ANISOU 2322 O ALA C 121 3681 2851 5005 -359 808 -429 O ATOM 2323 CB ALA C 121 -11.631 23.214 14.841 1.00 29.38 C ANISOU 2323 CB ALA C 121 3817 2704 4644 -355 802 -891 C ATOM 2324 N LEU C 122 -12.185 24.884 17.616 1.00 30.56 N ANISOU 2324 N LEU C 122 3978 2918 4715 -174 935 -220 N ATOM 2325 CA LEU C 122 -12.836 24.993 18.934 1.00 31.60 C ANISOU 2325 CA LEU C 122 4106 2980 4921 -100 1082 21 C ATOM 2326 C LEU C 122 -13.700 26.243 19.077 1.00 32.41 C ANISOU 2326 C LEU C 122 4211 3206 4899 -70 1060 90 C ATOM 2327 O LEU C 122 -14.814 26.186 19.547 1.00 32.12 O ANISOU 2327 O LEU C 122 4065 3091 5049 -56 1185 211 O ATOM 2328 CB LEU C 122 -11.775 25.018 19.989 1.00 32.05 C ANISOU 2328 CB LEU C 122 4316 3053 4809 28 1143 192 C ATOM 2329 CG LEU C 122 -10.967 23.706 20.117 1.00 33.41 C ANISOU 2329 CG LEU C 122 4446 3067 5181 56 1234 249 C ATOM 2330 CD1 LEU C 122 -9.796 23.837 21.093 1.00 33.59 C ANISOU 2330 CD1 LEU C 122 4579 3185 4997 196 1203 450 C ATOM 2331 CD2 LEU C 122 -11.876 22.586 20.547 1.00 34.81 C ANISOU 2331 CD2 LEU C 122 4489 3003 5734 52 1453 371 C ATOM 2332 N PHE C 123 -13.186 27.376 18.606 1.00 30.46 N ANISOU 2332 N PHE C 123 4056 3117 4401 -49 942 35 N ATOM 2333 CA PHE C 123 -13.875 28.660 18.660 1.00 28.20 C ANISOU 2333 CA PHE C 123 3771 2906 4038 0 959 111 C ATOM 2334 C PHE C 123 -15.134 28.537 17.843 1.00 31.59 C ANISOU 2334 C PHE C 123 3968 3373 4661 -62 892 107 C ATOM 2335 O PHE C 123 -16.204 29.057 18.217 1.00 33.26 O ANISOU 2335 O PHE C 123 4074 3556 5009 -11 996 255 O ATOM 2336 CB PHE C 123 -12.896 29.705 18.049 1.00 25.73 C ANISOU 2336 CB PHE C 123 3552 2702 3522 16 858 57 C ATOM 2337 CG PHE C 123 -13.441 31.080 17.888 1.00 25.86 C ANISOU 2337 CG PHE C 123 3554 2755 3518 75 900 144 C ATOM 2338 CD1 PHE C 123 -13.488 31.960 18.951 1.00 28.36 C ANISOU 2338 CD1 PHE C 123 4004 2970 3802 144 1038 185 C ATOM 2339 CD2 PHE C 123 -13.814 31.531 16.656 1.00 26.45 C ANISOU 2339 CD2 PHE C 123 3501 2965 3584 82 811 182 C ATOM 2340 CE1 PHE C 123 -13.954 33.269 18.774 1.00 30.49 C ANISOU 2340 CE1 PHE C 123 4254 3202 4128 210 1134 263 C ATOM 2341 CE2 PHE C 123 -14.302 32.825 16.466 1.00 28.89 C ANISOU 2341 CE2 PHE C 123 3762 3285 3929 170 887 335 C ATOM 2342 CZ PHE C 123 -14.378 33.698 17.523 1.00 30.12 C ANISOU 2342 CZ PHE C 123 4028 3267 4148 229 1073 375 C ATOM 2343 N ASP C 124 -15.036 27.887 16.704 1.00 30.80 N ANISOU 2343 N ASP C 124 3777 3348 4576 -162 709 -70 N ATOM 2344 CA ASP C 124 -16.146 27.738 15.780 1.00 35.50 C ANISOU 2344 CA ASP C 124 4139 4044 5305 -245 528 -136 C ATOM 2345 C ASP C 124 -16.887 26.415 15.974 1.00 43.20 C ANISOU 2345 C ASP C 124 4914 4823 6677 -382 531 -234 C ATOM 2346 O ASP C 124 -17.583 25.969 15.095 1.00 41.67 O ANISOU 2346 O ASP C 124 4519 4692 6621 -511 301 -409 O ATOM 2347 CB ASP C 124 -15.653 27.796 14.340 1.00 38.78 C ANISOU 2347 CB ASP C 124 4604 4693 5438 -268 296 -330 C ATOM 2348 CG ASP C 124 -15.367 29.192 13.858 1.00 39.23 C ANISOU 2348 CG ASP C 124 4732 4955 5217 -129 286 -157 C ATOM 2349 OD1 ASP C 124 -15.873 30.144 14.425 1.00 37.37 O ANISOU 2349 OD1 ASP C 124 4443 4687 5070 -47 396 70 O ATOM 2350 OD2 ASP C 124 -14.630 29.321 12.894 1.00 39.33 O ANISOU 2350 OD2 ASP C 124 4857 5134 4952 -87 214 -238 O ATOM 2351 N ILE C 125 -16.706 25.821 17.142 1.00 42.82 N ANISOU 2351 N ILE C 125 4917 4539 6814 -346 789 -109 N ATOM 2352 CA ILE C 125 -17.163 24.486 17.437 1.00 47.41 C ANISOU 2352 CA ILE C 125 5323 4851 7840 -453 890 -148 C ATOM 2353 C ILE C 125 -18.415 24.170 16.718 1.00 53.57 C ANISOU 2353 C ILE C 125 5761 5611 8981 -621 695 -268 C ATOM 2354 O ILE C 125 -18.418 23.304 15.896 1.00 64.95 O ANISOU 2354 O ILE C 125 7111 6991 10574 -791 505 -585 O ATOM 2355 CB ILE C 125 -17.384 24.268 18.911 1.00 47.30 C ANISOU 2355 CB ILE C 125 5329 4638 8006 -324 1249 178 C ATOM 2356 CG1 ILE C 125 -17.508 22.784 19.192 1.00 53.73 C ANISOU 2356 CG1 ILE C 125 5990 5128 9297 -406 1415 181 C ATOM 2357 CG2 ILE C 125 -18.627 24.996 19.312 1.00 50.99 C ANISOU 2357 CG2 ILE C 125 5622 5117 8636 -265 1360 403 C ATOM 2358 CD1 ILE C 125 -18.013 21.988 18.015 1.00 53.06 C ANISOU 2358 CD1 ILE C 125 5649 4934 9576 -657 1171 -171 C ATOM 2359 N MET C 126 -19.494 24.861 17.006 1.00 58.41 N ANISOU 2359 N MET C 126 6167 6267 9759 -577 731 -37 N ATOM 2360 CA MET C 126 -20.575 24.769 16.051 1.00 63.16 C ANISOU 2360 CA MET C 126 6409 6960 10628 -741 408 -171 C ATOM 2361 C MET C 126 -21.475 26.008 15.958 1.00 70.21 C ANISOU 2361 C MET C 126 7119 8059 11500 -632 350 99 C ATOM 2362 O MET C 126 -22.215 26.368 16.922 1.00 61.24 O ANISOU 2362 O MET C 126 5842 6766 10660 -517 668 442 O ATOM 2363 CB MET C 126 -21.341 23.476 16.131 1.00 62.91 C ANISOU 2363 CB MET C 126 6034 6608 11261 -951 414 -283 C ATOM 2364 CG MET C 126 -22.237 23.257 17.326 1.00 60.76 C ANISOU 2364 CG MET C 126 5506 6027 11553 -891 814 109 C ATOM 2365 SD MET C 126 -22.754 21.584 16.853 1.00 66.05 S ANISOU 2365 SD MET C 126 5790 6315 12990 -1227 678 -221 S ATOM 2366 CE MET C 126 -21.256 20.700 17.282 1.00 56.44 C ANISOU 2366 CE MET C 126 5000 4890 11555 -1154 954 -332 C ATOM 2367 N SER C 127 -21.388 26.606 14.756 1.00 70.11 N ANISOU 2367 N SER C 127 7115 8394 11131 -641 -24 -40 N ATOM 2368 CA SER C 127 -21.961 27.909 14.428 1.00 72.48 C ANISOU 2368 CA SER C 127 7292 8944 11302 -491 -104 235 C ATOM 2369 C SER C 127 -22.465 27.990 12.981 1.00 76.76 C ANISOU 2369 C SER C 127 7609 9856 11698 -575 -632 87 C ATOM 2370 O SER C 127 -22.342 29.038 12.336 1.00 75.74 O ANISOU 2370 O SER C 127 7544 10036 11198 -412 -746 252 O ATOM 2371 CB SER C 127 -20.935 29.008 14.723 1.00 65.66 C ANISOU 2371 CB SER C 127 6819 8152 9977 -280 126 371 C ATOM 2372 OG SER C 127 -19.653 28.480 15.023 1.00 57.83 O ANISOU 2372 OG SER C 127 6178 7055 8738 -302 241 166 O TER 2373 SER C 127 ATOM 2374 N SER D 106 -5.747 84.502 5.376 1.00 52.51 N ANISOU 2374 N SER D 106 6458 5946 7548 71 -2403 899 N ATOM 2375 CA SER D 106 -4.560 84.711 6.142 1.00 49.96 C ANISOU 2375 CA SER D 106 6271 5595 7116 63 -2102 863 C ATOM 2376 C SER D 106 -4.902 85.834 7.046 1.00 49.85 C ANISOU 2376 C SER D 106 6130 5479 7332 174 -1962 941 C ATOM 2377 O SER D 106 -4.320 86.892 6.975 1.00 49.83 O ANISOU 2377 O SER D 106 6238 5398 7298 230 -1918 1018 O ATOM 2378 CB SER D 106 -3.404 85.070 5.214 1.00 39.96 C ANISOU 2378 CB SER D 106 5262 4440 5480 49 -2100 901 C ATOM 2379 OG SER D 106 -3.568 86.399 4.768 1.00 41.50 O ANISOU 2379 OG SER D 106 5476 4597 5696 109 -2181 1145 O ATOM 2380 N GLY D 107 -5.887 85.616 7.891 1.00 73.41 N ANISOU 2380 N GLY D 107 8842 8472 10578 213 -1910 914 N ATOM 2381 CA GLY D 107 -6.312 86.669 8.790 1.00 81.41 C ANISOU 2381 CA GLY D 107 9682 9448 11802 382 -1781 888 C ATOM 2382 C GLY D 107 -5.474 86.805 10.046 1.00 77.91 C ANISOU 2382 C GLY D 107 9269 9054 11280 418 -1481 751 C ATOM 2383 O GLY D 107 -4.550 87.592 10.113 1.00 74.32 O ANISOU 2383 O GLY D 107 8991 8484 10763 461 -1431 701 O ATOM 2384 N THR D 108 -5.836 86.048 11.058 1.00 69.68 N ANISOU 2384 N THR D 108 8020 8203 10252 392 -1301 722 N ATOM 2385 CA THR D 108 -5.059 86.005 12.238 1.00 61.00 C ANISOU 2385 CA THR D 108 6942 7233 9003 415 -1043 616 C ATOM 2386 C THR D 108 -3.821 85.271 11.831 1.00 57.58 C ANISOU 2386 C THR D 108 6795 6715 8369 247 -1052 647 C ATOM 2387 O THR D 108 -2.856 85.245 12.548 1.00 53.08 O ANISOU 2387 O THR D 108 6322 6193 7651 242 -894 571 O ATOM 2388 CB THR D 108 -5.763 85.231 13.325 1.00 64.13 C ANISOU 2388 CB THR D 108 7022 7935 9409 391 -861 690 C ATOM 2389 OG1 THR D 108 -6.871 85.983 13.767 1.00 71.17 O ANISOU 2389 OG1 THR D 108 7600 8984 10457 593 -809 609 O ATOM 2390 CG2 THR D 108 -4.890 85.103 14.473 1.00 61.85 C ANISOU 2390 CG2 THR D 108 6776 7835 8890 405 -627 618 C ATOM 2391 N MET D 109 -3.873 84.669 10.663 1.00 53.57 N ANISOU 2391 N MET D 109 6395 6108 7852 133 -1256 723 N ATOM 2392 CA MET D 109 -2.745 83.874 10.156 1.00 53.23 C ANISOU 2392 CA MET D 109 6584 6018 7622 12 -1281 686 C ATOM 2393 C MET D 109 -1.591 84.828 9.805 1.00 50.59 C ANISOU 2393 C MET D 109 6480 5628 7115 55 -1225 645 C ATOM 2394 O MET D 109 -0.399 84.563 10.054 1.00 42.29 O ANISOU 2394 O MET D 109 5563 4589 5918 10 -1107 582 O ATOM 2395 CB MET D 109 -3.167 83.132 8.890 1.00 51.46 C ANISOU 2395 CB MET D 109 6395 5753 7404 -62 -1550 685 C ATOM 2396 CG MET D 109 -2.479 81.820 8.571 1.00 51.64 C ANISOU 2396 CG MET D 109 6515 5738 7368 -163 -1628 571 C ATOM 2397 SD MET D 109 -2.360 80.682 9.998 1.00 54.07 S ANISOU 2397 SD MET D 109 6655 6001 7886 -270 -1493 654 S ATOM 2398 CE MET D 109 -2.973 79.073 9.467 1.00 51.90 C ANISOU 2398 CE MET D 109 6248 5534 7938 -412 -1826 627 C ATOM 2399 N GLU D 110 -1.956 85.938 9.192 1.00 48.67 N ANISOU 2399 N GLU D 110 6250 5309 6932 130 -1336 720 N ATOM 2400 CA GLU D 110 -0.981 86.924 8.809 1.00 49.31 C ANISOU 2400 CA GLU D 110 6492 5304 6937 133 -1323 781 C ATOM 2401 C GLU D 110 -0.376 87.529 10.069 1.00 46.53 C ANISOU 2401 C GLU D 110 6115 4879 6687 197 -1148 647 C ATOM 2402 O GLU D 110 0.791 87.886 10.099 1.00 43.61 O ANISOU 2402 O GLU D 110 5867 4457 6247 145 -1082 646 O ATOM 2403 CB GLU D 110 -1.616 88.006 7.932 1.00 57.34 C ANISOU 2403 CB GLU D 110 7491 6211 8085 190 -1534 971 C ATOM 2404 CG GLU D 110 -0.636 88.608 6.906 1.00 73.68 C ANISOU 2404 CG GLU D 110 9730 8285 9979 100 -1592 1197 C ATOM 2405 CD GLU D 110 0.610 87.722 6.571 1.00 82.35 C ANISOU 2405 CD GLU D 110 10971 9600 10717 -15 -1445 1136 C ATOM 2406 OE1 GLU D 110 0.451 86.503 6.246 1.00 87.66 O ANISOU 2406 OE1 GLU D 110 11662 10446 11200 -33 -1464 986 O ATOM 2407 OE2 GLU D 110 1.769 88.252 6.628 1.00 76.11 O ANISOU 2407 OE2 GLU D 110 10248 8786 9884 -81 -1333 1221 O ATOM 2408 N ASN D 111 -1.183 87.617 11.113 1.00 44.59 N ANISOU 2408 N ASN D 111 5677 4679 6586 316 -1077 520 N ATOM 2409 CA ASN D 111 -0.725 88.092 12.362 1.00 42.31 C ANISOU 2409 CA ASN D 111 5339 4415 6324 414 -930 320 C ATOM 2410 C ASN D 111 0.278 87.133 13.027 1.00 39.22 C ANISOU 2410 C ASN D 111 5026 4179 5698 311 -766 277 C ATOM 2411 O ASN D 111 1.340 87.567 13.502 1.00 33.31 O ANISOU 2411 O ASN D 111 4366 3383 4909 314 -712 165 O ATOM 2412 CB ASN D 111 -1.890 88.387 13.268 1.00 47.33 C ANISOU 2412 CB ASN D 111 5707 5185 7090 601 -875 173 C ATOM 2413 CG ASN D 111 -1.497 89.304 14.404 1.00 63.42 C ANISOU 2413 CG ASN D 111 7685 7234 9176 784 -799 -134 C ATOM 2414 OD1 ASN D 111 -0.607 90.184 14.261 1.00 70.40 O ANISOU 2414 OD1 ASN D 111 8710 7852 10187 790 -898 -218 O ATOM 2415 ND2 ASN D 111 -2.144 89.113 15.562 1.00 73.83 N ANISOU 2415 ND2 ASN D 111 8765 8892 10394 935 -634 -310 N ATOM 2416 N LEU D 112 -0.045 85.839 13.015 1.00 36.19 N ANISOU 2416 N LEU D 112 4594 3937 5221 212 -735 380 N ATOM 2417 CA LEU D 112 0.857 84.823 13.536 1.00 35.00 C ANISOU 2417 CA LEU D 112 4501 3878 4919 113 -640 391 C ATOM 2418 C LEU D 112 2.182 84.851 12.758 1.00 33.47 C ANISOU 2418 C LEU D 112 4525 3558 4632 37 -673 368 C ATOM 2419 O LEU D 112 3.244 84.812 13.359 1.00 31.73 O ANISOU 2419 O LEU D 112 4361 3365 4330 24 -587 299 O ATOM 2420 CB LEU D 112 0.246 83.443 13.430 1.00 32.36 C ANISOU 2420 CB LEU D 112 4064 3598 4633 2 -690 540 C ATOM 2421 CG LEU D 112 1.085 82.253 13.872 1.00 33.77 C ANISOU 2421 CG LEU D 112 4278 3791 4762 -102 -664 598 C ATOM 2422 CD1 LEU D 112 1.551 82.476 15.290 1.00 33.44 C ANISOU 2422 CD1 LEU D 112 4169 3957 4579 -49 -492 592 C ATOM 2423 CD2 LEU D 112 0.305 80.958 13.758 1.00 34.62 C ANISOU 2423 CD2 LEU D 112 4237 3857 5062 -223 -787 773 C ATOM 2424 N SER D 113 2.105 84.910 11.436 1.00 32.63 N ANISOU 2424 N SER D 113 4510 3376 4512 -6 -796 435 N ATOM 2425 CA SER D 113 3.285 84.905 10.580 1.00 32.10 C ANISOU 2425 CA SER D 113 4594 3307 4296 -69 -796 440 C ATOM 2426 C SER D 113 4.191 86.079 11.010 1.00 30.78 C ANISOU 2426 C SER D 113 4460 3057 4176 -62 -723 436 C ATOM 2427 O SER D 113 5.387 85.926 11.233 1.00 28.79 O ANISOU 2427 O SER D 113 4252 2834 3853 -108 -639 388 O ATOM 2428 CB SER D 113 2.822 85.129 9.130 1.00 36.97 C ANISOU 2428 CB SER D 113 5262 3955 4830 -84 -944 550 C ATOM 2429 OG SER D 113 3.937 85.160 8.269 1.00 40.00 O ANISOU 2429 OG SER D 113 5745 4456 4997 -135 -907 581 O ATOM 2430 N ARG D 114 3.615 87.269 11.107 1.00 30.79 N ANISOU 2430 N ARG D 114 4415 2921 4363 2 -792 472 N ATOM 2431 CA ARG D 114 4.340 88.415 11.581 1.00 33.23 C ANISOU 2431 CA ARG D 114 4723 3064 4839 14 -798 429 C ATOM 2432 C ARG D 114 5.022 88.139 12.946 1.00 31.61 C ANISOU 2432 C ARG D 114 4487 2932 4592 54 -685 198 C ATOM 2433 O ARG D 114 6.177 88.473 13.119 1.00 33.90 O ANISOU 2433 O ARG D 114 4809 3160 4910 -9 -670 167 O ATOM 2434 CB ARG D 114 3.396 89.632 11.663 1.00 39.10 C ANISOU 2434 CB ARG D 114 5380 3591 5886 134 -944 420 C ATOM 2435 CG ARG D 114 4.001 90.789 12.451 1.00 52.27 C ANISOU 2435 CG ARG D 114 7007 5021 7833 192 -1008 249 C ATOM 2436 CD ARG D 114 2.977 91.888 12.847 1.00 62.60 C ANISOU 2436 CD ARG D 114 8184 6099 9503 395 -1172 83 C ATOM 2437 NE ARG D 114 3.534 93.267 12.871 1.00 75.98 N ANISOU 2437 NE ARG D 114 9855 7379 11637 401 -1384 54 N ATOM 2438 CZ ARG D 114 4.481 93.764 13.688 1.00 73.41 C ANISOU 2438 CZ ARG D 114 9514 6914 11464 407 -1425 -195 C ATOM 2439 NH1 ARG D 114 5.045 93.007 14.595 1.00 71.52 N ANISOU 2439 NH1 ARG D 114 9295 6970 10909 419 -1248 -431 N ATOM 2440 NH2 ARG D 114 4.859 95.054 13.592 1.00 76.82 N ANISOU 2440 NH2 ARG D 114 9892 6877 12418 394 -1691 -192 N ATOM 2441 N ARG D 115 4.315 87.551 13.920 1.00 29.83 N ANISOU 2441 N ARG D 115 4169 2875 4290 149 -615 70 N ATOM 2442 CA ARG D 115 4.915 87.295 15.242 1.00 31.00 C ANISOU 2442 CA ARG D 115 4274 3180 4323 196 -525 -105 C ATOM 2443 C ARG D 115 6.011 86.220 15.189 1.00 30.06 C ANISOU 2443 C ARG D 115 4231 3140 4050 74 -467 -24 C ATOM 2444 O ARG D 115 7.019 86.281 15.952 1.00 29.42 O ANISOU 2444 O ARG D 115 4153 3107 3918 74 -448 -135 O ATOM 2445 CB ARG D 115 3.857 86.904 16.256 1.00 31.01 C ANISOU 2445 CB ARG D 115 4115 3448 4220 315 -442 -170 C ATOM 2446 CG ARG D 115 2.816 87.995 16.398 1.00 31.10 C ANISOU 2446 CG ARG D 115 4005 3411 4402 493 -494 -332 C ATOM 2447 CD ARG D 115 1.784 87.623 17.428 1.00 34.56 C ANISOU 2447 CD ARG D 115 4219 4226 4685 626 -363 -397 C ATOM 2448 NE ARG D 115 1.113 88.847 17.813 1.00 37.64 N ANISOU 2448 NE ARG D 115 4472 4593 5236 869 -414 -705 N ATOM 2449 CZ ARG D 115 0.397 89.019 18.916 1.00 40.78 C ANISOU 2449 CZ ARG D 115 4635 5377 5482 1085 -296 -935 C ATOM 2450 NH1 ARG D 115 0.203 87.988 19.738 1.00 42.08 N ANISOU 2450 NH1 ARG D 115 4668 6019 5299 1041 -103 -776 N ATOM 2451 NH2 ARG D 115 -0.081 90.234 19.196 1.00 43.96 N ANISOU 2451 NH2 ARG D 115 4914 5695 6092 1352 -387 -1320 N ATOM 2452 N LEU D 116 5.871 85.259 14.290 1.00 26.55 N ANISOU 2452 N LEU D 116 3831 2698 3558 -10 -476 125 N ATOM 2453 CA LEU D 116 6.897 84.200 14.194 1.00 26.71 C ANISOU 2453 CA LEU D 116 3895 2759 3496 -80 -453 143 C ATOM 2454 C LEU D 116 8.207 84.799 13.608 1.00 27.94 C ANISOU 2454 C LEU D 116 4110 2851 3654 -134 -436 115 C ATOM 2455 O LEU D 116 9.350 84.355 13.977 1.00 27.59 O ANISOU 2455 O LEU D 116 4054 2850 3580 -156 -404 62 O ATOM 2456 CB LEU D 116 6.420 83.021 13.340 1.00 26.61 C ANISOU 2456 CB LEU D 116 3892 2734 3485 -119 -517 214 C ATOM 2457 CG LEU D 116 5.199 82.251 13.825 1.00 26.64 C ANISOU 2457 CG LEU D 116 3785 2771 3566 -123 -560 315 C ATOM 2458 CD1 LEU D 116 4.642 81.344 12.688 1.00 26.01 C ANISOU 2458 CD1 LEU D 116 3716 2596 3570 -165 -705 325 C ATOM 2459 CD2 LEU D 116 5.489 81.452 15.093 1.00 24.51 C ANISOU 2459 CD2 LEU D 116 3424 2598 3290 -140 -524 402 C ATOM 2460 N LYS D 117 8.059 85.790 12.723 1.00 25.85 N ANISOU 2460 N LYS D 117 3875 2497 3449 -165 -469 198 N ATOM 2461 CA LYS D 117 9.231 86.438 12.211 1.00 27.50 C ANISOU 2461 CA LYS D 117 4082 2675 3690 -253 -446 266 C ATOM 2462 C LYS D 117 9.910 87.310 13.262 1.00 28.10 C ANISOU 2462 C LYS D 117 4106 2626 3946 -256 -479 154 C ATOM 2463 O LYS D 117 11.117 87.377 13.264 1.00 27.13 O ANISOU 2463 O LYS D 117 3939 2517 3852 -333 -449 161 O ATOM 2464 CB LYS D 117 8.898 87.276 11.030 1.00 27.84 C ANISOU 2464 CB LYS D 117 4142 2672 3764 -314 -496 485 C ATOM 2465 CG LYS D 117 8.239 86.422 9.981 1.00 29.74 C ANISOU 2465 CG LYS D 117 4431 3087 3782 -291 -503 537 C ATOM 2466 CD LYS D 117 7.875 87.266 8.770 1.00 34.73 C ANISOU 2466 CD LYS D 117 5074 3748 4375 -349 -575 810 C ATOM 2467 CE LYS D 117 7.343 86.269 7.739 1.00 34.10 C ANISOU 2467 CE LYS D 117 5037 3915 4005 -303 -605 771 C ATOM 2468 NZ LYS D 117 7.133 86.894 6.391 1.00 39.07 N ANISOU 2468 NZ LYS D 117 5672 4724 4447 -354 -671 1061 N ATOM 2469 N VAL D 118 9.128 87.996 14.114 1.00 26.28 N ANISOU 2469 N VAL D 118 3852 2290 3843 -155 -556 14 N ATOM 2470 CA VAL D 118 9.677 88.739 15.234 1.00 27.07 C ANISOU 2470 CA VAL D 118 3895 2304 4087 -107 -633 -213 C ATOM 2471 C VAL D 118 10.454 87.764 16.147 1.00 27.55 C ANISOU 2471 C VAL D 118 3939 2585 3942 -92 -569 -323 C ATOM 2472 O VAL D 118 11.543 88.090 16.620 1.00 30.75 O ANISOU 2472 O VAL D 118 4300 2953 4431 -132 -627 -426 O ATOM 2473 CB VAL D 118 8.592 89.454 16.063 1.00 27.13 C ANISOU 2473 CB VAL D 118 3852 2266 4189 73 -715 -448 C ATOM 2474 CG1 VAL D 118 9.147 89.778 17.433 1.00 28.50 C ANISOU 2474 CG1 VAL D 118 3963 2519 4346 176 -779 -787 C ATOM 2475 CG2 VAL D 118 8.181 90.718 15.374 1.00 29.31 C ANISOU 2475 CG2 VAL D 118 4110 2205 4820 69 -869 -384 C ATOM 2476 N THR D 119 9.903 86.568 16.335 1.00 25.88 N ANISOU 2476 N THR D 119 3743 2574 3515 -52 -484 -259 N ATOM 2477 CA THR D 119 10.446 85.612 17.232 1.00 26.27 C ANISOU 2477 CA THR D 119 3762 2814 3407 -32 -463 -284 C ATOM 2478 C THR D 119 11.727 85.054 16.618 1.00 26.95 C ANISOU 2478 C THR D 119 3852 2856 3533 -127 -450 -214 C ATOM 2479 O THR D 119 12.778 84.902 17.338 1.00 26.39 O ANISOU 2479 O THR D 119 3726 2845 3456 -128 -493 -290 O ATOM 2480 CB THR D 119 9.453 84.468 17.541 1.00 25.24 C ANISOU 2480 CB THR D 119 3606 2853 3132 1 -413 -144 C ATOM 2481 OG1 THR D 119 8.346 84.980 18.288 1.00 26.93 O ANISOU 2481 OG1 THR D 119 3749 3217 3265 109 -389 -220 O ATOM 2482 CG2 THR D 119 10.183 83.398 18.357 1.00 25.55 C ANISOU 2482 CG2 THR D 119 3601 3040 3066 -9 -433 -67 C ATOM 2483 N GLU D 120 11.671 84.753 15.322 1.00 23.89 N ANISOU 2483 N GLU D 120 3500 2412 3165 -184 -400 -97 N ATOM 2484 CA GLU D 120 12.912 84.382 14.607 1.00 25.51 C ANISOU 2484 CA GLU D 120 3661 2646 3384 -240 -355 -77 C ATOM 2485 C GLU D 120 13.991 85.441 14.759 1.00 27.16 C ANISOU 2485 C GLU D 120 3788 2797 3736 -323 -371 -95 C ATOM 2486 O GLU D 120 15.153 85.098 15.020 1.00 28.80 O ANISOU 2486 O GLU D 120 3900 3064 3979 -339 -369 -142 O ATOM 2487 CB GLU D 120 12.656 84.030 13.125 1.00 25.91 C ANISOU 2487 CB GLU D 120 3741 2752 3350 -257 -293 3 C ATOM 2488 CG GLU D 120 13.872 83.574 12.402 1.00 26.29 C ANISOU 2488 CG GLU D 120 3698 2940 3351 -265 -214 -29 C ATOM 2489 CD GLU D 120 14.592 84.782 11.819 1.00 32.53 C ANISOU 2489 CD GLU D 120 4403 3777 4180 -392 -141 125 C ATOM 2490 OE1 GLU D 120 13.939 85.591 11.077 1.00 32.49 O ANISOU 2490 OE1 GLU D 120 4442 3755 4147 -458 -140 305 O ATOM 2491 OE2 GLU D 120 15.804 84.901 12.076 1.00 32.97 O ANISOU 2491 OE2 GLU D 120 4321 3880 4326 -437 -104 109 O ATOM 2492 N ALA D 121 13.660 86.731 14.660 1.00 29.05 N ANISOU 2492 N ALA D 121 4031 2879 4126 -377 -428 -59 N ATOM 2493 CA ALA D 121 14.718 87.726 14.749 1.00 27.92 C ANISOU 2493 CA ALA D 121 3773 2610 4223 -492 -494 -44 C ATOM 2494 C ALA D 121 15.295 87.678 16.177 1.00 29.90 C ANISOU 2494 C ALA D 121 3978 2872 4512 -428 -611 -297 C ATOM 2495 O ALA D 121 16.454 87.961 16.364 1.00 31.07 O ANISOU 2495 O ALA D 121 4000 2988 4818 -512 -667 -321 O ATOM 2496 CB ALA D 121 14.241 89.154 14.373 1.00 30.21 C ANISOU 2496 CB ALA D 121 4057 2632 4790 -568 -606 63 C ATOM 2497 N LEU D 122 14.496 87.434 17.214 1.00 28.44 N ANISOU 2497 N LEU D 122 3861 2768 4176 -282 -663 -476 N ATOM 2498 CA LEU D 122 15.102 87.418 18.576 1.00 29.04 C ANISOU 2498 CA LEU D 122 3879 2953 4202 -211 -791 -708 C ATOM 2499 C LEU D 122 15.983 86.178 18.764 1.00 31.02 C ANISOU 2499 C LEU D 122 4082 3382 4322 -216 -751 -620 C ATOM 2500 O LEU D 122 17.049 86.228 19.357 1.00 33.98 O ANISOU 2500 O LEU D 122 4357 3792 4762 -234 -862 -716 O ATOM 2501 CB LEU D 122 14.011 87.425 19.666 1.00 30.60 C ANISOU 2501 CB LEU D 122 4121 3333 4171 -36 -824 -893 C ATOM 2502 CG LEU D 122 13.148 88.685 19.667 1.00 32.54 C ANISOU 2502 CG LEU D 122 4375 3399 4591 38 -904 -1086 C ATOM 2503 CD1 LEU D 122 12.158 88.642 20.803 1.00 35.79 C ANISOU 2503 CD1 LEU D 122 4769 4111 4718 249 -901 -1317 C ATOM 2504 CD2 LEU D 122 14.025 89.912 19.881 1.00 36.84 C ANISOU 2504 CD2 LEU D 122 4838 3667 5494 -11 -1128 -1315 C ATOM 2505 N PHE D 123 15.526 85.047 18.265 1.00 29.41 N ANISOU 2505 N PHE D 123 3932 3260 3982 -190 -634 -453 N ATOM 2506 CA PHE D 123 16.206 83.770 18.414 1.00 29.86 C ANISOU 2506 CA PHE D 123 3936 3416 3994 -161 -641 -376 C ATOM 2507 C PHE D 123 17.528 83.845 17.658 1.00 31.99 C ANISOU 2507 C PHE D 123 4078 3636 4441 -234 -607 -381 C ATOM 2508 O PHE D 123 18.538 83.264 18.080 1.00 35.31 O ANISOU 2508 O PHE D 123 4383 4116 4917 -204 -678 -408 O ATOM 2509 CB PHE D 123 15.238 82.706 17.820 1.00 26.16 C ANISOU 2509 CB PHE D 123 3543 2941 3454 -125 -567 -234 C ATOM 2510 CG PHE D 123 15.818 81.310 17.642 1.00 27.37 C ANISOU 2510 CG PHE D 123 3636 3081 3682 -80 -609 -173 C ATOM 2511 CD1 PHE D 123 15.887 80.410 18.728 1.00 26.67 C ANISOU 2511 CD1 PHE D 123 3505 3054 3573 -32 -739 -57 C ATOM 2512 CD2 PHE D 123 16.203 80.866 16.371 1.00 26.95 C ANISOU 2512 CD2 PHE D 123 3551 2970 3720 -67 -537 -228 C ATOM 2513 CE1 PHE D 123 16.365 79.114 18.566 1.00 29.55 C ANISOU 2513 CE1 PHE D 123 3799 3315 4115 22 -839 10 C ATOM 2514 CE2 PHE D 123 16.714 79.561 16.203 1.00 29.75 C ANISOU 2514 CE2 PHE D 123 3826 3267 4210 25 -618 -262 C ATOM 2515 CZ PHE D 123 16.799 78.702 17.303 1.00 31.23 C ANISOU 2515 CZ PHE D 123 3974 3408 4483 66 -788 -139 C ATOM 2516 N ASP D 124 17.539 84.564 16.558 1.00 31.71 N ANISOU 2516 N ASP D 124 4029 3529 4492 -327 -502 -320 N ATOM 2517 CA ASP D 124 18.706 84.681 15.728 1.00 32.29 C ANISOU 2517 CA ASP D 124 3931 3654 4686 -410 -416 -263 C ATOM 2518 C ASP D 124 19.493 85.990 15.900 1.00 37.05 C ANISOU 2518 C ASP D 124 4392 4147 5539 -566 -492 -240 C ATOM 2519 O ASP D 124 20.303 86.289 15.083 1.00 39.47 O ANISOU 2519 O ASP D 124 4523 4517 5955 -681 -392 -100 O ATOM 2520 CB ASP D 124 18.344 84.529 14.263 1.00 30.69 C ANISOU 2520 CB ASP D 124 3745 3547 4370 -429 -240 -139 C ATOM 2521 CG ASP D 124 18.038 83.092 13.847 1.00 32.65 C ANISOU 2521 CG ASP D 124 4041 3895 4471 -275 -198 -232 C ATOM 2522 OD1 ASP D 124 18.544 82.162 14.444 1.00 30.91 O ANISOU 2522 OD1 ASP D 124 3763 3670 4311 -176 -276 -337 O ATOM 2523 OD2 ASP D 124 17.300 82.923 12.881 1.00 30.38 O ANISOU 2523 OD2 ASP D 124 3833 3669 4040 -253 -123 -200 O ATOM 2524 N ILE D 125 19.250 86.758 16.947 1.00 37.88 N ANISOU 2524 N ILE D 125 4543 4105 5745 -566 -681 -384 N ATOM 2525 CA ILE D 125 20.049 87.948 17.202 1.00 41.93 C ANISOU 2525 CA ILE D 125 4899 4438 6596 -711 -838 -420 C ATOM 2526 C ILE D 125 21.524 87.582 17.212 1.00 49.12 C ANISOU 2526 C ILE D 125 5565 5462 7637 -778 -838 -393 C ATOM 2527 O ILE D 125 21.967 86.764 17.983 1.00 47.04 O ANISOU 2527 O ILE D 125 5277 5331 7263 -663 -911 -530 O ATOM 2528 CB ILE D 125 19.722 88.605 18.539 1.00 45.03 C ANISOU 2528 CB ILE D 125 5353 4712 7045 -627 -1098 -732 C ATOM 2529 CG1 ILE D 125 20.523 89.875 18.707 1.00 47.53 C ANISOU 2529 CG1 ILE D 125 5491 4752 7818 -786 -1326 -810 C ATOM 2530 CG2 ILE D 125 20.097 87.704 19.689 1.00 43.54 C ANISOU 2530 CG2 ILE D 125 5164 4762 6617 -485 -1188 -909 C ATOM 2531 CD1 ILE D 125 20.349 90.818 17.559 1.00 53.77 C ANISOU 2531 CD1 ILE D 125 6222 5281 8928 -978 -1278 -515 C ATOM 2532 N MET D 126 22.268 88.180 16.312 1.00 52.21 N ANISOU 2532 N MET D 126 5744 5827 8268 -970 -755 -166 N ATOM 2533 CA MET D 126 23.680 87.964 16.272 1.00 60.27 C ANISOU 2533 CA MET D 126 6464 6977 9460 -1048 -742 -124 C ATOM 2534 C MET D 126 23.991 86.481 16.157 1.00 62.39 C ANISOU 2534 C MET D 126 6715 7531 9459 -854 -594 -201 C ATOM 2535 O MET D 126 24.470 85.881 17.099 1.00 58.16 O ANISOU 2535 O MET D 126 6146 7024 8928 -741 -749 -381 O ATOM 2536 CB MET D 126 24.331 88.541 17.536 1.00 62.35 C ANISOU 2536 CB MET D 126 6625 7057 10006 -1087 -1074 -358 C ATOM 2537 CG MET D 126 25.650 89.240 17.270 1.00 68.08 C ANISOU 2537 CG MET D 126 6974 7720 11174 -1326 -1140 -204 C ATOM 2538 SD MET D 126 25.303 90.889 16.708 1.00 72.87 S ANISOU 2538 SD MET D 126 7524 7933 12232 -1608 -1253 46 S ATOM 2539 CE MET D 126 24.238 91.346 18.056 1.00 61.64 C ANISOU 2539 CE MET D 126 6423 6221 10778 -1413 -1598 -444 C ATOM 2540 N SER D 127 23.722 85.894 14.997 1.00 63.74 N ANISOU 2540 N SER D 127 6896 7908 9413 -801 -332 -79 N ATOM 2541 CA SER D 127 24.104 84.495 14.845 1.00 61.77 C ANISOU 2541 CA SER D 127 6587 7869 9014 -591 -245 -221 C ATOM 2542 C SER D 127 24.804 84.256 13.512 1.00 68.22 C ANISOU 2542 C SER D 127 7139 9025 9756 -592 36 -124 C ATOM 2543 O SER D 127 25.456 85.150 12.973 1.00 77.81 O ANISOU 2543 O SER D 127 8106 10357 11099 -796 145 109 O ATOM 2544 CB SER D 127 22.877 83.589 14.965 1.00 58.37 C ANISOU 2544 CB SER D 127 6462 7376 8338 -412 -267 -327 C ATOM 2545 OG SER D 127 22.528 83.380 16.322 1.00 68.71 O ANISOU 2545 OG SER D 127 7916 8528 9661 -350 -499 -423 O TER 2546 SER D 127 HETATM 2547 S SO4 A 201 2.999 23.147 24.183 1.00 56.15 S HETATM 2548 O1 SO4 A 201 3.479 22.271 23.099 1.00 49.56 O HETATM 2549 O2 SO4 A 201 2.736 24.429 23.488 1.00 62.64 O HETATM 2550 O3 SO4 A 201 1.774 22.615 24.843 1.00 53.47 O HETATM 2551 O4 SO4 A 201 3.989 23.355 25.246 1.00 53.19 O HETATM 2552 S SO4 B 201 -0.918 89.417 22.923 1.00 58.08 S HETATM 2553 O1 SO4 B 201 -1.880 89.330 24.022 1.00 55.36 O HETATM 2554 O2 SO4 B 201 -0.644 88.036 22.447 1.00 68.90 O HETATM 2555 O3 SO4 B 201 -1.470 90.137 21.746 1.00 48.76 O HETATM 2556 O4 SO4 B 201 0.342 90.055 23.422 1.00 58.56 O HETATM 2557 S SO4 B 202 27.610 70.673 3.100 1.00117.78 S HETATM 2558 O1 SO4 B 202 28.823 69.861 2.843 1.00130.35 O HETATM 2559 O2 SO4 B 202 27.241 71.386 1.851 1.00127.53 O HETATM 2560 O3 SO4 B 202 26.525 69.759 3.514 1.00111.15 O HETATM 2561 O4 SO4 B 202 27.851 71.660 4.185 1.00123.02 O HETATM 2562 S SO4 B 203 17.890 77.549 -2.221 1.00118.73 S HETATM 2563 O1 SO4 B 203 18.720 78.787 -2.117 1.00104.59 O HETATM 2564 O2 SO4 B 203 17.538 77.222 -3.638 1.00 90.74 O HETATM 2565 O3 SO4 B 203 18.665 76.427 -1.658 1.00102.73 O HETATM 2566 O4 SO4 B 203 16.664 77.679 -1.377 1.00120.55 O HETATM 2567 O HOH A 301 -5.878 43.153 24.075 1.00 47.64 O HETATM 2568 O HOH A 302 -5.635 53.256 7.499 1.00 43.67 O HETATM 2569 O HOH A 303 -8.263 21.597 12.445 0.01 28.45 O HETATM 2570 O HOH A 304 -4.978 49.964 6.571 1.00 42.74 O HETATM 2571 O HOH A 305 -7.791 35.628 26.139 1.00 38.11 O HETATM 2572 O HOH A 306 -12.696 45.650 23.757 1.00 46.22 O HETATM 2573 O HOH A 307 3.069 47.947 20.104 1.00 45.10 O HETATM 2574 O HOH A 308 -0.472 29.247 25.623 1.00 44.80 O HETATM 2575 O HOH A 309 -18.652 49.399 3.329 1.00 48.67 O HETATM 2576 O HOH A 310 -8.173 54.165 11.147 1.00 36.47 O HETATM 2577 O HOH A 311 -17.920 59.781 16.779 1.00 55.98 O HETATM 2578 O HOH A 312 -12.858 43.025 24.738 1.00 40.74 O HETATM 2579 O HOH A 313 -5.678 37.461 25.148 1.00 33.67 O HETATM 2580 O HOH A 314 -3.891 37.025 26.513 1.00 50.42 O HETATM 2581 O HOH A 315 -1.077 39.430 22.571 1.00 31.11 O HETATM 2582 O HOH A 316 -2.312 34.613 26.050 1.00 47.74 O HETATM 2583 O HOH A 317 8.070 33.257 23.128 1.00 67.02 O HETATM 2584 O HOH A 318 0.105 33.318 21.980 1.00 37.74 O HETATM 2585 O HOH A 319 1.025 31.783 27.098 1.00 57.20 O HETATM 2586 O HOH A 320 -1.838 28.612 28.289 1.00 47.84 O HETATM 2587 O HOH A 321 -12.650 36.450 26.122 1.00 40.54 O HETATM 2588 O HOH A 322 -6.388 33.518 27.371 1.00 40.88 O HETATM 2589 O HOH A 323 8.863 48.094 15.480 1.00 56.51 O HETATM 2590 O HOH A 324 -9.899 24.134 11.463 1.00 41.73 O HETATM 2591 O HOH A 325 1.144 20.757 26.113 1.00 40.51 O HETATM 2592 O HOH A 326 -6.654 55.057 8.963 1.00 45.39 O HETATM 2593 O HOH A 327 -5.689 56.493 11.392 1.00 44.79 O HETATM 2594 O HOH A 328 -13.393 49.316 -1.705 1.00 57.64 O HETATM 2595 O HOH A 329 -19.685 48.696 10.505 1.00 52.64 O HETATM 2596 O HOH A 330 -16.565 30.375 21.374 0.50 49.34 O HETATM 2597 O HOH A 331 -6.711 45.558 24.133 1.00 58.88 O HETATM 2598 O HOH A 332 -0.121 38.214 24.854 1.00 52.82 O HETATM 2599 O HOH A 333 4.791 45.459 4.705 1.00 57.15 O HETATM 2600 O HOH A 334 7.265 34.147 17.770 1.00 54.64 O HETATM 2601 O HOH A 335 -17.745 37.177 12.744 1.00 63.69 O HETATM 2602 O HOH A 336 -19.025 38.954 12.017 1.00 59.96 O HETATM 2603 O HOH A 337 -19.458 33.046 9.132 1.00 45.53 O HETATM 2604 O HOH A 338 -17.599 32.204 7.681 1.00 57.05 O HETATM 2605 O HOH A 339 -18.361 30.924 10.316 1.00 62.58 O HETATM 2606 O HOH A 340 -8.193 56.306 25.774 1.00 56.63 O HETATM 2607 O HOH A 341 -16.901 42.521 5.560 1.00 50.87 O HETATM 2608 O HOH A 342 -15.011 47.602 -1.994 1.00 66.24 O HETATM 2609 O HOH A 343 -10.037 56.147 12.910 1.00 63.07 O HETATM 2610 O HOH A 344 -19.068 37.907 14.564 1.00 59.03 O HETATM 2611 O HOH B 301 25.572 60.625 8.111 1.00 61.64 O HETATM 2612 O HOH B 302 19.465 70.300 -1.754 1.00 66.29 O HETATM 2613 O HOH B 303 19.953 52.702 16.373 1.00 57.71 O HETATM 2614 O HOH B 304 22.441 67.025 14.527 1.00 56.64 O HETATM 2615 O HOH B 305 9.899 76.766 25.569 1.00 32.53 O HETATM 2616 O HOH B 306 7.904 75.018 24.583 1.00 33.94 O HETATM 2617 O HOH B 307 0.727 80.989 26.091 1.00 50.68 O HETATM 2618 O HOH B 308 2.462 80.045 23.585 1.00 40.96 O HETATM 2619 O HOH B 309 1.933 79.167 21.139 1.00 31.98 O HETATM 2620 O HOH B 310 14.753 75.388 25.789 1.00 59.13 O HETATM 2621 O HOH B 311 8.235 79.000 27.226 1.00 50.13 O HETATM 2622 O HOH B 312 9.391 82.382 28.105 1.00 53.54 O HETATM 2623 O HOH B 313 15.641 73.276 30.364 1.00 49.44 O HETATM 2624 O HOH B 314 16.621 75.184 29.414 1.00 56.34 O HETATM 2625 O HOH B 315 17.644 77.142 28.018 1.00 46.26 O HETATM 2626 O HOH B 316 16.866 80.628 25.702 1.00 49.83 O HETATM 2627 O HOH B 317 -7.791 70.089 13.545 1.00 49.19 O HETATM 2628 O HOH B 318 -2.812 73.990 3.795 1.00 37.21 O HETATM 2629 O HOH B 319 -3.805 70.104 5.503 1.00 39.78 O HETATM 2630 O HOH B 320 1.000 82.859 2.243 0.50 21.24 O HETATM 2631 O HOH B 321 2.985 84.625 1.628 1.00 40.78 O HETATM 2632 O HOH B 322 7.534 71.379 25.716 1.00 60.49 O HETATM 2633 O HOH B 323 7.759 69.152 23.589 1.00 43.46 O HETATM 2634 O HOH B 324 -6.335 64.194 15.815 1.00 38.88 O HETATM 2635 O HOH B 325 20.002 69.475 5.730 1.00 34.43 O HETATM 2636 O HOH B 326 21.672 62.236 3.596 1.00 51.89 O HETATM 2637 O HOH B 327 -4.096 82.455 23.291 1.00 53.19 O HETATM 2638 O HOH B 328 -5.519 75.430 1.146 1.00 31.98 O HETATM 2639 O HOH B 329 7.134 79.015 -0.716 1.00 41.84 O HETATM 2640 O HOH B 330 4.097 77.999 25.035 1.00 41.32 O HETATM 2641 O HOH B 331 7.617 81.396 0.429 1.00 28.93 O HETATM 2642 O HOH B 332 7.741 62.500 6.373 1.00 28.21 O HETATM 2643 O HOH B 333 2.145 74.633 23.651 0.01 34.15 O HETATM 2644 O HOH B 334 3.262 73.146 21.821 1.00 34.38 O HETATM 2645 O HOH B 335 -0.900 64.663 19.112 1.00 34.51 O HETATM 2646 O HOH B 336 0.240 71.738 -1.091 0.50 39.09 O HETATM 2647 O HOH B 337 22.141 63.590 10.892 1.00 30.71 O HETATM 2648 O HOH B 338 10.859 58.320 10.810 1.00 37.19 O HETATM 2649 O HOH B 339 7.896 58.961 6.844 1.00 42.54 O HETATM 2650 O HOH B 340 19.927 59.409 2.377 1.00 57.62 O HETATM 2651 O HOH B 341 17.200 83.705 2.097 1.00 55.32 O HETATM 2652 O HOH B 342 7.067 60.453 4.187 1.00 50.86 O HETATM 2653 O HOH B 343 5.815 75.080 25.981 1.00 49.74 O HETATM 2654 O HOH B 344 -2.361 71.674 4.946 1.00 43.03 O HETATM 2655 O HOH B 345 9.610 58.659 5.401 1.00 44.17 O HETATM 2656 O HOH B 346 11.791 58.868 3.901 1.00 44.63 O HETATM 2657 O HOH B 347 17.812 65.618 -1.552 1.00 52.53 O HETATM 2658 O HOH B 348 16.812 62.958 -2.087 1.00 48.91 O HETATM 2659 O HOH B 349 20.515 79.687 7.693 1.00 47.66 O HETATM 2660 O HOH B 350 21.751 80.636 9.607 1.00 55.40 O HETATM 2661 O HOH B 351 1.433 60.147 6.767 1.00 49.06 O HETATM 2662 O HOH B 352 9.786 56.851 26.540 1.00 48.62 O HETATM 2663 O HOH B 353 -1.261 67.754 3.000 0.50 38.87 O HETATM 2664 O HOH B 354 1.080 68.021 -3.063 0.50 32.29 O HETATM 2665 O HOH B 355 0.286 68.756 1.210 0.50 44.67 O HETATM 2666 O HOH B 356 -0.194 69.058 -1.144 0.50 31.35 O HETATM 2667 O HOH B 357 -0.580 71.921 1.317 0.50 33.13 O HETATM 2668 O HOH B 358 -13.485 80.369 7.746 1.00 55.55 O HETATM 2669 O HOH B 359 -13.089 75.619 4.145 1.00 55.72 O HETATM 2670 O HOH B 360 22.120 78.479 5.657 1.00 65.41 O HETATM 2671 O HOH B 361 9.531 54.249 14.165 1.00 53.12 O HETATM 2672 O HOH B 362 3.326 86.987 2.938 1.00 51.75 O HETATM 2673 O HOH B 363 0.001 81.898 0.001 0.50 35.84 O HETATM 2674 O HOH B 364 0.035 78.955 -0.030 0.50 47.25 O HETATM 2675 O HOH B 365 28.349 56.069 11.371 1.00 72.91 O HETATM 2676 O HOH C 201 -4.657 21.624 12.563 1.00 42.33 O HETATM 2677 O HOH C 202 -14.591 24.850 11.732 1.00 55.12 O HETATM 2678 O HOH C 203 7.816 24.379 17.536 1.00 65.79 O HETATM 2679 O HOH C 204 -17.921 21.534 14.489 1.00 58.84 O HETATM 2680 O HOH C 205 -16.165 32.724 13.811 1.00 43.72 O HETATM 2681 O HOH C 206 -16.580 27.638 21.316 0.50 38.86 O HETATM 2682 O HOH C 207 -20.524 24.840 12.654 1.00 53.89 O HETATM 2683 O HOH C 208 -18.310 31.177 16.412 1.00 54.97 O HETATM 2684 O HOH D 201 -3.862 90.875 9.753 1.00 70.38 O HETATM 2685 O HOH D 202 -2.634 85.030 15.946 1.00 57.41 O HETATM 2686 O HOH D 203 15.153 88.557 11.019 1.00 55.60 O HETATM 2687 O HOH D 204 18.098 89.052 14.241 1.00 46.10 O HETATM 2688 O HOH D 205 12.677 88.020 11.015 1.00 30.52 O HETATM 2689 O HOH D 206 7.181 90.646 11.333 1.00 37.46 O HETATM 2690 O HOH D 207 10.721 90.791 11.122 1.00 53.70 O HETATM 2691 O HOH D 208 -5.172 86.810 16.787 1.00 52.74 O HETATM 2692 O HOH D 209 -5.744 89.265 8.285 1.00 63.41 O HETATM 2693 O HOH D 210 4.665 88.353 7.449 1.00 52.41 O HETATM 2694 O HOH D 211 6.303 90.467 8.448 1.00 47.14 O HETATM 2695 O HOH D 212 8.936 90.687 8.667 1.00 51.83 O HETATM 2696 O HOH D 213 18.749 84.616 21.315 0.50 37.30 O HETATM 2697 O HOH D 214 18.710 81.642 21.375 0.50 60.77 O HETATM 2698 O HOH D 215 22.822 87.755 12.965 1.00 56.60 O HETATM 2699 O HOH D 216 24.139 86.988 10.131 1.00 73.22 O CONECT 221 1930 CONECT 1930 221 CONECT 2547 2548 2549 2550 2551 CONECT 2548 2547 CONECT 2549 2547 CONECT 2550 2547 CONECT 2551 2547 CONECT 2552 2553 2554 2555 2556 CONECT 2553 2552 CONECT 2554 2552 CONECT 2555 2552 CONECT 2556 2552 CONECT 2557 2558 2559 2560 2561 CONECT 2558 2557 CONECT 2559 2557 CONECT 2560 2557 CONECT 2561 2557 CONECT 2562 2563 2564 2565 2566 CONECT 2563 2562 CONECT 2564 2562 CONECT 2565 2562 CONECT 2566 2562 MASTER 432 0 4 18 0 0 6 6 2695 4 22 26 END
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Related entries of code: 4mi8
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Protein Sequence Similarity
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31aa, >2P1L_2|Chains... *
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PDBbind
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PDBbind
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RCSB PDB
PDBbind
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4mi8
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
murine gamma-herpesvirus 68 Bcl-2 homolog M11
Ligand Name
Beclin 1 BH3 domain-derived peptide
EC.Number
E.C.-.-.-.-
Resolution
2.1(Å)
Affinity (Kd/Ki/IC50)
Kd=1.38uM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2014) J.Biol.Chem. Vol. 289: pp. 8029-8040
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):
P89884
Q14457
Entrez Gene ID
NCBI Entrez Gene ID:
1497180
8678
ASD
Information of known allosteric effects of PDB entries
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